LOCUS       WP_457553521             105 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Desulfobacula
            sp.].
ACCESSION   WP_457553521
VERSION     WP_457553521.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacula sp.
  ORGANISM  Desulfobacula sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacula.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Desulfobacula sp."
                     /db_xref="taxon:2593537"
     Protein         1..105
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11520
     Region          2..102
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mylpekyqkf stlypeifni yqelgkktre sgpldkktqd liklgiavgn nskgavrsht
       61 rkalesgatk eeimhavlma lstigfpsmv aafgwvdevm qkggk
//
LOCUS       WP_457553887             197 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Campylobacter fetus].
ACCESSION   WP_457553887
VERSION     WP_457553887.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter fetus
  ORGANISM  Campylobacter fetus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Campylobacter fetus"
                     /db_xref="taxon:196"
     Protein         1..197
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21796
     Region          1..197
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mrvvgliggm swestltyyk vlneeirdrl gglhsakciv ysldfheiek fqsqnewqks
       61 gkvlldaaln lekagaecvm ictntmhkva dmitaslkip fihiadvtaq alkqngskka
      121 lllgtkytmt esfykdkisk nsievvvpnk sdtdfinsvi fnelcignik qsskiefiki
      181 ineskklgvd svilgct
//
LOCUS       WP_457554307             258 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_457554307
VERSION     WP_457554307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28008
     Region          4..254
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mahmldierv swspggaiav ldsvtlsvad gefvglvgpn gsgktsllrc vfryarpdag
       61 rvalgaqdvw rmrpravaqr iavlqqetpd dfgltvdelv gmgrtphkrp fdaetaddrr
      121 ivesalhdvg lverraqrfa slsggekqra llaralaqqp elllldeptn hldlrhqlel
      181 larvrrlgia tlatihdlnl aaaycdrlhv lahgrvvasg apadvltdal lrdvfgvval
      241 vdrhpvtsrp ritplhpe
//
LOCUS       WP_457554308             828 aa            linear   BCT 27-JAN-2026
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_457554308
VERSION     WP_457554308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..828
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=88539
     Region          1..814
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mrirhsflcv svlvvgsqsh atefnssfln idgsnnvdls qfsqadftlp geymldvqvn
       61 dlfyglqaie fiavdasgag kpclrpelva qfglkpslak dlprfqggrc vdlgaiegat
      121 vrylksdgrl kitipqaale fsdttylppe rwsegipgam ldyrviantn rnfgtgggqt
      181 nsiqaygtvg anwdawrfrg dyqaqsnvgn tayadrtfrf srlyafralp siqstvtfgd
      241 dyltsdifdt faltgasirs ddrmlppslr gyaplisgva rtnatvtvsq agrvlyvtrv
      301 spgafalqni ntsvqgtldv aveeedgsvq rfqvttaavp flaragqlry kaavgkprlf
      361 ggagitpffg fgeiayglpf dvtayggfia asgytsialg vgrdfgafga lsadvthara
      421 rlwwngttrn gnsyrinysk hfdgldadvr ffgyrfsere ytnfaqfsgd ptayglansk
      481 qrysatlskr fgdtstyfsy dqttyweran eqrvgltltr afsigtlrnl nvsvsafrtq
      541 sagasgnqvs vtatlpiggr htvtsnlttg sgstsvnagy iyddpdgrty qvnagatdgr
      601 asanasyrqr ssayqltaqa stlanayaaa slevdgsfva tqygvaahan gnagdtrllv
      661 stdgvpdvpl sgtlshtdsr gytvldgisp ynvydatvnv eklplevqvs npiqrmvltd
      721 gaigfvkfsa argsnlyltl tdpvgkplpf gasvqdmang kelgivgegg aafltqvqpk
      781 stlavrager tlctidtlpn qlqlegtpip vtcqtpgesh aaaarver
//
LOCUS       WP_457554309             742 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_457554309
VERSION     WP_457554309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..742
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79949
     Region          58..742
                     /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 mewatgtrlr aiaaaasvaf gaaagqayaq tapavnagaa asassaqgga aasastgtlp
       61 tinvnaaseg dgtvglvakr srtgtktdtp ineipqtinv vtaqqiemtg atdvnaalry
      121 vpgfssygsd nrsdwyaalr gftptayvng lqvpntinla swrvdpymid sitvlrgpts
      181 vlygagdpga iidvqtklad gervreagvq ignyarkqfm idvgdkldpd gkyayrfvgv
      241 ardgnaltgp nndqrvslap sfrwrpnadt sltlsatylq dwgdissnfl paqgtvlpnp
      301 sgqinkdvye gdpnfnyyrk kqwsvgyqfe qnltsawkfr qnvrlmhlsl dngsvwgngf
      361 vdgsttdvsr wagvfqmnys rfdidnnveg rfatgplqht lllgfqynrq tatdsewiaa
      421 applniynpv ytpvttsvfs npettgrtnt ytamntfgly aqdqikwnrw tltlggredw
      481 vnmrmddrag gtstkadvta ftgrvgltyq gdyglspyis yatsfnplig vnllggglpq
      541 ptrgkqieag lrwqppgknl mlnaaiyqin qtngitpalp sqddsgtksv qsgevrsrgi
      601 elsatgkvtp nlsliasyvy qdvkvikand nslnnwpvdi prprqmaslw adwtwhtgal
      661 aglgfgggvr yqsasaggsd naltvssvtl fdagvhydtr nwrfavnatn lanrhyisgc
      721 qsvnvcvfgt drtviataky nw
//
LOCUS       WP_457554312             328 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_457554312
VERSION     WP_457554312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 328)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..328
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35658
     Region          24..204
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          236..319
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtppdfecnr irffveivrs vnvdplsevl slletrdsyf tglraggqwa vaipppegik
       61 fnavvegscw ltvdgagapi rlrtgdcfll asprafslas dpsvtpvpaa dvyrnvehgi
      121 ahygepancf liggrfsyee gmplllgslp pvvvvsgdse qaavlrwalq rlahefgkps
      181 pgaslmvrhl ghmmlveilr ryvddgassd vgwlagfads rvstalvaih aeparrwtvd
      241 elatcchvsr stfalhfkrr lgfgpfeyvl rwrvqlamre lrrsnasisa iaqmlgydsd
      301 safghafkri agcsprayrh ditggagg
//
LOCUS       WP_457554318             859 aa            linear   BCT 27-JAN-2026
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_457554318
VERSION     WP_457554318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..859
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=91282
     Region          13..857
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 miqrlsslpp fvrwrprpcf lltlsvfast gamaqttsat qvaevqfddl flqrpggtrv
       61 dvsrfekgna aapgsyradl yvntnwigrt aitlrqvgds rnnvqpcfdr ellqqvgvdl
      121 aklspeatlm ltdsnhacat igmlvpdava tfdngeqrld vsipqaslsr aargyvdpry
      181 wdegvpaall syngniyrad nqgasstqay lgltaglnvg pwrfrhngnt tydthggthy
      241 qsvqtslqrs iarlkaqlvi gdaftdgtmf dsvgfrgvri asdermypes qrgyaptihg
      301 iansnalvqv rqngnivysa nvatgpfeid dlyatgyggd ldvivteadg sihtfkvpya
      361 savsslrpgi trfsvtagqy rspllsskpa lfqatvqhgf tnlitgyggm taapgylagl
      421 agvalntglg sfalditqan tdlpgmgtrh gqsvklsysk lisptntnia vaayrysssg
      481 ylglqdamql rsqqtggvng llsggvrrgq fqvmlnqglp egwgsfylsg stvnywnrsg
      541 ndtqfqagys nnfrrinygv svarqfdatq nrwdnrfmln vsiplnlgsr tlysstslqh
      601 dshgatlvqq sltgslgidn alsygvnvgh trgsgtgata nvggnvsyms pyatlsgnas
      661 kgtgftqygg gisggmvaya ggvafaptmg etmaiveakd angarvtags glridrfgha
      721 lvstltpfst neveidpkgv pmsvelkssa qhvaptagav vrlkyetegg gravimrarm
      781 adgepvpfga evsntagqnv gtvaqdgrvv lrgvktdtgt lkvkwgdtdg dhcslsytlp
      841 tenktskqrw idaeavctk
//
LOCUS       WP_457554319             375 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Campylobacter lari].
ACCESSION   WP_457554319
VERSION     WP_457554319.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter lari
  ORGANISM  Campylobacter lari
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Campylobacter lari"
                     /db_xref="taxon:201"
     Protein         1..375
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=40490
     Region          <87..368
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 medvfdqiit sivililscf ivyfissrll splqviqhgl nsffdfinhk tkdsaminvn
       61 tndelgamak ainenitktk naleqdakav eqsvetakei eagnltarit aipanpqlie
      121 lknvlndmld vlqakvgsnm neinrvfdsy kaldftteva nakggvevtt nvlgqeivam
      181 lrqssefasl ladesgklqs avkdltdsss sqassleeta aaleeitssm qnvshktsev
      241 iaqseeiknv tsiigdiadq inllalnaai eaaragehgr gfavvadevr nlaertqksl
      301 geieantnil vqsinemges ikeqttgitq indavaqidh vtqenlkian dsaaisenvn
      361 kiandileda kkkrf
//
LOCUS       WP_457554321             742 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_457554321
VERSION     WP_457554321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..742
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80214
     Region          58..742
                     /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 mewatgtrlr aiaaaasvaf gaaagqayaq tapavnagaa asassaqgga aasastgtlp
       61 tinvnaaseg dgtvglvakr srtgtktdtp ineipqtinv vtaqqiemtg atdvnaalry
      121 vpgfssygsd nrsdwyaalr gftptayvng lqvpntinla swrvdpymid sitvlrgpts
      181 vlygagdpga iidvqtklad gervreagvq ignyarkqfm idvgdkldpd gkyayrfvgv
      241 ardgnaltgp nndqrvalap sfrwrpnadt sltlsatylq dwgdissnfv pavgtvlpnp
      301 sgqinkdvye gdpnfnyyrk kqwsvgyqfe rnltpawtfr qntrlmhlsl dngsvfgngf
      361 vegsttdvsr wagvfqmnys rfdidnnveg rfatgplqht lllgfqynrq tatdsewlaa
      421 asplniynpv ytpvtlsvfs npdttfrtnt yttmntfgly aqdqikwnrw tltlggredw
      481 vnmrmddrag gtstkadvta ftgrvgltyq gdyglspyvs yatsfnplig vnllggglpq
      541 ptrgkqieag lrwqppgknl mlnaaiyqin qtnvltpalp dqdptgtksv qtgevrsrgi
      601 elsatgkvtr nlsliasyvy qdvknvkand vslnnwpvdi prprqmaslw adwtwhtgpl
      661 sglglgggvr yqsasagaad nsltvssvtl fdagvhydtr nwrfavngtn lfnrhyisgc
      721 qsmnvcvfgt drtviataky nw
//
LOCUS       WP_457554327             258 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_457554327
VERSION     WP_457554327.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28110
     Region          4..254
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mahmldierv swspggaiav ldsvtlsvad gefvglvgpn gsgktsllrc vfryarpdag
       61 rvaldaqdvw rmrpravaqr iavlqqetpd dfgltvdelv gmgrtphkrp fdaetaddrw
      121 ivesalhdvg lverraqrfa slsggekqra llaralaqqp elllldeptn hldlrhqlel
      181 larvrrlgia tlatihdlnl aaaycdrlhv lahgrvvasg apadvlteal lrdvfgvval
      241 vdrhpvtsrp ritplhpe
//
LOCUS       WP_457554328             576 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Clostridioides difficile].
ACCESSION   WP_457554328
VERSION     WP_457554328.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11604399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..576
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=63884
     Region          352..445
                     /region_name="3D_containing_proteins"
                     /note="Non-mltA associated 3D domain containing proteins,
                     named for 3 conserved aspartate residues; cd14667"
                     /db_xref="CDD:270620"
     Site            order(385,414..416,442..443)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:270620"
     Region          <451..575
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mvwinniklq vhikdgavyd itdivekvtw sgdykspsrt lefsivqsay dinfrqidip
       61 iastvcfyvd dkeiyrgmii nrskdssnns isfvskdmgf lltqsevsyn fkdklvedit
      121 kqvfndnkfa ignipktgvk ytkmfigvtg ydtimsayte askttkkkym iessvdkfnv
      181 iekgtvtlnv mfeegsnlin tsfsesmenv knkvivvdqy gnkisekidn eifkdvgvim
      241 qkviqqqens tvdiesefkg ieqtcslkgy gdvtcitgrg vkvkdsytgl vglfyidtdk
      301 hswdssgnye idldlnfqni mdektagqde qkeessdlgs gegtlngkev kaeftayyps
      361 ndpmegglyq kmdgkklvps nntcaaptql kfktqiqvkg tgtnidgkty tvtdrggvik
      421 vvngvykidi lmsskeecnr fgrrkgslii gdgtgytnva gkagtviaea kkhlgkpykw
      481 ggngpsnfdc sglmvycfkk vnvnlprtss qqskvgkkve qnnlqagdlv ffhnpvthvg
      541 lyigngeylh apqtgdivki sklsgrkdfn tarrvl
//
LOCUS       WP_457554330             165 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Clostridioides
            difficile].
ACCESSION   WP_457554330
VERSION     WP_457554330.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12204063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..165
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18825
     Region          <1..57
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqfraylrnr kltfalkevq dsdksllyia fdygflshea ftkafkgtyg vtpseyrknp
       61 kptvlltkit pfdcyflglg eismikstdg vkiyfatipa hkflyiknne sngywdfwrk
      121 qnliprqdhe ticglfdsik gklndaggsg qimaymnspd srlcd
//
LOCUS       WP_457554331             104 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Clostridioides difficile].
ACCESSION   WP_457554331
VERSION     WP_457554331.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..104
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=11952
     Region          <9..100
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlkagelyrn anyvfcnelg ipiddkrplr nlrsilnsln iepikfhglr ktyatrlfen
       61 dvppktvqvl mghydisitl niytqvmedk kveavekldk ifsl
//
LOCUS       WP_457554332              78 aa            linear   BCT 27-JAN-2026
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Clostridioides
            difficile].
ACCESSION   WP_457554332
VERSION     WP_457554332.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..78
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=9509
     Region          5..>78
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mytikisklp eselkvmryi wesdkvlisr eitksmeqky ewkdttiftv lkrlqrrefl
       61 etekidkrah ynvlvkek
//
LOCUS       WP_457554333             651 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Clostridioides difficile].
ACCESSION   WP_457554333
VERSION     WP_457554333.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..651
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74760
     Region          18..538
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          576..641
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mknnrleikv nymnlmtlen isksysekkl lenislgine gekigligvn gtgkstllki
       61 iagveesetg nitktngiri eylpqnptyn enstvleqvf ngtseelkll geyqeilekl
      121 nsnfteelnk kllsvhekid alnlwdlese aksvltklgi ndfnqkiael sggqrkrvsl
      181 asalitpcef lildeptnhl dndtidwlee ylnsrkgsll mithdryfld rvtnriield
      241 kgrlfsydgn ysiflekkme rlsleasied krqnlirtel awvrrgaqar stkqkarlqr
      301 fdelinkdsf kpdenldisv assrlgnkii eihnisksfe entvinnley tltrtdrigi
      361 igkngmgkst linilngeie pdsgyisige tvkigcfsqd dshmnidmra idyvkeasdy
      421 ietsdgtrit asqmcerflf ngtmqytlig klsggerrrl hllkilmtap nvllldeptn
      481 dldietlkil eeyldefkgv vvtvshdryf ldricnkifa yegngkihiy tgnysdyliy
      541 reiqgiefee skkesvkkdd sttpkkekpk ndkklkfsyn eqrefenids diekleskia
      601 tldestskfs tdftklqeil deksklekel eykyerweyl nnladeiann k
//
LOCUS       WP_457554615             184 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Bifidobacterium breve].
ACCESSION   WP_457554615
VERSION     WP_457554615.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..184
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20552
     Region          5..129
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(10,12,67..68,71)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            12
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(66,110..111,113..114,118)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(72,77..78,106,109..110,113..114,117,120)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95..97,106..107,110..111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(95,111,114,118,121,125)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(119,125..126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          141..183
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(142..144,177..178,180..182)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 masmiygyar istndqttsl qkdalekagc driftdvasg akahrpeldh mldllregdm
       61 vvvwkldrlg rsmqnlvdlm ttfdergmqf rsltesidts tpggtlvfni fgslaqferd
      121 lirertragl eavrargrkg grpakldekq vkearrlyes ktvtvdqiaa mmgvgrstiy
      181 rcln
//
LOCUS       WP_457555310             437 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Bifidobacterium longum].
ACCESSION   WP_457555310
VERSION     WP_457555310.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..437
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46631
     Region          15..418
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(24..25,28..29,31,64,114..115,117..119,122,142,
                     145..146,149,256,259..260,263..265,268,295,299,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mkkqrmifgl sllywglwla ililwmgrfv tsflsiylvs alrldegvvg tvvamygfga
       61 iigclfggtl sdrfgrqsmi iigeigaaaa llvvsvltdp vslgaalfvy gafaslpspa
      121 iaayiadvvp aerqqrayvl qswainfgya igpivanqlv kisyslmfyv eaavmiavti
      181 lliaffrevr hlgitvsvps avrhedecsv thaefagier pnhsdaapaa svkgamsrnw
      241 rrvltdtpfl gfsllmfgyf lvyfqstsgl piamtdlglg lgeysvllti nggmlcllqi
      301 pamklfarmg nsrvlvmgla vtvigyavqa aahswggfal avvlwtlgel gtfpiatttv
      361 aamapasarg tyqgvynvvw sasialapmi ggwtisnfgg rtlwiactvv liavtlglkl
      421 tkgsrdrama rslhdsl
//
LOCUS       WP_457559820             859 aa            linear   BCT 27-JAN-2026
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_457559820
VERSION     WP_457559820.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..859
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=91326
     Region          13..857
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 miqrlsslpp fvrwrprpcf llalsvfast gtmaqttsat qvaevqfddl flqrpggtrv
       61 dvsrfekgna aapgsyradl yvntnwigrt aitlrqvgds rnnvqpcfdr ellqqvgvdl
      121 aklspeatlm ltdsnhacat igmlvpdava tfdngeqrld vsipqaslsr aargyvdpry
      181 wdegvpaall syngniyrad nqgasstqay lgltaglnvg pwrfrhngnt tydthggthy
      241 qsvqtslqrs iarlkaqlvi gdaftdgtmf dsvgfrgvri asdermypes qrgyaptihg
      301 iansnalvqv rqngniiysa tvatgpfeid dlyatgyggd ldvivteadg sihtfkvpya
      361 savsslrpgi trfsvtagqy rspllsskpa lfqatvqhgf tnlitgyggm taapgylagl
      421 agvalntglg sfalditqan tdlpslgtrh gqsvklsysk lisptntnia vaayrysssg
      481 ylglqdamql rsqqtggvng llsggvrrgq fqvmlnqglp egwgsfylsg stvnywnrsg
      541 ndtqfqagys nnfrrinygv svarqfdatq nrwdnrfmln vsiplnlgsr tlysstslqh
      601 dshgatlvqq sltgslgidn alsygvnvgh trgsgtgata nvggnvsyms pyatlsgnas
      661 kgtgftqygg gisggmvaya ggvaftptmg etmaiveakd angarvtags glridrfgha
      721 lvstltpfst neveidpkgv pmsvelkssa qhvaptagav vrlkyetegg gravimrarm
      781 adgepvpfga evsdtagqnv gtvaqdgrvv lrgvktdtgt lkvkwgdtdg dhcslsytlp
      841 tenktskqrw idaeavctk
//
LOCUS       WP_457559821             828 aa            linear   BCT 27-JAN-2026
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_457559821
VERSION     WP_457559821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..828
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=88479
     Region          1..814
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mrirhsflcv svlvvgsqsh atefnssfls idgsnnvdls qfsqadftlp geymldvqvn
       61 dlfyglqaie fiavdasgag kpclrpelva qfglkpslak dlprfqggrc vdlgaiegat
      121 vrylksdgrl kitipqaale fndttylppe rwsegipgam ldyrviantn rnfgtgggqt
      181 nsiqaygtvg anwdawrfrg dyqaqsnvgn tayadrtfrf srlyafralp siqstvtfgd
      241 dyltsdifdt faltgasirs ddrmlppslr gyaplisgva rtnatvtvsq agrvlyvtrv
      301 spgafalqni ntsvqgtldv aveeedgsvq rfqvttaavp flaragqlry kaavgkprlf
      361 ggagitpffg fgeiayglpf dvtayggfia asgytsialg vgrdfgafga lsadvthara
      421 rlwwngatrn gnsyrinysk hfdgldadvr ffgyrfsere ytnfaqfsgd ptayglansk
      481 qrysatlskr fgdtstyfsy dqttyweran eqrvgltltr afsigtlrnl nvsvsafrtq
      541 sagasgnqvs vtatlpiggr htvtsnlttg sgstsvnagy iyddpdgrty qvnagatdgr
      601 asanasyrqr ssayqltaqa stlanayaaa slevdgsfva tqygvaahan gnagdtrllv
      661 stdgvpdvpl sgalshtdsr gytvldgisp ynvydatvnv eklplevqvs npiqrmvltd
      721 gaigfvkfsa argsnlyltl tdpvgkplpf gasvqdmang kelgivgegg aafltqvqpk
      781 stlavrager tlctidtlpn qlqlegtpip vtcqtpgesh aaaarver
//
LOCUS       WP_457559822             742 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_457559822
VERSION     WP_457559822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..742
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80157
     Region          58..742
                     /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 mewatgtrlr aiaaaasvaf gaaagqayaq tapavnagaa asassaqgga aasastgtlp
       61 tinvnaaseg dgtvglvakr srtgtktdtp vneipqtinv vtaqqiemtg atdvnaalry
      121 vpgfssygsd nrsdwyaalr gftptayvng lqvpntinla swrvdpymid sitvlrgpts
      181 vlygagdpga iidvqtklad gervreagvq ignyarkqfm idvgdkldpd gkyayrfvgv
      241 ardgnaltgp nndqrvalap sfrwrpnadt sltlsatylq dwgdissnfv pavgtvlpnp
      301 sgqinkdvye gdpnfnyyrk kqwsvgyqfe qnltsawkfr qnvrlmhlsl dngsvfgngf
      361 vdgsttdvsr wagvfqmnys rfdidnnleg rfatgplqht lllgfqynrq tatdsewlaa
      421 asplniynpv ytpvtlsvfs npdttirtnt yttmntfgly aqdqikwnrw tltlggredw
      481 vnmrmddrag gtstkadvta ftgrvgltyq gdyglspyvs yatsfnplig vnllggglpq
      541 ptrgkqieag lrwqppgknl mlnaaiyqin qtnvltpalp dqdttgtksv qtgevrsrgi
      601 elsatgkvtr nlsliasyvy qdvknvkand vslnnwpvdi prprqmaslw adwtwhtgpl
      661 sglglgggvr yqsasagaad nsltvssvtl fdagvhydtr nwrfavngtn lfnrhyisgc
      721 qsmnvcvfgt drtviataky nw
//
LOCUS       WP_457559823             386 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-directed DNA polymerase [Burkholderia cepacia].
ACCESSION   WP_457559823
VERSION     WP_457559823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Lampson,B.C., Inouye,M. and Inouye,S.
  TITLE     Retrons, msDNA, and the bacterial genome
  JOURNAL   Cytogenet Genome Res 110 (1-4), 491-499 (2005)
   PUBMED   16093702
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Inouye,S. and Inouye,M.
  TITLE     Structure, function, and evolution of bacterial reverse
            transcriptase
  JOURNAL   Virus Genes 11 (2-3), 81-94 (1995)
   PUBMED   8828137
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Inouye,M. and Inouye,S.
  TITLE     msDNA and bacterial reverse transcriptase
  JOURNAL   Annu Rev Microbiol 45, 163-186 (1991)
   PUBMED   1720608
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..386
                     /product="RNA-directed DNA polymerase"
                     /EC_number="2.7.7.49"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0003964 - RNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006278 - RNA-templated DNA biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44121
     Region          153..319
                     /region_name="RT_Bac_retron_I"
                     /note="Reverse transcriptases (RTs) in bacterial
                     retrotransposons or retrons. The polymerase reaction of
                     this enzyme leads to the production of a unique RNA-DNA
                     complex called msDNA (multicopy single-stranded (ss)DNA)
                     in which a small ssDNA branches out from a...; cd01646"
                     /db_xref="CDD:238824"
     Site            order(154..159,225..226,257,259..260,307..308)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238824"
     Site            order(154..159,225,259)
                     /site_type="other"
                     /note="putative NTP binding site [chemical binding]"
                     /db_xref="CDD:238824"
     Site            226
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238824"
ORIGIN      
        1 matrttttrt tscapapsad rgpisfaelv eayldcrrtk rnsnaalafe mrlernlrrl
       61 ydelvdgsyt pgrskcfvit rpkprevwaa afrdrivhhl lynrigprfe rsfiadscac
      121 ikgrgtlyaa qrleskvrsi tqnwsrrafy lkcdlanffv sidkrilldl llakisepfw
      181 rvltervlmh dpradfeyhg dpammqlvpp hkrlmeqadh lglpignlss qffanvyldv
      241 ldqrakhvlg arhyiryvdd fvflhespar lnailadvta flpaqlgari nprktilqpi
      301 drgidfvgqv ikpwrretrk rtrnealrrv aetpasdlmp vansyfgllr qaaashhdra
      361 rlanllrslg kavdhdltkt yrssha
//
LOCUS       WP_457559824             425 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_457559824
VERSION     WP_457559824.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..425
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46286
     Region          25..397
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkfesywldt rpafragceg pvegradvvv igggftglsa alalaqrgvs vvvleaaqva
       61 geasgrnggq cntgvaqdya slaarmgaep akqfyrayes avksvetiva ehaidcdfrr
      121 agklklaakp qhfaglaktf dalrrdvdpd ielieperir devashgfyg gllqrngaqm
      181 hmgkfgvgla haavragarv yehaavtqld rldgerhait ctrgrivadr vlvatgasqh
      241 gpfgwfrrri apvgsfivvt epladaqlnr lfphrrayvt srqignyfrv tpdnrllfgg
      301 rarfamsspr sdaksgdilr agmagyfpel advrldycwg glvditadrl pragqhdgly
      361 ysmgysghgv qmsvhmgrvm advlygatas npwreldwpa mpghfghawf lpfvgayyrv
      421 qdflh
//
LOCUS       WP_457560035             205 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane protein assembly factor BamD [Caminibacter sp.].
ACCESSION   WP_457560035
VERSION     WP_457560035.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Albrecht,R. and Zeth,K.
  TITLE     Structural basis of outer membrane protein biogenesis in bacteria
  JOURNAL   J Biol Chem 286 (31), 27792-27803 (2011)
   PUBMED   21586578
REFERENCE   3  (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 1003154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..205
                     /product="outer membrane protein assembly factor BamD"
                     /calculated_mol_wt=24265
     Region          15..>150
                     /region_name="BamD"
                     /note="Outer membrane protein assembly factor BamD,
                     BamD/ComL family [Cell wall/membrane/envelope biogenesis];
                     COG4105"
                     /db_xref="CDD:443281"
ORIGIN      
        1 mrktlfiipl llflgcsskn qiqknlkait ihsklvkavk ennfdkaddl fltmeaehpt
       61 siyikqdlli lylghlnygd fklakfylnq yetryaskde ipwceyqkik vdflsyhnay
      121 tnqkkildli kecknyklsy pnsqflpevn tiymkayltn lylddkiskl ykkegkikas
      181 keykvkvpkn svppqvpwyk kifyw
//
LOCUS       WP_457560306             432 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter sp.].
ACCESSION   WP_457560306
VERSION     WP_457560306.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..432
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47400
     Region          34..423
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 meeerknyfk ilqeiiqkqa kyirfdiimi shffgrwipy amaigivtgs laafmdlliv
       61 sinsflsenl ililfyplfv smivglgirg dktiagpgig fairhlksrs fikfksfisk
      121 lalsiltlsg gfiagregps fylgvalgew lgrvygigkk yknimgligg gaftgsllka
      181 plgssifame ienmhdfdyr pfvpmiiaav vsyltfsffr gthpfillye kptwtlqsip
      241 yiiimglvis viiyfytffy htfakfskti dakkrpligt aislpiligl yllikdtdil
      301 sapahmgiis kiaqhpypyy tdiaiiigti iitsftlafg ipgglvlpnl ligaavgnmf
      361 ghyfnqeivm fslagmgaal aagaktplaa ivmitemtha dvvipmtaav itsyttsfgf
      421 slylglekge hv
//
LOCUS       WP_457560328             440 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter sp.].
ACCESSION   WP_457560328
VERSION     WP_457560328.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..440
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49336
     Region          19..417
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mvakiknffn kkayifrdfl llsfitglvt glfvsvyifl tkwfmkflyh gdpvntisvl
       61 pvwyvymipi vsilivnfli sldstvkeyg itklaeivek rseiitiksl flkiiasvls
      121 issgfsvgne gpsaeigals afyvkklfki pekfiriivs vgassgiaav fvspltgitf
      181 aiesiaseff ksyiifmivg afsafsiave ffpaigflsp sgrfinfdyv wlnivfipii
      241 tffiyfylfl qekvlyvfnf kifekfgkyr nlffaifggf iigtilliep kacftghfvv
      301 qelfndfstm slkliialiv lriiattisq ysnavggmfl plmsigalig ygfgevmnmf
      361 hfvniqpyyf aaigaavfmg vlmklpftav vlaleitndy nvvlttgfav aviayvtkln
      421 fnikkfntvq idfkeilhik
//
LOCUS       WP_457560360             259 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Caminibacter sp.].
ACCESSION   WP_457560360
VERSION     WP_457560360.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..259
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27458
     Region          1..258
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 madilkigky eftsrlivgs gkypdfkttr datlasgaem itvavrrvni ldpneenlmd
       61 yfkdtdvkil pnsagcttae eaitlfrlvr eatgidiikl evigdtkktl ypdvietlka
      121 cevlakdgft vmaytnddpi makrledaga aavmplaapi gsglgvqnky nvvfvkdavn
      181 vpvivdagig tasdaavame lgadgvltnt aiaqaknsie maeamkyavi agrmaykagr
      241 ipkkpfatas spleglief
//
LOCUS       WP_457560432              95 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Caminibacter
            sp.].
ACCESSION   WP_457560432
VERSION     WP_457560432.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 95)
  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
REFERENCE   2  (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 1562707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..95
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10838
     Region          23..91
                     /region_name="Polbeta"
                     /note="Polymerase beta, Nucleotidyltransferase; pfam18765"
                     /db_xref="CDD:465859"
ORIGIN      
        1 mrlskneidf ikktinsilp stiyifgsrl dknkkggdld lylipktdln kkeklekigl
       61 iklileerll lkvdiiisnk nkkeidfeal kgvki
//
LOCUS       WP_457560761             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter sp.].
ACCESSION   WP_457560761
VERSION     WP_457560761.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118302
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40589
     Region          22..353
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
     Region          190..357
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrefwaifkk eiliilrntv lvifmiyift ldiylagvgi kvkpqhvsig yvdysnslmv
       61 kkilshlhkp eflppkrfln erdlkkaied kkiivglvfd sdfeknyykf gksqvnvlid
      121 staaaqaqvt liyldeilar fvnlkaplli qthrlfnqns nstwfmsvse lmsdvtllvl
      181 llvavvfvke kqegtwdiml lmpvntfsli fakvlsqvfi ilvgifisvg iifygvfgip
      241 yhgnltlffl lnlvfglslg gialviaavs ntvtevgqys flvmmplifl sgawtpiesm
      301 apwlqklsii spvryyieat qsiifrgasf idvwkdfaal aiigtilfii gyrkigrlf
//
LOCUS       WP_457560921             100 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Caminibacter
            sp.].
ACCESSION   WP_457560921
VERSION     WP_457560921.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..100
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10913
     Region          3..100
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 meliktlqkd apeeikgfle fmknvekdga isaknkelin iglavaaqce wcitfhtqna
       61 lklgatreei ieagmqavlm hggpalmymi pllkaleels
//
LOCUS       WP_457561109             574 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter sp.].
ACCESSION   WP_457561109
VERSION     WP_457561109.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..574
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63319
     Region          24..434
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mglstkkrrs wslkikrsil idtfligfig avsaqvflfl ldtvkkisny innnpyliei
       61 aknlnispsv livftitlgg lisgflvykf apeaeghgtd tvirafhrtg gylrpivvpi
      121 kiiasaitig tggsagkegp talfsagigs iysdwkkvsw rdrqiyvlia masglsavfk
      181 aplgtsffav evlyisteie srdliyilfg plvaytltgy ffgwhpiftf pdtlmltslw
      241 qyvdvvvlgi isgilgfflp nifyytrdff rslkinpifk paigaffvgi igiylpyilg
      301 ggyqtiqaai dgkligmfvl flllgkiaaf vltvgsggsg gvfaptlfig amlgaffasi
      361 fhlniavfvl iamaavfgaa artplasiim vlemsggydl laptmfgvla afvthnvmnk
      421 tfkpkyvsly eaqllnsnfs vinqieklkd ilvceaqtfg fdlkrvkndt litllengrp
      481 ikvgenkyvf fgtfhenekl elegkfkkyk gayvlyvfrn gewlhameid eikkgddvll
      541 yggydtifki kdeftpvsei fsklklqeel ieka
//
LOCUS       WP_457561232             440 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter sp.].
ACCESSION   WP_457561232
VERSION     WP_457561232.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..440
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48985
     Region          19..417
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mfekislfln kkgyvfrdfl llsflsgilt gvfvtvyifl tkffmkilyq gdpvktihnl
       61 pvwyvylvpv vsilivnyli sldetvreyg iaklsdivsq nstlitiksl flkiiasvls
      121 issgfsvgne gpsaeigalv syhiqkffki pekfikviis vgassgiaav fvspltgiaf
      181 aiesiageff ksyiifmivg afsafsiave yfpaigflsp sgrfinydyi wlniifipvi
      241 tffiyfylfl qdkllyffnl kvfekfgkyr nivfavfggm vigtilliep kacftghfvv
      301 qelfndfahm gfsliavlil lrivatsvsl ysnavggmfv plmsigalig ygfgeiinmm
      361 hlvniepyyf aaigasvfmg vlmklpftav vlsleitndy nvvlatgfav aviayvtkln
      421 fnikklntiq idfkevlkik
//
LOCUS       WP_457561279             418 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter sp.].
ACCESSION   WP_457561279
VERSION     WP_457561279.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..418
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46241
     Region          23..403
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mvtkfilssi ligiitgifi tiyvlltkll svflyfgnpf ervshlpvwy iylvplvsil
       61 ivnfliskde avkeygvrei aeaveqnrlf fgikdlflki fasslsiasg faignegpsa
      121 aigamianki heflklpkkl ikvslsigas ggiaaifvsp vtgimfaien iayefvksya
      181 gylilasvls fsvawhflep lifnystgkf ieyryifatg lfipvmtffv yfyltlkdkv
      241 lnflniflfe kyaqyknyif gvigalvist imlispyavf sghevvklli nnaahlplwm
      301 ifliivlrii atsvslyana vggvfialms igalvgygfg evmniyfpie pfyfaaigaa
      361 vfvgvnmklp ltaivlalei tydynviipt gisvvivtyl aslnfslkki tlrpriea
//
LOCUS       WP_457561329             147 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Caminibacter sp.].
ACCESSION   WP_457561329
VERSION     WP_457561329.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     gene            1..147
                     /gene="rimP"
     Protein         1..147
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=16569
     Region          1..140
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mreelknvik nivedngcel ydiedtiegd nrflrvyitk pggvtledca ainnllspif
       61 dvedpiegky flevsspgve rkltkpehfe ksigenvkvt tsdgkkvkge lksfidgvae
      121 igkekvnykd ikkaktyvdw stykfde
//
LOCUS       WP_457561451             192 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Caminibacter pacificus].
ACCESSION   WP_457561451
VERSION     WP_457561451.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..192
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21521
     Region          4..192
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mseivnflvd tigawgyigi fllmflessf fpfpsevvmi pagylaskge mnlylaifva
       61 vlgsvagawf nyliashmgr aflikfmsee kikklenffe nhghistfsg rlipgvrqyi
      121 sfpaglakmh plkftiytal gagiwvtila llgyfigenq qiihkylrei tiitlvvlvi
      181 iifvyiklkv kk
//
LOCUS       WP_457561464             252 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457561464
VERSION     WP_457561464.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..252
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27502
     Region          29..249
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mhtyvftlis gllsglalgl tggggsilav pllvylvgin ihlaivtsli avgatsliss
       61 itymrqnlvr fkvaflmaap gilstffgsl inkklnghll limfsflmfy igfrmlkkrn
      121 ienvksdtqn ilkilffgfi vgflsglfgv gggfllvpal ylgvnlsmke avgtslfiif
      181 myglfgmtsy ivekreiefl isaifvlggv fggfigayig ehlnqeklrk ifayftmama
      241 vfiflenigy fi
//
LOCUS       WP_457561453             376 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Caminibacter pacificus].
ACCESSION   WP_457561453
VERSION     WP_457561453.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..376
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42324
     Region          5..367
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(15..16,19..20,23,56,107..108,110..112,115,134,
                     137..138,141,210,213..214,217..219,222,249,253,298..299,
                     303,307,321,324..325,328..329,332)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mdknvvvlgi vsfftdlass mvntilplfi vyilnegvdk lgyvlaiatf lsyalrvvfg
       61 yfsdkygivk pfvvtgylis aiskpllyfs htwksvaflr gterigkair satkdtllsa
      121 yshshsgktf gfhkmldvag emtgalivfl ilmfigksee ifrlifafti ipgiisvflv
      181 iffvkdvkke kisknidfkk dkevikflff yfgflifafn dsffvikake sgftfemipl
      241 liivynltqt llsyflgvki ekegykkill isfvfgilsv iamkmsyivl gfvflgiftv
      301 gslnairsyi sdnafnkstv ygffyagvai saslasliig klwqnygenf ayvysitgmi
      361 fvllfylkdg yvrayh
//
LOCUS       WP_457561465             271 aa            linear   BCT 27-JAN-2026
DEFINITION  M90 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457561465
VERSION     WP_457561465.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Xu,Q., Gohler,A.K., Kosfeld,A., Carlton,D., Chiu,H.J., Klock,H.E.,
            Knuth,M.W., Miller,M.D., Elsliger,M.A., Deacon,A.M., Godzik,A.,
            Lesley,S.A., Jahreis,K. and Wilson,I.A.
  TITLE     The structure of Mlc titration factor A (MtfA/YeeI) reveals a
            prototypical zinc metallopeptidase related to anthrax lethal factor
  JOURNAL   J Bacteriol 194 (11), 2987-2999 (2012)
   PUBMED   22467785
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Gohler,A.K., Staab,A., Gabor,E., Homann,K., Klang,E., Kosfeld,A.,
            Muus,J.E., Wulftange,J.S. and Jahreis,K.
  TITLE     Characterization of MtfA, a novel regulatory output signal protein
            of the glucose-phosphotransferase system in Escherichia coli K-12
  JOURNAL   J Bacteriol 194 (5), 1024-1035 (2012)
   PUBMED   22178967
REFERENCE   3  (residues 1 to 271)
  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 271)
  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 10007100
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..271
                     /product="M90 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32306
     Region          25..267
                     /region_name="MtfA"
                     /note="Mlc titration factor MtfA, regulates ptsG
                     expression [Signal transduction mechanisms]; COG3228"
                     /db_xref="CDD:442461"
ORIGIN      
        1 mdnfknflll lwgaffvfii fqiishfryl qklkklkstp fpknlkkyie nlpqyqklne
       61 kqkrileyki qkflleknfi pvninlndei kiliafyacl psiayidfcy pnlkniyiyp
      121 hpvilknlqn gyvvqeeeii egeatgenvi iswdeakkei hhpnfrnvii hefahqldaa
      181 dgvidgippi etskynewvk imfgeykkfk qktlknrflg kfslidkyaa tneaeffavm
      241 seyyfmkpqi lkkhfpdiyk elknfykief i
//
LOCUS       WP_457561469             419 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Caminibacter pacificus].
ACCESSION   WP_457561469
VERSION     WP_457561469.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45730
     Region          29..369
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkkfvlalfv ivsllsares qqtrlaayek fvkvvnmiea yyvddinttt iinkalkgll
       61 peldahssyl dkkaykelki stngefgglg ivvgmkngvl tiispiddtp aykaglkagd
      121 iilkindkat idmsldeavn lmrgkpgtki tltivrkgqk pftvtitrai ikvksvkakd
      181 lenypkikyi rissfdknvv pslkkilanl knegkegiii dlrnnpggll nqavgtldlf
      241 idkgilvsqk grvksenevy yahsagtykn vpivvlvngg sasaseivsg slqdhkraii
      301 vgettfgkgs vqailpvnkd eairltvary ylpsgrtiqa kgvtpnivvh pakiqkeese
      361 elikeanlka hlkaelakie hkktkkenpk nlqkidgdlq lltgadilka liiqneskk
//
LOCUS       WP_457561473             499 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457561473
VERSION     WP_457561473.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Scheurwater,E., Reid,C.W. and Clarke,A.J.
  TITLE     Lytic transglycosylases: bacterial space-making autolysins
  JOURNAL   Int J Biochem Cell Biol 40 (4), 586-591 (2008)
   PUBMED   17468031
REFERENCE   2  (residues 1 to 499)
  AUTHORS   van Asselt,E.J., Thunnissen,A.M. and Dijkstra,B.W.
  TITLE     High resolution crystal structures of the Escherichia coli lytic
            transglycosylase Slt70 and its complex with a peptidoglycan
            fragment
  JOURNAL   J Mol Biol 291 (4), 877-898 (1999)
   PUBMED   10452894
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     'Holy' proteins. II: The soluble lytic transglycosylase
  JOURNAL   Curr Opin Struct Biol 4 (6), 810-813 (1994)
   PUBMED   7712284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12989934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..499
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /EC_number="4.2.2.n1"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008932 - lytic endotransglycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=59331
     Region          340..482
                     /region_name="Slt70-like"
                     /note="70kDa soluble lytic transglycosylase (Slt70) and
                     similar proteins; cd13401"
                     /db_xref="CDD:381604"
     Site            order(365,374,376,378,383..385,412,430..434,464)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381604"
ORIGIN      
        1 mkkllflipl flfaydvnlt nllvkpksyv rdfyltefik etnssslafk ayhalykkrm
       61 khlkilskfd ffkpmyqcvn psrkdirnid iacildnglw lssmaklspk dlsylysklp
      121 egkekeavwa flnhnyskif knrdlgyyfi lnypskvidq eindfspfyd kyfhlfvksa
      181 vkhdlpkiqi slnkipykrf gdktkwwlfv dalslgnekr avkilksvek kkskhyfwlw
      241 rltkkdkyld kllnnprvdf ytlyaheekn ipfdirhkvv yntiknpkyv qtdpwdvlkf
      301 wdefrkrrdl ykfakeldsq ksealkalvl dkahhyrvny fitpkmysdq nksfqafvya
      361 iarqesrfip asvsssyalg tmqimpflvr amkgdvfgqf dynqnvrlgv khlkwlfskl
      421 hnplmvayay nggigfvkrr vipvfkykgk yepflsmekv lfdesreygk kvlanyviys
      481 yifgeknvtl hellgktkk
//
LOCUS       WP_457561485             381 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Caminibacter pacificus].
ACCESSION   WP_457561485
VERSION     WP_457561485.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..381
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43202
     Region          46..354
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkksklqkff ekladllhwe ksskpevdls peiwselkpf rtpiiltili elfgtlgyiw
       61 idhfslldai yqtgitfttv gfgeiapisp lgrlftifli iagfavfsya vgvlvdvink
      121 grliallkek rmlykiarlk nhmvicyhne ytidvtkelr aahipfvvid nrddmeeiak
      181 kykypyfvkg dphttlslkk ahlssakgvi tlsnntpdni avvssvrlye kdikrhpyyi
      241 lsvaqsdedi eklkrlgane vlsptkliak rmtavtvdpd vknileefvy sldtpldlee
      301 itvskkswia ykklkeahlr elfnvtvvgi keeggkfipi pkgddvikpg dvllvigtak
      361 dmkkarkiir stkkpkeldf i
//
LOCUS       WP_457561488             277 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caminibacter pacificus].
ACCESSION   WP_457561488
VERSION     WP_457561488.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..277
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31303
     Region          35..271
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkklkpfika afiliafiii fqkiniqelk nikitspfyl flaflsfnls qiisalrvhm
       61 ylknikvtpt fkkqlmlyyv gmfyntllpg giggdaykay kfeksysqgy kkiikallid
      121 risglfaifi lisaliflss fkqfvifsai llivspfily flhkyffvef tksflknlfl
      181 siviqslqal aflfilfaln ihshlidfiv lffissiisv ipisvggvgl reltflygld
      241 mlhlnatigv vaaflffvis vissaigalf ikgvknv
//
LOCUS       WP_457561489             315 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457561489
VERSION     WP_457561489.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..315
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35696
     Region          5..180
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,90)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(39,89..90)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            88..90
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mklsvvvplm neednikyli eevdkalkdf dyelilvddg stdntveeik khmndktklv
       61 ilnrnygqts amaagievas gdiivtidgd lqndpsdipm mveklnegyd vvagirakrk
      121 depfrkflsk iankiirkvt gvhitdygct lkvfkkdvak nlqlygelhr fipilaemyg
      181 akitevpvkh herkfgksky gfnrtfkvis dlmylvfmqr fgqkpmhffg tvgfimfslg
      241 vlidfyllil klfgqniggr plltlgtmli lggiqlittg flaeimirty yesqgkkpyv
      301 ikeivtkdsq mrves
//
LOCUS       WP_457561495             261 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561495
VERSION     WP_457561495.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..261
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30235
     Region          146..253
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mkeilkeiie keaddliryw veefpeeerd eearyyedfl sffeecvekd ldihapesea
       61 lktflekiie ilgedrffnf knsvytcylk fpimkkleek nafeygiikk ltvffealts
      121 riiidllkkn eqvtmsamne leereapiae iwdgvlmlsi vgtldsnrvl kiidkilekl
      181 dkreiehvvv digaihdmns evarqiikln naihfmgsna yltgitpaia kslthldikl
      241 gdiktfsttk kamehilhge i
//
LOCUS       WP_457561471             481 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457561471
VERSION     WP_457561471.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Draper,J., Karplus,K. and Ottemann,K.M.
  TITLE     Identification of a chemoreceptor zinc-binding domain common to
            cytoplasmic bacterial chemoreceptors
  JOURNAL   J Bacteriol 193 (17), 4338-4345 (2011)
   PUBMED   21725005
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..481
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55500
     Region          <4..343
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          355..422
                     /region_name="CZB"
                     /note="Chemoreceptor zinc-binding domain; pfam13682"
                     /db_xref="CDD:433401"
ORIGIN      
        1 mnrvvitail vivaaylvfk geyigaigal lplvfvwwpk kevknentld kiqnvvekay
       61 ngeiyhriil dddktkeeki gwhinemldq iedllresqn tikaiiegkd yryilpsglh
      121 gefrnvayef ekaieslkis kkvelianlg krftqidggv penlrrvges iykiddsfke
      181 ialkvknssk qadetyyimq eskndfeels qkvmetssei eqmasqissi sdivelikdi
      241 adqtnllaln aaieaarage hgrgfavvad nvrelaektq katneiaiti qtlqqqfmni
      301 sdntskvvqi seksyktlen fenlldilqr elldvsnisd intlklifit fklhhiiyks
      361 nvyssvtreh vedflldina encmlgkwle ipeikeilik tkyygrfkky heeihnigqe
      421 vllrvkkegv trenedwyyd klvelekyak llfeefekfv etakeenlle qildaskkik
      481 i
//
LOCUS       WP_457561506             211 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457561506
VERSION     WP_457561506.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..211
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24761
     Region          11..209
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mieklkkisl ffniedkile eissfshlkk ynpdeiifye gekdkyfygi vtgsvlmydi
       61 dlkgniipkn qfgcgdifgl isqiqnreyc lsaksesdse iiridytkfq kfisnppfsd
      121 riikmlsnqi lqemefnklq kydatkrlvy allnfpkkfi rkkkyllake lnmspetlsr
      181 ilsklrneei icyceksikv ldeeklknll s
//
LOCUS       WP_457561507             417 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Caminibacter pacificus].
ACCESSION   WP_457561507
VERSION     WP_457561507.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 417)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..417
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45968
     Region          20..416
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 mvkvgivgvg tvgvsvvknl eknreiiksr agkeikvikg vvrdpnkkrd vnielvtdyk
       61 evtrdpqidi vvelmggvdk ayevvkdaln hgkavvtank allayhrfel qkiantpfey
      121 easvaggipv ikalrdglsa nhieeikgii ngtcnyilte mkkgrdyeev lkeaqekgya
      181 eadptfdvgg fdaahkllil asiaynidak peeiliegie ninltdiefa kefgyeikll
      241 giakkignei elrvhptlik keemiakvdg vmnavsvigd vvgetmyygp gaggdatasa
      301 visdiieiar gcikpmlgfk ipleldnvtl kpideiesky ylrvavndev gvlekiahil
      361 aknnisiesf lqkprngyvk llfsthkcke keikkaikei qelsfvlkpi nyiriee
//
LOCUS       WP_457561510             221 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561510
VERSION     WP_457561510.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..221
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24790
     Region          1..214
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mivygkrive yiiqkhpdiv keiliakkls knelkkfnkf kvklidnkta qklskngnhq
       61 gffakidftp qewditgdki lvlenvtdmg nigaitrtay algidlliit gikelkwdrv
      121 irtssgaald mkilpfknil ellnilktkk yhligadlgg kckpskkeki alimgnegeg
      181 lskrvkekld eiltiemkre fdslnvsvaa gilidritne c
//
LOCUS       WP_457561511              84 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA recognition motif domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457561511
VERSION     WP_457561511.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Muto,Y. and Yokoyama,S.
  TITLE     Structural insight into RNA recognition motifs: versatile molecular
            Lego building blocks for biological systems
  JOURNAL   Wiley Interdiscip Rev RNA 3 (2), 229-246 (2012)
   PUBMED   22278943
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Clery,A., Blatter,M. and Allain,F.H.
  TITLE     RNA recognition motifs: boring? Not quite
  JOURNAL   Curr Opin Struct Biol 18 (3), 290-298 (2008)
   PUBMED   18515081
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Maris,C., Dominguez,C. and Allain,F.H.
  TITLE     The RNA recognition motif, a plastic RNA-binding platform to
            regulate post-transcriptional gene expression
  JOURNAL   FEBS J 272 (9), 2118-2131 (2005)
   PUBMED   15853797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..84
                     /product="RNA recognition motif domain-containing protein"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=9350
     Region          1..82
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mktiyvgnin ydataedlrp ifaeygevls vkiindretg rskgfgfvem esgaetaiee
       61 ldgkeflgrr lrvnearpra pres
//
LOCUS       WP_457561515             292 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Caminibacter pacificus].
ACCESSION   WP_457561515
VERSION     WP_457561515.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..292
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32514
     Region          1..292
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mitvigiyif ivigffakki fkeeiegktl vilstyflqp fltlwgimlv plnfdliisp
       61 vvylgavfis liftsllafl flkdkkekii asltplignt gnlgiplsya lfgdigasia
      121 tmvnlaniff iysfgifffa kgeysfkdaf kkivkipvmw fgilalilni ggvrfpadim
      181 kilqmgafas ivvqllifgi yvaeikakev sfklslvtti nkflvfplis yfllkfchlk
      241 pifhqavlle vltplavtnv nlaalfnlyp qkvaylvilt silfigvimi fl
//
LOCUS       WP_457561518             238 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdate ABC transporter substrate-binding protein [Caminibacter
            pacificus].
ACCESSION   WP_457561518
VERSION     WP_457561518.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 238)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (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   4  (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   5  (residues 1 to 238)
  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   6  (residues 1 to 238)
  AUTHORS   Self,W.T., Grunden,A.M., Hasona,A. and Shanmugam,K.T.
  TITLE     Molybdate transport
  JOURNAL   Res Microbiol 152 (3-4), 311-321 (2001)
   PUBMED   11421278
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   9  (residues 1 to 238)
  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 11432494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..238
                     /product="molybdate ABC transporter substrate-binding
                     protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0015412 - ABC-type molybdate transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0030973 - molybdate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26721
     Region          4..238
                     /region_name="ModA"
                     /note="ABC-type molybdate transport system, periplasmic
                     Mo-binding protein ModA [Inorganic ion transport and
                     metabolism]; COG0725"
                     /db_xref="CDD:440489"
ORIGIN      
        1 mkkiflilla kiifaqtlii ysgitmkypi kemaakfekm ypglkvktlf gksgalykkm
       61 tamkkcdiyf pgsvkfinkn pkifldtaki gentlviivk kgnpkkiksl dslinpeisv
      121 vigspnssvg vktkevlskk gkrfyeilsn kaivaytsne ivanvisnad sglnwkgvvf
      181 wknykqyvdi ipidkkysps sdlvmgvtqf apnmimakrf lkfaksyegq kimrkwgf
//
LOCUS       WP_457561520              97 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Caminibacter pacificus].
ACCESSION   WP_457561520
VERSION     WP_457561520.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=11003
     Region          4..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnirvlkalk ekyqeegfli kgvvgsfarg ekfndidivy eidekfvery ggfggmirie
       61 nikseleksl gfkvdlials gmsksakkym lrdikyv
//
LOCUS       WP_457561521             108 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457561521
VERSION     WP_457561521.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..108
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12571
     Region          3..98
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 myekidfile mienieniik rhngivkale dfegqmaifm glaqigevln klpndfiien
       61 nlqeekngay ytrnyivhdy egvdlliver ilryslpelk nkllkakk
//
LOCUS       WP_457561522             678 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561522
VERSION     WP_457561522.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=77161
     Region          3..675
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtsvctycgv gceieaiven nrvtkikpvk ngissggelc ikgrygfefl nnrlkehlis
       61 yefikknaek mpfelqvrla nlyewdekfy kaplnlaldi aawklkdiie khspksiaai
      121 ggartniesa wlfqhfarni lktphvdnca rvchspslsg lkmsigegas svdfdsifda
      181 etifvigsnt teahpmvasr iikakkrgak livvdvreip lmkfadisvi lpfesnllfl
      241 naiakemier dlidkdfink rcvkfdeyke lmlndkydkh ffeklkgfek ikeqieeiak
      301 litkktifaw glgvtehidg teavnaisnl ammsgnfakg agvlplrgqn nvqgacdvgc
      361 lpyflpdyir pdeehiglmt pdvideilng nikaiinmge dilhihpnqn kihkafeele
      421 flmvmevmpn eitkradivf avksayeksg vyvnaerrlh lstplvkssl pddweiikel
      481 anrfggtlky eksedvfedc kkevgrfrga syerlkqkpl qwpikedgsd spvlhlekfs
      541 tsdgkghfhy hkyhlrgeve dilkgkkrww lntgralpqy nnsaqtkpse kltskydddi
      601 llvneihkne isqkvklrsk ygesaelkvk ftdkvrpytl yttfhfaknk inylfgdead
      661 hkvktarfka veveiinl
//
LOCUS       WP_457561524             658 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Caminibacter pacificus].
ACCESSION   WP_457561524
VERSION     WP_457561524.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 658)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..658
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=76556
     Region          <237..652
                     /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 mriktfifll nlgivgvlsl fiyfiyteqq sktvaviien ikkdlqdssy iaskilnknn
       61 dvyflrpvld rkvakndlir gfvladgnkk lfvsgdvdlk vpennvkkni nditlkdlle
      121 kkafvipikf ykqnkqkvyd lyvfldkdkl ksmfvdlkvk ylvfyfmiis aiffilnymv
      181 qyylinpllr lklyaekkdf epkfipikei ndiknaltqs fkeldtiinn lykssitdfl
      241 tglgnkklll kevekrikkg qkfcllfldl dnfkeindfy ghsvgdalii evanelknfv
      301 ksdevitrig gdefilllnd cdtielnkrl nellkrldkk wiirnyelst sasvgvaiyp
      361 hdgksfdell knadiamyea khrgrnkyvi fntdvkekis keytiktmlq kaieneefel
      421 fyqpkldrnk rvvgcealir wikdgkvvpp gefipvaeks gliyeigkwv ieesakrvke
      481 wesdeilkei slafnvsvvq mrregflndi rniiskikpn vsnleieite svfienkqra
      541 lhllellkrm gfkinlddfg tgyssisvlk efkidilkid ksfvdevlsk egrvyvktii
      601 dmsknlnllt vaegveyqeq fevlkelgvd yfqgylfakp lkkeefeefv kklntskf
//
LOCUS       WP_457561526             315 aa            linear   BCT 27-JAN-2026
DEFINITION  chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457561526
VERSION     WP_457561526.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 315)
  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 10002869
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..315
                     /product="chemotaxis protein"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=35521
     Region          6..169
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
     Region          186..297
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(290..293,295)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381151"
ORIGIN      
        1 mddktlkvgs nelelvdfrl fkkesdgtiy egvyginvak vreiikmpel telpgsedyi
       61 egifdlrgiv vpvvdlakwm ginvpsedea pikkrviite fnniligfiv hdakrirris
      121 wsdiepasfs aaqgkldrsk itgitriedg eillildles iveemgffes nldieedkle
      181 kfsgivllvd dsptarriek ealekmgfev ieatngeegl qkleelyaly genlkeklkl
      241 ilsdiempkm dgyhmaarih qdnrfnsipl ifsssisdaf sdirgkevga egylvkfdps
      301 kfytkiaevl keykg
//
LOCUS       WP_457561527             792 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator [Caminibacter
            pacificus].
ACCESSION   WP_457561527
VERSION     WP_457561527.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 792)
  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 792)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 792)
  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   5  (residues 1 to 792)
  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   6  (residues 1 to 792)
  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   7  (residues 1 to 792)
  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   8  (residues 1 to 792)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   9  (residues 1 to 792)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..792
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=89311
     Region          2..645
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          673..789
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mddmmelled flveafemie emdqdliele nnpddldlln kifrvahtik gsgsflnfdk
       61 lthlthhmea vldkarkgel ritpeimdvi lesvdamkai leyirdhged sspdveiesi
      121 vkkldaivng emvpadeege keaseqksns klenisieni ddidvselsp eeldavlekl
      181 vedintppee saqneeksqs eekpqeieek neekneekka pvqksqskpa nkenkpvske
      241 eqkkeikkql vstkeqtirv dvkrldqlmn ligelvlakn rlikiyndve eryegekfle
      301 elnqvvssis ivttdlqiav mktrmlpigk vfnkfprlvr dlsrelgkkv kliiegeete
      361 ldksiieeig dplvhmirna vdhgieppee rrkkgkpeeg tiwlkayneg nmivieikdd
      421 gkgmdpeilk kkaiekgiit pqeaenmsdk eafmlifkpg fstaekvtnv sgrgvgmdvv
      481 ktnieqlngi ieidsvpgkg ttiklkiplt laiiqallva sqedlfavpl snvietvriv
      541 eediytiegk svlklrdevl plvnmadife iekilepeky lyvvilglga tkiglivdrf
      601 igqeeiviks lgeflkglpg iagatirgdg rvtlivdvas lmklakethn kkivteslke
      661 akkkkekpsd yvvmivddsa mdrkimrqal eelgvtikea kdgvealnml kqndvdamli
      721 diemprmdgy tlaqeirkyn kyrklpliav tsratkadrv rgvevgmney itkpytkeyl
      781 qnvvkrnlkl eg
//
LOCUS       WP_457561529             278 aa            linear   BCT 27-JAN-2026
DEFINITION  ketopantoate reductase family protein [Caminibacter pacificus].
ACCESSION   WP_457561529
VERSION     WP_457561529.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..278
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31977
     Region          1..262
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkilvigvgg vggylaykli kcnkdvtisa tkktiekikk eglkiidvdk eeivfpktei
       61 kgiydlifvt vksynidnil pliknhsnen trvvpilngi ghfekfenln vkllkaciyi
      121 lsnkkdinvi hkktplfylc veddevvrka fegcdlkvkf sedikkdiwk kylfistfat
      181 lqsyyqkptg wimeqkrdev ekfldeviki akeegvdlsk erekvikqal nipyeskmsm
      241 qidfekgnkt evenltgyla kksdfinqyy lglrngik
//
LOCUS       WP_457561533             102 aa            linear   BCT 27-JAN-2026
DEFINITION  AtpZ/AtpI family protein [Caminibacter pacificus].
ACCESSION   WP_457561533
VERSION     WP_457561533.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Ruhle,T. and Leister,D.
  TITLE     Assembly of F1F0-ATP synthases
  JOURNAL   Biochim Biophys Acta 1847 (9), 849-860 (2015)
   PUBMED   25667968
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Pedersen,P.L.
  TITLE     Transport ATPases into the year 2008: a brief overview related to
            types, structures, functions and roles in health and disease
  JOURNAL   J Bioenerg Biomembr 39 (5-6), 349-355 (2007)
   PUBMED   18175209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..102
                     /product="AtpZ/AtpI family protein"
                     /GO_component="GO:0045259 - proton-transporting ATP
                     synthase complex [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11550
     Region          <19..71
                     /region_name="AtpZ"
                     /note="FoF1-type ATP synthase AtpZ/Atp1/AtpQ subunit,
                     putative Ca2+/Mg2+ transporter [Energy production and
                     conversion]; COG5336"
                     /db_xref="CDD:444120"
ORIGIN      
        1 mdvekkgrvg ksvwgaekls lgisivvail mgiglgiwmk nlfhqawllw lgvfwgvaaa
       61 imnirieykk lkkeleeaak dpkyknykik keeddildef gk
//
LOCUS       WP_457561539             164 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caminibacter pacificus].
ACCESSION   WP_457561539
VERSION     WP_457561539.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..164
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17035
     Region          1..>51
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mrkaftmiel ifvivilgil aavalpkflg vaqqaheanl ksfvgtlnrs vgptvwskai
       61 ssdgtgsvaa lkgedqnlss yvdipkefgt dadanltqyc nsssqfqail eanesvagkn
      121 yvvvcrdgns snslkfgllk vnslsgvtlg stvnggecia gecq
//
LOCUS       WP_457561540             144 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caminibacter pacificus].
ACCESSION   WP_457561540
VERSION     WP_457561540.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..144
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15533
     Region          1..>58
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkkaftmmel ifvivvigil aavalprlft gvsdaklaka ktqiatirsg iaslysknil
       61 agdsdkcpql easkndgkvf ekvvqggipe nqndvkwvfd nnstteinyt lkidnlegnf
      121 tyelnaslgc pfkcvngalc nklq
//
LOCUS       WP_457561542             497 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Caminibacter pacificus].
ACCESSION   WP_457561542
VERSION     WP_457561542.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..497
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53851
     Region          8..475
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mfskilqnyn akntkndila givvsvalip eviafsfvag vspivglyta filgliaaaf
       61 ggkpgmisga agsvavvvva lvqkygveyl ylaailagii qlligilgfa kfirlvpmpv
      121 vygfvnglai viaysqfqff kgesyiiyil valtmaimyf lpkftkaipa glgaiivita
      181 ivwgfhlhtk tigdlahikg afptfhwpdv plnletlkii lpysivmalv glieslltle
      241 vleemsgerg ngnkeakalg agnalsgmfg gmagcamigq tiinhtsggr grlsgitaav
      301 liilfvvffs kyiekiplav ligimfmvsi atfewasldk lkripkedaf vlivttliti
      361 ftdlavavis gviisalvfa wkhakvyfkt kmegdkkiye fegplffgst rsflesfdvk
      421 ndpkkvvmdf knvrvmdasg veaidkitkk yleagkklti rhlsneckkl levagpycty
      481 eeddpnykva idpeklk
//
LOCUS       WP_457561543             395 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457561543
VERSION     WP_457561543.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46028
     Region          76..389
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkktaflipv flfanqnils dlklkllnld eqrsiysake tqkswinpii lqysisqnns
       61 lhttkqniqt fsvsinqpif ktgaiyysik yaknlknynl kqielqkral ikqayelvyd
      121 ykinklneei allniqnaki dvkkkkedfl ngtgdstfln qaiinlnnik lgyedlkfne
      181 kqlkfsfknl sdldiekvkl pyfkiisknd finnnlqlis skindkikyd lykmqlgnql
      241 ltisfnasyn yqitdytnet skyhddsnny ynvglsvtlp idftstdkvk qtklsyiksr
      301 yetldtkrnl lntyamiisq iktlqkkkei ykenekayan liestkesik agnatvldle
      361 ilensykvmq inqkiidlqi qklllnlyyq vtskf
//
LOCUS       WP_457561548             179 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561548
VERSION     WP_457561548.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..179
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=20511
     Region          22..>139
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 maatpkvtpl wkeatfqseg ldaralitrt dlkgiitfas layrkmtkfr kedlvgnphs
       61 vvrhpfmpea afrdmwdtie rgehwngmvm nlrkdgkhyw vdvhvdpide ngnivndpsk
      121 iagyvavrre ptrkevqeay klykgmrkae llakstlknw erdlldildk lpesadafl
//
LOCUS       WP_457561552             298 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Caminibacter
            pacificus].
ACCESSION   WP_457561552
VERSION     WP_457561552.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..298
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33214
     Region          26..287
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mslprlatvv atltalvlav akvvvgfmsg svaviasald sildmvisif nniavrvses
       61 kpdhkfnygk gkieglaalf eglfisasgl fiiyegirki ihheaitein isiyvmlfsm
      121 latlalvlfl ayvvkktnhl viksdllhyk tdlltngavl vslivvkltg wyyidfilsi
      181 ligiyiikea seivkegfei lldvsldfet vekikeiikk eplvldyhcl rtrkagnrnf
      241 vdvhlvltpd mklklahtii envedkirai dpdkkwiini hadpyddshi nklleece
//
LOCUS       WP_457561558             108 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydroneopterin aldolase [Caminibacter pacificus].
ACCESSION   WP_457561558
VERSION     WP_457561558.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..108
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12495
     Region          1..103
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mykiviedls fkailgllek ernqeqlvvv caqieyedkk nfidyakvcd fiqniiiegk
       61 faliedaidv iieklknefp qmksihlkir kpeilknalv gvetlrkf
//
LOCUS       WP_457561559             487 aa            linear   BCT 27-JAN-2026
DEFINITION  Ppx/GppA phosphatase family protein [Caminibacter pacificus].
ACCESSION   WP_457561559
VERSION     WP_457561559.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Kristensen,O., Laurberg,M., Liljas,A., Kastrup,J.S. and Gajhede,M.
  TITLE     Structural characterization of the stringent response related
            exopolyphosphatase/guanosine pentaphosphate phosphohydrolase
            protein family
  JOURNAL   Biochemistry 43 (28), 8894-8900 (2004)
   PUBMED   15248747
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..487
                     /product="Ppx/GppA phosphatase family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55599
     Region          6..304
                     /region_name="GppA"
                     /note="Exopolyphosphatase/pppGpp-phosphohydrolase
                     [Nucleotide transport and metabolism, Signal transduction
                     mechanisms]; COG0248"
                     /db_xref="CDD:440018"
ORIGIN      
        1 makvtavidi gsnsarmavf kktsrfgfyl lraekskvri segayenggn lqdfaierai
       61 kalrefllia kslktrkilc vatsavrdap nkaeflkrvk delglkikvi dgdkeafygg
      121 vaaanllyek ngvtidiggg stefalivdk rieatislkl gtvrlkelff dkgdiegakt
      181 yikneleklg kvfdskkvfg iggtiralsq aimkkieypl dilhgftyei kehkdfleki
      241 ikmsdeellk agikperldv irpgtlifle alkylgakev itsgvgvreg vfltdllrnd
      301 nyrfpdnfnp svrtiidvyq idrkiasyet kialevfdll kdefklddky kmhltyaikl
      361 sragelvdfy eahkhtdyil lnslhygfrh cdrlliskii rfhkrkkikk keiekfkcll
      421 pkkdiveklc nifwvaklin inlsmpqvei tfskkdkkii ikgenlylak ersktrelff
      481 dleivnk
//
LOCUS       WP_457561561             433 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457561561
VERSION     WP_457561561.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..433
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46299
     Region          2..390
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrkigfleaf sigvggmvgg gifavlglti dlakgaapia fliagtiali taysyaklsv
       61 kfpseggsie yivqafgnnl fsatvnnlll vsyvimlaly asafgaygsa lflghdvtwl
      121 hkllavgvig ifafinllga fltgkaedil vytkvailli fvaigfytgt hyerlepqfw
      181 esylkiitgg liiflayegf eliansakdv inpqktlpra fyasvifvit lyvsiavvti
      241 lnvdfetakk aqdyvlaiaa epllgklgfv iiavaamlst asainatiyg agragyliak
      301 lgeipkdfak kikngyegmi ilgllgvifa tsfnienisv agsfgflvif glvnyanfkl
      361 rkitnsnpfi sllgaflclv saailigynl fhnpsaless awvvvivvai tiiyhklggk
      421 mkkvldedlr eki
//
LOCUS       WP_457561563             173 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine phosphate synthase [Caminibacter pacificus].
ACCESSION   WP_457561563
VERSION     WP_457561563.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Peapus,D.H., Chiu,H.J., Campobasso,N., Reddick,J.J., Begley,T.P.
            and Ealick,S.E.
  TITLE     Structural characterization of the enzyme-substrate,
            enzyme-intermediate, and enzyme-product complexes of thiamin
            phosphate synthase
  JOURNAL   Biochemistry 40 (34), 10103-10114 (2001)
   PUBMED   11513589
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Reddick,J.J., Nicewonger,R. and Begley,T.P.
  TITLE     Mechanistic studies on thiamin phosphate synthase: evidence for a
            dissociative mechanism
  JOURNAL   Biochemistry 40 (34), 10095-10102 (2001)
   PUBMED   11513588
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Begley,T.P., Downs,D.M., Ealick,S.E., McLafferty,F.W., Van
            Loon,A.P., Taylor,S., Campobasso,N., Chiu,H.J., Kinsland,C.,
            Reddick,J.J. and Xi,J.
  TITLE     Thiamin biosynthesis in prokaryotes
  JOURNAL   Arch Microbiol 171 (5), 293-300 (1999)
   PUBMED   10382260
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..173
                     /product="thiamine phosphate synthase"
                     /EC_number="2.5.1.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004789 - thiamine-phosphate
                     diphosphorylase activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19782
     Region          1..172
                     /region_name="ThiE"
                     /note="Thiamine monophosphate synthase [Coenzyme transport
                     and metabolism]; COG0352"
                     /db_xref="CDD:440121"
ORIGIN      
        1 masflsyfit dpsyslqqik eaikkhkptf vcyrnkeyfd kneimdfanf akkyskvfin
       61 ldslkddsll ehfegvhips srldeiteyk nkiiiasthn plevqkaqka dyitfspifk
      121 sknrcglgte vlnhicnmhp kvialggiis dkevekiknt kavgfgsiry fft
//
LOCUS       WP_457561568             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Caminibacter pacificus].
ACCESSION   WP_457561568
VERSION     WP_457561568.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46600
     Region          4..376
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(11..12,15..16,19,52,102..103,105..107,110,132,
                     135..136,139,205,208..209,212..214,217,245,249,295..296,
                     300,304,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 miylsllmai rflglfivmp vlalyamhlk gasefsvgva lgayalsqvf lqiqfgklad
       61 rydkkkilif glfllflgsl vcafsdniyt lifgrllqga gaiggvilay msdlsdenkr
      121 akifarmgqf ialsfaismi lgptigtkwg vdklflltai lalvsiylvi akvppapkiv
      181 hhtdskvslk difahkellk lffsgfmqkg lmsvffllip lvftqtfhwe ktslwkvyip
      241 alvfgffalp lgailaekkg kgkavfiisa lsitlalilf liglntqnyl falvgvivff
      301 fgfnllepvl qsfvskvaya nqkatalsts ntiqylgifl ggavagyfmk hgmlksflii
      361 siiiaslwvf alikmkpvkk fkiveytefd kdfieelkte knvydfyeke gvlivryid
//
LOCUS       WP_457561572             287 aa            linear   BCT 27-JAN-2026
DEFINITION  damage-control phosphatase ARMT1 family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561572
VERSION     WP_457561572.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Huang,L., Khusnutdinova,A., Nocek,B., Brown,G., Xu,X., Cui,H.,
            Petit,P., Flick,R., Zallot,R., Balmant,K., Ziemak,M.J.,
            Shanklin,J., de Crecy-Lagard,V., Fiehn,O., Gregory,J.F. 3rd,
            Joachimiak,A., Savchenko,A., Yakunin,A.F. and Hanson,A.D.
  TITLE     A family of metal-dependent phosphatases implicated in metabolite
            damage-control
  JOURNAL   Nat Chem Biol 12 (8), 621-627 (2016)
   PUBMED   27322068
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Perry,J.J., Ballard,G.D., Albert,A.E., Dobrolecki,L.E., Malkas,L.H.
            and Hoelz,D.J.
  TITLE     Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase
            that targets PCNA and is linked to the DNA damage response
  JOURNAL   Cell Rep 10 (8), 1288-1296 (2015)
   PUBMED   25732820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..287
                     /product="damage-control phosphatase ARMT1 family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33006
     Region          2..283
                     /region_name="DUF89"
                     /note="House-cleaning carbohydrate phosphatase, DUF89
                     family [Defense mechanisms]; COG1578"
                     /db_xref="CDD:441186"
ORIGIN      
        1 mhiskecylc iynqvfkite rlnlddekas evlrvgakil skydlsympp viaadvykki
       61 seilgiedlf ekekkeaike alkfkeilek rikkskdplf daakisvagn vidlgvhqey
      121 nlekeiknif emkffkndfn efreklknak tlcyladnag envfdeifik eikrfnpeiq
      181 vfyfvrgkpi indvtlkdle gleiwdlaev vdsgvptpgf cipfankkak difqtsdlvi
      241 skgmgnfecl fgecerevfy fskikcnvva rasksklgey miykgek
//
LOCUS       WP_457561575             790 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457561575
VERSION     WP_457561575.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 790)
  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 790)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   3  (residues 1 to 790)
  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   4  (residues 1 to 790)
  AUTHORS   Borziak,K. and Zhulin,I.B.
  TITLE     FIST: a sensory domain for diverse signal transduction pathways in
            prokaryotes and ubiquitin signaling in eukaryotes
  JOURNAL   Bioinformatics 23 (19), 2518-2521 (2007)
   PUBMED   17855421
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   7  (residues 1 to 790)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   8  (residues 1 to 790)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   9  (residues 1 to 790)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 790)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 790)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 790)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 790)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 790)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18684138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..790
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=91155
     Region          29..357
                     /region_name="FIST"
                     /note="FIST domain protein MJ1623, contains FIST_N and
                     FIST_C domains [Signal transduction mechanisms]; COG3287"
                     /db_xref="CDD:442517"
     Region          <407..786
                     /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 mkqysctfde knikeiyekt kdlnyktllv qvysgvviks yilnvvstvk eyfpnakivg
       61 ittdgeiids kitqnnvvvs fsffeksdie ivffeknnlf edgkklaska kkdtkllmif
      121 asgiefnadd lieginflnp slpvigslag dnakfkktyi fydekiskng vlgvyfnsev
      181 levyidssfg wvkfgrrmki tksdknivye ideqeafdvy syylgneikk yfpkigvefp
      241 liktvnnldv aravvgvrdk alifagalne gdivnfgiae askvlesskr vfqkllrnki
      301 ealfvfscma rrrfveklsf lelqmlknip ntgffgygef fngrflnqtl nvlalseggd
      361 lenkelyipk ndkvttiesl ihlvdvafne vrqklyidnv tklpnkaafd edvlrnpyga
      421 vlfdikkfss indkygevvg devlknlaki lqrfiiknak lyrisadyfi vlffeecnlg
      481 mfaysvieyf ynnplkikik deeyeidldl yaalvegveg rkikikadma lhyakvtken
      541 ivkyskdlki eekinkeiet lnfvkkaime nrvipvfqmi qkddlsfeal vriidedgkl
      601 vspfyfldsi kntryydeit rimieksfki fqdlphklsi nfsyediqne ktveflissi
      661 ekynmqnrvi ievletdsis eydvfenfvk kvkkygveia iddfgsgysn fiylanikpd
      721 yikidgslik sldenekfyk ivktivefak emdirviaef vkdekiyeic kklgidgmqg
      781 yfihipskdi
//
LOCUS       WP_457561577             451 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter substrate-binding domain-containing diguanylate cyclase
            [Caminibacter pacificus].
ACCESSION   WP_457561577
VERSION     WP_457561577.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 451)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   8  (residues 1 to 451)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10098929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..451
                     /product="transporter substrate-binding domain-containing
                     diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52148
     Region          29..246
                     /region_name="PBP2_BvgS_HisK_like"
                     /note="The type 2 periplasmic ligand-binding protein
                     domain of the sensor-kinase BvgS and histidine kinase
                     receptors, and related proteins; cd01007"
                     /db_xref="CDD:270228"
     Region          <292..449
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mrfliffvli kllfavdlns tqreylntrv fniatttkwe pfnteidgkl vgiavdywkl
       61 iakktginyk flikptwiev lqaieygdad lalgagktke rekyavftkp yvtfplviat
      121 rndvgfipni tflrnkiiav gkgytaeall kknypnlnvi svpsidealk mvkegkvyaa
      181 idilpvisyk inkyqydnlk isgqldikfp vrfminknek elvpiinkai deitfderen
      241 iykkwitaqk skpnyfqivi iiilaaiivm liiwvvklki klkyeheyei mleklasydk
      301 ltgiynrqkl eeflemfasv yqinnepfsv iffdvdnfkk inddfghqvg divlveissi
      361 iqssirkrdi fgrwggeefm iilenckide acniaenirr kiethnfgmn rpvtcsfgvs
      421 eyaggdlkyf llevdeklyk akregknrvi c
//
LOCUS       WP_457561583             347 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caminibacter
            pacificus].
ACCESSION   WP_457561583
VERSION     WP_457561583.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..347
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37776
     Region          21..344
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkkllalals vgalfafeya takketvnit rdyvanvysp kqvmvatrlm gyiksmpvee
       61 gdvvkkgqvl fevdpadiys mlnqargavl qaksgvlmae mayadalkdy erfknlykng
      121 avskrdfekm tlmknirkkq vdmakgmlkq aeaglaraea qlkyakvtsp idgvvtmkmk
      181 kvaemalpgy pvvilsdihv lkakstvkes didkfkvgmp vniyvpalkk tfpakvstii
      241 pagdnmthsf vikytfenhq gllpgmyaka kvvvgkqeav vvpfsalttr agivgvfvnd
      301 ngvarfvpvk qvgqvgdnia vtgleggeev ilyppanled gqkieeq
//
LOCUS       WP_457561588             335 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561588
VERSION     WP_457561588.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 335)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..335
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38959
     Region          <161..326
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtekdskfss ieardlneav splekfakkv fdklieegvp plpyyyriyf fnmlddedin
       61 frkhiyemia veesnenekd felerklkls fkyskellqr tamiyknant ikellnkyad
      121 eisfiaspka lektlkqfea kletinkkld lelnevkkly sknievlkei esnsmfdqry
      181 gvynkkyflk ivqkeiklid kfshvssvvt ikikdeilrq lknekniila nrsvskiilk
      241 tsrrtdtvah lgegifamll kntdrigask tierlsdmis tasvffegee veiqivggvv
      301 eikdkkdake yvenainvmr eaeeegmlyk vyege
//
LOCUS       WP_457561591             385 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457561591
VERSION     WP_457561591.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..385
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44490
     Region          2..384
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 myfiyekdal grtifeivfk ntgsiyakda vaymtahiln tkgtldkkek fysqleekai
       61 nltittnkef stvsmtflne kssfavkkli ellqnpnftq ealvkskkei lakkenlknn
      121 hdyiasknlf kaifkntple retigeniqn vtledikehf syfakenavf inggkkidia
      181 efietlpntk pkndlffkpk qshieekrev eqsyiyfaap fevkkeeyyl akiatfilga
      241 ggfgsrmmee irvkrgyays ayamnefkks yqilkghlqt klentidakn lvvdiinvfl
      301 ekgitreeld sakkfligse plrnetlsqr llrkfneyyl glgdgyfeke lnliknttld
      361 eindfikrhk eiknlsfsvv tndkn
//
LOCUS       WP_457561608             395 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Caminibacter pacificus].
ACCESSION   WP_457561608
VERSION     WP_457561608.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kasaragod,V.B. and Schindelin,H.
  TITLE     Structural Framework for Metal Incorporation during Molybdenum
            Cofactor Biosynthesis
  JOURNAL   Structure 24 (5), 782-788 (2016)
   PUBMED   27112598
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Nichols,J.D., Xiang,S., Schindelin,H. and Rajagopalan,K.V.
  TITLE     Mutational analysis of Escherichia coli MoeA: two functional
            activities map to the active site cleft
  JOURNAL   Biochemistry 46 (1), 78-86 (2007)
   PUBMED   17198377
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Schwarz,G.
  TITLE     Molybdenum cofactor biosynthesis and deficiency
  JOURNAL   Cell Mol Life Sci 62 (23), 2792-2810 (2005)
   PUBMED   16261263
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Nichols,J. and Rajagopalan,K.V.
  TITLE     Escherichia coli MoeA and MogA. Function in metal incorporation
            step of molybdenum cofactor biosynthesis
  JOURNAL   J Biol Chem 277 (28), 24995-25000 (2002)
   PUBMED   12006571
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Schrag,J.D., Huang,W., Sivaraman,J., Smith,C., Plamondon,J.,
            Larocque,R., Matte,A. and Cygler,M.
  TITLE     The crystal structure of Escherichia coli MoeA, a protein from the
            molybdopterin synthesis pathway
  JOURNAL   J Mol Biol 310 (2), 419-431 (2001)
   PUBMED   11428898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096840
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43589
     Region          9..395
                     /region_name="MoeA"
                     /note="MoeA family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (MoCF), an
                     essential cofactor of a diverse group of redox enzymes.
                     MoCF biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00887"
                     /db_xref="CDD:238452"
     Site            order(29,136,151..154,156,159..160,162,196,198,201,324,
                     363,391)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238452"
     Site            order(179..180,182,221,245)
                     /site_type="active"
                     /note="putative functional site [active]"
                     /db_xref="CDD:238452"
     Site            order(245..247,292..293,297,300)
                     /site_type="active"
                     /note="putative MPT binding site [active]"
                     /db_xref="CDD:238452"
ORIGIN      
        1 mfikvtrnea keiidsltsq kyyetitide aegrvlfedm kakfnipesd ksavdgyain
       61 idnltfpakl kiideapage aqkelkdgai fimtggvvpk ganavvried vekegdyivi
      121 kkpvkkgdli nfegeevktg nvvlkkgeil dykkvallan lghyqikvfk kvkigivvtg
      181 sevkepfeal dkagvknsnl yilkgllkpy adityygklp dnldemvkvf knaieendil
      241 issggaskgk ydftkeiakq igvdikfttt nirpgrplif gnkdkklffg lpgypaallv
      301 naveflipyv kkaagivnyq neykkavltt ktkakegrvd firgniecde kvtftpaytq
      361 qtsnylsial snalaviden egtkeageiv eyili
//
LOCUS       WP_457561609             133 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin synthase catalytic subunit, partial [Caminibacter
            pacificus].
ACCESSION   WP_457561609
VERSION     WP_457561609.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12) (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..133
                     /product="molybdopterin synthase catalytic subunit"
                     /EC_number="2.8.1.12"
                     /GO_component="GO:1990140 - molybdopterin synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
     Region          6..115
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(10,14,19,21..25,27,29,75,84,86,94,98)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(40,42,45,48,52,65,101..102,104,106..108)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(101,108)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
ORIGIN      
        1 pviptlerwy eefklegyga mipfigivrp dneieglsfd lylpmlnewf kkwqnlddak
       61 immahsfgdv mvgetsflca vftkhrregf kyleefvedf kanapiwkyd lkggkrifas
      121 drakelpgag lld
//
LOCUS       WP_457561610             103 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457561610
VERSION     WP_457561610.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..103
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          <1..81
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 kkvfgnqfve giilnlngee kelkvdgvfv fvgmkvnnel vknlvelnew gevkvnlkme
       61 tsqkglyaag diredsvkqv vaaagdgata ainalkyiek eel
//
LOCUS       WP_457561613             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457561613
VERSION     WP_457561613.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 358)
  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 358)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..358
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40430
     Region          161..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrflaimkkd ilillrntal mlfliyiftl diylagigik ikpqhvsvgy vdysnslivn
       61 kilthlhkpe fqtpkrflne ealkkaienk kimvglvfdg dfaknyyktg ksqvnvlids
      121 taaaqaqvtv iylneiltrf vnlhfplsiq thrlfnqnsn stwfmslael isdvvllvll
      181 lvatvfvkek eegtwdimll mpvssiltif akmfsqvvvi lvgvwvsvgl ilfgvfdmpi
      241 ngnlwhffll nllfafslgg iglviaaisn tvtevgqysf mlmmplifls gawtpissma
      301 pwlqklsiis pvryyiease siffrgasfy dlipyfvall iigmvlfyig ykkigrlf
//
LOCUS       WP_457561617             155 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457561617
VERSION     WP_457561617.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..155
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=17605
     Region          41..151
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mnfqewlkkn elslkckprt qrasyieffe gefkgdkipe fkrgevyfak ltdsaktrpf
       61 liyqndylnr acyeglyhtv vvlplsgqil ggdyrvlikk rdnmtrdsei vataigiist
      121 gkiifskglv tkltqeelqk vdsavkkvlg menai
//
LOCUS       WP_457561621             211 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457561621
VERSION     WP_457561621.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..211
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23555
     Region          2..203
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mkiiltgass gigaaikeel knyeiielcr nckhslnlan pgeiknlkfn dvigiihnag
       61 vgyfgqfedi kiekieemin vnflspmilt knhlkdikkn rgfiinisst saihpakmgv
      121 vyaatkaalr hfgnslfeev rksgvkvcni ipdltltnfh nntffkpsse emahlkpqdi
      181 akivkdiins pkhlvmqeiv vkpqyfklek n
//
LOCUS       WP_457561624             394 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Caminibacter pacificus].
ACCESSION   WP_457561624
VERSION     WP_457561624.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..394
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45875
     Region          55..391
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mrdyilqkea eeikfapmms vseflnrkpl fykeidvlrm praynlirnk ikippvihii
       61 gtngkgstgr flahtllkrg ykvghytsph imkfneriwi ngenisdefl eevhqklqkl
      121 lpknvidsls yfeyttflaa lsfegldfvi meaglggefd atnvfekeis lvttidldhq
      181 sflgdniidi attklnsiqn eaiigkqihe dvewvvqkki negkkiykyl dffereeiee
      241 lkkefkfakf lfpnfllams ylkkrgisfs pkdlddlrlp grfeeiekdl widvghnpla
      301 areivkslsk kvnlvyntya dkdyeeilki lkpkinklyl idvkndried kekikktadk
      361 lgidvdefkt ikkpmlvfgs fsvveeflke yygk
//
LOCUS       WP_457561629             728 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457561629
VERSION     WP_457561629.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 728)
  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 728)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..728
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84718
     Region          332..358
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          334..632
                     /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          399..424
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(400..401,404..405,407,431,434..435,438..439,
                     441..442,465,468..469,472..473,476)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          429..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          506..533
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(540,543..544,547..548,550,580,583..584,587..588,
                     615..616,640,643..644,647..648,651)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          540..573
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          578..633
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          603..724
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          638..664
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkglfslfv ifnllfgyel ivknekdvkv lndlgvkcek iangfvcaks pdkmqlkrlq
       61 yylknnlsiv seivgvqekl sdaskpvmsv kpvksaadik tpkkvaknsk tliktgyciq
      121 vvsarksqgl leifdktknl plsriekigp yyvlrigeek nenalqsvlq kakkinknay
      181 irkcdlipqr iiksnfkpka kkkqeikipq gevfnkifsp eeknklmeka fkegriylar
      241 nlsnqlkstn gykkdaflit vnilmqkkey krvcnmltql sdfykgknls eikekscfyy
      301 nyqkgveymn inpeialdfl kkaqkfksdd nllfataiay mnqydykkak eilqklyknd
      361 sdntaiklay aktlfnlgdf ktlerikdnn laffnhlely lkakklyneg kykeaekiav
      421 klfnyypnni nvlllngnif yklgkydlay iyykrvvkke pqnipalkgl rdvalankdi
      481 tsavkisdil knlkykdkkf neimkeyylf qadklaqegk fkdalkdvke aekytdsekd
      541 iylaygkiyf kmgeykkald yyrmlysrna pleireklir iyirlgkink akeiaqnspn
      601 eikaiyymem akylmnqkky peankyista leynpinsmq aheikawicy ylgdyecakr
      661 yfeksdlklp evrigyafvl aklgnknkay liaqgiknes knillqkarl mielgrekea
      721 keifnsid
//
LOCUS       WP_457561630             208 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561630
VERSION     WP_457561630.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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) (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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..208
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23865
     Region          126..>180
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkklaflgvf svlfgyqlgv kaqdaeklrn fgleckpage yciyaigsnk esllkvekyi
       61 rkelgiesyf vnntsdvtne ipsevvsdkt eqtieakqht evntdtssyv eekpietenv
      121 sdideskkyy syqvissprl sdakkayeki knlpyariek ignyyvvrvg lydhyreakk
      181 eglkymitrc fykksriike ndengssy
//
LOCUS       WP_457561631             378 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457561631
VERSION     WP_457561631.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..378
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43182
     Region          3..378
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mrvlivgagi igmtmawewr kkhpddeivi idkepheafh asgknsgvlh agfyyssdsl
       61 kakltargnk lmkefcyshn ipvnetgklv vakneneipt lfelakrsva neagayiitq
      121 eeaekidpna kthkyalysp ntatvnprev crvlkeelqk kdvkfifnmp fekfnesydf
      181 linaaglyad kiahnfgvgl eytmlpfkgl yrkylgedki ktqiypvpni knpflgvhft
      241 lmadntikig ptaipafwre nyvgferfdf refleiisle aklfftnafg frdlalyemr
      301 yyipqnline akklvknlrg efkpmtpgir aqllntqtle lvmdflvekn dnqihilnav
      361 spaftasfaf skyvleel
//
LOCUS       WP_457561633             416 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease, partial [Caminibacter pacificus].
ACCESSION   WP_457561633
VERSION     WP_457561633.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>416
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..369
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mgdlkktigv fsgiaiaigm vmgsglfglp glaidiagak lsllgwlaii lavipmiyif
       61 iklgikfpka gglstyakaa fgdwaefgvv avlsgtfiig ipalaiigge yltklfsisi
      121 elkyffaflf llfatiiniy gvqmaswink islifillli ivlviihpdy ltegikalnf
      181 ktenikinkl wevmallfwa flgwenlsfg leefknpkkt ipiiywgsff ivsmfyfmla
      241 llvsgavisg ikvsgasaia silsdnvtls kfliffmvvv iiananswvf gasrliysag
      301 kdgilfkklg ilnkkgipsn alitlmifya ffifalyyfk idlskiimiv sqnflvlylf
      361 siiafaklfs gtidrivlll ssvillfffq gfgvaiiypl illligfvry kktske
//
LOCUS       WP_457561637             266 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561637
VERSION     WP_457561637.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..266
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=28684
     Region          27..266
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mnqyldlalt wgikiigaia iyiigkwiak lltnlfrkml ersntdvtlv kflgdlvyfg
       61 livlviiaal gtlgvnttsf aaiigaagla vglalqgnia nfgagvvllf lrpfkvgdfv
      121 eaggatgvvd qigifnttfk tgdnriiivp nsniiggnit nysreairri dlvigvgyed
      181 dlklvkstle eilanhpkvl kdpapavala eladssvnfn vrpwvksedy wgvrsellei
      241 ikttfdekgi nipypqmdvh vdnkaa
//
LOCUS       WP_457561600             405 aa            linear   BCT 27-JAN-2026
DEFINITION  L-cysteine desulfidase family protein [Caminibacter pacificus].
ACCESSION   WP_457561600
VERSION     WP_457561600.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Mendez,J., Reimundo,P., Perez-Pascual,D., Navais,R., Gomez,E. and
            Guijarro,J.A.
  TITLE     A novel cdsAB operon is involved in the uptake of L-cysteine and
            participates in the pathogenesis of Yersinia ruckeri
  JOURNAL   J Bacteriol 193 (4), 944-951 (2011)
   PUBMED   21169490
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Tchong,S.I., Xu,H. and White,R.H.
  TITLE     L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from
            Methanocaldococcus jannaschii that catalyzes the breakdown of
            L-cysteine into pyruvate, ammonia, and sulfide
  JOURNAL   Biochemistry 44 (5), 1659-1670 (2005)
   PUBMED   15683250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..405
                     /product="L-cysteine desulfidase family protein"
                     /EC_number="4.4.1.28"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0080146 - L-cysteine desulfhydrase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44413
     Region          5..403
                     /region_name="CdsB"
                     /note="L-cysteine desulfidase YhaM [Amino acid transport
                     and metabolism]; COG3681"
                     /db_xref="CDD:442897"
ORIGIN      
        1 mygakeiils eikpalgcte paavalnaay lreygvydek nlkltvntnl lknamyvpip
       61 ntskrfgvkl afalgylfgd vndglnifkn lneekvkkal efsekvkvel iegselfiks
      121 ensyaeavti kfhdnieyvi skgelkefdn hqeevevksy vledkpfdiv ydlieqeksf
      181 efvreaveln malaeygmnh dvginvskqf sgdslkdkic kittsasdsr mdgvnmpams
      241 ltgsgnhgis atlpvwvyak ekgfseeetl kavalsmlit iyvklfigrl svicgaavas
      301 gcgvagaiay lesdretskk avkhviqnis tllcdggkma cslkvlqgas vgydsakfal
      361 namevyedgi ifedvtktik alkgikekms gvdeevvkim kekll
//
LOCUS       WP_457561643             310 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Caminibacter pacificus].
ACCESSION   WP_457561643
VERSION     WP_457561643.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181086
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..310
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36268
     Region          72..218
                     /region_name="CE4_DAC_u4_5s"
                     /note="Putative catalytic NodB homology domain of
                     uncharacterized bacterial polysaccharide deacetylases
                     which consist of a 5-stranded beta/alpha barrel; cd10973"
                     /db_xref="CDD:213028"
     Site            order(79..80,134,138,174..176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213028"
ORIGIN      
        1 mkklilfllp lwllaeahif vlhriddfrh pytntsskel ekyfkyiksh nykaitlskl
       61 aemiknrqnv dnivvftidd tyksfykngl pvfkkygipf tlfvyvkatn ekwgdfmtwq
      121 qvkdaakyge lgihsyahph lpnlsnqaii ndtkkaieif kkhmgyvpdm yaypygeydq
      181 rvkkiinsff piianqnsga vdiatpindl drialtgkvd iakklkikrl hadikiqreg
      241 nkitlikgkv fdkipyvniy itkmgwvyki pvkngsfsya pnfelkkyrn rviirynyki
      301 iskmvikykk
//
LOCUS       WP_457561647             247 aa            linear   BCT 27-JAN-2026
DEFINITION  Bax inhibitor-1/YccA family protein [Caminibacter pacificus].
ACCESSION   WP_457561647
VERSION     WP_457561647.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Guo,G., Xu,M., Chang,Y., Luyten,T., Seitaj,B., Liu,W., Zhu,P.,
            Bultynck,G., Shi,L., Quick,M. and Liu,Q.
  TITLE     Ion and pH Sensitivity of a TMBIM Ca2+ Channel
  JOURNAL   Structure 27 (6), 1013-1021 (2019)
   PUBMED   30930064
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Watanabe,N. and Lam,E.
  TITLE     Bax Inhibitor-1, a conserved cell death suppressor, is a key
            molecular switch downstream from a variety of biotic and abiotic
            stress signals in plants
  JOURNAL   Int J Mol Sci 10 (7), 3149-3167 (2009)
   PUBMED   19742129
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Zhou,J., Zhu,T., Hu,C., Li,H., Chen,G., Xu,G., Wang,S., Zhou,J. and
            Ma,D.
  TITLE     Comparative genomics and function analysis on BI1 family
  JOURNAL   Comput Biol Chem 32 (3), 159-162 (2008)
   PUBMED   18440869
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Reimers,K., Choi,C.Y., Bucan,V. and Vogt,P.M.
  TITLE     The Bax Inhibitor-1 (BI-1) family in apoptosis and tumorigenesis
  JOURNAL   Curr Mol Med 8 (2), 148-156 (2008)
   PUBMED   18336295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10179639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..247
                     /product="Bax inhibitor-1/YccA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=27166
     Region          35..241
                     /region_name="BI-1-like_bacterial"
                     /note="Bacterial BAX inhibitor (BI)-1/YccA-like proteins;
                     cd10432"
                     /db_xref="CDD:198414"
ORIGIN      
        1 mkfssndfkt nsnintmret ikqnsyqqsh viedinefvk rtyqllagsl iagavgayvg
       61 mgfvgnmvsa tgsltftywg avilefillf glfaaknktp lnlvllfaft fmtgftlspt
      121 lafyisanmg yvigeafflt aiafggltvf amttkrdftt mgkilfitll vvigasilni
      181 flhlpmlqli iasvsailfs ffilydtqni irgnvsseie aavmlyldfl nlfvsllqil
      241 gflnned
//
LOCUS       WP_457561652             143 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561652
VERSION     WP_457561652.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..143
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17010
     Region          8..>142
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mnkryiidee vrfedvnptn rpvvsrtdih gnilyvnsvf anmcgykkee mlgrphriir
       61 hpdmpkkvfe emwetikagk ewqgfvknlr kdgryywvda hispvkkngk ivgyisvrra
      121 vnddikreme rmyaemkene rsf
//
LOCUS       WP_457561653             144 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561653
VERSION     WP_457561653.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..144
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17076
     Region          23..>119
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 msdfnitnem kfldefefln kpiitrtdke gniifanslf skmsgfsrae ylgrphnivr
       61 hpdmpkeife qlwhmiligk awngyiknrt kcgkfywvea fiqpeyengi itgfaslqrr
      121 vsikivrrye kiykemrlke ltrg
//
LOCUS       WP_457561654             344 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Caminibacter
            pacificus].
ACCESSION   WP_457561654
VERSION     WP_457561654.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..344
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37360
     Region          30..333
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mmsakkyfal iaavtavfia flyfspklfn sytlivlgni yifiilavsy nlingvtgqf
       61 slepngfvai gayvtailml spevkeelym laeplplikd vflpnpfltl lisgivaalv
      121 altlafpvfr vrgdylaivt lgfgfiirif linnpeisng smgldsipgf asyfwigiac
      181 lltviliynv vyskygramk avrddedaal amgvntfkik tlafmtsaff egvgggllas
      241 sigaispdqf tfmltfqlli iivlgglgsm sgailgtilv lggmellrpl ddanwhlgsi
      301 hgipglrmvi fsllllliml farrgllgdk eiwdyfklkk ngvk
//
LOCUS       WP_457561655             258 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Caminibacter pacificus].
ACCESSION   WP_457561655
VERSION     WP_457561655.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..258
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29613
     Region          49..244
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnsnvlekif flflflllvy iisalylylt qnskvfqrky akeytpkyak klyfttsdgk
       61 rlegaylenk kgaplvlyfs gnannviefi dniavnikdy nflgfnypgy agsegepcee
      121 cilkyaleif dkykpqilig rslgtavaty vaanrdvekl vlitpfdsie hiaqirypil
      181 pislllkhkf kevewiknvk vpvsvlfvkn ddiiprksid nllkhipnln kkieiegvth
      241 griyeypnis kvieellk
//
LOCUS       WP_457561657             299 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Caminibacter
            pacificus].
ACCESSION   WP_457561657
VERSION     WP_457561657.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..299
                     /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=35283
     Region          7..285
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkakeytktl sillqlinkf yqgenlstsd iekiygvskr taqryinylr eagfniqkkg
       61 kkyyldtiid neketifeai lsiaknagie ekisplltkl kliskenvfy skfdiekidp
      121 qilkkietai kqkkiikmky kmnkrlinme ikpikisnfd gywyvnalnh kneyrtyhik
      181 sihelqvtnq tfdikenilk dvdkavniwf kpkgtpflve liadefatky lqripisktq
      241 kiiknsdets tiyleitdkn eiihkllmwi phlavvspkw lkkeidnyii qyiekfmkl
//
LOCUS       WP_457561659             369 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Caminibacter pacificus].
ACCESSION   WP_457561659
VERSION     WP_457561659.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..369
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43500
     Region          71..355
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mienprvslf nrngilyvqf yiegklkqks lkkpytkenv kfakkhivpq lerkilsgey
       61 kqlnkkakef eyyasiylrq kenlksydey knivvnqlfp lfkhkkvnei tkgeikewid
      121 krlqeispkr mrnilnilia ildiaieyeh iktnpaknik lpshktirem kpfteeevkl
      181 liknaegqfk nylavafytg mrpgeiialt lsdinldemy invnkrvrkg ktdtpktkns
      241 vrkvpilksl vpyiedlikk akekqtfnlf ttktgkryys sdklhkewys llekckfkkr
      301 vmyntrhtfa tlaikrgvpi fnvsqilghr ntqetletya kfinnehlni rrdidlftdt
      361 stdshskqa
//
LOCUS       WP_457561663             118 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457561663
VERSION     WP_457561663.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 118)
  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 118)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..118
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13103
     Region          3..>118
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mnrkilvved ekllndtist fltysnydvv saydgisave makqhnpdli lldvmlpcml
       61 gydvakairk fssvpilflt siedkeskqk afeagatdyl sksidlsvlv ekinqilk
//
LOCUS       WP_457561665             219 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561665
VERSION     WP_457561665.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..219
                     /product="phosphoribosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016772 - transferase activity,
                     transferring phosphorus-containing groups [Evidence IEA]"
                     /calculated_mol_wt=24079
     Region          2..219
                     /region_name="COG1926"
                     /note="Predicted phosphoribosyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:441529"
ORIGIN      
        1 mifkdrteag rllgekikel iqsgrivdpv vvalprggvp vaaeiakein apldilfvkk
       61 ipspvneeaa igsvsesglv fvntnaietl kargidvdes yiqqkaleki qemarkrdty
      121 kveplplegk dvilvddgia tgasmylaaq svvrdmprsi tiaapvapad envlemlrkv
      181 shnlviletp pmfmsvgqwy edfhqlsdke vkeilfqfr
//
LOCUS       WP_457561670             211 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457561670
VERSION     WP_457561670.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..211
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24300
     Region          9..207
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnlksfflfk glddkdieev kkftivkklk kdeivfyeke npaylhllve gvarvykvds
       61 kgneliihkf spvsliaela nlenmpypan camdsdgvil kiefekfkkf mkkgdvcfsi
      121 mssllrkmky ldgliqanlv ldtetkiakf iyenpeafed lkqhsiasll nikpetlsrk
      181 lkkfkqlgii envgsklkvk nrelikenft w
//
LOCUS       WP_457561667             441 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457561667
VERSION     WP_457561667.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..441
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48878
     Region          22..419
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mtlnpvkilk qsltklslir dfllaslltg fisgflvvvy diltkliskf lyrgdpleti
       61 hnlplwylvl iptlsilivn fivsvdksvk eygvseiaei vekdkemiti knlllkiias
      121 alsigsgfav gnegpsaaig amiaykihkl fklpnqlikp iisvgassgi aaifvspitg
      181 iafalesiay nfvktylkfi ivgslaaftv svlylkpfhf ifsagreidl kyiyytmlfi
      241 pfitffiyfy lilqdkilyl lnlklfnkfg iikdlifaii ggvtialiiy inpyagftgh
      301 nivtylinna yhipfiliie illlriiata fsiysnaigg mfvplmsiga lvgygfaell
      361 nlahlniepf yfaaigaavf mgvlmklpft sivlalevtn dynvviatgm svaiisyltr
      421 lnfnlkkfnt idinftnfkl h
//
LOCUS       WP_457561673             283 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caminibacter pacificus].
ACCESSION   WP_457561673
VERSION     WP_457561673.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32325
     Region          26..268
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkiinqiise iekvikgkke kikiilasff adkhvliedv pgvgkttlak tiakvlglef
       61 krvqfsadml psdivgvnyf dmqkkefvfk kgpifteill adeinratpk aqsalleame
      121 erqvsvdgkt yklsenffvi atqnpkehgi yplplsqldr fgicislgyp erefeklilk
      181 serievnsfs giekykrkak eiftdekiyd lvldlgkisr difetglstr alitlleisk
      241 ayamiegrdy videdvfeil kyvtphrlee nadkkiirly yqg
//
LOCUS       WP_457561675             377 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent rRNA methyltransferase [Caminibacter
            pacificus].
ACCESSION   WP_457561675
VERSION     WP_457561675.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 377)
  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 377)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..377
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=42873
     Region          2..375
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mkiyinksay eklkkrflwi yqneitkape cdagsvvdvy ykdtyvataf ynplskisar
       61 iisfekthlh knffkkriek aikkrelikn tnslrlihse adflpglivd kygdnlvvsf
      121 ttagmdnfkg iiieiliell npkgiyekgd kirekeglev inqtlygsvd defvivendk
      181 kfftslkegq ktgffldqrk nrkivgefgn ektldlfana ggfgiyanak ftkfveisal
      241 acsqieknct lnnlknyqii kadvfkflen ekekydliii dppafaktks arkgaikgwk
      301 ylivnslkll eeggflalfs cshsitskdl sdlalssavi ekcdlevief lkqdidhpyl
      361 lnvpnslylt gvllrrv
//
LOCUS       WP_457561678             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Caminibacter pacificus].
ACCESSION   WP_457561678
VERSION     WP_457561678.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=42011
     Region          89..>356
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
ORIGIN      
        1 minqykkegk nyqilklknn sltfyttsre nlknllnekv kltiitskvs ffeylftfya
       61 psfnikllpa dkidlfiekq hsssvmknlf kalflgesid fstrqklssl gvshlfalsg
      121 lhlgfisfvl yfvfsplyki fqkkfpyrnr ffdlgisvla vefvylyfts fppslirayv
      181 levlififam rfkelfslni lfftilfsfl iffskifsig fllsflgvfy iylffkhvkf
      241 sffssvflsf ymflvmfvws hyffgnfnyf qflsplvnii fsffypleif lhllgfggvf
      301 ddfilkylsl gsefyevkis fvwvvifgim sllaffskyl fyginllaff ivilai
//
LOCUS       WP_457561676             810 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457561676
VERSION     WP_457561676.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 810)
  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   3  (residues 1 to 810)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   6  (residues 1 to 810)
  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   7  (residues 1 to 810)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   11 (residues 1 to 810)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   12 (residues 1 to 810)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   13 (residues 1 to 810)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   14 (residues 1 to 810)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   15 (residues 1 to 810)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   16 (residues 1 to 810)
  AUTHORS   Zoraghi,R., Corbin,J.D. and Francis,S.H.
  TITLE     Properties and functions of GAF domains in cyclic nucleotide
            phosphodiesterases and other proteins
  JOURNAL   Mol Pharmacol 65 (2), 267-278 (2004)
   PUBMED   14742667
REFERENCE   17 (residues 1 to 810)
  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   18 (residues 1 to 810)
  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   19 (residues 1 to 810)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   20 (residues 1 to 810)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   21 (residues 1 to 810)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
REFERENCE   22 (residues 1 to 810)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   23 (residues 1 to 810)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
REFERENCE   24 (residues 1 to 810)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   25 (residues 1 to 810)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18594631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..810
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=93898
     Region          <109..>278
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
     Region          273..>381
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          <375..810
                     /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 mdvsilnqit kygfilkqgs kvyankrvie llglrkrnll ndlnkieeik eflnskksvf
       61 keivtiktki etkhisfyik ktidgfilla ddftkyirek hitdiviymn dvlaksknek
      121 elyekfikav ikkakfnacf vmkkqknalv pvawgndtdg ldcikdvtip ldektpllkt
      181 pvakaflegn iffnddtrin pdveplreem lkrnylssvg ipifkekkve avicickdev
      241 dffkgykkli eyiskalskt lenleeikfk nvllnainkg hewvvitdkk gkvvfvnetv
      301 ekitgykkse ligknpkifk sglhdeifyk elwetikkgr ifesiiinkk kdgsifylld
      361 kivpvgdyyi slgkditnek kyfhlieelk fkdpitglyn kegffkhard ylkkfkyesh
      421 ivlvvdvynf nvinhkygit egdevlkqlg kklrtvffer dliykfhtvn itlgrfngde
      481 faiflekade kcipkilnkl yevfsgtykv knekikldyn agisvypkda cdiedllnna
      541 sialinakke gpnivklysk eyskeiykfn dvlnliktsl eknrfelffq pivdaekeni
      601 vaaegllrir ekskiitpgv fidvlensny slnvsmkmld nienilkntk nvklsynlce
      661 kqfrntqaid klinigkkfp yrlqielier vlineklysq kvleklkdng iliaiddfgt
      721 gysslsyire lpvdiikidi sfirkmmqnh kdmaivktii nlakeldikt vaegvedesq
      781 vailkalgcd yiqgfyyykp mpkeeflkll
//
LOCUS       WP_457561681             103 aa            linear   BCT 27-JAN-2026
DEFINITION  LemA family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457561681
VERSION     WP_457561681.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..103
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
     Region          <1..103
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 lqeyiaaqqk lssalarlla vserypdlka sknflmlqsq legtenriav arrdyieavk
       61 rynlelrtip nkwiahllyp dakikptfti dqkdmktpev nfn
//
LOCUS       WP_457561682             283 aa            linear   BCT 27-JAN-2026
DEFINITION  TPM domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561682
VERSION     WP_457561682.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30593
     Region          1..224
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkviflilf sflfaiefpk ltgrvvdnaq ilspktkqtl namlksfeqn tsnqivvvtl
       61 kslqgnsien ygyqlgrhwg igqkeknngv llivapkerk vrievgygle gtltdaksfl
      121 iindiiipyf kkgdydtgvl kgvqaimdti kntfkpekke keeideaipi ggfallflsv
      181 llskyltflk rilpalflgv maflvvyfis qtllyalltg ggifaiialf nlknppppsn
      241 gdiemgeiit dygvftgggs sndgggfsgg ggdfggggss gsw
//
LOCUS       WP_457561688             498 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein,
            partial [Caminibacter pacificus].
ACCESSION   WP_457561688
VERSION     WP_457561688.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>498
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          8..498
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 malidlldvs kkfeaqkilc nvefhldege rvaligkngs gkstlmkiid gtiepdsgev
       61 itkngikikr llqqpkfnag vsvreaiene ltefkeayek ylkltqefse npdnkaiqne
      121 ldkitkfldf hnawnlddri ervlqefdlk kyenkdisll sggeqrrval aslllqkpdv
      181 llldeptnhl dvymtefled mllkekytfi vvshdryfid riatrvvele ncklrsfkgg
      241 yadyirqkee llkikekeye nelrllkree ewlrrgvkar lkrnegrkkr vlelrekvkq
      301 drseirkiem qlkrellake dekinkkkvm feienltksi gnkllikdft trilqkdkia
      361 ivgkngagks tllklligee kpdsgiikvg enlkigyldq rksmlddnkd lietfcpqgg
      421 dhvnvrgrnm hvygylrefl fppeyltkki gvlsggektr valallftkd fdilildept
      481 ndldiptini leeylidf
//
LOCUS       WP_457561690             323 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561690
VERSION     WP_457561690.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 323)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..323
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38095
     Region          <146..323
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkqkikyiil isltvvsisf leytknqkik eidnqivslk tpihflfnvq ymfnkamltq
       61 nkalklqyid taeyftnlik nnseikkflq rekikiskne dnpvkdskel yeiikniaek
      121 qylnilnsle nlkkfkniin qtfmmvdlsi ivltvlliil yenkrhknhl eeasfkdylt
      181 ntynrrkfye iasmlpndkk htlimldidh fkqindnygh ekgdfvlkev adiirhnirk
      241 ndyifrwgge efivllkntd ieggmkvvek lkedienhdf qglkitssfg icetnvindn
      301 ilqeldraly eskrngrnri tva
//
LOCUS       WP_457561696             127 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457561696
VERSION     WP_457561696.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 127)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..127
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <3..105
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 lpiryvavlg nndlhlysvv dkyelvtepf yfklagktwk lmhyprymfp ldtdiivygh
       61 thdvditfng knlilnpgev cardhgfstc mtldiedeky ivtlyyrkvg ekewkskvke
      121 flipkge
//
LOCUS       WP_457561704             388 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457561704
VERSION     WP_457561704.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..388
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42866
     Region          1..385
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(97..99,123,173,204,232,234..235,243)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(100,133,197,241..243,273,276)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            235
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfskriekls psltiaisqk arelkaqgkd vlafsagepd fdtpevikka aikaiedgft
       61 kytavagipe lleaiktklk rdndleyetd eivvsngakq slfnifacli degdeviipa
      121 pywvtypelv kyhggvpvsi etdestgfki taemlkkait pktkilllts psnptgavyt
      181 keelkaladv lkdtniwvvs demyekliyd gkftatasin edmlkrtitv nglskshamt
      241 gwrfgycask nkelvknmik lqsqstsnin sitqkaaipa llgeadadve mmrkefekrr
      301 dyvyeafnki pglsaakpag afyifvnhke impesmnfal tlledkgvav vpgvgfgseg
      361 yfrfsfatdi etikegikri eefvkais
//
LOCUS       WP_457561706             356 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561706
VERSION     WP_457561706.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 356)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41380
     Region          <190..350
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mfrlkillkn tgassviial lfvifaiiva ngyyivhsln kytkydslli nklgqirgni
       61 qrytkfkiik dsqklnqikn niefdfktik mlidnfpeti pekyrirfyd iytnlysiwq
      121 eiedtnekqe linksekawk iadsitammq nisekkieii skrfslasml aaasililil
      181 fvyrvirvgl ertsitdslt glynrlffne qivyniekyn rygepfsmmm fdidnfksin
      241 dtyghnegdr vlkeiaaiik ktirktdlpf ryggeefvii fpktkitsan iiaqrikkei
      301 eenikvysqk itisgavgey qdegiykfiq kidnklyeak rtgknkvlla asktki
//
LOCUS       WP_457561707             193 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Caminibacter pacificus].
ACCESSION   WP_457561707
VERSION     WP_457561707.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..193
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21256
     Region          4..189
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mfqhivdilv nfahslgyig iyfymllvgt fipvpselvl lpagylaakg dmnlylvwvc
       61 aalgslsgal inyflakwiv nkflkdkpvi ekvtkfwnqh gkisaflapl tpglgqyisi
      121 paglshmplr wfipltfsan liwtgflimi gyifgageaa hkevvygsli llggvivias
      181 iyvfrelkke tks
//
LOCUS       WP_457561708             460 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457561708
VERSION     WP_457561708.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..460
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50156
     Region          1..458
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mldkkhieel kkivgeedik tdkihlrays ydatkehyyp eavvfpkdee evskilkycn
       61 dnkiaviprg agsgftggal pvnggiilav ekymnkilei dekdmvavvq pgvvnahlqk
      121 aveekglfyp pdpasmdyst iggnvsenag gmraakygit kdyvmslkav lpngdiirag
      181 krtikdvagy nvagiliase gtlaviteit lkllpkpkmk ktymgifenv edamnavyks
      241 lasgampvam efmdslvvka lreklgvnlp dwagalligd vdgnveeein yqlgileksf
      301 kengckefkv ardeneanei wyarrnasqs itiygskkin edisvprskl pdalrvitqi
      361 gekyglvvpc fghagdgnih vnvmvdgsne eevkkgyeav eeifkavvdm ggtlsgehgi
      421 glskapfmki afseaelnlf krikeafdpn gilnpgkmgl
//
LOCUS       WP_457561710             517 aa            linear   BCT 27-JAN-2026
DEFINITION  L-aspartate oxidase [Caminibacter pacificus].
ACCESSION   WP_457561710
VERSION     WP_457561710.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..517
                     /product="L-aspartate oxidase"
                     /EC_number="1.4.3.16"
                     /GO_function="GO:0008734 - L-aspartate oxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0009435 - NAD+ biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56660
     Region          1..517
                     /region_name="NadB"
                     /note="Aspartate oxidase [Coenzyme transport and
                     metabolism]; COG0029"
                     /db_xref="CDD:439800"
ORIGIN      
        1 mkydilvigs giagmmaaie akelgsnvai vmkkspmann sfmakggina alnnmgdgds
       61 iehhiqdtlk agmglaeeea vrifceqapq ivrelhrkfk vpfttlpdgr laqrpfggtk
      121 fkrtvfaada tgpaimkaln kalnylnidt iknhfalnll indgkiagat fvdekgelkv
      181 iqakavivtt ggfaglyrgh ttnitdatgd giamglragl eamdmefvqf hptglegtny
      241 liseaargeg gklinsdgke fvdelntrdf vtraivkqlq kgkkvyldlt dipeeiintk
      301 linlkkrvks lkgidiskep ipisplahyt mggiktdtyc ftdieglfya geagnngvng
      361 anrlggnsls egavfgriag yqavkyshrq qtqiepkked iqkdkeliet lkntkidakk
      421 ikdeigeilf nklgilrngy aikkaldkfe dikremsqnh endsslneki eclnaldiak
      481 vlaksalyre esrgahfrmd ypesdhaflh htlekld
//
LOCUS       WP_457561711             666 aa            linear   BCT 27-JAN-2026
DEFINITION  EAL domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561711
VERSION     WP_457561711.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 666)
  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 666)
  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 666)
  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..666
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..666
                     /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=78298
     Region          428..655
                     /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 mryvdsiknh lptilqevki qikndktiye fvkteeeldk llslqekliq eylydfqkni
       61 ldekkcmqfy kdlkipyaiv vrslnyirke viialdkegv dketiiefse yfdkfinlta
      121 kvylkkdivt lkklrnsyfe dyllfkshis wvesiiesis eddiskfpli aaseckfeey
      181 lnypeslmvc idvnlcmylh dlhsllhkls ntfylyyaks ayseaymifk dlkeqilkfk
      241 giigelyfit ysnlevsffk lieiyktnkk efvtlidmks lkslnsiyge etitkalevi
      301 ekrlhrffek dqarslvvkg mtanfymlni dysydeykkm idniieiike pvildenkie
      361 ftpiiaglei eeyfdikkde mimilnhlkn kakqskcnkl lvinhyskem lkswlknryd
      421 skfikskien aelklayhpi fdiqtnkiys leilarivde dklipaglfi devysmnlie
      481 kldlavlrkl iedkekikqi tdkifinvsf nsllneeyle kleklidniq vglllelteq
      541 kfvdnveilf elnqkynlff avddfgtgyt slqsvvdlvk kgilkvlkid gsliknidde
      601 ynkkiinvis nmakelnlls vaeyveseei lneikkagin laqgyflakp alieelivek
      661 vekfgf
//
LOCUS       WP_457561713             390 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine desulfurase family protein [Caminibacter pacificus].
ACCESSION   WP_457561713
VERSION     WP_457561713.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..390
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42984
     Region          1..380
                     /region_name="NifS"
                     /note="Cysteine desulfurase/Cysteine sulfinate desulfinase
                     IscS or related enzyme, NifS family [Amino acid transport
                     and metabolism]; COG1104"
                     /db_xref="CDD:440721"
ORIGIN      
        1 mvyldnnstt pmdervkevy cdatkyfgni nviydlgiea rkklneaydi lypgigasde
       61 ddiiitsstt egnntviktf ldsylkgsgk khiittvaeh ssikatcaya kthgmevtyi
      121 ytdengrvnp kdienaired talisvlfas nesgaiqpik eisqiarkyg ipfhcdgaqa
      181 igkakinvre lgvdyftfsa hkfhgpkgvg glyvregapf vnlihggnqm ggkrggsvyl
      241 ngiiamaeav klanehldem ydkvaklrdk leeailkipd tktyvdkkyr lpntvvasfr
      301 giegeamlwd lnmhkiyaat gsscsserle gsevlealge dpeiahtgii fslsrftteq
      361 eidyvievlp kivkrlrdis mtyakvkpgd
//
LOCUS       WP_457561723             142 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit B family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561723
VERSION     WP_457561723.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Friedrich,T. and Weiss,H.
  TITLE     Modular evolution of the respiratory NADH:ubiquinone oxidoreductase
            and the origin of its modules
  JOURNAL   J Theor Biol 187 (4), 529-540 (1997)
   PUBMED   9299297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007134
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..142
                     /product="NADH-quinone oxidoreductase subunit B family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=15596
     Region          3..139
                     /region_name="HycG"
                     /note="Ni,Fe-hydrogenase III small subunit [Energy
                     production and conversion]; COG3260"
                     /db_xref="CDD:442491"
ORIGIN      
        1 msiitrspfl frintgscng cdvelattam iprydverlg crytgspkha dillvtgpit
       61 arskpyliev ldelprpfvv iaigtcptsc gifrdsysie gpldkyvevd vnvpgcpprp
      121 qaiidgvaka leiwkrkird fk
//
LOCUS       WP_457561727             332 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Caminibacter pacificus].
ACCESSION   WP_457561727
VERSION     WP_457561727.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..332
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37472
     Region          3..331
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnfftfltli igyfvyltyr pylldiaias lmaiafsrie iklsekiknr yllasfitlv
       61 fallifgpll yfiivagkfi thiniediki vilkaqnllt ylpneiagyi knwltddniq
      121 kiyqsimpiv gtltaksavf ikdaflivvf fffailygkd illyvkkvip lendklekly
      181 fttsevmsvv fystvftall egalfgfivs lyglnffffa vmyafaslip vvgglimwap
      241 vslyfyangn iqaaiviivy siviisiiad tfikpliiaw vkkffgndie fnslliffai
      301 vaglssfglw giiigpaita lfisvlkyye ki
//
LOCUS       WP_457561728             174 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caminibacter pacificus].
ACCESSION   WP_457561728
VERSION     WP_457561728.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 174)
  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 174)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..174
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20355
     Region          8..173
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 maieylehyt ykdyekwegd welingypya mspfalpshq risgkifrel desldncsec
       61 faliesevkf sedtvvrpdv lvkcgeiddi tltpeiifev vsensirrde ivkfdlykke
      121 gvmyyglvyp nekrvkiykl ingeyikisd lrdgifktdd ltcdikvdfs kvwl
//
LOCUS       WP_457561730              83 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase, partial [Caminibacter pacificus].
ACCESSION   WP_457561730
VERSION     WP_457561730.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 83)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>83
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          5..>83
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnflenkial itgassgiga atakklseyg vnliltgrde kklqqlknsl qtqtltfafd
       61 irnkkevekf vneilsithi dil
//
LOCUS       WP_457561736             115 aa            linear   BCT 27-JAN-2026
DEFINITION  2OG-Fe(II) oxygenase, partial [Caminibacter pacificus].
ACCESSION   WP_457561736
VERSION     WP_457561736.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..115
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
     Region          8..111
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 sflkgtelqv leykeggfyk chadnaseiv kngklvgykv vkperklttl mflnddykgg
       61 evefchlrfa ngdrvihkpk agemivfpsh glfshevkpv hgnnrfavvk wwdvv
//
LOCUS       WP_457561739             165 aa            linear   BCT 27-JAN-2026
DEFINITION  LOG family protein [Caminibacter pacificus].
ACCESSION   WP_457561739
VERSION     WP_457561739.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..165
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18572
     Region          7..>124
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mkiattfgas rvedpklyee gvelgkflae rgyvvkcggy gglmeavslg vreaggevig
       61 itlkyfdeir pentyltkki qtpdlferlk kliigsevfi aqtgsigtln eifmvwalky
      121 glgldfricl vgevyqefkt csfipkerls eieiyknlee fkrnf
//
LOCUS       WP_457561744             395 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Caminibacter pacificus].
ACCESSION   WP_457561744
VERSION     WP_457561744.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 395)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43756
     Region          27..387
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mndfkfnenl ykavdfitke kfekvilpqe lpkkglgent lnimaskvlg eatyldsplv
       61 fahmdpptpw iawamalwna rlnqnllhke lspfatqaee lvidwikdff gmdgghmcsg
      121 ssianltalw vardtknidt ivasesshis iekaakilnm rlikvpinnd gsidkksvpn
      181 lknaclvlna gttcsgaidd fsligqakwt hidaayagal kftseysnil ngieradsis
      241 lsahkwlyqp kdsaivmfkd nkkakevmsf gsdylssani giqgskgang vvllatllyf
      301 gkegidrlia yslknallfy dklkeieqie vfnkpicgit lfrpknmavn eflsklpkgm
      361 fskckikdke fvrsvalnpm adideivkfv nnvlk
//
LOCUS       WP_457561745             152 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Caminibacter pacificus].
ACCESSION   WP_457561745
VERSION     WP_457561745.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..152
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17045
     Region          2..124
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mdfmkeavye akkgvlnkeg gpfgavivkn gkiigkghnq vvklkdptah aeiqairdac
       61 knigsfdlsg cemyitcepc pmcfgaihwa riervyfaat redaanigfd dkfiwdvieg
      121 krednvlfky tpskealevm klwesmedkt ly
//
LOCUS       WP_457561741             458 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457561741
VERSION     WP_457561741.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..458
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=52177
     Region          2..327
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mrvaiigggv tgssiamyld slgvdvrlfe kndlvsgppi chlhaggnly reitlkekta
       61 llkesidfir lypqaidfrp tivavpvdde gepedlietl eilkneykkm iekdpknkvl
      121 gepedyykly ykkdleklke kelvkepktl dewmipfaky tnlnkikfpv ilvqeygvnv
      181 frlsaiakmi lekkgivrye eakvskkgdk wivngeefdy linaagfksg ivddalefkr
      241 drltefkaay vvknkkfdft wpeiifhgkr gtpkgmaqft pyangifqlh gmtkditlfd
      301 dglvssdees sypklpnhfi ekiekgwqke eaasrakrai ehmskfipef kdsevtyvpl
      361 fgaqqipgrd aelraveisf eenyarcevv kastvtsmad siakdlskrf gikykkqiei
      421 peilnlsdev itkkaceiak srgypedmgk rnfselks
//
LOCUS       WP_457561746             217 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Caminibacter pacificus].
ACCESSION   WP_457561746
VERSION     WP_457561746.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..217
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24709
     Region          1..217
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 miislynikg gvgktstcin lastasktkk vliidldiqg assyffgkkp kkrgifkkpi
       61 ekiikktnnp nidiipsdkq lvkyqgelkk llnlkydiif idapatlndl tkdilkysdi
      121 vlspvlpnil slrtynqlle tklnkniklf vnayenkpsh kqivkailkl pksqylktyi
      181 pksekienmp lykmsvvdky pysletkryq kllseli
//
LOCUS       WP_457561751             212 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Caminibacter pacificus].
ACCESSION   WP_457561751
VERSION     WP_457561751.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..212
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24840
     Region          30..209
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mkkwiflflv fatllygfnl sdikdffsed nlinllkeyg yiilfiwsim egetglvmag
       61 ilshtgdmnl wvaivvaalg gfigdqiyyy lgrfnknwvl kelnahrrkf akarlllrky
      121 ggwvifiqrf iygmrtiipm tigvlgydpk kyafinfisa fvwasvtiip syifgeqlle
      181 flkwlkqhwy fgimflavvw gilwyinkke es
//
LOCUS       WP_457561760             253 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561760
VERSION     WP_457561760.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  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 11459733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28534
     Region          109..253
                     /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 mknddllnin pkkdmkkpli yaaigflifi iiviavaifq nmssgknnei lppqpkteke
       61 ikpqeefkpl pietanenta dqnanqnenq nvnentqnna ntntnaqtpa atqtnttqnn
      121 trtqkpkpqv tqepvknekp qakeqktqki tkkpvkvtkp avttkpkkva ygkyyvqvaa
      181 llrnakpnkk flallkkygf nykyihtyiv kngekikvtk ilvgpyktrs dakralakik
      241 revtqnafiy kak
//
LOCUS       WP_457561763             292 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561763
VERSION     WP_457561763.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 292)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..292
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33563
     Region          <117..283
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 meelikeian ktmqdlekak kppyplyyrd vfnaianekg ilnqlnpkll ciaptldeii
       61 laktsetise isihtkdikn dsreiidevn vadadeikem vikfsanlie kvnqmeeriq
      121 elqseldkay kellidpltk vynrkalekd lgeilekgkd rnldlviaiv didnfkmvnd
      181 kyghlvgdfv likladtmks lirksdkiyr yggdefiivf nrstlenaek sieriiykiy
      241 rttlkykeny ikitisagit qhragdties iikradealy kakvekngyk il
//
LOCUS       WP_457561767             574 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Caminibacter pacificus].
ACCESSION   WP_457561767
VERSION     WP_457561767.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 574)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 574)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 574)
  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 10006830
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..574
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66975
     Region          <82..310
                     /region_name="COG2984"
                     /note="ABC-type uncharacterized transport system,
                     periplasmic component [General function prediction only]"
                     /db_xref="CDD:442223"
ORIGIN      
        1 mrvlfllfla vflfaknili insysiklpw tkgelegile kinnkqnlki fiefmdtkyf
       61 qptpmrmlny yyylkdkykn infdivittd dnalnfvrky knepifsnak vffagvnnlk
      121 ladtlsknvy agvfekkepl vnlnfakkiv pnlktvyvva dnsnsakavm keyknafkni
      181 ksptliylne knlenileti kkapknsaml lltpfsfsle dshisykyai alisqvfphp
      241 iiihtdllan vpnsnvvggk atdaltqgke agkkvleyls gtpmqkigft fekankmyln
      301 vlnlkkfgid ayalgyknai yvnkprtfye mykewiigsi iiffavlmmi vililkniql
      361 kkynekiskm nkeleekifs alselkekek lllhqtkvsa igemflmvsr kikeklykll
      421 ekeetkeeat yilnkltmie kyfndssvle fdlkeatkev vyslkdvlne glveikgeni
      481 yifgyknkfq qvildflynm skfqneieki ifefkedkie ihirfkhfsk nlidnfenvl
      541 nnelyytrli mqqyfcsecn yrvdknsvim eiil
//
LOCUS       WP_457561770             269 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457561770
VERSION     WP_457561770.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..269
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32623
     Region          12..>106
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          182..263
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mknyffkdek ipyieirkse dnnlrykehf hcefsigali kgttilsfen kkyhlnknel
       61 avfnpfelhs cnpyknqkrs yymmyvdtqw lfnlqknife vnefipiksa iiksekyyfk
      121 fiflcekiid snvlyleqea lleeffseif infldkkrkk etfeieklkk akkyiekhfy
      181 knitlfeisq hcelspyhfs rsfkkafgis phkflmnmri ekakkllkek nivdvayevg
      241 fydqshfhkv fksytaatpf eyknytpnf
//
LOCUS       WP_457561771             289 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caminibacter pacificus].
ACCESSION   WP_457561771
VERSION     WP_457561771.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..289
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32985
     Region          5..270
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrknnllyhf ialvtiiiws ltfiqtkill kylspeeill drfviawiif fiifpkikff
       61 slkeelifvf lgfsgifgyy ilenislslt sainvgiivt sapifttilk ittqktnskk
      121 vlfsiigfif viigllimei khiskpnlgd ilailgalff gaysfvlgkv nsktnsilit
      181 rksffwgivf lmiflffkhf nfsdikiyqn vdvwfnilfl sffatalcff mwkkavskie
      241 tkasnyiylv piintlaavf ilnenitasm lisiiiilsg lfisqkfgv
//
LOCUS       WP_457561772             246 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457561772
VERSION     WP_457561772.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26486
     Region          1..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mitaiiigif vgffsgflgi gggtvlvpvl lflgfgfkea vgisvtqmmm ssiygsylny
       61 kkgllkikng lslavggaig aalsglivky tskdilgaif ltlvfiaiir ffvtvkephd
      121 eppidnkklf figlfvgaia isvgvggail itpilvgflk yklkttvsls lffvvfssvs
      181 gfisqslagh inylegfsig iasligtyfg vklyhkvdtk ihkkillawy ififfamiyk
      241 lyfqgn
//
LOCUS       WP_457561777             253 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457561777
VERSION     WP_457561777.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28675
     Region          1..239
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mikirhlkkv fgskvvlrdv nldikdekit yilgmsgqgk stiikhivgl lkptageiwv
       61 deinvadadi qqlyevrkrv gftfqegalf dsmnifdnva fplkehtnmk kdeikkrvfe
      121 tlemvgldad rvaylyphel sggmrkraat araiilkpky ilydeptsgl dpiisdkitr
      181 miesltrehk mtsvvishdl ketfksadyv amlyngeiie ygtveefkns qnpivrafie
      241 gnsekyekia dgv
//
LOCUS       WP_457561781             276 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caminibacter pacificus].
ACCESSION   WP_457561781
VERSION     WP_457561781.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..276
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31301
     Region          6..274
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mlrkyadfll vlvalswgst filvkkaied lpafsflfvr fflafllmyv ffhkkieidk
       61 kilkaslilg flnfsayalq tvslyylpsn ivafltglfv iftpvsayff fkkeipkkvi
      121 iaailaflgi yfltqakfaf siyvflvilc affyalhinf tdifskkyni fslvtfqflf
      181 vaifslflip fedlhnikis ftvvfaiiit vvfatvfaff vqtfaqqftt ptktaiifal
      241 epvsaaflga ffgeslnikq iiggilvvis miiaei
//
LOCUS       WP_457561785             283 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Caminibacter
            pacificus].
ACCESSION   WP_457561785
VERSION     WP_457561785.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31482
     Region          10..283
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mtreqiykek kkiaifsiiv nltlslikii ggklsgsaal tadgihslsd laasfsvltg
       61 iviankkakd fpmglykven lvalisafai ffagyeiakd vffgepmkih nlpialiaiv
      121 ltviityfys rwekkkaiel nspslladae hvksdfftal vvlvgvigqy mgypiiekia
      181 vaivvyfifh sgweilvdai kvlldasvek etidkvreil dkedmiekin dikgrnagsf
      241 kfiyldidvk tdsikeahay vhkledkike aipevekvit hye
//
LOCUS       WP_457561789             214 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561789
VERSION     WP_457561789.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..214
                     /product="phosphoribosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016772 - transferase activity,
                     transferring phosphorus-containing groups [Evidence IEA]"
                     /calculated_mol_wt=23918
     Region          3..203
                     /region_name="COG1926"
                     /note="Predicted phosphoribosyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:441529"
ORIGIN      
        1 mtfkdrfdag vklsevfefp ensvifaipr ggvpvgyaia ktkkipmdli vvrklpipgn
       61 peagfgainm darailnpaf dalfsqipve eiakdvlnev lrrndlyrns rgysslkgkt
      121 aivvddgfas gysaiaayey lkklhpdkii aiapvcpket kkmlenyfde vycliesenk
      181 pfavasfydd fhdlsddevi dmlydlrken llhe
//
LOCUS       WP_457561790             163 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidylglycerophosphatase A family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561790
VERSION     WP_457561790.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Kumaran,D., Bonanno,J.B., Burley,S.K. and Swaminathan,S.
  TITLE     Crystal structure of phosphatidylglycerophosphatase (PGPase), a
            putative membrane-bound lipid phosphatase, reveals a novel
            binuclear metal binding site and two 'proton wires'
  JOURNAL   Proteins 64 (4), 851-862 (2006)
   PUBMED   16838328
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Chang,Y.Y. and Kennedy,E.P.
  TITLE     Phosphatidyl glycerophosphate phosphatase
  JOURNAL   J Lipid Res 8 (5), 456-462 (1967)
   PUBMED   4292860
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10731865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..163
                     /product="phosphatidylglycerophosphatase A family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17667
     Region          1..154
                     /region_name="PgpA"
                     /note="Phosphatidylglycerophosphatase A [Lipid transport
                     and metabolism]; COG1267"
                     /db_xref="CDD:440878"
ORIGIN      
        1 mnklnwfllt gfysgllpka pgtwgsvvgv iiaylviaym pnpnmtimll aalfsiigfk
       61 lvneyeangg ihddkrivid eiagvlitig vlgdlkhdtf iklllafisf rlfdiwkpsi
      121 igkidqkakg glgvmgddil agifggifag ilymgylklk tmi
//
LOCUS       WP_457561791             435 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457561791
VERSION     WP_457561791.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..435
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46979
     Region          4..417
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msekkafntl saamlgigtm vgigifivig lagsiagnlv wisfviggii allsgyslak
       61 lairfpsrgg iieylvqefg enpfsgslsv mfyfaqlvtl aavaksfgey garlfgyhsk
      121 fmidafavgi ilfftfinll gatlvaksen iivaiklial tiftiaalmt ikpqylsmkd
      181 appiinavfa igltffayqg ysvitnaied menpsktilk amfiaigvvt ilyvsvsiav
      241 lgnlplsevi kakdyalaea akpvfgelgf kimsvvalis atsainatiy aateisytla
      301 kkgelpkiye ynvfhsyegl listaliipm vlffnlseit tvaalsvlii qalvhfghik
      361 ltpktgankg viifafllmt fvvlatlyyn akqdikiiyy liggfviayi ieiilrklfn
      421 rtvkkqikgl tgelf
//
LOCUS       WP_457561798             207 aa            linear   BCT 27-JAN-2026
DEFINITION  LexA family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457561798
VERSION     WP_457561798.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Giese,K.C., Michalowski,C.B. and Little,J.W.
  TITLE     RecA-dependent cleavage of LexA dimers
  JOURNAL   J Mol Biol 377 (1), 148-161 (2008)
   PUBMED   18234215
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Erill,I., Campoy,S. and Barbe,J.
  TITLE     Aeons of distress: an evolutionary perspective on the bacterial SOS
            response
  JOURNAL   FEMS Microbiol Rev 31 (6), 637-656 (2007)
   PUBMED   17883408
REFERENCE   3  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11715193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..207
                     /product="LexA family transcriptional regulator"
                     /EC_number="3.4.21.88"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23284
     Region          6..72
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cl22854"
                     /db_xref="CDD:473980"
     Region          91..204
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mnfekvieki kdiisqevgn kkvlnkdvak algitpehls ilkkrnkipy eeiayfcakr
       61 kisinwllfd qdietianet ekfsqiryfk dinasaggga infdegyeil yidkriidkn
      121 ldainvigds meptikdgsi ifidrndkni rnggifvvnt nagvfvkrvn lkssgeieli
      181 sdnkaypset ikpneieivg rvvkifs
//
LOCUS       WP_457561801             459 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter substrate-binding domain-containing diguanylate cyclase
            [Caminibacter pacificus].
ACCESSION   WP_457561801
VERSION     WP_457561801.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   8  (residues 1 to 459)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10098929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..459
                     /product="transporter substrate-binding domain-containing
                     diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52832
     Region          37..248
                     /region_name="PBP2_BvgS_HisK_like"
                     /note="The type 2 periplasmic ligand-binding protein
                     domain of the sensor-kinase BvgS and histidine kinase
                     receptors, and related proteins; cd01007"
                     /db_xref="CDD:270228"
     Region          <282..456
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mriiwvlvlv vaslfaqvdl tpkeklfikn hlfhcvvtpn wapfnmlkdd kiegiaidyw
       61 klikhklnlk snckilpswt lvlediknkn sdivpatakt pqkqnfalft kpyatypivi
      121 atrnnigfin smaqlenrki vvgknysaae ilkkhfpnln iievkdikta ldyvsrgkaf
      181 aaidnlpvia yninkyqfan lkisgktpfd fkvrfmvrnd ypllvnaink aidsitpeek
      241 erifkkwvyv vyqtgidtkk lltiafiaig lililislvi yqffeikkrr kfetqlikta
      301 tidsltgifn rkhidymlqk eveeakryan plsiifcdid hfkdindkfg hkvgdivlee
      361 lakimkqnir ksdiigrwgg eefliilpht plnealrvae klqsairnye fpkigkitcs
      421 fgvtefksed siyrlmirvd qalyeakntg rdkivvkkd
//
LOCUS       WP_457561802             338 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561802
VERSION     WP_457561802.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39442
     Region          21..>127
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mkghsgissp ffivkkpvda iirdikkgds kdivelfran yddtyykksf ydpktwdemv
       61 eskkyypiva eidgkvvgqf lltvndkyng eigavvvhpd ykgrglmnkm fdylikkaes
      121 lglsaiygea imfhpfsqka nlkhgmieta lqlgevaswi aqkdikfekr sgtlvgykif
      181 nrqkrslytp kiyrklildr ykkaslpisk aairpikksl rlwenrllkl sgiiidgkik
      241 nfenrfntlf tkaklrgemv yadinlhtpe ieeiteflnk krffysgvlf yryngfdylr
      301 lqyenthnve erlnvcfsey ckflskfvir dkkrvarl
//
LOCUS       WP_457561804             158 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561804
VERSION     WP_457561804.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 158)
  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 158)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..158
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18175
     Region          8..121
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mieekikwne kyktltpkap silldhipsa knkkaldlag glgtnaeali nkgyditlid
       61 isdvaiskik npkiktfcld ldnyiipqne ydviimikyf nldllkqipk vlkkggyfaf
      121 ekipkykltt eeffeifkdf etifftkepf ryvgkltk
//
LOCUS       WP_457561816             295 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457561816
VERSION     WP_457561816.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..295
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32112
     Region          25..295
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mikylsafif lliislfsvy ygandfiayn irlprvlsai aagaalgiag fimqvvlknd
       61 laspftlgit hgalfgvsls vvfgigsvfl fsflgafivi vfilavaflr rlssqsiils
      121 giaisalfga gsmflqyfad esqlaniviw sfgdlskgdf fnifllffmi tlslvfflin
      181 swnfnalsle caknvgvkte tlifismiiv tllsalvvan ygiigfvglv aphivrffen
      241 sfksllilsa lygaillvis dyiarniiyp veipvgivts figapmflyl lmrkk
//
LOCUS       WP_457561817             253 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Caminibacter pacificus].
ACCESSION   WP_457561817
VERSION     WP_457561817.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29043
     Region          4..230
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 msfidlknvt ykyeneflal ddvsfsiekn ekvvllgsng sgkstilril aglyfpkkge
       61 yffggvkitk ksvkkdfrkk vgilfqnpds mifnptvfde iafslkefgf dniedrvnei
      121 akkfgiekll kksplhlsgg ekqkvmlasi lvyepeflil deptaamdpr ttgwfldfmy
      181 elelttiaat hdlalayels dralvmseeh kllydgdmee lmkdletlik anlihkhkhk
      241 hkkfihshyh lhf
//
LOCUS       WP_457561819              91 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457561819
VERSION     WP_457561819.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..91
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=10576
     Region          <10..87
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mifltedgll ildaismrlq avgealknid kkdkefllqv adkeywskii ktreiishhy
       61 inldaeivym icdekleelk dkiirlisle k
//
LOCUS       WP_457561832             227 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Caminibacter
            pacificus].
ACCESSION   WP_457561832
VERSION     WP_457561832.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  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 227)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..227
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26442
     Region          3..218
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mnlyqpkngy cynsdtmfly dfitkfnikg evlevgggcg vlgllikrdf pkisltiiek
       61 qkimtefiek nlkenslkae vinddfldye fdkrfdfiis nppfyqgtlk seneikkiar
      121 yeeflpmdkf fekvnrvlse rgefvfcyda krvdeiikkl pkplkitdmr fmhpkidkka
      181 tlvmirakrh aksmvfihpp ligfegeeys keaaeiykka atnsikv
//
LOCUS       WP_457561833             419 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457561833
VERSION     WP_457561833.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=50243
     Region          38..257
                     /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          136..160
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(137..138,141..142,144,167,170..171,174..175,
                     177..178,201,204..205,208..209,212)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          165..195
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          200..225
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          231..256
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..>387
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mrrkisllia gifiitgcat kqtpppigkk vipnedeyii kallaedsge fnksiaiyky
       61 lyqktkkpvy yekivedlfr erkfdevikk aeefnkehfd kkifeyeifa llekkeyeka
      121 knllkekfnk kdefyymmms yilikqnkld eavyylksly alnhsknvll elsdvlirlk
      181 kynealaylr thldlygcdf dvckrlaviy kqtydydnla niyeklgiyd ekylvyaini
      241 ymengeykka inlikkygln keylmmvyvq ekkfrkasav ayelyektsn pkyllkycey
      301 lyydhptkee ikdiakkley liafypnayl ynflgyvlid ndinvkkgly fvqkavelqp
      361 dnieyidsla wgyyklgkck eawdiiryiq tkdkeilkhk rliekcvrrg kregemvkw
//
LOCUS       WP_457561849             299 aa            linear   BCT 27-JAN-2026
DEFINITION  EAL domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457561849
VERSION     WP_457561849.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..299
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <29..295
                     /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 eleepyfifn neilvrfrmg isfqkkeylr aemalnkake lkkdivfgsd aienkenyge
       61 hikwlkklkn aidndrivpf fqpiydknek ivkyealvrm idedgkvisp fffldvakks
      121 rlyleitkim lskslrtird nkvsisinit ledmedeemr efiikkidec iykdkvtfei
      181 venedirese iikefldslr akgvslyidd fgsgyanfdy llklhpegvk idgsliknil
      241 ndknsqvmvk tlinfakese ifivaefven reifemlrdm gvdyfqgyyf sppkpdier
//
LOCUS       WP_457561864             212 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457561864
VERSION     WP_457561864.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..212
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24220
     Region          1..208
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mliaknlshs fdyllfenin lqinpkdkia iigssgsgks tllhilsall kpqngiveye
       61 gkdiysisek elieirkkef giifqfhylf ntftalenlq aaailaqrev dmkllerlki
      121 kdvinqniqt lsggqqqrvs iarvltkhpk iifadeptgn ldkenanevi dvlfeycden
      181 naalltvthd yeiakrferv yelkdkrlni wk
//
LOCUS       WP_457561867             490 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caminibacter pacificus].
ACCESSION   WP_457561867
VERSION     WP_457561867.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 490)
  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 490)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..490
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56442
     Region          111..481
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mdninlkeiq elkeknkfle divtnlldki tnleesleil kenkinevit fdddyfeeke
       61 ylpldqkvdf vhkrlmfvts eiakinkeig rhdlyygevv piegevnkke ilvvcadyph
      121 knnmyggafi parvraykka gynvsvciak ypvgkkelei hehegvkiyi gdfdllekrl
      181 revnpgaivv hspilqnynt fkklgvedrl ifiyhgfevr dvghlyynfd eevmkrirni
      241 lqmdmnrkil alevfrnkki akvfvsnffk nlaindigva pfnvhvisnl iesdlfnyvk
      301 kkpedrlkif sirpfdnkny ggdlivdtil rlseksffke lsfhvqgfgk kfkemtaplr
      361 kfdnvkvveg ilrrediakl hkqhgialip trfdtqgvsv geamssglvp vtnkvaaipe
      421 fvpencamla ednnveqlak gieelyhnpd mfleksfnaa qhirkicspe ntvnkeieli
      481 nkiveskgnd
//
LOCUS       WP_457561870             395 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caminibacter pacificus].
ACCESSION   WP_457561870
VERSION     WP_457561870.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  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 395)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46104
     Region          17..392
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mkkiavlvsn pciidarvir iseaevnlgy evkvfailke ntkeeeqkng vfykrikwnl
       61 sedvrkvipk fikikklkgf lvkraakfvk ydsfkntfee eilkynpdii hahdlitlpl
      121 gstikdkiga kliydahele vyrnpplpwy ekiwvkyiek kygkkadvvi tvnesiklil
      181 qnvfknkkiy virntpviek yqgpslrkkl gfdenkkill yvgkvstnrg idwvikeldk
      241 inenihfvcv ghrdekylek lknlakkykv qnrvhflepv ahqhvvdfik dadvgicain
      301 pvsksyfysl pnkvfemsma glpviatdlp eikkfldevg ngyyfsyknp ekihilvnei
      361 mknldqinkk eimkksrkya weneskkikk vldel
//
LOCUS       WP_457561872             419 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Caminibacter pacificus].
ACCESSION   WP_457561872
VERSION     WP_457561872.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48377
     Region          8..384
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlnkikpkse ftknvltlmt gttiaqaipi lispiltrly spenfgifal fastvsllsi
       61 iaggryegai iisktlresi yvliltifvs lifsiflfii ifllffvnki siikelgyls
      121 flvpfviisi iifqsfynfl nkikeyktla kvkvlqtsia sslniifalt ffknigliis
      181 yiitslflal ylfkkikkyf lynryflskk rllfvlkkyk nfpkydiasa flnnlslqlp
      241 ifllshfygv aivglfmlsr rivglpiiii sssittvfkq hatdeynkyg kcdkifintl
      301 kksilialpp siilffiapk lfefifgkew adagyitqil ipmfflrfvt splsymfyia
      361 nkqnlnllgq lilnlvivmi fftfneenyf tilylfsivf siyylfylyl sykfakgke
//
LOCUS       WP_457561873             365 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457561873
VERSION     WP_457561873.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..365
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41284
     Region          7..363
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkidfaklty qynlykeeid eaiakvlnhg kyimgpeine ledklceftg akntvtcssg
       61 tdalllamma ldiepgdeii ttpftfiata etiallkakp vfvdidetty nvdpkkieek
      121 itsktkgiis vslygqpsdl deineiakkh nlfhivdgaq sfgatykeka evhncdiytt
      181 sffpakplgc ygdggavltn ndelaekmkm lrvhgqnkry hhkyiglgar ldtiqaaill
      241 vklkhyekdl klrqdvaeky nkqlpnnivk ptlkedrtsa waqysirvkn rdelqvklke
      301 agiptavhyp mplhmqecfq ylgykkgdfp iaekvseeim slpmnpylsn eeieyiikkv
      361 eefak
//
LOCUS       WP_457561874             191 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561874
VERSION     WP_457561874.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10213561
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..191
                     /product="acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20748
     Region          <8..55
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     Site            order(23,25..26,31,43,51)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100038"
     Region          36..154
                     /region_name="LbH_WxcM_N_like"
                     /note="WcxM-like, Left-handed parallel beta-Helix (LbH)
                     N-terminal domain: This group is composed of Xanthomonas
                     campestris WcxM and proteins with similarity to the WcxM
                     N-terminal domain. WcxM is thought to be bifunctional,
                     catalyzing both the isomerization...; cd03358"
                     /db_xref="CDD:100048"
     Site            order(57,59,67,75,77,83,89..91,108,110,113,132,148)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100048"
     Site            order(59,61,89,91,110,112..113,118,130..131,136..137,
                     146..147,149)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100048"
     Site            order(59,61,89)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:100048"
     Site            order(89,91,110,112..113,118,128,130..131,136..137,144,
                     146..147,149,153)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100048"
ORIGIN      
        1 mskyfvhess yvddnveige gtkiwhfchv lsntkigknc sfgqncvigp nvkvgngvkv
       61 qnnisiydgv eieddvflgp smvftnvinp rafiqrkdef kktllkkgcs iganativcg
      121 vtigeyalig agavvnkdvk pyalmvgvpa rqigwvdkag nrmnfdehgi aidsfdgtky
      181 klendeikvl g
//
LOCUS       WP_457561877             120 aa            linear   BCT 27-JAN-2026
DEFINITION  JAB domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457561877
VERSION     WP_457561877.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 120)
  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 120)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..120
                     /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]"
     Region          <2..120
                     /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 ettedivnel keysdkkqey fiaiyldgad riiekrviti gildktiihp revfapaiel
       61 raasviiahn hpsgnpspsr ydiiltdrlk esaeilgidl iehmiiskeg yysfnengyi
//
LOCUS       WP_457561882             227 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561882
VERSION     WP_457561882.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..227
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25426
     Region          1..222
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mkscgiiggm swessaeyyk lineqinrkl gglhsakiil ysvdfqeiae yqknnlweks
       61 aevlsnaaks lekagadfvm iatntmhkva dkvkssisip lldirdslie eikaknlknv
      121 lllgtkftme dsfyvdylkk rgvdvvvpes qdreiihkvi fdelclgitk dsskkeflki
      181 iekydtegvi lgcteigmli sqkdtsktil dttkihcnfa vkimcqc
//
LOCUS       WP_457561886             463 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein [Caminibacter pacificus].
ACCESSION   WP_457561886
VERSION     WP_457561886.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..463
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51235
     Region          1..243
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mrtevkvglf iligllslly mtfqiktled fkqkgypvya ivndasgitk kskvklrgvs
       61 igyvdsmkll dngvklklli rkgvkipvgs eiavaqdnvl ggkylkiips nntaylqpkg
      121 vikkyvpsas medvltnink avgdvrella klnstinqqt idnihemitn lkissqrlnd
      181 ilattqtklp kildnanalv vsyketgdii krkipeilnk tdmllaklnk tgeilntklp
      241 kladeyinlg knanqllven kkglkntina asdffasgsk sfqklddmla smqksqiqvd
      301 ifsnymtrdd yfkttaniay mpnptkyyiv gvtstkdyst enpgdkdkiy fnaelgkryd
      361 nllirggiie stggvgadyf ldkdrvklsa diydfnsvnd irgnnpnlsl katylylkhl
      421 efiagvdnil nadartfflg vgvkfidndl ktiiagggts flk
//
LOCUS       WP_457561903             172 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiX family flavin prenyltransferase [Caminibacter pacificus].
ACCESSION   WP_457561903
VERSION     WP_457561903.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 172)
  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 10012639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..172
                     /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=19121
     Region          1..172
                     /region_name="PRK06029"
                     /note="UbiX family flavin prenyltransferase"
                     /db_xref="CDD:235677"
ORIGIN      
        1 mkkilvcvsg asgaslglkl yslippeyer flvlsehaki vlekeenifl nddiaaapas
       61 gsfgidvtfi vpcsmntlak ialgiadnli traaqvaike kkkliiapre mpfseiyleh
      121 mlklsklqnv iiappviayy nkpetiddme kfligkwfdl vgienklfkr wk
//
LOCUS       WP_457561910             599 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457561910
VERSION     WP_457561910.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..599
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=67232
     Region          <314..590
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mgieraivay mlstgklphd llvkwnsaia yqkdiikkyp kiakqileit aeiekirgti
       61 nsynekkhiv sqmkeivgyg glihnfknyv lrgkdkyken fdrkyallnk kikeyealge
      121 speekklide iktvfdkyyn glpavvqgyq enltvheldk ivkvndspai kafkilstkg
      181 iklsglspkd wivlstriin kiktfidklg kdiliqihdi vksttiylcs vlviviliil
      241 tvvvlsfvis kdlvestekl keglleffrf lnrettqake iqinsndelg qmakvinqni
      301 skieeglmqd aamiqglvre vekmkngvle griyeqasnp dlekvrvifn emqdslekii
      361 gkdvnktvkv ldsamhkdft kriqnaigkv elavnsvldt ivsilsvnke ngdilsqtas
      421 elkekmhalk daakeasyel sevanimqnl nneifeisnq tktvidqsqd iknvvgiiqe
      481 iadqtnllal naaieaarag ehgrgfavva devrklaekt qkslseidan inlltqsitn
      541 igeaiikqtd eianatakie dvnektklme nsveevntia eevndmadkm lenvkknkf
//
LOCUS       WP_457561916             187 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457561916
VERSION     WP_457561916.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..187
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22500
     Region          1..182
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mdkiffngve ikykitkkpi knvylrvked hvevsashfv pksfiekfil knaehiikkf
       61 enqkyyflfg kkylnngidv kelykqktpe ivlpfvyeya kkmnlhpskv sfrfnksrwg
      121 scsykdsiil nyylaklpvd iieyivvhel ahikhknhqk efwslvgeyi pdykdrikrl
      181 rklekef
//
LOCUS       WP_457561937             412 aa            linear   BCT 27-JAN-2026
DEFINITION  WYL domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457561937
VERSION     WP_457561937.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Blankenchip,C.L. and Corbett,K.D.
  TITLE     Bacterial WYL domain transcriptional repressors sense
            single-stranded DNA to control gene expression
  JOURNAL   Nucleic Acids Res 52 (22), 13723-13732 (2024)
   PUBMED   39588753
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Muller,A.U., Leibundgut,M., Ban,N. and Weber-Ban,E.
  TITLE     Structure and functional implications of WYL domain-containing
            bacterial DNA damage response regulator PafBC
  JOURNAL   Nat Commun 10 (1), 4653 (2019)
   PUBMED   31604936
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..412
                     /product="WYL domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49048
     Region          232..408
                     /region_name="WYL"
                     /note="WYL domain; pfam13280"
                     /db_xref="CDD:433082"
ORIGIN      
        1 mkgivvrykt lsnpeklkey ekeydlvlpq kmgkssnhil dgeikeikkw ideynikelf
       61 itnlsnkeae klkkklgiev eiikntknis dkifalllll krlsikgnlk vkddfewlke
      121 kleknitkat flnylkdiei ilnddrfnsr evvevkhink seielnlirk gdlilkifne
      181 iddveklsey lveiddetmy mldeitkkrv kslkekiiyk qkpfenldnv rdiflefeea
      241 iknkkiidfi rkengvthyn viplklvfme nnwylagadk nkvkffrlnf iddfkigkke
      301 fskkdlkkey ikfleefetp ftdygkkwkk lvlkihknka hyfekkkhfp mekekkrdde
      361 gnliiecayt qplevlpiik kwlpfveive sedgsveeel kkdlllalnk lp
//
LOCUS       WP_457561947             356 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Caminibacter pacificus].
ACCESSION   WP_457561947
VERSION     WP_457561947.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /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=40958
     Region          1..257
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mkilhtsdlh ighsvsgidr geeyerffew fegvanekkp dcvivagdvf dvyfpsneai
       61 rqyydfllsl knktkkviii ggnhdsfktl kapkeilkyl dvvvvsgsed dfcefvefdd
      121 fvvvavsylr egilkkyddd iekaifklyq eklkeakekf sgkkvvttah fsvsgaslgd
      181 serdiyvgnl efvskdvfeg ydyvalghih kpqkitenii ysgsplalsf ketyqknivf
      241 ieddniefin vpkfrefasi kgsfkevyek isemkdafle ivldeivdse klkllkngen
      301 hivkitlpyv keiknfevkk vtpediikei fnekeiieaf yeikkevede fgkved
//
LOCUS       WP_457561949             351 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457561949
VERSION     WP_457561949.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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 12168893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..351
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39988
     Region          284..343
                     /region_name="TPR_19"
                     /note="Tetratricopeptide repeat; pfam14559"
                     /db_xref="CDD:434038"
ORIGIN      
        1 mkksilfita alffagcstk evpinitqkp navtskairn irvdylvndt inlreniirk
       61 mydvnaiipg yfqinipnye silngyvkkt skeitytktv pikntkspcv ymlysckavs
      121 gavfckdkps tiltpgaydk ikkssyknsn yilyknsiyk vtykckptrk kikcqkksln
      181 iqahititdk knntlldkty yadfnddsck nvkyyenknv yslnysikek ipelsyklas
      241 eiiddiaphq itiyttlfek pdidmnskde dilqntiknf sppaneaqis iltnllskyp
      301 qsavikydla vfltstgryq eakslleslk ttdsdiisak eklltylqnt f
//
LOCUS       WP_457561954             243 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457561954
VERSION     WP_457561954.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..243
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26409
     Region          1..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mfyievffiv lalstffalg gvgsavalvp ilhmlgvnfn lskaiglfvn tsttitatim
       61 nikrkvldfk famplalslv fsapigayls kyipqiyvky lfiafllfag tmllfgkkeq
      121 kfkydkpwvm vvlgaivgvi sgllgigggs llmpllillg fdakklavtm sfvipfstfs
      181 afltylsivk idwtllgvat vaailggyig nyimhfhlnq kqikkiigil lyiiaakmll
      241 sal
//
LOCUS       WP_457561956            1024 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caminibacter pacificus].
ACCESSION   WP_457561956
VERSION     WP_457561956.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..1024
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113829
     Region          1..1008
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfeffykrgy llsaiilgmf vfgviglikm pknlfpdanr pevviftqvp gatasvvatt
       61 vskpieeema tlsnvyqiks tnvanfsivh vvfdytktlq qasvdvsnal nrikdklpkn
      121 sipaiylvgd ftapvdvfal spkndsitlp eikkiathfi kpkllsnpni gnvevfggyd
      181 savmvkidpl klkkygisfd dlikiiqttd lnmpigfvkt knsfitlsfy gekddvkklk
      241 nllikpnvrl kdianiswsy qtnntlyign napsiaisvq rapsgsvlat sdaareemkk
      301 ieklypnikv tisdtqrnli etsninmlea lrdaiiftli vlliflanfr alaaaalsip
      361 mvffgtiayl yltgqglniv iytaiilalg mltddavvvl enierhlenk edlqkaiyeg
      421 tkevlkpifa gsvstiaiif plmfvggype kifkplietl ivalliswfl svtfipklst
      481 llykkgfkkt rveiffekly qntiaklikp yvgilhfsng kfyvlrrmll iagamivlml
      541 svknimpiig rdvmppmdtg imkahiefss nlnaeesekr lkpfltwlnk qpwlekssia
      601 igtqkdvlsi tgggggnsin mtiiatdrfh rkktiwqled evrnelakip gikkigvydf
      661 gatalstina pldvrvlsdt ykqlpkeaqk iekllynvkg lttimktwdk dfnevvikid
      721 tnkalsygia pagiayqial kdmpvamltn lssmnvqfvr vrfnkqfeni ealkllpidt
      781 kkgpiplgei aqikndftys kidrynlqya idvegyrktr pvslitddad kllkehgikn
      841 ykqagdisem ndsfgrlika iavgvvilil tlmvvyqslr lalimivvlp lsmigaswal
      901 liankpscmp smvgllllfg iiiknavlli dfykefehsg kspfeaaies vkvrfrpvmm
      961 tafgtiagmi pialewavgl erlspiadva iggllvgtfl tlvyvpmlay stdprnkktn
     1021 plks
//
LOCUS       WP_457561957             356 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caminibacter
            pacificus].
ACCESSION   WP_457561957
VERSION     WP_457561957.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39550
     Region          48..356
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkvlkivipi iiaialafgg ykliqlkkem dakektatly pivvkmykpe ykevtltlpa
       61 vaevknsnev aiatkfpgki lyiknlgekv kkgdllvkid dselksqlnt idskiaslkd
      121 kinaqkisle nlikthirtk kllevkmasi eqyqneeski atlkaaikad enslkslysq
      181 kqsildnlky ttiyantngv vsaklfnkgd iapmlkpilk itpnsgnyll vllpkeekai
      241 iykskeypli plkstingik aykaevedkn llpgekvnvk vvtfqgkgtf lpfntiltie
      301 nknyiftpkt keihikasgv egvvieekid tpviqaepdi llkikagypi kvenkg
//
LOCUS       WP_457561958             420 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457561958
VERSION     WP_457561958.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..420
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47388
     Region          122..413
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkklslvlia aslyaadigt lfdaikkqpe tkidnlqvkn akivkksvin slyptvnifs
       61 saehynapfs lrpvtptqsa yllktndsip fsqniirigf dvsmplfikt iydnkekmsh
      121 iinaakykak lnllqresml viylsnlnyl yslkkalsvq knsiqesika ievgvkvgri
      181 pefkllrlkd avnqidikin didskiadtn skiytltkih lkkpinfqts svkkeeflav
      241 kpikenikas lldikakkdd flpkvffkis anrgfgwayn tkdsvalnta sagiyinwni
      301 fnkkrnsevq kakieymnsk ltlqktikel tsqiekidkt lkivnrslsl akksvkikee
      361 llksakvafk lgtmtvdeyl nyendlalak anvanlkatk nsliaqkafi ygnnfkkvfk
//
LOCUS       WP_457561959             180 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Caminibacter
            pacificus].
ACCESSION   WP_457561959
VERSION     WP_457561959.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..180
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21028
     Region          2..139
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkekilktal khfaksgyen tsmkeiaedl gitkpalyyh ykskndlyne ifkhhfqilk
       61 fqkqstnken iihyiktmsk ffhqnpdiak lfakelsceg ehlqeetlki msrtikflqe
      121 slpndinpff iqtliisaft tfqntlnlrk kvskliqksp dfniddeitm tilsyikaks
//
LOCUS       WP_457561963             540 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC1 kinase family protein [Caminibacter pacificus].
ACCESSION   WP_457561963
VERSION     WP_457561963.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..540
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=62255
     Region          4..454
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mfknslyelk rtkeiifvla kygfgdiies lgipvpfket pklsrserir kaieelgptf
       61 iklaqllslr pdlvpldlak efeklqdsvt plpfeemkrv ledefekpyt eifeedfell
      121 asasigqvyk arlktgeiva vkilkpniee kiyadiailq rlakllrdrf liygvdleki
      181 veefaksikk eldfniealn lkrfannfrn nsdikvpkly ekysskrvlt mefiegikis
      241 didalkkagy dlkeitkkgf dliceqifih rffhadphpg nlmvsngkiv fldfgimgrl
      301 sdedrqyfve miyyvikqqe ekaalyvlkl skvqgeidis sfkkemadii ssyfysslkq
      361 velraliedm lkvmqrykiy fkednyllak alvtmegigk klypefnaae eikpfiikiy
      421 kqtispfnil krsheinkav mefitqapsd lneiigklkr gelkvefehv gleefeeaie
      481 ksfnrlstsi iiaslligss mllsshippl fknislfgii gfifasilgv iliftvlrkk
//
LOCUS       WP_457561971             357 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxyqueuosine reductase QueH [Caminibacter pacificus].
ACCESSION   WP_457561971
VERSION     WP_457561971.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Zallot,R., Ross,R., Chen,W.H., Bruner,S.D., Limbach,P.A. and de
            Crecy-Lagard,V.
  TITLE     Identification of a Novel Epoxyqueuosine Reductase Family by
            Comparative Genomics
  JOURNAL   ACS Chem Biol 12 (3), 844-851 (2017)
   PUBMED   28128549
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..357
                     /product="epoxyqueuosine reductase QueH"
                     /EC_number="1.17.99.6"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0052693 - epoxyqueuosine reductase
                     activity [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0008616 - tRNA queuosine(34) biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42123
     Region          4..173
                     /region_name="QueH"
                     /note="Epoxyqueuosine reductase QueH; pfam02677"
                     /db_xref="CDD:460650"
ORIGIN      
        1 miahlccsvd agyflkrlke eypneeiigy fydpnihpys efklrsldtk riceklgiey
       61 vegeydyltw yqktkglene pekgsrcsvc fdlsleeaar fakekgddkv ttsllmspmk
      121 sheqleaigk vvkrkygvdf invdfrkkgg tqaqqqyare nqmyrqdycg ciygiwqqks
      181 hqeiidelis pwpfqvlpss ieekleiyek rieledkgkk ykiikenfln yrllsakvev
      241 kkeviasyvl fysyldrpqr vriefekngi gyanraqvif vkvskineil nkrydnvsei
      301 ykkpltiqee levrknitet efnlspiivl defeevrydi dinskiysdn keilief
//
LOCUS       WP_457561972             266 aa            linear   BCT 27-JAN-2026
DEFINITION  rod shape-determining protein MreC [Caminibacter pacificus].
ACCESSION   WP_457561972
VERSION     WP_457561972.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Martins,A., Contreras-Martel,C., Janet-Maitre,M., Miyachiro,M.M.,
            Estrozi,L.F., Trindade,D.M., Malospirito,C.C., Rodrigues-Costa,F.,
            Imbert,L., Job,V., Schoehn,G., Attree,I. and Dessen,A.
  TITLE     Self-association of MreC as a regulatory signal in bacterial cell
            wall elongation
  JOURNAL   Nat Commun 12 (1), 2987 (2021)
   PUBMED   34016967
  REMARK    Erratum:[Nat Commun. 2022 Jan 11;13(1):329. doi:
            10.1038/s41467-022-28008-1. PMID: 35017540]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..266
                     /product="rod shape-determining protein MreC"
                     /GO_component="GO:0005618 - cell wall [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=30287
     Region          6..242
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional"
                     /db_xref="CDD:237560"
ORIGIN      
        1 mnkryiflfs vllilffqip fvkknviiaf naiketflnl kknindelna isnnkklike
       61 leeknkklsf elsrlnaify tckdlkkfkf irkpgleftq avsyvklpdf tsvyvtfdkp
      121 vphpiglvyn nfaagmivkr vgnygvalln snpktsyavy igkneipgif ygkenvikyi
      181 pkfkpikvgd lvitsgldni fykgalvgki teikekklyq eakiklfydt lnptyfyavt
      241 nkaliapdtn atdtntteen ltkptk
//
LOCUS       WP_457561976             157 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457561976
VERSION     WP_457561976.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>157
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
     Region          9..>156
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 midskkkhii iahrgyrskm pentifafkk alnhadmfef dvqftkdkip iimhdvsllr
       61 ttnaqevfpn kksynvenft feeikkldni swfikqnpyh lsqkeleeik klpknsiptl
      121 ketlefikky nfpanleikh sffskiktsk iickmis
//
LOCUS       WP_457561977             140 aa            linear   BCT 27-JAN-2026
DEFINITION  cell division ATP-binding protein FtsE, partial [Caminibacter
            pacificus].
ACCESSION   WP_457561977
VERSION     WP_457561977.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Hung,L.W., Wang,I.X., Nikaido,K., Liu,P.Q., Ames,G.F. and Kim,S.H.
  TITLE     Crystal structure of the ATP-binding subunit of an ABC transporter
  JOURNAL   Nature 396 (6712), 703-707 (1998)
   PUBMED   9872322
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..140
                     /product="cell division ATP-binding protein FtsE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          <1..138
                     /region_name="FtsE"
                     /note="Cell division ATPase FtsE [Cell cycle control, cell
                     division, chromosome partitioning]; COG2884"
                     /db_xref="CDD:442130"
ORIGIN      
        1 hlgvvfqdfr lipewtilkn vmlpllikgi dkqeaealal kelkkvklsh kadkypaels
       61 ggeqqraaia raiihrpimi ladepisgld eysaslvmdl fklandngit ilvashsmpq
      121 dfsreyrqlh iekgevyels
//
LOCUS       WP_457561978             368 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Caminibacter
            pacificus].
ACCESSION   WP_457561978
VERSION     WP_457561978.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 368)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..368
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42570
     Region          1..368
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrwiviflav lvfgasvttt kkeikktqii iskmndkldk lareirkkqq sinslnskin
       61 slnqeiaklq etlkdankvl gelndlkkgy vekenrikne iidflstnyy ldtqevdnvn
      121 dliyneiskk ileanaqkia kivkqsktin qnissineki dqiikkqqel kskkekllsl
      181 lkarkkeiqa lnrqkllykk rlealirkqk nlqnrlaqlk iikkrkqtsv qqpnynvkta
      241 vykgqktipp lrgrvikkfg syidpvykir iyndsitikp yqknaivrai mpgkvvyige
      301 nndkkiivik hkgdifsiya nldkisplik kgkyvkrgqi iarvtdtlef evtykekpin
      361 plkvislr
//
LOCUS       WP_457561980             706 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Caminibacter pacificus].
ACCESSION   WP_457561980
VERSION     WP_457561980.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 706)
  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
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..706
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82160
     Region          3..680
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mkkdfeqllq riqnikttee akklllsrvd tpkirkaldf aikahsgqkr ksgedyvihp
       61 ilvatitsyf ndnedviiaa ilhdvvedte ytiwyikdef gsevanlveg ltkiveirgs
      121 slapstsnek laksamtfrk mllasindir vlviklcdrl hnmmtldalp phkqkriaee
      181 tlvvytpiah rlgiatikni ledlafkyll peeykkiddy ikkhkeefql rlnefiqkie
      241 klllkngfke nefeiksrik hyystylkmq rkgisiqevl dllavriivk kpiecyetlg
      301 lvhlnfrpli srfkdyiaip kengyqtiht tvydgnsiie vqirtedmdk naefgiaahw
      361 kyklntalpn lewlkdmkye edvedfyela kndlfsediv vyspkfdtft lprgataldf
      421 ayaihtdvgn kaveayvnke kvsllhqlkt gdivrivtgd kniprcswin alktskakye
      481 qkrlcrqkel eidrkvaiai lstifdldkf kiralikann lcesvpkivd dknflkevvk
      541 kiyqtikkrn llyfkniklk eyvfgnikil snkpiqdisf hycchpkfgd kivglldkke
      601 veihhrfcnn aenkiqkavf vewvkndqnr yflvvslpnr kgelskfinf ltrldifihs
      661 islgkesnnc kleiefddkk rdliknkisk eyrviefipi kdayng
//
LOCUS       WP_457561985             262 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook-basal body protein [Caminibacter pacificus].
ACCESSION   WP_457561985
VERSION     WP_457561985.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Saijo-Hamano,Y., Matsunami,H., Namba,K. and Imada,K.
  TITLE     Architecture of the Bacterial Flagellar Distal Rod and Hook of
            Salmonella
  JOURNAL   Biomolecules 9 (7) (2019)
   PUBMED   31284631
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Dingwall,A., Garman,J.D. and Shapiro,L.
  TITLE     Organization and ordered expression of Caulobacter genes encoding
            flagellar basal body rod and ring proteins
  JOURNAL   J Mol Biol 228 (4), 1147-1162 (1992)
   PUBMED   1474584
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Zuberi,A.R., Ying,C., Bischoff,D.S. and Ordal,G.W.
  TITLE     Gene-protein relationships in the flagellar hook-basal body complex
            of Bacillus subtilis: sequences of the flgB, flgC, flgG, fliE and
            fliF genes
  JOURNAL   Gene 101 (1), 23-31 (1991)
   PUBMED   1905667
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Homma,M., Kutsukake,K., Hasebe,M., Iino,T. and Macnab,R.M.
  TITLE     FlgB, FlgC, FlgF and FlgG. A family of structurally related
            proteins in the flagellar basal body of Salmonella typhimurium
  JOURNAL   J Mol Biol 211 (2), 465-477 (1990)
   PUBMED   2129540
  REMARK    Erratum:[J Mol Biol 1990 Sep 20;215(2):331]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..262
                     /product="flagellar hook-basal body protein"
                     /GO_component="GO:0009425 - bacterial-type flagellum basal
                     body [Evidence IEA]"
                     /GO_process="GO:0071973 - bacterial-type
                     flagellum-dependent cell motility [Evidence IEA]"
                     /calculated_mol_wt=29640
     Region          5..258
                     /region_name="FlgG"
                     /note="Flagellar basal body rod protein FlgG [Cell
                     motility]; COG4786"
                     /db_xref="CDD:443816"
ORIGIN      
        1 mingyydvtg amvtqfnrln visnnlanvn tpgfkqddii igdferlfse krselplenn
       61 tkeaakwinh nlnkvpqive eytnfslgdm qrtsnpldia lkrknlffti saqdgeritr
      121 agnfelddkg ylvtkegfkv lntknepiki plnaknlvid sdanvyvnnq kiatlkivsi
      181 dnpktlkkvg dkmwefvpgs esintknstl qgfleksnvn piremtdlie tnrlveryqk
      241 amttfmddlq kdaieklgsv ra
//
LOCUS       WP_457561988             156 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Caminibacter
            pacificus].
ACCESSION   WP_457561988
VERSION     WP_457561988.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..156
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17680
     Region          1..147
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mfnvvlfnpq ippntgnigr lcvnagarlh ivkpigfdis ekavkragld ywdkldlkvw
       61 esvdeflknv dtsrcffatt ktktpyfqkk fkpgdylifg setkgidekv lnehkencit
      121 ipmtregrsl nlavsvgivl yeairqnfde fidfsq
//
LOCUS       WP_457561990             421 aa            linear   BCT 27-JAN-2026
DEFINITION  OmpP1/FadL family transporter [Caminibacter pacificus].
ACCESSION   WP_457561990
VERSION     WP_457561990.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..421
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46595
     Region          5..421
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkktlllssv lvatlfasgy ripeqslkgi alsaanvana sgadsayynp anmvfnedkn
       61 sfellttmih lnkvkfqndn gevyysrked fivpqfhfts kdhngwrfgf svtypaglsk
      121 rwddtipeag akeftlktie lnpviakkvn enigvafgir fvksegianv lglksngdgt
      181 ytplyseyln gdsfdkgwna avafrsddrt lrlaatyrsk inlslsgdas gfynlylitg
      241 npadaakvia fntpgkvtvp lpavlnlaia kkfgkttlef vfdrtywhsy kkldfdfkdp
      301 avnaifgtpk pkdwkdsnty rfgithqcse kltamlgyay despvpnsti dfslpdsdkh
      361 ifsggikykl ddrmsvgisa lytkqktrra svydpitkty tngefkegga vlfaagfdyt
      421 f
//
LOCUS       WP_457561991             659 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease R family protein [Caminibacter pacificus].
ACCESSION   WP_457561991
VERSION     WP_457561991.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Domingues,S., Moreira,R.N., Andrade,J.M., Dos Santos,R.F.,
            Barria,C., Viegas,S.C. and Arraiano,C.M.
  TITLE     The role of RNase R in trans-translation and ribosomal quality
            control
  JOURNAL   Biochimie 114, 113-118 (2015)
   PUBMED   25542646
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..659
                     /product="ribonuclease R family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75838
     Region          1..592
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
ORIGIN      
        1 mkefayklvk gidrkdiprd krdiindlia lgivtsgkii qlkskyrigk vdvtkkgfgf
       61 lipigvkekd ylieahhlng askgdlvvae rlfnkkgrpk akvvyileka faytvaylty
      121 efkngkkqpv lkniktdmpi fvsekkktlk klpdgavfkv nnytakieev lgvlqdpwvd
      181 ekislalynk keefskkaik earaygdyvd ksmypdrvdl tdlpfctidp ptakdhddai
      241 yfdkeknely vaiadvseyv ylngnidrea kergfsiyfp hkaipmlpre lsenicslke
      301 hedrlafvfk itlneknevv keelfeaiin shrkysydrv defldgkfen iddidkeile
      361 wlmplwdrvk niraqrlktg lefesdeikm tldengmikd vtleketpsh kliedcmlla
      421 nkaaakmidf gifrvhdkps qtsldelyse lgalgidvdv dekdftkvve giqsqakemg
      481 ikkfvdklii rsqqqaryda tntghfalgf erythftspi rrysdltlhr ilkatikgek
      541 kildyilrnv ealvvklsel ereamkvewd fydrkyarya dlhigdvykg iiedteippi
      601 akiledkllg arvflkdkqk fnlfekvdie ivkaniatak ikgkvkkees esiiesgge
//
LOCUS       WP_457562000             120 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Caminibacter pacificus].
ACCESSION   WP_457562000
VERSION     WP_457562000.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..120
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13266
     Region          1..120
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mqnkkilivd ddainrklls vtlkkigyev ieaengveal tkitpeislv lldlkmpvmd
       61 giqfmqalkn ekpeclnipi lvlttddekk edarlagake vlikpispie lpdkiasyik
//
LOCUS       WP_457562003             536 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562003
VERSION     WP_457562003.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 536)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..536
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61732
     Region          <349..536
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkkkiliiia fimiistiir tfivgasfln ysnsliknqt nlivdilrev idkdkflhii
       61 qnshpikkie fikgrkneli ysfkdktiis ivpfnelesl kivfsaknyf dkllmaiaql
      121 ilialislii iillvnhflk pyleilekie estnnilkgn fnnkielklk geakdfvnsy
      181 nyflqklkes fgvieekyta liekeksndp lndaketieq lanifkfkri ieednsyeti
      241 lerlidvike fgikhfaiig iennekiakl ihsesdiccn vlenykncra yrlkkeinsl
      301 kmkkeclshy cdtnhiclpf sstgnftgil kiiftdeeke hvlkvlpyik aylneistii
      361 eskytlellh nqnikdpltr lynrryldni lptliegakr rngklgfiml dmdhfkqvnd
      421 tyghdagdrv leklaeiivn sirksdiavr lggeefliia tnvkdkedlr kiaekirlsv
      481 kaqqfylssg lvinktisig aamfpddced gnecikladk alyeaknsgr drvviy
//
LOCUS       WP_457562010             133 aa            linear   BCT 27-JAN-2026
DEFINITION  Fur family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457562010
VERSION     WP_457562010.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..133
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15262
     Region          1..130
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mksyksllee snlkttpqrl ailkeldkkg hasieeiyed ikemfpsisl atiykninal
       61 keenvisevc lhqkpkfeit kephahfick kcgaiedvpf eeiinneiek kypntqkely
      121 iygickkckd gns
//
LOCUS       WP_457562019             177 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562019
VERSION     WP_457562019.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..177
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=20448
     Region          21..>118
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mrkpkvtpid kevflkeedf ivsktdlksr ilygnkifiq isgweenell gqphnilrhp
       61 dmpraafkil ydhiengkew fgfvknlrkd ggfywvfani sptfdtngni igyysvrrkp
      121 regfknviep lyshlksieq sggmeaavde inklaqklnm sfneimikiq kgiidei
//
LOCUS       WP_457562020             358 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Caminibacter pacificus].
ACCESSION   WP_457562020
VERSION     WP_457562020.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10020374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..358
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=41129
     Region          7..349
                     /region_name="rodA_shape"
                     /note="rod shape-determining protein RodA; TIGR02210"
                     /db_xref="CDD:274033"
ORIGIN      
        1 mpvkkfdfil illllpfiai slflvneish rlfikeliyi gigiivfiav flipirkllw
       61 lipvfywini allvlvdffg vrilgarrwl kipfthftiq psefmkttll lmlgyliyky
      121 pprpvytfke flklsvyiii pfvliakepd lgtalitliv gfgvlfivgv dkkvwisigi
      181 fgiifapvyy kyimkdyqkk rieqflnkps yhvrqsliai gsgglkgkdk neatqtqlkf
      241 lpiassdfif ayyverfgfi gasfliflyf slifyllkra eklkddyfak vmyagvalml
      301 fvytfvnmam tmnlapvvgv plplishggt sfinfmilfa ilenlvarke flhthgvk
//
LOCUS       WP_457562022             681 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562022
VERSION     WP_457562022.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 681)
  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 681)
  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 681)
  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..681
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..681
                     /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=77274
     Region          3..674
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 misvctycgv gceidaeikd gkivkihqvk ngkssggelc ikgrygyefl nkrlqkhlis
       61 ydfikreaen mpfflqvrla nlyeyderfy eapfslaadi aawkikdiin kygnrsiagi
      121 ggartnlesa ylfqkfirnt lksphvdnca rvchspslsg lkmsigegas svsfdeifna
      181 eaimiigsnt tqahpmvasr iikakkrglk iivvdvreip imkfadisvi lpfesnllfv
      241 naiakeilkn slqndefikn rcvkfeeyke lilkdkydkh ffeklkgfeh iksqieeisk
      301 iitshktifa wglgvtehid gtesvnaisn lammsgnigk sgagvlplrg qnnvqgacdv
      361 gclpyylpdy vrppedfvgl mtpdiieavl edkikaiinm gedilhihpn qnkiakafek
      421 leflavmevm dneitkkadi vfavksayek tgvyvnaerr chlstplvds nlpddwevik
      481 hienrikgdy dykstedifn eicattgrfr ggsyemlrnf pkpwplsees eilhkekfst
      541 pdgkghfhyh kyhvrgevkd llegkrkwyl ntgrelaqyn naaqtkhsek llkkydddil
      601 lvneihkeqi gdkvvlksvy geskplkvkf tksvrpftlf ttfhfaknhi nylfgdeadh
      661 kvktarfksv evevinvtpa k
//
LOCUS       WP_457562027             230 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Caminibacter pacificus].
ACCESSION   WP_457562027
VERSION     WP_457562027.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..230
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=26542
     Region          <1..207
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mrvllfgfdd fgekvasyie kknleiivfd ekeyekakdk lydvrfyhsi ddaveeledf
       61 dvvlavlrde dknlflclsl kdkfpnkkli akvsnkdndy kyklagvdkt inpyevtanr
      121 imtilkkplt lkvieeiife dnhlafaeve ipkgsfldgk yikdiykeis snyniliiai
      181 vdkemsenvq fitrgvnhki dagdilivvg dmeeierfke dldllriang
//
LOCUS       WP_457562032             488 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457562032
VERSION     WP_457562032.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..488
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=53705
     Region          2..480
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkprvvilga gisghtaaln lkrklgnkge vivvspnsny qwvpsniwvg tghmkpedvy
       61 fplkpvydkm kidfkqakal sihpegdage nkpyvtienv sgtdagkkek vyydflinat
      121 gpklnfeatp glgpdasgtv sicsynhadh awselskvie kmkkgqkqki viglghggat
      181 cqgaaleytl nvaslikdlg ledmadiryi tnemfigdlg magayvknag yvahtkniis
      241 alfyeygvrw hhqssvykve pgkiyyetyq geeltmdydf amlippfsgv gitavgpnge
      301 dytdrlfkpn klmivdadye sakkpyhews gddwpkklqn ptypnifaig iafapphtis
      361 kphttpngrp ltpapprtgm psavmghata mniaewileg kpsfkhkasm aeiasicvvs
      421 igygfrgiag smsvyptipd ynkypdfgrd inytigevgv aghwfkylmh hlflykakak
      481 pgwwlipd
//
LOCUS       WP_457562033             242 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562033
VERSION     WP_457562033.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>242
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          2..242
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviiiggg pagltaglya srlgaktlll ekltpggqit lsseienypg vcdvksglel
       61 mmcwpaqaqk fgceikseea vkiqkenshf ivktpkneyk sktliiatgs tpkkagfege
      121 ieytgkgvsy cavcdgffyk dkivaviggg dtaleealyl skiakkvyli hrrdkfraap
      181 vtqkkvfetk nieiifnatv kkvfgnqfve giilnlngee kelkvdgvfv fvgmkvnnel
      241 vk
//
LOCUS       WP_457562038             192 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562038
VERSION     WP_457562038.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 192)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 192)
  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 192)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..192
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <1..189
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 vslilrfyda segevlindk niknydlhsl rekiayipqn ihifndtiaa niaygkeide
       61 ekvknalkka nlldfvesle ngiytilneg gsnlsggqrq riaiaralyk npdvlildea
      121 tsaldnksea vimktienln dklvfivahr lstienadei lvfkngkivc kgkkeellen
      181 cetfkrlykg nm
//
LOCUS       WP_457562042             258 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457562042
VERSION     WP_457562042.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..258
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28053
     Region          2..256
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mwdlintsiy asillsiaig iigslivink ataitgsiah gsfggigigi flgtsilltt
       61 tiftvilali lalitifyrh radsligviw avgmsigiif lslapgynad alsylfgnil
      121 lvenkdlllm givdlilivs ilvlynrfla msydmeflki rginsnllft yflvltslti
      181 visvraigii lilalftipp liaekftkrf yqmiilssil afifmstgiv isyfydlspt
      241 piiviiaaag lflslfkr
//
LOCUS       WP_457562043             237 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457562043
VERSION     WP_457562043.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 237)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..237
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28204
     Region          7..>89
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <157..236
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlkiqndifl itskyqntqf kphfhdtysf alitdgecvv nfknktthyk kndfriinpy
       61 eihyvksgiw gyksvvfeks yvnsitkeii nkeniifknk ikssklnslf lkmyekqeen
      121 iyfffeells fskeiklpki tlkksieyid enftqkikle nladlehisk yhflrlfknq
      181 tgltphqyii ikrlnfalel mkkeknlayv aviagfsdqs hfikefkkvf gftpkek
//
LOCUS       WP_457562045             296 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457562045
VERSION     WP_457562045.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..296
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=33812
     Region          16..52
                     /region_name="S4"
                     /note="S4 domain; pfam01479"
                     /db_xref="CDD:396182"
     Site            order(27,28..29,31..32,35..36,38,45..52)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          72..274
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mgfvekefei kdekvldflv kkvgfnlrea kraidrgrvs vngkrvtqks qkatgklkci
       61 mfepngyglk pifetthfai fdkpsgvaih pkklantksl lddvralwgn danlvhrldk
      121 etsglvmask nkfaesilkr afqdkdikks ylalvkgrld kemtikkpia vnkdenikvk
      181 viihpegkes vtivkpikif dnytlvecdl ltgrqhqirv hlfsighpiv gdplygvdnd
      241 fadrylnklv tekeriektg anrlmlhsyk lefefmnnky iiksdsffev lknfin
//
LOCUS       WP_457562052             131 aa            linear   BCT 27-JAN-2026
DEFINITION  LemA family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562052
VERSION     WP_457562052.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>131
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
     Region          1..>131
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mkkinlvflm liaflingcm innvpkydee vkakwaqlmn eykrradlip nlvktvkaya
       61 khedkvftev tklrsqvahm kvdinnakel qeyiaaqqkl ssalarllav serypdlkas
      121 knflmlqsql e
//
LOCUS       WP_457562056             206 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562056
VERSION     WP_457562056.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 206)
  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 206)
  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 10616537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>206
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          9..93
                     /region_name="Glyco_tranf_2_4"
                     /note="Glycosyl transferase family 2; pfam13704"
                     /db_xref="CDD:433416"
ORIGIN      
        1 mltmtilvkn eidiieknir fhakkgvdsf vvmdnnstdg trelleelsk efeitiidek
       61 gtynqakwmt klthiarkky npswlipnda defwyaetdl kealknqkka vltvdrfnfl
      121 lyeglknwwe seirvenpif yrkntqlsse nisiiltkis pkviikpkgl lwirggnhka
      181 lhlfdfrdyf rhydkikrfe kirvfh
//
LOCUS       WP_457562057             361 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease, partial [Caminibacter pacificus].
ACCESSION   WP_457562057
VERSION     WP_457562057.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>361
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          18..238
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          146..348
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mesfkiafrn lirmgrrtfl tgsliaigvv fvvlsithae sfknpmiaqi tdsvmgelqi
       61 hkkgyvssld slpldknlpp ktvkkieekl nsmpeiysys krlkfggmis nytdstnirl
      121 ngidpemeak tlpllkerln ghlpkegeiv ipeliakglk lkkgdvvvlv atnkngsmna
      181 ktfkisgvvg iisgpggrdg yinikdarkl lrikkpeine mviklknpem lekvnkelig
      241 ftktiqkpkl evhtwiklsp faniikmldi mtfsieiili sivlvsilnv mimsvferik
      301 qigtmkamgt sksfivsmfv neglllgifg fiigvaasva fvyligdihy nfgrqsnlll
      361 v
//
LOCUS       WP_457562059             209 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457562059
VERSION     WP_457562059.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..209
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23776
     Region          1..197
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkillleddf tladtlkevl esegfevdia nsaqeayekt fnekydlyif dinlpdengi
       61 evlknlrdad detptiyita ltdlntmska fdagaddfik kpfepeelli rlkaklkphh
      121 diikindiey dpqtkevkkn gkiislgfvl kdifhelitn knkvvpkdrl leltnahsda
      181 tlrvnitklk nklgidikni rgegytiel
//
LOCUS       WP_457562058             223 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562058
VERSION     WP_457562058.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..223
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24983
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mvkltnvhks yksgeievkv legldlyiqk gefvaligps gsgkttilni igaldkadsg
       61 nvevagvdit nrdekeltkf radhlgyifq dfnlievfsv fenvnfplkv ihkrkddekv
      121 kalledigms dqinkfpdql sggqkqrvav aralvtdpli vladeptanl dsvtshkvie
      181 lmrkmqrefn ttfifsthdt hlidevdrvl ylqdgkiikd erk
//
LOCUS       WP_457562063             239 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457562063
VERSION     WP_457562063.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..239
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26448
     Region          1..234
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mnlslialsf vlvlipsiia yklnigieke ilknsirall qltalgfvlg flfkitnply
       61 yipvvlfmll ysayiakkrt eysykaafls ltlattiilt ilislkiisl kpnefipiag
      121 miignalnty tltierlkre ielqreliea fiaigarysd alkimqrqai kaalipvnnm
      181 lqtigvvaip gittgmllag asplkavtyq iviiymlvsi nlfsslfgsf fyirekgay
//
LOCUS       WP_457562060             348 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457562060
VERSION     WP_457562060.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 348)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 348)
  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 348)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..348
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40915
     Region          <117..344
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnyekkflis sfliifsilf afilyinyns ynlqvgflnn ktkkeliics ykmncpktdi
       61 nfipknkkpk peilklqedk nsffmvfdvp ylkkyylkls iskteylnal kkikenifrq
      121 fivelafili fsliltyily kplkeaykin etfikdilhd lntpltslkl niyllkkeig
      181 enqrikkleq nikailnyqe nlknflsnnp nqvetfnikd lideklsfys inyphikhtn
      241 sadceitink nafnsvieni isnafkynkk ggeikiymkd kkliiedtgi giknpqkvfn
      301 rfykenergi gigmnivkkl cdelkidiki eseknrgtkv ildlsryc
//
LOCUS       WP_457562067             297 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caminibacter pacificus].
ACCESSION   WP_457562067
VERSION     WP_457562067.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 297)
  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 297)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 297)
  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   5  (residues 1 to 297)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..297
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33577
     Region          4..281
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mvkklkqelk kaivaqdeli dslvaalfvd ghilveglpg vakttaikhl ssmldfkfsr
       61 iqftpdllps diiggeiysm qkdefyikkg pifadlilad einrapakvq salleamqer
      121 qvsigdksyd lkepflvmat mnpieeegvy dlpkaqldrf lmkvivnypl ekeaekailn
      181 vfnkkfsfpk fsssqffntk rqigkitvnp etidyiaeli iafrkdeeie vgpsprasia
      241 lyklakftay ensrnfamps dvlkyikpvl rhritldies eksedevidk iikkvka
//
LOCUS       WP_457562081             353 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Caminibacter pacificus].
ACCESSION   WP_457562081
VERSION     WP_457562081.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..353
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40158
     Region          2..352
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mykkeldilr kkgrfrerki ydeniidlas ndylglaqne nvrknafsha lnfkshgaka
       61 smlvngyhpa hklledylke lnnfedalvl gsgflanmal felgrkgdlf lvdeeyhasg
      121 ivgakltkae vrffkhndfe dlkiksedfk kykrvfvvte gifsmmgdkv kkeicefaqe
      181 igfliideah svgicgenll gvtqeydlnp qktikmgtlg ktlgsygayi ladeeiisyl
      241 lnraksviyt talspidsll ayyalkeiqe nlshyktlvn qrkltynles likiipaksn
      301 eflqkrqkel lnrnvlvgai rpptvkspif rvilrtnidl ktidetikfl gek
//
LOCUS       WP_457562083             627 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457562083
VERSION     WP_457562083.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 627)
  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 627)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..627
                     /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=74522
     Region          397..607
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkyrikldki vllfffilsi fifaalffqy nysknvliqn fvnkhyldti kiresfksll
       61 dkaqyyfkta edenlkflnt lplfyskgnf dvngiakiln ensvfgkyev fkidrnykiv
      121 dgsykpdigy dlgkfkaykq ilndvftgkk didissphld vssmnlkryy livspdkkyl
      181 lqlafvvdmf kdakklyeki lkntpdlkkl kiyyvdnyli tpinfknryq qklplnimwq
      241 rtndifqkil kysnvkidlp kndikkqnim lsklvedifk tkhciiknld ldrhqlvfft
      301 mikgvfeksn srliietiyd tskleanies irkrfllifl avvlgifviy kfvidkvsye
      361 ikeivshmke nkrvenvssf ieeiyelknr yndyhekinq eiaknrrlle enkrfivdtv
      421 hqiktpmsvi tlnldyvkni lstkegfndd einesieevd aaiqmllnsy ndlsyiasne
      481 tvdykpqmln lsqiveerin ffsliakann keirydidkd vyfninrief erlvdnnisn
      541 aikysnkkdi yvslkkeddr iilkiesyge riknpievfe rnyrehshkr glgiglnivk
      601 nicekyqisy ktyykdgkni feyifsi
//
LOCUS       WP_457562085             299 aa            linear   BCT 27-JAN-2026
DEFINITION  PDC sensor domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562085
VERSION     WP_457562085.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Cheung,J., Bingman,C.A., Reyngold,M., Hendrickson,W.A. and
            Waldburger,C.D.
  TITLE     Crystal structure of a functional dimer of the PhoQ sensor domain
  JOURNAL   J Biol Chem 283 (20), 13762-13770 (2008)
   PUBMED   18348979
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13036975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..299
                     /product="PDC sensor domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34203
     Region          <44..140
                     /region_name="PDC1_HK_sensor"
                     /note="first PDC (PhoQ/DcuS/CitA) domain of
                     methyl-accepting chemotaxis proteins, diguanylate-cyclase
                     and similar domains; cd18773"
                     /db_xref="CDD:350341"
ORIGIN      
        1 mhireikdfq kirkearayf cyllqrnlpn klpeitidvv idglekiihe lpfanaayvl
       61 dakgmqisrm itlkneyqet mvevnqanrt yfykavkekk ciltdpypsl vggdmvvsaa
      121 ypifnnkgel lyvavidipl rellkfmhee kgekwfhnfn rvvyglfsla lfsivvllfi
      181 dgvkmffsyn laqldvkkmf estilltlsl alfdlvktlv seevieekee hpfaihktmi
      241 kflgsivial aieglmlvfk famispqklm yaavllaavt flliglayym ksvgkdikd
//
LOCUS       WP_457562087             319 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caminibacter pacificus].
ACCESSION   WP_457562087
VERSION     WP_457562087.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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 319)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..319
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37791
     Region          1..285
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 miklleieny rrlqsfkfdg fkrinlitga nnigktslle aisfatlenp dsvvlnlfqi
       61 lqrrdpelpi rhknepvdsf irdikkrykf fkiksnltki vfessdsiey lfevkvndkv
      121 rkyiqivnpy mlpdvdtkhy vfivdaggsi iklkelykyv qanedeefid enirlfdkni
      181 ekfkiindep svkiknlndy ipiselgegl krfifillaf ykvkdkknsl vlideiengi
      241 wyknyelvwk niiylskkfd vqvfatthsk eliesfvkvi ekenfedmsf iellqdgymh
      301 fdkdtlklei endfevrgw
//
LOCUS       WP_457562094             279 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Caminibacter pacificus].
ACCESSION   WP_457562094
VERSION     WP_457562094.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..279
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31917
     Region          25..222
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkrlgrglga iledaeagyl kelpesgvne idiekiipnp yqprrefsee sieelassik
       61 khgllqpviv ikeddkyilv agerrlrask klgktkikai vapyskedlr eyalieniqr
      121 edlnpveiay sleslikehg ftheelaksi gksrsyvtni lrilsmpeiv kenlkqnkit
      181 lghakvlsgl deqeinevvk kivenswnvr dtekfvkklk nknqtekndn eelneeliei
      241 ayklkkmglk teigkdyikl klrnetdfen lkkllgnin
//
LOCUS       WP_457562099             209 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457562099
VERSION     WP_457562099.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..209
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24019
     Region          19..195
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mliaiiedee dllellefnl qkegydvvgf lnskrvkdfi qeenpdlliv drnlpfvegt
       61 klvknlreeg ydipviflta knsdeniieg feaggddyit kpfnmkellm rvkavlkrnh
      121 kfeniisykn mklnldtktl niedetirlt paefnllklf fenpkrivpk seiadvleig
      181 eksvnvainr lnhkinilea irgvgyklk
//
LOCUS       WP_457562053             246 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase,
            partial [Caminibacter pacificus].
ACCESSION   WP_457562053
VERSION     WP_457562053.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479176
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..246
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - obsolete lipid glycosylation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          <4..244
                     /region_name="murG"
                     /note="undecaprenyldiphospho-muramoylpentapeptide beta-N-
                     acetylglucosaminyltransferase; Provisional; PRK00726"
                     /db_xref="CDD:234825"
ORIGIN      
        1 nvkavfsvgg ysaapasfga ifsntplfih eqnahigsln kilkpfskkf fntflyndpy
       61 pvedkffera rirkelktii flggsqgava indfamriap llkqknikii hqsgkrdfer
      121 vknfyeknsi eadvfdfdkn liekiekadf aisragastl felaanqipt lfvpypyaag
      181 dhqyhnakfl adknaalvir qnelkieild kilnlnleem sknlknvnkk egakyiadri
      241 ldvlsv
//
LOCUS       WP_457562100             259 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457562100
VERSION     WP_457562100.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..259
                     /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=30179
     Region          41..248
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkekilnylk sklfskelqq lenlkeenrk lkkelkkqki mnsfkdevis aishefknpi
       61 siingyieti lesnlppqtq qkflnkiqkn ttrlselidr lylitklenk klkpsfstfr
      121 ldllikdliq sfdeerisln ltpttitadk klieivlsnl isnalkyskk eitinlneky
      181 levidkglgi dkqniemikq kffriakndw dnslglglai vehilklhht hleiesekgk
      241 gskfyfdits lkdkehpqq
//
LOCUS       WP_457562101             185 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter, partial [Caminibacter pacificus].
ACCESSION   WP_457562101
VERSION     WP_457562101.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..185
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..185
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 iyylgpiism llaiwflker gnfyiyisgv lavigavvaa ggvhfqegii vaflaavsyg
       61 algffskiat mhhravavta wqilisifit apflflndwh lslqgiivaf itgvihtala
      121 lflwydalny ikvsiasilq yldivfamil aflflgqvpq ihqilgagli iiagilstfk
      181 ekakk
//
LOCUS       WP_457562102             515 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562102
VERSION     WP_457562102.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..515
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          <1..488
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 lsrkktiqrk ikeiiismkv ehyltkeqil erylnqiylg hgyygiktat lgyfhkplne
       61 lslkeiamli alpkgpslyd ptkhyelnlk ranwilkrmy sigwitdrey rnalletpkv
      121 ykqmvtpkaq yavdtaikql kkefpnllsg gydihlsidl ptqkaaeeav kwnyerllkk
      181 nkkldpnqln galitinqqt gdvlalvggv dyeksefnrv tqskrsvgsa ikpfiyqial
      241 nlgynpasmi pdisrtfkip gdtpeedkyw kpknyekntl glitlrqalv hsrnlatinl
      301 vmsigldrii kgleefgfkn fphdmsitlg slgispwnfs kyytiisnyg vktyprlvlk
      361 vvniknneti efkekheqiq pdyqaylmin imqdvvkkgt grkaqvkgiq iagktgttnd
      421 ykdawfcgft pntetiiwfg nddstslgkg maggsvsapv fkryytkllq ihpellrefk
      481 vpkgvkyfqi nghkelftkm spppkqelke eapif
//
LOCUS       WP_457562110             216 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457562110
VERSION     WP_457562110.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 216)
  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 216)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..216
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25349
     Region          1..204
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkillvedde figeaikdyl emqgnkvdyf ssptkaleti ypshydifll dinmpeingy
       61 efyeelknyt sdvpvifita ysdidhveka fklgaadyik kpfelkelel rikrlvfknt
      121 nrikitdnys fdlgklklfy kdeeveltqn eryfleilvk nigqvvdmst lrdyvwegkd
      181 icdntirtqv kklrsklken fiknvrgsgy kiekng
//
LOCUS       WP_457562113             140 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Caminibacter pacificus].
ACCESSION   WP_457562113
VERSION     WP_457562113.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..140
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15995
     Region          1..135
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mrkflalalf vvsvfafews gkvtwamnyq lakqlaqkeh klimvdialt kcppcrylat
       61 kvytddkvan yinqnfvpvf yladqdqipa eveayftgst ptilfikpng elyfrmigar
      121 ppqmflkilk dvnekykgak
//
LOCUS       WP_457562121             285 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA dihydrouridine synthase, partial [Caminibacter pacificus].
ACCESSION   WP_457562121
VERSION     WP_457562121.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>285
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
     Region          10..285
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mststhksak yflaplagyt dlpfrsvvkk fgcdmtfsem invnaiaynn ektkkmmqks
       61 pletpyfiqv aannvenaik aveiinemee vdgidinlgc pvnkarrsgf ggvllkdenk
      121 eklkeivcai vktskkpvsa kmrlefdeiv avdrakmled lgiefltvhg rtvkqmykgh
      181 anyeeikkvv eavnipvian gditdyekak fvleytgavg vaigrgavgk pwiflemkqq
      241 gditpqqkke vilehfdqmi ywygeygvil frkhahaysk giaka
//
LOCUS       WP_457562124             249 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Caminibacter
            pacificus].
ACCESSION   WP_457562124
VERSION     WP_457562124.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..249
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27660
     Region          4..243
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mvindyqtaa kiikdskfpv aftgagisve sgippfrgpt glwskydpki ldidffmsnp
       61 aeswkyikei fydymgntqp ndahkflawl eeigklkgvi tqnidnlhqk agskkviefh
      121 gtankmecie ckrkfpsdsi slenlpplcp ecqgilkpdf vffgepippk afeesirlce
      181 nadclivvgt tgeimpasql pilakqngak iieiniepsn ytnsitdifl ndkatvasnk
      241 lkeelekii
//
LOCUS       WP_457562129             365 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562129
VERSION     WP_457562129.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..365
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42993
     Region          78..360
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mklyiaigvv vlnllylfft knlkyfffkk rkniflrlly srvykigipf lllidvntff
       61 ylfddrfpns nvkfflnlfl iswlfyevlk yiiytaitik vskkenvrre lfslvinltk
      121 vlivivifva vlshlgvnit aiitslgigg viiglaaket ignffdsirl vsedafhvgd
      181 wietkdfegf vteigltatq irtfdngliv ipnsklanew vknwsrrmig rrikfwlkik
      241 yttdtdelrr vvneirvmlq khpfivtddk iksrlrkkmq knalfsiedk ygvrktllvy
      301 vdkfdeysid iliyafsitv dweewlrvkq dvmlkvldii knsklelayp tnvifyderk
      361 nlwkn
//
LOCUS       WP_457562132             179 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562132
VERSION     WP_457562132.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..179
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=20797
     Region          110..179
                     /region_name="DjlA"
                     /note="DnaJ domain-containing protein [Posttranslational
                     modification, protein turnover, chaperones]; COG1076"
                     /db_xref="CDD:440694"
ORIGIN      
        1 mhflhsinse tlntilligg giivffiflk sllssgssnd yskngyyyyq rrgysyketn
       61 rkkdndysyy gydknysygn ynynqnsnns ynnssnnnss nnskkeyqsf tsknpyqvlg
      121 cketdstdti kkaykklika fhpdiiagyn lhedfitfak irtqqinday nkirklrgf
//
LOCUS       WP_457562133             358 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457562133
VERSION     WP_457562133.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..358
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41302
     Region          1..358
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mkpfivmdvl kkaremkdvi hleigepdll pspkvktall eavkndkffy teakglrklr
       61 ekiskhyknf ydvevdpeni iittgtstgf liafhfakki atptpgypcy enfaelenke
      121 fikipikfpe yklktedles idfdtlmiss pnnptgtiys kkelkeicef tknnskllis
      181 delyhglvyt dnyttalkyn knaiiingfs kffcmpglri gwmivpenlk reaeiiaqni
      241 lisaptlsqy aaleafdyeh lqktkeefqk rrdflyeelk difpiakpeg afylwcdisk
      301 ysndslkfan emlekakvat tpgidfgeyn nfiriaytkn ieelkiaakr iknfinsi
//
LOCUS       WP_457562134             195 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Caminibacter pacificus].
ACCESSION   WP_457562134
VERSION     WP_457562134.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21300
     Region          2..185
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdylilafvg fvaaltpgpd ifyvirqglc ngsknsliav agilsgnivy lslvylglgt
       61 igknpyfqli vgilgaiylf riaviifnek vsikkecdit kniykealfl nlsnpkamif
      121 favvvtpfls knimlsflal flgialaflt gavisskinl eekllnlink iasvvfvffa
      181 iklliiafea fkeif
//
LOCUS       WP_457562148              90 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562148
VERSION     WP_457562148.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..90
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10407
     Region          <20..81
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mkkttsemie elkakgfkdi fiwsdskgty ydwhkhpyde irvmlkgemi intkenqyhl
       61 kggdvlnvpa gevheayvle dceyicgsky
//
LOCUS       WP_457562149             108 aa            linear   BCT 27-JAN-2026
DEFINITION  OmpA family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562149
VERSION     WP_457562149.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..108
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          1..102
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(4..5,38..39,42,46..47,50,93,97)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 nfdfnkayvk kiyypqikkv aevlksnpkl kievagytdn vgsasynqkl sykrakavad
       61 ilikkygvds krivvkgyge kyplvpntta tnralnrrve ivaisglk
//
LOCUS       WP_457562155             421 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562155
VERSION     WP_457562155.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..421
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48478
     Region          4..420
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mfkfseisdm cikcgkcipg ctihrvnpde atsprgfldi lkgveegdie idknfkdtve
       61 scflcnqcve vcpnslptdf mienarakva ekfgiawykr afffllkhrw aydlvsklgf
      121 yfqtcgfkie eekkairsrf slpmlhkgrl lpafrktsfl kkypekipak npqkrvaifi
      181 gcmanynyte vgdalvkilk fldidifipk kqaccgapay ftgdfkttee likrnieyfe
      241 tfidevdail vpeatctaml kkdyeeyiky hmnnewlkrh ekvkakifgt tewlykytdl
      301 ekrlnkklns svtyhdachf gkvfnirkep raliskvvei kemedpnvcc gfggitmqte
      361 kfhlarkegl ikaemikkvd aeyvsaecsa crmqitehld kvgdnkifvh pleiiakaie
      421 g
//
LOCUS       WP_457562164             663 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Caminibacter pacificus].
ACCESSION   WP_457562164
VERSION     WP_457562164.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..663
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75791
     Region          1..615
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mkfldelnda qkeaathidg allilagags gktktittrl ayllslgidp antltltftn
       61 kaanemrera lsllegqnip hppllstfhk fglmflklyi hlinrdnnfv iidsddqrki
      121 ikqissdlpp nfiskeisky knsfltpdev yalatdsvyk nlahiyekyq nyllennlvd
      181 fddlllltyk ilnenddlad eisdkyqyim vdeyqdtnei qllllkrlck nhnnicvvgd
      241 ddqsiygfrg anhknildfe kdfnakvikl einyrstnqi lnaannlisf nknrygkkli
      301 sargdgkdie ilrnyneiae aemiakkird linqgvdpke iavlyrinal srsiedglrn
      361 ygipyklvgg mkfyereeik dlisylrllv nphddysfkr vvnkprrgig katiakieea
      421 kgdksfieyi kendlsiisk kaaktlkdfv ntlellskms ldelpenlee ifelsksykd
      481 edkarnieef ygmmrersdl nireflnels letdqdkitm dminvmtiha skglefdhlf
      541 vigmeegffp lndadieeer rlayvaitra rkdltlsyve sryihgkrsp vnksrfltea
      601 glikgervel kessaiktgs lvkhkvfgtg rvlginkagn ktklkidfgg svreilsdfv
      661 ekv
//
LOCUS       WP_457562168             360 aa            linear   BCT 27-JAN-2026
DEFINITION  PilZ domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562168
VERSION     WP_457562168.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..360
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42990
     Region          240..338
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 msknrfyken fsafikenek ffktveskft hnflellkkk npnipitsql kneienlyks
       61 lfledyssqn fklnaifilk ernvdiedil nkvflllana fikytlkekn aiaklkklts
      121 lfefyieyli fhvneeefft yhlpkelkey yltnevlnlf nvykgvpith kttiltlned
      181 rgyieveans yqiiaakfqk eiyllepttn ttfkayidyv ypqrkvlklt niekiqrntp
      241 krnyirvqps tdinvkikkh kdifttkmyd islkgmavis dektvdigdf vklefilegy
      301 ffemtaevrs itklndsfrf hfyfeptpsq erilekyitk rekeiikelh kylkaefidv
//
LOCUS       WP_457562173             321 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-ACP synthase III [Caminibacter pacificus].
ACCESSION   WP_457562173
VERSION     WP_457562173.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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   3  (residues 1 to 321)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..321
                     /product="beta-ketoacyl-ACP synthase III"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0033818 -
                     beta-ketoacyl-acyl-carrier-protein synthase III activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35148
     Region          1..320
                     /region_name="PRK09352"
                     /note="beta-ketoacyl-ACP synthase 3"
                     /db_xref="CDD:236475"
ORIGIN      
        1 myakftsiga yvppkiltne dlekivdtsd ewitkrtgik trhivenevt sdlaykaald
       61 alknakmsae didmiivati tpdyftmpst acvvadklgi arpavdisaa ctgfiyalah
      121 akafiesgmy knvliigaet lskivnwkdr ttcvlfgdga gaaiisaten keeaiididi
      181 nsdgkyqdyl itpgrgvkyg cdtdriwlem kgnetfkvai ktlsqsvrdi lkrnnmtsdd
      241 idwfiphqan yriidavara ikmpseksvl tvhkygntss asipmaindm ykegklkkgd
      301 imlldafggg ftwgsalvpf n
//
LOCUS       WP_457562178             315 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457562178
VERSION     WP_457562178.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..315
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36123
     Region          8..315
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 melpksqqel lqnleklieq tyeaekefie lknilngvie flpqalwvvd ksgevivkns
       61 kadefdfipq kgeievndkv flvqtsnikd ktiisatdit eqkrnerlia mgqmaahlah
      121 eirnpigsis illallkksc pqnemidemk saifrierii kstllfskgi rlnkrkflls
      181 slkkeleeni kyyshskein fvyflpdiei kadydllllv lqnmiinaid aieddekeeg
      241 lievlyektd kyhiiniyds gkdfedtnil fepfkstktk gnglglalsk eiitahegki
      301 elskekkgfk iylpi
//
LOCUS       WP_457562184             577 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family oligoendopeptidase [Caminibacter pacificus].
ACCESSION   WP_457562184
VERSION     WP_457562184.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..577
                     /product="M3 family oligoendopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=68346
     Region          43..564
                     /region_name="M3B_PepF"
                     /note="Peptidase family M3B, oligopeptidase F (PepF);
                     cd09610"
                     /db_xref="CDD:341073"
     Site            order(370..371,374,397,490,497,501)
                     /site_type="active"
                     /db_xref="CDD:341073"
ORIGIN      
        1 mmnwdltplf ssiseaeefl kqaefkaief ekkyknrlyt ltpeeflnvl kefeeiweni
       61 graltyiylv fatdstkgnf lgkfqelatk aeehlvwfel efiylpidkq qrfidnagvy
      121 kyylihlqee apyrlsekee kilmkkdlts ssafsrlfde tlsrlrfffe gkkyseeeil
      181 sklyspdrnv rkkaqvsltl glkphqella yiynqvkkdw kidhieirgy dspeeprhls
      241 nrvskksvda lvnsvnentt ivadyyeikk rllgydklfd ydryapiklt dktpeisfee
      301 akelvlnafk nfsntfyeia kkafdekwid vypkegkrgg afshsatpka hpyvllnytn
      361 qrrdvftlah elghaihqyl arevgylnqd tplttaetas ifaemllfee ikssldkkel
      421 ietyaakled vfatvfrqiv ftnferkvhk fdelkpedyn kiwmeenqkm fkdsvilten
      481 ykiwwsyiph fihspfycys yayaqllvft lyklykegfe nfeekyiefl kqggsippkk
      541 qlkelfgldi enenfwekgi aviremlsef kglcddi
//
LOCUS       WP_457562185             116 aa            linear   BCT 27-JAN-2026
DEFINITION  HIT family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562185
VERSION     WP_457562185.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..116
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
     Region          1..102
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(3,5..6,13,15,60,68,70,74,76)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(72,74,76..78)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            74
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 ffvmnrfpyn pghfmiipir hvgeyedlse kevchiakma qkgckilkdf gadginmgwn
       61 lgfdagagip ghihlhlvpr fkrdtnmmtt vfntrvysad fdkifeeike iskkyl
//
LOCUS       WP_457562189             672 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Caminibacter pacificus].
ACCESSION   WP_457562189
VERSION     WP_457562189.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..672
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76863
     Region          3..667
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mplsklnkeq lqaataplgh nlviasagtg ktstivgria ylleegikpe eillltftnk
       61 aaaemkerva rvipsaknie agtfhsvsyr wlkklnknit lktpkdlkil fksiydkrdf
      121 srlgieekpy sanylfdlys lylnsnapsf eewllqkaps hepyaliyed ifdeyenikk
      181 ehnlvdfnsl lieminhlkn gienpyrevl vdeyqdtnpl qneliesvkq eglfcvgdyd
      241 qsiyafngad isiistfdkr yenakvftlk knyrsygeil dianrviknn priypktlev
      301 trgysgeypk vlmyndtfee yrdiasrilt sttkreeiai lfrnnssada ieamlrekgi
      361 eckrkggtsf fdsreikitl dlltflinpk dimafihife yakgvgsaia geifealmtl
      421 gdgdaikgfl npdtskkvft kkrtsyqlgl fddfvtlgsv skfvnlgfde eflanpilrh
      481 pklsiegaef lhnfyqflkr ikrfknpqai fnelinskif dhiisniake rakdkngkid
      541 eeryheakek iknkvkilgn llknysdler flnamvlgas emsegsgvnl ltvhaskgle
      601 feevyivdmm egrfpnikls kpaggieeer rlfyvavtra kdrlffalak ndriknitye
      661 psrflkeagy kv
//
LOCUS       WP_457562190             139 aa            linear   BCT 27-JAN-2026
DEFINITION  macro domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562190
VERSION     WP_457562190.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Rack,J.G., Perina,D. and Ahel,I.
  TITLE     Macrodomains: Structure, Function, Evolution, and Catalytic
            Activities
  JOURNAL   Annu Rev Biochem 85, 431-454 (2016)
   PUBMED   26844395
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Karras,G.I., Kustatscher,G., Buhecha,H.R., Allen,M.D., Pugieux,C.,
            Sait,F., Bycroft,M. and Ladurner,A.G.
  TITLE     The macro domain is an ADP-ribose binding module
  JOURNAL   EMBO J 24 (11), 1911-1920 (2005)
   PUBMED   15902274
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>139
                     /product="macro domain-containing protein"
                     /GO_function="GO:0072570 - ADP-D-ribose binding [Evidence
                     IEA]"
     Region          4..>137
                     /region_name="YmdB"
                     /note="O-acetyl-ADP-ribose deacetylase (regulator of RNase
                     III), contains Macro domain [Translation, ribosomal
                     structure and biogenesis]; COG2110"
                     /db_xref="CDD:441713"
ORIGIN      
        1 mykivikkgd ifseksadfi vnpsntelil gsgvsgafrr vcgsalqnem rklapikqge
       61 vavtdcpghp eykkalhvai mdytsnnpsp tlevikkslq niekiiknht pckivlplmg
      121 vgvggldkee vikiykeff
//
LOCUS       WP_457562197             323 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Caminibacter pacificus].
ACCESSION   WP_457562197
VERSION     WP_457562197.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..323
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36202
     Region          1..314
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mnsarvkkfy ylmklgrefe laakreymng niagflhldi gqeavsvgtm qafdkgdvft
       61 hyrehvlala rgmepkrvma elfgkktgis kgkggsmhlf epkldfyggd aivaghlpia
      121 vgcayarkiq genagvfaif gdgasnagaf fesiniasaw klpiiffcen nyyaigthis
      181 wvspfvelyn kaknymptkr ingmdvcevy navmeakthi englspyfie aetyryeghs
      241 msdagkyrse eeleifkrkd pienlkkkai elgivdekyf qeadakvqnv ieeavkfaae
      301 spepedyelf edvfckecen alp
//
LOCUS       WP_457562198             324 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Caminibacter pacificus].
ACCESSION   WP_457562198
VERSION     WP_457562198.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..324
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35895
     Region          1..318
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mlyrealnka idesmaadns vvilgedvgr yggsyrvseg lfskygekrv idtpiaelsi
       61 vgnaigmaia glrpiaeimt anfsllamdq iinhaskfry msggkmtipl tirmpggvsr
      121 qlaaqhseny etlyssipgl ivlaasnaty ayyglksaif mndpvvfleh ellypmdmef
      181 keiknfdpfk aevvkegkdl tiitylkmry dvleaqkalq kagidaeiid lnslrpidie
      241 tiaksikktk kyviveedhk tggmgaeiaa qimencfydl dapvlriage dvpipynrkl
      301 ellsiptpek ivkkilkwka engi
//
LOCUS       WP_457562199             399 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562199
VERSION     WP_457562199.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..399
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44559
     Region          1..394
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 meykvtmpil sdtmdkgkli kwyvkegdrv kkgdklceve sdkatmdies fvngrvkkil
       61 vkegeevpvk sviaviesee skqetkneqe eikktkekns ktntdssidi delinsivne
      121 pstkvsgsas paakqkakkl gidieslqks gelptpahek dideviikky fspkaaklik
      181 eygldfdife lnrkiesdev mkyiktnnip kitklspnqi aviktvqnai kkptffvfee
      241 veitkkenik ltaqiikala tamqkhpltr silkgneilt yptsnisvav arddglfmcv
      301 iknaedksle einewlkeik tkklsiedls gstfgisnlg mfniksftal indndagiaa
      361 fgalnnnkme vsftidhril ngvdaakfin dfkeecknv
//
LOCUS       WP_457562200             431 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562200
VERSION     WP_457562200.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..431
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47156
     Region          1..431
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mydviviggg lgyaaaivls kagkkvalie knlehlggtc lhngcipskn llhraktlle
       61 lkegffdgev slnlkklqnh iskiitshtk avknqllmak veliedegyv tddgvllknq
      121 nktlqakyii iadgskprip egieydgkri itskealelk napkeitiyg sgaiglemas
      181 ffsaigtkvn llyrhsnisk kfpqiitekl eeqlknigvn lmpnseikea ktehskvicn
      241 ingkefstdy lllaagrvpk tdivqtdkik iqkgivtdey fqttmpnvya vgdcngklml
      301 ahaaraqaln vanqilgkke klilenipkf iytlplsyan igtkgvkeae fpinylgiag
      361 slygdelgiv kiyadeenfi tgadilapna eeligifssa laaevdidtl kkavfphpty
      421 seaidralrr f
//
LOCUS       WP_457562206             293 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caminibacter pacificus].
ACCESSION   WP_457562206
VERSION     WP_457562206.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10508826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..293
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33664
     Region          5..273
                     /region_name="LPG_synthase_TM"
                     /note="Lysylphosphatidylglycerol synthase TM region;
                     pfam03706"
                     /db_xref="CDD:461018"
ORIGIN      
        1 mvtkiiktvl laaiifyify gfdfskidls vispktvlls sfvlflgqii lsirfmyiid
       61 skflpaleti vvsnalnmil parlgeaaka vylkkfynyp ynvgisavfi erffdvimlf
      121 liiigwiyff vteeyvkksa iilfffiilv lvffntgfmr slvekipfey pkivyknins
      181 mfkkspvlif wsivlwgsyl lsyyiffdml gfkevvelfi vstvalmipl apaglgtfeg
      241 vvvfylhkyg iskedallla styhfllfav dmimfavfll lkdikfselk alk
//
LOCUS       WP_457562208             477 aa            linear   BCT 27-JAN-2026
DEFINITION  HD-GYP domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562208
VERSION     WP_457562208.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..477
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55458
     Region          <287..464
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mtdiryllnv kiplrvneel nevlgflqkg wvfyilvali fffaflymfr ryfeekkkfi
       61 nfdsilekla dtkdinveeq iimnelkiak niafyqsrgn vyilidskte kiefpfripk
      121 edldeyknig dnkvgyikns dekylllfad kkldiedykg hlklilnyye ktfeknikda
      181 vslvsdnaak sfmkinmnqe eflrfftsll kkivksekvy llknseniei qgnfkkdfyi
      241 rntpykvtvi keenlspqei kkigsfidla ghylvnfasn kkiidnyiel lklaveamei
      301 nnpfyknhse iveivsveta kalylsqkei dnialasklh digmigdmvn fldktelske
      361 elnllkqhpi igssivepin qtyeiadiik yhherydgrg ypfglkgvni pisanivalg
      421 efyagitsdr aykkgishde avkeikdlsn kyfeksivda flnvekrint kilkvkk
//
LOCUS       WP_457562212             116 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosylanthranilate isomerase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562212
VERSION     WP_457562212.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..116
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - L-tryptophan biosynthetic
                     process [Evidence IEA]"
     Region          <3..110
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 vekeffdklt ckylpvvrak eksdidkfee nykivdayvp eyggsgkrva lewfenrdns
       61 kiilaggltp envfevgryg fygvdvssgv eerpgkkdkr klrkfielak yglrcg
//
LOCUS       WP_457562213             817 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457562213
VERSION     WP_457562213.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 817)
  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 817)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   3  (residues 1 to 817)
  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   4  (residues 1 to 817)
  AUTHORS   Borziak,K. and Zhulin,I.B.
  TITLE     FIST: a sensory domain for diverse signal transduction pathways in
            prokaryotes and ubiquitin signaling in eukaryotes
  JOURNAL   Bioinformatics 23 (19), 2518-2521 (2007)
   PUBMED   17855421
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 817)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 817)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 817)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 817)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18684138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..817
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=94887
     Region          1..359
                     /region_name="FIST"
                     /note="FIST domain protein MJ1623, contains FIST_N and
                     FIST_C domains [Signal transduction mechanisms]; COG3287"
                     /db_xref="CDD:442517"
     Region          <400..817
                     /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 mktynliftt kkeleeffkk lpkkenliqi fsgvldkgki kevtdtiidv ypnakiigtt
       61 tdgeiidgkt tfkkivisvs lfdkvnvktl llpkykrsyl fgkefakklv tkdskvliaf
      121 adamsvnged fingiesesk iivsgglagd narfkhtfvf detniiqnga vgavlegdii
      181 vnnefgfnwe gigksmkiek aiknrvyrid gktpvelykh yfgeefdnia kigirfpliv
      241 krdkmyvara vlkqfddgsv llagnvnegd evrfgfgdvs silykdeelf kkisgfdves
      301 ifiyscmark rflggyikne irpfskvgsv sgfftygeff srthnyffnq tltvlalsen
      361 erkvkidyey nkpkkfftlk altnliknts qelnelnknl eeilrektkq imrksyemeh
      421 mfyydqltdl pnkylfekdi evydvegmvl vdirhffrfn dlygegigdl ilkeiakkll
      481 tlvdnknikl yrwgadqfif vgfekrnfvs lgkkvlellh eklivkidkt sipfdfeavv
      541 svvdkkyknm kakadlalny akrnnlnfii ydksldmess irneintlkk vkkaikedri
      601 ipvfqkieke dsvsyesllr ikennklitp geflevirfs yyyfevmkim iektlslfsk
      661 reekvslnft yrditnknvv kclidqikkh nmqnkvilei vesedlkdfq kvhefikrvr
      721 kegveiaidd fgsgysnfvy ltelkpdyik vdgsliknih kdynsyiitk nilnfaedmn
      781 cktiaeyven eeiykkvkem gfdgyqgnyi hkpqeep
//
LOCUS       WP_457562217             130 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase, partial [Caminibacter pacificus].
ACCESSION   WP_457562217
VERSION     WP_457562217.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>130
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          1..>130
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mrvilfdldg tlidsteail egfrvvfekf gktpasddev kkliglpldi mfenlgikeg
       61 vwdyvnayke hyrkiskqkt illpnakeai lkakefarlg ivttktglys kellehfgvm
      121 kyfevligre
//
LOCUS       WP_457562219             202 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562219
VERSION     WP_457562219.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..202
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23094
     Region          15..167
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mnlfdlyyed yekwfekhpk iyeeelktik tllpkgrgme vgvgsgrfaa plgikfgiep
       61 srkmaeiarn rgievleita eemnfeeefd filmvtticf vkdplktiqn cykalkkggf
      121 llvafvdkns plgktyeknk qnskfyapat ffskddiinl mkkagfknfe ckenlygdsl
      181 dnlkfkindc nggafkvirg kk
//
LOCUS       WP_457562220             103 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457562220
VERSION     WP_457562220.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..103
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=11822
     Region          1..101
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 myeqysivlv nldptigsei kktrpcviis pnemnfnikt liiapmtsks keyptrvkik
       61 ddffivldqi rtidkkrvik qlgkidlkti seikkilnim lve
//
LOCUS       WP_457562237              81 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-binding S4 domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562237
VERSION     WP_457562237.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Novel predicted RNA-binding domains associated with the translation
            machinery
  JOURNAL   J Mol Evol 48 (3), 291-302 (1999)
   PUBMED   10093218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..81
                     /product="RNA-binding S4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=9145
     Region          1..>81
                     /region_name="HslR"
                     /note="Ribosomal 50S subunit-recycling heat shock protein,
                     contains S4 domain [Translation, ribosomal structure and
                     biogenesis]; COG1188"
                     /db_xref="CDD:440801"
ORIGIN      
        1 mridkflnav nivkrrsiad emckegvvfi ngkkvkpakd vkvgdvieih ylsgikkyev
       61 lklpetktip kskkseyvke i
//
LOCUS       WP_457562246             382 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Caminibacter pacificus].
ACCESSION   WP_457562246
VERSION     WP_457562246.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..382
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42507
     Region          1..382
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mqkvdhkifi ivavlmlaga vfsftlpvfl emrrhlseyh flgryilfgs vgflimilla
       61 nlnpdkwfnk igwiifiisg ilvlilpflp esiapiinga krwikigpfk fapveffkig
      121 vifflswsft rkikkthhlk edikqflphl iflglfwili vfmlsdlgqv fvmislfilm
      181 llaaggklkt fgvmvlaavs iivpailfap yrfkrikdwl ytassnflpq pivdgssany
      241 gqviqsmnai hhggifgtgl gngifklgfl sdvhtdfvla giaeetgiig iglitfligy
      301 liyrifkiaf rsekkeyqlf algvgsliai qfiinglgvt slipikgltv pflsyggssl
      361 malctaigmv lmiskrakyi ke
//
LOCUS       WP_457562248             569 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562248
VERSION     WP_457562248.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..569
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=64985
     Region          41..554
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnnripaifl ffiffisvvf aafvflaiak pkgyftpkik itqsavrgdi ktkdytvaks
       61 eklygvyiyp kyldpdkkql fytlfsiytd ipvrelkrav iigkqnglsr iriatvdlkt
      121 kqnliylrkv ldkkrvfltd krtgirlgye iesldfkrvy pykdtlqpfl gryrkderrg
      181 dnglelyynd vlsakqdgyk igyrdvygni iydksakikr pingkdikln inlalqrkie
      241 kflsfqkqkl qakevlaavm dsksgkilai assnrydpah itprdipnmk isavrevfep
      301 gsvmkpitfa illennkvnp yevlnahngr wkpewrktpi rddepfnwls aedaivhssn
      361 ivlselslrl tpdeffnglk kfgfasgtgi dlpyevkgmi rsrrllnypi yksttaygyg
      421 ilvtfvqllk aynafnnygi evtprlanmp seskrvmsak naeimlkilr kvvlkgtgka
      481 aivdgiftag ktgtahvsmg kkgyqqiyns sfigfandkn hrytiavtff dikakwpnyf
      541 asksavptfr kiidiminen llketnatk
//
LOCUS       WP_457562251             427 aa            linear   BCT 27-JAN-2026
DEFINITION  NCS2 family permease [Caminibacter pacificus].
ACCESSION   WP_457562251
VERSION     WP_457562251.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..427
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45546
     Region          1..427
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mferifklse hgtnvstevr agfttflamm yivpvnasim sltgmpfdal itatavvtii
       61 atilngfwsn tpvamsvgmg lnayftfglv kgmhlpwqta lgivmisgli flvlsltrfr
      121 awvfesvpid lrraisagig afiafiglkg mgvivsnpat fvtlgnlhnp evllgvegfi
      181 laalfysyri kgafilsial tsitawvfgl gklpegiism pasiapiafk fdiwdalkls
      241 lvpvivtflv tdlfdtigtl agigmraglf kdpkelektl qadaaatvig aslgtsttts
      301 fiesaagvee ggrtgltavv tgllfittlf flpifkaipd naiypilvmv gvlmfgelrd
      361 vdfsdittsv svfltvilmp ltysitlgls agfvvyfila llrgekekit fgtasialig
      421 llmfivh
//
LOCUS       WP_457562249             363 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562249
VERSION     WP_457562249.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..363
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41882
     Region          73..358
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqqnsfesll nilnykflsl plykivlafv vlflflvlrr aftlyilkff rflvrktkte
       61 lddkflkaik nplrflfvia glyffflfle vdyaiikhil kgllifdifw alynivgefe
      121 eyiykglgkf grasrefvsf iikllkifiv sigiiallqd wginvtgfla slglgglafa
      181 laakdtaani fggiailtdn ifkigewvkv gnvegivedi gmrttkiraf dkrliilpna
      241 tiansaveny srrdkrrimm riglvyntpi etikkitdei remllnhpdi akdeslliyf
      301 dqfedsslsi fcyfftntav wkdylrired inlkiidive rngsafafps nsiyfetplk
      361 ier
//
LOCUS       WP_457562253             113 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457562253
VERSION     WP_457562253.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..113
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13621
     Region          1..113
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mlnrdkelfl rdiiesidai fdhikgyele dfkndrktyq avvkefeiig eatknvyell
       61 kekypnypwr liidfrnklt nedfgvdfvl iwntiflklp elkqmiekli kef
//
LOCUS       WP_457562255             366 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Caminibacter pacificus].
ACCESSION   WP_457562255
VERSION     WP_457562255.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..366
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40356
     Region          1..358
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 milatpgpve iplfvretfl ketihhrtpe fkeilleale rfkkithlpn avflsssgtg
       61 ameaavinsv kkkaltinag kfgerwgkic eahgiefkei kydwdtpasv deviaaieed
      121 kdidtffiqi sesagglrhp veeiaaeikl inpdiivvad gitalgvedi dtsnidivig
      181 gsqkafmlpp glamlglsdk avdrigkgrg fyfnlaneik kqkegttaft patsliialn
      241 evmkkleeig ldkhyettak rhkaiiaaie aiglsifpqv palsmaavyf ekaeelrkil
      301 ktkyevnvag gqdfmkgklf rinnmglied ykmehilnsv elaldelgir kydatavkvy
      361 sneklr
//
LOCUS       WP_457562260             403 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate
            ligase [Caminibacter pacificus].
ACCESSION   WP_457562260
VERSION     WP_457562260.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Gordon,E., Flouret,B., Chantalat,L., van Heijenoort,J.,
            Mengin-Lecreulx,D. and Dideberg,O.
  TITLE     Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:
            meso-diaminopimelate ligase from Escherichia coli
  JOURNAL   J Biol Chem 276 (14), 10999-11006 (2001)
   PUBMED   11124264
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..403
                     /product="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,
                     6-diaminopimelate ligase"
                     /EC_number="6.3.2.13"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008765 -
                     UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45299
     Region          <58..403
                     /region_name="murE"
                     /note="UDP-N-acetylmuramoylalanyl-D-glutamate--2,
                     6-diaminopimelate ligase; Provisional; PRK00139"
                     /db_xref="CDD:234660"
ORIGIN      
        1 mdlihylnns litdntkeld snklflktsq nskyakdikn yitpkellks lnlktkfigi
       61 tgtngkttta fvlgyllnsl gysvgiqgte gfyfngelke pktlttppif ttikrafkyk
      121 pdfyimevss haivqdrieg lefeakimts fsqdhldfhk smeeykqvke sffqddsiki
      181 ingkckmeng kliivniggy dfkvnpnnly vlekpivddi pmagefnkmn fslalktasl
      241 ltnsslstfd fslfkgvagr meivskdplv iidfahtpdg mekvlsaveg kkivvfgagg
      301 nrdkdkrhlm gevaskyady iivtndnprc enpqdiakdi ikgiskpyev ildrkeaikk
      361 alklakeknl tlmilgkgde kyiefcdkki pfsdkeavfe vis
//
LOCUS       WP_457562262             215 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562262
VERSION     WP_457562262.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..215
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
     Region          <1..200
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 ldlsslaiia galsvgigfg lqnivsnfvs giilmfersi kvgdyiqide ntrgevvdis
       61 mrstiirtnd ninliipnqs fiqnnvinwt lgddlvrfrv pfgvaygsdi dkvekvvlga
      121 ienaklhyik khptldvtpr vvflemgdss lnfelmvwvr gayarrprrt rseflkviyk
      181 alnnagieip fpqqdlhird svpieirvkk edkqn
//
LOCUS       WP_457562263             253 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Caminibacter pacificus].
ACCESSION   WP_457562263
VERSION     WP_457562263.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  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 253)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..253
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <27..244
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 isilisfviy liilmigykf idaiakqiem sfaklkrfns nvshelktpl aimkseieva
       61 lmnntkdcek tlksmlqein yinditekll fltketkkik ledvdleeli lelfekyaek
      121 iefeldfgde eydikgdktl lkmalsniie nsikyganki vikleknkhk iiltikdngi
      181 gipkeklpfi fdefyrvdes hnkkikgfgl glsivknilt lhkakikvns degkgvefii
      241 efplithqek ksa
//
LOCUS       WP_457562265             328 aa            linear   BCT 27-JAN-2026
DEFINITION  SagB/ThcOx family dehydrogenase, partial [Caminibacter pacificus].
ACCESSION   WP_457562265
VERSION     WP_457562265.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Ghilarov,D., Stevenson,C.E.M., Travin,D.Y., Piskunova,J.,
            Serebryakova,M., Maxwell,A., Lawson,D.M. and Severinov,K.
  TITLE     Architecture of Microcin B17 Synthetase: An Octameric Protein
            Complex Converting a Ribosomally Synthesized Peptide into a DNA
            Gyrase Poison
  JOURNAL   Mol Cell 73 (4), 749-762 (2019)
   PUBMED   30661981
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Breil,B.T., Ludden,P.W. and Triplett,E.W.
  TITLE     DNA sequence and mutational analysis of genes involved in the
            production and resistance of the antibiotic peptide trifolitoxin
  JOURNAL   J Bacteriol 175 (12), 3693-3702 (1993)
   PUBMED   8509324
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Genilloud,O., Moreno,F. and Kolter,R.
  TITLE     DNA sequence, products, and transcriptional pattern of the genes
            involved in production of the DNA replication inhibitor microcin
            B17
  JOURNAL   J Bacteriol 171 (2), 1126-1135 (1989)
   PUBMED   2644225
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>328
                     /product="SagB/ThcOx family dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
     Region          54..185
                     /region_name="McbC_SagB-like_oxidoreductase"
                     /note="oxidase similar to the microcin B17 processing
                     protein McbC; cd02142"
                     /db_xref="CDD:380318"
ORIGIN      
        1 mnaldyhlrt rhfpnrfaks lgyldwenqp spyksyfeae qiplkkltpp kktyeklylk
       61 nepnpinlet ialmlrysla inaqkvygps swyvrvnpss gnlhpeetyi ifkngvyhfn
      121 vknfslella ksdkniieng fliilnsipl reswkygera lryclldsgh aiaalrfstn
      181 llgwnmkkar iekeyflskf nfhqneeeif eaaffvfedk ipdidlkilk nlefktaysp
      241 lakekvrwei ifesanklkd etksefikkd isflpstfda yeiidnrrsa lgfkqkylpk
      301 ndfldildkt lhrkippfdv eitanlid
//
LOCUS       WP_457562271             438 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-glucose dehydrogenase family protein [Caminibacter pacificus].
ACCESSION   WP_457562271
VERSION     WP_457562271.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..438
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48844
     Region          1..421
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkisivglgy vgavcsaala neghqvigmd idktkvelin egkspivekd ldvlieknvk
       61 egrlrattnl keaiensdit fiavgtpsre ngsidlkyik eaaksigevl kdkkdfhivv
      121 mrstvlpgtg revvipiiee nsgkkvgvdf gyasnpeflr estaiwdfyh ppktvigasd
      181 ektadtleel ysfidineap lfkteieiae mvkyadnswh avkvtfgnei gmicsrlgid
      241 shkvmkifvs dtklnispyy lipgfafggs clpkdvkait ykakevdekt pllnslmesn
      301 eyqikrvfnh fikplkkkkv gilglsfkag tddlrespil eltetligkg yfvkifdmnv
      361 vkareegaak efletelhhi nerltdnlqe vidnseilii gnkdnrfrgl adkykdkfii
      421 dvaaiedris qgnyfriv
//
LOCUS       WP_457562273             126 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosylanthranilate isomerase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562273
VERSION     WP_457562273.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>126
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - L-tryptophan biosynthetic
                     process [Evidence IEA]"
     Region          1..>123
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 mrvkicgitn yedaklacdy gadalgfvfy kpsprfieag vakkiieklp pfvtkvalfv
       61 nmsaesinga meflkadiaq ihfdvekeff dkltckylpv vrakeksdid kfeenykivd
      121 ayvpey
//
LOCUS       WP_457562277             397 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Caminibacter pacificus].
ACCESSION   WP_457562277
VERSION     WP_457562277.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..397
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44816
     Region          29..395
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 manlliigag gvgrvsafka aknkdtfkni ilasrtkskc ddiakdikek lgieiktyal
       61 dankeenvid likkenidiv cnvalpyqnl pimhaciktg aayldtalae tednpdtyyd
      121 lqwaldedfk kahtmallgc gfdpgvtsim vkyaadylld eleeieiydc nfgdhgrhfa
      181 tnfdpeinlr elnlpgkywe ngewkttkpf eiqvkhkype cgeatsiliw heelesivkf
      241 fpnlksakfy mcfsdkylyh fnalknvgmf siepieiceg ckisplqfla kvlpdpqdlv
      301 knykgqtnig viakgkkdgk nktfyiynic dhekaieetg ahcvsyttgv paiigcklma
      361 kkiwwsegvh nveefdakpf feemekqglp ikvieve
//
LOCUS       WP_457562278             153 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562278
VERSION     WP_457562278.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Moynie,L., Giraud,M.F., Breton,A., Boissier,F., Daignan-Fornier,B.
            and Dautant,A.
  TITLE     Functional significance of four successive glycine residues in the
            pyrophosphate binding loop of fungal 6-oxopurine
            phosphoribosyltransferases
  JOURNAL   Protein Sci 21 (8), 1185-1196 (2012)
   PUBMED   22610485
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Vos,S., Parry,R.J., Burns,M.R., de Jersey,J. and Martin,J.L.
  TITLE     Structures of free and complexed forms of Escherichia coli
            xanthine-guanine phosphoribosyltransferase
  JOURNAL   J Mol Biol 282 (4), 875-889 (1998)
   PUBMED   9743633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..153
                     /product="phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0106130 - purine
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17893
     Region          1..147
                     /region_name="Hpt1"
                     /note="Hypoxanthine phosphoribosyltransferase [Coenzyme
                     transport and metabolism]; COG2236"
                     /db_xref="CDD:441837"
ORIGIN      
        1 mkkyyysyee flkdlntlqn kikdynpdcl laiarggmtl ghflaermdt kelyslnass
       61 yenekkvskp kifnipdlsh kkrvlllddi sdsgetldev mkilkkkfpn tqiksatify
      121 kentihkpdf vlkkadkwiv ffwdkegqei ien
//
LOCUS       WP_457562279             104 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457562279
VERSION     WP_457562279.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jurenas,D., Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Biology and evolution of bacterial toxin-antitoxin systems
  JOURNAL   Nat Rev Microbiol 20 (6), 335-350 (2022)
   PUBMED   34975154
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Kamruzzaman,M., Wu,A.Y. and Iredell,J.R.
  TITLE     Biological Functions of Type II Toxin-Antitoxin Systems in Bacteria
  JOURNAL   Microorganisms 9 (6) (2021)
   PUBMED   34208120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Rocker,A. and Meinhart,A.
  TITLE     Type II toxin: antitoxin systems. More than small selfish entities?
  JOURNAL   Curr Genet 62 (2), 287-290 (2016)
   PUBMED   26597447
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Goeders,N., Dreze,P.L. and Van Melderen,L.
  TITLE     Relaxed cleavage specificity within the RelE toxin family
  JOURNAL   J Bacteriol 195 (11), 2541-2549 (2013)
   PUBMED   23543711
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..104
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12425
     Region          5..92
                     /region_name="ParE_toxin"
                     /note="ParE toxin of type II toxin-antitoxin system,
                     parDE; pfam05016"
                     /db_xref="CDD:398610"
ORIGIN      
        1 mnfqikisey akndleiafd fyekqatnlg kiffdyiise iellsfygcl hqktfgyhrm
       61 iskkfpfaiy ydcnkeqkyi tivaildlrq npktiekyli kdrk
//
LOCUS       WP_457562289             145 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEA family DNA-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562289
VERSION     WP_457562289.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..145
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16224
     Region          18..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 mkktllalaf alsslmaidf ntaskaelmk vkgigpkkae aiiqyrkthk iksindlkni
       61 kgfnsktisk iknqksalkd kanakktalk nkkskmkakm nskkealknk kaklnakksq
      121 lkkmkkekmq klnskksafk nkvkf
//
LOCUS       WP_457562290             209 aa            linear   BCT 27-JAN-2026
DEFINITION  HesA/MoeB/ThiF family protein [Caminibacter pacificus].
ACCESSION   WP_457562290
VERSION     WP_457562290.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..209
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23650
     Region          1..187
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mfrrqievig eknqeklsek svlivgcggl gniiattisc iglrkiylid ydtielhnih
       61 rqfqfskedi gksksktlce kinrckntei ialegmfden meidvdlvfd atdnfevrkk
      121 idsfskakki pwiyasveet rgqvgvfrkt sfeifatkah evkgqlppmv nligsiasms
      181 glkcligeck evlyyvdfse dleinkfsf
//
LOCUS       WP_457562288             429 aa            linear   BCT 27-JAN-2026
DEFINITION  ammonium transporter [Caminibacter pacificus].
ACCESSION   WP_457562288
VERSION     WP_457562288.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, 57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..429
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45279
     Region          20..428
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mlfrllsllg laslafagea pkldsgntsw mmmatalvmf mspaglalfy agmtrakntl
       61 ntymmvfsay alatvvwvfw gysltfgddi agiignlkhi flngisyndl essgypsyvf
      121 iafqgtfaai tvaiasgsii ertkfstwll fvilwvtfvy apvahmvwgg gflyndgald
      181 faggtvvhmn gglagliaal migkrkgfpk tqmmpssvil talgaailwf gwfgfnagse
      241 faadniagsa flmtnfaaaa aamtwiildy ikfgkptllg aatgavaglv aitpaagfvn
      301 vvgaliigig gsvtaffgvt vlkkifkydd sldafgvhfi aglwgaiatg ffalkdlawa
      361 gsplhdkgdr lgqiwvqves vlvtivfvai mtaivlkvas lltggarvde eseiigldst
      421 ehgekgfhl
//
LOCUS       WP_457562305             320 aa            linear   BCT 27-JAN-2026
DEFINITION  DHH family phosphoesterase [Caminibacter pacificus].
ACCESSION   WP_457562305
VERSION     WP_457562305.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..320
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35576
     Region          6..312
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mqelfkkawe kikeaknivl vshinpdgda lgsslslypi lkrmgknvkv fnvtkplpqy
       61 ldflpnfdkv tnklpknvdl misfdcgsfd rlgidekppf linidhhisn tnygdiniid
      121 pkaastsqvv femlktngve idedsatciy talvtdtgsf qyesvnekvf qtaaelvkcg
      181 akpdfvakml fqrdrlsrlr llakaydtie lccegkvafv evtkemmeit gaikddtdti
      241 vnsvraiasv evacmlredd dgikislrsk nyadvskvav kygggghira agatiknefd
      301 fnkvknmlke dlkeivkvee
//
LOCUS       WP_457562306             445 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457562306
VERSION     WP_457562306.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..445
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50118
     Region          <299..426
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkklwilill lvigaggfvy fspmfeknpp kitiktdgyt nlknpievdl kddsgiksyt
       61 vvlmngnnte viasadnpnm gknvtlkikl pknikaneir lvitavdtsk whffagneaq
      121 ksvtlevdkv apdaqvvnns yaigrggsaa avvqvndknl kdayilvdgk ykfkltpfyk
      181 dgyyvaliaw piwennfdat lvaedyagnf vrehipyywr trgiynpkdv kirindkfin
      241 qvakrlleri gmsipndpve ifkkvnetvr kineakisqi tspvyeekin sfyirrfnpl
      301 pgsakradfg ekrhyyykge qisfaihkgv dlakikraki yannngrvva neyigiygna
      361 liiyhglgly tlyghtsefk vkkgdsvhng mviartgatg avfgdhlhfg vyvqgipvqp
      421 lewmdshwik tnilnvinga krmik
//
LOCUS       WP_457562299             398 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457562299
VERSION     WP_457562299.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..398
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=44721
     Region          3..392
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 makkvlvlgg gfaalesaiw lrkygfdvtv itnreymyvy pisiwiptge isfedctldw
       61 kelskvhgfd vkfkkvtkid innkavyceg eekncdfdyl iiaigadkvk hkgsehfmsi
      121 cgapeeslki kekldelikr gegklafgfg gnpkdpsnvr ggpafevmfn ihnklkklgi
      181 rnkfditffa pmpkpgarmg ekalkvmdmw fnkldikqik gkkitefved gvifedgskl
      241 esdltmfipa gngpalfkdt glplneagfi kineycevmh dfdetssdkf pifaigdsaa
      301 idgpdwrakq ghlaevmarv aaynikmmee gkearkeyis hinilclmds gdgaafvyrd
      361 nkkailiplp iighwmkkgw gwyfknskln kipripgm
//
LOCUS       WP_457562317              74 aa            linear   BCT 27-JAN-2026
DEFINITION  FeoA family protein [Caminibacter pacificus].
ACCESSION   WP_457562317
VERSION     WP_457562317.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 74)
  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 74)
  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 74)
  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..74
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..74
                     /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=8122
     Region          1..73
                     /region_name="FeoA"
                     /note="Fe2+ transport protein FeoA [Inorganic ion
                     transport and metabolism]; COG1918"
                     /db_xref="CDD:441522"
ORIGIN      
        1 mklnelnigd eaivrkvlas eplksrllsm gitkgekikv lkhtlakntf evevnrvpia
       61 lrseeaalve veki
//
LOCUS       WP_457562319             112 aa            linear   BCT 27-JAN-2026
DEFINITION  P-II family nitrogen regulator [Caminibacter pacificus].
ACCESSION   WP_457562319
VERSION     WP_457562319.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Huergo,L.F., Chandra,G. and Merrick,M.
  TITLE     P(II) signal transduction proteins: nitrogen regulation and beyond
  JOURNAL   FEMS Microbiol Rev 37 (2), 251-283 (2013)
   PUBMED   22861350
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..112
                     /product="P-II family nitrogen regulator"
                     /GO_function="GO:0030234 - enzyme regulator activity
                     [Evidence IEA]"
                     /GO_process="GO:0006808 - regulation of nitrogen
                     utilization [Evidence IEA]"
                     /calculated_mol_wt=12373
     Region          1..112
                     /region_name="GlnK"
                     /note="Nitrogen regulatory protein PII [Signal
                     transduction mechanisms, Amino acid transport and
                     metabolism]; COG0347"
                     /db_xref="CDD:440116"
ORIGIN      
        1 mkkveaiikp fklddvkeal feagvsgitv sevkghgrqq ghtelyrgae yvvdflpkik
       61 ielvvkdnel ekvleviqes artgkigdgk ifvipvekai rirtgeedee ai
//
LOCUS       WP_457562320             390 aa            linear   BCT 27-JAN-2026
DEFINITION  ammonium transporter [Caminibacter pacificus].
ACCESSION   WP_457562320
VERSION     WP_457562320.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, 57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..390
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41571
     Region          6..387
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdlawaldtf falfaftlii lmvpgfamle aglvrtknvt avltvntmiy lvaslvfflw
       61 gyvlafggwd gssmsmyaaf lfqlafvgkt vnimsggvse rtriiplaif tifmagliyp
      121 lvvnwtwgan mlkgtfldis amhdlagstv ihstgawall aailiigprk grytkdgkvr
      181 vipasniplv vlgafllwig wfgfnggsvg sisskeaant valvvmntnn agligglavm
      241 vlsyltykkf ditmilngal gglvaitaga dvvspyaall igliggilvf yavpffdklr
      301 lddpvgalsv hlvngiwgti atgiwgkgvs laaqikgvvv vgifafvasy iiiwvinkiv
      361 pfraneedei egldvsecgi esypefkrai
//
LOCUS       WP_457562323             660 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457562323
VERSION     WP_457562323.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..660
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=75215
     Region          131..660
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnfihklslk tkvitvvlls iimivyftgk elvrhfdfek kkaqlteliv lsqslsklih
       61 etqkergvsa gylgshgkkf aemlpkqral tderikeymq vlknidfaky spefkqeiek
      121 lnqylkmlpe irnkvnnfqi slkdevkwys qmnanilkii gyaarfapnd kismdlaayt
      181 sflkakerag ieravlsatf gadkfapgmy tklirliseq nayiddfltf anermkklyy
      241 ktikepefae vqrmrdiais hhktggfnid peywfktitk kinalkridd siakiivkdv
      301 nsikdnaiie aiiglisiii vlffsyliir sfslqlnslk nlilmiardk dlsievriye
      361 ddefgeirra lrtflaslhe vmmsahtssi enkqvatnle ksfgsiteni qkeanivtna
      421 settnelrek lneeaensne vknaivdane slqeaiklik dtmeniqlna enenelamrl
      481 qqlsqdaeqv knvltvirei adqtnllaln aaieaarage hgrgfavvad evrklaertq
      541 kslgeidati nvivqainsa stdmnknien vnrvtektge vqgriqevst kmeevvvkvd
      601 qnveevekvv kimedfikkm neiqklssen kekvlsnqsy ihriatlade llkeisqfki
//
LOCUS       WP_457562325             255 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562325
VERSION     WP_457562325.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28705
     Region          1..254
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 mlkvdkvtkq fggvvaikdv sfevkpleif alvgpngagk ttlfniitgv leptsgkvyf
       61 kdeditglsp vkivekgiar tfqnirlfss ltvlenvlig fhnhieynff eslfrlprff
      121 keekihkeka meilkflgie qyadynakal sygnqrkvei aralatepdl llldepaagm
      181 npketdelad tvfklrseme ktilfiehdm kfvqkiadrv mvldygktif egkpadmmkd
      241 etvikaylgd idveg
//
LOCUS       WP_457562326             359 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457562326
VERSION     WP_457562326.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..359
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40773
     Region          5..330
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkvfdyviig agiagslagy flrdknvlvv dkkgkleaas gaagaflfpk vgydtaytrf
       61 inegivssie fykrigvdth tkgvlilprd erdiekfkky ekeiklpfkk rgegfffeig
      121 svidpeevke kldfpfekle vktlkkeeyw vindeikaks vilasgyesi vdipyiqirp
      181 iwgerieieg nwdkskcdiy yhkncsvgcn gvmkigathk rncleckene qealelikka
      241 reiidikeye ikdvkggfra astdyfpvvg qvidvdktll ndkhiikgdm pkkifyiegl
      301 yiingmggrg fsnayvcakm lkdfiengad lgwvdtkrlf ikwarksgea ylrsknvks
//
LOCUS       WP_457562331             746 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457562331
VERSION     WP_457562331.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 746)
  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 746)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..746
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=88200
     Region          157..412
                     /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          <168..664
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          307..333
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(309..310,313..314,316,344,347..348,351..352,
                     354..355,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..376
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          381..409
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfflffpvf lfglqlnidy gnakqpyevl tiynkfpfec slkektficv fdktpktpvf
       61 keesrffqvi pkfskkftit ikiksdnfki fafednlykk plitpfrlkk akkwvivane
      121 qylentnkgl dfyykhavyp yigaidenlr pirgenamdi akyfeilkay kkgrdvldei
      181 dqfvkeypns iflsdvlylk lkildrenqs edvvqlgkew ikkfayspkl pevllligen
      241 yskmglisda syffnriite ypntkyayka miyfadqlyt mgdekkafkl yekalystkd
      301 invaslaalr laqrymdkgq vkkaieyyek iykankefll kdkrkayela krlasekvyn
      361 lainigedll krlkklddly epllynlalw syeagdyqks lkfinkylke fpygdysdni
      421 kalrdkvlfe vpeqnltkkl qyidkvlney kntdiakkal vekikilykl kkydeilklq
      481 keiknipkkl fpqkdtfikk vaseyakell ekgycqkaie likkyklnlk edekvyscam
      541 kvkdcklasa icnkyldnps devfvkwmkr kiealwcmrd yknvvtavdd lcqiernchk
      601 ylmykffalw nlgkykqalk taqklekyqt iqnadayiki vnwamqnkdy llaatyakki
      661 idlqnrfnay pyspfvdfvf akytknknea ikvleklipk vkgedlaray fmlanltgkk
      721 dylqkclnvk dsklwkglck dalnlf
//
LOCUS       WP_457562332             155 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562332
VERSION     WP_457562332.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 155)
  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   5  (residues 1 to 155)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..155
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=17022
     Region          7..>102
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 msvlilavai ilaimsltqk ntvpavlsfv lmmfllgiyy ilmdekllgl fqifvytggi
       61 vvltlfgvtv igskfpkyei rpwavsvvti viigliivpf lipdipyegk aiplkdqvki
      121 ftdfyaqiai fmgvvaasvl ygsirmlhtl khgke
//
LOCUS       WP_457562333             112 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit A [Caminibacter pacificus].
ACCESSION   WP_457562333
VERSION     WP_457562333.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Berrisford,J.M., Baradaran,R. and Sazanov,L.A.
  TITLE     Structure of bacterial respiratory complex I
  JOURNAL   Biochim Biophys Acta 1857 (7), 892-901 (2016)
   PUBMED   26807915
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 112)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002876
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..112
                     /product="NADH-quinone oxidoreductase subunit A"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=12199
     Region          4..99
                     /region_name="NuoA"
                     /note="NADH:ubiquinone oxidoreductase subunit 3 (chain A)
                     [Energy production and conversion]; COG0838"
                     /db_xref="CDD:440600"
ORIGIN      
        1 metiiiygtg ilagvlllyf lgiavapynp geikndhfec glppssevpm kanfgyfifa
       61 iafivfdmag lffslfvfad npealkwamv fgillfaait vsmkeyrnak sa
//
LOCUS       WP_457562334             569 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562334
VERSION     WP_457562334.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..569
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65833
     Region          <309..556
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mvenikeflk npkkskiyki lniskeevev lkhmlemyie gqedvkvrni lqkiysddkl
       61 eafehigtik nlieegwvvv ssfgakspel salelfnanv slsvaflkll engdlelvip
      121 qktpykdhle ylhdqflrid iyeqlanlkn sfsnetasik rlqsklklie stikervkkt
      181 qidlpvlnfm iendfnfnek eeiiflallk eeytggsena relnrlldli sadeierikn
      241 rslldenskl vsegiidyde lfgafggytk iyfisediln elihprrkhk lehlvkdtif
      301 dlvepknsle dvvlpkptme mvkrvlkqid krvvnllkkw gikqnndlda kiifyghpgt
      361 gktltahaia kelnkpvlsl dsskilsmyv geseknvrrl fdeyyeisek lktkpvllln
      421 eadqflstrt taafssadkm hnqmqnifle qlekfegvli attnlletid safsrrfdyk
      481 ikfekptfke rvklwqkklp knadfeedfd vnelakydlt gaqieliikn talkvamkkk
      541 pifklkdfie eiksekksaf dsekevgfv
//
LOCUS       WP_457562336             142 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562336
VERSION     WP_457562336.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 142)
  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 142)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>142
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..>111
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkialiedei hlneaiklfl elesfnvesf knireflres dnnydiiiad itlpdgnflq
       61 elskhkkige etkiiimsah geldnikkaf dlgaedfikk pfepeeiilr vkklfktkkt
      121 klteniyydp esktiltpns ke
//
LOCUS       WP_457562343             420 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457562343
VERSION     WP_457562343.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..420
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49522
     Region          <131..415
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkklilllit tysfsqlinc drykivtvyd lfdkiekndk vrygrlnels fkdksynfki
       61 yidgymktgk kvtdnvvdnv hftersvkih adkllysslk kynsqilkin allnslnikn
      121 rvnsdlvlgl ntysnllflq qkidilnkii krqksiydyl inrynegvgs kidvlnakid
      181 lanlnqnlis sykdyaqnli ifnylygdnk nkdyyfmpfl pkfaislkql qkevlknnyn
      241 akiaklnlkk sfynyqkssl hpininfysf agytqsiqkt fnlgsdlnsf dwemgvtfni
      301 plydaqlkqa renskvnyli qreayksdiq kilrnvykiy qniiyerkni kiirkkidvy
      361 keeidfyqnr iysglneytq yatvlknyln eminlrnsvn rlntdilllk ilsgrsigen
//
LOCUS       WP_457562351             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease subunit [Caminibacter pacificus].
ACCESSION   WP_457562351
VERSION     WP_457562351.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=22298
     Region          27..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 mdiinylndh ldltilaaiv iafvlslipk idypiekltn ffmiisvial isltllvsyd
       61 viarklfhgg sialqelewh lydivflfai aytlskdkhv rvdifydkfs fklkktinli
      121 tilffvipls vliiveaipf vqmsyaqhes sgdpgglccr wiiksamiwa favvylqsia
      181 elrkiyyqlk hhkge
//
LOCUS       WP_457562352             430 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease [Caminibacter pacificus].
ACCESSION   WP_457562352
VERSION     WP_457562352.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..430
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..430
                     /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=46100
     Region          1..403
                     /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 mtgiilfvva fillmlgipv afafgasaif aalldpnlgl evfgllpyri ygimqnftlm
       61 avplfifmgf ilekskiaen mleaigklfg pvrgglaiai vivgailaas tgivgasvvm
      121 mtiislpvml kygysprlas gviaasgtlg qlippsivli ilgavmqisv gdlfkaaiip
      181 gliivglyii yilviafikp evapaiktde pysqillqal kslvapfili alvlgsifag
      241 fatptesaai galgaiiltf fygtlnlell ryasvetvki tamifmilig atafslvfne
      301 sgagdivtef ftdsisnqyi fiaitmilif ilgffidfie itfivipill piveefnidp
      361 lwfalliain lqtsfltppf gfslfylkga agdmiktsdl ykgiipfiii qliallivlf
      421 epklvyllvk
//
LOCUS       WP_457562356             254 aa            linear   BCT 27-JAN-2026
DEFINITION  inositol monophosphatase family protein [Caminibacter pacificus].
ACCESSION   WP_457562356
VERSION     WP_457562356.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..254
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28938
     Region          1..241
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(29,33,39,60..61,75..80,205..206)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(32,34,81..82,84..89,141..143,145,147..148,157..158,
                     161,164..165,169,174..180,188,192..195)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mfektiqivk eageifkegy ykdkeivlkg kkdlvteydi kveeflkekl kpfntnfiae
       61 esiynekihk tfiidpidgt tnyahqvphc aisvayyenn revfgivynp ilnelfyakk
      121 gegaylkgkk ievsknecfq raliatgfpy ssaeneadlk wvisklnkvl prcqdirrlg
      181 saaldlcyva cgryegfyei nlkpwdvaag kiivqeagge vsnnfgesyn ifedrcivat
      241 nmkihrelvn lleg
//
LOCUS       WP_457562361             193 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Caminibacter pacificus].
ACCESSION   WP_457562361
VERSION     WP_457562361.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..193
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22233
     Region          7..173
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(48,50,52..53,116..117,133,173)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 meilvkpcge fytncyivdr kiiidpgiga yefvrehvdk plaiinthgh fdhmwddkti
       61 kemydipiyi hkndafmlen dpfgynppkv kpdylleegd ikigdydiki rhfpghtpgs
      121 itieigdemf sgdfifdgsi grvdfpyssa edmrksiekf lkipydkrvl pghgptttik
      181 kaqkflptwl eyl
//
LOCUS       WP_457562362             326 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562362
VERSION     WP_457562362.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 326)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..326
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38329
     Region          68..324
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mfsldkfrke tvdisfflfl fisvfyfigv ffglfvvdks llkielflvl fdivlfgayk
       61 kkkisyfifs yvltfsivfm itmifflnth vvyrsfwfia slpyiflyng kalgifvafy
      121 svilmliafe kglfpitfqd fidyliadlm vasisyffit qmekyekkvi eeqkkldiqa
      181 ktdyltnvln rrgfikeied kkgvigifdl dhfkkindty ghefgdeylr hfvkvlknsl
      241 rkddiigrfg gdefvvlfin skkddlnkwv edfykklels pykgikvsvs iglanyegdl
      301 qksfnladna lyisknkrnk vtffee
//
LOCUS       WP_457562363             188 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Caminibacter
            pacificus].
ACCESSION   WP_457562363
VERSION     WP_457562363.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..188
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21740
     Region          7..161
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mnrfnkdait wddlprrvel akkvvqnvkp fvknkkvlef gcgtglvgin iadvtkelig
       61 idtsekmvek fnekakklnl nakafvknif eendkydaiv ssmtihhikd ikklskklye
      121 ltdtvfiadl vkedgtfhtr gnedvehfgf sidelknffs ewkmdykiih tikkhkdfdv
      181 flitlqkk
//
LOCUS       WP_457562365             121 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase, partial [Caminibacter pacificus].
ACCESSION   WP_457562365
VERSION     WP_457562365.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..121
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <2..112
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 ilkakefarl givttktgly skellehfgv mkyfevligr ehvenpkphp epilkalhqm
       61 nankeaawmi gdtcldmvsa keagikyvgv efkyesqenm rkcaeiikpd vlkaveyifq
      121 c
//
LOCUS       WP_457562367             484 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Caminibacter pacificus].
ACCESSION   WP_457562367
VERSION     WP_457562367.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53783
     Region          67..483
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mdrkalinii kflalvglii eamfsmalit akiynekigy ffeywlgsii ffglililfr
       61 khhmklsike ailsvnlvwi mggvlgaipl mflthvsfvd gffesvsgft ttgatiysdi
      121 sdlpksalml rsvmhwiggm giivlsigll slinptasla lfkseatgit pekitpklkq
      181 tamklwqvyi litildlill kiegmnwfda inhafatist ggfstksesl gywihnpwil
      241 wtttifmlls ginfiahika mkgdfsgfkn eetkwyiglf lvlsvaltlv hyfqsndtlf
      301 fdatnaffti ssiltttgfa tldysqwgqa aiaiifmaml lggnagstag gpkiiryivm
      361 fknlkfqikk flfpnaifsv kidkkpismn tinsvgafff lyimtntiia lylyangydt
      421 mtsisaaiac vgnigpgfgh vgpvdnfaff tdtqkivlai gmiigrleff tvlmllsrdf
      481 wkkf
//
LOCUS       WP_457562372             423 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457562372
VERSION     WP_457562372.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..423
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46970
     Region          25..409
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mdkslkltfi lftlitgiit gifiviygll tkflsyllfw gdpfesiehl pwwylylipt
       61 vsilivnymi skddsvkeyg vaeiaqavee nrlvftwksl fnkivasals lssgfavgne
      121 gpsaaigamv adkfheffkl pkkllkvsls vgasggiaai fvspitgimf aieniayefv
      181 rdfagylils svtafsvaly fleplifnys agkfieyrni fagilfipvi tffiyfylil
      241 kdklleflnk fltsrflkyk nyifaliggg vigtillisp yaafsghelv nflindklhl
      301 aysvifviiv lriiatavsi yanavggifi almsigalvg ygyaemfnaf fsnitiepfy
      361 faaigaalfm gvnmklplta lvvaleityd ynvivptgil yiivsflvtl tfdihkmifk
      421 gkk
//
LOCUS       WP_457562369             541 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457562369
VERSION     WP_457562369.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..541
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58813
     Region          30..399
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mhlistyalg hlvgylpqdt lkllsnytnh ttlnpfmllv vitiggllsg llvyifapea
       61 eghgtdtvir afhrnggylr pivvpikila saitigtgga agregptalf sagigsmyan
      121 frkvgikkrq vfvligmasg lsavfkaplg tsifaievly tnnefetrel iyilfgpfia
      181 ytitgflfgw qpifsvpdie vtqistylki ailgvvsgii gfilpntfyg vrdlfrkipi
      241 lphfkpalga fvvgliaiyf pqvlgggygf iqesingnlv gvillsllia kilafsftvg
      301 sggsggvfap slfigamlga fmayvfkess avfavigmaa vfgaaartpl stivmvaemt
      361 ggysllapat lgvlsaffvh diliktlkpk yvslyeaqll skdyspiyqv ekireiltch
      421 skmlnlekav ldredlldll ergeeveigg gkyiffgtft kkvklqegey fkkyknvdvi
      481 yvfrngkwlp gfvvnsileg devllvgskd aidrikdefv pisqtfsklr vqheeieglk
      541 n
//
LOCUS       WP_457562374             188 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562374
VERSION     WP_457562374.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  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 188)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>188
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          25..>188
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mkeifkkiit dfiekeikni kkrdidipld tkkivtlvgi rrsgktyilf dlinelrrni
       61 drrnivyinf eddrlfgitl kdldllleay felfpqkree klyfffdeiq eienwekfir
      121 rvydnydvav yitgssskll skeistslrg rsinfevfpl sfreflefke ikinlyssks
      181 lsfirnal
//
LOCUS       WP_457562376             270 aa            linear   BCT 27-JAN-2026
DEFINITION  TIGR00282 family metallophosphoesterase [Caminibacter pacificus].
ACCESSION   WP_457562376
VERSION     WP_457562376.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 270)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..270
                     /product="TIGR00282 family metallophosphoesterase"
                     /EC_number="3.1.4.16"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29895
     Region          1..234
                     /region_name="YmdB"
                     /note="2',3'- and 3',5'-cNMP phosphodiesterase YmdB,
                     calcineurin family [Signal transduction mechanisms];
                     COG1692"
                     /db_xref="CDD:441298"
ORIGIN      
        1 mnilfigdiv gkpgrkmvkr ylpmlkkekk idyvignyen lahgfgitpk tfkemknagi
       61 diftggnhtf dkkkeaiell sageilrpln yfeapgswyy edeniivisa mgvccmpygk
      121 npfieldnfl kekkkfvfid fhaeataekr aifhllkkra saiigththv gtddleideg
      181 ccylsdvgit gcrdnvigmk idgpianmlt glkqhydvpd ncksifqavl iesdginakk
      241 ayklkafdds gimitqvage gevgngeivk
//
LOCUS       WP_457562379             538 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Caminibacter pacificus].
ACCESSION   WP_457562379
VERSION     WP_457562379.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..538
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59971
     Region          1..530
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mvspliivia llfialsfni pfarlkippi igyiftgiii snifsldkht ieivaelgiv
       61 flmfmiglef speklksmkk evfgfgfaem aivsgifglv fywffnidir ialiigsaia
      121 lsstaivlkl lnesreiskp ygrialgill fqdiavipil iaisiivnkd adltqlilkt
      181 lggfaalgvf iyiygkfiap fvishatktk sdeifmatvl lvvlvaaeia hffglsyslg
      241 aflagmilse tkykyqiead lvpfrdlllg iffvsvglmv ninfvihnif sillmtvafm
      301 lskagiiylm lkffvkhnri aiktafilsq igefafvifa llgkynlves dllqklvvvv
      361 vismiltpfi lryiykiadi fdkevqnfee felkpaevag hiiligydki gqrvarkltr
      421 agipyvaidk qielvkqglk ngdnvifgna ankrvlesln vkdasaviit tlneehthli
      481 tenilainpn lnvivltdde iekefyknhn vyvvdkskel aeklislalr celrkerg
//
LOCUS       WP_457562383             362 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562383
VERSION     WP_457562383.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 362)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..362
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42157
     Region          113..362
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnlkhykiri tifsililvt ffaiflsyev nkktinslke nlakkiyilr knellthekn
       61 lqnflknfkn aeiistkenp gykiidntvi sifrikdkti iikdsikqei spllqlatin
      121 livitvislm fftlmfcfie fllkrfkivr siianikqre feklppltpe knicdefrne
      181 ivklgreiet yikllslkve dykkkayide lthtfnrnfl keietkiflk akvssfptsv
      241 imididdfkk indtyghkkg devlahiaki lqnnlrkedi liryggeefl illnetelht
      301 altiakklik avesnplddm qitisagvsk ieyndknlyd svkradsnly kakrngknrv
      361 ei
//
LOCUS       WP_457562387              93 aa            linear   BCT 27-JAN-2026
DEFINITION  EscU/YscU/HrcU family type III secretion system export apparatus
            switch protein [Caminibacter pacificus].
ACCESSION   WP_457562387
VERSION     WP_457562387.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Galan,J.E. and Collmer,A.
  TITLE     Type III secretion machines: bacterial devices for protein delivery
            into host cells
  JOURNAL   Science 284 (5418), 1322-1328 (1999)
   PUBMED   10334981
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Hueck,C.J.
  TITLE     Type III protein secretion systems in bacterial pathogens of
            animals and plants
  JOURNAL   Microbiol Mol Biol Rev 62 (2), 379-433 (1998)
   PUBMED   9618447
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Kubori,T., Matsushima,Y., Nakamura,D., Uralil,J., Lara-Tejero,M.,
            Sukhan,A., Galan,J.E. and Aizawa,S.I.
  TITLE     Supramolecular structure of the Salmonella typhimurium type III
            protein secretion system
  JOURNAL   Science 280 (5363), 602-605 (1998)
   PUBMED   9554854
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..93
                     /product="EscU/YscU/HrcU family type III secretion system
                     export apparatus switch protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=10289
     Region          8..92
                     /region_name="YlqH"
                     /note="Type III secretion system substrate exporter,
                     FlhB-like [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2257"
                     /db_xref="CDD:441858"
ORIGIN      
        1 mkkstnikav alkykayedn apkvvakgkg vlaqkiiqka keydvslfqn ealadmllsv
       61 evgeeippkm yeavvevfvw lynleekaql skg
//
LOCUS       WP_457562390             322 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Caminibacter pacificus].
ACCESSION   WP_457562390
VERSION     WP_457562390.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Shek,R., Dattmore,D.A., Stives,D.P., Jackson,A.L., Chatfield,C.H.,
            Hicks,K.A. and French,J.B.
  TITLE     Structural and Functional Basis for Targeting Campylobacter jejuni
            Agmatine Deiminase To Overcome Antibiotic Resistance
  JOURNAL   Biochemistry 56 (51), 6734-6742 (2017)
   PUBMED   29190068
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..322
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016813 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear
                     amidines [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37612
     Region          4..310
                     /region_name="PAD_porph"
                     /note="Porphyromonas-type peptidyl-arginine deiminase;
                     pfam04371"
                     /db_xref="CDD:461280"
ORIGIN      
        1 mnylipewek qsfvqlvfph ketdwsccle eaiktfteia yaiaqyqkvl icyqdentis
       61 hlkhknfifr kvknndtwar dfgaisvkkd tqiklldfkf ngwglkfpan ydnlisrqlf
      121 nihksynfvl eggsidtngk tllttsqcll epnrnyplsk deieeflkne lfvdeiiwln
      181 hgflegddtd shidtlarfv dentivyckc sdssdihyke lakmeeelkk tsfniiplpl
      241 pspkywnnhr lpatyanfli innavllpvy ddlkdkyvyd lfnslfpdre iipidantli
      301 kqhgsihcit keyfnedfis te
//
LOCUS       WP_457562391             227 aa            linear   BCT 27-JAN-2026
DEFINITION  YaaA family protein [Caminibacter pacificus].
ACCESSION   WP_457562391
VERSION     WP_457562391.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..227
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=26312
     Region          2..207
                     /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 mkillapser kslggdksfn issfrelnpl reeaikkyde fiqktddikn fgdiktpike
       61 rpakeailry tgvafeyldy ptlpneakey lnenliifsn lfgilkptdl ipyytlkqgs
      121 kpgfdiykfy kekvteilds lnedfidlra kfyekiykpk navtfkfikn gkvvshfaka
      181 yrgtltrhia lhkpktieev lkiefpgiei meiqekkgik eivceik
//
LOCUS       WP_457562395             418 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457562395
VERSION     WP_457562395.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..418
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46267
     Region          23..401
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mnaklifssi iigiitgifi viyalatkyl sfllflgdpf etidklpvwy iylvpflsil
       61 ivnyliskne kvkeygvaei akavdenkmt fsikdlflki fasslslasg favgnegpsa
      121 aigamiaqkf hnifnlpkkl lkvslsigas sgiaaifvsp itgimfaien iayefvrdfa
      181 gylilasvia fsiawhflep lifnystgkf ieyryifati lfipvitffi yfylslkeiv
      241 lkflkekihl psknfvlaai gsfiigtili ispyaafsgh evvkilinds nhfplymifi
      301 liilrivats vslyanavgg vfialmsiga lvgygfgevm vyfdfpiepf yfaaigagvf
      361 mgvnmrlplt avvlalevty dynviiptgi svvivtylst lkfdirklst lihhkekt
//
LOCUS       WP_457562397             192 aa            linear   BCT 27-JAN-2026
DEFINITION  O-methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562397
VERSION     WP_457562397.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..192
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21718
     Region          30..192
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mtneyvkepr alkdivadtk kigfdmcgek dvgvllrvlg asksgeflel gtgtglstaw
       61 ildgmdensh litvdndekl lsiakkhlgh yknvefvcdd gnaflerlkk enkkfdfifa
      121 dtwagkyeml edtlemlnek afyiiddmlp qsnwpeghek kveklidylh nredleivnl
      181 gwssgvivcv kk
//
LOCUS       WP_457562400             657 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Caminibacter pacificus].
ACCESSION   WP_457562400
VERSION     WP_457562400.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..657
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79680
     Region          360..500
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
ORIGIN      
        1 msklnnlfkk nydkcylfgv slyeeifdkk nkyykvnysy niyqsdnqii kikenvfqgf
       61 ifeniidaid revnllefky ldflfedkii eklnretkci krfvknynfv vnnkkykfhf
      121 vlfyyfdnql kyriknlkke einslyydiq krlvnknfnq ikkysnvyvf iidmkrpfke
      181 ngirninlaq iyndsdikit kriifdiani lkkydfyiin higdgfvfic knvffntldl
      241 eknkeiinni ycdinnyinn vkiylnglyd kmksyklrgi lalcnelyef daefdsskky
      301 ffsfyldlif dnfnnkiikk fekteykanf yfyfletnpp hlfikyfknn eflpmkikrv
      361 ifielvrgcn skckyccehq yekkfmsktq mryiiafikn sknyefeiyi tggepllhdk
      421 lcdfvdslke ltnvkkiily tngillnkid ckkkfdkiii sidgydknty ivtrgidkfd
      481 evsknlksli yenvdvllki tlfpeyisyv nrfiefanni gierkqikfg ilsrnfckkc
      541 ncndndfdki mndyiknihn dnfiktyfnd ieylnpystp ikcdfkseki iiityegyik
      601 kcffqekink nfkiknflni eeyenkmddk lhdlpckyck caieiddfli krpkyey
//
LOCUS       WP_457562408             279 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457562408
VERSION     WP_457562408.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..279
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33275
     Region          26..>101
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mryfliflfv plfafdyfti kkadeffqkk eylkaakeyl kidsqkalld aansyykagd
       61 ykkaieiysk indkklqfdk lynmanayak lgmfqkaiel ykkalkikkd kdaqynlkll
      121 ekllkkkqpk qkqkqknnkq knnknknnke nkkqnnnqnk knqnkneqnq knnkkqnkdk
      181 nsnanknknn kqkenqqknn qnqnknqkkq sknnekkeqn kkfavnqkis kfknenkkpn
      241 qktlsvkesn ttdirmkfye kalknlqfns lliplrsqe
//
LOCUS       WP_457562409             468 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Caminibacter pacificus].
ACCESSION   WP_457562409
VERSION     WP_457562409.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..468
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52256
     Region          19..111
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
     Region          253..348
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 mkklilfllp llllanvsvk vnkkeltkge eliititatg kdikfpqinn idgynvigts
       61 lvsnieving amseslsksy iivpdknlti psfsviidgk vyktkpihii vktpkqtkgd
      121 ytldinlskk nlylgqsail dvklhykppv esiqlqkpqi kgflvqeilk tatdteaeyk
      181 flitplksge ftigplmani gilvkenpfn dpffnlsvss lkyktiysnq ikvkvnpipn
      241 dsvygdfkis lkaknivnag epntailkve gcgdfndlpd fkldipntti yaskadtnis
      301 ivdnelcgty tkkftiiadn dytipplklk eyngtlnvis tnpikvkvig akpittpkpp
      361 vtktstkptk qhtennknyy eyaiyliliv lgiglgyfis kitskekkdd ifskikkadq
      421 kelfnllipy sdipeikeil qkleeniykg tnhkinkkei ikiiktkn
//
LOCUS       WP_457562414             292 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Caminibacter pacificus].
ACCESSION   WP_457562414
VERSION     WP_457562414.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..292
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=32796
     Region          148..285
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mkkiilgsmi aagalfafpg mmggamkgna altgkplpgl kdstvlaeln gkkitvkdvn
       61 aylqgitgdn rirlqdlpaq hvkqfvqqyv emleiynska kditktpqyq aaakklavdm
      121 wlknqlqtik isdkearafy eknkdiyfkt tpkikarhiv vkdektaeki inelkglhgk
      181 aleekfaela kkysigpskv qggelgyfdp kqmvpafaka ceelkpgqmt lkpvktrfgy
      241 hvilvedkkd nnylpyeqvk mqiieylkrv klkdelqkik dsskvkytip ks
//
LOCUS       WP_457562416             320 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562416
VERSION     WP_457562416.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>320
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
     Region          1..316
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mnrrvnyiil avftllltag avyfiywlgk fnankkpkny yqaifhesvs glniaspvky
       61 mgvnigsvkk itinpnepns vivtftvdkn iplrkdsyav lelegitglk yieieggskn
      121 spilktskhh patiktipsf naklfealss ttdklntlld nlntildpkk ashlqnmlih
      181 lekisayldk nkymlkdtiq nfnqlqnnln ktitalrkdi hnltthtikt ekaftqnfnq
      241 lnsnvssfvk nsniliselt kktkegqfdl kdallesfkp idttsneikk atiklenlln
      301 elqnspsdii fkkanppkgp
//
LOCUS       WP_457562417             249 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562417
VERSION     WP_457562417.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27783
     Region          1..241
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mreiikvrnl ttkfgqkvvh dnisitiyeg eiygilgasg sgkstllrem illehsfkgl
       61 ieimgkditk lslkeeielk knwgvlfqfg alfsslnvle nisvvleeyt dlpeefiikt
      121 aisklkltgl keevayqmpk nlsggmvkra alaralaldp kllfldepts gldpvsaraf
      181 dslikelhsl fkptvvmvth dpqtianvld rfcilidkkv vfegtfdeav kstdkkvqkf
      241 lkpilmeie
//
LOCUS       WP_457562418             356 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaE family ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457562418
VERSION     WP_457562418.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39681
     Region          106..351
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mlkiitnhhl islvgsldkn tiqkayylkk eknmaidlke lksmdyegal flvelsknhk
       61 iinlpshlke lfnfvaqnak dlkipeqktn flfhasnyln diffaikent infllffgef
      121 iyfliflith pwkfrfketa aiivkagaga lpivgltsfl vgvvmayqga mqlskfgani
      181 fivdmldisi freiapliaa ivvagrsasa fsaeigvmkl teeidamktl gfepfwflvi
      241 prviamiiam plivffadmi gilggmiisa lslnigfdmf lnrtrdvlsl tqvfiglgka
      301 pffgiviali gtyrgfqvrn stqdigkytt ksvvnaifwv ialdaifsii fakfgi
//
LOCUS       WP_457562420             219 aa            linear   BCT 27-JAN-2026
DEFINITION  C39 family peptidase [Caminibacter pacificus].
ACCESSION   WP_457562420
VERSION     WP_457562420.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kanonenberg,K., Schwarz,C.K. and Schmitt,L.
  TITLE     Type I secretion systems - a story of appendices
  JOURNAL   Res Microbiol 164 (6), 596-604 (2013)
   PUBMED   23541474
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Lecher,J., Stoldt,M., Schwarz,C.K., Smits,S.H., Schmitt,L. and
            Willbold,D.
  TITLE     1H, 15N and 13C resonance assignment of the N-terminal C39
            peptidase-like domain of the ABC transporter Haemolysin B (HlyB)
  JOURNAL   Biomol NMR Assign 5 (2), 199-201 (2011)
   PUBMED   21347827
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Schwarz,C.K., Tschapek,B., Jumpertz,T., Jenewein,S., Lecher,J.,
            Willbold,D., Panjikar,S., Holland,I.B., Smits,S.H. and Schmitt,L.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            an oligomeric species of a refolded C39 peptidase-like domain of
            the Escherichia coli ABC transporter haemolysin B
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 5), 630-633
            (2011)
   PUBMED   21543878
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..219
                     /product="C39 family peptidase"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25382
     Region          4..190
                     /region_name="C39G"
                     /note="Predicted double-glycine leader peptidase, C39-like
                     (CLD) domain [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3271"
                     /db_xref="CDD:442502"
ORIGIN      
        1 mkkliifitv ilnaailhqk nfdiqkpvks wieiknenvv rqeydyscgs aalatilkyf
       61 ydlnisekei lnkildfkdl ndknkktled kdfmlsfydl aefakskgfk aiglaldmea
      121 lsklkapvil fvkirkdnhf tvfkgmdkny vyladpnfgn iklriskfkk ifylsnfkyp
      181 gkvlaiiplk ptkinhnfmk ikkssnfvye vikdkitdn
//
LOCUS       WP_457562423             287 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562423
VERSION     WP_457562423.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 287)
  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 287)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..287
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <4..281
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 aydtlsiglm lavfgylwfm mspmqeiini qyayfgakaa lerinevlel pkepifphkk
       61 dpfsqnvtie vknlsfkyke sdwilknana tikpntital igasgggktt faklisgffv
      121 pndgdilyng asfkeigldk irqnvalilq etrlfsdtlr fnltlgknfd eqeiwealrl
      181 aelkdtvekw pekldtyvgk ngvklsggqk qrvaiarall hkpkivilde stsaldiete
      241 dkvfkniepf lksrtsiiia hraetiskae eilmvknrei iklqkvl
//
LOCUS       WP_457562430             122 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Caminibacter pacificus].
ACCESSION   WP_457562430
VERSION     WP_457562430.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 122)
  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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..122
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14154
     Region          4..122
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkkriyynht daggivyhsn yitfceqars eiffshgiyf sqtsgyvikd lkakfiksak
       61 lgdiieiktk vkkirktsie llqeiykdde lifqlevtav yiqegkiski pkkhleilne
      121 yv
//
LOCUS       WP_457562433             309 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome-c peroxidase [Caminibacter pacificus].
ACCESSION   WP_457562433
VERSION     WP_457562433.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..309
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=35230
     Region          30..301
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mfkrlivffs fvllyaepis piplkvkyne dkallgkmlf fdpilsadnk vscaschspk
       61 yggadnkrfs igvfgrvdkp mnsptvynav fncwqfwngr aknlkqqafm antdpdemgm
      121 tpekveekln knnkykklfs lvykkdyisy dmvldaiaef ekalitpncr fdkylrgvhn
      181 aiteqekrgy flfksygcit chngknlggn sfqklgvlvv dvniirgrdr yevthlpydk
      241 yvykvptlrn ialtapyfhd gsvktlkeai vkmgifnlgv kipaedvedi eaflktltge
      301 tpeiiknmr
//
LOCUS       WP_457562435             528 aa            linear   BCT 27-JAN-2026
DEFINITION  single-stranded-DNA-specific exonuclease RecJ [Caminibacter
            pacificus].
ACCESSION   WP_457562435
VERSION     WP_457562435.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Cheng,K., Xu,H., Chen,X., Wang,L., Tian,B., Zhao,Y. and Hua,Y.
  TITLE     Structural basis for DNA 5 -end resection by RecJ
  JOURNAL   Elife 5, e14294 (2016)
   PUBMED   27058167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Lovett,S.T. and Kolodner,R.D.
  TITLE     Identification and purification of a single-stranded-DNA-specific
            exonuclease encoded by the recJ gene of Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2627-2631 (1989)
   PUBMED   2649886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..528
                     /product="single-stranded-DNA-specific exonuclease RecJ"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=60078
     Region          7..503
                     /region_name="RecJ"
                     /note="ssDNA-specific exonuclease RecJ, DHH superfamily,
                     may be involved in archaeal DNA replication intiation
                     [Replication, recombination and repair]; COG0608"
                     /db_xref="CDD:440373"
ORIGIN      
        1 mltkqkikei lssrieeids lsiphflllg diekaakris qaiknqekiv vvgdydvdgv
       61 sssaivklff ekigypieiv ipnrfihgyg lslnileeiq adliitvdng issfeaaeec
      121 kkrgidliit dhhmplimdn gqlkmdngqc mvaneknykl pdalaivnpk tspdfpfkei
      181 cgaevawylc aalkhemklk idlrefvdil aiaiiadvmp lnhmnrllvs mglkrlnkaq
      241 kpfskalkrf fnrefnaedi afqiaprlna agrmdsanla ykfliskdee eafrlfleld
      301 alnnqrkete keilesieve endkfivvsg dyhegvvgii asrlvhkykk paivfcdnge
      361 hlkgsgrslg nidifklvse csddilgfgg hklacglsik kenfyklkek lntiieiydd
      421 ddffiedfvl gelpfreidf elldilksfe pygegnpkpk fiasakimhi qnlkdnhykl
      481 ilsqddyilp giifrydgef devvrfkfti gennyfgrei qlmieefl
//
LOCUS       WP_457562450             317 aa            linear   BCT 27-JAN-2026
DEFINITION  TAXI family TRAP transporter solute-binding subunit [Caminibacter
            pacificus].
ACCESSION   WP_457562450
VERSION     WP_457562450.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Davies,J.S., Currie,M.J., Dobson,R.C.J., Horne,C.R. and North,R.A.
  TITLE     TRAPs: the 'elevator-with-an-operator' mechanism
  JOURNAL   Trends Biochem Sci 49 (2), 134-144 (2024)
   PUBMED   38102017
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Davies,J.S., Currie,M.J., North,R.A., Scalise,M., Wright,J.D.,
            Copping,J.M., Remus,D.M., Gulati,A., Morado,D.R., Jamieson,S.A.,
            Newton-Vesty,M.C., Abeysekera,G.S., Ramaswamy,S., Friemann,R.,
            Wakatsuki,S., Allison,J.R., Indiveri,C., Drew,D., Mace,P.D. and
            Dobson,R.C.J.
  TITLE     Structure and mechanism of a tripartite ATP-independent periplasmic
            TRAP transporter
  JOURNAL   Nat Commun 14 (1), 1120 (2023)
   PUBMED   36849793
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Rosa,L.T., Bianconi,M.E., Thomas,G.H. and Kelly,D.J.
  TITLE     Tripartite ATP-Independent Periplasmic (TRAP) Transporters and
            Tripartite Tricarboxylate Transporters (TTT): From Uptake to
            Pathogenicity
  JOURNAL   Front Cell Infect Microbiol 8, 33 (2018)
   PUBMED   29479520
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   6  (residues 1 to 317)
  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 10194373
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..317
                     /product="TAXI family TRAP transporter solute-binding
                     subunit"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34537
     Region          23..311
                     /region_name="PBP2_TAXI_TRAP_like_3"
                     /note="Substrate binding domain of putative TAXI proteins
                     of the tripartite ATP-independent periplasmic
                     transporters; the type 2 periplasmic binding protein fold;
                     cd13568"
                     /db_xref="CDD:270286"
     Site            order(29,33..35,63..65,83,114,144..146,189..190)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270286"
ORIGIN      
        1 mkklvigals aavlatsafa yeyitigtgg vtgvyyptgg aicrimnkmk kqtgikctve
       61 stggsvynin aikkgeldfg iaqsdvvyqa yngegkfkgk pfkglrvvms ihpelltlvv
      121 rkdsgiknff dlkghrinig npgsgneaav ktlfdyckkm nlndikveql kaaecpnalk
      181 dkkidgyfym vghptanikd aansvaidli sldnvpaaqk lvaekpyyaw gvipagmykg
      241 vnhptktygv kailvtsnkm dektvyyltk aildnfdkfk kmhpayknlt kkdllkgfdh
      301 nmmhpgavka fkeagll
//
LOCUS       WP_457562451             707 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter permease [Caminibacter pacificus].
ACCESSION   WP_457562451
VERSION     WP_457562451.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=77349
     Region          36..706
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mskpevfdad pnlekevdev ekealkegkv dkdleekilt elegqrnfpp ksvyywlial
       61 iafawslyql yvsyfpvnst ivrsihlafa mvlafliypi akkpkflkni qwwdwilaii
      121 gglgaayiai dyvglsnrpg dyltrdivig vifiiillea grrvigmals ivaivfllyd
      181 kfgqylpeii shkgasieki vaqmyltteg iygvplgvsa gfvflfvlfg slleragage
      241 yfiklayafl gkysggpaka svvasgltgi isgsstanvv ttgvftiplm kkagfppeka
      301 aavevaastn gqlmppvmga aafiiaeflg laytdviiaa aipavvsyla llyivhleak
      361 klglkgedpr nlppklktfi sglhylipvv ylmyvlivlr qsaqmaafsa iwllmvimii
      421 qypfyalfie krklqkqdfi qgfidifhgm vngarnmvpi alataiagiv vgsitltgig
      481 qvlldvidtl sngnilivll ltafislilg mglpttanyi vvasltapvm lqlaqdngfl
      541 ipaiaahlfv fyfgiladdt ppvgiaayaa agiakadpik tglqgfaydi rtailpfmff
      601 fntelllias tnewdyneft fisdpikiai ifitallgmf sfssatqgyf lkrinviqrl
      661 lflaavplfm lpnlmvkylh lpneyvsyai glviwaviff wqkaqka
//
LOCUS       WP_457562456             197 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457562456
VERSION     WP_457562456.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 197)
  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 197)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..197
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22932
     Region          23..>191
                     /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          52..82
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..184
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkilliisl tlslfaldik kayyssynye kmgdfkdaik vlipvykkyp dgytinlrla
       61 wlfylnknyq naikhyqkaa milpysvepk lglmrvynti gdydnslkvg nsllktdyyn
      121 yygnyyeiva lmgkknykva selaqkmltl yptsvlflnv laenywymgk kdtakkifnd
      181 vlildpnniv akeylkk
//
LOCUS       WP_457562463             286 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent thymidylate synthase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562463
VERSION     WP_457562463.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Graziani,S., Bernauer,J., Skouloubris,S., Graille,M., Zhou,C.Z.,
            Marchand,C., Decottignies,P., van Tilbeurgh,H., Myllykallio,H. and
            Liebl,U.
  TITLE     Catalytic mechanism and structure of viral flavin-dependent
            thymidylate synthase ThyX
  JOURNAL   J Biol Chem 281 (33), 24048-24057 (2006)
   PUBMED   16707489
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Leduc,D., Graziani,S., Meslet-Cladiere,L., Sodolescu,A., Liebl,U.
            and Myllykallio,H.
  TITLE     Two distinct pathways for thymidylate (dTMP) synthesis in
            (hyper)thermophilic Bacteria and Archaea
  JOURNAL   Biochem Soc Trans 32 (Pt 2), 231-235 (2004)
   PUBMED   15046578
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Mathews,I.I., Deacon,A.M., Canaves,J.M., McMullan,D., Lesley,S.A.,
            Agarwalla,S. and Kuhn,P.
  TITLE     Functional analysis of substrate and cofactor complex structures of
            a thymidylate synthase-complementing protein
  JOURNAL   Structure 11 (6), 677-690 (2003)
   PUBMED   12791256
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Myllykallio,H., Lipowski,G., Leduc,D., Filee,J., Forterre,P. and
            Liebl,U.
  TITLE     An alternative flavin-dependent mechanism for thymidylate synthesis
  JOURNAL   Science 297 (5578), 105-107 (2002)
   PUBMED   12029065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>286
                     /product="FAD-dependent thymidylate synthase"
                     /EC_number="2.1.1.148"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0050797 - thymidylate synthase (FAD)
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /GO_process="GO:0006231 - dTMP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006235 - dTTP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          1..214
                     /region_name="ThyX"
                     /note="Thymidylate synthase ThyX, FAD-dependent family
                     [Nucleotide transport and metabolism]; COG1351"
                     /db_xref="CDD:440962"
     Site            order(18..19,22,55..56,58..59,61,63,76..77,79..80,82,
                     85..89,92,116,126..127,129,133,152..153,155..159,165,167,
                     169,174,189)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:412038"
     Site            order(55,58,80..82,87..88,90,171,174,178,182..183,187)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:412038"
     Site            order(76..77,80,88..92,155,183)
                     /site_type="other"
                     /note="nucleotide binding pocket [chemical binding]"
                     /db_xref="CDD:412038"
ORIGIN      
        1 mnikildlny kptdiavgsa rscyfgkhiv tpenaakwdk knelldsifk aghhttlmhy
       61 hftvliegms rlliwrmlhs hpfynseqvs qryakmkien ftypknadke kwkkyyekmf
      121 fyyeeliekl tpeiekvlpk fkkkeakkra qefaryllpq gmnahlyhti nvitalryia
      181 aakvmpeane eakefakkle iemlridenl apliefakne kvvfpkidie kikkaknigd
      241 ervkvfdivd ydfelnenfa gvmrlssmll desilggfns yiklsl
//
LOCUS       WP_457562457             198 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457562457
VERSION     WP_457562457.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   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   3  (residues 1 to 198)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10361306
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..198
                     /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=23500
     Region          <35..>157
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Region          115..194
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(134,153..154,169,172,179..180,186,191)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mrilvfdyad iydfekefvn neddfytkii ekkydviiln fdfypslvei kkfladdiii
       61 ifvckicdef iykkalsvan ycysydelyk lkirleylek kviklksrvf kyknfifnls
      121 tnqlyqdskp lrltkaesdi lailiknrnk ylskediaam sesidsinsi kviisnlrkl
      181 gfeienvknl gyklkeek
//
LOCUS       WP_457562464             150 aa            linear   BCT 27-JAN-2026
DEFINITION  PulJ/GspJ family protein [Caminibacter pacificus].
ACCESSION   WP_457562464
VERSION     WP_457562464.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Lopez-Castilla,A., Vitorge,B., Khoury,L., Morellet,N., Francetic,O.
            and Izadi-Pruneyre,N.
  TITLE     1H, 15N and 13C resonance assignments and secondary structure of
            PulG, the major pseudopilin from Klebsiella oxytoca type 2
            secretion system
  JOURNAL   Biomol NMR Assign 11 (2), 155-158 (2017)
   PUBMED   28258547
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Korotkov,K.V. and Hol,W.G.
  TITLE     Structure of the GspK-GspI-GspJ complex from the enterotoxigenic
            Escherichia coli type 2 secretion system
  JOURNAL   Nat Struct Mol Biol 15 (5), 462-468 (2008)
   PUBMED   18438417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..150
                     /product="PulJ/GspJ family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17350
     Region          5..>41
                     /region_name="PulJ"
                     /note="Type II secretory pathway, PulJ/GspJ component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG4795"
                     /db_xref="CDD:443823"
ORIGIN      
        1 mrksftllev listlllafv fvamsnilts lkrtesilqs kkedkndyli ktlyydiina
       61 deinvsktan pkidtitlrt fnslykipkp yvkwvvykga liraesvdnf kenvgtidkf
      121 aknvkifkiy kkdgkflifv nnkffefkgr
//
LOCUS       WP_457562465             142 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caminibacter pacificus].
ACCESSION   WP_457562465
VERSION     WP_457562465.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..142
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16617
     Region          5..>35
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 msaikraftl ielilvifli slvsflvikl psysktytfk dirallypgg elyidknsvy
       61 iikngkkkki nfrysefqty dnnfnplkfk nhlfvykmkn gvgdslivke kkvyffkplw
      121 vrkfsslkda kdymnslnea lk
//
LOCUS       WP_457562471             501 aa            linear   BCT 27-JAN-2026
DEFINITION  GspE/PulE family protein [Caminibacter pacificus].
ACCESSION   WP_457562471
VERSION     WP_457562471.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..501
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=56538
     Region          6..497
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mksvkninpk aielenfnle egikfsllpa lledkkvfvt kendyvdaln yynklsvpfe
       61 iimtdeesfn rllnqylevk tkkdlednid evieeelsle dfvkesvdil nsensapvik
      121 fvnsmffqai kkrasdihie thelfglirf ridgvlitqa kiqkkltelv inrikvisnl
      181 disekrvpqd grcqikiank ttdirvsiip tyfgekavmr ilmesedipn lkelgfneei
      241 tqgfkelleh sygmilvtgp tgsgksttlh sflqtistpe kniitvedpv eykadninqi
      301 qvnnkvgltf akalrsilrq dpdiimvgei rdketatiai qaaltghlml stlhtnnaaa
      361 titrlmdmgi epflisssli gilsqrlvrk lcdcktedsl eeiekivkke pllqkyeisk
      421 iykpngcakc nftgyigrka vgelfimnde ikemiakgtn dielksamik hgmktlkeai
      481 feevlngtts lkeairvglk d
//
LOCUS       WP_457562472             395 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Caminibacter pacificus].
ACCESSION   WP_457562472
VERSION     WP_457562472.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44525
     Region          1..392
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mkfkyvgfnk egkkvkgiie asdiqeakqk lsdiaiidik qkrgfnisfg svkkselaki
       61 lnviglylka siplkkainl aknqtqnqkl qkflsfiede ikegktlsea iknqkiiklp
      121 pyivhsiqia qnssnldlil ienakflqee dkinskstqa liypsfiiii slilvivmmn
      181 tvvpkiikif qnlnqnlpti tkitisishf lqnnyillsv gfiiillafs faykkvlffr
      241 kiidslilkt pllkrlsisk nlgrfsslty tltnsgihfm navnlaskti dneilkekfq
      301 kalnevlegk klstslkkqn fpdisfieai alieetgesk nimqnlkeiy lqeydskvsi
      361 llsllepimi livggvigfi vismllpifs mnvmr
//
LOCUS       WP_457562477             194 aa            linear   BCT 27-JAN-2026
DEFINITION  trimeric intracellular cation channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562477
VERSION     WP_457562477.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..194
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21020
     Region          1..194
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mleiadiigi iafsisgfii gvrerldllg gilsafltal gggiirdvla drtifafsnf
       61 lagtlvlivl vlgfyfklhk fdvenktifv lsdaiglssf sisgaivgin agfniygvvf
      121 lalitavggg mlrdmlinki pfilrekfya tisiligvfl yifgtnveil iltlimgvii
      181 rliaykknwq lpki
//
LOCUS       WP_457562484             316 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457562484
VERSION     WP_457562484.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..316
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=35647
     Region          17..95
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(18,29..30,32..33,35..36,39..40,42,49..56,58)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          84..292
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mkkganikke iiattnervd kflskelnen rnqieqlikk glvkinsksi kkggvklkqg
       61 diieitfpkt eekeskkadf dipilyeded lliinkppgv vvhpapsyke atlvdwlkqk
      121 gyslstiagd erfgivhrid ketsgalvia knnkthefls nqlkdksmgr yylmllnepl
      181 keakcveapi arnpknrlkm aivnggkeak tlfvpiqdnl taaklftgrt hqirvhltkl
      241 gryisgdtty gkkeqkiprv mlharelylt hpngqklsii aplfddfknl iqgiddekis
      301 slsnifatyd gmcykq
//
LOCUS       WP_457562487             259 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457562487
VERSION     WP_457562487.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29984
     Region          5..257
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mkkrsslhif fsvvkalllr eiqtrfgtqk lgylwaliep mstiiifali kealhpngmp
       61 gisypvflas gmiayfmfrn iviksmdsft ankglfvykq vkpfdtilsr ylletnlhfi
      121 ivlvflfigw ylgldieckn ilgvltayiw lslfglslgi lfavlgfffe nfkkiigimf
      181 lplyfmsalf ydvsslppva qkilyynpvv hfmemihgny fygmdtkfvd ydymliwtiv
      241 pafvglwlyk kserkiims
//
LOCUS       WP_457562494             247 aa            linear   BCT 27-JAN-2026
DEFINITION  carbonic anhydrase [Caminibacter pacificus].
ACCESSION   WP_457562494
VERSION     WP_457562494.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..247
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27433
     Region          1..247
                     /region_name="Cah"
                     /note="Carbonic anhydrase [Inorganic ion transport and
                     metabolism]; COG3338"
                     /db_xref="CDD:442567"
ORIGIN      
        1 mkkllaslai samtagtlma snyahgtwsy sgktgpeywg dlkkeyimck igknqspidv
       61 sgavsatltp lniyydvkak tflnnghtvk aemkdgakly idgkefkllq fhfhtpsent
      121 ingeyfpmea hfvhstkdge lavvavmfki gkynpalqkl vdnmpkkpgv knnlcpanlk
      181 akdllpksle yyrfngsltt ppcsegvrwf vlkqpvevse kqikafekvm gknnrplqpi
      241 narvilk
//
LOCUS       WP_457562496             265 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Caminibacter pacificus].
ACCESSION   WP_457562496
VERSION     WP_457562496.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 265)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..265
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <8..251
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 leeicslnek leemnknlek rvkeesekri kqeelilres kyiqmgemmd avahqwkvpl
       61 saimlesgll kmiiekkgci ddeikksinn iqeyinhlne tldnfrnfln tknyeeflis
      121 eviesvknlv kdllvinnvr letqiknfki ygrkndfehi llslidnsik ifnqrniner
      181 vikikakdye iiyednaggf egdiekifdf nysktggsgi glyivkmild kyggdikaqn
      241 ikngirfiin lkkfrynsns kkike
//
LOCUS       WP_457562499             339 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease [Caminibacter pacificus].
ACCESSION   WP_457562499
VERSION     WP_457562499.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..339
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39964
     Region          3..336
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 myfryllkky fksfmlvfig lsflyvivdf mfnyaklpss snlqvlyafy vfiyasytlf
       61 plaiifgfll svssmikfne fvsfyslgfr pkkllkpfli falsvtalmy llqssklaya
      121 nqyatsiken fnyktynlfl kyknnivyik sinpfskmaw gikvfeiknr kitkviyakr
      181 avfendkwkt knaeimtlkq nvwqkeqkpl vflenftpki lsnlktldni sfydayitir
      241 yfkdidlnmi lsivffkift pllmiafliy lfftapihvr isnvslfmik svtfsvilwa
      301 gellifkfak qgilpfwtla vpflvvviid flvirrsyd
//
LOCUS       WP_457562501             250 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD-IIA family hydrolase [Caminibacter pacificus].
ACCESSION   WP_457562501
VERSION     WP_457562501.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..250
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28526
     Region          1..239
                     /region_name="NagD"
                     /note="Ribonucleotide monophosphatase NagD, HAD
                     superfamily [Nucleotide transport and metabolism];
                     COG0647"
                     /db_xref="CDD:440412"
ORIGIN      
        1 mrgyfidiqg tliddknflp lpgaveflky lnskkipfil ltnntkrdsk efidylknlg
       61 fefenyldpl mvlddyvkgk kiapygnekf velmkkyeid fknpdavvlg iklfsneefa
      121 diiemllrgs eligmhktsl yskgdkrypg lgailemley avnkdykvvg kpsatffnra
      181 keilgldydk itiisddlyg dllpakdlgm ksvlvlsgki kspeeitkkp deiyknledy
      241 lrngvinert
//
LOCUS       WP_457562512             125 aa            linear   BCT 27-JAN-2026
DEFINITION  ExbD/TolR family protein [Caminibacter pacificus].
ACCESSION   WP_457562512
VERSION     WP_457562512.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..125
                     /product="ExbD/TolR family protein"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13934
     Region          2..125
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mrkpelnitp fvdimlvlla ilmvsvtvtt yqeksvnlpq gskttpatkk atinivikkd
       61 gtvlvngeqf qlkdflenfn lkygnfnknv lvyiaadkdi kydtfmkvya gvvktgfrqi
      121 glltk
//
LOCUS       WP_457562520             487 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457562520
VERSION     WP_457562520.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 487)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..487
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57382
     Region          <212..481
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msqkrsksvf flvfliiimf lfsmiifvtf kkvekriskd tfdfllkevk sfsrnieryl
       61 llkygdllvv lnkkpllrsd vnlylssyit snfknvflay ydgkffrvig dgslnpkdrf
      121 dynerfeptr kdlwlkaikt kktiyykqdi kgiwttyiyp vldnnlkvsy lividfstep
      181 lsyidnnlii lkkslflfis vlllsvlils ifllydilrq kkmqkllkel qilnktlesr
      241 vkeeveksre kdrqlimqsr lalmgellsm iahqwrqpln viggvvadme mdmmlnendp
      301 kktkenleti kkmikhlsst iddfrkfyrk dnekieidfn eilqevlnia ssslknknik
      361 iknhlkckrk iktypnelkq vllnliknae dilierkien pkiiieifen ddkciievkd
      421 ngggvdkeyq dkifepyftt knekngtglg lymsknivek rlggeilqyn dtegavfriv
      481 lrmrdel
//
LOCUS       WP_457562516             166 aa            linear   BCT 27-JAN-2026
DEFINITION  FKBP-type peptidyl-prolyl cis-trans isomerase [Caminibacter
            pacificus].
ACCESSION   WP_457562516
VERSION     WP_457562516.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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 166)
  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..166
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..166
                     /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=17709
     Region          7..133
                     /region_name="SlpA"
                     /note="Peptidyl-prolyl cis-trans isomerase, FKBP type
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1047"
                     /db_xref="CDD:440668"
ORIGIN      
        1 matvygieyt vknskgevvd snvgqaplef vagkgqiipg lekevekmev geektvtvpa
       61 aeaygeyred miqtlprdqf egielekgmt lygqtpdgqm vavtvkdfnd qevtidynhp
      121 lagedltfdv kvvtkreatp eealtgqvga qahgghcgsg scgcgh
//
LOCUS       WP_457562522              82 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase, partial [Caminibacter pacificus].
ACCESSION   WP_457562522
VERSION     WP_457562522.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 82)
  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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>82
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
     Region          1..>82
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkpkiyekki ivskedidfn ghvnnlkyle wminvamehs thegfgveyy kthgvswvar
       61 khcieyklpa fegdelvlkt wi
//
LOCUS       WP_457562525             199 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562525
VERSION     WP_457562525.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 199)
  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 199)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..199
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23539
     Region          46..138
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mtkeliestl nyynknansl veryekanlk klqeyilkfv dkndfilelg fgsgreinfl
       61 lkncfeniyg idgceefvkk arerfksnnf yfsilpdini pknikfdfiy siavwmhlpt
      121 evyeetvnni inllkengkv llsfslderr ekgryfqkvd eilletlfkk nnmkkldeiv
      181 tvdslnrkiq wksviygkn
//
LOCUS       WP_457562532              93 aa            linear   BCT 27-JAN-2026
DEFINITION  EscU/YscU/HrcU family type III secretion system export apparatus
            switch protein [Caminibacter pacificus].
ACCESSION   WP_457562532
VERSION     WP_457562532.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Galan,J.E. and Collmer,A.
  TITLE     Type III secretion machines: bacterial devices for protein delivery
            into host cells
  JOURNAL   Science 284 (5418), 1322-1328 (1999)
   PUBMED   10334981
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Hueck,C.J.
  TITLE     Type III protein secretion systems in bacterial pathogens of
            animals and plants
  JOURNAL   Microbiol Mol Biol Rev 62 (2), 379-433 (1998)
   PUBMED   9618447
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Kubori,T., Matsushima,Y., Nakamura,D., Uralil,J., Lara-Tejero,M.,
            Sukhan,A., Galan,J.E. and Aizawa,S.I.
  TITLE     Supramolecular structure of the Salmonella typhimurium type III
            protein secretion system
  JOURNAL   Science 280 (5363), 602-605 (1998)
   PUBMED   9554854
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..93
                     /product="EscU/YscU/HrcU family type III secretion system
                     export apparatus switch protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=10313
     Region          8..92
                     /region_name="YlqH"
                     /note="Type III secretion system substrate exporter,
                     FlhB-like [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2257"
                     /db_xref="CDD:441858"
ORIGIN      
        1 mkkstnikav alkykayedn apkvvakgkg vlaqkiiqka keydvplfqn ealadmllsv
       61 evgeeippkm yeavievfvw lynleekaql skg
//
LOCUS       WP_457562535             418 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457562535
VERSION     WP_457562535.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..418
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46231
     Region          23..401
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mnaklifssi iigiitgifi viyalatkyl sfllflgdpf etidklpvwy iylvpflsil
       61 ivnyliskne kvkeygvaei akavdenkmt fsikdlflki fasslslasg favgnegpsa
      121 aigamiaqkf hnifnlpkkl lkvslsigas sgiaaifvsp itgimfaien iayefvrdfa
      181 gylilasvia fsiawhflep lifnystgkf ieyryifati lfipvitffi yfylslkeiv
      241 lkflkekihl psknfvlaai gsfiigtili ispyaafsgh evvkilinds nhfplymifi
      301 liilrivats vslyanavgg vfialmsiga lvgygfgevm vyvdfpiepf yfaaigagvf
      361 mgvnmrlplt avvlalevty dynviiptgi svvivtylst lkfdirklsi lihhkekt
//
LOCUS       WP_457562537             192 aa            linear   BCT 27-JAN-2026
DEFINITION  O-methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562537
VERSION     WP_457562537.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..192
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21773
     Region          30..192
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 msneyvkepr alknivadtk kigfdmcgek dvgvllrvlv asksgeflel gtgtglstaw
       61 ildgmdensh litvdndekl lgiakkhlgh yknvefvcdd gnaflerlkk enkkfdfifa
      121 dtwagkyeml edtlemlnek afyiiddmlp qsnwpeghek kveklidylh nredleivnl
      181 dwssgvivcv kk
//
LOCUS       WP_457562540             501 aa            linear   BCT 27-JAN-2026
DEFINITION  GspE/PulE family protein [Caminibacter pacificus].
ACCESSION   WP_457562540
VERSION     WP_457562540.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..501
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=56541
     Region          6..497
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mksvkninpk aielenfnle egikfsllpa lledkkvfvt kendyvdaln yynklsipfe
       61 iimtdeesfn rllnqylevk tkkdlednid evieeelsle dfvkesvdil nsensapvik
      121 fvnsmffqai kkrasdihie thelfglirf ridgvlitqa kiqkkltelv inrikvisnl
      181 disekrvpqd grcqikiank ttdirvsiip tyfgekavmr ilmesedips lkelgfneei
      241 tqgfkelleh sygmilvtgp tgsgksttlh sflqtistpe kniitvedpv eykadninqi
      301 qvnnkvgltf akalrsilrq dpdiimvgei rdketatiai qaaltghlml stlhtnnaaa
      361 titrlmdmgi epflisssli gilsqrlvrk lcdcktedsl eeiekivkke pllqkyeisk
      421 iykpngcakc nftgyvgrka vgelfimnde ikemiakgtn dielksamik hgmktlketi
      481 feevlngtts lkeairvglk d
//
LOCUS       WP_457562543             142 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caminibacter pacificus].
ACCESSION   WP_457562543
VERSION     WP_457562543.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..142
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16672
     Region          5..>35
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 msaikraftl ielilvifli slvsflvikl psysktytfk dirallypsg elyidknsvy
       61 iikngkkkki nfrysefqty dnnfnplkfk nhlfvykmkn gvgdsliike rkvyffkplw
      121 vrefsslkda kdyinslnea lk
//
LOCUS       WP_457562546             261 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562546
VERSION     WP_457562546.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>261
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          3..>261
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mrvlivgagi igmtmawewr kkhpddeivi idkepheafh asgknsgvlh agfyyssdsl
       61 kakltargnk lmkefcyshn ipvnetgklv vaknedevet lhelakrsva neagayiitq
      121 eeaekidpna kthkyalysp ntatvnprev crvlkeelqk kdvkfifnmp fekynesydf
      181 linaaglyad kiahkfgvgl eytmlpfkgl yrkylgedki ktqiypvpni knpflgvhft
      241 lmadntikig ptaipafwre n
//
LOCUS       WP_457562549             306 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457562549
VERSION     WP_457562549.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..306
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35062
     Region          <9..60
                     /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"
ORIGIN      
        1 msanifeqys ieeiskrtki spislrfikn keyekiprvk figfikiier efnvdlsdli
       61 eefdqanntt tkkekpqkti eetpkptqpq tseikekksy lviilaviil iiagailynf
      121 sktkqppven nitqneiqqp kprndnktni iqeqpqketa ieiqkpvstn trnivqptsq
      181 nneqnieatn nknttpntnn vsttqkittp ktapqkvqtt ysvtiipqkr vwyrainldt
      241 nktieyltsn pktlpkgnyy ikfghglvti eyankqinpd tkkivriilk ngkyeyiknp
      301 pagypk
//
LOCUS       WP_457562563             323 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562563
VERSION     WP_457562563.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 323)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..323
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38023
     Region          <146..323
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkqkikyiil isltvvsisf leytknqkik eidnqivslk tpihflfnvq ymfnkamltq
       61 nkalklqyid taeyftnlik nnseikkflq rekikiskne dnpvkdskel yeiikniagk
      121 qylnilnsle nlkkfkniin qtfmmvdlsi ivltvlliil yenkrhknhl eeasfkdylt
      181 ntynrrkfye iasmlpndkk htlimldidh fkqindnygh ekgdfvlkev adiirhnirk
      241 ndyifrwgge efivllkntd ieggmkvvek lkedienhdf qglkitssfg icetnvindn
      301 ilqeldraly eskrngrnri tva
//
LOCUS       WP_457562567             145 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEA family DNA-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562567
VERSION     WP_457562567.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..145
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16194
     Region          18..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 mkktllalaf alsslmaidf ntaskaelmk vkgigpkkae aiiqyrkthk iksindlkni
       61 kgfnsktisk iknqksalkd kanakkaalk nkkskmkakm nskkealknk kaklnakksq
      121 lkkmkkekmq klnskksafk nkvkf
//
LOCUS       WP_457562573             320 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457562573
VERSION     WP_457562573.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..320
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37681
     Region          31..>152
                     /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          63..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(65..66,69..70,72,95,98..99,102..103,105..106,129,
                     132..133,136..137,140)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          93..123
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdfrdplfsv ivffvivlls vivtliagri reyfrqkeie kllldfeyve iedlkldkas
       61 knallllaka yektgdyeka lkiylwinkn desidilrni aflyfkagfl ekskkvvyni
      121 lkvkprdkea lklliwidek lgnykeivdv ldvfnelgvd lpkekanali klithggcni
      181 edfckgfesf ediykkypfv rreyvaylfk ydprkaydvl dvyedldlyf yrndipknek
      241 fcnilaakke tkcdikapfe levlkyipkn lgelefeyic nackkvfply strcpnchel
      301 fsqklitkla ekknienief
//
LOCUS       WP_457562579             293 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caminibacter pacificus].
ACCESSION   WP_457562579
VERSION     WP_457562579.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10508826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..293
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33574
     Region          5..273
                     /region_name="LPG_synthase_TM"
                     /note="Lysylphosphatidylglycerol synthase TM region;
                     pfam03706"
                     /db_xref="CDD:461018"
ORIGIN      
        1 mvtkiiktvl laaiifyify gfdfskidls vispktvlls sfvlflgqii lsirfmyiid
       61 skflpaleti vvsnalnmil parlgeaaka vylkkfsnyp ynvgisavfi erffdvimlf
      121 liiigwiyff vteeyvkksa iilfffiilv lvffntgfmr slvekvpfey pkivyknins
      181 mfkkspvlif wsivlwgsyl lsyyiffdml gfkevvelfi vstvalmipl apaglgtfeg
      241 vvvfylhkyg iskedallla styhfllfav dmimfavfll lkdikfselk alk
//
LOCUS       WP_457562590             240 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-2,3-diacylglucosamine diphosphatase [Caminibacter pacificus].
ACCESSION   WP_457562590
VERSION     WP_457562590.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Bohl,H.O., Ieong,P., Lee,J.K., Lee,T., Kankanala,J., Shi,K.,
            Demir,O., Kurahashi,K., Amaro,R.E., Wang,Z. and Aihara,H.
  TITLE     The substrate-binding cap of the UDP-diacylglucosamine
            pyrophosphatase LpxH is highly flexible, enabling facile substrate
            binding and product release
  JOURNAL   J Biol Chem 293 (21), 7969-7981 (2018)
   PUBMED   29626094
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..240
                     /product="UDP-2,3-diacylglucosamine diphosphatase"
                     /EC_number="3.6.1.54"
                     /GO_function="GO:0008758 - UDP-2,3-diacylglucosamine
                     hydrolase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28150
     Region          15..220
                     /region_name="LpxH"
                     /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxH
                     [Cell wall/membrane/envelope biogenesis]; COG2908"
                     /db_xref="CDD:442152"
ORIGIN      
        1 mrvqnvslkk gacliadvhy kkgdekflsl lrywlenppp qifflgdifh lllpfdylie
       61 ynkdaielin rlarktevyy tpgnhdfnld tifknikiad afvdeeksvf lthgdltdkd
      121 ifykfyvfli rnylgnklln lvsfnfvnnw lfkailqkkv kclkifdfka kikskiadid
      181 ykmiveghyh qnesfdfgdk ryvnlgafvc dgsyfvyene ikgyqwmtkl sksaqtnsns
//
LOCUS       WP_457562599             368 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562599
VERSION     WP_457562599.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 368)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..368
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42512
     Region          1..368
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrwiviflav lvfgasvttt kkeikktqii iskmndkldk larairkkqq sinslnskin
       61 slnkeiaklq etlkdankvl gelndlkkgy vekenrikne iidflstnyy ldtqevdnvn
      121 dliyneiskk ileanaqkia kivkqsktin qnissineki dqiikkqqel kskkekllsl
      181 lkarkkeiqa lnrqkllykk rlealirkqk nlqnrlaqlk iikkrkqtsv qqpnynvkta
      241 vykgqktipp lrgrvikkfg syidpvykir iyndsitikp yqknaivrai mpgkvvyige
      301 nndkkiivik hkgdifsiya nldkisplik kgkyvkrgqi iarvtdtlef evtykekpin
      361 plkvislr
//
LOCUS       WP_457562606             100 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562606
VERSION     WP_457562606.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>100
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [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          3..>99
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskeakkeqi mktalelfak kgfytttiad iaremgmsvg nmynyfpske slakelliyt
       61 skkfgdeirk indmdisske kikkivelyf kmaktepelv
//
LOCUS       WP_457562630              74 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562630
VERSION     WP_457562630.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..74
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=8810
     Region          2..>46
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 meipplstmk dinrkyknla kkfhtdvggd sekikeinma yeilkdyimn frftfsedei
       61 lrqypdeflk kfkv
//
LOCUS       WP_457562634             298 aa            linear   BCT 27-JAN-2026
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Caminibacter pacificus].
ACCESSION   WP_457562634
VERSION     WP_457562634.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 298)
  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 298)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..298
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=34630
     Region          <15..296
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mekvfferie kinpkiidgl kekkefsfri nrhkadleai delreegynp kkvewsdyvy
       61 tlpiedrkkv tkskpytsnk iyiqnlssii aanaldiden dwvldlaaap ggkslifsek
      121 askvsavepd kkrffrmkrn fkehgakniq tynkdgrfvy katgpifdkv fldapcssea
      181 hidleegitw wnlkrvrrfs klqkeliisa feclkpggem iyatctfspe eneevidfll
      241 nrydnaevvk vdlpidniqe gmtkwedkey npevrkciri lpkdaysgff ftkikklp
//
LOCUS       WP_457562650             108 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator, partial [Caminibacter pacificus].
ACCESSION   WP_457562650
VERSION     WP_457562650.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>108
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
     Region          1..>103
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdlhnylgyl iisiltitsp gaaillainn smkydlravv fsslgnilgl fllslvamfg
       61 vgvliktsdm ffwilkiiga iyliylgvkh misghkefhl sqtnehir
//
LOCUS       WP_457562642             317 aa            linear   BCT 27-JAN-2026
DEFINITION  TAXI family TRAP transporter solute-binding subunit [Caminibacter
            pacificus].
ACCESSION   WP_457562642
VERSION     WP_457562642.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Davies,J.S., Currie,M.J., Dobson,R.C.J., Horne,C.R. and North,R.A.
  TITLE     TRAPs: the 'elevator-with-an-operator' mechanism
  JOURNAL   Trends Biochem Sci 49 (2), 134-144 (2024)
   PUBMED   38102017
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Davies,J.S., Currie,M.J., North,R.A., Scalise,M., Wright,J.D.,
            Copping,J.M., Remus,D.M., Gulati,A., Morado,D.R., Jamieson,S.A.,
            Newton-Vesty,M.C., Abeysekera,G.S., Ramaswamy,S., Friemann,R.,
            Wakatsuki,S., Allison,J.R., Indiveri,C., Drew,D., Mace,P.D. and
            Dobson,R.C.J.
  TITLE     Structure and mechanism of a tripartite ATP-independent periplasmic
            TRAP transporter
  JOURNAL   Nat Commun 14 (1), 1120 (2023)
   PUBMED   36849793
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Rosa,L.T., Bianconi,M.E., Thomas,G.H. and Kelly,D.J.
  TITLE     Tripartite ATP-Independent Periplasmic (TRAP) Transporters and
            Tripartite Tricarboxylate Transporters (TTT): From Uptake to
            Pathogenicity
  JOURNAL   Front Cell Infect Microbiol 8, 33 (2018)
   PUBMED   29479520
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   6  (residues 1 to 317)
  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 10194373
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..317
                     /product="TAXI family TRAP transporter solute-binding
                     subunit"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34579
     Region          23..311
                     /region_name="PBP2_TAXI_TRAP_like_3"
                     /note="Substrate binding domain of putative TAXI proteins
                     of the tripartite ATP-independent periplasmic
                     transporters; the type 2 periplasmic binding protein fold;
                     cd13568"
                     /db_xref="CDD:270286"
     Site            order(29,33..35,63..65,83,114,144..146,189..190)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270286"
ORIGIN      
        1 mkklvigals aavlatsafa yeyitigtgg vtgvyyptgg aicrimnkmk kqtgikctve
       61 stgvsvynin aikkgeldfg iaqsdvvyqa yngegkfkgk pfkglrvvms ihpelltlvv
      121 rkdsgiknff dlkghrinig npgsgneaav ktlfdyckkm nlndikveql kaaecpnalk
      181 dkkidgyfym vghptanikd aansvaidli sldnvpaaqk lvaekpyyaw gvipagmykg
      241 vnhptktygv kailvtsnkm dektvyyltk aildnfdkfk kmhpayknlt kkdllkgfdh
      301 nmmhpgavka fkeagll
//
LOCUS       WP_457562655              93 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Caminibacter pacificus].
ACCESSION   WP_457562655
VERSION     WP_457562655.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..93
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10412
     Region          12..>92
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mqiidfneie skeryklmag niiprpvawi vtqnngiinv apfsyftgvs skppllmvsi
       61 grkkptidep kdtfkniket kkasvclvpi emy
//
LOCUS       WP_457562657             396 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562657
VERSION     WP_457562657.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 396)
  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 396)
  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 18641711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>396
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <231..385
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(302..303,306..307,309,331,334..335,338..339,
                     341..342,365,368..369,372..373,376)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <316..392
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          329..359
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkglfslfv ifnllfgyel ivknekdvkv lndlgvkcek iangfvcaks pdkmqlkrlq
       61 yylknnlsit seivgvqekl sdaskpvmsv kpvksavdik tpkkvaknsk tliktgyciq
      121 vvsarksqgl leifgktknl plsriekigp yyvlrigeek nenalqsvlq kakkinknay
      181 irkcdlipqr iiksnfkpka kkkqeikipq gevfnkvfsp eeknklmeka fkegriylar
      241 nlsnqlkstn gykkdaflit vnilmqkkey krvcnmltql sdfykgknls eikekscfyy
      301 nyqkgveymn inpeialdfl kkaqkfksdd nllfataiay mnqydykkak eilqklyknd
      361 sdntaiklay aktlfnlgdf ktlerikdnn laffnh
//
LOCUS       WP_457562668             490 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562668
VERSION     WP_457562668.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   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 490)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..490
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..487
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 qqyyiayige divrkirdkf lshilsldlm ffktthsgel vsriindinr iqnaistqma
       61 nliqnilmai flmgvviyqn prlaffalii lpilvwpisi itkklkqlsk ksqaktadin
      121 khlsevfkni etikaynakk deikhfyenn lnffkinmkt krtqiiltpi leffsaiiaa
      181 iviivggkev idgsmsvgaf fsfmtalfmm tdpirkvaks isnmqeaiaa nerlkeifsi
      241 kphitsgkek lkeikkiefk nvtlkygdkt alkninynak kpkiiglvgd sgggkssfvs
      301 lilrfydane geilindkni knynlhslre kiayipqnih ifndtiaani aygkeideek
      361 vknalkkanl ldfvesleng iytilneggs nlsggqrqri aiaralygnp dvlildeats
      421 aldnkseavi mktienlkdk lvfvvahrls tienadeilv fkngkivckg kkeellence
      481 tfkrlykgnm
//
LOCUS       WP_457562685             517 aa            linear   BCT 27-JAN-2026
DEFINITION  L-aspartate oxidase [Caminibacter pacificus].
ACCESSION   WP_457562685
VERSION     WP_457562685.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..517
                     /product="L-aspartate oxidase"
                     /EC_number="1.4.3.16"
                     /GO_function="GO:0008734 - L-aspartate oxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0009435 - NAD+ biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56548
     Region          1..517
                     /region_name="NadB"
                     /note="Aspartate oxidase [Coenzyme transport and
                     metabolism]; COG0029"
                     /db_xref="CDD:439800"
ORIGIN      
        1 mkydilvigs giagmmaaie akelgsnvai vmkkspmann sfmakggina alnnmgdgds
       61 iehhiqdtlk agmglaeeea vrifceqapq ivrelhrkfk vpfttlpdgr laqrpfggtk
      121 fkrtvfaada tgpaimkaln kalndlnidt iknhfalnll indgkiagat lvdekgelkv
      181 iqakavivat ggfaglyrgh ttnitdatgd giamglragl eamdmefvqf hptglegtny
      241 liseaargeg gklinsdgke fvdelntrdf vtraivkqlq kgkkvyldlt dipeeiintk
      301 linlkkrvks lkgidiskep ipisplahyt mggiktdtyc ftdieglfya geagnngvng
      361 anrlggnsls egavfgriag yqavkyshrq qtqiepkked iqkdkeliet lkntkidakk
      421 ikdeigeilf nklgilrngy aikkaldkfe dikremsqnh endsslneki eclnaldiak
      481 vlaksalyre esrgahfrmd ypesdhaflh htlekld
//
LOCUS       WP_457562687             460 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457562687
VERSION     WP_457562687.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..460
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50170
     Region          1..458
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mldkkhieel kkivgeedik tdkihlrays ydatkehyyp eavvfpqdee evskilkycn
       61 dnkiaviprg agsgftggal pvnggiilav ekymnkilei dekdmvavvq pgvvnahlqk
      121 aveekglfyp pdpasmdyst iggnvsenag gmraakygit kdyvmslkav lpngdiirag
      181 krtikdvagy nvagiliase gtlaviteit lkllpkpkmk ktymgifenv edamnavyks
      241 lasgampvam efmdslvvka lreklgvnlp dwagalligd vdgnveeein yqlgileksf
      301 kengckefkv ardeneanei wyarrnasqs itiygskkin edisvprskl pdalrvitqi
      361 gekyglvvpc fghagdgnih vnvmvdgsne devkrgyeav eeifkavvdm ggtlsgehgi
      421 glskapfmki afseaelnlf krikeafdpn gilnpgkmgl
//
LOCUS       WP_457562689             388 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457562689
VERSION     WP_457562689.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..388
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42892
     Region          1..385
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(97..99,123,173,204,232,234..235,243)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(100,133,197,241..243,273,276)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            235
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfskriekls psltiaisqk arelkaqgkd vlafsagepd fdtpevikka aikaieegft
       61 kytavagipe lleaiktklk rdndleyetd eivvsngakq slfnifacli degdeviipa
      121 pywvtypelv kyhggvpvsi etdestgfki tpemlkqavt pktkilllts psnptgavyt
      181 keelkaladv lkdtniwvvs demyekliyd gkftatasin edmlkrtitv nglskshamt
      241 gwrfgycask nkelvknmik lqsqstsnin sitqkaaipa llgeadadve mmrkefekrr
      301 dyvyeafnki pglsaakpag afyifvnhke impesmnfal tlledkgvav vpgvgfgseg
      361 yfrfsfatdi etikegikri eefvkais
//
LOCUS       WP_457562690             415 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase, partial [Caminibacter pacificus].
ACCESSION   WP_457562690
VERSION     WP_457562690.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 415)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..415
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          153..403
                     /region_name="COG4938"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443965"
ORIGIN      
        1 hivyelnkfn lnidifeeik knlniepkkf ieyinknkir esditfdidi niddeiilek
       61 qleikidnni shiinelkni lenllseyln ktfnsetnil qkieikddik lnekisirfv
      121 ykkdqnneei linhfllall kyllnfkisq ktfyfpasrt gfvlafdeiv sglfidklgg
      181 tptntkltkp tkeflqnfad ikigkfedhd lfnkmmkdkn ikklieyiqk niihgiieek
      241 kehnytkyyl ntnnknlelh vtssatvell piivflkhfi tlndklliie epeahlhpka
      301 qiymarfial mvnygikvli tthsdyiine lnkliklnfi nqkkkekyye kndlsenfcl
      361 kpeqiaaylf keektkvkvk klfideygis nenidevlee ltenaillne widne
//
LOCUS       WP_457562694             363 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562694
VERSION     WP_457562694.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..363
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41856
     Region          73..358
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqqnsfesll silnykflsl plykivlafv vlflflvlrr aftlyilkff rflvrktkte
       61 lddkflkaik nplrflfvia glyffflfle vdyaiikhil kgllifdifw alynivgefe
      121 eyiykglgkf grasrefvsf iikllkifiv sigiiallqd wginvtgfla slglgglafa
      181 laakdtaani fggiailtdn ifkigewvkv gnvegivedi gmrttkiraf derliilpna
      241 tiansaveny srrdkrrimm riglvyntpi etikkitdei remllnhpdi akdeslliyf
      301 dqfedsslsi fcyfftntav wkdylrired inlkiidive rngsafafps nsiyfetplk
      361 ier
//
LOCUS       WP_457562695             427 aa            linear   BCT 27-JAN-2026
DEFINITION  NCS2 family permease [Caminibacter pacificus].
ACCESSION   WP_457562695
VERSION     WP_457562695.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..427
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45591
     Region          1..427
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mferifklne hgtnvstevr agfttflamm yivpvnasim sltgmpfdal itatavvtii
       61 stilngfwsn tpvamsvgmg lnayftfglv kgmhlpwqta lgivmisgli flvlsltrfr
      121 awvfesvpid lrraisagig afiafiglkg mgaivsnpat fvtlgnlhnp evllgvegfi
      181 laalfysyri kgafilsial tsitawvfgl gklpegiism pasiapiafk fdiwdalkls
      241 llpvivtflv tdlfdtigtl agigmraglf kdpkelektl qadaaatvig aslgtsttts
      301 fiesaagvee ggrtgltavv tgllfittlf flpiykaipd naiypilvmv gvlmfgelrd
      361 vdfsdittsv svfltvilmp ltysitlgls agfvvyfila llrgekekit fgtasialig
      421 llmfivh
//
LOCUS       WP_457562696             403 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate
            ligase [Caminibacter pacificus].
ACCESSION   WP_457562696
VERSION     WP_457562696.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Gordon,E., Flouret,B., Chantalat,L., van Heijenoort,J.,
            Mengin-Lecreulx,D. and Dideberg,O.
  TITLE     Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:
            meso-diaminopimelate ligase from Escherichia coli
  JOURNAL   J Biol Chem 276 (14), 10999-11006 (2001)
   PUBMED   11124264
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..403
                     /product="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,
                     6-diaminopimelate ligase"
                     /EC_number="6.3.2.13"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008765 -
                     UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45370
     Region          <58..403
                     /region_name="murE"
                     /note="UDP-N-acetylmuramoylalanyl-D-glutamate--2,
                     6-diaminopimelate ligase; Provisional; PRK00139"
                     /db_xref="CDD:234660"
ORIGIN      
        1 mdlihylnns litdntkeld snklflktsq nskyakdikn yitpkellks lnlktkfigi
       61 tgtngkttta fvlgyllnsl gysvgiqgte gfyfngelke pktlttppif ttikrafkyk
      121 pdfyimevss haivqdrieg lefeakimts fsqdhldfhk smeeykqvke sffqddsiki
      181 ingkwkmeng kliivnvggy dfkvnpnnly vlekpivddi pmagefnkmn fslalktasl
      241 ltnsslstfd fslfkgvagr meivskdplv iidfahtpdg mekvlsaveg kkivvfgagg
      301 nrdkdkrhlm gevaskyady iivtndnprc enpqdiakdi ikgiskpyev ildrkeaikk
      361 alklakeknm tlmilgkgde kymelcdkki pfsdkeavfe vis
//
LOCUS       WP_457562697             113 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457562697
VERSION     WP_457562697.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..113
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13587
     Region          1..113
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mlnrdkelfl rdiiesidai fdhikgyele dfkndrktyq avvkefeiig eatknvyell
       61 kekypnypwr liidfrnklt nedfgvdfvl iwntiflklp elkqmiekli kel
//
LOCUS       WP_457562700              90 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562700
VERSION     WP_457562700.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..90
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10394
     Region          <20..81
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mkkttsemie elkakgfkdi fiwsdskgty ydwhkhpyde irvmlkgemi intkesqyhl
       61 kagdvlnvpa gevheayvle dceyicgsky
//
LOCUS       WP_457562705             177 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine phosphate synthase [Caminibacter pacificus].
ACCESSION   WP_457562705
VERSION     WP_457562705.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Peapus,D.H., Chiu,H.J., Campobasso,N., Reddick,J.J., Begley,T.P.
            and Ealick,S.E.
  TITLE     Structural characterization of the enzyme-substrate,
            enzyme-intermediate, and enzyme-product complexes of thiamin
            phosphate synthase
  JOURNAL   Biochemistry 40 (34), 10103-10114 (2001)
   PUBMED   11513589
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Reddick,J.J., Nicewonger,R. and Begley,T.P.
  TITLE     Mechanistic studies on thiamin phosphate synthase: evidence for a
            dissociative mechanism
  JOURNAL   Biochemistry 40 (34), 10095-10102 (2001)
   PUBMED   11513588
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Begley,T.P., Downs,D.M., Ealick,S.E., McLafferty,F.W., Van
            Loon,A.P., Taylor,S., Campobasso,N., Chiu,H.J., Kinsland,C.,
            Reddick,J.J. and Xi,J.
  TITLE     Thiamin biosynthesis in prokaryotes
  JOURNAL   Arch Microbiol 171 (5), 293-300 (1999)
   PUBMED   10382260
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..177
                     /product="thiamine phosphate synthase"
                     /EC_number="2.5.1.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004789 - thiamine-phosphate
                     diphosphorylase activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20281
     Region          1..173
                     /region_name="ThiE"
                     /note="Thiamine monophosphate synthase [Coenzyme transport
                     and metabolism]; COG0352"
                     /db_xref="CDD:440121"
ORIGIN      
        1 masflsyfit dpsyslqqik eaikkhkptf vcyrnkeyfd kneimdfanf akkyskvfin
       61 ldslkddsll ehfegvhips srldeiteyk nkiiiasthn plevqkaqka dyitfspifk
      121 sknrcglgte vlnhicnihp kvialggiis dkeveeiknt kavgfgsiry ffnvlky
//
LOCUS       WP_457562708             287 aa            linear   BCT 27-JAN-2026
DEFINITION  damage-control phosphatase ARMT1 family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562708
VERSION     WP_457562708.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Huang,L., Khusnutdinova,A., Nocek,B., Brown,G., Xu,X., Cui,H.,
            Petit,P., Flick,R., Zallot,R., Balmant,K., Ziemak,M.J.,
            Shanklin,J., de Crecy-Lagard,V., Fiehn,O., Gregory,J.F. 3rd,
            Joachimiak,A., Savchenko,A., Yakunin,A.F. and Hanson,A.D.
  TITLE     A family of metal-dependent phosphatases implicated in metabolite
            damage-control
  JOURNAL   Nat Chem Biol 12 (8), 621-627 (2016)
   PUBMED   27322068
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Perry,J.J., Ballard,G.D., Albert,A.E., Dobrolecki,L.E., Malkas,L.H.
            and Hoelz,D.J.
  TITLE     Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase
            that targets PCNA and is linked to the DNA damage response
  JOURNAL   Cell Rep 10 (8), 1288-1296 (2015)
   PUBMED   25732820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..287
                     /product="damage-control phosphatase ARMT1 family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33053
     Region          2..283
                     /region_name="DUF89"
                     /note="House-cleaning carbohydrate phosphatase, DUF89
                     family [Defense mechanisms]; COG1578"
                     /db_xref="CDD:441186"
ORIGIN      
        1 mhiskecylc iynqvfkite rlnlddekas evlrvgaqil skydltympp viaadvykki
       61 seilgiedlf ekekkeaike alkfkeilek rikkskdplf daakisvagn vidlgvhqey
      121 nlekeiknif emkffkndfk efreklknak tlcyladnag envfdeifik eiklfnpeiq
      181 vfyfvrgkpi indvtlkdle gleiwdlaev vdsgvptpgf cipfankkak difqtsdlvi
      241 skgmgnfecl fgecerevfy fykvkcnvva rasksklgey miykgek
//
LOCUS       WP_457562715             347 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caminibacter
            pacificus].
ACCESSION   WP_457562715
VERSION     WP_457562715.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..347
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37818
     Region          21..344
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkkllalvls vgalfafeya takketvnit rdyvanvysp kqvmvatrlm gyiksmpvee
       61 gdvvkkgqvl fevdpadiys mlnqargavl qaksgvlmae mayadalkdy erfknlykng
      121 avskrdfekm tlmknirkkq vdmakgmlkq aeaglaraea qlkyakvtsp idgvvtmkmk
      181 kvaemalpgy pvvilsdihv lkakstvkes didkfkvgmp vniyvpalkk tfpakvstii
      241 pagdnmthsf vikytfenhq gllpgmyaka kivvgkqeav vvpfsalttr agivgvfvnd
      301 ngvarfvpvk qvgqvgdnia vtgleggeev ilyppanled gqkieeq
//
LOCUS       WP_457562709             790 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457562709
VERSION     WP_457562709.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 790)
  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 790)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   3  (residues 1 to 790)
  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   4  (residues 1 to 790)
  AUTHORS   Borziak,K. and Zhulin,I.B.
  TITLE     FIST: a sensory domain for diverse signal transduction pathways in
            prokaryotes and ubiquitin signaling in eukaryotes
  JOURNAL   Bioinformatics 23 (19), 2518-2521 (2007)
   PUBMED   17855421
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   7  (residues 1 to 790)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   8  (residues 1 to 790)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   9  (residues 1 to 790)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 790)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 790)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 790)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 790)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 790)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18684138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..790
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=91127
     Region          29..357
                     /region_name="FIST"
                     /note="FIST domain protein MJ1623, contains FIST_N and
                     FIST_C domains [Signal transduction mechanisms]; COG3287"
                     /db_xref="CDD:442517"
     Region          <407..786
                     /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 mkqysctfde knikeiyekt kdlnyktllv qvysgvviks yilnvvstvk eyfpnakivg
       61 ittdgeiids kitqnnvvvs fsffeksdie ivffeknnlf edgkklaska kkdtkllmif
      121 asgiefnadd lieginflnp slpvigslag dnakfkktyi fydekiskng vlgvyfnsev
      181 leayidssfg wvkfgrrmki tksdknivye ideqeafdvy syylgneikk yfpkigvefp
      241 liktvnnldv aravvgvrdk alifagalne gdivnfgiae askvlesskr vfqkllrnki
      301 ealfvfscma rrrfveklsf lelqmlknip ntgffgygef fngrflnqtl nvlalseggd
      361 lenkelyipk ndkvttiesl ihlvdvafne vrqklyidnv tklpnkaafd edvlrnpyga
      421 vlfdikkfss indkygevvg devlknlaki lqrfiiknak lyrisadyfi vlffeecnlg
      481 mfaysvieyf ynnplkikik deeyeidldl yaalvegveg rkikikadma lhyakvtken
      541 ivkyskdlki eekinkeiet lnfvkkaime nrvipvfqmi qkddlsfeal vriidedgkl
      601 vspfyfldsi kntryydeit rimieksfki fqdlphklsi nfsyediqne ktveflissi
      661 ekynmqnrvi ievletdsis eydvfenfvk kvkkygveia iddfgsgysn fiylanikpd
      721 yikidgslik sldenekfyk ivktivefak emdirviaef vkdekiyeic kklgidgmqg
      781 yfihipskdi
//
LOCUS       WP_457562718             392 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing response regulator [Caminibacter
            pacificus].
ACCESSION   WP_457562718
VERSION     WP_457562718.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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   3  (residues 1 to 392)
  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   4  (residues 1 to 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 392)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 392)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 392)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 392)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19441278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..392
                     /product="GGDEF domain-containing response regulator"
                     /EC_number="2.7.7.65"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45005
     Region          2..111
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(90..93,95)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
     Region          120..382
                     /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"
     Region          <227..391
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnilivedna myskilinyl skkilfasfs tissfkelkn ncdydlfivd fnlpdasgeq
       61 idflleknks viiisasden eikskyndki vdflkkddss tieylsrlik rlqknkninv
      121 lliedskamr nfqanilkri ninvitasdg eegleklkqn didllitdin lpktngievi
      181 krvrkeksie efpilavssn hdntssralk kgandfitkp fekeefivrv nnllemfesi
      241 kkykkevmtd pltgaynrmy lqtkldslfk iyetksiaml didffkqind tyghqcgdev
      301 lqtfvkviks tirrgdiiir yggeeflifm pnvnkkeali vvtkirialk dydftfsagi
      361 adegetlaem ikiaderlyk akesgrnrvi iq
//
LOCUS       WP_457562719             663 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Caminibacter pacificus].
ACCESSION   WP_457562719
VERSION     WP_457562719.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..663
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75762
     Region          1..615
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mkfldelnda qkeaathidg allilagags gktktittrl ayllslgidp antltltftn
       61 kaanemrera lsllegqnip hppllstfhk fglmflklyi hlinrdnnfv iidsddqrki
      121 ikqissdlpp nfiskeisky knsfltpdev yalatdsvyk nlahiyekyq nyllennlvd
      181 fddlllltyk ilnenndlad eisdkyqyim vdeyqdtnei qllllkklck nhnnicvvgd
      241 ddqsiygfrg anhknildfe kdfnakvikl einyrstnqi lnaannlisf nknrygkkli
      301 sargdgkdie ilrnyneiae aemiakkird linqgvdpke iavlyrinal srsiedglrn
      361 ygipyklvgg mkfyereeik dlisylrllv nphddysfkr vvnkprrgig katiakieea
      421 kgdksfieyi kendlsiisk kaaktlkdfv ntlellskms ldelpenlee ifelsksykd
      481 edkarnieef ygmmrersdl nireflnels letdqdkitm dminvmtiha skglefdhlf
      541 vigmeegffp lndadieeer rlayvaitra rkdltlsyve sryihgkrsp vnksrfltea
      601 glikgervel kessaiktgs lvkhkvfgtg rvlginkagn ktklkidfgg svreilsdfv
      661 ekv
//
LOCUS       WP_457562722             360 aa            linear   BCT 27-JAN-2026
DEFINITION  PilZ domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562722
VERSION     WP_457562722.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..360
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42917
     Region          240..338
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 msknrfyken fsafikdnek ffkaveskft hnflellkkk npnvpitsql kneienlyks
       61 lfledyssqn fklnaifilk ernvdiedil nkvflllana fikytlkekn aiaklkklts
      121 lfefyieyli fhvneeefft yhlpkelkdy yltnkvlnlf nvykgvpith kttiltlned
      181 rgyieveans yqiiaakfqk eiyllepttn ttfkayidyv ypqrkvlklt niekiqrntp
      241 krnyirvqps tdinvkikkh kdifttkmyd islkgmavis dektvdigdf vklefilegy
      301 ffemtaevrs itklndsfrf hfyfeptpsq erilekyitk rekeiikelh kylkaefidv
//
LOCUS       WP_457562725             577 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family oligoendopeptidase [Caminibacter pacificus].
ACCESSION   WP_457562725
VERSION     WP_457562725.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..577
                     /product="M3 family oligoendopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=68320
     Region          43..564
                     /region_name="M3B_PepF"
                     /note="Peptidase family M3B, oligopeptidase F (PepF);
                     cd09610"
                     /db_xref="CDD:341073"
     Site            order(370..371,374,397,490,497,501)
                     /site_type="active"
                     /db_xref="CDD:341073"
ORIGIN      
        1 mmnwdltplf ssiseaeefl kqaefkaief ekkyknrlyt ltpeeflnvl kefeeiweni
       61 graltyiylv fatdstkgnf lgkfqelatk aeehlvwfel efiylpidkq qrfidnagvy
      121 kyylihlqee apyrlsekee kilmkkdlts ssafsrlfde tlsrlrfffe gkkyseeeil
      181 sklyspdrnv rkkaqvsltl glkphqella yiynqvkkdw kidhieirgy dspedprhls
      241 nrvskksvda lvnsvnestt ivadyyeikk rllgydklfd ydryapiklt dktpeisfee
      301 akelvlnafk nfsntfyeia kkafdekwid vypkegkrgg afshsatpka hpyvllnytn
      361 qrrdvftlah elghaihqyl arevgylnqd tplttaetas ifaemllfee ikssldkkel
      421 ietyaakled vfatvfrqiv ftnferkvhk fdelkpedyn kiwmeenrkm fkdsviltdn
      481 ykiwwsyiph fihspfycys yayaqllvft lyklykegfe nfeekyiefl kqggsippkk
      541 qlkelfgldi edenfwekgi aviremlsef kglcddi
//
LOCUS       WP_457562728             574 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562728
VERSION     WP_457562728.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 574)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 574)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 574)
  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 10006830
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..574
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66979
     Region          <82..310
                     /region_name="COG2984"
                     /note="ABC-type uncharacterized transport system,
                     periplasmic component [General function prediction only]"
                     /db_xref="CDD:442223"
ORIGIN      
        1 mrvlfllfla vflfaknvli insysiklpw tkgelegile kinnkqnlki fiefmdtkyf
       61 qptpmrmlny yyylkdkykn infdivittd dnalnfvrky knepifsnak vffagvnnlk
      121 ladtlpknvy agvfekkepl vnlnfakkiv pnlktvyvva dnsnsakavm keyknafkni
      181 ksptliylne knlenileti kkapknsaml lltpfsfsle dshisykyai alisqvfphp
      241 iiihtdllan vpnsnvvggk atdaltqgre agkkvleyls gtpmqkigft fekankmyln
      301 vlnlkkfgid ayalgyknai yvnkprtfye mykewiigsi iiffavlmmi vililkniql
      361 kkynekiskm nkeleekifs alselkekek lllhqtkvsa igemflmvsr kikeklhkll
      421 ekdetkeeat yilnkltmie kyfndssvle fdlkeatkev vyslkdvlne glveikgeni
      481 yifgyknkfq qvildflynm skfqneieki ifefkedkie ihirfkhfsk nlidnfenvl
      541 nnelyytrli mqqyfcsecn yrvdknsvvm eiif
//
LOCUS       WP_457562733             283 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caminibacter pacificus].
ACCESSION   WP_457562733
VERSION     WP_457562733.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32428
     Region          26..268
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkiinqiise iekvikgkke kikiilasff adkhvliedv pgvgkttlak tiakvlglef
       61 krvqfsadml psdivgvnyf dmqkkefvfk kgpifteill adeinratpk aqsalleame
      121 erqvsvdgkt yklsdnffvi atqnpkehgi yplplsqldr fgicislgyp erefeklilk
      181 serieinsfr giekykrkak eiftdekiyd lvldlgkisr difetglstr afitlleisk
      241 ayamiegrdy videdvfeil kyvtphrlee nadkkiirly yqg
//
LOCUS       WP_457562735             211 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457562735
VERSION     WP_457562735.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..211
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24328
     Region          9..207
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnlksfflfk glddkdieev kkftivkklk kdeivfyeke npaylhllve gvarvykvds
       61 kgneliihkf tpvsliaela nlenmpypan camdsegvil kiefekfkkf mkkgdvcfsi
      121 mssllrkmky ldgliqanlv ldtetkiakf iyenpeafed lkqhsiasll nikpetlsrk
      181 lkkfkqlgii envgsklkvk nrelikenft w
//
LOCUS       WP_457562731             810 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457562731
VERSION     WP_457562731.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 810)
  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   3  (residues 1 to 810)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   6  (residues 1 to 810)
  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   7  (residues 1 to 810)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   11 (residues 1 to 810)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   12 (residues 1 to 810)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   13 (residues 1 to 810)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   14 (residues 1 to 810)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   15 (residues 1 to 810)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   16 (residues 1 to 810)
  AUTHORS   Zoraghi,R., Corbin,J.D. and Francis,S.H.
  TITLE     Properties and functions of GAF domains in cyclic nucleotide
            phosphodiesterases and other proteins
  JOURNAL   Mol Pharmacol 65 (2), 267-278 (2004)
   PUBMED   14742667
REFERENCE   17 (residues 1 to 810)
  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   18 (residues 1 to 810)
  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   19 (residues 1 to 810)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   20 (residues 1 to 810)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   21 (residues 1 to 810)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
REFERENCE   22 (residues 1 to 810)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   23 (residues 1 to 810)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
REFERENCE   24 (residues 1 to 810)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   25 (residues 1 to 810)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18594631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..810
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=93739
     Region          <109..>243
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
     Region          273..>381
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          <375..810
                     /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 mdvsilnqit kygfilkqgs kiyankrvie llglrkrnll ndlnkieeik eflnskkgvf
       61 keivtiktki etkhisfyik ktidgfilla ddftkyirek hitdiviymn dvlaksknen
      121 elyekfikav ikkakfnacf vmkkqknalv pvawgndtdg ldcikdatip ldektpllkt
      181 pvakaflegn iffnddtrin pdveplreem lkrnylssvg ipifkgkkve avicickdev
      241 dffkgykkli eyiskalskt fenleeikfk nvllsainkg hewvvitdkn gkivfvnetv
      301 ekitgykkse ligknpkifk sglhdemfyk elwetikkgk ifesviinkk rdgsifylld
      361 kivpvgdyyi slgkditnek kyfhlieelk fkdpitglyn kegffkhard ylkkfkyesh
      421 ivlvvdvynf nvinhkygis egdevlkqlg kklrtvffer dliykfhtsn itlgrfngde
      481 faiflekade ecipkilnkl yeafngtykv knekikldyn agislypkda sdiedllnna
      541 slallnakke gpnivklysk eyskeiykfn dvlnliktsl eknrfelffq pivdaekeni
      601 vaaegllrir kkseiitpgv fidvlensny slnvamkmld nienilkttk dikisynlce
      661 kqfrntqmid klinigkkfp yrlqielier vlineklysq kvleklkdng iliaiddfgt
      721 gysslsyire lpvdiikidi sfirkmmqnh kdmaivktii nlakelgikt vaegvedesq
      781 vailkalgcd yiqgfyyykp mpkeeflkll
//
LOCUS       WP_457562739             320 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562739
VERSION     WP_457562739.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..320
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36622
     Region          2..314
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkalitgatg glgrnlgefl nkknwevigf grnkkignsl gykfkafdls dpdetlkafe
       61 kadvvfhcaa lsspwgkyed ffkhnviatk nvitaikkye ikklihvstp siyfnfsdqr
      121 diketylpkk fvnhyaktky laeqevlnsd idsviirprg ifgeydsvli prlekiaakg
      181 flpvikeknp lvdvtyvgnv vysmylaaik ktpeksvfni tndesmhiye lfemvmktln
      241 kqvkfkkisy nkmmtiaktm effskikitk eplitqygvg liafdqtlci qnaknilnye
      301 pkysikegle ryarskyqtl
//
LOCUS       WP_457562745             130 aa            linear   BCT 27-JAN-2026
DEFINITION  very short patch repair endonuclease [Caminibacter pacificus].
ACCESSION   WP_457562745
VERSION     WP_457562745.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Tsutakawa,S.E. and Morikawa,K.
  TITLE     The structural basis of damaged DNA recognition and endonucleolytic
            cleavage for very short patch repair endonuclease
  JOURNAL   Nucleic Acids Res 29 (18), 3775-3783 (2001)
   PUBMED   11557809
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Tsutakawa,S.E., Jingami,H. and Morikawa,K.
  TITLE     Recognition of a TG mismatch: the crystal structure of very short
            patch repair endonuclease in complex with a DNA duplex
  JOURNAL   Cell 99 (6), 615-623 (1999)
   PUBMED   10612397
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Tsutakawa,S.E., Muto,T., Kawate,T., Jingami,H., Kunishima,N.,
            Ariyoshi,M., Kohda,D., Nakagawa,M. and Morikawa,K.
  TITLE     Crystallographic and functional studies of very short patch repair
            endonuclease
  JOURNAL   Mol Cell 3 (5), 621-628 (1999)
   PUBMED   10360178
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..130
                     /product="very short patch repair endonuclease"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006298 - mismatch repair [Evidence IEA]"
                     /calculated_mol_wt=15667
     Region          3..123
                     /region_name="Vsr"
                     /note="G:T-mismatch repair DNA endonuclease Vsr, very
                     short patch repair protein [Replication, recombination and
                     repair]; COG3727"
                     /db_xref="CDD:442941"
ORIGIN      
        1 mdsktakkik skntkiellm gkalwhkgmr yrkndktifg kpdfvfkkkk iaifcdsefw
       61 hgynylvkge rfktnidfwe kkilrnierd kevneklkkd gwivlrfwgk eiekeletcv
      121 nkikkvyesr
//
LOCUS       WP_457562753             270 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562753
VERSION     WP_457562753.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>270
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
     Region          <87..>270
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnrvvitail vivaaylvfk geyigaigal lplvfvwwpk keqknentld kiqnvvekay
       61 ngeiyhriil dddktkeeki gwhinemldq iedllresqn tikaiiegkd yryilpsglh
      121 gefrnvayef ekaieslkis kkvelianlg krftqidggv penlrriges iykiddsfke
      181 ialkvknssk qadetyyimq eskndfeels qkvmetssei eqmasqissi sdivelikdi
      241 adqtnllaln aaieaarage hgrgfavvad
//
LOCUS       WP_457562754             193 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562754
VERSION     WP_457562754.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..193
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22271
     Region          29..>155
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mneqkiaekl kagkrlskld apkklinkek vlsdndfivs ktdtkgyiiy cnrifvemag
       61 wsrfeligan hniirhpdmp kiafkilwdl iqnkqeffgf vknlrkdgsf ywvfayitpd
      121 ldlngnivsy tsfrkkpprk aievmsdiyr qlveaektgg isasyellkk llnandenvi
      181 dkyqklvfdl qkg
//
LOCUS       WP_457562757             182 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter, partial
            [Caminibacter pacificus].
ACCESSION   WP_457562757
VERSION     WP_457562757.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>182
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          10..>180
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mtreqiykek kkiaifsiiv nltlslikii ggklsgsaal tadgihslsd laasfsvltg
       61 iviankkakd fpmglykven lvalisafai ffagyeiakd vffgepikih nlpialiaiv
      121 ltviityfys rwekkkaiel nspslladae hvksdfftal vvlvgvigqy mgypiiekia
      181 va
//
LOCUS       WP_457562760             283 aa            linear   BCT 27-JAN-2026
DEFINITION  TPM domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562760
VERSION     WP_457562760.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Sirpio,S., Allahverdiyeva,Y., Suorsa,M., Paakkarinen,V.,
            Vainonen,J., Battchikova,N. and Aro,E.M.
  TITLE     TLP18.3, a novel thylakoid lumen protein regulating photosystem II
            repair cycle
  JOURNAL   Biochem J 406 (3), 415-425 (2007)
   PUBMED   17576201
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30592
     Region          1..224
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkviflilf sflfaiefpk ltgrvvdnaq ilspktkqtl ntmlknfeqn tsnqivvvtl
       61 kslqgnsien ygyqlgrhwg igqkgknngv llivapkerk vrievgygle gtltdaksfl
      121 iindiiipyf kkgdydtgvl kgvqaimdti kntfkpekke keeideaipi ggfallflsv
      181 llskyltflk rilpalflgv maflvvyfis qtllyalltg ggifaiialf nlknppppsn
      241 gdiemgeiit dygvftgggs snegggfsgg ggdfggggss gsw
//
LOCUS       WP_457562766             468 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Caminibacter pacificus].
ACCESSION   WP_457562766
VERSION     WP_457562766.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..468
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52282
     Region          19..111
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
     Region          253..348
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 mkklilfllp llllanvsvk vnkkeltkge eliititatg kdikfpqinn idgynvigts
       61 lvsnieving amseslsksy iivpdknlti psfsviidgk vyktkpihii vktpkqtkgd
      121 ytldinlskk nlylgqsail dvklhykppv esiqlqkpqi kgflvqeilk tatdteaeyk
      181 flitplksge ftigplmani gilvkenpfn dpffnlsvss lkyktiysnq ikvkvnpipn
      241 dsvygdfkis lkakniinag epntailkve gcgdfndlpd fkldipntti yaskadtnis
      301 ivdnelcgty tkkftiiadn dytipplklk eyngtlnvis tnpikvkvig akpittpkpp
      361 vtktsikptk qhtennknyy eyaiyliliv lgiglgyfis kitskekkdd ifskikkadq
      421 kelfnllipy sdipeikeil qkleeniykg tnhkinkkei ikiiktkn
//
LOCUS       WP_457562768             352 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoethanolamine transferase, partial [Caminibacter pacificus].
ACCESSION   WP_457562768
VERSION     WP_457562768.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10887874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..352
                     /product="phosphoethanolamine transferase"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009244 - lipopolysaccharide core region
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1900727 - osmoregulated periplasmic glucan
                     biosynthetic process [Evidence IEA]"
     Region          43..312
                     /region_name="LptA"
                     /note="Lipooligosaccharide Phosphoethanolamine Transferase
                     A (LptA) or Lipid A Phosphoethanolamine Transferase;
                     cd16017"
                     /db_xref="CDD:293741"
     Site            order(52,94,191,252..253,268)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293741"
     Site            order(52,94,191,253)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293741"
     Site            order(126,139,267..269)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293741"
ORIGIN      
        1 pnathfsyln tlfaidlwii dnlssqkthk fkpysvkkin ggrpivimim geslnfkrmh
       61 lygwdindtp nldklaktdk nfefvkaisg gintpvsivt ffnvkrepqn idlllsqktn
      121 llklakqngy ktywlsmqee gtsissllny adikktrkdf kekyddalik elkkipfnnk
      181 tfivlhlrad hapyekytpp tfykwnfhtd nntlyrrnsy ydsvlyvdyi isniinymkt
      241 hhknfiiyft sdhaemlgfp eeygkyghsq lvfgdtyvpf iyysdsfhkk lskkyynhyl
      301 iskmlakdlg yeitnpndng tyfvngvkid gsagflhykf knqkiiklkd kd
//
LOCUS       WP_457562778             378 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease, partial [Caminibacter pacificus].
ACCESSION   WP_457562778
VERSION     WP_457562778.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>378
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
     Region          1..378
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mivitlfgif flllllsvpv gvslgfsaii tafifegsda vidlasnlfs qldkyalmai
       61 pmfimagnll skgssakrii efakafvghl pgglpiaaif asiifaavsg sspatvaaig
      121 simfgaitaa gypktyaigt ittagslgil ippsivmiiy gvtaeqsigk lfmagvipgl
      181 ligfmlmavt yigakrlgfk rtkpatwkek wikfkeafwa lmtiviiigg iyggiftpte
      241 aaavsavwal fiaifiykdi klkdlgdvif esaktssmil fiianasmfa yfltlenipd
      301 mltqavvnmh ldkvqfliav niilliagnf mepssiimim vplllpvakm lgidpihfgv
      361 iitinmelgm ltppvgln
//
LOCUS       WP_457562784             277 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caminibacter pacificus].
ACCESSION   WP_457562784
VERSION     WP_457562784.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..277
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31257
     Region          35..271
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkklkpfika afiliafiii fqkiniqelk nikitspfyl flaflsfnls qiisalrvhm
       61 ylknikvtpt fkkqlmlyyv gvfyntllpg giggdaykay kfeksysqgy kkiikallid
      121 risglfavfi lisaliflss fkqfvifsai llivspfily flhkyffvef tksflknlfl
      181 siviqslqal aflfilfaln ihshlidfiv lffissiisv ipisvggvgl reltflygld
      241 mlhlnatigv vaaflffvis vissaigalf ikgvknv
//
LOCUS       WP_457562783             538 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Caminibacter pacificus].
ACCESSION   WP_457562783
VERSION     WP_457562783.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..538
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59985
     Region          1..530
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mvspliivia llfialsfni pfarlkippi igyiftgiii snifsldkht ieivaelgiv
       61 flmfmiglef speklksmkk evfgfgfaem aivsgifglv fywffnidir ialiigsaia
      121 lsstaivlkl lnesreiskp ygrialgill fqdiavipil iaisiivnkd adltqlilkt
      181 lggfaalgvf iyiygkfiap fvishatktk sdeifmatvl lvvlvaaeia hffglsyslg
      241 aflagmilse tkykyqiead lvpfrdlllg iffvsvglmv ninfvihnif sillmtvvfm
      301 lskagiiylm lkffvkhnri aiktafilsq igefafvifa llgkynlves dllqklvvvv
      361 vismiltpfi lryiykiadi fdkevqnfee felkpaevag hiiligydki gqrvarkltr
      421 agipyvaidk qielvkqglk ngdnvifgna ankrvlesln vkdasaviit tlneehthli
      481 tenilainpn lnvivltdde vekefyknhn vyvvdkskel aeklislalr celrkerg
//
LOCUS       WP_457562789             421 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562789
VERSION     WP_457562789.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..421
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48493
     Region          4..420
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mfkfseisdm cikcgkcipg ctihrvnpde atsprgfldi lkgveegdie idknfkdtve
       61 scflcnqcve vcpnslptdf mienarakva ekfgiawykr afffllkhrw aydlvsklgf
      121 yfqtcgfkie eekkairsrf slpmlhkgrl lpafrktsfl kkypekipak npqkrvaifi
      181 gcmanynyte vgdalvkilk fldidifipk kqaccgapay ftgdfkttee likrnieyfe
      241 tfidevdail vpeatctaml kkdyeeyiky hmdnewlkrh eklkakifgt tewlykytdl
      301 ekrlnkklns svtyhdachf gkvfnirkep raliskvvei kemedpnvcc gfggitmqte
      361 kfhlarkegl ikaemikkvd aeyvsaecsa crmqitehld kvgdnkifvh pleiiakaie
      421 g
//
LOCUS       WP_457562795             168 aa            linear   BCT 27-JAN-2026
DEFINITION  macro domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562795
VERSION     WP_457562795.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Rack,J.G., Perina,D. and Ahel,I.
  TITLE     Macrodomains: Structure, Function, Evolution, and Catalytic
            Activities
  JOURNAL   Annu Rev Biochem 85, 431-454 (2016)
   PUBMED   26844395
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Karras,G.I., Kustatscher,G., Buhecha,H.R., Allen,M.D., Pugieux,C.,
            Sait,F., Bycroft,M. and Ladurner,A.G.
  TITLE     The macro domain is an ADP-ribose binding module
  JOURNAL   EMBO J 24 (11), 1911-1920 (2005)
   PUBMED   15902274
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..168
                     /product="macro domain-containing protein"
                     /GO_function="GO:0072570 - ADP-D-ribose binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18661
     Region          4..168
                     /region_name="YmdB"
                     /note="O-acetyl-ADP-ribose deacetylase (regulator of RNase
                     III), contains Macro domain [Translation, ribosomal
                     structure and biogenesis]; COG2110"
                     /db_xref="CDD:441713"
ORIGIN      
        1 mykvvikkgd ifseksadfi vnpsntelil gsgvsgafrk vcgsalqnem rklapikqge
       61 vavtdcpgyp eykkalhvai mdytsnnpsp tlevikkslq niekiiknht pckvvlplmg
      121 vgvggldkee vikiykeffs knvdfncevv iygykdedya llkkyfek
//
LOCUS       WP_457562798             399 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562798
VERSION     WP_457562798.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..399
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44612
     Region          1..394
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 meykvtmpil sdtmdkgkli kwyvkegdrv kkgdklceve sdkatmdies fvngrvkkil
       61 vkegeevpvk sviaviesee skqetkneqe eikktkekns ktntdssidi delinsivne
      121 pstkvsgsas paakqkakkl gidieslqks gelptpahek dideviikky fspkaaklik
      181 eygldfdife lnhkiesdev mkyiktnnip kitklspnqi aviktvqnai kkptffvfee
      241 veitkkenik ltaqiikala tamqkhpltr silkdnellt yptsnisvav arddglfmcv
      301 iknaedksle einewlkeik tkkltiedls gstfgisnlg mfniksftal indndagiaa
      361 fgalnnnkme vsftidhril ngvdaakfin dfkeecknv
//
LOCUS       WP_457562799             432 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562799
VERSION     WP_457562799.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..432
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47311
     Region          1..432
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mydviviggg lgyaaaivls kagkkvalie rnlehlggtc lhngcipskn llhraktlle
       61 lkegffdgev slnlkklqnh iskiitshtk avknqllmak veliedegyv tddgvllknq
      121 nktlqakyii iadgskprip egieydgkri itskealelk napkeitiyg sgaiglemas
      181 ffsaigtkvn llyrhsnisk kfpqiitekl eeqlknigvn lmpnseikea itehskvicn
      241 ingkefstdy llvaagrvpk tdivqtdkik iqkgivtdey fqttmpnvya vgdcngklml
      301 ahaaraqaln vanqilgkke klilenipkf iytlplsyan igtkgvkeae fpinylgiag
      361 slygdelgiv kiyadeenfi tgadilapna eeligifssa laaevdidtl kkavfphpty
      421 seaidralrr fr
//
LOCUS       WP_457562804             310 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Caminibacter pacificus].
ACCESSION   WP_457562804
VERSION     WP_457562804.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181086
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..310
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36308
     Region          72..218
                     /region_name="CE4_DAC_u4_5s"
                     /note="Putative catalytic NodB homology domain of
                     uncharacterized bacterial polysaccharide deacetylases
                     which consist of a 5-stranded beta/alpha barrel; cd10973"
                     /db_xref="CDD:213028"
     Site            order(79..80,134,138,174..176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213028"
ORIGIN      
        1 mkklilfllp lwllaeahif vlhriddfrh pytntsskel ekyfkyiksh nykaitlskl
       61 aemiknrqnv dnivvftidd tyksfykngl pvfkkygipf tlfvyvkatn ekwgdfmtwq
      121 qvkdaakyge lgihsyahph lpnlsnqaii ndtkkaieif kkhmgyvpdm yaypygeydq
      181 rvkkiinsff piianqnpga vdiatpindl drialtgkvd iakklkikrl hadikiqreg
      241 nkitlikgkv fdkipyvniy itkmgwvyki pvkngsfsyt pnfelkkyrn rviirynyki
      301 iskmvikykk
//
LOCUS       WP_457562806             344 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Caminibacter
            pacificus].
ACCESSION   WP_457562806
VERSION     WP_457562806.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..344
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37408
     Region          30..333
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mmsakkyfal iaavtavfia flyfspklfn sytlivlgni yifiilavsy nlingvtgqf
       61 slepngfvai gayvtailml steikeelym laeplplikd vflpnpfltl lisgivsall
      121 altlafpvfr vrgdylaivt lgfgfiirif linnpeisng smgldsipgf asyfwigiac
      181 iltviliynv vyskygramk avrddedaal amgvntfkik tlafmtsaff egvgggllas
      241 sigaispdqf tfmltfqlli iivlgglgsm sgailgtilv lggmellrpl ddanwhlgsi
      301 hgipglrmvi fsllllliml farrgllgdk eiwdyfklkk ngvk
//
LOCUS       WP_457562807             258 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Caminibacter pacificus].
ACCESSION   WP_457562807
VERSION     WP_457562807.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..258
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29509
     Region          49..244
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnsnvlekif flflflllvy iisalylylt qnskvfqrky akeytpkyak klyfttsdgk
       61 rlegaylenk kgaplvlyfs gnannviefi dniavnikdy nflgfnypgy agsegepcee
      121 cilkyaleif dkykpqilig rslgtavaty vaanrdvekl vlitpfdsie hiaqirypil
      181 pislllkhkf kevewiknvk apvsvllvkn ddiipqksid nllkhipnln kkieidgvth
      241 griyeypnis kvieellk
//
LOCUS       WP_457562775             307 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease Z [Caminibacter pacificus].
ACCESSION   WP_457562775
VERSION     WP_457562775.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Redko,Y., Li de la Sierra-Gallay,I. and Condon,C.
  TITLE     When all's zed and done: the structure and function of RNase Z in
            prokaryotes
  JOURNAL   Nat Rev Microbiol 5 (4), 278-286 (2007)
   PUBMED   17363966
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Schiffer,S., Rosch,S. and Marchfelder,A.
  TITLE     Assigning a function to a conserved group of proteins: the tRNA
            3'-processing enzymes
  JOURNAL   EMBO J 21 (11), 2769-2777 (2002)
   PUBMED   12032089
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..307
                     /product="ribonuclease Z"
                     /EC_number="3.1.26.11"
                     /GO_function="GO:0042781 - 3'-tRNA processing
                     endoribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35048
     Region          3..298
                     /region_name="RNaseZ_ZiPD-like_MBL-fold"
                     /note="Ribonuclease Z, E. coli 3' tRNA-processing
                     endonuclease ZiPD and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07717"
                     /db_xref="CDD:293803"
     Site            order(36,61..62,64,66..67,139..140,207,227,266)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293803"
ORIGIN      
        1 mrftflgtsa grptkkrnvs alavefenes gwylfdcgeg tqhqilkagl siyklkaifi
       61 thihgdhcyg lfglitsrml egcteslliy apkgvkemve svvdisfehl gyklefveiy
      121 ggfeeefekf hlkvlplihs vpsyafyisq kpkvklnark lqndglmpgi fyqdikngkd
      181 vevdgkkyia skyldiregk kiiiagdnae pdflakylen tdlliheaty teevfeklet
      241 kylhttaanl akttekfrvk nliathispr fegeeileei kkfyngnafv andfdvfelk
      301 eelrrve
//
LOCUS       WP_457562808             299 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Caminibacter
            pacificus].
ACCESSION   WP_457562808
VERSION     WP_457562808.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..299
                     /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=35269
     Region          7..285
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkakeytktl sillqlinkf yqgenlstsd iekiygvskr taqryinylr eagfniqkkg
       61 kkyyldtiid neketifeai lsiaknagie ekisplltkl kliskenvfy skfdiekidp
      121 qilkkietai kqkkiikmky kmnkrlinme ikpikisnfd gywyvnalnh kneyrtyhik
      181 sihelqvtnq tfdikenilk dvdkavniwf kpkgtpflve liadefatky lqripisktq
      241 kiiknsdets tiyleitdkn eiihkllmwi phlavvspkw lkkevdnyii qyiekfmkl
//
LOCUS       WP_457562811             359 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome ubiquinol oxidase subunit I [Caminibacter pacificus].
ACCESSION   WP_457562811
VERSION     WP_457562811.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..359
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38984
     Region          <1..359
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mtnfwalitq pvaqvkflhv vsagytlasi fvlgisslyl lkgkhvefak ksatvaaafg
       61 lissifvavi gdehayevan tqptkiasae glyvgekgap ivafgipknl katevtsnee
      121 gfafkielpk mlsllgkrnp nafvpglkdl vngneeygiw plsklaavgk eakddllkyh
      181 eakkagdtaa meaakadfyk viwedpkngi kltkadligy gyfanpnidp nliyppvppv
      241 fyafhimvgl gfwfillfll ayvsilkgtf vqnklvqrla visvplpwia tsfgwmtaei
      301 grqpwtvfgv lptaesvtpi alqnvqatff mfltafvilg iaelkilftv vkngpkgah
//
LOCUS       WP_457562816             184 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562816
VERSION     WP_457562816.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>184
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          1..66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          65..160
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mtlgekikff renkglnlse lakkagvaks tlfkieenkt nptintiwai aevlgvpfge
       61 lvgegeikge gvsvvliekt eefesykmnl kenaeyiakp hfagakeriy vlsgeaivgp
      121 vdnpkniksg etiefradkt hiykskissv livtifypek ryfqedvfvd vfdeevyerl
      181 nnli
//
LOCUS       WP_457562818             179 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma carbonic anhydrase family protein [Caminibacter pacificus].
ACCESSION   WP_457562818
VERSION     WP_457562818.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..179
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19630
     Region          1..174
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 milrykddfp kihpsawiap sadiigdvei gedssiwfgc vvrgdvhyik igkrtsiqdl
       61 smihvthykk ekkigdgfpt iigddvtiah rvmlhgckig nacligmsat ildgaeigde
      121 sivgagalvt ggkkfpprsl ilgspakvvr eltdeeveni yknaqnyvky kneyidfir
//
LOCUS       WP_457562820             323 aa            linear   BCT 27-JAN-2026
DEFINITION  glutamate-1-semialdehyde 2,1-aminomutase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562820
VERSION     WP_457562820.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     gene            1..>323
                     /gene="hemL"
     Protein         1..>323
                     /product="glutamate-1-semialdehyde 2,1-aminomutase"
                     /EC_number="5.4.3.8"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042286 - glutamate-1-semialdehyde
                     2,1-aminomutase activity [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
     Region          3..>323
                     /region_name="PRK00062"
                     /note="glutamate-1-semialdehyde 2,1-aminomutase"
                     /db_xref="CDD:234607"
     Site            order(110..112,138..139,141,198,231,233..234,259)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(111..112,138..139,198,231,234,259)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            259
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mgifqeaqqy ivggvnspvr afksvggepp fiergegayi wdiegnkyld yiqswgplif
       61 ghcdkdtqea iieavkkgvs fgaptkveve lakevlelfp hldlirfvns gteatmsair
      121 largytgkdd iikfvgcyhg hsdsllvsag sgaatfgvps spgvpadftk htllaeynni
      181 esvkaafekg dvgcviiepi agnmslvpak kefleelrel cnhygavlil devmsgfras
      241 lrgsfdiygv eadivtfgkv igggmpvgaf agrkeimekl spvgpvyqag tlsgnpvams
      301 aglaqikklk ekpeiykdle dka
//
LOCUS       WP_457562828             428 aa            linear   BCT 27-JAN-2026
DEFINITION  phenylacetate--CoA ligase family protein [Caminibacter pacificus].
ACCESSION   WP_457562828
VERSION     WP_457562828.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 428)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..428
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48410
     Region          1..426
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 miwnevesak rediekiqlk rlkevvsrvy hlspfyrekf eklgitpddi ktlkdirklp
       61 ftkkqdlrdn ypfglftvpm sevvrihsss gttgkptvvg ytkhdmdvwn evmmrtyama
      121 dvtskdvvhn aygyglftgg lgfheaaqkm gativpasgg ftdrqlmlmr dfgatilcct
      181 psfalhlaev arkegpefrr dyklragffg aeptsegmrk evakvwdiey yevyglseii
      241 gpgvscscnk grglhinedh fypeiidpkt gevlpdgeeg elvittltkq alpiiryrtg
      301 ditrlykepc acgrtfvrme svsgraddml iingvnvfps qiehiiaene gvtlnyqiva
      361 dkkgyldkle iivevdenvm qseydsikkr lqhdflnnly inanvilvep gkiersmgka
      421 kriidkrp
//
LOCUS       WP_457562831             347 aa            linear   BCT 27-JAN-2026
DEFINITION  divergent polysaccharide deacetylase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562831
VERSION     WP_457562831.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Aragunde,H., Biarnes,X. and Planas,A.
  TITLE     Substrate Recognition and Specificity of Chitin Deacetylases and
            Related Family 4 Carbohydrate Esterases
  JOURNAL   Int J Mol Sci 19 (2) (2018)
   PUBMED   29385775
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..347
                     /product="divergent polysaccharide deacetylase family
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39651
     Region          <123..341
                     /region_name="YibQ"
                     /note="Uncharacterized conserved protein YibQ, putative
                     polysaccharide deacetylase 2 family [Carbohydrate
                     transport and metabolism]; COG2861"
                     /db_xref="CDD:442108"
ORIGIN      
        1 mkkkkttkkt qpknktvkkt qktsnnlilk sivfvlvlvi lglgaflgkl iyenketkke
       61 laktqinlke lqnkvsvlek elskpkpkak tkpeqttyse ikdyehavkt qppkkkekpk
      121 pivkltkkpk lviiiddvsf knqvkaiksi pfaitpsffp pnkyhpntai yakefkdymv
      181 hvpmeaiswn kpeihtlktt ssyyeiyttm vkikkefpnv kfinnhtgsk ftsdtasmkr
      241 lfkvlqienm gfvdskttph skaafadkyy diplysrnif ldnkedikyi hnqlkkavki
      301 akrrgyaiai ghphkitfqa lksaapilkg vqvvtidqly ksqngkn
//
LOCUS       WP_457562835             321 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-ACP synthase III [Caminibacter pacificus].
ACCESSION   WP_457562835
VERSION     WP_457562835.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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   3  (residues 1 to 321)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..321
                     /product="beta-ketoacyl-ACP synthase III"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0033818 -
                     beta-ketoacyl-acyl-carrier-protein synthase III activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35148
     Region          1..320
                     /region_name="PRK09352"
                     /note="beta-ketoacyl-ACP synthase 3"
                     /db_xref="CDD:236475"
ORIGIN      
        1 myakftsiga yvppkiltne dlekivdtsd ewitkrtgik trhivenevt sdlaykaald
       61 alknakmsae didmiivati tpdyftmpst acvvadklgi arpavdisaa ctgfiyalah
      121 akafiesgmy knvliigaet lskivnwkdr ttcvlfgdga gaaiisaten keeaiididi
      181 nsdgkyqeyl itpgrgvkyg cdtdriwlem kgnetfkvav ktlsqsvrdi lkrnnmtsdd
      241 idwfiphqan yriidavara ikmpseksvl tvhkygntss asipmaindm ykegklkkgd
      301 imlldafggg ftwgsalvpf n
//
LOCUS       WP_457562840             112 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457562840
VERSION     WP_457562840.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..112
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13017
     Region          3..110
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mfkaklefil qmiddiefii nrhgyitksl edregqlail malmqigetl nkidkkflen
       61 ydllndskga ysvrnfiahd yegvklsvie nilryniprl kdkilkiled ni
//
LOCUS       WP_457562847             484 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Caminibacter pacificus].
ACCESSION   WP_457562847
VERSION     WP_457562847.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53784
     Region          67..483
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mdrkalinii kflalvglii eamfsmalit akiynekigy ffeywlgsii lfglililfr
       61 khhmklsike ailsvnlvwi mggvlgaipl mflthvsfvd gffesvsgft ttgatiysdi
      121 sdlpksalml rsvmhwiggm giivlsigll slinptasla lfkseatgit pekitpklkq
      181 tamklwqvyi litildlill kiegmnwfda inhafatist ggfstksesl gywihnpwil
      241 wtttifmlls ginfiahika mkgdfsgfkn eetkwyiglf lvlsvaltlv hyfqsndtlf
      301 fdatnaffti ssiltttgfa tldysqwgha aiaiifmaml lggnagstag gpkiiryivm
      361 fknlkfqikk flfpnaifsv kidkkpismh tinsvgafff lyimtntlit lylyasgydt
      421 mtslsaaiac vgnigpgfgh vgpvdnfaff tdtqkivlai gmiigrleff tvlmllsrdf
      481 wkkf
//
LOCUS       WP_457562853             389 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457562853
VERSION     WP_457562853.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..389
                     /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=44883
     Region          8..380
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnnlrnelfy kfaltvflii affegalmfa fvksfdthlk dklalvaaei npthfnkeal
       61 vdiqhkykvf plfvrlikpm nkqqlknikl gykiqkirin gvrekvlsys aekngyivqi
      121 atlystnddr iniiktisil isfviyliil migykfidai akqiemsfak lkrfnsnvsh
      181 elktplaimk seievalmnn tkdcektlks mlqeinyind itekllfltk etkkikledv
      241 dleelilelf ekyaekiefe ldfgdeeydi kgdktllkma lsniiensik ygankivikl
      301 eknkhkiilt ikdngigipk eklpfifdef yrvdeshnkk ikgfglglsi vkniltlhka
      361 kikvnsdegk gvefiiefpl ithqekksa
//
LOCUS       WP_457562849             541 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457562849
VERSION     WP_457562849.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..541
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58897
     Region          30..399
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mhlistyalg hlvgylpqdt lkllsnytnh ttlnpfmllv vitiggllsg llvyifapea
       61 eghgtdtvir afhrnggylr pivvpikila saitigtgga agregptalf sagigsmyan
      121 frkvgikkrq vfvligmasg lsavfkaplg tsifaievly tnnefetrel iyilfgpfia
      181 ytitgflfgw qpifsvpdie vtqistyfki aflgvvsgii gfilpntfyg vrdlfrkipi
      241 lphfkpalga fvvgliaiyf pqvlgggygf iqesingnlv gvillsllia kilafsftvg
      301 sggsggvfap slyigamlga fmayvfkess avfavigmaa vfgaaartpl stivmvaemt
      361 ggysllapat lgvlsaffvh diliktlkpk yvslyeaqll skdyspiyqv ekireiltch
      421 skmlnlekav ldredlldll ergeeveigg gkyiffgtft kkvklqegey fkkyknvdvi
      481 yvfrngkwlp gfvvnsileg devllvgskd aidrikdefv pisqtfsklr vqheeieglk
      541 n
//
LOCUS       WP_457562855             413 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Caminibacter pacificus].
ACCESSION   WP_457562855
VERSION     WP_457562855.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..413
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=48301
     Region          3..369
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mkihldldsf fvsahrvfdk sllnkpvvvv krndkeifen hksevlnlnr gaftgdlivs
       61 kkeydksyfl engkirgivv tasyearelg iktgttlkea leiypkltvl lpdyklyhtl
      121 syklkeflkv kipfveqfsi deffgdlegw vddrdaflfc kdlkdeiwek fslpisigia
      181 kskwtaklat sfakpngvfm veevdefikd ipiekfpgig rriekrlker giltlgdvke
      241 nreyfyswgk pgvelykrvc gidneevker evrksigisr rfdvvydrre lvrrvhvlcr
      301 ylsflvlkyk lnptfyylki kykdktsska hvrihrlfne lllkeimttl fyradekemg
      361 vislslavsk fkresnlfdy ekdlklqnln eaifkirskf gvsalmsaee ihp
//
LOCUS       WP_457562856             207 aa            linear   BCT 27-JAN-2026
DEFINITION  LexA family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457562856
VERSION     WP_457562856.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Giese,K.C., Michalowski,C.B. and Little,J.W.
  TITLE     RecA-dependent cleavage of LexA dimers
  JOURNAL   J Mol Biol 377 (1), 148-161 (2008)
   PUBMED   18234215
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Erill,I., Campoy,S. and Barbe,J.
  TITLE     Aeons of distress: an evolutionary perspective on the bacterial SOS
            response
  JOURNAL   FEMS Microbiol Rev 31 (6), 637-656 (2007)
   PUBMED   17883408
REFERENCE   3  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11715193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..207
                     /product="LexA family transcriptional regulator"
                     /EC_number="3.4.21.88"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23284
     Region          6..72
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cl22854"
                     /db_xref="CDD:473980"
     Region          91..204
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mnfekvieki kdiisqeign kkvlnkdvak algitpehls ilkkrnkipy eeiayfcakr
       61 kisinwllfd qdietianet ekfsqiryfk dinasaggga infdegyeil yidkriidkn
      121 ldainvigds meptikdgsi ifidrndkni rnggifvvnt nagvfvkrvn lkssgeieli
      181 sdnkaypset ikpneveivg rvvkifs
//
LOCUS       WP_457562859             459 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter substrate-binding domain-containing diguanylate cyclase
            [Caminibacter pacificus].
ACCESSION   WP_457562859
VERSION     WP_457562859.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   8  (residues 1 to 459)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10098929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..459
                     /product="transporter substrate-binding domain-containing
                     diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52682
     Region          37..248
                     /region_name="PBP2_BvgS_HisK_like"
                     /note="The type 2 periplasmic ligand-binding protein
                     domain of the sensor-kinase BvgS and histidine kinase
                     receptors, and related proteins; cd01007"
                     /db_xref="CDD:270228"
     Region          <282..456
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkviwsivia vvslfaqvdl tpkeklfikn hlfhcvvtpn wapfnmlkdd kiegiaidyw
       61 klikhklnlk snckilpswt lvlediknkn sdivpatakt pdkqnfalft kpyatypivi
      121 atrnnigfin smaqlenrki vvgknysaae ilkkhfpnln iievkdikta ldyvsrgkaf
      181 aaidnlpvia yninkyqfan lkisgkapfd fkvrfmvrnd ypllvsaink aidsitpeek
      241 erifkkwvyv vyqtgidtkk lltiafiaig lililialvi yqffeikkrr kfetqlikta
      301 tidsltgifn rkhidymlqk eveeakryan slsiifcdid hfkdindkfg hkvgdivlee
      361 lakimkqnir ksdiigrwgg eefliilpht plnealrvae klqsairnye fpkigkitcs
      421 fgvtefksed siyrlmirvd qalyeakntg rdkivvkkd
//
LOCUS       WP_457562875             253 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562875
VERSION     WP_457562875.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  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 11459733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28489
     Region          109..253
                     /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 mknddllnin pkkdmkkpli yaaigflifi iiviavaifq nmssgknnei lppqpkteke
       61 ikpqeefkpl pietanenta nqnanqnenq nvnentqnna ntntnaqtpa atqtnttqnn
      121 tqtqkpkpqi tqepvknvkp qakeqktqki tkkpvkvtkp avttkpkkva ygkyyvqvaa
      181 llrnakpnkk flallkkygf nykyihtyiv kngekikvtk ilvgpyktrs dakralakik
      241 revtqnafiy kak
//
LOCUS       WP_457562888             365 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562888
VERSION     WP_457562888.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..365
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42993
     Region          53..360
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mklyiaigvv vlnllylfft knlkyfffkk rkniflrlly srvykigipf lliidvntff
       61 ylfddrfpns nvkfflnlfl iswlfyevlk yiiytaitik vskkenvrre lfslvinltk
      121 vlivivifva vlshlgvnit aiitslgigg viiglaaket ignffdsirl vsedafhvgd
      181 wietkdfegf vteigltatq irtfdngliv ipnsklanew vknwsrrmig rrikfwlkik
      241 yttdtdelrr vvneirvmlq khpfivtddk iksrlrkkmq knalfsiedk ygvrktllvy
      301 vdkfdeysid iliyafsitv dweewlrvkq dvmlkvldii knsklelayp tnvifyderk
      361 nlwkn
//
LOCUS       WP_457562885             179 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562885
VERSION     WP_457562885.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..179
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=20721
     Region          110..179
                     /region_name="DjlA"
                     /note="DnaJ domain-containing protein [Posttranslational
                     modification, protein turnover, chaperones]; COG1076"
                     /db_xref="CDD:440694"
ORIGIN      
        1 mhflhsinse tlntilligg giivffiflk sllssgssnn yskngyyyyq rrgysyeetn
       61 rkkdndysyy gydknyssgn ynynqnsnns ynnssnnnss nnskkeyqsf tsknpyqvlg
      121 cketdstdti kkaykklika fhpdiiagyn lhedfitfak irtqqinday nkirklrgf
//
LOCUS       WP_457562894             141 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator, partial [Caminibacter pacificus].
ACCESSION   WP_457562894
VERSION     WP_457562894.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..141
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
     Region          <2..138
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 dtffwilkii gaiyliylgv khmisghkef hlsqtnehir nynpkkvfik gflvaatnpk
       61 pilfftaifp lflstnhpvv lqffimtftf maisfvslmt ygliskhaka wffdekslew
      121 fykisgavfv lmgigmlfik k
//
LOCUS       WP_457562895             196 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Caminibacter pacificus].
ACCESSION   WP_457562895
VERSION     WP_457562895.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21840
     Region          4..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfwfiplvif lavaifspgp nnviamsvgf nngfkrviph llavvvgfsi mlfvvgigik
       61 elilkyqsaf evmkylcsfy llylaykiat skpnlntnea kpitfkesll fqvinpkswi
      121 aalsivtiyl pkdnflaalf itiiisdili ilaisawavl gksfnkifks ekttkifnfs
      181 maillvvsvl milfve
//
LOCUS       WP_457562896             298 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562896
VERSION     WP_457562896.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..298
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34269
     Region          39..296
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mifedisele kivenndiqk alslikppkk fplaktkkrs almvsahqvk hlnkidslpa
       61 diimlnledg vpkdkkeiar vmigvflsri ekidkeivir vnaldeggkk dieflekfnf
      121 nafripkvrs iediddvfmk tekeihasie tkeaffnlke lkhpklttfy igiydllnel
      181 kishsvidln nplihrilsd ftltarylni tpigfvyqqy kdlegfknwc llqknlgmqg
      241 vgcitpaqce iankifdedl efakmivkrf esegpftidg lfvdepiykn ylqmldns
//
LOCUS       WP_457562898             407 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562898
VERSION     WP_457562898.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Draper,J., Karplus,K. and Ottemann,K.M.
  TITLE     Identification of a chemoreceptor zinc-binding domain common to
            cytoplasmic bacterial chemoreceptors
  JOURNAL   J Bacteriol 193 (17), 4338-4345 (2011)
   PUBMED   21725005
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>407
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <59..336
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          366..>407
                     /region_name="CZB"
                     /note="Chemoreceptor zinc-binding domain; pfam13682"
                     /db_xref="CDD:433401"
ORIGIN      
        1 mnskiigtit allflivagy ggfkgdfvtl glgvlgilas aalffqksqt tsstksslik
       61 kisktieras egdfneritn idpndplnsl awdvnnlldq leaferdike sisaakqgid
      121 yrdispqgyk grfratveiv neaiqaista lkeqarself itlndlgggv kteiqeikks
      181 fdeklrefmm kidelsteif egadesaqki enlatvlnel idfiahtnea inmlsqraee
      241 igkivelitd iadqtnllal naaieaarag ehgrgfavva deirklaert qkatseisit
      301 iktlqqetsd iqansekits mattsredvd nvnemiigfr dkslenkknv dyaltrmfid
      361 laklshlvyk lnafeavvee keipqskdne cefgkwlrne etikrig
//
LOCUS       WP_457562899             536 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457562899
VERSION     WP_457562899.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 536)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..536
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61701
     Region          <349..536
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkkkiliiia iimiistiir tfivgasfln ysnsliknqt nlivdilrev idkdkflhii
       61 qnshpikkie fikgrkneli ysfkdktiis ivpfnelesl kivfsaknyf dkllmaiaql
      121 ilialislii iillvnhflk pyleilekie estnnilkgn fnnkielklk geakdfvnsy
      181 nyflqklkes fgvieekytt liekeksndp lndaketieq lanifkfkri ieedssyeti
      241 lerlidvike fgikhfaiig iennekiakl ihsesdiccn vlenykncra yrlkkeinsl
      301 kmkkeclshy cdtnhiclpf sstgnftgil kiiftdeeke hvlkvlpyik aylneistii
      361 eskytlellh nqnikdpltr lynrryldni lptliegakr rngklgfiml dmdhfkqvnd
      421 tyghdagdrv leklaeiivn sirksdiavr lggeefliia tnvkdkedlr kiaekirlsv
      481 kaqqfylssg lvinktisig aamfpddced gnecikladk alyeaknsgr drvviy
//
LOCUS       WP_457562905             318 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457562905
VERSION     WP_457562905.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..318
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35901
     Region          114..315
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mresifknkk tglilallfy iglgyflyqa askinytwkw dmipkyfvyh qkepitspcd
       61 gkleikgdka ivicenkkiy tfnikgykle fkngdylyed deiayksvlk pgpflmglwv
      121 tikisiismv iafiigliia imrlsgipal dyigsvyvtv irgtpllvql fifyfivati
      181 fnlprfwagv mslsifygay iaeilrgaiq avdkgqheaa kslgfnawqr myyiilpqal
      241 rkalpalvge lislikdssl vsiisitdlt kvgreivant fspfetwltv aalylmltsi
      301 lsfighklek rmkvkggf
//
LOCUS       WP_457562906             276 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caminibacter pacificus].
ACCESSION   WP_457562906
VERSION     WP_457562906.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..276
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31233
     Region          6..274
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mlrkyadfll vlvalswgst filvkkaied lpafsflfvr fflafllmyv lfhkkieidk
       61 kilkaslilg flnfsayalq tvslyylpsn ivafltglfv iftpvsaylf fkkeipkkvi
      121 iaailaflgi yfltqakfaf siyvflvilc affyalhinf tdifskkyni fslvtfqflf
      181 vaifslflip fedlhnikis ftvvfaiiit vvfatvfaff vqtfaqqftt ptktaiifal
      241 epvsaaflga ffgeslnikq iiggilvvis miiaei
//
LOCUS       WP_457562908             100 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caminibacter pacificus].
ACCESSION   WP_457562908
VERSION     WP_457562908.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 100)
  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 100)
  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 12168893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..100
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          38..>78
                     /region_name="TPR_19"
                     /note="Tetratricopeptide repeat; pfam14559"
                     /db_xref="CDD:434038"
     Region          52..79
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 tiyttlfekp didmnskded ilqntiknfs ppaneakisi ltnllskypq savikydlav
       61 fltstgryqe akslleslkt tdsdiisake klltylqntf
//
LOCUS       WP_457562910             356 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Caminibacter pacificus].
ACCESSION   WP_457562910
VERSION     WP_457562910.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /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=40982
     Region          1..257
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mkilhtsdlh ighsvsgidr geeyerffew fegvanekkp dcvivagdvf dvyfpsneai
       61 rqyydfllsl rdkakkviii ggnhdsfktl kapkeilkyl dvvvvsgsed dfcefvefdd
      121 fvvvavsylr egilkkyddd iekaifklyq eklkeakekf pgkklvttah fsvsgaslgd
      181 serdiyvgnl efvskdvfeg ydyvalghih kpqkitenii ysgsplalsf ketyqknivf
      241 ieddniefin vpkfrefasi kgsfkevyek isemkdafle ivldeivdse klkllkngen
      301 hivkitlpyv keiknfevkk vtpediikei fdekeiieaf yeikkevede fgkved
//
LOCUS       WP_457562919            1160 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457562919
VERSION     WP_457562919.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 1160)
  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 1160)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1160
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..1160
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=136950
     Region          <8..651
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          268..519
                     /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          357..385
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          421..451
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          489..517
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          556..584
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(557,560..561,564..565,567,591,594..595,598..599,
                     601..602,624,627..628,631..632,635)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          589..618
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          623..650
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkktvlalla fsflfsqeiq vdyqalqksv eqnpqdvknr lvlasyylkt lqvkkakkll
       61 seilkidpnn kkakellynl kllknateyk kffstpnqyi sslydkndyk nlmsffeyyt
      121 rlngykklsd dsifkaarvf mwegkyqksl nalkhaknke sldyyeiiay dlyylgdpka
      181 ekylkilyns tgnieyaktl ldlylinrdi pnakklllsl shatknkkli ekykkkiaqi
      241 eseyindlyq eykenptfnn lkrlvlglyd tdkekaysll qeyiknnpad nqakiffaqi
      301 ltwdgdtnha lkylkefqnn leaklligki lawqgnydka aiylsdvydh gnpeekyeal
      361 kmlgfiamwk ndnlkakeif krllkqnpnd eevkealmil ngnikpviak yekllkrepd
      421 naeyilklad lyymdknyqk sayyyekylk yhpekievyk tlgdiylelk nyykgfgdwe
      481 yyanykntke aylelaqryy wngfnkealk vldellkqyp dfkeaailka kilkinprfv
      541 dsssaatide yynnraqkll vygdrayfnn lfatakdyyh eylsinpdny dvrekyaytl
      601 ektgdyanaa geffllmwgk ktplieyhya ynlqksgklq eakkiykkll ntlpkplpan
      661 ieqflqnwkk awesmdfnky akfydkkisn nvywrlrken ifknagfisv giynpllikk
      721 egdtyvvkfy qvyasqkrkd kgyktlwikc kndkckiike kwqageytpy npnnsiekyi
      781 renlneikqs qtpkleivpt ikpettkknt qqpkininin qtieekkeen kvlnenlqsl
      841 innnskivla pdvkkdllpv nevlnisqlk vvkltpktit iseykqkilp wqikmdydyf
      901 hdnknttmht igakiyknnh lysifalfkw yhlkengkkt aslagigykn lkysidvfyd
      961 kstkksigfd fetkindynl finkhnmvys trtvcstnht kikaeltkft qldylrglww
     1021 slayervdds nniftpqidy dfygfnkkty tgtfyfsgwy qfnskstdcy yspkksdtni
     1081 igikldknin khftghiqgg igysfwdkty lyslkghikt anyksffskl gcevsnssts
     1141 svtkkgyqsi eciweidkqw
//
LOCUS       WP_457562892             528 aa            linear   BCT 27-JAN-2026
DEFINITION  single-stranded-DNA-specific exonuclease RecJ [Caminibacter
            pacificus].
ACCESSION   WP_457562892
VERSION     WP_457562892.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Cheng,K., Xu,H., Chen,X., Wang,L., Tian,B., Zhao,Y. and Hua,Y.
  TITLE     Structural basis for DNA 5 -end resection by RecJ
  JOURNAL   Elife 5, e14294 (2016)
   PUBMED   27058167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Lovett,S.T. and Kolodner,R.D.
  TITLE     Identification and purification of a single-stranded-DNA-specific
            exonuclease encoded by the recJ gene of Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2627-2631 (1989)
   PUBMED   2649886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..528
                     /product="single-stranded-DNA-specific exonuclease RecJ"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=60106
     Region          7..503
                     /region_name="RecJ"
                     /note="ssDNA-specific exonuclease RecJ, DHH superfamily,
                     may be involved in archaeal DNA replication intiation
                     [Replication, recombination and repair]; COG0608"
                     /db_xref="CDD:440373"
ORIGIN      
        1 mltkqkikei lssrieeids lsiphfllls diekaakris qaiknqekiv vvgdydvdgv
       61 sssaivklff ekigypieiv ipnrfihgyg lslnileeiq adliitvdng issfeaaeec
      121 kkrgidliit dhhtplimdn gqlkmdngqc mvaneknykl pdalaivnpk tspdfpfkei
      181 cgaevawylc aalkhemklk idlrefvdil aiaiiadvmp lnhmnrllvs mglkrlnkar
      241 kpfskalkrf fnrefnaedi afqiaprlna agrmdsanla ykfliskdee eafrlfleld
      301 alnnqrkete keilesieve endkfivvsg dyhegvvgii asrlvhkykk paivfcdnge
      361 hlkgsgrslg nidifklvse csddilgfgg hklacglsik kenfyklkek lntiieiydd
      421 ddffiedfvl gelpfreidf elldilksfe pygegnpkpk fiasakimhi qnlkdnhykl
      481 ilsqddyilp giifrydgef devvrfkfti gennyfgrei qlmieefl
//
LOCUS       WP_457562922             210 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457562922
VERSION     WP_457562922.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 210)
  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 210)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..210
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24213
     Region          1..200
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkialiedei hlneaiklll elesfnvesf knireflres dnnydiiiad itlpdgnflq
       61 elskhkkige etkiiimsah geldnikkaf dlgaedfikk pfepeeiilr vkklfktkkt
      121 klteniyydp esktiltpns keiltkkeam llellikhrg rfvsfdtiaa tiwdepvssn
      181 tiaalikrlr qkiknknlit skreigymlv
//
LOCUS       WP_457562924             567 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457562924
VERSION     WP_457562924.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..567
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65592
     Region          <307..554
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mvenikeflk npkkskiyki lniskeevev lkhmlemyie gqedvkvrni lqkiysddkl
       61 eafehigtik nlieegwvvv ssfgakspel salelfnanv slsvaflkll engdlelvip
      121 qktpykdhle ylhdqflrid iyeqlanlkn sfsnetasik rlqsklklie stikervkkt
      181 qidlpvlnfm iendfnekee iiflallkee ytggsenare lnrlldlisa deieriknrs
      241 lldensklvs egiidydelf gafggytkiy fisedilnel ihprrkhkle hlvkdtifdl
      301 vepknsledv vlpkstmemv krvlkqidkr vvnllkkwgi kqnndldaki ifyghpgtgk
      361 tltahaiake lnkpvlslds skilsmyvge seknvrrlfd eyyeiseklk tkpvlllnea
      421 dqflstrttt afssadkmhn qmqnifleql ekfegvliat tnlletidsa fsrrfdykik
      481 fekptfkerv klwqkklpkn adfeedfdvk elakydltga qieliiknta lkvamkkkpv
      541 fklkdfieei ksekksafds ekevgfv
//
LOCUS       WP_457562932             314 aa            linear   BCT 27-JAN-2026
DEFINITION  arsenate reductase ArsC [Caminibacter pacificus].
ACCESSION   WP_457562932
VERSION     WP_457562932.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..314
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=36002
     Region          3..127
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(8,10..15,103,105)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mkkvlilctg nscrsimaeg linkflegie aksagskpsg kvnsnaikal kkmgawcddy
       61 hsksitdlkn eefdlaitvc dnareacpfy pnakktihip fedpdgkdfs afeetieemq
      121 krliprvike lsfednflin kikgdlaeni crvhfenmgy dvskvgveni ssvfahlngy
      181 eknyieklkl lfqrmpdlli thnekkeaal fevkynknln tqddlknfsk ylherydyhi
      241 ntlklpvyfy vvtnkkpyvy vlkanhtngn tggfypadss wldkfpifsk enakksfrev
      301 yfsviypals dife
//
LOCUS       WP_457562940             163 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidylglycerophosphatase A family protein [Caminibacter
            pacificus].
ACCESSION   WP_457562940
VERSION     WP_457562940.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Kumaran,D., Bonanno,J.B., Burley,S.K. and Swaminathan,S.
  TITLE     Crystal structure of phosphatidylglycerophosphatase (PGPase), a
            putative membrane-bound lipid phosphatase, reveals a novel
            binuclear metal binding site and two 'proton wires'
  JOURNAL   Proteins 64 (4), 851-862 (2006)
   PUBMED   16838328
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Chang,Y.Y. and Kennedy,E.P.
  TITLE     Phosphatidyl glycerophosphate phosphatase
  JOURNAL   J Lipid Res 8 (5), 456-462 (1967)
   PUBMED   4292860
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10731865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..163
                     /product="phosphatidylglycerophosphatase A family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17723
     Region          1..154
                     /region_name="PgpA"
                     /note="Phosphatidylglycerophosphatase A [Lipid transport
                     and metabolism]; COG1267"
                     /db_xref="CDD:440878"
ORIGIN      
        1 mnklnwfllt gfysgllpka pgtwgsivgv iiaylviiym pnpnmtimll aalfsiigfk
       61 lvneyeangg ihddkrivid eiagvlitig vlgdlkhdtf iklilafisf rlfdiwkpsi
      121 igkidqkakg glgvmgddil agifggifag ilymgylklk tmi
//
LOCUS       WP_457562947             584 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide biosynthesis protein [Caminibacter pacificus].
ACCESSION   WP_457562947
VERSION     WP_457562947.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..584
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=67141
     Region          109..223
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          268..542
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(272,274..277,297..298,319..321,342..344,346,361,384,
                     400,422..425,428..429)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(298,300,304,308,317..320,323,326,344..347,350,354,
                     357,360,429..430,435)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(346,386..388,396,423..424,430..432,435..436,
                     447..449,453,455,490,514,517)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(362,386,396,400)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mnfiknvifs knilnflvii vltfitfawt flifhkpfdi kivlvvivar iissififkd
       61 ysmswrqatp ksfliksavn ivafciympf fynkiyiyff vselffylfl inflmfsysl
      121 ylnkskkhkt ktliiygssk agqkladefk dseykllyfv ddsiktknks idgigviste
      181 klkkvlknka dllviavske ekenlknlyn slefaakkiq ilptyeeiln sekysnflkd
      241 vtiedllark pkdldkkvir eflenktvli tgaggsigse icrqcelngv kklilvdnce
      301 ynlyrideem tinrkcylvd vskkedieiv fqkekpqivi haaaykhvpl ceenpksavi
      361 nniigtknvi dlsikhnaen filistdkav rptnimgatk rvceiyaqnv pskntkisav
      421 rfgnvldssg svvpkfrkli kqnkpltvth peitryfmli peacqlvlqa gslakngeif
      481 ildmgepvki vdlakkmlkl ygkdennivf tglrpgekly eelllneadk ktrfesifva
      541 kpihfdfnel nkhieklinl ydkddiikal kdivkefnhn dlke
//
LOCUS       WP_457562948             198 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Caminibacter pacificus].
ACCESSION   WP_457562948
VERSION     WP_457562948.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Miyake,K. and Iijima,S.
  TITLE     Bacterial capsular polysaccharide and sugar transferases
  JOURNAL   Adv Biochem Eng Biotechnol 90, 89-111 (2004)
   PUBMED   15453186
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..198
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23213
     Region          7..198
                     /region_name="Bac_transf"
                     /note="Bacterial sugar transferase; pfam02397"
                     /db_xref="CDD:460547"
ORIGIN      
        1 myekfgkrvf diifsslgli iffplmvlia iaikissqgs iffkqkrvgk nfkefeiykf
       61 rtmvenaekn gpsvtvdgde ritkigkflr ktkldelpql fnvlkgdmsl vgprpevmky
      121 vnekkedykr ilkirpgitd yaaiefrnee eilkkyddle kayieiiqpk kielyykyle
      181 nmsflediki ilktlkvi
//
LOCUS       WP_457562949             377 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457562949
VERSION     WP_457562949.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..377
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42837
     Region          2..374
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnipfhktpv tqeeinavin vmksgwltmg pttiefekkf kefigskeav svnsataalh
       61 lalkaigike gdevivptnt fvataevvty fnavpvlcdi eetthninvn kieslitdkt
      121 kaiipvhfag qpcdmdeiye iakeynlkii edaahalpst ykgqkigslk ntditcfsfy
      181 atktlavgeg gmattdneky akhmrinrlh giskdawdry tdkgswyyev vdngnkyntt
      241 diasaiglvq lkrqyellek rksiakkynq afennekiqp lrikkdrtts whlyvikvpn
      301 rdfvinelkr rgvncsvhfi pvhkhpyykt rynlndknye iannvfkksv slpiypdmsd
      361 neidyvienv levlknv
//
LOCUS       WP_457562950             404 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caminibacter pacificus].
ACCESSION   WP_457562950
VERSION     WP_457562950.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 404)
  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 404)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..404
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46781
     Region          5..400
                     /region_name="GT4_WbuB-like"
                     /note="Escherichia coli WbuB and similar proteins;
                     cd03794"
                     /db_xref="CDD:340825"
ORIGIN      
        1 mskiiwiind yagsayhgme frnyyfakew vkrgyevyii sasymhlfkk lpetngvftf
       61 ekidginyvw tkvinygksd nkkrvfkwfe fagklfflpf skmkkpdvii aspmapflvv
      121 payklakkfn akfiyevkdi wplsiielgn ispkhpliki mswcekfavk nadfivsslq
      181 nydehlkedl nierdfvwin ngisleemqk ieplpkqied iipknkfiig yagtvgiana
      241 ldsfleaaqm lkynnkiffl ivgdgreken ltkkygylkn vlfippvkks qvqsllnkfd
      301 vcyiglqnqn lfkygvspnk lfdymysakp iiyainsgkn nivklancgi sveaensegi
      361 kkaiinlynm seddrkklga ngkryvlenf tyeklaqkye rlfq
//
LOCUS       WP_457562952             463 aa            linear   BCT 27-JAN-2026
DEFINITION  L-aspartate oxidase, partial [Caminibacter pacificus].
ACCESSION   WP_457562952
VERSION     WP_457562952.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..463
                     /product="L-aspartate oxidase"
                     /EC_number="1.4.3.16"
                     /GO_function="GO:0008734 - L-aspartate oxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0009435 - NAD+ biosynthetic process
                     [Evidence IEA]"
     Region          17..460
                     /region_name="NadB"
                     /note="Aspartate oxidase [Coenzyme transport and
                     metabolism]; COG0029"
                     /db_xref="CDD:439800"
ORIGIN      
        1 aaiwsakfln dagfttlmit knqvwdcnsf yaqggvtman dkndvplhie dtlkagsfhn
       61 kkeaveilsk asvklkqell eygfrfdpgv tregahsvsr vyhkggdatg reihkfllqk
      121 dksylldeai vfdiliedgv aygvsvlhks kkyniyannv iiasggvgal ykydtnarti
      181 sgdmqglave kgivlkdmem tqfhptvfie mkfsqklllt ealrgegahv idekgrrflf
      241 dydergelag rdivsraifm hqqkghkvfl dvsmfdeeff kkrfptiytk lrdydinvpy
      301 epipispafh ymmggievdl nskvkgfenl yavgevaytg vhganrlasn sllecfifak
      361 kaakeiiekk fstkeknfei nseelfkndd klyknllreq mwrnvgiird ekglkealsf
      421 ieetipklgr iaklrfltak eivkaalnrk eslgahyrkd ena
//
LOCUS       WP_457562938             395 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Caminibacter pacificus].
ACCESSION   WP_457562938
VERSION     WP_457562938.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 395)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43709
     Region          27..387
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mndfkfnenl ykavdfitke kfekvilpqe lpkkglgent lkimaskvlg eatyldsplv
       61 fahmdpptpw iawamalwna rlnqnllhke lspfatqaee svidwikdff gmdgghmcsg
      121 ssianltalw vardtknidt ivasesshis iekaakilnm rlikvpinnd gsidkksvpn
      181 lknaclvlna gttcsgaidd fsligqakwt hidaayagal kftseysnil ngieradsis
      241 lsahkwlyqp kdsaivmfkd nkkakevmsf gsdylssani giqgskgana vvllatllyf
      301 gkegidrlia nslknallfy dklkeieqie vfnkpicgit lfrpknmavn eflsklpkgm
      361 fskckikdke fvrsvalnpm adideivkfv nnvlk
//
LOCUS       WP_457562929             118 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457562929
VERSION     WP_457562929.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 118)
  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 118)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..118
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13072
     Region          3..>118
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mnrkilvved ekllndtist fltysdfdvv safdglsave makkhnpdli lldvmlpcml
       61 gydvakairk fssvpilflt siedkeskqk afeagatdyl sksidlsvlv ekinqilk
//
LOCUS       WP_457562941             436 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457562941
VERSION     WP_457562941.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..436
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47044
     Region          3..416
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 makkafntls tatlgigtmv gvgifivigl agsiagnlvw isfviggiia llsgyslakl
       61 airfpsrggi ieylvqefge npfsgslsvm fyfaqlvtla avaksfgeyg arlfgyhstf
      121 midafavgii lfftfinllg atlvakseni ivaiklialt iftiaalmti kpqylsmkda
      181 ppiinavfai gltffayqgy svitnaiedm enpsktvlka mfiaigvvti lyvsvsiavl
      241 gnlplsevik akdyalaeaa kpvfgelgfk imsvvalisa tsainatiya ateisytlak
      301 kgelpkiyey nvfhsyegll istaliipmv lffnlseitt vaalsvliiq alvhfghikl
      361 tpktgankgv iifafllmtf vvlatlyyna kqdikiiyyl iggfviayii eiilrklfnr
      421 tvkkqikglt gelfqh
//
LOCUS       WP_457562918             384 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457562918
VERSION     WP_457562918.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 384)
  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 384)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 384)
  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 384)
  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 11440297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..384
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44060
     Region          2..334
                     /region_name="BcsA"
                     /note="Glycosyltransferase, catalytic subunit of cellulose
                     synthase and poly-beta-1,6-N-acetylglucosamine synthase
                     [Cell motility]; COG1215"
                     /db_xref="CDD:440828"
     Region          34..211
                     /region_name="CESA_like"
                     /note="CESA_like is the cellulose synthase superfamily;
                     cd06423"
                     /db_xref="CDD:133045"
     Site            119..121
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133045"
ORIGIN      
        1 mlllffsilk tifktadekh lekinktlnh kvsiivpayn eekiiaksle slvnqtyqnl
       61 eiivvddgst drtseiakyf kkhsngkkvk vlkksnggka sainhgirhs tgelimvvda
      121 dskleknavk lmeryfidpn vaavagsvyv snqtnlltkl qaleyiegln mvrngqallk
      181 lvniipgpig mfrkdalyev glydndtfae dcdvtlklit rgykidfesd avayteapeh
      241 lldlikqryr wtrgilqaik khkgllwnir knpaasftmw ymlfesvfwp fmdvwtnmfi
      301 iylsvfsgvs ilifywwsif tildmagaly cilitnnrls lvfyavfyrl yfisiiniak
      361 ifstieewfg iemtwgkler kgkl
//
LOCUS       WP_457562925             112 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit A [Caminibacter pacificus].
ACCESSION   WP_457562925
VERSION     WP_457562925.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Berrisford,J.M., Baradaran,R. and Sazanov,L.A.
  TITLE     Structure of bacterial respiratory complex I
  JOURNAL   Biochim Biophys Acta 1857 (7), 892-901 (2016)
   PUBMED   26807915
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 112)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002876
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..112
                     /product="NADH-quinone oxidoreductase subunit A"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=12185
     Region          4..99
                     /region_name="NuoA"
                     /note="NADH:ubiquinone oxidoreductase subunit 3 (chain A)
                     [Energy production and conversion]; COG0838"
                     /db_xref="CDD:440600"
ORIGIN      
        1 metiiiygtg ilagvlllyf lgiavapynp geikndhfec glppssevpm kanfgyfifa
       61 iafivfdmag lffslfvfad npdalkwamv fgillfaait vsmkeyrnak sa
//
LOCUS       WP_457562959             659 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease R family protein [Caminibacter pacificus].
ACCESSION   WP_457562959
VERSION     WP_457562959.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Domingues,S., Moreira,R.N., Andrade,J.M., Dos Santos,R.F.,
            Barria,C., Viegas,S.C. and Arraiano,C.M.
  TITLE     The role of RNase R in trans-translation and ribosomal quality
            control
  JOURNAL   Biochimie 114, 113-118 (2015)
   PUBMED   25542646
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..659
                     /product="ribonuclease R family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75844
     Region          1..592
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
ORIGIN      
        1 mkefayklvk gidrkdiprd krdmindlia lgivtsgkii qlkskyrigk vdvtkkgfgf
       61 lipigvkekd ylieahhlng askgdlvvae rlfnkkgrpk akvvyileka faytvaylty
      121 efkngkkqpv lkniktdmpi fvsekkktlk klpdgavfkv nnytakieev lgvlqdpwvd
      181 ekislalynk keefskkaik earaygdyvd ksmypdrvdl tdlpfctidp ptakdhddai
      241 yfdkeknely vaiadvseyv ylngnidrea kergfsiyfp hkaipmlpre lsenicslke
      301 hedrlafvfk itlneknevv keelfeaiin shrkysydrv defldgkfen iddtdkeile
      361 wlmplwdrvk niraqrlktg lefesdeikm tldengmikd vtleketpsh kliedcmlla
      421 nkaaakmidf gifrvhdkps qtsldelyse lgalgidvdv dekdftkvve giqsqakemg
      481 ikkfvdklii rsqqqaryda tntghfalgf erythftspi rrysdltlhr ilkatikgek
      541 kildyilrnv ealvvklsel ereamkvewd fydrkyarya dlhigdvykg iiedteippi
      601 akiledkllg arvflkdkqk fnlfekvdie ivkaniatak ikgkvkkees esiiesgge
//
LOCUS       WP_457562960             421 aa            linear   BCT 27-JAN-2026
DEFINITION  OmpP1/FadL family transporter [Caminibacter pacificus].
ACCESSION   WP_457562960
VERSION     WP_457562960.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..421
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46509
     Region          5..421
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkktlllssv lvatlfaggy ripeqslkgi alsaanvana sgadsayynp anmvfnedkn
       61 sfellttmih lnkvkfqndn gevyysrked fivpqfhfts kdhngwrfgf svtypaglsk
      121 rwddtipeag akeftlktie lnpvvakkvn enigvafgir fvksegianv lglksngdgt
      181 ytplyseyln gdsfdkgwna avafrsddqt lrlaatyrsk inlslsgdas gfynlylitg
      241 npadaakvva fntpgkvtvp lpavlnlaia kkfgkttlef vfdrtywhsy kkldfdfkdp
      301 avnaifgtpk pkdwkdsnty rfgithqcse kltamlgyay despvpnsti dfslpdsdkh
      361 ifsggikykl ddrmsvgisa lytkqktrra svydpitkty tngefkegga vlfaagfdyt
      421 f
//
LOCUS       WP_457562967             338 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562967
VERSION     WP_457562967.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39428
     Region          21..>127
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mkghsgissp ffivkkpvda iirdikkgds kdivelfran yddtyykksf ydpktweemv
       61 eskkyypiva eidgkvvgqf llsvndkyng eigavvvhpd ykgrglmnkm fdylikkaes
      121 lglsaiygea imfhpfsqka nlkhgmieta lqlgevaswi aqkdikfekr sgtlvgykif
      181 nrqkrslytp kiyrklildr ykkaslpisk aairpikksl rlwenrllkl sgiiidgkik
      241 nfenrfntlf tkaklrgemv yadinlhtpe ieeiteflnk krffysgvlf yryngfdylr
      301 lqyenthnve erlnvcfsdy ckflskfvir dkkrvarl
//
LOCUS       WP_457562969             158 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562969
VERSION     WP_457562969.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 158)
  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 158)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..158
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18101
     Region          8..121
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mieekikwne kyktltpkap silldhipsa knkkaldlag glgtnaevll nkgydvtlid
       61 isdvaiskik npkikticld ldnyiipqne hdviimikyf nldllkqipk alkkggyfaf
      121 ekipkykltt eeffeifkdf etifftkepf ryvgkltk
//
LOCUS       WP_457562970              90 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457562970
VERSION     WP_457562970.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Jurenas,D., Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Biology and evolution of bacterial toxin-antitoxin systems
  JOURNAL   Nat Rev Microbiol 20 (6), 335-350 (2022)
   PUBMED   34975154
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Kamruzzaman,M., Wu,A.Y. and Iredell,J.R.
  TITLE     Biological Functions of Type II Toxin-Antitoxin Systems in Bacteria
  JOURNAL   Microorganisms 9 (6) (2021)
   PUBMED   34208120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Rocker,A. and Meinhart,A.
  TITLE     Type II toxin: antitoxin systems. More than small selfish entities?
  JOURNAL   Curr Genet 62 (2), 287-290 (2016)
   PUBMED   26597447
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Goeders,N., Dreze,P.L. and Van Melderen,L.
  TITLE     Relaxed cleavage specificity within the RelE toxin family
  JOURNAL   J Bacteriol 195 (11), 2541-2549 (2013)
   PUBMED   23543711
REFERENCE   6  (residues 1 to 90)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..90
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=10698
     Region          1..90
                     /region_name="YafQ"
                     /note="mRNA-degrading endonuclease YafQ (mRNA
                     interferase), toxin component of the YafQ-DinJ
                     toxin-antitoxin module [Translation, ribosomal structure
                     and biogenesis, Defense mechanisms]; COG3041"
                     /db_xref="CDD:442275"
ORIGIN      
        1 myklvetkty mkklkkflkk npqimpkyek tivllennpy hsslrlhkls gklqnfysvs
       61 idmnyriivd fiiiedkifl idigthddiy
//
LOCUS       WP_457562965             186 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor transporter transmembrane component T
            [Caminibacter pacificus].
ACCESSION   WP_457562965
VERSION     WP_457562965.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Zhang,P.
  TITLE     Structure and mechanism of energy-coupling factor transporters
  JOURNAL   Trends Microbiol 21 (12), 652-659 (2013)
   PUBMED   24156876
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
REFERENCE   4  (residues 1 to 186)
  AUTHORS   ter Beek,J., Duurkens,R.H., Erkens,G.B. and Slotboom,D.J.
  TITLE     Quaternary structure and functional unit of energy coupling factor
            (ECF)-type transporters
  JOURNAL   J Biol Chem 286 (7), 5471-5475 (2011)
   PUBMED   21135102
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15320375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..186
                     /product="energy-coupling factor transporter transmembrane
                     component T"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22047
     Region          8..180
                     /region_name="EcfT"
                     /note="T component of ECF-type transporters; cd16914"
                     /db_xref="CDD:410987"
     Site            order(10..11,13..14,17..18,56,60..61,64..65,83,87,94,
                     97..98,103,112,116..117,119..121,123..124,127..128,
                     131..132,156..157,159..160,161..162,164..165,167..168,172,
                     175..176)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(136..143,158,162)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mkdnflkiaf ialfflflsl rdikiisfll alliivtfii dknlkiffka lksillfnlg
       61 vslgyiilay fkhinpwhyi lyinlkvilm tyyvfwffsk vsivrffsfs kelsylltit
      121 lsqifsykkt ftdfrdafra rvvnvrdkek tfitntfkff ltkamkdske ralamkargf
      181 feegek
//
LOCUS       WP_457562976             172 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiX family flavin prenyltransferase [Caminibacter pacificus].
ACCESSION   WP_457562976
VERSION     WP_457562976.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 172)
  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 10012639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..172
                     /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=19135
     Region          1..172
                     /region_name="PRK06029"
                     /note="UbiX family flavin prenyltransferase"
                     /db_xref="CDD:235677"
ORIGIN      
        1 mkkilvcisg asgaslglkl yslippeyer flvlsehaki vlekeenifl nddiaaapas
       61 gsfgidvtfi vpcsmntlak ialgiadnli traaqvaike kkkliiapre mpfseiyleh
      121 mlklsklqnv iiappviayy nkpetiddme kfligkwfdl vgienklfkr wk
//
LOCUS       WP_457562980             532 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457562980
VERSION     WP_457562980.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 532)
  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 532)
  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 532)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..532
                     /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          1..529
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 dncarvchsp slsglkmsig egassidfds ifdaetifvi gsntteahpm vasriikakk
       61 rgaklivvdv reiplmkfad isvilpfesn llflnaiake mierdlidkd finkrcvkfd
      121 eykelmlndk ydkhffeklk gfekikeqie eiaklitkkt ifawglgvte hidgteavna
      181 isnlammsgn fakgagvlpl rgqnnvqgac dvgclpyflp dyirpdeehi glmtpdvide
      241 ilngnikaii nmgedilhih pnqnkihkaf eeleflmvme vmpneitkra divfavksay
      301 eksgvyvnae rrlhlstplv ksslpddwei ikelanrfgg tlkyeksedv fedckkevgr
      361 frgasyerlk qkplqwpike dgsdlpvlhl ekfstsdgkg hfhyhkyhlr gevedilkgk
      421 krwwlntgra lpqynnsaqt kpsekltsky dddillvnei hkneisqkvk lrskygesae
      481 lkvkftdkvr pytlyttfhf aknkinylfg deadhkvkta rfkaveveii nl
//
LOCUS       WP_457562985             458 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457562985
VERSION     WP_457562985.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..458
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=52095
     Region          2..327
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mkvavigggv tgssiamyld nlgvdvtlfe kndlvsgppi chlhaggnly reitlkekia
       61 llkesidfir lypqaidfrp tivavpvdde gepedlietl eilkneykkm iekdpknkvl
      121 gepedyykly ykkdleklke kelvkepktl dewmipfaky tnlnkikypv ilvqeygvnv
      181 frlsaiskmi lekkgivrye eakvskkgdk wivngeefdy linaagfksg ivddalefkr
      241 drltefkaay vvknkkfdft wpeiifhgkr gtpkgmaqft pyangifqlh gmtkditlfd
      301 dglvssdees sypklpnhfi ekiekgwqke eaasrakrai khmskfipef kdsevtyvpl
      361 fgaqqipgrd aelraveisf eenyarcevv kastvtsmad siakdlskrf gikykkqiei
      421 peilslsdea itkkaceiak srgypedmgk rnfselks
//
LOCUS       WP_457562986             165 aa            linear   BCT 27-JAN-2026
DEFINITION  LOG family protein [Caminibacter pacificus].
ACCESSION   WP_457562986
VERSION     WP_457562986.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..165
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18512
     Region          7..>131
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mkiattfgas rvedpklyee gvelgkflae rgyvvkcggy gglmeavsrg vreaggevig
       61 itlkyfdeir penpyltkki qtpdlferlk nlivgsevfi aqagsigtln eifmvwalky
      121 glgldfricl lgeayeefkt csfipkerls eieiykslee fkrnf
//
LOCUS       WP_457562989             218 aa            linear   BCT 27-JAN-2026
DEFINITION  2OG-Fe(II) oxygenase [Caminibacter pacificus].
ACCESSION   WP_457562989
VERSION     WP_457562989.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..218
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=25006
     Region          111..214
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 mvpisqkiya lddiwqmdfe kyplashyne ypflvfenlv skdeckraln slsscdykak
       61 lvgsgldesi rktiihtptk eikevfekaf faikekvekf ygvsflkgte lqvleykegg
      121 fykchadnas eivkngklvg ykvvkperkl ttlmflnddy eggevefchl ryangdrvih
      181 kpkagemivf pshglfahev kpvygnnrfa vvkwwdvv
//
LOCUS       WP_457563005              78 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system HicA family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457563005
VERSION     WP_457563005.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..78
                     /product="type II toxin-antitoxin system HicA family
                     toxin"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /calculated_mol_wt=8687
     Region          1..71
                     /region_name="YcfA"
                     /note="Predicted RNA binding protein YcfA, dsRBD-like
                     fold, HicA-like mRNA interferase family [General function
                     prediction only]; COG1724"
                     /db_xref="CDD:441330"
ORIGIN      
        1 mppipiistk dfikflefkg fvlvrqkgsh krfkhsngks itvpdhgkan lkrgllkgml
       61 nsidvevdel idflnkgk
//
LOCUS       WP_457563006              72 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system HicB family antitoxin [Caminibacter
            pacificus].
ACCESSION   WP_457563006
VERSION     WP_457563006.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Winter,A.J., Williams,C., Isupov,M.N., Crocker,H., Gromova,M.,
            Marsh,P., Wilkinson,O.J., Dillingham,M.S., Harmer,N.J.,
            Titball,R.W. and Crump,M.P.
  TITLE     The molecular basis of protein toxin HicA-dependent binding of the
            protein antitoxin HicB to DNA
  JOURNAL   J Biol Chem 293 (50), 19429-19440 (2018)
   PUBMED   30337369
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Bibi-Triki,S., Li de la Sierra-Gallay,I., Lazar,N., Leroy,A., Van
            Tilbeurgh,H., Sebbane,F. and Pradel,E.
  TITLE     Functional and structural analysis of HicA3-HicB3, a novel
            toxin-antitoxin system of Yersinia pestis
  JOURNAL   J Bacteriol 196 (21), 3712-3723 (2014)
   PUBMED   25112480
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Makarova,K.S., Grishin,N.V. and Koonin,E.V.
  TITLE     The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin
            system in archaea and bacteria
  JOURNAL   Bioinformatics 22 (21), 2581-2584 (2006)
   PUBMED   16895922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..72
                     /product="type II toxin-antitoxin system HicB family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /calculated_mol_wt=7980
     Region          2..>53
                     /region_name="HicB"
                     /note="Antitoxin component HicB of the HicAB
                     toxin-antitoxin system [Defense mechanisms]; COG1598"
                     /db_xref="CDD:441206"
ORIGIN      
        1 mkfnvivked kldggyiayv pelkgcftqa dsldelkkni ieaievslde neeispifgi
       61 wevdinaans yn
//
LOCUS       WP_457563009             112 aa            linear   BCT 27-JAN-2026
DEFINITION  P-II family nitrogen regulator [Caminibacter pacificus].
ACCESSION   WP_457563009
VERSION     WP_457563009.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Huergo,L.F., Chandra,G. and Merrick,M.
  TITLE     P(II) signal transduction proteins: nitrogen regulation and beyond
  JOURNAL   FEMS Microbiol Rev 37 (2), 251-283 (2013)
   PUBMED   22861350
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..112
                     /product="P-II family nitrogen regulator"
                     /GO_function="GO:0030234 - enzyme regulator activity
                     [Evidence IEA]"
                     /GO_process="GO:0006808 - regulation of nitrogen
                     utilization [Evidence IEA]"
                     /calculated_mol_wt=12499
     Region          1..112
                     /region_name="GlnK"
                     /note="Nitrogen regulatory protein PII [Signal
                     transduction mechanisms, Amino acid transport and
                     metabolism]; COG0347"
                     /db_xref="CDD:440116"
ORIGIN      
        1 mkkieaiikp fkldevkeal ieaeitgitv sevkghgrqh ghtelyrgae yvvdflpkvk
       61 leifvnddfv ektveiiteh aktgkigdgk ifimpveeai rirtgergrd av
//
LOCUS       WP_457563010             373 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563010
VERSION     WP_457563010.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 373)
  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 373)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..373
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          40..277
                     /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          44..69
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(45..46,49..50,52,76,79..80,83..84,86..87,110,
                     113..114,117..118,121)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          74..104
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(151,154..155,158..159,161,185,188..189,192..193,
                     195..196,218,221..222,225..226,229)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          151..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          183..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          248..369
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          249..277
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(250,253..254,257..258,260,284,288..289,292..293,
                     295..296,316,319..320,323..324,327)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 lykndsdnta iklayaktlf nlgdfktler ikdnnlaffn hlelylkakk lynegkykea
       61 ekiavklfny ypnninvlll ngnifyklgk ydlayiyykr vvkkepqnip alkglrdval
      121 ankditsavk isdilknlky kdkkfneimk eyylfqadkl aqegkfkdal sdvkeaekyt
      181 dsekdiyvay gkiyfkmgey kkaldyyrml ysrnapleir ekliriyirl gkinkakeia
      241 qnspneikai yymemaryym kqkkypeank yittaleynp insmcayeik awvcyylgdy
      301 gcaksyfeks dlklpevrlg yafvlakmgn kekayliaqg iktrskniml qkarlmielg
      361 rekeakeifn sid
//
LOCUS       WP_457563016             394 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Caminibacter pacificus].
ACCESSION   WP_457563016
VERSION     WP_457563016.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..394
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45953
     Region          55..391
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mrdyilqkea eeikfapmms vseflnrkpl fykeidvlrm praynlirdk ikippvihii
       61 gtngkgstgr flahtllkrg ykvghytsph imkfneriwi ngenisdeyl edihqklqkl
      121 lpknvidsls yfeyttflaa lsfegldfvi meaglggefd atnvfekeis lvttidldhq
      181 sflgdniidi attklnsiqn eaiigkqihe dvewvvqkki negkkiykyl dffemeeiee
      241 lkkefkfakf lfpnfllams ylkkrgisfs pknlddlrlp grfeeiekdl widvghnpla
      301 areivkslpk kvnlvyntya dkdyeeilri lkpkinklyl idvkndried kekikktaek
      361 fgidveefnt ikkpmlvfgs fsvveeflke yygk
//
LOCUS       WP_457563020             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563020
VERSION     WP_457563020.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..359
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=41998
     Region          <168..350
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
ORIGIN      
        1 mkkivsiifl fsfifassln ckrdelfivg lnkkkdiiec lksgyefsdk sietllsdgd
       61 edilrylvky knrklqnkff piyfinkgkf fdefktntlq dnvakcritk ekdvckravn
      121 laiqledydt alvlayksnq vyllknyign lkkeylicyy lktypptayk lsknlqvycp
      181 fkipnkliye kylnnsltea aennetikai rflkqgadpn tkgrpvyiav akdnypltka
      241 lldygafthy inpyfgfniv fsasadspel lklilkvape syvnqvvkig yetdyplhya
      301 fknhryenmk ilfehgakir ddgfiyycaf kdnkkmldlf kkygydlnkk yekyknlcq
//
LOCUS       WP_457563022             419 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457563022
VERSION     WP_457563022.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46042
     Region          1..369
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mgdlkktigv fsgiaiaigm vmgsglfglp glaidiagak lsllgwlaii lavipmiyif
       61 iklgikfpka gglstyakaa fgdwaefgvv avlsgtfiig ipalaiigge yltklfsisi
      121 elkyffaflf llfatiiniy gvqmaswink islifillli ivlviihpdy ltegikalnf
      181 ktenikinkl wevmallfwa flgwenlsfg leefknpkkt ipiiywgsff ivsmfyfmla
      241 llvsgavisg ikvsgasaia silsdnvtls kfliffmvvv iiananswvf gasrliysag
      301 kdgilfkklg ilnkkgipsn alitlmifya ffifalyyfk idlstiimiv sqnflvlylf
      361 siiafaklfs gtidrivlll ssvillfffq gfgvaiiypl illligfvry kktniitig
//
LOCUS       WP_457563023             233 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563023
VERSION     WP_457563023.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..233
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26073
     Region          <2..228
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkialhvpcy inelnpeivr ktllilrhfg lnvsvpknqt ccgqpfinsg qpttlpeqfn
       61 eifkdydyiv spsssctsti rsqelevskk myelceflhd ilqvreiakn ypkkialhns
      121 chslrhlleg apselnipyf nkvkkvlgge iveakrdecc gfggvfsvke gfisyvmgrs
      181 klddlissgg kvitgvdfsc lmhlkgiaek dgddieikhi seiiyesifg eek
//
LOCUS       WP_457563025             261 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563025
VERSION     WP_457563025.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..261
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30249
     Region          146..253
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mkevlkeiie keaddliryw veefpeeerd eearyyedfl sffeecvekd ldihapesea
       61 lktflekiie ilgedrffnf knsvytcylk fpimkkleek nafeygiikk ltvffealts
      121 riiidllkkn eqvtmsamne leereapiae iwdgvlmlsi vgtldsnrvl kiidkilekl
      181 dkreiehvvv digaihdmns evarqiikln naihfmgsna yltgitpvia kslthldikl
      241 gdiktfsttk kamehilhge i
//
LOCUS       WP_457563029             417 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Caminibacter pacificus].
ACCESSION   WP_457563029
VERSION     WP_457563029.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 417)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..417
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45954
     Region          20..416
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 mvkvgivgvg tvgvsvvknl eknreiiksr agkeikvvkg vvrdpskkrd vnielvtdyk
       61 evtrdpqidi vvelmggvdk ayevvkdaln hgkavvtank allayhrfel qkiantpfey
      121 easvaggipv ikalrdglsa nhieeikgii ngtcnyilte mkkgrdyeev lkeaqekgya
      181 eadptfdvgg fdaahkllil asiaynidak peeiliegie ninltdiefa kefgyeikll
      241 giakkignei elrvhptlik keemiakvdg vmnavsvigd vvgetmyygp gaggdatasa
      301 visdiieiar gcikpmlgfk ipleldnvkl kpideiesky ylrvavndev gvlekiahil
      361 aknnisiesf lqkprngyvk llfsthkcke keikkaikei qelsfvlkpi nyiriee
//
LOCUS       WP_457563030             211 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457563030
VERSION     WP_457563030.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..211
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24795
     Region          11..209
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mieklkkisl ffniedkile eissfshfkk ynpdeiifye gekdkyfygi vtgsvlmydi
       61 dlkgniipkn qfgcgdifgl isqiqnreyc lsaksesdse iiridytkfq kfisnppfsd
      121 riikmlsnqi lqemefnklq kydatkrlvy allnfpkkfi rkkkyllake lnmspetlsr
      181 ilsklrneei icyceksikv ldeeklknll s
//
LOCUS       WP_457563036             202 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563036
VERSION     WP_457563036.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..202
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23121
     Region          15..167
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mnlfdlyyed yekwfekypk iyeeelktik tllpkgrgme vgvgsgrfaa plgikfgiep
       61 srkmaeiarn rgievleita eemdfeeefd filmvtticf vkdplktiqn cykalkkggf
      121 llvafvdkns plgktyeknk qnskfyapat ffskddiinl mkkagfknfe ckenlygdsl
      181 dnlkfkindc nggafkvirg kk
//
LOCUS       WP_457563038             258 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563038
VERSION     WP_457563038.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..258
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28037
     Region          2..256
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mwdlintsiy asillsiaig iigslivink ataitgsiah gsfggigigi flgtsilltt
       61 tiftvilali lalitifyrh radsligviw avgmsigiif lslapgynad alsylfgnil
      121 lvenkdlllm givdlilivs ilvlynrfla msydmeflki rginsnllft yflvltslti
      181 visvraigii lilalftipp liaekftkrf yqmiilssil afifmsagii isyfydlspt
      241 piiviiaaag lflslfkr
//
LOCUS       WP_457563027             496 aa            linear   BCT 27-JAN-2026
DEFINITION  ArnT family glycosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563027
VERSION     WP_457563027.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 496)
  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   3  (residues 1 to 496)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..496
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56958
     Region          1..354
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mekrlkialf laiainffft lhltplfnld egafseatre mlknhdfitt ylngalrfdk
       61 piliywlqal svtifglnef alrlpsalaa tfwafgiywf akkifdektg vlsaffmvta
      121 lqigliakaa iadallnmfi afsmfslyly iqnqnkkyly ftfafigfgf ltkgpvavli
      181 platffiysl ikkdfkfflk ttfdlkgivl fliialpwyi aeymaqgdkf ikgfflkhni
      241 drfetslekh kgslfyyipv iligmlpwts lllkyltklk nylkeqndff lfgsiwfffv
      301 fiffslsgtk lphyviygyt pvfifmgvaf kelkseflys lplilfvlal lilpsfalnl
      361 tknkeaviai ktimplfniw yyislgavli lsllklgken ktiilgfsmv filnyvgwiy
      421 aharaipvkq aaifakkhni knvyletnlp sfsvyfdkit prkkakkgev alikskntkg
      481 ykvlfkkglv algvke
//
LOCUS       WP_457563039             240 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563039
VERSION     WP_457563039.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..240
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27298
     Region          1..214
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mravevknly fkyekewvle dinfsledke fmaiigpngg gkttllkill gflkpstgev
       61 kiygkppkdn sqiigyvpqh tnfsldipit vfdivlqgrl kkgkffyske dkekaneiln
      121 klkiyqfkdr kikdlsggqr qkvliaralv sepkivmmde ptsaidptgq keildliesl
      181 eitrlvvshd ikillrdvdk iayihkkavi hegpklnipk dkhfceveli eflkdescgt
//
LOCUS       WP_457563041             237 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457563041
VERSION     WP_457563041.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 237)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..237
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28243
     Region          7..>89
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          156..236
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlkiqndifl itskyqntqf kphfhdtysf alitdgecvv nfknktihyk kndfriinpy
       61 eihyvksgiw gyksvvfeks fvnsitkeii nkeniifknk instklnslf lkmyekqeen
      121 iyfffeells fskeiklpki tlkksieyid enftqkikle nladlehisk yhflrlfknq
      181 tgltphqyii ikrlnfalel mkkeknlayv avragfsdqs hfikefkkvf gftpkek
//
LOCUS       WP_457563045             162 aa            linear   BCT 27-JAN-2026
DEFINITION  carbon-nitrogen hydrolase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563045
VERSION     WP_457563045.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>162
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          13..>162
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(38,95,99,102,127..128,130..131,150)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(38,95,127)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mkkielvnfk tskdyeynlk rviniiknsp adfllfpevc ltgfdyenwd nvnrfaktai
       61 qelsslkkaf altlinnnkn yfclfdnglk ykrakynlfg nekeyfeige kpkifewrgl
      121 kiaslvcfel rfleywqsfr gvdiifvpar wgkermphfk tl
//
LOCUS       WP_457563046             176 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563046
VERSION     WP_457563046.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 176)
  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 176)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..176
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20530
     Region          1..122
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mlakrydsad mrefyefiip ylkgktlfdi gcgscmdvvf ftslgfdvec vepsiefrki
       61 cskkdssiki ynqklphikl skkydvvili gvwmhlrkfy yvkaienlks llkrkgvlil
      121 sfstkkrdgf dsinpknlkf lflkngfrll kenisndsld rkidwvtqvy ildkit
//
LOCUS       WP_457563049             405 aa            linear   BCT 27-JAN-2026
DEFINITION  L-cysteine desulfidase family protein [Caminibacter pacificus].
ACCESSION   WP_457563049
VERSION     WP_457563049.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Mendez,J., Reimundo,P., Perez-Pascual,D., Navais,R., Gomez,E. and
            Guijarro,J.A.
  TITLE     A novel cdsAB operon is involved in the uptake of L-cysteine and
            participates in the pathogenesis of Yersinia ruckeri
  JOURNAL   J Bacteriol 193 (4), 944-951 (2011)
   PUBMED   21169490
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Tchong,S.I., Xu,H. and White,R.H.
  TITLE     L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from
            Methanocaldococcus jannaschii that catalyzes the breakdown of
            L-cysteine into pyruvate, ammonia, and sulfide
  JOURNAL   Biochemistry 44 (5), 1659-1670 (2005)
   PUBMED   15683250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..405
                     /product="L-cysteine desulfidase family protein"
                     /EC_number="4.4.1.28"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0080146 - L-cysteine desulfhydrase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44396
     Region          5..403
                     /region_name="CdsB"
                     /note="L-cysteine desulfidase YhaM [Amino acid transport
                     and metabolism]; COG3681"
                     /db_xref="CDD:442897"
ORIGIN      
        1 mygakeiils eikpalgcte paavalnaay lreygvfdek nlkltvntnl lknamyvpip
       61 ntskrfgvkl afalgylfgd vndglnifkn lneekvkkal efsekvkvel iegselfiks
      121 ensyaeavti kfhdnieyvi skgelkefdn hqeevevksy vledkpfdiv ydlieqeknf
      181 efvreaveln malaeygmnh dvginvskqf sgdslkdkic kittsasdsr mdgvnmpams
      241 ltgsgnhgis atlpvwvyak ekgfseeeal ksvalsmlit iyiklfigrl svicgaavas
      301 gcgvagaiay legdretskk avkhviqnig tllcdggkma cslkvlqgas vgydsakfal
      361 namevyedgi mfedvtktik alkgikekms gvdeeivkim kekll
//
LOCUS       WP_457563050             108 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydroneopterin aldolase [Caminibacter pacificus].
ACCESSION   WP_457563050
VERSION     WP_457563050.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..108
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12551
     Region          1..103
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mykiviedls fkailgllek ernqeqlvvv caqieyedkk nfidyakvcd iiqntiieek
       61 ftliedaidv lieklknefp qmksihlkir kpeilknalv gvetlrkf
//
LOCUS       WP_457563055             356 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaE family ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563055
VERSION     WP_457563055.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="MlaE family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39736
     Region          106..351
                     /region_name="MlaE"
                     /note="Permease subunit MlaE of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG0767"
                     /db_xref="CDD:440530"
ORIGIN      
        1 mlkiitnhhl islvgsldkn tiqkayylkk eknmtidlke lksmdyegal flvelsknhk
       61 iinlpphlke lfnfvaqnak dlkipeqktn flfhatnyln diffaikent infllffgef
      121 iyfliflith pwkfrfketa aiivkagaga lpivgltsfl vgvvmayqga mqlskfgani
      181 fivdmldisi freiapliaa ivvagrsasa fsaeigvmkl teeidamktl gfepfwflvi
      241 prviamiiam plivffadmi gilggmiisa lslnigfdmf lnrtrdvlsl tqvfiglgka
      301 pffgiviali gtyrgfqvrn stqdigkytt ksvvnaifwv ialdaifsii fakfgi
//
LOCUS       WP_457563056             315 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563056
VERSION     WP_457563056.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>315
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
     Region          1..256
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mnrkinyiil avftllltag avyfiywlgk fnankkpkny yqaifhesvs glniaspvky
       61 mgvnigsvkk itinpnepns vivtftvdkn iplrkdsyav lelegitglk yieieggskn
      121 spilktskhh patiktipsf naklfealsn ttdklnklld nlntildpkk ashlqnmlih
      181 lekisayldk nkymlkdtiq nfnqlqnnln ktitalrkdi hnltthtikt ekaftqnfnq
      241 lnsnvssfvk nsniliselt kktkegqfdl kdallesfkp idttsneikk atiklenlln
      301 elqnspsdii fkkan
//
LOCUS       WP_457563061             395 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457563061
VERSION     WP_457563061.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46011
     Region          76..389
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkktaflipv flfanqnils dlklkllnld kqrsiysake tqkswinpii lqysisqnns
       61 lhttkqniqt fsvsinqpif ktgaiyysik yaknlknynl kqielqkral ikqayelvyd
      121 ykinklneei allniqnaki dvkkkkedfl ngtgdstfln qaiinlnnik lgyedlkfne
      181 kqlkfsfknl sdldiekvkl pyfkiisknd finnnlqlis skindkikyd lykmqlgnql
      241 ltisfnasyn yqitdytnet skyhddsnny ynvglsvtlp idftstdkvk qtklsyiksr
      301 yetldtkrnl lntyamiisq iktlqnkkki ykenekayan liestkesik agnatvldlk
      361 ilensykvmq inqkiidlqi qklllnlyyq vtskf
//
LOCUS       WP_457563043             296 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457563043
VERSION     WP_457563043.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..296
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=33772
     Region          16..52
                     /region_name="S4"
                     /note="S4 domain; pfam01479"
                     /db_xref="CDD:396182"
     Site            order(27,28..29,31..32,35..36,38,45..52)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          72..274
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mgfvekefei ndekvldflv kkvgfnlrea kraidrgrvs vngkrvtqks qratgklkci
       61 mfepngyglk pifetthfai fdkpsgvaih pkklantksl lddvralwgn danlvhrldk
      121 etsglvmask nkfaesilkr afqdkdikks ylalvkgcld kemtikkpia vnkdenikvk
      181 viihpegkes vtivkpikif dnytlvecdl ltgrqhqirv hlfsighpiv gdplygvdnd
      241 fadrylnklv tekeriektg anrlmlhsyk lefefmnnky iiksdsffev lknfin
//
LOCUS       WP_457563068             415 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caminibacter pacificus].
ACCESSION   WP_457563068
VERSION     WP_457563068.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 415)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=48042
     Region          1..405
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 miidfnfynf ksfadktefs miaddkeskn nfniekfkll ktavvygpna ggksnffkal
       61 kfyvdlilqs shfdpavkid sqkfklnkky lneptvfecr fiienlyyry gfsikdgiie
      121 sewlyhrpkg reariferng qeiirgkfke gknveektke ntlflsaltq wnsetakkit
      181 mffksinfis tnlpvsitld fiekgiinkn dflnilknad mglidfknek ieiepgekip
      241 sellgagiil tdngkpyynk lttyhpvfdd knnlsgsvef dffkdesdgt kkyfgllgpl
      301 latlktgsvl fvdefdtrvh plllrimvkl fhsdknkkna qliftthntn ilspqlfgrd
      361 qiwfankdry gkselyslle ikgvrknsnf ekdylngkyg avpylkkilk efdmq
//
LOCUS       WP_457563070             259 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter, partial [Caminibacter pacificus].
ACCESSION   WP_457563070
VERSION     WP_457563070.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..259
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          24..259
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 msiwsglpsg vfvffrvvfa fpfifyfaik ragireffkl kpfwplfvsg ialgvnwvff
       61 fwavntidva savsiyylgp iismllaiwf lkergnfyiy isgvlaviga vvaaggvhfq
      121 egiivaflaa vsygalgffs kiatmhhrav avtawqilis ifitapflfl ndwhlslqgi
      181 ivafitgvih talalflwyd alnyikvsia silqyldivf amilaflflg qvpqihqilg
      241 agliiiagil stfkekakk
//
LOCUS       WP_457563047             172 aa            linear   BCT 27-JAN-2026
DEFINITION  uroporphyrinogen-III C-methyltransferase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563047
VERSION     WP_457563047.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Rehse,P.H., Kitao,T. and Tahirov,T.H.
  TITLE     Structure of a closed-form uroporphyrinogen-III C-methyltransferase
            from Thermus thermophilus
  JOURNAL   Acta Crystallogr D Biol Crystallogr 61 (Pt 7), 913-919 (2005)
   PUBMED   15983414
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Vevodova,J., Graham,R.M., Raux,E., Schubert,H.L., Roper,D.I.,
            Brindley,A.A., Ian Scott,A., Roessner,C.A., Stamford,N.P.,
            Elizabeth Stroupe,M., Getzoff,E.D., Warren,M.J. and Wilson,K.S.
  TITLE     Structure/function studies on a S-adenosyl-L-methionine-dependent
            uroporphyrinogen III C methyltransferase (SUMT), a key regulatory
            enzyme of tetrapyrrole biosynthesis
  JOURNAL   J Mol Biol 344 (2), 419-433 (2004)
   PUBMED   15522295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..172
                     /product="uroporphyrinogen-III C-methyltransferase"
                     /EC_number="2.1.1.107"
                     /GO_function="GO:0004851 - uroporphyrin-III
                     C-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009236 - cobalamin biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0019354 - siroheme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
     Region          <1..171
                     /region_name="CysG"
                     /note="Uroporphyrinogen-III methylase (siroheme synthase)
                     [Coenzyme transport and metabolism]; COG0007"
                     /db_xref="CDD:439778"
ORIGIN      
        1 ekgkhsksqd einelilkya kdgkivgrlk gghpfvfgrg yeefeaiane gfevevvegl
       61 tsaisaptea mipvtqrgkk dsfivvsahl kgarvnlnwv dlllrenirv vvlmglsrvk
      121 diqkkafdig vdekkevyiv snatkntkvi ktmlknlvie akkaekpavi if
//
LOCUS       WP_457563080             180 aa            linear   BCT 27-JAN-2026
DEFINITION  MotE family protein [Caminibacter pacificus].
ACCESSION   WP_457563080
VERSION     WP_457563080.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Eggenhofer,E., Haslbeck,M. and Scharf,B.
  TITLE     MotE serves as a new chaperone specific for the periplasmic
            motility protein, MotC, in Sinorhizobium meliloti
  JOURNAL   Mol Microbiol 52 (3), 701-712 (2004)
   PUBMED   15101977
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Albertini,A.M., Caramori,T., Crabb,W.D., Scoffone,F. and Galizzi,A.
  TITLE     The flaA locus of Bacillus subtilis is part of a large operon
            coding for flagellar structures, motility functions, and an
            ATPase-like polypeptide
  JOURNAL   J Bacteriol 173 (11), 3573-3579 (1991)
   PUBMED   1828465
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..180
                     /product="MotE family protein"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=20424
     Region          30..170
                     /region_name="MotE"
                     /note="Flagellar motility protein MotE, a chaperone for
                     MotC folding [Cell motility]; COG3334"
                     /db_xref="CDD:442563"
ORIGIN      
        1 mgkftkllfi plflfavdnq klldcydifa qkkaeleaea ekileqkeal ealkntymal
       61 ikkkelklkq keaeinatlq kieeekkqiq klleenkkil eeikkakldk vaqsyakmra
      121 knaaeilsnm pekdalkilq klqpkilaki fakmdpqiaa klsdallkiq kdnnassanp
//
LOCUS       WP_457563083             222 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563083
VERSION     WP_457563083.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 222)
  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 222)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>222
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          26..>101
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mryfliflfv plfafdyfti kkadeffqkk eylkaakeyl kidsqkalld aansyykagd
       61 ykkaieiysk indkklqfdk lynmanayak lgmfqkaiel ykkalkikkd kdaqynlkll
      121 ekllkkkppk qkqkqknnkq knnknknnke nkkqnnnqnk knqnkneqnq knnkkqnknk
      181 nsnanknnkq kenqqknnqn qnknqkkqsk nnekkeqnkk fa
//
LOCUS       WP_457563084             102 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563084
VERSION     WP_457563084.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>102
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <16..>102
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(17..19,21..22,26,29,38,40,42,46..47,50..52,54..55,
                     59,62,71,73,75,79..80,83..85,87..88,92,95)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          40..71
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          73..102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnsryeelli mavdfarngq seylkemikh glnvnlkdtk gntllmlsay nghletskml
       61 lnsgaevdsr ndrgqtplgg vafkgdlehi ellikhgadi na
//
LOCUS       WP_457563085             474 aa            linear   BCT 27-JAN-2026
DEFINITION  catalase [Caminibacter pacificus].
ACCESSION   WP_457563085
VERSION     WP_457563085.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..474
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54670
     Region          2..474
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mkkltttagi pigdnqnslt agprgpllmq dfalleklah qnreriperv vhakgsgayg
       61 vfrvtnditk ytkakvfepd setrifirfs tvagergaad aerdvrgfai kfytkegnwd
      121 lvgnntpvff irdpykfpdf ihtqkrhpvs nlrsnnamwd fwtlhpeslh qvtilfsdrg
      181 ipasyrhmng ygshtyslin eknerfwvkf hfktkqgikt ltneeaqeii gkdreshqrd
      241 lfeaiergef pkwevkiqim smeeakevdf npfdvtkvwp hkdfplidvg eielnenpkh
      301 yfaeveqacf spsnvvpgis fspdrmlqar ifsyadahry rvgtwyemlp vnrpvvevnh
      361 yhadgamrfd epvgsdayye pnsfggpkdd peyieppfpv dgdgyrynhr ddsdyfsqpr
      421 alfelmsenq kkqlfkniaa smqgveerfi nkaltlfeqi speyaqgvkn elki
//
LOCUS       WP_457563086             390 aa            linear   BCT 27-JAN-2026
DEFINITION  ammonium transporter [Caminibacter pacificus].
ACCESSION   WP_457563086
VERSION     WP_457563086.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, 57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..390
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41563
     Region          6..387
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdlawaldtf falfaftlii lmvpgfamle aglvrtknvt avltvntmiy ivaslvfffw
       61 gyvlafggwd gssmsmyaaf lfqlafvgkt vnimsggvse rtriiplaif tifmagliyp
      121 lvvnwtwgan mlkgtfldis amhdlagstv ihstgawall aailiigprk grytkdgkvr
      181 vipasniplv ilgafllwig wfgfnggsvg sisskeaant valvvmntnn agligglavm
      241 vlsyltykkf ditmilngal gglvaitaga dvvspyaali igliggilvf yavpffdklk
      301 lddpvgalsv hlvngiwgti atgiwgkgvs laaqikgvvv vgifafvasy iiiwainkiv
      361 pfraneedei egldvsecgi esypefkrai
//
LOCUS       WP_457563087             660 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457563087
VERSION     WP_457563087.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..660
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=75259
     Region          131..660
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnfihklslr tkvitvvlls iimivyftgk elvrhfdfek kkaqlteliv lsqslsklih
       61 etqkergvsa gylgshgkkf aemlpkqral tderikeymq vlknidfaky spefkqeiek
      121 lnqylkmlpe irnkvnnfqi slkdevkwys qmnanilkii gyaarfapnd kismdlaayt
      181 sflkakerag ieravlsatf gadkfapgmy tklirliseq nayiddfltf anermkklyy
      241 ktikepefae vqrmrdiais hhktggfnid peywfktitk kinalkridd siakiivkdv
      301 nsikdnaiie aiiglisiii vlffsyliir sfslqlnslk nlilmiardk dlsievriye
      361 ddefgeirra lrtflaslhe vmmsahtssi enkqvatnle ksfgsiteni qkeanivtna
      421 settnelrek lneeaensne vknsivdane slqeaiklik dtmeniqlna enenelamrl
      481 qqlsqdaeqv knvltvirei adqtnllaln aaieaarage hgrgfavvad evrklaertq
      541 kslgeidati nvivqainsa stdmnknien vnrvtektge vqgriqevst kmeevvvkvd
      601 qnveevekvv kimedfikkm neiqklssen kekvlsnqsy ihriatlade llkeisqfki
//
LOCUS       WP_457563088             255 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563088
VERSION     WP_457563088.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28733
     Region          1..254
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 mlkvdkvtkq fggvvaikdv sfevkpleif alvgpngagk ttlfniitgv leptsgkiyf
       61 kdeditglsp vkivekgiar tfqnirlfss ltvlenllig fhnhieynff eslfrlprff
      121 kqekihkeka meilkflgie qyadynakal sygnqrkvei aralatepdl llldepaagm
      181 npketdelad tvfklrseme ktilfiehdm kfvqkiadrv mvldygktif egkpadmmkd
      241 etvikaylgd idveg
//
LOCUS       WP_457563089             359 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457563089
VERSION     WP_457563089.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..359
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40789
     Region          5..328
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkvfdyiiig agiagslagy flrdknvlvv dkkgkleaas gaagaflfpk vgydttytrf
       61 inegivssie fyksigvdth tkgvlilprd erdiekfkky ekeiklpfkk rgegfffeig
      121 svidpeevke kldfpfekle vktlkkkeyw vindeikakn vilasgyesi vdipyiqirp
      181 iwgerieieg iwdkskcdiy yhkncsvgcn gvmkigathk rncldckene qealelikka
      241 reiidikeye ikdvkggfra astdyfpvvg qvidvdktll ndkhiikgdm pkeifyiegl
      301 yiingmggrg fsnayvcakm lkdfiengvd lgwvdtkrlf ikwarksgea ylrsknvks
//
LOCUS       WP_457563100             166 aa            linear   BCT 27-JAN-2026
DEFINITION  shikimate kinase [Caminibacter pacificus].
ACCESSION   WP_457563100
VERSION     WP_457563100.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..166
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19089
     Region          6..165
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 msagnviltg fmgsgkstig rilakelnty fidtdnliey fenrsikeif ekegeesfrk
       61 kerycfewik nnvkntvisv gggfpvfipe ikeagvviyl kvdfddilkr msedeiakrp
      121 lfqdikkake lfskrdniyr qladyiienr didetikkik giidas
//
LOCUS       WP_457563102             198 aa            linear   BCT 27-JAN-2026
DEFINITION  uracil-DNA glycosylase [Caminibacter pacificus].
ACCESSION   WP_457563102
VERSION     WP_457563102.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 198)
  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   2  (residues 1 to 198)
  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 10178243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..198
                     /product="uracil-DNA glycosylase"
                     /EC_number="3.2.2.27"
                     /GO_function="GO:0004844 - uracil DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=22780
     Region          44..188
                     /region_name="UDG-F4_TTUDGA_SPO1dp_like"
                     /note="Uracil DNA glycosylase family 4, includes
                     Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA
                     polymerase, and similar proteins; cd10030"
                     /db_xref="CDD:381680"
     Site            order(49..53,56,62..63,90,172)
                     /site_type="active"
                     /db_xref="CDD:381680"
     Region          49..53
                     /region_name="motif A"
                     /note="motif A [structural motif]"
                     /db_xref="CDD:381680"
ORIGIN      
        1 mgdwknrlke fyktraefik ahlnenidft dvfdpyleek ndnpimiige apgenevkqk
       61 qpfvgkagen lnylisisgf drkrdflitn afpfrtfqdk knrtpkakel kigaellkke
      121 ieivkpkiil llgnsaikaf sylvkdvknl qkcgyydins eigklkigvc yhpsplafnr
      181 keireslekf fknlskav
//
LOCUS       WP_457563107             243 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter, partial [Caminibacter pacificus].
ACCESSION   WP_457563107
VERSION     WP_457563107.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>243
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          5..241
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrknnllyhf ialvtiiiws ltfiqtkill kylspeeill drfviawiif fiifpkikff
       61 slkeelifvf lgfsgifgyy ilenislslt sainvgiivt sapifttilk ittqktnskk
      121 vlfsiigfif viigllimei khiskpnlgd ilailgalff gaysfvlgkv nsntnsilit
      181 rksffwgivf lmiflffkhf nfsdikiyqn vdvwfnilfl sffatalcff mwkkavskie
      241 tka
//
LOCUS       WP_457563109             246 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457563109
VERSION     WP_457563109.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26516
     Region          1..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mitaiiigif vgffsgflgi gggtvlvpvl lflgfgfkea vgisvtqmmm ssiygsylny
       61 kkgllkikng lslavggaig aalsglivky tskdilgtif ltlvfiaiir ffvtvkephd
      121 eppidnkklf figlfvgaia isvgvggail itpilvgflk yklkttvsls lffvvfssvs
      181 gfisqslagh inylegfsig iasligtyfg vklyhkvdtk ihkkillawy ififfamiyk
      241 lyfqgn
//
LOCUS       WP_457563115             193 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563115
VERSION     WP_457563115.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..193
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22191
     Region          7..173
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(48,50,52..53,116..117,133,173)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 meilvkpcge fytncyivdr kiiidpgiga yefvrehvdk plaiinthgh fdhmwddkti
       61 kemydipiyi hkndafmlen dpfgynppkv kpdylleegd ikigdydiki rhfpghtpgs
      121 itieigdemf sgdfvfdgsi grvdfpyssa edmkksiekf lkipydkrvl pghgptttik
      181 kaqkflptwl eyl
//
LOCUS       WP_457563116             188 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Caminibacter
            pacificus].
ACCESSION   WP_457563116
VERSION     WP_457563116.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..188
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21754
     Region          7..161
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mnrfnkdait wddlprrvel akkvvqnvkp fvknkkvlef gcgtglvgin iadvtkelig
       61 idtsekmvek fnekakklkl nakafvknif eendkydaiv ssmtihhikd ikklskklye
      121 ltdtvfiadl vkedgtfhtr gnedvehfgf sidelknffs ewkmdykiih tikkhkdfdv
      181 flitlqkk
//
LOCUS       WP_457563119             438 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-glucose dehydrogenase family protein [Caminibacter pacificus].
ACCESSION   WP_457563119
VERSION     WP_457563119.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..438
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48866
     Region          1..421
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkisivglgy vgavcsaala neghqvigmd idkikvnlin egkspivekd ldvlieknvk
       61 egrlrattnl keaiensdit fiavgtpsre ngsidlkyik eaaksigevl kdkkdfhivv
      121 mrstvlpgtg revvipiiee nsgkkvgvdf gyasnpeflr estaiwdfyh ppktvigasd
      181 ektadtleel ysfidineap lfkteieiae mvkyadnswh avkvtfgnei gmicsrlgid
      241 shkvmkifvs dtklnispyy lipgfafggs clpkdvkait ykakevdekt pllnslmesn
      301 eyqikrvfnh fikplkkkkv gilglsfkag tddlrespil elteilivkg yfvkifdenv
      361 vkareegaak efletelhhi nerltdnlqe vidnseilii gnkdnrfkgl adkykdkfii
      421 dvaaiedris qgnyfriv
//
LOCUS       WP_457563126             488 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457563126
VERSION     WP_457563126.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..488
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=53810
     Region          2..480
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkprvvvlga gisghtaaln lkrklgnkge vivvspnsny qwvpsniwvg tghmkpedvy
       61 fplkpvydkm kidfkqakal sihpegdage nkpyvtieyv sgtdagkkek vyydflinat
      121 gpklnfeatp glgpdasgtv sicsynhadh awkelskvie kmkkgqkqki viglghggat
      181 cqgaaleytl nvaslikdlg ledmadiryi tnemfigdlg magayvknag yvahtkniis
      241 alfyeygvrw hhqssvykve pckiyyetyq geeltldydf amlippfsgv gitavgpnge
      301 dytdrlfkpn klmivdadye sakkpyhews gddwpkklqn ptypnifaig iafapphtis
      361 kphttpsgrp ltpapprtgm psavmghata mniaewileg kpsfrhkasm aeiasicvvs
      421 igygfrgiag smsvyptipd ynkypdfgrd inytigevgv aghwfkylmh hlflykakak
      481 pgwwlipd
//
LOCUS       WP_457563135             463 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein [Caminibacter pacificus].
ACCESSION   WP_457563135
VERSION     WP_457563135.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..463
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51207
     Region          2..243
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mktevkvglf iligllslly mtfqiktled fkqkgypvya ivndasgitk kskvklrgvs
       61 igyvdsmkll dngvklklli rkgvkipvgs eiavaqdnvl ggkylkiips nntaylqpkg
      121 vikkyvpsas medvltnink avgdvrella klnstinqqt idnihemitn lkissqrlnd
      181 ilattqtklp kildnanalv vsyketgdii krkipeilnk tdmllaklnk tgeilntklp
      241 kladeyinlg knanqllven kkglkntina asdffasgsk sfqklddmla smqksqiqvd
      301 ifsnymtrdd yfkttaniay mpnptkyyiv gvtstkdyst enpgdkdkiy fnaelgkryd
      361 nllirggiie stggvgadyf ldkdrvklsa diydfnsvnd irgnnpnlsl katylylkhl
      421 efiagvdnil nadartfflg vgvkfidndl ktiiagggts flk
//
LOCUS       WP_457563139             385 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563139
VERSION     WP_457563139.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..385
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44492
     Region          2..384
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 myfiyekdal grtifeivfk ntgsiyakda vaymtahiln tkgtldkkek fysqleekai
       61 nltittnkef stvsmtflne kssfavkkli ellqnpnftq ealekskkei lakkenlknn
      121 hdyiasknlf kaifkntple retigeniqn vtledikehf syfakenavf inggkkidia
      181 efietlpntk pkndlffkpk qshieekrev eqsyiyfaap fevkkeeyyl akiatfilga
      241 ggfgsrmmee irvkrgyays ayamnefkks yqilkghlqt klentidakn lvvdiinafl
      301 ekgitreeld sakkfligse plrnetlsqr llrkfneyyl glgdgyfeke lnliknttld
      361 eindfikrhk eiknlsfsvv tndkn
//
LOCUS       WP_457563149             239 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563149
VERSION     WP_457563149.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..239
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26464
     Region          1..234
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mnlslialsf vlvlipsiit yklnigieke ilknsirall qltalgfvlg flfkitnply
       61 yipvvlfmll ysayiakkrt eysykaafls ltlatsiilt ilislkiisl kpnefipiag
      121 miignalnty tltierlkre ielqreliea fiaigarysd alkimqrqai kaalipvnnm
      181 lqtigvvaip gittgmllag asplkavtyq iviiymlvsi nlfsslfgsf fyirekgay
//
LOCUS       WP_457563150             114 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Caminibacter pacificus].
ACCESSION   WP_457563150
VERSION     WP_457563150.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 114)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 114)
  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 114)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..114
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <10..110
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 hikhtnsadc eitinknafn svieniisna fkynkkggei kiymkdkkli iedtgigikn
       61 pqkvfnrfyk energigigm nivkklcdel kidikieset nrgtkvildl sryc
//
LOCUS       WP_457563157             362 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563157
VERSION     WP_457563157.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 362)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..362
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42133
     Region          113..362
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnlkhykiri tiflvlifvt ffaiflnyei nkktieclke nlakkiyilr knellthekd
       61 lakflknfnn atittkvqkp gykinddsvv svfrindkti iikdsikeei spllqlakin
      121 livisiislm ffgimflfid fllkrfkkvr niiahikqre feklppltpe knicdefrne
      181 iiklgreiet yikllslkve dykkkayide lthtfnrnfl keieskiflk akvssfptsv
      241 imididdfkk indtyghkkg devlthiaki lqnnlrkedi liryggeefl illnetelht
      301 alaiakklik avesnplnnl katisagvsk ieyndknlyd svkradsnly kakrngknrv
      361 ei
//
LOCUS       WP_457563165             291 aa            linear   BCT 27-JAN-2026
DEFINITION  patatin-like phospholipase family protein [Caminibacter pacificus].
ACCESSION   WP_457563165
VERSION     WP_457563165.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..291
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32665
     Region          1..268
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mnvslvlsgg aargytfigv veelqahgfk ftsisgtsmg sligaltacn klnkykewvm
       61 sldfidiltf lkppfnrldg dkifnkikel vgdykiedlp vkftavatdl tkkkevwfqk
      121 gdlwtavkas saipgvfepv vlnghvlvdg gvlnlmpvap amsdmsdlii ainanadpvf
      181 rkfdipkeir kkqnifeevw skifsekedv inqsinlmmd vifryrcaey rpdieikipk
      241 nlakwyefhk apelieigri larealedaq kqgiitlkke knaknihkks s
//
LOCUS       WP_457563167              53 aa            linear   BCT 27-JAN-2026
DEFINITION  P-II family nitrogen regulator, partial [Caminibacter pacificus].
ACCESSION   WP_457563167
VERSION     WP_457563167.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 53)
  AUTHORS   Huergo,L.F., Chandra,G. and Merrick,M.
  TITLE     P(II) signal transduction proteins: nitrogen regulation and beyond
  JOURNAL   FEMS Microbiol Rev 37 (2), 251-283 (2013)
   PUBMED   22861350
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..53
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..53
                     /product="P-II family nitrogen regulator"
                     /GO_function="GO:0030234 - enzyme regulator activity
                     [Evidence IEA]"
                     /GO_process="GO:0006808 - regulation of nitrogen
                     utilization [Evidence IEA]"
     Region          <1..53
                     /region_name="GlnK"
                     /note="Nitrogen regulatory protein PII [Signal
                     transduction mechanisms, Amino acid transport and
                     metabolism]; COG0347"
                     /db_xref="CDD:440116"
ORIGIN      
        1 kleifvnddf vektveiilt haktgkigdg kifilpveea irirtgergr dav
//
LOCUS       WP_457563169             292 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Caminibacter pacificus].
ACCESSION   WP_457563169
VERSION     WP_457563169.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..292
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32460
     Region          1..292
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mitvigiyif ivigffakri fkdeiegktl vilstyflqp fltlwgimlv plnfdliisp
       61 vvylgavfis liftallafl flkdkkekii asltplignt gnlgiplsya lfgdigasia
      121 tmvnlaniff iysfgifffa kgeysfkdaf kkivkipvmw fgilalilni ggvrfpadim
      181 kilqmgafas ivvqllifgi yvaeikakev sfklslvtii nkflvfplis fvllkfchlk
      241 pifhqavlle vltplavtnv nlaalfnlyp qkvaylvilt silfigvimi fl
//
LOCUS       WP_457563174             399 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Caminibacter pacificus].
ACCESSION   WP_457563174
VERSION     WP_457563174.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..399
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=47308
     Region          132..>399
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
ORIGIN      
        1 maflsknrfw flaffllfvv rcqisffeyl sfknhkflnv earvinqykk egknyqilkl
       61 knnsltfytt srenlknlln ekvkltiits kvsffeylft fyapsfnikl lsadkidlfi
      121 ekqhsssvmk nlfkalflge sidfstrqkl sslgvshlfa lsglhlgfis fvlyfvfspl
      181 ykifqkkfpy rnrffdlgil vlavefvyly ftsfpaslir ayvlevlifi famrfkelfs
      241 lnilfftilf sfliffskif sigfllsflg vfyiylffkh vkfsffssvf lsfymflvmf
      301 vwshyffgnf nyfqflsplv niifsffypl eiflhligfg gvfddfilky lslgsefyev
      361 kisfvwvvif gimsllaffs kylfyginll affivilai
//
LOCUS       WP_457563124             755 aa            linear   BCT 27-JAN-2026
DEFINITION  SEL1-like repeat protein [Caminibacter pacificus].
ACCESSION   WP_457563124
VERSION     WP_457563124.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 755)
  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 755)
  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 755)
  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 755)
  AUTHORS   Mittl,P.R. and Schneider-Brachert,W.
  TITLE     Sel1-like repeat proteins in signal transduction
  JOURNAL   Cell Signal 19 (1), 20-31 (2007)
   PUBMED   16870393
REFERENCE   5  (residues 1 to 755)
  AUTHORS   D'Andrea,L.D. and Regan,L.
  TITLE     TPR proteins: the versatile helix
  JOURNAL   Trends Biochem Sci 28 (12), 655-662 (2003)
   PUBMED   14659697
REFERENCE   6  (residues 1 to 755)
  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 18639778
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..755
                     /product="SEL1-like repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=88790
     Region          23..>225
                     /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          32..62
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          69..96
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          99..165
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          <422..>683
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          <549..>645
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          549..575
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          582..611
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          618..645
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mrifgflvga sliffigcad krlakvyykn gnyekayeey ykfakkgfpd asykiakliy
       61 lekiqkppyl erkyalnayr sgyadsalyi adsffrekny qealkwydki sfdkfrikdf
      121 enymtciesl dnikekvsyl dklnayakks nnpklqtilg kyylqetpfy npekgivllk
      181 kaydkgfyqa gvalgifyik ngkkqegyki lknvayqdkn aayylgnyly demvtkekll
      241 nsgcitcnfd tpedffvkkl tiykynnlft rrnvkkayei syklgnkkal yklirldied
      301 ntfeltpkty sgfdlkgavk flksqndves klvlaaiyek ylylnsykka keiynwyidi
      361 dkinaywhly qyekrfenki nlellsylve qrfvpaivem ayqmslqnkd vennkkvley
      421 yanqgnipal nclgslyske ilkpksrsif yfkkacnleq kpfyipeedl kianyynvml
      481 nkvnkdltin yyyaqmknrq aqlniskfyr khcnydklki wldklikead kkginyyyss
      541 vlekyidgdy ekalnalekd dslqsdlvla rvyangwyvd fdpkkaeeyy qkainkgykp
      601 ailniaalye kinvngkynn kivslyneai naglkdakir lakfyisqne kqkalkilrs
      661 mpnnpkanyl lyiltgriky asntetnygy lllakaevys kkaprialyy aframlcntp
      721 ktpkvaielm krinnarvid siykrakrap kcyln
//
LOCUS       WP_457563179             486 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563179
VERSION     WP_457563179.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 486)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..486
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56965
     Region          <212..481
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msqkrsksvf flvfliiimf lfsmiifvtf kkvekriskd tfdfllkevk sfsrnieryl
       61 llkygdllvv lnkkpllrsd vnlylssyit snfknvflay ydgkffrvig dgslnpkdrf
      121 dynerfeptr kdlwlkaikt kkpiyykqdi kgiwttyiyp vldnnlkvsy lividfstep
      181 lsyidnnlii lkkslflfis vlllsvlils ifllydisrq kkmqkllkel qilnktlesr
      241 vkeeveksre kdrqlimqsr lalmgellsm iahqwrqpln viggvvadme mdmmlnendp
      301 kktkenleti kkmikhlsst iddfrkfyrk dnekrvvsid eilkevlnia ssslknknik
      361 iinrlkcnrk lkiypnelkq vllnliknae dilverkidn pkivieifen ddkciievkd
      421 ngggvdekhk dkifepyftt knekngtglg lymsknivek rlggeiiqyn dnegavfriv
      481 lskdak
//
LOCUS       WP_457563182             262 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook-basal body protein [Caminibacter pacificus].
ACCESSION   WP_457563182
VERSION     WP_457563182.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Saijo-Hamano,Y., Matsunami,H., Namba,K. and Imada,K.
  TITLE     Architecture of the Bacterial Flagellar Distal Rod and Hook of
            Salmonella
  JOURNAL   Biomolecules 9 (7) (2019)
   PUBMED   31284631
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Dingwall,A., Garman,J.D. and Shapiro,L.
  TITLE     Organization and ordered expression of Caulobacter genes encoding
            flagellar basal body rod and ring proteins
  JOURNAL   J Mol Biol 228 (4), 1147-1162 (1992)
   PUBMED   1474584
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Zuberi,A.R., Ying,C., Bischoff,D.S. and Ordal,G.W.
  TITLE     Gene-protein relationships in the flagellar hook-basal body complex
            of Bacillus subtilis: sequences of the flgB, flgC, flgG, fliE and
            fliF genes
  JOURNAL   Gene 101 (1), 23-31 (1991)
   PUBMED   1905667
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Homma,M., Kutsukake,K., Hasebe,M., Iino,T. and Macnab,R.M.
  TITLE     FlgB, FlgC, FlgF and FlgG. A family of structurally related
            proteins in the flagellar basal body of Salmonella typhimurium
  JOURNAL   J Mol Biol 211 (2), 465-477 (1990)
   PUBMED   2129540
  REMARK    Erratum:[J Mol Biol 1990 Sep 20;215(2):331]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..262
                     /product="flagellar hook-basal body protein"
                     /GO_component="GO:0009425 - bacterial-type flagellum basal
                     body [Evidence IEA]"
                     /GO_process="GO:0071973 - bacterial-type
                     flagellum-dependent cell motility [Evidence IEA]"
                     /calculated_mol_wt=29653
     Region          5..258
                     /region_name="FlgG"
                     /note="Flagellar basal body rod protein FlgG [Cell
                     motility]; COG4786"
                     /db_xref="CDD:443816"
ORIGIN      
        1 mingyydvtg amvtqfnrln visnnlanvn tpgfkqddii igdferlfse krselplenn
       61 tkeaakwinh nlnkvpqive eytnfslgdm qrtsnpldia lkrknlffti saqdgeritr
      121 agnfelddkg ylvtkegfkv lntknqpiki plnaknlvid sdaniyvnnq kiatlkivsi
      181 dnpktlkkvg dkmwefvpgs esintknstl qgfleksnvn piremtdlie tnrlveryqk
      241 amttfmddlq kdaieklgsv ra
//
LOCUS       WP_457563184             292 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Caminibacter pacificus].
ACCESSION   WP_457563184
VERSION     WP_457563184.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..292
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=32826
     Region          148..285
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mkkiilgsmi aagalfafpg mmggamkgna altgkplpgl kdstvlaeln gkkitvkdvn
       61 aylqgitgdn rirlqdlpaq hvkqfvqqyv emleiynska kditktpqyq aaakklavdm
      121 wlknqlqtik isdkearafy eknkdiyfkt tpkikarhiv vkdektaeki inelkglhgk
      181 aleekfaela kkysigpskv qggelgyfdp kqmvpafaka ceelkpgqmt lkpvktrfgy
      241 hvilvedkkd nnylpyeqvk mqiieylkrv klkdelqkik dsskvkymip ks
//
LOCUS       WP_457563187             276 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 1 family protein [Caminibacter pacificus].
ACCESSION   WP_457563187
VERSION     WP_457563187.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..276
                     /product="complex I subunit 1 family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31170
     Region          4..273
                     /region_name="NADHdh"
                     /note="NADH dehydrogenase; pfam00146"
                     /db_xref="CDD:459690"
ORIGIN      
        1 misailtvla pvfggfvygi erivkarmqr rvgppllqpf ydffklmdkr plmihslhal
       61 mgimyfvaew falavlllgn dlliavffhv iavlalviga ssvrspysvl galrelmhmi
      121 syeplmvlmv vsfylivgsf dirdilsyqg ypileiplvf vaflltipmm lqkspfdiae
      181 ahqeiiggpe ieysgpfyea lytgkwieyi yvftfvflfg gnhywlgall vvgvfilinl
      241 idnstarldf rkmvkfawgi lipmaalnvi llalwq
//
LOCUS       WP_457563188             360 aa            linear   BCT 27-JAN-2026
DEFINITION  hydrogenase large subunit [Caminibacter pacificus].
ACCESSION   WP_457563188
VERSION     WP_457563188.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Friedrich,T. and Weiss,H.
  TITLE     Modular evolution of the respiratory NADH:ubiquinone oxidoreductase
            and the origin of its modules
  JOURNAL   J Theor Biol 187 (4), 529-540 (1997)
   PUBMED   9299297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461653
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..360
                     /product="hydrogenase large subunit"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=40684
     Region          <1..360
                     /region_name="HycE2"
                     /note="Ni,Fe-hydrogenase III large subunit [Energy
                     production and conversion]; COG3261"
                     /db_xref="CDD:442492"
ORIGIN      
        1 mgkivvpfgs qhvalpepis flfdteneii tkveahigyv hrgiekaait rfeytqlpyl
       61 tarvcglcsi thagavvhgi eklmdievnk ridylrmlvv eldrihshml anghvaevvg
      121 yenlfmqtfr aredvmdvle ritgnrvqyd yqtiggvard idletakfak kklkklkdnv
      181 lkvmefhdsd ytfglktkgi gviskemaak yntagpiara sgletdvrae fdylpfeevg
      241 ykmqlrhegd vwarnmvrfd evlnsiemce nildnlpege hqvkvkgrpk getvvrveap
      301 rgecfyylka sgkkvmdrvr irvptyanip ilkelflgak ysdaqaivls fdpcmsctar
//
LOCUS       WP_457563200             404 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Caminibacter pacificus].
ACCESSION   WP_457563200
VERSION     WP_457563200.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..404
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44496
     Region          7..396
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mkinspkdlp ikrgdrvfvr cdfnvpldef gnitddrrir malptikyll dndckivias
       61 hlgrpkgefn ekfslkpvak rlshllkqdv imakdvvgsd akekaanlke gevlllenvr
      121 fdsretknde gfakelsefg dfyindafgv shrahasvea itrfydscrk aggflllkei
      181 nffhkllenp vrpfvavvgg skvsgklqal vnllpkvdkm vigggmaftf lkamgynvgn
      241 slveddlide alkimaeakr lgvkfylpvd iviadkfaed amvkyvtyqe ipdgwmgldi
      301 gpatvrlfge vlwdaqtilw ngpmgvyemd kfsrgtfkis heiarshgik vvgggdtada
      361 vqragddeem tfistgggas lellegkklp gvaaleipde vscq
//
LOCUS       WP_457563212             216 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457563212
VERSION     WP_457563212.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 216)
  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 216)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..216
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25121
     Region          3..206
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mniliveddy dlhdtikdfl elqgfkcdsa fdgqsaveki yekdfdvvil dvklpemngf
       61 evakrvrefs kvpiifltsl dgekdveegf lsggddyirk pfslkelklr idaiikrvyg
      121 dservkirdf efdlknmtly kdgkevhlkp khakllkffi knknqvvskd eifnaiydyd
      181 eevnenslrv fikdlrnilg kdsietlkdr gyrfvg
//
LOCUS       WP_457563213             117 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamylcyclotransferase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563213
VERSION     WP_457563213.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Oakley,A.J., Coggan,M. and Board,P.G.
  TITLE     Identification and characterization of gamma-glutamylamine
            cyclotransferase, an enzyme responsible for
            gamma-glutamyl-epsilon-lysine catabolism
  JOURNAL   J Biol Chem 285 (13), 9642-9648 (2010)
   PUBMED   20110353
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Oakley,A.J., Yamada,T., Liu,D., Coggan,M., Clark,A.G. and
            Board,P.G.
  TITLE     The identification and structural characterization of C7orf24 as
            gamma-glutamyl cyclotransferase. An essential enzyme in the
            gamma-glutamyl cycle
  JOURNAL   J Biol Chem 283 (32), 22031-22042 (2008)
   PUBMED   18515354
  REMARK    Erratum:[J Biol Chem. 2008 Nov 14;283(46):32152]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..117
                     /product="gamma-glutamylcyclotransferase family protein"
                     /EC_number="4.3.2.8"
                     /GO_function="GO:0061929 -
                     gamma-glutamylaminecyclotransferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13673
     Region          1..107
                     /region_name="YtfP"
                     /note="Predicted gamma-glutamylamine cyclotransferase
                     YtfP, GGCT/AIG2-like family [Amino acid transport and
                     metabolism]; COG2105"
                     /db_xref="CDD:441708"
ORIGIN      
        1 mivfvygslk rgkrlhsylk nakflgegvt crpyplivsk sgwypyliek nggykikgev
       61 ykitpkllki ldkieespny yyrkkicvki ngktvkawty fvrkppkftk kelikef
//
LOCUS       WP_457563214             264 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Caminibacter
            pacificus].
ACCESSION   WP_457563214
VERSION     WP_457563214.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..264
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30227
     Region          16..260
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mneikaaaka ikeakyllit agagmgvdsg lpdfrgdegf wraypiakkl glnfqalanp
       61 rwfdinprla wafyghrlnl yrsttphegf killnmpqek fvftsnvdgq fqkagfsenk
      121 iveihgsihy lqctepcsde iwenneiiei dmekfealnf pyckecgkia rpnilmfgdf
      181 rfvenrvdrq lenfnrwlsk iddklvivei gagkavptvr hmserirdmy kaklirinpr
      241 esdgadieik kgakevltmi sqyl
//
LOCUS       WP_457563221            1020 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caminibacter pacificus].
ACCESSION   WP_457563221
VERSION     WP_457563221.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..1020
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113507
     Region          1..1008
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfeffykrgy lltaiilgmf vfgviglikm pknlfpdanr pevviftqvp gatasvvatt
       61 vskpieeema tlsnvyqiks tnvanfsivh vvfgytktlq qasvdvsnal nrikdklpkn
      121 sipaiylvgd ftapvdvfal spknnsitlp eikkiathfi kpkllsnpni gnvevfggyd
      181 savmvkidpl klkkygisfd dlikiiqttd lnmpigfvkt knsfitlsfy gekddvkklk
      241 nllikpnvrl kdiadiswsy qtnntlyign napsiaisvq rapsgsvlat sdaareemkk
      301 ieklypnikv tisdtqrnli etsninmlea lrdaiiftli vlliflanfr alvaaalsip
      361 mvffgtiayl yltgqglniv iytaiilalg mltddavvvl enierhlenk edlqkaiyeg
      421 tkevlkpifa gsvstiaiif plmfvggype kifkplietl ivalliswfl svtfipklst
      481 llykkgfkkt kveiffekly qntiarlikp yvgilhfsng kfyvlrrmll mmgamivlml
      541 svknimpiig rdvmppmdtg imkahiefss nlnaeesekr lkpfltwlnk qpwlekssia
      601 igtqkdvlsi tgggggnsin mtiiaidrfh rkktiwqled evrnelakip gikkigvydf
      661 gatalstina pldvrvlsdt ykqlpkeaqk iekllynvkg lttimktwdk dfnevvikid
      721 tnkalsygit pagiayqial kdmpvamltn lssmnvqfvr vrfnkqfeni ealkllpidt
      781 kkgpiplgei aqikndftys kidrynlrya idvegyrktr pvslitddad kllkehgikn
      841 ykqagdisem ndsfgrlika iavgvvilil tlmvvyqslr lalimivvlp lsmigaswal
      901 liankpscmp smvgllllfg iiiknavlli dfykefehsg kspfeaaies vkvrfrpvmm
      961 tafgtiagmi pialewavgl erlspiadva iggllvgtfl tlvyvpmlay atdprnkkds
//
LOCUS       WP_457563222             356 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caminibacter
            pacificus].
ACCESSION   WP_457563222
VERSION     WP_457563222.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39560
     Region          48..356
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkvlkivipi iiaialafgg yrliklkkea dakektatly pivvkmykpe ykevtltlpa
       61 vaevknsnev aiatkfpgki lyiknlgekv kkgdllvkid dselksqlnt idskiaslkd
      121 kinaqkisle nlikthirtk kllevkmasi eqyqneeski atlkaaikad enslkslysq
      181 kqsildnlky ttiyantngv vsaklfnkgd iapmlkpilk itpnsgnyll vllpkeekai
      241 iykekeypli plkstingik aykaevedkn llpgekvnvk vvtfqgkgtf lpfntiltie
      301 nknyiftpkt keihikasgv egvvieekid tpviqaepdi llkikagypi kvenkg
//
LOCUS       WP_457563223             420 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457563223
VERSION     WP_457563223.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..420
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47328
     Region          122..413
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkklslvlia aslyaadigt lfdaikkqpe tkidnlqvkn akiakksvin slyptvnifs
       61 saehynapfs lrpvtptqsa yllktnasip fsqniirvgf dvsmplfikt iydnkekmsh
      121 iinaakykak lnllqresml viylsnlnyl yslkkallvq knsiqesika ievgvkvgri
      181 pefkllrlkd avnqidikin didskiadtn skiytltkih lkkpinfqts svkkeeflav
      241 kpikenikas lldikakkdd flpkvffkis anrgfgwayn tkdsvalnta sagiyinwni
      301 fnkkrnsevq kakieymnsk ltlqktikel tsqiekidkt lkivnrslsl akksvkikee
      361 llksakvafk lgtmtvdeyl nyendlalak anvanlkatk nsliaqkafi ygnnfkkvfk
//
LOCUS       WP_457563226             540 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC1 kinase family protein [Caminibacter pacificus].
ACCESSION   WP_457563226
VERSION     WP_457563226.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..540
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=62276
     Region          4..456
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mfknslyelk rtkeiifvla kygfgdiies lgipvsfket pklsrserir kaieelgptf
       61 iklaqllslr pdlvpldlak efeklqdsvt plpfeemkrv ledefekpyt eifeedfell
      121 asasigqvyk arlktgeiva vkilkpdiee kiyadiailq rlakllrdrf liygvdleki
      181 veefaksikk eldfniealn lkrfannfrn nsdikvpkly ekysskrvlt mefiegikis
      241 didtlkkagy dlkeitkkgf dliceqifih rffhadphpg nlmvsngkiv fldfgimgrl
      301 sdedrqyfve miyyvikqqe ekaalyvlkl skvqgeidis sfkkemadii ssyfysslkq
      361 velraliedm lkvmqrykiy fkednyllak alvtmegigk klypefnaae eikpfiikiy
      421 kqtispfnil krsheinkav mefitqapsd lneiigklkr gelkvefehv gleefeeaie
      481 ksfnrlstsi iiaslligss mllsshippl fknislfgii gfifasilgv iliftvlrkk
//
LOCUS       WP_457563229             174 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caminibacter pacificus].
ACCESSION   WP_457563229
VERSION     WP_457563229.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 174)
  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 174)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..174
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20407
     Region          8..173
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 maieylehyt ykdyekwegd welingypya mspfalpshq risgkifrel desldncnec
       61 faliesevkf sedtvvrpdv lvkcgeiddi titpeiifev viensirrde ivkfdlykke
      121 gvmyyglvyp nekrvkiykl ingeyikisd lrngifktdd ltcdikvdfs kvwl
//
LOCUS       WP_457563238              76 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Caminibacter pacificus].
ACCESSION   WP_457563238
VERSION     WP_457563238.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..76
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8554
     Region          <20..72
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkkvviflgv mlfakdfvfc tschngrkev klstltkqei vkklhefkns kkgtmsyiak
       61 glsekdikkv aekygk
//
LOCUS       WP_457563181             268 aa            linear   BCT 27-JAN-2026
DEFINITION  respiratory chain complex I subunit 1 family protein, partial
            [Caminibacter pacificus].
ACCESSION   WP_457563181
VERSION     WP_457563181.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 268)
  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   3  (residues 1 to 268)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Schneider,D., Pohl,T., Walter,J., Dorner,K., Kohlstadt,M.,
            Berger,A., Spehr,V. and Friedrich,T.
  TITLE     Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Biochim Biophys Acta 1777 (7-8), 735-739 (2008)
   PUBMED   18394423
REFERENCE   6  (residues 1 to 268)
  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   7  (residues 1 to 268)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Weidner,U., Geier,S., Ptock,A., Friedrich,T., Leif,H. and Weiss,H.
  TITLE     The gene locus of the proton-translocating NADH: ubiquinone
            oxidoreductase in Escherichia coli. Organization of the 14 genes
            and relationship between the derived proteins and subunits of
            mitochondrial complex I
  JOURNAL   J Mol Biol 233 (1), 109-122 (1993)
   PUBMED   7690854
REFERENCE   9  (residues 1 to 268)
  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
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Weiss,H., Friedrich,T., Hofhaus,G. and Preis,D.
  TITLE     The respiratory-chain NADH dehydrogenase (complex I) of
            mitochondria
  JOURNAL   Eur J Biochem 197 (3), 563-576 (1991)
   PUBMED   2029890
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..268
                     /product="respiratory chain complex I subunit 1 family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
     Region          1..265
                     /region_name="HyfC"
                     /note="Formate hydrogenlyase subunit HyfC [Energy
                     production and conversion]; COG0650"
                     /db_xref="CDD:440415"
ORIGIN      
        1 qpyidfakli hkelvyakes sqisriavfm ilapivvvvf lmppvfhgsf yislidafti
       61 tgllslstff lmllgldsas afggigssre afisalvepa miltifsisl igqsigiska
      121 vlnlndyfdi nhaasfvlaa isffiiliae ngripvdnpe thleltmvhe amilestgad
      181 laliemasal kfaifatlfv slflpfgvnl cwclavtvfi lklilvsvav alievntakl
      241 rlfkvpnllg iaiifgflsl fiyyvvge
//
LOCUS       WP_457563241             254 aa            linear   BCT 27-JAN-2026
DEFINITION  inositol monophosphatase family protein [Caminibacter pacificus].
ACCESSION   WP_457563241
VERSION     WP_457563241.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..254
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28864
     Region          1..241
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(29,33,39,60..61,75..80,205..206)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(32,34,81..82,84..89,141..143,145,147..148,157..158,
                     161,164..165,169,174..180,188,192..195)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mfektiqivk eageiskegy ykdkeivlkg kkdlvteydi kveeflkekl kpfntnfiae
       61 esiynekihk tfiidpidgt tnyahqvphc aisvayyenn revfgivynp ilnelfyakk
      121 gegaylngkk ievsknecfq raliatgfpy ssaeneadlk wvisklnkvl prcqdirrlg
      181 saaldlcyva cgryegfyei nlkpwdvaag kiivqeagge vsnnfgesyn ifedrcivat
      241 nmkihrelvn lleg
//
LOCUS       WP_457563244             268 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit, partial
            [Caminibacter pacificus].
ACCESSION   WP_457563244
VERSION     WP_457563244.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..268
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..>248
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 gtvekvyvqn gskvkpgdki lklstksldl dieklktdik ntqkeiseak kayynyasln
       61 itkkelkkma llhskgyase fevdnykkny lneltnienq kkslktqiln ltstlenqki
      121 elkklllqkq kanavspvyg fvanlsvspt qeitanqkic eilnidtikv kaglppgllp
      181 fvkvgqrvri dfitepqyst yakitkinpi vdkkfqnmti eievknknyl iqpqtralim
      241 iflspkdqek vkklteskgg iieipsdi
//
LOCUS       WP_457563246             320 aa            linear   BCT 27-JAN-2026
DEFINITION  DHH family phosphoesterase [Caminibacter pacificus].
ACCESSION   WP_457563246
VERSION     WP_457563246.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..320
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35593
     Region          6..312
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mqelfkkawe kikeaknivl vshinpdgda lgsslslypi lkrmgknvkv fnvtkplpqy
       61 ldflpnfdkv tdklpknvdl misfdcgsfd rlgidekppf linidhhisn teygdiniid
      121 pkaastsqvv femlktngve idedsatciy talvtdtgsf qyesvnekvf qtaaelvkcg
      181 akpdfvakml fqrdrlsrlr llakaydtie lccegkvafv evtkemmeit gaikddtdti
      241 vnsvraiasv evacmlredd dgikislrsk nyadvskvav kygggghira agatikdefd
      301 fnkvknmlke dlkeivkvee
//
LOCUS       WP_457563247             445 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563247
VERSION     WP_457563247.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..445
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50081
     Region          <299..426
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkklwilill liigaggfvy fspmfeknpp kitiktdgyt nlknpievdl kddsgiksyt
       61 vvlmngnnte viasadnpnm gknvtlkikl pknikaneir lvvtavdtsk whffagneaq
      121 ksvtlevdkv apdaqvvnns yaigrggsaa avvqvndknl kdayilvdgk ykfkltpfyk
      181 kgyyvaliaw piwennfdat lvaedyagni vrehipyywr trgiynpkdv kirindkfin
      241 qvakrlleri gmsipndpve ifkkvnetvr kineakisqi tspvyeekin sfyirrfnpl
      301 pgsakradfg ekrhyyfkge qisfaihkgv dlakikraki yannngrvva neyigiygna
      361 liiyhglgly tlyghtsefk vkkgdsvhng mviartgatg avfgdhlhfg vyvqgipvqp
      421 lewmdshwik tnilnvinga krmik
//
LOCUS       WP_457563259             263 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Caminibacter pacificus].
ACCESSION   WP_457563259
VERSION     WP_457563259.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 263)
  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 263)
  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..263
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..263
                     /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=30522
     Region          2..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mkiayksdih ldfwvkeknr nkikdfikni lfpktadvli iagdlghdnl qnalfleeik
       61 kyygvvlvtf gnhdlyllde eslnkyktsh arlselkeyi rfiegvyfld gdiadvagik
      121 ilgaggwydf syavrhgisl evirgqwevi msdakyihpk idpptfssfe kekirsfiyd
      181 adivfthvpp lyikcfddvl mnsfytfygy dlfannvkyw ifghchqahd fyydtvrflc
      241 splgypvgrr gefgirnlnl egl
//
LOCUS       WP_457563264             250 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD-IIA family hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563264
VERSION     WP_457563264.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..250
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28539
     Region          1..239
                     /region_name="NagD"
                     /note="Ribonucleotide monophosphatase NagD, HAD
                     superfamily [Nucleotide transport and metabolism];
                     COG0647"
                     /db_xref="CDD:440412"
ORIGIN      
        1 mrgyfidiqg tliddknflp lpgaveflky lnskkipfil ltnntkrdsk efidylknlg
       61 fefenyldpl mvlddyikgk kiapygnekf velmkkyeid fknpdavvlg iklfsneefa
      121 diiemllrgs eligmhktsl yskgdkrypg lgailemlky avnkdykvvg kpsatffnra
      181 keilgldydk itiisddlyg dllpakdlgm ksvlvlsgki kspeeitkkp deiyknledy
      241 lrngvinert
//
LOCUS       WP_457563266             395 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563266
VERSION     WP_457563266.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 395)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46301
     Region          <138..381
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mtyiysmidk nnsvyflass ltqkdikngd iyaymqkype atetlknvfk ngkiafeesk
       61 drwgyfrsil ipidskygry vigadlkisd ikksfdeyki klflilglvd ifalmiaffy
      121 yrlvkeekkh leeicslnek leemnknlek rvkeesekri kqeelilres kyiqmgemmd
      181 avahqwkvpl saimlesgll kmiiekkgci ddeieksinn iqeyvnhlne tldnfrnfvn
      241 tknyeeflis evvesvknlv kdlliinnvr letqiknfki ygrkndfehi llslidnsik
      301 ifnqrniner vikikakdye iiyednaggf egdiekifdf nysktggsgi glyivkmild
      361 kyggdikaqn ikngirfiin lkkfrynsns kkike
//
LOCUS       WP_457563270             309 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA dihydrouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457563270
VERSION     WP_457563270.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..309
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=34750
     Region          10..306
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mststhksak yflaplagyt dlpfrsvvkk fgcdmtfsem invnaiaynn ektkkmmqks
       61 pletpyfiqv aannvenaik aveiinemee vdgidinlgc pvnkarrsgf ggvllkdenk
      121 eklkeivcai vktskkpvsa kmrlgfdeiv avdrakmled lgiefltvhg rtvkqmykgh
      181 anyeeikkvv eavnipvian vdvtdyekak fvleytgavg vaigrgavgk pwiflemkqq
      241 gditpqqkke vilehfdqmi ywygeygvil frkhahaysk giakasefrs kinevkdtkt
      301 arelieeyf
//
LOCUS       WP_457563277             253 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457563277
VERSION     WP_457563277.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27539
     Region          29..250
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mhtyvftlis gllsglalgl tggggsilav pllvylvgii nihlaivtsl iavgatslis
       61 sitymkqnlv rfkvaflmaa pgilstflgs linkklnghl llimfsflmf yigfrmlkkr
      121 nienvksdtq nilkilffgf ivgflsglfg vgggfllvpa lylgvnlsmk eavgtslfii
      181 fmyglfgmts yivekreidf lisaifvlgg vfggfigayi gehinqeklr kifayftmam
      241 avfiflenig yfi
//
LOCUS       WP_457563278             271 aa            linear   BCT 27-JAN-2026
DEFINITION  M90 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563278
VERSION     WP_457563278.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Xu,Q., Gohler,A.K., Kosfeld,A., Carlton,D., Chiu,H.J., Klock,H.E.,
            Knuth,M.W., Miller,M.D., Elsliger,M.A., Deacon,A.M., Godzik,A.,
            Lesley,S.A., Jahreis,K. and Wilson,I.A.
  TITLE     The structure of Mlc titration factor A (MtfA/YeeI) reveals a
            prototypical zinc metallopeptidase related to anthrax lethal factor
  JOURNAL   J Bacteriol 194 (11), 2987-2999 (2012)
   PUBMED   22467785
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Gohler,A.K., Staab,A., Gabor,E., Homann,K., Klang,E., Kosfeld,A.,
            Muus,J.E., Wulftange,J.S. and Jahreis,K.
  TITLE     Characterization of MtfA, a novel regulatory output signal protein
            of the glucose-phosphotransferase system in Escherichia coli K-12
  JOURNAL   J Bacteriol 194 (5), 1024-1035 (2012)
   PUBMED   22178967
REFERENCE   3  (residues 1 to 271)
  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 271)
  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 10007100
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..271
                     /product="M90 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32300
     Region          25..267
                     /region_name="MtfA"
                     /note="Mlc titration factor MtfA, regulates ptsG
                     expression [Signal transduction mechanisms]; COG3228"
                     /db_xref="CDD:442461"
ORIGIN      
        1 mdnfknflll lwgaffvfii fqiisyfryl qklkklkstp fpknlkkyie nlpqyqklne
       61 kqkrilgyki qrflleknfi hvninlndei ktliafyacl psiayidfcy pnlkniyiyp
      121 hpvilknlqn gyvvqeeeii egeatgenvi iawdeakkei hhpnfrnvii hefahqldaa
      181 dgvidgippi etskynewvk imfgeykkfk qktlknrflg kfslidkyaa tneaeffavm
      241 seyyfmkpqi lkkhfpdiyk elknfykief i
//
LOCUS       WP_457563281             757 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent Clp protease ATP-binding subunit, partial
            [Caminibacter pacificus].
ACCESSION   WP_457563281
VERSION     WP_457563281.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>757
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          5..757
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 meklfekltn qmmeaiesgl slalhnknpe vhplhvlwgl ltntntvlnq alnkmgvdkv
       61 aielevksav drlpkvdnit kesirigrel iqslqnaeal atrmgdkfia vdtwlmanld
      121 mfkdtlgkfv dlmelkktle airgdkkies ksadenldal nkygidltek arkgeldpvi
      181 grdeeinrmt qilirktknn pillgepgvg ktalveglaq rivkkevpts lqnkkivald
      241 mtaliagaky rgefedrlka vvdevksnpn iilfideiht ivgagasegs mdaanilkpa
      301 largelrtig attlkeyrky fekdaalqrr fqpvkvdeps vneairilrg lrerleahhh
      361 vlikdeaiva avkltdryik drflpdkaid aideaaaeir mqiesepfel akikreieql
      421 mvekealqle lesagnkeki qkrieeieke lanleeekrk leakfeeekr vlkkiaeike
      481 qieklkneae iakregnfhk aaeieygkiv elrkeleele kkweemqkqg tllknavdee
      541 avadvvskwt gipvnkmlqs elekilhied elkkwvvgqd eavaavarai krnkaglgdp
      601 nrpigsfmfl gptgvgktet aktlarflfd dekalirfdm seymdkisvs kligaapgyv
      661 gyeeggqlte avrrkpysvi lfdeiekahp dvfnillqvl ddgrltdnkg vtvdfkntii
      721 iltsniasdi imeikdpnar keavwaelkr rmkpefl
//
LOCUS       WP_457563285             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563285
VERSION     WP_457563285.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30175
     Region          20..276
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 meaktlpllk erlnghlpke geivipelia kglklkkgdv vvlvatnkng smnaktfkis
       61 gvvgiisgpg grdgyinikd arkllrikkp einemviklk npellekvnk eligftktiq
      121 kpklevhawi klspfaniik mldimtfsie iilisivlvs ilnvmimsvf erikqigtmk
      181 amgtsksfiv smfvneglll gifgfiigva asvafvylig dihynfgrqs nlllvphidy
      241 ksvlsvgamv viiaiiasly pafkaaslkp iealrs
//
LOCUS       WP_457563287             223 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563287
VERSION     WP_457563287.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..223
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25025
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mvkltnvhks yksgeievkv legldlyiqk gefvaligps gsgkttilni igaldkadsg
       61 nvevagvdit nrdekeltrf raehlgyifq dfnlievfsv fenvnfplkv ihkrkddekv
      121 kalledigms dqinkfpdql sggqkqrvav aralvtdpli vladeptanl dsvtshkvie
      181 lmrkmqrefn ttfifsthdt hlidevdrvl ylqdgkiikd erk
//
LOCUS       WP_457563288             230 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Caminibacter pacificus].
ACCESSION   WP_457563288
VERSION     WP_457563288.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 230)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 230)
  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 230)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>230
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <117..>230
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnyekkflis sflvifsilf vfilyinyns ynlqvgflnn ktkkeliics ykmncpktdi
       61 nfipknkkpk peilklqedk nsffmvfdvp ylkkyylkls iskteylnal kkikenifrq
      121 fivelafili fsliltyily kplkeaykin etfikdilhd lntpltslkl niyllkkeig
      181 enqrikkleq nikailnyqe nlknflsnnp nqvetfnikd lideklsfys
//
LOCUS       WP_457563296             284 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Caminibacter pacificus].
ACCESSION   WP_457563296
VERSION     WP_457563296.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 284)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..284
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..278
                     /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 iamyeakhrg rnkyvifntd vkekiskeyt iktmlqkaie ngefelfyqp kldrnkrvvg
       61 cealirwirn gkvvppgefi pvaeksgliy eigkwviees akrvkewesd dilkeislaf
      121 nvsvvqmrre gflndireii kninpniskl eveitesvfi enkqralhll ellkrmgfki
      181 nlddfgtgys sisvlkefki dvlkidksfv devlskegrv yvktiidmsk nlnlltvaeg
      241 veyqeqfevl kelgvdyfqg ylfakplrke efeefvkkln tsdf
//
LOCUS       WP_457563300             209 aa            linear   BCT 27-JAN-2026
DEFINITION  7-carboxy-7-deazaguanine synthase QueE, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563300
VERSION     WP_457563300.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Bruender,N.A., Grell,T.A., Dowling,D.P., McCarty,R.M., Drennan,C.L.
            and Bandarian,V.
  TITLE     7-Carboxy-7-deazaguanine Synthase: A Radical
            S-Adenosyl-l-methionine Enzyme with Polar Tendencies
  JOURNAL   J Am Chem Soc 139 (5), 1912-1920 (2017)
   PUBMED   28045519
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Dowling,D.P., Bruender,N.A., Young,A.P., McCarty,R.M., Bandarian,V.
            and Drennan,C.L.
  TITLE     Radical SAM enzyme QueE defines a new minimal core fold and
            metal-dependent mechanism
  JOURNAL   Nat Chem Biol 10 (2), 106-112 (2014)
   PUBMED   24362703
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..209
                     /product="7-carboxy-7-deazaguanine synthase QueE"
                     /EC_number="4.3.99.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016840 - carbon-nitrogen lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          1..202
                     /region_name="QueE"
                     /note="Organic radical activating enzyme NrdG/QueE
                     [Coenzyme transport and metabolism]; COG0602"
                     /db_xref="CDD:440367"
ORIGIN      
        1 tpsvfvrvgg cnlrcpgfgd kgcdsyyavd kryqkewelk siedikteik kylkfdphlv
       61 itggeptlyf kelypliewf egqitretna tididfekfp ayknvafams vklsnsgeey
      121 nkrvkknvik syaknaqksf fkfvidkdlk keieditkni dlpiycmplg atkeelekna
      181 pfvfefclkn gyrysdrihi rlfgkkkgv
//
LOCUS       WP_457563302             277 aa            linear   BCT 27-JAN-2026
DEFINITION  CvfB family protein [Caminibacter pacificus].
ACCESSION   WP_457563302
VERSION     WP_457563302.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Matsumoto,Y., Xu,Q., Miyazaki,S., Kaito,C., Farr,C.L.,
            Axelrod,H.L., Chiu,H.J., Klock,H.E., Knuth,M.W., Miller,M.D.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A., Sekimizu,K. and
            Wilson,I.A.
  TITLE     Structure of a virulence regulatory factor CvfB reveals a novel
            winged helix RNA binding module
  JOURNAL   Structure 18 (4), 537-547 (2010)
   PUBMED   20399190
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Matsumoto,Y., Kaito,C., Morishita,D., Kurokawa,K. and Sekimizu,K.
  TITLE     Regulation of exoprotein gene expression by the Staphylococcus
            aureus cvfB gene
  JOURNAL   Infect Immun 75 (4), 1964-1972 (2007)
   PUBMED   17283102
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Bycroft,M., Hubbard,T.J., Proctor,M., Freund,S.M. and Murzin,A.G.
  TITLE     The solution structure of the S1 RNA binding domain: a member of an
            ancient nucleic acid-binding fold
  JOURNAL   Cell 88 (2), 235-242 (1997)
   PUBMED   9008164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..277
                     /product="CvfB family protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31779
     Region          16..276
                     /region_name="CvfB"
                     /note="Predicted RNA-binding protein YitL, contains S1
                     domains, virulence factor B family [General function
                     prediction only]; COG2996"
                     /db_xref="CDD:442235"
ORIGIN      
        1 mieeylklgs qnklkiskkt pqglyleale gdkvllpnry vtddmkigde ievfiyndse
       61 dryvattdkp kyeygefgvf rvvdvtkfgv fvewgmpkdl fmplanmkke lkkgdsvigk
      121 ivydektdrl mldsklsrhi nkaknydvnd evkiiviakt plgykcivdn kyegmlfdne
      181 ifedvrvgqk kkafvknvra dgkldlslqk igsrddvldk vyeklkeiks inlttksnpe
      241 dikkvfgisk kafkyaintl lkeekivqen gsikikf
//
LOCUS       WP_457563309             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease subunit [Caminibacter pacificus].
ACCESSION   WP_457563309
VERSION     WP_457563309.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=22278
     Region          27..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 mdiinylndh ldltilaaiv iafvlslipk idypiekltn ffmiisvial isltllvsyd
       61 viarklfhgg sialqelewh lfdivflfai aytlskdkhv rvdifydnfp fklkktinli
      121 tilffvipls vliiveaipf vqmsyaqhes sgdpgglccr wiiksamiwa favvylqsia
      181 elrkiyyqlk hhkge
//
LOCUS       WP_457563320             367 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563320
VERSION     WP_457563320.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>367
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          237..367
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(269,312)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(274,277..278,282,286,308,310..313)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(304,332)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mriktfifll nlgivgvlsl fiyfiyteqq sktvaviien ikkdlqdssy iaskilnknn
       61 dvyflrpvld rkvakndlir gfvladgnkk lfvsgdvdlk vpennvkkni nditlkdlle
      121 kkafvipikf ykqnkqkvyd lyvfldkdkl ksmfvdlkvk ylvfyfmiis aiffilnymv
      181 qyylinpllr lklyaekkdf epkfipikei ndiknaltqs fkeldtiinn lykssitdfl
      241 tglgnkklll kevekrikkg qkfcllfldl dnfkeindfy ghsvgdalii evanelkkfi
      301 hsdelitrig gdefvlllnd cdtlklnkrl nellkrldkk wiirnyelst sasvgvaiyp
      361 hdgksfd
//
LOCUS       WP_457563327             417 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Caminibacter pacificus].
ACCESSION   WP_457563327
VERSION     WP_457563327.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 417)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..417
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45954
     Region          20..416
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 mvkvgivgvg tvgvsvvknl eknreiiksr agkeikvvkg vvrdpnkkrd vnielvtdyk
       61 evtrdpqidi vvelmggvdk ayevvkdaln hgkavvtank allayhrfel qkiantpfey
      121 easvaggipv ikalrdglsa nhieeikgii ngtcnyilte mkkgrdyeev lkeaqekgya
      181 eadptfdvgg fdaahkllil asiaynidak peeiliegie ninltdiefa kefgyeikll
      241 giakkignei elrvhptlik keemiakvdg vmnavsvigd vvgetmyygp gaggdatasa
      301 visdiieiar gcikpmlgfk ipleldnvtl kpideiesky ylrvavndev gvlekiahil
      361 aknnisiesf lqkprngyvk llfsthkcke keikkaikei qelsfvlkpi nyiriee
//
LOCUS       WP_457563328             211 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457563328
VERSION     WP_457563328.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..211
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24773
     Region          11..209
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mieklkkisl ffniedkile eissfshlkk ynpdeiifye gekdkyfygi vtgsvlmydi
       61 dlkgniipkn qfgcgdifgl isqiqnreyc lsaksendse iiridyskfq kfisnppfsd
      121 riikmlsnqi lqemefnklq kydatkrlvy allnfpkkfi rkkkyllake lnmspetlsr
      181 ilsklrneei icyceksikv ldkeklknil s
//
LOCUS       WP_457563317             365 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563317
VERSION     WP_457563317.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..365
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
     Region          14..355
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 daiakdiker lgieietyei damdvdatak litdtksdiv lnvalpyqdl aimdaclkag
       61 ahyvdtanye hpdeakfeyk eqwakhedfk kaglmallgs gfdpgvtnvf tafaaqelld
      121 eieyldildc nagdhgypfa tnfnpeinir eitqkgkyye ngewkeiepm svkfkwnypn
      181 vgeypsylly heelesltkn fpsikrarff mtfsdnylwh lnalqnvgmt siepikiaeg
      241 ceispmeflk kvlpdpaslg prtkgqthig viatgykngv kkryyiynic dhqcafrevg
      301 aqcvsyttgv pamigakmia tktwfeagvk nmeefparpf lyalnkhglp wfveelptdg
      361 lpidn
//
LOCUS       WP_457563331             404 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Caminibacter pacificus].
ACCESSION   WP_457563331
VERSION     WP_457563331.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..404
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44487
     Region          7..396
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mkinspkdlp ikrgdrvfvr cdfnvpldef gnitddrrir malptikyll dndckivias
       61 hlgrpkgefn ekfslkpvak rlshllkqdv imakdvvgpd akekaanlke gevlllenvr
      121 fdsretknde gfakelsefg dfyindafgv shrahasvea itrfydschk aggflllkei
      181 nffhkllenp vrpfvavvgg skvsgklqal vnllpkvdkm vigggmaftf lkamgynvgn
      241 slveddlide alkimaeakr lgvkfylpvd iviadkfaed amvkyvtyqe ipdgwmgldi
      301 gpatvrlfge vlwdaqtilw ngpmgvyemd kfsrgtfkis heiarshgik vvgggdtada
      361 vqragddeem tfistgggas lellegkklp gvaaleipde vscq
//
LOCUS       WP_457563335             250 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD-IIA family hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563335
VERSION     WP_457563335.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..250
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28514
     Region          1..239
                     /region_name="NagD"
                     /note="Ribonucleotide monophosphatase NagD, HAD
                     superfamily [Nucleotide transport and metabolism];
                     COG0647"
                     /db_xref="CDD:440412"
ORIGIN      
        1 mrgyfidiqg tliddknflp lpgaveflky lnskkipfil ltnntkrdsk efidylkslg
       61 fefenyldpl mvlddyvkgk kiapygnekf velmkkyeid yknpdavvlg iklfsneefa
      121 diiemllrgs eligmhktsl yskgdkrypg lgailemlky avnkdykvvg kpsatffnra
      181 keilgldydk itiisddlyg dllpakdlgm ksvlvlsgki kspeeitkkp deiyknledy
      241 lrngvinert
//
LOCUS       WP_457563339             264 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Caminibacter pacificus].
ACCESSION   WP_457563339
VERSION     WP_457563339.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=30635
     Region          2..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mkiayksdih ldfwvkeknr nkikdfikni lfpktadvli iagdlghdnl qnalfleeik
       61 kyygvvlvtf gnhdlyllde eslnkyktsh arlselkeyi rfiegvyfld gdiadvagik
      121 ilgaggwydf syavrhgisl evirgqwevi msdakyihpk idpptfssfe kekirsfiyd
      181 adivfthvpp lyikcfddvl mnsfytfygy dlfannvkyw ifghchqahd fyydtvrflc
      241 splgypvgrr gefgirnlni nlkg
//
LOCUS       WP_457563341             194 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457563341
VERSION     WP_457563341.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 194)
  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 194)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..194
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22407
     Region          1..177
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkiavieddk elnrlitkal tnegyevesf fdgesvlgek fdlylldldi pkisgielid
       61 llnapiiiis antkgeiidl afkkgvvdyi kkpfikeell nklkrffpkk ikikeyifnp
      121 kkrlliknnd tilltkdetk flslfinkdf atldeiyati eksdnalyif lsrlkkktki
      181 efenikgygy kikt
//
LOCUS       WP_457563342             530 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563342
VERSION     WP_457563342.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 530)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 530)
  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 530)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..530
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=62794
     Region          <313..508
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mffsvviifl dysyinsqkk klfiekelif ykieyltsnf lheilneynk nlpeikrahl
       61 yllknldkni tqiqkklgkn fhifitdknl tiikttfkyd knfslnflen llkthksihi
      121 sppicepatt dfisysdlyk ngivtqigyv yktpkieyfk neikkikeky pfiknislyf
      181 ihpktsyaqy cniltplhkk ptkremlchn kkgmeiykel lrknplitcd kmyilsynpf
      241 ekdsyiilqi diskhimean ikkttriiii afviiaiiaf sililinril kslnefkhsi
      301 ineqkyekkp ikelkdtiea ynntleklkk aieskddfih famhelatpi siltlymdey
      361 edlkpaikkl lssyknlsyc iqktshpkre tdltelieyr ikffreilnh enkkvildle
      421 qlticanpee meilidnnlk naikysksdi ikirlknkvl efenegfikd kekifekfyr
      481 eenikggfgl glhitkvice nhnikikliq kngkvifqyd lkdtdencsd
//
LOCUS       WP_457563344             155 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563344
VERSION     WP_457563344.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 155)
  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   5  (residues 1 to 155)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..155
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=17063
     Region          7..>102
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 mnililavai ilaimsltqk ntvpavlsfv lmmfllgiyy ilmdekllgl fqifvytggi
       61 vvltlfgvtv igskfpkyei rpwavsvvti viigliivpf lipdipyegk aiplkdqvki
      121 ftdfyaqiai fmgvvaasvl ygsirmlhtl khgke
//
LOCUS       WP_457563345             323 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 1/NuoH family protein [Caminibacter pacificus].
ACCESSION   WP_457563345
VERSION     WP_457563345.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   3  (residues 1 to 323)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..323
                     /product="complex I subunit 1/NuoH family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=36222
     Region          5..321
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 msvgeilfyi lvfpglvfll awtffvfyfs rkvlaylhkr vgphyngpag slqtvydvfk
       61 lltkesitpk sadpylfnii piitplvaal pvilipwtpl inngqgildt qygvlglvvl
      121 igvepfllfl tgfgsnnkys flggmrilaq mlsmeapffl aalspallfg tmnlyeimys
      181 ntwlttlill pgaiifiitm lgileqppfh ipdaeqeivy gfyteyagtn ytllkfaeft
      241 eilvvsaaai tlffggyrgi ffdsfwwlfl kiallavvmv airasnprlr ldqmlkfcws
      301 wltplavlnl vwvifaklyi lga
//
LOCUS       WP_457563347             567 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563347
VERSION     WP_457563347.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..567
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65572
     Region          <307..554
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mvenikeflk npkkskiyki lniskeevev lkhmlemyie gqedvkvrni lqkiysddkl
       61 eafehigtik nlieegwvvv ssfgakspel salelfnanv slsvaflkll engdlelvip
      121 qktpykdhle ylhdqflrid iyeqlanlkn sfsnetasik rlqsklklie stikervkkt
      181 qidlpvlnfm iendfnekee iiflallkee ytggsenare lnrlldlisa deieriknrs
      241 lldensklvs egiidydelf gafggytkiy fisedilnel ihprrkhkle hlvkdtifdl
      301 vepknsledv vlpkptmemv krvlkqidkr vvnllkkwgi kqnndldaki ifyghpgtgk
      361 tltahaiake lnkpvlslds skilsmyvge seknvrrlfd eyyeiseklk tkpvlllnea
      421 dqflstrtta afssadkmhn qmqnifleql ekfegvliat tnlletidsa fsrrfdykik
      481 fekptfkerv klwqkklpkn adfeedfdvn elakydltga qieliiknta lkvamkkkpi
      541 fklkdfieei ksekksafds ekevgfv
//
LOCUS       WP_457563349             210 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457563349
VERSION     WP_457563349.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 210)
  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 210)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..210
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24241
     Region          1..200
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkialiedel hlneaiklll elenfnvesf knireflres dndydiiiad islpdgnflq
       61 elskhkkige etkiiimsah geldnikkaf dlgaedfikk pfepeeiilr vkklfktkkt
      121 klteniyydp esktiltpns keiltkkeam llellikhrg rfvsfdtiaa tiwdepvssn
      181 tiaalikrlr qkiknknlit skreigymli
//
LOCUS       WP_457563356             341 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563356
VERSION     WP_457563356.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 12168893
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>341
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          284..>329
                     /region_name="TPR_19"
                     /note="Tetratricopeptide repeat; pfam14559"
                     /db_xref="CDD:434038"
ORIGIN      
        1 mkksilfita alffagcstk evpinitqkp navtskeirn irvdylvndt inlreniirk
       61 mydvnaiipg yfqintpnye silngyvkkt skeitytktv pikntkspcv ymlysckavs
      121 gavfckdkps tiltpgaydk ikkssyknsn yilyknsiyk vtykckptrk kikcqkksln
      181 iqahltitdk knntlldkty yadfnddsck nvkyyenknv yslnysikek ipelsyklas
      241 eiiddiaphq itiyttlfek pdidmnskde dilqntiknf sppaneaqis iltnllskyp
      301 qsavikydla vfltsagryq eakslleslk ttdsdiisak e
//
LOCUS       WP_457563352            1116 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457563352
VERSION     WP_457563352.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 1116)
  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 1116)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..1116
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=132327
     Region          <8..651
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          265..519
                     /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          357..385
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          421..451
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          489..517
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          556..584
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(557,560..561,564..565,567,591,594..595,598..599,
                     601..602,624,627..628,631..632,635)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          589..618
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          623..650
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkktiltlla fsflfsqeiq vdyqalqksv eqnpqdvknr lvlasyylkt lqvkkakkll
       61 seilkidpnn kkakellynl kllknateyk kffstpnkyi sllydkkdyk nlmnffeyyt
      121 rlngykklsd dsifkaarvf mwegkyqksl nalkhaknkk sldyyeiiay dlyylgdpka
      181 ekylkilyns tgnieyaktl ldfylinrdi pnakklllsl shatknkkli ekykkkiaqi
      241 eseyindlyq eyknnptftn lkklvlalyd tnkekaysll qeyiknnpad nqakiffaqi
      301 ltwdgdtnha lkylkefhnn veaklligki lawqgnydka aiylsdvydh gnpkekyeal
      361 kmlgfiamwk ndnlkakeif krllkqnpnd eevkealmil ngnikpviak yekllkrepd
      421 naeyilklad lyymdknyqk sayyyekylk yhpekievyk tlgdiylelk nyykgfgdwe
      481 yyanykntke aylelaqryy wngfnkealk vldellkqyp dfkeaailka kilkinprfv
      541 dsssaatide yynnraqkll vygdrayfnn lfataknyyh eylsinpdny evrekyaytl
      601 ektgdyanaa geffllmwnk ktplieyhya ynlqksgklq eakkiykkll ntlpkplpan
      661 ieqflqewkk awesmdfnky akfydkkisn nvywrlrken ifknagfisv giyspllikk
      721 egdvyvvkfy qvyasqkrkd kgyktiwikc kndkckiike kwqageytpy nptnslekyi
      781 kenlnkikkk qtpkleivqn lvkqpdtnkk enekkyfken nltkniqiip ikknivstkn
      841 qqkvlpwqit tkynfyhdtq kttmhllgik ifknnksysl fglykwyhlk ekgtkssyla
      901 gigykndkft adifydtstk ksigfdfytk vnhlnlflnk hnmvysrrtv cstnhikika
      961 eitkytqldd lrglwwslay ervddsnnif tpqidydfye fnkktytgtf yfsgwyqfns
     1021 kttscyyspk ktdaniigik lnknlnqalk thiqggigys fwdktylysi kgyiknintk
     1081 klytklgcki snsssssvtt hgfqsieclw eidkkw
//
LOCUS       WP_457563359            1024 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caminibacter pacificus].
ACCESSION   WP_457563359
VERSION     WP_457563359.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..1024
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113993
     Region          1..1008
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfeffykrgy llsaiilgmf vfgviglikm pknlfpdanr pevviftqvp gatasvvatt
       61 vskpieeema tlsnvyqiks tnvanfsivh vvfdytktlq qasvdvsnal nrikdklpkn
      121 sipaiylvgd ftapvdvfal spkndsitlp eikkiathfi kpkllsnpni gnvevfggyd
      181 savmvkidpl klkkygisfd dlikiiqttd lnmpigfvkt knsfitlsfy gekddvkklk
      241 nllikpnvrl kdiadiswsy qtnntlyign napsiaisvq rapsgsvlat sdaareemkk
      301 ieklypnikv tisdtqrnli etsninmlea lrdaiiftli vlliflanfr alaaaalsip
      361 mvffgtiayl yltgqglniv iytaiilalg mltddavvvl enierhlenk edlqkaiyeg
      421 tkevlkpifa gsvstiaiif plmfvggype kifkplietl ivalliswfl svtfipklst
      481 llykkgfkkt kveiffekly qntiarlikp yvgilhfsng kfyvlrrmll mmgamivlml
      541 svknimpiig rdvmppmdtg imkahiefss nlnaeesekr lkpfltwlnk qpwlekssia
      601 igtqkdvlsi tgggggnsin mtiiaidrfh rkktiwqled evrnelvkip gikkigvydf
      661 gatalstina pldvrllsdt ykqlpkeaqk iekllynvkg lttimktwdk dfnevvikid
      721 tnkalsygit pagiayqial kdmpvamltn lssmnvqfvr vrfnkqfeni ealkllpidt
      781 kkgpiplgei aqikndftys kidrynlqya idvegyrktr pvslitddad kllkehgikn
      841 ykqagdisem ndsfgrlika iavgvvilil tlmvvyqslr lalimivvlp lsmigaswal
      901 liankpscmp smvgllllfg iiiknavlli dfykefehsg kspfeaaies vkvrfrpvmm
      961 tafgtiagmi pialewavgl erlspiadva iggllvgtfl tlvyvpmlay stdprnkktn
     1021 plks
//
LOCUS       WP_457563360             356 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caminibacter
            pacificus].
ACCESSION   WP_457563360
VERSION     WP_457563360.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39561
     Region          48..356
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkvlkivipi iiaialafgg yrliklkkea dakektatly pivvkmykpe ykevtltlpa
       61 vaevknsnev aiatkfpgki lyiknlgekv kkgdllvkid dselksqlnt idskiaslkd
      121 kinaqkisle nlikthirtk kllevkmasi eqyqneeski atlkaaikad enslkslysq
      181 kqsildnlky ttiyantngv vsaklfnkgd iapmlkpilk itpnsgnyll vllpkeekai
      241 iykekeypli plkstingik aykaevedkn llpgekvdvk vvtfqgkgtf lpfntiltie
      301 nknyiftpkt keihikasgv egvvieekid tpviqaepdi llkikagypi kvenkg
//
LOCUS       WP_457563361             420 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457563361
VERSION     WP_457563361.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..420
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47378
     Region          122..413
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkklslvlia aslyaadigt lfdaikkqpe tkidnlqvkn akivkksvin slyptvnifs
       61 saehynapfs lrpvtptesa yllktndsip fsqniirigf dvsmplfikt iydnkekmsh
      121 iinaakykak lnllqresml viylsnlnyl yslkkalsvq knsiqesika ievgvkvgri
      181 pefkllrlkd avnqidikin didskiadtn skiytltkth lkkpidfqts svkkeeflav
      241 kpikenikas lldikakkdd flpkvffkis anrgfgwayn tkdsvalnta sagiyinwni
      301 fnkkrnsevq kakieymnsk ltlqktikel tsqiekidkt lkivnrslsl akksvkikee
      361 llksakvafk lgtmtvdeyl nyendlalak anvanlkatk nsliaqkafi ygnnfkkvfk
//
LOCUS       WP_457563364             540 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC1 kinase family protein [Caminibacter pacificus].
ACCESSION   WP_457563364
VERSION     WP_457563364.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..540
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=62342
     Region          4..456
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 mfknslyelk rtkeiifvla kygfgdiies lgipvpfket pklsrserir kaieelgptf
       61 iklaqllslr pdlvpldlak efeklqdsvt plpfeemkrv ledefekpyt eifeedfell
      121 asasigqvyk arlktgeiva vkilkpniee kiyadiailq rlakllrdrf liygvdleki
      181 veefaksikk eldfniealn lkrfannfrn nsdikvpkly ekysskrvlt mefiegikis
      241 didelkkvgy dlkeitkkgf dliceqifih rffhadphpg nlmvsngkiv fldfgimgrl
      301 sdedrqyfve miyyvikqqe ekaalyvlkl skvqgeidis sfkkemadii ssyfysslkq
      361 velraliedm lkvmqrykiy fkednyllak alvtmegigk klypefnaae eikpfiikiy
      421 kqtispfnil krsheinkav mefitqapsd lneiigklkr gelkvefehv gleefeeaie
      481 ksfnrlstsi iiaslligss mllsshippl fknislfgii gfifasilgv iliftvlrkk
//
LOCUS       WP_457563368             332 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Caminibacter pacificus].
ACCESSION   WP_457563368
VERSION     WP_457563368.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..332
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37445
     Region          3..331
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnfftfltli igyfvyltyr pylldiaias lmaiafsrie iklsekiknr yllasfitlv
       61 fallifgpll yfiivagkfi thiniediki vilkaqnllt ylpneiagyi knwltddniq
      121 kiyqsimpiv gtltaksavf ikdaflivvf fffailygkd illyakkvip leddklekly
      181 fttsevmsvv fystvftall egalfgfivs lyglnffffa vmyafaslip vvgglimwap
      241 vslyfyangn iqaaiviivy siviisiiad tfikpliiaw vkkffgndie fnslliffai
      301 vaglssfglw giiigpaita lfisvlkyye ki
//
LOCUS       WP_457563367             174 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caminibacter pacificus].
ACCESSION   WP_457563367
VERSION     WP_457563367.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 174)
  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 174)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..174
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20402
     Region          8..148
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 maieylehyt ykdyekwegd welingypya mspfalpshq risgkifrel desldncsec
       61 faliesevkf sedtvvrpdv lvkcgeiddi tltpeiifev vsensirrde ivkfdlykke
      121 gvmyyglvyp nekrvkiykl ingeyikisd lrngifktdd ltcyikvdfs kvwl
//
LOCUS       WP_457563371             179 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caminibacter pacificus].
ACCESSION   WP_457563371
VERSION     WP_457563371.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..179
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20968
     Region          6..175
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mclveyytyd dykkwegdwe lirgcpvama pspvkshqnl vamfayefnr nflnceecev
       61 lveedwivee dtvlrpdvsi vcneqneyit kapeivvevv skstakrdek ikfdiyekem
      121 vkyyilaype flkakvykne ngkfikigdf sneklkisdt scegeidfdt ifkklrskk
//
LOCUS       WP_457563384             314 aa            linear   BCT 27-JAN-2026
DEFINITION  arsenate reductase ArsC [Caminibacter pacificus].
ACCESSION   WP_457563384
VERSION     WP_457563384.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..314
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=35938
     Region          3..127
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(8,10..15,103,105)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mkkvlilctg nscrsimaeg linkflegie aksagskpsg kvnanaikal kkmgawcddy
       61 hsksitdlkn eefdlaitvc dnareacpvy pnakktihip fedpdgkdfs afeetieemq
      121 krliprvike lsfednflin kikgdlaeni crvhfenmgy dvskvgveni ssvfahlngy
      181 eknyieklkl lfqrmpdlli thnekkeaal fevkynknln tqddlknfsk ylherydyhi
      241 ntlklpvyfy vvtnkkpyvy vlkanhtngn tggfypadss wldkfpifsk enakksfrev
      301 yfsviypals dife
//
LOCUS       WP_457563386             376 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Caminibacter pacificus].
ACCESSION   WP_457563386
VERSION     WP_457563386.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..376
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42338
     Region          5..367
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(15..16,19..20,23,56,107..108,110..112,115,134,
                     137..138,141,210,213..214,217..219,222,249,253,298..299,
                     303,307,321,324..325,328..329,332)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mdknvvvlgi vsfftdlass mvntilplfi vyilnegvdk lgyvlaiatf lsyalrvvfg
       61 yfsdkygivk pfvvtgylis aiskpllyfs htwksvaflr gterigkair satkdtllsa
      121 yshshsgktf gfhkmldvag emtgalivfl ilmfigksee ifrlifafti ipgiisvflv
      181 iffvkdvkke kisknidfkk dkevikflff yfgflifafn dsffvikake sgftfemipl
      241 liiiynltqt llsyflgvki ekegykkill isfvfgilsv iamkmsyivl gfvflgiftv
      301 gslnairsyi sdnafnkstv ygffyagvai saslasliig klwqnygenf ayvysitgmi
      361 fvllfylkdg yvrayh
//
LOCUS       WP_457563387             179 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563387
VERSION     WP_457563387.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..179
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          1..179
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 awgyigifll mflessffpf psevvmipag ylaskgemnl ylaifvavlg svagawfnyl
       61 iashmgrafl ikfmseekik klenffenhg histfsgrli pgvrqyisfp aglakmhplk
      121 ftiytalgag iwvtilallg yfigenqqii hkylreitii tlvvlaiiif vyiklkvkk
//
LOCUS       WP_457563393             310 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Caminibacter pacificus].
ACCESSION   WP_457563393
VERSION     WP_457563393.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181086
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..310
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36277
     Region          72..218
                     /region_name="CE4_DAC_u4_5s"
                     /note="Putative catalytic NodB homology domain of
                     uncharacterized bacterial polysaccharide deacetylases
                     which consist of a 5-stranded beta/alpha barrel; cd10973"
                     /db_xref="CDD:213028"
     Site            order(79..80,134,138,174..176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213028"
ORIGIN      
        1 mkklilfllp lwllaeahif vlhriddfrh pytntsskel ekyfkyiksh nykaitlskl
       61 aemiknrqnv dnivvftidd tyksfykngl pvfkkygipf tlfvyvkatn ekwgdfmtwq
      121 qvkdaakyge lgihsyahph lpnlsnqaii ndtkkaieif kkhmgyvpdm yaypygeydq
      181 rvkkiinsff piianqnpga vdiatpindl drialtgkvd iakklkikrl hanikiqreg
      241 nkitlikgkv fdkipyvniy itkmgwvyki pvkngsfsya pnfelkkyrn rviirynyki
      301 iskmvikykk
//
LOCUS       WP_457563401              83 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol kinase, partial [Caminibacter pacificus].
ACCESSION   WP_457563401
VERSION     WP_457563401.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Li,D., Lyons,J.A., Pye,V.E., Vogeley,L., Aragao,D., Kenyon,C.P.,
            Shah,S.T., Doherty,C., Aherne,M. and Caffrey,M.
  TITLE     Crystal structure of the integral membrane diacylglycerol kinase
  JOURNAL   Nature 497 (7450), 521-524 (2013)
   PUBMED   23676677
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Van Horn,W.D. and Sanders,C.R.
  TITLE     Prokaryotic diacylglycerol kinase and undecaprenol kinase
  JOURNAL   Annu Rev Biophys 41, 81-101 (2012)
   PUBMED   22224599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10198050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..83
                     /product="diacylglycerol kinase"
                     /EC_number="2.7.1.107"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004143 - ATP-dependent diacylglycerol
                     kinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006654 - phosphatidic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          <4..78
                     /region_name="DAGK_IM"
                     /note="Integral membrane diacylglycerol kinase; cd14264"
                     /db_xref="CDD:260133"
ORIGIN      
        1 fvtplspllf fldflsvpps llassliftl itealntave ytvdlvtdew hefakkakdt
       61 asaavffslv qaaviwginl fls
//
LOCUS       WP_457563404             395 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Caminibacter pacificus].
ACCESSION   WP_457563404
VERSION     WP_457563404.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44512
     Region          1..392
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mkfkyvgfnk egkkvkgiie asdiqeakqk lsniaiidik qkrgfnisfg svkkselaki
       61 lnviglylka siplkkainl aknqtqnqkl qkflsfiede ikegktlsea iknqkiiklp
      121 pyivhstqia qnssnldlil ienakflqee dkinskstqa liypsfiiii slilvivmmn
      181 tvvpkiikif qnlnqnlpti tkitisishf lqnnyillsv gfiiillafs faykkvlffr
      241 kiidslilkt pllkrlsisk nlgrfsslty tltnsgihfm navnlaskti dneilkekfq
      301 kalnevlegk klstslkkqn fpdisfieai alieetgesk nimqnlkeiy lqeydskvsi
      361 llsllepimi livggvigfi vismllpifs mnvmr
//
LOCUS       WP_457563405             501 aa            linear   BCT 27-JAN-2026
DEFINITION  GspE/PulE family protein [Caminibacter pacificus].
ACCESSION   WP_457563405
VERSION     WP_457563405.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..501
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=56538
     Region          6..497
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mksvkninpk aielenfnle egikfsllpa lledkkvfvt kendyvdaln yynklsipfe
       61 iimtdeesfn rllnqylevk tkkdlednid evieeelsle dfvkesvdil nsensapvik
      121 fvnsmffqai kkrasdihie thelfglirf ridgvlitqa kiqkkltelv inrikvisnl
      181 disekrvpqd grcqikiank ttdirvsiip tyfgekavmr ilmesedipn lkelgfneei
      241 tqgfkelleh sygmilvtgp tgsgksttlh sflqtistpe kniitvedpv eykadninqi
      301 qvnnkvgltf akalrsilrq dpdiimvgei rdketatiai qaaltghlml stlhtnnaaa
      361 titrlmdmgi epflisssli gilsqrlvrk lcdcktedsl eeiekivkke pllqkyeisk
      421 iykpngcakc nftgyvgrka vgelfimnde ikemiakgtn dielksamik hgmktlkeai
      481 feevlngtts lkeairvglk d
//
LOCUS       WP_457563409             142 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caminibacter pacificus].
ACCESSION   WP_457563409
VERSION     WP_457563409.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..142
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16668
     Region          5..>35
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 msaikraftl ielilvifli slvsflvikl psysktytfk dirallypsg elyidknsvy
       61 iikngkkkki nfrysefqty dnnfnplkfk nhlfvykmkn gvgdsfvvke kkvyffkplw
      121 vrefsslkda kdymnslnea lk
//
LOCUS       WP_457563410             150 aa            linear   BCT 27-JAN-2026
DEFINITION  PulJ/GspJ family protein [Caminibacter pacificus].
ACCESSION   WP_457563410
VERSION     WP_457563410.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Lopez-Castilla,A., Vitorge,B., Khoury,L., Morellet,N., Francetic,O.
            and Izadi-Pruneyre,N.
  TITLE     1H, 15N and 13C resonance assignments and secondary structure of
            PulG, the major pseudopilin from Klebsiella oxytoca type 2
            secretion system
  JOURNAL   Biomol NMR Assign 11 (2), 155-158 (2017)
   PUBMED   28258547
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Korotkov,K.V. and Hol,W.G.
  TITLE     Structure of the GspK-GspI-GspJ complex from the enterotoxigenic
            Escherichia coli type 2 secretion system
  JOURNAL   Nat Struct Mol Biol 15 (5), 462-468 (2008)
   PUBMED   18438417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..150
                     /product="PulJ/GspJ family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17321
     Region          5..>41
                     /region_name="PulJ"
                     /note="Type II secretory pathway, PulJ/GspJ component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG4795"
                     /db_xref="CDD:443823"
ORIGIN      
        1 mkksftllev listlllafv fvamsnilts lkrtesilqs kkedkndyli ktlyydiina
       61 deinvsktan pkidtltlrt fnslykipkp yvkwvvykga liraesvdnf kenvgtidkf
      121 aknvkifkiy kkdgkflifv nnkffefkgr
//
LOCUS       WP_457563414             420 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457563414
VERSION     WP_457563414.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..420
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49508
     Region          <131..415
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkklilllit tysfsqlinc drykivtvyd lfdkiekndk vrygrlnels fkdksynfki
       61 yidgymktgk kvtdnvvdnv hftersvkih adkllysslk kynsqilkin allnslnikn
      121 rvnsdlvlgl ntysnllflq qkidilnkii krqksiydyl inrynegvgs kidvlnakid
      181 lanlnqnlis sykdyaqnli ifnylygdnk nkdyyfmpfl pkfaislkql qkevlknnyn
      241 akiaklnlkk sfynyqkssl hpininfysf agytqsiqkt fnlgsdlnsf dwemgvtfni
      301 plydaqlkqa renskvnyli qreayksdiq kilrnvykiy qniiyerkni kiirkkidvy
      361 keeidfyqnr iysglneytq yatvlknyln eminlrnsvn rlntdilllk ilsgrsvgen
//
LOCUS       WP_457563411             448 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent thymidylate synthase [Caminibacter pacificus].
ACCESSION   WP_457563411
VERSION     WP_457563411.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Graziani,S., Bernauer,J., Skouloubris,S., Graille,M., Zhou,C.Z.,
            Marchand,C., Decottignies,P., van Tilbeurgh,H., Myllykallio,H. and
            Liebl,U.
  TITLE     Catalytic mechanism and structure of viral flavin-dependent
            thymidylate synthase ThyX
  JOURNAL   J Biol Chem 281 (33), 24048-24057 (2006)
   PUBMED   16707489
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Leduc,D., Graziani,S., Meslet-Cladiere,L., Sodolescu,A., Liebl,U.
            and Myllykallio,H.
  TITLE     Two distinct pathways for thymidylate (dTMP) synthesis in
            (hyper)thermophilic Bacteria and Archaea
  JOURNAL   Biochem Soc Trans 32 (Pt 2), 231-235 (2004)
   PUBMED   15046578
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Mathews,I.I., Deacon,A.M., Canaves,J.M., McMullan,D., Lesley,S.A.,
            Agarwalla,S. and Kuhn,P.
  TITLE     Functional analysis of substrate and cofactor complex structures of
            a thymidylate synthase-complementing protein
  JOURNAL   Structure 11 (6), 677-690 (2003)
   PUBMED   12791256
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Myllykallio,H., Lipowski,G., Leduc,D., Filee,J., Forterre,P. and
            Liebl,U.
  TITLE     An alternative flavin-dependent mechanism for thymidylate synthesis
  JOURNAL   Science 297 (5578), 105-107 (2002)
   PUBMED   12029065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18522596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..448
                     /product="FAD-dependent thymidylate synthase"
                     /EC_number="2.1.1.148"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0050797 - thymidylate synthase (FAD)
                     activity [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /GO_process="GO:0006231 - dTMP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006235 - dTTP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=52443
     Region          1..214
                     /region_name="ThyX"
                     /note="Thymidylate synthase ThyX, FAD-dependent family
                     [Nucleotide transport and metabolism]; COG1351"
                     /db_xref="CDD:440962"
     Site            order(18..19,22,55..56,58..59,61,63,76..77,79..80,82,
                     85..89,92,116,126..127,129,133,152..153,155..159,165,167,
                     169,173)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:412038"
     Site            order(76..77,80,88..92,155)
                     /site_type="other"
                     /note="nucleotide binding pocket [chemical binding]"
                     /db_xref="CDD:412038"
     Region          <281..400
                     /region_name="ThyX"
                     /note="FAD-dependent thymidylate synthase (ThyX),
                     mechanistically and structurally unrelated to thymidylate
                     synthase (ThyA); cl42216"
                     /db_xref="CDD:478033"
     Site            order(290..291,294,301..305,378)
                     /site_type="other"
                     /note="nucleotide binding pocket [chemical binding]"
                     /db_xref="CDD:412038"
     Site            order(294..296,300..301,303,367,369,373,377..378,382)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:412038"
ORIGIN      
        1 mnikildlny kptdiavgsa rscyfgkhiv tpenaakwdk knelldsifk aghhttlmhy
       61 hftiliegms rlliwrmlhs hpfynseqvs qryakmkien ftypknadke kwkkyyekmf
      121 fyyeeliekl tpeiekvlpk fkkkeakkra qefaryllpq gmnahlyhti nvitalryit
      181 aakvmpeane eakefakkle iemlridenl aplidfakne kvvfskidie kikkaknigd
      241 ervkvfdivd ydfelnenfa gvmrlssmll desilggfns yiklslsada qnqrhrrspa
      301 vrpklediyk rdyyippiiq gesleiykra veesyeffek erdvlgfgea ayallnahni
      361 eivehddfne fahkaqmrlc ynaqeeifdi vyeqvkqlkk agvkaadkfl ppcsiryaqg
      421 irpvcpeger fcgvkvwklg fdeyervi
//
LOCUS       WP_457563418             477 aa            linear   BCT 27-JAN-2026
DEFINITION  HD-GYP domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563418
VERSION     WP_457563418.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..477
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55401
     Region          <281..464
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mtdiryllnv kiplrvneef nevlgfmqkg wvlyilvavi fffaflymfr ryfeekkkfv
       61 nfdailekla dtkdinveeq iimnelkiak niafyqsrgn vyilidskte kiefpfripk
      121 edldeyknig dnkvgyikns dekylllfad kkldiedykg hlklilnyye ktfeknikda
      181 vslvsdnaak sfmkinmnqe eflrfftsll kkivksekvy llkngeniei qgnfkkdfyi
      241 rntpykvtvi keenlspqei kkigsfidla ghylvnfasn kqiidnyiel lklaveamei
      301 nnpfyknhse iveivsveta kalylsqkei dnialasklh digmigdmvn fldktelske
      361 elnllkqhpi igssivepin qtyeiadiik yhherydgrg ypfglkgvni pisanivalg
      421 efyagitsdr aykkgishde avkeikdlsn kyfeksivda flnvekrint kilkvkk
//
LOCUS       WP_457563419             225 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457563419
VERSION     WP_457563419.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..225
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25725
     Region          6..178
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(9,11,88)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(37,87..88)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            86..88
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mndaaivipm yneeavienv leellqkvpy diivvddcst dnsyqkackk gvylirhivn
       61 lgqgaaiqtg ieyarklgkk yvvtfdsdgq hsvediepfl eklrndeadi vlgsrflgkt
      121 enmstfkkyf lklsryftym ttgimlsdsh ngfrainikd fpnfeikqnr mahaseiidl
      181 irknsmryve mpctikytdy skqkgqstln ainivfeylt grlik
//
LOCUS       WP_457563422             322 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caminibacter
            pacificus].
ACCESSION   WP_457563422
VERSION     WP_457563422.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..322
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36302
     Region          33..>302
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkkslvflil vlifsgcakt kedkaihikd dnvtlrlegm aypskkfvly saangtvekv
       61 yvqngskvkp gdkilklstk sldldieklk tdikntqkei seakkayyny aslnitkkel
      121 kkmallhskg yasefevdny kknylneltn ienqkkslkt qilnltstle nqkielkkll
      181 lqkqkanavs pvygfvanls vsptqeitan qkiceilnid tikvkaglpp gllpfvkvgq
      241 rvridfitep qystyakitk inpivdkkfq nmtieievkn knyliqpqtr alimiflspk
      301 dqekvkklte skggiieips di
//
LOCUS       WP_457563426             431 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563426
VERSION     WP_457563426.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..431
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47184
     Region          1..431
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mydviviggg lgyaaaivls kagkkvalie rnlehlggtc lhngcipskn llhraktlle
       61 lkegffdgev slnlkklqnh iskiitshtk avknqllmak veliedegyv tddgvllknq
      121 nktlqakyii iadgskprip egieydgkri itskealelk napkeitiyg sgaiglemas
      181 ffsaigtkvn llyrhsnisk kfpqiitekl eeqlknigvn lmpnseikea ktehskvicn
      241 ingkefstdy lllaagrvpk tdivqtdkik iqkgivtdey fqttmpnvya vgdcngklml
      301 ahaaraqaln vanqilgkke klilenipkf iytlplsyan igtkgvkeae fpinylgiag
      361 slygdelgiv kiyadeenfi tgadilapna eeligifssa laaevdidtl kkavfphpty
      421 seaidralrr f
//
LOCUS       WP_457563427             399 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563427
VERSION     WP_457563427.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..399
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44618
     Region          1..394
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 meykvtmpil sdtmdkgkli kwyvkegdrv kkgdklceve sdkatmdies fvngrvkkil
       61 vkegeevpvk sviaviesee skqetkneqe eiketkekss ktntdssidi delinsivne
      121 pskkvsgsas paakqkakkl gidieslqks gelptpahek dideviikky fspkaaklik
      181 eygldfdife lnrkiesdev mkyiktnnip kitklspnqi aviktvqnai kkptffvfee
      241 veitkkenik ltaqiikala tamqkhpltr silkdneilt yptsnisvav arddglfmcv
      301 iknaedksle einewlkeik tkklsiedls gstfgisnlg mfniksftal indndagiaa
      361 fgalnnnkme vsftidhril ngvdaakfin dfkeecknv
//
LOCUS       WP_457563428             324 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Caminibacter pacificus].
ACCESSION   WP_457563428
VERSION     WP_457563428.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..324
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35808
     Region          1..318
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mlyrealnka idesmaadns vvilgedvgr yggsyrvseg lfskygekrv idtpiaelsi
       61 vgnaigmaia glrpiaeimt anfsllamdq iinhaskfry msggkmtipl tirmpggvsr
      121 qlaaqhseny etlyssipgl ivlaasnaty ayyglksaif mndpvvfleh ellypmdmef
      181 keiknfdpfk aevvkegkdl tiitylkmry dvleaqkalq kagidaeiid lnslrpidie
      241 tiaksikktk kcviveedhk tggmgaeiaa qimencfydl dapvlriage dvpipynrkl
      301 ellsiptpek ivtkilkwka engi
//
LOCUS       WP_457563429             323 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Caminibacter pacificus].
ACCESSION   WP_457563429
VERSION     WP_457563429.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..323
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36172
     Region          1..314
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mnsarvkkfy ylmklgrefe laakreymng niagflhldi gqeavsvgtm qafdkgdvft
       61 hyrehvlala rgmepkrvma elfgkktgis kgkggsmhlf epkldfyggd aivaghlpia
      121 vgcayarkiq genagvfaif gdgasnagaf fesiniasaw klpiiffcen nyyaigthis
      181 wvspfvelyn kaknymptkr ingmdvcevy navmeakthi englgpyfie aetyryeghs
      241 msdagkyrse eeleifkrkd pienlkkkai elgivdekyf qeadakvqnv ieeavkfaae
      301 spepedyelf edvfckecen alp
//
LOCUS       WP_457563434             168 aa            linear   BCT 27-JAN-2026
DEFINITION  macro domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563434
VERSION     WP_457563434.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Rack,J.G., Perina,D. and Ahel,I.
  TITLE     Macrodomains: Structure, Function, Evolution, and Catalytic
            Activities
  JOURNAL   Annu Rev Biochem 85, 431-454 (2016)
   PUBMED   26844395
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Karras,G.I., Kustatscher,G., Buhecha,H.R., Allen,M.D., Pugieux,C.,
            Sait,F., Bycroft,M. and Ladurner,A.G.
  TITLE     The macro domain is an ADP-ribose binding module
  JOURNAL   EMBO J 24 (11), 1911-1920 (2005)
   PUBMED   15902274
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..168
                     /product="macro domain-containing protein"
                     /GO_function="GO:0072570 - ADP-D-ribose binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18691
     Region          4..168
                     /region_name="YmdB"
                     /note="O-acetyl-ADP-ribose deacetylase (regulator of RNase
                     III), contains Macro domain [Translation, ribosomal
                     structure and biogenesis]; COG2110"
                     /db_xref="CDD:441713"
ORIGIN      
        1 mykivikkgn ifseksadfi vnpsntelil gsgvsgafrr vcgsalqnem rklapikqge
       61 vavtdcpghp eykkalhvai mdytsnnpsp tlevikkslq niekiiknht pckivlplmg
      121 vgvggldkee vikiykeffs knvdfdcevv iygykdedya llkkyfek
//
LOCUS       WP_457563439             321 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563439
VERSION     WP_457563439.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..321
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
     Region          <3..317
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 nirnffnaeg aikafiagav asgiillgfa lfsfttdsfn yaemnvsgkf tliavaimla
       61 gifykltvvp mhgwaadaya qvnhaaaail sgviksvvlv atfkafykfl iaypvatvli
      121 fsffaivtmt lanfmalwqk riskilafss iahsgyalip faaaasaysy agvlyyavay
      181 iflqtnvfli lndlrrelgv kylqdikgly kvaplhslff tiqlfslagi pllagflska
      241 vafyagvdag lwvivliall nsalavgyyv wiikhiyfdd tkstttitmt pgsligqlil
      301 lagtvyfgiv agniinatva f
//
LOCUS       WP_457563440             746 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457563440
VERSION     WP_457563440.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 746)
  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 746)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..746
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=88171
     Region          157..412
                     /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          <168..664
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          268..296
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          301..334
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..376
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          381..409
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfflffpvf lfalqlnidy gnakkpyevl tiynkfpfec slkektficv fdktpktpvf
       61 keesrffqvi pkfskkftit ikiksdnfki fafednlykk plitpfrlkk akkwvivane
      121 qylentnkgl dfyykhavyp yigaidenlr pirgenamdi akyfeilkay kkgrdvldei
      181 dqfvkeypns iflsdvlylk lkildrenqs edvvqlgkew ikkfayspkl pevllligen
      241 yskmglisda syffnriite ypntkyayka miyladqlyt mgdekkafkl yekalystkd
      301 mnvaslaalr laqrymdkgq vkkaieyyek iykankefll kdkrkayela krlasekvyn
      361 lainigedll krlkklddly epllynlalw syeagdyqks lkfinkylke fpygdysdni
      421 kalrdkvlfe vpeqnltkkf qyidkvlney kntdiakkal vekiktlykl kkydeilklq
      481 keiknipkkl fpqkdtfikk vaseyakell ekgncqkaie likkyklnlk edekvyscam
      541 kvkdcklasa icnkyldnps devfvkwmkr kiealwcmrd yknvvtavdd lcqiernchk
      601 ylmykffalw nlgkykqalk taqklekyqt iqnadayiki vnwamqnkdy llaatyakki
      661 idlqnrfnay pyspfvdfvf akytknknea ikvleklipk vkgedlaray fmlanltgkk
      721 dylqkclnvk dsklwkglck dalnlf
//
LOCUS       WP_457563443             359 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457563443
VERSION     WP_457563443.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..359
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40702
     Region          5..330
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkvfdyiiig agiagslagy flrdknvlvv dkkgklegas gaagaflfpk vgydtaytrf
       61 inegivssie fyksigvdth tkgvlilprd erdiekfkky ekeiklpfkk rgegfffeig
      121 svidpeevke kldfpfekle vktlkkeeyw vlndeikakn vilasgyesi vdipyiqirp
      181 iwgerieieg iwdkskcdiy yhkncsvgcn gvmkigathk rncleckene qealelieka
      241 keiidiknyq ikdikggfra astdyfpvvg qvidvdktll ndkhiikgdm pkeifyiegl
      301 yiingmggrg fsnayvcakm lkdfiengad lgwvdtkrlf ikwarksgea ylrsknvks
//
LOCUS       WP_457563444             255 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563444
VERSION     WP_457563444.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28705
     Region          1..254
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 mlkvdkvtkq fggvvaikdv sfevkpleif alvgpngagk ttlfniitgv leptsgkvyf
       61 kdeditglsp vkivekgiar tfqnirlfss ltvlenvlig fhnhieynff eslfrlprff
      121 kqekihkeka meilkflgie kyadynakal sygnqrkvei aralatepdl llldepaagm
      181 npketdelad tvfklrseme ktilfiehdm kfvqkiadrv mvldygktif egkpadmmkd
      241 etvikaylgd idveg
//
LOCUS       WP_457563451             397 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Caminibacter pacificus].
ACCESSION   WP_457563451
VERSION     WP_457563451.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..397
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44844
     Region          29..395
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 manlliigag gvgrvsafka aknkdtfkni ilasrtkskc ddiakdikek lgieiktyal
       61 dankeenvid likkenidiv cnvalpyqnl pimhaciktg aayldtalae tednpdtyyd
      121 lqwaldedfk kahtmallgc gfdpgvtsim vkyaadylld eleeieiydc nfgdhgrhfa
      181 tnfdpeinlr elnlpgkywe ngewkttkpf eiqvkhkype cgeatsiliw heelesivkf
      241 fpnlksakfy mcfsdrylyh fnalknvgmf siepieiceg ckisplqfla kvlpdpqdlv
      301 knykgqtnig viakgkkdgk nktfyiynic dhekaieetg ahcvsyttgv paiigcklma
      361 kkiwwsegvh nveefdakpf feemekqglp ikvieve
//
LOCUS       WP_457563452             153 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563452
VERSION     WP_457563452.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Moynie,L., Giraud,M.F., Breton,A., Boissier,F., Daignan-Fornier,B.
            and Dautant,A.
  TITLE     Functional significance of four successive glycine residues in the
            pyrophosphate binding loop of fungal 6-oxopurine
            phosphoribosyltransferases
  JOURNAL   Protein Sci 21 (8), 1185-1196 (2012)
   PUBMED   22610485
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Vos,S., Parry,R.J., Burns,M.R., de Jersey,J. and Martin,J.L.
  TITLE     Structures of free and complexed forms of Escherichia coli
            xanthine-guanine phosphoribosyltransferase
  JOURNAL   J Mol Biol 282 (4), 875-889 (1998)
   PUBMED   9743633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..153
                     /product="phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0106130 - purine
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17942
     Region          1..147
                     /region_name="Hpt1"
                     /note="Hypoxanthine phosphoribosyltransferase [Coenzyme
                     transport and metabolism]; COG2236"
                     /db_xref="CDD:441837"
ORIGIN      
        1 mkkyyysyee flkdlntlqn kikdynpdcl laiarggmtl ghflaermdt kelyslnass
       61 yeyekkvskp kifnipdlsh kkrvlllddi sdsgetldev mkilkkkfpn tqiksatify
      121 kentihkpdf vlkkadkwiv ffwdkegqei ien
//
LOCUS       WP_457563453             104 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457563453
VERSION     WP_457563453.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Jurenas,D., Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Biology and evolution of bacterial toxin-antitoxin systems
  JOURNAL   Nat Rev Microbiol 20 (6), 335-350 (2022)
   PUBMED   34975154
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Kamruzzaman,M., Wu,A.Y. and Iredell,J.R.
  TITLE     Biological Functions of Type II Toxin-Antitoxin Systems in Bacteria
  JOURNAL   Microorganisms 9 (6) (2021)
   PUBMED   34208120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Rocker,A. and Meinhart,A.
  TITLE     Type II toxin: antitoxin systems. More than small selfish entities?
  JOURNAL   Curr Genet 62 (2), 287-290 (2016)
   PUBMED   26597447
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Goeders,N., Dreze,P.L. and Van Melderen,L.
  TITLE     Relaxed cleavage specificity within the RelE toxin family
  JOURNAL   J Bacteriol 195 (11), 2541-2549 (2013)
   PUBMED   23543711
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..104
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12438
     Region          5..92
                     /region_name="ParE_toxin"
                     /note="ParE toxin of type II toxin-antitoxin system,
                     parDE; pfam05016"
                     /db_xref="CDD:398610"
ORIGIN      
        1 mnfqikisey akndleiafd fyekqatnlg kiffdyiise iellsfygcl hqkifgyhrm
       61 iskkfpfaiy ydcnkeqkyi tivaildlrq npktiekyli kdrk
//
LOCUS       WP_457563457             188 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Caminibacter pacificus].
ACCESSION   WP_457563457
VERSION     WP_457563457.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (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   4  (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 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..188
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21020
     Region          1..172
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mklidlfdki vrgiliflts fgiaggilla finvvarfvf hegidwafel tnylfiwsaf
       61 fgaaylfrig ghikvtlild llpdklakld vllvdliiia ylatvgyfgy lfifdpdlgv
      121 yssgevsvdl gipmwipyiv iplsslfgil mvifkmkeni ttpaekirgk sesemiieev
      181 renmgevq
//
LOCUS       WP_457563466             369 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Caminibacter pacificus].
ACCESSION   WP_457563466
VERSION     WP_457563466.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..369
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43531
     Region          71..349
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mienpkvslf nrkgklyvqy yingrcvqks lkrdytkeni klakkyvipe ierkillgei
       61 qdnrvkpkef eyyatiylrq kenlksyyey enivvnqlfp lfkhkkvnei tkgeikewvd
      121 krlnevtpkr lrniqnilia ildiaveyeh iqinpaknik lpshvkvrem kpfneeevkl
      181 linnaegqfk cylaiafytg mrpgeiialt isdinlkemy invnkrirkg eidtpktkns
      241 irkvpvfqnl kpyleelikk akenktfnlf ttktgkryys sdklhpqwya llqkcniekr
      301 vmyntrhtfa tlaikrgvpi fnvsqilghr ntqetletya kfinnehlql drnlelftds
      361 stdsvskka
//
LOCUS       WP_457563469             296 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457563469
VERSION     WP_457563469.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..296
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=33798
     Region          16..52
                     /region_name="S4"
                     /note="S4 domain; pfam01479"
                     /db_xref="CDD:396182"
     Site            order(27,28..29,31..32,35..36,38,45..52)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          72..274
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mgfvekefei kdekvldflv kkvgfnlrea kraidrgrvs vngkrvtqks qkatgklkci
       61 mfepngyglk pifetthfai fdkpsgvaih pkklantksl lddvralwgn danlvhrldk
      121 etsglvmask nkfaesilkr afqdkdikks ylalvkgrld kemtikkpia vnkdenikvk
      181 viihpegkes vtivkpikif dnytlvecdl ltgrqhqirv hlfsighpiv gdplygvdnd
      241 fadrylnklv tekeriektg anrlmlhsyk ldfefmnnky iiksdsffev lknfin
//
LOCUS       WP_457563470             237 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457563470
VERSION     WP_457563470.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 237)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..237
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28247
     Region          7..>89
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          156..236
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlkiqndifl itskyqntqf kphfhdtysf alitdgecvv nfknktthyk kndfriinpy
       61 eihyvksgiw gyksvvfeks yvnsitkeii nkeniifknk instklnslf lkmyekqeen
      121 iyfffeells fskeiklpki tlkksieyid enftqkikle nladlehisk yhflrlfknq
      181 tgltphqyii ikrlnfalel mkkeknlayv avragfsdqs hfikefkkvf gftpkek
//
LOCUS       WP_457563471             259 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563471
VERSION     WP_457563471.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..259
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28156
     Region          2..256
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mwdlintsiy asillsiaig iigslivink ataitgsiah gsfggigigi flgtsilltt
       61 tiftvilali lalitifyrh radsligviw avgmsigiif lslapgynad alsylfgnil
      121 lvenkdlllm givdlilivs ilvlynrfla msydmeflki rginsnllft yflvltslti
      181 visvraigii lilalftipp liaekftkrf yqmiilssil afifmstgiv isyfydlspt
      241 piiviiaatg lflslfkkt
//
LOCUS       WP_457563472             137 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457563472
VERSION     WP_457563472.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..137
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15731
     Region          2..130
                     /region_name="VapC"
                     /note="VapC family ribonuclease, toxin component of the
                     VapBC toxin-antitoxin module, contains PIN domain [Defense
                     mechanisms]; COG1848"
                     /db_xref="CDD:441453"
ORIGIN      
        1 mkvlldiniv ldffmerepy fkeikkifna vekrkidgfl cassmdtihy lvqkaynkkt
       61 addviykllk lfdvtpvtke vllealnsgf ndfedsiiys saylqgidfi itrdkkgfkt
      121 skvkvltpve flskivd
//
LOCUS       WP_457563474             231 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563474
VERSION     WP_457563474.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..231
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25960
     Region          1..231
                     /region_name="COG1237"
                     /note="Metal-dependent hydrolase, beta-lactamase
                     superfamily II [General function prediction only]"
                     /db_xref="CDD:440850"
ORIGIN      
        1 mkfsivfdny vaneklesfw gfscvindyf lfdtgsngra lvrnmvkmgv dinalkylfi
       61 shphwdhigg idsvldvnpy mtlflpdsls klyirdlkrl srevkvihen ptklfgkfys
      121 tgvmmpigeq slvidegdfs ivvtgcahpg ivnivrraie mlnkpvlyal ggfhlmrsge
      181 eeiievvkel kvlgveyvtp thcsgdlaie ifkeeygeny ipggvgriie f
//
LOCUS       WP_457563476             103 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457563476
VERSION     WP_457563476.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..103
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=11792
     Region          1..101
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 myeqysivlv nldptigsei kktrpcviis pnemnfnikt liiapmtsks keyptrvkik
       61 ddsfivldqi rmidkkrvik qlgkidlkti seikkilnim lve
//
LOCUS       WP_457563479             658 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease J [Caminibacter pacificus].
ACCESSION   WP_457563479
VERSION     WP_457563479.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..658
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=75984
     Region          105..655
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mekekkeitl deaikntiee nlkndteksq nnnqnqnqek sekkeykknn yqknnqkrtt
       61 ykslqpqknv neknfvwfkd lnkafdenek ihqarlscfn kidsnkkgwv rftplgglde
      121 iggncavlet edsaiiidcg msfpsedmhg vdilipdfsy lreirhkikg liithghedh
      181 igavpylfke mqfpiygtsl plamienkfk ehkmlqyksy frsvkkrhpi qigdfkvewi
      241 hmthsivdss slaiqtpigt iihtgdfkid htpidgyppd lhrlahygek gvlalfsdst
      301 nsykpgvtps esvvgktfed lfmktkgrvi mstfssnihr vyqaiekgik fgrkvciigr
      361 smeqnlnvam dlgyiklprd ifidpyeigk yqdeeiliit tgsqgesmsa lyrmaidehr
      421 hvkikegdqi iisakaipgn eptvsqlinf lmkkgakvay hefseihvsg hasqeeqklm
      481 lrlvkpkyff pvhgeynhlm khretaistg mdeknifvme dgeqweitpk kvrkvknvkv
      541 gkiyidnqin eqietdvvid rqklanegii mivaqvdkqn kkligrprvt tfgiiadked
      601 kafakemedl linyidhakd yvyeknrife nelrnvirkh vfrktkkypt ivpmvyfm
//
LOCUS       WP_457563461             307 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease Z [Caminibacter pacificus].
ACCESSION   WP_457563461
VERSION     WP_457563461.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Redko,Y., Li de la Sierra-Gallay,I. and Condon,C.
  TITLE     When all's zed and done: the structure and function of RNase Z in
            prokaryotes
  JOURNAL   Nat Rev Microbiol 5 (4), 278-286 (2007)
   PUBMED   17363966
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Schiffer,S., Rosch,S. and Marchfelder,A.
  TITLE     Assigning a function to a conserved group of proteins: the tRNA
            3'-processing enzymes
  JOURNAL   EMBO J 21 (11), 2769-2777 (2002)
   PUBMED   12032089
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..307
                     /product="ribonuclease Z"
                     /EC_number="3.1.26.11"
                     /GO_function="GO:0042781 - 3'-tRNA processing
                     endoribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35006
     Region          3..298
                     /region_name="RNaseZ_ZiPD-like_MBL-fold"
                     /note="Ribonuclease Z, E. coli 3' tRNA-processing
                     endonuclease ZiPD and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07717"
                     /db_xref="CDD:293803"
     Site            order(36,61..62,64,66..67,139..140,207,227,266)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293803"
ORIGIN      
        1 mrftflgtsa grptkkrnvs alavefenes gwylfdcgeg tqhqilkagl siyklkaifi
       61 thihgdhcyg lfglitsrml egcteslliy apkgvkemve svvdisfehl gyklefveiy
      121 ggfeeefekf hlkvlplihs vpsyafyisq kpkvklnark lqndglmpgt fyqdikngkd
      181 vevdgkkyia skyldiregk kiiiagdnae pdflakylen tdlliheaty teevfeklet
      241 kylhttaanl aktaekfrvk nliathispr fegeeileei kkfyngnafv andfdvfelk
      301 eelrrve
//
LOCUS       WP_457563485             188 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563485
VERSION     WP_457563485.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..188
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22002
     Region          24..134
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mrsikyynkn aeilakryds admrefyefi ipylkgktll digcgscrdv vfftslgfdv
       61 ecvepsiefr kicskkdssi kiynqklphi klskkydvvi ligvwmhlrk fyyvkaienl
      121 ksllkrkgvl ilsfstkkrd gfdsinpknl kfiflkngfr llkenisnds ldrkidwvtq
      181 vyildkit
//
LOCUS       WP_457563488             227 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563488
VERSION     WP_457563488.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..227
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
     Region          <1..226
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 lvkilkfldi difipkkqac cgapayftgd fktteelikr nieyfetfid evdailvpea
       61 tctamlkkdy eeyikyhmnn ewlkrhekvk akifgttewl ykytdlekrl nkklnssvty
      121 hdachfgkvf nirkeprali skvveikeme dpnvccgfgg itmqtekfhl arkeglikae
      181 mikkvdaeyv saecsacrmq itehldkvgd nkifvhplei iakaieg
//
LOCUS       WP_457563492             220 aa            linear   BCT 27-JAN-2026
DEFINITION  cell division ATP-binding protein FtsE [Caminibacter pacificus].
ACCESSION   WP_457563492
VERSION     WP_457563492.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Hung,L.W., Wang,I.X., Nikaido,K., Liu,P.Q., Ames,G.F. and Kim,S.H.
  TITLE     Crystal structure of the ATP-binding subunit of an ABC transporter
  JOURNAL   Nature 396 (6712), 703-707 (1998)
   PUBMED   9872322
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..220
                     /product="cell division ATP-binding protein FtsE"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=24434
     Region          4..218
                     /region_name="FtsE"
                     /note="Cell division ATPase FtsE [Cell cycle control, cell
                     division, chromosome partitioning]; COG2884"
                     /db_xref="CDD:442130"
ORIGIN      
        1 maiivdannf sifydntqii kpssfkintg dfvfltgvsg sgktsiikal ygelrpkgsl
       61 rigefemski sksqlatlrr hlgvvfqdfr lipewtilkn vmlpllikgi dkqeaealal
      121 kelkkvklsh kadkypaels ggeqqraaia raiihrpimi ladepisgld eysaslvmdl
      181 fklandsgit ilvashsmpq dfsreyrqlh iekgevyels
//
LOCUS       WP_457563493             706 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Caminibacter pacificus].
ACCESSION   WP_457563493
VERSION     WP_457563493.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 706)
  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
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..706
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=82120
     Region          3..680
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mkkdfeqllq riqnikttee akklllsrvd tpkirkaldf aikahsgqkr ksgedyvihp
       61 ilvatitsyf ndsedviiaa ilhdvvedte ytiwyikdef gsevanlveg ltkiveirgs
      121 slapstsnek laksamtfrk mllasindir vlviklcdrl hnmmtldalp phkqkriaee
      181 tlvvytpiah rlgiatikni ledlafkyll peeykkiddy ikkhkeefql rlnefiqkie
      241 klllkngfke nefeiksrik hyystylkmq rkgisiqevl dllavriivk kpiecyetlg
      301 lihlnfrpli srfkdyiaip kengyqtiht tvydgnsiie vqirtedmdk naefgiaahw
      361 kyklntalpn lewlkdmkye edvedfyela kndlfsediv vyspkfdtft lprgataldf
      421 ayaihtdvgn kaveayvnke kvsllhqlkt gdivrivtgd ksiprcswin alktskakye
      481 qkrlcrqkel eidrkvaiai lstifdldkf kiralikann lcesvpkivd dknflkevvk
      541 kiyqtikkrn llyfkniklk eyvfgnikil snkpiqdisf hycchpkfgd kivglldkke
      601 veihhrfcnn aenkiqkavf vewvkndqnr yflvvslpnr kgelskfinf ltrldifihs
      661 islgkesnnc kleiefddkk rdliknkisk eyrviefipi kdayng
//
LOCUS       WP_457563497             288 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Caminibacter pacificus].
ACCESSION   WP_457563497
VERSION     WP_457563497.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..288
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32370
     Region          1..284
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 masllfvfll gyifkkikgd yskeiieiit nivmpifify yiikleitpk lliisaitll
       61 sislgimisl mislilkldk pstgalmlvt sfgsssfvgi piikalypsk flvyiifygq
      121 tnflfflifg siiisltspk ndkkelnfik kllktptfda flfalilkpl klnvdflkiv
      181 adsliflail tigmrfefkk lfknikiafl vnflkmflip tivflivkyf lginsalkia
      241 iiasampsma laviyglqak lkeeilisvm slgillsfiw ipiftkii
//
LOCUS       WP_457563499             305 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457563499
VERSION     WP_457563499.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..305
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=34423
     Region          6..84
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(7,18..19,21..22,24..25,28..29,31,38..45,47)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          73..281
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mattnervdk flskelnenr nqieqlikkg lvkvnsksik kggvklkqgd iieitfpkte
       61 ekeskkadfd ipilyededl liinkppgvv vhpapsykea tlvdwlkqkg yslstiagee
      121 rfgivhridk etsgalviak nnktheflsn qlkdksmgry ylmllneplk eakcveapia
      181 rnpknrlkma ivnggkeakt lfvpiqdnlt aaklftgrth qirvhltklg ryisgdttyg
      241 kkeqkiprvm lharelylth pngqklsiia plfddfknli qgiddekiss lsnifatydg
      301 mcykq
//
LOCUS       WP_457563506             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563506
VERSION     WP_457563506.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          20..260
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 kkpikidipk keleipeiiv eakcltkkfg sfiaddcidl tlkkgeilgl lgangagktt
       61 likmllglyp idagelkllg tpiksykdri klkskigyvs qlfslykdlt iienlkyfgk
      121 myklsnsein krieeystll gfkeylnyfp kdvplginqr fsvaaalmhd pvvlfldept
      181 sgvdtiaraa fwkmlrkike nwkiailitt hymseaeycd rvvvlkqgkk ivdeevkklh
      241 eqfpglsfee iflefykenr
//
LOCUS       WP_457563504             451 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter substrate-binding domain-containing diguanylate cyclase
            [Caminibacter pacificus].
ACCESSION   WP_457563504
VERSION     WP_457563504.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 451)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   8  (residues 1 to 451)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10098929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..451
                     /product="transporter substrate-binding domain-containing
                     diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52197
     Region          29..246
                     /region_name="PBP2_BvgS_HisK_like"
                     /note="The type 2 periplasmic ligand-binding protein
                     domain of the sensor-kinase BvgS and histidine kinase
                     receptors, and related proteins; cd01007"
                     /db_xref="CDD:270228"
     Region          <292..449
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mrfliffvli kllfavdlns tqreylntrv fniattmkwe pfnteidgkl vgiavdywkl
       61 iakktginyk flikptwiev lqaieygdad lalgagktke rekyavftkp yvtfplviat
      121 rndvgfipni tflrnkiiav gkgytaeall kknypnlnvi svpsidealk mvkegkvyaa
      181 idilpvisyk inkyqydnlk isgqldikfp vrfminksek elvpiinkai deitfderen
      241 iykkwitaqk skpnyfqivi iiilaaiivm liiwvvklki klkyeheyei mleklasydk
      301 ltgvynrqkl eefldmftnv yqvnkepfcv iffdvdnfkk inddfghqvg divlveissi
      361 iqssirkrdi fgrwggeefm iilenckide acniaenirr kiethnfgmn rpvtcsfgvs
      421 eyaggdlkyf llevdeklyk akregknrvi c
//
LOCUS       WP_457563508             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563508
VERSION     WP_457563508.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 358)
  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 358)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..358
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40404
     Region          161..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrflaimkkd ilillrntal mlfliyiftl diylagigik ikpqhvsvgy vdysnslivn
       61 kilthlhkpe fqtpkrflne ealkkaienk kimvglvfdg dfaknyyktg ksqvnvlids
      121 taaaqaqvtv iylneilarf vnlhfplsiq thrlfnqnsn stwfmslael msdvvllvll
      181 lvatvfvkek eegtwdimll mpvssiltif akmfsqvvvi lvgvwvsvgl ilfgvfdmpi
      241 ngnlwhffll nllfafslgg iglviaaisn tvtevgqysf mlmmplifls gawtpissma
      301 pwlqklsivs pvryyiease siffrgasfy dlipyfvall iigmvlfyig ykkigrlf
//
LOCUS       WP_457563509             225 aa            linear   BCT 27-JAN-2026
DEFINITION  LOG family protein [Caminibacter pacificus].
ACCESSION   WP_457563509
VERSION     WP_457563509.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..225
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25662
     Region          41..210
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mrdiqkefld nrnkekdvwr ifrvisdftd afdeledlpp avsifgsara keddiyyqka
       61 meiakklkek gfaiitgggp gimeaacrga ggcvglnill pheqktnpyv ttplkfkyff
      121 trkvtflkys vatvmmpggf gtldelsevl tlvqtgrmsr ipivfygkky yehlikffdt
      181 mlehnyispd dkklfiltdd vdeaveyisn nieeyfksll kanqt
//
LOCUS       WP_457563513             320 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Caminibacter pacificus].
ACCESSION   WP_457563513
VERSION     WP_457563513.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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 10789902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..320
                     /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=37724
     Region          60..194
                     /region_name="YafK"
                     /note="Murein L,D-transpeptidase YafK [Cell
                     wall/membrane/envelope biogenesis]; COG3034"
                     /db_xref="CDD:442269"
ORIGIN      
        1 mrrilalifi ttavfaqnli dtyrfegvns likqiektiq skdywlkrik nddvkfgyfq
       61 sphfilfcnk raktlqvfay kdgklnevam fsniivgklg dkekegdlkt pigvytlink
      121 ikpsntfygp lafvtsypnl fdkvhhkngy giwihgkpld gergdvskgc ivlnndeilr
      181 ldrlinykkt tleiteyplf arkedvaqil atlykwryaw knsdlkkyis fydkdfqrsn
      241 gmnlkefiay kkrvfrnkrg kkveiyfkni kivpyqnikn lpiyeitfhe dyispgyefh
      301 gykeiymikr gdkfkiliek
//
LOCUS       WP_457563515             315 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563515
VERSION     WP_457563515.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..315
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36151
     Region          8..315
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 melpksqqel lrnleklieq tyeaekefie lknilngvie flpqalwvvd ksgevivkns
       61 kadefdfipq kgeievndkv flvqtsnikd ktiisatdit eqkrnerlia mgqmaahlah
      121 eirnpigsis illallkksc pqnemidemk saifrierii kstllfskgi rlnkrkflls
      181 slkkeleeni kyyshskein fvyflpdiei kadydllllv lqnmiinaid aieddekeeg
      241 lievlyektd kyhiiniyds gkdfedtnil fepfkstktk gnglglalsk eiitahegki
      301 elskekkgfk iylpi
//
LOCUS       WP_457563527             531 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome ubiquinol oxidase subunit I [Caminibacter pacificus].
ACCESSION   WP_457563527
VERSION     WP_457563527.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..531
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58568
     Region          5..531
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mhvdltmlew araqfamtal fhfffvpftl gmsfivaffe tiyvktgkqe wkeitqfwql
       61 ifginfalgl stgiihefef gtnwstyswv vgdlfgapla vegivaffme atfaaisffg
      121 wkrvskgvhl asswllaigs nlsalwilia ngfmqhpsne fgffnidtsr lemtnfwali
      181 tqpvaqvkfl hvvsagytla sifvlgissl yllkgkhvef akksatvaaa fglissifva
      241 vigdehayev antqptkias aeglyvgekg apivafgipk nlkatevtsn eegfafkiel
      301 pkmlsllgkr dpnafvpglk dlvngneeyg iwplsklaav gkeakddllk yheakkagdt
      361 aameaakadf ykviwedpkn gikltkadli gygyfanpni dpnliyppvp pvfyafhimv
      421 algfwfillf ilayvsimkg tfvenrlvqk lavisvplpw iatsfgwmta eigrqpwtvf
      481 gvlptaesvt pialqnvqat ffmfltafvi lgiaelkilf tvvkngpkga h
//
LOCUS       WP_457563531              55 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563531
VERSION     WP_457563531.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 55)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 55)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..55
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>55
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          4..>55
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mseivnflvd tigawgyigi fllmflessf fpfpsevvmi pagylaskge mnlyl
//
LOCUS       WP_457563532             517 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide biosynthesis protein [Caminibacter pacificus].
ACCESSION   WP_457563532
VERSION     WP_457563532.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18500220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..517
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=58264
     Region          51..157
                     /region_name="FlaA1"
                     /note="NDP-sugar epimerase, includes UDP-GlcNAc-inverting
                     4,6-dehydratase FlaA1 and capsular polysaccharide
                     biosynthesis protein EpsC [Cell wall/membrane/envelope
                     biogenesis, Posttranslational modification, protein
                     turnover, chaperones]; COG1086"
                     /db_xref="CDD:440703"
     Region          202..478
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(206,208..211,231..232,255..256,277..279,281,296,319,
                     335,357..360,363..364)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(232,234,238,242,255,258,261,279..282,285,289,292,
                     295,364..365,370)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(281,321..323,331,358..359,365..367,370..371,
                     382..384,388,390,425,450,453)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(297,321,331,335)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mneakkllya hifaylvfai lfntfrdffn pmprsailid ffmslffigg lriskrlyle
       61 sfkkeklkpt lvigatpkas aiiknfisde teywptaiid dnpsiintyf snlkvypmaa
      121 iedlinklhi ksviiakdmd skeldrlfek lknldvedik iakllgdrve elkdisiedl
      181 larkpkdldt eaiknfienk tvlitgaggs igseiarqcr kfgarklill dnaeynlysi
      241 teelsdfdmv pvmqsvtdke aiektlakyr pdivvhaaay khvplvefnp kaavinnilg
      301 tknvidaaie ngvkkfvlis tdkavrptni mgatkrvcel yaqnvdsket eivsvrfgnv
      361 lgssgsvipk fkeqiknggp ltvthpevtr yfmlipeacq lvlqaaaiak ggeifildmg
      421 epvkivdlak kmlklygken eieieftglr pgeklfeell ldeteqktky dsiyvtkptv
      481 ydierlnkdi eallnvpeee ivnklknivk efnhnvn
//
LOCUS       WP_457563533             324 aa            linear   BCT 27-JAN-2026
DEFINITION  MraY family glycosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563533
VERSION     WP_457563533.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..324
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36791
     Region          26..272
                     /region_name="GT_WbpL_WbcO_like"
                     /note="The members of this subfamily catalyze the
                     formation of a phosphodiester bond between a
                     membrane-associated undecaprenyl-phosphate (Und-P)
                     molecule and N-acetylhexosamine 1-phosphate, which is
                     usually donated by a soluble UDP-N-acetylhexosamine
                     precursor; cd06854"
                     /db_xref="CDD:133464"
     Site            86..87
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            195..198
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(243,254..257)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mfyvcitvfs flltyvlmvi arkknimdip nersshsvpt prggglaivi afflgvfyly
       61 ykgeipgnll lallsglpiv iisliddivs lsskirflvq mcstglalyf lggleklnfi
      121 ifeiegvwln vvaffgvlwl inlynfidgi dgyaaseaif vslaafilfr esiflllaaa
      181 vggflpfnwq kakifmgdvg saflgfvfgi fivytankei silywlillg lfwfdatftl
      241 frrikneepf tkphkkhayq rivqagfshq ktviyamvvn ivtfvviyis keseylfyvf
      301 iiylcllyll tklidykrpf yasv
//
LOCUS       WP_457563536             264 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457563536
VERSION     WP_457563536.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..264
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31106
     Region          5..>114
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnnekvsiiv pnyngekfik dtidsvkkqs yqnwemiivd dcstdgspni iknlalqder
       61 ikpfflekns grpavprnfa mkkatgkyia fldnddlwhs kkleyqvsim kktgisftst
      121 rkidfkdfei pqnveiksle nislqkithd rlllkniipn ssvvvekkli ddmkfnvsmd
      181 ykavednhmw lrlhqkieys lklmepllfy rivntsisrs klsmakktwn mlkeyevnge
      241 rlgwrrfyyf gsyifyslke riki
//
LOCUS       WP_457563545             419 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Caminibacter pacificus].
ACCESSION   WP_457563545
VERSION     WP_457563545.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45731
     Region          29..369
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkkfvlalfv ivsllsares qqtrlaayek fvkvvnmiea yyvddinttt iinkalkgll
       61 peldahssyl dkkaykelki stngefgglg ivvgmkngvl tiispiddtp aykaglkagd
      121 iilkindkat idmsldeavn lmrgkpgtki tltivrkgqk pftvtitrai ikvksvkakd
      181 lenypkikyi rissfdknvv pslkkilanl knegkegiii dlrnnpggll nqavgtldlf
      241 idkgilvsqk grvksenevy yahsagtykn vpivvlvngg sasaseivsg slqdhkraii
      301 vgettfgkgs vqailpvnkd eairltvary ylpsgrtiqa kgvtpdivvh pakiqkeese
      361 elikeanlka hlkaelakie hkktkkenpk nlqkidgdlq lltgadilka liiqneskk
//
LOCUS       WP_457563552             237 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563552
VERSION     WP_457563552.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>237
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          4..237
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mvindyqtaa kiikdskfpv aftgagisve sgippfrgpt glwskydpki ldidffmsnp
       61 aeswkyikei fydymgntqp ndahkflawl eeigklkgvi tqnidnlhqk agskkviefh
      121 gtankmecid ckrkfysdsi sletlpplcp ecqgilkpdf vffgepippk afeesirlce
      181 nadclivvgt tgeimpasql pilakqngak iieiniepsn ytnsitdifl ndkatva
//
LOCUS       WP_457563561             358 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457563561
VERSION     WP_457563561.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..358
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41248
     Region          1..358
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mkpfivmdvl kkaiemkdvi hleigepdll pspkvktall eavkndkffy teakglrklr
       61 ekiskhyknf ydvevdpeni iittgtstgf liafhfakki atptpgypcy enfaelenke
      121 fikiptkfpe yklktedles idfdtlmiss pnnptgtiys keelkeicef tknnskllis
      181 delyhglvyt dnyttalkyn knaiiingfs kffcmpglri gwmivpenlk reaeiiaqni
      241 lisaptlsqy aaleafdyeh lqktkeefqk rrdflyeelk difpiakpeg afylwcdisk
      301 ysndslkfan emlekakvat tpgidfgeyn nfiriaytkn ieelkiaakr iknfinsi
//
LOCUS       WP_457563562             195 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Caminibacter pacificus].
ACCESSION   WP_457563562
VERSION     WP_457563562.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21320
     Region          2..185
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdylilafvg fvaaltpgpd ifyvirqglc ngsknsliav agilsgnivy lslvylglgt
       61 igknpyfqli vgilgaiylf riaviifnek vsikkecdit kniykealfl nlsnpkamif
      121 favvvtpfls knimlsflal fmgialaflt gaiisskinl eekllntink iasvvfvffa
      181 iklliiafea fkeif
//
LOCUS       WP_457563568             547 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Caminibacter pacificus].
ACCESSION   WP_457563568
VERSION     WP_457563568.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 547)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 547)
  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 547)
  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 547)
  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..547
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..547
                     /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=59656
     Region          1..544
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 msffeiavii lylvaigwlg wmgysktkts tdyllagrdt hpfvmalsyg atfistaaiv
       61 gfggvaawlg nsllwltfln ifvgvfiafv fignptrkmg lrldahtfpe flgkrydskf
      121 iqvfaaliil afmplyatav liggvqflsv yfgvdyhial lifsliitay vlagglkgvm
      181 ytdalqgaim ffamvflifm vinslggida afakldkvwq itvvdrlsgv slkdlvpgsg
      241 dfmmklsqiw gfegwnkmpv fmspgwlfvi ttitlgvgig vlaqpqlivr fmtvkskkel
      301 nravlvggif ilamtgvifi vgsltnawyf enmggknale aagaigkvip hfintamphw
      361 fsfiflfali saamstlssq fhtmgtavgr diletfgank ekttlwtkig ivavilfsvf
      421 laykfqkapa iiarstaiff alcasiflpa fifglfskri tkpaaiasmi vgflvssfwl
      481 lfchfkeaka lgvakalfgv nsllghskwa fvdalvialp lstltlliit altkpdekii
      541 krafgrd
//
LOCUS       WP_457563569             139 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563569
VERSION     WP_457563569.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Hahn,Y., Lee,J., Seong,C., Yoon,J. and Chung,J.H.
  TITLE     Structural analysis of phylogenetically conserved J domain protein
            gene
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 325-333 (1999)
   PUBMED   10542335
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Cheetham,M.E. and Caplan,A.J.
  TITLE     Structure, function and evolution of DnaJ: conservation and
            adaptation of chaperone function
  JOURNAL   Cell Stress Chaperones 3 (1), 28-36 (1998)
   PUBMED   9585179
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..139
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=15809
     Region          70..139
                     /region_name="DjlA"
                     /note="DnaJ domain-containing protein [Posttranslational
                     modification, protein turnover, chaperones]; COG1076"
                     /db_xref="CDD:440694"
ORIGIN      
        1 milktgiiti kdaviltkrq iakkitiivi tdtiktsygn ynynqnsnns ynnssnnnss
       61 nnskkeyqsf tsknpyqvlg cketdstdti kkaykklika fhpdiiagyn lhedfitfak
      121 irtqqinday nkirklrgf
//
LOCUS       WP_457563547             481 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457563547
VERSION     WP_457563547.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Draper,J., Karplus,K. and Ottemann,K.M.
  TITLE     Identification of a chemoreceptor zinc-binding domain common to
            cytoplasmic bacterial chemoreceptors
  JOURNAL   J Bacteriol 193 (17), 4338-4345 (2011)
   PUBMED   21725005
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..481
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55499
     Region          <4..343
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          355..422
                     /region_name="CZB"
                     /note="Chemoreceptor zinc-binding domain; pfam13682"
                     /db_xref="CDD:433401"
ORIGIN      
        1 mnrvvitail vivaaylvfk geyigaigal lplvfvwwpk kevknentld kiqnvvekay
       61 ngeiyhriil dddktkeeki gwhinemldq iedllresqn tikaiiegkd yryilpsglh
      121 gefrnvayef ekaieslkis kkvelianlg krftqidggv penlrrvges iykiddsfke
      181 ialkvknssk qadetyyimq eskndfeels qkvmetssei eqmasqissi sdivelikdi
      241 adqtnllaln aaieaarage hgrgfavvad nvrelaektq katneiaiti qtlqqqfmni
      301 sdntskvvqi seksyktlen fenllnilqr elldvsnisd intlklifit fklhhiiyks
      361 nvyssvtreh vedflldina encmlgkwle ipeikeilik tkyygrfkky heeihnigqe
      421 vllrvkkegv trenedwyyd klvelekyak llfeefekfv etakeenlle qildaskkik
      481 i
//
LOCUS       WP_457563571              84 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563571
VERSION     WP_457563571.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 84)
  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 84)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>84
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..>84
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkillvedde figeaikdyl emqgnkvdyf ssptkaleti ypshydifll dinmpeingy
       61 efyeelknyt sdvpvifita ysdi
//
LOCUS       WP_457563577             216 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457563577
VERSION     WP_457563577.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 216)
  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 216)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..216
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25137
     Region          3..206
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mniliveddy dlhdtikdfl elqgfkcdsa fdgksaveki yekdfdvvil dvklpemngf
       61 evakrvrefs kvpiifltsl dgekdveegf lcggddyirk pfslkelklr idaiikrvyg
      121 dservkirdf efdlknmtly kdgkevhlkp khakllkffi knknqvvskd eifnaiydyd
      181 eevnenslrv fikdlrnilg kdsietlkdr gyrfvg
//
LOCUS       WP_457563578             117 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamylcyclotransferase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563578
VERSION     WP_457563578.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Oakley,A.J., Coggan,M. and Board,P.G.
  TITLE     Identification and characterization of gamma-glutamylamine
            cyclotransferase, an enzyme responsible for
            gamma-glutamyl-epsilon-lysine catabolism
  JOURNAL   J Biol Chem 285 (13), 9642-9648 (2010)
   PUBMED   20110353
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Oakley,A.J., Yamada,T., Liu,D., Coggan,M., Clark,A.G. and
            Board,P.G.
  TITLE     The identification and structural characterization of C7orf24 as
            gamma-glutamyl cyclotransferase. An essential enzyme in the
            gamma-glutamyl cycle
  JOURNAL   J Biol Chem 283 (32), 22031-22042 (2008)
   PUBMED   18515354
  REMARK    Erratum:[J Biol Chem. 2008 Nov 14;283(46):32152]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..117
                     /product="gamma-glutamylcyclotransferase family protein"
                     /EC_number="4.3.2.8"
                     /GO_function="GO:0061929 -
                     gamma-glutamylaminecyclotransferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13728
     Region          1..107
                     /region_name="YtfP"
                     /note="Predicted gamma-glutamylamine cyclotransferase
                     YtfP, GGCT/AIG2-like family [Amino acid transport and
                     metabolism]; COG2105"
                     /db_xref="CDD:441708"
ORIGIN      
        1 mivfvygslk rgkrlhsylk nakflgegvt crpyplivsk svwypyliek kggykikgev
       61 ykitpkllki ldkieeapny yyrkkicvki kgktvkawty fvrkppkftk kelikef
//
LOCUS       WP_457563579             264 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Caminibacter
            pacificus].
ACCESSION   WP_457563579
VERSION     WP_457563579.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..264
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30205
     Region          1..260
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mneiksaaka ikeakyllit agagmgvdsg lpdfrgdegf wraypiakkl glnfqalanp
       61 rwfdinprla wafyghrlnl yrsttphegf killnmphek fvftsnvdgq fqkagfsenk
      121 iveihgsihy lqciepcsde iwenneiiei dmekfealnf pyckecgkia rpnilmfgdf
      181 rfvenrvdrq lenfnrwlsk iddklvivei gagkavptvr hmserikdky kaklirinpr
      241 esdgadieik kgakealtmi sqyl
//
LOCUS       WP_457563585             299 aa            linear   BCT 27-JAN-2026
DEFINITION  PDC sensor domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563585
VERSION     WP_457563585.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Cheung,J., Bingman,C.A., Reyngold,M., Hendrickson,W.A. and
            Waldburger,C.D.
  TITLE     Crystal structure of a functional dimer of the PhoQ sensor domain
  JOURNAL   J Biol Chem 283 (20), 13762-13770 (2008)
   PUBMED   18348979
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13036975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..299
                     /product="PDC sensor domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34148
     Region          <44..140
                     /region_name="PDC1_HK_sensor"
                     /note="first PDC (PhoQ/DcuS/CitA) domain of
                     methyl-accepting chemotaxis proteins, diguanylate-cyclase
                     and similar domains; cd18773"
                     /db_xref="CDD:350341"
ORIGIN      
        1 mhireikdfq kirkearayf cyllqrnlpn klpeitidvv vdglekiihe lpfanaayvl
       61 dakgmqiskm itlkseyqet mvevnqanrt yfykavkekk ciltdpypsl iggdmvvsaa
      121 ypifnnkgel lyvavidipl rellkfmhee kgekwfhnfn rvvyglfsla lfsivvllfi
      181 dgvkmffsyn laqldvkkmf estilltlsl alfdlvktlv seevieekee hpfaihktmi
      241 kflgsivial aieglmlvfk famispqklm yaavllaavt flliglayym ksvgkdikd
//
LOCUS       WP_457563587             627 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563587
VERSION     WP_457563587.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 627)
  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 627)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..627
                     /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=74478
     Region          397..607
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkyrikldki vllfffilsi fifaalffqy nysknvliqn fvnkhyldti kiresfksll
       61 dkaqyyfkta edenlkflnt lplfyskgnf dvngiakiln ensvfgkyev fkidrnykiv
      121 dgsykpdigy dlgkfkaykq ilndvftgkk didissphld vssmnlkryy livspdkkyl
      181 lqlafvvdmf kdakklyeki lkntpdlkkl kiyyvdnyli tpinfknryq qklplnimwq
      241 rtndifqkil kysnvkidlp kndikkqnim lsklvedifk tkhciiknld ldrhqlvfft
      301 mikgvfeksn srliietiyd tskleanies irkrfllifl avvlgifviy kfvidkvsye
      361 ikeivshmke nkrvekvssf ieeiyelknr yndyhekinq eiaknrrlle enkrfivdtv
      421 hqiktpmsvi tlnldyvkni lstkegfndd einesieevd aaiqmllnsy ndlsyiasne
      481 tvdykpqmln lsqivaerin ffsliakann keirydidkd vyfninrief erlvdnnisn
      541 aikysnkkdi yvslkkeddr iilkiesyge riknpievfe rnyrehshkr glgiglnivk
      601 nicekyqisy ktyykdgkni feyifsi
//
LOCUS       WP_457563589             353 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Caminibacter pacificus].
ACCESSION   WP_457563589
VERSION     WP_457563589.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..353
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40171
     Region          2..352
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mykkeldilr kkgrfrerki ydeniidlas ndylglaqne nvrknafsha lnfkshgaka
       61 smlvngyhpa hklledylke lnnfedalvl gsgflanmal felgrkgdlf lvdeeyhasg
      121 ivgakltkae vrffkhndfe dlkkksedfk kfkrvfvvte gifsmmgdkv kkeicefaqe
      181 igfliideah svgicgenll gitqeydlnp qktikmgtlg ktlgsygayi ladeeiisyl
      241 lnraksviyt talspidsll ayyalkeiqe nlshyktlvn qrkltynles likiipaksn
      301 eflqkrqkel lnrnvlvgai rpptvkspif rvilrtnidl ktidetikfl gek
//
LOCUS       WP_457563590             645 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457563590
VERSION     WP_457563590.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..645
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=73655
     Region          2..618
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mikkifagfl illlilvlag agyalylyns trfasakiiy ynpplsakfy drngnlldvr
       61 fskenrfyvk ykdipprvie tllatedtsf fehpgvnfna ilraiikdik agkkvegast
      121 itqqlvrniy lsrkktiqrk ikeiiismkv ehyltkeqil erylnqiylg hgyygiktat
      181 lgyfhkplne lslkeiamli alpkgpslyd ptkhyelnlk ranwilkrmy sigwitdrey
      241 rnalletpkv ykqmvtpkaq yavdtaikql kkefpnllsg gydihlsidl ptqkaaeeav
      301 kwnyerllkk nkkldpnqln galitinqqt gdvlalvggv dyeksefnrv tqskrsvgsa
      361 ikpfiyqial nlgynpasmi pdisrtfkip gdtpeedkyw kpknyekntl glitlrqalv
      421 hsrnlatinl vmsigldrii kgleefgfkn fphdmsitlg slgispwnfs kyytiisnyg
      481 vktyprlvlk vvniknneti efkekheqiq pdyqaylmin imqdvvkkgt grkaqvkgiq
      541 iagktgttnd ykdawfcgft pntetiiwfg nddstslgkg maggsvsapv fkryytkllq
      601 ihpellrefk vpkgvkyfqi nghkelftki spppkqelke eapif
//
LOCUS       WP_457563591             292 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caminibacter pacificus].
ACCESSION   WP_457563591
VERSION     WP_457563591.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..292
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32286
     Region          14..292
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mknnnsfkpe sadnkkglie migatfiwgs tplmsiwsgl psgvfvffrv vfafpfifyf
       61 aikragikef fklkpfwplf vsgialgvnw vfffwtvnti dvasavsiyy lgpiismlla
      121 iwflkergnf yiyisgvlav igavvaaggv hfqegiivaf laavsygalg ffskiatmhh
      181 ravavtawqi lisifitapf lflndwhlsl qgiivafitg vihtalalfl wydalnyikv
      241 siasilqyld ivfamilafl flgqvpqihq ilgagliiia gilstfkeka kk
//
LOCUS       WP_457563593             233 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563593
VERSION     WP_457563593.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..233
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26032
     Region          <2..228
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkialhvpcy inelnpeiar ktllilrhfg lnvsvpknqt ccgqpfinsg qpttlpeqfn
       61 eifkdydyiv spsssctsti rsqelevskk myelceflhd ilqvrdiakn ypkkialhns
      121 chslrhlleg apselnipyf nkvkkvlgge iveakrdecc gfggvfsvke gfisyvmgrs
      181 klddlissgg evitgvdfsc lmhlkgiaek dgddieikhi seiiyesifg eek
//
LOCUS       WP_457563596              92 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457563596
VERSION     WP_457563596.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..92
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10592
     Region          29..91
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvtykefkkk alsnpevkqe yenlkpifei kkqliqarln kgltqeevak rmntsksnis
       61 rleslsnkyv pnlmtlikya nalgckidfr ii
//
LOCUS       WP_457563597             110 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457563597
VERSION     WP_457563597.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Jurenas,D., Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Biology and evolution of bacterial toxin-antitoxin systems
  JOURNAL   Nat Rev Microbiol 20 (6), 335-350 (2022)
   PUBMED   34975154
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Kamruzzaman,M., Wu,A.Y. and Iredell,J.R.
  TITLE     Biological Functions of Type II Toxin-Antitoxin Systems in Bacteria
  JOURNAL   Microorganisms 9 (6) (2021)
   PUBMED   34208120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Rocker,A. and Meinhart,A.
  TITLE     Type II toxin: antitoxin systems. More than small selfish entities?
  JOURNAL   Curr Genet 62 (2), 287-290 (2016)
   PUBMED   26597447
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Goeders,N., Dreze,P.L. and Van Melderen,L.
  TITLE     Relaxed cleavage specificity within the RelE toxin family
  JOURNAL   J Bacteriol 195 (11), 2541-2549 (2013)
   PUBMED   23543711
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Ramage,H.R., Connolly,L.E. and Cox,J.S.
  TITLE     Comprehensive functional analysis of Mycobacterium tuberculosis
            toxin-antitoxin systems: implications for pathogenesis, stress
            responses, and evolution
  JOURNAL   PLoS Genet 5 (12), e1000767 (2009)
   PUBMED   20011113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..110
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12751
     Region          1..108
                     /region_name="COG4679"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:443715"
ORIGIN      
        1 mkwqilffne kveedtlsfp pkilakllhi felieelgpk igepyikyld nglleirakg
       61 qegigrsifc yqkennivil hsfikksqkt pkkelrialq rkkelengnl
//
LOCUS       WP_457563601             458 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457563601
VERSION     WP_457563601.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..458
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=52239
     Region          2..327
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mrvaiigggv tgssiamyld nlgvdvtlfe kndlvsgppi chlhaggnly reitlkekia
       61 llkesidfir lypqaidfrp tivavpvdde gepedlietl eilkneykkm iekdpknkvl
      121 gepedyykly ykkdleklke kefvkepkil dewmipfaky tnlnkikypv ilvqeygvnv
      181 frlsaiakmi lekkgivrye eakvskkgdk wivngeefdy linaagfksg ivddalefkr
      241 drltefkaay vvknkkfdft wpeiifhgkr gtpkgmaqft pyangifqlh gmtkditlfd
      301 dglvssdees sypklpnhfi ekiekgwqke eaasrakrai khmskfipef kdsevtyvpl
      361 fgaqqipgrd aelraveisf eenyarcevv kastvtsmad siakdlckrf gikykkqiei
      421 peilnlsdev itkkaceiak srgypedmgk rnfselks
//
LOCUS       WP_457563604             404 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caminibacter pacificus].
ACCESSION   WP_457563604
VERSION     WP_457563604.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 404)
  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 404)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..404
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46769
     Region          4..400
                     /region_name="GT4_WbuB-like"
                     /note="Escherichia coli WbuB and similar proteins;
                     cd03794"
                     /db_xref="CDD:340825"
ORIGIN      
        1 msktiwiind yagsayhgme frnyyfakew vkrgyevyii sasymhlfkk lpetngvftf
       61 ekidginyvw tkvinygksd nkkrvfkwfe fagklfflpf skmkkpdvii aspmapflvv
      121 payklakkfn akfiyevkdi wplsiielgn ispkhpliki mswcekfavk nadfivsslq
      181 nydehlkedl nierdfvwin ngisleemqk ieplpkqied iipknkfiig yagtvgiana
      241 ldsfleaaqm lkynnkiffl ivgdgreken ltkkygylkn vlfippvkks qvqsllnkfd
      301 vcyiglqnqn lfkygvspnk lfdymysakp iiyainsgkn nivklancgi sveaensegi
      361 kkaiinlynm seddrkklga ngkryvlenf tyeklaqkye rlfq
//
LOCUS       WP_457563605             377 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Caminibacter
            pacificus].
ACCESSION   WP_457563605
VERSION     WP_457563605.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..377
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42851
     Region          2..374
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnipfhktpv tqeeinavin vmksgwltmg pttiefekkf kefigskeav svnsataalh
       61 lalkaigike gdevivptnt fvataevvty fnavpvlcdi eetthninvn kieslitdkt
      121 kaiipvhfag qpcdmdeiye iakeynlkii edaahalpst ykgqkigslk ntditcfsfy
      181 atktlavgeg gmattdneky akhmrinrlh giskdawdry tdkgswyyev vdngnkyntt
      241 diasaiglvq lkrqyellek rksiakkynq afennekiqp lrikkdrtts whlyvikvpn
      301 rdfiinelkr rgvncsvhfi pvhkhpyykt rynlndknye iannvfkksv slpiypdmsd
      361 neidyvienv levlknv
//
LOCUS       WP_457563609             432 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457563609
VERSION     WP_457563609.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..432
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48751
     Region          113..396
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkkvslvlia tgilwaenft qikneitnsl syklaqkkvq iyekklkavk aknygsldfe
       61 ynavhffnqp emkltspqpv avapdgvhli yqdvkatlpm adknhfigei kysyplftgf
      121 gisnlikkse lelikqklel knvkreliln aaklyssiya lkcninalkf aknalntare
      181 kadalykegl inkssvdein akyyeviadi knlksqkesl lnmlsyllnk kidkidgiiv
      241 kkinfspdfq krpdvkaike tlkisdvdik laksklypqi gfvaglkrea dnliltkndy
      301 qnidksylgi gikyniyngg atkseiemak iakasaliyy knylnkvktd yqndlanyka
      361 lffrlkaake evkargsyye yikakfnegl adssdlndai aklaaakakr daikaqiffl
      421 gvklrydgge ne
//
LOCUS       WP_457563603             201 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetyl glucosamine 2-epimerase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563603
VERSION     WP_457563603.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 201)
  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 201)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Tanner,M.E.
  TITLE     Understanding nature's strategies for enzyme-catalyzed racemization
            and epimerization
  JOURNAL   Acc Chem Res 35 (4), 237-246 (2002)
   PUBMED   11955052
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..201
                     /product="UDP-N-acetyl glucosamine 2-epimerase"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0008761 - UDP-N-acetylglucosamine
                     2-epimerase activity [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
     Region          <1..200
                     /region_name="WecB"
                     /note="UDP-N-acetylglucosamine 2-epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0381"
                     /db_xref="CDD:440150"
ORIGIN      
        1 enlkkegfds fdckiiksgd vmqdaamfyk eyakkpqnvk iedkfilsti hraentdden
       61 rlknifeale tiaeekqvil plhprtkkii qnlglklkni tiiepvgyle mvwlldnsdm
      121 vitdsgglqk eafffkkpci tlrdetewve liengfnvla gadknkildv yknfkfnddf
      181 eidlygncka seriirelln v
//
LOCUS       WP_457563616             253 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457563616
VERSION     WP_457563616.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=29302
     Region          61..240
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mkkekayill akqegisnra akdlidrglv ythdrkikia rgllpvntrf kiekvpepkk
       61 ifedenilvv dkppyitsee iskkfkypll hrldketsgi lvltknedfr kkaieefkkq
      121 nvykeylawv kgivaepeti dlpikviktk sgafakvsad gedavteiep ilafrtkski
      181 kaiihtgkth qirahlkaid hpiigdekyg gepykrvmlh hhkfkifdye fespeprdfk
      241 mqeqrdnsrk kkk
//
LOCUS       WP_457563622             322 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein [Caminibacter pacificus].
ACCESSION   WP_457563622
VERSION     WP_457563622.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..322
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36110
     Region          1..316
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mnrrvnyiil avftllltag avyfiywlgk fnankkpkny yqaifhesvs glniaspvky
       61 mgvnigsvkk itinpnepns vivtftvdkn iplrkdsyav lelegitglk yieieggskn
      121 spilktskhh patiktipsf naklfealss ttdklntlld nlntildpkk ashlqnmlih
      181 lekisayldk nkymlkdtiq nfnqlqnnln ktitalrkdi hnltthtikt ekaftqnfnq
      241 lnsnvssfvk nsniliselt kktkegqfdl kdallesfkp idttsneikk atiklenlln
      301 elqnspsdii fkkanplkgp ge
//
LOCUS       WP_457563627             210 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563627
VERSION     WP_457563627.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..210
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23855
     Region          1..201
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mrvilfdldg tlidsteail egfrvvfkkf gktpasddev kkliglpldi mfenlgikeg
       61 vwdyvnayke hyrkiskqkt illpnakeai lkakefarlg ivttktglys kellehfgvm
      121 kyfevligre hvenpkphpe pilkalhqmn ankeaawmig dtcldmvsak eagikyvgve
      181 fkyesqenmr kcaeiikpdv lkaveyifqc
//
LOCUS       WP_457563630             817 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457563630
VERSION     WP_457563630.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 817)
  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 817)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   3  (residues 1 to 817)
  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   4  (residues 1 to 817)
  AUTHORS   Borziak,K. and Zhulin,I.B.
  TITLE     FIST: a sensory domain for diverse signal transduction pathways in
            prokaryotes and ubiquitin signaling in eukaryotes
  JOURNAL   Bioinformatics 23 (19), 2518-2521 (2007)
   PUBMED   17855421
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 817)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 817)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 817)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 817)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18684138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..817
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=94888
     Region          1..359
                     /region_name="FIST"
                     /note="FIST domain protein MJ1623, contains FIST_N and
                     FIST_C domains [Signal transduction mechanisms]; COG3287"
                     /db_xref="CDD:442517"
     Region          <400..817
                     /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 mktynliftt kkeleeffkk lpkkenliqi fsgvldkgei kevtdtiidv ypnakiigtt
       61 tdgeiidgkt tfkkivisvs lfdkvnvktl llpkykrsyl fgkefakklv tkdskvliaf
      121 adamsvnged fingiesesk iivsgglagd narfkhtfvf detniiqnga vgavlegdii
      181 vnnefgfnwe gigksmkiek aiknrvyrid gktpvelykh yfgeefdnia kigirfpliv
      241 krdkmyvara vlkqfddgsv llagnvnegd evrfgfgdvs silykdeelf kkisgfdves
      301 ifiyscmark rflggyikne irpfskvgsv sgfftygeff srthnyffnq tltvlalsen
      361 erkvkidyey nkpkkfftlk altnliknts qelnelnknl eeilrektkq imrksyemeh
      421 mfyydqltdl pnkylfekdi evydvegmvl vdirhffrfn dlygegigdl ilkeiakkll
      481 tlvdnknikl yrwgadqfif vgfekrnfvs lgkkvlellh eklivkidkt sipfdfeavv
      541 svvdkkyknm kakadlalny akrnnlnfii ydksldmess irneintlkk vkkaikedri
      601 ipvfqkieke dsvsyesllr ikennklitp geflevirfs yyyfevmkim iektlslfsk
      661 reekvslnft yrditnknvv kclidqikkh nmqnkvilei vesedlkdfq kvhefikrvr
      721 kegveiaidd fgsgysnfvy ltelkpdyik vdgsliknih kdynsyiitk nilnfaedmn
      781 cktiaeyven eeiykkvkem gfdgyqgnyi hkpqeep
//
LOCUS       WP_457563631             200 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosylanthranilate isomerase [Caminibacter pacificus].
ACCESSION   WP_457563631
VERSION     WP_457563631.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..200
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - L-tryptophan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22435
     Region          1..194
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 mkvkicgitn yedaklacdy gadalgfvfy kpsprfieag vakkiieklp pfvtkvalfv
       61 nmsaesinga meflkadiaq ihfdvekeff dkltckylpv vrakeksdid kfeenykivd
      121 ayvpeyggsg krvalewfen rdnskiilag gltpenvfev grygfygvdv ssgveerpgk
      181 kdkrklrkfi elakyglrcg
//
LOCUS       WP_457563634             399 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Caminibacter pacificus].
ACCESSION   WP_457563634
VERSION     WP_457563634.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..399
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45031
     Region          29..395
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 manlliigag gvgrvsafka aknkdtfdni ilasrtkskc deiakdiknk lgieiktyal
       61 dankeenvid likkenidiv cnvalpyqnl pimhaciktg aayldtalae tednpdtyyd
      121 lqwaldedfk kahtmallgc gfdpgvtsim vkyaadylld eleeieiydc nfgdhgrhfa
      181 tnfdpeinlr elnlpgkywe ngewkttkpf eiqvkhkype cgdatsiliw heelesivkf
      241 fpnlksakfy mcfsdkylyh fnalknvgmf siepieiceg ckisplqfla kvlpdpqdlv
      301 knykgqtnig viakgkkdgq nktfyiynic dhekaieetg ahcvsyttgv paiigcklma
      361 kkiwwsegvh nveefdakpf feemekqglp ikvievene
//
LOCUS       WP_457563632             613 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter substrate-binding domain-containing diguanylate cyclase
            [Caminibacter pacificus].
ACCESSION   WP_457563632
VERSION     WP_457563632.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 613)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 613)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   7  (residues 1 to 613)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   8  (residues 1 to 613)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   9  (residues 1 to 613)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   10 (residues 1 to 613)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10098929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..613
                     /product="transporter substrate-binding domain-containing
                     diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71161
     Region          215..428
                     /region_name="PBP2_BvgS_HisK_like"
                     /note="The type 2 periplasmic ligand-binding protein
                     domain of the sensor-kinase BvgS and histidine kinase
                     receptors, and related proteins; cd01007"
                     /db_xref="CDD:270228"
     Region          <460..609
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mrlillffav flygfnfyip enysgeipnn fkikkykslk dvnftdslvl issdnlpyvl
       61 khnlkilipv gekreyilsn idslskikti anldlpskil ldkvngryke vnatfkdfqe
      121 kkidaivvek krgnedyfdf ylpsygivfn kylivyknnm pnlkninrkf ekifdfkikp
      181 vyvsliltgy ylntkidfnk ilfenyyvqk eaeeklkvav tpnwppfdiy knkelqgigi
      241 dffkliakka glnyrfvrvn ywpdvlemik ekeaditpnt setpdrkkya lfskpyysfp
      301 lgivcnsnsh iksfsqvrei avgkdftaek lmrahypglr yievknvkea lsmaaknkni
      361 cavdmlpvil wniqklsmyn lsliyqtpfk fnlqimvrkd rpdlvqkinm aidslsqeek
      421 nriinryigg ilkeekntnw wpfvligfiv lvfsvsiilk yrkssmtdel tgilnrrgii
      481 keakkisves tllffdidhf kkindtyghd fgdyvlkelt klitqnirns dvfgrwggee
      541 fvlilrgtky pdglkvaeki rkiienhdfk gvkvtisigv apfrgdlqka vekadealyk
      601 aknggrnqvk gie
//
LOCUS       WP_457563635             153 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457563635
VERSION     WP_457563635.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Moynie,L., Giraud,M.F., Breton,A., Boissier,F., Daignan-Fornier,B.
            and Dautant,A.
  TITLE     Functional significance of four successive glycine residues in the
            pyrophosphate binding loop of fungal 6-oxopurine
            phosphoribosyltransferases
  JOURNAL   Protein Sci 21 (8), 1185-1196 (2012)
   PUBMED   22610485
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Vos,S., Parry,R.J., Burns,M.R., de Jersey,J. and Martin,J.L.
  TITLE     Structures of free and complexed forms of Escherichia coli
            xanthine-guanine phosphoribosyltransferase
  JOURNAL   J Mol Biol 282 (4), 875-889 (1998)
   PUBMED   9743633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..153
                     /product="phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0106130 - purine
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17835
     Region          1..147
                     /region_name="Hpt1"
                     /note="Hypoxanthine phosphoribosyltransferase [Coenzyme
                     transport and metabolism]; COG2236"
                     /db_xref="CDD:441837"
ORIGIN      
        1 mnkyyygyee flndldtlqn qikdynpdcl laiarggmtl ghflaermdt kelyslnass
       61 yenetkvskp kifnipdlsh kkrvlllddi sdsgetldev ikilktkypn ieiksatify
      121 kentihkpdy vlkkadrwiv ffwdkegqki ien
//
LOCUS       WP_457563636             300 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563636
VERSION     WP_457563636.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>300
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
     Region          29..>300
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 msnlliigag gvgrvatfka amndhifkni vlasrtkekc daiakdiker lgvevktaqi
       61 damdvdatak likdtksdiv lnvalpyqdl aimdaclkag ahyvdtanye hpdeakfeyk
      121 eqwakhedfk kaglmallgs gfdpgvtnvf tafaaqelld eieyldildc nagdhgypfa
      181 tnfnpeinir eitqkgkyye ngewkeiepm svkfdweypk vgkfpsylly heelesltkn
      241 fpsikrarff mtfsdkylwh lralqnvgmt siepievceg ckispmeflk kvlpdpaslg
//
LOCUS       WP_457563647             193 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563647
VERSION     WP_457563647.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..193
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22205
     Region          7..173
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(48,50,52..53,116..117,133,173)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 meilvkpcge fytncyivdr kiiidpgiga yefvrehvdk plaiinthgh fdhmwddkti
       61 kemydipiyi hkndafmlen dpfgynppkv kpdylleegd ikigdydiki rhfpghtpgs
      121 itieigdemf sgdfifdgsi grvdfpyssa edmkksiekf lkipydkrvl pghgptttik
      181 kaqkflptwl eyl
//
LOCUS       WP_457563650             267 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563650
VERSION     WP_457563650.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12089052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..267
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30735
     Region          3..263
                     /region_name="Hydrolase_3"
                     /note="haloacid dehalogenase-like hydrolase; pfam08282"
                     /db_xref="CDD:429897"
     Site            order(6..10,37..38,195,217..218,221..222)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 mifitdldkt flksdlsisd fsrrvwnefk yplsvatars ykgsigllkg lkldfpmill
       61 dgamiakpdg eilkitsldk ntgdsiieev yknfkdypli vgfdeigdek flypkklnpy
      121 qkhllenykn dsrvlnidnf ralkhnlkmv ylgqkeflee iekfiknhfd vetklteday
      181 gpywfltvlh keadkahglk hleemmnidk ekvtvfgdni ndigmfewag tsvavknale
      241 evkkradivl phtndedava kylkeik
//
LOCUS       WP_457563654             445 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563654
VERSION     WP_457563654.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..445
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50079
     Region          <309..426
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkklwilill liigaggfvy fspmfeknpp kitiktdgyt nlknpievdl kddsgiksyt
       61 vvlmngnnte viasadnpnm gknvtlkikl pknikaneir lvvtavdtsk whffagneaq
      121 ksvtlevdkv apdaqvvnns yaigrggsaa avvqvndknl kdayilvdgk ykfkltpfyk
      181 kgyyvaliaw piwennfdat lvaedyagni vrehipyywr trgiynpkdv kirindkfin
      241 qvakrlleri gmsipndpve ifkkvnetvr kineakisqi tspvyeekin sfyirrfnpl
      301 pgsakkadfg ekrhyyykge qisfaihkgv dlakikraki yannngrvva neyigiygna
      361 liiyhglgly tlyghtsefk vkkgdsvhng mviartgatg avfgdhlhfg vyvqgipvqp
      421 lewmdphwik tnilnvinga krmik
//
LOCUS       WP_457563655             198 aa            linear   BCT 27-JAN-2026
DEFINITION  uracil-DNA glycosylase [Caminibacter pacificus].
ACCESSION   WP_457563655
VERSION     WP_457563655.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 198)
  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   2  (residues 1 to 198)
  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 10178243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..198
                     /product="uracil-DNA glycosylase"
                     /EC_number="3.2.2.27"
                     /GO_function="GO:0004844 - uracil DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=22781
     Region          44..188
                     /region_name="UDG-F4_TTUDGA_SPO1dp_like"
                     /note="Uracil DNA glycosylase family 4, includes
                     Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA
                     polymerase, and similar proteins; cd10030"
                     /db_xref="CDD:381680"
     Site            order(49..53,56,62..63,90,172)
                     /site_type="active"
                     /db_xref="CDD:381680"
     Region          49..53
                     /region_name="motif A"
                     /note="motif A [structural motif]"
                     /db_xref="CDD:381680"
ORIGIN      
        1 mgdwknrlke fyktraefik ahlnenidft dvfdpyleek ndnpimiige apgenevkqk
       61 qpfvgkagen lnylisisgf drkrdflitn afpfrtfqdk knrtpkakel kigaellkke
      121 ieivkpkiil llgnsaikaf sylvkdvknl qkcgyydids eigklkigvc yhpsplafnr
      181 keireslekf fknlskav
//
LOCUS       WP_457563656             166 aa            linear   BCT 27-JAN-2026
DEFINITION  shikimate kinase [Caminibacter pacificus].
ACCESSION   WP_457563656
VERSION     WP_457563656.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..166
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19061
     Region          6..165
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 msagnviltg fmgsgkstig rilakelnty fidtdnliey fenrsikeif ekegeesfrk
       61 kerycfewik nnvkntvisv gggfpvfipe ikeagvviyl kadfddilkr msedeiakrp
      121 lfqdikkake lfskrdniyr qladyiienr didetikkik giidas
//
LOCUS       WP_457563660             288 aa            linear   BCT 27-JAN-2026
DEFINITION  EAL domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563660
VERSION     WP_457563660.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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 288)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..288
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <6..286
                     /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 eislsagige siekadmalk yaknkkmgki vifdenleiv knykeymewk niikqalrdd
       61 kiipyvqpiv daktketkky evllrlehng kiyppffleh akraglyvdl qkvmikksfe
      121 vfskidskfs inlsvmelsn vsfkkylldm idkykvsekl tielledekl mdeellgfli
      181 flkemvgvei aiddfgsgns nisylirkmp vtilkldgsl ikdmmknenn kkliqvivsm
      241 akifelktia efvenaeiae clekygvdcl qgyyfskpfd innlkekg
//
LOCUS       WP_457563662             435 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457563662
VERSION     WP_457563662.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..435
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47009
     Region          4..417
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msekkafntl saamlgigtm vgigifivig lagsiagnlv wisfviggii allsgyslak
       61 lairfpsrgg iieylvqefg enpfsgslsv mfyfaqlvtl aavaksfgey garlfgyhsk
      121 fmidafavgi ilfftfinll gatlvaksen iivaiklial tiftiaalmt ikpqylsmkd
      181 appiinavfa igltffayqg ysvitnaied menpsktilk amfiaigvvt ilyvsvsiav
      241 lgnlplsevi kakdyalaea akpvfgelgf kimsvvalis atsainatiy atteisytla
      301 kkgelpkiye ynvfhsyegl listaliipm vlffnlseit tvaalsvlii qalvhfghik
      361 ltpktgankg viifafllmt fvvlatlyyn akqdikiiyy liggfviayi ieiilrklfn
      421 rtvkkqikgl tgelf
//
LOCUS       WP_457563666             122 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563666
VERSION     WP_457563666.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 122)
  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 122)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..122
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <4..111
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 rkvyalgiad fiqkpvflee iifklkkycp krirlndiei dfynkivskn gelvkltqke
       61 asllflllqy knrivtyemi rddiygytyp sdnaihllvs rlkrklklni isvpkegyil
      121 kv
//
LOCUS       WP_457563667             366 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Caminibacter pacificus].
ACCESSION   WP_457563667
VERSION     WP_457563667.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..366
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40357
     Region          1..358
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 milatpgpve iplfvretfl ketihhrtpe fkeilleale rfkkithlpn avflsssgtg
       61 ameaavinsv kkkaltinag kfgerwgkic eahgiefkei kydwdtpasv deviaaieed
      121 kdidtffiqi sesagglrhp veeiaaeikl inpdivvvad gitalgvedi dtsnidivig
      181 gsqkafmlpp glamlglsdk averigkgrg fyfnlaneik kqkegttaft patsliialn
      241 evmkkleeig ldkhyettak rhkaiiaaie aiglsvfpqn palsmaavyf ekaeelrkil
      301 ktkyevnvag gqdfmkgklf rinnmglied ykmehilnsv elaldelgir kydatavkvy
      361 sneklr
//
LOCUS       WP_457563670             427 aa            linear   BCT 27-JAN-2026
DEFINITION  NCS2 family permease [Caminibacter pacificus].
ACCESSION   WP_457563670
VERSION     WP_457563670.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..427
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45519
     Region          1..427
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mferifklse hgtnvstevr agfttflamm yivpvnasim sltgmpfdal itatavvtii
       61 atilngfwsn tpvamsvgmg lnayftfglv kgmhlpwqta lgivmisgli flvlsltrfr
      121 awvfesvpid lrraisagig afiafiglkg mgvivsnpat fvtlgnlhsp evllgvegfi
      181 laalfysyri kgafilsial tsitawvfgl gklpegiism pasiapiafk fdiwdalkls
      241 lvpvivtflv tdlfdtigtl agigmraglf kdpkelektl qadaaatvig aslgtsttts
      301 fiesaagvee ggrtgltavv tgllfittlf flpifkaipd naiypilvmv gvlmfgelrd
      361 vdfsdittsv svfltvilmp ltysitlgls agfvvyfila llrgekekit fgtasialig
      421 llmfivh
//
LOCUS       WP_457563671             363 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563671
VERSION     WP_457563671.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..363
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41878
     Region          73..358
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqqnsfesll nilnykflsl plykivlafv vlflflvlrr aftlyilkff rflvrktkte
       61 lddkflkaik nplrflfvia glyffflfle vdyaiikhil kgllifdifw alynivgefe
      121 eyiykalgkf grasrefvsf iikllkifiv sigiiallqd wginvtgfla slglgglafa
      181 laakdtaani fggiailtdn ifkigewvkv gnvegivedi gmrttkiraf dkrliilpna
      241 tiansaveny srrdkrrimm riglvyntpi etikkitdei relllnhpdi akdeslliyf
      301 dqfedsslsi fcyfftntav wkdylrired inlkiidive rngsafafps nsiyfetplk
      361 ier
//
LOCUS       WP_457563673             382 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Caminibacter pacificus].
ACCESSION   WP_457563673
VERSION     WP_457563673.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..382
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42535
     Region          1..382
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mqkvdhkifi ivavlmlaga vfsftlpvfl emrrhlseyh flgryilfgs vgflimilla
       61 nlnpdkwfnk igwiifiisg ilvlilpflp esiapiinga krwikigpfk fapveffkig
      121 vifflswsft rkikkthhlk edikqflphl iflglfwili vfmlsdlgqv fvmislfilm
      181 llaaggklkt fgimvlagis iiipailfap yrfkrikdwl ytassnflpq pivdgssany
      241 gqviqsmnai hhggifgtgl gngifklgfl sdvhtdfvla giaeetgiig iglitfligy
      301 liyrifkiaf rsekkeyqlf algvgsliai qfiinglgvt slipikgltv pflsyggssl
      361 malctaigmv lmiskrakyi ke
//
LOCUS       WP_457563672             569 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563672
VERSION     WP_457563672.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..569
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=64987
     Region          41..554
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnnripaifl ffiffisvvf aafvflaiak pmgyfnpkik itqsavrgdi ktkdytvaks
       61 eklygvyvyp kyldpdkkql fytlfsiytd ipvrelkrav iigkqnglsr iriatvdlkt
      121 kqnliylrkv ldkkrvfltd krtgirlgye iesldfkrvy pykdtlqpfl gryrkderrg
      181 dnglelyynd vlsakqdgyk igyrdvygni iydksakikr pingkdikln inlalqrkie
      241 kflsfqkqkl qakevlaavm dsksgkilai assnrydpah itprdipnmk isavrevfep
      301 gsvmkpitfa illennkvnp yevlnahngr wkpewrktpi rddepfnwls aedaivhssn
      361 ivlselslrl tpdeffnglk kfgfasgtgi dlpyevkgmi rsrrllnypi yksttaygyg
      421 ilvtfvqllk aynafnnygi evtprlanmp seskrvmsak naeimlkilr kvvlkgtgka
      481 aivdgiftag ktgtahvsmg kkgyqqiyns sfigfandkn hrytiavtff dikakwpnyf
      541 asksavptfr kiidiminen llketnatk
//
LOCUS       WP_457563677             284 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457563677
VERSION     WP_457563677.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..284
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34030
     Region          9..104
                     /region_name="Glyco_tranf_2_4"
                     /note="Glycosyl transferase family 2; pfam13704"
                     /db_xref="CDD:433416"
ORIGIN      
        1 mltmtilvkn eidiieknir fhakkgidsf vvmdnnstdg trelledlkk efeitiidek
       61 gtynqakwmt klthiarkky npswlipnda defwyaetdl kealknqkka vltvdrfnfl
      121 lyeglnnwwe seirvenpif yrkntqlsse nisiiltkis pkviikpkgl lwirggnhka
      181 lhlldfrdyf rhydkikrfe kirvfhypir syeqfkknie nrkkllekga kmgphykrwv
      241 kllrvgklee efynnlvfkq neinvlkkyg vvvedkrmkn cfny
//
LOCUS       WP_457563678             565 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563678
VERSION     WP_457563678.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 565)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 565)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 565)
  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 565)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..565
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64026
     Region          1..563
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mfqllkeylp yyknykkeif faiigmilvs aataataylv kpvldkifiq kneqmlyilp
       61 laiiaayllk gigavlqqyy vsyigedivr qirdkflnhi lnfeldyfkk thsgelvsri
      121 indinriqna isnqmanmlr dilmaiflla vviyqnprla ffaliilpii iypigkiskk
      181 lkklskeaqv ktaelnqhls eifknietik aynakkyeld efkkhnlkyl kinlktiktr
      241 aflipiletl satiaaivii iggkeviegk msvgaffsfm talfmltdpi rrismsyskm
      301 qdaiaanerl kelfkklpqi ssgkeklkei nditfknvsl kygdktalkn inykakkpki
      361 iglvgdsggg kssfvslilr fydasegevl indkniknyd lhslrekiay ipqnihifnd
      421 tiaaniaygk eideekvkna lkkanlldfv eslengiyti lneggsnlsg gqrqriaiar
      481 alygnpdvli ldeatsaldn kseavimkti enlkdklvfi vahrlstien adeilvfkng
      541 kivckgkkee llencetfkr lynke
//
LOCUS       WP_457563681             123 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system death-on-curing family toxin,
            partial [Caminibacter pacificus].
ACCESSION   WP_457563681
VERSION     WP_457563681.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Cruz,J.W., Rothenbacher,F.P., Maehigashi,T., Lane,W.S., Dunham,C.M.
            and Woychik,N.A.
  TITLE     Doc toxin is a kinase that inactivates elongation factor Tu
  JOURNAL   J Biol Chem 289 (11), 7788-7798 (2014)
   PUBMED   24448800
  REMARK    Erratum:[J Biol Chem. 2014 Jul 11;289(28):19276]
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Castro-Roa,D., Garcia-Pino,A., De Gieter,S., van Nuland,N.A.J.,
            Loris,R. and Zenkin,N.
  TITLE     The Fic protein Doc uses an inverted substrate to phosphorylate and
            inactivate EF-Tu
  JOURNAL   Nat Chem Biol 9 (12), 811-817 (2013)
   PUBMED   24141193
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Van Melderen,L. and Saavedra De Bast,M.
  TITLE     Bacterial toxin-antitoxin systems: more than selfish entities?
  JOURNAL   PLoS Genet 5 (3), e1000437 (2009)
   PUBMED   19325885
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Garcia-Pino,A., Christensen-Dalsgaard,M., Wyns,L., Yarmolinsky,M.,
            Magnuson,R.D., Gerdes,K. and Loris,R.
  TITLE     Doc of prophage P1 is inhibited by its antitoxin partner Phd
            through fold complementation
  JOURNAL   J Biol Chem 283 (45), 30821-30827 (2008)
   PUBMED   18757857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..123
                     /product="type II toxin-antitoxin system death-on-curing
                     family toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
     Region          12..121
                     /region_name="Doc"
                     /note="Prophage maintenance system killer protein
                     [Mobilome: prophages, transposons]; COG3654"
                     /db_xref="CDD:442871"
ORIGIN      
        1 knelinkkea telfgqeren sfkgiirniy qtfggvdllp tieekaanlf yyivkdhpfv
       61 dgnkrigafm fvlflsknny lydendelki nsnalvslal liahsnpnek dliiklimnl
      121 ige
//
LOCUS       WP_457563682             209 aa            linear   BCT 27-JAN-2026
DEFINITION  HesA/MoeB/ThiF family protein [Caminibacter pacificus].
ACCESSION   WP_457563682
VERSION     WP_457563682.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..209
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23621
     Region          1..187
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mfrrqievig eknqeklsek svlivgcggl gniiattisc iglrkiylid ydtielhnih
       61 rqfqfskedi gksksktlce kinrcentei ialdgmfden meidvdlvfd atdnfevrkk
      121 idsfakakki pwiyasveet rgqvgvfrkt sfeifatkah evkgqlppmv nligsiasms
      181 glkcligeck evlyyvdfse dleinkfsf
//
LOCUS       WP_457563698             187 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563698
VERSION     WP_457563698.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..187
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22519
     Region          1..182
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mdkiffngve ikykitkkpi knvylrvked hvevsashfv pksfiekfil knaehiikkf
       61 enqkyyflfg kkylnngidv kelykqktpe ivlpfvyeya kkmnlhpskv sfrfnksrwg
      121 scsykdsiif nfylaklpvd iieyivvhel ahikhknhqk efwslvgeyi pdykdrikrl
      181 rklekef
//
LOCUS       WP_457563697             271 aa            linear   BCT 27-JAN-2026
DEFINITION  TIGR00282 family metallophosphoesterase [Caminibacter pacificus].
ACCESSION   WP_457563697
VERSION     WP_457563697.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..271
                     /product="TIGR00282 family metallophosphoesterase"
                     /EC_number="3.1.4.16"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30068
     Region          1..234
                     /region_name="YmdB"
                     /note="2',3'- and 3',5'-cNMP phosphodiesterase YmdB,
                     calcineurin family [Signal transduction mechanisms];
                     COG1692"
                     /db_xref="CDD:441298"
ORIGIN      
        1 mnilfigdiv gkpgrkmvkr ylpmlkkekk idyvignyen lahgfgitpk tfkemknagi
       61 diftggnhtf dkkkeaiell sageilrpln yfeapgswyy edeniivisa mgvccmpygk
      121 npfieldnfl kekkkfvfid fhaeataekr aifhllkkra saiigththv gtddleideg
      181 ccylsdvgit gcrdnvigmk idgpianmlt glkqhydvpd ncksifqavl iesdginakk
      241 ayklkafdds gimitqiage gevgnceivk l
//
LOCUS       WP_457563684             249 aa            linear   BCT 27-JAN-2026
DEFINITION  TatD family hydrolase [Caminibacter pacificus].
ACCESSION   WP_457563684
VERSION     WP_457563684.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..249
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28920
     Region          2..249
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 miidththld nekfiddvde virrakdagv ekfiipaadp kdlpraiela qnyedvyfav
       61 gfhpvdidky deklitcfit hpkcvavgei gldyhwvkep ekrqkqielf hrqieiskey
      121 dkpiivhird atedsvkvie ahpdikgvfh cynaahqllk fsdrfyygig gvitfknark
      181 llevfpkipk drviietdap yltphphrgk rnepyytiyv rdkiaelwgv tpqeveeitt
      241 qnakrlfki
//
LOCUS       WP_457563706             140 aa            linear   BCT 27-JAN-2026
DEFINITION  ketopantoate reductase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563706
VERSION     WP_457563706.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>140
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          1..>131
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkilvigvgg vggylaykli kcnkdvtisa tkktietikk eglkvidvdk eeivfpktei
       61 kgiydlifvt vksynidnil pliknhsnen trvvpilngi ghfekfenln vkllkaciyi
      121 lsnkkdinvi hkktplfylc
//
LOCUS       WP_457563680             403 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate
            ligase [Caminibacter pacificus].
ACCESSION   WP_457563680
VERSION     WP_457563680.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Gordon,E., Flouret,B., Chantalat,L., van Heijenoort,J.,
            Mengin-Lecreulx,D. and Dideberg,O.
  TITLE     Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:
            meso-diaminopimelate ligase from Escherichia coli
  JOURNAL   J Biol Chem 276 (14), 10999-11006 (2001)
   PUBMED   11124264
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..403
                     /product="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,
                     6-diaminopimelate ligase"
                     /EC_number="6.3.2.13"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008765 -
                     UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45351
     Region          <58..403
                     /region_name="murE"
                     /note="UDP-N-acetylmuramoylalanyl-D-glutamate--2,
                     6-diaminopimelate ligase; Provisional; PRK00139"
                     /db_xref="CDD:234660"
ORIGIN      
        1 mdlihylnns litdntkeld snklflktsq nskyakdikn yitpkellks lnlktkfigi
       61 tgtngkttta fvlgyllnsl gysvgiqgte gfyfngelke pktlttppif ttikrafkyk
      121 pdfyimevss haivqdrieg lefeakimts fsqdhldfhk smeeykqvke sffqddsiki
      181 ingkckmeng kliivniggy dfkvnpnnly vlekpivddi pmagefnkmn fslalktasl
      241 ltnsslstfd fslfkgvagr meivskdplv iidfahtpdg mekvlsaveg kkivvfgagg
      301 nrdkdkrhlm gevaskyady iivtndnprc enpqdiakdi ikgiskpyev ifdrkeaikk
      361 alklakeknl tlmilgkgde kymefcdkki pfsdkeavfe vis
//
LOCUS       WP_457563713             276 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caminibacter pacificus].
ACCESSION   WP_457563713
VERSION     WP_457563713.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..276
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31301
     Region          6..274
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mlrkyadfll vlvalswgst filvkkaied lpafsflfvr fflafllmyv ffhkkieidk
       61 kilkaslilg flnfsayalq tvslyylpsn ivafltglfv iftpvsayff fkkeipkkvi
      121 iaailaflgi yfltqarfaf siyvflvilc affyalhinf tdifskkyni fslvtfqflf
      181 vaifslflip fedlhnvkis ftvvfaiiit vvfatvfaff vqtfaqqftt ptktaiifal
      241 epvsaaflga ffgeslnikq iiggvlvvis miiaei
//
LOCUS       WP_457563722             321 aa            linear   BCT 27-JAN-2026
DEFINITION  3-phosphoshikimate 1-carboxyvinyltransferase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563722
VERSION     WP_457563722.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Marques,M.R., Pereira,J.H., Oliveira,J.S., Basso,L.A., de
            Azevedo,W.F. Jr., Santos,D.S. and Palma,M.S.
  TITLE     The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a
            model for development of novel antimicrobials
  JOURNAL   Curr Drug Targets 8 (3), 445-457 (2007)
   PUBMED   17348837
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Stallings,W.C., Abdel-Meguid,S.S., Lim,L.W., Shieh,H.S.,
            Dayringer,H.E., Leimgruber,N.K., Stegeman,R.A., Anderson,K.S.,
            Sikorski,J.A., Padgette,S.R. and Kishore,G.M.
  TITLE     Structure and topological symmetry of the glyphosate target
            5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein
            fold
  JOURNAL   Proc Natl Acad Sci U S A 88 (11), 5046-5050 (1991)
   PUBMED   11607190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>321
                     /product="3-phosphoshikimate 1-carboxyvinyltransferase"
                     /EC_number="2.5.1.19"
                     /GO_function="GO:0003866 - 3-phosphoshikimate
                     1-carboxyvinyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009423 - chorismate biosynthetic process
                     [Evidence IEA]"
     Region          1..>321
                     /region_name="PRK02427"
                     /note="3-phosphoshikimate 1-carboxyvinyltransferase;
                     Provisional"
                     /db_xref="CDD:235037"
ORIGIN      
        1 milevisgkk feekfkvdad ksishrcaif slltsgqnvi knylraedtl nslkiaeslg
       61 akveddgeti kieapkklqe andvlycgns gttiriymgl lagidgffvl tgdqylrkrp
      121 marvanplrs igakidgrdn gnlaplairg gelksfdyes kiasaqvksa lilaglnadg
      181 eshykepfls rdhtermlkg mgaeietkin ddlscevfik plskpleplv itvpndpssa
      241 fffavaaait ksvaiienvt lnptrieayk vlekmgveie yvekenkyep igdiivkgke
      301 lkgvevskni pwlidelpal a
//
LOCUS       WP_457563730             253 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563730
VERSION     WP_457563730.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  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 11459733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28534
     Region          109..253
                     /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 mknddllnin pkkdmkkpli yaaigflifi iiviavaifq nmssgknnei lppqpkteke
       61 ikpqeefkpl pietanenta dqnanqnenq nvnentqnna ntntnaqtpa atqtnttqnn
      121 trtqkpkpqv tqepvknekp qakeqktqki tkkpvkvtkp avttkpkkvv ygkyyvqvaa
      181 llknakpnkk flallkkygf nykyihtyiv kngekikvtk ilvgpyktrs dakralakik
      241 revtqnafiy kak
//
LOCUS       WP_457563729             469 aa            linear   BCT 27-JAN-2026
DEFINITION  anthranilate synthase component I family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563729
VERSION     WP_457563729.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..469
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53625
     Region          13..463
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 mvfdkflvde fspiaiyntl sslfpsermf lfesvinntd gnysfifige kervsykdyk
       61 tyyfdgekee vldkdpfsff keyyskidke kykklsrelk igfvdgfvgy igydmvkvfe
      121 pvlkpvmdnl kdetdipdly mirpkivvgf shksseltvi indkkyekhl yvirdsinst
      181 ykhlpikpak ileepkfvfs kekffemvkn akenikagdi fqivlsnrlk vkaivdrfsf
      241 yrklrsknps pylyyldidd faivgsspev mvrlnddlil lrpiagtrkr gatlkedlem
      301 ehdmindpke vaehimlvdl grndvgrvak agsvkveelm rveryshvmh mvsdvvgeld
      361 skydmfdlfk atftagtmtg apkikameli akyeglkrgy yagsigyfgf dgnmdsaiti
      421 rtalikddev ifqagagvva dskpeleyke vnnklgalva tlkdldggn
//
LOCUS       WP_457563734             574 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Caminibacter pacificus].
ACCESSION   WP_457563734
VERSION     WP_457563734.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 574)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 574)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 574)
  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 10006830
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..574
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66949
     Region          <82..310
                     /region_name="COG2984"
                     /note="ABC-type uncharacterized transport system,
                     periplasmic component [General function prediction only]"
                     /db_xref="CDD:442223"
ORIGIN      
        1 mrilfllfla vflfaknvli insysiklpw tkgelegile kinnkqnlki fiefmdtkyf
       61 qptpmrmlny yyylkdkykn infdivittd dnalnfvrky knepifsnak vffagvnnlk
      121 ladtlsknvy agvfekkepl vnlnfakkiv pnlktvyvva dnsnsakavm keyknafkni
      181 ksptliylne knlenileti kkapknsaml lltpfsfsle dshisykyai alisqvfphp
      241 iiihtdllan vpnsnvvggk atdaltqgke agkkvleyls gtpmqkigft fekankmyln
      301 vlnlkkfgid ayalgyknai yvnkprtfye mykewiigsi iiffavlmmi vililkniql
      361 kkynekiskm nkeleekifs alselkekek lllhqtkvsa igemflmvsr kikeklhkll
      421 ekeetkeeat yilnkltmie kyfndssvle fdlkeatkev vyslkdvlne glveikgeni
      481 yifgyknkfq qvildflynm skfqneieki ifefkedkie ihirfkhfsk nlidnfenvl
      541 nnelyytrli mqqyfcsecn yrvdknsvim eiil
//
LOCUS       WP_457563737             209 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Caminibacter pacificus].
ACCESSION   WP_457563737
VERSION     WP_457563737.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..209
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23803
     Region          1..197
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mkillleddf tladtlkevl esegfevdia nnaqeayekt fnekydlyif dinlpdengi
       61 evlknlrdad detptiyita ltdlntmska fdagaddfik kpfepeelli rlkaklkphh
      121 diikindiey dpqtkevkkn gkiislgfvl kdifhelitn knkvvpkdrl leltnahsda
      181 tlrvnitklk nklgidikni rgegytiel
//
LOCUS       WP_457563736             402 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563736
VERSION     WP_457563736.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..402
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44461
     Region          18..238
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          146..402
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mesfkiafrn lirmgrrtfl tgsliaigvv fvvlyityae sfknsmiaqi tdsvmgelqi
       61 hkkgyvssld slpldknlpp ktvkkieekl nsmpeiysys krlkfggmis nytdstnirl
      121 ngidpemeak tlpllkerln ghlpkegeiv ipeliakglk lkkgdvvvlv atnkngsmna
      181 ktfkisgvvg iisgpggrdg yinikdarkl lrikkpeine iviklknpem lekvnkelig
      241 ftktiqkpkl evhtwiklsp faniikmldi mtfsieiili sivlvsilnv mimsvferik
      301 qigtmkamgt sksfivsmfv neglllgifg fiigvaasva fvyligdihy nfgrqsnlll
      361 vphidyksvl svgamvviia iiaslypafk aaslkpieal rs
//
LOCUS       WP_457563742             208 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA threonylcarbamoyladenosine dehydratase [Caminibacter
            pacificus].
ACCESSION   WP_457563742
VERSION     WP_457563742.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..208
                     /product="tRNA threonylcarbamoyladenosine dehydratase"
                     /EC_number="6.1.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008641 - ubiquitin-like modifier
                     activating enzyme activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0061503 - tRNA threonylcarbamoyladenosine
                     dehydratase [Evidence IEA]"
                     /calculated_mol_wt=23247
     Region          12..204
                     /region_name="YgdL_like"
                     /note="Family of activating enzymes (E1) of ubiquitin-like
                     proteins related to the E.coli hypothetical protein ygdL.
                     The common reaction mechanism catalyzed by E1-like enzymes
                     begins with a nucleophilic attack of the C-terminal
                     carboxylate of the ubiquitin-like...; cd00755"
                     /db_xref="CDD:238384"
     Site            order(25,27,29,49,51,60,71,108,114)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238384"
     Site            order(29,115,130..131,137)
                     /site_type="other"
                     /note="putative substrate interface [chemical binding]"
                     /db_xref="CDD:238384"
ORIGIN      
        1 mrydrckklf gkfehlqkln vlicgvggvg gyaldclyrs gvknitivdf dtfditnqnr
       61 qigseflgek kvevlarlyp gvtpidmklt pqnienldle kydividaid dlnakialil
      121 kaypkivssm gaakrieptk iridsiwktq ndpfakkird rlkkenfkgd fkavfslekp
      181 ipcdmgsfvg vtgafgfalc sevlkdfv
//
LOCUS       WP_457563748            1039 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caminibacter pacificus].
ACCESSION   WP_457563748
VERSION     WP_457563748.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..1039
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116913
     Region          1..1020
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkriieffik naafthtlfi iviisailay knvpkelfpp atldkiliqg aypgarpetl
       61 dkmavvpied elktyqevss vesvissgnf vitvnlkpgs nklellnefk nvvanirqdl
      121 psdmteptvt iakkafplmf isvasntlnk dqllkaadev kkelsklkdl tqveirgdsd
      181 kniyfeldnk kiealgldkt llinalssvn tifpvgkved skhyfvsmfp qgvkdfkntl
      241 ikvgdkivrl sdiaivkkay atptqigkyn gipnitidvr kgesgdaial skkireilke
      301 yhkkhpevif gistdtskwv rnrfntvvsn iifglilvff imwiflnwri slvvtlgipt
      361 sfaiamiald yynfslnlls mlgalialgm ivdeaivvge niyrhmemgk tklqaaidgt
      421 vevfwpvvaa amttvlaflp mllikgeigv fikilpvmit ililsslfea fvflplhske
      481 ilkvvpskke ifwekfqnly rktlevifrf ryvalffflv ivpfllamgf khskfqlfpt
      541 fdasqiyvng kfesnytitq taqaikpiek vlkkylgpdv egfttvvgmq mnnkgeanvg
      601 enyfhifvdl kdkkptdfyn kyiapifqpi kvtgqtrtvt aqqlamelkk eykhikipgl
      661 telnvivpqa gvvksdivis iagdnqekil kaikmlesam akikgvyniy ddaelgayel
      721 kikpnaygek lgfsegnifs qlraffgeae yaktfdkdgi vkiiikdink dkidelkyfr
      781 ltipgtnqli eldkvadfiv krsfkkihky dgiaaksvya svnkkiltvn dfykkidpvl
      841 ekikkeglki liggaaktsk efmndlkeal vvaillifli lvlmfdsill pfviisvipl
      901 sflgvifgnm vmhmnmtmlg migivglagv vvndgivmvd fikkakniee illfasyrlr
      961 pvlltsittf fglftlmffp ygqsailqpl aialgfglmw gtilnlfylp vfyyilnknr
     1021 lnnnsgflkr ayekifkrg
//
LOCUS       WP_457563770             517 aa            linear   BCT 27-JAN-2026
DEFINITION  L-aspartate oxidase [Caminibacter pacificus].
ACCESSION   WP_457563770
VERSION     WP_457563770.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..517
                     /product="L-aspartate oxidase"
                     /EC_number="1.4.3.16"
                     /GO_function="GO:0008734 - L-aspartate oxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0009435 - NAD+ biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56711
     Region          1..517
                     /region_name="NadB"
                     /note="Aspartate oxidase [Coenzyme transport and
                     metabolism]; COG0029"
                     /db_xref="CDD:439800"
ORIGIN      
        1 mkydilvigs giagmmaaie akelgsnvai vmkkspmann sfmakggina alnnmgdgds
       61 iehhiqdtlk agmglaeeea vrifceqapq ivrelhrkfk vpfttlpdgr laqrpfggtk
      121 fkrtvfaada tgpaimkaln kalndlnidt iknhfalnll indgkiagat fvdekgelkv
      181 iqakavivtt ggfaglyrgh ttnitdatgd giamglragl eamdmefvqf hptglegtny
      241 liseaargeg gklinsdgke fvdelntrdf vtraivkqlq krkkvyldlt dipeeiintk
      301 linlkkrvks lkgidiskep ipisplahyt mggiktdtyc ftdieglfya geagnngvng
      361 anrlggnsls egavfgriag yqavkyshrq qtqiepkked iqkdkeliet lkntkidakk
      421 ikdeigeilf nklgilrngy aikkaldkfe dikremsqnh endsslneki eclnaldiak
      481 vlaksalyre esrgahfrmd ypesdhaflh htlekld
//
LOCUS       WP_457563753             227 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563753
VERSION     WP_457563753.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..227
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25442
     Region          1..222
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mkscgiiggm swessaeyyk lineqinrkl gglhsakiil ysvdfqeiae yqknnlweks
       61 aevlsnaaks lekagadfvm iatntmhkva dkvkssisip lldirdslie eiktknlknv
      121 lllgtkftme dsfyvdylkk rgvdvvvpes qdreiihkvi fdelclgvtk dsskkeflki
      181 iekydtegvi lgcteigmli sqkdtsktil dttkihcnfa vkimcqc
//
LOCUS       WP_457563771             666 aa            linear   BCT 27-JAN-2026
DEFINITION  EAL domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563771
VERSION     WP_457563771.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 666)
  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 666)
  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 666)
  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..666
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..666
                     /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=78240
     Region          428..655
                     /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 mryvdsiknh lptilqevkv qikndktiye fvkteeeldk llslqekliq eylydfqkni
       61 ldekkcmqfy kdlkipyaiv vrslnyirke viialdkegv dketiiefse yfdkfinlta
      121 kvylkkdivt lkklrnsyfe dyllfkshis wvesiiesis eddiskfpli aaseckfeey
      181 lnypeslmvc idvnlcmylh dlhsllhkla ntfylyyaks ayseaymifk dlkeqilkfk
      241 giigelyfit ysnlevsffk lieiyktnkk efvtlidmks lkslnsiyge etitkalevi
      301 ekrlhrffek dqarslvvkg mtanfymlni dysydeykkm idniieiike pvildenkie
      361 ftpiiaglei eeyfdikkde mimilnhlkn kakqskcnkl lvinhyskem lkswlknryd
      421 skfikskien aelklayhpi fdiqtnkiys levlarivde dklipaglfi devysmnlie
      481 kldlavlrkl iedkekikqi tdkifvnvsf nsllneeyle kleklidniq vglllelteq
      541 kfvdnveilf elnqkynlff avddfgtgyt slqsvvdlvk kgilkvlkid gsliknidde
      601 ynkkiinvis nmakelnlls vaeyveseei lneikkagin laqgyflakp alieelivek
      661 vekfgf
//
LOCUS       WP_457563751             385 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563751
VERSION     WP_457563751.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..385
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44479
     Region          2..384
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 myfiyekdai grtifeivfk ntgsiyakda vaymtahiln tkgtldkkek fysqleekai
       61 nltittnkef stvsmtflne kssfavkkli ellqnpnftq ealekskkei lakkenlknn
      121 hdyiasknlf kaifkntple retigediqn vtledikehf syfakenavf inggkkidia
      181 efietlpntk pkndlffkpk qshieekrdv eqsyiyfaap fevkkeeyyl akiatfilga
      241 ggfgsrmmee irvkrgyays ayamnefkks yqilkghlqt klentidakn lvvdiinvfl
      301 ekgitqeeld sakkfligse plrnetlsqr llrkfneyyl glgdgyfeke lnliknttld
      361 eindfikrhk eiknlsfsvv tndkn
//
LOCUS       WP_457563780             527 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457563780
VERSION     WP_457563780.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..527
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59023
     Region          <242..518
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkeivgyggl ihnfknyvlr gkdkykenfd rkyallnkki keyealgesp eekklideik
       61 tvfdkyyngl pavvqgyqen ltvheldkiv kvndspaika fkilstkgik lsglspkdwi
      121 vlstriinki ktfidklgkd iliqihdivk sttiylcsvl viviliiltv vvlsfviskd
      181 lvesteklke glleffrfln rettqakeiq insndelgqm akvinqnisk ieeglmqdaa
      241 miqglvreve kmkngvlegr iyeqasnpdl ekvrvifnem qdslekiigk dvnktvkvld
      301 samhkdftkr iqnaigkvel avnsvldtiv silsvnkeng dilsqtasel kekmhalkda
      361 akeasyelse vanimqnlnn eifeisnqtk tvidqsqdik nvvgiiqeia drtnllalna
      421 aieaarageh grgfavvade vrklaektqk slseidanin lltqsitnig eaiikqtdei
      481 anatakiedv nektklmens veevntiaee vndmadkmle nvkknkf
//
LOCUS       WP_457563772             390 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine desulfurase family protein [Caminibacter pacificus].
ACCESSION   WP_457563772
VERSION     WP_457563772.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..390
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43014
     Region          1..380
                     /region_name="NifS"
                     /note="Cysteine desulfurase/Cysteine sulfinate desulfinase
                     IscS or related enzyme, NifS family [Amino acid transport
                     and metabolism]; COG1104"
                     /db_xref="CDD:440721"
ORIGIN      
        1 mvyldnnstt pmdervkevy cdatkyfgni nviydlgiea rkklneaydi lypgigasde
       61 ddiiitsstt egnntviktf ldsylkgsgk khiittvaeh ssikatcaya kthgmevtyi
      121 ytdengrvnp kdienaired talisvlfas nesgaiqpik eisqiarkyg ipfhcdgaqa
      181 igkakinvre lgvdyftfsa hkfhgpkgvg glyvregapf vnlihggnqm ggkrggsvyl
      241 ngiiamaeav klanehldem ydkvaklrdk leeailkipd tktyvdkkyr lpntvvasfr
      301 giegeamlwd lnmhkiyaat gsscsserle gsevlealge dpeiahtgii fslsrftteq
      361 eidyvievlp kivkrlrdis mtyakvkpsd
//
LOCUS       WP_457563789             235 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563789
VERSION     WP_457563789.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>235
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
     Region          4..>235
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mfkfseisdm cikcgkcipg ctihrvnpde atsprgfldi lkgveegdie idknfkdtve
       61 scflcnqcve vcpnslptdf mienarakva ekfgiawykr afffllkhrw aydlvsklgf
      121 yfqtcgfkie eekkairsrf slpmlhkgrl lpafsktsfl kkypekisak npqkrvaifi
      181 gcmanynyte vgdalvkilk fldidifipk kqaccgapay ftgdfkttee likrn
//
LOCUS       WP_457563797             659 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease R family protein [Caminibacter pacificus].
ACCESSION   WP_457563797
VERSION     WP_457563797.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Domingues,S., Moreira,R.N., Andrade,J.M., Dos Santos,R.F.,
            Barria,C., Viegas,S.C. and Arraiano,C.M.
  TITLE     The role of RNase R in trans-translation and ribosomal quality
            control
  JOURNAL   Biochimie 114, 113-118 (2015)
   PUBMED   25542646
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426128
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..659
                     /product="ribonuclease R family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75872
     Region          1..592
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
ORIGIN      
        1 mkefayklvk gidrkdiprd krdiindlia lgivtsgkii qlkskyrigk vdvtkkgfgf
       61 lipigvkekd ylieahhlng askgdlvvae rlfnkkgrpk akvvyileka faytvaylty
      121 efkngkkqpv lkniktdmpi fvsekkktlk klpdgavfkv nnytakieev lgvlqdpwvd
      181 ekislalynk keefskkaik earaygdyvd ksmypdrvdl tdfpfctidp ptakdhddai
      241 yfdkeknely vaiadvseyv ylngnidrea kergfsiyfp hkaipmlpre lsenicslke
      301 hedrlafvfk itlneknevv keelfeaiin shrkysydrv defldgkfen iddidkeile
      361 wlmplwdrvk niraqrlktg lefesdeikm tldengmikd vtleketpsh kliedcmlla
      421 nkaaakmidf gifrvhdkps qtsldelyse lgalgidvdv dekdftkvve giqsqakemg
      481 ikkfvdklii rsqqqaryda tntghfalgf erythftspi rrysdltlhr ilkatikgek
      541 kildyilrnv ealvvklsel ereamkvewd fydrkyarya dlhigdvykg iiedteippi
      601 akiledkllg arvflkdkqk fnlfekvdie ivkaniatak ikgkvkkees esiiesgge
//
LOCUS       WP_457563801             536 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563801
VERSION     WP_457563801.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 536)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..536
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61703
     Region          <349..536
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkkkiliiia fimiistiir tfivgasfln ysnsliknqt nlivdilrev idkdkflhii
       61 qnshpikkie fikgqkneli ysfkdktiis ivpfnelesl kivfsaknyf dkllmaiaql
      121 ilialislii iillvnhflk pyleilekie estnnilkgn fnnkielklk geakdfvnsy
      181 nyflqklkes fgvieekyta liekeksndp lndaketieq lanifkfkri ieednsyeti
      241 lerlidvike fgikhfaiig iennekiakl ihsesdiccn vlenykncra yrlkkeinsl
      301 kmkkeclshy cdtnhiclpf sstgnftgil kiiftdeeke hvlkvlpyik aylneistii
      361 eskytlellh nqnikdpltr lynrryldni lptliegakr rngklgfiml dmdhfkqvnd
      421 tyghdagdrv leklaeiivn sirksdiavr lggeefliia tnvkdkedlr kiaekirlsv
      481 kaqqfylssg lvinktisig aamfpddced gnecikladk alyeaknsgr drvviy
//
LOCUS       WP_457563805             477 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Caminibacter pacificus].
ACCESSION   WP_457563805
VERSION     WP_457563805.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Draper,J., Karplus,K. and Ottemann,K.M.
  TITLE     Identification of a chemoreceptor zinc-binding domain common to
            cytoplasmic bacterial chemoreceptors
  JOURNAL   J Bacteriol 193 (17), 4338-4345 (2011)
   PUBMED   21725005
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436174
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..477
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=53383
     Region          <59..336
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          366..431
                     /region_name="CZB"
                     /note="Chemoreceptor zinc-binding domain; pfam13682"
                     /db_xref="CDD:433401"
ORIGIN      
        1 mnskiigtit allflivagy ggfkgdfvtl glgvlgilas aalffqksqt tsstksslik
       61 kisktieras egdfneritn idpndplnsl awdvnnlldq leaferdike sisaakqgid
      121 yrdispqgyk grfratveiv neaiqaista lkeqarself itlndlgggt kteiqeikks
      181 fdeklrefmm kidelsteif egadesaqki enlsivlnel idfiahtnea inmlsqraee
      241 igkivelitd iadqtnllal naaieaarag ehgrgfavva deirklaert qkatseisit
      301 iktlqqetsd iqansekits mattsredvd svnemiigfr dkslenkknv dfaltrmlid
      361 laklshlvyk lnafeavvee keipqtkdne cefgkwlrse etihrigclk eykeikdvih
      421 knihnftnaa lectkdksci krkdeiidif kkvednskkl shkldemfeh ytkepcs
//
LOCUS       WP_457563806             356 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Caminibacter pacificus].
ACCESSION   WP_457563806
VERSION     WP_457563806.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10020374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=40504
     Region          30..347
                     /region_name="rodA_shape"
                     /note="rod shape-determining protein RodA; TIGR02210"
                     /db_xref="CDD:274033"
ORIGIN      
        1 mrkfdfllil lllpfifvsl ylvheishkl fikeliyisi givvfiavyf ipirkllwvi
       61 pivywiniil lllvdlvgik ilgaqrwlki piinltiqps efmkttlllm lgyliyrypp
      121 rptytlkefl rlslyiiipf lliakepdlg talilliigf gvlfivgvdk kiwitlivgg
      181 vlfapvayky llkdyqkkri enflthpsyh vkqsmiaigs ggfsgkskne atqtqlkflp
      241 iassdfifay lverfgflga igiiflyfvl ilhllnvaek lkddyfakvm fagvalmifv
      301 ysyiniamtm nlgpvvgvpl pllshggtsf infmilfail enlisrkdfi nthgvk
//
LOCUS       WP_457563815             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Caminibacter pacificus].
ACCESSION   WP_457563815
VERSION     WP_457563815.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..356
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=42011
     Region          89..>356
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
ORIGIN      
        1 minqykkegk nyqilklknn sltfyttsre nlknllnekv kltiitskvs ffeylftfya
       61 psfnikllpa dkidlfiekq hsssvmknlf kalflgesid fstrqklssl gvshlfalsg
      121 lhlgfisfvl yfvfsplyki fqkkfpyrnr ffdlgisvla vefvylyfts fppslirayv
      181 levlififam rfkelfslni lfftilfsfl iffskifsig fllsflgvfy iylffqhvkf
      241 sffssvflsf ymflvmfvws hyffgnfnyf qflsplvnii fsffypleif lhllgfggvf
      301 ddfilkylsl gsefyevkis fvwvvifgim sllaffskyl fyginllaff ivilai
//
LOCUS       WP_457563811             254 aa            linear   BCT 27-JAN-2026
DEFINITION  inositol monophosphatase family protein [Caminibacter pacificus].
ACCESSION   WP_457563811
VERSION     WP_457563811.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..254
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28914
     Region          1..241
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(29,33,39,60..61,75..80,205..206)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(32,34,81..82,84..89,141..143,145,147..148,157..158,
                     161,164..165,169,174..180,188,192..195)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mfektiqivk eageifkkgy ykdkeivlkg kkdlvteydi kveeflkekl kpfntnfiae
       61 esiynekihk tfiidpidgt tnyahqvpqc aisvayyenn revfgivynp ilnelfyakk
      121 gegaylngkk ievsknecfq raliatgfpy ssaeneadlk wvisklnkvl prcqdirrlg
      181 saaldlcyva cgryegfyei nlkpwdvaag kiivqeagge vsnnfgesyn ifedrcivat
      241 nmkihrelvn lleg
//
LOCUS       WP_457563818             157 aa            linear   BCT 27-JAN-2026
DEFINITION  SixA phosphatase family protein [Caminibacter pacificus].
ACCESSION   WP_457563818
VERSION     WP_457563818.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..157
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17988
     Region          3..135
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mkilfirhsl avdrdefrgh dferplnekg kkrakkffek vkkiypdidy iitstalrak
       61 qtaeilknfy pqalyeetpl llpgagleel kkvlknegvi aivghepdls nfikeimyap
      121 nlkiklqkps laeleegvlk sllqykqlka ldeknhs
//
LOCUS       WP_457563817             810 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457563817
VERSION     WP_457563817.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 810)
  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   3  (residues 1 to 810)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   6  (residues 1 to 810)
  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   7  (residues 1 to 810)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   11 (residues 1 to 810)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   12 (residues 1 to 810)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   13 (residues 1 to 810)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   14 (residues 1 to 810)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   15 (residues 1 to 810)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   16 (residues 1 to 810)
  AUTHORS   Zoraghi,R., Corbin,J.D. and Francis,S.H.
  TITLE     Properties and functions of GAF domains in cyclic nucleotide
            phosphodiesterases and other proteins
  JOURNAL   Mol Pharmacol 65 (2), 267-278 (2004)
   PUBMED   14742667
REFERENCE   17 (residues 1 to 810)
  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   18 (residues 1 to 810)
  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   19 (residues 1 to 810)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   20 (residues 1 to 810)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   21 (residues 1 to 810)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
REFERENCE   22 (residues 1 to 810)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   23 (residues 1 to 810)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
REFERENCE   24 (residues 1 to 810)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   25 (residues 1 to 810)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18594631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..810
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=93897
     Region          <109..>278
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
     Region          273..>381
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          <375..810
                     /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 mdvsilnqit kygfilkqgs kvyankrvie llglrkrnll ndlnkieeik eflnskksvf
       61 keivtiktki etkhisfyik ktidgfilla ddftkyirek hitdiviymn dvlaksknek
      121 elyekfikav ikkakfnacf vmkkqknalv pvawgndtdg ldcikdvtip ldektpllkt
      181 pvakaflegn iffnddtrin pdveplreem lkrnylssvg ipifkekkve avicickdev
      241 dffkgykkli eyiskalskt lenleeikfk nvllnainkg hewvvitdkk gkvvfvnetv
      301 ekitgykkse ligknpkifk sglhdeifyk elwetikkgr ifesiiinkk kdgsifylld
      361 kivpvgdyyi slgkditnek kyfhlieelk fkdpitglyn kegffkhard ylkkfkyesh
      421 ivlvvdvynf nvinhkygit egdevlkqlg kklrtvffer dliykfhtvn itlgrfngde
      481 faiflekade kcipkilnkl yevfsgtykv knekikldyn agisvypkda cdiedllnna
      541 sialinakke gpnivklysk eyskeiykfn nvlnliktsl eknrfelffq pivdaekeni
      601 vaaegllrir ekskiitpgv fidvlensny slnvsmkmld nienilkntk nvklsynlce
      661 kqfrntqaid klinigkkfp yrlqielier vlineklysq kvleklkdng iliaiddfgt
      721 gysslsyire lpvdiikidi sfirkmmqnh kdmaivktii nlakeldikt vaegvedesq
      781 vailkalgcd yiqgfyyykp mpkeeflkll
//
LOCUS       WP_457563826             227 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Caminibacter
            pacificus].
ACCESSION   WP_457563826
VERSION     WP_457563826.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  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 227)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..227
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26447
     Region          3..218
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mnlyqpkngy cynsdtmfly dfitkfnikg evlevgggcg vlgllikrdf pkinltiiek
       61 qkimtefiek nlkenslkae vinddfldye fkkrfdfiis nppfyqgtlk seneikkiar
      121 yeeflpmdkf fekvnrvlse rgefifcyda krvdeiikkl pkplkitdmr fmhpkidkka
      181 tlvmirakrh aksmvvihpp ligfegeeys keaakiykka atnsikv
//
LOCUS       WP_457563838             413 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Caminibacter pacificus].
ACCESSION   WP_457563838
VERSION     WP_457563838.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..413
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=48239
     Region          3..369
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mkihldldsf fvsahrvfdk sllnkpvvvv krndkeifen hksevlnlnr gaftgdlivs
       61 kkeydksyfl engkirgivv tasyearelg iktgttlkea leiypkltvl lpdyklyhtl
      121 syklkeflkv kiplveqfsi deffgdlegw vddrdaflfc kdlkdeiwek fslpisigia
      181 kskwtaklat sfakpngvfm veevdefikd ipiekfpgig rriekrlker giltlgdvke
      241 nreyfyswgk pgvelykrvc gidneevkek evrksigisr rfdvvydrre lvrrvhvlcr
      301 ylsflvlkyk lnptfyylki kykdktsska hvrihrlfne lllkeimttl fyradekemg
      361 vislslavsk fkresnlfdy ekdlklqnln eaifkirskf gvsalmsaee ihp
//
LOCUS       WP_457563842             145 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457563842
VERSION     WP_457563842.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..145
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17427
     Region          10..121
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mseidrikel flydiivaia kikyiankfd npedlkydfl hwdsiirefe ivgeamnyci
       61 kfnlfenekd krkvidfrni lihkyfgidp eavlniaktn ldwlehmiyd rikqiepqlk
      121 eelkkemiee nknldfvkka ldkiq
//
LOCUS       WP_457563840             442 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter substrate-binding domain-containing diguanylate
            cyclase, partial [Caminibacter pacificus].
ACCESSION   WP_457563840
VERSION     WP_457563840.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 442)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 442)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   8  (residues 1 to 442)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10098929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>442
                     /product="transporter substrate-binding domain-containing
                     diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          37..248
                     /region_name="PBP2_BvgS_HisK_like"
                     /note="The type 2 periplasmic ligand-binding protein
                     domain of the sensor-kinase BvgS and histidine kinase
                     receptors, and related proteins; cd01007"
                     /db_xref="CDD:270228"
     Region          <282..442
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mriiwvlvlv vtslfaqvdl tpkeklfikn hlfhcvvtpn wapfnmlkdd kiegiaidyw
       61 klikhklnlk snckilpswt lvlediknkn sdivpatakt pqkqnfalft kpyatypivi
      121 atrnnigfin smaqlenrki vvgknysaae ilkkhfpnln iievkdikta ldyvsrgkaf
      181 aaidnlpvia yninkyqfan lkisgktpfd fkvrfmvrnd ypllvsaink aidsitpeek
      241 erifkkwvyv vyqtgidtkk lltiafiaig lililialvi yqffeikkrr kfetqlikta
      301 tidsltgifn rkhidymlqk eveeakryan plsiifcdid hfkdindkfg hkvgdivlee
      361 larimkqnir ksdiigrwgg eefliilpht plnealrvae klqsairnye fpkigkitcs
      421 fgvtefksed siyrlmirvd qa
//
LOCUS       WP_457563846              97 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457563846
VERSION     WP_457563846.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 97)
  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 10004355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..97
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11284
     Region          2..90
                     /region_name="MJ0604"
                     /note="Predicted nucleotidyltransferase, MJ0604 family
                     [General function prediction only]; COG1708"
                     /db_xref="CDD:441314"
ORIGIN      
        1 mrlnqkylqt ikqafketfk kgevylfgsr vdkekkggdi dlylivdept lknklkflak
       61 ikkilgdqki dvvfqkdknr liekealkwg kkiieis
//
LOCUS       WP_457563850             516 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoethanolamine transferase [Caminibacter pacificus].
ACCESSION   WP_457563850
VERSION     WP_457563850.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10887874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..516
                     /product="phosphoethanolamine transferase"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009244 - lipopolysaccharide core region
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1900727 - osmoregulated periplasmic glucan
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=60829
     Region          207..476
                     /region_name="LptA"
                     /note="Lipooligosaccharide Phosphoethanolamine Transferase
                     A (LptA) or Lipid A Phosphoethanolamine Transferase;
                     cd16017"
                     /db_xref="CDD:293741"
     Site            order(216,258,355,416..417,432)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293741"
     Site            order(216,258,355,417)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293741"
     Site            order(290,303,431..433)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293741"
ORIGIN      
        1 mkilgnfifa vlftlflllp dfianfwwkn yyiftsknti keiiitfvia fiisflpkkq
       61 kifwglffia lsfvqigyyg yfrtymppyq ldllfseykd iidslksivf lviflifali
      121 gilfilnffh hktkpkthky tslilitlli ifpfimakkk avympnathf sylntlfaid
      181 lwiidnlspq kthkfkpytv kkinggrpiv imimgeslnf krmhlyrwdv ndtpnldkla
      241 ktdknfefak aisggintpv svvtffnvkr epqnigllls qktnllklak qngyktywls
      301 mqeegtsiss llnyadikkt rkdfkekydd alikelkkip fnnktfivlh lradhspyee
      361 ytpksfykwp fnyenyhkyk iysyydsvly vdyiisniin ymkahhknfv iyftsdhgem
      421 lgfpdehgky ghsqlvfgdt yvpfiyysda fhkklskkyy nhyliskmla kdlgyeitnp
      481 ndngtyfvng vkidgsagfl hykfknqkii klkdkd
//
LOCUS       WP_457563849             289 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457563849
VERSION     WP_457563849.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 289)
  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 289)
  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 10616537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..289
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34121
     Site            order(19,21,45,101,103)
                     /site_type="active"
                     /db_xref="CDD:133005"
     Region          21..118
                     /region_name="Glyco_tranf_2_4"
                     /note="Glycosyl transferase family 2; pfam13704"
                     /db_xref="CDD:433416"
ORIGIN      
        1 midyffhkvd kpkitmvilv kneediiekn irfhsklgvd nfvvmdnnse dstrdilkel
       61 skeieitiid ekgpyaqskf mtrlnkiakk kynpdwiinn dadefwipkn gknlkevlnf
      121 kggvlqvprs nmilyegins wmeseyrvan qilsredyen tnivlgkigr kvivnphgyi
      181 ktnsgnhsae hiafwkkqef rdihiyhypi rsyeqfekti anrakllkig akmgvhykkw
      241 aklyeeeklr eefekmifdn eklkclqdin iikkditpke lfkkfgllk
//
LOCUS       WP_457563852             115 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol kinase [Caminibacter pacificus].
ACCESSION   WP_457563852
VERSION     WP_457563852.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Li,D., Lyons,J.A., Pye,V.E., Vogeley,L., Aragao,D., Kenyon,C.P.,
            Shah,S.T., Doherty,C., Aherne,M. and Caffrey,M.
  TITLE     Crystal structure of the integral membrane diacylglycerol kinase
  JOURNAL   Nature 497 (7450), 521-524 (2013)
   PUBMED   23676677
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Van Horn,W.D. and Sanders,C.R.
  TITLE     Prokaryotic diacylglycerol kinase and undecaprenol kinase
  JOURNAL   Annu Rev Biophys 41, 81-101 (2012)
   PUBMED   22224599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10198050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..115
                     /product="diacylglycerol kinase"
                     /EC_number="2.7.1.107"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004143 - ATP-dependent diacylglycerol
                     kinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006654 - phosphatidic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=12815
     Region          5..110
                     /region_name="DAGK_IM"
                     /note="Integral membrane diacylglycerol kinase; cd14264"
                     /db_xref="CDD:260133"
     Site            order(5,10,14,17,25,28,30,65,68..69,72,76..77,89..91,
                     93..94,96)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:260133"
     Site            order(12..18,20..21,48..50,52..53,56,59,63..64,66..67,
                     69..71,73..75,77..78,83,85..86,89,92,95..96,99..100,103,
                     107,110)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:260133"
     Site            order(16,24,65,72,76,90..91)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:260133"
     Site            order(24,72)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:260133"
ORIGIN      
        1 mkkkynlfkn asyalqgilt llkerafqle llfvipllal lffldlsalq ksimaaslif
       61 ilitealnta veytvdlvtd ewhefakrak dtasaavffs lvqaaviwgi nlfls
//
LOCUS       WP_457563854             173 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563854
VERSION     WP_457563854.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..173
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <1..161
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 hydiflldin mpeingyefy eelknytsdv pvifitaysd idhvekafkl gaadyikkpf
       61 elkelelrik rlvfkntnri kitdnysfdl gklklfynde eveltqnery fleilvknig
      121 qvvdmstlrd yvwegkdicd ntirtqvkkl rsklkenfik nvrgsgykie kng
//
LOCUS       WP_457563863             283 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caminibacter pacificus].
ACCESSION   WP_457563863
VERSION     WP_457563863.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32325
     Region          26..268
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mkiinqiise iekvikgkke kikiilasff adkhvliedv pgvgkttlak tiakvlglef
       61 krvqfsadml psdivgvnyf dmqkkefvfk kgpifteill adeinratpk aqsalleame
      121 erqvsvdgkt yklsdnffvi atqnpkehgi yplplsqldr fgicislgyp erefeklilk
      181 serieinsfs giekykrkak eiftdekiyd lvldlgkisr difetglstr alitlleisk
      241 ayamiegrdy videdvfeil kyvtphrlee nadkkiirly yqg
//
LOCUS       WP_457563864              63 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563864
VERSION     WP_457563864.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 63)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 63)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 63)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10638360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>63
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          27..>58
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
ORIGIN      
        1 maatpkvtpl wkeatfqseg ldaralitrt dlkgiitfas layrkmtkfr kedlvgnphs
       61 vvr
//
LOCUS       WP_457563867             395 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caminibacter pacificus].
ACCESSION   WP_457563867
VERSION     WP_457563867.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46058
     Region          76..389
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkktaflipv flfanqnils dlklkllnld eqrsiysake tqkswinpii lqysisqnns
       61 lhttkqniqt fsvsinqpif ktgaiyysik yaknlknynl kqielqkral ikqayelvyd
      121 ykinklneei allniqnaki dvkkkkedfl ngtgdstfln qaiinlnnik lgyedlkfne
      181 kqlkfsfknl sdldiekvkl pyfkiisknd finnnlqlis skindkikyd lykmqlgnql
      241 ltisfnasyn yqitdytnet skyhddsnny ynvglsvtlp idftstdkvk qtklsyiksr
      301 yetldmkrnl lntyamiisq iktlqkkkei ykenekayan liestkesik agnatvldle
      361 ilensykvmq inqkiidlqi qklllnlyyq vtskf
//
LOCUS       WP_457563869             497 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Caminibacter pacificus].
ACCESSION   WP_457563869
VERSION     WP_457563869.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..497
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53880
     Region          8..475
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mfskilqnyn akntkndila givvsvalip eviafsfvag vspivglyta filgliaaaf
       61 ggkpgmisga agsvavvvva lvqkygveyl ylaailagii qlligilgfa kfirlvpmpv
      121 vygfvnglai viaysqfqff kgesyiiyil valtmaimyf lpkftkaipa glgaiivita
      181 ivwgfhlhtk tigdlahikg afptfhwpdv plnletlkii lpysivmalv glieslltle
      241 vleemsgerg ngnkeakalg agnalsgmfg gmagcamigq tiinhtsggr grlsgitaav
      301 liilfvvffs kyiekiplav ligimfmvsi atfewasldk lkripkedaf vlivttliti
      361 ftdlavavis gviisalvfa wkhakvyfkt kmegdkkiye fegplffgst rsflesfdvk
      421 ndpkevvmdf knvrvmdasg veaidkitkr yleagkklti rhlsneckkl levagpycty
      481 eeddpnykva idpeklk
//
LOCUS       WP_457563871              66 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caminibacter pacificus].
ACCESSION   WP_457563871
VERSION     WP_457563871.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..66
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=7183
     Region          1..>49
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mrkaftmiel ifvivilgil aavalpkflg vaqqaheanl ksfvgtlnrs dllfgvkqfh
       61 qteqea
//
LOCUS       WP_457563876             151 aa            linear   BCT 27-JAN-2026
DEFINITION  GspE/PulE family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563876
VERSION     WP_457563876.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..151
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
     Region          <1..151
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 vlstlhtnds vsainrmidm gaepymvgas ligveaqrlv ktnckyciee ykpseaylep
       61 ikhllpknvk fyrgkgcekc nmtgfsgrtl iteiflndek legmiaknkd rveildylks
      121 qkgfknmfyd glvkaargit pleeiykvak p
//
LOCUS       WP_457563881             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Caminibacter pacificus].
ACCESSION   WP_457563881
VERSION     WP_457563881.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46572
     Region          4..376
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(11..12,15..16,19,52,102..103,105..107,110,132,
                     135..136,139,205,208..209,212..214,217,245,249,295..296,
                     300,304,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 miylsllmai rflglfivmp vlalyamhlk gasefsvgva lgayalsqvf lqiqfgklad
       61 kydkkkilif glfllflgsl vcafsdniyt lifgrllqga gaiggvilay msdlsdenkr
      121 akifarmgqf ialsfaismi lgptigtkwg vdklflltai lalvsiylvi akvppapkiv
      181 hhtdskvslk difahkellk lffsgfmqkg lmsvffllip lvftqtfhwe ktslwkvyip
      241 alvfgffalp lgailaekkg kgkavfiisa lsitlalilf liglntqnyl falvgvivff
      301 fgfnllepvl qsfvskvaya nqkatalsts ntiqylgifl ggavagyfmk hgmlksflii
      361 siiiaslwvf alikmkpvkk fkiveytefd kdfieelkte knvydfyeke gvlivryid
//
LOCUS       WP_457563878             173 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine phosphate synthase [Caminibacter pacificus].
ACCESSION   WP_457563878
VERSION     WP_457563878.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Peapus,D.H., Chiu,H.J., Campobasso,N., Reddick,J.J., Begley,T.P.
            and Ealick,S.E.
  TITLE     Structural characterization of the enzyme-substrate,
            enzyme-intermediate, and enzyme-product complexes of thiamin
            phosphate synthase
  JOURNAL   Biochemistry 40 (34), 10103-10114 (2001)
   PUBMED   11513589
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Reddick,J.J., Nicewonger,R. and Begley,T.P.
  TITLE     Mechanistic studies on thiamin phosphate synthase: evidence for a
            dissociative mechanism
  JOURNAL   Biochemistry 40 (34), 10095-10102 (2001)
   PUBMED   11513588
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Begley,T.P., Downs,D.M., Ealick,S.E., McLafferty,F.W., Van
            Loon,A.P., Taylor,S., Campobasso,N., Chiu,H.J., Kinsland,C.,
            Reddick,J.J. and Xi,J.
  TITLE     Thiamin biosynthesis in prokaryotes
  JOURNAL   Arch Microbiol 171 (5), 293-300 (1999)
   PUBMED   10382260
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..173
                     /product="thiamine phosphate synthase"
                     /EC_number="2.5.1.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004789 - thiamine-phosphate
                     diphosphorylase activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19779
     Region          1..172
                     /region_name="ThiE"
                     /note="Thiamine monophosphate synthase [Coenzyme transport
                     and metabolism]; COG0352"
                     /db_xref="CDD:440121"
ORIGIN      
        1 masflsyfit dpsyslqqik eaikkhkptf vcyrnkeyfd kkeimdfanf akkyskvfin
       61 ldslkddsll ehfegvhips srldeiteyk nkiiiasthn plevqkaqka dyitfspifk
      121 sknrcglgte vlnhicnihp kvialggiis dkeveeiknt kavgfgsiry fft
//
LOCUS       WP_457563883             287 aa            linear   BCT 27-JAN-2026
DEFINITION  damage-control phosphatase ARMT1 family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563883
VERSION     WP_457563883.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Huang,L., Khusnutdinova,A., Nocek,B., Brown,G., Xu,X., Cui,H.,
            Petit,P., Flick,R., Zallot,R., Balmant,K., Ziemak,M.J.,
            Shanklin,J., de Crecy-Lagard,V., Fiehn,O., Gregory,J.F. 3rd,
            Joachimiak,A., Savchenko,A., Yakunin,A.F. and Hanson,A.D.
  TITLE     A family of metal-dependent phosphatases implicated in metabolite
            damage-control
  JOURNAL   Nat Chem Biol 12 (8), 621-627 (2016)
   PUBMED   27322068
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Perry,J.J., Ballard,G.D., Albert,A.E., Dobrolecki,L.E., Malkas,L.H.
            and Hoelz,D.J.
  TITLE     Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase
            that targets PCNA and is linked to the DNA damage response
  JOURNAL   Cell Rep 10 (8), 1288-1296 (2015)
   PUBMED   25732820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..287
                     /product="damage-control phosphatase ARMT1 family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33110
     Region          2..283
                     /region_name="DUF89"
                     /note="House-cleaning carbohydrate phosphatase, DUF89
                     family [Defense mechanisms]; COG1578"
                     /db_xref="CDD:441186"
ORIGIN      
        1 mhiskecylc iynqvfkite rlnlddekas evlrvgakil skydltympp viaadvykki
       61 seilgiedlf ekekkeaike alkfkeilek rikkskdplf daakisvagn vidlgvhqey
      121 nlekeiknif emkffkndfn efreklknak tlcyladnag envfdeifik eirrfnpeiq
      181 vfyfvrgkpi indvtlkdle gleiwdlaev vdsgvptpgf cipfankkak difqtsdlvi
      241 skgmgnfecl fgecerevfy fykvkcnvva rasksklgey miykgek
//
LOCUS       WP_457563886             790 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional diguanylate cyclase/phosphodiesterase [Caminibacter
            pacificus].
ACCESSION   WP_457563886
VERSION     WP_457563886.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 790)
  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 790)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   3  (residues 1 to 790)
  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   4  (residues 1 to 790)
  AUTHORS   Borziak,K. and Zhulin,I.B.
  TITLE     FIST: a sensory domain for diverse signal transduction pathways in
            prokaryotes and ubiquitin signaling in eukaryotes
  JOURNAL   Bioinformatics 23 (19), 2518-2521 (2007)
   PUBMED   17855421
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   7  (residues 1 to 790)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   8  (residues 1 to 790)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   9  (residues 1 to 790)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 790)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 790)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 790)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 790)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 790)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18684138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..790
                     /product="bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=91169
     Region          29..357
                     /region_name="FIST"
                     /note="FIST domain protein MJ1623, contains FIST_N and
                     FIST_C domains [Signal transduction mechanisms]; COG3287"
                     /db_xref="CDD:442517"
     Region          <407..786
                     /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 mkqysctfde knikeiyekt kdlnyktllv qvysgvviks yilnvvstvk eyfpnakivg
       61 ittdgeiids kitqnnvvvs fsffeksdie ivffeknnlf edgkklaska kkdtkllmif
      121 asgiefnade lieginflnp slpvigslag dnakfkktyi fydekiskng vlgvyfnsev
      181 levyidssfg wvkfgrrmki tksdknivye ideqeafdvy syylgneikk yfpkigvefp
      241 liktvnnldv aravvgvrdk alifagalne gdivnfgiae askvlesskr vfqkllrnki
      301 ealfvfscma rrrfveklsf lelqmlknip ntgffgygef fngrflnqtl nvlalseggd
      361 lenkelyipk ndkvttiesl ihlvdvafne vrqklyidnv tklpnkaafd edvlrnpyga
      421 vlfdikkfss indkygevvg devlknlaki lqrfiiknak lyrisadyfi vlffeecnlg
      481 mfaysvieyf ynnplkikik deeyeidldl yaalvegveg rkikikadma lhyakvtken
      541 ivkyskdlki eekinkeiet lnfvkkaime nrvipvfqmi qkddlsfeal vriidedgkl
      601 vspfyfldsi kntryydeit rimieksfki fqdlphklsi nfsyediqne ktveflissi
      661 ekynmqnrvi ievletdsis eydvfenfvk kvkkygveia iddfgsgysn fiylanikpd
      721 yikidgslik sldenekfyk ivktivefak emdirviaef vkdekiyeic kklgidgmqg
      781 yfihipskdi
//
LOCUS       WP_457563890             309 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA dihydrouridine synthase [Caminibacter pacificus].
ACCESSION   WP_457563890
VERSION     WP_457563890.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..309
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=34667
     Region          10..306
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mststhksak yflaplagyt dlpfrsvvkk fgcdmtfsem invnaiaynn ektkkmmqks
       61 pletpyfiqv aannvenaik aveiinemee vdgidinlgc pvnkarrsgf ggvllkdenk
      121 eklkeivsai vktskkpvsa kmrlgfdeiv avdrakmled lgiefltvhg rtvkqmykgq
      181 anyeeikkvv eavnipvian gditdyekak fvleytgavg vaigrgavgk pwiflemkqq
      241 gditpqqkke vilehfdqmi ywygeygvil frkhahaysk giakasefrs kinevkdakt
      301 arelieeyf
//
LOCUS       WP_457563893             162 aa            linear   BCT 27-JAN-2026
DEFINITION  methyltransferase family protein [Caminibacter pacificus].
ACCESSION   WP_457563893
VERSION     WP_457563893.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..162
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18431
     Region          34..144
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mkfrflywig llvavlladi ffpppkvfll silgilfiiy gvvlnyiagk tlkllghkvk
       61 tkkfsppdkm vkagiyscmr hpgqfgnlmi lfgvsmlsgk vwsvifvgwv lafglwfils
      121 veepegvekf gfdyckykie vppfnfsikc lvegyrflkq if
//
LOCUS       WP_457563891             260 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase, partial [Caminibacter pacificus].
ACCESSION   WP_457563891
VERSION     WP_457563891.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 260)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>260
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          1..>249
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mliefefenf ksfknrtyfs mestniddle hhlidnkylk tsaifgangs gksnlirafl
       61 kfslivknsi diekqkryph epfkldiktk deptffrilf lkentffeyl feidkngnil
      121 reelyqkein knkkylfkre rqtitynkrs fkeakgleek trenalflsv vnqfngkiak
      181 kiydfitqef iiikdtdcne kleiiaksll knkeirdntv eilskldfsi kdieikketl
      241 panvleqikn dedipkkikd
//
LOCUS       WP_457563895             298 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563895
VERSION     WP_457563895.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..298
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34298
     Region          39..296
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mifedisele kivenndiqk alslikppkk fplaktkkrs almvsahqvk hlnkidslpa
       61 diimlnledg vpkdkkeitr vmigvflsri ekidkeivir vnaldeggkk dieflekfnf
      121 nafripkvrs iediddvfmk tekeihasie tkeaffnlke lkhpklttfy igiydllnel
      181 kishsvidln nplihrilsd ftltarylni tpigfvyqqy kdlegfknwc llqknlgmqg
      241 vgcitpaqcq iankifdedl efakmivkrf esegpftidg lfvdepiykn ylqmldns
//
LOCUS       WP_457563896             133 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Caminibacter
            pacificus].
ACCESSION   WP_457563896
VERSION     WP_457563896.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 133)
  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 133)
  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
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..133
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15572
     Region          3..127
                     /region_name="VapC"
                     /note="VapC family ribonuclease, toxin component of the
                     VapBC toxin-antitoxin module, contains PIN domain [Defense
                     mechanisms]; COG1848"
                     /db_xref="CDD:441453"
ORIGIN      
        1 mdkifldtni iidlldskrk nhtkaknlfi kliendyevf isedmittiy yilkgnekil
       61 effekiiekw nivgfgkdti lesinyckkh ktdledvlqc icaknngcel fitndkkfin
      121 cgikivnydf fnl
//
LOCUS       WP_457563897             196 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Caminibacter pacificus].
ACCESSION   WP_457563897
VERSION     WP_457563897.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21919
     Region          4..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfwfiplvif lavaifspgp nnviamsvgf nygfkrviph llavvvgfsi mlfvvgigik
       61 elilkyqsaf evmkylcsfy llylaykiat skpnlntnea kpitfkesll fqvinpkswi
      121 aalsivtiyl pkdnflaalf itiiisdili ilaistwavl gksfnkifks ekttkifnfs
      181 maillvvsvl milfve
//
LOCUS       WP_457563905             350 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563905
VERSION     WP_457563905.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..350
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <2..347
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 geikhfyenn lnffkinmkt krtqiiltpi lelfsatiaa iviivggkev idgsmsvgaf
       61 fsfltalflm tdpirkvaks tsnmqeaiaa nerlkeifsi kphitsgkek lkeikkiefk
      121 nvtlkygdkt alkninynak kpkiiglvgd sgggkssfvs lilrfydane geilindkni
      181 knynlhslre kiayipqnih ifndtiaani aygkeideek vknalkkanl ldfvesleng
      241 iytilneggs nlsggqrqri aiaralyknp dvlildeats aldnkseavi mktienlndk
      301 lvfivahrls tienadeilv fkngkivckg kkeellence tfkrlykgnm
//
LOCUS       WP_457563910             577 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family oligoendopeptidase [Caminibacter pacificus].
ACCESSION   WP_457563910
VERSION     WP_457563910.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..577
                     /product="M3 family oligoendopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=68359
     Region          43..564
                     /region_name="M3B_PepF"
                     /note="Peptidase family M3B, oligopeptidase F (PepF);
                     cd09610"
                     /db_xref="CDD:341073"
     Site            order(370..371,374,397,490,497,501)
                     /site_type="active"
                     /db_xref="CDD:341073"
ORIGIN      
        1 mmnwdltplf nsiseaeefl kqaefkaief ekkyknrlyt ltpeeflnvl kefeeiweni
       61 graltyiylv fatdstkgnf lgkfqelatk aeehlvwfel efiylpidkq qrfidnagvy
      121 kyylihlqee apyrlsekee kilmkkdlts ssafsrlfde tlsrlrfffe gkkyseeeil
      181 sklyspdrnv rkkaqvsltl glkphqella yiynqvkkdw kidhieirgy dspedprhls
      241 nrvskksvda lvnsvnentt ivadyyeikk rllgydklfd ydryapiklt dktpeisfee
      301 akelvlnafk nfsntfyeia kkafdekwid vypkegkrgg afshsatpka hpyvllnytn
      361 qrrdvftlah elghaihqyl arevgylnqd tplttaetas ifaemllfee ikssldkkel
      421 ietyaakled vfatvfrqiv ftnferkvhk fdelkpedyn kiwmeenqkm fkdsvilten
      481 ykiwwsyiph fihspfycys yayaqllvft lyklykegfe nfeekyiefl kqggsippkk
      541 qlkelfgldi enenfwekgi aviremlsef kglcddi
//
LOCUS       WP_457563912             319 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Caminibacter pacificus].
ACCESSION   WP_457563912
VERSION     WP_457563912.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..319
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36243
     Region          1..258
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkrfaligaa gyiaprhlka ikdtgnelva amdrcdsvgi idsyfpdadf fieferfdrh
       61 idklkragek idyvsittpn ylhdahirwa lrngaqaice kplvlnpwti dslkeienet
      121 gkkvntilql rlhpsivalk ekvtkelqen pnkvydidlt yltsrgkwyf iswkgdekks
      181 ggiatnigih ffdmlswifg eveenivhvk teyanagflk lkhanvrwfl sviydyipde
      241 ikakgqrtyr sitvdgeeie fsggftdlht rsyeevlkgn gfgldeakps ieivstirnl
      301 npvglkgeyh pfakkvsnv
//
LOCUS       WP_457563913             422 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide sugar dehydrogenase [Caminibacter pacificus].
ACCESSION   WP_457563913
VERSION     WP_457563913.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..422
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=47095
     Region          3..414
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mkkiaiiglg yvglplavaf sekypvvgyd iaqwrvdeln sgydrtlevs eedlkaaldr
       61 gikftnklde ikdanvyivt vptpidnhkn pdltplqkas ealgkvlkkg diviyestvy
      121 pgcteevcvp ilekvsglkf nedffvgysp erinpgdkkh tvkkilkvts gstpeiakei
      181 demyasiiea gthlapsikv aeaakviena qrdiniafvn elalifdklg idtksvleaa
      241 gtkwnflkft pglvgghcig vdpyyltyka keigyhpeii lagrrlndnm gifvanklvk
      301 lmiheghtik nskvlvlgit fkencpdirn srvidvirel qdfkvnvdvy dpwadkeevk
      361 heyglelkdn invndydgiv lavshkefke leepikkakq nsnlvvydik sffdenlvdg
      421 rl
//
LOCUS       WP_457563916             182 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Caminibacter pacificus].
ACCESSION   WP_457563916
VERSION     WP_457563916.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..182
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20515
     Region          12..178
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mqiidfneie skeryklmag niiprpvawi vtqnngiinv apfsyftgvs skppllmvsi
       61 grkkptidep kdtfkniket kkasvclvpi emyeimdktg evlpsnisea ekfgieleri
      121 denfppivkg ckraflcely gtfeneemat ipfflkiekm iidgdfepva rvgkgyarlc
      181 di
//
LOCUS       WP_457563918             117 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457563918
VERSION     WP_457563918.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..117
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13636
     Region          6..115
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mynicdkidf vlekisllee ilkenkitfa lkdekvlkpa ilmhlmqige slnsiykkfp
       61 eliekydled avkgsynvrn fiahdyegmn laiiemilrk eisklktklk rvknece
//
LOCUS       WP_457563900             306 aa            linear   BCT 27-JAN-2026
DEFINITION  respiratory chain complex I subunit 1 family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563900
VERSION     WP_457563900.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 306)
  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   3  (residues 1 to 306)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Schneider,D., Pohl,T., Walter,J., Dorner,K., Kohlstadt,M.,
            Berger,A., Spehr,V. and Friedrich,T.
  TITLE     Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Biochim Biophys Acta 1777 (7-8), 735-739 (2008)
   PUBMED   18394423
REFERENCE   6  (residues 1 to 306)
  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   7  (residues 1 to 306)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Weidner,U., Geier,S., Ptock,A., Friedrich,T., Leif,H. and Weiss,H.
  TITLE     The gene locus of the proton-translocating NADH: ubiquinone
            oxidoreductase in Escherichia coli. Organization of the 14 genes
            and relationship between the derived proteins and subunits of
            mitochondrial complex I
  JOURNAL   J Mol Biol 233 (1), 109-122 (1993)
   PUBMED   7690854
REFERENCE   9  (residues 1 to 306)
  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
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Weiss,H., Friedrich,T., Hofhaus,G. and Preis,D.
  TITLE     The respiratory-chain NADH dehydrogenase (complex I) of
            mitochondria
  JOURNAL   Eur J Biochem 197 (3), 563-576 (1991)
   PUBMED   2029890
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..306
                     /product="respiratory chain complex I subunit 1 family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=33494
     Region          15..303
                     /region_name="HyfC"
                     /note="Formate hydrogenlyase subunit HyfC [Energy
                     production and conversion]; COG0650"
                     /db_xref="CDD:440415"
ORIGIN      
        1 minyiltili ifliapfllg ltksikmfml fkkpvspfqp yinfaklihk elvyakessq
       61 isriavfmil apivvvvflm ppvfhgsfyi sfidaftitg llslstfflm llgldsasaf
      121 ggigssreaf isalvepami ltifsislig qsigiskavl nlndyfdinh aasfvlaais
      181 ffiiliaeng ripvdnpeth leltmvheam ilestgadla liemasalkf aifatlfvsl
      241 flpfgvnlcw clavtvfilk lilvsvaval ievntaklrl fkvpnllgia iifgflslfi
      301 yyvvge
//
LOCUS       WP_457563919             191 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563919
VERSION     WP_457563919.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..191
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21711
     Region          5..175
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mnankivcvg rnyvehikel nnempsepvy fmkpfssvsd divlpgyspm hyegeicfli
       61 gdrlkvgfgf dftlreiqse lkkkglpwer akafrgaavf sdfvefenme dlglevyknn
      121 eliqkadvsl mmfkprelfe didrifglna gdivmtgtpk gvglveegde fegrilekgr
      181 vivskkwkvk k
//
LOCUS       WP_457563920             230 aa            linear   BCT 27-JAN-2026
DEFINITION  7-carboxy-7-deazaguanine synthase QueE [Caminibacter pacificus].
ACCESSION   WP_457563920
VERSION     WP_457563920.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bruender,N.A., Grell,T.A., Dowling,D.P., McCarty,R.M., Drennan,C.L.
            and Bandarian,V.
  TITLE     7-Carboxy-7-deazaguanine Synthase: A Radical
            S-Adenosyl-l-methionine Enzyme with Polar Tendencies
  JOURNAL   J Am Chem Soc 139 (5), 1912-1920 (2017)
   PUBMED   28045519
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Dowling,D.P., Bruender,N.A., Young,A.P., McCarty,R.M., Bandarian,V.
            and Drennan,C.L.
  TITLE     Radical SAM enzyme QueE defines a new minimal core fold and
            metal-dependent mechanism
  JOURNAL   Nat Chem Biol 10 (2), 106-112 (2014)
   PUBMED   24362703
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..230
                     /product="7-carboxy-7-deazaguanine synthase QueE"
                     /EC_number="4.3.99.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016840 - carbon-nitrogen lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26575
     Region          3..223
                     /region_name="QueE"
                     /note="Organic radical activating enzyme NrdG/QueE
                     [Coenzyme transport and metabolism]; COG0602"
                     /db_xref="CDD:440367"
ORIGIN      
        1 mkkipiseif ysiqgegkyc gtpsvfvrvg gcnlrcpgfg dkgcdsyyav dkryqkewel
       61 ksiediktei kkylkfdphl vitggeptly fkelypliew fegqitietn atididfekf
      121 paykkvafam svklsnsgee ynkrvkknvi ksyaknakks ffkfvidkdl kkeieditkn
      181 ihlpiycmpl gatkeelekn apfvfefclk ngyrysdrih irlfgkkkgv
//
LOCUS       WP_457563925             133 aa            linear   BCT 27-JAN-2026
DEFINITION  arsenate reductase ArsC [Caminibacter pacificus].
ACCESSION   WP_457563925
VERSION     WP_457563925.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..133
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=14887
     Region          3..123
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(8,10..15,103,105)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mkkvlilctg nscrsimaeg linkyfknik aysagsnpsg kvnpnakkvl ieenawkedy
       61 hsktiqeamk napfdlvitv cdnaakecpv ipgaktvhip fedpdgkdyg eflktkeeik
      121 krlfselrkh frv
//
LOCUS       WP_457563933             269 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Caminibacter pacificus].
ACCESSION   WP_457563933
VERSION     WP_457563933.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..269
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32563
     Region          12..>106
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          182..263
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mknyffkdek ipyieirkse dnnlrykehf hcefsigali kgttilsfen kkyhlnknel
       61 avfnpfelhs cnpyknqkrs yymmyvdtqw lfnlqknife vnefipiksa iiksekyysk
      121 fiflcekiid snvlyleqea lleeffseif infldkkrkk etfeieklkk akkyiekhfy
      181 knitlfeisq hcelspyhfs rsfkkafgis phkflmnmri ekakkllkek nivdvayevg
      241 fydqshfhkv fksytaatpf eyknytpnf
//
LOCUS       WP_457563935             246 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457563935
VERSION     WP_457563935.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26500
     Region          1..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mitaiiigif vgffsgflgi gggtvlvpvl lflgfgfkea vgisvtqmmm ssiygsylny
       61 kkgllkikng lslavggaig aalsglivky tskdilgaif ltlvfiaiir ffvtvkephd
      121 eppidnkklf figlfvgaia isvgvggail itpilvgflk yklkttvsls lffvvfssvs
      181 gfisqslagh inylegfsig iasligtyfg vklyhkidtk ihkkillawy ififfamiyk
      241 lyfqgn
//
LOCUS       WP_457563934             289 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caminibacter pacificus].
ACCESSION   WP_457563934
VERSION     WP_457563934.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..289
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32989
     Region          5..270
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrknnllyhf ialvtiiiws ltfiqtkill kylspeeill drfviawiif fiifpkikff
       61 slkeelifvf lgfsgifgyy ilenislslt sainvgiivt sapifttilk ittqktnskk
      121 vlfsiigfif viigllimei khisktnlgd ilailgalff gaysfvlgkv nsktnsilit
      181 rksffwgivf lmiflffkhf nfsdikiyqn vdvwfnilfl sffatalcff mwkkavskie
      241 tkasnyiylv piintlaavf ilnenitasm lisiiiilsg lfisqkfgv
//
LOCUS       WP_457563937             259 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563937
VERSION     WP_457563937.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..259
                     /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=30135
     Region          41..248
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkekilnfik sklfskelqq lenlkeenrk lkkelkkqki mnsfkdevis aishefknpi
       61 siingyieti lesnlppqtq qkflnkiqkn ttrlselidr lylitklenk klkpsfstfk
      121 ldllikdliq sfdeerisln ltpttitadk klieivlsnl isnalkyskk eitinlneky
      181 levidkglgi dkqnlemikq kffriakndw dnslglglai vehilklhht hleiesekgk
      241 gskfyfdits lkdkehpqq
//
LOCUS       WP_457563941             218 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Caminibacter pacificus].
ACCESSION   WP_457563941
VERSION     WP_457563941.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..218
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24713
     Region          25..218
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkrlgrglga iledaeagyl kelpesgvne idiekiipnp yqprrefsee sieelassik
       61 khgllqpviv ikeddkyilv agerrlrask klgktkikai vapyskedlr eyalieniqr
      121 edlnpveiay sleslikehg ftheelaksi gksrsyvtni lrilsmpeiv kenlkqnkit
      181 lghakvlsgl deqeinevvk kivenswnvr dtekfvkk
//
LOCUS       WP_457563952             357 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxyqueuosine reductase QueH [Caminibacter pacificus].
ACCESSION   WP_457563952
VERSION     WP_457563952.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Zallot,R., Ross,R., Chen,W.H., Bruner,S.D., Limbach,P.A. and de
            Crecy-Lagard,V.
  TITLE     Identification of a Novel Epoxyqueuosine Reductase Family by
            Comparative Genomics
  JOURNAL   ACS Chem Biol 12 (3), 844-851 (2017)
   PUBMED   28128549
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..357
                     /product="epoxyqueuosine reductase QueH"
                     /EC_number="1.17.99.6"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0052693 - epoxyqueuosine reductase
                     activity [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /GO_process="GO:0008616 - tRNA queuosine(34) biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42139
     Region          4..173
                     /region_name="QueH"
                     /note="Epoxyqueuosine reductase QueH; pfam02677"
                     /db_xref="CDD:460650"
ORIGIN      
        1 miahlccsvd agyflkrlke eypneeiigy fydpnihpys efklrsldtk riceklgiey
       61 vegeydyltw yqktkglene pekgsrcsvc fdlsleeaar fakekgddkv ttsllmspmk
      121 sheqleaigk vvkrkygvdf invdfrkkgg tqaqqqyare nqmyrqdycg ciygiwqqks
      181 hqeiidelis pwpfqvlpss ieekleiyek rieledkgkk ykiikenfln yrllsakvev
      241 kkeviasyvl fysyldrlqr vriefekngi gyanraqvif vkvskineil nkrydnvsei
      301 ykkpltiqee levrknitet efnlspiivl defeevrydi dinskiysdn keilief
//
LOCUS       WP_457563955             433 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457563955
VERSION     WP_457563955.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..433
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46243
     Region          2..390
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrkigfleaf sigvggmvgg gifavlglti dlakgaapia fliagtiali tahsyaklsv
       61 kfpseggsie yivqafgnnl fsatvnnlll vsyvimlaly asafgaygsa lflghdvtwl
      121 hkllavgvig ifafinllga fltgkaedil vytkvailli fvaigfytgt hyerlepqfw
      181 esylkiitgg liiflayegf eliansakdv inpqktlpra fyasvifvia lyvsiavvti
      241 lnvdfetakk aqdyvlaiaa epllgklgfv iiavaamlst asainatiyg agragyliak
      301 lgeipkdfak kikngyegmi ilgllgvifa tsfnienisv agsfgflvif glvnyanfkl
      361 rkitnsnpfi sllgaflclv saailigynl fhnpsaless awvvvivvai tiiyhklggk
      421 mkkvldedlr eki
//
LOCUS       WP_457563957             481 aa            linear   BCT 27-JAN-2026
DEFINITION  Ppx/GppA phosphatase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563957
VERSION     WP_457563957.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Kristensen,O., Laurberg,M., Liljas,A., Kastrup,J.S. and Gajhede,M.
  TITLE     Structural characterization of the stringent response related
            exopolyphosphatase/guanosine pentaphosphate phosphohydrolase
            protein family
  JOURNAL   Biochemistry 43 (28), 8894-8900 (2004)
   PUBMED   15248747
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..481
                     /product="Ppx/GppA phosphatase family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
     Region          1..298
                     /region_name="GppA"
                     /note="Exopolyphosphatase/pppGpp-phosphohydrolase
                     [Nucleotide transport and metabolism, Signal transduction
                     mechanisms]; COG0248"
                     /db_xref="CDD:440018"
ORIGIN      
        1 vidigsnsar mavfkktsrf gfyllreeks kvrisegaye nggnlqdfai eraikalsef
       61 lliakslktr kilcvatsav rdapnkaefl krvkdelglk ikvidgdkea fyggvaaanl
      121 lyekngvtid igggstefal ivdkrieati slklgtvrlk elffdkgdie gaktyiknel
      181 eklgkvfdsk kvfgiggtir alsqaimkki eypldilhgf tyeikehkdf lekiikmsde
      241 ellkagikpe rldvirpgtl iflealkylg akevitsgvg vregvfltdl lrndnyrfpd
      301 nfnpsvrtii dvyqidrkia syetkialev fdllkeefkl ddkykmhlty aiklsragel
      361 vdfyeahkht dyillnslhy gfrhcdrlli skiirfhkrk kikkkeiekf kcllpkkdiv
      421 eklcnifwva klininlsmp qveitfskkd kkiiikgenl ylakersktr elffdleivn
      481 k
//
LOCUS       WP_457563958             360 aa            linear   BCT 27-JAN-2026
DEFINITION  PilZ domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563958
VERSION     WP_457563958.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..360
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43037
     Region          240..338
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 msknrfyken fsafikenek ffktveskft hnflellkkk npnipitsql kneienlyks
       61 lfledyssqn fklnaifilk ernvdiedil nkvflllana fikytlkekn aiaklkklts
      121 lfefyieyli fhvneeefft yhlpkelkey yltnkvlnlf nvykgvpith kttiltlned
      181 rgyieveans yqiiaakfqk eiyllepttn ttfkayidyv ypqrkvlklt niekiqrntp
      241 krnyirvqps tyinvkikkh kdifttkmyd islkgmavis dektvdigdf vklefilegy
      301 ffemtaevrs itklndsfrf hfyfeptpsq erilekyitk rekeiikelh kylkaefidv
//
LOCUS       WP_457563963             707 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter permease [Caminibacter pacificus].
ACCESSION   WP_457563963
VERSION     WP_457563963.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=77325
     Region          36..706
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msksevfdad pnlekevdev ekeavkegkv dkdleekilt elegqrnfpp ksvyywlial
       61 iafawslyql yvsyfpvnst ivrsihlafa mvlafliypi akkpkflkni qwwdwilaii
      121 gglgaayiai dyvglsnrpg dyltrdivig vifiiillea grrvigmals ivaivfllyd
      181 kfgqylpeii shkgasieki vaqmyltteg iygvplgvsa gfvflfvlfg slleragage
      241 yfiklayafl gkysggpaka svvasgltgi isgsstanvv ttgvftiplm kkagfppeka
      301 aavevaastn gqlmppvmga aafiiaeflg laytdviiaa aipavvsyla llyivhleak
      361 klglkgedpr nlppklktfi sglhylipvv ylmyvlivlr qsaqmaafsa iwllmvimii
      421 qypfyalfie krklqkqdfi qgfidifhgm vngarnmvpi alataiagiv vgsitltgig
      481 qvlldvidtl sngnilivll ltafislilg mglpttanyi vvasltapvm lqlaqdngfl
      541 ipaiaahlfv fyfgiladdt ppvgiaayaa agiakadpik tglqgfaydi rtailpfmff
      601 fntelllias tnewdyneft fisdpikiai ifitallgmf sfssatqgyf lkrinviqrl
      661 lflaavplfm lpnlmvkylh lpneyvsyai glviwaviff wqkaqka
//
LOCUS       WP_457563970             100 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Caminibacter pacificus].
ACCESSION   WP_457563970
VERSION     WP_457563970.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 100)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..100
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11434
     Region          1..73
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(9..10,14..16,30..32,41..44,46..47,50..51,53..54,
                     60..62,67..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mdeflktvsa lkdetrikil kfllihnerc vceleasfnm lqsrlsrhlk ilkeagflns
       61 krdgkkvlys ikpvtgfkka alkeienmki nlpklkecsi
//
LOCUS       WP_457563971             369 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457563971
VERSION     WP_457563971.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 369)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (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   6  (residues 1 to 369)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..369
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43555
     Region          <136..358
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlaekkslkr fllvyilstm fliavgewfy yklalhsvik ndimtiqkel snflkdkkfk
       61 llidrqvpfk iddtkyavfv ngefmygdfn kninepflvk dnklyykkil fkrwgkieii
      121 feknikkeve nikkellvfa vfaflfvcii afilgkiflr pmrdvinnle sfirdtthem
      181 ntpisvilsn ieilkmknvp lkelkriena afrlskifkd ltfvrlhhqq krdivkvdla
      241 efiqnrlvmf etqienknik iiknlhneii eidkedltrl idnilsnaik ysspnkeifi
      301 nlkdgvfsvv negeiknlke itkkfvrens seggfglgly ivkeickryg fefkiknene
      361 yvktevvfk
//
LOCUS       WP_457563976             279 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457563976
VERSION     WP_457563976.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..279
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          26..>101
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
ORIGIN      
        1 mryfliflfv plfafdyfti kkadeffqkk eylkaakeyl kidsqkalld aansyykagd
       61 ykkaieiysk indkklqfdk lynmanayak lgmfqkaiel ykkalkikkd kdaqynlkll
      121 ekllkkkppk qkqkqknnkq knnknknnke nkkqnnnqnk knqnkneqnq knnkkqnqnk
      181 nsdanknknn kqkenqqknn qnqnknqkkq sknnekkeqn kkfavnqkis kfknenkkpn
      241 qktlsvkesn ttdirmkfye kalknlqfns lliplrsqe
//
LOCUS       WP_457563977             468 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Caminibacter pacificus].
ACCESSION   WP_457563977
VERSION     WP_457563977.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..468
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52295
     Region          19..111
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
     Region          253..348
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 mkklilfllp llllanvsvk vnkkeltkge eliititatg kdikfpqinn idgynvigts
       61 lvsnieving amseslsksy iivpdknlti psfsviidgk vyktkpihii vktpkqtkgd
      121 ytldinlskk nlylgqsail dvklhykppv esiqlqkpqi kgflvqeilk tatdteaeyk
      181 flitplksge ftigplmani gilvkenpfn dpffnlsvss lkyktiysnq ikvkvnpipn
      241 dsvygdfkis lkaknivnag epntailkve gcgdfndlpd fkldipntti yaskadtnis
      301 ivdnelcgty tkkftiiadn dytipplklk eyngtlnvis tnpikvkvig akpittpkpp
      361 vtktsikptk qhienkknyy eyaiyliliv lgiglgyfis kitskekkdd ifskikkadq
      421 kelfnllipy sdipeikeil qkleeniykg tnhkinkkei ikiiktkn
//
LOCUS       WP_457563982             401 aa            linear   BCT 27-JAN-2026
DEFINITION  GspE/PulE family protein, partial [Caminibacter pacificus].
ACCESSION   WP_457563982
VERSION     WP_457563982.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>401
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
     Region          3..>401
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mvgadliqqg litqeqlnka leikkqhpsk klldilydlk fiskdvflke lskeleipyv
       61 enlneirlrd ikipinvlkq tkavpievky dkvviamedp lnwnaqayfk rlfpdkklef
      121 vlahkediek vlklienkyq isqiindikk elkgedvvag qqtaimrlil yiiknaierk
      181 asdihiesee egaivrirvf gtlyefldfd edvfnaiasr ikleagmdvs ekrkpqdgaf
      241 slefnrnkfd frvstlptvw gesivirild krnilkkldd igisdknlql lrqglskpng
      301 iflvtgptgs gksttlyasi nelvgvetkl itvedpveyk lrgiqqvqvn pkagftfada
      361 lrsilrqdpd kimigeirdl etleiaikaa ltghlvlstl h
//
LOCUS       WP_457563985             347 aa            linear   BCT 27-JAN-2026
DEFINITION  divergent polysaccharide deacetylase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457563985
VERSION     WP_457563985.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Aragunde,H., Biarnes,X. and Planas,A.
  TITLE     Substrate Recognition and Specificity of Chitin Deacetylases and
            Related Family 4 Carbohydrate Esterases
  JOURNAL   Int J Mol Sci 19 (2) (2018)
   PUBMED   29385775
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..347
                     /product="divergent polysaccharide deacetylase family
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39590
     Region          <123..341
                     /region_name="YibQ"
                     /note="Uncharacterized conserved protein YibQ, putative
                     polysaccharide deacetylase 2 family [Carbohydrate
                     transport and metabolism]; COG2861"
                     /db_xref="CDD:442108"
ORIGIN      
        1 mkkkkttkkt qpkkktvkkt qktsnnlilk sivfvlvlvi lglgaflgkl iyenketkke
       61 laktqinlke lqnkvsvlek elskpkpkak tkpeqttyse ikdyehavkt qppkkkekpk
      121 pivkltkkpk lviiiddvsf knqvkaiksi pfaitpsffp pnkyhpntai yakefkdymv
      181 hvpmeaiswn kpeihtlktt ssyyeiyttm vkikkefpnv kfinnhtgsk ftsdtasmkr
      241 lfkvlqienm gfvdskttph skaaladkyy diplysrnif ldnkedityi hnqlkkavni
      301 akrrgyaiai ghphkitfqa lksaapilkg vqvvtidqly ksqngkn
//
LOCUS       WP_457563987             180 aa            linear   BCT 27-JAN-2026
DEFINITION  ketopantoate reductase family protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457563987
VERSION     WP_457563987.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..180
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          <1..164
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 gighfekfen lnvkllkaci yilsnkkdin vihkktplfy lcveddevvr kafegcdlkv
       61 kfsedikkdi wkkylfistf atlqsyyqkp tgwimeqkrd evekfldevi kiakeegvdl
      121 seerekvikq alnipyeskm smqidfekgn ktevenltgy lakksdfinq yylglrngik
//
LOCUS       WP_457563988             100 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457563988
VERSION     WP_457563988.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..100
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=11680
     Region          3..98
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mfraklefil qmiddiefii nrhgyitksl edregqlail malmqigetl nkidkkflkn
       61 ydllndskga ysvrnfithd ygyniprlkd kilkiledni
//
LOCUS       WP_457563998             304 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Caminibacter
            pacificus].
ACCESSION   WP_457563998
VERSION     WP_457563998.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..304
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32764
     Region          5..296
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 msigfilqqi ingfslgsmy aliaiwytlv ygvlrlinfa hgdimmvgaf mafiffkilg
       61 lnfyvavlfs iiftaivgil tyvsaykpll dkgapkisll itaigisffl eslfnvianq
      121 ylggtyqafy fpkwfshiih ignvtipvlt iivpvltlll lgvvlfilyk tkvgiairal
      181 afdittvklm gansnmiiaf vfalgsalaa iggvayamay psidpymgml vglkafaaav
      241 vggigsvtga viggfilgfa evaipgffpe lggwkdafaf iflifvllfk ptgimgidfe
      301 rqrf
//
LOCUS       WP_457563999             144 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457563999
VERSION     WP_457563999.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..144
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17034
     Region          23..>119
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 msdfnitnem kfldefefln kpiitrtdke gniifanslf skmsgfsrae ylgrphnivr
       61 hpdmpkeife qlwhtiltgk awngyiknrt kcgkfywvea fiqpeyengi itgfaslqrr
      121 vsikivrrye kiykemrlke ltrg
//
LOCUS       WP_457564000             143 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457564000
VERSION     WP_457564000.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..143
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=17033
     Region          8..>142
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mnkryiidee vrfedvnptn rpvvsrtdih gnilyvnsvf anmcgykkee mlgrphriir
       61 hpempkkvfe emwetikagk ewhgfvknlr kdgryywvda hispvkkngk ivgyisvrra
      121 vnddikreme rmyaemkene rsf
//
LOCUS       WP_457564006             265 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457564006
VERSION     WP_457564006.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..265
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          1..243
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 itlsseieny pgvcdvksgl elmmcwpaqa qkfgceikse eaikiqkens hfivktpkne
       61 yksktliiat gstpkkagfe geieytgkgv sycavcdgff ykdkivavig ggdtaleeal
      121 ylskiakkvy lihrhdkfra apvtqkkvfe tknieiifna tvkkvfgnqf vegiilnlng
      181 eekelkvdgv fvfvgmkvnn elvknlveln ewgevkvnlk metsqkglya agdiredsvk
      241 qvvaaagdga taainalkyi ekeel
//
LOCUS       WP_457564012             142 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin synthase catalytic subunit [Caminibacter pacificus].
ACCESSION   WP_457564012
VERSION     WP_457564012.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12) (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..142
                     /product="molybdopterin synthase catalytic subunit"
                     /EC_number="2.8.1.12"
                     /GO_component="GO:1990140 - molybdopterin synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16245
     Region          15..124
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(19,23,28,30..34,36,38,84,93,95,103,107)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(49,51,54,57,61,74,110..111,113,115..117)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(110,117)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
ORIGIN      
        1 mvevfkggvp viptlerwye efklegygam ipfigivrpd neieglsfdl ylpmlnewfk
       61 kwqnlddaki imahsfgdvm vgetsflcav ftkhrregfk yleefvedfk anapiwkydl
      121 kggkrifasd rakelpgagl ld
//
LOCUS       WP_457564017             309 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome-c peroxidase [Caminibacter pacificus].
ACCESSION   WP_457564017
VERSION     WP_457564017.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..309
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=35242
     Region          30..301
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mfkrlivffs fvllyaepis hiplkvkyne dkallgkmlf fdpilsadnk vscaschspk
       61 yggadnkrfs igvfgrvdkp mnsptvynav fncwqfwngr aknlkqqafm antdpdemgm
      121 tpekveekln knnkykklfs lvykkdyisy dmvldaiaef ekalitpncr fdkylrgvhn
      181 aiteqekrgy flfksygcit chngknlggn sfqklgvlvv dvniirgkdr yevthlpydk
      241 yvykvptlrn ialtapyfhd gsvktlkeai vkmgifnlgv kipaedvedi eaflktltge
      301 tpeiiknmr
//
LOCUS       WP_457564025             175 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Caminibacter pacificus].
ACCESSION   WP_457564025
VERSION     WP_457564025.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 175)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..175
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20266
     Region          2..153
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mkvgiisdth kkvgrakkai dflmdknief lvhagdivre eileymealp iryvavlgnn
       61 dlhlysvvdk yelvtepfyf klagktwklm hyprymfpld tdiivyghth dvditfngkn
      121 lilnpgevca rdhgfstcmt ldiedekyiv tlyyrkvgek ewkskvkefl ipkge
//
LOCUS       WP_457564026             112 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457564026
VERSION     WP_457564026.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..112
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13073
     Region          3..110
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mfkaklefil qmiddiefii nrhgyitksl edregqltil mplmqigetl nkidkkflen
       61 ydllndskga ysvrnfiahd yegvklsvie nilryniprl kdkilkiled ni
//
LOCUS       WP_457564029             158 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caminibacter pacificus].
ACCESSION   WP_457564029
VERSION     WP_457564029.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 158)
  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 158)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..158
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18118
     Region          8..121
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mieekikwne kyktltpkap silldhipsa knkkaldlag glgtnaeali nkgyditlid
       61 isdvaiskik npkiktfcld ldnyiipqne ydvitmikyf nldllkqipk alkkggyfaf
      121 ekipkykltt ekffeifkdf etifftkepf rfvgkltk
//
LOCUS       WP_457564034             271 aa            linear   BCT 27-JAN-2026
DEFINITION  M90 family metallopeptidase [Caminibacter pacificus].
ACCESSION   WP_457564034
VERSION     WP_457564034.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Xu,Q., Gohler,A.K., Kosfeld,A., Carlton,D., Chiu,H.J., Klock,H.E.,
            Knuth,M.W., Miller,M.D., Elsliger,M.A., Deacon,A.M., Godzik,A.,
            Lesley,S.A., Jahreis,K. and Wilson,I.A.
  TITLE     The structure of Mlc titration factor A (MtfA/YeeI) reveals a
            prototypical zinc metallopeptidase related to anthrax lethal factor
  JOURNAL   J Bacteriol 194 (11), 2987-2999 (2012)
   PUBMED   22467785
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Gohler,A.K., Staab,A., Gabor,E., Homann,K., Klang,E., Kosfeld,A.,
            Muus,J.E., Wulftange,J.S. and Jahreis,K.
  TITLE     Characterization of MtfA, a novel regulatory output signal protein
            of the glucose-phosphotransferase system in Escherichia coli K-12
  JOURNAL   J Bacteriol 194 (5), 1024-1035 (2012)
   PUBMED   22178967
REFERENCE   3  (residues 1 to 271)
  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 271)
  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 10007100
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..271
                     /product="M90 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32264
     Region          24..267
                     /region_name="MtfA"
                     /note="Mlc titration factor MtfA, regulates ptsG
                     expression [Signal transduction mechanisms]; COG3228"
                     /db_xref="CDD:442461"
ORIGIN      
        1 mdnfknflll lwgaffvfii fqtishfryl qklkklkstp lpqnlkkyie nltqyqklne
       61 kqkrileyki qkflleknfi pvninlndei kiliafyacl psiayidfcy pnlkniyiyp
      121 hpvilknlqn gyvvqeeeii egeatgenvi iswdeakkei hhpnfrnvii hefahqldaa
      181 dgvidgippi etskynewvk imfgeykkfk qktlknrflg kfslidkyaa tneaeffavm
      241 seyyfmkpqi lkkhfpdiyk elknfykief i
//
LOCUS       WP_457564035             252 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caminibacter pacificus].
ACCESSION   WP_457564035
VERSION     WP_457564035.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..252
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27440
     Region          29..249
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mhtyvftlis gllsglalgl tggggsilav pllvylvgin ihlaivtsli avgatsliss
       61 itymkqnlvr fkvaflmaap gilstflgsl inkklnghll limfsflmfy igfrmlkkrn
      121 ienvksdtqn ilkilffgfi vgflsglfgv gggfllvpal ylgvnlsmke avgtslfiif
      181 myglfgmtsy ivekreiefl isaifvlggv fggfigayig ehlnqeklrk ifayftmama
      241 vfiflenigy fi
//
LOCUS       WP_457564041             295 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Caminibacter pacificus].
ACCESSION   WP_457564041
VERSION     WP_457564041.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..295
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32126
     Region          25..295
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mikylsafif lliislfsvy ygandfiayn irlprvlsai aagaalgiag fimqvvlknd
       61 laspftlgit hgalfgvsls vvfgigsvfl fsflgafivi vfilavaflr rlssqsiils
      121 giaisalfga gsmflqyfad esqlaniviw sfgdlskgdf fnifllffmi tlslvfflin
      181 swnfnalsle caknvgvkte tlifismiiv tllsalvvan ygiigfvglv aphivrffen
      241 sfksllilsa lygaillvis dyiarniiyp leipvgivts figapmflyl lmrkk
//
LOCUS       WP_457564042             253 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Caminibacter pacificus].
ACCESSION   WP_457564042
VERSION     WP_457564042.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..253
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29028
     Region          4..230
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 msfidlknvt ykyeneflal dnvsfsiekn ekvvllgsng sgkstilril aglyfpkkge
       61 yffggvkitk ksvkkdfrkk vgilfqnpds mifnptvfde iafslkefgf dniedrvnei
      121 akkfgiekll kksplhlsgg ekqkvmlasi lvyepeflil deptaamdpr ttgwfldfmy
      181 elelttiaat hdlalayels dralvmseeh kllydgdmee lmkdldtlik anlihkhkhk
      241 hkkfihshyh lhf
//
LOCUS       WP_457564047             491 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457564047
VERSION     WP_457564047.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 491)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..491
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57372
     Region          <234..477
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mkinnlnnei krkllienll vgfiiflsvl agvisylffk effykytdsk lysaamnane
       61 fvlgekfykk alsdtlhkec dknyslkltr faknagvtyi ysmidknnsv yflassltqk
      121 dikngdiyay mqkypeatet lknvfkngki afeeskdrwg yfrsilipid skygryviga
      181 dlkisdikks fdeykiklfs ilglvdifal miaffyyrlv keekkhleei cslnekleem
      241 nknlekrvke esekrikqee lilreskyiq mgemmdavah qwkvplsaim lesgllkmii
      301 ekkgciddei kksinniqey inhlnetldn frnflntkny eeflisevie svknlvkdll
      361 vinnvrlesq iknfkiygrk ndfehillsl idnsikifnq rninerviki takdyeiiye
      421 dnaggfegdi ekifdfnysk tggsgiglyi vkmildkygg dikaqnikng irfiinlkkf
      481 rynsnskkik e
//
LOCUS       WP_457564055             487 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457564055
VERSION     WP_457564055.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 487)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..487
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57383
     Region          <212..481
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msqkrsksvf flvfliiimf lfsmiifvtf kkvekriskd tfdfllkevk sfsrnieryl
       61 llkygdllvv lnkkpllrsd vnlylssyit snfknvflay ydgkffrvig dgslnpkdrf
      121 dynerfeptr kdlwlkaikt kktiyykqdi kgiwttyiyp vldnnlkvsy lividfstep
      181 lsyidnnlii lkkslflfis vlllsvlils ifllydilrq kkmqkllkel qilnktlesr
      241 vkeeveksre kdrqlimqsr lalmgellsm iahqwrqpln viggvvadme mdmmlnendp
      301 kktkenleti kkmikhlsst iddfrkfyrk dnekieidfn eilqevlnia ssslknknik
      361 iknhlkckrk iktypnelkq vllnliknae dilierkien pkiiieifen ddkciievkd
      421 ngggvdeeyq dkifepyftt knekngtglg lymsknivek rlggeilqyn dtegavfriv
      481 lrmrdel
//
LOCUS       WP_457564057             128 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase, partial [Caminibacter pacificus].
ACCESSION   WP_457564057
VERSION     WP_457564057.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>128
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
     Region          1..128
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkpkiyekki ivskedidfn ghvnnlkyle wminvamehs thegfgveyy kthgvswvar
       61 khcieyklpa fegdelvlkt winevkkllv irkyeiyknd klithgfsew vfvdfktqrp
      121 kkipedii
//
LOCUS       WP_457564061             333 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Caminibacter pacificus].
ACCESSION   WP_457564061
VERSION     WP_457564061.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 333)
  AUTHORS   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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..333
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <8..327
                     /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 lnkrlnellk rldkkwiirn yelstsasvg vaiyphdgks fdellknadi amyeakhrgr
       61 nkyvifntdv kekiskeyti ktmlqkaien eefelfyqpk ldrnkrvvgc ealirwikdg
      121 kvvppgefip vaeksgliye igkwvieesa krvkewesde ilkeislafn vsvvqmrreg
      181 flndirniis kikpnvsnle ieitesvfie nkqralhlle llkrmgfkin lddfgtgyss
      241 isvlkefkid ilkidksfvd evlskegrvy vktiidmskn lnlltvaegv eyqeqfevlk
      301 elgvdyfqgy lfakplkkee feefvkklnt skf
//
LOCUS       WP_457564062             678 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457564062
VERSION     WP_457564062.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=77190
     Region          3..675
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtsvctycgv gceieaiven nrvtkikpvk ngissggelc ikgrygfefl nnrlkehlis
       61 yefikknaek mpfelqvrla nlyewderfy kaplnlaldi aawklkdiie khspksiaai
      121 ggartniesa wlfqhfarni lktphvdnca rvchspslsg lkmsigegas svdfdsifda
      181 etifvigsnt teahpmvasr iikakkrgak livvdvreip lmkfadisvi lpfesnllfl
      241 naiakemier dlidkdfink rcvkfdeyke lmlndkydkh ffeklkgfek ikeqieeiak
      301 litkktifaw glgvtehidg teavnaisnl ammsgnfakg agvlplrgqn nvqgacdvgc
      361 lpyflpdyir pdeehiglmt pdvideilng nikaiinmge dilhihpnqn kihkafeele
      421 flmvmevmpn eitkradivf avksayeksg vyvnaerrlh lstplvkssl pddweiikel
      481 anrfggtlky eksedvfedc kkevgrfrga syerlkqkpl qwpikedgsd spvlhlekfs
      541 tsdgkghfhy hkyhlrgeve dilegkkrww lntgralpqy nnsaqtkpse kltskydddi
      601 llvneihkne isqkvklrsk ygesaelkvk ftdkvrpytl yttfhfaknk inylfgdead
      661 hkvktarfka veveiinl
//
LOCUS       WP_457564070             394 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Caminibacter pacificus].
ACCESSION   WP_457564070
VERSION     WP_457564070.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..394
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45941
     Region          55..391
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mrdyilqkea eeikfapmms vseflnrkpl fykeidvlrm praynlirnk ikippvihii
       61 gtngkgstgr flahtllkrg ykvghytsph imkfneriwi ngenisdefl eevhqklqkl
      121 lpknvidsls yfeyttflaa lsfegldfvi meaglggefd atnvfekeis lvttidldhq
      181 sflgdniidi attklnsiqn eaiigkqihe dvewvvqkki negkkiykyl dffeideiee
      241 lkkefkfakf lfpnfllams ylkkrgisfs pkdlddlrlp grfeeiekdl widvghnpla
      301 areivkslpk kvnlvyntya dkdyeeilki lkpkinklyl idvkndriee kekrkktaek
      361 lgidveefkk ikkpmlvfgs fsvveeflke yygk
//
LOCUS       WP_457564069              94 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Caminibacter pacificus].
ACCESSION   WP_457564069
VERSION     WP_457564069.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     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=10780
     Region          1..88
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrlsqkeiet ikkiindffg eseiylfgsr vddmkvggdi dlfvipknre gnlfekkika
       61 svklenllql pvdivvhydf erliekealk gikl
//
LOCUS       WP_457564073             462 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Caminibacter pacificus].
ACCESSION   WP_457564073
VERSION     WP_457564073.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..462
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52625
     Region          1..386
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtfndfnlkk eilrrleeig fekpspiqek aipvvlegkd vvaqaqtgtg ktaafglpil
       61 skmkkgekal vitptrelai qvseeifrfg kylgihtatv yggssysrqi khiqnsefiv
      121 atpgrlldll ksgkidiass yvildeadem ldmgflddik eifkfvpsdr qtllfsatmp
      181 epiknlarti lkepefitit rkqvtnenik eyfyvidene rkdalirlid yknpskaivf
      241 crtkkdvddi aeylrgagfe akglhgdmdq rkreeviraf kndrleilva tdvaargldv
      301 nnvthvfnyh lpldpesyvh rigrtgragk egmavslvtp hefralnriq kiskielkei
      361 ptlsdvknse ikkiiekvse vepnaksiei veelqneydl ftiaskfasm lfekeadgke
      421 rigkslkeak rllerekqfs nrnrdsrgrg rgrhrnnrgr rr
//
LOCUS       WP_457564064             606 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein, partial [Caminibacter
            pacificus].
ACCESSION   WP_457564064
VERSION     WP_457564064.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..606
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
     Region          77..606
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 lsklihetqk ergvsagylg shgkkfaeml pkqraltder ikeymqvlkn idfakyspef
       61 kqeieklnqy lkmlpeirnk vnnfqislkd evkwysqmna nilkiigyaa rfapndkism
      121 dlaaytsflk akeragiera vlsatfgadk fapgmytkli rliseqnayi ddfltfaner
      181 mkklyyktik epefaevqrm rdiaishhkt ggfnidpeyw fktitkkina lkriddsiak
      241 iivkdvnsik dnaiieaiig lisiiivlff syliirsfsl qlnslknlil miardkdlsi
      301 evriyeddef geirralrtf laslhevmms ahtssienkq vatnleksfg siteniqkea
      361 nivtnasett nelreklnee aensnevkna ivdaneslqe aiklikdtme niqlnaenen
      421 elamrlqqls qdaeqvknvl tvireiadqt nllalnaaie aaragehgrg favvadevrk
      481 laertqkslg eidatinviv qainsastdm nknienvnrv tektgevqgr iqevstkmee
      541 vvvkvdqnve evekvvkime dfikkmneiq klssenkekv lsnqsyihri atladellke
      601 isqfki
//
LOCUS       WP_457564074             728 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caminibacter pacificus].
ACCESSION   WP_457564074
VERSION     WP_457564074.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 728)
  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 728)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..728
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84677
     Region          332..358
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          334..632
                     /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          399..424
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(400..401,404..405,407,431,434..435,438..439,
                     441..442,465,468..469,472..473,476)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          429..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          506..533
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(540,543..544,547..548,550,580,583..584,587..588,
                     615..616,640,643..644,647..648,651)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          540..573
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          578..633
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          603..724
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          638..664
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkglfslfv ifnllfgyel ivknekdvkv lndlgvkcek itngfvcaks pdkmqlkrlq
       61 yylknnlsiv seivgvqekl sdaskpvmsv kpvksaadik tpkkvaknsk tliktgyciq
      121 vvsarksqgl leifdktknl plsriekigp yyvlrigeek nenalqsvlq kakkinknay
      181 irkcdlipqr iiksnfkpka kkkqeikipq gevfnkifsp eeknklmeka fkegriylar
      241 nlsnqlkstn gykkdaflit vnilmqkkey krvcnmltql sdfykgknls eikekscfyy
      301 nyqkgveymn inpeialdfl kkaqkfksdd nllfataiay mnqydykkak eilqklyknd
      361 sdntaiklay aktlfnlgdf ktlerikdnn laffnhlely lkakklyneg kykeaekiav
      421 klfnyypnni nvlllngnif yklgkydlay iyykrvvkke pqnipalkgl rdvalankdi
      481 tsavkisdil knlkykdkkf neimkeyylf qadklaqegk fkdalsdvke aekyadsekd
      541 iylaygkiyf kmgeykkald yyrmlysrna pleireklir iyirlgkink akeiaqnspn
      601 eikaiyymem akylmnqkky peankyista leynpinsmq aheikawicy ylgdyecakr
      661 yfeksdlklp evrigyafvl aklgnknkay liaqgiknes knillqkarl mielgrekea
      721 keifnsid
//
LOCUS       WP_457564013             395 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Caminibacter pacificus].
ACCESSION   WP_457564013
VERSION     WP_457564013.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kasaragod,V.B. and Schindelin,H.
  TITLE     Structural Framework for Metal Incorporation during Molybdenum
            Cofactor Biosynthesis
  JOURNAL   Structure 24 (5), 782-788 (2016)
   PUBMED   27112598
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Nichols,J.D., Xiang,S., Schindelin,H. and Rajagopalan,K.V.
  TITLE     Mutational analysis of Escherichia coli MoeA: two functional
            activities map to the active site cleft
  JOURNAL   Biochemistry 46 (1), 78-86 (2007)
   PUBMED   17198377
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Schwarz,G.
  TITLE     Molybdenum cofactor biosynthesis and deficiency
  JOURNAL   Cell Mol Life Sci 62 (23), 2792-2810 (2005)
   PUBMED   16261263
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Nichols,J. and Rajagopalan,K.V.
  TITLE     Escherichia coli MoeA and MogA. Function in metal incorporation
            step of molybdenum cofactor biosynthesis
  JOURNAL   J Biol Chem 277 (28), 24995-25000 (2002)
   PUBMED   12006571
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Schrag,J.D., Huang,W., Sivaraman,J., Smith,C., Plamondon,J.,
            Larocque,R., Matte,A. and Cygler,M.
  TITLE     The crystal structure of Escherichia coli MoeA, a protein from the
            molybdopterin synthesis pathway
  JOURNAL   J Mol Biol 310 (2), 419-431 (2001)
   PUBMED   11428898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096840
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..395
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43545
     Region          9..395
                     /region_name="MoeA"
                     /note="MoeA family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (MoCF), an
                     essential cofactor of a diverse group of redox enzymes.
                     MoCF biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00887"
                     /db_xref="CDD:238452"
     Site            order(29,136,151..154,156,159..160,162,196,198,201,324,
                     363,391)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238452"
     Site            order(179..180,182,221,245)
                     /site_type="active"
                     /note="putative functional site [active]"
                     /db_xref="CDD:238452"
     Site            order(245..247,292..293,297,300)
                     /site_type="active"
                     /note="putative MPT binding site [active]"
                     /db_xref="CDD:238452"
ORIGIN      
        1 mfikvtrnea keiidsltsq kyyetitide aegrvlfedm kakfnipesd ksavdgyain
       61 idnltfpakl kiideapage aqkelkdgai fimtggvvpk ganavvried vekegdyivi
      121 kkpvkkgdli nfegeevktg nvvlkkgeil dykkvallan lghyqikvfk kvkigivvtg
      181 sevkepfeal dkagvknsnl yilkgllkpy adityygklp dnldemikvf knaieendil
      241 issggaskgk ydftkeiakq igvdikfttt nirpgrplif gnkgkklffg lpgypaallv
      301 naveflipyv kkaagivnyq neykkavltt ktkakegrvd firgniecde kvtftpaytq
      361 qtsnylsial snalaviden egtkeageiv eyili
//
LOCUS       WP_457564076             208 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457564076
VERSION     WP_457564076.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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) (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="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..208
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23895
     Region          126..>180
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkklvflgvf svlfgyqlgv kaqdaeklrn fgleckpage yciyaigsnk esllkvekyi
       61 rkelgiesyf vnntsdvtne tpsevvsdkt eqtieakqht evntdtssyv eekpietenv
      121 tdideskkyy syqvissprl sdakkayeki knlpyariek ignyyvvrvg lydhyreakk
      181 eglkymitrc fykksriike ndengssy
//
LOCUS       WP_457564077             378 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caminibacter pacificus].
ACCESSION   WP_457564077
VERSION     WP_457564077.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..378
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43212
     Region          3..378
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mrvlivgagi igmtmawewr kkhpddeivi idkepheafh asgknsgvlh agfyyssdsl
       61 kakltargnk lmkefcyshn ipvnetgklv vakneneipt lfelakrsva neagayiitq
      121 eeaekidpna kthkyalysp ntatvnprev crvlkeelqk kdvkfifnmp fekynesydf
      181 linaaglyad kiahkfgvgl eytmlpfkgl yrkylgedki ktqiypvpni knpflgvhft
      241 lmadntikig ptaipafwre nyvgferfdf refleiisle aklfftnafg frdlalyemr
      301 yyipqnline akklvknlrg efkpmtpgir aqllntqtle lvmdflvekn dnqihilnav
      361 spaftasfaf skyvleel
//
LOCUS       WP_457564079             416 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caminibacter pacificus].
ACCESSION   WP_457564079
VERSION     WP_457564079.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..416
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45803
     Region          1..369
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mgdlkktigv fsgiaiaigm vmgsglfglp glaidiagak lsllgwlaii lavipmiyif
       61 iklgikfpka gglstyakaa fgdwaefgvv avlsgtfiig ipalaiigge yltklfsisi
      121 elkyffaflf llfatiiniy gvqmaswink islifillli ivlviihpdy ltegikalnf
      181 ktenikinkl wevmallfwa flgwenlsfg leefknpkkt ipiiywgsff ivsmfyfmla
      241 llvsgavisg ikvsgasaia silsdnvtls kfliffmvvv iiananswvf gasrliysag
      301 kdgilfkklg ilnkkgipsn alitlmifya ffifalyyfk idlstiimiv sqnflvlylf
      361 siitfaklfs gvidrivlll ssvillfffq gfgvaiiypl illligfvry kktske
//
LOCUS       WP_457564091             135 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease, partial [Caminibacter pacificus].
ACCESSION   WP_457564091
VERSION     WP_457564091.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 135)
  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 135)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         <1..135
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <5..133
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 vwvsvglilf gvfdmpingn lwhffllnll fafslggigl viaaisntvt evgqysfmlm
       61 mpliflsgaw tpissmapwl qklsiispvr yyieasesif frgasfydli pyfvalliig
      121 mvlfyigykk igrlf
//
LOCUS       WP_457564097             322 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Caminibacter pacificus].
ACCESSION   WP_457564097
VERSION     WP_457564097.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Shek,R., Dattmore,D.A., Stives,D.P., Jackson,A.L., Chatfield,C.H.,
            Hicks,K.A. and French,J.B.
  TITLE     Structural and Functional Basis for Targeting Campylobacter jejuni
            Agmatine Deiminase To Overcome Antibiotic Resistance
  JOURNAL   Biochemistry 56 (51), 6734-6742 (2017)
   PUBMED   29190068
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..322
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016813 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear
                     amidines [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37566
     Region          4..310
                     /region_name="PAD_porph"
                     /note="Porphyromonas-type peptidyl-arginine deiminase;
                     pfam04371"
                     /db_xref="CDD:461280"
ORIGIN      
        1 mnylipewek qsfvqlvfph ketdwscclk eaiktfteia yaiaqyqkvl icyqdentis
       61 hlkhknfifr kvknndtwar dfgaisvkkd tqiklldfkf ngwglkfpan ydnlisrqlf
      121 nihksynfvl eggsidtngk tllttsqcll epnrnyplsk deieeflkne lfvdeiiwln
      181 hgflegddtd shidtlarfv dentivyckc sdssdihyke lakmeeelkk tsfniiplpl
      241 pspkywnnhr lpatyanfli innavllpvy ddvkdkyvyd lfnslfpdre iipinantli
      301 kqhgsihcit keyfnedfis ae
//
LOCUS       WP_457564108             283 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Caminibacter
            pacificus].
ACCESSION   WP_457564108
VERSION     WP_457564108.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..283
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31482
     Region          10..283
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mtreqiykek kqiaifsiiv nltlslikii ggklsgsaal tadgihslsd laasfsvltg
       61 iviankkakd fpmglykven lvalisafai ffagyeiakd vffgepmkih nlpialiaiv
      121 ltviityfys rwekkkaiel nspslladae hvksdfftal vvlvgvigqy mgypiiekia
      181 vaivvyfifh sgweilvdai kvlldasvek etidkvreil dkedmiekin dikgrnagsf
      241 kfiyldidvk tdsikeahay vhkledkike aipevekvit hye
//
LOCUS       WP_457564102             362 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457564102
VERSION     WP_457564102.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 362)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..362
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42052
     Region          113..362
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnlkhykiri tifsililvt ffaiflsyev nkktinslke nlakkiyilr knellthekn
       61 lqnflknfkn aeiistkenp gykiidntvi sifrikdkti iikdsikqei spllqlatin
      121 livitvislm fftlmfcfie fllkrfkivr siianikqrk feklppltpe knicdefrne
      181 iiklgreiet yikllslkve dykkkayide lthtfnrnfl keieskiflk akvssfptsv
      241 imididdfkk indtyghkkg devlahiaki lqnnlrkedi liryggeefl tllnetelht
      301 alaiakklik avesnplnnl katisagvsk ieyndknlyd svkradsnly kakrngknrv
      361 ei
//
LOCUS       WP_457564110             163 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidylglycerophosphatase A family protein [Caminibacter
            pacificus].
ACCESSION   WP_457564110
VERSION     WP_457564110.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Kumaran,D., Bonanno,J.B., Burley,S.K. and Swaminathan,S.
  TITLE     Crystal structure of phosphatidylglycerophosphatase (PGPase), a
            putative membrane-bound lipid phosphatase, reveals a novel
            binuclear metal binding site and two 'proton wires'
  JOURNAL   Proteins 64 (4), 851-862 (2006)
   PUBMED   16838328
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Chang,Y.Y. and Kennedy,E.P.
  TITLE     Phosphatidyl glycerophosphate phosphatase
  JOURNAL   J Lipid Res 8 (5), 456-462 (1967)
   PUBMED   4292860
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10731865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..163
                     /product="phosphatidylglycerophosphatase A family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17786
     Region          1..154
                     /region_name="PgpA"
                     /note="Phosphatidylglycerophosphatase A [Lipid transport
                     and metabolism]; COG1267"
                     /db_xref="CDD:440878"
ORIGIN      
        1 mnklnwfllt gfysgllpka pgtcgsivgv iiaylviiym pnpnmtimll aalfsiigfk
       61 lvneyeangg ihddkrivid eiagvwitig vlgdwkhdtf iklllafisf rlfdiwkpsi
      121 igkidqkakg glgvmgddil agifggifag ilymgylklk tmi
//
LOCUS       WP_457564111             228 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein, partial [Caminibacter pacificus].
ACCESSION   WP_457564111
VERSION     WP_457564111.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 228)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>228
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
     Region          <64..228
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mekykfgese vfssfpitks ffdkwiknrc gkvesddkkf cvireddnty lissskcfns
       61 yiskltenai fdsltgaynk keilealkkq lenyirykke pfsvmifdid ffkkvndtyg
      121 hlagdfilke fvkiikklir ksdilgrfgg eefvlilpnt kisgamklae riknaienht
      181 fnfnstpikv ttsigitsas ltdsvdslla radealyeak rkgrnrie
//
LOCUS       WP_457564112             261 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Caminibacter pacificus].
ACCESSION   WP_457564112
VERSION     WP_457564112.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..261
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30381
     Region          146..253
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mkevlkeiie keaddliryw veefpeeerd eearyyedfl sffeecvekd ldihspesea
       61 lktflekiie ilgedrffnf knsvytcylk fpimkkleek kafeydiikk ltiffealts
      121 riiidllkkn eqvtmsamne leereapiae iwdgvlmlsi vgtldsnrvl kiidkilekl
      181 dkreiehvvv digaihdmns evarqiikln naihfmgsna yltgitpaia kslthldikl
      241 ddiktfsttk kamehilhge i
//
LOCUS       WP_457564114             496 aa            linear   BCT 27-JAN-2026
DEFINITION  ArnT family glycosyltransferase [Caminibacter pacificus].
ACCESSION   WP_457564114
VERSION     WP_457564114.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 496)
  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   3  (residues 1 to 496)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..496
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57092
     Region          1..354
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mekrlkialf laiainffft lhltplfnld egafseatre mlknhdfitt ylngalrfdk
       61 piliywfqal svtifglnef alrlpsalaa tfwafgiywf akkifdekig vlsaffmvta
      121 lqigliakaa iadallnmfi afsmfslyly iqnqnkkyly ftfafigfgf ltkgpvavli
      181 platffiysl ikkdfkfflk ttfdlkgivl fliialpwyi aeymaqgdkf ikgfflkhni
      241 drfetslekh kgslfyyipv iligmlpwts lllkyltklk nylkeqndff lfgsiwfffv
      301 fiffslsgtk lphyviygyt pvfifmgvaf kelkseflys lplilfvlal lilpsfalnl
      361 tknkeaviai ktimplfniw yyiflgvvli lsllklgken ktiilgfsmv filnyvgwiy
      421 aharaipvkq aaifakkhni knvyletnlp sfsvyfdkit prkkakkgev alikskntkg
      481 ykvlfkkglv algvke
//
LOCUS       WP_457564115             110 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caminibacter
            pacificus].
ACCESSION   WP_457564115
VERSION     WP_457564115.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..>110
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          17..>107
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mkiliigggp agataarlla kefdvtliqd rvwdkpcggg vkkrvfeefs ldnslilhlq
       61 drvfmvykne kieiplkgdn laivrrldfd aylrneaqke gakliygkfk
//
LOCUS       WP_457564118             423 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter pacificus].
ACCESSION   WP_457564118
VERSION     WP_457564118.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..423
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46883
     Region          25..409
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mdkslkltfi lftlitgiit gifiviygll tkflsyllfl gdpfesiehl pwwylylipt
       61 vsilivnymi skddsvkeyg vaeiaqavee nrlvftwksl fnkivasals lssgfavgne
      121 gpsaaigamv adkfheffkl pkkllkvsls vgasggiaai fvspitgimf aieniayefv
      181 rdfagylils svtafsvaly fleplifnys agkfieyrni fagilfipvi tffiyfylil
      241 kdklleflnk fltsrflkyk nyifaliggg vigtillisp yaafsghelv nflindklhl
      301 aysvifviiv lriiatavsi yanavggifi almsigalvg ygyaemfnaf fsnitiepfy
      361 faavgaalfm gvnmklplta lvvaleityd ynvivptgil yiivsflvtl tfdihkmifk
      421 gkk
//
LOCUS       WP_457564121             389 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caminibacter pacificus].
ACCESSION   WP_457564121
VERSION     WP_457564121.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..389
                     /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=44911
     Region          8..380
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnnlrnelfy kfaltvflii affegalmfa fvksfdthlk dklalvaaei npthfnkeal
       61 vdiqhkykvf plfvrlikpm nkqqlknikl gykiqkirin gvrekvlsys vekngyivqi
      121 atlystnddr iniiktisil isfviyliil migykfidai akqiemsfak lkrfnsnvsh
      181 elktplaimk seievalmnn tkdcektlks mlqeinyind itekllfltk etkkikledv
      241 dleelilelf ekyaekiefe ldfgdeeydi kgdktllkma lsniiensik ygankivikl
      301 eknkhkiilt ikdngigipk eklpfifdef yrvdeshnkk ikgfglglsi vkniltlhka
      361 kikvnsdegk gvefiiefpl ithqekksa
//
LOCUS       WP_457564123             646 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein [Caminibacter
            pacificus].
ACCESSION   WP_457564123
VERSION     WP_457564123.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 646)
  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..646
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..646
                     /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=73478
     Region          7..646
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 menekrlkli ktacsycgvg cgfvvdekir gdkthpnnkg llckkgslsd rvnnnrllkp
       61 lfrenkneef reisyqeaik ivagklkatk pqkigfylsg qmlnedyyia nklakgylkt
      121 snvdtnsrtc masavvamkr vwgsdyvplt mqdaidsdlv ifagsnaaes hivffnrikr
      181 akkrglkiiv idprftktak eadlyvpisp ggdtyfflav akrflelgvv desvvrevnv
      241 edgyferlke vnidknleka gvkrrifeef vkefienknv vgcwtmglnq ssegveknia
      301 finlfilsgk ifkpkngpls ltgqpnamgg revgglattl avhldyspen vkkveefwgv
      361 sgmptspglt ademikkenl efllvmhtdp vyhlpnrhlt ekkisqidfv vevnayknse
      421 tskfanliip aapfgekrgt qtnldrlisk iipfrekkak qdyeilcdia kelgfsgfdf
      481 ssddevfrey qemtklsdmn iyeakefpfr wgenlsdlkr inllwvepkn rtplpnetys
      541 filvtmrvan hwhsmsktsq vikdevdfve mneedmrelg vssgeivrve seygsvevrv
      601 nkarikrkvv aipmhfrkin ylvhnildpl skepdynttr vrvekv
//
LOCUS       WP_457564129             405 aa            linear   BCT 27-JAN-2026
DEFINITION  L-cysteine desulfidase family protein [Caminibacter pacificus].
ACCESSION   WP_457564129
VERSION     WP_457564129.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Mendez,J., Reimundo,P., Perez-Pascual,D., Navais,R., Gomez,E. and
            Guijarro,J.A.
  TITLE     A novel cdsAB operon is involved in the uptake of L-cysteine and
            participates in the pathogenesis of Yersinia ruckeri
  JOURNAL   J Bacteriol 193 (4), 944-951 (2011)
   PUBMED   21169490
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Tchong,S.I., Xu,H. and White,R.H.
  TITLE     L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from
            Methanocaldococcus jannaschii that catalyzes the breakdown of
            L-cysteine into pyruvate, ammonia, and sulfide
  JOURNAL   Biochemistry 44 (5), 1659-1670 (2005)
   PUBMED   15683250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..405
                     /product="L-cysteine desulfidase family protein"
                     /EC_number="4.4.1.28"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0080146 - L-cysteine desulfhydrase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44408
     Region          5..403
                     /region_name="CdsB"
                     /note="L-cysteine desulfidase YhaM [Amino acid transport
                     and metabolism]; COG3681"
                     /db_xref="CDD:442897"
ORIGIN      
        1 mygakeiils eikpalgcte paavalnaay lreygvydek nlkltvntnl lknamyvpip
       61 ntskrfgvkl afalgylfgd vndglnifkn lneekvkkal efsekvkvel iegselfiks
      121 ensyaeavti kfhdnieyvi skgelkefdn hqeevevksy vledkpfdiv ydlieqeksf
      181 efvreaveln malaeygmnh dvginvskqf sgdslkdkic kittsasdsr mdgvnmpams
      241 ltgsgnhgis atlpvwvyak ekgfreedal kavalsmlit iyvklfigrl svicgaavas
      301 gcgvagaiay legdretskk avkhviqnis tllcdggkma cslkvlqgas vgydsakfal
      361 namevyedgi ifedvtktik alkgikekms gvdeevvkim kekll
//
LOCUS       WP_457564133             134 aa            linear   BCT 27-JAN-2026
DEFINITION  HepT-like ribonuclease domain-containing protein [Caminibacter
            pacificus].
ACCESSION   WP_457564133
VERSION     WP_457564133.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Jia,X., Yao,J., Gao,Z., Liu,G., Dong,Y.H., Wang,X. and Zhang,H.
  TITLE     Structure-function analyses reveal the molecular architecture and
            neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin
            system
  JOURNAL   J Biol Chem 293 (18), 6812-6823 (2018)
   PUBMED   29555683
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Yao,J., Guo,Y., Zeng,Z., Liu,X., Shi,F. and Wang,X.
  TITLE     Identification and characterization of a HEPN-MNT family type II
            toxin-antitoxin in Shewanella oneidensis
  JOURNAL   Microb Biotechnol 8 (6), 961-973 (2015)
   PUBMED   26112399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..134
                     /product="HepT-like ribonuclease domain-containing
                     protein"
                     /EC_number="3.1.27.-"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15782
     Region          3..95
                     /region_name="HEPN"
                     /note="HEPN domain protein, predicted toxin of MNT-HEPN
                     system [Defense mechanisms]; COG2361"
                     /db_xref="CDD:441928"
ORIGIN      
        1 mvdifiaidk ikryiqpfks atellydeks wdavirelei igeatnkllk ydflendyri
       61 ivdfrniivh eyfgineniv wevvneylde fkqklinesk kldlslaika akkenkhnkn
      121 vlnflkeled vlss
//
LOCUS       WP_457564134             277 aa            linear   BCT 27-JAN-2026
DEFINITION  CvfB family protein [Caminibacter pacificus].
ACCESSION   WP_457564134
VERSION     WP_457564134.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Matsumoto,Y., Xu,Q., Miyazaki,S., Kaito,C., Farr,C.L.,
            Axelrod,H.L., Chiu,H.J., Klock,H.E., Knuth,M.W., Miller,M.D.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A., Sekimizu,K. and
            Wilson,I.A.
  TITLE     Structure of a virulence regulatory factor CvfB reveals a novel
            winged helix RNA binding module
  JOURNAL   Structure 18 (4), 537-547 (2010)
   PUBMED   20399190
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Matsumoto,Y., Kaito,C., Morishita,D., Kurokawa,K. and Sekimizu,K.
  TITLE     Regulation of exoprotein gene expression by the Staphylococcus
            aureus cvfB gene
  JOURNAL   Infect Immun 75 (4), 1964-1972 (2007)
   PUBMED   17283102
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Bycroft,M., Hubbard,T.J., Proctor,M., Freund,S.M. and Murzin,A.G.
  TITLE     The solution structure of the S1 RNA binding domain: a member of an
            ancient nucleic acid-binding fold
  JOURNAL   Cell 88 (2), 235-242 (1997)
   PUBMED   9008164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..277
                     /product="CvfB family protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31757
     Region          16..276
                     /region_name="CvfB"
                     /note="Predicted RNA-binding protein YitL, contains S1
                     domains, virulence factor B family [General function
                     prediction only]; COG2996"
                     /db_xref="CDD:442235"
ORIGIN      
        1 mieeylklgs lnklkiskkt pqglyleale gdkvllpnry vtddmkigde ievfiyndse
       61 dryvattdkp kyeygefgvf rvvdvtkfgv fvewgmpkdl fmplanmkke lkkgdsvigk
      121 ivydektdrl mldsklsrhi kkaknydvnd evkiiviakt plgykcivdn kyegmlfnne
      181 ifedvrvgqk kkafvknvrv dgkldlslqk igsrddvldk vyeklkeiks inlttksnpe
      241 dikkvfgisk kafkyaintl lkeekivqen giikins
//
LOCUS       WP_457564139             315 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caminibacter pacificus].
ACCESSION   WP_457564139
VERSION     WP_457564139.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..315
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35669
     Region          5..180
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,90)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(39,89..90)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            88..90
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mklsvvvplm neednikyli eevdkalkdf dyelilvddg stdntveeik khmndktklv
       61 ilnrnygqts amaagievas gdiivtidgd lqndpsdipm mveklnegyd vvagirakrk
      121 depfrkflsk iankiirkvt gvhitdygct lkvfkkdvak nlqlygelhr fipilaemyg
      181 akitevpvkh herkfgksky gfnrtfkvis dlmylvfmqr fgqkpmhffg tvgfimfslg
      241 vlidfyllil klfgqsiggr plltlgtmli lggiqlittg flaeimirty yesqgkkpyv
      301 ikeivtkdsq mrves
//
LOCUS       WP_457564140             277 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caminibacter pacificus].
ACCESSION   WP_457564140
VERSION     WP_457564140.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..277
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31273
     Region          35..271
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkklkpfika afiliafiii fqkiniqelk nikitspfyl flaflsfnls qiisalrvht
       61 ylknikvtpt fkkqlmlyyv gmfyntllpg giggdaykay kfeksysqgy kkiikallid
      121 risglfaifi lisaliflss fkqfvifsai llivspfily flhkyffvef tksflknlfl
      181 siviqslqal aflfilfaln ihshlidfiv lffissiisv ipisvggvgl reltflygld
      241 mlhlnatigv vaaflffvis vissaigalf ikgvknv
//
LOCUS       WP_457564143             381 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Caminibacter pacificus].
ACCESSION   WP_457564143
VERSION     WP_457564143.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..381
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43175
     Region          46..354
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mkksklqkff ekladllhwe ksskpevdls peiwselkpf rtpiiltili elfgtlgyiw
       61 idhfslldai yqtgitfttv gfgeiapisp lgrlftifli iagfavfsya vgvlvdvink
      121 grliallkek rmlykiarlk shmvicyhne ytidvtkelr aahipfvvid nrddmeeiak
      181 kykypyfvkg dphttlslkk ahlssakgvi tlsnntpdni avvssvrlye kdikrhpyyi
      241 lsvaqsdedi eklkrlgane vlsptkliak rmtavtvdpd vknileefvy sldtpldlee
      301 itvskkswia ykklkeahlr elfnvtvvgi keeggkfipi pkgddvikpg dvllvigtak
      361 dmkkarkiir stkkpkeldf i
//
LOCUS       WP_457564146             538 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Caminibacter pacificus].
ACCESSION   WP_457564146
VERSION     WP_457564146.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..538
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59987
     Region          1..530
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mvspliivia llfialsfni pfarlkippi igyiftgiii snifsldkht ievvaelgiv
       61 flmfmiglef speklksmkk evfgfgfaem tivsgifglv fywffnidir ialiigsaia
      121 lsstaivlkl lnesreiskp ygrialgill fqdiavipil iaisiivnkd adltqlilkt
      181 lggfaalgvf iyiygkfiap fvishatktk sdeifmatvl lvvlvaaeia hffglsyslg
      241 aflagmilse tkykyqiead lvpfrdlllg iffvsvglmv ninfvihnif sillmtvafm
      301 lskagiiylm lkffvkhnri aiktafilsq igefafvifa llgkynlves dllqklvvvv
      361 vismiltpfi lryiykiadi fdkevqnfee felkpaevag hiiligydki gqrvarkltr
      421 agipyvaidk qielvkqglk ngdnvifgna ankrvlesln vkdasaviit tlneehthli
      481 tenilainpn lnvivltdde iekefyknhn vyvvdkskel aeklislalr celrkerg
//
LOCUS       WP_457564147             314 aa            linear   BCT 27-JAN-2026
DEFINITION  KpsF/GutQ family sugar-phosphate isomerase [Caminibacter
            pacificus].
ACCESSION   WP_457564147
VERSION     WP_457564147.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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..314
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..314
                     /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=34108
     Region          1..309
                     /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 mdfrkiarev ldieadallk advsgiekav eiayntkgkl ivtgvgksgl igskiaatla
       61 stgtpsffih ptealhgdlg mitkddsvla isysgeseel ikilphikrf evpliamtgr
      121 mdstlaryad vvlnihvdke acplnvapts sttltlamvd alavclmkkr nftkedfasf
      181 hpggslgkkl fvkvkdlmke efpvvdedvs lkdaiikmte gklghvlfld ngkvkailsd
      241 gdlrrammse nfdlnkkaie fatlnpktin kemlasdala fmednkiqfl pvidnygnvv
      301 gvihihhlve agik
//
LOCUS       WP_457564096             227 aa            linear   BCT 27-JAN-2026
DEFINITION  YaaA family protein [Caminibacter pacificus].
ACCESSION   WP_457564096
VERSION     WP_457564096.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter pacificus
  ORGANISM  Caminibacter pacificus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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..227
                     /organism="Caminibacter pacificus"
                     /db_xref="taxon:1424653"
     Protein         1..227
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=26286
     Region          2..205
                     /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 mkillapser kslggdksfn issfkelnpl reeaikkyde fiqktddikn fgdiktpike
       61 rpakeailry tgvafeyldy ptlpneakey lnenliifsn lfgigkptdl ipyytlkqgs
      121 kpgfdiykfy kekvteilds lnedfidlra kfyekiykpk navtfkfikn gkvvshfaka
      181 yrgtltrhia lhkpktieev lkiefpdiei meiqekkgik eivceik
//
LOCUS       WP_457564345             402 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein, partial [Caminibacter sp.].
ACCESSION   WP_457564345
VERSION     WP_457564345.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 402)
  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 402)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 402)
  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 402)
  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 10135482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..>402
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          91..289
                     /region_name="GT2_RfbC_Mx_like"
                     /note="Myxococcus xanthus RfbC like proteins are required
                     for O-antigen biosynthesis; cd04184"
                     /db_xref="CDD:133027"
     Site            order(129,180..181,263)
                     /site_type="active"
                     /note="Probable Catalytic site [active]"
                     /db_xref="CDD:133027"
     Site            order(181,263,265)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:133027"
     Region          348..>397
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
ORIGIN      
        1 mlkkiidiam ndykkgddpl rifkkswary kkhgflgmky rlekewlkln pnvtqinnqq
       61 fndrissryi yqapklteei kkeiknfqkk plisiimsvf nvepkwlkka iesvenqwyd
      121 ncelciadda stkketiefl ktiknpkiki kfldknlgis gasnealkma egeyialmdn
      181 ddeltpdaly evvkvineke aefiysdedk iemsgefvep hfkpdfapdm flsqnyishl
      241 gvikkelvek vggweigleg sqdydlylkv lehtdkiyhi pkvlyhwrki pgstaaeytq
      301 ksyaqeagrk alenamkrrg ikakvknglt pgtykvkyei kgeplvsivi pfkdkpellr
      361 qcigsilekt tyknfeiigi snnseeketf eemkrlesld kr
//
LOCUS       WP_457564430             253 aa            linear   BCT 27-JAN-2026
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase,
            partial [Caminibacter sp.].
ACCESSION   WP_457564430
VERSION     WP_457564430.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..>253
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
     Region          <15..252
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mesvfferin kinpeifegl kekkefsfri nrhkadfeav eelkkegynp kpvswseyvy
       61 tlpieerkki tksapytqnk iyiqnlssii aansldiden dwvldlaaap ggkslifsek
      121 arlvsavepd kkrffrmkrn fkehgakniq tynkdgrfvy katgemfdkv fldapcssea
      181 hieldkgitw wnlkrvkrfs klqkelmisa fealkpggem iyatctfspe eneenvdfll
      241 rryknaeivp vnl
//
LOCUS       WP_457564493             102 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein, partial
            [Caminibacter sp.].
ACCESSION   WP_457564493
VERSION     WP_457564493.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         <1..102
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          5..102
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 eimeliktlq kdapeeikgf lefmknvekd gaisaknkel iniglavaaq cewcitfhtq
       61 nalklgatre eiieagmqav lmhggpalmy mipllkalee ls
//
LOCUS       WP_457564805             205 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane protein assembly factor BamD [Caminibacter sp.].
ACCESSION   WP_457564805
VERSION     WP_457564805.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Albrecht,R. and Zeth,K.
  TITLE     Structural basis of outer membrane protein biogenesis in bacteria
  JOURNAL   J Biol Chem 286 (31), 27792-27803 (2011)
   PUBMED   21586578
REFERENCE   3  (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 1003154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..205
                     /product="outer membrane protein assembly factor BamD"
                     /calculated_mol_wt=24251
     Region          15..>150
                     /region_name="BamD"
                     /note="Outer membrane protein assembly factor BamD,
                     BamD/ComL family [Cell wall/membrane/envelope biogenesis];
                     COG4105"
                     /db_xref="CDD:443281"
ORIGIN      
        1 mrktlfiipl llflgcsskn qiqknlkait ihsklvkavk ennfdkaddl fltmeaehpt
       61 siyvkqdlli lylghlnygd fklakfylnq yetryaskde ipwceyqkik vdflsyhnay
      121 tnqkkildli kecknyklsy pnsqflpevn tiymkayltn lylddkiskl ykkegkikas
      181 keykvkvpkn svppqvpwyk kifyw
//
LOCUS       WP_457564909             259 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Caminibacter sp.].
ACCESSION   WP_457564909
VERSION     WP_457564909.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..259
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27496
     Region          1..258
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 madilkigky eftsrlivgs gkypdfkttr datlasgaem itvavrrvni ldpneenlmd
       61 yfkdtdvkil pnsagcttae eaitlfrlvr eatgidiikl evigdtkktl ypdvietlka
      121 cevlakdgft vmaytnddpi makrledaga aavmplaapi gsglgvqnry nvvfvkdavn
      181 vpvivdagig tasdaavame lgadgvltnt aiaqaknpie maeamkyavi agrmaykagr
      241 ipkkpfatas spleglief
//
LOCUS       WP_457564958             440 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Caminibacter sp.].
ACCESSION   WP_457564958
VERSION     WP_457564958.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter sp.
  ORGANISM  Caminibacter sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Caminibacter sp."
                     /db_xref="taxon:2848135"
     Protein         1..440
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49364
     Region          19..417
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mvakiknffn kkayifrdfl llsfitglvt glfvsvyifl tkwfmkflyh gdpvntisvl
       61 pvwyvymipi vsilivnfli sldstvkeyg itklaeivek rseiitiksl flkiiasvls
      121 issgfsvgne gpsaeigals afyvkklfki pekfiriivs vgassgiaav fvspltgitf
      181 aiesiaseff ksyiifmivg afsafsiave ffpaigflsp sgrfinfdyv wlnivfipii
      241 tffiyfylfl qekvlyvfnf kifekfgkyr nlffaifggf iigtilliep kacftghfvv
      301 qelfndfstm slklivilii lrivattisq ysnavggmfl plmsigalig ygfgevmnmf
      361 hfvniqpyyf aaigaavfmg vlmklpftav vlaleitndy nvvlttgfav aviayvtkln
      421 fnikkfntvq idfkeilhik
//
LOCUS       WP_457565159             485 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457565159
VERSION     WP_457565159.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 485)
  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 485)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 485)
  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 485)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..485
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=55266
     Region          5..482
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mqfnqkinil liedeeydvk rvqktiapls dqirikkiva dgqsalealk kspnyfdvvi
       61 mdyqllggit genlirkike vdatlqiivi tkmtvnitdf dfanrlieag amwyctkypg
      121 diedfiyqpt dfilsilnaf ekrrllkkeq sskrkleqsi eellqqkali geseamralr
      181 skiakiaqqe atvlilgesg tgkelvathl hylsrrrfek fltincgslp hdlieselfg
      241 fekgsftgav ekkiglfeaa nqgtlfldei gelpmsaqvk llrvlqdgei dkigrtdkvk
      301 vdvrvvaatn kdlvsavqqk tfredlfyrl nvinlyippl rerkedipll lehffkhfah
      361 tmgvdvpqis ssamdylqgf dwpgnvrqlq nvvqrllynv dgmidvsdvk dslglapksr
      421 aavdsengfe wdpihitpwr eierafrkky fefvrkraas daqaarllgl appnfhrmck
      481 elelk
//
LOCUS       WP_457565162             338 aa            linear   BCT 27-JAN-2026
DEFINITION  dipeptide epimerase [Caldithrix abyssi].
ACCESSION   WP_457565162
VERSION     WP_457565162.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Lukk,T., Sakai,A., Kalyanaraman,C., Brown,S.D., Imker,H.J.,
            Song,L., Fedorov,A.A., Fedorov,E.V., Toro,R., Hillerich,B.,
            Seidel,R., Patskovsky,Y., Vetting,M.W., Nair,S.K., Babbitt,P.C.,
            Almo,S.C., Gerlt,J.A. and Jacobson,M.P.
  TITLE     Homology models guide discovery of diverse enzyme specificities
            among dipeptide epimerases in the enolase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 109 (11), 4122-4127 (2012)
   PUBMED   22392983
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Kalyanaraman,C., Imker,H.J., Fedorov,A.A., Fedorov,E.V.,
            Glasner,M.E., Babbitt,P.C., Almo,S.C., Gerlt,J.A. and Jacobson,M.P.
  TITLE     Discovery of a dipeptide epimerase enzymatic function guided by
            homology modeling and virtual screening
  JOURNAL   Structure 16 (11), 1668-1677 (2008)
   PUBMED   19000819
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..338
                     /product="dipeptide epimerase"
                     /EC_number="5.1.1.-"
                     /GO_function="GO:0016855 - racemase and epimerase
                     activity, acting on amino acids and derivatives [Evidence
                     IEA]"
                     /calculated_mol_wt=37579
     Region          2..309
                     /region_name="L-Ala-DL-Glu_epimerase"
                     /note="L-Ala-D/L-Glu epimerase catalyzes the epimerization
                     of L-Ala-D/L-Glu and other dipeptides. The genomic context
                     and the substrate specificity of characterized members of
                     this family from E.coli and B.subtilis indicates a
                     possible role in the metabolism of...; cd03319"
                     /db_xref="CDD:239435"
     Site            order(20,129,152,154,178,205,230,280,282,302,304)
                     /site_type="active"
                     /db_xref="CDD:239435"
ORIGIN      
        1 mievktkrln lahtwtisrn ssnfknnvfv rierdgivgy geaapnvryg edhvkttqri
       61 neakkifeqn nlfhfaeikd alektildqs cakaaldial mdwigkafnl plyklwglnp
      121 ekapvtsfsi gidtvevikq kvreaeaypi lkikvgtdrd reiikavrsv tdkpirvdan
      181 egwkskeeal ekikwlkdqg vefieqpmpa emldetawlr dradmpiiad eavktaadip
      241 klakaydgin iklmksgglq ealrmigmak slgmkimlgc miessvaisa aahlapfvdy
      301 adldgnllis ndpfsgvkve kgkfvfndkp glgvegkf
//
LOCUS       WP_457565167             244 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457565167
VERSION     WP_457565167.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..244
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28248
     Region          21..141
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 myeqfaryyd lifpfrdaty rflkswlknd rnrildlgcg tggylarfaq eghevvgidl
       61 netmlqmakq rcpqgtwlal nlknldelpa rlprdrnerf dlifctgnvl sylapdelgq
      121 aigaifnllk pqghwifqvv nwqnilrqtt fvfpvienre qgvrfirayn nltpagaifq
      181 trlekdgkii fedahrlfah dshdlralhe knnfkkvgfy gdfkktpfqp eesgaligvf
      241 kken
//
LOCUS       WP_457565161             332 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457565161
VERSION     WP_457565161.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   9  (residues 1 to 332)
  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 19806637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..332
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          63..187
                     /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          72..114
                     /region_name="SH3_16"
                     /note="Bacterial dipeptidyl-peptidase Sh3 domain;
                     pfam18348"
                     /db_xref="CDD:436429"
     Region          <193..330
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 dkslavfdfh lqkengqwvl tgettvpqar tallqkldsl lqqnvhdqsl ilphpdlgds
       61 swaivrvsva nlrrdpahts elvdqsimgn vlrllkryks wylvqthygy lgwmtkysfv
      121 rtdqegvenw qkarrimvyw pvdriyseps dasvpvvdvv mnctlkelnr rgkwilvetp
      181 dqrrgyilkk hvgplvenrd psqvsssall ntafqlmgip ylwggnsakg sdcsgftqta
      241 fkhhgiqlpr darqqallge qvvpaedfsn vmpgdllffg qserithvgi slggykfihq
      301 drevrinsfn pqdddfnayr kktlklikri lk
//
LOCUS       WP_457565169             263 aa            linear   BCT 27-JAN-2026
DEFINITION  uroporphyrinogen-III synthase [Caldithrix abyssi].
ACCESSION   WP_457565169
VERSION     WP_457565169.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..263
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29129
     Region          3..237
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mklknktivi trqpeqartl tqliekeggk allfptiatv aadeniagqe rviarleqfd
       61 wliftsenav kfflkrlqdg aiqlpaikia avgtrtaetl ekegipihli pddfsakgli
      121 dafttselrg tkilipssnl areelqtglk lhgaqvetvi fyktvpnpnf dhkafrslll
      181 nkqidvitff spsafnflve ilcleglnll qtsetrlaai gqttarainm qglkvhiipk
      241 istskgmvea iinyyegked erk
//
LOCUS       WP_457565176             339 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Caldithrix abyssi].
ACCESSION   WP_457565176
VERSION     WP_457565176.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..339
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37335
     Region          8..335
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mandkpqvwv fveqrsgtpa dvsfellskg yklanqlkgs lkavvighnm kdvakrtfky
       61 gadealvvdh pslkeyntlp ysrilsqlid erqprivlfg atfigrdlap rvashtksgl
      121 tadctdlqis dvtylrkdyk dlllqirpaf ggniiatiit pdtrvqmatv regvmemhel
      181 ekavngkite ipytpdptde lvkiiehhre eskvnlkaap iivaggygmg skenfqllye
      241 ladllggeva gsraavdagf ieherqvgqt gvtvrprlyi acgisgaiqh ragmeeskki
      301 iainndpeap ifdichygiv gdamevipkf ievfkhklk
//
LOCUS       WP_457565177             296 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Caldithrix abyssi].
ACCESSION   WP_457565177
VERSION     WP_457565177.1
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 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..296
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32284
     Region          4..295
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 msykivvlvk qvpdtanisg evmkpdgtvn ramlpaifnp edkvalelal qvkdrhgaqv
       61 iamtmgppka sevlreclym gadeailisd rkfagadtla tsyvlsaalq kigdydlvfa
      121 grqaidgdta qvgpqtaekl gipqitytee ivnlskkqit vkrkidggqe vvegklplll
      181 tvvkdaaipr pfkarrvmay knartlmele klvegnslls idtlqdeyqs kglfiktwtm
      241 ddlnveperc glhgsptkvh kvesvvlasn ehikieptke gigllidkll edhvlg
//
LOCUS       WP_457565180             350 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caldithrix
            abyssi].
ACCESSION   WP_457565180
VERSION     WP_457565180.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..350
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38680
     Region          42..340
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkmvkiklfi vfilstlifl qscnnkkdka aeikpvavrv vkpqittlqe kisyvgtiqa
       61 yrevkiisrv pgtilslpaa egirvkkgev variyapele atvqrlqaev dywtrryead
      121 qrleaenaip peqvamsrra ylsakasleg aqsnldktie rspfdgevlr wmvdpgqpvm
      181 pgqpililgd nntevqvevi eeelkrglqt gtpvvlhkkd gtsvqsavre iaplasgisr
      241 tfivriavpp slrnewrkge svklgfilks vsnavavpie aiadrdvkph iflvrddkay
      301 rqdvrpgiqq gnlvqvdfpy ngqdlvvvtn lellsdgipv ftvqtgeagk
//
LOCUS       WP_457565181            1032 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457565181
VERSION     WP_457565181.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1032
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112873
     Region          1..1026
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mtlprfslqn kytiyalsia aiifgvlayi slpiqlfpdt applvnvltp ypgaaakdva
       61 dlvsdpiete caalegvhkv tstsqdglsl vsiefnydrd vdiaavdvqn aisrirsklp
      121 rqigepqvlk fstsdrpvlt mgltgenlve irrlaedila pelqrvagva lvdvfgghqp
      181 eisvlvdrnk leayrlrlpm ivnaitthnv slpagqirse grqysfrvde rsrtpedirn
      241 ivlttpmgkr irvgdiatvs egsaedlsrf hvngksaiam qifkqddant vdvveraqqk
      301 faelqkrypq ikmieaeesa sftrqvvsnm fgsvwqalll aaiiiflfls sfqrglvvti
      361 smpmsflltf agmkffgiev nlvtltaiil svgmvvdasv vilenitrry hedklspkea
      421 alagaeeiqf aviagnattl vvlvpllfly gfigktfgpl astliiaflg sllvsltlvp
      481 iltelvtreg gkleklaiki tapwnramek lrrfyigllt rslkarwlvf vtaialfivg
      541 lgllrylgme llpkmdggts fvtvetpsgs sldeteavvr qveqiimqep everistqig
      601 fepgmhsfgg ggvqgptnaf isitltprte rdetiwqiqd rirqklakip niqnyvvres
      661 gstakvttaa sivvsvrged elvlnklgdq ileivrgvpg vvnpyrswrm dqrsillsvd
      721 eeraqelglp paaisqeltq sldginagil rgplgedtpi rvryskafre teqdayavra
      781 lspgdgkifp vgavasgrev kvqglvtren leptlqilal hqdrplnfvt advekavaqi
      841 vapqgysirl egenkdmaes rdelmgalgi aviaiylllv aqfrswvhpi tvmmaiplsl
      901 igvsiallia gksvsmpvmv glillvgivv nnsiilidfi rqrreagaer qkaiidsvat
      961 rfrpimmtsf stivgmipla mewalgaerf splaiavigg mtaatfltml vipilydtfd
     1021 elgnkirnvs lk
//
LOCUS       WP_457565187             776 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457565187
VERSION     WP_457565187.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..>776
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          17..>776
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          254..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          308..345
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          350..389
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          394..435
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          447..499
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 imrrvvlfsl llflihcnvf aqkqkltpil hypdiygdwv vfvaggdiwk anindgqair
       61 ltmhdgeetf pkfspdgsli aftgeydgns dvyvmnadgs qirrvtlhpg gdvvvgwhpt
      121 knkiifrsnr lsyqrfsrlf minpdgsgle tlimheaaqg sfspdgqkiv ynrlgrefrt
      181 wkryfggtaq dlyifdferm kdekitdfpg tdrlpmwign eiyfssdrdg vlniyaldve
      241 tkkvrqitrh kdydvrfpsa gpqrivyelg gylyyvdvkn pqpkkidivi htdapeirpy
      301 lkkvdeavtq iaiapngkra llvargeift vpakegptrn ltnssgsrek davwspdgkw
      361 iayfsdadge yqlyvmdpfg estpqqlthf kngyrhtirw spdskklaft dqtltlyvfd
      421 lhkkklikvd kaefenvdvs ldlkpiydfn wspdgrfiay skmdstlvnk iyiydlqegk
      481 trcvseglfn dfhpvfsrdg ehlffisnrr fdptycdfew emvykklagi yaytlrkdgp
      541 alfplksdeh lepdrqgpkk eegsvtvrid fdglqqriea lpvkrgnyry lavndealfy
      601 lnkeegdfnr fefrkhwpmd lyafdfekne erpvvkkvdg yqlsadgsti ifkqgkkvgl
      661 vpasakeaeg ewlnlsdlkm wyeplaewqq iyreawrmer dfyyepgmng ldwakiydry
      721 lpmvrrsvcr qdirfvigem igelgtshty vfggdvqrka qrvnvgllga dyevdg
//
LOCUS       WP_457565189             698 aa            linear   BCT 27-JAN-2026
DEFINITION  RecQ family ATP-dependent DNA helicase [Caldithrix abyssi].
ACCESSION   WP_457565189
VERSION     WP_457565189.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Larsen,N.B. and Hickson,I.D.
  TITLE     RecQ Helicases: Conserved Guardians of Genomic Integrity
  JOURNAL   Adv Exp Med Biol 767, 161-184 (2013)
   PUBMED   23161011
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Rezazadeh,S.
  TITLE     RecQ helicases; at the crossroad of genome replication, repair, and
            recombination
  JOURNAL   Mol Biol Rep 39 (4), 4527-4543 (2012)
   PUBMED   21947842
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Bernstein,K.A., Gangloff,S. and Rothstein,R.
  TITLE     The RecQ DNA helicases in DNA repair
  JOURNAL   Annu Rev Genet 44, 393-417 (2010)
   PUBMED   21047263
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Chu,W.K. and Hickson,I.D.
  TITLE     RecQ helicases: multifunctional genome caretakers
  JOURNAL   Nat Rev Cancer 9 (9), 644-654 (2009)
   PUBMED   19657341
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Cobb,J.A., Bjergbaek,L. and Gasser,S.M.
  TITLE     RecQ helicases: at the heart of genetic stability
  JOURNAL   FEBS Lett 529 (1), 43-48 (2002)
   PUBMED   12354611
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..698
                     /product="RecQ family ATP-dependent DNA helicase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=79023
     Region          2..556
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
     Region          <560..694
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdqntaerll kiavgnaaar fregqweaid alvnqrrkll vvqrtgwgks lvyfistril
       61 rdrgggptii ispllalmrn qieaaerigi raqtinstnt kewkeiteqv ladqidaili
      121 sperlanesf letlllpiae rvgllvvdea hcisdwghdf rpdykrlvnv lrhlppnlpl
      181 lgttatandr viedvrrqlg didvirgplm rkslalqtgr ltdqaerlaw laehlpqlpg
      241 tgivyvltvr daervanwlk qqgikaaayy sgvedenfed shsyrlflee qflsnrikal
      301 vatsalgmgy dkpdvsfvih yqapasvisy yqqvgragra iplahgvlls gredeeihey
      361 frqtafppah hvhailnale ksdglsirql eaqinlrssq iekalkvlsv enpspvfkdg
      421 skwkrtavdy rmnhemiarl taqrerewre iqqyidsdrc lmvhlarald dpyaeecgrc
      481 ancvgkpvve lktsepliik akrflrhsei ifkprrqvam gafvqygfrg nfpeelraee
      541 grilsrwgda gwgrivaenk hngyfndelv eavkemieqr wrpdpqpqwv acipsqrhpe
      601 lvpdfarrla rslklpfvec iikvaenepq klqqnrfyqc rnldgvfein dqvldtpvll
      661 vddiidsgwt mtvaaallrq agsglvypla lastsand
//
LOCUS       WP_457565191             545 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565191
VERSION     WP_457565191.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   4  (residues 1 to 545)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183286
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>545
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
     Region          33..522
                     /region_name="AmyAc_CMD"
                     /note="Alpha amylase catalytic domain found in
                     cyclomaltodextrinases and related proteins; cd11338"
                     /db_xref="CDD:200477"
     Site            order(133,135,201,251,295..296,324,326,392..393,462,466)
                     /site_type="active"
                     /db_xref="CDD:200477"
     Site            order(253,298..303,306,326..327,348,376)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200477"
     Site            order(295,324,393)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200477"
ORIGIN      
        1 mrifligfli asvaiscvrq apkaeqntdw asgivwyqif perfnngdpa ndptadevpg
       61 adlqpgwqih pwtsdwykmq pwekkqsdrf ydvvftrryg gdligviekl dylkelgvea
      121 iyfnpvfeap slhkydgssy hhidnnfgpd akgdmqrlrq anetedpstw iwtkadslfl
      181 qlikeaharg ikividgvfn htgteffafq dviknqqnsh yahwysvvsw ddpttpqnef
      241 dykgwwgvkt lpelkedeng ivdgprqyif natrrwmdpn gdgdpsdgid gwrldvaeev
      301 akpfwkewya lvkkvnpgai vvteiwhdas gwiaenltda tmnymfsrav meffinhkma
      361 isaeefakkm ndikeryglk nlnllwsmld shdtdrlasm ilnpdrgydr eagprdnpqy
      421 vvrkpnqder kiqklivafq mtfagapiiy ygdeagmwga ddpddrkpmt wpgmkfdpes
      481 hhplpgktrp vdengfdpel fnfykkliqi rqqhpvlkqg dfqfisqsmt ndllvikrvl
      541 neqqa
//
LOCUS       WP_457565194             236 aa            linear   BCT 27-JAN-2026
DEFINITION  DivIVA domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565194
VERSION     WP_457565194.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Kang,C.M., Nyayapathy,S., Lee,J.Y., Suh,J.W. and Husson,R.N.
  TITLE     Wag31, a homologue of the cell division protein DivIVA, regulates
            growth, morphology and polar cell wall synthesis in mycobacteria
  JOURNAL   Microbiology (Reading) 154 (Pt 3), 725-735 (2008)
   PUBMED   18310019
  REMARK    Erratum:[Microbiology. 2008 Jul;154(Pt 7):2168]
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Edwards,D.H. and Errington,J.
  TITLE     The Bacillus subtilis DivIVA protein targets to the division septum
            and controls the site specificity of cell division
  JOURNAL   Mol Microbiol 24 (5), 905-915 (1997)
   PUBMED   9219999
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Cha,J.H. and Stewart,G.C.
  TITLE     The divIVA minicell locus of Bacillus subtilis
  JOURNAL   J Bacteriol 179 (5), 1671-1683 (1997)
   PUBMED   9045828
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466463
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..236
                     /product="DivIVA domain-containing protein"
                     /GO_process="GO:0009987 - cellular process [Evidence IEA]"
                     /calculated_mol_wt=27241
     Region          1..125
                     /region_name="DivIVA"
                     /note="Cell division septum initiation protein DivIVA,
                     interacts with FtsZ and MinD [Cell cycle control, cell
                     division, chromosome partitioning]; COG3599"
                     /db_xref="CDD:442818"
ORIGIN      
        1 mkltpidikk qefktalrgy drvevetyle yvaeeyerll qnnqrlekev galkaelrhy
       61 kdvektlkqt lyevqqtsql skktsekeae lirreaevqa kkmiedarae vsvlkrelad
      121 lkqqkdslit rlryllssql elleiletdd aqldklkskt hqvfkgskra lpvqeksakk
      181 tapaekepei niqndktpaa pqpekkqaks sdekkskksa dffkdifgdd lddflk
//
LOCUS       WP_457565196             322 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Caldithrix abyssi].
ACCESSION   WP_457565196
VERSION     WP_457565196.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..322
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=37225
     Region          17..92
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(17,29..30,32..33,35..36,39..40,42,49,50..55,57)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          82..315
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 meekktiivt esevgfrldq flagkfpeys rsyfnrlikn ndvlvnnqps ksgyllrlgd
       61 eisvhlkrtq idmepepipi nivyededll vidkpagmvv hpgkgnesnt lvnallyhtn
      121 sladtgeavr pgivhrldkd tsgllviakn draqrhlrrq fdtkeifriy walvwgdfde
      181 dtgvirepia rsrknpikfv vdprgrdavt rfkvlqrfqy vtlleirlet grthqirvhm
      241 rhinhpvvgd qlyngretql lnlpqnlrkr gehllkllph qtlharklsf lhprtgqrvd
      301 feadlpenfk talqklpdlf ml
//
LOCUS       WP_457565199             468 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate ammonia-lyase [Caldithrix abyssi].
ACCESSION   WP_457565199
VERSION     WP_457565199.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Fibriansah,G., Veetil,V.P., Poelarends,G.J. and Thunnissen,A.M.
  TITLE     Structural basis for the catalytic mechanism of aspartate ammonia
            lyase
  JOURNAL   Biochemistry 50 (27), 6053-6062 (2011)
   PUBMED   21661762
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..468
                     /product="aspartate ammonia-lyase"
                     /EC_number="4.3.1.1"
                     /GO_function="GO:0008797 - aspartate ammonia-lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006531 - aspartate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51164
     Region          5..462
                     /region_name="AspA"
                     /note="Aspartate ammonia-lyase [Amino acid transport and
                     metabolism]; COG1027"
                     /db_xref="CDD:440650"
ORIGIN      
        1 mkayrkekdl lgareipada lygihtlrav enfplsgrtv hpalihayga vkwacaktna
       61 elgylpeevy rplaqaceem adgkldahil vdalqggagt slnmnvnevl anralqlagk
      121 qpgqyefihp lehvnlhqst ndtfptalrv aairllkqle nelvrlletl qnlekkfahv
      181 vkigrtelqd avlttmgrtf gayadaisrd rwrvykaeer lrvvnlggta igtgitaprr
      241 yifkvvqhln aitglglara enlidatqns dalveadgil qtcavnlhki sndlrwlssg
      301 phaglneiil parqagssvm pgkinpvipe avmqtamtvm gnhtrlvqac aagnlelnaf
      361 mpliadalle nfslltkash ilnrmalkdl qvneanckkq venstailta lvgrlgyeki
      421 qqvaqkmqqt gqsvreivis egwldestfn eltsaeavnr lgteertk
//
LOCUS       WP_457565202             380 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding response regulator [Caldithrix abyssi].
ACCESSION   WP_457565202
VERSION     WP_457565202.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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 380)
  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 380)
  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   5  (residues 1 to 380)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20860620
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..380
                     /product="ATP-binding response regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42919
     Region          4..69
                     /region_name="REC"
                     /note="cheY-homologous receiver domain; smart00448"
                     /db_xref="CDD:214668"
     Region          38..375
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mqalkvlvad deigmrkgvq kvlkkahfkl ekldheirfe ileaedgrqt iellqkepid
       61 lllldykmpe vsglevlewi kkekrdvtti mitayasldv avsatkngaf dflakpftpe
      121 elrtvvekat rnliaqreak rlaeekrkir fqflsvlahe lkapiaaves ylrlmqgraa
      181 geelknydhi isrslirleg mrklifdlld ltriesgekk relrtidlvp iaknsietls
      241 vlaserdiei tlkapeslkl tadhseleii lnnlisnaik ynkdhgkvev ilkesdsqvi
      301 iqvsdtgigm tpeeqsrlfq efvrikneqt rnilgsglgl sivkkiaqly ngtvsvksek
      361 nvgstftval piqqeqqvke
//
LOCUS       WP_457565155             450 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter, partial [Caldithrix abyssi].
ACCESSION   WP_457565155
VERSION     WP_457565155.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>450
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          15..439
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mkpaakssra lgeekigpll frlsvpatvg mlamalynvv dtifigrglg alaiagvsiv
       61 mpiqmlifsl sqtlglgaas iisrrlgakd lggaknafgn vlllniviss livflgylfa
      121 eellylfgsq gamvsyahdy fvyilfgtpf lmfdmilnnv nraegnikfa mmtmvmaavl
      181 niifdpifif tlklgvkgaa lasvlsqflt llvllyyfys grsnltfewk yfspnfkmmk
      241 eilaigassf arhgaasvla ailnhslfif ggemavaiyg iinrilrmtf mplfglvqaf
      301 lpitgynyga gnyervlqtl kfavkyatlt vigififlmi faqpifflfn ddpvlvkega
      361 ralrmiillt pligfqmiga gyfqalgkal aafilaiarq ilfllplifi lprfykldgi
      421 wlafpaadil avgvtlllvv pewkrlkakv
//
LOCUS       WP_457565205             357 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565205
VERSION     WP_457565205.1
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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..357
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
     Region          53..357
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 nkakkisgik ienccysvlk gekmlkeyks eywtftprdr qkskkeekrf aeihciinpa
       61 saarrtrgrw lrllkvlqnt wpdeltftit dfaghatlia rqaveqgskk ivvmggdgti
      121 qetvngllan hqtcleeisl gilssgtgqg laqslglprd lpaqwtvicq gkkrridlar
      181 aifldeekqw qrrlfvnecq iglgadvvqn lsfktkklgg cvgfgftalr talrqpsfki
      241 rlrlndaysv taqvlgvvia ngaftgggmq lapkallddg qldvllihdq salqrlrnfp
      301 siytgkhgmk gafsfyrvrr vallsshkap iaadgeilgs lpltvealps altvtvp
//
LOCUS       WP_457565206             253 aa            linear   BCT 27-JAN-2026
DEFINITION  methyltransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457565206
VERSION     WP_457565206.1
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 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..253
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28578
     Region          66..172
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mlslketwrr wefelrivvs flivalicai sfafypkspl caavvgrwfg lsassattla
       61 yllasvfmaa asllrmwags lltsrrmmrf avqsdglvia gpyrlvrnpi ylsdliafag
      121 falilphvgl lmpfllwlhy hqiiryeeqa lqrshgasfe ryasqvnrlf pgrralkqla
      181 tarrefiinr dglmhnalyl lfipgflfsa rthnlwhall iglpavglwt ylhvriglsg
      241 pspfssrikr skp
//
LOCUS       WP_457565209             342 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457565209
VERSION     WP_457565209.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..342
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40136
     Region          182..317
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          208..236
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(209,212..213,216..217,219,243,246..247,250..251,
                     253..254,277,288..289,292..293,296)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          241..271
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          276..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkfalnvlla lsvtlssaar lqasddawie kvmawtidgy fqkaedflne riartdsais
       61 pcfylasvln skmthfenid dagkfehllt yiikksnerl eqkdlsdsal akyyfyrgsa
      121 ygylayfqgq ngrwvkalen gikaikdlta cteidsamye aylglgtyky wrstklkfvl
      181 wlpfladqre egiadikral rsssnsryma mhqliyilid ykhydealqy areaiahfpe
      241 sqfmwwayah vyykrhdypq avkayqhllk lierhpesnp shwldcqlri aelyrrmgqn
      301 dlarraaeki wqkrsefpet eknrkrlara erllqelneg qy
//
LOCUS       WP_457565213             247 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase family protein [Caldithrix abyssi].
ACCESSION   WP_457565213
VERSION     WP_457565213.1
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 11467867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..247
                     /product="carboxylesterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28460
     Region          12..247
                     /region_name="COG4099"
                     /note="Predicted peptidase [General function prediction
                     only]"
                     /db_xref="CDD:443275"
ORIGIN      
        1 mgwkpcyhva lislfflfmg camqtkttkq gsdllqkkfl kttivktvem nyllylpqdf
       61 ekeskkwplm iflhgagerg ndlelvkrhg ppklveqgrq fpfilvapqc pldrwwnvee
      121 ldawldvlln elpvdrsriy ltglsmggfg twfwailrpd rfaaiapicg wgnpleaakl
      181 kdipvwvfhg ardpviplqr sqemvealek agaevkftiy peaghdswsq tydnpelyhw
      241 flkhqkk
//
LOCUS       WP_457565214             592 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Caldithrix abyssi].
ACCESSION   WP_457565214
VERSION     WP_457565214.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..592
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67291
     Region          2..591
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mfksvlhilf nsinqypkkd lfifyrdhhw qtwsyqevge kvrllahglm arglqpgdri
       61 ailsdnlpew pvtdfavfgl rgvvvpiypt lmprqiayil ndakvkaifv qnalqydkit
      121 aikkevpsle miftyeplsg vatfdkllqe gavhaqsfpn afeesmenid peelcslvyt
      181 sgttgepkgv mlchrgfvfd ivqsearlrl raddvflsfl plshlyerla ghwcpiyrga
      241 tihyargidt vvediavarp timvsvprly ekianamqek aeqssalarn ifywsigtgl
      301 eyhekrragk vnkwlerryr laeklvfnkv kaklggrfrh piaggaplsv etlkifeaig
      361 lpiiegygmt ethliialtp pgevrygscg kpidgikvki addgevlvsg pllmkgyynk
      421 pditkevidd egwlhtgdig ymdeenylfl tdrkkniivt sggkniapap iehklktsky
      481 ieevclvgdk rkfvsalvvp ayeilkewak snkidfdsme sllkndqvlk lyeeeierlq
      541 egfarfekvk kfallaepfs qerneltpsl kikrrvveqn ykdiiesfye eg
//
LOCUS       WP_457565217            1050 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Caldithrix abyssi].
ACCESSION   WP_457565217
VERSION     WP_457565217.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Putnam,A.A. and Jankowsky,E.
  TITLE     DEAD-box helicases as integrators of RNA, nucleotide and protein
            binding
  JOURNAL   Biochim Biophys Acta 1829 (8), 884-893 (2013)
   PUBMED   23416748
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Flaus,A., Martin,D.M., Barton,G.J. and Owen-Hughes,T.
  TITLE     Identification of multiple distinct Snf2 subfamilies with conserved
            structural motifs
  JOURNAL   Nucleic Acids Res 34 (10), 2887-2905 (2006)
   PUBMED   16738128
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1050)
  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 18766567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1050
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=122666
     Region          2..>107
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
     Region          353..1030
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mkidirdlkd rvpdiifkqg leyfkqgrvk ikqwdnisvl atvqgtypyi vrltvnehsf
       61 estctcpyny tckhvvaval kiideqrsae seqvtqqdnw reyfekliti qkvdnefsqe
      121 vrwkliyimh laenywnikp vkvymkkdgs ygrmqepsfg elsgqnvfrt sgdliaisyl
      181 eriqtqqpsv yyrgrletsy ldfgldagql fyllrnselh lknedgtigp rirfgkrpwk
      241 lifklnldee ndlyifrpyf vrdeeqvpit kdmkiltvnp iwffyknkln lcdfplsyay
      301 iksfidenle vkvkkseyqs fisdylaklp ifpyvefppg ievseintvt gkrlyleeme
      361 dqlvvsfsvf yndieiaysy pndeylhydt ssrrvirvrr dretearlre qiletniled
      421 tpglfyasfe esldwlfdgl pklheqgfei lgeeklvrfr vnrapanfgl svssetdwfd
      481 ielsltfdgi qvtlaelkka irsnkkfvkl rdgsiarlpq kliekityml nfgkvegdsl
      541 rfanyhvtfi dqlladadqk kidvlsqekl krldqfekik eyplpeglkg tlrdyqkagy
      601 dwmnflkeyg fggiladdmg lgktiqtlal llkeikenpk kpnlvvvpts lifnwmqeiq
      661 rftpqikylv hygtrrtrdi rrlkkfplil ttyghvrrdi illkeiefny aildesqnik
      721 nplsetskav rllnarnrla ltgtpvennt mdlwaqfafi npgllgdlnf fketfmrpie
      781 keqnvqvasa lrrlifpfil rrtkedvake lppkveniif spmtddqqkl ynkwrtaykd
      841 silaeiesqg lnkskfkvle gltrlrqiac hpglvepnfh dgagkfdalm emiaeivsek
      901 hkvlifsqfv kmlhiirnkl dedgisyayl dgqtkdrqaq velfqnnenv riflislkag
      961 gtglnltaad yvihydpwwn pavemqatdr ayrigqtkkv faykliskds veekivklqe
     1021 kkrhlvdsli ateegffksl tkediidlfd
//
LOCUS       WP_457565220             660 aa            linear   BCT 27-JAN-2026
DEFINITION  bi-domain-containing oxidoreductase, partial [Caldithrix abyssi].
ACCESSION   WP_457565220
VERSION     WP_457565220.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11579189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..660
                     /product="bi-domain-containing oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
     Region          15..305
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(23,25..26,29,92,96,116..121,139..140,144,166,
                     183..184,186,208..209,231..233)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
     Region          331..641
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 qqpdrvkqvl dkikteglis taqavwnkln epthlgysnv gvivdkgqlv dqfevgqrvv
       61 sngphaemvr vpwtlaaaip dsvsdeaasf tvagsicleg vrlanptige tvvvvglgll
      121 gqltaqilqa ngchvlafdv ikekvefakt fgieaaqsks ipenieyvlg ktnglgadav
      181 iitastased vlsqcalmsr krgrivligv ipitvprnlf yekeltfqvs saygpgrydp
      241 qyeggndypl pyvrwtakrn meaflflleq kkihvdrlit hrfpfeqavk ayetiekenp
      301 igiileyqgq vkrdsmvhfr plsdkakqkv dklsigfigv gnfaksmllp hlkklgaplq
      361 mvassdglsa svaakkfgip katsdrnlvl qdpeintvfi strhdsharl viqalqnnkh
      421 vfvekplavt leqlkevyqa akqypeqhlm vgfnrrfspf sqklkralee rgnpisiiit
      481 vnagyipqeh wvhdpvmggg riigegchfi dlarffvgas iktvqalsth ghsetdedkt
      541 millsfedgs qacihylang harfpkerve vfssqrvfqi dnfkslvsyg spvketglkq
      601 dkghfqeikr flesveksgq plipaeelfe vhlatllveq akieqkamsl saywkeldsn
//
LOCUS       WP_457565227             782 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Caldithrix abyssi].
ACCESSION   WP_457565227
VERSION     WP_457565227.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..782
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=88189
     Region          1..397
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(98..100,124,174,205,234,236..237,245)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(101,134,198,243..245,274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            237
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mlserikhig vsptmkiaak aiamraqgid vvdfsvgepd fptpqfikda gkqaidqnit
       61 kytmnagtme lrkaiaeyly kehgveydpa kqilvsngak qaifnvimal isdgdevivp
      121 apywvsypem vrlaggrpvi vetheengfr ltpeqlkqni sastrafilc npsnptgaay
      181 sqddlmelak vleeeeifii adeiysrlvy dnfrftsfas isaklkerti lingfskafs
      241 mtgwrigyla gpkeiveaan kiqshstsna nsisqfaalq alkgpsyevg rmvaefqrrr
      301 nyvvqrlrai pdisvtepqg afyvfpnisa yfgkehkghy irnsyglayy llreanvvvv
      361 pgaafgsdqh irisysasme qiekgmkrma ealrrlktpt kikfvqlnny rtkvrkkapl
      421 eskinyeqre aliaeaeahl kfnqyfewna ningliiqlr tnsahlndfw ienwypaqle
      481 sdlephgviy avdgvvgrep hafyhsesst gllfnsdyyg alrslaltlv adlgerlfdl
      541 htvrgfsgdf qgrgfvligp rgtqktplfy qllqdenmal hsndllfvrf gggfaaadva
      601 erkfylptqh aeyfpaleal fekckcenvi tnrvdceyqn cvnaeqcsmd rgapycfmas
      661 ktstamldpy wiggmerhvk ridlqflfll tndplaeplk eldaehalql lrrgsssgaa
      721 mpgqgkdqpf ynpyllphde lrlkqhqerf lrllqfvkvv qlntanqtpa rlaerlkemi
      781 tg
//
LOCUS       WP_457565225             996 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator, partial
            [Caldithrix abyssi].
ACCESSION   WP_457565225
VERSION     WP_457565225.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 996)
  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   3  (residues 1 to 996)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   4  (residues 1 to 996)
  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   5  (residues 1 to 996)
  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   6  (residues 1 to 996)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   7  (residues 1 to 996)
  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   8  (residues 1 to 996)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   9  (residues 1 to 996)
  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   10 (residues 1 to 996)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   11 (residues 1 to 996)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   12 (residues 1 to 996)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   13 (residues 1 to 996)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   14 (residues 1 to 996)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20662018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..996
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          74..221
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          233..483
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          482..853
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          866..988
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 qdfgipvvqn rafhlqagdr mielrsrpiv wqkqqayfvs mydmterlks eqryqalnrv
       61 yrmllranea llqahdensl lkdickivve dggyhfawvg fadndrhktv rpmahfgqee
      121 gylkdikvsw gknkfgqgpt grairsgqav tvqnwskdpi vapwrkngks fnfkasialp
      181 lkngdetfga lniyskeqis fepletelll klagnlsygi qnlrlkkake kneqalaesy
      241 trfrnlfnsv pvalyifsmd eklfeansff lkmtgfekve dlkafafkhg gmsveadkvl
      301 kvletedaih eletqwrtnn gnliwvkesi rvvrdhqgki lyyegmaedi tarkaaeqal
      361 kaseqkyrri vdlaqegiwm ldararttfv nqkmadmlgy eaqemigrny fdfivkdnkk
      421 eavaqwhkql qgkniqhelc flkkdgtkmw glvssrpile edfqgalkmv vditekklin
      481 qqleetnrql msllesssav iysarwqngm vaplqitanl knifgyepqe linnpvlwin
      541 nihpedkeqv ikaitkinqp gkysfeyrvk dragnylwvy demripadwr egtftihglw
      601 iditekkkle gqflraqcme slgalaggia hdlnniltpi llatevlrmr dkkpanekvm
      661 hmiessaqrg keliqqilsf argvegehkp vqvrhiiaev griiketfpk sinfkmsvak
      721 dlwpvladat qinqvlmnlc vnardampeg gkleiraenv vfdehyslmh qtaqpgdyik
      781 isvidsgqgi peklinkifd pffstkevgk gtglglstvh tiiqqhngfi nvysepgngt
      841 tfnvylpank saeveesrei aedlkgegqt ilviddeaai reiisntlkd sgyrvltasd
      901 gaqgvaifaq qknkidlvlt dismpymdgh sairsilkik pdvdiiamsg lehdvkvdin
      961 rpikmlnkpf tsqkllktmk evlavstktk ekqtan
//
LOCUS       WP_457565235             176 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Caldithrix abyssi].
ACCESSION   WP_457565235
VERSION     WP_457565235.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..176
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20285
     Region          81..175
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnllkhssvv vlllailasc aifseqrplk skkvirdgre mlygkisleq lfydypdwkt
       61 eyasyvpqke iiaklkqiep rgrvliflgt wcpdserevp rffkildaag lssklpvemw
      121 avdrkkslpn elpqkyhiey vptfifeinn reigriiesp ealyleedvl nilsgk
//
LOCUS       WP_457565240             253 aa            linear   BCT 27-JAN-2026
DEFINITION  RtcB family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565240
VERSION     WP_457565240.1
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 10004203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>253
                     /product="RtcB family protein"
                     /EC_number="6.5.1.8"
                     /GO_function="GO:0008452 - RNA ligase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
     Region          8..>253
                     /region_name="RtcB"
                     /note="RNA-splicing ligase RtcB, repairs tRNA damage
                     [Translation, ribosomal structure and biogenesis];
                     COG1690"
                     /db_xref="CDD:441296"
ORIGIN      
        1 mknpkipikk idenlyeiep fgdmrvagrv yaspemmegl leeqaplqqv invahlpgie
       61 kyslampdih wgygfpiggv aatdwqegvi spggvgydin cgmrlattsl redevkkrld
      121 kliqelfkai ptgvgsshai kklskndlkk vaqegvqwvi qqgygkaedl evieekgrmp
      181 fadfsavsqr aiergldqlg tlgsgnhfle vdvvdriyde qaaaalglfe gqivvlihsg
      241 srgfgyqicd dyl
//
LOCUS       WP_457565242             804 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase [Caldithrix abyssi].
ACCESSION   WP_457565242
VERSION     WP_457565242.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..804
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93239
     Region          200..801
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mairienndi ylavrdlvhy ppdqplissf plpqrgvlgq kahrrvqesk qkhfglfhre
       61 ftvnrayayr dftfhiqgri dgvyqlsdrm eieeiksvil rpaefkrlqi eryphfseql
      121 lfyayllqds fdglevqtfl ilvnlinnqq rsfpivynrm qvermlqarf eeivqrilde
      181 rqklaerqal irkiqfdlpe erpqqqmmmd evrqalesga hlmasaptgt gktaaalypa
      241 irhaylnnkk iffitskttq qriavetvlp liaqglplka mvitasekmc lndvffchqs
      301 fcpyikdynq rllssnllpn llandfidpa aissaaagaq lcpfevsmdl lahvdliigd
      361 ynyvfdpaaq lrrlfmskdf sdwiliidea hnlyergmny lspqierrkl aeliaftaqq
      421 rarvyrdlts glkefksmld qlqregelny ehqqyfltql dlkqldeafk qfeaafiryl
      481 iykirakkli vddpleaify qlrrfvrvah iedrafvaff namndgvlhi qccdpshylg
      541 eiidrfhgvi amsatldpme fyrnllgfsa vrtrflqlds pfplenrkli ivpgistryk
      601 drlrnapkia eiirntisvk pgnylvffps feflqlvnvf lnqipgekii qkpgmkaker
      661 dealdklrag haphllmavm ggifsegvdf sgnmaigviv igpalpqvsf erellrqyye
      721 etyhmgeeya yiypgmnkvi qavgrlirsa tdkgvvllig drfaderfnl llpdywfrke
      781 ddveitsdyl kalknfwqkm drad
//
LOCUS       WP_457565188             161 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565188
VERSION     WP_457565188.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Rocha,S.T., Shah,D.D. and Shrivastava,A.
  TITLE     Ecological, beneficial, and pathogenic functions of the Type 9
            Secretion System
  JOURNAL   Microb Biotechnol 17 (6), e14516 (2024)
   PUBMED   38924452
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Gorasia,D.G., Veith,P.D. and Reynolds,E.C.
  TITLE     The Type IX Secretion System: Advances in Structure, Function and
            Organisation
  JOURNAL   Microorganisms 8 (8) (2020)
   PUBMED   32752268
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Lasica,A.M., Ksiazek,M., Madej,M. and Potempa,J.
  TITLE     The Type IX Secretion System (T9SS): Highlights and Recent Insights
            into Its Structure and Function
  JOURNAL   Front Cell Infect Microbiol 7, 215 (2017)
   PUBMED   28603700
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16073716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..161
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
     Region          83..159
                     /region_name="Por_Secre_tail"
                     /note="Secretion system C-terminal sorting domain;
                     pfam18962"
                     /db_xref="CDD:436869"
ORIGIN      
        1 knmvvwqdti nwagwkmlmv pldsiggsgd ynfhsvvvkq lnrgytegal ylddaqydmi
       61 italedenpa nllpaklalh qnypnpfnpl ttivyqipes gevqlalynv lgqkiadvvk
      121 arqqpgtyki tiradnlasg vylyrlkfkd qvrvkklivl k
//
LOCUS       WP_457565253             195 aa            linear   BCT 27-JAN-2026
DEFINITION  3-phosphoshikimate 1-carboxyvinyltransferase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565253
VERSION     WP_457565253.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Marques,M.R., Pereira,J.H., Oliveira,J.S., Basso,L.A., de
            Azevedo,W.F. Jr., Santos,D.S. and Palma,M.S.
  TITLE     The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a
            model for development of novel antimicrobials
  JOURNAL   Curr Drug Targets 8 (3), 445-457 (2007)
   PUBMED   17348837
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Stallings,W.C., Abdel-Meguid,S.S., Lim,L.W., Shieh,H.S.,
            Dayringer,H.E., Leimgruber,N.K., Stegeman,R.A., Anderson,K.S.,
            Sikorski,J.A., Padgette,S.R. and Kishore,G.M.
  TITLE     Structure and topological symmetry of the glyphosate target
            5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein
            fold
  JOURNAL   Proc Natl Acad Sci U S A 88 (11), 5046-5050 (1991)
   PUBMED   11607190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..195
                     /product="3-phosphoshikimate 1-carboxyvinyltransferase"
                     /EC_number="2.5.1.19"
                     /GO_function="GO:0003866 - 3-phosphoshikimate
                     1-carboxyvinyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009423 - chorismate biosynthetic process
                     [Evidence IEA]"
     Region          <1..192
                     /region_name="AroA"
                     /note="5-enolpyruvylshikimate-3-phosphate synthase [Amino
                     acid transport and metabolism]; COG0128"
                     /db_xref="CDD:439898"
ORIGIN      
        1 fssaaffitg alllpgselm iknvslnptr tgflevlkqm gaqleiyltq qepepageiv
       61 irpqklqnie ipeelipnii deipilsiva arsegtlvlr haselrfkes drikaivqnl
      121 rqigveveef edgfqicgpq sfkggkittf gdhriamsfa iadllsdepi epddpdcaav
      181 sfpdfydilk svvqa
//
LOCUS       WP_457565254             296 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase, partial [Caldithrix abyssi].
ACCESSION   WP_457565254
VERSION     WP_457565254.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10870074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>296
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          7..215
                     /region_name="ST1585-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Sulfolobus
                     tokodaii ST1585 protein; MBL-fold metallo hydrolase
                     domain; cd07726"
                     /db_xref="CDD:293812"
     Site            order(68,70,72..73,152..153,169,215)
                     /site_type="active"
                     /db_xref="CDD:293812"
ORIGIN      
        1 mkeilkglal inldqpvegf rdfiscwllq knglnilidp gpastilhlt salnkagvek
       61 idlillthih idhaggtgll lkkfpearvv chpkaikhli npeklwagsl qvlgslaevy
      121 gpvapvpqan lgfahlieqn gltieavetp ghashhlvyk iddllflgev agvnvplqgs
      181 sylriatppv fkyeiyrasl qkaaqlkaqh fcfghyghrt dgeqiftqal nqlelwlsvi
      241 qkniekdvle edvileqllq kdaqlqsfhl lpadiqtrer yfcknsikgm mgylle
//
LOCUS       WP_457565255             291 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caldithrix abyssi].
ACCESSION   WP_457565255
VERSION     WP_457565255.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..291
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32255
     Region          3..275
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtrlkedlgl lsvtvfwgtt fivsklllse mslavymfyr mavaalamtl ialkfkkawn
       61 kqvlrhglil gvllyasyff qmwgitqtsa snagfitgls vvlvpvlgfl fykeetplqv
      121 wgsvilavtg llllsganpf kwsvgdlkvl icaiifafhi iytgrfsrvn nvylltavql
      181 vaiaafsfla flpevqtlst islknvilli ylalfgtvft flmqtsmqrf ttvartaiif
      241 smepvfaalf afliageklt aegwlgglfi vlamvnaefp yqslrrqkqk s
//
LOCUS       WP_457565257             423 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457565257
VERSION     WP_457565257.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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   2  (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   3  (residues 1 to 423)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..423
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47134
     Region          26..423
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mrwknwlenn ilenkvllrf frideellri glqgivehkl rsfltmlgii fgvaaviaml
       61 aigegarrqt lsqiralgln niiiqssdgd gkpgekgnil fsdaealqqi lstidalapv
      121 iryeteayyk trskpvkltg tnarffklmn lkveqgglfn ewddehfqkv cvlgaevard
      181 lflaenplgk lvkldklwfr vigvlahqpv stvgasevnf nrqifaplqt lyvrfdrpar
      241 dsqlqqlvlh vpdenkivat aritesvltr rhqnqkdfkm ivpeqllrqs aetqrlfniv
      301 mgtiagisll vggigimnim lasvlertre igirrslgat rkdilsqfll eavllsligg
      361 lagiftgyvl sygitllsdw etyvswwsva lavgvsagvg iafgffpark aaelnpieal
      421 rye
//
LOCUS       WP_457565258             427 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caldithrix
            abyssi].
ACCESSION   WP_457565258
VERSION     WP_457565258.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..427
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48432
     Region          38..394
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mskswfksrr fritltaivv llivflflpe kdqallftvk rgdlliripv dgelqavesf
       61 ivkapsnvwg nirivklape gsivkkgdfl iqfdtseqmq rlqeaqnkle talanlastk
      121 adiqnemael endikmetys leqarlqakn aiyeaenkrr eielnlkkae lryaqllrkk
      181 eslqkihqar lrqaeleveq arlevkqrqe dlkrltiysp adglvvykkv wesggmtklk
      241 vgytpwrsqa lieipshskm kvmasinene isrvkkgqqv evrldaikdt lfsgtvtdia
      301 tlarqddeke knvfdieili neadprlkpg mtahcnilvq kienvlqvpi davqikegks
      361 fvldedgnpi aiktgqsndd fvviteglke gdriqlrasa sdtpaqnkvk pkkkkpksvs
      421 rrviilr
//
LOCUS       WP_457565265             807 aa            linear   BCT 27-JAN-2026
DEFINITION  Lon protease family protein [Caldithrix abyssi].
ACCESSION   WP_457565265
VERSION     WP_457565265.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     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=91911
     Region          72..793
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mlkkcllsad qlkkdvslak ikfnttkdip pldtvigqer avssinfalq mdksgynlfv
       61 sgrygsgrtt ivmdlvkrfa rqgpppqdci iiynfeapde pyailmppge grrfknrfqk
      121 lirnlrrdll ksleskqydd ergkviekyq kkkqellqtl eveahaldiq iqpsnmgflt
      181 iptkngkpln qeefqllphe erekitnnla yvqkriqevv kninildrdl hdeledltqk
      241 tarfvvnnhf ahllekyhdf peiknylhqa aediikdvan flgksesesp lplqqgpqid
      301 kyqvnivvdn tkhngspvvy etnptytnlf griekkayqg fvytdytmik pgsllnangg
      361 ylvidaeqll khpfayeslk rslrsgelri edfpeligla tttslrprpi plkvkvilig
      421 qaylyrllhs ydeefgkifk vradfdvevk etpttvkqyv qfisrvvhee klrhfdrsgv
      481 eaiieyayrl adhkkrlsir faelvriire ssfwaaqkrh klvsrqdvem aidnliyrhn
      541 lieekiheai rertinidvt gfkvgeingl avydvgdhvf grpnritint yigsrgiini
      601 ereaklsgki hdkgvlilag ffyekfgndm plsfsasitf eqsysgidgd sassaelyal
      661 isalsgvpin qgiavtgsvn qkgevqaigg vnekiegffk vcqsrglngq qgviipqanv
      721 knlllkdevv eavragkfhi wavdniedgl yiltgqkcgl rhkdgsytqn sifekvrqrl
      781 vefarqtqaf rqqisemskk dqddsee
//
LOCUS       WP_457565262             114 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Caldithrix abyssi].
ACCESSION   WP_457565262
VERSION     WP_457565262.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 114)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..114
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13164
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrelvkifka lsdqnrlril kmlevrplcv ceitavlqla tstvskhlsi lreaklitde
       61 kqgkwvnyrl nrqgnisyvn ellpllsqwl pddptilkdr dkvktihrqt icqv
//
LOCUS       WP_457565275             369 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Caldithrix abyssi].
ACCESSION   WP_457565275
VERSION     WP_457565275.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..369
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42355
     Region          101..362
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mayirtlptg kyrveirrnq ktiqnktfad rshaeqwaad feekidrils ikpkklkrls
       61 pakveelggi alfqklgvev sfmtfhslan eyigqwagkd enmirraefw lnvfgdkpik
      121 siksshieki lnqyatgkvn gygrdkpksn ntllrmksvl sgifiyavek kyldknptqk
      181 vrikaqqnqi erflsdderg rlleackrss wdkmyllill aittgmrkse lsnlrwsdid
      241 fdrglatlad tkngsprinp ipafvleemk pirqigngli ffspnnpdkp fdfrkqwniv
      301 rkranlenfr fhdlrhtaas ylvmagatlh eagqilghks eqttkryahl stdhkaalae
      361 rvmskvflg
//
LOCUS       WP_457565283             438 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565283
VERSION     WP_457565283.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..438
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50463
     Region          3..341
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mvkkivgiiv gilvilmamg cgrrdsaqqq rsiekkelty wcatnpqevk larelvdewn
       61 rihkdvpvkl qtlpasqsse eallaaiagn ttpdicsnmw pgamdefisa gglvrldtfp
      121 dfwpyilerv sedqlktfqa rdgghyqipw ktnpimvfyn krifkkagvk apletysqfl
      181 daaekivrdf dgdgqadywm lyrdikpiww qrlfdyypfy icasggktlf kgdkidfdnd
      241 asvkvfqffr tmyqkgympv aqfqgdqfla grlaaqisgp wlvayiqkfa pegfeygimp
      301 iprpddykgp iytygdpkni sifkttkypr qawkfaqwli srhadlrlle icdqipirkn
      361 llndstfaay fkkkpqmtvf arqapftrgv dgvadlkeif naisqeyeas viygrrtare
      421 avkravkrvk virewnrq
//
LOCUS       WP_457565280             813 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 2 protein [Caldithrix abyssi].
ACCESSION   WP_457565280
VERSION     WP_457565280.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..813
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=95472
     Region          10..687
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mknrhflnkn wqvflhkerk thpafaipqk gvaatvpgti htdlfnagii phpfydmnek
       61 dlqwidwndy ryecrfdlpa gldlkqsifl vfegldtiad islngqklae tknmfrsyrf
      121 kfnallkekg nllqiifksa rvygqeyrpe ieqmsstlhp erafvrksqy afgwdwgpqf
      181 atcglwrpvy llqaecgika vtfdalaflp esvkvkseil lwgnvpkgsr leinlqieek
      241 sgrqrmyrkt lkrisnengv efevespalw wpngmgravl hklevalfdk ndqllardek
      301 kvgirqcelv tteygeaafy fkinelplfa qgvnwipaha flpeikkety rrllemaaqa
      361 nmniirvwgg giyeddyfyq lcdelgllvw qdfmfacsay pedddfvaev kaeveenvfr
      421 lrhhpsiilw ngnnenewiw hfehpglvek mpgyrlfhew ipnwlnqfdp frsywpsspw
      481 gmdadpndtn sgnrhvwdiw srwvdyteve ndqslfvtef gfqapahyqt lkkvipqdrf
      541 laqsesfewh nkqvegnerl frflaghlpv vttmadfiyl tqlnqafalr aclgywrlcq
      601 srtmgaiiwq lndcwpvtsw slidselrpk lsyyqvrrif aretvflrqs ennielhvlq
      661 phedqphevk vvgltedgka vqelffkeie qfysilplrl pkesvrshsv liatlydrag
      721 kriardilnl krwkylnlaf qdsnlrlvae nglwvecvns pcffieirhp dknfldqgft
      781 llpgerqqil aeeefesvll demeifclnr ylq
//
LOCUS       WP_457565287             487 aa            linear   BCT 27-JAN-2026
DEFINITION  SLC13 family permease [Caldithrix abyssi].
ACCESSION   WP_457565287
VERSION     WP_457565287.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..487
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53101
     Region          89..481
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 myslrqrigl fsgpilflll lfirpsggmn pqalkvaava llmtiwwite aipipatall
       61 plvlfpglgv lkaseasapy ahhliflfmg gfliaiamek wnlhkrvalh tirlvgfssn
      121 riilgfmiat aflsmwisnt attmmmvpig mavikqsvdf ieksddyain ttpphfkfgt
      181 almlgiayaa siggvatiig tppntilvgf ieqtyhmqir fvqwmmfgvp lavimlliaw
      241 lyltrfasvp eidrlpggke lleaelkkig kmtkaegyvl tvfgmvallw igrgfihfgp
      301 stihdatiam ggaillfmip vnwkegifvl dwqsavrlpw dvillfgggl slargfsesg
      361 laqwigeqfv vlqgmnilii ifivtffslm lteitsntat aavlipvlgs vaaamhvhpf
      421 lliipagvaa syafmlpvat ppnaivfgsr yltipqmari gvvlnligaf litllvhfal
      481 phiwnlk
//
LOCUS       WP_457565292              76 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457565292
VERSION     WP_457565292.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..76
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8700
     Region          1..65
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mknkiryyrh itnemtqqql aqkvnvarqt iiaiekgsfn psvklalkia hvfqikvddl
       61 feldedelpe tkedas
//
LOCUS       WP_457565296             516 aa            linear   BCT 27-JAN-2026
DEFINITION  alanine/glycine:cation symporter family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565296
VERSION     WP_457565296.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..516
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=55761
     Region          3..513
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 maeqllqfft qardfvwgvp llillvgtgi yltiilkglq irklfyslyl glikrkekgd
       61 hpgdishfqa lmtalsatvg tgniagvata itvggpgalf wmwitglfgm atkyseavla
      121 vkyrqvdeng tmsggpmyyi qnglklrwlg ilfaifaava afgignmvqs nsvaealsls
      181 fniphtytgl vlmiltvlvi vggiksigkv tgllvpvmii fyfssallil llhldqlpai
      241 fvlifksafs ghaaaggflg atvmltirqg vsrgvfsnes glgsspiaaa aaitkhpvsq
      301 alvsmtqtfi dtlvictmtg lvillsgmwt agpdltgakl tssafsdtlp avswlpqnyg
      361 glivsiglvl faystilgws yygekaleyl teigpavrkf iiyllvaitl mpfyivqhvq
      421 ngkmllssvl iliyiwvyvr irrhllepdl ktivilyraa fgtyvlvgtv aqlelvwima
      481 dvfnglmafp nligllglsg vvvkvtndyf rkkmki
//
LOCUS       WP_457565314             425 aa            linear   BCT 27-JAN-2026
DEFINITION  two-component system sensor histidine kinase NtrB [Caldithrix
            abyssi].
ACCESSION   WP_457565314
VERSION     WP_457565314.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 425)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..425
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /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_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=48413
     Region          53..419
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mskhyqqrke aasavkkfyt llnqaqqsdk gaaasgaqel evkyellrkr fedlerhynf
       61 hkavlynlss giviinndgt iiyanqsalq mldmelvslq nksikflfad pkqgekflqk
      121 lltenkqlqs eeaffktnhr kifpigltts pffdlkdrkk hgfiihfrdi saqleqrrql
      181 ermerlamlg elaagiahei rnplasiksa aqvleesfka ddfraqlatr ivkaidrsnd
      241 lltrffdftr prkpvqefhd vemlidgiyl llaprfkkkk inflknsqpn lpqvfvdpgq
      301 ieqvfmnlfl naidampkgg dlsvtislvs hdvqeaeqng dsksvcvqvq dtgtgipeen
      361 lekifnpfft tkssgiglgl sisnrlmqen ggkievqskk drgttfslyf pvpenerqds
      421 wlkef
//
LOCUS       WP_457565315             444 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Caldithrix abyssi].
ACCESSION   WP_457565315
VERSION     WP_457565315.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49136
     Region          16..436
                     /region_name="BtlA"
                     /note="MFS-type transporter involved in bile tolerance,
                     Atg22 family [General function prediction only]; COG2270"
                     /db_xref="CDD:441871"
ORIGIN      
        1 meksgdliie rpvtitvekr rlrkeifawt lydfantsys vivvtvvyai yfkeyivgdf
       61 tislggwvrn pgdflwglgg sismaivals spimgaiady snrkkrflfv ytmacvsvma
      121 llyflepgmi vaglllfiig nigfegalvf yngflpqist pqnigkisgy gfavgyvgsl
      181 isllialpya trafaandls imrptfvlaa afffvfslpf fvlvkerivn apavsgnyik
      241 agyrrtlqti krmrefpeil kfllayfiyi dgvntviyfs gifasttlgf smreviqffa
      301 ivqssaisga yvfgyltdkf gpkktimitl llwivvtiga yfthsasmfy vvgliagvam
      361 gssqsasral mgkliprgme aefygfyalm gkfssilgpf tfglvsiltg sqryaiisll
      421 fffvtglili nrvnekvtyk rfvl
//
LOCUS       WP_457565318             532 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Caldithrix abyssi].
ACCESSION   WP_457565318
VERSION     WP_457565318.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..532
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=61336
     Region          41..354
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mpkrtrflff vlivvllvvi hnnykyvlyn ylspaeqsay klertfkvid ryyvdsvdwq
       61 aatgkaisga lrtldphsiy lspeqvkral edfeghyygi giqfdiindy ptvvsvfpgs
      121 psaraglqag dqfieiegqs aykismdevp kklkgpkgtr vkvkirrpfm depfevtlir
      181 deipittvnt yfkvdsitgy vwinrfaftt seeleaalld leeagikqli ldlrdngggl
      241 lrqavsvvgk fiegnklvvy tkgrlksfne kyytedyrdg kvrdyplivl inhntasase
      301 ivagalqdyd ralivgtrsf gkglvqnefe lpdqsrirlt iakyytpsgr liqrpyknks
      361 areyftevwd dsleqelads lqnthvyyts kgrkvfgggg ihpdveivft dslhakwmmq
      421 llekrvffkt ilqwagklkr wsadfkrfek nfevsdkmla tlkqiaqden ikltpleikr
      481 eknylkqrlk aeaaryfwgm safyrmllkt drqfketmry feqakallkd gn
//
LOCUS       WP_457565319             302 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein [Caldithrix abyssi].
ACCESSION   WP_457565319
VERSION     WP_457565319.1
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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..302
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33586
     Region          4..298
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mmekrtflfi lnpisglkkn kksieqiihk efqahstidy qiqytqfpgh arqlareaaa
       61 qnvsvvvavg gdgtmnevas slvgtetvlg iiprgsgngy arslkiplkv kqairvlqyg
      121 qvkqvdvgki nefyffgvag vgfdayigaq fqafglrgpl pyfyigvrey frysyegftl
      181 kfngqslhvn pllitvantp qygmnatiap qakvddgile lcvlnpmsvf kaamelhhlf
      241 dgtiekvkay rhfsvkevei ereyekgvfh tdgeprmgpk vlkisllpqk ikvlvpgekl
      301 kl
//
LOCUS       WP_457565325            1021 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457565325
VERSION     WP_457565325.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1021
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112454
     Region          1..1017
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkltevsvkr pvatflltlt vvvlglfsip kipvsfwpef vapvvvvlvp ypgvgpeeie
       61 eqiakpleee lstlddldel etvcqngmlr imvrfdwgvd fdqakldvqd ktnkarskfp
      121 realepkilq vqdfilpgiq lgfysekrsl devrefvdkk iknqilrlpd vatatlfggf
      181 drnveirvdp qklnfyelsl pqvaaaiare nrdvtagkik sdfneqivkl sgkftdldqi
      241 kklivankfg rpvylqdiaq vkftrkerlv vsrlngkeiv glsvreksgg ntvamvkqvr
      301 rlmeelkpvf padinvkvie dqsifinnav rnvvrnalig svlaaivifl flgslrntli
      361 ialsiplsvi atfllikwfg lsiniislgg lalgvgmivd ssvvvlenif rhlqkngrqn
      421 rlqtvvnatq evgmaitsst ltsivvflpl aflvglaavl lgelaltvvf altlaiival
      481 tvvpllsyrl mrvdqkmsgv rklsawwqka iekltqsyrk giafslrhrv ftlllagiil
      541 aaslavifpr ldvvllpvin qgqfevqmel pvgtklekti evttkiekki lqmpevektf
      601 tvigqavrig etksnsakit vdvksrfleq idrvmneirs ycqtipalkt kvkqidatag
      661 mqtqpinvri ngdnlqtlkt lgdsaltrik ripgvvnits slqegvpeyr ltidrlkate
      721 lgisfteaan alrsavlgnp isrfsaygqe ydivlklqes alqdintvlq lplvtrdgrv
      781 iplgrlvkve tdrgpgeikh fdqqrvvqil adiqgrsrre vnaevhkila elplpagyfi
      841 tyggmsrgik dsfislgnal liaiflvyvv mgsqfnsfih pftialsipl aivgvlaglw
      901 vfnasistna flgsimlvgi vvnngillld yigqlrargl tkneaiiegg atrlrpilit
      961 slttifgmlp ialglgegge alkplgavvv gglststflt lfiipvvysl ldrfkkkqel
     1021 n
//
LOCUS       WP_457565309             247 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565309
VERSION     WP_457565309.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..247
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
     Region          148..237
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 vpfeawdvgr gtyddatddi rcltggysgg atpgvfdfay qdpafgfpat dwidirkpin
       61 eqgsypvfaq diesgvfsys wwdnsveils giiicdygga atlpptntvi rfittkgpde
      121 nltftfnapg kiendpelmk kdvekinvfp npyyaassme pdrfthfvtf nhlpphaiir
      181 iftlngalvr kleklddsqf frwdlknekg wrvasglyiv hidmpelgkq kvlklmvitg
      241 eevldyy
//
LOCUS       WP_457565329             738 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin-containing oxidoreductase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565329
VERSION     WP_457565329.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Hille,R.
  TITLE     Molybdenum and tungsten in biology
  JOURNAL   Trends Biochem Sci 27 (7), 360-367 (2002)
   PUBMED   12114025
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Hille,R.
  TITLE     The Mononuclear Molybdenum Enzymes
  JOURNAL   Chem Rev 96 (7), 2757-2816 (1996)
   PUBMED   11848841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..738
                     /product="molybdopterin-containing oxidoreductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=83173
     Region          5..738
                     /region_name="BisC"
                     /note="Anaerobic selenocysteine-containing dehydrogenase
                     [Energy production and conversion]; COG0243"
                     /db_xref="CDD:440013"
ORIGIN      
        1 mktkmkrref ikiagagags lvvgsklyas fnskdeqnll adgkiertpt ycemcfwkca
       61 gwvykkdgkp wkiignpddp nsrgrfcprg tggigaytdp drlkkpllrv ekngkqvfke
      121 vswdealdfi agrmkdiaqk hgpecialfs hgsggsyfkt llhafgsnnv aapsyaqcrg
      181 preeaymltf geavgspert diinakclvl lgshigenmh ngqvqefsea vahgatvitv
      241 dprfstaask skywlpikpg tdlalllawi hviiyeelyd keyvkkytfg feqlkeavkd
      301 ktpewaypit tikphvirqt aremaknapa tivhpgrhvt wygddtqrvr agailnallg
      361 swgrrggfyf pskahlpkmp tpkfpkvkrd wrkafpnkyp vahlalssgi cdatipsper
      421 ecsfkgwivy gtnlpmtlpq pektleaiqh lellvaidil paeitgwadv vlpectyler
      481 ydnlrlspgr vpsialrapa fepkyeskpa ywmarelakr lgledyfpae tieeyldyql
      541 kaigssleem kkigvkflpe eaqklyledg edfefptptg kielystild eygfdpipqy
      601 taheeppegy yrllygrapm htfgrttnnp nlhdlmeent vwinskvakq wgikngeyit
      661 lenqdgvrst pvkakvteri rhdavfmvhg fghsdkrlrr aygkgaddqr litrvkidpl
      721 mggtgmrvnf vtfrkeea
//
LOCUS       WP_457565337             317 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565337
VERSION     WP_457565337.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>317
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          212..>315
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
ORIGIN      
        1 marakqpckn hpdrltarrc yhchapvcse cisklerhyf cgrwcfvkwk agqfflrvkk
       61 ipnlqiylla slilltnlfl ffyfnhklds lkkitrqqpp tsksvtqrds awfyvdstfr
      121 pidgkfglsl rvsdglsvsv wrdgklmrfa sgqggkiqiq dipllfgdnk fviwahqadg
      181 athlvdslni fyrsarlefl arpfiqgaid srmvaltfda gssdrgaqei lkilrdkglr
      241 ctmfitgrfl ekfpqvvmqm vkdghevgnh tyghphltty eqnrlhhnga hvgrefvisq
      301 llkvdslfma ltgrrla
//
LOCUS       WP_457565339             474 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Caldithrix abyssi].
ACCESSION   WP_457565339
VERSION     WP_457565339.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 474)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..474
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54212
     Region          6..471
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mmtldefqkf ahqlvdwmvd yyrniehfpv ksqvepgeil nqlpqeapek aedfstvfed
       61 fkqiilpgmt hwqspnffay fpanasypsl laemltatla aqcmiwetsp aateleervm
      121 dwlkkamglp pqwegviqdt aststlvall tarerysefs anergmapfa plrvycstet
      181 hssiekavml ggfgkenlvk vavddqlrld psalekaier dlkagkkpla vvatlgttgt
      241 taidplkpia aicaryalwl hvdaafagta lllpeyrwmi egveqvdsfv fnphkwmfth
      301 fdcsayyvkd rqallrtmsv lpeylktstr grvkeyrdwg iqlgrrfral klwfvlrsfg
      361 legirqilrn hlqwaaglee eikgqndfel maprtlnlvc fryhppavsd eqkldeinqt
      421 llqrlnasgr lflthtrvrg kytlrmvtgq tylqkkhvqq awqfikqtar emtl
//
LOCUS       WP_457565340             362 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Caldithrix abyssi].
ACCESSION   WP_457565340
VERSION     WP_457565340.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>362
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          22..>362
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mctvlkevnl taineanlta qkisrkttsv ivlfsifliv ismvaslylt rrivrpirqt
       61 tdtvkkigrg qldqkvaidn ddeigqlaae fnkmtgrlaa yekmnieqii vekrkseaii
      121 ssipaaiivt datgsiilmn dvarglfnle kndlsdkkit elinhqaitr lfspdaskqk
      181 keksglislt lnnevtffem rsifvldrhk hvqnvvillq dvtsfkkler lksefmatis
      241 helktpltsl nmtidillrr vkgplnqtql dllqgaqndi krlkafvtel leysriesgn
      301 yplnlqsiev eqliayaarp flqsfskkni tfkntirapl ktftadfqgl arvlsnllqn
      361 ai
//
LOCUS       WP_457565343             445 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-glucose dehydrogenase family protein [Caldithrix abyssi].
ACCESSION   WP_457565343
VERSION     WP_457565343.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..445
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=49860
     Region          1..438
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mriavvgtgy vglvagtcfa dvgndvicvd ndvnkiemln ngkipiyepg leemvkrnvt
       61 qerlvfttdi ksaveksqii fiavgtppke dgsadlqhvl avareigkhm ngpkiivnks
      121 tvpvgtadkv reevkkhthy dfsvvsnpef lkegaaiddf lkpdrvvvgt dneetaetmr
      181 nlyapfvrtg kpilimdvrs aeltkyaana mlatkisfin eianlcekvg advemvrkgi
      241 gtdrrigpyf ifpgtgyggs cfpkdvkaii rtareygmel kileavesvn nrqktilldk
      301 iknyfnndlk gkvlavwgls fkpntddmre apaisliral vkegakirah dpealkeaew
      361 rfedllkkke vflikkryea legadgliim tewnefrepd fylikemlkr svifdgrnly
      421 dpkrmakisi dyfpigrpss leykk
//
LOCUS       WP_457565344             756 aa            linear   BCT 27-JAN-2026
DEFINITION  GumC family protein [Caldithrix abyssi].
ACCESSION   WP_457565344
VERSION     WP_457565344.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..756
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=85582
     Region          15..724
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 metrvpgnfe tdtwegdeqp lhltdyiril yrgrwliils fiavfsatvl ytfttdptye
       61 asavllvesn dsmdralfnl ttfgtqtnll nnqieilksr niaervvkrl eksayrdsis
      121 ffkkledgsd ltfnqrvaiv mssleveprr dtdiitltyq agspfeaafl anviseefak
      181 lnaetnrmev semrkfiedr laikakelke seealkkfqe rekiasldae tqelvtrlse
      241 tesfleqari elnsklqlkk nleeklnerk etlpanlsei stpyiqtlqq elarvvaert
      301 syvtaletqv qskrefftpe lvryderika lkkkireeaa kiansemisd plrisqdlvn
      361 qlinlsgeit ateakiaale dvlkvynqrl enlpdkvlql vrlerrkqvd eqtymmltqk
      421 leeakiqesa qarnvkiidr aikpnrpvkp nkrmnlmlga ilglglgvgi tfmieyldrs
      481 vrkpedmerm gynvlatipk ieldkveksk ikqnesakie arlithidpk spvseayrtl
      541 rtnlqfskie kdlktilvts agpkegkstt aanlsialaq agnrvvivdg dlrrpilhsv
      601 fgttkeeglt nhlagsisye qvfketvven lslvtsgvlp pnpsellask kmedflnklc
      661 edfdivvlds ppviavtdas ilstkvdgtl lvvyagqter daikraanml nsvsarllgi
      721 vlngfdvqgi ygsyyyyyyh hyyggegksk pkrkfi
//
LOCUS       WP_457565350             300 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Caldithrix abyssi].
ACCESSION   WP_457565350
VERSION     WP_457565350.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..300
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33821
     Region          3..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          152..294
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mdikrilvpt dfsetaraal dqalflaary naeltvlhar llfeddpael ehklkdlkae
       61 ekevehalld klrkktadhs hlnikheiir gysapsailg yinnkefdlv vigthgrsgl
      121 ehfligsvae kvvryarcpv ltvrsaeyik ekfenilvpl dfsepamhal ktaanwveee
      181 ggelhllyav eqevhpalya wgmksvfdmi pdikekvekr meeaiaqipk lkkvavkkvi
      241 regkphkvia kyveeekphl ivigthgmvg ldrfllgstt erviravkip vltvknknvi
//
LOCUS       WP_457565355             449 aa            linear   BCT 27-JAN-2026
DEFINITION  PhoH family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565355
VERSION     WP_457565355.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 449)
  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 449)
  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
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Clissold,P.M. and Ponting,C.P.
  TITLE     PIN domains in nonsense-mediated mRNA decay and RNAi
  JOURNAL   Curr Biol 10 (24), R888-R890 (2000)
   PUBMED   11137022
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Kim,S.K., Makino,K., Amemura,M., Shinagawa,H. and Nakata,A.
  TITLE     Molecular analysis of the phoH gene, belonging to the phosphate
            regulon in Escherichia coli
  JOURNAL   J Bacteriol 175 (5), 1316-1324 (1993)
   PUBMED   8444794
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>449
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          12..449
                     /region_name="YlaK"
                     /note="Predicted ribonuclease YlaK, contains NYN-type
                     RNase and PhoH-family ATPase domains [General function
                     prediction only]; COG1875"
                     /db_xref="CDD:441479"
ORIGIN      
        1 mrldlnpksk edrrrclild tnvllhdpsa ifrfeenivl iplfvldeid skksdpqlgf
       61 nareisqkle qliqrtenwe egisipngrg gilyfvnnfm sknfpdeltl nykdnamlsq
      121 imglqerfpe rdfilvtkdr nlrikgwalh iacedylhdk iseeyldsff qpvkhlqltg
      181 eeinelfksk atenwaisyr kkwrlaeneg valfdpgeqf fgmamrkghq lkyfdyfstr
      241 ildmppkvld aenqqynfeq avcmqqamdd sikiqiiigk agtgkthiai aaalekvfke
      301 rkydsiklik pvitksrlge digflpgslk rklipkmrpf veklrlftse qsdegyrkll
      361 dsgviellnl adirgadlan sfvifdeaqn anpfqmrtlg trlgedtkli vlgdptqids
      421 vyldkysnal inlyenalqn papfiahic
//
LOCUS       WP_457565360             124 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Caldithrix abyssi].
ACCESSION   WP_457565360
VERSION     WP_457565360.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..124
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14274
     Region          34..117
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mssrsdyvcs vevvdqqkvt hvnqvlpekm vtrqmaeffk slsdptrlri vqalleeelc
       61 vcdisaivdi sisaishqlr llrsmhivkf rkqgkmvyys ledehisrml eialehlnek
      121 aner
//
LOCUS       WP_457565362             445 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caldithrix abyssi].
ACCESSION   WP_457565362
VERSION     WP_457565362.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..445
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49122
     Region          58..439
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkivialita fvivigcagp vlqvkqvepr pvieevtsag sslkgelspe gtitvlkalq
       61 lalqsnpqlt vfsleirare aaalqesflp npelaveven fagggalagf kasettislg
      121 qlielagkra rrtqaaalqa elagwdfesk rlevyaqvvk nfydvlaiqk lvklnkeilt
      181 lteefkdqis lrvtsgrtsp aelsraevev anarialeqs qrrlqaarqr laatwgatta
      241 afdsvtgnfe nvsalpafea lqnalqknpe wlrwdtetrl kqaqlalaka lripdptita
      301 gyrrfndlgq qafvagfsip lnifnrnqgg ikeaalrakq tafqetfsrl qlqtelstmy
      361 qnisavqqsi falkneiipk arqafetisr gyqlgkfnfl evldarrslf sarqaylqnl
      421 adyhqlraei erltgksles fkier
//
LOCUS       WP_457565367             280 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565367
VERSION     WP_457565367.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..280
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30947
     Region          13..269
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mayvkpnpet dyafilgvss gfgeatalal aregfniigv hmdrgealnh veelkrlike
       61 ngveaiffnk naaseknrkq videikthfg qsenkkqikv mlhslafgsl apyihhdlde
      121 rltqkqlemt invmanslvy wtqdlveehl lgqgskifam tssgslrvip yygavsaaks
      181 aleshvrqla lelapykmtv nairagvtft palrkipghe tmidlalsqi pfkrltqpsd
      241 iakfilalat sdelwatgnv fnvdggevit ayhstfhhkr
//
LOCUS       WP_457565369             244 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caldithrix abyssi].
ACCESSION   WP_457565369
VERSION     WP_457565369.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..244
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27134
     Region          4..233
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 meaiiflfav lvifvayfvk gftgfgpali liptlsyfya ppqviflsal ldvfggiyll
       61 akvyrlinwk fvlpilalff pgayigakll nafdvallkt llglamiffi gliwfntlas
      121 shkfkiktsh kislplafla giggglfgis gpllviyfkl afkkasfraq liaifafgaa
      181 wrlllyhslg tevsfnmwql fifitvmfla vvtgnrwqlr inpikfdrfv aavllipslt
      241 lllf
//
LOCUS       WP_457565371             303 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457565371
VERSION     WP_457565371.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..303
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36991
     Region          108..>206
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
ORIGIN      
        1 mttifdlfdn ileeaerefy rhrfeqalek wqsyyqitak veynliikei kklvkeinpa
       61 kikslsdlhr cfrllrqryl ekqihpytyr iftklltdly ekefkthaee ddlathaifl
      121 ylegdlekak rllerylkkd tenmearvfe ghiylkqgeq kkaiavltkn lflaadqlye
      181 ddlylsqfkm lygrlhseyg rkdvalwlla feawfrnylv feqdegfyki mlrkeqneri
      241 irvkytlaek yrhfvrclyi seysrlfikt nkgmineiet ymeqldvalf tryrkkrkpl
      301 kmn
//
LOCUS       WP_457565372             332 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Caldithrix abyssi].
ACCESSION   WP_457565372
VERSION     WP_457565372.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..332
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=38084
     Region          26..329
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 msflknsglk iwwgvlplff inplfsqqvr llftgdvlla hhfeyyvkqr itypfdkipw
       61 fkeadvsvin leapftrsds amekpyvfka kpkyvevlky ggvdlvnlan nhiydygkeg
      121 lletletler aglafigagr ninqarkpai feikglklaf mgyyglrahe eshpatetep
      181 gtalrklkyi kedikqlkdr vdfitvifhw gqekknipea dqirfahrvi dygadlivgh
      241 hphvlqgvek ykkgvivysl gnfifggnsr tyeetavlqv nipvqnpenw svkmlpvavr
      301 ywqpallega rrdsvlkhlk eyseifeqtp ln
//
LOCUS       WP_457565373             304 aa            linear   BCT 27-JAN-2026
DEFINITION  patatin-like phospholipase family protein [Caldithrix abyssi].
ACCESSION   WP_457565373
VERSION     WP_457565373.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..304
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33771
     Region          19..281
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mkklkiglvl ggggarglah igvikglvrh gipihcvsga smgaivgaay alfadihkve
       61 svfkdfftge kyralkgnsv dlssveeped ffhfiaqvvk rrivinmavn rrglissdrl
      121 etaikylipn vkieemsipf actalnlvsg keyvfkkgkl htallasasi pgylapvken
      181 nfewvdgaai nnfpvevckq mgaqfnivcd vsagleeakn fknvvevfir thkaavhkln
      241 ekllekadfv lkppigdkkw tefeeidffi qqgelaveqn ikllkkelkk rsgwfynlkr
      301 kylh
//
LOCUS       WP_457565385             410 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caldithrix abyssi].
ACCESSION   WP_457565385
VERSION     WP_457565385.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 410)
  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 410)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..410
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47268
     Region          4..400
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mqkniailhy scppvvggve eiirqqaslf hryhhpvkvl agvgdyfqsg idfyfsplls
       61 sqnseikklq qkpvenqaql kaiaqkifns lkkalqrfdv liahnvlsmp ynlpltnalh
      121 qlanekvisv vnwnhdspff ynnypqeldl epfrilktyn pnihyvtise sravefrely
      181 qlaenditvi pngidpirff rldpqtvrli qeqelfmadl imvqpsrlhp rknielsiev
      241 lhalrqkgln akllvtgayd pherktvryh qklirlaerl nvlnslvmva dyqfngggkl
      301 pasrvtmhdl ylisdvlfmp skiegfgipl leagmiklpi vcsdippfrs iapneaiyfd
      361 lkeepqqiae kiqavvqnnr tarwfrkvmk dyvwdniyek dlkpflekit
//
LOCUS       WP_457565387             354 aa            linear   BCT 27-JAN-2026
DEFINITION  mevalonate kinase family protein [Caldithrix abyssi].
ACCESSION   WP_457565387
VERSION     WP_457565387.1
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 11446334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..354
                     /product="mevalonate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38720
     Region          6..318
                     /region_name="ERG12"
                     /note="Mevalonate kinase [Lipid transport and metabolism];
                     COG1577"
                     /db_xref="CDD:441185"
ORIGIN      
        1 mirvtapgkm illgeyavle dapalvcavd vrasvqigrl agnefvfsap slnlhelpfv
       61 ilpnahvrfd palgqealrk ltlfagimey vysrlpdplk nqglriaint dafyaeqfhs
      121 kmgfgssaaf caalvkglvv iskldmteaq ifrlalsahh haqgkmgsgi dvaasyfggy
      181 lhyeriyend pvnklpqpvs pcaglyfrpv ftgksasttk lvggvkqlke krpevydpim
      241 erlkalsvqg lrafeqrqve lflekvrefy itlknlgdqs gmpiisgvhq kladlahrag
      301 vvykpsgags gdiglifsdd rqrfseaiti iknsgyfpld vdvategvrl eksf
//
LOCUS       WP_457565394             189 aa            linear   BCT 27-JAN-2026
DEFINITION  D-sedoheptulose-7-phosphate isomerase [Caldithrix abyssi].
ACCESSION   WP_457565394
VERSION     WP_457565394.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Harmer,N.J.
  TITLE     The structure of sedoheptulose-7-phosphate isomerase from
            Burkholderia pseudomallei reveals a zinc binding site at the heart
            of the active site
  JOURNAL   J Mol Biol 400 (3), 379-392 (2010)
   PUBMED   20447408
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Seetharaman,J., Rajashankar,K.R., Solorzano,V., Kniewel,R.,
            Lima,C.D., Bonanno,J.B., Burley,S.K. and Swaminathan,S.
  TITLE     Crystal structures of two putative phosphoheptose isomerases
  JOURNAL   Proteins 63 (4), 1092-1096 (2006)
   PUBMED   16477602
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Eidels,L. and Osborn,M.J.
  TITLE     Phosphoheptose isomerase, first enzyme in the biosynthesis of
            aldoheptose in Salmonella typhimurium
  JOURNAL   J Biol Chem 249 (17), 5642-5648 (1974)
   PUBMED   4606909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..189
                     /product="D-sedoheptulose-7-phosphate isomerase"
                     /EC_number="5.3.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008968 - D-sedoheptulose 7-phosphate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:1901135 - carbohydrate derivative
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=20011
     Region          1..187
                     /region_name="GmhA"
                     /note="Phosphoheptose isomerase [Carbohydrate transport
                     and metabolism]; COG0279"
                     /db_xref="CDD:440048"
ORIGIN      
        1 mknhfeesiq vkrltfnhca ptieqavdim vksfkdgkkl llcgnggsaa daqhiaaefv
       61 irlsheldrp alpaialttd tsvltagsnd lgyelvfarq vealgqsgdv llgittsgns
      121 pniiraaema rkkgmatigf lgndggrgks lfdapivvps vsvqhiqeah itighiivel
      181 vektlfaak
//
LOCUS       WP_457565395             215 aa            linear   BCT 27-JAN-2026
DEFINITION  Mur ligase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565395
VERSION     WP_457565395.1
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 11433699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>215
                     /product="Mur ligase family protein"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008764 -
                     UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
                     [Evidence IEA]"
     Region          6..>215
                     /region_name="MurD"
                     /note="UDP-N-acetylmuramoylalanine-D-glutamate ligase
                     [Cell wall/membrane/envelope biogenesis]; COG0771"
                     /db_xref="CDD:440534"
ORIGIN      
        1 mkdlqnvkgk kvsvlgaars glaaarllkn kgahvfvsdr aparqkqdal eflmreqidh
       61 efgqhsprvf eadfcvlspg ipvasevvqe mlkrnipvvs eievaswfye grliavtgsn
      121 gktttttlig emlrrrypqa vvagnigqpf sdfadqstnd awgvvevssf qletidqfhp
      181 dqavllnyap nhldryasye eymeakwrit knlqp
//
LOCUS       WP_457565397             555 aa            linear   BCT 27-JAN-2026
DEFINITION  Rqc2 family fibronectin-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565397
VERSION     WP_457565397.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Takada,H., Crowe-McAuliffe,C., Polte,C., Sidorova,Z.Y., Murina,V.,
            Atkinson,G.C., Konevega,A.L., Ignatova,Z., Wilson,D.N. and
            Hauryliuk,V.
  TITLE     RqcH and RqcP catalyze processive poly-alanine synthesis in a
            reconstituted ribosome-associated quality control system
  JOURNAL   Nucleic Acids Res 49 (14), 8355-8369 (2021)
   PUBMED   34255840
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Lytvynenko,I., Paternoga,H., Thrun,A., Balke,A., Muller,T.A.,
            Chiang,C.H., Nagler,K., Tsaprailis,G., Anders,S., Bischofs,I.,
            Maupin-Furlow,J.A., Spahn,C.M.T. and Joazeiro,C.A.P.
  TITLE     Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated
            Quality Control
  JOURNAL   Cell 178 (1), 76-90 (2019)
   PUBMED   31155236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441769
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..555
                     /product="Rqc2 family fibronectin-binding protein"
                     /GO_component="GO:1990112 - RQC complex [Evidence IEA]"
                     /GO_function="GO:0001968 - fibronectin binding [Evidence
                     IEA]"
                     /GO_process="GO:0072344 - rescue of stalled ribosome
                     [Evidence IEA]"
                     /calculated_mol_wt=64535
     Region          89..551
                     /region_name="RqcH"
                     /note="Ribosome quality control (RQC) protein RqcH,
                     Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) and
                     RNA- (NFACT) binding domains [Translation, ribosomal
                     structure and biogenesis, Posttranslational modification,
                     protein turnover, chaperones]; COG1293"
                     /db_xref="CDD:440904"
ORIGIN      
        1 mfknyylfse llkeiqpais gqkitsafty rkdevvlelg ngqfiligia anepylllka
       61 ahnisqarya lfeklygqti rnagllnfdk hlfietesyr leaiffpphn nvfllsadrq
      121 ilkafkdkte ypaklpetqe kldlrgieas llndlivknp tlkvrgflqn hfaalnkvml
      181 neilfrtqld peqalselne eqkerlisvl lkikeeltag kaylyfdkya dlirwislir
      241 leqfqesydf keydsinhal gvfyyekrvr qefeklkalc ktalqkrlrf lnsslerlke
      301 hadlrkrkte aelkgnlllt fkndippgar evelanifse rqekikikln psksvvenaq
      361 ryfnkfknvq hnqqvlqikm dtyrremeei dqllkqleqi rtlqrlksfs drlremkliq
      421 dgsasnkkaa penlkyvfnr lildgkwevy igrdgktndl ltfhfankwd iwlhaqgvsg
      481 ahviirvpnr nqtppahvie qaariaaahs kartsstvpv iytqvryvsr irkappgtvk
      541 fqnekvlfvs pmnln
//
LOCUS       WP_457565399             248 aa            linear   BCT 27-JAN-2026
DEFINITION  uracil-DNA glycosylase, partial [Caldithrix abyssi].
ACCESSION   WP_457565399
VERSION     WP_457565399.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 248)
  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   2  (residues 1 to 248)
  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 10178243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>248
                     /product="uracil-DNA glycosylase"
                     /EC_number="3.2.2.27"
                     /GO_function="GO:0004844 - uracil DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
     Region          81..244
                     /region_name="UDG-F4_TTUDGA_SPO1dp_like"
                     /note="Uracil DNA glycosylase family 4, includes
                     Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA
                     polymerase, and similar proteins; cd10030"
                     /db_xref="CDD:381680"
     Site            order(81,84,152,168)
                     /site_type="other"
                     /note="Fe-S cluster binding site [ion binding]"
                     /db_xref="CDD:381680"
     Site            order(108..112,115,121..122,148,222)
                     /site_type="active"
                     /db_xref="CDD:381680"
     Region          108..112
                     /region_name="motif A"
                     /note="motif A [structural motif]"
                     /db_xref="CDD:381680"
ORIGIN      
        1 mnekelieni eqffrwyrqv ydselildhp varvsiaeps gpavqkgrlg hvqtqnisrr
       61 avqyrqtspe lqafyeeird cqqcelhktr knfvfgygna qaevmfvgea pgreedeqgl
      121 pfvgaagkll dkmfasigls rdnvyianvl kcrppdnrdp rpeeiarcep ylikqiqmik
      181 pklivalgrf aaqsllrleq plgvmregdh qyqnipvivt yhpaallrnp alkqkawqdl
      241 kkikrfld
//
LOCUS       WP_457565407             634 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565407
VERSION     WP_457565407.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..634
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
     Region          102..633
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 ilfipiifgc iftyryfand hknetqielk wlsdtkkdli edflkshity lnllaansdi
       61 vktfskatql nsaqknrinr iiahitnren invsfiestt gaifyqskpq ndfnksvyea
      121 sfsdsplsea vqnatqskkl svsdfrydpf anepvlfmal pvlnnrrevl gvialqipqk
      181 sidqilqrgl slkptlqvyl vdkngnvlst agsqkqglsi kisqftnfnt ctrifdfaqr
      241 dafacaspvs faafssgqfk wivvsqilyd qfsaplrnli iffiilctfl llfgaaaaya
      301 vgsrvsrsie svisdiqqit tgnlnadikv idgeheigkl tyslknfvdq lkaqlrdlle
      361 ninvisssss eisatiaqit asssetatai sqtassseev sqlatsfnek akeslkvgek
      421 aveitnqgte afnqinqgiq evkkqmdqva amvidlskqs qtigeitaav keiaeqsnil
      481 ainasieatk ageygkgfav vanevrnlad qskkstqqiq nildtiqesi sktvlqveqt
      541 nktidgsvdf vqkayhsmtn lsssieslit vlseisdfsr eqlvgtsqik eamenikeat
      601 tqnldgmhql eeviedlkkt senlksiisi yqls
//
LOCUS       WP_457565406             747 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator [Caldithrix
            abyssi].
ACCESSION   WP_457565406
VERSION     WP_457565406.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 747)
  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 747)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 747)
  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   5  (residues 1 to 747)
  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   6  (residues 1 to 747)
  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   7  (residues 1 to 747)
  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   8  (residues 1 to 747)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   9  (residues 1 to 747)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..747
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=83980
     Region          1..614
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          623..745
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mdqdferell eifkaeaedy ltilndglla leegaderav eemfrtthsl kgaaravnfs
       61 aveelcqaie slfskiknke lklnegirav lirsiehlne llnqnnfnas cdidilkqlq
      121 aaasgeikaa akekaqkrpa arpkaaqkpe asrpeaagqt pekttapepa patqpksada
      181 aqetirisyq kirelftqse dliaikikqk fyidhinqly dqleaigkkr rqwlvasdsa
      241 dalnselfre fslikkqvdl lkntlendlf qitamidkhl ddikqlmmfp fstitnyler
      301 straiaremn kkielkiygk eveldkhtle llkdplihli rnsldhgiep peerlmrgkp
      361 evgkitievl pprdqsivik vsddgrgldl akikqkslkk nlvtqaeldd mnesqvlsli
      421 fhsglstkde vsklsgrglg mavvleniek lggslkveny ypngstfylt iplsfatsrg
      481 iliytndfra iiptkfvrlp mrlevaqlkt venqlvvnln gqniplfsla slldiktedr
      541 etpqylnili lrldeqheia vsvdqvlder eiilkklnpp leevrflsgv tilgdgslvp
      601 vlnvhdifaa csdrfkpmai kkqkpkqilv vedsitsrvl lknvlesagf kvqtaingqq
      661 awqilqkqtf dliisdvqmp emdgveltrk ikaeqkmksi pvilltslgs esdrkkglea
      721 ganayfikqd fkqkslldli hkligte
//
LOCUS       WP_457565419             948 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457565419
VERSION     WP_457565419.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..948
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=109692
     Region          41..480
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          531..946
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkkyflfwai isllvmssca hlnqdrtaet aeqqnafsln tplpfdttii kgqlpnglty
       61 likqnakpek rlflrlvvkv gsvveedneq giahfcehma fngtkhfkkq elidflesig
      121 mrfgadlnay tsfdqtvyml evptdslpli rqafqivedw ahnvlydpqe idrergvvie
      181 ewrrgrgayq rvrdqflpvl fkesryakrl pigkkeilet fphevplnfy kkwyrpelma
      241 vivvgdfdpq tlkdltlehf snlqnppnap ervyypvppq nqtifslakd pelpvaqiei
      301 dykrdpdtar vvadyrkslm esmisqmlsk rlqeytsrpn ppfnyayssm mrlvqtkeif
      361 tiacaarsed ilsgyktlli esrralehgf tpselerqkk silsylkkaf nerdkqnskk
      421 lieeytrhvl ymesvpgiek efeivkqilp gislaeinql tgellqnpdr viavmgpdke
      481 gvyfptedtl ktilaavdtm kiapyvdqki akqlvdkqit pgsvvkeinh sdigviewhl
      541 sngarillkp tdfkndeilm ngfsfggysl apdsiydsar fssaiasasg lgkfnriqlr
      601 kflagkvvrl nagiskdtee fngsssvkdf esllqmvyln fvsprfdsta fqsliarqks
      661 wlknkeldpe avyndslivw ltqrhprylp vneqtlsrir lkpaadfyrq rfdnpgdftf
      721 ifvgsfkpet irplletyig gipgheerek wgsqdytppd qvvekrlykg vdpksvntii
      781 fsgpfnwsfe nvrkglfmad ileiklreri reaesgtysi gvrgkfyhip rqryellirf
      841 scdpkrveel tadvfqqids llqfgpqekd lqkvremylk dyeeglkqng fwrsrlhysl
      901 fhqipfdhvl rmddiyrsit lhdvhqmake llnkkrylra vllpekln
//
LOCUS       WP_457565356             423 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565356
VERSION     WP_457565356.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Rocha,S.T., Shah,D.D. and Shrivastava,A.
  TITLE     Ecological, beneficial, and pathogenic functions of the Type 9
            Secretion System
  JOURNAL   Microb Biotechnol 17 (6), e14516 (2024)
   PUBMED   38924452
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Gorasia,D.G., Veith,P.D. and Reynolds,E.C.
  TITLE     The Type IX Secretion System: Advances in Structure, Function and
            Organisation
  JOURNAL   Microorganisms 8 (8) (2020)
   PUBMED   32752268
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Lasica,A.M., Ksiazek,M., Madej,M. and Potempa,J.
  TITLE     The Type IX Secretion System (T9SS): Highlights and Recent Insights
            into Its Structure and Function
  JOURNAL   Front Cell Infect Microbiol 7, 215 (2017)
   PUBMED   28603700
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16073716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..423
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
     Region          344..420
                     /region_name="Por_Secre_tail"
                     /note="Secretion system C-terminal sorting domain;
                     pfam18962"
                     /db_xref="CDD:436869"
ORIGIN      
        1 ygwdvgndpv lidpnvvslp rcgismnssg fgviagpghl gwhdpdsgyy ynetkityav
       61 tydygvtwsa wdtvsfgamg iptyhnaeds llwdvtiigt dtiytpyqgp tflgtnfdms
      121 vlvdenntiy vafnclwgkp gdggwypspy ysgiwlakkt etgvwegshv aynngvyegd
      181 eqisgmsayf fdselqvsrd dqgnlymawl drrrtqvqvs rfnrysdpet ygsdatyktd
      241 iyaahsidgg vswsdqinct dspgvdeyel slspnsanqt argdygkiwy sfciadtlng
      301 dpavdayiel anevwvgeas nfnppaaigd etpvvrtysl eqnypnpfnp tttiefvplt
      361 ngratlsvfn tagqkvatlf ngnvikgeny qltfdatgla sgvyfyklqt eqgveikkmv
      421 lmk
//
LOCUS       WP_457565420             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565420
VERSION     WP_457565420.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>218
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <37..143
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mkrtlflilf ffafalaqka pfsiealyki knvsqlqisp dgkqivfvat synlhkgasn
       61 selylmnmdg sklrrltfnp asdfsprwsp dgqqilfvst rkngaqawvi sasggearrl
      121 tdfpmgvqdv kwrsadqiif vsevfpecga dpecneeieq smkngplqah madallyrhw
      181 tsykdgkrnh lilfdlkskk ytditpgdyd ypplwggf
//
LOCUS       WP_457565422             133 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase, partial [Caldithrix abyssi].
ACCESSION   WP_457565422
VERSION     WP_457565422.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>133
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
     Region          58..>120
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkkvlfflls vslilsackd rktmdeniql kkqikelklk lmqyeklaqn mqflieemeg
       61 vkarivtnyg nielklfpqk apltcfnfit haesgyydgl lfhrvikgfm iqggdpntrg
      121 gnvqsyglgg plv
//
LOCUS       WP_457565424             174 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclic nucleotide-binding domain-containing protein [Caldithrix
            abyssi].
ACCESSION   WP_457565424
VERSION     WP_457565424.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..174
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=19952
     Region          30..134
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(96..97,106..108)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
ORIGIN      
        1 mledsvwtni frkkegeked ilsvlkripl fqdlskkelr qlerilhqrt yragevvfne
       61 gdpgvgmyii eegevritlg rdqrvlavls kgdffgemal lleaprtasa iaskpsilyg
      121 ffqpdlfsil etyprtgnki llrlsqmiae rlrrsnienr elreklqsls ekgk
//
LOCUS       WP_457565427             266 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457565427
VERSION     WP_457565427.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 266)
  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 266)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..266
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31255
     Region          21..144
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpynfhddrk kyfqmqtevt ehfiipfieq awalpeggrv leigcgeagv lkafikrgwr
       61 avgvdlapek lalarqlmhd qikdgrleli neniyeerfk qkfkkqfdli ilkdviehip
      121 dqprllsylh tflreqgvif fafppwympf gghqqmcasf lkkmpyfhll pmplyrlvlk
      181 magessnkie alaankrtgi tierferilk ksgyailtkr fylfnpiyry kfgltpkeqy
      241 aliarlpyir dflttgvyyl vtrskd
//
LOCUS       WP_457565434             164 aa            linear   BCT 27-JAN-2026
DEFINITION  FmdB family zinc ribbon protein [Caldithrix abyssi].
ACCESSION   WP_457565434
VERSION     WP_457565434.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 164)
  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 10021090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..164
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18936
     Region          1..50
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpiyefychr cntiykflsr tintekipnc pkcetvkler rvstfatiss lnndsegdde
       61 fagidekrme rvleslahea ehidennprq laslmrkfak eaginfgegm eeairrmekg
      121 edpeqieeel gdaienedpf llksfrhikg qkarpkiddh lydl
//
LOCUS       WP_457565425             732 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457565425
VERSION     WP_457565425.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 732)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 732)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 732)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>732
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          1..>729
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mrlfsiiwlv ihlaladfay ssnfifprtp apspdgqqia fsfqgdiwim paaggqarri
       61 tgnpgydyap kwspdgrria fssdrygndd vfvidldggs lrrltfftnp dvvqqwspdg
      121 qnilfgsrrd fyyhrnplty qvpveggtpf evipeytqqg rlspdgqfll fvrgrvdvfr
      181 kgyrgssntd ifiydfkkqt yrqltefegn dlfplwgldg kliyfvserd gvmnlwqmnp
      241 dgsqkkqltf fkedgirype isadgawitf erlfdiyrfd vnsgraqkie lqlpvdyvqn
      301 pytyqkysge aremaisadg keiafvirge ifvinkdgrf lnqitqspwr dedidwypgr
      361 dtlafvsdra gnrniyliys ddpqqralsr atrfkmerlt asprdefspr fspdgrwlay
      421 vrgkgdlivr emesgrektv isgwstpdfs wspdgqwlay siedeefnrd vylhhlesgk
      481 rynisqhpdn dyapawskdg rrlafisrri anntdvwmvf lrkeddrktr eeweeyfsql
      541 kekkkgkkhr vqvkidepqk lfkrlrrvts lpgsetefcw spdgqfvafk tnsagksdlw
      601 kvkwdgsdlq altrdgtapf nliwqaknkr iyflkrggki asispegkda ksikfsarlr
      661 vekfqeqrqk fneawrtlne rfydpqfhga dwqalyqkyf paacnaptlr dfndivrmml
      721 gelnashlgi st
//
LOCUS       WP_457565388              74 aa            linear   BCT 27-JAN-2026
DEFINITION  non-canonical purine NTP pyrophosphatase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565388
VERSION     WP_457565388.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Davies,O., Mendes,P., Smallbone,K. and Malys,N.
  TITLE     Characterisation of multiple substrate-specific (d)ITP/(d)XTPase
            and modelling of deaminated purine nucleotide metabolism
  JOURNAL   BMB Rep 45 (4), 259-264 (2012)
   PUBMED   22531138
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Savchenko,A., Proudfoot,M., Skarina,T., Singer,A., Litvinova,O.,
            Sanishvili,R., Brown,G., Chirgadze,N. and Yakunin,A.F.
  TITLE     Molecular basis of the antimutagenic activity of the house-cleaning
            inosine triphosphate pyrophosphatase RdgB from Escherichia coli
  JOURNAL   J Mol Biol 374 (4), 1091-1103 (2007)
   PUBMED   17976651
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burgis,N.E. and Cunningham,R.P.
  TITLE     Substrate specificity of RdgB protein, a deoxyribonucleoside
            triphosphate pyrophosphohydrolase
  JOURNAL   J Biol Chem 282 (6), 3531-3538 (2007)
   PUBMED   17090528
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Noskov,V.N., Staak,K., Shcherbakova,P.V., Kozmin,S.G., Negishi,K.,
            Ono,B.C., Hayatsu,H. and Pavlov,Y.I.
  TITLE     HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and
            mutagenesis in the yeast Saccharomyces cerevisiae
  JOURNAL   Yeast 12 (1), 17-29 (1996)
   PUBMED   8789257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>74
                     /product="non-canonical purine NTP pyrophosphatase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009143 - nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
     Region          2..>74
                     /region_name="RdgB"
                     /note="Inosine/xanthosine triphosphate pyrophosphatase,
                     all-alpha NTP-PPase family [Nucleotide transport and
                     metabolism]; COG0127"
                     /db_xref="CDD:439897"
ORIGIN      
        1 mkiliatgnk hkreeiqqil nglevelisi dqlpesieve etgetftena rlkaeayfel
       61 tglpvladds glev
//
LOCUS       WP_457565428             210 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase [Caldithrix abyssi].
ACCESSION   WP_457565428
VERSION     WP_457565428.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Wyatt,M.D., Allan,J.M., Lau,A.Y., Ellenberger,T.E. and Samson,L.D.
  TITLE     3-methyladenine DNA glycosylases: structure, function, and
            biological importance
  JOURNAL   Bioessays 21 (8), 668-676 (1999)
   PUBMED   10440863
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..210
                     /product="DNA-3-methyladenine glycosylase"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003905 - alkylbase DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=23575
     Region          13..210
                     /region_name="Mpg"
                     /note="3-methyladenine DNA glycosylase Mpg [Replication,
                     recombination and repair]; COG2094"
                     /db_xref="CDD:441697"
ORIGIN      
        1 mlltkllrsp skskkltqdf ylrgdvaqia rmllgkvlvs eiegirtagi iveteaysgk
       61 ndrashaykn rrtertrvmy eedgrayvyl iygmyhllnv vtnragkpda vliraieple
      121 gvehmlarrk qkrvipdltn gpgkltralg itlahygvyl sgdllwiedr gialpphfit
      181 agprigiaya gedaarpwrf wvkdnpfvsk
//
LOCUS       WP_457565441             117 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Caldithrix abyssi].
ACCESSION   WP_457565441
VERSION     WP_457565441.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..117
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=13905
     Region          4..85
                     /region_name="Phage_int_SAM_4"
                     /note="Phage integrase, N-terminal SAM-like domain;
                     pfam13495"
                     /db_xref="CDD:463898"
ORIGIN      
        1 mtrlfdrfvq dmqlrnfses tirsytyalk qlaahfdkap elineqeika yflynrnvkh
       61 wsraafsvsi saikfffekt lqkqwhvfgl vrpprdkslp eilrlkevnk ifscikm
//
LOCUS       WP_457565444             427 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457565444
VERSION     WP_457565444.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 427)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..427
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47946
     Region          6..267
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mhlsiwdima paffeclilv gihsylgihv ikrkvifvdl alaqvaalgt tvgflfgimp
       61 gtsgaywfsl gfaiigaaif slsrfrheki pqeaiiglvy alaaaiailv idkaphgaeh
      121 ikelltgsil wvkwktifha alvylavgvf hfifrekfll isndpekayd sglnvrlwdf
      181 lfyvsfgvvi thsvgtagvl lvfvflvvpa itsimitdvl wkqlligwsm gllvsvlgly
      241 fsyiadlpsg ptivtlyglm lflvalilyv iktpdrgkam ariglgivat ilvvllfrfm
      301 gqffhnhkdh aerqsaatls sphtdqadhs aaqasldsll rvftetrnla drfeiaksit
      361 eidrrqglrr liellkecpy pflreeifqe ilryskqdfg ydsmkdfnen rpafkrmekw
      421 lqtlqpf
//
LOCUS       WP_457565445             346 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter substrate-binding protein [Caldithrix
            abyssi].
ACCESSION   WP_457565445
VERSION     WP_457565445.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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   2  (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   3  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hantke,K.
  TITLE     Bacterial zinc transporters and regulators
  JOURNAL   Biometals 14 (3-4), 239-249 (2001)
   PUBMED   11831459
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Claverys,J.P.
  TITLE     A new family of high-affinity ABC manganese and zinc permeases
  JOURNAL   Res Microbiol 152 (3-4), 231-243 (2001)
   PUBMED   11421271
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435238
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..346
                     /product="metal ABC transporter substrate-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38969
     Region          1..333
                     /region_name="ZnuA"
                     /note="ABC-type Zn uptake system ZnuABC, Zn-binding
                     component ZnuA [Inorganic ion transport and metabolism];
                     COG0803"
                     /db_xref="CDD:440566"
ORIGIN      
        1 mktikwwfll liflpigsls annklnvvtt lstyadiaqk iggqyvtvqy ivpgnqdahf
       61 vrpkpsfavl lnradvfvst gldlelwvpt lvdmsknpri rsgeigyvsa sdgidlldkp
      121 avfsrseggv hiygnphiit gplnfkkiae nieigleknd pahadyfrqn lqkfkqqide
      181 rmfgkelvql mggdlltklt qsgklidflq sksfndrkli dylggwmkea lifrgkkiva
      241 yhknwayfqq tfglkvigyv epkpgippsp khveellqkm rrnqvkvlms anyfsenkvr
      301 eicekvgaip vivpmgvdga pgtedvfklv dywishlrea flqaeq
//
LOCUS       WP_457565450             195 aa            linear   BCT 27-JAN-2026
DEFINITION  3-phosphoshikimate 1-carboxyvinyltransferase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565450
VERSION     WP_457565450.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Marques,M.R., Pereira,J.H., Oliveira,J.S., Basso,L.A., de
            Azevedo,W.F. Jr., Santos,D.S. and Palma,M.S.
  TITLE     The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a
            model for development of novel antimicrobials
  JOURNAL   Curr Drug Targets 8 (3), 445-457 (2007)
   PUBMED   17348837
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Stallings,W.C., Abdel-Meguid,S.S., Lim,L.W., Shieh,H.S.,
            Dayringer,H.E., Leimgruber,N.K., Stegeman,R.A., Anderson,K.S.,
            Sikorski,J.A., Padgette,S.R. and Kishore,G.M.
  TITLE     Structure and topological symmetry of the glyphosate target
            5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein
            fold
  JOURNAL   Proc Natl Acad Sci U S A 88 (11), 5046-5050 (1991)
   PUBMED   11607190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..195
                     /product="3-phosphoshikimate 1-carboxyvinyltransferase"
                     /EC_number="2.5.1.19"
                     /GO_function="GO:0003866 - 3-phosphoshikimate
                     1-carboxyvinyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009423 - chorismate biosynthetic process
                     [Evidence IEA]"
     Region          <1..192
                     /region_name="AroA"
                     /note="5-enolpyruvylshikimate-3-phosphate synthase [Amino
                     acid transport and metabolism]; COG0128"
                     /db_xref="CDD:439898"
ORIGIN      
        1 fssaaffitg alllpgselm iknvslnptr tgflevlkqm gaqleinltq qepepageiv
       61 irpqklhnie ipeelipnii deipilsila arsegtlvlr haselrfkes drikaivqnl
      121 rqigveveef edgfqvcgpq sfkggkittf gdhriamsfa iagllgeepi eaddpgcaav
      181 sfpdfydilk svvqa
//
LOCUS       WP_457565454             148 aa            linear   BCT 27-JAN-2026
DEFINITION  ligand-binding sensor domain-containing protein, partial
            [Caldithrix abyssi].
ACCESSION   WP_457565454
VERSION     WP_457565454.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Zhang,Z., Liu,Q. and Hendrickson,W.A.
  TITLE     Crystal structures of apparent saccharide sensors from histidine
            kinase receptors prevalent in a human gut symbiont
  JOURNAL   FEBS J 281 (18), 4263-4279 (2014)
   PUBMED   24995510
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Hoch,J.A.
  TITLE     Two-component and phosphorelay signal transduction
  JOURNAL   Curr Opin Microbiol 3 (2), 165-170 (2000)
   PUBMED   10745001
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Perraud,A.L., Weiss,V. and Gross,R.
  TITLE     Signalling pathways in two-component phosphorelay systems
  JOURNAL   Trends Microbiol 7 (3), 115-120 (1999)
   PUBMED   10203840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>148
                     /product="ligand-binding sensor domain-containing protein"
                     /GO_function="GO:0140299 - molecular sensor activity
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          34..>140
                     /region_name="COG3292"
                     /note="Periplasmic ligand-binding sensor domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:442521"
ORIGIN      
        1 migtmlktsq yefvkglvfl gllllicstn rltaqhrpvk fehlsssdgl sqnkvfditq
       61 dhqgfiwiat edglnrydgf nfkifknipg nssslfyngi ncvyvskdgl vwtggqnggl
      121 grfdaqsetf vnflhdaqnp gaiaenfv
//
LOCUS       WP_457565456             368 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457565456
VERSION     WP_457565456.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 368)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..368
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39722
     Region          18..278
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mspqieiqlv avvvavacal pgvflvlrrm amlsdaisha illgivlaff itqdlsspfl
       61 vlaatltgvl tvtmvemlnr trlvkedtai glvfpllfsi gviliaryag kvhldtdavl
      121 lgelafapfd rlvlfgvdig pkalyvmggi lalnllfivl ffkelklatf daqlaaslgf
      181 apgvihyslm tlvsvtavga feavgsilvv almigppata yllvdsvlgm lllssgvgll
      241 aaisgywsah lfdvsiagsm atmvgiiffl tlllapqrgl ialarrrkkq qidfslemll
      301 vhllnhegmp eeeqecriah lpdhlhwegq liervikkge rekmlqraga flkltekgrk
      361 kaessltr
//
LOCUS       WP_457565464             152 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase, partial [Caldithrix abyssi].
ACCESSION   WP_457565464
VERSION     WP_457565464.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..152
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
     Region          <26..86
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 sirqiakknl eqgfyitrns wgkigkiafs lspgelfgpl kldenrysii klieikkagt
       61 tpfeeirdrv rsdlllqkak qvytqvlcdr ikqydievnf ealnrikvlk gnmlvlkshf
      121 pvrsavpats ywgitdrwyq qfnhviwkie nh
//
LOCUS       WP_457565461             615 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Caldithrix abyssi].
ACCESSION   WP_457565461
VERSION     WP_457565461.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..615
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70870
     Region          27..614
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mrsvlglvll ffllqalhsq eifdvkahyt kkevyipmrd gvklftsiyl prdttrdypi
       61 lmlrtpysvy pygedkykkr lgpsqkfaee gfifvyqdvr gkfmsegqfv nmrpyiadkn
      121 grevdettdt ydtidwlikn lahnngcvgi wgisypgfya amsvidahpa lkavspqapi
      181 adwfigddmh hngafslvla fnffatfgqp rpaptnrwpa rfkhgtpdgy qffldlgalp
      241 nankkyfkhq iafwdsamah etydyfwqrr silphlrnvk pavlvvggwf daedlygpln
      301 iykkieeedr qnknflvmgp wshgawergk gdrlgdirfg sntseffqds vlfpffmhhl
      361 kgapaveqae alcfdtgllk wsrferwpta vqernlylsa qgrltftapq aeqgydeyls
      421 dpakpvpfta kitntwgktf mvedqrfaar rpdvlvykse ilespltlag pltatiyvst
      481 tgsdadfvvk lidvwpdtar dfkpnpcqvr mggyqqlira eimrakfrns yttpepltpg
      541 qvtpitirln dvyhtfkpgh rlmvqiqssw fplfdrnpqk finiyrarde dfqkathrvy
      601 fsrqypshlk lpvve
//
LOCUS       WP_457565465             188 aa            linear   BCT 27-JAN-2026
DEFINITION  methyltransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457565465
VERSION     WP_457565465.1
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 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..188
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21376
     Region          75..187
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mslfalfqav cliwilseil lgrltyhkpe kqerdkrslk miwitiiisi pagvflglqn
       61 fgrfplpgki sigvgtflia vgltirwlai ltlrryftsn vqilkdhqiv sygfyslirh
      121 payagsllsf lglglafnsw pacitifvpv slaflyrikv eeeallkafg keydayrqrt
      181 kklipfiy
//
LOCUS       WP_457565460             256 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Caldithrix abyssi].
ACCESSION   WP_457565460
VERSION     WP_457565460.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..256
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28257
     Region          1..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mhilaiinnk ggvgkttsav nlaaafaekg katllvdldp aasasmhlgl dptrnerqtl
       61 cdyllsgqgk ladfiyptsf kgldcipsep alsefyeemv qeqevdffiq pqdfperyel
      121 vlldcppnlg nlaynalais gfvlipvqtq flaltglelt lktvqkvqrh lnpdlkilgy
      181 fgtqfdrrtr aanevvqllk drfadqvfet vigvntklte aynaqkpiln yassargake
      241 yraladeilk rlkktt
//
LOCUS       WP_457565468             884 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Caldithrix abyssi].
ACCESSION   WP_457565468
VERSION     WP_457565468.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..884
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=100996
     Region          30..>89
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          126..815
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mekwlksisf ifvsivffqf nlyagttgki agrvidaqtk ealaganvvi lntslgasvd
       61 ldgtyyiini ppgvydieas figyqtvrkq kvvvtvdrtt tvnfelqptv letevvevva
      121 erediirdlt atsqkvsgaq irqlpvenlg dilslqagvt qdpgggihlr ggrsdeiqyy
      181 vdgiavtnpf grglavpvqn nviqemevis gtfnaeygqa msgivnivtk eggdqtnvsf
      241 saysgdfvst hddvfmninh idpfsqkyve gaisgpvplf nkriyyfisg rfrdeenwly
      301 gkrlhmpsdt adftspdpen wavqytgdgk iipmnpsrev syqakltfkp fsnlkmsynf
      361 lgnssrwkny dhhnkynpey ipthysqgit nlfvlthtis astfhefrms yywdkyerhc
      421 rkdpfdpfyd qgihkkidvp qdvfavggvd agfeyrenlt taikydlvsq vnkynlikig
      481 veyrrhdlkd ewfvvrkdeg tnwqlqiddl ssfahnyyhk kplelaayiq dkieiedlvv
      541 nagirfdyfd pnskvpvnmt dpsnkrgape dyayrdatvk tqisprfgla fpisdrgnih
      601 vayghffqip dlgrlyenpe fevigrfesf ignadlepqr ttmyeiglqq qliqnlvmnv
      661 tcyfkdirhl agtklyktfe qdeygqyann dygnvwgita sldlrkmgmi sanldytyqi
      721 aegngsdpkq afydarnrde saktlipldw dqrhvlnaiv tvsgkswgis siskfhtgfp
      781 ytpittynra pniqlknegr rkaefnmdlr lyksihfgki ttrffvnien vfdnlrneyr
      841 peiterdlrv hepktflnsl yeyrfnpatq pmprlvkvgl dvem
//
LOCUS       WP_457565472             767 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Caldithrix abyssi].
ACCESSION   WP_457565472
VERSION     WP_457565472.1
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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..767
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86959
     Region          5..749
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mnicksllfl iftvtligcq nqnkdftqyv npfigtgghg htfpgatvpf gmvqlspdtr
       61 isgwdacggy hysdttiigf shthlsgtgc idygdilfmp tvgklhlqpg teenpqsgyr
      121 srfshekema eagyyrvfld dyqiqvelta tqrvgfhkyt fsasdeaqii idllhglgpd
      181 nvieaklnfv ndslitglrr segwardqkv yfaalfsrpf eeygiavdnk leksrrtatg
      241 knikayvkyk tgqseailvk vgisavseeg alknlkkeap dwdferirtr akeawnrhfn
      301 kievqggtre qritfytaly hamiapnlfm dvdgkyrgmd gkihqakdfv nytifslwdt
      361 fraahplfti idqkrtidfi rtllakyqeg gilpiwelag nytgtmigyh aipvivdayi
      421 kgirdfdael ayqamkysam qdhrglkyyk tlgyipfdke ahqsvsrtve yayddwciaq
      481 makalgkdkd fklfnaraqf yknvfdaevg fmrgkdsngq wripfdpaai htkggedfte
      541 gnswqytffa pqdlenfidl fggaepfvkk ldslfyqepp enpslpditg llgqyaqgne
      601 pshhiaylyn yagkpwktqr ivrtivdsly tanpdglcgn edcgqmsawy ifsamgfypv
      661 cpglkeyvfg spvfdkvtiy lengrqftik tenngkdnly iqsvkkddls ysktyithdd
      721 ilnggtltfk mgdkpnkywg vhkddlphss vdiklsvdel kaflqkq
//
LOCUS       WP_457565474             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Caldithrix abyssi].
ACCESSION   WP_457565474
VERSION     WP_457565474.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..372
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=40560
     Region          6..304
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mgyeqderiv mtldaggtnf vfsaiqknqe iidpirlpsn ahdlelclqt iidgftrvkk
       61 qlpepavais fafpgpadyp dgiigdlvnl pafrggvalg pmleeifqlp vfinndgdly
      121 afgealagyl pyinnllkia gspkrfqnlv gftlgtgfga givrkgelfi gdnsgagevw
      181 llrnklhptm nveesvsira irrvyaqltn ilfeespspk eifeigmgkr pgnkeaaiea
      241 fqtmaealgd aianvltlid glavigggls gahplflqkm idemngkyrn fqgneyrrlv
      301 pivfnlennk dldkflqgek keitipktnk kiiydalprl gvgiskigts raialgayay
      361 alneldsksk rn
//
LOCUS       WP_457565486             323 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565486
VERSION     WP_457565486.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..323
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37460
     Region          <15..>162
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mpdknlnise aalqltevvs linqvndfsi aldmildtcv eylkiphvgv arfkedeekf
       61 qivksrnfdq nlkdrfrfnl ftpinnfvir kertsafknl gsriqigner felesafktl
      121 yllpfrfheq ingfliihiy qseddlsest ltllesfvnl vapifhvfgp lkthkrggen
      181 iiskiikdri nearlglfpv sfaifriqlw qemissvalq dtvqtyqqvf ekklrqlgdv
      241 iwltldtaff ifpnadlfti eslcsalkee iesnfnrqdd qveinvkyvs isypqsgkeg
      301 ydiinqlwlr lfdelqadfa tnh
//
LOCUS       WP_457565492             336 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter substrate-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565492
VERSION     WP_457565492.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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   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 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   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 336)
  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 10194659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..336
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38243
     Region          25..323
                     /region_name="PBP2_TRAP_Tp0957_like"
                     /note="Uncharacterized substrate-binding protein of the
                     Tripartite ATP-independent Periplasmic transporter family;
                     the type 2 periplasmic-binding protein fold; cd13670"
                     /db_xref="CDD:270388"
     Site            order(165,167,189,206..207,210,231)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270388"
ORIGIN      
        1 msvkisrmvl filvatgflf skpivikfat lapdgsswmk imrefaaeik ektdgqvifk
       61 iypggiqgde kdvlrkirin qlqgagftgv gmgeilpevr vldtpfffkn yaeldyvlnk
      121 fdpyfaqrfk kkgftligwa evgsvyifts kkvqtvddfk kikmwiwegd pvaeatfkaf
      181 glnpiplsvt dvltslqtgl iegvytspla clvlqwftkv kyvvdvplti sngavlisnr
      241 afkkispehq qivretgyqy frrltetsrk dnetslmnmq qngiqllkls spenlkrfde
      301 igeqarrsli gklydeelli kiestlqefr tkknre
//
LOCUS       WP_457565494             431 aa            linear   BCT 27-JAN-2026
DEFINITION  NfeD family protein [Caldithrix abyssi].
ACCESSION   WP_457565494
VERSION     WP_457565494.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..431
                     /product="NfeD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46522
     Region          1..431
                     /region_name="NfeD"
                     /note="Membrane-bound serine protease NfeD, ClpP class
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1030"
                     /db_xref="CDD:440653"
ORIGIN      
        1 mkkffliail iltvnasaev vhriiiegvi npvateyitk sieqaeetnv ealiiqldtp
       61 gglmesmhki vkaiqasevp vivyvapsgs ragsagvfit yaahiaamap stnigsahpv
      121 fggsptgaqp dtattstlme kvvndavaki rslaekrgrn adwaekaite sanitekeal
      181 klkvidfiap svdsllslid grqveldvgv vktlrtanaq vitfemnwrq rlldiisnpn
      241 vayillmlgi ygilfelysp gailpgvvgg iclilglyal qtlpvnyagf lliifavilf
      301 lleikipsyg lltiggiisl imgsvmlfes plpflrvswq vitfvvtlsv lffvfaigma
      361 irthrkkptt gdagligeig evykplnpeg tikvhgeywk avsdepckkg qkvevvefnr
      421 ntlvlkvkpv k
//
LOCUS       WP_457565496             227 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system protein [Caldithrix abyssi].
ACCESSION   WP_457565496
VERSION     WP_457565496.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..227
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26052
     Region          20..>85
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mntfiqkpkn rkiatgqkkm vfqrflared gfslmelivt lviigsisai aygvvllnar
       61 mfgtlsgeis trwelrktln imredfleln panilsisng neiyfkking dkvrysylnq
      121 tlsrrknsea wevlltnvtt ppfayfdsnm nptnnkneiv yikaslavnk ngnvrsaedl
      181 fflrnltikq pkigndsddd kdhdhkdddd dddnnhqhhh rhrhged
//
LOCUS       WP_457565497             255 aa            linear   BCT 27-JAN-2026
DEFINITION  prepilin peptidase [Caldithrix abyssi].
ACCESSION   WP_457565497
VERSION     WP_457565497.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Berry,J.L. and Pelicic,V.
  TITLE     Exceptionally widespread nanomachines composed of type IV pilins:
            the prokaryotic Swiss Army knives
  JOURNAL   FEMS Microbiol Rev 39 (1), 134-154 (2015)
   PUBMED   25793961
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Zhang,H.Z., Lory,S. and Donnenberg,M.S.
  TITLE     A plasmid-encoded prepilin peptidase gene from enteropathogenic
            Escherichia coli
  JOURNAL   J Bacteriol 176 (22), 6885-6891 (1994)
   PUBMED   7961448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..255
                     /product="prepilin peptidase"
                     /EC_number="3.4.23.43"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28436
     Region          6..254
                     /region_name="PulO"
                     /note="Prepilin signal peptidase PulO (type II secretory
                     pathway) or related peptidase [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport]; COG1989"
                     /db_xref="CDD:441592"
ORIGIN      
        1 mktidilvil fglatgsfln vcaarlplkr svlwgrsqcp vcghqiswyd nipllsfvll
       61 kgkcryckak islqypliea fsalvtyaly lkfglsitav fygifiyfli viglidfktk
      121 lilnrllipl ftagvlinff geiipfkdal sgaflgggim wmaailgaki fkkeamgmgd
      181 vklafvagff lgwqhillal ylgfviallf ilaiwlfkkk eapslipmgp flalgfivyl
      241 fygklliqwy lswls
//
LOCUS       WP_457565505             199 aa            linear   BCT 27-JAN-2026
DEFINITION  5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase family
            protein [Caldithrix abyssi].
ACCESSION   WP_457565505
VERSION     WP_457565505.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Parveen,N. and Cornell,K.A.
  TITLE     Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical
            enzyme for bacterial metabolism
  JOURNAL   Mol Microbiol 79 (1), 7-20 (2011)
   PUBMED   21166890
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Pugmire,M.J. and Ealick,S.E.
  TITLE     Structural analyses reveal two distinct families of nucleoside
            phosphorylases
  JOURNAL   Biochem J 361 (Pt 1), 1-25 (2002)
   PUBMED   11743878
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..199
                     /product="5'-methylthioadenosine/S-adenosylhomocysteine
                     nucleosidase family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0008782 - adenosylhomocysteine
                     nucleosidase activity [Evidence IEA]"
                     /GO_function="GO:0008930 - methylthioadenosine
                     nucleosidase activity [Evidence IEA]"
                     /GO_process="GO:0009164 - nucleoside catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019284 - L-methionine salvage from
                     S-adenosylmethionine [Evidence IEA]"
                     /GO_process="GO:0019509 - L-methionine salvage from
                     methylthioadenosine [Evidence IEA]"
                     /GO_process="GO:0046124 - purine deoxyribonucleoside
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=21917
     Region          1..196
                     /region_name="MtnN"
                     /note="Nucleoside phosphorylase/nucleosidase, includes
                     5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
                     MtnN and futalosine hydrolase MqnB [Nucleotide transport
                     and metabolism, Coenzyme transport and metabolism];
                     COG0775"
                     /db_xref="CDD:440538"
ORIGIN      
        1 mltivsalra etepiiqamp rvealpcgag slrryrhfdl lrvgvgeqra vqsfkayler
       61 yrpsqvvlmg fagalnaqvs igqvfaieki ihagssqtla lplpetfgrl araslltvak
      121 altdggeknk freqfktdlv dmesfylaal cherhiecfa lkgvsdlads aanmqfkknf
      181 ksvslilfet lksilqiek
//
LOCUS       WP_457565506             280 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caldithrix abyssi].
ACCESSION   WP_457565506
VERSION     WP_457565506.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..280
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32573
     Region          1..210
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkisviipvy nrpqmvkrai esvlaqteaa heilvindgs tdetprilek fgtritvvnq
       61 phkgvsaarn tgirlargew ialldsddew lpeklamare fheshpqyli fqsqeiwirh
      121 gkrvnpkkkh qkyggwifrq slplcivsps aviihqsvfk kvglfdenfp vcedydlwlr
      181 varlfpigld srpgivkygg hedqlsrkyw gidyyrvlai ekhlkennlp sdlrqaalee
      241 ilkklqvlis gyqkrgrrnf qleekwrryr eqlislkenl
//
LOCUS       WP_457565508             789 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Caldithrix abyssi].
ACCESSION   WP_457565508
VERSION     WP_457565508.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 789)
  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 789)
  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 789)
  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..789
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..789
                     /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=91350
     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 mrrkilqlml aifvvvallv vvgsfwgyat fksslpvleg evqipllkes vtvyrdsmgi
       61 pqvvarsetd ayfalgylha adrlfqidlt rrvatgrlse llgpstlfid ryqrmlghyr
      121 lakkfvaqld sqdrerlqay lkgiaywvkh tdalpfeyll lrkefkpytm eellsvlsfq
      181 twfanylqss dtwflqiaer lgrekakdfe kpyplwapft vpqqnqfslq twlfkryfse
      241 dllpyhmahs snswvvapqk sasgfamlas dphletrrlp qfwylcglhv naanlhvlgi
      301 stpglpftim ghngkaawaf tvggidvsei yqekrhpqds tlyfngrewy rcqtlvdtiy
      361 isgedepyil rykqtengpv iwtadsmkad yalhwagfdv nlaksvqaaf rlakldnfed
      421 frravtsfga ldanwtyadi rgnigyqlgt pipirpfkst klpvpgwids lkwqgfqple
      481 ktphslnpqr gwlatcnnkq ddanldyplm gkfaadrilr isellsqnrk fsvqdmqnfq
      541 mdrvdryhqr wqkimlgvlr qngryaladr lkkwdgsmes dsreaalvml flqnlkkyml
      601 edelgeqlkf lfddrfeqiy lqgpddyfdd lrtkdkiesr eeitnralqt tleqwqdrpw
      661 gefltltmah pfarvpllsn vlnlkygpip wggseatlna sffwedkqnp ghfkaivgps
      721 wrfvidfsdp dqasfvlpag isgnplspyf fnffeywksg krwivpispe kikqrakltl
      781 kltpmtdre
//
LOCUS       WP_457565509             312 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD:protein FMN transferase [Caldithrix abyssi].
ACCESSION   WP_457565509
VERSION     WP_457565509.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..312
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=34307
     Region          1..293
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mgtvyhikli ddvnasisek elqsavdsll ndinrqmsty qpqseisrfn rwrstepfkv
       61 speflrvvqk alqiyletdg afditvgplv dlwgfgrkga rfeppdsqqi arilqrvgah
      121 qlkvcgdtal cklnpdleid lgaiakgygv davsrllken gftnfmveig gevyasgkkg
      181 drpwrigvdq pqynappgqm veavlnlenc avatsgdyrn ffeyrgkiys heldphtgwp
      241 vanglasvtv iapdcmtada lataimvmgd erglplinsk kgtealilkr egekglkalw
      301 skgmknyllq gn
//
LOCUS       WP_457565521             395 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Caldithrix abyssi].
ACCESSION   WP_457565521
VERSION     WP_457565521.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 395)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..395
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41688
     Region          5..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 msglkevviv saartpvgsf ggvlkdvpat klgsiaikga lekggvpfdq vdevimgnvl
       61 qanegqapar qaalgagldt svacmtinkv cgsglksvml aaqaimvgda evivaggmen
      121 msqvpyylpk arygyrmghg elvdgmikdg lwdvyndfhm giaaelcase cnvpreaqde
      181 yaimsykral kaqeeglfne eivpvevpqr kgdpiivsed eepknvkfek iphlrpafkk
      241 dgtvtaanas kindgaaavv vmslekanel glkpmarivs qasfakkpey fttapadsin
      301 lalkkagltv edidlfeine afavvaiinn rllnlpvekv nvhggavaig hpigasgtri
      361 lttllyamkh rsakrglasl cigggeastl vvelm
//
LOCUS       WP_457565523              63 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565523
VERSION     WP_457565523.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 63)
  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 63)
  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..63
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>63
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          3..>50
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtirelvlkn rscrrfkqne avsvellrsw idlarlspss anlqplkyii sssaqtnasi
       61 fst
//
LOCUS       WP_457565526             453 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase [Caldithrix abyssi].
ACCESSION   WP_457565526
VERSION     WP_457565526.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..453
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49325
     Region          1..452
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mlrfnfkffa lalltlmvli sckqearqpk niivfiadgc gfnqvaagey yqfgekgkav
       61 yqsfpikfai stfpvdglye pqkawksfay vlqkptdsaa satalatgvk tkngilgmds
      121 tftplqnive vveqagkatg vvttvpfnha tpagfvahne srknyhqiar emifkstidl
      181 imgaghpeyd dnaqklqepv fkfisdsafq elkqgkignd adgdgaveyw tfiedsadfa
      241 glvsgqtper vfglakvist lqfnragdks adaftvpfnk glpdlrtmtq aainvldddp
      301 dgfflmvegg aidwaghana pgrlieekld fdkavqaaie wveknsnwde tliivtgdhe
      361 tgyltgpgak teydgstafs veevwpalkn ngkgkmpdme fhshghtnsl ipffakgqgs
      421 glfkgevdgt dpvrgkfidn sdvgkvlksf fnk
//
LOCUS       WP_457565528             409 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565528
VERSION     WP_457565528.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..409
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45202
     Region          25..346
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mskiydvvvv gggpagsaaa lfcvrqglev cviekaqfpr dkicgdaisg ksmtmlkele
       61 lldevttlps arinaitfgn pdhdtvtipl lgdkrrgipp glvikrllfd eflfnkvrks
      121 aasvyegyqv nrlifdgdrv igvetrgteh vnsisvlgkv iigadgfnsi varhtglyeh
      181 dpehwvvalr qyyknvkgln dtielhyide vqpgylwlfp agdnvanigi gmlhksmkkr
      241 nvnlseamqk ainspffadr faeaeplekp mgwnlpvask hrknyghgfl llgdaaglid
      301 pftgegigna lfsakiaaet vaeavkqndf teeflkrydq klwqalgdel qvsaklqrig
      361 rispllnfvi kkaarsnhvr eiisgmmanq ipktefanpl fylklffsn
//
LOCUS       WP_457565530             240 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457565530
VERSION     WP_457565530.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Quigley,A., Dong,Y.Y., Pike,A.C., Dong,L., Shrestha,L.,
            Berridge,G., Stansfeld,P.J., Sansom,M.S., Edwards,A.M., Bountra,C.,
            von Delft,F., Bullock,A.N., Burgess-Brown,N.A. and Carpenter,E.P.
  TITLE     The structural basis of ZMPSTE24-dependent laminopathies
  JOURNAL   Science 339 (6127), 1604-1607 (2013)
   PUBMED   23539603
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Pryor,E.E. Jr., Horanyi,P.S., Clark,K.M., Fedoriw,N.,
            Connelly,S.M., Koszelak-Rosenblum,M., Zhu,G., Malkowski,M.G.,
            Wiener,M.C. and Dumont,M.E.
  TITLE     Structure of the integral membrane protein CAAX protease Ste24p
  JOURNAL   Science 339 (6127), 1600-1604 (2013)
   PUBMED   23539602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574322
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..240
                     /product="M48 family metallopeptidase"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27568
     Region          82..229
                     /region_name="M48C_Oma1-like"
                     /note="Oma1 peptidase-like, integral membrane
                     metallopeptidase; cd07324"
                     /db_xref="CDD:320683"
     Site            order(125..126,129,179,183,223)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320683"
     Site            order(125,129,179,223)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320683"
ORIGIN      
        1 madifyklgk rvgkslakgr ylynsafapk tealkaeyrl gsilareiea qntvfdspyh
       61 qlllesllkq lktrvknker yfyikilesd dlnafalpgg fifltsalvq nierdkdela
      121 fvlshemvhi iarhpfkkmv tnysmealsk vfrsgsiaav ygrdmikkli nsqysqsney
      181 yadeygarlm ysaafdpaga iqllqrfkrw kgngdrfnyf ashpsideri lhlkkliklk
//
LOCUS       WP_457565531             332 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel beta subunit family protein [Caldithrix abyssi].
ACCESSION   WP_457565531
VERSION     WP_457565531.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 332)
  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 14442711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..332
                     /product="potassium channel beta subunit family protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:0008076 - voltage-gated potassium
                     channel complex [Evidence IEA]"
                     /GO_function="GO:0015459 - potassium channel regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37637
     Region          1..318
                     /region_name="AKR_AKR6C1_2"
                     /note="AKR6C family of aldo-keto reductase (AKR); cd19143"
                     /db_xref="CDD:381369"
     Site            order(19..21,27,49,54,82,122,152..153,178,207..212,216,
                     218,226..228,268,285..289,293,296..297)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381369"
     Site            order(49,54,82,122)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381369"
ORIGIN      
        1 meyrflgksg lkvsalsfga wvtfgeqvde eiayqcmkea ydagvnffdn aevyaqgqae
       61 immgnilkkt gwkrsdlvls tkifwggsgp ndcglsrkhi fegtnaalkr lqvdyvdlif
      121 chrpdlytpi eetvwamnli iqqgkalywg tsewsaeqir hahefalreh lipptmeqpe
      181 ynmfnrekve keflnlyrdi glgtttwspl asgiltgkyn ngipegsrls lkgyqwlrsr
      241 leseegrkkl ektrqltria delgvtmaqm aiawclknpd vstvitgasn psqvrqnmea
      301 lkaldllsde vmekiesilq nkprppmdlr nl
//
LOCUS       WP_457565532             916 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457565532
VERSION     WP_457565532.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..916
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=102689
     Region          28..452
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          465..894
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpifryllli lfltfslafs kndddlkala kqidipfqkf vlkngltliv hedhkapiva
       61 vnvwyhvgsk nekpgktgfa hlfehlmfng senyndeyfk pfekvgatgm ngttnrdrtn
      121 yfetvpvnal dmalwmesdr mghligaidq akldeqrgvv qnekrqgenq pygkvwtwiv
      181 qntypkghpy swttigsmed lnaasledvh ewfknyygaa naylviagdi ntdsvrqkve
      241 qyfgdvppgp pvtkhdvwva kmqgthrmva edrvpqariw kvwnipqwgs keavmldlas
      301 svlgsgknsr lykrlvykdq iatdvsatvy lgeiggqfmi saaarpgvdl kkvekaidee
      361 lqkflqkgps ekelkrvkvq hlsrfvkgie qiggfrgkan ilaknevfgg spdyfkktvn
      421 wvvnaapkav haatkkwlsd gvfilevhpf peysttgkdv drsklpetgt ppepkfpaye
      481 kikldnglei fytkrttvpv vnmslvidag yaadqfaspg tanmtlamld egtpdmssle
      541 isekldmlga nlragsnldv sfvnlnvlkt tlpeamriys evilhptfpq kelerlkkqi
      601 iagikreqsq pvqmalrvlp rylygighay gnpltgsgti esvkkmtrdd likfhktwfk
      661 snnaklivvg niekdelekl vkkyfgkwka gtvpqknisd valkpaqill idkpaseqsl
      721 iiagqilppk sdpdnlaiem mnkvlggtft srlnmnlree khwsygarti vsnargpslf
      781 fayapvqidk tkesiqemlk eingmrsekp vtpeelekvk nneilklpgt wetgaavlhs
      841 iqeivtfglp edfwsqypnl irslsleqvq naakkalhpd hliwvvvgdr tkieepikql
      901 gvaevkvidv egnvie
//
LOCUS       WP_457565540             138 aa            linear   BCT 27-JAN-2026
DEFINITION  GtrA family protein [Caldithrix abyssi].
ACCESSION   WP_457565540
VERSION     WP_457565540.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8) (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..138
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15940
     Region          3..138
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mapqikerli rmikfgliga sglivnnlfl wifhgklhls levasplaiv iaifnnfswn
       61 dlftwgrdrh krrytyfhrl iryytsaalg glinyatlli ltskfdwpyi lsnligiglg
      121 misnfllsef wvfrkksd
//
LOCUS       WP_457565541             372 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 39 protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565541
VERSION     WP_457565541.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Ernst,J.F. and Prill,S.K.
  TITLE     O-glycosylation
  JOURNAL   Med Mycol 39 Suppl 1, 67-74 (2001)
   PUBMED   11800270
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 372)
  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 372)
  AUTHORS   Gentzsch,M. and Tanner,W.
  TITLE     The PMT gene family: protein O-glycosylation in Saccharomyces
            cerevisiae is vital
  JOURNAL   EMBO J 15 (21), 5752-5759 (1996)
   PUBMED   8918452
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10590977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..372
                     /product="glycosyltransferase family 39 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          <1..94
                     /region_name="PMT_2"
                     /note="Dolichyl-phosphate-mannose-protein
                     mannosyltransferase; pfam13231"
                     /db_xref="CDD:433048"
ORIGIN      
        1 yailsvpdtp llffwiltlf lflkfyqtqr arwlylmgvt lgfgliskyt mvallpglfa
       61 fllfdkklrr wfvtphpylt fvimllvfsp vviwnaqndw asfafqfsnr aakfkpltsk
      121 yivqlffsql flltplvfgl lvyfvkkqiq trfkdrllnl lfwsgfviig gfiyvslrsl
      181 vkmnwllpgy lgwilgavfv lkaetirssr wiksgmyfsv fllliahiiq lvpnmplgeg
      241 ntwsgwpdaa qkihalqqkm ggrkkvfifs ngyksaallk fylpdhqdty aeniynrpal
      301 qfdiwgtpds ligknalyvi ddrreykddl kyvrkyfdsv elieqfeykf ldrfhtrtiy
      361 cyeaknyhgt an
//
LOCUS       WP_457565543             650 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565543
VERSION     WP_457565543.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..650
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
     Region          197..649
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 syqsfskmfk iiksgqgklt vdhpakrffk alkvlilqnt vltsrflisl ihafiawtfi
       61 lyflvnlsdl irafdsefll fghsapgrwy vlfvdifsvl avvsmaifll rrflfkseql
      121 kirenvrllp eveagikrds livglfilfh vgfrwlgesf llahkgadpw qpaasffanl
      181 wigmapdtln ilyhfcwwla iglilafipy fpyskhahlf mgpinfffkk hpegytllep
      241 idfedeeaeq fgqatlahqe igqlidayac imcnrcqevc payttgkels psaleinkry
      301 flnsngqqll ndkenlpsfl efalsesalw acttcgacve vcpvgneply dllgirrdrv
      361 lmesqfpkql qnafvgmern gnpwnmnedr lawtkvdqtl kvptvkenpd feilywvgca
      421 gafdqkgqri araftkilnq aqvnfavlgn desctgdsar ragneylfam laennvqnln
      481 aanvkkivtt cphclhtlrn eypqfggeye vlhhsqfinq liaqgkvqlk tgqiegltfh
      541 dpcylgrhnr eydaprgvln avssirvkem enarensfcc gaggaqmwke eepgeeavrr
      601 krlqqaqqid aklvstacpf cltmltdasn etnagievkd laeivaerls
//
LOCUS       WP_457565546             946 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Caldithrix abyssi].
ACCESSION   WP_457565546
VERSION     WP_457565546.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..946
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=108465
     Region          27..116
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          102..833
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mngfnkifli llimsgsllw aqkpgtirgl vtdketgepl vgvniivkgt yygastdleg
       61 ffiipkiepg vytievsyvs ykviqqtgvk vepgqtltln fqmepsilal gqeitvigek
      121 plmdleqttt artltedeik nrivenvtdl vsqqvgvtkq ddalyirgsr syesqylveg
      181 lsvqdplagt gfglrlssya iqeievltgg ykaeygqats giisvktksg gdklegyfsy
      241 ktdhlfgqfr dkdfsfntdh wdfslsgpep itnimnkagl klpgrfyffl nlqnkifddy
      301 tratakqlhs siaptlgglv dqdffaprqn nlwsaliklt wkidpthklt ytynrslvin
      361 qntqtlqtnl nyveprpgfp ykymklldnf ntfthdneqi sliwnhtlns ttfyelkfsr
      421 yfaqlrsewg ddlwngytqp ldvprlpvey ytpygdstkv rvipgdgfyd ygnalswhdh
      481 fmysytikgd lthhsgdvht fktgieisfk emqlidiqep fagpygssqd ifhvypadga
      541 iyfqddirfg gfilnaglrl dywapgafad raiedttnfi spdqrekykk dsfnffgrrv
      601 karlmprigv sfpvsnnqml yfnyghfskr prpqfvysgl stvsarsayq tygnpalnpe
      661 tsvkyelglr nqftendvls isayykdifd yvkttrfrlp grggqtayty vnldyararg
      721 ieieyktrig kylfgnvaas ysitttkssn assilqidrs atgqdvpire syaawdrpwq
      781 isgnlsfrvt kdqkpeifgi klfnqwnlnl hffaqagrry tpvvfsgqyr sdgrpiylte
      841 ydveektlys kigsnwkwvd lsfkkyfdlw dvhyifyfei rnlfnnknaq iinpvtgray
      901 eygdpvpisw ndpvypdrhw phdpypfdpa ryraprhill gfslef
//
LOCUS       WP_457565549             418 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA recombination protein RmuC, partial [Caldithrix abyssi].
ACCESSION   WP_457565549
VERSION     WP_457565549.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..418
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          65..415
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 nkehtkmtla ltlivgfslg liiglglmyf fmsrqqktae qlarefheks eqqklqeler
       61 iiahmrdsfg nlsmkalres seqflklane vlkdqsrlge ekldgkkkli dqtlgqmkee
      121 lskvenmikq ienerkqsfg qlsqqlkqsv eqsqrlqeit nqlsaalshs qvrgqwgerm
      181 aedvlrlagf reginylkqs rvqdarsrpd ftfllpqnlk vnmdvkfplt nylnylnaen
      241 eqekeryktl flrdvrarik evttrdyinp adhtvdyviv fipneqvyaf inehdisild
      301 ealrnkvilc spitlyavla virqavdnfr leqtaanils llkdfskqwe rfkeamqkmg
      361 kkiddakney tklvttrttq lerplrkien vrlpeqlqsg dapllpepen dereengl
//
LOCUS       WP_457565551             286 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457565551
VERSION     WP_457565551.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..286
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=32904
     Region          <10..281
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mivrknepvq eieltigdvs kivlisqshf wdgdntenyi vvirditrqk hledrmkrqe
       61 qltavgqlaa gvaheirnpl nsistivqql kkdfkptrde dvynelidiv ytevkrinqk
      121 ineflrfsrp epirpskfkl sdwlnsiikq yqptfedrqi efvlqlnwdg evfwdadqmr
      181 gvmsnliqna idamterkrl eigvtkendk iiikvtdsgk gippeqldki fnlyfttkad
      241 gtgiglsivq rivfehdgmi qvsserdkgt tftitlprti aldssq
//
LOCUS       WP_457565553             319 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-glucuronic acid decarboxylase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565553
VERSION     WP_457565553.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Walsh,R.M. Jr., Polizzi,S.J., Kadirvelraj,R., Howard,W.W. and
            Wood,Z.A.
  TITLE     Man o' war mutation in UDP-alpha-D-xylose synthase favors the
            abortive catalytic cycle and uncovers a latent potential for
            hexamer formation
  JOURNAL   Biochemistry 54 (3), 807-819 (2015)
   PUBMED   25521717
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..319
                     /product="UDP-glucuronic acid decarboxylase family
                     protein"
                     /EC_number="4.1.1.35"
                     /GO_function="GO:0048040 - UDP-glucuronate decarboxylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36435
     Region          1..304
                     /region_name="UGD_SDR_e"
                     /note="UDP-glucuronate decarboxylase (UGD) and related
                     proteins, extended (e) SDRs; cd05230"
                     /db_xref="CDD:187541"
     Site            order(7,9..12,31..36,55..57,71..75,90,112..114,143,147,
                     170..173,184)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187541"
     Site            order(60..61,96..97,100..101,103..104,157)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(77,140,172,183..185,188..189,200..202,207,209,244,
                     270,274)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(91,114,143,147)
                     /site_type="active"
                     /db_xref="CDD:187541"
ORIGIN      
        1 mrilvtggag figshlcetl lnkghdvlcl dnfftgqken iwhlmdnkrf elirhdvtqp
       61 illevdriyh facpaspihy qynpvktikt svmgtihmlg lakrvrarim lastsevygd
      121 pkvhpqkesy wgnvnpigir scydegkrva etlmmdyhrq nkvdikivri fntygprmai
      181 ndgrvvsnfi iqaltnqnit vygrgnqtrs fqyiddlidg vermmnvedf igpvnlgnph
      241 eftilelaek vieltnsrsk ivfkplpadd pvqrkpfigl akekldwepr ikledglkkt
      301 iayfdevlsr lpdkkpiid
//
LOCUS       WP_457565557             132 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Caldithrix abyssi].
ACCESSION   WP_457565557
VERSION     WP_457565557.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..132
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14744
     Region          45..131
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mdvlfyivmv fvgfivfiqi yarvqglmkr gkeipridgk ignalaqnas tllyfytptc
       61 sackvmtpvi drlqtefkni lkinlasdle igkkfgimgt pslvlvkdnk iksfvvgakn
      121 etfirkllnn hq
//
LOCUS       WP_457565558             367 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565558
VERSION     WP_457565558.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..367
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..363
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 aiavknnagl nakhlmvkea asktsldipk tdfyysyden niaennlpld vwganqsfkf
       61 ptlyltqrsk nkahimaqkq kyalsetalk revsrayyti iylnnveaky rfldslltrf
      121 aqaakmrydv getnkleylt alakkkeaev mlaqtrqkik sayaelnawl qtdsayvlpp
      181 lkltqlplts idssnpglny yrqmlraanl dvslqrqsfl peinvgvfvg snnganakky
      241 ygfdvgisvp ilffeqrsni qrakiqrqii rqnykdydak lkahiqslma mlhsykksvd
      301 yyqttgrela kellqnanka yqngeidflq yiqlvrnsls iemdylnnln qynqtvlsln
      361 ylvlnek
//
LOCUS       WP_457565559             377 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caldithrix
            abyssi].
ACCESSION   WP_457565559
VERSION     WP_457565559.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..377
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42361
     Region          54..375
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkalkmisiv tvllalfaac tttenqqeae napaenqiii taeqftssnm elgkitlqyf
       61 seriratgmi dvppqykadv svyyggtvkd vrllagqsvk kgatlftlen pdyvqmqqdy
      121 ltaksrlnyl raeyerqkkl faenvasqkk ylkaesdyft vlsdfkalgq klrllnidpe
      181 sldynkvatf teikapisgy vtqvnitrgq flspnevavs ivntehlhle lkvfekditk
      241 ikkgqsirfr lpdndtdyye glvflvgqav yspertinih ghlknealss qfipgmyiea
      301 eilvneeqyp alptdavvnv esgnyilvkk sftnnqyifv qeavkigksn dgytqilnad
      361 rfgdaeilik gafnlih
//
LOCUS       WP_457565560             434 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Caldithrix abyssi].
ACCESSION   WP_457565560
VERSION     WP_457565560.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..434
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47409
     Region          4..429
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkpskklsll evismavgtm igasifsifg lgakiagqnl peafmlsafy alivaysyai
       61 lgskiisnag piafilkgig dniitgalsi lmwltyivsi alfvkgfagy flpffhitvt
      121 pvsmaiveif visfftslnf fgskavgkae fyivlikvsi llififggfl tihwlrvqpl
      181 ldtvhvsgmi nasiifflsy mgfglitnas eniknpernv plaiyisifi vmfiyvfisi
      241 vtignlplpd iikaqenala vaarpflgnf gfilisigal fsissalnas ifgganiaya
      301 laksgelpks ferkvwfqst eglyftsgla ltaalfldlg aiasitstif tviyifvlys
      361 hlklykqfgg nrfiigfnli vllivfsalm nyqwqtnkaa ffisifaflg aglleyayrr
      421 ftnrkirhkg iaps
//
LOCUS       WP_457565561             392 aa            linear   BCT 27-JAN-2026
DEFINITION  exo-beta-N-acetylmuramidase NamZ family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565561
VERSION     WP_457565561.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Muller,M., Calvert,M., Hottmann,I., Kluj,R.M., Teufel,T.,
            Balbuchta,K., Engelbrecht,A., Selim,K.A., Xu,Q., Borisova,M.,
            Titz,A. and Mayer,C.
  TITLE     The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the
            founding member of a family of exo-lytic peptidoglycan
            hexosaminidases
  JOURNAL   J Biol Chem 296, 100519 (2021)
   PUBMED   33684445
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..392
                     /product="exo-beta-N-acetylmuramidase NamZ family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0033922 - peptidoglycan
                     beta-N-acetylmuramidase activity [Evidence IEA]"
                     /calculated_mol_wt=45218
     Region          1..392
                     /region_name="YbbC"
                     /note="Uncharacterized conserved protein YbbC, DUF1343
                     family [Function unknown]; COG3876"
                     /db_xref="CDD:443084"
ORIGIN      
        1 mvqtgldvli aedfallknk kvgllcnqas iasdfrhaie rfkeghqkgr felkalfgpq
       61 hglfghtqdn miewegyvdh ysgatvysly gehrkptpqm lenidvlavd lqdvgaryyt
      121 fiwtmalcme acsennvqma vldrpnpigg rqvegpwlnm dfksfvgwhp lpvrhgltig
      181 evaiylkerf ypavqlkvvq lknwrrsmyf detglpwgmp spnmptvdta vvypgmclle
      241 atnisegrgt trpfeifgap wmdhwqfsar mnelglpgvh frplefqptf nkyqgevcrg
      301 cfihvydrsk fkpflttial lretiqlygs ffqwknppye yeyhkmpfdi lvgndwlrpm
      361 leqgaplsem evkwqnerap hsseieearl ye
//
LOCUS       WP_457565562             234 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565562
VERSION     WP_457565562.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26041
     Region          2..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miqvqnlslf yeelqalnav hltlkpgvic glagingagk sslincllgl isefegqisi
       61 nghdvrkdrs wikshcgyap eetelfdylt gleflqlias vkrlsqpqka ikslselfdm
      121 adflpmliag yshgmrqkml lsaalmgepd fifideaing ldtlsllrlk kylqtlkgqg
      181 ktvviashvl pllvdwcdei lilhqgrllk tlvrnemqnd drsieqifme iigq
//
LOCUS       WP_457565571             375 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565571
VERSION     WP_457565571.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..375
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=41377
     Region          16..367
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mhmqakklpg lkigrfnlpt piiqggmgvg islsglasav aneggvgvis svglgllfse
       61 eqlnyrkanm hflrheirka rqmtngvigl nimvalsdfd nmlqiaieee vdivfmgagl
      121 plrfpknytp emirnfktyf vpivssaraa qlifqywgkt fgripeavvv egpkagghlg
      181 fkreqiddpq fqleklipev vdtvkvfeer fereipviaa ggifsgadil kflelgasgv
      241 qmatrfvath ecdasedfkn ayvqskkedi viidspvglp graiknsflq evkegqkkpf
      301 kcswkclktc dfrttpycia dalanaqrgm lekgftfags naykvdkivs vnelfltlek
      361 eylqavkarq pqavy
//
LOCUS       WP_457565572             454 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457565572
VERSION     WP_457565572.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 454)
  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 454)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 454)
  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 454)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..454
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=51552
     Region          20..445
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 myhilaiddd lnflddlssl lkfhnyvtrg innphkalsl lnkdkfhcvl ldvqmpgmdg
       61 islleqikek hptipvimis gqstlaiavk aikqgafdfl ekgadldrll itlknaiahy
      121 nwlkerrlli nellenyqmi gqskamqqif nqidfvaptd skvlitgetg tgkeliarai
      181 qlksnrstrp fvrincaaip etliesvffg hkkgsftgai kdqpgkfela dggtlfldei
      241 gelplyaqak llnvlqdgei ekigaqktqk vdvriiaatn kdlmtmikek kfredlfhrl
      301 nvfhihvppl reriddvppl vehyikhyan elnkkivgis pagmnilvqy dwpgnvrmlr
      361 nvvsravmfa qsnvisegev slaldmdryq plfaqntmtl aeflefqerq flrqmlilcn
      421 gnkqqmaqrl gvdratlwrk lkrynlsmad eqsq
//
LOCUS       WP_457565574            1046 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Caldithrix abyssi].
ACCESSION   WP_457565574
VERSION     WP_457565574.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Putnam,A.A. and Jankowsky,E.
  TITLE     DEAD-box helicases as integrators of RNA, nucleotide and protein
            binding
  JOURNAL   Biochim Biophys Acta 1829 (8), 884-893 (2013)
   PUBMED   23416748
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Flaus,A., Martin,D.M., Barton,G.J. and Owen-Hughes,T.
  TITLE     Identification of multiple distinct Snf2 subfamilies with conserved
            structural motifs
  JOURNAL   Nucleic Acids Res 34 (10), 2887-2905 (2006)
   PUBMED   16738128
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1046)
  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 18766567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1046
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=121009
     Region          2..526
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
     Region          409..1026
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mkfdldllqr etgitvfnkg knyfktkrvk iiqatsdrve sfvygmheyk viiqqkdsaf
       61 yvecncpyfv tsdrickhiv atifeyeqlr dekinvvaea aswqalippe esdikkksrn
      121 rvafvlsffp tswqikpvlr yikkdgtlgr evnfnlqyfs aydfetnpde lmalgflsgl
      181 trisnsigfm ygseygqilh ylrdslllyn fnswenipis flkepfdlhf siekeedqyv
      241 fklflktang dqkimvndqf lllsseriyf fydmkiwpvk qkisahlllp fcnaenglii
      301 pekempqflk dvypqfleak aetelpdsvq ltvmdslvkk alylsevegn lhisvsffyg
      361 gqqediqpik vdalpfkkht mllqkkqyil iarqeevenf ylniltehrl vrqenefvla
      421 kkvdaldwlf dtipelakkg feiygeekld klkvrraaar litqvssgtd wfdlnveidf
      481 dglrmsyqev vkalrknknf irlsdgsaak igqdtlnkia liktfgsrsk rdgtvrlskt
      541 qallideiln dsaqaeadqa frdhlkklks fkairpvelp knfrgelrpy qkagldwlvf
      601 lneyglggcl addmglgkti qalallqlqk eklkknlvsl ivaptsvltn wqneaarftp
      661 dlkvylhagl ereknvrhfe qfdliitsya llwrdfdllk eisfhyvild esqkiknpqs
      721 vtaraayrlr ashrlvmtgt piennlaelw sqfqfinpgm lgalkaftth fgkaiekqgd
      781 qekaeqlrrl iypfilrrtk dmvakelppk venilfcdms dqqqkayekw rdyyralilk
      841 tinekglnrs kmkvlegltr lrqlaihpam vennhksdsg kfyalhdile evikenhkvl
      901 lfsqfvkalt lvrqgldqrs ipylyldgst knrqklvdkf qnnskikifl islkagglgl
      961 nltaadyvih ldpwwnpave aqamdrahri gqskkvfvyk mitrgsveek ilalqqrkkn
     1021 laeqlittda affknlekdd ivqlfs
//
LOCUS       WP_457565579             516 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565579
VERSION     WP_457565579.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 516)
  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..516
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..516
                     /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=59338
     Region          288..511
                     /region_name="AmiC"
                     /note="N-acetylmuramoyl-L-alanine amidase [Cell
                     wall/membrane/envelope biogenesis]; COG0860"
                     /db_xref="CDD:440621"
ORIGIN      
        1 mfrrkflkki sygiglalfn plhwlraqer sllkiekdgr iigqipfllk qnqcyikltd
       61 fadlnhlgqf tntsrrktll imdqakfkft hdnsfvvvnd ralqilyapf wkegalwvav
      121 aelvelinef tqyhlqfddv hkllrftvrn initsiqieh ksngtlialn atrsfaaddl
      181 ktkmvngwly leivggrgee kalsrkinds tvreiraaql dqllsigfhl kkepqayeal
      241 yddvngqill tvhektiqkd npektddaqt qsideelerq ksewmihtiv idpghggkdp
      301 gavgyyklke kdivlsvgll lgdylkkrlp gvkilytrdr dvfiplwkrt kfanenqgrl
      361 fislhcnssk srrargfety flsaekdeka revvltenes ikfetahdqk ryeginfvla
      421 tlaqnafiky sqylasvvqk mlrkflrplg mkdrgvkqgp fwvmvgatmp nilvemgyiy
      481 nkneakllrr kstqskiala laegivkfkn dfesal
//
LOCUS       WP_457565578             286 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565578
VERSION     WP_457565578.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..286
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31050
     Region          1..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkigfiglgi mgsrmainli kngfslivfn rtrekaqpll eagaewaesp aelakkvdll
       61 itmlstpeav eqlalgengf lnhlphggtw mdcttvnpsf srkmaalaee hhirfvdapv
      121 agskkpaeeg qllflvggkr edvvfceplf kamgkkhlhv gpsgqgaalk mlfnlllgea
      181 mlafaealam geklgfertq lldilldapv tapfvagkrq kiesgvydae fplqwmqkdl
      241 qlasltayeq slalpalnvi kevfalakqq glaekdfsai faylnk
//
LOCUS       WP_457565586             318 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caldithrix abyssi].
ACCESSION   WP_457565586
VERSION     WP_457565586.1
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 10508826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..318
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36924
     Region          12..278
                     /region_name="LPG_synthase_TM"
                     /note="Lysylphosphatidylglycerol synthase TM region;
                     pfam03706"
                     /db_xref="CDD:461018"
ORIGIN      
        1 mkeqikqklt fvfkyfigla lliwilarvd rqqmiqtlle irpatfalif vlvflnlwiq
       61 frrwrylieq qssdfsykdl ipsffagftf rlilpgghae iskifllpgk krgkvmafai
      121 ekffqtyvkt ilvlaglpfl faqfkwlfws aaillivayp ffplllktrw lqkfqekevh
      181 yhkiflrali fsvgvflclm lqyfillnda hqidfnatfl tviyiwgagl ipvsvsglgv
      241 reniaafvlq kygipastav gisllifiin aiipaligvf fiyrrqhhfk daretfkvvs
      301 sqiynhgkkr faknkdtd
//
LOCUS       WP_457565589             256 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Caldithrix abyssi].
ACCESSION   WP_457565589
VERSION     WP_457565589.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..256
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28247
     Region          3..254
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkilvvagq kggigktttv vnlgaslaif nktvllvdld pqgsvgisfq ldeyhvklgm
       61 ydvivnnmal snaiinsgld tldiapmnvr neemeielys ralkidlvkt iltpvrnlyd
      121 fiivdcppnl gamtlnglva adeviipvls eyyslkslgk flntlknisk kynknlkigg
      181 ilvtmydarv rkqkeimeyl rstfkelvfk sfiprnskvs eapsvgkpvi lhdirsrgal
      241 sylklaeeii eknnkn
//
LOCUS       WP_457565590             330 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Caldithrix abyssi].
ACCESSION   WP_457565590
VERSION     WP_457565590.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..330
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=36647
     Region          212..330
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mekfyirsqd ieqkihsvkl pylawkvlfl lgekqsvaal aeilgddeqt iegalktlid
       61 eqlaveieae apsekaeeka eileetpepa vpeieeeeee aeaapeqeev vseeapveip
      121 eakekeesdl seieeeesft giedfdipgv eeelveeses disevesdie lpqleeetek
      181 ldfdfenmee pavaeaekae ekeeeketkp agaptllvid dsivirkmve lalegedlil
      241 etatsgkegl kaldevkpdv vvldlmlpdi ngidllktik aslnipviml sgkdspqmie
      301 kakaegadaf lpkpfrdeel vktihellqk
//
LOCUS       WP_457565593            1029 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457565593
VERSION     WP_457565593.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1029
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114250
     Region          1..1022
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mklveisikk ritlsmiyli iigfalfsfs qlkvdlfpdi dfpvvgiite ysgigpqdme
       61 nlvarpieea vsatknvkkv ssqvsqgvcl tllefdwgtd idkaendvrk ridlvrdflp
      121 eeasepltfa fdpsmmpinf ilinsptmgp aelrqlgedr iepllerveg vatvetqggl
      181 erqinvrldp vklaahtlsp vdvvrairsa ggllpagsie tsttnfnlhi asefksldrl
      241 kqvvlkyerg rplllkdvat vedgfkelrs dvrvnynqgv ymrvfkqsda ntvqacrnvr
      301 qaveemkefl pedvelkivy dqsdyilrsv gnlgdtafla fiiafaviyf flrnfrgsii
      361 mglaipvsvi stfavmmlan ltlniismag lalaigmlvd nsivvleniy rhremgqers
      421 aaanngasev amaitastlt tigvflpvlf vpgiagelfn dmvvtiafsl faslmialtl
      481 vpmlsarllk teaemtrirl arfknwvtrl lqrltqryma llrwalrhks vviglttvlf
      541 ltslslinfi ggeflpksdq gfialtilre kgtpldqtrk tvlqleniik qdipeasdvl
      601 aifgsgegif alfggagsea inlrirlspm eersrsqmei edalrkrldq ipgityqiiq
      661 qgmistdrai evkffgydlh qakqlaeqlk ekmekipglv didlnmkegg qeiriipdvr
      721 rlndlklspl lvadiistai qgkvaarfre sgdeydilvq ldrpfrnske slrhlliptf
      781 sgkmipleqv ahieetdaps tiyrenqerf vsvgcelsdi dlssavriir slidelnvpa
      841 efqvviggta edqqesffyl tiaffaaill vymimasqfe slldpfiimf tvplsiigvl
      901 walfitgttl svmalvgivm lvgivvnngi vlvdyinqlr qqgkglyeav eqggqvrlrp
      961 vlmtalttil gmvplalevg sgsenwapla raviggltts tlltlvivpv myvifeqvgd
     1021 kvrvwwekl
//
LOCUS       WP_457565594             338 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit, partial
            [Caldithrix abyssi].
ACCESSION   WP_457565594
VERSION     WP_457565594.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..338
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          6..337
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 vsvlvikpds irtfieitgs lqasndalvy srlseevkei vkpvgskvrk gavivrldds
       61 mvlqakkqae aalasarary qkvkqdfery qrlykqqais qqqwqqmqaa mqeaeaalrq
      121 mkanlaqvse qfehslikap fdglvgsvyf dvgqmaaagq pvvkiinpdl mkaklyipds
      181 yyhrlkvgqk vyahfpaqag keftgqiiri draidptsrt vaveaifcnd qglltsglyg
      241 lfkielqvrr rtvvvpdnai lsqtsvrvdp qtgkptahrk yyafvvkqgr aaqtevrtnl
      301 sagdrievvq glsfgdsliv vgqrmikdgq ktkvveay
//
LOCUS       WP_457565605             364 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caldithrix abyssi].
ACCESSION   WP_457565605
VERSION     WP_457565605.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..364
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40444
     Region          8..356
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 msdlrplkia mltsfpldlt vgsgvvrmil gyaaafqkag hhvqifhpsf rsdsylklal
       61 qrlkfnrala eqrfeafdli igsdfdghal krltapkvvl nagiladiir fergkiaril
      121 qhlarrecqn vqsaaltvvp shytarrlhq lyktpasria viplgidleq wrqwknacqp
      181 lslketvils varqyprkgi kdlilafkkt varvdnvrli vvgggpqaea nrslarqlnl
      241 tgkitfvgdl kdqtqlagyy rsahifclps yhetfglvfl eamyfglpiv ayastaipev
      301 vnpeqgllcp pgdidslsek lltligsakl rnkmgasgke rvkqfswqns aaqllkranf
      361 fgnr
//
LOCUS       WP_457565606             464 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Caldithrix abyssi].
ACCESSION   WP_457565606
VERSION     WP_457565606.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 464)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  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 464)
  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 464)
  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..464
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..464
                     /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=51702
     Region          22..456
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mssrlaldil pllvylillf rvglrarrsn adekefllsg rqltipafva tlvttwyggi
       61 lgigefvyss gvsawlvmgl pyyvfallfa lflaprirka envsipdmmy rmhgkrvgai
      121 sglfvvlmts papyilmlav llkyflhwpl lpaivvsavi svsyvywggf rsvvqtdklq
      181 flfmfggfll lvfflafkvl ppahlferld aqhlsikgnl swqqivvwfs iaswtfidpg
      241 fhqrcaaars pqvarrgili sivfwalfdg ltllsglyaf allpgiepil aypalasqyl
      301 ppflrglffv glfatimsti dsytflsaig igrdliwemq kkksadankq vrfglivtgi
      361 iavfmaysip svvelwyslg slfipplifp vlgafwkklk ipssyfvtmm vgsfliglal
      421 fiwgrlqavd gqavypfgve pffpafafsl avlligkitr naer
//
LOCUS       WP_457565607             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457565607
VERSION     WP_457565607.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..411
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46109
     Region          13..411
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 maninaffsh iseylimawq alvshklrsf lttlgiligv ttiisiwtti eglnqyvfgq
       61 lsnigastvy vqkypwvikg dfwkyrnrkp itykeyqalm ehctlaehis peifaaknir
      121 ykskkfenif vigtseqyaf tanvapeigr flteldvynn ryvcvlgrev adrlfdkenp
      181 lgkkifigdr kylvvgvler kgnffgqsmd nfvivpfgtf rrvygghrel rialltkpek
      241 lenmkdqirs ilrrvrkvhp tkeddfsinq qdmltdlyks ltttlfaivf viggislvvg
      301 gigimnimlv svaertreig vrkaigatrr nilsqflfea ivissiggli givlgfiags
      361 lilaqmnltg gvsltsvlig fgfsgfvgvt agfypaykaa rlnpidslry e
//
LOCUS       WP_457565608             252 aa            linear   BCT 27-JAN-2026
DEFINITION  Yip1 family protein [Caldithrix abyssi].
ACCESSION   WP_457565608
VERSION     WP_457565608.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shaik,S., Pandey,H., Thirumalasetti,S.K. and Nakamura,N.
  TITLE     Characteristics and Functions of the Yip1 Domain Family (YIPF),
            Multi-Span Transmembrane Proteins Mainly Localized to the Golgi
            Apparatus
  JOURNAL   Front Cell Dev Biol 7, 130 (2019)
   PUBMED   31417902
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10522553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..252
                     /product="Yip1 family protein"
                     /GO_function="GO:0031267 - small GTPase binding [Evidence
                     IEA]"
                     /GO_process="GO:0016192 - vesicle-mediated transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28347
     Region          34..247
                     /region_name="Yip1"
                     /note="Yip1 domain; pfam04893"
                     /db_xref="CDD:461468"
ORIGIN      
        1 mdeslnnqnn qqepmpasev epaapklslw qqlvkvfsdp vnffnhlrsn ptwlfpflli
       61 vlmsivftaa tkdqmleyrk qlildsdkmt eemkdmaleq lenmtptayy iqsvvgsvig
      121 saivfaiaag lfllagnffl ggkatfkqmf alyvwgnivs lvempvkmil ilqknsaevy
      181 tslallmdpq qsdtvlfkll navdiftiwk iilwsigfgi iyrfsakksy ltvislyviy
      241 vlisvglgrl fv
//
LOCUS       WP_457565613             230 aa            linear   BCT 27-JAN-2026
DEFINITION  Na(+)/H(+) antiporter subunit B [Caldithrix abyssi].
ACCESSION   WP_457565613
VERSION     WP_457565613.1
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 10014005
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..230
                     /product="Na(+)/H(+) antiporter subunit B"
                     /calculated_mol_wt=24619
     Region          3..229
                     /region_name="PRK12567"
                     /note="putative monovalent cation/H+ antiporter subunit B;
                     Reviewed"
                     /db_xref="CDD:237140"
ORIGIN      
        1 mikrvvsfmv llgfafifgk mlinwlpmse lngvarayve repqelgavn vvtaivvtyr
       61 gldtlgevsv lflaatgval llrrrknstq nkenkrpase flktgssllm pfivmfgvyi
      121 finghlspgg gfqggavias amllmlltfp dyrlnhtvlg wvesasgvsy vlvgvlglll
      181 aggfldnril plgtygails agaipliyvf iglkvgaela gvlenlkqeq
//
LOCUS       WP_457565615             485 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565615
VERSION     WP_457565615.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 485)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 485)
  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 485)
  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 485)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>485
                     /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]"
     Region          1..470
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 malidiiivi afllltffvg sffykwvgep ddfyvagrkl tpfilaavit atnvnlysfv
       61 gqagiaykhg isilwqtwtg nmalvfsglf iipimrrlrv rtipeflsmr ynksvrllvg
      121 ilwvfrlafw lgvvlytavv aaqaitgits ylfwivafai iaiiytmlgg mwsvaftdvi
      181 qfvfmlggal ivlpmamkav gwmpgliekl penslqlvrq sgtynwkfil aifllgiqwa
      241 svdqgllqra fgaestktva kgmvlagiit tpfallwnlp glaaavlypn lqnpdqaipt
      301 llsqmlppvi lglvvvglls sqlstisgnl ngvatlftnd iyetlkkrqa tnkeilfmar
      361 fitflvglfm igfaflvpkm ggaveaylti igimdmplfi vgilygllwk ratsagairg
      421 ylagaaagii gkfyfqfdfn lttflsavta llvmplvsyl trpenkekie iiwkarrtsa
      481 eeeas
//
LOCUS       WP_457565617             680 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 36 protein [Caldithrix abyssi].
ACCESSION   WP_457565617
VERSION     WP_457565617.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 680)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..680
                     /product="glycoside hydrolase family 36 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016052 - carbohydrate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77308
     Region          290..591
                     /region_name="GH36"
                     /note="glycosyl hydrolase family 36 (GH36); cd14791"
                     /db_xref="CDD:269892"
     Site            order(295,325,365,432,436,484,502,505)
                     /site_type="active"
                     /db_xref="CDD:269892"
ORIGIN      
        1 mriffllivf ltfvscqkqp titneflkie fnpllhsrvs aladqsrplm dtfqpaeqli
       61 lqdrridafs lqqfksgtfq dsigagkelk ltgifedsal kiekqvyikm ydqfpqmavf
      121 qvryknlggq pllvegwinh rytllpeqkt tpsywsfqaa syperpdwvl pvergfyken
      181 yqgmnasdyg ggipvvdlwr tdaglavghl altpklvslp vrfdstaega tlaitskrrl
      241 slqtgesftt lptfltvhrg dffrplqsys qmmqkrglkf kpypetayqp iwcawgyerg
      301 ftveqiegal pkvkevgldw aviddgwqta egdwflhpkk fprgdrdmra lvdrihamgl
      361 kaklwfvpla adpgtrllke hsdmlllned gstqlitwwd syylcpayep trqyfkglit
      421 kiikdwdfdg lkldgqhqna vppcynpahn harpeeavea lpaffdmiyq taisikpdav
      481 veicpcgdaa sffnmavenq pvasdptssw qirlkgkahk almgpqapyy gdhvelsdgk
      541 ddfastigig gvpgtkfvwp pesyfnketg higltpekek iwkkwislyk kyqlakgqyv
      601 gtlydlgydr peahviqkgd tlfyafyadd fngtielrgl pakktltvyd yenaknlgtv
      661 sserpflkaq fkkhlliyvk
//
LOCUS       WP_457565618             604 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565618
VERSION     WP_457565618.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Rocha,S.T., Shah,D.D. and Shrivastava,A.
  TITLE     Ecological, beneficial, and pathogenic functions of the Type 9
            Secretion System
  JOURNAL   Microb Biotechnol 17 (6), e14516 (2024)
   PUBMED   38924452
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Gorasia,D.G., Veith,P.D. and Reynolds,E.C.
  TITLE     The Type IX Secretion System: Advances in Structure, Function and
            Organisation
  JOURNAL   Microorganisms 8 (8) (2020)
   PUBMED   32752268
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Lasica,A.M., Ksiazek,M., Madej,M. and Potempa,J.
  TITLE     The Type IX Secretion System (T9SS): Highlights and Recent Insights
            into Its Structure and Function
  JOURNAL   Front Cell Infect Microbiol 7, 215 (2017)
   PUBMED   28603700
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16073716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..604
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=66436
     Region          526..598
                     /region_name="Por_Secre_tail"
                     /note="Secretion system C-terminal sorting domain;
                     pfam18962"
                     /db_xref="CDD:436869"
ORIGIN      
        1 mrfvliilsm ttfllaqtfs vartsattit qsvnaslnpq klliyygwps mingatnnqq
       61 aadtlgqydf vvlgdglekt shgdhantve iinlihasys trifgyidag vttqnlslse
      121 igirikewka tgadgiffdd fgydfqtsre rqnavidsah aqgmpvcvna wnpddvfsse
      181 vdanfnptge pthlsaddfy lsesyqieag nyqseatwqs kadkldayqq sigfgiwsvt
      241 tnnsaniydq hqfhyawhsa llyghkatgw geylfssnnn sapfrprpvv dsgsafltav
      301 qhnnpqhsre tntgliwirt ddhsygfsss sitidgnfsd wagvgsyvtd pqgdysdanl
      361 dlltgyytyd astlflrtdv agayyatant gdgyhiyidt dknaatglny gwwsmgadym
      421 ieqvsgsapn lyqytgtgsd wswsfvgsvs eahsgassem avafsdlgvt tgdeiyiqwa
      481 ssaawsdqdy mqddlggsrt pavlgttsav enadlapqdf vlkqnypnpf ngttvieyrl
      541 ksgaavhlal ydvngrllkt lvdayqpagq hrvlidmnhl asgvyfyrlk ikkqqatrmm
      601 ifnk
//
LOCUS       WP_457565623             393 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Caldithrix abyssi].
ACCESSION   WP_457565623
VERSION     WP_457565623.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 393)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..393
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45741
     Region          62..374
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mkivfknfsl fltllllfaa csnksgdegk sepplsetll lndynpqsiy riprtevkra
       61 rypiidihsh pyaqseqdie rwlqimdeag iektiiltcs ygeafdsiaa iyskygdrfe
      121 lwcgfdytgy dqpgwaekav aelercvrmg argvgelgdk glgmyysnlf arrpgtkakg
      181 mhlddprmdl llkkcgemgi pvnvhvadpi wmyqpmdstn dglmnaytwr ikkekgillh
      241 dqlinmlena vkrhpnttfi achfanlsyd ltrlgkllek ypnlwadnsa ryaetatipr
      301 fvrafyqkyq drllygtdny fdphmyrvtf riletadehf yeknlfnyhw ayygfdlpda
      361 vlkklyrqna lrllqqrdek lkrylkkaei anh
//
LOCUS       WP_457565624             270 aa            linear   BCT 27-JAN-2026
DEFINITION  class II fructose-bisphosphate aldolase [Caldithrix abyssi].
ACCESSION   WP_457565624
VERSION     WP_457565624.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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   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 270)
  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..270
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..270
                     /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=29319
     Region          5..268
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mhtslkqalq ngqtllacnf ynletlqgvl qaaaemqrpi ilqltassie ymglqtavnm
       61 artaikesga qawlhldhaa spelvlrcle agfdsvmida sdrpfeenla vtqkvvamar
      121 pfgalveael gyvaklgqst ektgftephe aaqfveqsgv dllavaigsa hgfykqtprl
      181 dierlkairq atpaalvlhg ssgipveqir aainagiqki nlateiknif mqtlkktlkt
      241 tdeidlrkvf paarqevtql vknkmealdl
//
LOCUS       WP_457565626             319 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Caldithrix abyssi].
ACCESSION   WP_457565626
VERSION     WP_457565626.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..319
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35174
     Region          7..306
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mgsvkydviv vgelnvdlil nkidgfpemg kekladqmtl tlgsssaifa snlsalgarv
       61 afigkighdq fgqltldslq kkgvstefii qdknlntgat ivlnyeedra mithpgamnh
      121 ltiqdisaeq lkqarhlhfs syflqpgikk dvgqlfrmar elglttsfdm qwdpeekwel
      181 daanilpyvd iflpnrqelv yltgqvnlke avhklganin tvvvklgneg shlfdvrakk
      241 eirlpafkne qvvdaigagd sfnagfifkf iqgapleecq rfgnlcgain ttaaggttaf
      301 rnfdqvmkia kerfgyeek
//
LOCUS       WP_457565634             473 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 125 protein [Caldithrix abyssi].
ACCESSION   WP_457565634
VERSION     WP_457565634.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..473
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54085
     Region          32..471
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 merrqflkag sffmagavvg lpdwlearsf ksqrpvpakr kfssqaveqt iqqvkadivd
       61 qevawmfenc fpntldttva fseregrpet fvitgdipam wlrdssaqvw pylklakede
      121 slkaliagvi nkqvnfilld pyanafynep klgewakdlt emkpgvherk weidslcypi
      181 rlsygywqvt gdvsvfddnw kkaalsiyrt freqqrlesp gpytfmrvtd ratdtvplqg
      241 ygfptrkigl ihsmfrpsdd acifpflvps nwfaaqslrq maeifnavwn dtewaarfsd
      301 fadeieallq khavvehaah gpvfayeidg fgnhlfmdda nvpgllslpy lgavdrkdei
      361 yqntrrlils adnpyffkgr agegiggphv aldyiwpmsv imraltsdde keiltclrtl
      421 kkthagtgfm hesfqkdnpq kytrswfawa ntlfgelilt irekhpdllk rei
//
LOCUS       WP_457565638             448 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase, partial [Caldithrix abyssi].
ACCESSION   WP_457565638
VERSION     WP_457565638.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20661115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>448
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          36..125
                     /region_name="DUF3887"
                     /note="Protein of unknown function (DUF3887); pfam13026"
                     /db_xref="CDD:432940"
     Region          160..448
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mhklifaliv wlmvgagvqa qkvepsdewq kpialaaqfi dlleqaqfds avgymdanms
       61 kalpaeklra mwqslqqqmg nfkarsgvrt etvqvyrvvy vtcefekgkl dakvvfdqqn
      121 kigglffvph qqaqgwqppd yvdthaftei dtlkipttwq lpaslslpng pgpfpavvlv
      181 hgsgpndrde tigpnkpfrd lawglatrgi avlryekrtr iypnivdslh gqftlieetv
      241 edalagvsfl rdiveidpek iivlghslgg yaipriaryy prlagfiima gsarplpdll
      301 qeqyryifnl dgqitaeeqv klqeldslva lirnetflkk adptqlilga ppaywldlmq
      361 ydplkmierf rkpilvlqgg rdyqvtkrdf dlwkkhlkhn pkatfkyyyq lnhlfmsgeg
      421 matpqeyekp ghvdkqvied iatwiksh
//
LOCUS       WP_457565641              76 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565641
VERSION     WP_457565641.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..76
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <1..76
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 ssllnyvqnl egrlliihgt vdpvvvlqns wlylrkaidl qkqvdyfvyp gdehnmlgqd
       61 rvhlyqkisd yflehl
//
LOCUS       WP_457565645             841 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457565645
VERSION     WP_457565645.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..841
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          2..>227
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          <526..840
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 lllisvqllt aqnnnvvihq ldnglqvlli qnpalpmvgv nvavkvgsay etfatsgmsh
       61 mlehllfngt tsrtqkqlyd dvdrigaynn antgqyytny mmvvpaenik qalelqsdml
      121 fhsilpedkf ekekgivlee isktfadpda qlernlndil yeghalslpt lgtyatikgl
      181 vrdqvfefyk nfyvpnnmrm svignfdtae mlkmieefyg reepgqvllp efsdwsigfd
      241 rqhlktvqtg kviqrfyqge kpvvefifpi ngtfghiffr llderladka velnqrlgdl
      301 adrvemqtln spvadflevk ltlsvarpdv eklrqqvehf vaqmdfyssd eaiearanki
      361 ktgflknlek phmfgiynah liavlgfdqm lasfekenii ksarqlnqfk idgvpivvln
      421 lplkeskqdt qkiklvtklf kgqdgaptli irqnpasqlv amhylikhka lwqskygkka
      481 aqilhdcfaq rlkseqnlav sqkyglsvta ndnpyipmdd iylhpdfgyl riealnddlp
      541 glihflnsql kdfkptveef qkavvkfsrk ggmmsrrgdp akklfdqlld eqvyetlpys
      601 egpeeieyqs llefasnyfq panmiiavvs sekpeevkkw faefkgmpld qepppvtkki
      661 klhdrpveie klgngqrsyi fwgfvktida qdapplkvls lllgdkivfq irekqgmayr
      721 mraginvhnd ralfyvsqgt vpenvdallk qypsffnpqv iedfneeavi ksvnmflgrm
      781 mfrrlssinq ayylthsyyf hqninydedf lqalkqvtlk dvrrvaqkyl qvenpikiiv
      841 r
//
LOCUS       WP_457565653             403 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Caldithrix abyssi].
ACCESSION   WP_457565653
VERSION     WP_457565653.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 403)
  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 403)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..403
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=45167
     Region          128..396
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrgmlffliv igifvgitfl vrymarianr kiwqsslidr laffypygvl laiglilass
       61 sagrrhlmme vsttlafvlf vlsmalllal pltfiiyfvy ravfaaqqks kkqkqafsve
      121 rratlkwmtg avpllflgas argfagafnq vqtpqielhf knlpralidf kilhlsdlhl
      181 gyyfnlddle qlvatlsgqt fdlvvitgdc addikqlpda lqlidqipat hrkffslgnh
      241 eyfrglpqil kiidrspvel lrnrsvtlnh rgtllrltgi ddpvfmgrdi sdflqkaiqa
      301 gtanasplpf nillshrpqa ldfappfgid lvlaghthgg qlgfnrrslf enwnihkylw
      361 gpyqngatql ytsagvghwf pfrlgcppea piiilkndpd vni
//
LOCUS       WP_457565654             415 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Caldithrix abyssi].
ACCESSION   WP_457565654
VERSION     WP_457565654.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 415)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..415
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48175
     Region          16..414
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrfrlaisck fnsiarvyfi fwlifgfihf nlsvlhaqvg idgslnknrn llkelesqid
       61 elrqkilatq kkksslatqi qllehemali srsrgileqe irllqsrise senklretnq
      121 qledlqalya aravyaykyg rikniellls srslnqamvr lkhlrqiarh denlirtirn
      181 kkkqieqikr slekslqqkd malksleekt rqyvarkkek qrllsrikrn qanyqqlltr
      241 knreraslld liaalekerl kqekqtpdra spkksgvvfk fknfekargk lpwpvkgkvi
      301 shfgkkrdpv lktyvkntdi eikakpgspv rcvfpgvvrv iqylpgygnl vivdhgkgyy
      361 svyshlaeiy vywdspveqn qiigkvsdsg yngspslgfg iyshnkihnp ehwle
//
LOCUS       WP_457565655             374 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine desulfurase family protein [Caldithrix abyssi].
ACCESSION   WP_457565655
VERSION     WP_457565655.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..374
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41502
     Region          1..370
                     /region_name="NifS"
                     /note="Cysteine desulfurase/Cysteine sulfinate desulfinase
                     IscS or related enzyme, NifS family [Amino acid transport
                     and metabolism]; COG1104"
                     /db_xref="CDD:440721"
ORIGIN      
        1 mkriyldnaa ttpmvsevie amhewntrff gnpssvhhfg qiararleec rdiiadflgv
       61 pskkffftsg gtegnnwilk svatqltsek khilisaleh asvfetarfl kkqgadidfi
      121 epdgeglitv dqiqkvlrkd tafisimyvn netgiinpvk eiadfckknn iqfhcdavqa
      181 lgkvdfelqe mdvdfltvsa hkihgpkavg avyikepall epflhggqqe agtragtenv
      241 sgiigfaraa qwiasrrsqr dkvkqlqsyf eerlkelfkk vvviggdapr tpfisqvafp
      301 gvdnqnllmr ldlngiavsv gsacssgtlk psrvlqkmhl addvvrsalr fsfsylntme
      361 eiettlenlk ilis
//
LOCUS       WP_457565660             551 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase, partial [Caldithrix abyssi].
ACCESSION   WP_457565660
VERSION     WP_457565660.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Kannan,N., Taylor,S.S., Zhai,Y., Venter,J.C. and Manning,G.
  TITLE     Structural and functional diversity of the microbial kinome
  JOURNAL   PLoS Biol 5 (3), e17 (2007)
   PUBMED   17355172
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10196507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>551
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
     Region          13..275
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,75,91..94,98,100,137,139,
                     141..142,144,154..155,158,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,75,91..94,98,139,141..142,
                     144,154..155)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,98,100,137,139,141,158,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(154..160,162..163,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          395..458
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          490..551
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
ORIGIN      
        1 mnsqqfigkv fghfrilepa gqggmglvfk alnthldkiv alkmiapgls lnekllnrfk
       61 tearalarle nphivrisdl leangqwfiv meyiegdtlr drlkgkrplp lkevieiseq
      121 ilsalqhahs agivhrdikp snilltqdnl vkvtdfglak iqenslihth isavggtlyy
      181 mspeqvrslk etdhrtdiys lgitiyqmat gtvpfdpaqt dfdiretivr kplprpstfn
      241 pylppefdaf imkaieknpd drfqsavema qrlaelkekl kdklengrpa gseiddeinf
      301 dryafdikdd fsdvslapei pvektpppas peeddeeakd lsemsqltrm telvkskrlw
      361 lisllpilii lfiiylislp ppsgsvptqs avtmlslhsr ppgarvymng epigqtpids
      421 ltiqkgsial riekagfvsy dstlmvkggq hlaldiallr kaavkedakl aqtkplapvp
      481 qskpvsetrv tfnstpskad vyldnrhigq tplsyvlksg qtlnlrvrka gfkeltrqit
      541 vperqnwnln l
//
LOCUS       WP_457565664             404 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Caldithrix abyssi].
ACCESSION   WP_457565664
VERSION     WP_457565664.1
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 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..404
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44431
     Region          1..398
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 misiqeamer iwarlpekkk etldiseatg rvlahrvtaa epsprftnsa mdgmavrfed
       61 lqslpvelsi vgesragvpf qgivqngqav ristgavlpq gadtvipied cqveqsrvkv
      121 ltakkkganv rkkgeefesg evllasgttl fpehlallaa qgiqrvevya rprvvllttg
      181 sevksfkeei adyeirdsnl lmlgeaikla ggalvvsdrl pddfsltvqk lkeaqnkadv
      241 ivlsggvsvg phdhvkkaaa eagfsevfwk vnqqpgkplf faardntllf glpgnpvsaf
      301 msmahyvypv lrrlqgfddd ravcvarars rleinkkraq llrvrlektd egwhfiplkr
      361 qgshmitsis qadgyivvgp vetiekdetr nvylfpwrks yglc
//
LOCUS       WP_457565665             123 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator, partial [Caldithrix abyssi].
ACCESSION   WP_457565665
VERSION     WP_457565665.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..123
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          1..122
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 rgketillve deasvrhfae kalsnfgfki hsasngreal elvkksnlkp dllitdlvmp
       61 emngkelaik lqnlfpelkv iyvsgytddh ivqngllekg ihfvpkpysv eqlaskikev
      121 lqt
//
LOCUS       WP_457565666             441 aa            linear   BCT 27-JAN-2026
DEFINITION  3-isopropylmalate dehydratase large subunit, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565666
VERSION     WP_457565666.1
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 10000557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>441
                     /product="3-isopropylmalate dehydratase large subunit"
                     /EC_number="4.2.1.33"
                     /GO_function="GO:0003861 - 3-isopropylmalate dehydratase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
     Region          1..412
                     /region_name="LeuC"
                     /note="Homoaconitase/3-isopropylmalate dehydratase large
                     subunit [Amino acid transport and metabolism]; COG0065"
                     /db_xref="CDD:439835"
ORIGIN      
        1 mtiiekilar hagkktvkpg divdveidvr iardfggpnv vknlvengle iddpsktfft
       61 fdtnptgsdq kyaanqhfcr qfarekgikv fdinvgigth taieeglaip gatlvstdsh
      121 anivgavcaf gqgmgdqdia avwatgkawf kvppsaklil kgerpkgita kdivlnllhh
      181 fgangllgla vevqgeever ltlderitia smatemgaii llfepndevm aycekrsgkk
      241 iekitadpda qydqvfeldl stfvpmvsrp ghpddsvdit kigkvkidsa figsctngri
      301 edlriaasil kgrkvapgvv lkivpstdev wqqmmeesll kifkeagalv gnagcagcaa
      361 gqigqngpge itistgnrnf agkqgkgevy laspavvtas aiagyittpd qlperpvtfd
      421 elqatvfsyq akgkpqiqkr e
//
LOCUS       WP_457565667             702 aa            linear   BCT 27-JAN-2026
DEFINITION  S8/S53 family peptidase [Caldithrix abyssi].
ACCESSION   WP_457565667
VERSION     WP_457565667.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15411925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..702
                     /product="S8/S53 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76894
     Region          117..595
                     /region_name="Peptidases_S8_S53"
                     /note="Peptidase domain in the S8 and S53 families;
                     cl10459"
                     /db_xref="CDD:415849"
     Site            order(194,260,532)
                     /site_type="active"
                     /db_xref="CDD:173787"
     Site            order(194,532)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173787"
     Region          624..699
                     /region_name="Por_Secre_tail"
                     /note="Secretion system C-terminal sorting domain;
                     pfam18962"
                     /db_xref="CDD:436869"
ORIGIN      
        1 mrffvllfls vsllfaqyid pylthlskts lsktsepril nmivkgdeni ahalyqngfd
       61 vqsavgefat vrvpqqrind lltvkgikki fygvkskpln svavryqnvf sayekgytgs
      121 nviagiidtg idfyhpmfik ngqtrilaiw dqsldgnppq gysygtefte aqinqdlqsg
      181 spysivnhhd tdghgthvag sfvgadptat padtldggar dasivvvktt fqnadildai
      241 nyifdiaeqq nkpcvinisl ghqygphdgt ddfnsavqnl vgpgrivvra agndgakavh
      301 yfndtevsse sirflytdyl tlwlengdrl tsvslswssg sitnvtlngh ktssgidlyl
      361 ipgtahnngk iavyvfmdnn tlknetftlt lnglqdsngn nrivrhawad ssvfespyga
      421 fsqgtlygnn fypytlsnda cnplvvtvga fitraswpas ngytyhypns gdnggiasfs
      481 sigptgsegq kpdviaggai ilsarsqdas ygveflppap ytdhyaymqg tsmaspvasg
      541 aiallleknp dwgpnelfdy lhnhargtqr eagvtaeelk vkdnpntwdr vfgygaidln
      601 dafvtdineq stqspetfal fqnypnpfnp lttieyylpk tqrvtlriyn argqliqtlv
      661 egqqfkgtkk ivfnasnlas giyfyrlkte qgqltrkmvl ik
//
LOCUS       WP_457565673             101 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Caldithrix abyssi].
ACCESSION   WP_457565673
VERSION     WP_457565673.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..101
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11882
     Region          5..96
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(25,28)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mtlnefhell skhsivvgyf stescnvckv lrpqvqqice qfdivhfeyv diekapelrg
       61 qflvfsvpti iifvdgreyk rlnrymslqd fedelkrmva y
//
LOCUS       WP_457565680             115 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565680
VERSION     WP_457565680.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>115
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
     Region          6..115
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mdiprywrlr nqryhlqgak ceqcgqlyfp pravcpacks rslsayrfkg tgrvyshsll
       61 yqtsdrfegq apyvvaivel eegvrltaql tdvdvdevav gmpvemvvrk iyeeg
//
LOCUS       WP_457565682             481 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Caldithrix abyssi].
ACCESSION   WP_457565682
VERSION     WP_457565682.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Hvorup,R.N., Winnen,B., Chang,A.B., Jiang,Y., Zhou,X.F. and
            Saier,M.H. Jr.
  TITLE     The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter
            superfamily
  JOURNAL   Eur J Biochem 270 (5), 799-813 (2003)
   PUBMED   12603313
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Soldo,B., Lazarevic,V., Pagni,M. and Karamata,D.
  TITLE     Teichuronic acid operon of Bacillus subtilis 168
  JOURNAL   Mol Microbiol 31 (3), 795-805 (1999)
   PUBMED   10048024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..481
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53629
     Region          11..415
                     /region_name="MATE_tuaB_like"
                     /note="Uncharacterized subfamily of the multidrug and
                     toxic compound extrusion (MATE) proteins; cd13127"
                     /db_xref="CDD:240532"
ORIGIN      
        1 mqertlqqks vrgvkwqigt eilargiqla tifvlarllm padfgligma liftqlayvl
       61 fdmglsvpli qkkdlearhy qtafsvflll aivfytavfs aaplaarffk neqlisilrw
      121 lsvifflyal rgvaairltk qlrframgvl qlisvlvyga iaialalnga gvwsfvaaii
      181 gqelvltaaf llvlkewyap vlsrstlael tgfgatvfvt ritgylnvnl pnivigrwlg
      241 esalgfysvg yqlvdfpvqr isknilrvmf ptfskvqdnp qefnyfyqet lrglllavlp
      301 ifagmalvap efvnifygpn wqplipvlqi ltivglsrsl wtlssvvfla kgrpqtelki
      361 nlayfvslli vlslvyaagl qavvssvall ifsfmlvfll sslkmmkfsl kqwiktarap
      421 llgsvlmaip lwalkmqilm hlnmlprlll iialagllyv vsvllidrsl fsylrrimns
      481 k
//
LOCUS       WP_457565685             400 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565685
VERSION     WP_457565685.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45070
     Region          16..331
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mekaekqtfe vivvgagiag slaarllaqk gisvlllekd dyagktkacg glfdrsyfer
       61 fvgderiieq rirknifhlp wgdvtydcdq vtvkrrifdr hlaqeakkag avlmnrkkvi
      121 sfevkrpgev eatvkemgsd rlwqvrasii lladgphsva fqnpffkrql kkkywayaqv
      181 yevkgvalpr neahiyfspr lyrwgygwif pykkesnvgv gailselakr plkqklfefl
      241 rifpqtapll kgrpivdkkg gyipmwllnr lsddsqlvlg daggmvsplf gaginyamea
      301 aeacvpvvqn alksgdfsar alkaydleik krfgrelrkq malakiiifs khfgkllpvk
      361 ilsiiafgvk ysrwnkikil aypwlgrpmv gapnrgkasd
//
LOCUS       WP_457565693             291 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457565693
VERSION     WP_457565693.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..291
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32507
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 madlsyykki ildnfdkltk nqkkiaqfll dhpeeialss ieniaeklnv gkativrlaq
       61 tlgykgflel ktelsnklrd dlsptkkfkn alkthtdksd firtlatnem nniqktienl
      121 drdqfnkavr ifvsatnift mglgissfla eiasyylnrv tmrarafthg sltleeqiis
      181 lkkddallvi slppysyqti eatetaqykg vkivsitdki tspiaqycdv vfiaetnniv
      241 fintvgailt iiyslaagig lsdratslta lslfekvesd ygfdihsdff k
//
LOCUS       WP_457565695             433 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565695
VERSION     WP_457565695.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 433)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 433)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 433)
  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 433)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>433
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          2..>433
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mdvfrlfrql wpylmryrlk lflglifivi snliaivnpq ivrqaidylk gdiqtmrlfq
       61 yagliilitl vqgvfrflmr rtvivvsrlv efdlrnelfa rlqslsqnff qrtptgdlia
      121 rmtsdlnair svmgpgimyt intattmilv fvmmisisrl ltliallpip llvflvsyfs
      181 rqinkrysav qaqfaeistr vqenlagiri iksyvkekse lqdfnrinre yinkslhyvk
      241 vhaafrpmmm llvglsvvlt lliggrliis gtitlgqfva fnmylgmlvw psialgwvlg
      301 lfyqgvasmk rlnlifdarp divdapdvkk vtrlhgairf erlnfsyang ssevlkdidf
      361 qveagqvval igrtgsgkst iikliariyd apddsilidd ipikkiplkt lrehigyvpq
      421 etflfsdtir nni
//
LOCUS       WP_457565698             286 aa            linear   BCT 27-JAN-2026
DEFINITION  cell division protein FtsX [Caldithrix abyssi].
ACCESSION   WP_457565698
VERSION     WP_457565698.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..286
                     /product="cell division protein FtsX"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=31469
     Region          1..282
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 msfmftvkeg lkglgrarla tfltittvtl alvligffia lfinidrwvg ekrksieiev
       61 fleplisear aqkiagqlka lpgieqikfi skkaaaerfk kefgqdveav lganplppsf
      121 vlhlspahrn aqairsisrn iekiegvtev vyasgalali dryttiiyli lgglglvliv
      181 iiiilihnsi rliiyarkei ieimklvgat rafirrpflv eglfyglvgg mladgalwaa
      241 vylirsfiyp qmympdaiyg illalgvtvg fissqvsink hldsll
//
LOCUS       WP_457565703             237 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565703
VERSION     WP_457565703.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..237
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26696
     Region          33..227
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlrsllayvf avlhtlfcsl aaivfglfnp yskivdkiir lwargllkaa gvkvvvhgqe
       61 klrkdqpyif msnhqgafdi lagvvaipvt mrfiakkelf ripifahsmr tvgmipidrg
      121 nsaearksle eaartlqngv svlifpegtr trdgnikpfk kggfvlalks glpimpmvft
      181 gslnimrkns lklhkgtihv yfldevdtsq ysfeqrnell kevrkrivdf yetvrle
//
LOCUS       WP_457565704             544 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing response regulator [Caldithrix abyssi].
ACCESSION   WP_457565704
VERSION     WP_457565704.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 544)
  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 544)
  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   3  (residues 1 to 544)
  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   4  (residues 1 to 544)
  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   5  (residues 1 to 544)
  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   6  (residues 1 to 544)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   7  (residues 1 to 544)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   8  (residues 1 to 544)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   9  (residues 1 to 544)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   10 (residues 1 to 544)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   11 (residues 1 to 544)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   12 (residues 1 to 544)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   13 (residues 1 to 544)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   14 (residues 1 to 544)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13461630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..544
                     /product="GGDEF domain-containing response regulator"
                     /EC_number="2.7.7.65"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=62686
     Region          32..542
                     /region_name="pleD"
                     /note="response regulator PleD; Reviewed; PRK09581"
                     /db_xref="CDD:236577"
     Region          <342..543
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnknkikily ieddpdaral mgdilryqgy ayyeasrgle girlakkhkp dliiidlmlp
       61 dmqgsevtth lksqpdlksi piialtaaee edireyvlaa gcdgyiskpi ninefvfkie
      121 eflagkresv speferellq ryninlverl krkvseleql nknltklnqd liasreelar
      181 yndllfylna lanelrsled pqkmlrilpa kivegfaidr civfhydsde svispfslhg
      241 ninansenln fkmgrdllal lkeergllwv kdahqiknpl lkkiadtlns vsfvvgylke
      301 fgrkdisdsf viegeteeld aifdidekfl iyfdkcqtnk kfatyeiril rsflhtvavi
      361 fenmllfnql kklykiksee airdgltnvy nyryfvrelr kevartkryk tpfslimldi
      421 dffktyndlh ghlegdevlr aisrllilnt rstdivaryg geefviilpg ikkkeavtfa
      481 eklrrlikdy qfpdkvhivp csltislgva scpedsddpv nlvrladqal yqakqqgrdq
      541 vcvv
//
LOCUS       WP_457565707             323 aa            linear   BCT 27-JAN-2026
DEFINITION  2-hydroxyacid dehydrogenase [Caldithrix abyssi].
ACCESSION   WP_457565707
VERSION     WP_457565707.1
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 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..323
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=35594
     Region          6..312
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(11..12,14,55..57,77,105..106,109..110,112..113,116,
                     120,122,130,132,134,136..142,144..148,166..167,170..171,
                     269..270,277,283..289,291..294,296)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(56,78..80,103,240,287,290)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(79..80,107,156..160,178..180,183,210..212,216..217,
                     238..240,264..265,287,289..290)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mnnrfkvfvt kkipqagiql lkqkgyqvtv hhgdipisrt elekavaeyd alicllsdti
       61 dkeilskark lkvianyavg ynnidvqeaa krkifvtntp dvltaatadl twalilavsr
      121 rvveadrflr kgrfkgwepe lllgmeikgk tlgivgagri gqavarrapg fglnivyyst
      181 qskpafeeet narylsldel vtvadivslh cpltpqtvhl lnkerifamk kgailintar
      241 gpvvdeealv aalkkghlfg agldvfehep evhpellkln nvvllphigs atvetrdema
      301 rmaarnvisv lekneavnpv nff
//
LOCUS       WP_457565705             636 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Caldithrix
            abyssi].
ACCESSION   WP_457565705
VERSION     WP_457565705.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..636
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=73272
     Region          214..635
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mstrkiletv fvytialilf vvfdlllnrf tespfltftv tiillllfqp yllrflkkil
       61 lpktyflttk aqrileklnn dlnhathfne vasllyqafd elfseqafif yiveedkyyp
      121 ahyhnvtdke llafdlkseh legiplqtlh ikklektqlp refiriahen nlnslfafrg
      181 hnqifaflli npeqifffhe aeawkifeki qkkaglilen talivdlrnr nyqmrkllev
      241 ghkilssfdi kqildfilsv srqvahydaa aiflfdehsg elknisydgy dpaiienlhl
      301 kigegsigwv vanktidvid dvrksdhyyr lrdetlsqca iplifdekvl gviclesdrl
      361 sffnehlvel lqlfgqmaai aihnanqfkv mlekqalehe linaghiqka llvqrfprik
      421 gldisavnip skivsgdlyd iiqydeftvg laigdvsgkg apaaitmala laglrsqrqf
      481 fmtscdivyr lnnllyessv egnyvsffya lvstqkkkii ftnaghnppi llkndgqivw
      541 lkdggivlgf qpdiqfkqqe lefehgdiil mytdgiteam naleeefgee rlinllkenr
      601 hlpvyelrqk iieavqnfsr krehddditl vlckfe
//
LOCUS       WP_457565709             223 aa            linear   BCT 27-JAN-2026
DEFINITION  B3/B4 domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565709
VERSION     WP_457565709.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Roy,H., Ling,J., Irnov,M. and Ibba,M.
  TITLE     Post-transfer editing in vitro and in vivo by the beta subunit of
            phenylalanyl-tRNA synthetase
  JOURNAL   EMBO J 23 (23), 4639-4648 (2004)
   PUBMED   15526031
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Mosyak,L., Reshetnikova,L., Goldgur,Y., Delarue,M. and Safro,M.G.
  TITLE     Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
  JOURNAL   Nat Struct Biol 2 (7), 537-547 (1995)
   PUBMED   7664121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..223
                     /product="B3/B4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=24713
     Region          1..212
                     /region_name="B3/B4"
                     /note="B3/B4 domain (DNA/RNA-binding domain of
                     Phe-tRNA-synthetase) [General function prediction only];
                     COG3382"
                     /db_xref="CDD:442609"
ORIGIN      
        1 mkitisasei ikqripglkl glvygcgasv skacpefeag fdelqsylnr hystaplssn
       61 pvighvrrmy rkigweptry rpssealarr ilqgkglyri fnlvdlgnlv saryhlpmgl
      121 ydadkisgdi lldvgrages yqgigkgeih aegklilrdd lgifgnptad skrtaldqat
      181 ksilaifftp peveapylqq alddlttyyr pyvkdlekei isf
//
LOCUS       WP_457565712             251 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565712
VERSION     WP_457565712.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..251
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27338
     Region          1..246
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 misfegknvi vtggsrgiga aivrmfsklg agvaynyhkn lhaaerlhte lqkygtdvyf
       61 adcdvrdfre vrsfvrnaie klgtihilvn nagiweygpi dkmsvdqwrk tmqtnldgtf
      121 yftrevvahm leqsiaghii niastagqrg epyyshyaat kgalisftks laaelgprgi
      181 hvncvapgwv ktdmtekama qqekeivkgi plgfvgeadd iagpviflas nlaryingei
      241 lnvnggnvlc g
//
LOCUS       WP_457565716             275 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidate cytidylyltransferase [Caldithrix abyssi].
ACCESSION   WP_457565716
VERSION     WP_457565716.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..275
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30312
     Region          4..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mkellirvav aivgiplllf vilkgglffy lfsvivtiig qwemynllkq kggrpmpvag
       61 mlsgqallai lysgfspllc lavvglvlyi fgyemfkndg sallntssti mgviyptmfw
      121 gallflrqna hhvfqadynf sgifiltmfv aiwicdtfay ffgmkfgkhr lfarvspkks
      181 wegavaglag allvylivyf qkiipislev aivsglivgv vgqfgdlves wfkrdagvkd
      241 ssallpghgg ildrfdsvlf ssmaflilyf ilqlr
//
LOCUS       WP_457565719             716 aa            linear   BCT 27-JAN-2026
DEFINITION  CHASE2 domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565719
VERSION     WP_457565719.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 716)
  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 716)
  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..716
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..716
                     /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=82690
     Region          13..656
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkwlkktlig aglgvfaall vwlitrytah dlfytyeakt ydwrikkkfe krptiddiii
       61 vdideranqk lgkysqwprk yhaqivdflh ragamaigld ilydrdiwqp dqdrefvrtv
      121 reagnvytai yfakadsdnw lpvmksepeg feaerfyytm plenasrfrr eermesrfve
      181 llnasrgvgh vnfngdidgi vrrihlftnf nhhlyptlgf kifmdalgvd svlfdvrnqv
      241 mnlyrenerl mgiptdeygn myinwagpfk tfryisfydv lkaeernlpp eifknkivll
      301 gtslaglydl rnvpfqrafp gveihaniiy tlinqnfitk mnekstllll iligvvlgli
      361 lirtkplfsv afsivlgfly vivvtiiffe qnywieiiap lmtillsfsl iyvyryitee
      421 kdkrfirstf shfvtksvvd ellanpekik lggekkectv lfsdvagftt iseqlepeel
      481 vqllneylte mtnivfkydg mldkyegdai mavfgapier gnhayqacat alemqeklsa
      541 mrevwkrqnr pelymrigin tgpmvvgnmg sesrfdytvm gdavnlgarl epankiygth
      601 imigegtvkk agdtiivrpl dllrvkgkte pvwvyelvgl sekglsddml rvldlfkkgl
      661 nhylkrdwds ainyfmqala irendgpsqc ylercnffke nppaddwdgv ytqttk
//
LOCUS       WP_457565727             458 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565727
VERSION     WP_457565727.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          142..458
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkeqfgrrsa qwatllvlif lgfnlllaqd vksiaghweg qielpgqale ididffvded
       61 gllsgdisip lqaakdlpld eieiagrkvr fklpgvpgna sfqgklsedg qrisgqfnqs
      121 gqgfpfslsr aatkaaraka alrgfdafia raikdwqvpg lamaivcndq vvfqggfgyr
      181 dlykklpvtp ktlfaigsst kafttfvlgq lvddgklewd qplrrflpef elqdpflsqr
      241 ltprdlvthr sglprhdmlw ynnhkltrke vvrrlrylea nadlrtkfqy nnlmfltagy
      301 ltesltgqtw eeavrqrilq plemkatnfs vqqsqksadf alpyteeenq lkripfrqid
      361 ligpagsins niadlshwlm vhlnngvykg rqminsatla dihtphmttg atakhpqisp
      421 adyalgwfad tyrghrrlhh ggnidgftam vmlfpddg
//
LOCUS       WP_457565729             217 aa            linear   BCT 27-JAN-2026
DEFINITION  deoxynucleoside kinase [Caldithrix abyssi].
ACCESSION   WP_457565729
VERSION     WP_457565729.1
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 10787652
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..217
                     /product="deoxynucleoside kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019136 - deoxynucleoside kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006139 - nucleobase-containing compound
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=26268
     Region          4..206
                     /region_name="Dck"
                     /note="Deoxyadenosine/deoxycytidine kinase [Nucleotide
                     transport and metabolism]; COG1428"
                     /db_xref="CDD:441037"
ORIGIN      
        1 mnrkrklyva iagnigagkt tltrmlsqkl gwkayyekvi dnpyledfyk dmkrwsfhlq
       61 ifflshrfkt qqeitewpgs ciqdrsiyed aeifaatlhk qgfmsdrdfe nykalfeimt
      121 sylrkpdlii ylqasterlf qhikkrgray eqqidrdyle qlnqayeewi erartegmnv
      181 ftfnmehrdf ehnerdfnil yksirdlenq twiegvy
//
LOCUS       WP_457565731             545 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator, partial
            [Caldithrix abyssi].
ACCESSION   WP_457565731
VERSION     WP_457565731.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 545)
  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 545)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 545)
  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   5  (residues 1 to 545)
  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   6  (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   7  (residues 1 to 545)
  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   8  (residues 1 to 545)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..545
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <32..379
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          422..543
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 wetlrnysei iksisgdyyk ttgamtkvir flerhisqls vlskslhndl lkarmvpias
       61 lferfkrpir dlareqkkev eliiedndae mdramiealy epllhilrna vdhgieksse
      121 rkkagkdpva kiilrarqek nqvvievvdd grgidlekvr kkivslklat aeeaasmpes
      181 rlleyifwpe fstkgkatqt sgrgigldvv amelqklkgi irvkttpgqg tvfslrvplt
      241 livshamlik fhdislaipl lavmesikis ekdillddrr kyiqvrgkll pyidlddilk
      301 fpderqvkps vknvalvlhd sgvsvavgve eilgrqdiii knlgnllqnv elisggtilp
      361 dgevalildy aaiihrveae yfgamreqvl irkvlpktrk kvvkaeeprp svseitvktv
      421 vgrkprimvv ddsasvrsfv sgflkkhgfe tveatdgeda lqkaretevd lvitdlqmpk
      481 mdgfelseql raiekykdlp iiiltaqvgk kqeqkseavg anafvskpfk eddlirmvkt
      541 fvkve
//
LOCUS       WP_457565735             268 aa            linear   BCT 27-JAN-2026
DEFINITION  XdhC family protein [Caldithrix abyssi].
ACCESSION   WP_457565735
VERSION     WP_457565735.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..268
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29764
     Region          2..259
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mkeiyqklae aieqnrsgvl ltvidvkgss pgkmggkmlv fedgehfgtv gggqieylai
       61 qealdnmsrn aawrnsyvls edagmlcggk veilyepfgq kekliifgag hvgsaladla
      121 pkanfyttvv dnrpeyaree rlpaahrvlc gdypqvfeel rfdentyimv mthghgfdqi
      181 iadyclkqpf kylgvigsrk kartffkelt eaghtqeeia rvfmpvgfdi gaetpfeiai
      241 simaeliavr yekplegrsl kklvakke
//
LOCUS       WP_457565736             203 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457565736
VERSION     WP_457565736.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 203)
  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 10005267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..203
                     /product="nucleotidyltransferase family protein"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22844
     Region          6..201
                     /region_name="MocA"
                     /note="CTP:molybdopterin cytidylyltransferase MocA
                     [Coenzyme transport and metabolism]; COG2068"
                     /db_xref="CDD:441671"
ORIGIN      
        1 maddfsqwsa vilaagrsqr fgapkvlqsf ngvpfvtrir knleergiqe mvlvlgfqaq
       61 nliphipdvg yfkiavnsnf dlgqfsslqv glqqvhpqak givmclvdqp hvasttylrl
      121 lesarrfpra fllprfanrg ghpviipavf fkeiiqadar qvtlreimlk hakdirrvav
      181 ddpavledid tretllelek kyr
//
LOCUS       WP_457565738             193 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565738
VERSION     WP_457565738.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 193)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 193)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 193)
  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 193)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..193
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <4..187
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 pddsiliddi pikkiplktl rehigyvpqe tflfsdtirn niafarpdas leeiewaarm
       61 aevhqsivef pdgydtllge rginlsggqk qrltlarall kkpsillldd alsavdnlte
      121 erilqhlkqv mknktcfwvs hrisairhad lilvldqgqi vergthesll algglyadif
      181 ekqqleefvt qvd
//
LOCUS       WP_457565740             428 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457565740
VERSION     WP_457565740.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..428
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50023
     Region          2..425
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpgikiefee yqlpnglhvi lhqdrqipiv ainlwyrvgs rnerpgktgf ahlfehmmfq
       61 gsqhvppemh fqliqsvggt lngstyfdrt nyyetlpshy lemglwlesd rmgfllpaln
      121 eekfrtqlev vknerrqrye nqpyglwlek ilelafpady pyhwpvigym sdlekatldd
      181 irqffktyya pnnaslvlsg dfdvtqakkl ieqyfaeipp yenippvnkh fsaynqgekl
      241 seihdhvqlp rlhfayhlpg isssevyhgd fiasvlnggk sarfiqklvr qkqivqdiqt
      301 fvlpmidtsl ffivatpkpd qsiedirrei deemerilne pitqqemerv knqiiaqkvr
      361 elqsvsvrad llnmyytyyq nanhlneeid vymnitpddl mstaqkfltp qnrvgviylp
      421 ekkeqrlk
//
LOCUS       WP_457565739              67 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565739
VERSION     WP_457565739.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 67)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..67
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
     Region          <1..57
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 eyagrikvvk lntdqnpqva arynimsipt lllfkdgevv dqivgavpky mitgkldyyt
       61 asahamn
//
LOCUS       WP_457565741             456 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457565741
VERSION     WP_457565741.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..456
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51973
     Region          10..436
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkdkvnreki pqpgqprpfn fpefrayrlp eglqtitvhk nnlplvnlly hvsfsplddr
       61 pghegqasll sllllegtkk ltgaqiagrf ealganynth igwsgfyfel nilkehlekg
      121 lelsrqilye svlpdhefar lkqealvdrl qikdmagria nerllkllfp dhryglpveg
      181 lsasiekitv eelrslynqv flkrqptiif tgnieedeal sltekyfasq qnkapheakv
      241 arfeqsakpk malvhkpnaa qielrvaqfi pprqhpdffk irlmneifgg yflsrlnlnl
      301 rekhgytygi hsqltyrpqv gmllisasiq sefitqalqe vfkethkmke egvsadelss
      361 aagyligvfp tafetidqis daiahivtyn lpadyyrtfr ekiaevtveq vneaaqkylk
      421 pqnmqvvlvg drnvvekalk enyeievfdi kgnplk
//
LOCUS       WP_457565750             587 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Caldithrix abyssi].
ACCESSION   WP_457565750
VERSION     WP_457565750.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 587)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..587
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=67654
     Region          <121..581
                     /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 mislfkkrkv rsledyfdif qkipmeiavf dlsgkfifin nyyftngiqp keflqkdeey
       61 yfyrlqidpa amnlrrkyfe ralksgqltr fteklyftek nrtfyykrif lplldsknkk
      121 viavvlfgnn lthlvlsqke lkylayhdrl tglrnrdafy eqlnqvvkea arvrdmlsai
      181 lfidldnfkf indtlghdyg dnvlreaarr mvrllrksdq vfrlggdeft vllrsikkev
      241 daglvaeklv kalsepyeik dqvitsisps igislipndg lktedlvksa diamyevkne
      301 gkagykffaq qmterslkrl qivnelkevi eaqsfdeqft mhyqpilasn gkvnnfkiig
      361 vealirwknp rlgnvspaef ipiaeeshli nyfnkwiidr tlgdfneisk fhnnglylsi
      421 nvsplglkse dfarslqnal lenhlnprni qleitetslm degtsihkni salvgmgvel
      481 aiddfgtgya slnylqnipa qtikidrsyi skinsdvknk dmirailamg kslnknmvae
      541 gvetsehlef lrqndckqfq gylfskpidv dslidifskh nmeitlp
//
LOCUS       WP_457565751             394 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565751
VERSION     WP_457565751.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..394
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43354
     Region          21..374
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrlfffivl ficthlllaq plprvspedv gldpqvlqqa drvieqaiad siipgavllv
       61 mrsnkiayhk aygyrqlvpq kkpmelntif dlasitkpla tatsimilld rgylrlkdav
      121 dlyvpefksy kgpfsdkpir lihllthtsg lppyapvael kekygspapd sliryiatvk
      181 rhhapgtyfk ysclnfitlq rvvksitgqp ldvfakrnif eklgmkntfy tlpknkiqac
      241 aaterlenge vligkvhdpl ariinggvsg nagvfstaed lavfsamlln qgawngqril
      301 nrltvqkmis vpagfeafgr algwdvsspy nsnlgdlfss kafghtgytg tsiaidpeyq
      361 vavilltnrv hptdsgsvvr lrslisnivg asik
//
LOCUS       WP_457565756             577 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457565756
VERSION     WP_457565756.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 577)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..577
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66082
     Region          221..568
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mikkmllqkn sglnlrffiy fllfayvpll ifsvvgyfln kqilrqiyln dqqqylitwe
       61 knfnkiveve kgvytillnn lddhekiftl khsgsaivsk plalsengki ivpreideqs
      121 vkkvynlihs esslyfnqdd atfwlkvdle seriliikyp lhnllttdfa lqqntrlyli
      181 sendgvvisk qeirlfdksp flkttqlqaf idelvnneaw itiiddfepg wkvafqrste
      241 tifrplrkfl fqiivanlal gilllffaif taqsisrpir mlaeaakris hghlnekfpi
      301 kgkdeirela aefetmrqkl lesyqnlekk ieertralke aqfqishqek masigllaag
      361 iaheignplt sissmtqiik rkvndenvkq ylntilenie risrivrelv dfarpsslea
      421 twvnvndvvr naygivkydr raktvdfqln lqenlpnlfl apdqllqvil nmllnamdal
      481 kegkgkieit trleddhvii siadtgvgip qehlnkifep ffttkdvghg tglglsvsyg
      541 iiknfngsiq vksevgkgsi ftiklpvksn meqmnes
//
LOCUS       WP_457565757             163 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565757
VERSION     WP_457565757.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..163
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18141
     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 mievpdlanl skevfyelly rqaramvede rdaianmanl sallfysmen inwagfyllk
       61 redelvlgpf qgkpacvrik vgsgvcgtav kkektlivdd vhqfpghiac dsasnseivv
      121 pmikngkmlg vldidspmlk rfseadrigl erivkvliey tdf
//
LOCUS       WP_457565763             291 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Caldithrix abyssi].
ACCESSION   WP_457565763
VERSION     WP_457565763.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..291
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33007
     Region          67..240
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mvkiilyill lsvlgiiaff illnsilhri fhhspvenkr tpdevglvyn eifietvhhk
       61 klqmfevpaq nqgkvvflcv hgwantvdnf leiaarlvkm gsvyllntrn hgksarensm
      121 tilkyetdir hamdyiekkf genikiillg hslggaaall tasddkrvag vvsistfsdm
      181 ekilrqgfvk sslpewfing lltyiefrig rtlkhvspaw iinkldvpvl lihgtkdevv
      241 dymemekifk eakkkqaekf vakghnhssl lkdenvaiai esfikkqfln k
//
LOCUS       WP_457565775             276 aa            linear   BCT 27-JAN-2026
DEFINITION  carbonic anhydrase [Caldithrix abyssi].
ACCESSION   WP_457565775
VERSION     WP_457565775.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..276
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31422
     Region          42..271
                     /region_name="Cah"
                     /note="Carbonic anhydrase [Inorganic ion transport and
                     metabolism]; COG3338"
                     /db_xref="CDD:442567"
ORIGIN      
        1 mkqkmtlfal atiliffvac nenqnkmnek aqkskteqtn nkemkkdcdd vhwthhsget
       61 gpenwknlcd gfadcggssq spvdiitadv vegkelaapi fkygkskvdi innshtvqfn
      121 isgentvnln gktykllqfh yhalsehtid gkhfpievhf vhkhsdtdfa vigfmfvegq
      181 eydlfskyld kfptskgeyk sdetidllsl lpenksyyyy sgslttppct evvswyvlkn
      241 pveaskkqie afskilnnny rpvqplnnri ieifrq
//
LOCUS       WP_457565783             112 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin, partial [Caldithrix abyssi].
ACCESSION   WP_457565783
VERSION     WP_457565783.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..112
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
     Region          <1..108
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(5,8,79)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 pkdftpgcta eacnlrdnyd alqkkglvvl gvsfdkpekh kafkekyqlp fpllsdttks
       61 vadkygakgt ftgflfakri tylideqgnv lhvfekvnag nhaqqildfl ek
//
LOCUS       WP_457565785             154 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEA family DNA-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565785
VERSION     WP_457565785.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 154)
  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 154)
  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..154
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..154
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17126
     Region          86..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 msltpaerra llmvalvfai safiqwvrph kvttkqfdyt lqdslfrals adtlqkttsv
       61 pqaqtapkrn vkstkkkkev lkpksidint anastliklp rigpktaqai idyrtehgpf
      121 ksieeldevk gigpktierl rpfiiitmpd stgr
//
LOCUS       WP_457565790             821 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457565790
VERSION     WP_457565790.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 821)
  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 821)
  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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..821
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=95676
     Region          <482..818
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mlailiaflt mqalkpffap nrvqidkktf fkqkigefyy ndfdhdgfse hvifktipew
       61 seigvkyyns kdmlvdqwnf serwiykavf fadfdndshd eiyfftqgnd siflysfdpr
      121 ftnqfliyrq fivrapepnp hpqkawdvqn vdavfydsdh dgyqemfini mtghslqprr
      181 ifkfdikrrr ivaksplmga yggklrlfdl dgdktpelff qasyapnnya pqsipypdnq
      241 swlmvfnldl qfafepipfp pafsvnyyti fqtnvqtyia acktyigkld vqpalylftp
      301 dgqlirerkl vsenhwtvfg lpfdnprhly vcnfngnlye ldhnlktvkt ikppyaiyai
      361 idqmdydndl qdeylasgas gilmiiepdf eeitvipeei nygyatiysv ckrgkaetdl
      421 ifqtdslvya vqykhnpwyv fryptgigma fvlffvitgl lfraqrfsss iqmrrqlfhf
      481 spigfllldf kgrlrsvnsk feqtlklsap lspgvhfsea lqerpqivsf iqhlihsqkl
      541 kerefrlflp dgntqfllrg fvhkgllgtp sgylievvpl nneqserklq lwsktiqkma
      601 hdiktplstv qllvqtarir lskhpqnqad eigkdldtas qqlsrirema kqflrftnle
      661 rpnlqrvslr sllehtlqrf sfyldedlhi eweldeqhdq ifmdptliem vfqiiienai
      721 damngkgtil itsnlvenie enfkkyieie fidngpgmdk dilkhifdpf fttkengtgm
      781 gltlarkiie dhlgkisvfs esgkstviri tipyreetyg i
//
LOCUS       WP_457565791             456 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457565791
VERSION     WP_457565791.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 456)
  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 456)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 456)
  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 456)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..456
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=51439
     Region          4..447
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mafkvflidd dvvylkslke flevnnfqae issnprkava tfqnkefdcv lldlkmpgld
       61 giqllekfle irtdvpiimv sgegtiplai kairmgaydf ieksddpnri litlsnaiek
      121 rklfleksvl kaqidetysi vgqseaiqki ldkiemvars nakvlitges gtgkelvara
      181 ihnnslragk pfvkincaai psmlleself ghkkgaftga hqdykgkflv adggtlflde
      241 igdmspelqa kllrvlenne vevignplpi kvdvrliaat nqnlpqlird gkfredlfhr
      301 lnviqvhipp lrerpedipp ladhfikmfa qtynkpvrgi seqalqilkq newtgnirel
      361 rnviekvivl tdkeiidtqe inealgsapt aqrlsfsngk slkkaleeye kfyieqtlkq
      421 hswkildsak aldidrtalf rkmrkfgiqk ddyvrs
//
LOCUS       WP_457565798             448 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caldithrix abyssi].
ACCESSION   WP_457565798
VERSION     WP_457565798.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..448
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50869
     Region          104..427
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrktvitisl ifcilkmgvs gdiialswdq vmelgvrqnl elqmlrqdvn hqklnvyram
       61 sdflptlnys fqavnnlelp vlvfmgnqfr igtkynftha lqaqyplflg garivnlkiq
      121 nharksllqm lkgkeeeivl kaieayfqvi lsrdllavsr raqqaaranf qqvkkfyeag
      181 aasqldflra qsklsqtipa vtsalnalrm seenlkfmln isvhdsvvvl dslaekdflg
      241 plkelelpal qqmaqesrpd lkslehqlqi ggqkewlags rflpqivaaa svqhqaflet
      301 aavksedytr aksasislqw plfeggkrvl ewqqaviqkr kaayqkellk rtimlevknn
      361 wnqfrlskqn lkslkqafee aketlrlanl tykegvstqv evlnaqtaft daearyrkgi
      421 fdyniaqlkl lkalgklhwl wqsngten
//
LOCUS       WP_457565804             184 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565804
VERSION     WP_457565804.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 184)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  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 18658991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>184
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          <21..178
                     /region_name="FtsN"
                     /note="Cell division protein FtsN [Cell cycle control,
                     cell division, chromosome partitioning]; COG3087"
                     /db_xref="CDD:442321"
     Region          103..176
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msklftllti viglnlifgc aaakkkvaqp aaeeravtti dgkfdesfdp lsledddivi
       61 krnnrgakaa kpglealdlt daqstsenea ipdslltyke vdgfrvqifa grsvetatmt
      121 kskaqidfep hrlkvyfife apfykirigd ftdrnqaera relarkigyr eafvvrskvr
      181 vaen
//
LOCUS       WP_457565799             206 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457565799
VERSION     WP_457565799.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24430
     Region          7..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnnlsnakse dtrnrifqaa aelfanygfe rvsirqicea vgvqkptlyy yfkdketlil
       61 emirftqqiv qairkdyvdc ktdflekirg llygrkyfve typhffrfya mlhlfstter
      121 vrmemltlml plldeftsil kqgqeqgyia pdedlemlmq tilgtlngls mrkfvfqeed
      181 afsdenlqrv fdfwqkhlfl npkkrg
//
LOCUS       WP_457565805             296 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565805
VERSION     WP_457565805.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..296
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33617
     Region          33..288
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mnkklsflli vllfflagck rqpadfqras feriislspn ltetlyalgq gdkivavsdy
       61 cfyppevnhk eriggllnpn lekilllkpd lligtpahae larklqayqi pfvllpndgl
      121 ndvfftidsl grllncpgra kqllktikds lsyyqalsrq ivkrapraal iigrdpgsvr
      181 hltvvgphtf ldsvwtflgg knifsdlavk ysqvgqesfl trqpdliief kfkeqwsarr
      241 dslnkiewqp lskipavkhn qiyvltgdyt lipgprvyel ardyyrilrq yaqkpf
//
LOCUS       WP_457565812             273 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54 interaction domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565812
VERSION     WP_457565812.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..273
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31374
     Region          <2..272
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mhnqstrkdr pfvpincatl penlleself ghergaftga hkmkkgllei adggtvflne
       61 igelplntqs klltvleykt frrvggnedi nvdvriiaat nrdlekavke gkfrldllyr
      121 lkvfqielpp lrerredipl lidhfvkfla kkfgkdikgv treslqlleh ydwpgnvrel
      181 invleravil enseyiqlds lpfelkeipp pakindvenw leipedgfsl yqvekkiiel
      241 vlkkagynks kaakllgitr dtlrykikky kll
//
LOCUS       WP_457565816             324 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter, partial [Caldithrix abyssi].
ACCESSION   WP_457565816
VERSION     WP_457565816.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>324
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <77..312
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mslkeqikkn pmfrylmvlt iastaglqiw rtlfnnfave vahlggnhvg iiqgvrevpg
       61 flallaifll kliaehklsa lsililglgv gltgffpsft glivttlims fgfhyyettn
      121 qsltlqyfdr qtspwvfgki rsisaasniv aglfiyllty llsyrnlylt gglfivlial
      181 wallqdpvdk nlpvqhkkmi vkkkywlyya ltflagarrq ifvafavfll vkkfqfsire
      241 vtvlfivnnt inyflsplig kaiirfgerk vlsveyfsli fiflayafvq nrwviallyi
      301 ldhiffnfai airtyfqkig dpkd
//
LOCUS       WP_457565818              85 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565818
VERSION     WP_457565818.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>85
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          3..>85
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 melkdrvaiv tgghkgigka lsvklaqhgv hvamvgrdva aldaaaseik klgvqalavq
       61 gdlcekdvid rfvrqviekf grldi
//
LOCUS       WP_457565820             261 aa            linear   BCT 27-JAN-2026
DEFINITION  transporter [Caldithrix abyssi].
ACCESSION   WP_457565820
VERSION     WP_457565820.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   van den Berg,B., Bhamidimarri,S.P. and Winterhalter,M.
  TITLE     Crystal structure of a COG4313 outer membrane channel
  JOURNAL   Sci Rep 5, 11927 (2015)
   PUBMED   26149193
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Arai,H., Ohishi,T., Chang,M.Y. and Kudo,T.
  TITLE     Arrangement and regulation of the genes for meta-pathway enzymes
            required for degradation of phenol in Comamonas testosteroni TA441
  JOURNAL   Microbiology (Reading) 146 (Pt 7), 1707-1715 (2000)
   PUBMED   10878134
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..261
                     /product="transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29073
     Region          30..259
                     /region_name="Phenol_MetA_deg"
                     /note="Putative MetA-pathway of phenol degradation;
                     pfam13557"
                     /db_xref="CDD:463920"
ORIGIN      
        1 mknlipwlsl lfifsfnslf aqyydaisid rpgqsntytt lkkmrfqies gftytvdknf
       61 pgnenlemvk mqmasttlrf gltkkfelrl gsqftyqrek ildqkssiss ieglnlgakl
      121 rvleskgiip dgallmtvgl pvgskelisd kvepgamfig shplseaarf eynagftyrn
      181 adfmeyfysl vlsvnfseqt safievartd pakgealsvf dfgisvltsr tvifdiyggk
      241 glnkeapdwf isvgggirlp r
//
LOCUS       WP_457565824            1758 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565824
VERSION     WP_457565824.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1758)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 1758)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1758
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..1758
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
     Region          <362..658
                     /region_name="AAT_like"
                     /note="Aspartate aminotransferase family. This family
                     belongs to pyridoxal phosphate (PLP)-dependent aspartate
                     aminotransferase superfamily (fold I). Pyridoxal phosphate
                     combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine...; cd00609"
                     /db_xref="CDD:99734"
     Site            509
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 pymarggysw rnptplirfi qdwfengqle tllydtgrqn gqkelmlgsg glnenlrilf
       61 ftlnqflerl patillfnrp epacagdfsa lrfqvlpqde msalelishf fnqqpqrphf
      121 lilgsipseh frrqarqlal qfplfivevn dapnhlslar ealleqrvlr fltpavfrpq
      181 lkdlstiiva grsdyiqhle tihfqlkgtp sapeaellyy llkqnvpsap sareqvdasq
      241 kpdlpslrta gslihrlerr lenasrhpad lttrllqtaq raehsaqrvi hrrlsfsplq
      301 slpddvwage tvwelienff dwldhpqwaq aleerfldaf vavhpqydrn aclavsgsar
      361 talgilgfhg pvkkvitfdl gwtyehcfpq vrvlpinpme nfssaevike iqkliekdad
      421 lltsgaliin nphnatgali pqkaleeifr waiskglyli ddlsyqnvgp wpeprrtpta
      481 rqtinklikk gllhadavkr litchslskt dsfagarltv leipdsslrs qfeihlkeik
      541 phrlplliay lfyrngrerv esywhfrnql faermatlqr amdelpgern pfkiriqapq
      601 gsmyplmiie alpagislds lstilanqgi glvplttfar taagyqmark afrltlgghi
      661 sgerlyyqtr rvlidlnrii aqeaslfqka llisepapvg epwqpllsql kelalqefek
      721 hsandkqmqe sqttfqrqfl perlqsiraq fhsrffiwqk wrqkdsaerq rllreilene
      781 fykddlnrrq qrfftrlfdr tvhptqifsi qvdqqarqii dafltqqqit agqlqtlara
      841 llnefqgrsv pinsiqesde llldldslnd aellaalqgk eelptflsyw gdwdgssrps
      901 gqghrliaav llknvarmar ilelllklep dlkidaalnd alvsfpqrrk kfwqllnqit
      961 hltnqlekry rslspasvhp srwrkigmkl hlvpdpltvl wqhndrlerk mlqlreqrrs
     1021 nleyyfqlnk qlrktlrqhl hlllnhlghp elfyrlifyr dllkrfaltp rihqnmitah
     1081 dpfaidttvf nlteinelga rfgnpglila lqismcsrsd aiikveqklr arreavlrna
     1141 pelpmpfiri iplfeeidvv kniegyldel wayaqthhst sqsvenrlre mlceifvags
     1201 dlsqqvsqtv ashlyketrf kvvrwlarkg lagqirlklg sgepmqrqgg fyddrgslpa
     1261 ftlnrqnrqr lfkelnassa racdfavtpl rgvissgdlr tfqstiseki rmisaferan
     1321 flfhyknlqt yfekeivras eplvqtrlrf gergekelkr ltlgwtdplf ekflqirmtn
     1381 fkqivygree divgihlasy fisrmvpafr drptvrpgri qtgdagqrvi erlsrvlpqa
     1441 khgtmlraig hnraqtmilg iaqlttglfr alkefvneqq gllsqqlllq erilphlpvy
     1501 eilkdlrlyq didlkfwsrl epffppgnsa vsslredmal inefiplfqk elirrhglpv
     1561 tdffenghfk inllpalrpd lavllqpdlf ntrpqklfdq iepplpqqwq mqvqelleip
     1621 vqitrwrtki wglieqkvam qvesfvqlaq aimhlmkqqn sageslsqnf tkfqrnfeqi
     1681 ssglraltde nlkqfllaal qyltisrqeg sevpihvmra lhdverivri esqplteaeq
     1741 qelrfyilqi arltgeng
//
LOCUS       WP_457565825             354 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Caldithrix abyssi].
ACCESSION   WP_457565825
VERSION     WP_457565825.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..354
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=40108
     Region          40..192
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          173..352
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mkrghryivf tmaifslili actkkevkpd lafagekhlk nirmltngge naeayfsfde
       61 sqliyqskhd sikcdqifim nldgsdkrmv stgkgrttcs yflpgdqqii yasthgvden
      121 cppppdfsrg yvwkvyssyd lyianadgsd pqpflpspgy daeatvsprg dkivftsqrn
      181 gdldiytvni dgsglkqlth eigydggaff swdgskivyr ayhpgteeel kryrkllaee
      241 liepnnfqlf vmdadgsnkr qithndfanf apffhpdnkr iifcsnmgtt estqrdfnlw
      301 minedgtglk qitffkgfdg fpmfthdgkk lvfasnrfnk kkgetnvfia dwve
//
LOCUS       WP_457565826             152 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase III subunit chi [Caldithrix abyssi].
ACCESSION   WP_457565826
VERSION     WP_457565826.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Marceau,A.H., Bahng,S., Massoni,S.C., George,N.P., Sandler,S.J.,
            Marians,K.J. and Keck,J.L.
  TITLE     Structure of the SSB-DNA polymerase III interface and its role in
            DNA replication
  JOURNAL   EMBO J 30 (20), 4236-4247 (2011)
   PUBMED   21857649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Stukenberg,P.T., Studwell-Vaughan,P.S. and O'Donnell,M.
  TITLE     Mechanism of the sliding beta-clamp of DNA polymerase III
            holoenzyme
  JOURNAL   J Biol Chem 266 (17), 11328-11334 (1991)
   PUBMED   2040637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..152
                     /product="DNA polymerase III subunit chi"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=17627
     Region          1..133
                     /region_name="DNA_pol3_chi"
                     /note="DNA polymerase III chi subunit, HolC; pfam04364"
                     /db_xref="CDD:461276"
ORIGIN      
        1 mqkiifielp varkeqyvtd iteslfalnk sihifaqknk lvaldrllwv rkpdsflpha
       61 ifqesdqens dllepillid rpvrltadvl ilhdplpvdq igsyeliidf aelydqnrlk
      121 dsrqrykvfr dsgrfdlsfe klgsflklik as
//
LOCUS       WP_457565833             294 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein [Caldithrix abyssi].
ACCESSION   WP_457565833
VERSION     WP_457565833.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..294
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32596
     Region          1..257
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mkkrlfstef kvgltvviat filvygiiwg kgyslkthkh qlqlvfdnig gmvpgdpvtv
       61 ngvkegkvvn idwkgrdvlv tielddrvkl yedatftiis aellagmkve ifpgrserrl
      121 nlakqpfrgk yggrivdvgl tidklaqdms altfrldttt alinsllrtg qlqenitstl
      181 enlnaisagf aslpdtlset ltqlnaairn vnrlinenrq pvasslkeie smgkninqlt
      241 qnlnktlkei qtqrgtlgkv mydstlynnl nktlltvdsl adrlrkkglk lsif
//
LOCUS       WP_457565834             423 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457565834
VERSION     WP_457565834.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..423
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49104
     Region          23..288
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(23..24,27..28,30,54,57..58,61..62,64..65,88,91..92,
                     95..96,99)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          23..47
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          52..82
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          87..115
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          121..149
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..420
                     /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          190..217
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          225..252
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          258..286
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(259,262..263,266..267,269,293,296..297,300..301,
                     303..304,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          291..321
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          328..356
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          362..391
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrylviflll llsqllfaqn qtlqkaliyf sqnryaqaek llfqhaqthp gdptplnllg
       61 hiymirqnfk kaiqvfqkaq elrpddgaia lnlgkalekt gyftlaqrqy lramqdtslt
      121 rlakmalaql yykqshfkka lklyreliky darngyffkq agrcalkvsk digqaetylq
      181 qalrftpgdl dvyvllynly kkkndwpnal qiaqqgliqf pqnrqlllav gdsyfatgky
      241 dqaispyrsa lqagdssayv fkklgaayyy lndypsalls lkksvkrddq dpityyflgl
      301 tqkalnlkka aivslnkavs lslpdfltdi yfhlaeayqk qkkytraiam ykklmetdss
      361 qvmplfylat iyddyyedrq tplryykkfl eqagdsvder yknyalermk iireklhflk
      421 grk
//
LOCUS       WP_457565835             292 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin family protein [Caldithrix abyssi].
ACCESSION   WP_457565835
VERSION     WP_457565835.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..292
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34375
     Region          152..268
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mkinmlfvff iligglhsqt lqtpwfqqlr qsfescqsle qldslsqqfe aqnqnrpqrl
       61 iafyqiysny vyviaqkyfi slktdeekea falkvkklhe mkkqyllkad qlcqklqgds
      121 ideeiqtfck yfkmaagrir ferqlkehqp lpdfeftdsr gqqhklsdfr gryvllhfwn
      181 mhskpcvdel tyllqafnqf drkkiqiisv hitvgkpdlk weaetlsnli qemglnwiqv
      241 sgeqtqaike lyfvrnfptl ylldaqgral ksgkslresq liatlselft dq
//
LOCUS       WP_457565844             343 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Caldithrix abyssi].
ACCESSION   WP_457565844
VERSION     WP_457565844.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..343
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39271
     Region          91..321
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(97..98,234,238,274..276)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mrdalkkiyf glidligknk rtlekkrpsv tiltyhsvvs dsapifeyey rncvtvsafd
       61 nqikmlkkif kviplqeave rlqtgklten yavvtfddgy rnnfehafsv lkkhavsaaf
      121 fvttgliggn dclwtdwvty lvfhstnkti elnfngwhra filnseeqki rasieirdlm
      181 ksatlseeem llnqlkaqvs idahpvaanp dryafmnweq vktmadqgme igshthrhal
      241 lnmlsneeaq relaeskrmi eektnasckf faypngqlkd fndahiemmr emgylaaltq
      301 vpgsnkvged lfrlkrinis nkmfppifka yvcgtiehng hhy
//
LOCUS       WP_457565846             457 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caldithrix abyssi].
ACCESSION   WP_457565846
VERSION     WP_457565846.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 457)
  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 457)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..457
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53242
     Region          <154..451
                     /region_name="GT4_WbuB-like"
                     /note="Escherichia coli WbuB and similar proteins;
                     cd03794"
                     /db_xref="CDD:340825"
ORIGIN      
        1 msrkknilfl ttnfppnpsv gtrrvakilk ymdhsrfnff vltlkeeyyn relgermgnq
       61 dkipasvkvf rtdksdltri ftfakqklgh flkkrktnka spakkekkte sagngqasgw
      121 kavlidklrs fffaffefpd kyigwlphav aqgariikhe kidiilttap phslfliali
      181 lkkithkklv ldfrdpwais rwdrgnifry gmerlveklc vqgadqlffv tpkmrdeylk
      241 lypgekkekf qlfyngfdpd dfqveveede rdvrgpfrfv hlgtlykrrn petlfmaikn
      301 lheqkqispg kvrfefigsv vselqfifkk vkelqiedyv tfkppvsfee sirtmfqada
      361 llliqpetdl qipakmfeyi yigkpilaia eensathqll qeanagilap skdiekiqqa
      421 vvtilrkkrs fnpraeyval fnyqkyakkf erildgl
//
LOCUS       WP_457565850             382 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caldithrix abyssi].
ACCESSION   WP_457565850
VERSION     WP_457565850.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 382)
  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 382)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 382)
  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 382)
  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 10157743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..382
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43725
     Region          16..265
                     /region_name="CESA_like_1"
                     /note="CESA_like_1 is a member of the cellulose synthase
                     (CESA) superfamily; cd06439"
                     /db_xref="CDD:133061"
     Site            131..133
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133061"
ORIGIN      
        1 mdviffwssv lilgyiylgy plilfilsri inkpvkaden nlptvalvis afneeavike
       61 kientlgldy pphklqiwvv sdastdhtde vvrsfvndrv hllrmeersg ktsgitrvmq
      121 kiesevvvfs dansmydkka irelvkyfad pkigyvvgya ryyengdpag sqeevywsle
      181 ikikineski gsvvggdgai yairkdlfkp lapddindfv npiqivlqgf rgvfnpyavc
      241 yeeaapsffk eywrkrrivn rswrglwkna avlnpfktgi faweifshkl lrwlgglfvi
      301 tsfasnaliv nksgfyavtm tlhvlfhlaa fagfyrdrkg kdsagiikfi fyfdmvnwas
      361 lqgiwdsfrg ktyttwktir qe
//
LOCUS       WP_457565852             372 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Caldithrix abyssi].
ACCESSION   WP_457565852
VERSION     WP_457565852.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..372
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43748
     Region          7..359
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mnliqyhfne ldklkskwae lhaksdasnp ftsfewiniw lghflndesa cqvhvvlddr
       61 eevvgiiplv nihekhtgvt fkglsfaans hsfrtrllvl pekkqeiikf wleavcqnqd
      121 fdylrfkefl ydetvvnilk dkklrfslee pkqppyldle gdwesyfggl rghfrrnlrr
      181 rlrnaekeyg kieyrvfdgs deeldafvlq glkleasgwk gkqgsailks qtvkdfyfdv
      241 ahnffkrgll hlgglyfger lvafnfsiiy dqvfyllkva ydesvakfsp gqimtylllk
      301 rlfeqklkrf dflgpampwk lewtgqfnqh stlyiygntf kgsylytlns kllpalrkie
      361 flkklkqkii kr
//
LOCUS       WP_457565856             191 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565856
VERSION     WP_457565856.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 191)
  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 191)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>191
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
     Region          27..122
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mpsavkkvee paehrdisrp afgieayvvk esvslrqgpa ftssikatlq dgealrilen
       61 rngwyhvite sglkgwvrsn lvgprnlskt lmatafndsi mprfsaqlfi dknkpyrviy
      121 lqfadgktsk pysiikriar ayqkkvyhgt vtvhlikpns rkpvktytfk gleisdiplp
      181 vlpvgilygl k
//
LOCUS       WP_457565857             477 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457565857
VERSION     WP_457565857.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..477
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=53213
     Region          1..469
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mskvviigag faghtaalyl gstlgknhei tvinkqdyfl fipslvwvgv ghmkpektyf
       61 klapvyrkvh vnfvhgsate vhpdeqfvva qragdgakvk ldydyliiat gpklnfegtk
      121 nlgphhgfth sictldhavq trdkylelle rmkkgekfki vigtghpaat cqgaafeyls
      181 nihkdlvkkg lrdkaelvwf snepklgdfg vkgieikkng rlltsedwlr difsqydikw
      241 eiqkgayavd ektiywedlq gnrgetsydf amlipqflgs pmkyldrdgn disskvvnka
      301 glvlvdaiyg ldyeqleqnp dawpavyqnp tyknifaagi afappgpisr psvnpnglsi
      361 tpapprtgmv sgiigrivak nvidlikrgr mthaermsem faaciasmgd slwdgeagim
      421 iiypvvpdmr kypnemgrdn fvthmelgla gawmkrmiht tfmwkfqarp gwsiipe
//
LOCUS       WP_457565858             189 aa            linear   BCT 27-JAN-2026
DEFINITION  Spy/CpxP family protein refolding chaperone [Caldithrix abyssi].
ACCESSION   WP_457565858
VERSION     WP_457565858.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Zhou,X., Keller,R., Volkmer,R., Krauss,N., Scheerer,P. and Hunke,S.
  TITLE     Structural basis for two-component system inhibition and pilus
            sensing by the auxiliary CpxP protein
  JOURNAL   J Biol Chem 286 (11), 9805-9814 (2011)
   PUBMED   21239493
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Kwon,E., Kim,D.Y., Gross,C.A., Gross,J.D. and Kim,K.K.
  TITLE     The crystal structure Escherichia coli Spy
  JOURNAL   Protein Sci 19 (11), 2252-2259 (2010)
   PUBMED   20799348
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Danese,P.N. and Silhavy,T.J.
  TITLE     CpxP, a stress-combative member of the Cpx regulon
  JOURNAL   J Bacteriol 180 (4), 831-839 (1998)
   PUBMED   9473036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007827
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..189
                     /product="Spy/CpxP family protein refolding chaperone"
                     /GO_function="GO:0044183 - protein folding chaperone
                     [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=20547
     Region          1..127
                     /region_name="CpxP"
                     /note="Periplasmic chaperone Spy, Spy/CpxP family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3678"
                     /db_xref="CDD:442894"
ORIGIN      
        1 mrktiislfv vltlmvsfst vfsqgmgwqr pgagvwatvn lnltsdqmqk lqtmqqdylk
       61 eitpiqselt lktqelrtlm vnpaanadqi makqnevfsl rqklqkvalk yrlnarkilt
      121 peqiallpag cglgfvfggg yglgagmgrr afyrgqgrgm gmgagmgfga grgrgmgagr
      181 giycpyrvw
//
LOCUS       WP_457565860             607 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiD family decarboxylase [Caldithrix abyssi].
ACCESSION   WP_457565860
VERSION     WP_457565860.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Mondal,A., Roy,P., Carrannanto,J., Datar,P.M., DiRocco,D.J.,
            Hunter,K. and Marsh,E.N.G.
  TITLE     Surveying the scope of aromatic decarboxylations catalyzed by
            prenylated-flavin dependent enzymes
  JOURNAL   Faraday Discuss 252 (0), 208-222 (2024)
   PUBMED   38837123
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Marshall,S.A., Payne,K.A.P., Fisher,K., Titchiner,G.R., Levy,C.,
            Hay,S. and Leys,D.
  TITLE     UbiD domain dynamics underpins aromatic decarboxylation
  JOURNAL   Nat Commun 12 (1), 5065 (2021)
   PUBMED   34417452
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Marshall,S.A., Payne,K.A.P. and Leys,D.
  TITLE     The UbiX-UbiD system: The biosynthesis and use of prenylated flavin
            (prFMN)
  JOURNAL   Arch Biochem Biophys 632, 209-221 (2017)
   PUBMED   28754323
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Jacewicz,A., Izumi,A., Brunner,K., Schnell,R. and Schneider,G.
  TITLE     Structural insights into the UbiD protein family from the crystal
            structure of PA0254 from Pseudomonas aeruginosa
  JOURNAL   PLoS One 8 (5), e63161 (2013)
   PUBMED   23671667
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..607
                     /product="UbiD family decarboxylase"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67913
     Region          9..432
                     /region_name="UbiD"
                     /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase;
                     pfam01977"
                     /db_xref="CDD:426542"
ORIGIN      
        1 myrsllecil dlekhghlir iqeevdprle maaihrrvfa aggpallfer vkgspfpavs
       61 nlfgtlerar fifrktlpkv emmmrmaahp esalknplqt lkvlpaivdl lprkvrsapv
      121 lkrrtrvsql pqlqswpadg gafltlpqvl tldpdnpsll ksnlgmyrvq isgnqyqpde
      181 qiglhyqihr gigvhharal qrgeklkvsi flggppahtl aavmplpegm selsfaglla
      241 grrfrylnyr gwivsaeadf vilgtmeeel lpegpfgdhl gyyslahdfp vlrvetvfhr
      301 pkaifpftvv grppqedtif gkliheitap mipkslpgvk avhavdetgv hplllaigse
      361 ryvpyqqrqp melltqaqai lgfgqlslak yllivaeedd pqlnindiqa ffrhllsrid
      421 lqrdlhffte ttidtldysg aklnhgskvv maaagkirre lgyrlpqnlk lppdfknlkr
      481 impgvlalea kafatyeraq kemralkeav pfsladsfpl lvvvddsefv gtslanflwv
      541 tftrsnpshd iygigefveh khwgckgsli idarikphha pplqedptie krvdelaarg
      601 hslhgvi
//
LOCUS       WP_457565861             521 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457565861
VERSION     WP_457565861.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   4  (residues 1 to 521)
  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   5  (residues 1 to 521)
  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 521)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20598104
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..521
                     /product="PAS domain-containing 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=60917
     Region          54..138
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Region          <141..516
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mminentsls eidvikneeq lltfipksvl gslfknfsit fymlkpdkqy gyrflymgks
       61 verllgfkpm dfvsdaglwl rlihdqdrpf llkngrrhle hkyqkltyrm kncegkyrwl
      121 rdelqpvfkd gkldyfvglw vdvsdeksfe elskenmtrf qtliaasgqi iwstdasgrv
      181 vedvpgwraf tgqsleqvkg egwlssihpe dlsnvqkawn halatktdfk gefrirrhdg
      241 vyrwfivrav pvrnegvdvh gwigacadit eqvereelle nyaarleqsn rdlqefayia
      301 shdlqepark ilafgdrlfa kfknrldeqg vdylkrmmna skrmqnlins lltlsrvetr
      361 gkpferidlt rivdevisdl elnikqvkgq iateklpaie adetqiyqlf enlirnalkf
      421 hrkdvnprik vywskkksnn rrvtivvedn gigietqyad rifkpfqrlh ardeyegsgm
      481 glaicrrive rhhgkiyfes elnkgtkffv elpvkqkkek i
//
LOCUS       WP_457565871             131 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator, partial [Caldithrix abyssi].
ACCESSION   WP_457565871
VERSION     WP_457565871.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..131
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          14..130
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 qkeaqvaqgr qqlvlivedd pevrslleas lkklnyrvmt aangaealki insakdeida
       61 iitdlvmpei dgvtlakkvr emgiaipvlf gtgyadehle kivdsdysrf ilqkpyrlee
      121 lakklnevlg n
//
LOCUS       WP_457565862             654 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing hybrid sensor histidine kinase/response
            regulator, partial [Caldithrix abyssi].
ACCESSION   WP_457565862
VERSION     WP_457565862.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 654)
  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   3  (residues 1 to 654)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 654)
  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   6  (residues 1 to 654)
  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   7  (residues 1 to 654)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   8  (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   9  (residues 1 to 654)
  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   10 (residues 1 to 654)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   11 (residues 1 to 654)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   12 (residues 1 to 654)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..654
                     /product="PAS domain-containing hybrid sensor histidine
                     kinase/response regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          24..280
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          192..523
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          532..651
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 wsysereall laadilgaav qrernekkml enaskfqrfi dvatfgilli kkeriifans
       61 tmvnimkmts esemvgksln evvhpddlpe veknieklyk tanqshefef rmirpnntva
      121 iveglasfie eekdtflifi kdisdrkkte qelkktykil nrlleanttv lfsgplterf
      181 spnhisqnik glmgfeaqei ienpqiyfdg lhpedrakvl kameqfkktg risleyrfkh
      241 knghfiwiyd eravvkeent epemngfwld islkkkyeqq ytraqrlesl gtlaggiahd
      301 lnnvltpilm gtellkhmvk dekaikslel metsaqrgas likqvlafar gtegertvvq
      361 vryliseavk mveqtfpkhi qlsidvaddl wpimadasqi hqvlmnmlvn ardampnggs
      421 lqiaaenlml deqyalslgn apkgpyvmit isdtgagiaa dmidkifdpf fttkeigkgt
      481 gmglatahri idehggfinv yseankgtsf kiylpaqkta reeapvkedd vpmgegqcil
      541 liedevsvre itkktletng yavftaadgp egiavfadnl dtinliitdm smplmdgpsv
      601 vralkrinet ikiiaisgrd devsslklin vpfiqkpfta stllkevhqa ltek
//
LOCUS       WP_457565876             247 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457565876
VERSION     WP_457565876.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..247
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28612
     Region          33..146
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 msisgfkenw fknwfgeeyi evyahrdeqd akdlirlivk nihitkqtki ldaacgpgrh
       61 acllknwsdf vfgldlsmsl lkrarqncpl elvrgdiral pfktrfevvv slftsfgyff
      121 ddgenlqvlk eyhrvlkkgg vffldflnas yvqkhlkget vrtingkkiv etrrivgkrv
      181 ekaitieqkg rqreflesvr lynlfelkal lnaagfkiqk vfgdyqgrpf eaqsprlifl
      241 tvkkarq
//
LOCUS       WP_457565877             327 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565877
VERSION     WP_457565877.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..327
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36930
     Region          3..323
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 makifltgat gfvgshlaek llqqghelrv llrttsnlrw iadlnlesfy gsldnpqsll
       61 sglkdidvvi hcaaltkalk nedyykvnfe gtkklvdlii nnnlpvkrfv fissqaaagp
      121 assfepvtee dephpvseyg kskllaekyi leqkgklpft iirppavygp rdtdvlqffq
      181 tvkrgiipkw qnrdkyasfv yvkdlvegia laaehekard kiyfiadaqp yswddlarvv
      241 mdffktkaih vpiplgavki iaavserwsk itkqpsiinr qkvaellpdf wicspkkiqk
      301 elgfatqtsl engvkqtlew yvehkwi
//
LOCUS       WP_457565879            1191 aa            linear   BCT 27-JAN-2026
DEFINITION  UvrD-helicase domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565879
VERSION     WP_457565879.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1191
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=138341
     Region          1..1162
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mqltdeqkra ldfsrnisvt agagagktrl lverfmeiav kkyhgrprla rkilaitftn
       61 kaagemreri araveerlkn aedpaayqhl lgirdqlnsv aistihsfca rvlreypiea
      121 glppdfseld emqtnmlmnr aidqlfeqvn geqdaekraa yfelfqhfdp qkvkvllrra
      181 llqpfemahi vrrfaqfdde qayfdfvsel wlnairqlwp qqalrqvmtl aghltdrllp
      241 gasnnavkkh qhmvslktlv akpeleledf rkiiaaleaf tassgkaygs lrqfggkksw
      301 aagseeailq lsehsarlle lkqnfdpgpp pqqadrqfyh lfkiilemyr aarelfeqlk
      361 teipgvdfed lliktlrllq nneqireelv rryefimvde fqdtnalqwq iiellatedg
      421 alqphkifvv gdpkqsiygf rnadirifkt vkeklalaag vknapeypgn vvlknsfrfl
      481 prlnafindl fadllqpqah nmyevefepl vaqrtamekg rlelallree dglneeeyma
      541 qtidrlvrqe kvtcherqgd eeverpltfg diaillrsrn allaveqslr rwnipfktvk
      601 gvgfwqkqei ydfyhllhfl aapsndfylv allrsrlflv pdhvlfllnq qpgenywqkl
      661 sgeldgpfde ghrqklldir allrrwievr daiplgellr mvlddlkyrt lisaqingeq
      721 llaniekfid hvlrfnksgm ngllelirqv ellieedske gepqlnlddr etvkvmtiha
      781 akglqfpvvf vpylnaknvd nvrqavfmep eigiampfrs dgpyqsqdfc llnllkaekq
      841 krelaeakri fyvaatrsse hlflsarikn dtiqrtsvle wlneffsrrg vdlldrqtel
      901 fkaadyrlhl vygykpqnre geeikglfeg lehlkgelqk plevdekrlq lyrplqerpg
      961 piifsatrlm tyvqdaqnyy qryhlgffes dyqlfadniy qmddslvkgk ifhrflelvt
     1021 enerdddall driffefevf dgekraeleg eilalkekif qssvglqilq aaearneltv
     1081 mmhlgqdfft gtldriiknk qglwqvvdyk tnrisaaqvr elarqyewqm kgyalllskl
     1141 ypqqehfpva lyfvhpdqlh eirytpaeie kiyaeftsli eeiktkypvr g
//
LOCUS       WP_457565882             294 aa            linear   BCT 27-JAN-2026
DEFINITION  FMN-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565882
VERSION     WP_457565882.1
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 10008166
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..294
                     /product="FMN-binding protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=33066
     Region          201..289
                     /region_name="COG3976"
                     /note="Uncharacterized conserved protein, contains
                     FMN-binding domain [General function prediction only]"
                     /db_xref="CDD:443175"
ORIGIN      
        1 mlktsgkkil ltihitmvsi wlgsltsill lqigkralts ahfflvdrfi faifdsvimy
       61 iaiavaisgl lfsmftnwgf fkfhwitikw itifllagii iflaspsing maaisdifrh
      121 ecesnldylk fesnvvlfta iqlvtlvlli llsvfkpwga rkqrfkvnrk iiissgliig
      181 allivgntmq ylqlnhyrhl plseitltqv adgiypgran ygfeyevrvh vknhaienie
      241 ilknrdsfya rlaegikhki iraqqihida vtgatttski lmkavedall sgne
//
LOCUS       WP_457565888             262 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM hydrolase/SAM-dependent halogenase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565888
VERSION     WP_457565888.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kornfuehrer,T., Romanowski,S., de Crecy-Lagard,V., Hanson,A.D. and
            Eustaquio,A.S.
  TITLE     An Enzyme Containing the Conserved Domain of Unknown Function DUF62
            Acts as a Stereoselective (Rs,Sc)-S-Adenosylmethionine Hydrolase
  JOURNAL   Chembiochem 21 (24), 3495-3499 (2020)
   PUBMED   32776704
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Deng,H. and O'Hagan,D.
  TITLE     The fluorinase, the chlorinase and the duf-62 enzymes
  JOURNAL   Curr Opin Chem Biol 12 (5), 582-592 (2008)
   PUBMED   18675376
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Eustaquio,A.S., Pojer,F., Noel,J.P. and Moore,B.S.
  TITLE     Discovery and characterization of a marine bacterial SAM-dependent
            chlorinase
  JOURNAL   Nat Chem Biol 4 (1), 69-74 (2008)
   PUBMED   18059261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004885
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..262
                     /product="SAM hydrolase/SAM-dependent halogenase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29172
     Region          2..249
                     /region_name="COG1912"
                     /note="Stereoselective (R,S)-S-adenosylmethionine
                     hydrolase (adenosine-forming) [Coenzyme transport and
                     metabolism, Defense mechanisms]"
                     /db_xref="CDD:441516"
ORIGIN      
        1 miitfmtdfg tkdgyvgsvk gvllkeapda livditheip pfnipqaayc llnyynsfpd
       61 rtvhlvvvdp gvgserkpli iqtmnyhfvg pdngvfdfvl kkeayrafei lpelvnpegy
      121 sstfhgrdif apaaallakg vkpeeiaapl drviindkke lacegnicki pivsidhfgn
      181 iifalsredl khwkksiklv nfktfssqti leyyaqqepg kplalwnsqn mleialtqgr
      241 aadffnvnpe kdravieltd vs
//
LOCUS       WP_457565892             269 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease, partial [Caldithrix abyssi].
ACCESSION   WP_457565892
VERSION     WP_457565892.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 269)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>269
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          17..269
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mktiifkkyl knlslmfltf caicwltapy lwqiitslkp taelsqlppf fpsridwshy
       61 rvvlsssdfq rfilnsliva sltsllafaa gsltsfataf fnfrkkalll ssilaismfp
      121 piaivsplfl mikaanlrdt ywalilpyss falpfmvwtl hnffkqvpae ileaarldgc
      181 tnfqlyrrvv lplsrpaift tsilvfifaw nefvfaltft atpksqtipv gialfpgiye
      241 ipwgdiaaas ivvtlplill vfifekqii
//
LOCUS       WP_457565894             360 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfotransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457565894
VERSION     WP_457565894.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..360
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=42964
     Region          66..309
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 metliglktn ewwklyrlnm fhlplnqipn clkltilsir nsiyarkeae efgqqieete
       61 iqkppvfilg hwrsgttllh kllskdpqfa fpnvyevynp wtflitekll kdrleklppe
      121 krpmdnvvva yndpaedefa lslmslkspl igwafpihea yfdryltmhn iseeerqewk
      181 kwfvyflkkl tllykkqlvl ksphhtarvk tlleifpdak fihiardpyr ifqstvnlyk
      241 ntvaklsmqk rdlekdieai inrykamydf yfeerqlikp ghlveikfed lekdfvtgie
      301 qiydalkidg wptykpilqa ymesqppykk ntyapidekw kakinnvwqk tfsewgyplq
//
LOCUS       WP_457565885              50 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Caldithrix abyssi].
ACCESSION   WP_457565885
VERSION     WP_457565885.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 50)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 50)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 50)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     New connections in the prokaryotic toxin-antitoxin network:
            relationship with the eukaryotic nonsense-mediated RNA decay system
  JOURNAL   Genome Biol 4 (12), R81 (2003)
   PUBMED   14659018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..50
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..50
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0097351 - toxin sequestering activity
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045927 - positive regulation of growth
                     [Evidence IEA]"
                     /calculated_mol_wt=5766
     Region          3..>44
                     /region_name="PhdYeFM_antitox"
                     /note="Antitoxin Phd_YefM, type II toxin-antitoxin system;
                     pfam02604"
                     /db_xref="CDD:460615"
ORIGIN      
        1 mgefkkqmar wlkttkntgr plittqngkr aavvmsteef dnlqyierfm
//
LOCUS       WP_457565899             440 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerate kinase type-2 family protein [Caldithrix abyssi].
ACCESSION   WP_457565899
VERSION     WP_457565899.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Yang,C., Rodionov,D.A., Rodionova,I.A., Li,X. and Osterman,A.L.
  TITLE     Glycerate 2-kinase of Thermotoga maritima and genomic
            reconstruction of related metabolic pathways
  JOURNAL   J Bacteriol 190 (5), 1773-1782 (2008)
   PUBMED   18156253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..440
                     /product="glycerate kinase type-2 family protein"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47825
     Region          2..439
                     /region_name="GckA"
                     /note="Glycerate-2-kinase [Carbohydrate transport and
                     metabolism]; COG2379"
                     /db_xref="CDD:441946"
ORIGIN      
        1 menfnkvakr misaalqavd pfnliieqcr lkdnelvigr vkrnltqyrh iyvlgagkas
       61 aamaqalekl lgerisgglv ivkygharpt qkikileagh plpdentlea tnqllqlara
      121 akkddlvifl lsgggsalle qlpdgvtlkd lqklnqlllg cganieeina vrkhvslvkg
      181 gqlakqiypa elvslilsdv igdplagias gptapddstf egawkvvlky glseklphii
      241 lqrlqrgkgg qipetpkand svfkkvsnii lgnnllalkk aretaqqsgf naliltdraq
      301 gevaeiskll aaifernfse qeltrspgci llggeptvtl rgnglggrnq emalqmllhl
      361 qkverpfyfc svgtdgtdgp tdaagawidh rsfqkarskk ldieaylqkn dsyhffakld
      421 qliktgptgt nvmdimillf
//
LOCUS       WP_457565900             288 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Caldithrix abyssi].
ACCESSION   WP_457565900
VERSION     WP_457565900.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..288
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32277
     Region          1..288
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mlnylillfg vfvtswssif irwigdvhpl visfyrlffs vlvlspfllk rmksgrhlps
       61 nvflkntlfl ilsgfflamh fftwiqslqw ttvgnsifle sthpifavil syfvlkekss
      121 pliiggiala llgifvivns dmgahpfatl gdflavasaf claaylliar fyrqkidllp
      181 ylvlvyaaaa lftlllilfl kinflnlalk swfflgllal gpnlighsll nwasrkmpvy
      241 lvnlamqgea vlatfyaall lneipgeqfy fgaglillav sfiflnrr
//
LOCUS       WP_457565903             470 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acyl-AMP ligase, partial [Caldithrix abyssi].
ACCESSION   WP_457565903
VERSION     WP_457565903.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>470
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
     Region          24..>469
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(211,214..219,221..222)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(238,258..260,337,340..343,368..372,377,418)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 maeqkhiqhf kekeiktlve llrwraqtqp nkraytylkd gkksiemtyg eldararala
       61 atlqkkgleg hralllyppg ldyivgffgc lyanviavpa yppdpnrlnr slprlqaivn
      121 dskstialtt dsilymirmm rmgnkigntl grmpflrkfr ttmryfsssk sgvaeshslg
      181 dlewlsadkv ptslgddwne pavtedsiaf lqytsgstgd pkgvilthyn llanskiiyd
      241 lmqypkngeg vfwipiyhdm gliggvlqpl ygevpstlms pitflqhplr wieamnnisk
      301 dkvvgtaapn fayelcikka tpekikhfdl snwfvalnga epvrastmdr fteifgkvgf
      361 kkeaffpayg laeatllvtg snkdegpvyl hvdkyafkkn kilevpaede nsqtlissgy
      421 shplqkvviv npdtfeeckp geigeiwvkg psvspgyydr pketeetfhn
//
LOCUS       WP_457565912             568 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Caldithrix abyssi].
ACCESSION   WP_457565912
VERSION     WP_457565912.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..568
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63213
     Region          24..563
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mrtmalwlml tlglitacqk gpeadlilln grivtldshn tiaqalavkg drilavgkta
       61 eiekmkgett rvidlkgala tpglieghah flglgeallr ldltrtrswq divdsvahra
      121 aqakagewii grgwhqekwd srpkklvegy pvhdalsqvs penpviltha sghalfinrk
      181 amemagitrq tpnpkggkii rdargnptgv llenamdlvw kvyhqqvgen pqqqklraak
      241 kamraclkng itsfhdagas fadieffkrl aeteqlkvrl yvmilepdqr lrqmlsqyrl
      301 igyannfltv raikrymdga lgshgawlfk pyddapgsvg ynvispdsll atariaikhg
      361 fqlcthaigd ranhevldvy ervfkenpdk qdlrwrieha qlihpvdvpr faslgviaam
      421 qgihctsdgp wveqrigekr areeaylwqt lwqsgavvan gtdapvepid planfyalit
      481 rrmkngayfy peqsldamqa lkaytynnay aafeeqlkgs lepgkladvt vfsrdilndp
      541 pykipstkvl ytiiggkivy qaadrtve
//
LOCUS       WP_457565914             379 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565914
VERSION     WP_457565914.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Zalatan,J.G., Fenn,T.D., Brunger,A.T. and Herschlag,D.
  TITLE     Structural and functional comparisons of nucleotide
            pyrophosphatase/phosphodiesterase and alkaline phosphatase:
            implications for mechanism and evolution
  JOURNAL   Biochemistry 45 (32), 9788-9803 (2006)
   PUBMED   16893180
REFERENCE   2  (residues 1 to 379)
  AUTHORS   O'Brien,P.J. and Herschlag,D.
  TITLE     Functional interrelationships in the alkaline phosphatase
            superfamily: phosphodiesterase activity of Escherichia coli
            alkaline phosphatase
  JOURNAL   Biochemistry 40 (19), 5691-5699 (2001)
   PUBMED   11341834
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Coleman,J.E.
  TITLE     Structure and mechanism of alkaline phosphatase
  JOURNAL   Annu Rev Biophys Biomol Struct 21, 441-483 (1992)
   PUBMED   1525473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10887878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..379
                     /product="alkaline phosphatase family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..358
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Site            order(3,38..39,60,160,164,207..208,315)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(3,38..39,60,160,164,208,315)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            340..342
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
ORIGIN      
        1 sfdgfrwdyl drgitpnlqk madegvrait fepafpsktf pnhytivtgl ypvnhglinn
       61 sffdpftkqr yrlgdtsavr naywyrgeal wetarrqgvl sasffwpgse vhlsyrhpny
      121 fkrydgsiph ieringvidw lqlpeekrpq llflyfsdtd tyghrygpes ekineaislv
      181 drylgvlrsk ldsigmkdkv nlivlsdhgm tqlrpdgqil lykllkdqav rvdgygplvq
      241 iftrspeake eifqrlnqnr mnfsvykked lpdyfhykns pfvgdivava hlgytfvrsp
      301 eelekvrrhp skgnhgydnh tldmqgifva agpafktaya cqtlhnvdvy plvckilgiv
      361 pngkidgkle riefilker
//
LOCUS       WP_457565913             112 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565913
VERSION     WP_457565913.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>112
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          1..>112
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 meqalqrarq aineaqavvi aagagmgvds glpdfrgneg fwnnypvarr lglsfadlan
       61 prwftenpel awafyghrln lyrqtqpheg fallleygkr lpggyfvfts nv
//
LOCUS       WP_457565919             533 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457565919
VERSION     WP_457565919.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 533)
  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 533)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..533
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=61425
     Region          264..498
                     /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          283..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..349
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          355..387
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          393..421
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(394,397..398,401..402,404,428,431..432,435..436,
                     438..439,461,464..465,468..469,472)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          426..456
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          460..485
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgelisflss gipggifllf ivlfvinlsl fflknselms patwkknlit lnlaailfya
       61 alwfitqppk pqervvvlpt qikdtlsltp eeflltetfe kaalnntndr ylvhrwewlf
      121 etikprqrsq yaewqrtara lrprfivesr mengqmtclv ldvkknkrvq iagkkeqgvg
      181 wfirrvdgel glfkdtpsip qidrtilaar lalynkdyar vlalvegred ipartlkaav
      241 liekglqvdv dqerakyvpv knpdfekakq ilvpivkqrk ntpeidllmg rmlirekeyt
      301 aaemflkkay vedpensrvh fnlsfllpdr lkdigynsrv qilkraiyld pgyrdavyql
      361 aneiylsgrg tlgsiqeain iinrfleihp gdpemlsllg tlyiktnyvk kalpiykalf
      421 eefpddsdsy ynlgvcyyml deyntalpyf lkaiemdrhl dsylyvgmiy rkmgkldsal
      481 kyfrervark tgdddtyake amagirsvli qmeeekiaak adsskqssth qrd
//
LOCUS       WP_457565929             314 aa            linear   BCT 27-JAN-2026
DEFINITION  histone deacetylase family protein [Caldithrix abyssi].
ACCESSION   WP_457565929
VERSION     WP_457565929.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Li,Y., Han,Q., Liu,Y., Yin,J. and Ma,J.
  TITLE     Role of the histone deacetylase family in lipid metabolism:
            Structural specificity and functional diversity
  JOURNAL   Pharmacol Res 210, 107493 (2024)
   PUBMED   39491635
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Yang,X.J. and Seto,E.
  TITLE     The Rpd3/Hda1 family of lysine deacetylases: from bacteria and
            yeast to mice and men
  JOURNAL   Nat Rev Mol Cell Biol 9 (3), 206-218 (2008)
   PUBMED   18292778
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hildmann,C., Riester,D. and Schwienhorst,A.
  TITLE     Histone deacetylases--an important class of cellular regulators
            with a variety of functions
  JOURNAL   Appl Microbiol Biotechnol 75 (3), 487-497 (2007)
   PUBMED   17377789
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Gregoretti,I.V., Lee,Y.M. and Goodson,H.V.
  TITLE     Molecular evolution of the histone deacetylase family: functional
            implications of phylogenetic analysis
  JOURNAL   J Mol Biol 338 (1), 17-31 (2004)
   PUBMED   15050820
REFERENCE   5  (residues 1 to 314)
  AUTHORS   de Ruijter,A.J., van Gennip,A.H., Caron,H.N., Kemp,S. and van
            Kuilenburg,A.B.
  TITLE     Histone deacetylases (HDACs): characterization of the classical
            HDAC family
  JOURNAL   Biochem J 370 (Pt 3), 737-749 (2003)
   PUBMED   12429021
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Bertos,N.R., Wang,A.H. and Yang,X.J.
  TITLE     Class II histone deacetylases: structure, function, and regulation
  JOURNAL   Biochem Cell Biol 79 (3), 243-252 (2001)
   PUBMED   11467738
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Leipe,D.D. and Landsman,D.
  TITLE     Histone deacetylases, acetoin utilization proteins and
            acetylpolyamine amidohydrolases are members of an ancient protein
            superfamily
  JOURNAL   Nucleic Acids Res 25 (18), 3693-3697 (1997)
   PUBMED   9278492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..314
                     /product="histone deacetylase family protein"
                     /EC_number="3.5.1.98"
                     /GO_component="GO:0000118 - histone deacetylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004407 - histone deacetylase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34821
     Region          21..308
                     /region_name="HDAC_classII"
                     /note="Histone deacetylases and histone-like deacetylases,
                     classII; cd09992"
                     /db_xref="CDD:212518"
     Site            order(126..127,135..136,164,166,251,293)
                     /site_type="active"
                     /db_xref="CDD:212518"
ORIGIN      
        1 mgrlaiifhp lflehnpgig hperperlka ildylneknf lnrvdqfqps easeealrli
       61 hdqshidfik hqagkegvml dagdtvlskh svgaalhaag agaralelvf kegydkvfaa
      121 vrppghhaer sramgfcvfn nvaiaarlaq rekfaekili idwdvhhgng tqhafyedpt
      181 vfyfslhqyp lfpmtglree tgsgpgkgft lnvplsygqg daeyvehver slaaiesrfk
      241 pdlilisagf dahvkdpigg mrlttagfyk ltemvaqfan ryctgriisf leggyhlnal
      301 aesvhqhlvc mlkh
//
LOCUS       WP_457565932             125 aa            linear   BCT 27-JAN-2026
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Caldithrix
            abyssi].
ACCESSION   WP_457565932
VERSION     WP_457565932.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..125
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14403
     Region          1..108
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mktnrkriki iydddcpfcv rsaallrqld rkgrfvflke svadarrllk gqsfedfnsm
       61 vviyegqwyr kgravrqigr vlglgwaadl lplavlnfvy qfianrrfvf skllfttqkc
      121 scskg
//
LOCUS       WP_457565938             631 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caldithrix abyssi].
ACCESSION   WP_457565938
VERSION     WP_457565938.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 631)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 631)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 631)
  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 631)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..631
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72063
     Region          1..620
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mklymqvlgf ikpywkgivl iivltfsyvi fnnlsiwisi dfvrelfspa yvqqqsvppd
       61 svqvvssade lqdivknsqg iyqklnskik sfiirkdrle tlkivclvif laflmknvsq
      121 ysrklllifi qarvvvdirn klqrkflhlp lsffhqhhsg tltsivfndv naiqqvlnqs
      181 fgkiilsplq iianiiillm isvklslitf iilpisffvi ykigqsirrr srrvfqqvad
      241 vvlafqesis ainivkifts ekreeerfkk tnfqyfqklf raerikiatt pineillvlt
      301 lvtllwiggr mvyqneglqp edfvrflvfl famfkpiqef sginnvmqtg laaaervfnv
      361 ldqpeetyda pdaielkefk keikydhvyf kynnedefel qdlhftikkg etvafvghsg
      421 agkttivdll prfypvsagr itidgidinr iklfslrkli glvsqetvlf ndtirgniay
      481 ghpdaseeai ikaakaanaw dfiqqfelgl dthigergvk lsggqkqrla iarailknpp
      541 ilildeatsa ldteserlvq ealdhlmqsr tvlviahrls tirnankiiv mhhgkidaig
      601 thaelyekss iyrtlyenql ligqikkkpa s
//
LOCUS       WP_457565937             207 aa            linear   BCT 27-JAN-2026
DEFINITION  superoxide dismutase [Caldithrix abyssi].
ACCESSION   WP_457565937
VERSION     WP_457565937.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..207
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23538
     Region          4..202
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mphqlpelgf synalepfid amtmeihhtk hhgayvnnln aaldkhpdlh nksieellgq
       61 lstvpadiqt avrnnggghw nhsffwallk knengkpvge lakafdsafg sfdafkeqfh
      121 kagmtrfgsg wawlivndqk qlvigstpnq dnplmdisef rgtpvlgvdv wehayylkyq
      181 nrrneylnnf fnvinwekve enflqal
//
LOCUS       WP_457565939             541 aa            linear   BCT 27-JAN-2026
DEFINITION  B12-binding domain-containing radical SAM protein [Caldithrix
            abyssi].
ACCESSION   WP_457565939
VERSION     WP_457565939.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..541
                     /product="B12-binding domain-containing radical SAM
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=62242
     Region          1..427
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mrivfiqppi edfystpirl qpiglaylsg vlkkhfpevd vivkdfqqgw gkrsiplpda
       61 lrflkdyyrf pdrspfstfy hyyrfgasee qvlkevgaln pdligismlf tayapqalql
      121 arilkkslnv pillggsdvs aranellalp fvdfvirgeg erpvvrfvee wlgkrrfdkv
      181 pnlgfktahe klvfndlqen faidelpfpd faglnlehyr lgrrklsfli ssrgcpyrca
      241 fcsvhqtfgh rlrlrsveni lqemelrlaa gvrafdfedd nltldqrrfk tlckeiikny
      301 aaydlkllam nglayfkldd qtlelmkdag fgelnislvs lnqpvlkqlk rpfnlqkfer
      361 vvqtahalgm svisyqilgl pgesvdsmlq tliylsrlpl rigvspfylt pgmplegslp
      421 ehkkpwwvvg rlsslsaten karrqriftl fvlarmvnfl keldlsgksl slkeilaerk
      481 hwqgrdltgl eilfklltey rfyvfdgndf rhhpafdvdl fkkfmeevkw ikrldggtis
      541 v
//
LOCUS       WP_457565942             436 aa            linear   BCT 27-JAN-2026
DEFINITION  lamin tail domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565942
VERSION     WP_457565942.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Eldirany,S.A., Lomakin,I.B., Ho,M. and Bunick,C.G.
  TITLE     Recent insight into intermediate filament structure
  JOURNAL   Curr Opin Cell Biol 68, 132-143 (2021)
   PUBMED   33190098
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Dittmer,T.A. and Misteli,T.
  TITLE     The lamin protein family
  JOURNAL   Genome Biol 12 (5), 222 (2011)
   PUBMED   21639948
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Dhe-Paganon,S., Werner,E.D., Chi,Y.I. and Shoelson,S.E.
  TITLE     Structure of the globular tail of nuclear lamin
  JOURNAL   J Biol Chem 277 (20), 17381-17384 (2002)
   PUBMED   11901143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..436
                     /product="lamin tail domain-containing protein"
                     /GO_component="GO:0005882 - intermediate filament
                     [Evidence IEA]"
                     /calculated_mol_wt=47037
     Region          41..151
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Region          289..403
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
ORIGIN      
        1 mktlhiisti ilaiifavag cklddtvsad qetpphqsay qlfinefmas ndacctdeng
       61 eyddwielyn gsedtvslag fylsddksdp kkfqipltad lrilphgfvv lwadgqpeqg
      121 vthldfklss ggedivltep dgytvvdeyt feaqetdvsm grvpdggtdw qrfttptpga
      181 pnvqgetsvp ptiktiqvlp dtinagdvvt iraqivdedg dlaqvsltyg aadslnttvn
      241 mtaendslfs shlgpfadgt rvffyivasd dadhstrsdt lsfevgyvpp alyineflas
      301 ndssnadenv eyddwieiyn aesrpinigg myisddkgdl tawqiptsds aattipaggf
      361 lllwadkqpe qgvlhvnikl ssggedivlt apngttvids ltfgeqttdv smgrlpdgsd
      421 nwvsftnptp gasnhq
//
LOCUS       WP_457565954             346 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfotransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457565954
VERSION     WP_457565954.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..346
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=41229
     Region          19..230
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mvqellpelq vkhrklnpvf vighgrsgts iliklirkyl kinfgtesqf ilryydaleh
       61 ygdlnrrenl lnlledivqe ryfkrikkrf nfdldkekvl sslkfpsysg llqaiflqfa
      121 qyhgmerwgd ktpeyifgld kilrlfpdaq fihivrdgrd valsefkthf gpknihcaae
      181 ewkkrinlaq nffatlkddq kfelryedll qnpvlifqql idffgiddqd kslirfiakn
      241 ivcdlkrgnf nkwhtalsks qiyrfervah reltayhypl ifshftkpsl ietyywrlhs
      301 kfkrllvpgt iednlyrirl rvksrllplr kklqfvagah rkvsfn
//
LOCUS       WP_457565969             407 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457565969
VERSION     WP_457565969.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..407
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46618
     Region          <191..407
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 mpkidfsner vkanfkaflf llgialvisg iwysqrlvsv lekktaeavq friklleesl
       61 nnpnsntdid flfneviqna dypliytdte nnprswrnid peidnksmde fthkdslklf
      121 nalkkikeen apipikyqnk ivlgyyyygy pdvlyklrrf pylaiisala fglvgyigfs
      181 yikkseqqfi wvgmaketah qlgtpltsis gwlellrlnn glketaieei qkdlqrlnkv
      241 anrfskigsr ptvkkadiip iinnvvdyfn rrlpniqktv iietnfkdqk lianvnedlf
      301 swvlenlikn aidamrsgve gkiviqamkd vdknelyidi idngkgipsn ekrkifkpgf
      361 stkkrgwglg lslakriien yhggrlilke tknnkgstfr islklqa
//
LOCUS       WP_457565970              85 aa            linear   BCT 27-JAN-2026
DEFINITION  zf-HC2 domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457565970
VERSION     WP_457565970.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Laity,J.H., Lee,B.M. and Wright,P.E.
  TITLE     Zinc finger proteins: new insights into structural and functional
            diversity
  JOURNAL   Curr Opin Struct Biol 11 (1), 39-46 (2001)
   PUBMED   11179890
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..85
                     /product="zf-HC2 domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10317
     Region          13..46
                     /region_name="zf-HC2"
                     /note="Putative zinc-finger; pfam13490"
                     /db_xref="CDD:463895"
ORIGIN      
        1 mnlspkskkh fecediekyi qqyldnmlde ekkrlfeehi eyclpcdkkv efekkfkevv
       61 rlkvkqelpk evvqqkikfi lksik
//
LOCUS       WP_457565973             398 aa            linear   BCT 27-JAN-2026
DEFINITION  dipeptidase [Caldithrix abyssi].
ACCESSION   WP_457565973
VERSION     WP_457565973.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..398
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44951
     Region          27..394
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 msffsllili hfliaqphqk mdvsllhena fvadlhcdai yrylrgidls ketqghvdip
       61 klrqggvdlq vfacfapapq ndmeknqsak nvlrqidgvy rliegnknfl slvtsydqig
      121 qlkeenktgi migieggyai endlallrdf yrlgvrimtl thwthtdwad asgdstttfg
      181 glnefgvkvv qemnrlgmii dvshvhdetf wdvinistkp ivashsccra lskhhrnlsd
      241 emllalaqng gmiginfepg ylnaefwner drlkeklaek fglprsrner rkadpeklkl
      301 frqelktete rlkqkyqidv klvvdhiehv iqvtgsadyv glgsdfdgis ttpiglenaa
      361 aipnitkell krgydkddie kilgknflri fkevgspl
//
LOCUS       WP_457565978             122 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter, partial [Caldithrix abyssi].
ACCESSION   WP_457565978
VERSION     WP_457565978.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..122
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
     Region          <1..117
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 dvpyflliga faglanmvpy vgpltgtila vlvvfisngq fnqmamvaga faviqlldnv
       61 vvqplvvars vqmhpllvif aviaggqffg ilgmflavpa aaivkvfvme myhtykkvnf
      121 am
//
LOCUS       WP_457565988             450 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457565988
VERSION     WP_457565988.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 450)
  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 450)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..450
                     /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=51333
     Region          60..450
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mllkniikak gelfpfldin ilqdrlgwsi klrwlaiagy fmatlvakyl mefkipyhli
       61 wltlcillii nifyflvqkf lknisfftel filsvhifvd lvflslllhf sggvenpiyl
      121 fylfhvvlss ivfprsypyl fstlvvilfa lllfaeysgi lphysifgah lhlnlsaigl
      181 tlfvfaitvy vttyiclgfm kifreskqvi dkqnlelqka nqqrmqffry ashelkspiv
      241 aikttidsvl anfgkeinpa gvdllqrasn raeqmlsiik dllelskaqq rtlnkttevi
      301 nvnrvldevi aqegvlaaek rinlildvnf dsltvhmhkd dlekilrnlv nnairytsee
      361 gsvtvkaikd knqlifqisd tgigieekdi dhifnefyra enaknmvgmg tglglslvkq
      421 ivesyggkie vksklnkgst ftvylplrth
//
LOCUS       WP_457565991             237 aa            linear   BCT 27-JAN-2026
DEFINITION  polyprenyl synthetase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457565991
VERSION     WP_457565991.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wallrapp,F.H., Pan,J.J., Ramamoorthy,G., Almonacid,D.E.,
            Hillerich,B.S., Seidel,R., Patskovsky,Y., Babbitt,P.C., Almo,S.C.,
            Jacobson,M.P. and Poulter,C.D.
  TITLE     Prediction of function for the polyprenyl transferase subgroup in
            the isoprenoid synthase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), E1196-E1202 (2013)
   PUBMED   23493556
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Chen,A., Kroon,P.A. and Poulter,C.D.
  TITLE     Isoprenyl diphosphate synthases: protein sequence comparisons, a
            phylogenetic tree, and predictions of secondary structure
  JOURNAL   Protein Sci 3 (4), 600-607 (1994)
   PUBMED   8003978
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>237
                     /product="polyprenyl synthetase 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]"
     Region          1..>236
                     /region_name="IspA"
                     /note="Geranylgeranyl pyrophosphate synthase [Coenzyme
                     transport and metabolism]; COG0142"
                     /db_xref="CDD:439912"
ORIGIN      
        1 msqqakiffn dlkplldqfq erlvaigqkh qvplfyepiq yvltlpgkri rplltilanq
       61 tcggrlnsal ypalavellh nftlvhddim dndalrrgqp tvhkkwdvat ailagdglmg
      121 lafkklleap egdlltmmrr ftdvmliice gqgldkmfet qsevseeqyl emirrktavl
      181 ielscelgal sasaaaenie rfrqfgynlg mafqiqddvl dimadesklg ktvgsdw
//
LOCUS       WP_457565996             713 aa            linear   BCT 27-JAN-2026
DEFINITION  S46 family peptidase [Caldithrix abyssi].
ACCESSION   WP_457565996
VERSION     WP_457565996.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Nakamura,A., Suzuki,Y., Sakamoto,Y., Roppongi,S., Kushibiki,C.,
            Yonezawa,N., Takahashi,M., Shida,Y., Gouda,H., Nonaka,T., Tanaka,N.
            and Ogasawara,W.
  TITLE     Structural basis for an exceptionally strong preference for
            asparagine residue at the S2 subsite of Stenotrophomonas
            maltophilia dipeptidyl peptidase 7
  JOURNAL   Sci Rep 11 (1), 7929 (2021)
   PUBMED   33846449
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Sakamoto,Y., Suzuki,Y., Nakamura,A., Watanabe,Y., Sekiya,M.,
            Roppongi,S., Kushibiki,C., Iizuka,I., Tani,O., Sakashita,H.,
            Inaka,K., Tanaka,H., Yamada,M., Ohta,K., Honma,N., Shida,Y.,
            Ogasawara,W., Nakanishi-Matsui,M., Nonaka,T., Gouda,H. and
            Tanaka,N.
  TITLE     Fragment-based discovery of the first nonpeptidyl inhibitor of an
            S46 family peptidase
  JOURNAL   Sci Rep 9 (1), 13587 (2019)
   PUBMED   31537874
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Sakamoto,Y., Suzuki,Y., Iizuka,I., Tateoka,C., Roppongi,S.,
            Fujimoto,M., Inaka,K., Tanaka,H., Masaki,M., Ohta,K., Okada,H.,
            Nonaka,T., Morikawa,Y., Nakamura,K.T., Ogasawara,W. and Tanaka,N.
  TITLE     S46 peptidases are the first exopeptidases to be members of clan PA
  JOURNAL   Sci Rep 4, 4977 (2014)
   PUBMED   24827749
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Suzuki,Y., Sakamoto,Y., Tanaka,N., Okada,H., Morikawa,Y. and
            Ogasawara,W.
  TITLE     Identification of the catalytic triad of family S46 exopeptidases,
            closely related to clan PA endopeptidases
  JOURNAL   Sci Rep 4, 4292 (2014)
   PUBMED   24598890
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12106229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..713
                     /product="S46 family peptidase"
                     /EC_number="3.4.14.-"
                     /GO_function="GO:0008239 - dipeptidyl-peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070009 - serine-type aminopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=82472
     Region          21..711
                     /region_name="Peptidase_S46"
                     /note="Peptidase S46; pfam10459"
                     /db_xref="CDD:431297"
ORIGIN      
        1 mkqvfiftli lltfsfglqa degmwllnql nqlgleekgl qmeeteiynp geislanavv
       61 nlgrasaelv ssdgliltnh hvafgavqra stggtdyltn gflaktrdee ipapgyvari
      121 llemkdvtad vlkgmdqind pvkrmraier rikemeeave qeredydari asmfsgkqyi
      181 lfkyqrfedv rmvfipprai gnyggdvdnw mwprhtgdfs flriymspdg rgtkysednv
      241 pfqpkrwiki aqeplkagdf tfiigfpgrt nrystsfyvd fyqnkyypll inefqdvinm
      301 ldeigkqske lqikavgttk wlnnslknyq gnlegmqrik llqqkkalee kvqefissde
      361 nlkrqygdll nrfeqefqks irsydrdffl syfrflagti psvansiygv ayerakpaee
      421 repsfsekdv qrsiqrlqyr ymsfapeidk allkrmllkf knfppeqriq gldfiftdyk
      481 siddflehay astrltdvdy arslffksle elnqmddpfi rmaralqpef dkirkekeen
      541 kalmqelskq wievlmayek rpfypdangt irftygnvag ytprdavwyk pfttltgvme
      601 ketgewpfiv peklkelyak kdygqwidpe lkdvpvafln ecditggnsg spvfnakgel
      661 vgiafdgnwe altgdwqfad giqrainvdi ryvlfitekf aganhilqem gik
//
LOCUS       WP_457566016             463 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Caldithrix abyssi].
ACCESSION   WP_457566016
VERSION     WP_457566016.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..463
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50795
     Region          49..463
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mivvliipll isfnfaepde iaflqtmgvl livalplfll trgevtldik dgflivtlgw
       61 tlyalfgalp fyfsgfipsy tdaffetmsg ftttgasilt diealpegll fwrslthwlg
      121 gmgiillsla ilpllgiggm qlfkaevpgp tpdrltprik htaellwvvy vaisvieava
      181 lklagmnwfd awchtfgtma tggfstknas vgafnsglid yiiivfmiia gtnfslhyra
      241 fkgkffsyfr dpetltfmai ilaatvfiai dilsilgyeq fsfrhvlfqv vsiitttgyg
      301 tsdyeqwpil skvvliilmy fggcagstgg gmkiirsiil fkfainqvkq llhpnavfvv
      361 rvgkrsvpqe ivtniagftl lyillsiigv lfmsglglnw etcigsvaat innigpgfgs
      421 vgptenyahl pvigkwflsf lmlagrleiy tvlvlfvpif wkr
//
LOCUS       WP_457565989             433 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457565989
VERSION     WP_457565989.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..433
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
     Region          349..432
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 ifpengaqnp lyftvqipei qfpyftrkek yqmislpfvt drsladlftd dlgaydaeky
       61 rlfdwdaqql kfveqkqlet vlppgkalyl iardslqlda gdlqsvptnv nfeipvasgw
      121 nmianpfpfp vawqevtqnw pgapvlyyyt gtgwiianvl epykgyavki sdktavaipp
      181 spaqnslara ailtdldwqv qltarsgiye devnfvgacs ttdghsetal vpepptigsf
      241 vslyfendds qkmaadirpa geegyqfdfr vnwntglaay vnikpdslpe gwtwklvspt
      301 grlcyselpa klsspgvrlr livgsadfvq kksenflpvp eqfqlsqnfp npfnqsttfk
      361 lqlpeadrlt ieifdingrr vktlvknfkf eagyhqfkwn gknngnsvva sgmyilrlkg
      421 akysavkkii lqk
//
LOCUS       WP_457566018             374 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566018
VERSION     WP_457566018.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  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 374)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>374
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          1..372
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 midrpidrtr vrqlldqfpv taiigprqsg kttlakqfka dyyfdlenpq hlaqlehpli
       61 tldelqgliv ideiqrqpdl fpvlrhlvdt ypkqkylilg sasrnlikqs geslagriay
      121 fqlegfrpsd vgienwkklw lrgalppsyl aksdrqsfiw rqqyistfle rdipqlgiqi
      181 partlrrfwm mlshyhgqil nyseigrsfg isdvtvrkyv eiledtfmlr tlwpwhanlk
      241 krlvkrpkly fkdsglfhal msietmeqlm ahpklgaswe gfalnvlcrl lgkedqsyff
      301 wathagaeld llwheggkhy gaefkfvdap vltksmksam hdlnldylyv iypgksnykl
      361 sdnaaalsfs rmaa
//
LOCUS       WP_457566019             546 aa            linear   BCT 27-JAN-2026
DEFINITION  two-component system sensor histidine kinase NtrB [Caldithrix
            abyssi].
ACCESSION   WP_457566019
VERSION     WP_457566019.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 546)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 546)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 546)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..546
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /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_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=62009
     Region          185..546
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mkkflnrlns idqlfallrv ltlvgglvwv llapipggqr kllfynffff svysillyvy
       61 iyhhppqirk aylvvlvldl iflsiltryt ggfhsdfilg ffllvalhsf yfglkfglav
      121 atasallyll cahtqinaqn finlilriaf fylvagsmgl lsrkeardrq rieqlyndln
      181 rhraeleqer dklakilmgi daglvllnrd qrilwmnrva eewfgpvqnl kdqfcgyalw
      241 rssdicndcp terclksgki etkeiefktd nhqlkffrvt aaplmneage ieqilelmqd
      301 itrekelnlq mihksklaai gelassiahe innplsaiav ciqqitdvmq sngheaanan
      361 diklclksmk neiqrckkit tglldisrks thrrvplnln qvlrnvlmlv rykaekehkn
      421 ieldlqqplp eiigeadela qvfinlilna leftptgksi yiksgtqnhq fvfvkvqdeg
      481 ygipiqnlnk ifdpffttkp rgagtglgla isqrivrahg gsiqvesklh qgtvftvllp
      541 varrea
//
LOCUS       WP_457565992             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ceramide glucosyltransferase, partial [Caldithrix abyssi].
ACCESSION   WP_457565992
VERSION     WP_457565992.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 354)
  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 354)
  AUTHORS   Leipelt,M., Warnecke,D., Zahringer,U., Ott,C., Muller,F., Hube,B.
            and Heinz,E.
  TITLE     Glucosylceramide synthases, a gene family responsible for the
            biosynthesis of glucosphingolipids in animals, plants, and fungi
  JOURNAL   J Biol Chem 276 (36), 33621-33629 (2001)
   PUBMED   11443131
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 354)
  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 10118552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>354
                     /product="ceramide glucosyltransferase"
                     /EC_number="2.4.1.80"
                     /GO_function="GO:0008120 - ceramide glucosyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006687 - glycosphingolipid metabolic
                     process [Evidence IEA]"
     Region          47..278
                     /region_name="Glucosylceramide_synthase"
                     /note="Glucosylceramide synthase catalyzes the first
                     glycosylation step of glycosphingolipid synthesis;
                     cd02520"
                     /db_xref="CDD:133012"
     Site            order(54,56,142)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133012"
ORIGIN      
        1 mltvivyfya lilgislihl avsavvtarr mkqkpdlkil nelkslpris ilkplkgidd
       61 nlelnlrsff eldypdyeli fglqntddpa lpivnklmma ypgvnarivv enseiglnpk
      121 innlhnmeky irgryvlisd sntqvkpefl nymlaailkp dvglvtatir gigakklaai
      181 fenlhintyv spnvfvadal sgipvvigks ilistqllkr mggfkafknf laedyllglk
      241 tkslglkvst ipimvdnvni ewslkrfinr htrwakirrn mhihhyfies vsnpialavi
      301 lalllhnalg agllllvtlv kmahdiylsr lmksdlkwyh ffltpvkdll isil
//
LOCUS       WP_457566023             560 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54 interaction domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566023
VERSION     WP_457566023.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..560
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=64577
     Region          85..559
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mekllqqfdr rlseimeefr yfsdlfpkdh aahdrltsif aalfslqsat qkmlnqvkqs
       61 pisdfdqser lyemlyknsl ilttetdkqk lldlaidsii emsgaqrgfl alidekqnyt
      121 iissrkmdrq siksakkkvs ntvirrvlqn qktiafqkpt rqkeltdiss vlqkgsfpli
      181 cvplfindki rgviyldqft kdlspaiial vknfvtqlsn flhtnelldq lkdrnraleq
      241 qlkkqnqfgk ivckskamlq vlqtinqvaa tdvtvlihgq tgtgkelvar aihenslrvn
      301 gpfievdcga lppniiesel fgykrgaftg anqdkmglle sanggtlfld einnlstnfq
      361 vkllrvlqqk tirrlgdtqe rkvdfrliva sstdlkeemk kkrfredlfy rintisvflp
      421 plrerkedip vlvnhfikry sekynrpvqs ftadflqale rytwpgnire lehvieravv
      481 lssrtvlnvt dlpeeifgnq kemllsqhye sldkfiteak kmyiekilke cqgkkveaar
      541 rlkinrsylf slikqlqiki
//
LOCUS       WP_457566024             280 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457566024
VERSION     WP_457566024.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..280
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30989
     Region          13..269
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mayvkpnpet dyafilgvss gfgeatalel aregfniigv hmdrgealnh veelkrlike
       61 ngveaiffnk naaseknrkq videikahfg qsenkkqikv mlhslafgsl apyihhdlde
      121 rltqkqlemt invmanslvy wtqdlveehl lgqgskifam tssgslrvip yygavsaaks
      181 aleshvrqla lelapykmtv nairagvtft palrkipghe tmidlalsqi pfkrltqpsd
      241 iakfilalat sdelwatgnv fnvdggeiit ayhstfhhkr
//
LOCUS       WP_457566028             227 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caldithrix abyssi].
ACCESSION   WP_457566028
VERSION     WP_457566028.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25174
     Region          3..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mvlikienls kvyntsavpv qalkninief ekgeftaivg psgsgkttfl nmiggldrpt
       61 egeitvngik lsalkgsklv eyrlhhigfv fqaynlipvf talenvefim llqgvpkeer
      121 qrrakellha vgladrmhnr pgqlsggqqq rvavaralas rpqfvladep tanldsksad
      181 dlldlmekln rdfnmtfifs thdarvirra rrvvtlcdgm vekdrtt
//
LOCUS       WP_457566029             403 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457566029
VERSION     WP_457566029.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..403
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44871
     Region          17..229
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..402
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mlfalawkni wrnktrsliv ilaiafglwg glfsgglmva lgdsmvksai drdlahiqih
       61 hpkydenksi qrfipqaeei ilklktvqgl agisartrfl gmassatssy pvqicginaq
      121 qekevttiyq rlvagsyfns pkenaivigq klaqrlnlrl hsklvlgfeg ldgelinvac
      181 rvvgiyrtes srfdeshvfl kseflvsnig rpaiheiair lkdssqltek tnllkswfpd
      241 llveswkers petafisdmm ilytyfflvf ilfavlfgit ntmfmsvvdr vrelgmlmai
      301 gmkrmrvftm illesimlsi tggfvgviig gltifltnht ginltifkas leffgsssvl
      361 yptlppelya yltilivfta saaaimpaik airleparai rtl
//
LOCUS       WP_457566030             404 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457566030
VERSION     WP_457566030.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..404
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45430
     Region          20..237
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          140..404
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 myiqlswrni wrnkkrtlia vasvffavit avntrsmqlg sydymihsta rfysgylqiq
       61 npqywekrsl ensmvqdsln fdrlsalshv mgvtprleaf tllsfgsttr vgqvigidps
      121 redqttglrs rlvegsflne deyaaiisqg larmlglsig dslvlygqay hgqiaaallp
      181 ikgivqypir elnntmvylp lktaqdiflm pgritsvvvl ldgnrhlnqa rsqllkiipq
      241 hyrvidwqtm lpelyqsiql dnvsgmlmla ilyvviafgl fgtilmmine rrkefgilia
      301 vgmkksrill vtmseiifis lagalsgilg alplvlyftr hpiritgeaa rsfelfgiep
      361 ifsfssdpti ffnqalvvfl ialatfiypv fflkklephe amha
//
LOCUS       WP_457566036             413 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Caldithrix abyssi].
ACCESSION   WP_457566036
VERSION     WP_457566036.1
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 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..413
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45223
     Region          3..412
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mksynsflva qqqveeaari lnldkattef lkwpqrefkf tfpvrmddgr feifhayrvq
       61 ynyargpakg girfhpdetv dvvralaawm twktavvdlp lggakggvvc dprhlsqkel
      121 eniarayira sadilgvdkd vpapdvyttp qtmawmldef etivrkhqpg vftdkplpig
      181 gtegrrdats rggvisvrea ckflniepkt faiqgfgnag qraallheel lggkliaacd
      241 srggilnpdg inakelvthk lktgtvlnfp garhipsdav leldvdvlyp aalenaisek
      301 naglikakii celangpttp eadlilyqrn ifvlpdilas aggvtvsyfe mlqnsggemw
      361 eeatvharld kkisnafqsf sdalrekgvh prlaamvvgv arvaeackir gwv
//
LOCUS       WP_457566041             739 aa            linear   BCT 27-JAN-2026
DEFINITION  heme lyase CcmF/NrfE family subunit [Caldithrix abyssi].
ACCESSION   WP_457566041
VERSION     WP_457566041.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Brausemann,A., Zhang,L., Ilcu,L. and Einsle,O.
  TITLE     Architecture of the membrane-bound cytochrome c heme lyase CcmF
  JOURNAL   Nat Chem Biol 17 (7), 800-805 (2021)
   PUBMED   33958791
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Stevens,J.M., Mavridou,D.A., Hamer,R., Kritsiligkou,P.,
            Goddard,A.D. and Ferguson,S.J.
  TITLE     Cytochrome c biogenesis System I
  JOURNAL   FEBS J 278 (22), 4170-4178 (2011)
   PUBMED   21958041
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Sanders,C., Turkarslan,S., Lee,D.W. and Daldal,F.
  TITLE     Cytochrome c biogenesis: the Ccm system
  JOURNAL   Trends Microbiol 18 (6), 266-274 (2010)
   PUBMED   20382024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..739
                     /product="heme lyase CcmF/NrfE family subunit"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015232 - heme transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=83532
     Region          4..578
                     /region_name="CcmF"
                     /note="Cytochrome c biogenesis protein CcmF [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG1138"
                     /db_xref="CDD:440753"
ORIGIN      
        1 mitgimatvl tfvalmlsvv ayylydrrre eslltfarta fyaagvlivf qtvlllygil
       61 ahhfewsyvf syssrdlslf ylistfwagq egtfllwllf gviyglwilh lrkedepmvm
      121 sffnlimafi amilikknpf tyvweinpin favgvippdg aglnpllqdp wmvihppvmf
      181 agysatmlpf sfaltalvkr nydnwvkpaf pfvvftamtl gagiilggyw ayttlgwggy
      241 wawdpvenss lipwlfslal ihglliqkrq ggmkkinlll simtfilvlw gsfltrsgil
      301 tdfsvhsfge seissyligf vllfmaigll iflfrvnevk yhpvhtdlat resfmnlgil
      361 ilvlmgiftl vgtswpllsg lfkekaesfa ieyynymagp favlmavlia ispllrwkss
      421 swdklrtvav havisfvlgi ifffagvkqi ipllimtlsv fmilingqlv ikmlrkknwg
      481 fggylvhtgl glmmigiits svydhsvktt fpkdmpkevf gyeivyqgrm paangkdhvv
      541 lmvdgkktma kfywsdysqa wmvgpsvenk wirdlyispi qiippedtmt sghtvtlikg
      601 qktdfhnfll lfkaydmnsh qmgademmlk aiveiydkns gelvgeirpg isikgddrqp
      661 lpatfvdnks kvflnginve qksitivvne anetpeagke ilaaevtikp finilwlgtv
      721 imlvgflfsl yyrfnerrk
//
LOCUS       WP_457566042             214 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566042
VERSION     WP_457566042.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 214)
  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 214)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 214)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 214)
  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 214)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..214
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          11..214
                     /region_name="CcmA"
                     /note="ABC-type transport system involved in cytochrome c
                     biogenesis, ATPase component [Posttranslational
                     modification, protein turnover, chaperones]; COG4133"
                     /db_xref="CDD:443308"
ORIGIN      
        1 gsvkvlsefk meliaekivk rfgnflvlrn isfqvksgss iaitgangsg kttlvkilcn
       61 lmaptrgkvl yrnngnvier gdiyryiglv gpylqlyqel taqenidffa rmrnlknyse
      121 kirkmmelfk lagreddpvk tyssgmqqrl kyicalmhdp eilfvdeprs nldqegiqav
      181 yrileehkke kilvistndq ddllladqii kvgn
//
LOCUS       WP_457566048             457 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54 interaction domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566048
VERSION     WP_457566048.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..457
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52110
     Region          9..444
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvdpkieckn lteiildnit egvftidhef nitsfnkaas qitgfpteqa igkkcydvfr
       61 sdiceegcvl kkaiengkns yskivyiitr kgfripikvt gaalkdkkgn ilggvqtfrd
      121 lsteddlrkf irrnysyhdi vsknpamwkl fdllpqvads nstvlieges gtgkelvarv
      181 ihqlsaradk nfvaincggl pdnlleself gykagaftda rrdkigrial aeggtlflde
      241 igdisqafqv kllrflqekt yeplgsveti nanvriiaat nknleelvae gnfrkdlyyr
      301 ikvvrlhipp lrqrkedipl lidhfirrfn nlqgksiegv sprvleilmr hsypgnvrel
      361 eniiehafvl cnediiqekh lpidlfeqrp eeiqdeyqkk lnemeaelil rtleehnwnr
      421 qaaaralnih kttlfrkikr lgiklphvdg rhrhvnd
//
LOCUS       WP_457566049             376 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c3 family protein [Caldithrix abyssi].
ACCESSION   WP_457566049
VERSION     WP_457566049.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Louro,R.O.
  TITLE     Proton thrusters: overview of the structural and functional
            features of soluble tetrahaem cytochromes c3
  JOURNAL   J Biol Inorg Chem 12 (1), 1-10 (2007)
   PUBMED   16964504
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Der Vartanian,D.V. and LeGall,J.
  TITLE     A monomolecular electron transfer chain: structure and function of
            cytochrome C3
  JOURNAL   Biochim Biophys Acta 346 (1), 79-99 (1974)
   PUBMED   4364940
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169255
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..376
                     /product="cytochrome c3 family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43082
     Region          82..165
                     /region_name="Cytochrom_C3"
                     /note="Heme-binding domain of the class III cytochrome C
                     family and related proteins; cd08168"
                     /db_xref="CDD:173979"
     Site            order(89,92,102,105..107,117,140,143,146..147,160,
                     163..164)
                     /site_type="other"
                     /note="heme-binding residues [chemical binding]"
                     /db_xref="CDD:173979"
     Region          205..298
                     /region_name="Cytochrom_C3"
                     /note="Heme-binding domain of the class III cytochrome C
                     family and related proteins; cd08168"
                     /db_xref="CDD:173979"
     Site            order(211,214,222,225..227,231,260,263,266..267,293,
                     296..297)
                     /site_type="other"
                     /note="heme-binding residues [chemical binding]"
                     /db_xref="CDD:173979"
ORIGIN      
        1 mkklitifgf lmilsvvgwa qrvehhasfp lrcsechyce kptynepclk icpdfiregi
       61 tvrhsvedap tlliidtlqn qyapavfthr lhaqmgemmg gceschhhnp pgrvrpciec
      121 hkverdmkdl srpslkgayh qlcinchrsw dtdwsktsdc yfchekaskd vtkdkqhlek
      181 laqkrhplpe ipdvyvlksd yeegpivtfy hkqhivafgl dckschknna cadchnptlk
      241 kekaklehdn clpchetaid encekchgtq kkppfdhaqt gwplkpfhkr lpcqgchkdq
      301 vefsalktdc nschktnwqv gtfnhsvtgi qldenhveid cetchlnrkf nqrpqcsech
      361 ddksfpadvp gkvmkd
//
LOCUS       WP_457566051             764 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Caldithrix abyssi].
ACCESSION   WP_457566051
VERSION     WP_457566051.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..764
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=83559
     Region          36..763
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 maenkiiksk yffeeeeieq laevsthqyr pwekneklkv vgkglprldg ydkvsgsavy
       61 tfdvilprma haatlrcphp hariksidts eaeklkgvlg ilthenapri ewygrsflfd
      121 phlryegdev acvvaeseri arqavrsikv eyeilpfvvd aqqalqknap qlyedgnlmr
      181 gkpskyergd lekglqeadv vlerrfdtqv vvhnptephv svvkwdgdhl tiwdstqgvf
      241 svrsrvasvl glpesnvrvi kkymgggfga kleagkytvm aallakkigr pvrialdrre
      301 mnlavgnrpd syqtlkagvk kdgtltalyl ksigsagayp agtgcawplr smyacpnvkv
      361 eeysvyinag rarayrapgh vqgffaleql idelaekvgm dplefrlkny adkepnwnip
      421 yttkllkeay lkgakaigwe rrnktpgeqp gpvktgigms sqiwwggggp payanlklnr
      481 dgsvqiiags qdlgtgtyti laqvaaevld ipvekievil gdtdvapycg ssggsttaps
      541 vspavrdaae qmkaklfsaa aahlgvpesq lkyaggkfys ageksasldi gqlarkmger
      601 vlvttgrrea npegyavntf gvqfaevevd tetgkvrvkk ivaaydlgrv lnrqmldnqi
      661 hggiiqglgy alfeerlidr nigklvnanl hdykiptikd tpeieiyivs egdeklsntg
      721 vkgvgepaii ptpaaianav ynaigvrmts lpmtpdkvlm alqs
//
LOCUS       WP_457566052             202 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Caldithrix abyssi].
ACCESSION   WP_457566052
VERSION     WP_457566052.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..202
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21569
     Region          53..200
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mseqskkssl srrqflkgvg tgvagsiaas kiaralplee lekaspppgq vlitlkvngq
       61 ekrfhvepqt tlaevlrerl qltgtkvvcn hgecgactvl ldgkavysch mlaidaqgke
      121 ittiegllsg eelhplqkaf vkkdgyqcgf ctpgqvmaar alllkkpnps redvlegmsg
      181 nlcrcaaypk iidsvleaak ik
//
LOCUS       WP_457566058             178 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566058
VERSION     WP_457566058.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 178)
  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 178)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..178
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21443
     Region          38..>131
                     /region_name="COG4627"
                     /note="Predicted SAM-depedendent methyltransferase
                     [General function prediction only]"
                     /db_xref="CDD:443666"
ORIGIN      
        1 mspvsrdrss kwtyilfqqk kwfseeqycd tlknftfihh nleyglpfen esvhfiyash
       61 liehifkedv lnlfkeahrv lrkdgvirls tpdldlaikl fdqgqteeal yfffknskkd
      121 yqyftihkyl ynfkllekyl reagfkkvyr csfkqgrvpd idrldnrpeq slfveavk
//
LOCUS       WP_457566059             355 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Caldithrix abyssi].
ACCESSION   WP_457566059
VERSION     WP_457566059.1
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 psyivihhsg tstkasfedv vnkekqerkn argayrldps fhsvitydgv ihnycrwdsi
      241 gwhvakgprv snanslglcf vgnfrnrssg knkpseqqie agarllalwr ylydieeknv
      301 vrhsdvrrgk iicpgenfpm erlvarstql lkswkqddti lkeleqfkkq ryiyv
//
LOCUS       WP_457566062             366 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566062
VERSION     WP_457566062.1
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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..366
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..355
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 glptypisrl sfgelggrif sfimfltlig wfgimtesmv atfytqifpe sglnvpvayr
       61 pflalfsgmg itaicffgfk aitwlnrfti pglifltffa lvkvlqkpnl iakvltwkpi
      121 nhhvsiytgt twvvgsliia avtapdfnry crrsrdtvys vllgnvpvvy flsimgmvfa
      181 ilsgaaegkt aveaadlssv fasqgwnigp vpgvylaafi ligaiittnv anlypgamal
      241 vtvlkgagky wpyledravl tllvgflgsl aascgllsrf efflealtyf avpligimgt
      301 dffllknrkt ikgllnvsam itwivfslga mfkvlpgggl atvfysavly yilekkfgel
      361 fylrrn
//
LOCUS       WP_457566063             524 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Caldithrix abyssi].
ACCESSION   WP_457566063
VERSION     WP_457566063.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..524
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58643
     Region          5..523
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mktslfynar ifpsvhshpf hwliaqngrv tvlgrekdei prlpiearfd lqgrvvipaf
       61 gdahvhslwa akafmeidls gaqslaealn ilkesktryq pgqwvvgrgf nknrwkdgvp
      121 arvlldrifp qnpvylesqd chsawvnsla ftnvgvkent pdppggrflr epegafsglv
      181 ldramerfkn alpapdeqql lqaldrfvgq lltngitsih tmegaqafsl wekyflrfgr
      241 kmrvvfyfpq eemdeliksg lysgygdpwl riggikffsd gslgsqtaam rqpyenqpdn
      301 mglllfnede llervkraes hclataihai gdravqlvlk vlqqtaalrk qhglvsrieh
      361 aqlvppdllp lfrqyglaas mqpihiaddv eiadrywger srfaypfrsl reinvplafg
      421 sdapvapadp lkgifsavfr ksrfqlskpt wtaeealdvw qavqaftegv alaadasafq
      481 gslltgkwad fivlsddifs mpaermlnvn vektildgsi vhav
//
LOCUS       WP_457566065             246 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane lipoprotein-sorting protein [Caldithrix abyssi].
ACCESSION   WP_457566065
VERSION     WP_457566065.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Okuda,S. and Tokuda,H.
  TITLE     Model of mouth-to-mouth transfer of bacterial lipoproteins through
            inner membrane LolC, periplasmic LolA, and outer membrane LolB
  JOURNAL   Proc Natl Acad Sci U S A 106 (14), 5877-5882 (2009)
   PUBMED   19307584
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..246
                     /product="outer membrane lipoprotein-sorting protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0042953 - lipoprotein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044874 - lipoprotein localization to
                     outer membrane [Evidence IEA]"
                     /calculated_mol_wt=28432
     Region          23..238
                     /region_name="LolA_like"
                     /note="proteins similar to periplasmic molecular chaperone
                     LolA, the outer membrane lipoprotein receptor LolB and the
                     periplasmic protein RseB; cd16329"
                     /db_xref="CDD:319986"
     Site            order(42,44,47,49,59,61,63,73,75,84,86,96,98,178,191,193,
                     205,208,210,219,221,223,226)
                     /site_type="other"
                     /note="hydrophobic core"
                     /db_xref="CDD:319986"
ORIGIN      
        1 mrsvinlifv slfiiwgnvv aqdaqsivak adavvnapkd qkatltmili dkngnqkqri
       61 aeflqkgddk rimrftapad qkgiaflglp ndvqylympa fhkvrriash vkntkfagtd
      121 ftyddlssfs yakdynakll sqddqfwvle ltpkpgvnkd ygklkmwvrk dnyypakvef
      181 ydkggnlwkv merrqiekvg kywvskemei kdlkeehati mkleniefdt glpdklftkr
      241 ylkrak
//
LOCUS       WP_457566066             970 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457566066
VERSION     WP_457566066.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Sandhu,P. and Akhter,Y.
  TITLE     Evolution of structural fitness and multifunctional aspects of
            mycobacterial RND family transporters
  JOURNAL   Arch Microbiol 200 (1), 19-31 (2018)
   PUBMED   28951954
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Hand,N.J., Klein,R., Laskewitz,A. and Pohlschroder,M.
  TITLE     Archaeal and bacterial SecD and SecF homologs exhibit striking
            structural and functional conservation
  JOURNAL   J Bacteriol 188 (4), 1251-1259 (2006)
   PUBMED   16452406
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
REFERENCE   4  (residues 1 to 970)
  AUTHORS   Arkowitz,R.A. and Wickner,W.
  TITLE     SecD and SecF are required for the proton electrochemical gradient
            stimulation of preprotein translocation
  JOURNAL   EMBO J 13 (4), 954-963 (1994)
   PUBMED   8112309
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..970
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=108659
     Region          1..950
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 merlaesvvk yripiiisvv fltvffgyql knikvnsdlf sylreddpdv qlfnrigkey
       61 agtsiamvgi gaddvfthkt lnvinritek ikqidgvatv msltdvldir sfegslevgr
      121 lidknnipdd pqklrqirsy tlskdmyngr ivspdgkvti iiarlkqnad kqevarkiqe
      181 iaqkeagsyq lyfsglpmqm levndiiisd mlylvplval vlvfmlyfsf rtkrgvilpl
      241 ltviistiwa mglmsllgve lsiisnimpv lliaigsayg ihmiaryked ikgaadtisc
      301 ikhslstvgv piilagmttv vgffsfagsy ltavndfgif tgigvifalv isitflpafl
      361 tflkkpeikt inkegkkena ldrfldrlaf fvlkneklii ilggllviis iiglprikre
      421 vnmieyfked tdiriaevmm ekkfggstpv qvlvkgdlkn pfvlkemrkf ekflesvpyv
      481 skpqsiadli cemnkvmnnh ytipdtregv anlwffiege sileqlvnne gnegiiqanl
      541 atmatgkilk svnmindyik nemdtslvav kinqdnaqei inlkipeitq lilsdftrhr
      601 ieievdraql rrlireiylt krvqfddrtl ndisekvvdf flneseieid dealirqitd
      661 qildlvksgn piseaaikkt ltrqlasrgs ydadeiadta yslfvildey wqyqrimegv
      721 dliiarfape aknnaklrda lrddlwvlne kvialpsava sskglegdrv svqfvqsgmp
      781 liftklddsl mksqiqslfi alvlvtiili iqlnsvtggl isitpiiltv llnfalmayl
      841 dipldnatmm iasiaigigi dysihfthrf keefsrsddp lkaleatmlt tgrailtnal
      901 avgagfiili faqlipiqrf gwltattmlf ssigavtflp alilftrarf vgnfrnfsfp
      961 dkivgkkrgr
//
LOCUS       WP_457566067             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566067
VERSION     WP_457566067.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22503
     Region          7..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msakaiadkk kfileiaqsl fahfglsktt iediarkahm gkasiyyyfa nkeaifkevi
       61 ekegrilqek lidavnkeht pqgkirsyii trmttikdla nyysalrdey lkhysfieki
      121 rtsydafeit mlstilnagh kegvfeveds nltaetivaa mkglefhwsi qnskkeivek
      181 vesllrilfk gierre
//
LOCUS       WP_457566072             535 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing SpoIIE family protein phosphatase, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566072
VERSION     WP_457566072.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 535)
  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 535)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11453254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>535
                     /product="GAF domain-containing SpoIIE family protein
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
     Region          <37..>211
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
     Region          <278..535
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mkatylssfr erhkseletk eadkrllels slfelsqlln ssldlrsild nvllipmgrm
       61 lisrglalik edkrfkvlnf kglprdwagk tlhianapte plllstltsn eawihlfkea
      121 kielllpils knqikgligf gsklthqpys sdeidflfsi cniagqaien aliiaelkkv
      181 nrsldekiqe lktlfeigke lnqifeeeli lkqlsfslmg qmlvnqffvv qkkengwqvv
      241 frkgshfped ccqavlndcd rlaridhpll vnesedfrhl lnynihlvvp meiknaiggf
      301 iflgarmdqk pyeplqlefv stlaniamis lensrliqet iekermeeel siardiqnrl
      361 lprsfpeisg ldihglnips kqvggdyfdi lplsdgqiil tiadvsgkgm pasllmsnlq
      421 aglhtlyter yslaqitqkl nqliykntsi ehfitffilk lnpqtgafey vnaghnppfl
      481 itpdgkleql tegglllgvv pdasyeagag llpagalitm ytdgvtecmn iadee
//
LOCUS       WP_457566074             197 aa            linear   BCT 27-JAN-2026
DEFINITION  indole-3-glycerol phosphate synthase TrpC, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566074
VERSION     WP_457566074.1
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 10000629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>197
                     /product="indole-3-glycerol phosphate synthase TrpC"
                     /EC_number="4.1.1.48"
                     /GO_function="GO:0004425 - indole-3-glycerol-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - L-tryptophan biosynthetic
                     process [Evidence IEA]"
     Region          3..>197
                     /region_name="TrpC"
                     /note="Indole-3-glycerol phosphate synthase [Amino acid
                     transport and metabolism]; COG0134"
                     /db_xref="CDD:439904"
ORIGIN      
        1 mkilekivrq kqkevallkr riplkdlkqk waistakkys liekmknsae frficevkra
       61 spsagwikhe vdpagqakay aaggaaaisv ltdrhffngl qedltqirha vdlpllrkdf
      121 iideyqvwes almgadlill ivrildtdql erflslasel glevlvelhg kkdieklpah
      181 ietlpvilgv nnrnldt
//
LOCUS       WP_457566076             505 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566076
VERSION     WP_457566076.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>505
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
     Region          7..505
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mahtkfvhsf ledsaqrypd kdaffvnnrw ytfdyierha nqlasfliyl gvrkgdrvaf
       61 yiensveyvi tyyailkiga itvalnteat amnvdyilqd cdvqnlivgq kfykrlqsli
      121 dkdylthfiv wdsgklkses snpkikylpq acqsfpseli hrriidldva sivytsgstg
      181 qprgatlthl nivtntrsiv dyleltaedr imvvlpfyyi ygksllnthf fvggsvvvdn
      241 rfmfpnvvlk tmqeqkvtgf sgvpstftil lhrsnvrkmq fdslryvtqa ggamapavqk
      301 evaqvfapak lfimygatea sarlsyldpe dlprkwgsig kgipnvdlfi adangnrlpp
      361 etqgeivarg animlgywnh peetrkvlkh glyytgdlgv mdeegfiyvv grskdmikig
      421 gnrasakeie dalyehpqva daavigvadd tlgeapkafv vlkdressnm eetlrnflak
      481 rlasykipky fefrenlpkn ksgki
//
LOCUS       WP_457566081             377 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566081
VERSION     WP_457566081.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..377
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43673
     Region          8..366
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(234..235,238,310,314,355)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(234,238,310,355)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mqeltreqqa kryerikliv sisesvlsfl llvlflttgy saelrdwthq ltenaylrfl
       61 lfmavagfgl slftfpfefy sgfilehryq lsnqtlwdwi keklkenlvg laiglplala
      121 fyflllnypq swwfwlsvvi flfsvllgrl apqlifplfy kfeplkddel lkrmerlaki
      181 gkfdlqgifr fnmskdtkka naaftglgks rriiigdtll enfthdeiea vfahevghfv
      241 hkhlyrlmaa gtlqtfvgfy lahliywdll trmgftgpad laalpliaii ltvymllvsp
      301 lsnalsrhye rqadlyalrr ssnprafasa llklseqnls dkqphplvef ffhshpsiqk
      361 rvkmvedflq gkkieqv
//
LOCUS       WP_457566082             507 aa            linear   BCT 27-JAN-2026
DEFINITION  HAL/PAL/TAL family ammonia-lyase [Caldithrix abyssi].
ACCESSION   WP_457566082
VERSION     WP_457566082.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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 507)
  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 507)
  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..507
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..507
                     /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=55063
     Region          1..499
                     /region_name="HutH"
                     /note="Histidine ammonia-lyase [Amino acid transport and
                     metabolism]; COG2986"
                     /db_xref="CDD:442225"
ORIGIN      
        1 maivldgksl tieklvriar fnekvelape alerikacra mlekkiaare vmygintgig
       61 efsevvlsde qveqfqkyli ynhaagigep apieyvraam agrinvhahg rsgvrpeitl
      121 tliemlnkgv tpvvcqkgsv gasgdlapms qiallllgeg eafyqgqrlp gkaameragi
      181 kipglkardg latingsnll tamsalhlyd mdrwlrqaei aaamsleall anlkpyderl
      241 hkvrgfdgav rsarairqcl qgsdlysgki kqrvqdaysm rstpqvigaa rdairyartq
      301 veielngvgd npiffvedel tltganfqgt pvalpmdmag aavtmvsvms errmnrlnnp
      361 alsaglppfl tkgagmfsgl mlsqytadsl iveqrilsvp aaiqsipaaa dqedfvsmgm
      421 ntaiknaqil dnaygilgie fmaaaqaldf rqhqfgrgvq takkiirkyv pyldedrply
      481 pdhtkmkalv ksgeileave sevgslr
//
LOCUS       WP_457566083             395 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Caldithrix abyssi].
ACCESSION   WP_457566083
VERSION     WP_457566083.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118301
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..395
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44723
     Region          25..360
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
ORIGIN      
        1 mktsptkllq airrevailf kdvdillivl vsplfyalfy gtvyvhkvet dipvividqd
       61 nsalsrklir sldasqnllv vrvtqdavea ksaiedwqtq gaiwipadfs ktlksgrqah
      121 lkvylntsrf lpsndinrav qqtvatlaag vrlryfqarg lnfdqateqi qplrvddrnl
      181 fnvrqsygdf lipgvlalil qqtllfglam svarefelns feewqktskd ntllmftgkg
      241 ifyftlylay slfffsviyg vlhlpfhgry gtfllltalf llnvtlwgmi igsffrskiv
      301 alqtlvfssy plfllsgfsw plqsmpwwik nlstllpsts yflamqrvta mnagpadivp
      361 ellhllllfv lstglaywrf qylqksvplg asvrv
//
LOCUS       WP_457566085             485 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caldithrix abyssi].
ACCESSION   WP_457566085
VERSION     WP_457566085.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..485
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55402
     Region          150..477
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkrnylsyvv lfllfagihl gqaqtltlde aidralknne likrqeerli qkehanleaw
       61 gnflpqvkve agythlnkpl eidlnflreg llqlqtsdqv kmanlqslil ngrpltdael
      121 arvqqqayla ldaalppfal afkdqdyksa tllgvqplfl ggkliaakkf asselqaskq
      181 elyktrndvi qqvvknylav vlmnevvktr qnvlqamlrh qiqaqklfaq glisksdvlr
      241 arvavaearr nlfddqnkle laeialrhil alddqtpivi ndslvykaln dsletflrla
      301 regqpvlkll sfkeqsaaqk faaeraeflp qvaafgkyem ypeylsilep rwavglrlqi
      361 nlfngfkdyn klqearhlkk evhllkthtq rqidlwvqka yrqmrnaetr ylqlasdial
      421 arenlrsqqk rfeaglgtsl dvidanlile keqiarhqsl fdyyrsmvel faaagnpaki
      481 keiwk
//
LOCUS       WP_457566088             111 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566088
VERSION     WP_457566088.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 111)
  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   2  (residues 1 to 111)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..111
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [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          <1..111
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 eqdgrngmka llelaerpda ifavndpvai gaydvlkqkg lkipddmgiv gfsnnpissf
       61 vhpplttvhq payemgkkaa elllqqidsq veevslvkev lktrlivres a
//
LOCUS       WP_457566094             425 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457566094
VERSION     WP_457566094.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 425)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 425)
  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 425)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..425
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49641
     Region          108..403
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msgrrpikll nkttafylif sflvffisaf imskmanqyi dsyvqnrfsk fdwrlkkhlt
       61 kdstlsrlpr ylklrrlsdr qllqklpvvk dtiiynesid eyqhyrkrla aikvgkdyyv
      121 yetrvhvgdf yrlrddflas mffvfgalal gliafnyfls gylfrpfyqi lnvmktykvg
      181 qqtsapaist tteefikmqk lfqkmldqie kdyrnlkeyt edmahemqtp laiirnkles
      241 lmrdeaaler hgeaiqviyr qinhlshlgn vlnlitrien gefkntriir tkpiieehlq
      301 svkelaelkg lkitfdlnee hafnidpylf elvlknlvrn aiqhaptgas itiktdeqal
      361 iisnvgaeld fppqqlfkrf vkrknngetl glglalvkki cdlnelnvsy eylngrhifk
      421 iskta
//
LOCUS       WP_457566102            1090 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Caldithrix abyssi].
ACCESSION   WP_457566102
VERSION     WP_457566102.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1090)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 1090)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..1090
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
     Region          1..962
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
     Region          845..1087
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 prpavqtfng ssldrlypke llerlkafsr engatlfmtl laafeallhr ysgqdsilvg
       61 spianrrqte lenligffvn nlvlkgefdd dpdfvtllqr vrkntleaya hqdlpfenlv
      121 eilqperdms hapifqvmfv mqntpvqpvq lsdvrlepii peqkiakydl slvvmetedg
      181 lfaefeyntd lfrketierl hnhfqklled vlqspqkpvs tlsliteqel klftrewnri
      241 pseppldvci qtlfeqraar tpdktavvye nerltfeqln iranrlahyl reigvgpeki
      301 vaislergqq miisllavlk aggaylpidp eypsdrlnym lkdsrakwli tsqqlkekfs
      361 dfsgqliiqe eiesvlkakp adnpqivnrp qnlayiiyts gstgrpkgvm lqhrglvnlv
      421 fslggfygvn aqsrtlqfas fsfdasveei fntlingatl ylidrqtlls gtglvnalks
      481 ykitnvtlpp sllnvlnpqd fphlknitsa geactpeian kwaqgrrfvn gygptentvc
      541 atvynveepl kgntvpighp ihnvqvyvln ramihqpigv pgelyiggpg largylnrpd
      601 ltaerfvpnp fsekpgerly rtgdlvrflp dgnleflgri dkqvkirgfr velgeieati
      661 rqhkgvkgva vnavktttne talaayllve erekfdlaal kqeikkilpd ymvpaafill
      721 defpltpngk inyralpvpq fdqsgevkqt vkarntlear lvdiwkevlg vttigvtdsf
      781 felgghslla mklltaveqk lgkdvnlvsf freptiehma rlieedapfe sgatlvklks
      841 gddrqplffv hpsggsvhhy aelakllkth rsvygiqaqg ldgkmplhqt vedmasayiq
      901 tikqkqphgp ylisswslgv iivhemarqf kamgdevalv lqldqgpdvt yekpadnaem
      961 lvnmfkryfk ldidylrtld easqfkfvik kakkhkvipr fvrlndfkry ilvnetqima
     1021 wvnyrqkpye geivllrsee nakadppdlg wakmvqkvri idvpgdhism llqphvqiva
     1081 dkidrllkdl
//
LOCUS       WP_457566101             249 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566101
VERSION     WP_457566101.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 249)
  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 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..249
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=28551
     Region          18..186
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtewiewrqc pfrfkdanei hvwllpvehs erfmpflsad erhraqkfrv psaraqfvvs
       61 raalrlliaa ychldpaeiq fklnphgkpy lenhpiffnv shsydwalig lspkfeigid
      121 iekmrpdlnl rqlagrffsa deveqlnslp shlyaegffn awtrkeayik argkglaipl
      181 sgfsvslkps epavlksteh dpqalqqwkl seipapqgyk aalvvrssrf nikhwsgkel
      241 fklknnssa
//
LOCUS       WP_457566105             232 aa            linear   BCT 27-JAN-2026
DEFINITION  galactokinase, partial [Caldithrix abyssi].
ACCESSION   WP_457566105
VERSION     WP_457566105.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 232)
  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 232)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..232
                     /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]"
     Region          <1..211
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 kpcglmdqma catggiiyid fkepqrptfq kidfdferyd yrllvvntgg shadltadya
       61 siphemrqva salgqkvcrd vdedtffral pqlrkkvgdr avlrafhfir enqrvleqvk
      121 alhdkdfdlf lklmnesgns sfkwlqnift sqqineqnlt lalaltedyl akvgrgacrv
      181 hgggfagtiq allpvqaldd yidkmeyvfg knsvsllkir sigtqylnll me
//
LOCUS       WP_457566106             132 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy-metal-associated domain-containing protein, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566106
VERSION     WP_457566106.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>132
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          15..78
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mekenkakfy tfvpiegmtc aacvtrvekg lrqaphvatv nvnlaaeqaa lgldsdqvnt
       61 qeileyvqks gydvkrakit iplaglqdta malkveeair pllgvvnfnv ntveeaglle
      121 yvpgmldlee va
//
LOCUS       WP_457566069             147 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate kinase family protein [Caldithrix abyssi].
ACCESSION   WP_457566069
VERSION     WP_457566069.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolution and classification of P-loop kinases and related proteins
  JOURNAL   J Mol Biol 333 (4), 781-815 (2003)
   PUBMED   14568537
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Schulz,G.E.
  TITLE     Structural and functional relationships in the adenylate kinase
            family
  JOURNAL   Cold Spring Harb Symp Quant Biol 52, 429-439 (1987)
   PUBMED   2841070
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Schulz,G.E., Schiltz,E., Tomasselli,A.G., Frank,R., Brune,M.,
            Wittinghofer,A. and Schirmer,R.H.
  TITLE     Structural relationships in the adenylate kinase family
  JOURNAL   Eur J Biochem 161 (1), 127-132 (1986)
   PUBMED   3023080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..147
                     /product="adenylate kinase family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019205 - nucleobase-containing compound
                     kinase activity [Evidence IEA]"
                     /GO_process="GO:0006139 - nucleobase-containing compound
                     metabolic process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=16135
     Region          1..>143
                     /region_name="Adk"
                     /note="Adenylate kinase or related kinase [Nucleotide
                     transport and metabolism]; COG0563"
                     /db_xref="CDD:440329"
ORIGIN      
        1 myiilfgapg vgkgtqakli sqkyhipqis tgdmlreair qgtelgkkae eiiargdlvs
       61 ddimlglide risrpdckng fildgfprti kqangldrlf kekkltspvc ieitvpetvi
      121 ikrltsrric ekcgaifdpv gnpfppi
//
LOCUS       WP_457566114             757 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein [Caldithrix abyssi].
ACCESSION   WP_457566114
VERSION     WP_457566114.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 757)
  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 757)
  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 757)
  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..757
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..757
                     /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=84562
     Region          37..757
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mgvtrrefik tsaaaaaaas igtallpggi kplfadsgmq whksvcrfcg vgcgvmigvk
       61 ngkvvavrgd kfntinkghl cikgfylhkv iysktrlthp mikkngkfek vswdealdfv
      121 akkfneirkq hgpdalafyg sgqaeteety manklfkgci gtnnmegnpr lcmasavggy
      181 ltslgldeps gtyddiekae lflligsnta eahpilferi vrhkaknpnv kiviidprtt
      241 ptdqvadlhl fpkpgwdlai lhamariiik egyadeqfik dnvvikgndk knmtfeqykq
      301 flekytpeya skisgvpaed ivkaarlfgq aktamsmwtm ginqrtrgvw annlitnlhl
      361 ltgkigkpgs dtfsltgqpn acggvreggg lchllpghrk vanakhreev akvwgvpvkn
      421 iqpkpgkhti amftalnegk ikgiyimctn paqslpnask ywkglkeqfv vvaesffpta
      481 ttqyadvvlp aafwaekegv ygcterrsqy mpkviepmge arwdafilrd lgirmgfkke
      541 fekyqtaedi wneyltltkg rdmdlsgaty rrlkevrglr wpvpsedhpg tykryvkgdp
      601 ifdelpaekk kgrwiyfygk pegkaviwar pdkgpeeptd dqypfalttg rvlehwhtnt
      661 mtgtvpelnr avpkayvein pedakalgia nkdqvivetr rgklkiearv inrpekgtlf
      721 ipwhweewma nvltidafdp gskepeykvc aarikka
//
LOCUS       WP_457566117             469 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566117
VERSION     WP_457566117.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 469)
  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 469)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 469)
  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 469)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..469
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=53476
     Region          1..458
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkfqihivdd eqtvaqslkr ilstsereie vsnsgfealk ktetksfdlf ildyrlgdmd
       61 giqllehlkn tsadaiyifi tafgnvetav ramkagafdf iqkdqnpevi rftvqraldt
      121 irlrkevell knsifqergp rkmvaespvm keilqiaeky aqtdctilit getgtgknvl
      181 aefihyqsnr fnnpflainc ctipanlmes elfgyekgaf tgahtngkvg lieranegtl
      241 fldeigeltp dlqakllyii erqeflrigs vepqkvntri iaatnvdlek mieeknfrsd
      301 lyyrlnvasi klpplrerke dilplsklfi eefnkrfnkn vkqiaddaad ylinapwkgn
      361 irelknller vmilteedtl sfrelqkaft pfsndhspek naffslhlnp skgtnllqes
      421 qkqlviqalk kcncnrssaa rmlgiprttl nfylkkfdlq seepalkns
//
LOCUS       WP_457566118             235 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmannosamine-6-phosphate 2-epimerase [Caldithrix abyssi].
ACCESSION   WP_457566118
VERSION     WP_457566118.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Arif,T., Currie,M.J., Dobson,R.C.J., Newson,H.L., Poonthiyil,V.,
            Fairbanks,A.J., North,R.A. and Rendle,P.M.
  TITLE     Synthesis of N-acetylmannosamine-6-phosphate derivatives to
            investigate the mechanism of N-acetylmannosamine-6-phosphate
            2-epimerase
  JOURNAL   Carbohydr Res 510, 108445 (2021)
   PUBMED   34607125
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Currie,M.J., Manjunath,L., Horne,C.R., Rendle,P.M., Subramanian,R.,
            Friemann,R., Fairbanks,A.J., Muscroft-Taylor,A.C., North,R.A. and
            Dobson,R.C.J.
  TITLE     N-acetylmannosamine-6-phosphate 2-epimerase uses a novel
            substrate-assisted mechanism to catalyze amino sugar epimerization
  JOURNAL   J Biol Chem 297 (4), 101113 (2021)
   PUBMED   34437902
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..235
                     /product="N-acetylmannosamine-6-phosphate 2-epimerase"
                     /EC_number="5.1.3.9"
                     /GO_function="GO:0047465 - N-acylglucosamine-6-phosphate
                     2-epimerase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006051 - N-acetylmannosamine metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0019262 - N-acetylneuraminate catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25697
     Region          7..234
                     /region_name="NanE"
                     /note="Putative N-acetylmannosamine-6-phosphate epimerase
                     [Carbohydrate transport and metabolism]; COG3010"
                     /db_xref="CDD:442247"
ORIGIN      
        1 meekkttvln qlkgglivsc qseppepfar pslilamara almggavgir anlprnvrhl
       61 vkkldvpiia lykkkyensd vfitptirel kaliksgapv ialdatqrer pggerledli
      121 hfarmhsncl lmadvstvhe gveaarlgfd ligttlagyt aytahrfdsq gpdfhllkel
      181 vrevgdqtpv iaegriwqpe qakkcldlga favvvgtait rpwvltarfv qalrv
//
LOCUS       WP_457566124             151 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidylglycerophosphatase A family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566124
VERSION     WP_457566124.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Kumaran,D., Bonanno,J.B., Burley,S.K. and Swaminathan,S.
  TITLE     Crystal structure of phosphatidylglycerophosphatase (PGPase), a
            putative membrane-bound lipid phosphatase, reveals a novel
            binuclear metal binding site and two 'proton wires'
  JOURNAL   Proteins 64 (4), 851-862 (2006)
   PUBMED   16838328
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Chang,Y.Y. and Kennedy,E.P.
  TITLE     Phosphatidyl glycerophosphate phosphatase
  JOURNAL   J Lipid Res 8 (5), 456-462 (1967)
   PUBMED   4292860
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10731865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..151
                     /product="phosphatidylglycerophosphatase A family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16488
     Region          2..146
                     /region_name="PgpA"
                     /note="Phosphatidylglycerophosphatase A [Lipid transport
                     and metabolism]; COG1267"
                     /db_xref="CDD:440878"
ORIGIN      
        1 mkkgliyvig aglgtgyapv apgtagslla vllfflwpqa sffwlmtaiv ffligvpist
       61 aiekehgqdp slvvidevvg qwlaliflpl fnwkialaaf llfrlfdiwk pfpinrsqsl
      121 kagwgimvdd vlagiyaniv lqivlrsgll r
//
LOCUS       WP_457566125             208 aa            linear   BCT 27-JAN-2026
DEFINITION  regulatory protein RecX [Caldithrix abyssi].
ACCESSION   WP_457566125
VERSION     WP_457566125.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..208
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=24364
     Region          56..208
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 mqitrieras kskphyhlya ddallmtvte etllhfrihk gltlsdalqe eifahdqlqr
       61 cleqayryls rrshfrkela rklttkgypp hvieqaldyl dqkgylndhd lmyqfihdai
      121 rlkqygphli krklfergld seeidaales ayppelqaat cqrlaikkwk slqglepsrg
      181 rqklfaflqq rgfnseniqp vienlfed
//
LOCUS       WP_457566129             743 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Caldithrix
            abyssi].
ACCESSION   WP_457566129
VERSION     WP_457566129.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 743)
  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 743)
  AUTHORS   Scheurwater,E., Reid,C.W. and Clarke,A.J.
  TITLE     Lytic transglycosylases: bacterial space-making autolysins
  JOURNAL   Int J Biochem Cell Biol 40 (4), 586-591 (2008)
   PUBMED   17468031
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   5  (residues 1 to 743)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   6  (residues 1 to 743)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
REFERENCE   7  (residues 1 to 743)
  AUTHORS   Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     'Holy' proteins. II: The soluble lytic transglycosylase
  JOURNAL   Curr Opin Struct Biol 4 (6), 810-813 (1994)
   PUBMED   7712284
REFERENCE   8  (residues 1 to 743)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     A conserved domain in putative bacterial and bacteriophage
            transglycosylases
  JOURNAL   Trends Biochem Sci 19 (3), 106-107 (1994)
   PUBMED   8203016
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18640158
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..743
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=89127
     Region          124..401
                     /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          265..292
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          272..380
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          301..329
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(302,305..306,309..310,312,339,342..343,346..347,
                     349..350,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          334..367
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          372..400
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          565..716
                     /region_name="Slt70-like"
                     /note="70kDa soluble lytic transglycosylase (Slt70) and
                     similar proteins; cd13401"
                     /db_xref="CDD:381604"
     Site            order(595,604,606,608,613..615,618,649,668..672,698)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381604"
ORIGIN      
        1 mkinkylpiv lfvvlldfqa ifnsnwdnvs erqiifnkld klyhqqnfya yydslqnfll
       61 kvnprisdgt kfkfafaayq nkdfkkaarl fselkesgfl psysayfeir siwgmdtsra
      121 lplardylkq yrnspladsl liplaetcyr qkkflearky fqlaierkir ktqrvefkkk
      181 aadclwlsgr kdaalkeyyq iikkhpshqv ceqlvdeleq kasewyrkkf lkiypvlskh
      241 rrydearikl ekfiretsdv klqeearyll vrnyyaqgry staligfknl lanlknkale
      301 pkirlylara ylavgnvqks idlykeyadr yprrrmaaev iwkvalleer mgrlqdalsf
      361 yqklyrrwph ssfgsearfr ygytlfrlgk ieqaervfnk irfsrtkdff knraaywvsi
      421 cremksdtlt asrirrdlar nmwddyytlk syllekeymd stnalikafk rirnplnyyg
      481 kgfqkhidhf ervfliddll grsyavaels tlkidrreiq ewialaetyk rlkeygrayr
      541 lydqinqrfy sklaygeklf ilrerfpyyy dqivdkfcrr yglekelvlg likqesafdh
      601 raksfanayg lmqlipatar dmaflagkrl knidllfdpe fnihlgtlyl kqlhrqfkgd
      661 kakilaayna gphrvkrwlk lnysnhtdgf ieniefketr nyvkrvmkny waykllyndf
      721 qvdrrtllsm eddlenwsla fgf
//
LOCUS       WP_457566121             264 aa            linear   BCT 27-JAN-2026
DEFINITION  4Fe-4S binding protein [Caldithrix abyssi].
ACCESSION   WP_457566121
VERSION     WP_457566121.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Beinert,H.
  TITLE     Recent developments in the field of iron-sulfur proteins
  JOURNAL   FASEB J 4 (8), 2483-2491 (1990)
   PUBMED   2185975
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417435
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..264
                     /product="4Fe-4S binding protein"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30258
     Region          25..229
                     /region_name="NapH"
                     /note="Polyferredoxin NapH [Energy production and
                     conversion]; COG0348"
                     /db_xref="CDD:440117"
ORIGIN      
        1 mipilnvlki tfvtgnyysl riwkiefvdp lfalqdfllt lslnrtlllg liipvviaff
       61 agkifcsfic pynllaewlr kifpgkgrvy pvhsrrywgi lvgwlilaal agfpilyfvs
      121 mpgqigvffs dliflkmvgt esliivvlla ldvvvfnriw crelcpvgal lqrfhykkgl
      181 ivsysemdcv csmnetespc vmrcpihinp ksnkiypscf ncgecvkecy fygealkmnf
      241 mnltanltpr yqlrkeepik keem
//
LOCUS       WP_457566130             371 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566130
VERSION     WP_457566130.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 371)
  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 371)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133569
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..371
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40771
     Region          8..343
                     /region_name="GT4_GT28_WabH-like"
                     /note="family 4 and family 28 glycosyltransferases similar
                     to Klebsiella WabH; cd03811"
                     /db_xref="CDD:340839"
     Site            order(20,197..199,259,281)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340839"
ORIGIN      
        1 mgkktkinvl hletalewrg gqqqiaylvh gllragihta lvappaakvs eyfrknalpf
       61 levkarhgwd lqaarkvarf igenrfnivh ahsshalslg llikllapsv kliasrrvdf
      121 svkkpligal kynnrlidri vcisenianv lmadgvdsgk lsviysgidp drfkaqpaed
      181 lrkelgipre hlvvgtvaal vghkdyptll raaalvvkrn prvtfcavge gadrpqlegl
      241 qrrlglgdrf rfvgfradld rfyalfdvfa lssykeglgt svldalacgl pvvasraggi
      301 vemiedekng llvpprddqa lanallrllq detlrqglar narpsvekfs fkrmvdkhir
      361 lyeqllaggg f
//
LOCUS       WP_457566134             304 aa            linear   BCT 27-JAN-2026
DEFINITION  respiratory chain complex I subunit 1 family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566134
VERSION     WP_457566134.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 304)
  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   3  (residues 1 to 304)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Schneider,D., Pohl,T., Walter,J., Dorner,K., Kohlstadt,M.,
            Berger,A., Spehr,V. and Friedrich,T.
  TITLE     Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Biochim Biophys Acta 1777 (7-8), 735-739 (2008)
   PUBMED   18394423
REFERENCE   6  (residues 1 to 304)
  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   7  (residues 1 to 304)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Weidner,U., Geier,S., Ptock,A., Friedrich,T., Leif,H. and Weiss,H.
  TITLE     The gene locus of the proton-translocating NADH: ubiquinone
            oxidoreductase in Escherichia coli. Organization of the 14 genes
            and relationship between the derived proteins and subunits of
            mitochondrial complex I
  JOURNAL   J Mol Biol 233 (1), 109-122 (1993)
   PUBMED   7690854
REFERENCE   9  (residues 1 to 304)
  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
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Weiss,H., Friedrich,T., Hofhaus,G. and Preis,D.
  TITLE     The respiratory-chain NADH dehydrogenase (complex I) of
            mitochondria
  JOURNAL   Eur J Biochem 197 (3), 563-576 (1991)
   PUBMED   2029890
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..304
                     /product="respiratory chain complex I subunit 1 family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=33060
     Region          6..304
                     /region_name="HyfC"
                     /note="Formate hydrogenlyase subunit HyfC [Energy
                     production and conversion]; COG0650"
                     /db_xref="CDD:440415"
ORIGIN      
        1 mmeaiwtkig yalaslflif nygllligvt mkiiarvhgr igppiwqpyv dilksfsmrt
       61 avshgimfyl gpvfrlaggi glyllipavy gstwlqnfsf sgdlllvmyf iffgmlgmal
      121 gagegghpfs amgimrglsq vtasevpfal avialaaqhq tlsiteivaa qqggiahwnm
      181 vtnpiataag mlaylgmmmh apfnvhmapq eipvgpptey nssflvllqs nrsvfaaakl
      241 ilfmnlffgg atsimemvik tflifqfcvv vgvvfprfkv eqsvrwllka ptligvlavl
      301 iysf
//
LOCUS       WP_457566138             415 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caldithrix abyssi].
ACCESSION   WP_457566138
VERSION     WP_457566138.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..415
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47345
     Region          20..409
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrlltillil isvsfgqqqq lqnlverale nnpalkargh hvqaakelid pagalpdpmi
       61 slglmnvpsn sfafdqepmt gkqlafsqai pfpgklglkk klaeieaqka tdvqgelelq
      121 iirnvkqiyf kifdldraie vternqtvlk nftqiaqtry tvgsgiqqdv lkaqvefarf
      181 edrlislkek raalnaqlna llnlsqdqal ekteiwsfea ndipfdtlks rllknnpvlk
      241 awqknteqsa vrvrlakkel lpdftftfay tqrevlqsgl ggndflsavv glkiplyfwk
      301 kqdkqlqarr fqkkesteqf ndiknrllas lndayqraqk kaeliqlyqa tiipqasqal
      361 nsaiasyqnd qvdfltllnn lmvlfnyere yyrliseyyq qlaqieylta kqiik
//
LOCUS       WP_457566140            1053 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457566140
VERSION     WP_457566140.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1053
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=117386
     Region          1..1037
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mlekiieasi nnrllviift afiafagiya ifntpvdaip dlsdvqviif tdypgqapqv
       61 vedqvtyplt samlsvpyak vvrgysffgl sfvyiifedg tdlywarsrv leylnyvssr
      121 lpagvtpqlg pdatgvgwvy eyvldggdky nlqelrslqd wylryeltsv pgvaevasig
      181 gyvkqyqvev dpnklkayni plnkvkmaik rsnndvggrl vemgetefmv rglgyiksre
      241 dvenipvgvd qngtpilikn ianvsigael rrglaewnge getvggivvm rwgenalkti
      301 ervkqklkel ekglpegvti ksaydrsgli iraidnlrek lveellvval vsiifllhfr
      361 safvavftlp mgilisflim yfqginanim slggiaiaig amvdaaivmi enahkhlerd
      421 rgkkehwqii msaskevgpa lfysllivtl sflpvftlqa qegrlfkpla ytktyamaas
      481 aiiaititpv lmgffvrgri rsekenpisr ilirlyrpvi dfvlrfrwlt iggavvlili
      541 tilplqrlgs efmpplnegd llympttdpg isitkarell qqtdkiiksf pevhhvfgki
      601 graetatdpa plsmiettim lkpkeewrpg mtmeklikel daaiqfpglt nawtmpiktr
      661 idmlstgikt pvgvkvmgpd lqtlsdlaer ianvlkdvkg tlsvfpdktv ggnyldfkin
      721 rleaaryglt vgdvqdvitt aiggmnvtyt veglerypvn vrynrelrdn isalkrvlvp
      781 tptgaqvple yladieikkg ppviksenar rtawlyvdir didvgtyvkn akkavfdkvd
      841 fpegyslvws gqyeymqraq krlqivvpit lviiflllyf nfknvtesmi vmfslpfali
      901 ggiwfmyilg ynfsvavgvg fialaglsae tgvvmlvyld nvyndwkkrg mirkldhlkq
      961 ivvegavdrv rpklmtvatt mlglmpilwg tgtgsqtmkr iaapmigglv sstvltlivi
     1021 paiyflwksr elkrmsaqfa kdeaeenngn etf
//
LOCUS       WP_457566141             719 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Caldithrix abyssi].
ACCESSION   WP_457566141
VERSION     WP_457566141.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..719
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78167
     Region          90..717
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; cd07552"
                     /db_xref="CDD:319850"
     Site            order(372,374,674..675,702,706)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319850"
     Site            order(416..418,478,494..496,523,563..565,585,588,591,610,
                     613)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319850"
ORIGIN      
        1 mnnkkhhden gmkhdadehg hhhsehehse haskhtdqhh hvhqsdegdh aghtqsaghe
       61 hdhaargqkh dhhdhhqmmv adfrkrfwis laltvpvlll spmiqkflgf slrftgdlvv
      121 sfvlasaiyf yggwpflkgm vqelrkkipg mmtlislait vayfysamvv fglagkiffw
      181 elatlidiml lghwiemksv mgaskaleel aklmpseahk lvgedkvidv plnelikgdr
      241 vlvkpgekip adgvvisges svnesmltge skpvykgead kviggsinge gslvievhrt
      301 gkdsflsqvi dlvkeaqesk sktqdlanra afwltliaif aggltffvwm vimhqdlsfa
      361 lertvtvmvi tcphalglav plvvavstai sasrgllirn raaferarnl qaiifdktgt
      421 ltkgefgvtd vvvfdesiqi eelvdlagsv eshsehpiak aisnkaakkl pvqdfkaipg
      481 kgaygmvdgr kvmvvspgyl kqenitinnd tvselfeqgk tvvfvlindr lhgaialade
      541 irpesfeair slkkmgiktm mltgdnkqva rwvseelgld qyfaevlpdq kalkvkevqa
      601 qglivamtgd gvndapalat advgiaigag tdvavetadv vlvnsnpldv vaiislakat
      661 yrkmiqnlaw atgynafaip laagvlyssg iilspamgav lmslstivva inarmlkik
//
LOCUS       WP_457566142             333 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase [Caldithrix abyssi].
ACCESSION   WP_457566142
VERSION     WP_457566142.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..333
                     /product="fatty acid desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38356
     Region          24..287
                     /region_name="Delta12-FADS-like"
                     /note="The Delta12 Fatty Acid Desaturase
                     (Delta12-FADS)-like CD includes the integral-membrane
                     enzymes, delta-12 acyl-lipid desaturases, oleate
                     12-hydroxylases, omega3 and omega6 fatty acid desaturases,
                     and other related proteins, found in a wide range of...;
                     cd03507"
                     /db_xref="CDD:239584"
     Site            order(75,79,111,114..115,273,276..277)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:239584"
ORIGIN      
        1 mkntltlkqi nqqlapfaqp stkkslwelf vtltsylglw tlmvyllkqn vsyvyilplt
       61 vlgglfmvrt fiifhdachg sfcktrtank wigritgllt ftpfeewrqa hnmhhassgd
      121 ldrrgvgdvw tmtvdeykqa sklkrlayrl yrhplvmfgl gpfflflvsn rlpgkdskke
      181 arrgvwltnl aavimvtgis lligfktflm iqipvmfvgg lagiwlfyvq hqfentywsh
      241 ndewnvveas ikgssyyqlp ailhwfsgni gyhhihhlrs gipfynlpac qkqidlfrev
      301 epltiskslk svklhlwder qkkligfkdl kaa
//
LOCUS       WP_457566145              97 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566145
VERSION     WP_457566145.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 97)
  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 97)
  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 10453187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..97
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=10926
     Region          53..80
                     /region_name="TPR_1"
                     /note="Tetratricopeptide repeat; pfam00515"
                     /db_xref="CDD:459840"
ORIGIN      
        1 mppgwqenpd qlnsfawwcf enkinldeaa alakkalela ddpldkanil dtlaeilslq
       61 gkhqeaikae ekaielnpkd klfkrnlekf rqragvi
//
LOCUS       WP_457566152             358 aa            linear   BCT 27-JAN-2026
DEFINITION  mannose-1-phosphate guanylyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566152
VERSION     WP_457566152.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Pelissier,M.C., Lesley,S.A., Kuhn,P. and Bourne,Y.
  TITLE     Structural insights into the catalytic mechanism of bacterial
            guanosine-diphospho-D-mannose pyrophosphorylase and its regulation
            by divalent ions
  JOURNAL   J Biol Chem 285 (35), 27468-27476 (2010)
   PUBMED   20573954
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 358)
  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
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Shinabarger,D., Berry,A., May,T.B., Rothmel,R., Fialho,A. and
            Chakrabarty,A.M.
  TITLE     Purification and characterization of phosphomannose
            isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A
            bifunctional enzyme in the alginate biosynthetic pathway of
            Pseudomonas aeruginosa
  JOURNAL   J Biol Chem 266 (4), 2080-2088 (1991)
   PUBMED   1846611
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..358
                     /product="mannose-1-phosphate guanylyltransferase"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0004475 - mannose-1-phosphate
                     guanylyltransferase (GTP) activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40623
     Region          1..351
                     /region_name="CpsB"
                     /note="Mannose-1-phosphate guanylyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0836"
                     /db_xref="CDD:440598"
ORIGIN      
        1 mhiilmaggm gtrfwprsrk nspkqllnlv gdktmirmty ervkgltddk niliitnqel
       61 keaihqqipe iplkniiaep fgkntapcig laaaivrkra smeepmvilp adhlikevdi
      121 fqdiirtsve yarqndalit lgitpaypet gygyiqrgea vatlnnrtvy kvktfaekpn
      181 leaaqlflqs gdflwnsgmf iwkvgtiwke fvthqpemae gfeeiyqsid snrfeetvld
      241 vymrvksisi dyaimevaqs vyiieadfkw ndvgsweaay aisekdeqqn aitaqnqvvi
      301 dsknnliyap kklvalidve nlavveteda ilickkdssq rvkeviddlk qrnleeyl
//
LOCUS       WP_457566153             310 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566153
VERSION     WP_457566153.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 310)
  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 310)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..310
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35480
     Region          42..70
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(43,46..47,50..51,53,77,80..81,84..85,87..88,111,
                     114..115,118..119,122)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          48..299
                     /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          75..105
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          110..138
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          166..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          196..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(197,200..201,204..205,207,231,234..235,238..239,
                     241..242,265,268..269,272..273,276)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          229..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          264..292
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrwiivfmls illsacavfk ppekaapkia tpaaplkiqs aidslinegi nhhasgndtl
       61 aiacwlkvmn ytdtipdvfn ylgvayqklg qferaldyfk ravqldsayy eafnnagyml
      121 lylnqfdeak kyfekalsln pqferakdnl klveqiltgk lnwqvfslae siqkkgdyle
      181 eiegyqkvlq mdssyakahn nlgviyyyeg ktdsafkhir lalyynpdyp eainnlgylh
      241 keagnydlal rlffkaltlk pryigalnnl getyylkgel qnarrvfetv ldleknnrva
      301 kkwlqkldsl
//
LOCUS       WP_457566161             227 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566161
VERSION     WP_457566161.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..227
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <12..211
                     /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          25..58
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          63..92
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          105..133
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..166
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 tfynlqsfqs cieaaencld lnadynaked lyrligfsym smgqdqkaie nleqsiridr
       61 ssvkqqyalf nlaklyfkhq kyqqawelln eaegfffqnd keywlsilym kgfvkyyqnq
      121 lneaerifee llenapggkq rasalfglaf iafdrkdylk tinlceatak ldenfydket
      181 lgfltaasfh ylgrndvfek yyqqmiktyp egryrkeldm ikskisn
//
LOCUS       WP_457566155             109 aa            linear   BCT 27-JAN-2026
DEFINITION  PilZ domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566155
VERSION     WP_457566155.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..109
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12089
     Region          <31..100
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mgrgakrlet enllafklfd aqkrivlqgv vktidisrtg isidsfdpme vgspieltig
       61 fgenvvkakg tvkncvkrsr ktyhvgiefe ylsdedlnki amvypeilq
//
LOCUS       WP_457566163             570 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Caldithrix abyssi].
ACCESSION   WP_457566163
VERSION     WP_457566163.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19642224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..570
                     /product="peptidylprolyl isomerase"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=66512
     Region          3..289
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase PrsA; PRK03002"
                     /db_xref="CDD:101162"
     Region          126..>237
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
     Region          409..531
                     /region_name="Rotamase_2"
                     /note="PPIC-type PPIASE domain; pfam13145"
                     /db_xref="CDD:432992"
ORIGIN      
        1 mkkilavvgl mvglyilsgc glsddtvarv gketitvddy kfvlqrrfpg kaiakidsaq
       61 rwsilnymie kylqanaakd lgldttrlyl selanfqarl ignkyfekvi vdvlvpedei
      121 reafekqrde vkarhiliqy kgarnskakr skeealklae kvareaksgk tsfnylaeky
      181 sddpsakgnk gdlgyftwgq mvdefqkaaf smkpgeisdp ietpygyhii kvedrrknpf
      241 fdennyqwqk kdikrnryfa hqdtalkmwd ahkkalkeky haelvkanid svarlakkkq
      301 qngyykpkny skaekqivla swnngellld dlflmyegkr faalqrrltn pqkleqtvdq
      361 imlarliene arkmglfedf evktnlkdyk vqklsalays kevkqkvept eeeikayyek
      421 hadefvkpae ieiweislkd kkkaekvlrl arqgynfekl aekytedkyy kkkkgylgfk
      481 tknrrgavsq eafklgenki ggpvryrnmy vvfktgklhp etirsyeeay pqikvrvrnk
      541 klkerreqwl aelkdrytvk inkkvvdnlq
//
LOCUS       WP_457566164             535 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566164
VERSION     WP_457566164.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..535
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=61872
     Region          <173..>532
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mgnmlktlwk vpvvkhaikn kilqqshtvf nkmvkdyleg apnidkaknf vallrelvyp
       61 fkndihvlwn sngnanawrd lteslnyvik nsvrlkmmid rqlvlklkpi nkfivppegl
      121 aideafafkl gqndyflfth hsnddfirqi fknfyyqfyv maialnagle kkrltdqiqr
      181 lknqlleste kiseveknlk krmheidqif qvsnelftih dreglintal ltlvgqlgcd
      241 rafillknkd getfsdfysk gfgseqnvyk lensdalary fesggeilyt demkfkgeaa
      301 dlipffketg armvapvman kkligimacg eklfggdydl idkrifkvls ntinlaftnl
      361 qvyeqvases fvdkntgian kkyfeqrvqe ekslmlrqns tlgllvmrfk nadeifnhle
      421 ehqinrldri viqrispvvr tedflalies gkyallmpgi tdetihiamn rfkekmaslt
      481 lpdefhlkei efefefaifp dqeeafeekv iqllgkkeek tengedfftd ldfnv
//
LOCUS       WP_457566168             455 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Caldithrix abyssi].
ACCESSION   WP_457566168
VERSION     WP_457566168.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..455
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=49405
     Region          11..445
                     /region_name="MATE_NorM_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Vibrio cholerae
                     NorM; cd13131"
                     /db_xref="CDD:240536"
     Site            order(255,259,285,288,367,371,398,424,428)
                     /site_type="other"
                     /note="cation binding site [ion binding]"
                     /db_xref="CDD:240536"
ORIGIN      
        1 mrqfysnyse hlketlrlay pvsiahlghv mlgvvdsmmv ghvgadhlaa aslvnglafl
       61 flvfglglsl vitplvaiar gqknliacgq ilqnglwfnt lftmalsgvi yfaaplltml
      121 nqppevakla vpyaqiigls fipfvvfqsq kqfleglglt kpamfvmlla nlvnvlgnwl
      181 lifghwglpa lhltgagist litrvaqala llffialdrr fksfeislsf kklsmarike
      241 ivrlgiptgf qhffevgafs fsavmigwlg skqlaahqia lsmasmsfmi algitaagti
      301 rvghflgrnd phnlkraglt tvilsvavms afglifvllr yklptlfvkd eeviriaasl
      361 lviaalfqis dgtqaagiai lrgltdvkip milsfiaywi fglpvgyvlg fvfklhvngi
      421 wlgllsglsf agivflfrfy yylkklpisg kpaga
//
LOCUS       WP_457566172             443 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin family protein [Caldithrix abyssi].
ACCESSION   WP_457566172
VERSION     WP_457566172.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..443
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50896
     Region          313..442
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mvsaffwavf wcsivlaaap dtlliktekh kgfgpfrhgv hplkalekdn pwyhaqpeik
       61 gipdslenll vayeevdflq hayqsfkngk ipeeryqslq kmsafdagmn fvsdkplkvl
      121 ipvaagfdsk grlvviadrn nnydlsddpa yvvptklpgq lywgryhdgl pfaidyeyfd
      181 gsqikkgttw lyvdydfsty hlpdsalkkr plqiatnfae yrsgrfelng sqyelviyns
      241 rpvyrgstrl kikkiskndy ranysneikv gekiqigdvf yrfekvlrag eyvklvkvse
      301 vekdsgvevg lqalpfsaaa ldgktidlka lrgnyvllnf wgtwckpcva eipllkeiyq
      361 tysdknfkfi gianderikv kkfveqhkip wpqivqetsk eiinlyqvks ypmtflidpe
      421 gkiiekkirg qrlkqklkei faf
//
LOCUS       WP_457566173              87 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caldithrix abyssi].
ACCESSION   WP_457566173
VERSION     WP_457566173.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 87)
  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 87)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..87
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=10029
     Region          <2..87
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mkgapdliie ilspssayyd lvekkelyeq fgvkeywivd pkkqrievfv lkdkkfvlkq
       61 rierqgnivs tvikdlqinl gtifsqv
//
LOCUS       WP_457566179             606 aa            linear   BCT 27-JAN-2026
DEFINITION  carbamoyltransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457566179
VERSION     WP_457566179.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Parthier,C., Gorlich,S., Jaenecke,F., Breithaupt,C., Brauer,U.,
            Fandrich,U., Clausnitzer,D., Wehmeier,U.F., Bottcher,C., Scheel,D.
            and Stubbs,M.T.
  TITLE     The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic
            reaction
  JOURNAL   Angew Chem Int Ed Engl 51 (17), 4046-4052 (2012)
   PUBMED   22383337
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450873
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..606
                     /product="carbamoyltransferase family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016743 - carboxyl- or
                     carbamoyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68489
     Region          3..594
                     /region_name="COG2192"
                     /note="Predicted carbamoyl transferase, NodU family
                     [General function prediction only]"
                     /db_xref="CDD:441795"
ORIGIN      
        1 mrtyilgisa fyhdsaavil kdgeiiaaaq eerftrkkhd hafpqraiay clkeagisar
       61 qldhvvfyek pflkfnrile tylttaplgi rsflmaipvw lgqklwipdl irkelnyngp
      121 lyfaehhesh aasaffpspf sraailtmdg vgewatssig lgrdnaiell feqqfphslg
      181 llysaftyft gfkvnsgeyk vmglapygep rfvqtileel ldlkedgsfk lnmkyfnylg
      241 gltmtgrrfa qlfggpprkp eapltqremd laasvqqvte eivlrmarhv kkitgekklc
      301 laggvalncv angkllrsgl fddlwiqpaa gdaggalgaa llihyhylkn krqsdekldr
      361 qkgsylgpqf sdeqiktflr svgapfeela edqlyekvaa elakgkvvgw fqsrmefgpr
      421 algnrsilgd arhpqmqrim nlkikfresf rpfapavlee easawfkidr pspymllvad
      481 vhpekrltsd qdmhlkgler lkinrsqipa vthvdysarl qtvnaqtnpr fyrllkafqa
      541 ktgcpvlint sfnvrgepiv atpqeayqcf lrtemdwlam grcllrkedq paqhitkarq
      601 eafeld
//
LOCUS       WP_457566183             603 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor plug domain-containing protein [Caldithrix
            abyssi].
ACCESSION   WP_457566183
VERSION     WP_457566183.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 603)
  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   4  (residues 1 to 603)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..603
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69314
     Region          29..570
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrcilllli flmalygqqs psitfelkep iiitasraps slmsaartvs vldsgaisrl
       61 pvhsvqdalg yiagidlqqr gsqgvqadvs lrgagyeqtl ilidgikvnd pqsghhnlnl
      121 afslqdieri evlkgsgsrl ygpnamggvi niitkkpltk kldfsiiggd frynefnlny
      181 dfqalkanhr lslnrsnssg yrpntdftiq tatyknsfai khnpfhftaa ynakdfgasr
      241 fyhpafpyqk ektetfflnm agqifsdatm ptfspkiywr rhhddflldy trpewyhnkh
      301 qtdvlgaell tafssrlgrt silgewqhsk ivssnlgdhq rnmagfsaeq qftvrrwqiv
      361 lgssfyyynr wgwqispgvd vslqltphft lyasggtgfr pptftelyyy spanrgnpql
      421 kpersvdiea garfrtkrtl tsfglfrryg snlidwifes egqywqaenv lqlttsglev
      481 ssqwttqrhl lknihfnyty ltsdkagrqi iskyvfnylr hqfilgidqq fvnrrlaisw
      541 klryedrins qayfltdvhv swqikrwrif shisnlfdqk yqdfasipqp grwfkmgvrf
      601 svf
//
LOCUS       WP_457566184             149 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase, partial [Caldithrix abyssi].
ACCESSION   WP_457566184
VERSION     WP_457566184.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..149
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <1..132
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 geissydfye afsrdfnlnl syqrfvdywv dvfapipgme dlfwqvkkry pvgllsdtde
       61 lhwnycrekf pfiksvekpt lsfeigalkp dkkcylkaae nvgfapevcl fiddrevnvq
      121 gakkagmqav lfegveklkg dfkklgiev
//
LOCUS       WP_457566186             215 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566186
VERSION     WP_457566186.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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) (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 11459657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..215
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24779
     Region          <114..214
                     /region_name="FtsN"
                     /note="Cell division protein FtsN [Cell cycle control,
                     cell division, chromosome partitioning]; COG3087"
                     /db_xref="CDD:442321"
ORIGIN      
        1 mkllikeqtr lftsgiliil tlsvalfade nwqqwlklyq sgqyaalkqk leqvspepqn
       61 sleylffktl fikdgaravk nyqmiyekss gwlkrlaaqk lhdyyfalgl ylkaegyasf
      121 iketpqekaa spasyktdda kyviqfgafs smnnarkrqk elsqkridsq ivvrkinnkn
      181 fycvwvkgga tfadtdqlak qlkkqlgiey riike
//
LOCUS       WP_457566187             261 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Caldithrix abyssi].
ACCESSION   WP_457566187
VERSION     WP_457566187.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28530
     Region          1..259
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtllitvliv gmlvggissv lglgggiilv palnvvfrlp hseaiatsla tiafitflnt
       61 vrfarrneid wtlvfyllif savssgfggf lvtflseqil laifilfliy vliqmfigyq
      121 srhsvpkqks rwywmsligv ssglisgttg vgggiiitpl lfksrlvkeg hvvpltnaim
      181 flnaffalip lafaqsaehs fwgvglihfd ralllflgai pasilgtkyq aripvklkkv
      241 fialilllil grmifrwias f
//
LOCUS       WP_457566190             319 aa            linear   BCT 27-JAN-2026
DEFINITION  iron-containing alcohol dehydrogenase, partial [Caldithrix abyssi].
ACCESSION   WP_457566190
VERSION     WP_457566190.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Shanbhag,A.P., Ghatak,A. and Rajagopal,S.
  TITLE     Industrial light at the end of the iron-containing (group III)
            alcohol dehydrogenase tunnel
  JOURNAL   Biotechnol Appl Biochem 70 (2), 537-552 (2023)
   PUBMED   35751426
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carpenter,E.P., Hawkins,A.R., Frost,J.W. and Brown,K.A.
  TITLE     Structure of dehydroquinate synthase reveals an active site capable
            of multistep catalysis
  JOURNAL   Nature 394 (6690), 299-302 (1998)
   PUBMED   9685163
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..319
                     /product="iron-containing alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..316
                     /region_name="PDDH"
                     /note="1,3-Propanediol (1,3-PD) dehydrogenase; cd08188"
                     /db_xref="CDD:341467"
     Site            order(33..35,38,41,74..75,77,96..97,115,123,130,134,199,
                     203,213)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341467"
     Site            order(130,134,199,213,217)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341467"
ORIGIN      
        1 fdgvqpnptv gnvdegvaly kkencdiiia vgggspidca kgiglvltng gsikdyegld
       61 ksknpmppfi avnttagtas emtrftiitd tdrhvkmaiv dwhvtpnvai ndpelmvsmp
      121 vsltaatgmd althaveayv stiatpvtds aalkaielig kylrpavang dnmeardkma
      181 yaeflagmaf nnaslgyvha mahqlggfyd lphgvcnail lphvqrfnmi acperfvdia
      241 kalgenvegl stieaadval eaiqrlssdi gipsglkelg vkeedlptla dnamkdacgl
      301 tnprratkee iiqifknam
//
LOCUS       WP_457566159             577 aa            linear   BCT 27-JAN-2026
DEFINITION  carbon starvation CstA family protein [Caldithrix abyssi].
ACCESSION   WP_457566159
VERSION     WP_457566159.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Hwang,S., Choe,D., Yoo,M., Cho,S., Kim,S.C., Cho,S. and Cho,B.K.
  TITLE     Peptide Transporter CstA Imports Pyruvate in Escherichia coli K-12
  JOURNAL   J Bacteriol 200 (7) (2018)
   PUBMED   29358499
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Schultz,J.E. and Matin,A.
  TITLE     Molecular and functional characterization of a carbon starvation
            gene of Escherichia coli
  JOURNAL   J Mol Biol 218 (1), 129-140 (1991)
   PUBMED   1848300
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..577
                     /product="carbon starvation CstA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62100
     Region          1..555
                     /region_name="CstA"
                     /note="Carbon starvation protein CstA (peptide/pyruvate
                     transporter) [Energy production and conversion, Amino acid
                     transport and metabolism]; COG1966"
                     /db_xref="CDD:441569"
ORIGIN      
        1 msvllmvllt ffgyilmyrl ygkylarvif kltdeavvps kefedgidyv ptrkeiifgh
       61 hftsiagtgp ivgpaiaviw gwvpallwvf lgsimmgavh dfgalvismr nkgksiseft
      121 aryinsrtrf ffflivflal wiviaifglv iaiifnifps svlpvwlqip isialgyviy
      181 rrkgniilws viavlllygt mvlgsyfpik mptvagippt gvwtiilliy afwasvlpvt
      241 tllqprdfin ayqlliamfl mtmgilaaav sgrlelvapa iqmhpaeaps mwpflfitia
      301 cgaisgfhsl vasgtsskqv ksepdalfvg ygsmltegal atlviaavaa giglgyhsgg
      361 ktlfgleaws thyaswtaaa glgskiaafv tgaanflssl gipqsiavvi mgvfvasfag
      421 ttldtatriq ryiiselasn inlpvltkrh patafavisa gllafasgad gkgaltlwpm
      481 fgavnqtlaa lalivitlyl rgrgglkwmv sglpalfmag mtlwasilnq lnfvsaqkil
      541 llsingiiil lvlwiavegl ikffsdnqkg vdvqieh
//
LOCUS       WP_457566194             363 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457566194
VERSION     WP_457566194.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 363)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..363
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41378
     Region          5..360
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mnkkywlvii vvliltityf hyhtptsiwq fhlilmqlyf ipillaafqf gvkggvisal
       61 aitvfylphv flqwgglvet nllrflqvll fnvigyltgl kaegerkete kyrklaeklk
      121 elneqqkqqs elllemerkl rmadrlaiig eltaslahev rnplasirgs iqilkeqape
      181 nlkaseffti lehetqrint vvdnylnfar rpaqskstin lyevldilik mveskarkqn
      241 vsiqtafeen lplfdsdpna lkqvlmnlll nglqampegg rlivqarqdn gqliisiidr
      301 gkgmteeqle kifqpfyttk kegtglglsi vkriadennw qikaesklne gsrfdliipl
      361 psa
//
LOCUS       WP_457566196             639 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Caldithrix abyssi].
ACCESSION   WP_457566196
VERSION     WP_457566196.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Baharin,A., Ting,T.Y. and Goh,H.H.
  TITLE     Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure,
            Molecular Properties, and Applications
  JOURNAL   Plants (Basel) 11 (10) (2022)
   PUBMED   35631755
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18487223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..639
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=73537
     Region          <50..>129
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          <194..541
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
     Region          380..632
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrklifmtlm lafslnflvf cqtgkkeqqp plipmedffk nptktsfkls pdgehiaflq
       61 pwksrlnvfv qkigeeqatr itsaenrdia gfawandqri iyvqdkagde nfklyavnid
      121 gsnpavltpf ekvrvgiidd leddpehmii qmnkrdprvf dayrinintg ememiaqnpg
      181 nisqwitdwq gdirlaittd gvntsllyrk dknspfktil ttnfketmqp lffsfedpti
      241 iyaksnlnrd kqalvkfdld nareleviyk hpevdiagvm yskkrkvltg asyvtdrrry
      301 vffdderrql qtdlekllpg yevavvdfnk nedkclvrty sdktrgsyfl ydlnskqltr
      361 ladispwlke eymaemqpit fksrdgltih gyltlpkgle pknlpvvvnp hggpwyrdvw
      421 gfnpevqfla nrgyavlqin frgstgygkk fwelsfkqwg kkmqdditdg vqwlikqgia
      481 dpkriaiygg syggyatlag laftpdlyac gidyvgvsnl ftflntippy wkpyldmfhe
      541 mvghpqrdsl llaeaspvfh adkikaplfi aqgandprvn kaesdqmvea lrkrgvevey
      601 mvkdneghgf rneenrfdfy ramekflaeh lggrmmekq
//
LOCUS       WP_457566197             265 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566197
VERSION     WP_457566197.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..265
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29575
     Region          64..259
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(135..136,139,198,202,242)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(135,139,198,242)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrrasiillp llaflmacst vpitgrkqln iipapqilsm sfqqyeqfls ehkvitgtpe
       61 armvqrvgqk iqnaveryfa ekgmsnrlsg yqwefhlved pqinawcmpg gkvvvytgil
      121 pitqnetgla vvmgheiaha vaehgnerms qgllvqlggl alskaleekp eetrnlflta
      181 fgigsqvgvl lpysrlheke adhlglifma magydpreav kfwermakms ggnkppefls
      241 thpsdetrik nlkkilpdal kyykk
//
LOCUS       WP_457566202             413 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caldithrix abyssi].
ACCESSION   WP_457566202
VERSION     WP_457566202.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..413
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47691
     Region          83..393
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mntvffqnir dfftdlpllk effilalill gsflvylaak rmgnkiarkf aartktrldd
       61 ifiehkviev laffipllii knflfllpli gntvdvivnl lltflsartv stllmagnsy
      121 yelkprarrr piksylqivv ivvyivafii migiltrqpp wmllsglgam taiillifrd
      181 tilsfvagiq inmydllhvg dwiempqfga dgdvidialh tikvqnwdks itivpthkil
      241 ensfrnwrgm eeaggrrikr siyidqnsik fcdqemidrf lkiqlihdyv knkleelery
      301 nrehniddsv mvngrrmtni gtfrayaaay iknhpkinqr ltkmvrqlpp gpqglpieiy
      361 aftndirwev yesiqadifd hllavvpefe lrifqnpsgk dfaqlttqih srg
//
LOCUS       WP_457566206             317 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566206
VERSION     WP_457566206.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  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 317)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>317
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          7..317
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mkalfpdkhy vnleepdtrl faihdprafl sqgpkgliid eaqrvpelfs yiqsmvdrqk
       61 rsgqfiltgs qhfllhekvs qslagrvalf kllpfslkel flhfnqltpf edylfkgfyp
      121 piydrqlrpt dwysayvsty verdvrqlln ikdldqftlf lklcagrigq llnynslane
      181 lgiavntvkg wisvlkasfv vftlmpyyks ynkrlvksqk lyfydvglas yllgirdksh
      241 lqnhflrgel fenlviadli kfaynngfep nfyfwrdqtg heidllidtn grqrafeikt
      301 sstistaffk nltfwqk
//
LOCUS       WP_457566204              99 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin, partial [Caldithrix abyssi].
ACCESSION   WP_457566204
VERSION     WP_457566204.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>99
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
     Region          28..>98
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mkwllsiafi lalstllfgg dilktgskap dfelpdsegk ihrlsdyrgk mvalyfypkd
       61 ftpgctaeac nlrdnydalq kkglvvlgvs fdkpekhka
//
LOCUS       WP_457566207             306 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566207
VERSION     WP_457566207.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>306
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
     Region          1..267
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mkskaqkirl gifiviglll ligmvlilsi ekyfkekdiy yikyenvsvs gldagsavky
       61 lgvhigsvek ieinpqnisq iivtigvrrg tpikqdvvad istigitglk iielrggtqe
      121 apllkpggyi qpgrslteei tgkaevlaek melilnnliq ltdpinqkki iqlveesqla
      181 ikrvnrilak teprlnsmas kldtslthls faarsarttl eriesvvgsd tlkktmrnia
      241 evaeklnkan iynldedlnf avdrlnnllr qmdllinmng vrfnqtmeql nqtvrylnsa
      301 arqide
//
LOCUS       WP_457566208             848 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Caldithrix
            abyssi].
ACCESSION   WP_457566208
VERSION     WP_457566208.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..848
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=98262
     Region          401..843
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mvqtdrfkld rllsplrnff rqepalrkkl fiylaifsgl ffvttgeiip sstvhsiffv
       61 amfifwfksn qiilnkikat pafylavffa agflhnfllg fvnvsadapg likypqlllf
      121 qalwllmiws agllftsesk nrqgylalaa lflfishhll ifghpisqwi fylmifyslm
      181 krstwlenls raelgvylil vfalyvqfqr peyfdqmkki adstdnalwt yslpyllyyt
      241 gkiylivlli kiplvliyny apisrklwla slfqstipqf vqlalllfif flfisgwqad
      301 nlrqevfrlc keavegqktt lkvektsvkq lyhkthntrv ftrdlsvatl qrtsaqklil
      361 ffrpetlsgd slfavhldst flrelfsqtn liigsglvay rfrpnpflay lyrirfwqag
      421 airinplgli npflslkrny ehiltwppna ferenpkile wtklnaypii vgriffslde
      481 ddtyfaidif ydlkdlfqwn fmtqvllili fvfflinslv irrvvklgvq inqliirria
      541 qlrkavrais ggnldyrvtf tgddeftela shfnrmsrdl krfmnearek erlnqelkia
      601 hevqlkmlpt slpkiagyqi aadlttanev ggdfydvfal ddhryliaig dvsgkgmsaa
      661 fymaqiisll rysrpfiddl kklvlqlndf lmkevldsnv fvtiilgild akrstfqyir
      721 aghplpiiie skadqkalke iqtkgiglgi trsasvlekn leikkiklkt gqtlilytdg
      781 fteatieada enkiiygeer fkqhlmrcfh sdpermlici kndlerfyga rpkfddqtil
      841 ilqkepss
//
LOCUS       WP_457566221             171 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566221
VERSION     WP_457566221.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..171
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          1..134
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 vsvellrswi dlarlspssa nlqplkyiis ssaqtnasif stlawagyls dwpgpaeger
       61 paayivilad rkikfpidcd hgiaaqsill gateagyagc iigsiqrnel rqilkipdhl
      121 eillvlalgk paetivleea gkdgdirywr ddkgvhhvpk rplneiivke f
//
LOCUS       WP_457566209             119 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566209
VERSION     WP_457566209.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..119
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          4..116
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 tacidkmarf lgvarnktle ahiltieavv nafehgssar gqvyveftms srelvilvrd
       61 qgsgfdptkv kdpnledkma gshrrgwglk ilktmsdech iesdsngtri rlvknliee
//
LOCUS       WP_457566238             303 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Caldithrix
            abyssi].
ACCESSION   WP_457566238
VERSION     WP_457566238.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..303
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33362
     Region          20..297
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mvhghhhshg hddtrlpttr llitmalnfa itiaeliggl lsgslslisd alhnfsdgia
       61 iiisyialkl kkrsvtprht fglkraeifa aalnsgvllv itlylfyhaa irlinpaeik
      121 gdlmifvagi glianvigtw llarpakdsl nlksaylhll adaissfavl lggvaiyywn
      181 ifwvdpilti liglyilkes yhilqgaihi lmegaptnis idevkqaves lpevnnlhhi
      241 hlwmvgdndi hleghvdved mllsesgqll nkiehllqdk fnikhvtlql ecnhcsnahm
      301 igh
//
LOCUS       WP_457566224             162 aa            linear   BCT 27-JAN-2026
DEFINITION  GSCFA domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566224
VERSION     WP_457566224.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10556255
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>162
                     /product="GSCFA domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
     Region          21..>162
                     /region_name="GSCFA"
                     /note="GSCFA family; pfam08885"
                     /db_xref="CDD:430286"
ORIGIN      
        1 mkfrteinid radqtiqhid piitlgscfa eniskalkeh yfhvlenpfg vlynplsier
       61 alrfiiedkt ftqndlifhq qewhsfwhhs sfshhdaqvc lhnintaiqq ahhflkkarw
      121 livtfgtafv yflkkqktav anchklpete ferrlislae it
//
LOCUS       WP_457566236             200 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Caldithrix abyssi].
ACCESSION   WP_457566236
VERSION     WP_457566236.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..200
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22720
     Region          <96..181
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkklswiigl fmfvlllgcr gqisekppih pvpdmddqpk fkaqeenrff tdgsamrvpv
       61 pgtvargeyh eneeyftgkd engkpidyip eavtlallkr gqeryniyca pchsrvgdgl
      121 gmvvkrgfpp ppsfhqdnir ayadghifdv isngirnmpa ykhqipvkdr waivayfral
      181 qrsqhatikd vpeelrdkik
//
LOCUS       WP_457566212             375 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium ion-translocating decarboxylase subunit beta, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566212
VERSION     WP_457566212.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Kress,D., Brugel,D., Schall,I., Linder,D., Buckel,W. and Essen,L.O.
  TITLE     An asymmetric model for Na+-translocating glutaconyl-CoA
            decarboxylases
  JOURNAL   J Biol Chem 284 (41), 28401-28409 (2009)
   PUBMED   19654317
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Buckel,W.
  TITLE     Sodium ion-translocating decarboxylases
  JOURNAL   Biochim Biophys Acta 1505 (1), 15-27 (2001)
   PUBMED   11248185
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004830
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>375
                     /product="sodium ion-translocating decarboxylase subunit
                     beta"
                     /EC_number="7.2.4.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
     Region          1..375
                     /region_name="OadB"
                     /note="Na+-transporting oxaloacetate/methylmalonyl-CoA
                     decarboxylase, beta subunit [Energy production and
                     conversion]; COG1883"
                     /db_xref="CDD:441487"
ORIGIN      
        1 mhilekmvmn tgfanltagn ivmivvgcia iylaivkkye pllllpigfg vivgnipynp
       61 alplgvydtv angasqnsvl syiywgvqsg vlppmiflgi galtdfssli sspksvllga
      121 aaqigifgtf vgalflgfda lesasigiig gadgptsifl ssqlaphllg piaiaaysym
      181 alvpviqppi mkllitekea rirmkaprav sktekilfpi vtvivaalia pgsltlvgml
      241 mlgnllkesg vtdrlarsvg nalldictvl lsfavgastq asvfltpnsl gifalgltsf
      301 miataggllf akfmnlflke kinpligaag vsavpdsarv vqhyalkydk dnhllmhama
      361 pnvsgvigsa iaagv
//
LOCUS       WP_457566239             788 aa            linear   BCT 27-JAN-2026
DEFINITION  GumC family protein [Caldithrix abyssi].
ACCESSION   WP_457566239
VERSION     WP_457566239.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..788
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=88999
     Region          20..760
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mssekmnmge gypgngkpla qsytgfenee evmklqdylq iilrrkwivl vsflvvflta
       61 vvytinsqpv yqaqatvlvn tqskgqggll lfdptglgfa qnlnneleil ksrsvanava
      121 rellakkyyd nsqeilhcir apeedelgre ilseeeltgv lirtvefepv rdsevikiia
      181 ksgdprdaal ianqfarayy ernlrmsrtr skaareflek qliakqeqla kaeealqrym
      241 eqtgivsvdd esqkvieqla tvqaqyenvs ielesvkesl nfyrkqiarq epnvarimsd
      301 asdpyirllq eeiarlevek ditisqnpha aedpiykekl ikidsqidnl rkklrkrtnd
      361 ylksvlpgql tdpakylvev kqkifdtqiq vqaleakkka lavvlldyqk qfdripkrsi
      421 efarlqrarl saeklyllve ekyqeatiae qsqfgyieii dqaivpklpi spkirmnlml
      481 gallglglgv glvflleyld vsirtpedlk rrgwqplsvi psmdsqmiae laqnkenpai
      541 ddhliallsp rssvaegyrr lrtnlqyarl dkplksflvt spnpkegktt tasnlaitfs
      601 qaglntllvd tdlrrpaihr lfglpkepgl tnhlfgqntl deithkevip hlsvmtsglv
      661 ppnpseilaa pqthelidrl ksmydvvifd tapvlavtda silatqvegt lliilagtti
      721 fdelehsieq lervnahilg vamnnfdikr aygsyygqyk sryygyygyy tyghtggkka
      781 kkkrtets
//
LOCUS       WP_457566243             197 aa            linear   BCT 27-JAN-2026
DEFINITION  GSCFA domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566243
VERSION     WP_457566243.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10556255
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..197
                     /product="GSCFA domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
     Region          <1..136
                     /region_name="GSCFA"
                     /note="GSCFA family; pfam08885"
                     /db_xref="CDD:430286"
ORIGIN      
        1 ivtfgtafvy flkkqktava nchklpetef errlislaei tepwlrlldl lrqfnpqlki
       61 ifsvspirhl rdglpenqks katlilathq lvnssadyfy fpayeivldd lrdyrfyead
      121 lthpnqqava yiwgkfkamf fdrttqqilk emadfykrtt hrfrnpasps aknfmtetea
      181 lrkmllqkyp ylkqrdf
//
LOCUS       WP_457566242             230 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Caldithrix abyssi].
ACCESSION   WP_457566242
VERSION     WP_457566242.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..230
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27370
     Region          9..230
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
     Region          99..203
                     /region_name="HAD_like"
                     /note="Haloacid Dehalogenase-like Hydrolases; cl21460"
                     /db_xref="CDD:473868"
ORIGIN      
        1 mkltfikqil fdaddtlwen nvyyikatnd fldllvekgl nreqlqhefd elelwvvker
       61 gygshnfvyi levlyeryqn lidyrqfksi vqrfedhpnn pklfegvidt lnalkekytl
      121 yvltkgdfke qeqkiinagi dkivngyfiv hekedavyqq iltqrnwkak etcmvgnspk
      181 sdinpalrvg myaiyipyan twkldyeevk pvqgryfkvq rfsdlkdyfl
//
LOCUS       WP_457566246              89 aa            linear   BCT 27-JAN-2026
DEFINITION  chemotaxis protein CheW, partial [Caldithrix abyssi].
ACCESSION   WP_457566246
VERSION     WP_457566246.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>89
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          29..>89
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 metndkntll kerakrlaqk aflpeeikda rtivlfslnn elyaidvqqi raiqpfrgat
       61 qipgvspvva gvinvsgviy tvldlkqif
//
LOCUS       WP_457566251             433 aa            linear   BCT 27-JAN-2026
DEFINITION  anthranilate synthase component I family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566251
VERSION     WP_457566251.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..433
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=48905
     Region          51..432
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 midwvepyle kltfraekeg aftsggapcf ylpgwqlpdg qkveiyieqf favlspagre
       61 qilvkraeqs eeidgdlfrl lksiearrvq sehffyllll sydfgaarng iqheidfysl
      121 pewylilpar gylrygdanq vlrfdagsag lacrpplqtl aqgngaaqse pqtgylkkiq
      181 rirdliasge fyqlnftlrf skpadrpgfe ifkewykktg aprsfylals eaeilsispe
      241 rfwlqkgqtv ltepikgtik rsadagedlr lkqlllkskk draeldmitd llrndlakvc
      301 rtgsvlvkkr hdlrtfshvh hlvsevggrl lpgknfvdli datfpggsis gcpkiaamqy
      361 inrleahnrs fytgsfflrf plrnvtdssi lirtailkdg yvhyqagggi vidsepqkey
      421 eeclakaapf lkd
//
LOCUS       WP_457566250              67 aa            linear   BCT 27-JAN-2026
DEFINITION  macro domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566250
VERSION     WP_457566250.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Rack,J.G., Perina,D. and Ahel,I.
  TITLE     Macrodomains: Structure, Function, Evolution, and Catalytic
            Activities
  JOURNAL   Annu Rev Biochem 85, 431-454 (2016)
   PUBMED   26844395
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Karras,G.I., Kustatscher,G., Buhecha,H.R., Allen,M.D., Pugieux,C.,
            Sait,F., Bycroft,M. and Ladurner,A.G.
  TITLE     The macro domain is an ADP-ribose binding module
  JOURNAL   EMBO J 24 (11), 1911-1920 (2005)
   PUBMED   15902274
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>67
                     /product="macro domain-containing protein"
                     /GO_function="GO:0072570 - ADP-D-ribose binding [Evidence
                     IEA]"
     Region          11..>67
                     /region_name="YmdB"
                     /note="O-acetyl-ADP-ribose deacetylase (regulator of RNase
                     III), contains Macro domain [Translation, ribosomal
                     structure and biogenesis]; COG2110"
                     /db_xref="CDD:441713"
ORIGIN      
        1 mkrvkigsvv lelvqgnian qpemeavvna anamlapggg vagaihsaag pglyeecrpl
       61 apirpgq
//
LOCUS       WP_457566255             197 aa            linear   BCT 27-JAN-2026
DEFINITION  GSCFA domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566255
VERSION     WP_457566255.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10556255
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..197
                     /product="GSCFA domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
     Region          <1..136
                     /region_name="GSCFA"
                     /note="GSCFA family; pfam08885"
                     /db_xref="CDD:430286"
ORIGIN      
        1 ivtfgtafvy flkkqktava nchklpetef errlislaei tepwlrlldl lrqfnpqlki
       61 ifsvspirhl rdglpenqks katlilathq lvdssadyfy fpayeivldd lrdyrfyead
      121 lthpnqqava yiwgkfkamf fdrttqqilk emadfykrtt hrfrnsasps aknfmtetea
      181 lrkmllqkyp ylkqrdf
//
LOCUS       WP_457566261             969 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Caldithrix abyssi].
ACCESSION   WP_457566261
VERSION     WP_457566261.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..969
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=110687
     Region          32..121
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          107..863
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mvakrlvkfi vlflffflsi lslhaqspkg kimgqvtdak sgqplagani yiegatlgaa
       61 sdlegfyyil nvpagkhtvv cqmvgyqtvr ktqvevvvdr ttrvdfrlae aieetepvev
      121 vaqkpavvrd ltatsnfmda reiesapiqg lremmqlnan vtrnpngtfs irgggafdvq
      181 vqfngieqis sntgvpgynf mgeksntswk ydynplgveq mevisggfsa eygnaqsgiv
      241 kvvtkeggse fhgdfrvevr ppgkyhygpy lygpetvewk nwgsfdkwqr wrdenapnip
      301 ddslythcyq kwianhspae gnrsnplgvy dyrklmyrry lfgfggplsk dgklrfflsa
      361 eyrntparip sversqiyqn yslnltyqlt kndklkfltq yqgyrgsvws gsddirwasi
      421 igqwpqykyv lifdspkeet tttqslswth vfssktflea mvwhqrevyi ernrsiitat
      481 dpwliragpw deefrrivya ftslyaldnr tdvwnasvdl tsqvtnrhll kigakaqywd
      541 tryngesgar lnafisysgf aeyyhaypyy falyaqdkie veeivanvgl rfegfnmncd
      601 apadrfrpfy fgtgqgggpf igdpgdprtr kpkthlavsp rfglsfpige dmafrlqygh
      661 fysmplfrqt isrstwqgwr mygnpdlgfk ktisyeiglq kgikghrldi aayyndrvqq
      721 tvrvnihspq gsqqiapqnp yyisyenngy gatkgieisl nriapgdwny rlsysfartt
      781 fgaygamdiy pdpndprsfl errsandfvt sqdrthtfra lisyrlaqkf lkllpdflgv
      841 hsasasmiys aksgtpftyv tsydqftdvi nnrrypleqk tdlsitiksk lwglspalsl
      901 rvenlfndkw ltplldatel rnwveygitr dtppsddpnd pqariykfry yqtyrnmpta
      961 lylslgvsf
//
LOCUS       WP_457566264             849 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457566264
VERSION     WP_457566264.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 849)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>849
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          1..>849
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          66..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..204
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          211..243
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mrkgivillm lffgagllqa eshlmrfadv shdyivftye ndlwlapitg gkakritrsd
       61 greifakfsp dgskiaftan ydggndvyvm nrdgseprrl tfhpasdlvi dwypdgkhil
      121 frsrrewpyr adklykisid ggmpekvnvd raglaalspd gkklaynris refrnwkrye
      181 ggmaqdiwvg tmargdyrpi trfrgtdnfp mwhesglyft sdsidgtmnl yhydfktkqf
      241 tqlthyndyd vkypslgpdh iifqyaesly lldlntrqik pvpiempsdr tlvrefllek
      301 penyvytfal spkgkralln irgeivnmpv eegvtyhltp nssdsrekna iwspdgqwia
      361 ffsdktgeee lylvrptggk wkqitkngfa frtnpkwspn skyiifhdkf mrlnlvdvat
      421 gkitvvdqge yddawydwgi qtynwspdsr wiayskleqs lypsiflynv etgerfrvtd
      481 sftkdwspsf spdgkylyfl snrtfkpimg fvdqnhifln mtrpyililk kgdpspfapk
      541 ndwddedade sesradnvvi ttedfaarii papvkagnlf rleaiddgll ylkktenefl
      601 kyqfvddenr atnlelhrfs lkdqkdetlm egigqyhlsa dkkrliyrag trfgvvdlgk
      661 akvgdgalnf kdvtliidkl defkqifaea wriqrdwfyd knmhglnwqk vresyekfvp
      721 fcgtrgdlny ligemiaeln aghtyvyggd lehgksvrcg llgadfvmen gfpkiarivh
      781 gdnssealss pfeqpgcpik vgdyilgidg lklkknanly qylqnkagkv veilynnspt
      841 vegaktylv
//
LOCUS       WP_457566265             147 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566265
VERSION     WP_457566265.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 147)
  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 147)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 147)
  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 10099350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..147
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          2..128
                     /region_name="Ferritin_like_AB"
                     /note="Uncharacterized family of ferritin-like proteins
                     found in archaea and bacteria; cd01045"
                     /db_xref="CDD:153104"
     Site            order(21,24,89,119,122)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153104"
ORIGIN      
        1 saqkiknsvg krmlerland eknhvvrfkq lyeavtnnsv dqvkfserep ttfemifnrl
       61 kdqlegavee lgekgvddqe iiemaidlen ttrffykeaa qkakdekikn fyellakeed
      121 ahyevlqkal qfledpslff gmgdsrl
//
LOCUS       WP_457566270             419 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caldithrix abyssi].
ACCESSION   WP_457566270
VERSION     WP_457566270.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..419
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48254
     Region          31..410
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 miqrrgrrfl fvclfllfpt lllsqtlsla ecvkqavqas yqlrasefrs qsarkdyalk
       61 kagnlpqffg llsyereqlt pygfsrqwsl lqadwalgdf llktqniaqk raiaagqave
      121 gqrlavarrt vllfiealkq kevnallkqr lhnlqlheki tralwqsgsk neldvlqtea
      181 eilelkeeme ktlsrrrlll nelaliigrs aadslrqlpl nsaqiantpl pvfdeerlkn
      241 hplwrmlqfk veaarltqka vrasqlprlq vsfgfvqdgd ptgdgnywla sagirfplfq
      301 wnrsqiarqk rqmvfktirs eqsaalrqlr ieaqraltel kklkrilqlq qqrvkkteqm
      361 vhlartqyka glitnleflt iqeqftasqi alrntqldya aqlaqfylvt nqpeklqaw
//
LOCUS       WP_457566271             307 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caldithrix
            abyssi].
ACCESSION   WP_457566271
VERSION     WP_457566271.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..307
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33918
     Region          39..306
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mknsrlivlm fftlllacsq hndtlpggad gklriktatv sradmadtvr fygrvslrye
       61 sllasqfdgr lsgfsllpgd qvakeqkige iippqreall qvlpqmdarl rplllkqikt
      121 ipltsplags vlkvfrhngd vlqkgeaivh igdlsildvy gdlplkalpq arhlkeiqvh
      181 fidfphpdma lkvaavaggv drqkqtvair ltlpnpdglf rpgmivrmff pgerhrnvlt
      241 iprsallehe glysafvvkn ntveervlki gikddkriev laglkegerv atqkaysltd
      301 gmevvve
//
LOCUS       WP_457566272            1012 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457566272
VERSION     WP_457566272.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1012
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112548
     Region          1..1007
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkglsrfsve nkralvfsal flavigfyli yqipegvfpd atfprimvia dyglaplkev
       61 emeiakpiee avmmvegvrn vratisrgsa einvdfqwdq dmfrayqlvq aavsgiqhel
      121 ppgiqlevrr fttstypvag ysltsdkldl lqlrdlaiyt irpqlasipg ifnievmggh
      181 qreywvnidp qklaafrldy rqikaalqkt nrlsfvgrln ethklylnia dnrflnlddi
      241 kktivayrdq tpvtlaqiat vepavketfi acesnlkpav lvtiikqpkt navaimnqve
      301 qrwqelarvl ppdvhvqkwy dmtdfikrsi rsvrdaillg alltmiilll flkrlritll
      361 taviipiall itfifiklfg mnlnlmslgg laasigilvd naivvvenie ryleqgkpkk
      421 eavilatgei ippllgatlt tlvvfiplif ltgvpgiffr alastlsiai fvsmllavfl
      481 tpalavifis trpkkpgrfl pqiiavqqrg lrfllrrpva tllfiallgl iavtsylrip
      541 sgflpewdeg tivhdylapp gssiegtksm lksvaqfims lpdveayslr tgrslahprt
      601 handgdfvin lkkghklssf eimdmirefd arheprlepe lfqvlpdrln dlsgeiapiv
      661 ikvfgknlrl iqevaariad slkqvdgavd vyrgfsrgep eltirvspea vgrfgltvde
      721 vqnairfalw gevattmmqg lkvipvriry pkadfnhmek irrlplylsr idrvvelqel
      781 ahiekvpgkt didhenlvqv vnvkahisgr dlgsvigdvk tmlnriplpp gvtiriggqy
      841 esqqrafrel ilillfgall vytillfefk sfrtaavill gtalsvsgvf vlllitgipl
      901 disafmgmim iigvvvnngi lfidyaekfl ketpdvaral lkagqvrlrp ilmttlstif
      961 gflplalalg egsemlqpla vsmiggmsls valslflipg mywivnrpss sk
//
LOCUS       WP_457566262             997 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosylformylglycinamidine synthase subunit PurL [Caldithrix
            abyssi].
ACCESSION   WP_457566262
VERSION     WP_457566262.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Sampei,G. and Mizobuchi,K.
  TITLE     The organization of the purL gene encoding
            5'-phosphoribosylformylglycinamide amidotransferase of Escherichia
            coli
  JOURNAL   J Biol Chem 264 (35), 21230-21238 (1989)
   PUBMED   2531746
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..997
                     /product="phosphoribosylformylglycinamidine synthase
                     subunit PurL"
                     /EC_number="6.3.5.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004642 -
                     phosphoribosylformylglycinamidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006189 - 'de novo' IMP biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=110651
     Region          177..995
                     /region_name="PurL1"
                     /note="Phosphoribosylformylglycinamidine (FGAM) synthase,
                     synthetase domain [Nucleotide transport and metabolism];
                     COG0046"
                     /db_xref="CDD:439816"
ORIGIN      
        1 mqtakhvqiv lkdsmrdvag lhvqsdakkf lhidtgkvkt gkiysivhpm pddtllafar
       61 nslcdciihd lyidrlftse rfpayilisk lpgvtddegv saqkamcdfl nipfdygahv
      121 iftheiyyfe nplnderlkt iaeellgnpl vnrfeygkfs gqvtyipevh lesqpqvqti
      181 difvsdeelq kisrerllal dlhemqaiqa yyqnqlvqaa rekhgisqlp tdceieviaq
      241 twsehckhke fnatitykdl dngaqktihs lfktyirrst eiireryeka ghnwllkifs
      301 dnagvvrvdd qrvfvwkvet hnspsaldpy ggaltgivgv nrdpmgtgvg gasllfntdv
      361 lcfgppdyqg kllpgqlhpr rimtgvvkgi edggnksgip tvngsvvfde ryrgkplvfc
      421 gtggvmpayv dgkpswekri dpgdriimag grvgkdgihg atfssqeide hsprsavqig
      481 spitqknlad fmqvavargl iksstdngag glsssigela tipkgafvql aniplkyagl
      541 qpweifvses qermtlvvep qkvealfala edfevelsdi gyftdsgfld vrygeqkvay
      601 ldliflhdgv ptkrmeaewk kpklsepiik esldyndvll kllgslnics retiirrydh
      661 evkgksivkp lmgqngyapq daavlrldfd syvgiaisng ilprygdidp yqmaagsfde
      721 avrgiiavgg rlpdpqtdpd ifwsvndnfc vpdslyhpqn npdgklklak lvqmnealfd
      781 matffnipmt sgkdsmkndf ikegvkisvp ptilfsmvak ipdvrktitt dfkhegdliy
      841 qvghtydelg asefyhlfge lganvprvrk eqalriyrkm mqaieqqllt sahdcsdggl
      901 avalaecafg gnlgalvelp dfdlslnall faeshsrfvv svapqnqpaf ekimgddafl
      961 igqvsgrqkl eiehqnktvl aldvqtmlda wrsglvf
//
LOCUS       WP_457566273             216 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caldithrix abyssi].
ACCESSION   WP_457566273
VERSION     WP_457566273.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..216
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          <2..193
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 lqrsgarfir hqvqnirrhe dhfiiddqfr ckilvgaggt ncpvyrtffa rhkprqpekr
       61 iatmelefpf awrdshcylw ffdndlagys wyvpkgnghl nigiggkfai lekkkqtiqq
      121 hwqffvnklm qkqlidsepq avkgyqyflr qddqvqmkdi yligdaagla tidmgegigp
      181 aiqsgllaae ailtgqpysi aripkfslwd ilfwwr
//
LOCUS       WP_457566277             267 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-2,3-diacylglucosamine diphosphatase [Caldithrix abyssi].
ACCESSION   WP_457566277
VERSION     WP_457566277.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Bohl,H.O., Ieong,P., Lee,J.K., Lee,T., Kankanala,J., Shi,K.,
            Demir,O., Kurahashi,K., Amaro,R.E., Wang,Z. and Aihara,H.
  TITLE     The substrate-binding cap of the UDP-diacylglucosamine
            pyrophosphatase LpxH is highly flexible, enabling facile substrate
            binding and product release
  JOURNAL   J Biol Chem 293 (21), 7969-7981 (2018)
   PUBMED   29626094
REFERENCE   2  (residues 1 to 267)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..267
                     /product="UDP-2,3-diacylglucosamine diphosphatase"
                     /EC_number="3.6.1.54"
                     /GO_function="GO:0008758 - UDP-2,3-diacylglucosamine
                     hydrolase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31071
     Region          45..249
                     /region_name="LpxH"
                     /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxH
                     [Cell wall/membrane/envelope biogenesis]; COG2908"
                     /db_xref="CDD:442152"
ORIGIN      
        1 mfehvyqsgy ltsleqesha fakqlirqle gphfesyfgv avetfdtmii sdihlgskvs
       61 rtrkliellt svrfkrliin gdvfdsinmr rlnkehwqvl sllrkltnsk sdheviwirg
      121 nhdgysdllt qllgikiyne ylfsiadkka lalhgdifds ftsrfplvsd iadylyrlsf
      181 yvdpiklrfs rwlkrnsktf irntvkvrer amayarhrqa dyvicghthh adeyqegnit
      241 ylncgcwtea pshfvgilge qvkvipy
//
LOCUS       WP_457566279             376 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566279
VERSION     WP_457566279.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 376)
  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 376)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..376
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=44910
     Region          6..285
                     /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          35..63
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(36,39..40,43..44,46,70,73..74,77..78,80..81,104,
                     107..108,111..112,115)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          68..98
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          103..130
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          150..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          187..217
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          222..250
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          229..361
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          255..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(256,259..260,263..264,266,291,294..295,298..299,
                     301..302,330,333..334,337..338,341)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          289..324
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          329..357
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mhdiqlkiqe lekkhqwqqi idllkplvqq geisvyilra lgfaysqldr ynearycykq
       61 wielephraq pyyhvgftfy dagqwneave wfeqalerfp dymvclyrkg valfmagknr
      121 kakedlkkai vvyqnaddve fkrrlskyyy rsifylgkcy lqirfyknar acfekilaed
      181 rrayiddlyv kynlalslmh lkefaraeqi vaeltrlkpr aewlydfwgr llvkqqryve
      241 aieklelalk irvqpyilid rarahfligk tqlakadlne alrrdrkgkh killelakia
      301 lqekqfaqam syarraiefk qriyeadyae ahlllsdiyr atgenqkaqq efqiaqelcp
      361 dlaweddlll ktriil
//
LOCUS       WP_457566284             637 aa            linear   BCT 27-JAN-2026
DEFINITION  Na+/H+ antiporter NhaC family protein [Caldithrix abyssi].
ACCESSION   WP_457566284
VERSION     WP_457566284.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Pragai,Z., Eschevins,C., Bron,S. and Harwood,C.R.
  TITLE     Bacillus subtilis NhaC, an Na+/H+ antiporter, influences expression
            of the phoPR operon and production of alkaline phosphatases
  JOURNAL   J Bacteriol 183 (8), 2505-2515 (2001)
   PUBMED   11274110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..637
                     /product="Na+/H+ antiporter NhaC family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70334
     Region          342..>613
                     /region_name="NhaC"
                     /note="Na+/H+ antiporter NhaC/MleN [Energy production and
                     conversion]; COG1757"
                     /db_xref="CDD:441363"
ORIGIN      
        1 mrffriflil flilnlnllf gqsptlenkk vvylshlkyd lilshagads sslseiylet
       61 antrvplnar fdsstqkiil pavsfpqsgh yrlvaknlnw qtelkvipnw lsilppfvai
      121 vfamlfrqvi islffgiwlg vtflfdynpf sgflntltey igkaptdper mailifslal
      181 ggmvgvisrs ggtmgivhsl rrfasnrrkg qlatwlmgvl iffddyantl ivgntmrplt
      241 drlkisrekl sylvdstaap vatmaiistw igyqlslmnd sfqtlnldln ayivfiktip
      301 ynfypifslm fgffiaffnr dlfsmyraek rcvtkgtvlr egavpladle nselkpkegv
      361 plrwynalip ilvviittls glwftgyyna saqgllsenm sglryvslvv gsadsfsvlm
      421 wasfsggiva ivlalvqril nldqtlqawv ggvkamvmaa iiltlawaig nictdlqtan
      481 yviyltrdfl sphlipviaf isagiialst gtswgtmail ipivipmayq lpkldptigp
      541 llqdhiflss iasilagatf gdhcspisdt timssmatga dhvdhvrtql pyalisalis
      601 liagylligy gaspwlslfi gliliiliir flgkkve
//
LOCUS       WP_457566285             353 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Caldithrix abyssi].
ACCESSION   WP_457566285
VERSION     WP_457566285.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..353
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39614
     Region          4..333
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdfnkvrvav igvghlgsih aklyteipea elvgvfdidr qtcervagel nvkafesles
       61 lwpavdavni vtpttthfni amealqnnkh vfiekpvtdk ifqaydlkkf aehkglkiqi
      121 ghierfnpav laltdvqinp lfiethrlat fkprgtdvav vldlmihdid lvlkfvksep
      181 trisangvgv vssnidiana riefkngcva nltasrisak kmrkmrifqk dayismdfne
      241 gyseifylen eehpifengt lalslgelel gelrreikyn rlkrddvnpl qlelisfida
      301 vknnlepait iqdginalgl aqkvmkeinr hqkylsrqmg laihqsavkn aee
//
LOCUS       WP_457566286             391 aa            linear   BCT 27-JAN-2026
DEFINITION  alanyl-tRNA editing protein [Caldithrix abyssi].
ACCESSION   WP_457566286
VERSION     WP_457566286.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..391
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA deacylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) deacylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=44909
     Region          1..230
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mtekfyyhnp ytakivatvl dvrekdgerw vltdqtvfyp ggggqlpdrg liekqtvtdv
       61 kekngkiwhk lqkdasqfvp gqkvtmeidw pyrfyqmqqh tgqhllsavl eragwptvsv
      121 hlgeahtlie vegrlpetae lhnlekqaqt miaralavkt hwvtaddmdr fplrrppakf
      181 dnlrvveieh ldysacggth lqntaeigli kivgcekirg rarikalige rafeymeqlh
      241 qtsvllrekl ntdhlqfner vaqlqeelhy lkrlkkfyqq yfvnftsrel aestnealvv
      301 fkmeqgeqdd aaaiakklsq tyhkvaliqf drrffltsps aerfdtikfi kenaehleir
      361 gggpqgycqg vmkrnnlnqi aetvnmalks i
//
LOCUS       WP_457566287             269 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566287
VERSION     WP_457566287.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..269
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29925
     Region          2..254
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mikkisknrl kffrqlqkkk yrqehglyvv sglravqeal saaeiaiesv lideaqlhlm
       61 nelprtidke vltlsgdefr qlveektpqg ialvvkkphf sldvrrlpqa llyleeindp
      121 gnlgtlmrsa awfgwqaill sknsvdpyap ktvrasagti ahlqiyenvg aaeleqlkka
      181 gryrliaasa htgqelttft lnsrtkriva lgseahglsk riltlsdwqv nikrpgkges
      241 lnlamagtif lyhftlissl dfkgagkhe
//
LOCUS       WP_457566300             482 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Caldithrix abyssi].
ACCESSION   WP_457566300
VERSION     WP_457566300.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..482
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=52575
     Region          4..481
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mtandwlklm pliilaatpl vmmlaisvkr shviavvlsv igllvsfiav paaysasgdq
       61 igklliidky alfyfvlmfw atiaiiipsy qylemrfkgn reeyyllmlt atlgsavlaa
      121 sthfvsfflg leilsvslya liaylrqtne gieagfkyli laavssafli fgmalvfakt
      181 gsmefgaiia flkeksnydl iavggvalmm vgfgfklavv pfhmwspdvy egapapvtaf
      241 iasvskggil allfrffgdf nivqskplfa ifaviailsm fggnllallq tnikrllays
      301 siahfgyilv afmagnaqqn fkgveaatfy ivsyfitiig afiivgliss eeregmelke
      361 yrglywrhpw lsvalsammf slagipltsg fiakyyilss gisvklwtlv iiliinsalg
      421 vyyylrvtve mfsnvneeek agllkpnvgi fsglllallt valvwlgvfp tgliasiqaa
      481 mf
//
LOCUS       WP_457566304             203 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Caldithrix abyssi].
ACCESSION   WP_457566304
VERSION     WP_457566304.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 203)
  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 10119458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..203
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22243
     Region          7..195
                     /region_name="MurNAc-LAA"
                     /note="N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA
                     (also known as peptidoglycan aminohydrolase, NAMLA
                     amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC
                     3.5.1.28) is an autolysin that hydrolyzes the amide bond
                     between N-acetylmuramoyl and L-amino...; cd02696"
                     /db_xref="CDD:119407"
     Site            order(10,24,84,165)
                     /site_type="active"
                     /db_xref="CDD:119407"
     Site            order(10,24,84)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:119407"
ORIGIN      
        1 mavfctdagh ggvdsgavwq gvrekdinlq vtlqlnqwlk qkghrvfttr rsddhvpplr
       61 trcklvnahh rqkapafdai isihcnvaar fepslddylp lpqrrglyvi yseesqagtq
      121 laqviarack eqgiqlahgg kistvelgrs lawihqtlpp avlvelgflt npeerallqd
      181 asyqqtliqa iaaglenais pvt
//
LOCUS       WP_457566305             195 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566305
VERSION     WP_457566305.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..195
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
     Region          <1..145
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 kmgintigdl arfppqvlkq klgsagehfy rlahgfderp vitreevksv snehtfgkdv
       61 ddmdvvrkql vylaekvgyr lrkkglkgkt ihlklrydnf stitrnmtis pptnqtrqiv
      121 dvaldlfekn yisgrkvrlv gvgvsgfdtq aarqtnlfdv ldekqqkldq vqdlladrfg
      181 rhivqraesl kkkkk
//
LOCUS       WP_457566311             163 aa            linear   BCT 27-JAN-2026
DEFINITION  FliO/MopB family protein [Caldithrix abyssi].
ACCESSION   WP_457566311
VERSION     WP_457566311.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Fabiani,F.D., Renault,T.T., Peters,B., Dietsche,T., Galvez,E.J.C.,
            Guse,A., Freier,K., Charpentier,E., Strowig,T., Franz-Wachtel,M.,
            Macek,B., Wagner,S., Hensel,M. and Erhardt,M.
  TITLE     A flagellum-specific chaperone facilitates assembly of the core
            type III export apparatus of the bacterial flagellum
  JOURNAL   PLoS Biol 15 (8), e2002267 (2017)
   PUBMED   28771474
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Simpson,D.A., Ramphal,R. and Lory,S.
  TITLE     Characterization of Pseudomonas aeruginosa fliO, a gene involved in
            flagellar biosynthesis and adherence
  JOURNAL   Infect Immun 63 (8), 2950-2957 (1995)
   PUBMED   7622217
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..163
                     /product="FliO/MopB family protein"
                     /GO_component="GO:0009425 - bacterial-type flagellum basal
                     body [Evidence IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=17614
     Region          42..163
                     /region_name="FliO"
                     /note="Flagellar biogenesis protein FliO [Cell motility];
                     COG3190"
                     /db_xref="CDD:442423"
ORIGIN      
        1 mltlrkilgm vcviavlaat gaaqtqtffa dtsaqmsdst vpaaqqfeqt psltghyikl
       61 llitfvllga lylilrilrk lqygnttlkn epirvlskty lsskhslwvv ivgrnkyllg
      121 vtdhsinlid nlgpaaeeel lsaspgalps fgnlldkikr tss
//
LOCUS       WP_457566312             162 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar basal body-associated FliL family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566312
VERSION     WP_457566312.1
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 10003978
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..162
                     /product="flagellar basal body-associated FliL family
                     protein"
                     /GO_component="GO:0009425 - bacterial-type flagellum basal
                     body [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0071978 - bacterial-type
                     flagellum-dependent swarming motility [Evidence IEA]"
                     /calculated_mol_wt=18247
     Region          1..161
                     /region_name="FliL"
                     /note="Flagellar basal body-associated protein FliL [Cell
                     motility]; COG1580"
                     /db_xref="CDD:441188"
ORIGIN      
        1 maeekvqeak nptkwgliia lfgvqilvav alvyflilpr lspassgepe aqkkeqkvdk
       61 kepgilvtid nltinpkgsf grryavfeva levpdekaka eiekfkpkiv dayllylrsk
      121 tvedltikld idlmkqemve kvnmilgqpl vqnlyftrfv le
//
LOCUS       WP_457566313             226 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook assembly protein FlgD [Caldithrix abyssi].
ACCESSION   WP_457566313
VERSION     WP_457566313.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Moriya,N., Minamino,T., Imada,K. and Namba,K.
  TITLE     Genetic analysis of the bacterial hook-capping protein FlgD
            responsible for hook assembly
  JOURNAL   Microbiology (Reading) 157 (Pt 5), 1354-1362 (2011)
   PUBMED   21349976
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..226
                     /product="flagellar hook assembly protein FlgD"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=24784
     Region          1..226
                     /region_name="FlgD"
                     /note="Flagellar hook-capping protein FlgD [Cell
                     motility]; COG1843"
                     /db_xref="CDD:441448"
ORIGIN      
        1 mgdminsitn tnvvnstqqn ivsdnadlgk yeflqllvtq lknqdplspm qsqdfaaqla
       61 qfsslerlmd idnslqqgmd admllaqtih ntmattfigk evlaygdsfs llsgesasls
      121 felngsvkea tieiydendq lvrtikmtel ekgrhsvewd gmdeagnaln ggiyhfkvka
      181 ideqdnavtv qtftrgivsa vkyeqgqpvl lvdgkeiyfg evvqig
//
LOCUS       WP_457566318             394 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Caldithrix abyssi].
ACCESSION   WP_457566318
VERSION     WP_457566318.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..394
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46784
     Region          80..383
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 midnpsilli ftgagprsvn vkkwldlfan sevqisimfr nitqqekqnl kkhyphlnfi
       61 ffktinelkn lslikryqyi reisctidql kvdvihlhga fynymvyplf flktrpvliy
      121 nvwgsdfnlk fkkklkntfi lkalikksdl vltnwfqlal eikehfpslk ekiktipwgv
      181 sdelfnppnq eyirrlkref giaddeyvll ytrglvqnsn hdkllksisl ipenlkfkli
      241 ihntksksvi aqnlkkyvqk kgldrkvifs ehylsdsqmq alyhmadlvf slttkeqfsq
      301 viveailadc hlilhqnpay hflkevfrfn ielvdvfkpa qlaqrieyfi qnrfrpqyqy
      361 ekmvidrlfr fsakrneflk lyrdliaekm gken
//
LOCUS       WP_457566321             408 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Caldithrix abyssi].
ACCESSION   WP_457566321
VERSION     WP_457566321.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..408
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46905
     Region          240..397
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mkrfsslvil vflfltfcsk mttntdhpvn feagqlslti dmkkapaeva ylkgflarad
       61 hdtiffdfei vdglayatin evengewylq vdaydesgnr kysgsvyvfv eagkitpvfl
      121 nlvkifggid itvswggvpq nmmllmalna sdnwrillmk edgskifdli dgrypmwind
      181 qrdkfmflrn gdelcefdls thnvkfiasl gvnanflfys rplnrilfdy kyfgdysylw
      241 qlasvnvdgq dfhtilsdts kkkypatppn sdwiyyhvnh ngrfqiyrik hdgsqnqpvi
      301 agdfhcefps fnrsgqqmvy tkisldssyk avvihnltth qeqeidvsql gqptypafsy
      361 dgadvifsvi vgpehkdrql frfntntnnl tqitagreyf wyarpvfw
//
LOCUS       WP_457566322             371 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Caldithrix abyssi].
ACCESSION   WP_457566322
VERSION     WP_457566322.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..371
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41935
     Region          12..370
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mqvplldlka qyrtikheid pvvqeviesq yfilgpkvae feeavanycq anyalgvssg
       61 tdallialma idiqpgdevi tttysffata gsiarlhakp vfvdidpqtf nidpakiedk
      121 itektraiip vhlygqmadm dpimeiarkh nlyviedaaq aigseyvdgr ragsighigc
      181 fsffpsknlg gfgdgglvtt ndqklyeklk ylrnhgahpk yyhkmiggnf rldalqaavl
      241 nvklkhldew tagrqknadf ydqgieqral qkyvtppvrk egyrhifnqy ilraqkrdel
      301 vqylkehqig ceiyypvtfn nqecfkylgy gkgdfplaek aadetlaipi ypeltddqkn
      361 yvldtilnfy k
//
LOCUS       WP_457566324             315 aa            linear   BCT 27-JAN-2026
DEFINITION  1-aminocyclopropane-1-carboxylate deaminase/D-cysteine
            desulfhydrase [Caldithrix abyssi].
ACCESSION   WP_457566324
VERSION     WP_457566324.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Thibodeaux,C.J. and Liu,H.W.
  TITLE     Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase:
            characterization of an unusual pyridoxal 5'-phosphate-dependent
            reaction
  JOURNAL   Biochemistry 50 (11), 1950-1962 (2011)
   PUBMED   21244019
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Nagasawa,T., Ishii,T., Kumagai,H. and Yamada,H.
  TITLE     D-Cysteine desulfhydrase of Escherichia coli. Purification and
            characterization
  JOURNAL   Eur J Biochem 153 (3), 541-551 (1985)
   PUBMED   3908101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..315
                     /product="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35220
     Region          6..313
                     /region_name="Acd"
                     /note="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase, PLP-dependent ACC
                     family [Amino acid transport and metabolism]; COG2515"
                     /db_xref="CDD:442005"
ORIGIN      
        1 mkypkhlhft qlntplvklk dhpfgyqlyv krddftgiel sgnkvrkldf llqealtkga
       61 krvitcggvq snhcrataym atklglkttl vlkgeepenf itgnfllnri igadihfise
      121 tayqhvdeym selagrysek tyvipeggsn algawgyvka fdeitqqlpe adaivaptgs
      181 igthagllfa rwlkkhpcqi vsinvcdtad ffrqkllhla qdfklqfapq mtiyeddihi
      241 vdgfvgtgyg qvtereiski kevaqkygfl ldpvytvkaw mglemllkeg klpgekivfl
      301 htggifglfa hgnrf
//
LOCUS       WP_457566328             122 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase, partial [Caldithrix abyssi].
ACCESSION   WP_457566328
VERSION     WP_457566328.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>122
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          13..>122
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 misntellkr lqktkalild mdgvlvdtep lhmeafarfl dalklpfdnd flygfigfsv
       61 pdnirkiyne rlhitdetvi qqgikqrdai ylkllestpl hplpgieglv dycqkkqfkl
      121 gv
//
LOCUS       WP_457566331            1204 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566331
VERSION     WP_457566331.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1204)
  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 1204)
  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 1204)
  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 1204)
  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   5  (residues 1 to 1204)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 1204)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18685335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1204
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>1204
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          5..868
                     /region_name="COG3292"
                     /note="Periplasmic ligand-binding sensor domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:442521"
     Region          773..1144
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          1156..>1201
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mikklflllm lgatlwaqey pvhfytieeg lpsneiysiv qdsigemwia trrglckydg
       61 fhwqldttig kmgmylphfl elddagrvwv ggvhigqgfc ylnnktwhti slpdslalfs
      121 plktfkvigs sdghifilav thknqlayff qnqwkvidls ridpesskil tvsknnnqfl
      181 iltdrrlltf ngtdfkefdf pplfekekii slqvletphs pakmgrllll tpnyiyeyqa
      241 peiikkipln kqvkslladp pfqliedgfg gvflgnkfrl fhfnnylnkw vlikhhripe
      301 pldaidiyld qeknlwiasy mgllkiptlr flnfneysgl letevtsinq fgrgtmifgh
      361 dngftlydgk qfkkfaigdv qapsdrsrkr fmeflkltdd tiiaaaqqmg lvkihqsgry
      421 eiippppger intvaklnkk ellvgtyhgl fkfsnnafyp ylheltkhli irrmllladh
      481 tlllatlnrg vvviredqki sevwnhrhlk sksvydikys pqgkilvata aglfefsqds
      541 lipvdkelin eeayailvdn enkiwigtgr gvqiidsign ithydyfngl agqecnrdal
      601 fqdssgriwi gtigglslyq plydfkvrpp linfldfisd idfdlqpekk gdliikflci
      661 sfkderqial ryrlkgyhew qyiprlfapv lsfldvppgd yqlevqarnv egawsavvqs
      721 stfhipapfy rswyfialvl flisiityll vfarikerla qqleaevnar tkalkeseek
      781 frrlftdsld gifitsiegk mldineagie ilgydskdel lklnvkkdly anpedrekil
      841 tliktqggvk nyplkakrkd gkiidvaisa tpildeqgnv vglsgyfrdm tewnamkeql
      901 ahsqrmeslg mlaggvahdf nnilagilgy aslmkmkmdp ddkmfryidi ieksaqraad
      961 ltqqllifsr kgqpklqpvq vnecvnetik lirstfpkti eieteldekl peimadptql
     1021 sqmilnlcvn ardampdgeg kisfrtrevi vehpeayknp dareghfvql tiadtgsgip
     1081 deiknkifep ffttkprgkg tgmglamvyg fvrnlggfiq fhsklnegtt fqihfpvkpi
     1141 hleekhlshk selktghghi lvvddeemvr nfckmalery gytaetasng qealdcftkn
     1201 qnnf
//
LOCUS       WP_457566332             342 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Caldithrix
            abyssi].
ACCESSION   WP_457566332
VERSION     WP_457566332.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..342
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37928
     Region          45..341
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mritgillll fsfalvingc skekdeaknl eqiyaekgip vkvqtvqpap fqkasyynai
       61 lrgfressvf aalgdridki yvkvgdyvqk dqvllsfptd npaaqyyqak vafenarrti
      121 ermkkllksg gisqqdfdna qtqfevaran wdavkqavkv kapisgyvtk invretdnvd
      181 vkaelatitq tdrmkaeiwi aeseineihd glpalarwng feikgkviqv nmamdlkqra
      241 fkailefdnp dntvksgvta eieivtidre kaivvdqtsl lkeggqhyvf vnnngkaekr
      301 pvkigpqsga kvllleglkp gdqlivegqf llkdgskini ig
//
LOCUS       WP_457566333            1033 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Caldithrix abyssi].
ACCESSION   WP_457566333
VERSION     WP_457566333.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1033
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114221
     Region          1..1014
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfladisikr pvmvtmgllv filfgalayf gltldlmpqv dipvitvqtv ypgagpkeie
       61 nqvskkieda vgtiskldfm qsysmegvsf viiqfklgkd idianqeikd rinsilnqlp
      121 rdiqlpvvek fdvsafpimd vlltgnmplt elyeladkkv kdrlaqiegv gkvnviggqk
      181 reirialdnr vvfenaislp qlsqilaaqn lnlpgghfiq gsqelsvrvd gefdrvealk
      241 kleiptafgm qqlgklatvs dagaeirqrs iffdnknkir qdnvvllsii ksadgntvkm
      301 aeeirkelpn ikaelppaas isiihdrsnf ikssvedtln niilgvlftg lvllfflhdl
      361 rstiivalam ptsilstlll iklsdfslnv mtlmglstav gilvtnsvvv lenifrhkem
      421 ghrrrdaagk gtaeiavavi astltnivvf lpiasmtsiv gqffkefalt vtyatifsli
      481 vsftitpmla slllpevetk khrlgqrlea mfhrweqwyq silvwmvksk ksafsvvaft
      541 vllfvvslfv aarvgfeffp ltdegdilie lelpqgyqle esarlvntve erlrkhnevk
      601 hilttigmls dldvgvnlak mqvklvdvsm relrsdqian qfiqeladip nakirvaais
      661 smggdqapit fylmgqdndr levykrqime kirkipglin lntssrsgkp eitikpyrqr
      721 laetgltvtd laftiraame glvttryrea gneydirvtl ddravdspee iknltvvspr
      781 giyrlaqlat fevsqgyski mhkdkykaie ftaynapgvp lgevvaqinq kmseidfkpg
      841 ykydwggdaq mmaetttdml rtfliaialt ymllaaimes ftqpliilgt iplgligvfw
      901 alfitgktmn tismmaivml vgivvnnail lldytnilrr qgkkvkealv eacptklkpi
      961 imstvaimlg maplalgigs sgveirqpmg ivsiggllvs agltllvipa lyflttqsdk
     1021 dakseslkte tek
//
LOCUS       WP_457566334             440 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Caldithrix abyssi].
ACCESSION   WP_457566334
VERSION     WP_457566334.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..440
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50315
     Region          25..433
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkpikwtlll tflllvgsvq aenydlaafi elvkknsddl klaakelema aaqkreawat
       61 alpkisaegn yrrnlletyl yvdfptadgs lvrqkfkitk nneytftaal lqpifsfkvg
      121 talraakqye rmsqfifqss dqeiitfakk gfyqalllkr vwqlkeetvk narenynmvk
      181 kqyqaglase fqlyqaevrw knsipeaqqa rknyelllyn lktlagldle aqvdfvgnle
      241 kvppmpepls fdriienrpd ykaqlweqkl rrtavaaakg eflptvdgtf ayafsaqsdl
      301 wklenknnnf ilglklsipi flggyniaqv qkakieldks rlrlqkarkq iatelksiyl
      361 rldeaqksik aaesalqtae kgfqiaqtsa qnglitqlel kdarlqydga rlnwylavyn
      421 yldayfdwqk avgkvdelve
//
LOCUS       WP_457566342             234 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566342
VERSION     WP_457566342.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>234
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
     Region          20..>232
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
ORIGIN      
        1 melisaksfr kklqgvdvdl itlkndggmq mqvtnygarv vslltpdehg nlsdvvagyd
       61 dldayvqdpy yfgaiigrca nriadgkfsl fgksyqltln vgkdhvhggi fglhakvwim
      121 eqlserevll svgspngeeg ypgsvhfear yllrednsvy isltarsdqp tivnmthhsy
      181 fnlsgftsss dtsqnildhr lkveadyftp inerllptge irpvagsald frdf
//
LOCUS       WP_457566340             556 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Caldithrix abyssi].
ACCESSION   WP_457566340
VERSION     WP_457566340.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..556
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61546
     Region          27..545
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mknesddilk sqfdfasqvs qanreywqke kariqeerka ihlgggpkni erqhaknrlt
       61 arerikhlid pgtvfyelgt yaaykmyeew ggapaagtic glgyiegrlc miiandatvk
      121 agsffpmtak kviraqtiaf knhlptiylv dsagiflplq edvfpdqddf grvfylnarm
      181 sakgipqita imgmcvagga ylpvmtdtvl mtegsglflg gpalvraaig qvvsaeelgg
      241 atmhaeisgt idfkepndpa alkhirklvk qmghakqspi rrieardpry pigdlykimt
      301 fnptqeydvr eiiarlvdns efveykkdyg qtlvcgyahi ggypvgiian qkrhirkkgk
      361 ppqfggviyt esaekaarfi mdcnqntipl lfihdvngfm vgleaeqngi ikagakmvna
      421 vsnsvvpkis liiggsygag nyamcgkayd pnfiyswpts kyavmggaqa antlldlrvr
      481 qmersgkkls daekeelfkt iketyeeqtd pryaaarlwv delilpeetr qrlivtleav
      541 snipefetfn pgviqt
//
LOCUS       WP_457566297             414 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF and HD-GYP domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566297
VERSION     WP_457566297.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Sequence Conservation, Domain Architectures, and Phylogenetic
            Distribution of the HD-GYP Type c-di-GMP Phosphodiesterases
  JOURNAL   J Bacteriol 204 (4), e0056121 (2022)
   PUBMED   34928179
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Sun,S. and Pandelia,M.E.
  TITLE     HD-[HD-GYP] Phosphodiesterases: Activities and Evolutionary
            Diversification within the HD-GYP Family
  JOURNAL   Biochemistry 59 (25), 2340-2350 (2020)
   PUBMED   32496757
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Wigren,E., Liang,Z.X. and Romling,U.
  TITLE     Finally! The structural secrets of a HD-GYP phosphodiesterase
            revealed
  JOURNAL   Mol Microbiol 91 (1), 1-5 (2014)
   PUBMED   24236493
REFERENCE   4  (residues 1 to 414)
  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   5  (residues 1 to 414)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12186785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..414
                     /product="GAF and HD-GYP domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46907
     Region          23..184
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
     Region          <181..393
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mlshtqklnr lvefgleish vadldlllek vlsearflfn adagsiyike geklrftisq
       61 netlqkrlpk gqkliytsft lpinnqsiag yvanndqaln ipdvyqlrpd lpfsfnkefd
      121 rmsdyhtqsm ltipmkntrn qivgvlqlin aqddqgkiip fdaedepivk hfaiyaanai
      181 eraqmtrdti ermirmaelr dpretgphan rvaafsvely eayaqkknlp qkevectrda
      241 lrmaamlhdv gkvaisdtil kkpgklsdde yeimkkhtih garlfidprs dfdefsaiva
      301 lnhherwdgn gypghvdpas gaplpgyqgk sgkargkree eiplfgriva ladvydalss
      361 arvykkawse ekvlqiieee rgkqfdpqlv dcffarldmi rslaskypdk npae
//
LOCUS       WP_457566345             394 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent rRNA methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566345
VERSION     WP_457566345.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..394
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=45027
     Region          3..394
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mktvilkkgr eksllrkhpw ifsgavksve gqpqsgetva vqdwqgrflg rgaysprsqi
       61 vvrmwsfeqd eaidnaffek rllqalrlrs tsgidresta vrliasdadg lpgiivdryn
      121 qflvcqflsa gaeywkktiv hllqkllepq giyersdvdv rkkegltptr gllagqeppa
      181 lleineqeir flvdvkrghk tgfyldqrvn rrmvrqwsag retlncfayt ggfglaalkg
      241 gakhvtnled vagllelqek nfklnqfkse ryenvkadvf rqlrryhteg rrfdliildp
      301 pkfvdsqhhl mrasrgykdi nrlafellrp egvlftfscs glmkmdlfqk ivadaalean
      361 reaqilqwlf qapdhpiklh ipeslylkgl lcrv
//
LOCUS       WP_457566351             381 aa            linear   BCT 27-JAN-2026
DEFINITION  DmpA family aminopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566351
VERSION     WP_457566351.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Bompard-Gilles,C., Villeret,V., Davies,G.J., Fanuel,L., Joris,B.,
            Frere,J.M. and Van Beeumen,J.
  TITLE     A new variant of the Ntn hydrolase fold revealed by the crystal
            structure of L-aminopeptidase D-ala-esterase/amidase from
            Ochrobactrum anthropi
  JOURNAL   Structure 8 (2), 153-162 (2000)
   PUBMED   10673442
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Fanuel,L., Thamm,I., Kostanjevecki,V., Samyn,B., Joris,B.,
            Goffin,C., Brannigan,J., Van Beeumen,J. and Frere,J.M.
  TITLE     Two new aminopeptidases from Ochrobactrum anthropi active on
            D-alanyl-p-nitroanilide
  JOURNAL   Cell Mol Life Sci 55 (5), 812-818 (1999)
   PUBMED   10379365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10115574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..381
                     /product="DmpA family aminopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40301
     Region          29..360
                     /region_name="DmpA"
                     /note="L-Aminopeptidase D-amidase/D-esterase (DmpA)
                     family; DmpA catalyzes the release of N-terminal D and L
                     amino acids from peptide susbtrates. DmpA is synthesized
                     as a single polypeptide precursor, which is
                     autocatalytically cleaved to the active...; cd02253"
                     /db_xref="CDD:239071"
     Site            order(80,100..101,265,269,272,315..319,321)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:239071"
     Site            order(85..88,90..92,94,96..97,100,114,117,125,147,
                     272..273,284..288,320,324,327)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:239071"
     Site            order(147,219,251,289..290)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239071"
     Site            250..251
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:239071"
ORIGIN      
        1 mkrnllpfll lipilllagt kraadyglki gvlppgplna itdvkgvkvg hvtiikgdsv
       61 rtgvtailph ggnifqekvp aavyvgngfg kltgstqvee lgnletpiil tntlsvpvaa
      121 galidytlgl pgneavrsvn plvgetndgw lndirgrhvt kqhvlqaihs aksgrveegc
      181 vgagtgtvcf gfkggigtas rklpesiggw tvgvlvqsnf ggvlqiagap vgrelgafyl
      241 sdrlnstpdg scmivvatda plsarnlkrl akralfslar iggigsngsg dyviafstak
      301 earvpyrqkd afqqnkrlrn ermsplflaa ieateeailn slftatttrg fmgrevealp
      361 mdkvlnilkq hrlinerrea p
//
LOCUS       WP_457566356             264 aa            linear   BCT 27-JAN-2026
DEFINITION  damage-control phosphatase ARMT1 family protein, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566356
VERSION     WP_457566356.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Huang,L., Khusnutdinova,A., Nocek,B., Brown,G., Xu,X., Cui,H.,
            Petit,P., Flick,R., Zallot,R., Balmant,K., Ziemak,M.J.,
            Shanklin,J., de Crecy-Lagard,V., Fiehn,O., Gregory,J.F. 3rd,
            Joachimiak,A., Savchenko,A., Yakunin,A.F. and Hanson,A.D.
  TITLE     A family of metal-dependent phosphatases implicated in metabolite
            damage-control
  JOURNAL   Nat Chem Biol 12 (8), 621-627 (2016)
   PUBMED   27322068
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Perry,J.J., Ballard,G.D., Albert,A.E., Dobrolecki,L.E., Malkas,L.H.
            and Hoelz,D.J.
  TITLE     Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase
            that targets PCNA and is linked to the DNA damage response
  JOURNAL   Cell Rep 10 (8), 1288-1296 (2015)
   PUBMED   25732820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..264
                     /product="damage-control phosphatase ARMT1 family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..257
                     /region_name="DUF89"
                     /note="House-cleaning carbohydrate phosphatase, DUF89
                     family [Defense mechanisms]; COG1578"
                     /db_xref="CDD:441186"
ORIGIN      
        1 kekvvnkvln ylttidynvp ppvigkevyr iihqvtgnhd pyhelkikyn slglayyddl
       61 lkivfrnpep vlmaaklava gnvidfgaqv keidiqktih tvedlyfein dferfiedlk
      121 qsrkilylad nageivfdrl fieilqryyp elgleftvav rgapiindat redalmvgmd
      181 kiarivdsgd dtpamvldqa sdelkqafeq admviskgmg nyetlderhe liyyllrvkc
      241 pvvskiinak egslvfkrne dfnd
//
LOCUS       WP_457566360             627 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Caldithrix abyssi].
ACCESSION   WP_457566360
VERSION     WP_457566360.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 999995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..627
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70154
     Region          17..616
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(24..25,28..29,32,63,118..119,121..123,126,142,
                     145..146,149,424,427..428,446..448,451,485,489,547..548,
                     552,556,572,575..576,579..580,583)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
ORIGIN      
        1 masnsskket rnpwlwvpsi yfaegipyiv vmmvsvimyk rlgvsntdia lytswlylpw
       61 vikplwspiv dliktkrfwi lamqlligag lagvgltipl pnffkfrlif fwllafssat
      121 hdiaadgfym lgltqrqqaw fvgvrstfyr famitgqgll iifagylesn tglqsvqlnv
      181 laepgqstve mvnpdcltie plqgelrivh fpedtlivpt tplkkekads ilsfvrqwnv
      241 ehgfavpdqr fvhkskseks wwtnhvsepl gnwikenfgh hadpslesdl tgnigliyfy
      301 lsnkpeedqe vvinfgrtag dksifllegs aygsrlifne qnwnkpaiav iqldpklkhr
      361 smatftatag niplawsltf llmaalfiaf fiyhkmilpf pasdqpgate glanilrefi
      421 atfveffkke rigliiafll lyrlgesqlv klaspfllda qeagglaltt gqvgfvygtv
      481 gilaltlggl lggflaarhg lkfwlwpmai ainlpdavyi ylsaaqpdsl fiinvcvaie
      541 qfgygfgfta ymlymiyasq grhktahfai ttgfmalgmm ipgmfsgwiq eligyhnffi
      601 wvmiatipgf lilpfipldk dfgkknv
//
LOCUS       WP_457566363             423 aa            linear   BCT 27-JAN-2026
DEFINITION  exo-beta-N-acetylmuramidase NamZ family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566363
VERSION     WP_457566363.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Muller,M., Calvert,M., Hottmann,I., Kluj,R.M., Teufel,T.,
            Balbuchta,K., Engelbrecht,A., Selim,K.A., Xu,Q., Borisova,M.,
            Titz,A. and Mayer,C.
  TITLE     The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the
            founding member of a family of exo-lytic peptidoglycan
            hexosaminidases
  JOURNAL   J Biol Chem 296, 100519 (2021)
   PUBMED   33684445
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..423
                     /product="exo-beta-N-acetylmuramidase NamZ family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0033922 - peptidoglycan
                     beta-N-acetylmuramidase activity [Evidence IEA]"
                     /calculated_mol_wt=47898
     Region          41..423
                     /region_name="YbbC"
                     /note="Uncharacterized conserved protein YbbC, DUF1343
                     family [Function unknown]; COG3876"
                     /db_xref="CDD:443084"
ORIGIN      
        1 mmkkliflff vgaififsgc qarltkgvtp krdaekispq kvilgienfl nnykslvkgk
       61 rvalltnpsg vdsrlkstad ilfedktinl talfgpehgi rgaiyagehv kdeidphtgl
      121 pvfslygahk kptkkmlenv dvilvdiqdi glrgytyiyt malvmeaaae sgkqvivldr
      181 pnpidgirie gnlvekgfes fvglypipyr hgmtigelar yfnqefdihc dlqvvpmvgw
      241 trdmlwdqtg llwvptsphv phwktilymg atgtigelrt isegvgytsp felvgapwid
      301 gydfarelna lnlpgvifrp lyfkpyyasy kgevcqgvql hitnphtfns yqtglyilqt
      361 llklypqhdp fkfenrvsmf qkiigcnwii edlkaghsvs eialkwqael eqfkmkreky
      421 lmy
//
LOCUS       WP_457566364             127 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator, partial [Caldithrix abyssi].
ACCESSION   WP_457566364
VERSION     WP_457566364.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 127)
  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 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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>127
                     /product="response regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          4..117
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
ORIGIN      
        1 miriliaddh aivraglkqi vaqekdmive geagsvdell qllpqkewsv lildinmpgr
       61 sgldvlkeik trypalpvli lsiydeeqyg lrairsgadg ylkkisapee lisairklis
      121 ggkyisp
//
LOCUS       WP_457566366             198 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdenum cofactor guanylyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566366
VERSION     WP_457566366.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Guse,A., Stevenson,C.E., Kuper,J., Buchanan,G., Schwarz,G.,
            Giordano,G., Magalon,A., Mendel,R.R., Lawson,D.M. and Palmer,T.
  TITLE     Biochemical and structural analysis of the molybdenum cofactor
            biosynthesis protein MobA
  JOURNAL   J Biol Chem 278 (28), 25302-25307 (2003)
   PUBMED   12719427
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Lake,M.W., Temple,C.A., Rajagopalan,K.V. and Schindelin,H.
  TITLE     The crystal structure of the Escherichia coli MobA protein provides
            insight into molybdopterin guanine dinucleotide biosynthesis
  JOURNAL   J Biol Chem 275 (51), 40211-40217 (2000)
   PUBMED   10978347
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   5  (residues 1 to 198)
  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 10002369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     gene            1..198
                     /gene="mobA"
     Protein         1..198
                     /product="molybdenum cofactor guanylyltransferase"
                     /EC_number="2.7.7.77"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061603 - molybdenum cofactor
                     guanylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=22054
     Region          7..189
                     /region_name="MobA"
                     /note="Molybdopterin-guanine dinucleotide biosynthesis
                     protein A [Coenzyme transport and metabolism]; COG0746"
                     /db_xref="CDD:440509"
ORIGIN      
        1 mkikeasaai iaggksrrfg spkhqalfcg rpliewsiel aaslseriil iasekqleqk
       61 fglpvaediv pgkgplggil talkhietew lfvlpvdmpl lkkdiyfklw errkngrpvv
      121 avsdtgiesm vslwrrshaa lieslimsdq lkinvalrkl naeevffpae fsvffsninf
      181 kedlarleki skargras
//
LOCUS       WP_457566379             210 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphate ABC transporter ATP-binding protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566379
VERSION     WP_457566379.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Fredrick,K. and Ibba,M.
  TITLE     The ABCs of the ribosome
  JOURNAL   Nat Struct Mol Biol 21 (2), 115-116 (2014)
   PUBMED   24500425
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..210
                     /product="phosphate ABC transporter ATP-binding protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
     Region          1..210
                     /region_name="PstB"
                     /note="ABC-type phosphate transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1117"
                     /db_xref="CDD:440734"
ORIGIN      
        1 gksthlrvyn riyelyrdqr aegevfldde nilsentnli klrkrvgmif qkptpfpmsv
       61 fenvayglrl hyklskselt grveealkra alwdevkdkl nqpgtalsgg qqqrlciara
      121 iaiepeillm deptsaidpi atakieelve slknrytivi vthnmqqaar isdytaffyk
      181 gyiveygetr qiftnpkkke tenyitgrfg
//
LOCUS       WP_457566380             257 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Caldithrix abyssi].
ACCESSION   WP_457566380
VERSION     WP_457566380.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..257
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28584
     Region          14..253
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mtqsktglnh stdnlldqta aliadsrclv aftgagisve sgippfrgqg glwnkvdpcl
       61 leigyfeknp lqswrlikql fyqtlkkakp naahhglarl ekagylktii tqnidylhqq
      121 agsarvleyh gtykylkclq cgyrteakes mlvelpplcp rcrgvlkpdf vffgeaipqk
      181 vamesekear kadlmliigs tgevypaami petafhhgsk iveiniepsn ythsithifl
      241 rgrateivse iierlki
//
LOCUS       WP_457566383             426 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease [Caldithrix abyssi].
ACCESSION   WP_457566383
VERSION     WP_457566383.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..426
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46269
     Region          16..426
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mttlliivgl illtlfgtpl fviisgiall lfhlaeidss aiiielyrlt sqpiflaipl
       61 ftfagyllae sntprrlvnl sraligwlpa glaivalvss alftaftgas gvtiialggl
      121 lhpimlreky pekftlgllt asgnlglllp pslpiilygl vaqtpidqlf aagivpsilm
      181 ivmlsiyiil frrkqlkelk irkstprerw qalkesawei plpfiiiggi ygglftatea
      241 aavtaiyvfi ievfiyrdis lrrglpvvvr ksmemvgsii vilaaalgla nyftdaqipm
      301 rileamktfi dspivfllfl nlflllvgav mdifsaimvi vpiiipiaas fgidpvhlgi
      361 iflanlgigy stppvgmnlf iaslrfeksi tflyraalpf liillialal ityipalsig
      421 ilplim
//
LOCUS       WP_457566382             436 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin family protein [Caldithrix abyssi].
ACCESSION   WP_457566382
VERSION     WP_457566382.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..436
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50197
     Region          304..414
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mlksvlcfvv glsylmagnt eitirlkpvn adslkiieps fsparpvken kllekitayp
       61 anyatrklfq fhiqnflkls klfkedsvlr asvkssalpa tidfleriyp ppplddivsa
      121 cwledgqgnd ffvfdannde dftndrilkf kdfdqvfape hsgqyvmaee lvtveifdgq
      181 qvktqkmlla ffkaqkpggk nlvffsnrli rmgelkldge vfncilftil pdvnykitdf
      241 lwidlnhdkr ynrkkdfyeq lyqpftlrnk sygvkaldiw grsltlkeld aqktppiavg
      301 lacpefevaf idstkfslaq akgrylvidf wmcsdqfcdm mskkllekls dqnivywisc
      361 pygaqsyerl kamggiaegd frhfvaphei erfrrlfqvr tnkvlfvinp qgkiesienf
      421 tqdqteqilr qisead
//
LOCUS       WP_457566381             278 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566381
VERSION     WP_457566381.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 278)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..278
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31721
     Region          17..255
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mhlimlmiqk lktlpswfns lsalvllfii ayvdlqfsfp lfflylipvs vsallapral
       61 gvvisivsfa lyslininfk avdpltfeia gngillfwvs flalklkeqw slnqahrfsd
      121 eltgglsksl flqraeeelh rshrykrpit layldcsrlk kvredqnfny ekeilkniaq
      181 imkqnlrktd lftrvdednf limlpdinag gartalqkiq slirlksiaa nwplefniga
      241 itfmqppldm qavlesvssm aqnqtdsgnf lqhqqlyh
//
LOCUS       WP_457566387             460 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566387
VERSION     WP_457566387.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 460)
  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 460)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 460)
  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 460)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..460
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=52207
     Region          5..452
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mpdfkiliid depaqlislk tflqrrnyvv ftassgnegl nilkansidl vltdyrmpdi
       61 sglevvkatq kinpeipvvv itaysqieea vqvmkentfd ylskpidlda levlikkare
      121 rqylisenki lreqlkeryr fqsiisqsga meavlnmagr varskatvli lgesgtgkel
      181 iaraihyasd radkplviin saalspnlle selfghekga ftgaiaqrig rfeqadggtl
      241 fidevgdlpm qtqvkllral qfgefervgg sktikvdvrv iaatnrdlee liqkgefred
      301 lyyrlnvvti hipplrerks dipvlirhfi ekyarenqkn vvgiskeaqd ylmryhfpgn
      361 vreleniier avvlardeii tledlpqglt vqtersildp fdfshpyeek laafervmie
      421 ealkqkhgnq sqaarllgis erhlrsrmqr lnivntmrnr
//
LOCUS       WP_457566391             914 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor, partial [Caldithrix abyssi].
ACCESSION   WP_457566391
VERSION     WP_457566391.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>914
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          27..115
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          100..874
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkylrfisii liiffvnslw agttgkitgq vkdarsgepl pgvnvvvegt algastdleg
       61 yyvitnippg mysltfsmvg yaahkvtgvr vnidqttvin aklqeqvleg eeivvvasrp
      121 vvekdvaasr anisseeika ipvvnvssvv glqagiegls irggglseva fvmdgitlrn
      181 erdnspftgi sltaveemqv qaggfsaeyg nirsgvvnvv tkegkkdrys vaflgryrap
      241 apkhfghspn spesywirpy vddavcwtgt rngnwdyytq rqypefkgwn qisfetlqnd
      301 dpnddltpea aqqvflfqhr rqldiqipdy vgdfsfggpv pviskdlgnl rfyssfrktq
      361 dayliplqdd ayrtwtfqtk vtsdvgsgkk lmfsgllgre tgvdrfrdgt pgmftaswqi
      421 grelsngpky idarmfatdy wgpartdykn lgvkwthaid ektfyeasfs ifrseyhkgi
      481 gryrdrtkky lfgnsyyide gpfgfepmsv agingmrmga gfsnardssk vttyslnldy
      541 tkqinrfnni kvggefvlth sqvnygryde flpsantqtk wdrkpvrgal yiqdklefeg
      601 miatigvrmd yfhaggewyd lesnpynpai nllvdenvsg ldsllpskpt khlftfsprl
      661 aiafpvtens klyfnyghfr qlpqpedlyi lrensflnqi trvgnpnsel qktvayelgy
      721 ehnilnqflv raagyykdit lqptlvlyen ldgsvsyyrq epnnyedirg feitinknrg
      781 rwvrgfvnyt ymvstygyfg ygryyenpaq qrqyevttsf yyqtkpkprp faranldfft
      841 pqefgpkilg fqplsdinfn ilanwkagry etwagggnip glfanvqwvd ylnfdlrirk
      901 nfriknfgnl effv
//
LOCUS       WP_457566402             307 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566402
VERSION     WP_457566402.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..307
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35759
     Region          35..163
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          35..63
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..97
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(73..74,77..78,80,104,107..108,111..112,114..115,138,
                     141..142,145..146,149)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          102..132
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          137..162
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnsisknflv svfsifllws cynmdppvra qqpsafyfyq mavqskirgd tpkaleqinr
       61 airlnqkisl fyvfkaqifd smqvsdsavf yykksltlrs hapeilkrlg elalqaqrpn
      121 eaayyfrkay ieapdsvdfl lklaqirlqq neirqaenll deyrltqkrk erpvsplffv
      181 iradlamskg dslsaarfya rshcgeclsk eqaewafetl lktqnleayf dllagvrknr
      241 hfpeallyyy rglyyqaign aheavqqfer ayqkgvrkkk llktliqfya gqnkmervkv
      301 lqseiqe
//
LOCUS       WP_457566406             336 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457566406
VERSION     WP_457566406.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10617647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..336
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38513
     Region          15..303
                     /region_name="Pyr_redox_3"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     pfam13738"
                     /db_xref="CDD:404603"
ORIGIN      
        1 mkkinkeiii igggpaglka aeiarqkkid yvilergkpg qswseirpdm lmlspclpqr
       61 dwtslssklp iwkmdvlrpy ctaaqfaryl eaycdffqld vqthqpvlsv drdatgyvvk
      121 tktheytapi llvgtgifgn pyfpeipgik dnpyvmhshf ykdkmdfknq rilvvgggns
      181 aaetaidlvg yslvylvtrd elqffsdtrk lyhirgvyes ylkelismei irykayqkit
      241 hvdqnvvyfk nwqlevdkvi fatgyhgdlk vlknfkigvn kknypdvtes gesiqyprlf
      301 figplfflgf stnvihgfvk qipksldkie qllrel
//
LOCUS       WP_457566413             363 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP pyrophosphokinase [Caldithrix abyssi].
ACCESSION   WP_457566413
VERSION     WP_457566413.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Das,B. and Bhadra,R.K.
  TITLE     (p)ppGpp Metabolism and Antimicrobial Resistance in Bacterial
            Pathogens
  JOURNAL   Front Microbiol 11, 563944 (2020)
   PUBMED   33162948
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Steinchen,W., Schuhmacher,J.S., Altegoer,F., Fage,C.D.,
            Srinivasan,V., Linne,U., Marahiel,M.A. and Bange,G.
  TITLE     Catalytic mechanism and allosteric regulation of an oligomeric
            (p)ppGpp synthetase by an alarmone
  JOURNAL   Proc Natl Acad Sci U S A 112 (43), 13348-13353 (2015)
   PUBMED   26460002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..363
                     /product="GTP pyrophosphokinase"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015969 - guanosine tetraphosphate
                     metabolic process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42113
     Region          2..289
                     /region_name="YjbM"
                     /note="ppGpp synthetase catalytic domain (RelA/SpoT-type
                     nucleotidyltranferase) [Nucleotide transport and
                     metabolism, Signal transduction mechanisms]; COG2357"
                     /db_xref="CDD:441924"
ORIGIN      
        1 mkvfeiiaey qnryplnkef seklkllfer lliahnisfl qietrvkslp sfldkvyrvl
       61 sagkefsync tdlvgirlit yyledvyqig elieqtfkvh yknleydsln rspdqfgyss
      121 lhfkvslspe ynypldvqkf knnvfeiqir tvaqhawati dhklryktte kipklilrqi
      181 fqlsalfela diqfsnikkq leaqasddlk ryqagdlsak inaltlgyfl kthqttidvl
      241 vkeakkigfn etsiqqdpnt iryllilfkr lgiesmaele qlfdealqkk eiilkniyri
      301 isnssyapid ypfpvillil itlrlkiidf daidvqeiil klmgnpeasl dvppadqalp
      361 iqq
//
LOCUS       WP_457566414             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Caldithrix abyssi].
ACCESSION   WP_457566414
VERSION     WP_457566414.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..205
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23290
     Region          38..189
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mksqldrlmt rivrasalvv vnlllmvvfs fagqegrtvp pdsvvdftlk dankkefrla
       61 ehlgqimils fipntknktl garwlensrf cvqklkskfn gdimalglke mtdfpmflpr
      121 sfiraklrke pfpylidweg kvfaqfavqs tpvlmvvdag gkivyrqelt adtdrfnalc
      181 tqiealieqq qrseqkaasr eeene
//
LOCUS       WP_457566415             193 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566415
VERSION     WP_457566415.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22181
     Region          6..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvaftkrqre ivntaiqlia ekgiqeltik nlskkigiae saiyrhfdsk fdiligiltl
       61 fkdnintlnr qildmdlspr aklevmleqr fkyfsekptv aavifseelf rndsrlskav
      121 feimqenqns migiisegqa kgefrkevsa eelsfmiiga vrlivtrwrm tdfsfdlvee
      181 gqklwqtiki lit
//
LOCUS       WP_457566417              62 aa            linear   BCT 27-JAN-2026
DEFINITION  patatin-like phospholipase family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566417
VERSION     WP_457566417.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>62
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
     Region          14..>62
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mlalvlwlgi plyaqkplkv glalsgggar giahigvima leennipidl iagtsmgsiv
       61 gg
//
LOCUS       WP_457566412             320 aa            linear   BCT 27-JAN-2026
DEFINITION  MlaD family protein [Caldithrix abyssi].
ACCESSION   WP_457566412
VERSION     WP_457566412.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..320
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34738
     Region          6..314
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 meslrqnnnf kisvylmvml savllgiify ivgsnqklfa dkyslymfkp qaeslvpgaf
       61 itlsglkvgv vgemkltnra ekpgvlielk idkkyrefit pssvaqiktm gmlgdryvdi
      121 slgkaaetpl regaliaskd spdleqvmvd aaasvsqlrs vlnnvdlltr qmvegpgtma
      181 slindgamag dlkqslnnlk eisgaanngr gnaarflnds tlyqsllatt rqlqkitaqi
      241 aegqgtlgkm vfdssaaghl qnvvqksdsl ldalngngtv gallkdrayy eelftltrel
      301 rtliedikkh pekygsfsif
//
LOCUS       WP_457566397             425 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine synthase [Caldithrix abyssi].
ACCESSION   WP_457566397
VERSION     WP_457566397.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 425)
  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 425)
  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 425)
  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..425
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..425
                     /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=46852
     Region          7..405
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 menryfyrct qcgreyaarh ietqfvylcp hcgraepnap ltgvleviyd ykqivgvlsm
       61 qrfltfrpgv pwqypqlwpl eydpatlqlk gleprllhnl tlpsnqllel ewegrafsvl
      121 detrnptfsf kdrasilvvl kaiqmgvkei aaastgnags slagicarsg lkaqiwapqa
      181 ipqakllqik aygaiihlvq gdydlafdqs ieisrqnqwy nrntaynplt iegkksaafd
      241 lfiqtngrlp dvifvpvgdg viisglfkgl rdlkalgwie rlprliavqs sgsdalvrym
      301 qegkfvfkka ntladsisag aprnlylaar svresqgqai avsdeaivka qmilarkygl
      361 laepaaaasf agflkllaea kldrserpll lltgnglkdv ealkrigefg tarfsngtke
      421 tgdvq
//
LOCUS       WP_457566416             167 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566416
VERSION     WP_457566416.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 167)
  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 167)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 167)
  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 167)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>167
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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          2..>167
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mkqfsilvvd dekiqresla gflakkryqv ykagnfdaal qiikqnaidl vltdvkmsgk
       61 sgydllkavk einpsitvii mtaygnieea vaamkdgayd yltkplelde vellvnrafq
      121 fkrlteenae lrqklsdkhr ftniisaspl meealnmaar sansras
//
LOCUS       WP_457566422             248 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-2,3-diacylglucosamine diphosphatase [Caldithrix abyssi].
ACCESSION   WP_457566422
VERSION     WP_457566422.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Bohl,H.O., Ieong,P., Lee,J.K., Lee,T., Kankanala,J., Shi,K.,
            Demir,O., Kurahashi,K., Amaro,R.E., Wang,Z. and Aihara,H.
  TITLE     The substrate-binding cap of the UDP-diacylglucosamine
            pyrophosphatase LpxH is highly flexible, enabling facile substrate
            binding and product release
  JOURNAL   J Biol Chem 293 (21), 7969-7981 (2018)
   PUBMED   29626094
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..248
                     /product="UDP-2,3-diacylglucosamine diphosphatase"
                     /EC_number="3.6.1.54"
                     /GO_function="GO:0008758 - UDP-2,3-diacylglucosamine
                     hydrolase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29136
     Region          1..240
                     /region_name="LpxH"
                     /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxH
                     [Cell wall/membrane/envelope biogenesis]; COG2908"
                     /db_xref="CDD:442152"
ORIGIN      
        1 mkayfisdlh lgareienpe lqrervnglf tqilkdathl fvvgdffdfw feyktvipkq
       61 yfpvlfylqk mrekgievhy lagnhdfflg sffdryldvk thadeavvel kskrffifhg
      121 dgvdpddkgy rilkrilrsa fnqklfrlih pdlgirlakl vsgtsrkynk vnlkkrseda
      181 yvrfaeqkfa egfdyvvmgh rhnplvheaq gkkyvnlgdw ivnysyavfd gndlklkfft
      241 nqsqrtpk
//
LOCUS       WP_457566409             843 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor, partial [Caldithrix abyssi].
ACCESSION   WP_457566409
VERSION     WP_457566409.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>843
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          26..116
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          90..801
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 maklekiiva illssvlala gttgkisglv tdantgeplp ganiyvqvgg qtigaasdvd
       61 gyfvilnvpp gsytvkaayi gytpveinnv vvridltttl nikmkqqvle aetvvvearr
      121 pivvkdisns qlnleakaie nmpitsinqa lvlqagiess adgiiirgss prqvlymvdg
      181 lsmndersnt pysfnsitai eeiqvqtggf naeygdlrag lvnvvtkegs tdrynlsifs
      241 nvrdiaflgq akkhfgpsly srdsyfnkpy fdpavmwtgt nngawddytq rqypkfqgwn
      301 aisyatlqdn dptndltpeg akrlfewqrr rqgeihepdy vidmsfngpd pimslvpdwk
      361 nkynprfhls fyktkemfvf plsrsgyneh qtqlkytfnp tssmkviltg mygeifsvsp
      421 yqwtttptgr llrsqsevan llssttgasi lympgyyspg diyrtlvgak ishalssrtf
      481 ydasfqykvs ryktfqmalr dtskkyepvp gyftdeapyg ywgyavagid gtsmggwmnl
      541 grdrsvisty sfdfnltsqv nsknqiktgl rfvyniydin sgtyspsmst wtrsmvykvk
      601 pyrigfyvqd kleyegfian igvrldysdp dvewydlspy dpylkagygn lieeeaprtk
      661 akpqfavspr lgvshpisen aklyfnyghf rtepassyrf rlqresnglv tylgnpelry
      721 ektvayelgy ehnlfdmfll kiagyykdis nqpswvyyrn ingsvsyykm sdlnyedirg
      781 ieftltkryg rwvtgfvnyt ydvqtsgyfg ylryyedpne qrqylrenpy qskprpqpya
      841 rvn
//
LOCUS       WP_457566425              83 aa            linear   BCT 27-JAN-2026
DEFINITION  GIY-YIG nuclease family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566425
VERSION     WP_457566425.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10179946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..83
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
     Region          1..66
                     /region_name="GIY-YIG_SLX1_like"
                     /note="Catalytic GIY-YIG domain of yeast
                     structure-specific endonuclease subunit SLX1 and its
                     homologs; cd10449"
                     /db_xref="CDD:198396"
     Site            order(1..2,13..15)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198396"
     Site            order(2,13,15,23,27,59)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198396"
     Site            59
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198396"
ORIGIN      
        1 lyilyssrld ryyvgishdp eerlkyhnsf prgwtvrgrp wqlvftkkfa drptaekwer
       61 yikkqkkrsl lekiisgefm wee
//
LOCUS       WP_457566426              67 aa            linear   BCT 27-JAN-2026
DEFINITION  GIY-YIG nuclease family protein [Caldithrix abyssi].
ACCESSION   WP_457566426
VERSION     WP_457566426.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10179946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..67
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=8203
     Region          5..67
                     /region_name="GIY-YIG_SLX1_like"
                     /note="Catalytic GIY-YIG domain of yeast
                     structure-specific endonuclease subunit SLX1 and its
                     homologs; cd10449"
                     /db_xref="CDD:198396"
     Site            order(5..7,18..20)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198396"
     Site            order(7,18,20,28,32,64)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198396"
     Site            64
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198396"
ORIGIN      
        1 mkdyflyily ssrldryyvg ishdpeerlk yhnsfprgwt vrgrpwqlvf tkkfkdrpta
       61 ekretfi
//
LOCUS       WP_457566428             281 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54 interaction domain-containing protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566428
VERSION     WP_457566428.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Morett,E. and Segovia,L.
  TITLE     The sigma 54 bacterial enhancer-binding protein family: mechanism
            of action and phylogenetic relationship of their functional domains
  JOURNAL   J Bacteriol 175 (19), 6067-6074 (1993)
   PUBMED   8407777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..281
                     /product="sigma-54 interaction domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008134 - transcription factor binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <1..268
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 lhenswrkdq pfwavncaai petlleself gyekgaftga akrhlgyfer anhgtlfidd
       61 iddlpmkmqv kllrvlqeqe liriggwesv kidvrvitat kvdlkqrmke grfredlfyr
      121 lniipivlpp lrerkedipq likhflqkqn aahiwrlfsp ellqrlsqyd wpgnvrelen
      181 fverfvafsg mqsfdpfsll pgvtsgkqqp lpessaffsy hsfndfmaak ekeiidwamk
      241 qtnnniskaa dllklprttl rsklekinrr kagggeksvr v
//
LOCUS       WP_457566430             722 aa            linear   BCT 27-JAN-2026
DEFINITION  Tex family protein [Caldithrix abyssi].
ACCESSION   WP_457566430
VERSION     WP_457566430.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Fuchs,T.M., Deppisch,H., Scarlato,V. and Gross,R.
  TITLE     A new gene locus of Bordetella pertussis defines a novel family of
            prokaryotic transcriptional accessory proteins
  JOURNAL   J Bacteriol 178 (15), 4445-4452 (1996)
   PUBMED   8755871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..722
                     /product="Tex family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /calculated_mol_wt=81034
     Region          2..722
                     /region_name="Tex"
                     /note="Transcriptional accessory protein Tex/SPT6
                     [Transcription]; COG2183"
                     /db_xref="CDD:441786"
ORIGIN      
        1 mteiemiqlv aeelnlkalq vkntielldt gntvpfiary rkevtgslde nqiraiqdrm
       61 qylraleark etilksieeq gkltpelkek ilkatklqev edlylpykpk krtratvare
      121 kgleplaeii lkqevtegsa eeiavkfvne ekevrtvqea lqgamdivae visddaevrk
      181 qireatfktg llesvvknae ertpyemyyd ysepvnsipp hrilainrge tegvlkvsve
      241 vdsqkmigli ealyvkneks ifidylrqai adsftrlifp siqrevrsal tekadehaia
      301 vfaenlrnll lqppvrgkmi mgidpgfrtg ckvavidqtg kylegatiyp hppqerylea
      361 ksivralvnk yqvdiiaign gtasretemm vaeliremkd erkveyiivn eagasvysas
      421 kvaqqefpdl eaamrgnisi arrlldplae lvkidpkhig vglyqhdvnq krlaealqqv
      481 vesavnmvgv nvntasasll kyvsgltsrt ansivkyrde hgpfrnreei kkvdgigeva
      541 yqqaagflri pdgdnpldnt sihpesyeat rkllekfkvd dihqggkllr lkikqekvdi
      601 palleelgig eptfndildn lekpgldprd elpkpifksd vlkmedlreg milkgtvrnv
      661 vdfgafvdig vkqdglvhvs rmakkfvknp yellsvgdvi evkvvsidle rgriglsmvl
      721 de
//
LOCUS       WP_457566437             277 aa            linear   BCT 27-JAN-2026
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase,
            partial [Caldithrix abyssi].
ACCESSION   WP_457566437
VERSION     WP_457566437.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..277
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
     Region          <1..273
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 alckklnepp dfdvhintqk ispkkfknll kekkvpfvea pfdstivrvk dvqpflrerw
       61 fekgycviqd esaalvveqm altekskild mcaapggkya qllkkrlsqg mvvaadidke
      121 rlkrvkqnvq klglegglfv vadgknppfk kvfdhilida pctglgvirk hpdikwrrkf
      181 eeiiefskiq edlleaadri ltengrliys tctidyfene nvakdflqkh aekyavqkpk
      241 vahpsmlsed fvriqphrhe mdgsfcavfk kikddae
//
LOCUS       WP_457566440             302 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase, partial [Caldithrix abyssi].
ACCESSION   WP_457566440
VERSION     WP_457566440.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 302)
  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   5  (residues 1 to 302)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..302
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          1..290
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 kvivgqtymi erlligllsn ghillegvpg laktltvktl sqtiqtkfqr iqftpdllpa
       61 dligtliynq kdgqfttkkg pifsnlilad einrspakvq salleamqer qvtigentfp
      121 leepflvlat qnpieqegty plpeaqvdrf mlklsvgyps keeeleiirr qtrketvepq
      181 avisprelik ardvvkevyv dekiekyvvd vvfatrypee fgldelkgli tygasprasi
      241 yltqaakaha flrgrgyvtp edvraismdv mrhriilsye aeaeelsted virkvlnrve
      301 vp
//
LOCUS       WP_457566441             206 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566441
VERSION     WP_457566441.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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   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 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>206
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Site            order(33..34,37..38,40,68,71..72,75..76,78..79,106,
                     109..110,113..114,117)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          33..57
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          38..129
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          66..97
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          102..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvrkalvvmi agmivfsacq keektriaen dvlqlanayy tnglyeaavr qylqylkdyp
       61 lpagrvanty ytigdiyfer ikdyekaley ylkvkylfpe splqkevgkk ivaclerler
      121 sqdamrmmqs eaaldtsgls rnrpgqvlae igerkitqgd ldfeisklpp avqeqfndpq
      181 kkrellqqli lqdllyesar rqgldk
//
LOCUS       WP_457566442             408 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator, partial [Caldithrix abyssi].
ACCESSION   WP_457566442
VERSION     WP_457566442.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 408)
  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 10067910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>408
                     /product="response regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          <74..134
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cd00156"
                     /db_xref="CDD:381085"
     Region          <239..322
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(306..307,308,310)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
ORIGIN      
        1 msdkkqgfhp fdsplvehgy gtrfqgfqhl mrhrirdill vsslydlyvf eedgrlyeli
       61 reeyqglnls hvpeitrvsr gedalalase ekrfdliitt phiedmdstq lareirqagl
      121 kipvvllayd nrelsellnh adsrvfdrif iwtgnfrivv aivkhledim nveqdtrlvg
      181 vqsiiliedn irfysaylpl lyteilkqsq rlilegvnlt hkylrmrarp killcttyee
      241 aweyfikyqh tilgvisdid fkkggkhdpe aglkfaaevr krhddipvll qsnnaqfqdr
      301 aleigahfvl kdsptllqel rkftitqfgf gdfifrtpeg vevgratdli sleeqlktvp
      361 pesikyhaer nhfstwlkar tefwlahklr prkvsdfpsl edlrqhli
//
LOCUS       WP_457566445             397 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Caldithrix abyssi].
ACCESSION   WP_457566445
VERSION     WP_457566445.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..397
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43937
     Region          115..397
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mktfwkvsfw vvlgvlagvl mreylpmhsa eqeqpldtsl vtearaqett gqqlqthren
       61 aitravqkvt pavvsvnvtk inryvqrspf fndpffrqff pelfndrive qpvesigsgf
      121 fisddgyvvt nehvvgeate iivamadgke ypaklidrdr vsdiallkve ghfpsikfgd
      181 sdkvligewa ialgnpfglf vknqptvtvg visavnrnfs plegriyedm iqtdaainpg
      241 nsggplcnad gevigmntfi ltgdpqshgs vgvgfaipsn riqqvveklk rrrgkdtnvw
      301 igmyvsnlnp yiarslgyps vqgvyvrrid rhspaekagv qlgdvivein getissyada
      361 qaiilsldlr vgdkmrlkiw regklldidl vlekype
//
LOCUS       WP_457566449             432 aa            linear   BCT 27-JAN-2026
DEFINITION  3-isopropylmalate dehydratase large subunit [Caldithrix abyssi].
ACCESSION   WP_457566449
VERSION     WP_457566449.1
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 10000557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..432
                     /product="3-isopropylmalate dehydratase large subunit"
                     /EC_number="4.2.1.33"
                     /GO_function="GO:0003861 - 3-isopropylmalate dehydratase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47218
     Region          1..430
                     /region_name="LeuC"
                     /note="Homoaconitase/3-isopropylmalate dehydratase large
                     subunit [Amino acid transport and metabolism]; COG0065"
                     /db_xref="CDD:439835"
ORIGIN      
        1 mgmtitekil aksagkkevr pgenvwlnvd vlmthdvcgp ptfqimeref gekarvwdke
       61 kvvifpdhyi ftadahanrn vnilreyaqk yqlpnyydvg terykgvchi alaeegydrp
      121 gtvligtdsh tctagafglf atgvgntdaa fvlgtgkiwe kvpesmkfif egempqylta
      181 kdlilqilgd ittdgatyra mefdghavhn lnidermtlt nmaveaggmn giiavdevvr
      241 tylaqkdifd ydefesdada ryhsvyrydv qkmepvvamp hspdnrelar nvagtkitrc
      301 yigsctggkf tdfynaakil qgkkvkaptf vvpastavar rlreeslngs tieqilldag
      361 cviapsscaa clggpadtvg rsvdgdvvis ttnrnfpgrm gskksevyla spltvaasav
      421 ngvitdprem md
//
LOCUS       WP_457566451             154 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease, partial [Caldithrix abyssi].
ACCESSION   WP_457566451
VERSION     WP_457566451.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 154)
  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 154)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..154
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
     Region          1..151
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 imtpapkvih qivksniekf lrkfveekdl glvldapcdv yfdeqnvlqp diffisknrs
       61 hiitedmikg apdliievls pnsayydlie kkalyerykv qeywladpkl kwievyilkd
      121 qkfhlhqrae knqtihshll knfslpleqv ftkl
//
LOCUS       WP_457566452             691 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Caldithrix abyssi].
ACCESSION   WP_457566452
VERSION     WP_457566452.1
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 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..691
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=79020
     Region          43..>395
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          75..221
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          413..667
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpfksfhrli llmfiilffs hsfavaesde rlltpqellq lkmvataqvs pdgnyiaytv
       61 rvpraadddp gsayselyvm alktrqitpf itgkvrvvgv qwrpdskait fldkregdef
      121 rqvyeirldg geaypitdvq knisrylwhp sgkmlvfsat eppsekekfl rkkgydfify
      181 eeewkhinly aydlttkeer qitrditvld fifdpqgsql farmteknli dyhymfthwy
      241 kvnlkdgsyq kvsqnkgklg nasvspdgrw laynaglneh dsdfsqafli sldepqkeav
      301 nitppkyrgh itwvgwlsnn kmlylaaegv envlyeynvk ngkrkkilhs aqqgvifdvp
      361 smsrdrkvfv ftghsatfpr evflwkkgkr ltrlttlnpw ladktlgeqk vihyaardgl
      421 qieglliypv dyqqgkkypl vvqvhggpes hysngwisry atpgqtlaar gyfvfypnyr
      481 astgygvefa mqgfgdpagk efddiadgik ylidqglvdp qrvglgggsy ggyaaawfat
      541 yytdlvkaac mfvgvsdmis kkgttdipye ellvhagkki eeewqkiler spiywahqsr
      601 tallifggta dtrvhpsqsl elyrrfkmnd ktvrlvqypg eghgnarqpg qidvlyrvld
      661 wydwylkenh pvdgpmppld isekyglslp e
//
LOCUS       WP_457566469             104 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator, partial [Caldithrix abyssi].
ACCESSION   WP_457566469
VERSION     WP_457566469.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..104
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          1..100
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 rnsgivvdgv ssgrlalhkl eqetydlvlt diqmpgmdgk eliqkirqkl peipiliisa
       61 yeeekfeaei ktmkkiqmva kpfdqttile kirallnsnd isan
//
LOCUS       WP_457566470             380 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566470
VERSION     WP_457566470.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..380
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44881
     Region          5..372
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 msilinilkt dsefdalqke wqqlveevkp dsifltfewl htwwqiyker fvrpqpaiit
       61 vrnietreli ailplfshlk ihgrkkglkt lqlmgteies sdyldlicap dkkvvilkki
      121 fgeprvvdff lrfdvllfen ihddstllle keelanilnt nvyhyrikvc pflplpqsae
      181 qlmsslsknf rsnlkrarnk leragfriel vehfsqiera ienlfalhdq rfkakqaask
      241 fnferrgtfh qqiariflkn nwlqlyqiwd kdkvigslyc ykfngsmmym qggfdpaytq
      301 yglgnqiilk aiedaiamgl kkfdfmrgne pykykwtkek iflhklifpi slkaklffaw
      361 qdltlnlkki vklmiskikq
//
LOCUS       WP_457566472             165 aa            linear   BCT 27-JAN-2026
DEFINITION  HIT family protein [Caldithrix abyssi].
ACCESSION   WP_457566472
VERSION     WP_457566472.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..165
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19200
     Region          23..150
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(49,51..52,59,61,107,115,117,121,123)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(119,121,123..125)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            121
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mkqlwapwrm kyilneidkn tgcifcqfpk anddekylip yrsekcfvil nkfpynnghv
       61 mvvpyqhtgd ylelseevll dmqrtiqkti qvlnavmhph alnigmnlgr iagagiddhl
      121 hyhivprwdg dtnfmpviad tkvvsesled tflkmrnefq klfqk
//
LOCUS       WP_457566473             610 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Caldithrix abyssi].
ACCESSION   WP_457566473
VERSION     WP_457566473.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..610
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=68016
     Region          4..509
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mhqevfiqla ailvlgilaq wiswkihlps ilvllltgfl vgpvlnwidp dklfgvalfp
       61 ivslsvaiil fegglslsyr qlknlkdvvl rlvtigvalt fglvaltahy vlnmnwhiaa
      121 lfgsilvvtg ptviipllhh lrvkreigqv ilwegivndp igatmaliaf eviiaeslgq
      181 ailvsvlgif ktlligtllg algafllvfl mkrywlpefl hnpvtlmvli iifglsnhfq
      241 eesgllavtl mgifmanqkm apvkhilefk enlrliliav lfillsarle lsvipftdpt
      301 ayfflfllif virpvmvsls tigtslnwre rvllfwmapr givaaavssi fglylvekgm
      361 pegmqlmsyt ffvivgtvaf ygltagrvas llklsfahpq gilivgahaw grklarffkg
      421 qgidvllvds nkhnvkmaer egceaqegni llenfqegld lsgigklfal tsndevntla
      481 clhfadllgr enifqiayhe pqlngepdrn pmwrgrilfd keltfekles llknggelkv
      541 fkidehytfd dflqqedrky plilkkvngk levwaedkmp epeigdqila ivlpvkngqm
      601 engkqerdll
//
LOCUS       WP_457566479             205 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566479
VERSION     WP_457566479.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..205
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23261
     Region          12..155
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mapnterikk rynrvavvfd llekpmekft sswrreiike vygkvlevgv gtgknipyya
       61 pdvevvaidf skkmlekara kyqhifpdvt fiemdvqqld fsdnsfdcvv tscvfcsvpl
      121 pvlglkeirr vlkpggklvm lehvrsqkkl vgplmdilnp iplflygani nrrtvanlrq
      181 agfkqitetn lwadtfkkiv aingk
//
LOCUS       WP_457566488             334 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566488
VERSION     WP_457566488.1
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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..334
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
     Region          1..330
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 gvhpqvmkal qdcnvgheig ygddpytmra terfkehfgg qtgvyfvygg tganvtglqv
       61 llkpyqavlc aetahiyvde cgapekftgc klmpiktkdg klrveqlepf lsmlnfehhv
      121 qpavisitqp temgtvytve eikaiarfak annmrlhmdg arlanaaayl dlpfksftvd
      181 agvdvlsfgg tknglmfgea vlifnplfqq dfkyirkqgm qlhskmryia aqfdaylkdd
      241 lwlknarqan rmaqmlaeri kevpqititq avqtngvfav vppqiieplk keyffyiwna
      301 aahevrwmts fdtteqdien fvntlkrilk kylt
//
LOCUS       WP_457566482             141 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Caldithrix abyssi].
ACCESSION   WP_457566482
VERSION     WP_457566482.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>141
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          11..>138
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mteaeiiivg ggpagascaa elhragrdal ildkktfprt klcagwvtpr vwkmlgvkpq
       61 eyphsiilfk klhyifgkkr ltvptrqysi rryefdhwll qrsgarfirh qvqnirrhed
      121 hfiiddqfrc kilvgaggtn c
//
LOCUS       WP_457566491             352 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 peptidase family protein [Caldithrix abyssi].
ACCESSION   WP_457566491
VERSION     WP_457566491.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 352)
  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..352
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..352
                     /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=38831
     Region          35..350
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mfsrrnflks aafllsalpf tayarkesks asakilkppa lhegdtigli tpasplfefh
       61 rtvieatekl knlgynvkla rnidkkwgyl agsiqervdd lhqmfdddev kaimairggy
      121 gsaqllpyld yeliarnpki ligysdital llgihaatgl vtfhgpvavs tftdyttrhm
      181 krvftttapp iqiedapyea nlqtsnriwt yrggvtegrl iggnltlfqs llgtpfaatt
      241 qdailffeei geepydldrm lthlkmagif dqckgvifdr mpsvkpadyk pgfnsslsve
      301 evidmifkdf dfpvcvgfsl ghikdkptmp lgikaqldad agrltlleaa vv
//
LOCUS       WP_457566492             293 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566492
VERSION     WP_457566492.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>293
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          71..292
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 miflaryqkt alqivlifva igllwlvlfs nilpeltgfk lapslvyfvf lilaalylyk
       61 alsvplekse qisralshne rkyrtlveei nevifvidqm grityispai tlltgfspne
      121 ligrlfvefi dprdeetvfk afkerlrgqv aplqyrilsk dgssrwvrsl skpykneqgn
      181 igvrgvlmdv tdlvekdmal iesearwral veqapdyiit tdlkgkiefv nrsffnvpek
      241 qiigqmihdl vpttqmkrvq eaiekvtqkg glhrfeieln vegqkhwylv rtg
//
LOCUS       WP_457566507             500 aa            linear   BCT 27-JAN-2026
DEFINITION  ligand-binding sensor domain-containing protein, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566507
VERSION     WP_457566507.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Zhang,Z., Liu,Q. and Hendrickson,W.A.
  TITLE     Crystal structures of apparent saccharide sensors from histidine
            kinase receptors prevalent in a human gut symbiont
  JOURNAL   FEBS J 281 (18), 4263-4279 (2014)
   PUBMED   24995510
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hoch,J.A.
  TITLE     Two-component and phosphorelay signal transduction
  JOURNAL   Curr Opin Microbiol 3 (2), 165-170 (2000)
   PUBMED   10745001
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Perraud,A.L., Weiss,V. and Gross,R.
  TITLE     Signalling pathways in two-component phosphorelay systems
  JOURNAL   Trends Microbiol 7 (3), 115-120 (1999)
   PUBMED   10203840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>500
                     /product="ligand-binding sensor domain-containing protein"
                     /GO_function="GO:0140299 - molecular sensor activity
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          6..>456
                     /region_name="COG3292"
                     /note="Periplasmic ligand-binding sensor domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:442521"
ORIGIN      
        1 mktnqifvwl ivfgstlfaq kfsveyynye dglpsdlikq tiqdnlgfvw fatdgglarf
       61 dglrfkvfdr qlpsryvksi fplkkdtlmv ctdqglvlvk erpikvditp ifktspdlsd
      121 salyypksiy rdhknnlwis epnsvarilp gnkikryrfp dyvesksyln sffflenerq
      181 dllllsqsgf affydsksds fiqvsiksrs pfyaindvyk fendrcflat sqgvyelsfs
      241 dptalrarlr fkiknvlslt idrtgylwmg tsgsglyysp nwqkssavis fdklkfkvin
      301 dlyvskggei wagsdngval iykpffekiv gfsnyaiqnl aydgqkhiva tngqevyqls
      361 ehpgryqlkl rlkssdalfs tigvnsreiv lgnfngnitl lrkglrrnip lvtnhtvfsl
      421 atdrdntiwi tqgdfkgltr lrppknievv dersglqgfp vvvkafsnkl yiggsgdsty
      481 lyeyrlnqkk lvnlslplsk
//
LOCUS       WP_457566506             129 aa            linear   BCT 27-JAN-2026
DEFINITION  TPM domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566506
VERSION     WP_457566506.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Cerutti,M.L., Otero,L.H., Smal,C., Pellizza,L., Goldbaum,F.A.,
            Klinke,S. and Aran,M.
  TITLE     Structural and functional characterization of a cold adapted
            TPM-domain with ATPase/ADPase activity
  JOURNAL   J Struct Biol 197 (3), 201-209 (2017)
   PUBMED   27810564
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Sinha,A., Eniyan,K., Sinha,S., Lynn,A.M. and Bajpai,U.
  TITLE     Functional analysis of TPM domain containing Rv2345 of
            Mycobacterium tuberculosis identifies its phosphatase activity
  JOURNAL   Protein Expr Purif 111, 23-27 (2015)
   PUBMED   25782739
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Aran,M., Smal,C., Pellizza,L., Gallo,M., Otero,L.H., Klinke,S.,
            Goldbaum,F.A., Ithurralde,E.R., Bercovich,A., Mac Cormack,W.P.,
            Turjanski,A.G. and Cicero,D.O.
  TITLE     Solution and crystal structure of BA42, a protein from the
            Antarctic bacterium Bizionia argentinensis comprised of a
            stand-alone TPM domain
  JOURNAL   Proteins 82 (11), 3062-3078 (2014)
   PUBMED   25116514
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Wu,H.Y., Liu,M.S., Lin,T.P. and Cheng,Y.S.
  TITLE     Structural and functional assays of AtTLP18.3 identify its novel
            acid phosphatase activity in thylakoid lumen
  JOURNAL   Plant Physiol 157 (3), 1015-1025 (2011)
   PUBMED   21908686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>129
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          6..129
                     /region_name="COG3762"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442976"
ORIGIN      
        1 mdpakflske eqqqiiraiq eaeketsgei rlhiesrckd dplerakaif qklkmhqtal
       61 rngvivylaa ddhkfaiwgd kginekvpen fwedvkeama elfkqnrfae glekgismig
      121 dklkeyfpy
//
LOCUS       WP_457566509              93 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566509
VERSION     WP_457566509.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..93
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <1..>71
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 gdkitffsdr dgnyeiylmn ndgsaqqrlt snpaedlnpv fspdgnkilf hsdregnfdl
       61 ylldltqsae qisvsevlsr idqalqkiee eek
//
LOCUS       WP_457566513             324 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 5 protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566513
VERSION     WP_457566513.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Schroeder,H.R., Yeager,F.M., Boguslaski,R.C. and Vogelhut,P.O.
  TITLE     Immunoassay for serum thyroxine monitored by chemiluminescence
  JOURNAL   J Immunol Methods 25 (3), 275-282 (1979)
   PUBMED   762437
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>324
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
     Region          44..324
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mkfiyriylf lfaviffamc nasvdneeea kqeewaeagv inqrlgrgin lgnaleapke
       61 gdwgvvlqse yfqlikeagf nsvripvrws ahakvdspft idpsfmervs wavnqafang
      121 llavinihhy delfadppah kqrflalwkq iaerfqqhsq nllfeilnep hdqltpalwn
      181 dylaealtvi rktnplrtvi igtanwggid aldelvlpdd erliltfhyy qpfqfthqga
      241 ewvsgsdawl gtkwlgapqe iqaiqkdfdr vsqwaalhsi avfmgefgay rkadfasrvr
      301 wtstvareae krnfswaywe fcag
//
LOCUS       WP_457566516             316 aa            linear   BCT 27-JAN-2026
DEFINITION  2-oxoacid:ferredoxin oxidoreductase subunit beta, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566516
VERSION     WP_457566516.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Chen,P.Y., Li,B., Drennan,C.L. and Elliott,S.J.
  TITLE     A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes
            C-C bonds from CO2
  JOURNAL   Joule 3 (2), 595-611 (2019)
   PUBMED   31080943
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Yan,Z., Fushinobu,S. and Wakagi,T.
  TITLE     Four Cys residues in heterodimeric 2-oxoacid:ferredoxin
            oxidoreductase are required for CoA-dependent oxidative
            decarboxylation but not for a non-oxidative decarboxylation
  JOURNAL   Biochim Biophys Acta 1844 (4), 736-743 (2014)
   PUBMED   24491525
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Fukuda,E. and Wakagi,T.
  TITLE     Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from
            Sulfolobus sp. strain 7
  JOURNAL   Biochim Biophys Acta 1597 (1), 74-80 (2002)
   PUBMED   12009405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>316
                     /product="2-oxoacid:ferredoxin oxidoreductase subunit
                     beta"
                     /EC_number="1.2.7.-"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          13..316
                     /region_name="PRK11867"
                     /note="2-oxoglutarate ferredoxin oxidoreductase subunit
                     beta; Reviewed"
                     /db_xref="CDD:237006"
ORIGIN      
        1 mnnqdrvatq plkltaadfa skseprwcpg cgdyaiyaqm kkilpelgip kekfvfvsgi
       61 gcssrfpyym ntfgvhsihg raptvasgik lanpelkvfi itgdgdglsi ggnhfihlcr
      121 rnidvtvilf nnriygltkg qysptsvkgq itksspygtl enpfnpvlma masgatfvar
      181 tidrnpkhla eilrraaehk gtsfvevyqn cvifndgafe dlyskdtkdd ralymekgkp
      241 yifgknhdkv lkwncsrfea vpydeanppe nllihdeknl saeiefglas ltdnphlptp
      301 mgifrqvete tyeell
//
LOCUS       WP_457566519             415 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Caldithrix abyssi].
ACCESSION   WP_457566519
VERSION     WP_457566519.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 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   7  (residues 1 to 415)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     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=48048
     Region          1..414
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mitkidvknf ksfdhlniel snfnvvigpn asgksnfvqi frflkdieqs glenavslqg
       61 gveylrnmki nnnqnfslsi eaddifgfvr pyrnkyfgik itktkyefel tffkrkknfk
      121 iskdqlnlsc efkiltkekn qlkelenlge gsidlirkns qikirlnkpl afpfseeeif
      181 psflwekfnv innllienpf ftfpaineif sdihiydfdp rlpkratpis gkveleedgs
      241 nmalilknil sdqdkkrklf nlmqevlpyi hnlnvekfad ksllfkvqee fienqyipas
      301 aisdgtinlt aiiltlffek nkliiieepe rnihpfligk liglmkdaar nkqiiltthn
      361 aefvkhtele nlflckrdsk gfskiikpad nkeiksflnn eigvedlfvq dlldi
//
LOCUS       WP_457566521             312 aa            linear   BCT 27-JAN-2026
DEFINITION  patatin-like phospholipase family protein [Caldithrix abyssi].
ACCESSION   WP_457566521
VERSION     WP_457566521.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..312
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34045
     Region          1..304
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mikkpkialv lgsgaargla higvlkvleq egipidlivg csmgamvgga faaglssqqi
       61 eeiacetnwr rvvqilfprr frrdglldgq rveeflisll geeaiedlpr qfacvatdir
      121 qgeeiilnsg slvnairasi sfpflfqpvh lngnylvdgg vvnpvpvsva rqmgaelvia
      181 vnvtpsvknr trvlssgkli tsqklkaahs assflqrlfg nfmeklpapn lsvrkknsea
      241 kmgiqqqmah vamtmenmil mlrlqdsppd ilvtpdisaf qffdfnkare iiaigqqame
      301 ekielitsrl tq
//
LOCUS       WP_457566525             252 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Caldithrix abyssi].
ACCESSION   WP_457566525
VERSION     WP_457566525.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..252
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28817
     Region          1..251
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(26..27,29..30,33..34,71,75..76,79..80,114,118,125,
                     128..129,134,149,153..154,156..158,160..161,164..165,
                     168..169,191..192,194..196,198..200,202..203,205..206,210,
                     213..214,220,222)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(152,156,159..160,162..163,205,208..209,211..216,
                     219..221,225,227)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(173..180,193,196..197,200)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 melilqqtqn dhwmvrlnsl gkmlsaiili agilalpfrs sfhlfwltaw tfaliavals
       61 infklikyfs rsavmflllt ialpfhpaya qeaawikidg itlyqsgvqq laatflkamq
      121 ilavslivvv ttpytrllks lqrfkipdwv lailmymfrl iflmeqemar mkramnarsa
      181 kiglkrklqi liaftgvyla rlmdrsergy qamiargfrg kiefwdeesw gvkdgillai
      241 satfflgvvl wr
//
LOCUS       WP_457566526             620 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Caldithrix abyssi].
ACCESSION   WP_457566526
VERSION     WP_457566526.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..620
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=68707
     Region          35..601
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrriliaill igsfsgihar qqqsadtlav ftsrdsivvi gnriatsvrn laysyqivsg
       61 emvqqlsghs alemvdlnfp sayvlenkal gygvgregag ilnlrgiggk pntgvlvlln
      121 ghpdfmgifg hplpdvygne dierieilag psstvfgdha mggvvnlvta pqfkhlarvr
      181 aefgsfgtqi fsvalqkkia knglfftark qksdghisqt sfeslhlqgg wqyqintawk
      241 llvqgryvpy qfddpargev drlnlgayak ikrgtaeisl qnntqkwkga fqlyanaghh
      301 efydgfksdd fsygfsayqf mqysgalafa ggmdviyygg kakndfaklp ngapivnpda
      361 hdltsagvyg vvfytplpqv nlkaglryqy nslplnqisp flgasytman glhfylnyqt
      421 gfraptlmel ylfpsanpel knekvqsvel gtsfaysksg qvrvalfknk vrdliqalpt
      481 ltpppptrfv ngpqsdqwgv evlikqkvls nlfaqigygf lepdlltayn pkhqikylls
      541 yqkeryylnv ygkfvqklya gnnetlplpd yhllnvqagv nvfnldlfvr llnaldenyl
      601 srpdfpapgr qvrvgftfrl
//
LOCUS       WP_457566471             177 aa            linear   BCT 27-JAN-2026
DEFINITION  SagB/ThcOx family dehydrogenase, partial [Caldithrix abyssi].
ACCESSION   WP_457566471
VERSION     WP_457566471.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Ghilarov,D., Stevenson,C.E.M., Travin,D.Y., Piskunova,J.,
            Serebryakova,M., Maxwell,A., Lawson,D.M. and Severinov,K.
  TITLE     Architecture of Microcin B17 Synthetase: An Octameric Protein
            Complex Converting a Ribosomally Synthesized Peptide into a DNA
            Gyrase Poison
  JOURNAL   Mol Cell 73 (4), 749-762 (2019)
   PUBMED   30661981
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Breil,B.T., Ludden,P.W. and Triplett,E.W.
  TITLE     DNA sequence and mutational analysis of genes involved in the
            production and resistance of the antibiotic peptide trifolitoxin
  JOURNAL   J Bacteriol 175 (12), 3693-3702 (1993)
   PUBMED   8509324
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Genilloud,O., Moreno,F. and Kolter,R.
  TITLE     DNA sequence, products, and transcriptional pattern of the genes
            involved in production of the DNA replication inhibitor microcin
            B17
  JOURNAL   J Bacteriol 171 (2), 1126-1135 (1989)
   PUBMED   2644225
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>177
                     /product="SagB/ThcOx family dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
     Region          10..177
                     /region_name="McbC_SagB-like_oxidoreductase"
                     /note="oxidase similar to the microcin B17 processing
                     protein McbC; cd02142"
                     /db_xref="CDD:380318"
     Site            order(10,12,65..67,69,149,152..153,158,162,173..176)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380318"
ORIGIN      
        1 mrentspvki pllrpdqqda lalnqlllkr kshrnfkpqs itlkelsqll waaqgavapg
       61 rrtapsagai fpfriltaie lappqmsvgl ylfepdafrl klmakgafre klyqacmfqe
      121 cilqaplcli lyakltmver vygerafnyi flegghigqn iylaatalnl gtvavga
//
LOCUS       WP_457566528             202 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Caldithrix abyssi].
ACCESSION   WP_457566528
VERSION     WP_457566528.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..202
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23103
     Region          10..184
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 maineiqhff dhqalgwdys fdeqklkrlr wifkhrigal kgpvldlgcg tgvllkvfpq
       61 vlsdrsslil emdlsmamlh qaqekrfgll nkvyfvqadg hrlplaeksm nsvvafqvlp
      121 hfidplhvfq evyrtlkkdg rfvilhlmdh hklnalhrsa ggavedhylp pveevaamla
      181 senfviddfl ekedcyliig rk
//
LOCUS       WP_457566529             454 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease, partial [Caldithrix abyssi].
ACCESSION   WP_457566529
VERSION     WP_457566529.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>454
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..454
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 mkilyryiik ehigpfvmsl svimfillmn flvkyigqif gkglsawvii kliifnlawm
       61 falavpmatl vavlmafgrl ssdneitilk ssgislyrii rpalfaafvl mlamiffndr
      121 ilpesnhqak lmfrsirqkk ptlqlepsif ytvdrytivv nriekplpde wldlanllgp
      181 eyrgkpetdr lvdvtifdqs dakadvtita eegymtyspa kkslvftlfr gefhkmdrqk
      241 tgeyerslfe kqvvyipaee flyeerkdtd rsdremtvsm mrrkveyfrn qiqirqknft
      301 nitdqnlagl qrlilksdsv qaasvdslaa gisenkwkaa yhkakrvvdr yynqaktntk
      361 fidmqnravn kylveihkkf sipfasivfv ligaplgira rkgsmgvgis lsigffllyw
      421 vfliggedla drglitpfwa mwganiivgl agiy
//
LOCUS       WP_457566531              98 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566531
VERSION     WP_457566531.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..98
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
     Region          <1..93
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 glllgvvpda syeagagllp agalitmytd gvtecmniad eefgekrlqe ilryngaqls
       61 aralnerive rlnqfarqmp qsdditlltv krkgkveg
//
LOCUS       WP_457566534             740 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Caldithrix abyssi].
ACCESSION   WP_457566534
VERSION     WP_457566534.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..740
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85075
     Region          2..727
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 medflnelne eqrkavlatd gpvliiagag sgktrtltyr iaylikkqla kpseilavtf
       61 tnkaaremke rlttllgsqa lplwmgtfhs vcarilrtea eriglsrnft iydvddsvra
      121 lrkilsskgl spqkfnpkvv qsrisrlknh fvlpenlleq elddeydqiv aevyqaymaf
      181 lkknealdfd dllirpiqvf ddfpeikaky nkkfqyilvd eyqdtnhaqy lllkrlvner
      241 knlcvvgded qsiygwrgad iknilnfnrd fpearifkle enyrshnnil qaanavvrnn
      301 ksrlgknlwt rkqdgpkikl vvaddeadea lkvveiihde mythkrsfkd iailyrtnaq
      361 sraledqlrr naisytiigg vkfydrkeik dvlaylkvlv npadsvalrr iinfplrgvg
      421 ettvnkierf aemenitlfd algrveevan isatmgsrvk qfylmmkkfm elkdelnave
      481 lastlvseag imhhyqteyd qyesesrien ikelfatmeq ftreregegr dsdlaaflee
      541 vslmtdidtw nessnavtlm tlhsakglef pvvcitglem glmplqrtsa dlkeleeerr
      601 lfyvgmtram eslyltyaky rrrynagtyn tpslfldeip tellefktri agtrgasrgk
      661 rkterkakle ayfqnddqnq dksgeffvgq kvyhetfgkg qiiqlegsgd kmkitvhfgr
      721 dgitkklikk fanltpleen
//
LOCUS       WP_457566535            1209 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566535
VERSION     WP_457566535.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 1209)
  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 1209)
  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 1209)
  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 1209)
  AUTHORS   D'Andrea,L.D. and Regan,L.
  TITLE     TPR proteins: the versatile helix
  JOURNAL   Trends Biochem Sci 28 (12), 655-662 (2003)
   PUBMED   14659697
REFERENCE   5  (residues 1 to 1209)
  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 18646691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..1209
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=139761
     Region          61..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          63..346
                     /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          97..125
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          130..164
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..1148
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          174..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(176..177,180..181,183,211,214..215,218..219,
                     221..222,248,251..252,255..256,259)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          205..239
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..272
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          281..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          795..1078
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(795..796,799..800,802,829,832..833,836..837,
                     839..840,864,867..868,871..872,875)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          795..819
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          827..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          863..891
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          899..932
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          938..966
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(939,942..943,946..947,949,976,979..980,983..984,
                     986..987,1010,1016..1017,1020..1021,1024)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          971..1004
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1009..1040
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1045..1078
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1094..1208
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Site            order(1094..1095,1097,1123,1126..1127,1130..1131,
                     1133..1134,1162,1165..1166,1169..1170,1173)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1121..1153
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1161..1189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkiwiywii allisisgaq nresddfsyp lklyeqefyd laaqqfikfy ntypnsdkvd
       61 daryyaglal ykikeyqkar aefqalalef pkspfaaeaw fyvgdcaekl geysdavkay
      121 eslrvlypqd trtatatfka glinvqqlnd paraaqlfni iierypdskv yfpalvkkaa
      181 vsfrlgrind arsllrrafe vqdkdqaala eayliqgrin nflglidqaq qdfkqaiald
      241 sgsqiaamaa idltnvliqt gdyktaisll ekqvasneqp elknqliyll advyflsgny
      301 nkaqssyqtv aaqndslqfi iqlkralsyq kqnfiseaak lmaqtmgnsa lersavyqka
      361 vafyidfleq nryyqqaasf iyhkltaekt ivqkaqlvvh lvkilaqknq wieiinlvqp
      421 fvlapepfpe kddllfyfal akekseefdq aayyfnklvh efqasvyseq akkhlrflnd
      481 fkiidqdfal nhlaelllvs leaggqdkga vlfelgkfyf hdlknytkae qvfksalnsg
      541 anrpgdiyyy lgqtylkqle yqeflnrpvg nllqlanenf kkaieneatc sapdvsawll
      601 vratlkpdsq knrngkrfie allqkypnsa lkeewlrtla idmafdsshv qeslkyfril
      661 ieqfqqseqy pqyllsyarl lqetnpadar aiyqrivdgf mfsreaalai adlidmyiaq
      721 qnfdaainlf erfqvyfyys emldqlkmrm geiylkagqy draiafytqt intpflndii
      781 llrefennei lkdiyflaea frlkgdansa irfyrlyllv epngqfadea hfkagelyfn
      841 sgkyflaken fkavskqdpr lftqaviqag niyfleddya naaqfyqqal knidvpdlkl
      901 kvrqkyilsl irqgkiteal nliktyekqf kanpdalaqf yielgnyhrl qknfskaeqy
      961 fkrvkkkykn sdyvddaeyf lgiilitqnk hkealkilte fpekypesdq lpgvyntlgt
     1021 iyfrsekydn aiamfkkala hcqncelenn imsnlikvys ltgfwdaaqa marnylekfp
     1081 eaddrldkki iiarayinln qfqnavdylk sikaeadaer epeiqfyige allragqyee
     1141 aiaefvkipl lskktklqwe asalyysgqc yeklgridda irmykeiikr pgidlvlkkd
     1201 aekrikqiq
//
LOCUS       WP_457566537             475 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Caldithrix abyssi].
ACCESSION   WP_457566537
VERSION     WP_457566537.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12795692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..475
                     /product="peptidylprolyl isomerase"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=55469
     Region          148..254
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
     Region          395..>468
                     /region_name="Rotamase_2"
                     /note="PPIC-type PPIASE domain; cl29122"
                     /db_xref="CDD:452928"
ORIGIN      
        1 mrklfslliv lllmtvacqk neisnpekdi aqvgklsvdk qvfmnrfrms kgfaeakkfs
       61 iddvvkfide yfvknyllvn klldqgieee kemkeameql kiramtgmng plyrqvipan
      121 vevsdqeiqe lydkskykvk iaylrvsskh ladslysalr rganfgkiar kysldvqtfe
      181 hggevpnyif pgsldpefek aifglkkgql srpiyiagwy nivkildkkp iehrplseik
      241 aqlkqrllqy klnqirnnyi dslfikyeas fnkelyplik kafvpidrvg kldvsaipke
      301 kldeplvtyk ggqftlnsfv tiynksmasr rvplryddei enhvktmvig nlmyadgvar
      361 gllndeqfks lyqrirmqkl erealkrlvn eqikitddel kayyeqhkre wnnqnfetvk
      421 rfvrnrlmge rareykdqla aqlrseydvl yneplikevv dslnamkkaa rvrkf
//
LOCUS       WP_457566540             267 aa            linear   BCT 27-JAN-2026
DEFINITION  3-phosphoshikimate 1-carboxyvinyltransferase, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566540
VERSION     WP_457566540.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Marques,M.R., Pereira,J.H., Oliveira,J.S., Basso,L.A., de
            Azevedo,W.F. Jr., Santos,D.S. and Palma,M.S.
  TITLE     The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a
            model for development of novel antimicrobials
  JOURNAL   Curr Drug Targets 8 (3), 445-457 (2007)
   PUBMED   17348837
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Stallings,W.C., Abdel-Meguid,S.S., Lim,L.W., Shieh,H.S.,
            Dayringer,H.E., Leimgruber,N.K., Stegeman,R.A., Anderson,K.S.,
            Sikorski,J.A., Padgette,S.R. and Kishore,G.M.
  TITLE     Structure and topological symmetry of the glyphosate target
            5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein
            fold
  JOURNAL   Proc Natl Acad Sci U S A 88 (11), 5046-5050 (1991)
   PUBMED   11607190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>267
                     /product="3-phosphoshikimate 1-carboxyvinyltransferase"
                     /EC_number="2.5.1.19"
                     /GO_function="GO:0003866 - 3-phosphoshikimate
                     1-carboxyvinyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009423 - chorismate biosynthetic process
                     [Evidence IEA]"
     Region          3..>267
                     /region_name="AroA"
                     /note="5-enolpyruvylshikimate-3-phosphate synthase [Amino
                     acid transport and metabolism]; COG0128"
                     /db_xref="CDD:439898"
ORIGIN      
        1 mpklkgtvll pgdksishra alfsairegt syfenfnfnr dcqatlaclr avgveietme
       61 dtsvringke pgrwqkpahp lnaensgtta rllsallanl pfpttligda slsrrpmkri
      121 iepltqmgad irsnngylpl effpvsglkg idyelpvasa qvksavlmag lfaegatrvi
      181 etipsrdhte rllnlpveid argrkiirsr rglpipdism kipgdfssaa ffitgalllp
      241 gselmiknvs lnptrtgfle vlkqmga
//
LOCUS       WP_457566544             416 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566544
VERSION     WP_457566544.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..416
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45538
     Region          3..415
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mktvemvmpk mgesitegti lkwlkkegdv vgndeiilei stdkvdseip tpvpgklvkl
       61 lasegdvvev gkpialieve geaeealtep aasekreaki etpdeksnik skntagrtnr
      121 fytpvvlnia rehgvpmsel eqlegsgagg rvtkkdilrf ieerekgpkv ataaapamet
      181 nvfaggpsdi iamdnmrkri aehmvhskqt sahvslytev dmqavetiis rnkkafkere
      241 gfsltytpfi veatvkalke fpflnasidg dnivlkkyyn igiavavekg livpnifnad
      301 nknllglara lydvamrars kklkpdeimn gtfsisnfgv fgtvvgfpii nqpqvailgv
      361 gavkkrpvvi ndaiairpim ylsltidhrl idgamgsqfl ervreyleky dpamiv
//
LOCUS       WP_457566552             342 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Caldithrix abyssi].
ACCESSION   WP_457566552
VERSION     WP_457566552.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..342
                     /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=39950
     Region          98..333
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 makdeifnei eskmlnkikl nvkeydelyr kgldlikkmp nsqellisil eeyeerldel
       61 ppidiqvenl enfdeklkek ikalilfgtq aallnenakm hhqlrvvnqk ykdlisvvth
      121 efknaltsiy gynrilkkrv enqdydrllp midnidrltk nlftmvdtll nmslieegkl
      181 slnrqifdfm edvitpline fepqlkeknq kivlkksdki lyngdlhllq vvfrnlimna
      241 lqygdedsei eidfnkgees leiyflnygm gvqkeqiphl fekfsrftkl qgrhnvgigl
      301 ytvkniielh ggkitvesnp gewikfiitl pltlqrmdaq ng
//
LOCUS       WP_457566545             181 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA dihydrouridine synthase, partial [Caldithrix abyssi].
ACCESSION   WP_457566545
VERSION     WP_457566545.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Finet,O., Yague-Sanz,C., Kruger,L.K., Tran,P., Migeot,V.,
            Louski,M., Nevers,A., Rougemaille,M., Sun,J., Ernst,F.G.M.,
            Wacheul,L., Wery,M., Morillon,A., Dedon,P., Lafontaine,D.L.J. and
            Hermand,D.
  TITLE     Transcription-wide mapping of dihydrouridine reveals that mRNA
            dihydrouridylation is required for meiotic chromosome segregation
  JOURNAL   Mol Cell 82 (2), 404-419 (2022)
   PUBMED   34798057
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Bou-Nader,C., Bregeon,D., Pecqueur,L., Fontecave,M. and Hamdane,D.
  TITLE     Electrostatic Potential in the tRNA Binding Evolution of
            Dihydrouridine Synthases
  JOURNAL   Biochemistry 57 (37), 5407-5414 (2018)
   PUBMED   30149704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>181
                     /product="tRNA dihydrouridine synthase"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
     Region          6..>181
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mviefgkfki erglflapme nvsdypfrmi ckelgadvvy sefisseali reaekaflkm
       61 tikaqehpig iqiygnrvea mvkaaqlaee kgpdfidinf gcpvkkvalk gagagllrdi
      121 plmvkisaav aravslpvta ktrlgwdahs iqivdvakrl edvgieaitl hartraqgyk
      181 g
//
LOCUS       WP_457566558             258 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566558
VERSION     WP_457566558.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 258)
  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 258)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 258)
  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 258)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>258
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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          3..>258
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mekkhrllav dddidflkal kklltkfefd vevaidpfka veqiknnsyd cilldmkmpg
       61 ldgiqlmdki meedplvpvi fisgqsnipl avhamkkgay dfiekpiepe rlimmlkhai
      121 ernawskerd mlltaideky qmigespvmk evfkkikifs tadakvlitg etgtgkelva
      181 nilhynspra gkpfikinca aipnellese lfghvkgaft gavetkkgkf hlaqdgtlfl
      241 deigdmdiyl qakllkil
//
LOCUS       WP_457566561             338 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Caldithrix
            abyssi].
ACCESSION   WP_457566561
VERSION     WP_457566561.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 338)
  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   2  (residues 1 to 338)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..338
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38308
     Region          4..338
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mkkqrkitia diareagvsa mtvsrylngk gpvaastaer ikaiierlqy npnwlarsls
       61 skksmiigvt ipriehalld nyiaqilsgv tdvalqndyr imllpfnpeh gtdnefsnwy
      121 hskmfdglil lktmhrdpri kslaeqkipf vlanhkyyap dvhfidvnnk lgirlavdyl
      181 vengrsriaf vagdlretna rdrwnafckt mqeqnltvnk ewvihgqfnq eiayresekl
      241 fraktipdav vcsddymalg virrikergl ripddvavig fddieiaayi qpalttvrqp
      301 iekigrlaae sllkllngka dqpirrllsv qlikresa
//
LOCUS       WP_457566562             339 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566562
VERSION     WP_457566562.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Rocha,S.T., Shah,D.D. and Shrivastava,A.
  TITLE     Ecological, beneficial, and pathogenic functions of the Type 9
            Secretion System
  JOURNAL   Microb Biotechnol 17 (6), e14516 (2024)
   PUBMED   38924452
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Gorasia,D.G., Veith,P.D. and Reynolds,E.C.
  TITLE     The Type IX Secretion System: Advances in Structure, Function and
            Organisation
  JOURNAL   Microorganisms 8 (8) (2020)
   PUBMED   32752268
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lasica,A.M., Ksiazek,M., Madej,M. and Potempa,J.
  TITLE     The Type IX Secretion System (T9SS): Highlights and Recent Insights
            into Its Structure and Function
  JOURNAL   Front Cell Infect Microbiol 7, 215 (2017)
   PUBMED   28603700
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Henrissat,B. and Bairoch,A.
  TITLE     Updating the sequence-based classification of glycosyl hydrolases
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 695-696 (1996)
   PUBMED   8687420
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15493915
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..339
                     /product="T9SS type A sorting domain-containing protein"
                     /EC_number="3.2.1.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_function="GO:0033916 - beta-agarase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38803
     Region          33..213
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Site            order(107,109,111,119,121,123,136,138,153,193,195)
                     /site_type="active"
                     /db_xref="CDD:185683"
     Site            order(119,121,123)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185683"
     Region          261..337
                     /region_name="Por_Secre_tail"
                     /note="Secretion system C-terminal sorting domain;
                     pfam18962"
                     /db_xref="CDD:436869"
ORIGIN      
        1 mskyrlflki llvlvmgggp vfaqrlihfa gvdwwvkngg pygpgpnyws dsaqnvwida
       61 qgrlhlairk vndiwycsev ytvkpttfge hrflvdgyid rmdknivlgl fvyaddqaei
      121 dieyakwgyq nktdvgsytv qpystpgnqy sfespldssk tthffdwqpe yvlfgsmrgh
      181 yygappssny yiaqwaysga dnpsasrqlh thinfwlnqg qapqdlsile viitdvvqpl
      241 ntsalkgeek lplavelrqn fpnpfnswtt ieyaiiqatr vtlsvfning ekvkelvnrr
      301 qkpgvyqlrf daqnlpsgmy fyqlktetft arrkmliik
//
LOCUS       WP_457566565             430 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457566565
VERSION     WP_457566565.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48324
     Region          61..381
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mkrsfkryfk garikttrpf vkssiftqth idsgawmkyd ydvliagagp agsaaakala
       61 qkglkvllid rkafprekvc gdgltpgavk llnelevfdf leatqiyain airfvtprlq
      121 alevpfqsrh dkagfliier rhldhallqs alhsgarflq aevsgvvrrq gricgvtikk
      181 ekqverltak lvigadgags ivarsagvpk ippthrflai rgyikgfktm ehavefiwts
      241 elkpgyfwif ptghnqanig lglpadlyqk ksinlkkhff ellnrpllre riledmaidg
      301 lkawpiplag lyktprvfdg amlvgdagyw vdplsgegih nalktgmiaa nvaleafdvd
      361 dfsasflrry eaeawkelgp virrsvwfvr gmryapwlle sffwfarhsq gafrrffshl
      421 stdfefvlrd
//
LOCUS       WP_457566568             333 aa            linear   BCT 27-JAN-2026
DEFINITION  DHH family phosphoesterase [Caldithrix abyssi].
ACCESSION   WP_457566568
VERSION     WP_457566568.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     A novel family of predicted phosphoesterases includes Drosophila
            prune protein and bacterial RecJ exonuclease
  JOURNAL   Trends Biochem Sci 23 (1), 17-19 (1998)
   PUBMED   9478130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..333
                     /product="DHH family phosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37496
     Region          11..294
                     /region_name="NrnA"
                     /note="nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and
                     oligoRNAs [Nucleotide transport and metabolism, Signal
                     transduction mechanisms]; COG0618"
                     /db_xref="CDD:440383"
ORIGIN      
        1 mgkqnnafqi lkkmiddhnh fvvishiytd gdalgavmaf yhylkslgkk veaiipgslp
       61 arydflktrq ainrhsksrl kkiieradvi livdisaler mdewyapvma skakkvcidh
      121 hpdmceqmdl kiidvqriat ceivydffkt qgikitddma lalytgilsd sggfrfegts
      181 gktleiaaql arknidpawv yrqvyeysnk nqlrfwghvl aglqsegvid wavvsretlq
      241 kfnvnieeln glidiirrda aaqifamfve kkngevmvgl rskngfdvgq larrfggggh
      301 fhaagfsssl plrevvqmtl eqikqdqvls pee
//
LOCUS       WP_457566570             452 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding
            subunit, partial [Caldithrix abyssi].
ACCESSION   WP_457566570
VERSION     WP_457566570.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..452
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
     Region          <1..437
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 pyagamrgfg spqpifaqes imdeiaiqlg krpdeirein gfkagsvtat ghqlldhdvn
       61 lltvlktave ksdfsrkwqk yqqqnkrlap mvsagiaanp qnlvldksdl lepeaqlrkg
      121 iglavsfrgc slgaegidav aaylllqqdg salllsglae ngqgmrttya ivaaevlgid
      181 pqdiyyldqd thhvgdsgpt vasratlmgg gatkaaaeil rrrledalrk kwnltkdtef
      241 ifkdrivrvk ddpdrampfs evcnlaysqg vnlsaigwya gpevhwdeef gqgpayftyv
      301 ygchvaevtv nmitgevyvd rvvavhdpgt vinllgaqgq vyggvtqgag yglweeisvd
      361 egfirelnfd qyliptskdi gpiepifvqg ndphgawgak slgeptlelt aaaianavrn
      421 atgkrffhlp lnleeilleh klypgskkrg sv
//
LOCUS       WP_457566572             290 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566572
VERSION     WP_457566572.1
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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..290
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32231
     Region          3..275
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipeieyyka knlketleal dhfngearli aggtdiipgf hinssrfrdi hvlidisqvp
       61 eltniewqdd glhiggaatf tsivensiiq ekypllvasa aqigsvqirn ratiagnfvn
      121 napcadsvpp llvydaqivv qslketrrlp ladfllkpyk tqlqpqevvk eiilpelldd
      181 yrgefyklgr rrgvsisrit lavllrlegn iisdmriasg avtpigkrfp elenlakgkp
      241 aeeeflrela vslgrqvldi tglrwssayk lpvlqqaffn mmlkiisgnn
//
LOCUS       WP_457566584             265 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Caldithrix abyssi].
ACCESSION   WP_457566584
VERSION     WP_457566584.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..265
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30489
     Region          61..221
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(67..68,133,137,173..175)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mqtkniviln yhkiskrmdi gltarhpddf erdlrlfheq gfksvtfldl ikapeklppr
       61 aliitfddgy rsviehaypl meqfgfkgvv yiptdyigks ndwdvqfggk kyvhlnaqel
      121 kfladsgfei gshgashrsf kamplrqced elkrskiile qiaqkpvvsi sypfgqfnrq
      181 ilalsrnagy rfgvgsifyr slasldglsv malrrfniyr sdsmrtvrkk ltanfnsiya
      241 yrdwliqqgs matvlwqkvf ktkdv
//
LOCUS       WP_457566580             627 aa            linear   BCT 27-JAN-2026
DEFINITION  T9SS type A sorting domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566580
VERSION     WP_457566580.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..627
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=70365
     Region          544..625
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mlrvlivlcl vvalsaqtyi ipdlqrddfk dfktwwsini sgenhtwgvf ngyfmatlnn
       61 pnngqqggel pvdmtgmeni gfstaylmhv yskddtiqai irvktlnalp pgsrgwgfwr
      121 seelpitinq atwvfeqkad piyswaslet wwraritrgl qfhksvdltv nnqnwhvyri
      181 vrfgrqyyei yvdddptpvv radtsdlggi lnedygfdcw ndnliyrytq sattgndtve
      241 vyyagwlgss sfvvdyveii sgnykyghtv apqgavrlre vineidngvq dglwkgpyqf
      301 tvgggpclil atakaeeldg ygddddlkiv ldgkdfgynt prswdgdtdq gqpktividt
      361 vlspgtheis fyseatpily datvleapng qvvinqtlne sapagsvdfl wktfefdcds
      421 gqvaiyisgs adeepgwnyr nypdpngvfa didstdddel rveldnwdyg wgtdsammgn
      481 tlfgdsktil imqdvpaghh vlklyanetp tvykvivyve nkaaaspler rtalaqsfel
      541 ganypnpfnp sttipfkipq aghvvlqild vngriiqtli dkrlqpgayq arwsgndflg
      601 kqtasgiyfy rlkfnkqvtt rkliklk
//
LOCUS       WP_457566588             719 aa            linear   BCT 27-JAN-2026
DEFINITION  protein-disulfide reductase DsbD family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566588
VERSION     WP_457566588.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Porat,A., Cho,S.H. and Beckwith,J.
  TITLE     The unusual transmembrane electron transporter DsbD and its
            homologues: a bacterial family of disulfide reductases
  JOURNAL   Res Microbiol 155 (8), 617-622 (2004)
   PUBMED   15380548
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Kimball,R.A., Martin,L. and Saier,M.H. Jr.
  TITLE     Reversing transmembrane electron flow: the DsbD and DsbB protein
            families
  JOURNAL   J Mol Microbiol Biotechnol 5 (3), 133-149 (2003)
   PUBMED   12766342
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12109673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..719
                     /product="protein-disulfide reductase DsbD family protein"
                     /EC_number="1.8.-.-"
                     /EC_number="1.8.1.8"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=79931
     Region          58..165
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          312..718
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 maltfyrntf gakrlfvlaa vigflilsmg rlalaqslfd qpkhvqaqvy seaawatpge
       61 tiwlaiemta deewhfyykn ygetgkptef ffdapegvqi gpvqwpypev iseedittfg
      121 ykgtqyflvp vtlkptvpag ksitikinvd wleckevcip gseelqitlp vkneppevne
      181 kytqlfadar fkiphpltdw qmsasgdeqf ykiqltppew fkndiqsmyf ipyddgiiqy
      241 eakqefkkkg dsylivlkrs qqteslvdtl kgvilaepgw rgqdsekgve vavpvsehla
      301 plassginsi wlailfsflg gmilnlmpcv lpvlsikimr fihqaqdeht kpwqhglvft
      361 agvltafwal aiallilkag geqlgwgfql qspafliils vfmfllglsm fgvfeigtsl
      421 tavggktpek sgffgsfmdg iiatvvatpc tapfmggalg faltqpayvs lliftflglg
      481 mafpfalvts ipallkyvpk pgrwmeslkq fmgfllvatv iwllwvlsqq vgslvvilvl
      541 fnllfasiaa wvygrwgnla mkertrylaw aialillvls ngyvlanyhk yaatpdamsa
      601 skdgiqwqpy sderlnqlla egkpvfidft aswclscqvn ekvafsseev qnkfkelgvv
      661 alkadwtsrd peitralsrf grqsvplyll ysgkagqkpq ilpevltpgi vldalesly
//
LOCUS       WP_457566582             476 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Caldithrix abyssi].
ACCESSION   WP_457566582
VERSION     WP_457566582.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..476
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=56417
     Region          141..272
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mvwvknglvl flislivvta ckkeeeppqv rhqwiamvds fdlwasrvdh afeyskdfkk
       61 akaitpellk syikhyflde lyllaeaktl kldedpeflk imkkikikem tkpngplfka
      121 ivpekfevdn kklellyqrl pyrltlqqil vtsksladsi ydalmkgadw nklvlkysnd
      181 lytakkegvl sdylvpgmaa peyeeaafsl wqkgqisrpv ktdfgyhiir lmyrekldvs
      241 sfnfeqerlk kiaqlsaknq firdyirslf dkfhltanke lypallnafe rkgvfgainp
      301 qkikesdmea ifikhdrdsm slggfveayn elnryeryrl erpedidimv rkiispelmy
      361 ydgvergldk dplyqdfiry nyrhelekia qkrlideaip isdqevkeyf drhrnlwkns
      421 kfkdvkpyvr nrllvekrkr yrgellnalr ekhpvkfnee iiqelvekyn kkkqaa
//
LOCUS       WP_457566589             442 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Caldithrix abyssi].
ACCESSION   WP_457566589
VERSION     WP_457566589.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..442
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=49549
     Region          6..431
                     /region_name="MATE_DinF_like"
                     /note="DinF and similar proteins, a subfamily of the
                     multidrug and toxic compound extrusion (MATE)-like
                     proteins; cd13136"
                     /db_xref="CDD:240541"
ORIGIN      
        1 mfdkrlnrqi fnlavpnils nlsvpllssv dtalvghlps piyigavaig smifnfvywg
       61 fgflrmgttg ltaqaygkqd hadmrlqlwr alffalgagi llivtqdlia yfafylidas
      121 pevekfaniy fririyaapa tlalyavhgw flgmqnarlp liitvtinfl nivfnlifvl
      181 qlkmtsdgva lgtllaqyag vflsffflir hykpyvsips fkdivewlel trffkvnfnl
      241 firtlsllfa fsfftaqsak lgdiplaans vliqlwmifa ygidgfafaa eslvgkflga
      301 ndrknlarli kqifilgsgl gllisivygl fdrqiaalft snravlntia qfmpwtivap
      361 flnsfcyiwd giyigatatr alrnamllai fgvylplhyl ltpvfgnhgm waallslmif
      421 rtvsltylsp khlkiqikti fr
//
LOCUS       WP_457566591             175 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566591
VERSION     WP_457566591.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 175)
  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 175)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 175)
  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 175)
  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 10118426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>175
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          5..>173
                     /region_name="Beta4Glucosyltransferase"
                     /note="UDP-glucose LOS-beta-1,4 glucosyltransferase is
                     required for biosynthesis of lipooligosaccharide; cd02511"
                     /db_xref="CDD:133005"
     Site            order(84,86)
                     /site_type="active"
                     /note="putative metal binding site [active]"
                     /db_xref="CDD:133005"
ORIGIN      
        1 mkkqtlsvcm ivkneerfia dclksvqava dqivvldtgs tdqtveiarg fgaeihhfnw
       61 cddfaaarna sikyatgdwi lwldaderll pesvpvlkkv lkpekkavay vvnirnvmad
      121 gktfklstgh rlfnnrkkiy fegrvheqiv yslarnggee rpseiqllhl gyals
//
LOCUS       WP_457566585             374 aa            linear   BCT 27-JAN-2026
DEFINITION  alanine dehydrogenase [Caldithrix abyssi].
ACCESSION   WP_457566585
VERSION     WP_457566585.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Dave,U.C. and Kadeppagari,R.K.
  TITLE     Alanine dehydrogenase and its applications - A review
  JOURNAL   Crit Rev Biotechnol 39 (5), 648-664 (2019)
   PUBMED   31018703
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143131
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..374
                     /product="alanine dehydrogenase"
                     /EC_number="1.4.1.1"
                     /GO_function="GO:0000286 - alanine dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0042853 - L-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41140
     Region          2..359
                     /region_name="L-AlaDH"
                     /note="Alanine dehydrogenase NAD-binding and catalytic
                     domains; cd05305"
                     /db_xref="CDD:240630"
     Site            order(13,15,21..22,43,45,136..137,140..141,144,147..149,
                     151,157..167,169,182,186..187,190..191,194,202,205..206,
                     209..213,214,216..219,283,304..308,311..312,315,318..319)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:240630"
     Site            order(16,76,95,300)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240630"
     Site            order(97,270)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:240630"
     Site            order(131,134..135,138,175..176,178..180,198..200,204,220,
                     238..240,249,267,270..271,298..302)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240630"
ORIGIN      
        1 mlnigivkel kpyesrvmit pegvgvltrn gltvyvenga gescgfddlq yeragaiilp
       61 tmekvfskaq liiqvqpphp vqfelltadh illsfmnlih qadrlttlvn tkstfisael
      121 lqdadgkypl lvgmseiagk mavflsamll ttpeggkgkl ltgtefsrps tmtivgagtv
      181 grtvaaiahd lgvkvnlltl kpekieeahk evpqihiqay nddllrellp qtdvlvvaih
      241 slkrefdiki trdmirlmek gsvlidisva eahvvetshl tnhdqptfiv egvvhycvpn
      301 igalvpqtas rvltkkllpy ikvlalkelk dalleepglv paigiykgki tnrmvadyyn
      361 qdfynifell elni
//
LOCUS       WP_457566594             511 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator [Caldithrix
            abyssi].
ACCESSION   WP_457566594
VERSION     WP_457566594.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 511)
  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   3  (residues 1 to 511)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 511)
  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   6  (residues 1 to 511)
  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   7  (residues 1 to 511)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   8  (residues 1 to 511)
  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   9  (residues 1 to 511)
  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   10 (residues 1 to 511)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   11 (residues 1 to 511)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   12 (residues 1 to 511)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18728560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..511
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58217
     Region          6..375
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          383..510
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkppsesdln rkilenvgda licfdeqgei vswnaaatem fgyrkkeavg qkmlfllfee
       61 eqrrlfeqki deveknkgph laptfelqvv gmhgqqipve vtlssfihkd aryftalmrd
      121 mrsrkkrdel knrtqqlqal srlagkiasd fnnvlsvvrg yvelmriqid ernpfakqie
      181 ailktiehae kldeqlmtfa qapgqttqnv dlarvysslk dlllkllepd islkedietd
      241 lwtvrgdpqa lkrmllnlfv nareampegg eiqfkiqnir lneaekderg isvgsdrfll
      301 iqiadtgrgm peevqkkife pffttderee krglglsvvy gmvqsmngvi lcdsqvgrgt
      361 tfsiylpase tdeeameera lesnggeeti lvvedvpevq llllellqtv gyktigvssy
      421 qeamdyyrah geeidliisd vvlpdqygte lirklleerp dlkyilisgy adqldieqnk
      481 mlfqghflqk pfhpstllqm vremldedga d
//
LOCUS       WP_457566596             751 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor, partial [Caldithrix abyssi].
ACCESSION   WP_457566596
VERSION     WP_457566596.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12154327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>751
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          22..95
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          102..744
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mktyllfflt lfvasnlfag siagkvidka tgeplaganv ylkgttmgaa sdqdgmyyfk
       61 apdgvytlvc nfvgyadqev eivvkgdvrh dfalteflft ktievladra keretpvaft
      121 niekeamelr lgsrdipmvl nttpsvyatq qgggagdari nvrgfnqrnv aimingvpvn
      181 dmengwvyws nwdgvgdata siqvqrglsa inlatpsigg tmnvitdptk tkpglkfkqe
      241 ygtgmflktt vvantglian kfafnaalvr ktgdglidkt wtdawayylg aswdinknnr
      301 veiyalgapq rhgqnlykqn iavydsayaa glsdydpaaf skfkergref nqnwapvnpa
      361 ykgkqawnes thdrysanfi nerenffhkp ivnlnwysnl tdrmtlynvf yysgghgggt
      421 gtygkvyrrd angvlggeny kfyygpspwi ydwdqtiemn rgpagtyyvd kkaltkengq
      481 slgilrnsrn nqwtigaisk inykvsdnik stigidwrka eidhyrevrd llggeyyidn
      541 sdefnpnkkv glgdkiayyf tndvdwlggf vqaeyskdrt taygmfgysg ikysylnhfk
      601 kgpdggklka etdvlpgyqv kggvsyrstd qtqvyanagy vskvpifddv iddyngikne
      661 dyenstftsv efgmnytsan rqfvlktnvy ytkwnnrtfr essfpfegee ylvylsgvnq
      721 ehygiefega yqpsrlwrld fagsighwmy t
//
LOCUS       WP_457566597             463 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457566597
VERSION     WP_457566597.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 463)
  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 10133673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>463
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          124..417
                     /region_name="M14_CPT"
                     /note="Peptidase M14 Carboxypeptidase T subfamily;
                     cd03859"
                     /db_xref="CDD:349432"
     Site            order(188,191,250,265..266,318..319,325,365,391)
                     /site_type="active"
                     /db_xref="CDD:349432"
ORIGIN      
        1 mfrfaillis fwllaglvya dfpaqsarty sevevfldkt ssfetlaaag lifdhikile
       61 ksaeglrfkt vvnssemeil kqsglsfkvl iadvvqdfla rqkqinaasl vredlpagfe
      121 ygsmggyytf devvneldsm rlnyphlita kqsigksien rdlwmvkisd npdvdeeepe
      181 vfftalhhar epgglmtlmy fmdyileqyg vdaqvtylid hreiyfvpvv npdgyvyneq
      241 tnpdgggqwr knrrpvqswy gidlnrnygy qwgyddagss pypfsdtyrg sapfsepetq
      301 airdfvnsrn ikcvlnyhty snvliypwsy iaaltpdsit ymeygdllts qnrygfgncn
      361 qtinynangd addwmygeqs ekakifaltp evgddsdgfw pdqsrivplc eenlksnlnl
      421 twlagaypra rsfqiifddn gngfaepgeq ikivcqskni gls
//
LOCUS       WP_457566600             617 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457566600
VERSION     WP_457566600.1
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 12122902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..617
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=68963
     Region          8..451
                     /region_name="FAD_oxidored"
                     /note="FAD dependent oxidoreductase; pfam12831"
                     /db_xref="CDD:432816"
ORIGIN      
        1 mkkikteili vgagasgvca aiqaarmgrk valveqspwl ggmltaagvs aidgnhklps
       61 glwgefrsrl ydhyggpqav etgwvsntlf epkvgerilr dmalsagdvh lfhgffpvev
      121 lmekdrimgv rfsndqkqqm eiralytida teygdvials gaefrygres aaetgepgap
      181 akadrfvqdl tyvavlkdyg pdadktisrp qdydphefkg ccrewgdefq kntidaqrml
      241 eygrlpgdkf minwprngnd yfshlavmdr agrlaeieks kavtlrfvyf iqqqlgfknl
      301 gladdefpts drlalipyir egrrivgkst lklqyilhpy saeaaglyqq giavgnypld
      361 hhhdkagiav deeyapipaf nvpfaclipq kvrgliaaek sisvthmvng ctrlqpvvmq
      421 igqaagaaaa lavekdrpve klnvrelqet llqagmwlmp ftdvtpehwa fkslqrvalc
      481 gllkgqgkas dwanefyifp ekpvtareav ealsalnpef kvnndlhfpe nlehsltrqe
      541 gvrmiwqalg spkesvnlfl ndvqdlavdf ilaqnlgtpw idfekelfyp kepmtrsvfa
      601 hlidhlfrpf kkplffe
//
LOCUS       WP_457566601             481 aa            linear   BCT 27-JAN-2026
DEFINITION  OmpP1/FadL family transporter [Caldithrix abyssi].
ACCESSION   WP_457566601
VERSION     WP_457566601.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..481
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54411
     Region          31..481
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mkrivalilf ftvnvfaqtv eeatllvene sgfgvkaaal gnaftaiadd ysaiywnpag
       61 laqikmqqmy gslnhlklnt eatflgnktt ldqgytkfqs fgyvypfpvr rgsmvlalgy
      121 qrtkdlnkiv qfsgfnpnsn dlafsiyndl gydglilpfd adlnlsqnik edghlsqwsi
      181 ggaidlapnf sagatvnfig gssdyrlkyl qedargtnsy diydadgqli enfyynyyqi
      241 eqlistdysg ielklgglwr lnqnlrvgan itfpmklsvd etwtyadels ydvyvigeda
      301 tyrfvepyds lgqfnynikv pfkfdlgfsy tfknlllaas gryvdwtqle lekgddapag
      361 yetyftrqnd mapliltdvf syslgaqlsi lnnslqlrag yryvpspikd seksfdktyv
      421 svgagfiisk ntqidvavir giyetdkyyr ydwdydqsle pmathekyqi driqvglrys
      481 f
//
LOCUS       WP_457566604             225 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566604
VERSION     WP_457566604.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 225)
  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 225)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>225
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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          2..>225
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 marikilvid dekligwsfk kefdnkyfev ttaesgeegi klfekdfhdi vfldnrlpgi
       61 qgldvlkklk qlrddvyiif mtaygsieta veamkmgaye yinkpfnhde irillqgikd
      121 kiqlvhevql lcrdkpmdlt fnhiigtsps irqaiqlakr iatskattvl llgesgtgkd
      181 ifasaihnqs trkdrpfvpi ncatlpenll eselfgherg aftga
//
LOCUS       WP_457566607             586 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566607
VERSION     WP_457566607.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 586)
  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 586)
  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 11419012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..586
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=68409
     Region          282..547
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          283..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(328,331..332,335..336,338,369,372..373,376..377,
                     379..380,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          328..355
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          360..397
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          408..434
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meeafnelfk ksrllwgdyy dflkkqinat tdslekkyle qqlravkkem eteprpqvar
       61 aftlfydtrh kkgfalplrf arsfedkiit hsttrtaien awlavqhtcg vyfpdrmfdl
      121 afdiseppaf sidgqslgls aavmiisqyf qrpipadvaf sacievngql tpvdffdeka
      181 agvqkhlkyi nqiicagsqt isksftkpei vpcqsleeal ihlwgqeflt qtliperenp
      241 erlfqallfy ekmqnnpavd qlldriieef aqakrpslkt iyvyalaekg lqlthksrls
      301 eakgyfeqar keltklgdhl dpaipvfevf nkygvwltdn yrfkeaesyf kralkllkry
      361 rhppyrlint mnslgqlyak tgrrqeaetl fleslkiadq teeyddrari ycylaenqil
      421 agqfeqaevy lhqadgslsp kkeiqrlfna fwramlyfrk ndaasfaryw gqwqkeswfl
      481 earedflhvq mikayavsll nlketdyfvs vveyfarqrd vltllllaqi dachflrhnd
      541 lmfydkqtvl nivrqakkhn sylkkqlpae ldsaeswral ckvicf
//
LOCUS       WP_457566609             603 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566609
VERSION     WP_457566609.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 603)
  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 10154684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..603
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70398
     Region          99..314
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06241"
                     /db_xref="CDD:349460"
     Site            order(109,112,172,181..182,211..212,217,300)
                     /site_type="active"
                     /db_xref="CDD:349460"
ORIGIN      
        1 mkkrsvfmlr iilifllims vrflgqarad dwqtyceksq fkatpdyaqt mafcekladf
       61 spwiqfisfg ksaqgrdlpl livnkdgrfd pqainreqkl valvqagiha geidgkdagf
      121 iflrdlvvhk khaslldhvv llfipifnvd ghersgpynr inqngpqemg wrttavnlnl
      181 nrdhlkadav emqawlklfn rwlpdffvdv hvtdgadyqy vvtynmdthg vldgglnqfl
      241 ksrfipaleh amqennlpii qyvmfknhyd pksgmlnwvp sprfshgytl lhnrpgllie
      301 nhmlkdyrtr vnatyhllet lfdlfddyqa plrrlikqad ratldadfla rpfpltfrrt
      361 gdstmidflg feyqtlksdv sgglwyrydn arpktfripf ydffvpervv nlplaylvpv
      421 ewktvidrla lhgityfels qdmelnlety rfkevkfass pyegrqmvrf ksepthfkri
      481 yhkgsvivpv kqrtarviah ilepdapdsf vrwgffnaif ekkeyaesyv mealarkmla
      541 eddrlrarfq ekmqadsafa rnprailnwf yrhspywdrf kdiypvgkit daqllnhllk
      601 gvn
//
LOCUS       WP_457566611             244 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457566611
VERSION     WP_457566611.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     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=27730
     Region          2..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 mkamilaagl gtrlrpltdq rpkalveigg ktlleinirr lkeagfkeli invhhhaqqi
       61 mdfvkknkaf glriafsvee qlldtgggvk karwffedcd aflvhnvdvl tdmdytnlfe
      121 nlketralac lavrqrdtqr yllfddrlal ggwqniqsge krimvednrp lkpysfmgvq
      181 vlssaifdff paetkfslie aylqlaaqkq kvcavieqqa rwldvgkkgs lleaellfad
      241 wlkk
//
LOCUS       WP_457566618             903 aa            linear   BCT 27-JAN-2026
DEFINITION  PD-(D/E)XK nuclease family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566618
VERSION     WP_457566618.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Gupta,R., Capalash,N. and Sharma,P.
  TITLE     Restriction endonucleases: natural and directed evolution
  JOURNAL   Appl Microbiol Biotechnol 94 (3), 583-599 (2012)
   PUBMED   22398859
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>903
                     /product="PD-(D/E)XK nuclease family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
     Region          19..886
                     /region_name="AddB"
                     /note="ATP-dependent helicase/DNAse subunit B
                     [Replication, recombination and repair]; COG3857"
                     /db_xref="CDD:443066"
ORIGIN      
        1 mnhiyvtcra pgsyfafqdq isehleqnhl talvivpvnr avrrlkrtlt nlagkralid
       61 ppvftfdrll lhiyqhlphp arllpadtml vliqeileqq aeafqyltrg qqvkgglvnr
      121 vwemtgelrs fgftstelag kdpqelevhp ekftdfvrll ekieeklgae fidepfarat
      181 aarqvtrqqf eklfpqvkal yisgyglfsp pmidfikrvg qwlpvhvqld flqanqelfr
      241 htlqalekfk ligariehks tpsflarflf nrkdrsqkrd lsrrihvvgl ssrerevafi
      301 agkirqlnaq gvplhkiavt fshlekyaqt irqvfedfgi pfnlstgfel irsplisafl
      361 dvltiieedf paeqtlaflq nqfvqkpeei dfdllnsviv karvralner slealkrfip
      421 lqaradeeng wnqekaleqv ellktllqpl fafpreaaad afrkkylelc erlgllrwyq
      481 tenprlterq kehnfraynr fvkvferslw tlsliygkts fksrqlmesl qravltatyn
      541 ltewpdygvq imprleilsv dfealflggl vdgdfprasv kdiffndrvr yelglvasee
      601 lldqdrflfy qlldggasqv yltypqyqqe ealvpssfla dlqdvalvdw qqpadddplf
      661 eneqklwkef glnlqwianp elrqgaienl rllralqpqn etllknlidq irislarsmg
      721 gafseyegnl slftvvtdal rqkyarhtws vsrletyarc pmqfflryvl kieaparree
      781 eltplergql lhtilfrfys elkemgqqdq pwrfvdrlma ialeefaalp ysglfwemek
      841 lrfsgnerlk gilpafleke eeraasmpfl pqnfelsfgy sgdfpadpqs ikeavllksg
      901 dqt
//
LOCUS       WP_457566616             107 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caldithrix abyssi].
ACCESSION   WP_457566616
VERSION     WP_457566616.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 107)
  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 107)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..107
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12368
     Region          <2..96
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mifhaplavd lseknvlqpd iifiakerqe ivtdknisga pdlvveilsp stayydlfdk
       61 kelyeqfgvk eywivdpmrq wieiynlqgn kfvltqklek qgrlnpl
//
LOCUS       WP_457566615             106 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Caldithrix abyssi].
ACCESSION   WP_457566615
VERSION     WP_457566615.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 106)
  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 106)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..106
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12139
     Region          51..>106
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mntgrafkys vyavffsvkm alnsrqmiss knqmhvmkvk etasiykaks kpftyqeylk
       61 lpddgqryev ingelimtps hltihqqisd eiflklggyv kqkilv
//
LOCUS       WP_457566619             564 aa            linear   BCT 27-JAN-2026
DEFINITION  lamin tail domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566619
VERSION     WP_457566619.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Eldirany,S.A., Lomakin,I.B., Ho,M. and Bunick,C.G.
  TITLE     Recent insight into intermediate filament structure
  JOURNAL   Curr Opin Cell Biol 68, 132-143 (2021)
   PUBMED   33190098
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Dittmer,T.A. and Misteli,T.
  TITLE     The lamin protein family
  JOURNAL   Genome Biol 12 (5), 222 (2011)
   PUBMED   21639948
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Dhe-Paganon,S., Werner,E.D., Chi,Y.I. and Shoelson,S.E.
  TITLE     Structure of the globular tail of nuclear lamin
  JOURNAL   J Biol Chem 277 (20), 17381-17384 (2002)
   PUBMED   11901143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..564
                     /product="lamin tail domain-containing protein"
                     /GO_component="GO:0005882 - intermediate filament
                     [Evidence IEA]"
                     /calculated_mol_wt=62777
     Region          13..135
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Region          303..396
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
ORIGIN      
        1 mllvflswpt lraqvvisev mfdvqgadyh defvelyncs seavdltgwq fsdstgtddl
       61 qdagyglllh pgqfavildg syfensttyd siippealil kisdgafgsg glantrperl
      121 tlidaggrei dayrysvdns pgysdekiil csaqvegnwa nsltaggtpg fknsvsprdl
      181 dlaftaeglt vlpqsmlqkg qivqvklryf nagtqafygq ttfrcfldln gnqkleilep
      241 ivferqlevg ldpgqgdsll feirlemsge lnliaellsd ldqnarnnqa mqklvvmdtq
      301 qalvineikf ltqeeepewi elyndsdqki llnnwaiadl kdtlvidrnl vlparsymvv
      361 aadsaifkiy dlpdsvvyvg qgfphlnnde dviflippwg gwveqapytv dwlmgeeyrk
      421 pslerinpql darlgrnwap cvkngtpgkq nsifssvrht qlkleaqpnp fspdgdghed
      481 ftvlslqvpa qtarvrvlif dmlgrqvcsl tenqfsgqdv aivwdgrdah kkrmrmgiyi
      541 vfaqmiddan gilqeakttv vvay
//
LOCUS       WP_457566620             414 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caldithrix abyssi].
ACCESSION   WP_457566620
VERSION     WP_457566620.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46670
     Region          12..347
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mlfdtdiaiv gagpagstas lflakqniah viidkaefpr dkicgdglsg kvvgvleeln
       61 pkwieemqad eahfldswgv rfvapngeai dlpfrinqsl perapgfisk rihfdqflfs
      121 kidhsiakvf lrtelkkver egqalilhlt qngkaltart rlllaaegdr svvarqlagy
      181 rmqrpyyyag lrayyenvad lhpqnfielh fleeclpgyf wifplpnnqa nvgvgilssd
      241 ikkrklnikk imlsaiennp tikerfknar midpikgwgl plgtvkhpls gdnyllvgda
      301 gslidpftge gignamfsar iaarlipqfl eagdfsaral krydaevydr mwselslsat
      361 lqklvrirwl fnfvikrins nphlqetfst mfndldnrak lrsplfylrl llnl
//
LOCUS       WP_457566621             296 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566621
VERSION     WP_457566621.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..296
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34231
     Region          4..272
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(4..5,8..9,11,35,38..39,42..43,45..46,69,72..73,
                     76..77,84)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          4..28
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          33..63
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          68..106
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          112..141
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          152..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(153..154,157..158,160,184,187..188,191..192,
                     194..195,218,221..222,225..226,229)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          182..212
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          217..245
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 midlakgiel fekgkinqae khfknilekq kenpevhfyl griafqkdqy daaisyfeka
       61 ieynpeeary hemygetlgl kaqqagmikg ammlrkvkaa fekalslnpe slmareglfm
      121 inlfapgvag gdekkamelf elikkqnath ghmaqalihl knnrleeaek efelavrqng
      181 ndreilmrsa rfflqrkkyd rvleiadlyi qhfpddprgy qlkgeahlse hnadealnwf
      241 nlaiekddlf fnayfhrakv flakgksema qkdvdfilnh peaskefker akklmk
//
LOCUS       WP_457566622             568 aa            linear   BCT 27-JAN-2026
DEFINITION  BamA/OMP85 family outer membrane protein [Caldithrix abyssi].
ACCESSION   WP_457566622
VERSION     WP_457566622.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Ma,X., Wang,Q., Li,Y., Tan,P., Wu,H., Wang,P., Dong,X., Hong,L. and
            Meng,G.
  TITLE     How BamA recruits OMP substrates via poly-POTRAs domain
  JOURNAL   FASEB J 33 (12), 14690-14702 (2019)
   PUBMED   31702961
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Heinz,E. and Lithgow,T.
  TITLE     A comprehensive analysis of the Omp85/TpsB protein superfamily
            structural diversity, taxonomic occurrence, and evolution
  JOURNAL   Front Microbiol 5, 370 (2014)
   PUBMED   25101071
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Hagan,C.L. and Kahne,D.
  TITLE     The reconstituted Escherichia coli Bam complex catalyzes multiple
            rounds of beta-barrel assembly
  JOURNAL   Biochemistry 50 (35), 7444-7446 (2011)
   PUBMED   21823654
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469158
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..568
                     /product="BamA/OMP85 family outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0051205 - protein insertion into membrane
                     [Evidence IEA]"
                     /GO_process="GO:0071709 - membrane assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=65421
     Region          <6..568
                     /region_name="BamA"
                     /note="Outer membrane protein assembly factor BamA [Cell
                     wall/membrane/envelope biogenesis]; COG4775"
                     /db_xref="CDD:443807"
ORIGIN      
        1 mafadfvqsv hikgeipvpe kqllktlkmn sgsvfsssml ahkekellry lmrrgylqar
       61 vdsvsvhsaa gdstrkiitf fvnggpefrm rktviksdsi aateyekvme lktgrlfdqd
      121 vlqkdlksml rlaadrghpf aqvevekint esangrgevd lqiriredrt ifikdvvfng
      181 lhytrpevvl rqilfkpgmr fsqswlnkie eriqrlqlfe qisppmmarv aedsvliimk
      241 leegsatsfd gvvgyvpppa ndtnargylt glielsfrnl lgsgrkfkif wektdrlsen
      301 fnfkylepwl lnypidaglg fsrevrdtly iaydlqtttq fnfnemfslf infnrhsvnp
      361 dslasyelgl aknrtyglei girydtrdyp fnpragvfyq ssytyglkqn lgptalierd
      421 slqkrvglns lslqvewyrq lfklqvialq fhlkrikgsh lqlsdyfwfg gsgsvrgyre
      481 rqfngylvsw lnveyrfitg rnarvflftd fgyyktiiqn mereasirgm giglrfrtpm
      541 gimgvdygla qgesfrqgki hvrltsqf
//
LOCUS       WP_457566623             604 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Caldithrix abyssi].
ACCESSION   WP_457566623
VERSION     WP_457566623.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..604
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67156
     Region          168..598
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 meqeeprieg lkafwntlki rfyevsdkvi havnislffv siaalvslal eygfyispqm
       61 eqiiervniv ivlyyvlqyf vkllftlekl eyirthwfes alvvliitea slvlhelgls
      121 qfqnylvdln vkaltrltiv gaqvviilti isgavrlnrr iaylrfhpaq tlmlsffivi
      181 vlgtlllklp ravapghqls wldslftats atcvtglivv dtgthfsmlg qliiltliqi
      241 gglgimtiss ffalflgrgm airerimlqe mlnverldai trlvkgvili tflmealgvv
      301 llffswdlpq wsvgqrlyhs vfhsvsafcn agfslnsdsl msfnqnyplm ltialliivg
      361 glgfvvmidl trgrifeysp kkrvhrysvh mrlvliitgv lliagtvlfl liepfegswt
      421 fkalnaffcs vtartagfnt vdighlttss alllmllmfi gaspgstggg iktttlgili
      481 asfisiirgk trielfrrsi sftilnralv vfafaisfim lssfllslte qadflnllfe
      541 eisafgtvgl srgitaglss wgkliiivsm fvgrvgvltl afaittpreh lrveypeekn
      601 vmvg
//
LOCUS       WP_457566627             340 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase,
            partial [Caldithrix abyssi].
ACCESSION   WP_457566627
VERSION     WP_457566627.1
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 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..340
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
     Region          <1..331
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 kdfiaefwlq nkdfilqkka tffdtstama fkyfadmnvd vavietglgg rldstnivrp
       61 qmvvltpidf dhqkqlgntl asiarekagi ikngapvfca pqkqealtvf lqhiqrpdqf
      121 nyltdlaacr ilessldgmr fevqfkktse khcfrtsqta dfqaqnitla lvagrayles
      181 qrlawseekt qqallnglwp grlqtvrkvp rvifdvshnp agiirtlsfv krkapehkih
      241 lligllehkd hkevvnflsr qnmniyltep qsikklavgk ladafikkgk svhiypdpve
      301 avqkilnrik kdellivmgs hyligyline fsgnpeysfy
//
LOCUS       WP_457566629             480 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566629
VERSION     WP_457566629.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 480)
  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 480)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 480)
  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 480)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..480
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=54204
     Region          4..473
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mhssnenili vddqkeilns lkrllkdrfe vavaesgeeg lalvrrqpfa vvvsdqrmpr
       61 mdgvtfleqv kkiqpdavri lltayadiea tisainqaqv fqyiskpfep defrqiltna
      121 lehyrlvqen krlqkelaea nkrlasenii lkqqverqld lgefigsspe ilrilklvkk
      181 vmdtpttvll lgetgtgkel lakiihynsn rkerlfvaqn caaipdtllq selfghvkga
      241 ftgairdkkg lfeladkgti fldeigdtsh alqlgllrvl qegeirplgs httkkvdvrv
      301 iaatnkdlea evkkgnfred lfyrlsvfpi vlpplrerkd dipdlvqhfi kkyaarigkr
      361 ipgitdgaln rllsyhfpgn ireleneier mvtladdgqa ldvsllspri aqrseatalt
      421 shltrlplkq aiyqledemi rqalkefkgn ilrsaqklgv srvglhkmlk rhnlnpsqfk
//
LOCUS       WP_457566631             149 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease, partial [Caldithrix abyssi].
ACCESSION   WP_457566631
VERSION     WP_457566631.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 149)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..149
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..147
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 rrfkdqqeil iqrpdtvlag lavvpddlal vqkkpeemsy qelvkfirel ktigadpkkw
       61 ivekhlkisl pfanfivvll gaplasrkrr ggmglnfgls laisftyfii irvgqvlghn
      121 gsldpllgaw lgnlifltag lialarvrk
//
LOCUS       WP_457566632             767 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase, partial [Caldithrix abyssi].
ACCESSION   WP_457566632
VERSION     WP_457566632.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 767)
  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 10154683
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>767
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          121..331
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06240"
                     /db_xref="CDD:349459"
     Site            order(131,134,185,209..210,240..241,248,317)
                     /site_type="active"
                     /db_xref="CDD:349459"
ORIGIN      
        1 mrnrlslmli filflqmgii nahsgdipsp asffgfqpge drqlfdyeql iaylkevaqv
       61 sdrikmvevg rtpydkpimv vfisdaqnia nldklrkinh elalnwrlke aeqrayiaeg
      121 kvfvlgtlsm hsgevgpsqa aplivydlat tqdaqkleil rnmvymmvps qnpdgmdmvv
      181 hhywrykgtk yegsslpgvy hkyvghdnnr dyvilsqkdt kaiarlynkt wlpqvvvekh
      241 qmgatgpryf vppmhdpiae nvdaaiwnws wifgsnmvkd mtaaglagvt qhylfddywp
      301 gstetsnwkn cislltecas cqyatpvyve ptelsvygkg laeykksinm slpweggwwr
      361 lsdivryeie stlsllktas lhraeilkmr ndlckkevrr greeapyyfl fprkqhdlse
      421 lvglvrllie hniqvfqltr nvefgeiqar agdiivplsq pfrpfvkevl eaqvyplrhy
      481 tpggeiikpy ditswslplh rgiackqidv fvpldsnals avdssfslfs qsrepfkyal
      541 fnvnknesfk aafqalkngh rvfrlkqnlt lnnrtlpags fvldreaeks venlltvapl
      601 ftsgeinpqm ltevklpria lmetyfhdmd agwtrfvldq ygiafevirp gevektklsa
      661 kfdliifpda skdilmegkh ksgknyymss lppefargmg kkgfqkilkf ldsggkiiaw
      721 grstelfmgl ltiekgknkk esfqlpvkni agdlrkkgly ipgsllr
//
LOCUS       WP_457566635             288 aa            linear   BCT 27-JAN-2026
DEFINITION  Rossmann-like and DUF2520 domain-containing protein [Caldithrix
            abyssi].
ACCESSION   WP_457566635
VERSION     WP_457566635.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..288
                     /product="Rossmann-like and DUF2520 domain-containing
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32138
     Region          6..250
                     /region_name="COG5495"
                     /note="Predicted oxidoreductase, contains short-chain
                     dehydrogenase (SDR) and DUF2520 domains [General function
                     prediction only]"
                     /db_xref="CDD:444246"
ORIGIN      
        1 mqnalvigcg kvgsslfnll vaagfervfv vdtikcfnke wapflgadsf fndlaalpea
       61 hfdllaictp ddqieevvgq lsdrslkaer ifhtsgskta dllqplksgg aiigslhplq
      121 sftrlflppe iwrgivctfq gdlplftylq timqpfgski vainirqkrq lhlaatiaan
      181 fqvalyswae qilkdaqlte gdlnqllgpl irrvgqnlne qplsrilsgp lqrgdegtih
      241 qhfsilkenn rphdaplyrl lslkllenpq feilqreklk kllenyet
//
LOCUS       WP_457566637             288 aa            linear   BCT 27-JAN-2026
DEFINITION  TraB/GumN family protein [Caldithrix abyssi].
ACCESSION   WP_457566637
VERSION     WP_457566637.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007931
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..288
                     /product="TraB/GumN family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32376
     Region          1..288
                     /region_name="TraB"
                     /note="Uncharacterized conserved protein YbaP, TraB family
                     [Function unknown]; COG3735"
                     /db_xref="CDD:442949"
ORIGIN      
        1 mkknlfglla vllivnilfa gpqhsiwevi gkqnkvflvg sfhlltedqy plpsvfdsvy
       61 dqsavvvfea dldslsspav vskflqkgll tgdrtlknvl sdsvftklkk tfeelgqpte
      121 lylkmkpwlv altlnqlnma rlgfkaelgi efyyarkvke earpvqsles vafqmglmek
      181 lseinadeli lqtiedigrs ettipelina wqsgnarald sllnasfkdf peigvfllik
      241 rnqawveqve rflrddrnyl vvvgaghlvg teglvellrk kgyrlkql
//
LOCUS       WP_457566640             359 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Caldithrix abyssi].
ACCESSION   WP_457566640
VERSION     WP_457566640.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..359
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=41420
     Region          <31..190
                     /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          33..61
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(34,37..38,41..42,44,68,71..72,75..76,78..79,102,
                     105..106,109..110,113)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          66..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          101..126
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mklkqifilf lvsiitscsh lsreslnghf ddaqshyltg qrflqqeewv qaeiefrkal
       61 dikpgyapal dglaqlalqk ndlaraeswl nqipetqsgw lpayltrarl kfkqgeyqks
      121 lsqlkriedr veqlrldslr veiaalklrn lirlrrwtea relitkfgah lasnggvekl
      181 ailpqeieqi intlpsefsh lifkkavsra elaeiiaewc ppagdvplsl weydppisfq
      241 airdlptdkn easairkvlg whimwafpdg rfyprdyvtr gelaivlqrl laadqlnlra
      301 mrekrvdypd vplntplwka irelsiyrlm vpeqskrfrp ekkvsgmevi rafqklkcl
//
LOCUS       WP_457566639             208 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566639
VERSION     WP_457566639.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 208)
  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 208)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 208)
  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 208)
  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 11663187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..208
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          <1..110
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
     Region          <38..207
                     /region_name="BcsA"
                     /note="Glycosyltransferase, catalytic subunit of cellulose
                     synthase and poly-beta-1,6-N-acetylglucosamine synthase
                     [Cell motility]; COG1215"
                     /db_xref="CDD:440828"
ORIGIN      
        1 itqpehsffa riqaldwayl qamaalnsna gkpisilgnn fafrleayrq vggferigfs
       61 vtedfalmea irkqtqwkii htidplnavy shplpdfksf fqqrlrwiag gkkmrpwgyf
      121 vtlfsavthl ttlialffnf tywavwlapt flmtadffvl faalkklnlr qllkyfpgfe
      181 mfyffyliaf sllsaaplkv ewkgrrhs
//
LOCUS       WP_457566649             843 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor, partial [Caldithrix abyssi].
ACCESSION   WP_457566649
VERSION     WP_457566649.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>843
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          26..116
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          90..801
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mvkfkktivg illssalafa gttgkisglv tdadtgeplp ganiyvqvgg qtmgaasdvd
       61 gyfvilnipp gsytvkaayv gyspveinnv vvridltttl nikmkqqlle aetvvvearr
      121 pivvkdisns qlnleakaie nmpitsinqa lvlqagiess adgiiirgss prqvlymvdg
      181 lsmndersnt pysfnsitai eeiqvqtggf naeygdlrag lvnvvtkegs tdrytlsifs
      241 nvrdiaflgq akkhfgpsly srdsyfnrpy fdpdvmwtgt nngawddytq rqypkfqgwn
      301 aisyatlqdn dpsndltpeg akrlfewqrr rqgeihepdy vidmsfngpd pimrlipewk
      361 nkynprfhls fyktkemfvf plsrsgyneh qtqlkytfnp tssmkviltg mygeifsvsp
      421 yqwtttptgr llrsqsevan llssttgasi lympgyyspg diyrtlvgak ishalssrty
      481 ydasfqykvs ryktfqmaer dtskkyepvp gyftdeapyg ywgyavagid gtsmggwmnl
      541 grdrsvisty sfdfnltsqv nsknqiktgl rfvyniydin sgtyspsmst wtrsmvykvk
      601 pyrigfyvqd kleyegfian igvrldysdp dvewydlspy dpflkagygd lieeeaprkn
      661 akpqfavspr lgvshpisen aklyfnyghf rtepassyrf rlqresnglv tylgnpelry
      721 ektvayelgy ehnlfdmfll kiagyykdis nqpswvyyrn ingsvsyykm sdlnyedirg
      781 ieftltkryg rwvtgfvnyt ydvqtsgyfg ylryyedpne qrqylrenpy qskprpqpya
      841 rvn
//
LOCUS       WP_457566651             242 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Caldithrix abyssi].
ACCESSION   WP_457566651
VERSION     WP_457566651.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (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   2  (residues 1 to 242)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..242
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26809
     Region          6..228
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mkkeviqvqs lcysyedkkd vlkdisftvk kgesvgiigp ngagkttlfl llcgilkptk
       61 gsirikgeev vyrafnpavg yvfqnpddql fsptvwddva fgpinmalpr eeinkriera
      121 ldicnckqla drpshhlsgg ekrmvaiasv lsmepeimiy deptasmdmr srrniiklvt
      181 snkktnlias hdmefiletc qrvilidsgk lirdghaaei msnselietc glevphslkn
      241 sg
//
LOCUS       WP_457566668             144 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase, partial
            [Caldithrix abyssi].
ACCESSION   WP_457566668
VERSION     WP_457566668.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..144
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
     Region          33..131
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 qltpsglfll alppilagvt vfrknrsrit akilwisaal alvngaleel lwrgtyltvf
       61 pdrwfwglly ptvgfalwhw apqrvrpskm pggvgaflmg alflglcwgg vawqtqsilf
      121 tipshvltdf lglggliyvd srnv
//
LOCUS       WP_457566671             633 aa            linear   BCT 27-JAN-2026
DEFINITION  BamA/OMP85 family outer membrane protein [Caldithrix abyssi].
ACCESSION   WP_457566671
VERSION     WP_457566671.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Ma,X., Wang,Q., Li,Y., Tan,P., Wu,H., Wang,P., Dong,X., Hong,L. and
            Meng,G.
  TITLE     How BamA recruits OMP substrates via poly-POTRAs domain
  JOURNAL   FASEB J 33 (12), 14690-14702 (2019)
   PUBMED   31702961
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Heinz,E. and Lithgow,T.
  TITLE     A comprehensive analysis of the Omp85/TpsB protein superfamily
            structural diversity, taxonomic occurrence, and evolution
  JOURNAL   Front Microbiol 5, 370 (2014)
   PUBMED   25101071
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Hagan,C.L. and Kahne,D.
  TITLE     The reconstituted Escherichia coli Bam complex catalyzes multiple
            rounds of beta-barrel assembly
  JOURNAL   Biochemistry 50 (35), 7444-7446 (2011)
   PUBMED   21823654
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469158
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..633
                     /product="BamA/OMP85 family outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0051205 - protein insertion into membrane
                     [Evidence IEA]"
                     /GO_process="GO:0071709 - membrane assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=72841
     Region          <31..622
                     /region_name="BamA"
                     /note="Outer membrane protein assembly factor BamA [Cell
                     wall/membrane/envelope biogenesis]; COG4775"
                     /db_xref="CDD:443807"
ORIGIN      
        1 mlnkakknik qlfffalilc ntyavfaagr kidkihfskv pfkgdqslqe iinsregkly
       61 eprlvkldri lltnyfknyg flnvyvrdsv aldprknkvt iyylidlgkr yffggvrfsg
      121 lhsitlnqle pafknlrige pfleakvsea irrvediyyn sgkpyvqitp eyiyeqdsli
      181 flylkikena tvyikdiqye gmklvqkfli rreleikkgd rynrralnks qqnlyatglf
      241 ryvrfdlepl agdstqavlk ilvqekearw igfrlgvahd qeiyygnkle ltlqgghrnl
      301 fgtgrslnfy ltpsfyydfg nnkifnsdnk atlvyvepwm fytrtpgvlq lafeqyrpln
      361 sahfniyrss fdvrkvfspg vemnggfsar kvdlikegei dttlitleqv rksavysvsf
      421 yakrdkrknm fnphdgsytd asvsfsysrg knendetein ryitmtaswq ryqpfrpkvl
      481 hfkrwnftla trikigaife pagnkeipid drffaggatt vrgyheqllg paaaydangk
      541 ivraaggkal flanaevrmp lfwllimetf vdagnvwael kdvnpltikp ttgiglavlt
      601 plgpiridfg ykllpkksdp sryaihagly faf
//
LOCUS       WP_457566675             457 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)(+) transhydrogenase (Re/Si-specific) subunit beta
            [Caldithrix abyssi].
ACCESSION   WP_457566675
VERSION     WP_457566675.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Brondijk,T.H.C., van Boxel,G.I., Mather,O.C., Quirk,P.G.,
            White,S.A. and Jackson,J.B.
  TITLE     The role of invariant amino acid residues at the hydride transfer
            site of proton-translocating transhydrogenase
  JOURNAL   J Biol Chem 281 (19), 13345-13354 (2006)
   PUBMED   16533815
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Jackson,J.B.
  TITLE     Proton translocation by transhydrogenase
  JOURNAL   FEBS Lett 545 (1), 18-24 (2003)
   PUBMED   12788487
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Buckley,P.A., Baz Jackson,J., Schneider,T., White,S.A., Rice,D.W.
            and Baker,P.J.
  TITLE     Protein-protein recognition, hydride transfer and proton pumping in
            the transhydrogenase complex
  JOURNAL   Structure 8 (8), 809-815 (2000)
   PUBMED   10997900
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..457
                     /product="NAD(P)(+) transhydrogenase (Re/Si-specific)
                     subunit beta"
                     /EC_number="7.1.1.1"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008750 - proton-translocating NAD(P)+
                     transhydrogenase activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=48179
     Region          1..454
                     /region_name="PntB"
                     /note="NAD/NADP transhydrogenase beta subunit [Energy
                     production and conversion]; COG1282"
                     /db_xref="CDD:440893"
ORIGIN      
        1 mvtitnivyl isasffiigl rwlgspktar kgnllsmlgm liaivvtlld knildftyii
       61 agliigaaig ayvaktvemt ampqmvalfn gfggaasalv ayseyvrvqg vmnidvsitl
      121 vlslligvvt lvgsliayak lqgimtgapi tfpgqkfang vllfvalalg gffvadpsve
      181 mfllviigva vilgitsvip iggadmpvvi sllnsysgla aamtgfvlsn nvliisgalv
      241 gasgiiltni mckamnrsla nvlfaavgtd gggsgvrkdk aevtqytaed aavvldtars
      301 viivpgygla vaqaqhvlhe laellkekgv qvryaihpva grmpghmnvl laeanvpydm
      361 lyemdqinde fqntdvalii gandvvnpaa rtdkdsplyg mpilnvdkar tvmiikrsls
      421 pgfagvdnql fydpktmmlf gdakemvtel mkevkni
//
LOCUS       WP_457566678             582 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566678
VERSION     WP_457566678.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 582)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 582)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>582
                     /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]"
     Region          7..556
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(55,58,401,404..405)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mqhlnwldlt vifaffliif aiaayytkka gestgnffls grnlpwylag tamvattfaa
       61 dtplavtelv arngiagnwl wwnlaiggml tvfffarlwr ragimtdlef velrydgrpa
      121 avlrgfraiy lglfmnaivm gwvnkameki fsvvlpefna fllvvlsasi iavyasasgl
      181 lgtartdsfq fvfamigciv lavilvqlpq vggmaslkek lnpqiinffp kigevsatgi
      241 tggalaltvg affahiglqw wstwypgadp ggggyvaqrm msakdekhsl fatlwftiah
      301 yavrpwpwii valaalillp raqnpdvirq enpalfvkve qafqnksllq tedpvfnspe
      361 fkamyekyen tvdpgvmypk lmlrylppgl lglliavfla aymstiasql nwgtsylind
      421 fyrrfirtsa seqhyvvvsr lgiifmtvfs llvtkyfltt isgawefiin asagmgavli
      481 lrwywwrina wseisamiap liiypfsvyv lglkspitly pivfgttvvw lavtfftrpv
      541 nleklksfyk rthpgglgwk riqemmpevk gdsgfgrlfl dw
//
LOCUS       WP_457566682             281 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Caldithrix abyssi].
ACCESSION   WP_457566682
VERSION     WP_457566682.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..281
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31585
     Region          7..280
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 miyrtqsirn asgeiirfdl rypegtsdap aiiilhgfkg fkdwgffpdl atslafsdyv
       61 titlnfsrng igsdgknfta leafarntis heledvqtli daikggridn hvinpeaigl
      121 lghsrgaava llsaleneeh igavvtwaav gnlyryseee isawkaqgyk evvnqrtgqv
      181 mrmnatyled leknkekfdl yhriedleap tlfihgsedt tvspeesekl hercgayskr
      241 leiieganht fgikhpfeks tepyaiardl teswfdrhlk y
//
LOCUS       WP_457566681             118 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Caldithrix abyssi].
ACCESSION   WP_457566681
VERSION     WP_457566681.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..118
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12797
     Region          <42..117
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mktnpttlfl afmlltlliv ggylllsdpf agtaqkgvhq fsqpqsqnqg amvfylqkca
       61 schgargegk ggnpslqntp fteaqiqeii kngrgempaf pelspeelkq lsrlikqf
//
LOCUS       WP_457566683             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Caldithrix abyssi].
ACCESSION   WP_457566683
VERSION     WP_457566683.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  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 328)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..328
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=37941
     Region          2..322
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 meaiekiike kiryifidei qriplllnev hylieefpgc qfimtgssar klrrggvnll
       61 agralerqlf pftyqeikes mnledllkyg slpplleknn tekreilnay vntylreeiq
      121 aegiarnigg fsrfldvaas qftellnfna iardcalpvr tvqsyyeile dtligfrllp
      181 wrksvrkrlr ahpkfyffdn gvtnalngml tsslagaikg klfeqfviqe vyrfkhylqs
      241 eanlffwrtn hgaevdllie khrqikyive ikvstiitga hlsgirafhe enpdvpayiv
      301 apvdqpyele gvkilpwqhf vlnlenfl
//
LOCUS       WP_457566685             453 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566685
VERSION     WP_457566685.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 453)
  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 453)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 453)
  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 453)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..453
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=51627
     Region          2..447
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mmkikvlivd ddtllsdema aflsrsgysv eqaqtltear stvsafapdi llldlklpdg
       61 sgldllpeir ekfpqttiil lsgygsipev vtaikqgaed fltkpldpdh lllrlqkvqt
      121 hkqlstrlki leldwenqrq miigqsrkmq evikqsqava qgnttvlisg etgtgkhlla
      181 yyihqnsprs eapfvyvnca tlsdqllesd lfghekgaft gavrqkegrv elarggtlfl
      241 deigelpitl qakllhfiey gefqrvggtk tlranvriic atnrnlqqei eqgrfredly
      301 frinvvrvei pplrerpedi pelfdfflqk fcrelgkpll nyspslrekl lrypwpgnir
      361 elrnalerav alcntwqlse edfpflksda pmqedplfap tdlqtaltrf krrylqrilq
      421 gvngnqsqaa rilhiqrtyl nrlikelkie tek
//
LOCUS       WP_457566686             291 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase, partial [Caldithrix abyssi].
ACCESSION   WP_457566686
VERSION     WP_457566686.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>291
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
     Region          5..286
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mcvkrvlitg ingyisqfll qtrpenveii gaarrddlsa halnidalik ldlsqavqpq
       61 lnalsgpvda vihtaavssl alcqkepela lrvnaqatre lahwcktnga rliylstdiv
      121 fkgdyppyde nskpepinhy glskwqgeia vqetmdnfai grialalapg lngtrnfidw
      181 flerlnnnet iplfkdeirt ptytvelarr fwqlalsrat giyhicgava ldrftlgqkl
      241 cdalgyghkl leaislndmt dyprpvdvsl vctqtpdgad fkipsilefl p
//
LOCUS       WP_457566689             327 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Caldithrix abyssi].
ACCESSION   WP_457566689
VERSION     WP_457566689.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..327
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36694
     Region          44..310
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mrhvqnilki iislgllgyl iyraeparli svlsnitekd gvaflvaafl lmllavffla
       61 lrwrvllksy gfhlktsqlf gfyligmffn nflptsiggd imriyklisa tddrtsafas
      121 viierlmgia atllmsifal iyisqqfhdn rllivavvmf laimvfftli lrdrsfniil
      181 kifdrftifk igqkfnklfe aihlfqekrm vlmevfmlsf isqffivsmn ylvavafsip
      241 vsfgyllmvv pisfvltmlp singigirdl gfvgllaqvg istaealtls flnliipmvi
      301 staggllfml qknkaipgge nvfdaki
//
LOCUS       WP_457566695             438 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N, partial [Caldithrix abyssi].
ACCESSION   WP_457566695
VERSION     WP_457566695.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>438
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
     Region          4..438
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mdnlsslsyf vpelfltaai lgviildlll kkehkiwtgi vsaaalvisv flifqqytlq
       61 aseifmgmli ldsmavyikl isavssiiii lfslpyftdk seyyvlilit tlgmflmgav
      121 ndilmiivam elvglmsyvl tgftkrnyrs neaslkyily aatstgvmaf glsylygltg
      181 etnllkiqqa lmnhpphqva ffitfvfila gigykiamvp fhfwlpdvye gapttitaff
      241 sigpkaagfa vlirffttvl shgssengvf lqnlqvhipq llailavltm tlgnlvalrq
      301 tnikrlmays siahagymlm amvvfntqgf kavlfyllvy lfmnfgafwv iiaisqklgs
      361 ekieafrglg yrspyaavam avfmfsltgl pplagfigkf ylfaavvndg wyvlailgvl
      421 nsvislyyya yvvkqmfl
//
LOCUS       WP_457566697             180 aa            linear   BCT 27-JAN-2026
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Caldithrix abyssi].
ACCESSION   WP_457566697
VERSION     WP_457566697.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..180
                     /product="NuoI/complex I 23 kDa subunit family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=20202
     Region          15..141
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 mveyfkniye avvtiligmg vtfkhlfvps vtvqypkekv elpprsrmql fvriedcigc
       61 rqceracpvd cieidlikad kdedlgltsn gkkkpfhvir fdidmskccf cnlctfpcpt
      121 ecihmtpdye yaqedrsnli fqfsnytaeq vaelqkreae kaaaraaaka ktggsgtpan
//
LOCUS       WP_457566699             192 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Caldithrix abyssi].
ACCESSION   WP_457566699
VERSION     WP_457566699.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..192
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21914
     Region          7..180
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 msekiilsvp ahldylaive sfvelvgkhi pvqnkellaq qlrftvneaf vnilqhtprp
       61 pdgmvvihfe fdpptlylrf pdrgkglkik dqyppyssem vgddylilkt lggelygyie
      121 nprtvklwfk evdtkmdkkq iiaqlkpggm glsiivkfmd evrfvkdeee ghyleikkyl
      181 tgdqesgrns ds
//
LOCUS       WP_457566705             163 aa            linear   BCT 27-JAN-2026
DEFINITION  Mur ligase family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566705
VERSION     WP_457566705.1
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 11433699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..163
                     /product="Mur ligase family protein"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008764 -
                     UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
                     [Evidence IEA]"
     Region          <1..163
                     /region_name="MurD"
                     /note="UDP-N-acetylmuramoylalanine-D-glutamate ligase
                     [Cell wall/membrane/envelope biogenesis]; COG0771"
                     /db_xref="CDD:440534"
ORIGIN      
        1 ailaaryagv seedikavlk tftgvehrle fvrelngvrf indskattve slyyalqsfr
       61 qpiiliaggk dkgsdfskln eqiagkvkav iligaatekm qkawqgikpl yaektleeav
      121 qkayelakpg dvvllspaca sfdmfkdfed rgrqfkeivr rla
//
LOCUS       WP_457566710             120 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566710
VERSION     WP_457566710.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..120
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13532
     Region          1..72
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 memirqdeva rriemirrqq gltqlqlara lhvsqaaisk ylkerippae vlyrlarlgq
       61 ttvewiltge ktywfgrqeg qvqetgatyd adlalakkis alpaearqav ialidllkkd
//
LOCUS       WP_457566722             314 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine protein kinase [Caldithrix abyssi].
ACCESSION   WP_457566722
VERSION     WP_457566722.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..314
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35470
     Region          10..>279
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mdvklkdlii tkklgeggva svylamhkkl gkpfalktll pkyaanpkik krflteagil
       61 lalkhpniir cydvfeednk iyllleyvpg lnlaqlieqi geplslnlml ayfkqilnal
      121 qylhekgivh rdikphnifv ydsgmgfseh svvklgdlgi akalgvsdlt rsdvrlgtys
      181 fmspeqiqnp anvdhrsdiy slgatfyyvc taktpypqkn nsitelvnai mtnniipias
      241 qnrnvpvwlq kiiikmmare peqrfktcne ilqrldeirl nklkktqnpg cllalanylt
      301 isfllilllm lmqn
//
LOCUS       WP_457566723             485 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566723
VERSION     WP_457566723.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10044413
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..485
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0051219 - phosphoprotein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=55311
     Region          5..96
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cd00060"
                     /db_xref="CDD:438714"
     Site            order(29..30,44..45,47,66)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
ORIGIN      
        1 mkhwtitvrn akrevliryq idqkrltigs gkatdlrlpg edvdeinlvv evkgpkliit
       61 pagktpailn gnilkatefv kagdqillgs yllsfqqapg pekkeqtepv weimltfsht
      121 gqtervktlp gyfcfdeqkr dmywspdlhd enrlvkvaie kgqfvarnlf nkpgilfngr
      181 plkkekiseg dtisingihc ifsltqgapk pkkksamrrl ydttfsytql kkekrinqil
      241 ipslfvlflv ffvfgiryiq gpnpqelrdq ivkklsseef trqsmaekee lladcvadis
      301 vlsdmkpyyq tiiqnlndle qqsgfkilsv vipsktiesl khfkqdlntl flynthlnrt
      361 ydsfiayqra adqfrespls snaqhlkita nqflsayrll dvesqkllki adsfsetmdw
      421 lktnanklsg iealsgvvll vndvsisyqn avnninqiqs kfepfvqdte eiesllikle
      481 khrgr
//
LOCUS       WP_457566727             302 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Caldithrix abyssi].
ACCESSION   WP_457566727
VERSION     WP_457566727.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 302)
  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..302
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..302
                     /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=34353
     Region          6..301
                     /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 mnpslvilaa gmgsryggvk qidqfgpnge tildysiyda iqvgfkkivf virreleadf
       61 kavfnpklen kvevhyvfqe ldnipsgfsv pserkkpwgt ahavmvtepa idepfavina
      121 ddfygrgayr ilfdflkaqs nqsaeyaivg yrldktlsdh gavsrgvcqs desgylqkiv
      181 ertkiyrkng kivyldenqg eheisgsvmv smnmmgftps ifkfmnvffk dflekeghnp
      241 kaefflpwvl drliqtdqak vkilptneqw fgvtykedkp ivqksirdli vegkypenlw
      301 df
//
LOCUS       WP_457566728             389 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566728
VERSION     WP_457566728.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     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=43314
     Region          16..53
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          79..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 mfksgnhrfl kglnckhiln llrthqglta rqlseqtglk iatvlnllkn lekhnqvirk
       61 ergastargg kkpliwdinp hfglalgvew lstelraali nfnfelierk tfvfpakltd
      121 sqkveffvks idefvatfnt lqrpivglgv glagiidpaa gcvvdslsfq srnfpllktl
      181 kacfpfpvfl dnesnvgalg lkwllpqfyd krnllyvtlh qcfsgmgtgf ifnhqlyrgr
      241 qnstgewpvl fspsffakla sqlaqihkgh pfidlvrnyn dlseifsaai alaeknepia
      301 lefmrfvsmp lagrlqllin lldpeyvvig gdileiskyl kshleqqifn egligkqklp
      361 glmfspfgay tnalgaaatv madiyspds
//
LOCUS       WP_457566730             284 aa            linear   BCT 27-JAN-2026
DEFINITION  phytanoyl-CoA dioxygenase family protein [Caldithrix abyssi].
ACCESSION   WP_457566730
VERSION     WP_457566730.1
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 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..284
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32788
     Region          33..273
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 miqfpaldtd ralkilyfpt pepvlkhyna pyplteeqvr fyqeegyvyl pkvvnresla
       61 ylqrviqaav llrkkdddra lheksayeqs flqcgylcwd fkpikdfvfg krfaglardl
      121 lqaehvrlwh dqalfkepgg ratdvhidss ywpidrpqls vtlwlalnpv ppekgclyfy
      181 pkshllekhe yvdifnkphf pqalsrekqv yvplnpgdat fhsgllyhga genktdrmre
      241 gmtviyiadg lrfdasdarn rthtscqgle dgdiidtryt pili
//
LOCUS       WP_457566732             373 aa            linear   BCT 27-JAN-2026
DEFINITION  HD-GYP domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566732
VERSION     WP_457566732.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..373
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43140
     Region          74..362
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mthedvfqev hnqiplnrkl tlihenlqny lpfidriafa lydsktdilr tflvsephah
       61 slclyeskls evpsllalkh erspriiedi srlygdskeh srrikesgyr ssytlpmfsd
      121 eallgfiffn srqkspfqga dlnllnlyah lifslilfel nqtrvllssl ktlskimhfk
      181 dpetgahler mahfsriiaa glaakgkyri ddefiqflsa faplhdigki gipdeilfkp
      241 qklepqefqv mkqhtlkgre iidliisnlq vkptayveml rhipelhhek lngrgyphgy
      301 ekdqipleaq iiavadifda ltsdrpykkk wtneealiyl kkhpsewsae ivqalednms
      361 kiveiqqkfk dke
//
LOCUS       WP_457566735             410 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIID/LytB domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566735
VERSION     WP_457566735.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Nocadello,S., Minasov,G., Shuvalova,L.S., Dubrovska,I., Sabini,E.
            and Anderson,W.F.
  TITLE     Crystal Structures of the SpoIID Lytic Transglycosylases Essential
            for Bacterial Sporulation
  JOURNAL   J Biol Chem 291 (29), 14915-14926 (2016)
   PUBMED   27226615
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Holland,S.K., Cutting,S. and Mandelstam,J.
  TITLE     The possible DNA-binding nature of the regulatory proteins, encoded
            by spoIID and gerE, involved in the sporulation of Bacillus
            subtilis
  JOURNAL   J Gen Microbiol 133 (9), 2381-2391 (1987)
   PUBMED   3129534
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Lopez-Diaz,I., Clarke,S. and Mandelstam,J.
  TITLE     spoIID operon of Bacillus subtilis: cloning and sequence
  JOURNAL   J Gen Microbiol 132 (2), 341-354 (1986)
   PUBMED   3011962
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..410
                     /product="SpoIID/LytB domain-containing protein"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /calculated_mol_wt=46975
     Region          11..410
                     /region_name="SpoIID"
                     /note="Peptidoglycan hydrolase (amidase) enhancer domain
                     SpoIID [Cell wall/membrane/envelope biogenesis]; COG2385"
                     /db_xref="CDD:441951"
ORIGIN      
        1 mkfkiilflf lslvifscqp rvkptkvsra pqikvllsrf nnvdsirleg ryslqleeal
       61 yelgkknnff yispsksgfk fysdnrlfvf nsnatvtltp enaqdshfef hknwykgkii
      121 lmlgdqqnil linqidleey lktvlvgemp snkdsyfeal kaqaicarty alermkknae
      181 kpfhvysdvr dqvysslerq trlasaavqa trgvvlmykd rfartyfhst cggmleditn
      241 ywggdsipyl ksrkdivghq facqpsphfr wqktfsfkqi dslfqikfhk sglpsnpqdt
      301 islhltlkvl qrtssgrvks leisyadtsv vlnnfsirkf fslpgkgalp sllfkmqavn
      361 dstlmirgag yghgvgmcqw galnmseqgf kyydilvnqy fpgtylkeiy
//
LOCUS       WP_457566739             192 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/polyprenol kinase family protein [Caldithrix
            abyssi].
ACCESSION   WP_457566739
VERSION     WP_457566739.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Rip,J.W., Rupar,C.A., Ravi,K. and Carroll,K.K.
  TITLE     Distribution, metabolism and function of dolichol and polyprenols
  JOURNAL   Prog Lipid Res 24 (4), 269-309 (1985)
   PUBMED   2819898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..192
                     /product="diacylglycerol/polyprenol kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=21181
     Region          5..191
                     /region_name="SEC59"
                     /note="Dolichol kinase [Posttranslational modification,
                     protein turnover, chaperones, Cell wall/membrane/envelope
                     biogenesis]; COG0170"
                     /db_xref="CDD:439940"
ORIGIN      
        1 mnqtlslrml lqrkaihfat aliplyyhys hnelavkwvt vvlavgflta dllrlkfsla
       61 kkiflnifgk llkqaeterr ltgatmlfvg maatvilfke qqavpallfv aladplaaiv
      121 gqlygknyfw ektlegsaaf yltasaiili ftsyswwglv vaiivtgvel lpmnmddnlv
      181 iplataflla lg
//
LOCUS       WP_457566742             728 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator [Caldithrix
            abyssi].
ACCESSION   WP_457566742
VERSION     WP_457566742.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 728)
  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   3  (residues 1 to 728)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 728)
  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   6  (residues 1 to 728)
  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   7  (residues 1 to 728)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   8  (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   9  (residues 1 to 728)
  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   10 (residues 1 to 728)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   11 (residues 1 to 728)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   12 (residues 1 to 728)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18728560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..728
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=82706
     Region          221..584
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          604..725
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mnkrftsfsf pavffflllt lcfslllaqe dvpapgnrik kqiekikndt eitsqqlsql
       61 knkialqkry dlilnliifl tvinflalyf yfnnkrrnwl ffndilnsln yplfvfkadn
      121 hkielanfaa eknfphkayf eeihdeeklv ieewldrlin krqavmheva ratpeghiky
      181 yqiylyplvn rrgkvahive ywvdttiqrr alerllrskq aleqskqefe kvissipdai
      241 ysalvdktgk ildsyyspvi ekitgyppsy fngdknnwsk ivhpedlpel rsrnkrafle
      301 kqnetrteyr iihkdgsiry irsavtlnfl englirvdgv lmdvteikkt emelmkiqkl
      361 esvgvlaggi ahdfnnilta ilgnislarm iakdnaqies rlveaekacl rakdltqqll
      421 tfskggtpvk katsladmlk eattfllrgs nikpefeipe nlwlvdadeg qlaqvinnlv
      481 inakqampgg gklnikayny fydgrsdlpl krgryvcflv edhgvgidek slqrifdpyf
      541 ttkktgtglg lavtfsiikk hsgyitaqsk vgqgttfyvy lpasdkkadk kkktaetysr
      601 lkgkvllmdd eelileigke ilnnfglnva lakngeeavq iyvealkkaq pfdlvildlt
      661 ipggmggket ikalqkvdqn vkaivssgys tdpvmsnfas ygfkgmvikp yrmsemyttv
      721 ksvlsdsn
//
LOCUS       WP_457566744             337 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Caldithrix abyssi].
ACCESSION   WP_457566744
VERSION     WP_457566744.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..337
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38665
     Region          1..336
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkklrvavvg lgkiaqiahl pflkkmeeve ivavcdvdek kmsailskfk iprwynlfde
       61 miekeeidal hicttnhyhy pmalmalqkg ipaliekpia lnvadaeria elsaktkvpv
      121 vvgmhnrfrd dvqllkefln ekelgdlfyl kagwlkkwtr etlltwetqk qyagggvlmd
      181 lgiqlidmal yllnkpvirs vrmfgynikp qfevedsmla vletadgmsm tfetswnlhl
      241 dhdiqyqhlf gkngsaylnp lriqkvlhgn lvtvtpiaee rvrdrylray erqvrhfinv
      301 vkgeeenmss ardavetmri vdalyrsmke gkeitlg
//
LOCUS       WP_457566749             234 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase [Caldithrix abyssi].
ACCESSION   WP_457566749
VERSION     WP_457566749.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..234
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27674
     Region          4..230
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mneskpliia hrgaknlape ntikacelal ehgasalevd lrmcgsgeiv lfhdywlwrh
       61 frkikavrks plkelkqlrf nhiayryqdn ictlseflah fkntvpinld iknlftnnlq
      121 liraivhdvk qhdmqdqiwl ssfspnflrv ikkefpeirt gylfrnfslv hryidkivka
      181 dawhphyrlv serflqisrr lkkevyiwti kdepvfkemv nqhfngiitd vlik
//
LOCUS       WP_457566752             232 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein,
            partial [Caldithrix abyssi].
ACCESSION   WP_457566752
VERSION     WP_457566752.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 232)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..232
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
     Region          <1..230
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 aevmicggae aaivpsgiag fnamkaistr neepqkasrp fdakrdgfvm gegggilile
       61 elehararga kiyaelvgvg ftadafhitq papggegair amkaalkdan lqptdvqyin
      121 ahgtstyfnd kneteaiksv fgdyayelvv sstksmtghl lgasgvleli atsltvqqnk
      181 vhptvnyefp dpacdlnyvp ntpiekevna alsnsfgfgg hnvtlcvkkf me
//
LOCUS       WP_457566757             349 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Caldithrix abyssi].
ACCESSION   WP_457566757
VERSION     WP_457566757.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 349)
  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 349)
  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 10135561
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..349
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40532
     Region          12..257
                     /region_name="GT_2_like_c"
                     /note="Subfamily of Glycosyltransferase Family GT2 of
                     unknown function; cd04186"
                     /db_xref="CDD:133029"
     Site            order(45,136..137)
                     /site_type="active"
                     /note="Probable Catalytic site [active]"
                     /db_xref="CDD:133029"
     Region          130..314
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
     Site            order(137,232,234)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:133029"
ORIGIN      
        1 mertevfpav tililnwngw qdtiecletv akqeftdfkv liidngsddd svekilawal
       61 geikdistrf sglvyplvpk pvpiqvlpdp etepnkamdy yllkldqnlg fargmnvgmr
      121 fvtsflksef vlllnndtvl dpkalgnlis ifkreprvam aqstiwyydw pdrianaggi
      181 ilpwgqtryy kkikasenkk iefingcalc vrrsvleqyg yltekfffge edfewslrar
      241 knkllmvavg nskvyhkiaa ssernwrkdg rkviifalnr lidlkdfwpr wqwqilrfls
      301 vfyfaflllt ryrigglktl kfartifkya gslkqlqked idfvlnnei
//
LOCUS       WP_457566758             354 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566758
VERSION     WP_457566758.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>354
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          20..339
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 milnsflkek yefivldtti pifyhewrif rffltlqfaa rlifilfrkr phimhihssn
       61 vasflekgfl illcklfsst kiilhlhgsr fefllknkpw frkmvkmvft mtdaiiilse
      121 nfkqlltnlv gtynyiiiph gvdkrlydet iverlndgkv rlsfiglige rkgcyelgva
      181 fkklvaehni knlhlemvgr eeepgeleai knfyerlgil pyvtfyglkv ghekikilkq
      241 sdifvlpsrh dsfgivnlea maaglpvist rqgaipeyli dgdngflfei gdvealteki
      301 rilynnqelr ekmglknkkk iatfysfdqi lkkydalyqq vhtgknqael ntpf
//
LOCUS       WP_457566750             191 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Caldithrix abyssi].
ACCESSION   WP_457566750
VERSION     WP_457566750.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..191
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22919
     Region          12..190
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mmqeelkese lsdrqaieac lkgdkekyri iverykeray ymalmfvknh edamdlsqea
       61 fyrayrslad fdpgrpfysw fyrilknlci nfvnhhrrkq pmdddmerqv qaegtfpdev
      121 fekneraeii wqalslldek dreiivlkef nefsyqeiad alqipigsvm srlyyarkrl
      181 lkklkqfegd l
//
LOCUS       WP_457566765             131 aa            linear   BCT 27-JAN-2026
DEFINITION  macro domain-containing protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566765
VERSION     WP_457566765.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Rack,J.G., Perina,D. and Ahel,I.
  TITLE     Macrodomains: Structure, Function, Evolution, and Catalytic
            Activities
  JOURNAL   Annu Rev Biochem 85, 431-454 (2016)
   PUBMED   26844395
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Karras,G.I., Kustatscher,G., Buhecha,H.R., Allen,M.D., Pugieux,C.,
            Sait,F., Bycroft,M. and Ladurner,A.G.
  TITLE     The macro domain is an ADP-ribose binding module
  JOURNAL   EMBO J 24 (11), 1911-1920 (2005)
   PUBMED   15902274
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..131
                     /product="macro domain-containing protein"
                     /GO_function="GO:0072570 - ADP-D-ribose binding [Evidence
                     IEA]"
     Region          <2..124
                     /region_name="YmdB"
                     /note="O-acetyl-ADP-ribose deacetylase (regulator of RNase
                     III), contains Macro domain [Translation, ribosomal
                     structure and biogenesis]; COG2110"
                     /db_xref="CDD:441713"
ORIGIN      
        1 glyeecrpla pirpgqavit gahglpnryv ihtlgpvygk dkpedkilae cyrnslklae
       61 kkriaslafp aistgifgyp vrdaarvaln tvismapqlk hvqkirfvly sdsdlkahee
      121 alealmntpg l
//
LOCUS       WP_457566763             824 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase family protein [Caldithrix abyssi].
ACCESSION   WP_457566763
VERSION     WP_457566763.1
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 11467867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..824
                     /product="carboxylesterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=93082
     Region          281..523
                     /region_name="COG4099"
                     /note="Predicted peptidase [General function prediction
                     only]"
                     /db_xref="CDD:443275"
ORIGIN      
        1 myrfkfflli ilffnpfvfa qqiidqylil eiphadrwsf vqvdpleqal vdgnfqlpfp
       61 gqqvkfgqrg ravwqkiktd ssgwyrpkdk rafyafftin aekektiild grghnlvyvn
      121 gqprvgnpyq shdqnsphgp efglsalpvq lkkgqntflf kcyrgrlkvv ihapsadlaf
      181 nandvtlpdl isgqrmdapa avvvlnntas plkdvtissd nplipetkvp iiqpfsvrkv
      241 pffikgrapq ekgnlpvtly lnwkgkrvaq tkinlrvvgt edvqkhtfis hidgsvqyfa
      301 inpaqihdgs pralvlsvhg agvealnqaq ayfpkkwthi vaatnrrpfg ynwedwgrld
      361 alevlntvkq kwnidpariy ltghsmgghg twqlgahypd qfgaigpsag wisyftyvkp
      421 essgqtgpve kmllranaps rtpllaenyk qlgvyiihgd sdrvvpvqes rkmveilkei
      481 ghrdfvyhee pgarhwwdrs depgadcvdw pplfdffarh arptpeqirq iqfvtaspgi
      541 satnrwitiy aqqrafefsk iniqvdpgnr kfhgktqnia rlkidlsplt pgqpvtveld
      601 gqilkdltwp akgalffeki dnrwlktsew pgqdkgphry ggfkdafrnq vlfvvgskgs
      661 keenawalak arydaeclwy qgngsvdiil drefdpekyq drnvilygna rtngawqkll
      721 kdcpiqiler eikfgsetlk gndlaalfvf prrdsdfasv gvvggtgikg mratntqkyl
      781 yagngypdfm vfqsaiyddg laaikaigyf snqwkldkan mvrq
//
LOCUS       WP_457566775             268 aa            linear   BCT 27-JAN-2026
DEFINITION  undecaprenyl-diphosphate phosphatase [Caldithrix abyssi].
ACCESSION   WP_457566775
VERSION     WP_457566775.1
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 10005023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..268
                     /product="undecaprenyl-diphosphate phosphatase"
                     /EC_number="3.6.1.27"
                     /GO_function="GO:0050380 - undecaprenyl-diphosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29592
     Region          3..268
                     /region_name="UppP"
                     /note="Undecaprenyl pyrophosphate phosphatase [Lipid
                     transport and metabolism]; COG1968"
                     /db_xref="CDD:441571"
ORIGIN      
        1 mdelikaivl gtiqgltefl pisssghlvi fshllsfega glmfdvfmhl gtlfsifvlf
       61 rkelwqmiis plamirgnpt qenryywrwd lyvilasipa avigltfedq ieqifgsvla
      121 afaflfvtgl mmasipfikk rskeitapms flmgfaqala ilpgisrsgs tifvgilsgg
      181 erekvarfsf imsipavaga vllklkhlig npvssselin ialgtlfsfa fgclaiwwll
      241 dfvkkgkiqw fgyyclalst agliyylf
//
LOCUS       WP_457566776             486 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium-dependent transporter [Caldithrix abyssi].
ACCESSION   WP_457566776
VERSION     WP_457566776.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Malinauskaite,L., Quick,M., Reinhard,L., Lyons,J.A., Yano,H.,
            Javitch,J.A. and Nissen,P.
  TITLE     A mechanism for intracellular release of Na+ by
            neurotransmitter/sodium symporters
  JOURNAL   Nat Struct Mol Biol 21 (11), 1006-1012 (2014)
   PUBMED   25282149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..486
                     /product="sodium-dependent transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=54735
     Region          1..434
                     /region_name="YocR"
                     /note="Na+-dependent transporter, SNF family [General
                     function prediction only]; COG0733"
                     /db_xref="CDD:440497"
ORIGIN      
        1 makskdffts rygliaatig mavgagniwr fprlagqygg sflipwllfl flwsiplliv
       61 efgvgkktrk gtigafskin krftwlgwfv gfcttailfy ysvvcgwslk yfllavrgki
      121 ftinheqmwq sfthfnpeal lyhfaaialg vfiiyrgivr gverfskiiv pllfvlllla
      181 avraitlpna eiglhyffri emhqflnyrl wldalsqsaw stgagwglll tyaiyarnqe
      241 nivsnsfltg ignnlasila glaiiptvfa lsanldqahe vlgagnqgla fialpqlfek
      301 mpaglffvsv fflslffaal sslismiela trvlmdfglk rkravlsigl atflfgapsa
      361 lsleffnnqd wvwglgllls glffafvvnw igvetflsew vnldlkrrgl kiggtilfkf
      421 liplqfvaml gwwfwqaiqw npetwwhplr tyslgttllq wmaviaaglw atkhfvrwla
      481 avkete
//
LOCUS       WP_457566777              84 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566777
VERSION     WP_457566777.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>84
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
     Region          1..>79
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 miksillpid gspyteavld ygdflaekfg ailriltvid irlfdwsvat sadsfvpimp
       61 stefqeesqr iqnekaekvi qkas
//
LOCUS       WP_457566779             760 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Caldithrix abyssi].
ACCESSION   WP_457566779
VERSION     WP_457566779.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 760)
  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 760)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..760
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86321
     Region          8..758
                     /region_name="YprA"
                     /note="ATP-dependent helicase YprA, contains C-terminal
                     metal-binding DUF1998 domain [Replication, recombination
                     and repair]; COG1205"
                     /db_xref="CDD:440818"
ORIGIN      
        1 milkpkvtle qlieklskda efqrnitrwl vleeqparfa pfpqnvdrrl vqalnekgit
       61 qlythqaeaf rkisagenvv ivtptasgkt lsynlpvfqt ilqnpearal ylfptkalsq
      121 dqvretqdli hrlqvdiksf tfdgdtpvdi rrtirsaghi vvtnpdmlhq gvlphhtlwi
      181 klfenlkfvv ldeihayrgv fgshlanlmr rlkricafyg sspqficssa tianpkelae
      241 qltgqpvtli dnngaprgkk hflfynppvv hrelglrrsv vnevrqivrk llptgaqmiv
      301 farsrlrvei lltylrqvas qlkinpnlvr gyrggylpke rrqienglkk geiqvvvstn
      361 alelgidigq ldisilagyp gsiastwqqa gragrrqgts ltllvassap ldqyiiehpe
      421 yfaeknpesa qidpdnlfil mshlkcaafe lpfeenevfa pditrplldy lveenvlrkt
      481 egkyfwmrei ypadevslrn sspenvviid tsdhnrvige vdlfsapelv hkdaiyiheg
      541 vqyhvdeldw dekkayvhqv kvnhytdait ktnikvldvl eeelrdsckk iygelavsrv
      601 ttgfkkikfn thenigmgrv hlpememqts amwwefddrl fsdpyfqesi igeglkgiay
      661 tlnnliplyv mcdvtdisvv pmvrapfshk ptiyvydkyq ggmglskkly eidrevlqgv
      721 aqhirrcpct hgcpsctgpt lentlfgkes alkilellkl
//
LOCUS       WP_457566782             249 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane lipoprotein-sorting protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566782
VERSION     WP_457566782.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kaplan,E., Greene,N.P., Crow,A. and Koronakis,V.
  TITLE     Insights into bacterial lipoprotein trafficking from a structure of
            LolA bound to the LolC periplasmic domain
  JOURNAL   Proc Natl Acad Sci U S A 115 (31), E7389-E7397 (2018)
   PUBMED   30012603
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Okuda,S. and Tokuda,H.
  TITLE     Model of mouth-to-mouth transfer of bacterial lipoproteins through
            inner membrane LolC, periplasmic LolA, and outer membrane LolB
  JOURNAL   Proc Natl Acad Sci U S A 106 (14), 5877-5882 (2009)
   PUBMED   19307584
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>249
                     /product="outer membrane lipoprotein-sorting protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0042953 - lipoprotein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044874 - lipoprotein localization to
                     outer membrane [Evidence IEA]"
     Region          24..241
                     /region_name="LolA_like"
                     /note="proteins similar to periplasmic molecular chaperone
                     LolA, the outer membrane lipoprotein receptor LolB and the
                     periplasmic protein RseB; cd16329"
                     /db_xref="CDD:319986"
     Site            order(41,43,46,48,57,59,61,71,73,82,84,93,95,180,193,195,
                     207,210,212,222,224,226,229)
                     /site_type="other"
                     /note="hydrophobic core"
                     /db_xref="CDD:319986"
ORIGIN      
        1 mktvylswil illtafslya deqakkivkk andkfrgrss yaeatltvvk pnwsrtlsmk
       61 iwalepdyal ilitspardr gtvtlkrkre vwnwipsirr mikippsmmm qswmgsdftn
      121 ddlvressmv edyfhkiirq etfagydcyv iqslpkpean vvwgkllswi skkdylflkt
      181 eyydedgplv ktmvaskvkk mddriipthl eliphnkpgq ktileyqklk fniklnpsff
      241 sqqnmkrvr
//
LOCUS       WP_457566784             978 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566784
VERSION     WP_457566784.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   2  (residues 1 to 978)
  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 10176287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..978
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=113890
     Region          29..532
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09604"
                     /db_xref="CDD:341067"
     Site            order(157,159..160,346..350,371,374..375,378,393,397,472)
                     /site_type="active"
                     /db_xref="CDD:341067"
ORIGIN      
        1 mrlkaicfsl liftmafsqk pyfqqevhyk idvtlnvlak tysgherlty inhspdtlty
       61 vwlhlypnay rnnntpfarq qmeqrisqfy fsdsaargyl kltalrsngk qlsyslknda
      121 ideakidlpl plfpgdtitl eidfegkfpr vfsrmgtwdg yyfaatqwyp kmvvydrlgw
      181 hpdsyldlge fygeyctfdv kitlpelfvi datgmlkddv aeetfmrqla dttryflnld
      241 kadrkqfikn wkhdrerqld lsktktvhfy aenvhdfawf aglhylvlrk ihnggvltnv
      301 lvrpesaynw rhvpdyvkkt vsfygkmvgp yqypkasvvq gqlragggme ypmitiisip
      361 hsdwenflem vvmhevghnw fmgmlgsder astfldegvn sfvelkyleh yygkynltnf
      421 kklffgldil rdlgdwqllq mafgtkvser tdlplnlrae eynrtnygvi nyqkgalmll
      481 aleeyltppv fwkgmreyfa rwngkhptvn dffqtmeevs gkeldwfved wyhstrycdf
      541 viktvkkkre gdslkievwv enkgtmkdmp apvmvvsasg dtlqkwwngn peqplvfktk
      601 dkpleievnp hhsifemsym nnqaglppvk ihffpqipsf etyeviilpy ywyesfvdkh
      661 rlggmiwggn pilkqwfwts kayyatktkr pgyrltltnr fhlplanytd vkaecfdvdg
      721 mrkkglyfsn yfqrrgkdyp kkylnfalea vdlyrddyye ssmfqkaryg vitmegkylt
      781 gkmltglsav frlqkgmqla gsktnylkve iggswwarvs knswfrlegy waniwgaayp
      841 rqesifagge idprhqkfvf srrgslapnr hytlgqgmkm ygygdpdnry flgksgaals
      901 ltvkpwkylp amygsgaalg qksmglkgdq lfaeaglkfn vasiemifpl yisdpapgek
      961 hlafrfllny sfrlsfgf
//
LOCUS       WP_457566788             149 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566788
VERSION     WP_457566788.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..149
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17593
     Region          1..95
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,34..36)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mtihelieks gfnrrtiyfy tqmellpppk gkgksfeyse ehlkrlqqik klqamryslk
       61 eirellsrpd fsleveatlt ptkafrqklv repevhafqs mddsntlwrr lrigteaelq
      121 ikwppsqetl enlenqvkel ihkikgelk
//
LOCUS       WP_457566791             292 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566791
VERSION     WP_457566791.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>292
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          28..221
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(31..32,34,58,68..69,72..73,75..76,110,113..114,
                     117..118,130)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          56..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          109..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mmrsfnlfig liialslivs rcgknpeaeg dnayaqgkyn qaltyylkvk keqpdnakin
       61 eklaltymqr gltlyklrkn ldafqlnyek sqeflpsdtl sehfkkeysk llyelalayh
      121 naspkndiqk ekyftltldy lqkaleydst ntqadaklse irtvnfqkyf dkgknfylqa
      181 rkdrrnanly lnaevyllqa vrlnpnseea knllkkvrqk tiaildisnd lplalaiggq
      241 kymdgnlals itvfnntvdp ysisperftl fdkqgnahqf vaektaefsk gl
//
LOCUS       WP_457566793             205 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566793
VERSION     WP_457566793.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..205
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22885
     Region          104..196
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 maftkcrmgh vyddskfsec pfcksaeede smvnldseet aalestvpdy dtlpqddppi
       61 qkrimsdeti pdqtvpdkil ekdeesalia qkratvkkri egflvtyshn pygdhyplyl
      121 gknsigrntn ndivindmam sgdhaiilfr gnktfiedkl svngtfindg eesidratlk
      181 dndiikmgkt vfkikiigea pgken
//
LOCUS       WP_457566797             419 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Caldithrix abyssi].
ACCESSION   WP_457566797
VERSION     WP_457566797.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..419
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=48588
     Region          242..416
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mkkmliilia fvfvsfvqaq kvsiknfrkl eltgkynyrn vllspdgrfl syvilnnkny
       61 yqyiydlqkd qtiklgkpis ssgdflqfgs vdaqertgel cwkyekkyne lyfdfvhvvn
      121 mgkenlytgv iklnnpdlsw fqgkdipenk sfmkypkied agfiqifyps fartvdyirg
      181 rpifyvaftv drrlvffdhq vngryksifq ikksdeekyd dfttkeiyte lvpkfspddn
      241 ylvfmrdyke nsdilladrk grkgrffsrd nistvaassa ietspewspd gtkiayfsdk
      301 ghtqkysiwi ydlrtgrnte lvsnvnlnds rnkgpqwvgn sgllyvandi qlkdplmyyh
      361 iptqkaiqlp tgtasnldis vvpigngtyr vaftsrgsve nkdeliwtki yvmdltiel
//
LOCUS       WP_457566799             367 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Caldithrix abyssi].
ACCESSION   WP_457566799
VERSION     WP_457566799.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
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 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..367
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41906
     Region          11..361
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnsksnkekp ilevkklrig lgrtfplfyp syetefsier ntilgivges gsgktltsma
       61 ilgihevypg ilqgeinyhf ssnvsvrlld rlslfknvng slypqvrfka wrnnveqlmr
      121 kiwgkyigiv fqdsvqslnp flsvgsqmmd altiqdlsee ekydrvmell kevnlrnpqa
      181 vfksfphels ggmaqrvmia mgiignpefv mldeptigld vtlqaaitdl llniwekrrl
      241 sgiiishdlk fisrvtqkim vmlggevwei gpahvltdlk eerkhpytky lllksdlnrq
      301 vetvetgtdv pvlqhgsdrg chyrtrcvfy nkyanpqlkk kcetqrppmi qvadnhsvrc
      361 wqfeqen
//
LOCUS       WP_457566800             521 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Caldithrix abyssi].
ACCESSION   WP_457566800
VERSION     WP_457566800.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 521)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 521)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 521)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..521
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60222
     Region          38..511
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mklkyllsnl lillvlqala qepisilryi ekdapatfdp itvkdpssik ltellfarly
       61 tqnryvervp eladgepelr ndnrvaivkl kpgikfsdgt pitaddvvft fkaainpqsd
      121 tfnksvfeni adikaldqyt vevdftypvm dakkylmffi ipkdaflspk irktlsycrn
      181 pepvsggykl kvssivgtry qleknnyykg tqepkiheve mnvypnprgh vdqlrnnqid
      241 llpfvlpeal siirndfrfk leaydanqyd fiafnlkndl lkfvqirqam nlafnrrdvl
      301 esfflnegel msgpfpsshp gynssvrpwe fdrnmaktil dhsgfvdsdg dgirdfngkp
      361 lefrllagla ndqnynaiin afiqqmklig ikiklnsyla difeeklirg dfdlvyfnik
      421 vtpagdyspf flsseaypgg knigyyynpv vdtlflqakl ttdfqlqtqi lqdvhkvlre
      481 dcpwiflwyl ryhaayvrkl knvtinpfff fttieewfye r
//
LOCUS       WP_457566807             185 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein, partial [Caldithrix
            abyssi].
ACCESSION   WP_457566807
VERSION     WP_457566807.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>185
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          1..>185
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlqifslfmv gtiagfmnvl agggssltlp alillgldga tangtnriai viqnifaigg
       61 fqqnnknefg dslkfslftl pgaiigalva vnlqdawfkr ilslvivfvi ismflprprh
      121 agaktskklw lylalfgvgf yggfiqvgvg filmatlfhl aqfdlvrvnv ykvfivliyt
      181 lpala
//
LOCUS       WP_457566808             406 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Caldithrix abyssi].
ACCESSION   WP_457566808
VERSION     WP_457566808.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 406)
  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 406)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 406)
  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 406)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..406
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=46298
     Region          1..374
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mfkilliddn eayceqikks lelknyyiey etnayrgley alqsewdvvl vdmvlgqqid
       61 glailkeikk kradipvili sgssvieaah ewieagaydy lekpidlerl iitlnhalel
      121 rkisrlnqsl vdelkrnist vglgntlsea lrilseasda perllilgek gtgkeliakl
      181 lhyncqrkys pfvahdcelq tesdeaalna lyknlfeqar ggtlflreih nlnlaaqkyl
      241 vnflhqnffn snpalpmvkn dvrfiasssi dlkalveqda flselfhlla nftikipplr
      301 ervedipllv nhfidlesrs lgikiekvse qaiqllqrqd wpgnitqlkn vnhymallqk
      361 ngvireqetk lalkldsiir dlhsgekmpd nykridellg arelpe
//
LOCUS       WP_457566809             326 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566809
VERSION     WP_457566809.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..326
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          33..61
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          67..318
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          67..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(68,71..72,75..76,78,106,109..110,113..114,116..117,
                     140,143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          100..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 nrkkiyfegr vheqivysla rnggeerpse iqllhlgyal sseeqrkkdl rnrqlllkmv
       61 keqphnayah ytlgqnynls gafekalkhy lialeknrfq pslqrqllnn iseaylklnd
      121 lanarsfalk saqlqedqig ayymlykiaq qqnqpdeaik wlqtlreknl aaqhgrlkle
      181 ndvllsdadv llslgelfik neqlkraqmc fdeifqygdn nrayvnrivd iwaqnrhfar
      241 aeqfldahls sndgqflelk gllqikqeny igaiqtytll fqlqpnnldi ikrlaglfyk
      301 igekekaesl ikmaadlnal tqkarv
//
LOCUS       WP_457566811             277 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Caldithrix abyssi].
ACCESSION   WP_457566811
VERSION     WP_457566811.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..277
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=30461
     Region          32..273
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 menvqfytqq ltdlafkllp qlllaivvli lglwaikflg rginraleks kvdvslqkfl
       61 vslisigfki lllisiasml giattsfvti igamglavgl alqgslanfa ggvlilllkp
      121 fkvgdvidaq gfigkvdqiq ifntilktfd nktifipnaa lsngnitnys ieptrrvdmt
      181 fgigynddlk kakqiltemv ekderilkep aptvalaelg dssvnfavrv wvkqedfwnv
      241 yydfqenvkl tfdaqgisip ypqrdvhlyq vdgggtk
//
LOCUS       WP_457566815             949 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Caldithrix abyssi].
ACCESSION   WP_457566815
VERSION     WP_457566815.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..949
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=107703
     Region          27..115
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          103..850
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mhkklirilf liialagylf sgttgkiagr vvdkntgepl sgcniiikgt qmggatdidg
       61 yyvilnippg vytlqaiyvg yvtqeiqnvt vkvdlttkin fklseasfeg eeiiviaerp
      121 liqqdatata svvgakeiem apiesfeqia qtkagvnvgp egslhfrggr ssevayiidg
      181 itvtdaihgg tsaidistna iqelslitgs fsaeygqams givnivtkeg gnnfsgnlsf
      241 qtgdivtsss nskyflsein nidpfntsei easlsgpilr nrlsfnvsar yfddkgylyg
      301 qrihtptdia dsiqtgdgaf vslnsnkkyn iqnklkwkvt nsinfyltti yenrkyqeyn
      361 htrskvpdgi pwqyktalqf igkithqfsk fayysvalgy ldkdykryld kdiyslkyvw
      421 ngysagqyfy pggtdnfrqf snqkqytikf dltsqlfknh eiktgvelkr lslfnhsyyl
      481 svdrraepfv dsnnngvwdv gepftdidrn gnwndarddn gdgipgntii legytndkwn
      541 rkptefafyi qdkmefkdmv vnlgirfdyf dpngrvlrdp tdpditnpik neniwkdygt
      601 dgipntndpd gtenngikdp gepevtlaer qtywykkadp tyqispriaf afpissngkl
      661 ffsyghffql ppytylyqdy enkvkpgliq tsmgnpglkp qktisyeigv eqqitrdmva
      721 ffkiyqrdmr niigqdivil pntdaygifv nrdygrvrgi nfslekrfts ffsasidyty
      781 qiaegnesnp tqrvrnyrlk ienlkkivpl dwdqphtlrl ngsigqpnnw mismigries
      841 gypytpqgan eivriaeens arkipiinfd lyakksfain mgnnsfifsv ygkiynlfdr
      901 lnekyvwdat gratyglgly ggefdpdwqr rphwfykprq iflgieysf
//
LOCUS       WP_457566823             110 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein, partial [Caldithrix abyssi].
ACCESSION   WP_457566823
VERSION     WP_457566823.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         <1..110
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          <1..77
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 awfakygywv iaanrflsgt rsvislfagf falrwlpvvl lsllsaavwn glliyggyll
       61 gvnwekivyl ihqynkfvli isvlviilvi llrvvrrrkn vksiegklnd
//
LOCUS       WP_457566824             257 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_457566824
VERSION     WP_457566824.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 257)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  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 20536068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..257
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29275
     Region          82..152
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
     Region          <160..257
                     /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 mfkykiaffi lsaalilnsc hpslikkske kdnidsvlfy qkedipdpfl dgllsppdhe
       61 vvqlkktitp kvkpkkfkei dgfrvqvfas vdsfnalsll nklkplvkds vyliheknlf
      121 kiqagdlpyr qqadslreli kqkgypgawt vqrkilipik estpiktaas sptvnmkrta
      181 dlsefyqiqv fattskqkaq sivdqlslry dfpceyrlqn qlykvllgrf atraeaesvl
      241 keikalgfkd awivhqp
//
LOCUS       WP_457566826             738 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566826
VERSION     WP_457566826.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..738
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84604
     Region          <17..167
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mknfgkillv lliwhgakaq nylwptsasd yltssfceyr pghyhsaidi ktwnqegyav
       61 yavedgtvyr irvsphgygk viylklkdgr favyahlqrf nrkleekvrq iqlknrryti
      121 dwrpkrwpvk kgeiiaytgq tgtgvphlhf eirdaqhral nplhfyrmrv kdqiaprlqe
      181 lliiplnkns avngsvlpks iplkkengiy vlnetvyarg kiglairgyd randvynkyg
      241 fyreqlyind slifeakydt ldfsktsqin igiyyplkal qnkrflklfk elynqldfyr
      301 tapdggviyv keqpvhfkii ikdfwdnqsv vrgrilpafn pppqilyarr lkdqlfvkal
      361 lprnlrtldl lhpgaggawq kvryyeivqq efrpqnqqil ikallnpvqt kkikivgvas
      421 dgrrfallnd fahsadtiaf klinygkywv aqlsppqnts lldietrlng vvihpvsnln
      481 drflelvipp gegdkqtlql rvakfqktvl dttihfavlf peksqhialf ndslqiettg
      541 qtvydtllfs arkndsvltl kdslpilsae ydfswypqpf rkgvrivvkt dstplpartl
      601 glyrfvsekg lryvggqsdt akqtvvmrsk glgsivaaad tvppvveilf papnarlkal
      661 kfvkisafds lsgldsdlnf rifiddqwmi pewdperklv latphwklka gqhrllvevq
      721 dragnvskqs lvffikgn
//
LOCUS       WP_457566827             628 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Caldithrix abyssi].
ACCESSION   WP_457566827
VERSION     WP_457566827.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   2  (residues 1 to 628)
  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 10176287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..628
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72819
     Region          54..532
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09604"
                     /db_xref="CDD:341067"
     Site            order(176,178..179,363..367,386,389..390,393,408,412,472)
                     /site_type="active"
                     /db_xref="CDD:341067"
ORIGIN      
        1 mfafllvaft lngiqatasd slyipinlqq ayekgtrayd gspgpeywqn hadyviqvkf
       61 eperrmifgr qkiiyynesp dsldrlvirl yqdlfkkgnp rdwgvnpgdl hegvkidslk
      121 lndrpldltg npsirrygtn miirlqnkia pestvkleie wqlqisrhsn irmgaydsts
      181 fhvaywypqi avyddlsgwd tfnytglqef yndfnnydvr isvpqnfvvw atgrlqnvee
      241 vlqekyqkry qkalesddvi hviteedlek gkitadkewn tfhyvarnvp dfafstsdhy
      301 lwdltsvqva pdrervlvga aykaessdfy kvaelsrksi lffsnempav afpypsltvf
      361 ngrggmefpm mvndgsvanw qgtvhltshe iahtyfpfmm gtnerkyawm degwavmlpf
      421 dfqareapgy dpiekaikry lsmagteldi pmivpsvvyg gdarnayrna synrsgvayy
      481 llerhlgret flkamhaymt rwqskhpmpf dffftfnhat gedlnwffkp wffefgypdl
      541 aiekvaedqq tltvkvikkg nlplpikltv vfqdssqtmi ekamdiwrsg knetvikisk
      601 ekpiieiqlg dkhipdlfdd nnwirmke
//
LOCUS       WP_457566831             418 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Burkholderia vietnamiensis].
ACCESSION   WP_457566831
VERSION     WP_457566831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..418
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44373
     Region          <218..350
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvkpaatpda fapgraqrlv ralvpaavlg alaafglaaa lpavsqlpga vdsgtavlpq
       61 rvlsdtpfpt aqhfvtsela htigerrafa drsaqpglfa slsahrndml gypnlfqyae
      121 pdrthgmrag dieltlsdtl drldvppevr iqlgdlvtgk mamrasaqrg dyyriaydtn
      181 ngtphltave lrvagrrfga iwfhapgaeh gayytldgap leaaaftmpv kwtrissffg
      241 ervhplsqam afhtgvdlaa ptgtpvdaaa dgvvsfvgtd pggyghyviv dhadgystyy
      301 ahlsayargl kvgetvkqgq rigsvgmtga atgphlhfev riandpvdpl vtlasaqtel
      361 sdmqrtafrq eaaqwrfrla sigttpfafa qgdgplwgdf avgpstlrsv fdthygas
//
LOCUS       WP_457566802             188 aa            linear   BCT 27-JAN-2026
DEFINITION  glutamate--tRNA ligase, partial [Caldithrix abyssi].
ACCESSION   WP_457566802
VERSION     WP_457566802.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Francklyn,C., Perona,J.J., Puetz,J. and Hou,Y.M.
  TITLE     Aminoacyl-tRNA synthetases: versatile players in the changing
            theater of translation
  JOURNAL   RNA 8 (11), 1363-1372 (2002)
   PUBMED   12458790
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Woese,C.R., Olsen,G.J., Ibba,M. and Soll,D.
  TITLE     Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary
            process
  JOURNAL   Microbiol Mol Biol Rev 64 (1), 202-236 (2000)
   PUBMED   10704480
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Siatecka,M., Rozek,M., Barciszewski,J. and Mirande,M.
  TITLE     Modular evolution of the Glx-tRNA synthetase family--rooting of the
            evolutionary tree between the bacteria and archaea/eukarya branches
  JOURNAL   Eur J Biochem 256 (1), 80-87 (1998)
   PUBMED   9746349
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Delarue,M. and Moras,D.
  TITLE     The aminoacyl-tRNA synthetase family: modules at work
  JOURNAL   Bioessays 15 (10), 675-687 (1993)
   PUBMED   8274143
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17564554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..>188
                     /product="glutamate--tRNA ligase"
                     /EC_number="6.1.1.17"
                     /GO_function="GO:0000049 - tRNA binding [Evidence IEA]"
                     /GO_function="GO:0004818 - glutamate-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006424 - glutamyl-tRNA aminoacylation
                     [Evidence IEA]"
     Region          5..>188
                     /region_name="GlnS"
                     /note="Glutamyl- or glutaminyl-tRNA synthetase
                     [Translation, ribosomal structure and biogenesis];
                     COG0008"
                     /db_xref="CDD:439779"
ORIGIN      
        1 mgytvrfaps ptgylhvgga rtaifnwlla rqsqgkfllr iedtdlqrst pqsvqqilns
       61 lrwlgldwdd evfyqsknrs rhvevanhll kkgkayrcfc skeeleekrr kfealklnqr
      121 ydgacrrlsp devqerlkrk qpfairfkvp qgqivfddlv hgrmvvdnst lddfiivrsd
      181 gtpvyqla
//
LOCUS       WP_457566864             144 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus lactis].
ACCESSION   WP_457566864
VERSION     WP_457566864.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus lactis
  ORGANISM  Enterococcus lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Enterococcus lactis"
                     /db_xref="taxon:357441"
     Protein         1..144
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17165
     Region          3..70
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 myryirkgkg mtqkevcndf ldrttlsrie kneteprfen acylleridv sldefrylan
       61 ienrdnrtrl iedfysiisn tesaqirkly rrcleftftc sdkkieeill ilrlylsadp
      121 idfdkteckg lvtpiwqrls kiev
//
LOCUS       WP_457566829             305 aa            linear   BCT 27-JAN-2026
DEFINITION  Na+/H+ antiporter NhaA [Burkholderia vietnamiensis].
ACCESSION   WP_457566829
VERSION     WP_457566829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Padan,E., Kozachkov,L., Herz,K. and Rimon,A.
  TITLE     NhaA crystal structure: functional-structural insights
  JOURNAL   J Exp Biol 212 (Pt 11), 1593-1603 (2009)
   PUBMED   19448069
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..305
                     /product="Na+/H+ antiporter NhaA"
                     /GO_function="GO:0015081 - sodium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0015385 - sodium:proton antiporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006885 - regulation of pH [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33213
     Region          19..>269
                     /region_name="Na_H_antiport_1"
                     /note="Na+/H+ antiporter 1; pfam06965"
                     /db_xref="CDD:429217"
ORIGIN      
        1 mpassfgess ahirrrrvah ylrtesgaav llvivtvval vwansplsna yfelwhldvg
       61 fnfgplrlhm dlhhwvndgl mvvfffligl evrqefahgs lrdrsrarla liagvtgvvl
      121 palvyvlivk lagseglhgw gavvgtdtaf mlgtlaivgp rlsgqlrvfl ltltvvddfl
      181 avsiigivys eeirivplli alaslvglwl lgrtrqwrat pyvlivivlw fatvysgiha
      241 slagmaagll ipayatqrhg vvaarqlfrd fwqspsaasa ravdcglsrg ickrldwavr
      301 istra
//
LOCUS       WP_457566887             123 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Escherichia fergusonii].
ACCESSION   WP_457566887
VERSION     WP_457566887.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..123
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13308
     Region          19..>101
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mrrtnhrnlv nvgilsgrip lislvqfiav aehlnfrhaa kalgisqssv sarvkaledn
       61 lgvllferha rgvrltdagr hfmervtagv dqldhavkta etgtgwqcla tagisaegkr
      121 tfr
//
LOCUS       WP_457566902             166 aa            linear   BCT 27-JAN-2026
DEFINITION  fimbrial protein [Enterobacter mori].
ACCESSION   WP_457566902
VERSION     WP_457566902.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..166
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17437
     Region          3..166
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mktlpliall aslsagatdv tlniegniyd ttcevdsssq nmvvdlgqav sgdfkdvgdt
       61 gpwkdfdlkl tncpptlava tisvdgkrda rhpfkfanng taggmalela drldyivlap
      121 qasfsavida sthtadfpma aryyttsmpv tagtfssvvq atftyq
//
LOCUS       WP_457566905             231 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein, partial [Enterobacter mori].
ACCESSION   WP_457566905
VERSION     WP_457566905.1
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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         <1..231
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
     Region          <31..231
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 laehfgvnia depapaaptp pvvtpppaet kislskvslt kekpainltk rdnfgeirin
       61 lnwhrgsgks gfagmfgskg idldlgafve lqdgyksviq algnafgdyr depyvqlkgd
      121 drtgdvsdge wlhingrewk hirevliyaf iyegvpswdk tdgvvtihvp dqppietrlt
      181 egenrrtlca iarlvnenga ikverinqyf kgqnemdraf gwgfrwrags k
//
LOCUS       WP_457567013             292 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Desulfurobacterium sp.].
ACCESSION   WP_457567013
VERSION     WP_457567013.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13493202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..292
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33068
     Region          <16..274
                     /region_name="PRK13914"
                     /note="invasion associated endopeptidase"
                     /db_xref="CDD:237555"
     Region          <156..274
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mvrklliava lcvlpvtara dlyivrrgds lykiarkyht tvetirrlng irgkllrpgq
       61 rlivpgrsrf akpkksvati nlletearel seaserelav ktlselnpqd iysitdtvet
      121 esellsdais tpldvpydnw slsilnlpqy kssllkilat ifkrykntpy vfgynnpsrg
      181 ldcssftmrv yrklgiylpr targqfnvgv pvdrehlkvg dlvffrtyar fpshvgiyig
      241 ngkfvhfsss nhglaissld sryfrkrfig akrvlsekki revvaklkeg lq
//
LOCUS       WP_457567125             388 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Desulfurobacterium sp.].
ACCESSION   WP_457567125
VERSION     WP_457567125.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..388
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=43288
     Region          1..388
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 msvkilegen lealiekaka sygndieily yevetrsgll pfkkkkyyrl ffkeadrked
       61 etkalkeeld tlkallselk eeikkspeks qqevlspyvp padlpshiks avpppsvnin
      121 fheftgdale llrilesknv fpdvareive pacgldletg kldlsvptlk ealekgiaek
      181 ikftgrisae nkpkivafvg ptgvgkttnl fkiasdlvin qqlkvgvvsi dtfkvgaiqq
      241 grmyanilni pfftvsegrk lketlanltd vdvilidtvg rshydywrlg eikailhgse
      301 kemevnlvis cnysneeaie vvnryrsifp vtallltkid etrkpgilln lpvktelsls
      361 ylstgqrvpe diklltpkkv adyllgdl
//
LOCUS       WP_457567298             446 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Desulfurobacterium sp.].
ACCESSION   WP_457567298
VERSION     WP_457567298.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..446
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48017
     Region          36..428
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mkfdrsffql vwqylkgcak vnlklrfdll sishflgrwi pyaftvgiit gsiaafmdvl
       61 iteinrlisv hdalfflypi vtalvvgytl vidpivggpg igyaivhlkt kyflpaklvv
      121 lkfisstlvl sggfiagreg psffigvaig ewlgkaygfs krfknllgli gggaftgall
      181 kaplgssifa melenmydfd yspfvpmiia aitsyltftf frgesafial tqepvwtlds
      241 ipylvimglv isfiiyiytf mfhtgscvsk ffeplkrpii gtvaslpvll vlyfatsdte
      301 ilaapahmgi vsklaqtplp vwidilivag vilvtsltlg fgipgglvlp nlligaavgn
      361 mfghlfpgqi vmfslagmga alaagaktpl aaivmitems hadvvipmta avitsyttsf
      421 gfslylgqei dikplikgaa hrgkdt
//
LOCUS       WP_457567386             256 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Enterobacter mori].
ACCESSION   WP_457567386
VERSION     WP_457567386.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter mori
  ORGANISM  Enterobacter mori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..256
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30025
     Region          9..194
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mdsvkhgtlv siitptfnsv ayiketyrsl ydqeyknwew vitddcstdd tfnvlqelsi
       61 tdtrvrpfkl dknsgaavar nnsidhsqgk yiafidaddy weknklslqi nymeeklidf
      121 cftsyvcesv sgnklykiid ashsanvfty kdmlkkkatl gcstvilnks lvknhrmpli
      181 rtgqdyafwl cllketnavl fnkcltryri mpgslsrnki kkakrqwyiy rklekisffy
      241 afyyfsfyaf raifrk
//
LOCUS       WP_457567538             369 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Desulfurobacterium sp.].
ACCESSION   WP_457567538
VERSION     WP_457567538.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..369
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41064
     Region          7..369
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          194..368
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mkaflgrfst liykellqfv rskgllifai yaftldiyfa atgisltlrn akffvldrdm
       61 tpisreyvyr fhkpyfnfqg yllddkqlgs tlledkaiav veipdhferd fkkgkaelgi
      121 iingaeivas ylfsayaaqi tydfivdhfp rkagigfiep darlyfnqna sskdfmgise
      181 lltvvtlfll ilpssaiire kergniemlv vspvrnytfm lakvvamsvv illctlasii
      241 fmvegilgiv vkgslidfai ftlvfvfaas glsmfiaais enmlqvsqls ililvpilyl
      301 sgswtpieam pkvlqylsyl splryyidga fgilikglpi tailpdfagl ialgsvvffa
      361 gsyflskkv
//
LOCUS       WP_457567699             387 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Desulfurobacterium sp.].
ACCESSION   WP_457567699
VERSION     WP_457567699.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..387
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=43328
     Region          1..387
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 msvkilegen lealiekakt eygndieily yevetrtgll pfrkkkhyrl ffkeagknee
       61 etkalkeele tlkallselk eeikqvpess rqdlvspylp psdipshiks svpvsssvnf
      121 heftgdalel lrllesknvf pdvareivep acgldletgk ldlsvptlre alekgiaeki
      181 kftgrisvkd rprvvafvgp tgvgkttnlf kiasdlvinr qlkvgvvsid tfkvgaiqqg
      241 rmyanilnip fftvsegrkl ketlasltdv dvilidtvgr shydywrlge ikailhgser
      301 dmevnlvisc nysneealev vnryrsifpv tallltkide trkpgillnl pvktelslsy
      361 lstgqrvped iklltprkva dyllgdl
//
LOCUS       WP_457568612             163 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Desulfurobacterium sp.].
ACCESSION   WP_457568612
VERSION     WP_457568612.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     gene            1..163
                     /gene="rimP"
     Protein         1..163
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=18599
     Region          7..158
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mneervsqiv ekvkellmpi leegnfelvd iefvrepigw vlriyadren ggitisdcqw
       61 iserigtild vedlihhpyn levsspgldr plkeqkdfek qvgnvvkikt teplgnqrnf
      121 kgeivstnse svtihdvsrn aeveipfkki ktarldldsl fnr
//
LOCUS       WP_457568733            1052 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction endonuclease subunit R [Enterococcus cecorum].
ACCESSION   WP_457568733
VERSION     WP_457568733.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus cecorum
  ORGANISM  Enterococcus cecorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1052)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1052)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1052)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1052)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Enterococcus cecorum"
                     /db_xref="taxon:44008"
     Protein         1..1052
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120343
     Region          1..1014
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mckfteatye eaiiklfenm gyeyiyapdy dryytcpfle dilkdslvri nrdlpmeaid
       61 dalsklknfd tgsllqknmi fmdylqngit vkffvkgeeq ssivrlidyk nvnnnsfyvv
      121 nqfmfidngn phrpdvilfi nglplvliel kspirdevda gnayrqirny mqdiptlfyy
      181 naicvisdmv tnkagtitsg ldrfmewktk dgnyedttya sfetfyegif qkerlldifk
      241 nfilfsgvsn srfkvlagyh qyfavrkaie rakiatktdg kggvfwhtqg sgkslsmvfy
      301 ahllqealds ptivvmtdri dlddqlyaqf sqcaeflrqt pvqaeskehl kslldgrsan
      361 giifttmfkf ergekplser rnivvmadea hrgqygfdek ivmseneyge keahtvigna
      421 riihdalpna tfigftgtpi sskdrntrev fgeyidvydm tqavedgatr pvyyesrvvh
      481 lkldehtlgl idstydvleq qsdketieks kkmlgqmesv lgadstiesl cddiiehyek
      541 hranlltgka mivaysrtia mkiyrcilek rptwtdkvgv vmtggnndpa dwkkiigtka
      601 ykeelarkfk dnddpmkiai vvdmwltgfd vpslatmyvy kpmrgynlmq aiarvnrvfk
      661 dkegglivdy vgiasalkna mkeytkrdqs tygdmniakm aypkfqeklq vckdllhgfd
      721 fsgfiggtpl tmaklitggv nyildasape rkelflkesm llkqssslcs smtteqerhe
      781 saymealrst ivkityggsd gktlsltein aqinellkaa vqsegvislf dssksggekf
      841 slfdpavlee isqmkeknia veilrklmae qvslykrtnv vqskkfseki aqlmnsyyng
      901 litneevike lletaeeian lyksgqelgl sqeelafyda ltkpehikdf ykndelialt
      961 reltemlrkn rtidwqkket araqmrkmvk rllkkykypp edyafaistv isqcelwtdy
     1021 veprkeekiy kyvsevelsk vaeekvpyne tk
//
LOCUS       WP_457568759             494 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor domain-containing diguanylate cyclase [Desulfurobacterium
            sp.].
ACCESSION   WP_457568759
VERSION     WP_457568759.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Heyl,A., Wulfetange,K., Pils,B., Nielsen,N., Romanov,G.A. and
            Schmulling,T.
  TITLE     Evolutionary proteomics identifies amino acids essential for
            ligand-binding of the cytokinin receptor CHASE domain
  JOURNAL   BMC Evol Biol 7, 62 (2007)
   PUBMED   17439640
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   6  (residues 1 to 494)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   8  (residues 1 to 494)
  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   9  (residues 1 to 494)
  AUTHORS   Mougel,C. and Zhulin,I.B.
  TITLE     CHASE: an extracellular sensing domain common to transmembrane
            receptors from prokaryotes, lower eukaryotes and plants
  JOURNAL   Trends Biochem Sci 26 (10), 582-584 (2001)
   PUBMED   11590001
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The CHASE domain: a predicted ligand-binding module in plant
            cytokinin receptors and other eukaryotic and bacterial receptors
  JOURNAL   Trends Biochem Sci 26 (10), 579-582 (2001)
   PUBMED   11590000
REFERENCE   11 (residues 1 to 494)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   12 (residues 1 to 494)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
REFERENCE   13 (residues 1 to 494)
  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 20324347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..494
                     /product="sensor domain-containing diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56646
     Region          65..>435
                     /region_name="CHASE4"
                     /note="Extracellular (periplasmic) sensor domain CHASE
                     (specificity unknown) [Signal transduction mechanisms];
                     COG3322"
                     /db_xref="CDD:442551"
     Region          <318..492
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mkyknikrsf igktlfmilv lvalsallsg vsdffvikkm eseikkkesc rikrafpall
       61 hlcdekignm lnsfgmwddm vqnvelknvs wikemfeddd mvtsqfdsyg vydfkeypvy
      121 vknrifskee vlkishfvre kfkkgqqgkp viffhnykdn iyhvgvlplc wndgsvasyg
      181 fiyfahevnn gtlkmysqil strvkavpgv kvlktsdliy sfpmkdidnk ivgmfsfyed
      241 tliinvfknm nrlfilimvi iliiyigafs fvansindam kktfgsitss lkrlsegdfn
      301 aledldefcq rkdelgslar niqkiarqls vnlstdpltg iynrlyfskk feeeierakr
      361 tgrplsfvif dlddfkkind tyghvagdlv lknfaksvss tvrsldtfar iggeefglil
      421 petdlktavq iverirkrlk dvyvpeidkk vkitfsagva gyrngdnmds lfhradvaly
      481 rakqkgknri eved
//
LOCUS       WP_457568935             369 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Desulfurobacterium sp.].
ACCESSION   WP_457568935
VERSION     WP_457568935.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..369
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41239
     Region          7..>298
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          194..368
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mkdflgrfst liykellqfv rskgllifai yaftldiyfa atgisltlrn akffvqdydm
       61 tpisreyvyk fhkpyfnfqg yvlndkqled klledkaiav ikipdnferd fkkgkaeigm
      121 iingaeivas ylfsayaaqi tynfilehfp fksgvgliep darlyfnqna sskdfmgise
      181 lltvvtlfll ilpssaiire kergniemlv vspvhnytfm lakvvamsvv illctmfsii
      241 fmvkgvlgit vkgnllefai ftlvfvfaas glsmfiaais enmlqvsqls vlvlvpilyl
      301 sgswtpieam pkvlqylsyl splkyyidga fgilikglsl sailpdlggl lilgsivffa
      361 gsyflskkv
//
LOCUS       WP_457569642             446 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Desulfurobacterium sp.].
ACCESSION   WP_457569642
VERSION     WP_457569642.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..446
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48231
     Region          36..428
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mkfdktflkl vwqylkgcak vnlklrfdll sishflgrwi pyaftvgiit gsiaafmdvl
       61 iteinrlisi hdalfflypi vtalvvgytl vidpivggpg igyaivhlkt kyflpvklvl
      121 lkfisstlvl sggfiagreg psffigvaig ewlgkaygfs krfknllgli gggaftgall
      181 kaplgssifa melenmydfd yspfvpmiia aitsyltftf frgesafial tqepvwtlds
      241 ipylvimgla isfiiylytf mfhtgscvsk ffepmkrpvi gtiaslpili alyfathdte
      301 ilaapahmgi vsklaqmplp vwidilivig vilvtsltlg fgipgglvlp nlligaavgn
      361 mfghlfpdqi vmfslagmga alaagaktpl aaivmitems hadvvipmta avitsyttsf
      421 gfslylgqei dikplikgvt krgkdt
//
LOCUS       WP_457569750             656 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Desulfurobacterium sp.].
ACCESSION   WP_457569750
VERSION     WP_457569750.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 656)
  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 656)
  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 18640031
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..656
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=77184
     Region          34..327
                     /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          39..67
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(40,43..44,47..48,50,78,81..82,85..86,88..89,120,
                     123..124,127..128,131)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          76..106
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          119..145
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(194,197..198,201..202,204,232,235..236,239..240,
                     242..243,269,272..273,276..277,280)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          194..221
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..314
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          230..260
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          265..291
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mivkvitvll slllfcngfa asnnatvknk gdelfvykpk vwlkrgmyqy kigsyntale
       61 yflkilakdk nkddyykkal fmlaktymki grkigdkqyl wqaldllqly fntvknvgwd
      121 fyytkahiye nlgfydksld iyrvaflkak nerqqiktvi gilrsavylk rpdivdeyyi
      181 llstsnlske dkkeleflkg lilfskgkyk eafkyffkty rqnesylien peyyylvaed
      241 iyrkgdyrla eqlfkriisl trdksvirka mlrlgdtelk kgdkklavat yynlvttypd
      301 speatiaklk lialmekdpv lkyrlqqtni kafkqplrfv letlihsrdt ylgafalanf
      361 gayvlqtnsd nlfkqlewei slvfprqlky eqkefivrew kpyllklspk rlcelyktnp
      421 dffkvifdkd tlikiaealg kcnereerlk liryiadrwk ddndllmlae altdskdfde
      481 slkilkkvkh knckyykiyi knlvflgrpv keylpilrki enkcpsddie ikayeilasi
      541 eqknpqralw iiekskdkia qfydkdpvlk laiyktisyl lainnyegcl kvidivepks
      601 gncflasakl islsrldkid laeailpkvk mckdtmskia qiiyedqiiy rklkne
//
LOCUS       WP_457569754             388 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Desulfurobacterium sp.].
ACCESSION   WP_457569754
VERSION     WP_457569754.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     Protein         1..388
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=43467
     Region          1..388
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 msvkilegdn lealiekaka aygndieily yevetktgwl pfkkkkyyrl ffkeadrked
       61 etkalkeeld tlksllselr eeikqvpens qqemlspyvp ppdlpshikp avssspnnvn
      121 fheftgdale llrilesknv ypdvareive pacgldletg kldlsvptlr ealekgiaek
      181 vkftgrisae dkpkivafvg ptgvgkttnl fkiasdlvin qqlkvgvvsi dtfkvgaiqq
      241 grmyanilni pfftvsegkk lketlanltd vdvilidtvg rshydywrlg eikailhgse
      301 remevnlvis cnysneeaie vvnryrsifp vtallltkid etrkpgilln lpvktelsls
      361 ylstgqrvpe diklltprkv adyllgdl
//
LOCUS       WP_457570344             163 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Desulfurobacterium sp.].
ACCESSION   WP_457570344
VERSION     WP_457570344.1
KEYWORDS    RefSeq.
SOURCE      Desulfurobacterium sp.
  ORGANISM  Desulfurobacterium sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Desulfurobacterium.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Desulfurobacterium sp."
                     /db_xref="taxon:2004706"
     gene            1..163
                     /gene="rimP"
     Protein         1..163
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=18535
     Region          7..158
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mneervsqli ekvkelllpi leegnfelvd iefvrepigw vlriyadren ggitisdcqw
       61 iserigtild vedlihhpyn levsspgldr plknqrdfek qvgnvvkikt tepldnqrnf
      121 kgeilsange gvtihdvsrn aeveipfeki ktakldldsl fnk
//
LOCUS       WP_457570517             158 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Desulfovulcanus sp.].
ACCESSION   WP_457570517
VERSION     WP_457570517.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     gene            1..158
                     /gene="rimP"
     Protein         1..158
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17860
     Region          6..156
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 melqwikkki sqlvkaqcql fglslwgief apgagkkrgl lriyvdapng vnvdqcakfs
       61 relsvildve diipasynle isspgldrif fspeqltdyi gqkikvklin pidnrknfsg
      121 tlqevkdnvf tiisdsgekw qfdfadtqkv qlkfefnd
//
LOCUS       WP_457570674             574 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Desulfovulcanus sp.].
ACCESSION   WP_457570674
VERSION     WP_457570674.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 574)
  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 574)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..574
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=65021
     Region          61..571
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          <344..571
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mmikmfwekl kpsfwdaagq egtgktlfny rrvwlivvvs iggvailpll imtfmnlsly
       61 ekamraeiny plarlisntr rslsyfleer ksaltfivqd ndftelrnqe rlaeiflnlk
      121 gafggfvdlg iidskgiqrs yigpyelkgr nykeqnwfke vigrgiyisd vfegyrhlph
      181 fviavkhfla dgdffvlrat idterfselv spidlradsd afivthdgvl qtksryygdm
      241 lskidislpa csekieicei qnkngqrfim gytyipnspf ilvllqkpvv llqswwnlkr
      301 evlvvlicsi iiilvvilgv atmlisriyt admsrlatlh naehankmas igrlaagvah
      361 einnplaiin eragliedlf tftdqyaqde klmslvdsii aqvdrcrsit qrllgfarhi
      421 dvqreeidlp kvvqevlvfl ekeakyrgiq iklqaekdlp tiicdrgqlq qiflniinna
      481 faavdeggyi qiemnklden rvrifiaddg cgippenlkr ifepffstkr kkggtglgls
      541 ityglvkklg geievesqvg kgskftiilp vgrd
//
LOCUS       WP_457571046             349 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Desulfovulcanus sp.].
ACCESSION   WP_457571046
VERSION     WP_457571046.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..349
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=39606
     Region          1..316
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 mqiktfrgkt ssevmarikk evgpdavils senitengqk wyevvvaler evegdikhqi
       61 pdksnfdldf rlewekfkks iydlvkpqln kenitprqrq vldflekqga gtdlildlys
      121 kmrqssntpv lkilgqaiki tpwtdkftsr rihafagpsg sgqtttllrl alemkrsskk
      181 ilvlnankdq aggrlylkhf aelsglvyle gdtldqnsle kfnsydyifi dlpgispgkt
      241 lsacltelkv ardvaihlvf spsysnehfd lfvckyshpq aqsliwtkld egcifgpiin
      301 lawkmdlpis ylsygpglkn ystsatqdnv wrlifkkelp neckvlnyk
//
LOCUS       WP_457571096             216 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease III domain-containing protein [Desulfovulcanus sp.].
ACCESSION   WP_457571096
VERSION     WP_457571096.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..216
                     /product="endonuclease III domain-containing protein"
                     /calculated_mol_wt=24994
     Region          1..216
                     /region_name="HP0602"
                     /note="3-Methyladenine DNA glycosylase, HhH-GPD/Endo3
                     superfamily [Replication, recombination and repair];
                     COG2231"
                     /db_xref="CDD:441832"
ORIGIN      
        1 mdrqtlllni fstlssalgp shwwpgetpf evaigailtq ntnwqnveka ifnlkqekll
       61 kpeklyslse qqlaqlirpa gyyrikakrl knflnflyye cdlnfdvlkk qelqelrpkl
      121 lqvsgigpet adsillyald katfvvdayt rrmfnrhglv vedityeelr sffmdvlppd
      181 iqlynefhal ivrtakkwcl kkkphcsdcp lahfla
//
LOCUS       WP_457571257             665 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Desulfovulcanus sp.].
ACCESSION   WP_457571257
VERSION     WP_457571257.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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 18640031
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..665
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=76614
     Region          <439..633
                     /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          527..555
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(528,531..532,535..536,538,567,570..571,574..575,
                     577..578,605,608..609,612..613,616)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          539..650
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          565..595
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          604..632
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtkkiylili iiflpvvcwa akeesvpydq wllnfkayda yvrylqtknp tpetiisqak
       61 llltlnrshs tldilkqfet lpgfdgqrlw lmgkayrmlg eydqaisnfv aaaeyfsnae
      121 lkelfsqeke ldrlwqdvct kwfwqnlfvq kkadqaelln savqvarkvw pdqdlwtrfa
      181 ntlsatdktl tyyfdehiph llakalsaqs iknwslsssh lnkittlkik nfwtrlekfi
      241 hepagslvei dlqavkssvf fevygsqlkk iianywfvpn ldlpswknfl dqlknlspeq
      301 glrlvenels ssllspkikp alkillfiyq iqtdrfdqal ktwailenyk diplslslsa
      361 tliaknyhpl ipfpehlypi skdllqaagl gfsstvtapf wletgeknek dllsaypldr
      421 llsylywknq leaqksyvaa khlaflfpet pagqsgflsl araayknghk alawkylqni
      481 reefldstkq ldlieakagi lmdlghtqes lktytlllnk apqrlsaekr lklallaqqs
      541 nkwelaenil tnlwqerknl spalqaeilf wlgegsqyqg ktdqaldyyl klawqfpeen
      601 iwaitamyra gqiyeqkgml eaaknlyqtv lkkaerksqk eaakqrltsi eakekrqive
      661 sgvmf
//
LOCUS       WP_457571573             170 aa            linear   BCT 27-JAN-2026
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Desulfovulcanus sp.].
ACCESSION   WP_457571573
VERSION     WP_457571573.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
REFERENCE   1  (residues 1 to 170)
  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 170)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..170
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19429
     Region          <34..>57
                     /region_name="PRK10819"
                     /note="transport protein TonB; Provisional"
                     /db_xref="CDD:236768"
     Region          <47..131
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mkkflfitll atsllafgca kkqvscttep ekpaqveeqi tqpepqpvve pepepapkvv
       61 qptpmeiyet ayaslptehk vvkgeclwwi aeykqiyndp fmwpliykan rdqiknpdli
      121 ypnqvfaipr dftlyelkks rrqagaprpy lppktanlpa klraelgwnf
//
LOCUS       WP_457571593             214 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Desulfovulcanus sp.].
ACCESSION   WP_457571593
VERSION     WP_457571593.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
REFERENCE   1  (residues 1 to 214)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  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 19959002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..214
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24430
     Region          <52..203
                     /region_name="ftsN"
                     /note="cell division protein FtsN; TIGR02223"
                     /db_xref="CDD:274041"
     Region          <138..211
                     /region_name="FtsN"
                     /note="Cell division protein FtsN [Cell cycle control,
                     cell division, chromosome partitioning]; COG3087"
                     /db_xref="CDD:442321"
ORIGIN      
        1 makkkadkrk kkvenkfkln ltlsgliylg ifiilgmvwa filgvyigrg ykpedvvpei
       61 arimpetksw snqsppasak qeilrpeqle fyeklkdqpn pklkkdtptr aetkgksrar
      121 skntktnsss akqnifsyty qvaafktlnq ankmqkklvt qgvmssitka fagdrpwfrv
      181 fvhfqgtpkq vekfknklkr igikqpilkr kkpl
//
LOCUS       WP_457572014              66 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Desulfovulcanus sp.].
ACCESSION   WP_457572014
VERSION     WP_457572014.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 66)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10596226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..66
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=7103
     Region          7..61
                     /region_name="Fer4_13"
                     /note="4Fe-4S single cluster domain of Ferredoxin I;
                     pfam13370"
                     /db_xref="CDD:433153"
ORIGIN      
        1 mdreifidql qcsgceacve ispevfaide ltgkayildp lagteeqiee aivtcpqdci
       61 slikan
//
LOCUS       WP_457572177             213 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Desulfovulcanus sp.].
ACCESSION   WP_457572177
VERSION     WP_457572177.1
KEYWORDS    RefSeq.
SOURCE      Desulfovulcanus sp.
  ORGANISM  Desulfovulcanus sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonauticaceae;
            Desulfovulcanus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12805053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Desulfovulcanus sp."
                     /db_xref="taxon:2956792"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /calculated_mol_wt=24054
     Region          3..>79
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          4..205
                     /region_name="PRK11552"
                     /note="putative DNA-binding transcriptional regulator;
                     Provisional"
                     /db_xref="CDD:236928"
ORIGIN      
        1 mspenkreki lkvaeklfge kgfkgvsire ittkaqanvs avnyyfgnkk glylavfeel
       61 wikraqaqrs ylqerlaaye sldinifvke vilsfltgpi skdikkyhha liqkelneps
      121 ealdlvlqka ifpmldllvn tlesiypgkl sseqkmiyai tliaisihfn lvgenllkfi
      181 pffskenqqe lvaqaisdll tngfkglclp nen
//
LOCUS       WP_457572649              54 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus cecorum].
ACCESSION   WP_457572649
VERSION     WP_457572649.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus cecorum
  ORGANISM  Enterococcus cecorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 54)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 54)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 54)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     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 54)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..54
                     /organism="Enterococcus cecorum"
                     /db_xref="taxon:44008"
     Protein         1..54
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6071
     Region          1..>42
                     /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 myqderkldf kplgiaikka reakgwtqey laqlvdltpr simgsvarfp issf
//
LOCUS       WP_457572651             230 aa            linear   BCT 27-JAN-2026
DEFINITION  bestrophin family protein [Elizabethkingia anophelis].
ACCESSION   WP_457572651
VERSION     WP_457572651.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..230
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26620
     Region          <1..230
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mfyrhfawlt alrfqlrepr swenmnqrsn sayrksryei pelnstleee lkqylsgeel
       61 eyilskknka tqltalqsee fgelkkagdi ndfqwtllqq siikftddqg kaeriknfpy
      121 prnfasiaty llfifvilap fglvkemdkl gegtflqayt vwfnipfsai iawafhtldt
      181 vgessvnpfe gsandipitq isrtieidmr dmldekdlpq pitpknnivl
//
LOCUS       WP_457572765            1052 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction endonuclease subunit R [Enterococcus cecorum].
ACCESSION   WP_457572765
VERSION     WP_457572765.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus cecorum
  ORGANISM  Enterococcus cecorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1052)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1052)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1052)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1052)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Enterococcus cecorum"
                     /db_xref="taxon:44008"
     Protein         1..1052
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120349
     Region          1..1014
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mckfteatye eaiiklfenm gyeyiyapdy drdytcpfle gvlkdslvri nrdlpmeaid
       61 dalsklknfd tgsllqknmi fmdylqngit vkffvkgeeq ssivrlidyq nvnnnsfyvv
      121 nqfmfidngn phrpdvilfi nglplvliel kspirdevda gnayrqirny mqdiptlfyy
      181 naicvisdmv tnkagtitsg ldrfmewktk dgnyedttya sfetfyegif qkerlldifk
      241 nfilfsgvsn srfkvlagyh qyfavrkaie rakiatktdg kggvfwhtqg sgkslsmvfy
      301 ahllqealds ptivvmtdri dlddqlyaqf sqcaeflrqm pvqaeskehl kslldgrsan
      361 giifttmfkf ergekplser rnivvmadea hrgqygfdek ivmseneyge keahtvigna
      421 riihdalpna tfigftgtpi sskdrntrev fgeyidvydm tqavedgatr pvyyesrvvh
      481 lkldehtlgl idstydvleq qsdketieks kkmlgqmesv lgadstiesl cddiiehyek
      541 hranlltgka mivaysrtia mkiyrcilek rptwtdkvgv vmtggnndpe dwkkiigtka
      601 hkeelarkfk dnddpmkiai vvdmwltgfd vpslatmyvy kpmrgynlmq aiarvnrvfk
      661 dkegglivdy vgiasalkna mkeytkrdqs tygdmniakm aypkfqeklq vckdllhgfd
      721 fsgfiggtpl tmaklitggv nyildastpe rkelflkesm llkqshslcs smtteqerhe
      781 aaymealrst ivkityggsd gktlsltein aqinellkaa vqsegvislf dssksggekf
      841 slfdpavlee isqmkeknia veilrklmae qvslykrtnv vqskkfseki aqlmnsyyng
      901 litneevike lletaeeian lyksgqelgl sqeelafyda ltkpehikdf ykndelialt
      961 reltemlrkn rtidwqkket araqmrkmvk rllkkykypp edyafaistv isqcelwtdy
     1021 veprkeekiy kyvsevelsk vaeekvpyne tk
//
LOCUS       WP_457573197             180 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Desulfolithobacter sp.].
ACCESSION   WP_457573197
VERSION     WP_457573197.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1903233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..180
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=20210
     Region          <35..>148
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mqqkikrkkl nltvkkelqk wlliritgiv llcslvaali lyfyarseit ssffdahlki
       61 rrvsdlllpv lltgsavsmv aglvlamflp qkiagpvyri ekdleevqkg eltkvihlrk
      121 gdllmdlade vnkatasvrq lvqeikdnyr saekavragd daqvemalhr leeslsrlkt
//
LOCUS       WP_457573218              63 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Desulfolithobacter sp.].
ACCESSION   WP_457573218
VERSION     WP_457573218.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 63)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 63)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10596226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..63
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=7159
     Region          11..61
                     /region_name="Fer4_13"
                     /note="4Fe-4S single cluster domain of Ferredoxin I;
                     pfam13370"
                     /db_xref="CDD:433153"
ORIGIN      
        1 maeilidtyf csncmtcvel cpevfyfned tekieltsin peitddvrqa vaycpekcie
       61 ikn
//
LOCUS       WP_457573319             156 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Enterococcus cecorum].
ACCESSION   WP_457573319
VERSION     WP_457573319.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus cecorum
  ORGANISM  Enterococcus cecorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Enterococcus cecorum"
                     /db_xref="taxon:44008"
     Protein         1..156
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17065
     Region          38..143
                     /region_name="cupin_HNL-like"
                     /note="Granulicella tundricola hydroxynitrile lyase
                     (GtHNL) and related proteins, cupin domain; cd02233"
                     /db_xref="CDD:380361"
     Site            order(47..48,79,81,102,104,106..107,126,128,130)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380361"
ORIGIN      
        1 makevwseqa aseeakaqhq asmifpigep ndayaqyftg qsylasvtdq qipvhnitfe
       61 pgcrnnwhih haksgggqil icvggigvyq eegkevvvmh pgdcvnipag vkhwhgatke
      121 hwfshlamav pgedtsnewl ekvseedyla aqplse
//
LOCUS       WP_457573478             589 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Desulfolithobacter sp.].
ACCESSION   WP_457573478
VERSION     WP_457573478.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 589)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 589)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..589
                     /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=63045
     Region          7..584
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,409,412..413)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mslqlmtylv vgatfalyif iaikarastt gefyvagkgv hpvlngmatg adwmsaasfi
       61 smagliafkg fdasvylmgw tggycllaml lapylrkygk ftvpefigdr yysntariva
      121 viclitaslt yvigqmkgig vafsrflevp fatgllvgma ivfiyavlgg mkgitytqia
      181 qycvlifayt vpaifislql tgnplpqigl gstmadgsgv ylldkldqvl vdlgfkayti
      241 qkgttinmfl ltlslmigta glphvitrff tvprvrdars sagwalvfia ilyttapavg
      301 amarlnlmnt iqigevgspd gnlkisdvpa wfvnwektgl lkhedknndg riqyyndknk
      361 efaakaeawg wkgnemtkvd rdimvlanpe ianlpnwvia lvaaggiaaa lstaagllla
      421 isssvshdll kgvfvpdmte knellasris magailvagy lglnppgfaa qvvalafgla
      481 assifpaimm gifskrvnnt gavlgmlsgl gvtlvyifwf kgwffikgta mlpntpdnwl
      541 fgispeafga vgalinfiva lvvsnmtkep pehiqalied irvpgsfsk
//
LOCUS       WP_457573503              78 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Enterococcus
            cecorum].
ACCESSION   WP_457573503
VERSION     WP_457573503.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus cecorum
  ORGANISM  Enterococcus cecorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Enterococcus cecorum"
                     /db_xref="taxon:44008"
     Protein         1..78
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=8921
     Region          <2..78
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 msrnefnqyt gfclvcpits tirpyptyvd ikspknitgq ivthqirsid yqhrnlqvve
       61 tcdtltwtda lsiiqnfi
//
LOCUS       WP_457573561             261 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Desulfolithobacter sp.].
ACCESSION   WP_457573561
VERSION     WP_457573561.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..261
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27471
     Region          1..254
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 mltiaetpfs srlfvgtgkf asselmarai easgaqmvtv alrrvdlnnp qddimthldr
       61 etihflpnts garnaeeair larlaraasg tnwlklevtp dprtllpdpv dtlkateqlv
      121 regfivlpym nadpilalrl qdagaaavmp lgapigtnlg vqtalqveii ieqarvpvvv
      181 dagigapsha aqamemgada vlvntaiava gdpvrmaraf kaaveagrea yeaglgrpsr
      241 qasasspqeg mltenldflq g
//
LOCUS       WP_457573966             491 aa            linear   BCT 27-JAN-2026
DEFINITION  ketol-acid reductoisomerase [Desulfolithobacter sp.].
ACCESSION   WP_457573966
VERSION     WP_457573966.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1924580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..491
                     /product="ketol-acid reductoisomerase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0004455 - ketol-acid reductoisomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53949
     Region          43..360
                     /region_name="ilvC"
                     /note="ketol-acid reductoisomerase; TIGR00465"
                     /db_xref="CDD:273093"
     Region          378..>449
                     /region_name="IlvC"
                     /note="Acetohydroxy acid isomeroreductase, catalytic
                     domain; pfam01450"
                     /db_xref="CDD:460215"
ORIGIN      
        1 metmftsnvf etevikladt qetivrggrd kfpllpkafe gikqigvigw gsqgpaqaqn
       61 lrdslegtdi rvkvglregs ssmasareag fteedgtlge mwevigesdm villisdaaq
      121 vehykrifet mkkgatlgls hgfllghles vgetfpdkmn vigvcpkgmg psvrrlyvqg
      181 kevngaginc sfaveqdidg ratdqalgwa igvgapyvfk ttlgheyrsd ifgergillg
      241 avhgiseamy rrfvmekgmd ekeafisvve nitgplsrti shdgilavyn nlddegkkif
      301 ermysaayhp afdilmeiyd evssgneirs vvmagkrfdr ypmgkidgtr mwkvgeevra
      361 srsgeppvnp etaglycavm maqidlliek ghclsevcne svieavdsln pymhfkgvay
      421 mvdncsttar lgsrkwaprf dynimqqafv aydqgapade nlvesfkkhl vhdvlatvat
      481 mrpsvdislt e
//
LOCUS       WP_457574038             119 aa            linear   BCT 27-JAN-2026
DEFINITION  EF-hand domain-containing protein [Desulfolithobacter sp.].
ACCESSION   WP_457574038
VERSION     WP_457574038.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000101
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..119
                     /product="EF-hand domain-containing protein"
                     /calculated_mol_wt=12593
     Region          <37..105
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mkvtrsliaa affsilalga gveaqatdls rpgplsfsdy dldsngvite qelntvreqr
       61 qaalkasgrr gigianapsf adldsngdgq itpeelrasr kamwekrgrg rgmgrgmgr
//
LOCUS       WP_457574039             532 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Desulfolithobacter sp.].
ACCESSION   WP_457574039
VERSION     WP_457574039.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 532)
  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 532)
  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 532)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19835834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..532
                     /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=60091
     Region          38..525
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          <299..527
                     /region_name="NtrY"
                     /note="Signal transduction histidine kinase NtrY involved
                     in nitrogen fixation and metabolism regulation [Signal
                     transduction mechanisms]; COG5000"
                     /db_xref="CDD:444024"
ORIGIN      
        1 msllhnspkr wrkrplpawl vyflvfglli tviqsvyfwq mnrvranlqh nateratmia
       61 kiieenlhls saahqtidti liafladnir fikyletiep lhsdelsala memglrgiti
      121 lrpdgqavsg peqwsadgls cspatdgqql kyiessrtay lvqpvtdqen lscvlvgwda
      181 gkildlrkkt srqalidsls alpginyirl stgrsapdld etvvllrkgd qvtaetriat
      241 gdgilvigld arrfvrrqes mrrqfimfgs lmlslglffg wilyryqqdn lrrtklfere
      301 lareredaal grttgtiahe irnplnainm glqrlslesd nltreqeeli ramreavqrt
      361 stivtelqrf arplhprprk idpvgmirri lslytsdcea cgievstelq tteefrgdrd
      421 llaelfdnli kngleaqveg grivirlkqr dnilelrvtn gpctlgsddl erflepyftt
      481 ktrgtglglp lcrriaeahg gsleihyenn sqtltvlvri pdqpatetkd sa
//
LOCUS       WP_457574081             153 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Desulfolithobacter sp.].
ACCESSION   WP_457574081
VERSION     WP_457574081.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     gene            1..153
                     /gene="rimP"
     Protein         1..153
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17205
     Region          6..151
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mesennpiiq dieayatpll rdmglelvev qyrreghgwv vrlfidregg vtiddcasvs
       61 rqlsawldve dlishaynle vsspglerpl kkredfirfa grkarvklqe pldgrrvftg
      121 iidrveedgv vllldegpvt lafdamarar lsl
//
LOCUS       WP_457574526             960 aa            linear   BCT 27-JAN-2026
DEFINITION  hybrid sensor histidine kinase/response regulator
            [Desulfolithobacter sp.].
ACCESSION   WP_457574526
VERSION     WP_457574526.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 960)
  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 960)
  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 960)
  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 960)
  AUTHORS   Mougel,C. and Zhulin,I.B.
  TITLE     CHASE: an extracellular sensing domain common to transmembrane
            receptors from prokaryotes, lower eukaryotes and plants
  JOURNAL   Trends Biochem Sci 26 (10), 582-584 (2001)
   PUBMED   11590001
REFERENCE   5  (residues 1 to 960)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The CHASE domain: a predicted ligand-binding module in plant
            cytokinin receptors and other eukaryotic and bacterial receptors
  JOURNAL   Trends Biochem Sci 26 (10), 579-582 (2001)
   PUBMED   11590000
REFERENCE   6  (residues 1 to 960)
  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   7  (residues 1 to 960)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   8  (residues 1 to 960)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20127652
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..960
                     /product="hybrid sensor histidine kinase/response
                     regulator"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=107518
     Region          3..>650
                     /region_name="CHASE"
                     /note="Extracellular (periplasmic) sensor domain CHASE
                     (specificity unknown) [Signal transduction mechanisms];
                     COG3452"
                     /db_xref="CDD:442675"
     Region          452..815
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          825..949
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkkylsvtrv llglltiacl sglfylpyrs vrtetieayn keqfilasqa areieaffnt
       61 ctsalyylas qpsiirldni grrlmedfht ihsseisavt ridatgriiy tapfnkkaig
      121 advssqahnk kimethkpvv sdvfmtvqgy pavayvypvf dgttyqgtis flipfeelar
      181 qyvaaieqgk ksrailisrt giglycplrn fdenivqpal slkerlaesp smlrmieamm
      241 agktgravfk ipksmhspna gatmhavyrp irlpdnnyws iavatpehlv lqtmtdfrnk
      301 wllattiaic avlvlsffls wslatsaeeh rrltveaqlh rllehlpigv vlwdqagqii
      361 yanrstlkll eennpeallg rrmidfvtpe freqvrtrhh qllqqktvps ttykiittkn
      421 nkrtveietv pfyfnerpcf isliqditdr faaeeirkrl vtaieqtres ilitnrdgii
      481 eyinpaftsi tgytreeilg kkpsilrsgk hdqafyrsmw qtitsgevwq gkivnrkkdg
      541 slfvematis pvrdkedkit hfvavkrdit heveleaqlh qaqkmeaigt laggiahdfn
      601 nilgaiigft dmalllcdpd spvyenlehi rqggqratdl vqqiltfsrr gatakhpvsv
      661 aplikeslkl lraslpatir inkmikapda kvlaspvqiq qiimnlctna fhsmgedggq
      721 ldiiletitl eenettnwvr lvirdtgcgi ekeilnrifd pffttkepgq gtgmglsvvh
      781 givhdlggti kvestpgngs vftvllpatg qgpepdlmet eeplprgneh ilivdderdi
      841 cttyrmmlgh lgyqvtdlcn peealerlrk dpdafdlvit dqtmpemtgm mllheirain
      901 pdlpvilctg yseqvdepra reagargllm kpidlqamar tvrrvldeag hhssgsdtls
//
LOCUS       WP_457574739             582 aa            linear   BCT 27-JAN-2026
DEFINITION  ARMT1-like domain-containing protein [Desulfolithobacter sp.].
ACCESSION   WP_457574739
VERSION     WP_457574739.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Huang,L., Khusnutdinova,A., Nocek,B., Brown,G., Xu,X., Cui,H.,
            Petit,P., Flick,R., Zallot,R., Balmant,K., Ziemak,M.J.,
            Shanklin,J., de Crecy-Lagard,V., Fiehn,O., Gregory,J.F. 3rd,
            Joachimiak,A., Savchenko,A., Yakunin,A.F. and Hanson,A.D.
  TITLE     A family of metal-dependent phosphatases implicated in metabolite
            damage-control
  JOURNAL   Nat Chem Biol 12 (8), 621-627 (2016)
   PUBMED   27322068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 68603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..582
                     /product="ARMT1-like domain-containing protein"
                     /calculated_mol_wt=67380
     Region          <249..362
                     /region_name="ARMT1-like_dom"
                     /note="Damage-control phosphatase ARMT1-like domain;
                     cl15397"
                     /db_xref="CDD:472798"
ORIGIN      
        1 mreplkitsg sdpdrdawlt nfytenhmay eafpdmvasp eqlnfivhmd geqyyypcsd
       61 elfsaiiekr adtlltpayi riwsrleklv revisdpyrr qyllslltik yqhdtssmvl
      121 lpsrlekrll giftnisdis rplaarreme nkrvarflas rdfleafngr eglritektt
      181 lddidlqvhl lrlqrlllls tvkeiwqdeh ppsmdrlrrv mntsietegw hwfcerlarv
      241 lsgqhkpyll wlggrageiv fdlaiirilm klgikvilav kqafyyeqvs fadvledpvl
      301 ekamagaavi gdpriskkel lgmldkdnrl lvisdgtgeq fnplltsvtf arafkesdlv
      361 vsrcpesrec innhfqftrd lvsilredtg klaihlkphh pavirfsead lrakaqhliy
      421 markekekgr kimfysaivg sipgqletak kilnvfvehl rstltdvvii npgehfeegm
      481 daddimymwe ifqrsgvidi wrfqtysdie kafelmgekv ppewsgkdat ystgctkemq
      541 ialemqqkyp emqligppwe kfkrrqeygi gklydrvlte sr
//
LOCUS       WP_457574880             214 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease III domain-containing protein [Desulfolithobacter
            sp.].
ACCESSION   WP_457574880
VERSION     WP_457574880.1
KEYWORDS    RefSeq.
SOURCE      Desulfolithobacter sp.
  ORGANISM  Desulfolithobacter sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfolithobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Desulfolithobacter sp."
                     /db_xref="taxon:3003268"
     Protein         1..214
                     /product="endonuclease III domain-containing protein"
                     /calculated_mol_wt=24077
     Region          1..214
                     /region_name="HP0602"
                     /note="3-Methyladenine DNA glycosylase, HhH-GPD/Endo3
                     superfamily [Replication, recombination and repair];
                     COG2231"
                     /db_xref="CDD:441832"
ORIGIN      
        1 mttarllkei ytslldhfgp qnwwpgdtpf evmvgavltq ntnwqnveka ianlkeagvm
       61 sfeamaaldr erlagyirpa gyynikagrl qnlfahitdn wdgdleyfls lprerlreel
      121 lavkgigpet adsiilyaaa qpvfvidayt hrilsrhglv dgsfgyyelq elfmdnleed
      181 valfneyhal lvrvgkefck ksrpdcagcp legl
//
LOCUS       WP_457575128             325 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Elizabethkingia anophelis].
ACCESSION   WP_457575128
VERSION     WP_457575128.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..325
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37428
     Region          23..245
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 msffitilsf nfslgqnysq fdksdtisis srvfqserki ivtkpknikp dskenscily
       61 ldanfrnlng iflqsannli snneipssyl igivqedrds elleknklld fiteevvpll
      121 kknynisqni tiaghsfgay fatyaflksn nifnsciais paywpnnedv lklmakivkn
      181 nsvtgnfyll tgdkrwdeis lrkyifkaqk ilnnnkkirf nfydlkgfsh natptvgfgl
      241 glnfiydewe wgnileeqee rltdfpdfwg hleikgdalf hlkrvseakt vyqeaprkvp
      301 idkdlsgnek ieitkrlnnk ikncy
//
LOCUS       WP_457575427             217 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease III domain-containing protein [Desulfomarina sp.].
ACCESSION   WP_457575427
VERSION     WP_457575427.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..217
                     /product="endonuclease III domain-containing protein"
                     /calculated_mol_wt=24459
     Region          1..214
                     /region_name="HP0602"
                     /note="3-Methyladenine DNA glycosylase, HhH-GPD/Endo3
                     superfamily [Replication, recombination and repair];
                     COG2231"
                     /db_xref="CDD:441832"
ORIGIN      
        1 mgrkncylea ykklldhfgp qgwwpgetsf eimvgavltq ntnwqnvtla idnlrnagvl
       61 syeqllvlsl enlaelirps gyynvkagrl rnvllmienl yggdpelfyq ddmvsarenl
      121 lsvrgvgpet adsillyacn hpvfvvdayt hrvfsrhnlv eeetdytamq slfmenlpee
      181 telyneyhal ivavakkfck knkprcgscp lsglneg
//
LOCUS       WP_457575536            1350 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Desulfomarina sp.].
ACCESSION   WP_457575536
VERSION     WP_457575536.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 1350)
  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 1350)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1350
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..1350
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=155967
     Region          69..816
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          77..339
                     /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          97..127
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          132..160
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkadftqscq teyslgmass vkfftsavff lilfffplns nvaaeiaptr titvvaespd
       61 vpgwkkiwdn arekvkaddy dsavilykkl hnlkpnieea nweyfkvlmn kglikeatri
      121 inslleknps kneyllgsgr iflsekkyns alkqfgrvye fdpdgsfsvn alggmivsle
      181 gekkknvllp lleqlhlrqn tdtsivqkli etaaalgknd kalhyfsllr qnrqlkhids
      241 kilflvagvl ekkgdrreas qlweeylrrt gdyfpfhkkl vayyldggkr esalphlirl
      301 srrshaddal lkqiaeiylh ttgrpdkalt ylekylakhp edrkikkkik niqailandf
      361 laivendgaw llwrdlaqit pnrlaiyrem atllekkgkk delfevlkii shhnpedsgt
      421 iykiisicre kknyplalky leklpesakn tkkffllkgd lefmsgreis slisyanglk
      481 kdekdlklrq tcirlagrlg fvdkvnflfe gtpdpqeknk nfsfifnyle qlrynfffss
      541 ldtalgkyyk lfasnpqhil klrllqaqsl rargnrakae ellrlivaee gpvpevffdl
      601 avtsaevrni saarvwkegf vqffpadpki rekrkferkk nylegiisla egdveqtvak
      661 tvnlenlrlk kkeglflsdl eyklkkklcw llledgnidg skellkellk ikefdpervv
      721 lrhvmetlsg aeakagpekd slyinrqpvl srfiqvalta lhhnefdfgr qilktvlknm
      781 pesivgmnll aefsyysgkm kepvtifkki vkrypsekyf ikklvmsegk leryqqglsv
      841 lvehntnlte llanrsfplp avdfeeillf armqwgagnr neslklyefl lnppvvdile
      901 krfefeeiyy lyltkeksfw nslkfllqtk peivaelmqp pflidnlkne tgkiiaeyys
      961 lytwqkmien eylarkaivr rdyetaerny krmledagsr eglydlasiy drrgqyrkea
     1021 qvyeairssg ttserlessi esnslkisph tglsvnlvsr kgrggymnle krgvgfslmf
     1081 tpdlqkdikf efsrniyeev tgpdsltssf lestgtvelt gntdfifsaa aerlsddaet
     1141 kfyysvglhs qlddfftgfi egyrkkiddt llaikdsmys egleiglsae tplglnlgvs
     1201 yrhryysdgn sqngfhgwss ynlygesilw alrydyeflk nnscndcsda egdgeieekt
     1261 ywkpdtfdeh ritlhfkhlv sgnygsdrll syyifdnsvg yednenaiyi gkfdiflems
     1321 hhyllkgnfv fqknsdfeek tvlfslfyrw
//
LOCUS       WP_457576251             426 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease, partial [Desulfomarina sp.].
ACCESSION   WP_457576251
VERSION     WP_457576251.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..>426
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          7..370
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          239..423
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrlfasitke lllltrdrag lvllfimpaf lviiitliqd qvttttaeil fadrdggtag
       61 reikkffqas tsfelidtid gqpvtavqae klvaggqfhf avilpenlsr tiekksgflv
      121 rkqffpeekl tppvdgptit vwfdpsvqgs fraalnsslg aiikgietrq tmekifallp
      181 ekirasmppa mrsfaadsfs spdfsvpeil sdstftaikq rfatemgfsv qptavqqnvp
      241 awtifgiffi vlplagsiis ernsgtlkrl kvmpvnystv magkllaytl islaqfgvif
      301 lasqyilplf gverfnagte laafgvvlla vicaangygi flgtfcrtye qvsmfgpvsi
      361 vigaafggvm vpvyalpdfi rplsilsply wgqagfydll lrqgnlysil peagalfgfg
      421 lllcta
//
LOCUS       WP_457576671             110 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Desulfomarina
            sp.].
ACCESSION   WP_457576671
VERSION     WP_457576671.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..110
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11956
     Region          8..105
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mdkfhssnrt yhdiskrypd viealerlgt tirglgplde ktshliqiaa aatgrsegav
       61 hshtrraika gatreeiyht llllistigf pqtmaaiswc rdilegsgge
//
LOCUS       WP_457577484             152 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Desulfomarina sp.].
ACCESSION   WP_457577484
VERSION     WP_457577484.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     gene            1..152
                     /gene="rimP"
     Protein         1..152
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17405
     Region          1..151
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mseyiletie vflrqllpsm elelfdiqfr reghgwvlrv fidadrgvtl edcskvsrel
       61 shyldiedfi dhayhlevss pglerplrsv tdfarflgkt arvklsekrd gqkifegiie
      121 evdgsdillk ledqssvkfs favvnkarlt is
//
LOCUS       WP_457577525             336 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Desulfomarina sp.].
ACCESSION   WP_457577525
VERSION     WP_457577525.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14206253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..336
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=38326
     Region          27..335
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK00059"
                     /db_xref="CDD:234605"
     Region          203..333
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mhnsqtapff klfffiffis tlclkpvnsr teiidkvvav vnndiitlse veqeaeglyr
       61 aiaqknsgds llqaldrare ktldalidkk liiqrakqfh vsvsqkeidn ayeqvrtrag
      121 ldkttfkkkl kesgmtekmy rsnletrllq kkllsydvrs kvviteamiv dyfdehytkk
      181 vkkgsfyllq igftwddtgd pqkdtenrqh arrtaervhk lalsgqkfrk lakkfsslps
      241 agdggdigif tldemapamr kavadlkpga isdiveigts fqffkllsgn kdaiivtasy
      301 edvkkeikqk lyekklkeay sdwvkklkdk ayirkl
//
LOCUS       WP_457577565              64 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Desulfomarina sp.].
ACCESSION   WP_457577565
VERSION     WP_457577565.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 64)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 64)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10596226
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..64
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=7307
     Region          6..61
                     /region_name="Fer4_13"
                     /note="4Fe-4S single cluster domain of Ferredoxin I;
                     pfam13370"
                     /db_xref="CDD:433153"
ORIGIN      
        1 mripvidlgr cseclgcvei apqifrynef lgymevaemd tyekkdvdea ikncpedcis
       61 weev
//
LOCUS       WP_457577655             127 aa            linear   BCT 27-JAN-2026
DEFINITION  5-carboxymethyl-2-hydroxymuconate Delta-isomerase [Desulfomarina
            sp.].
ACCESSION   WP_457577655
VERSION     WP_457577655.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12040845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..127
                     /product="5-carboxymethyl-2-hydroxymuconate
                     Delta-isomerase"
                     /calculated_mol_wt=14492
     Region          2..125
                     /region_name="CHMI"
                     /note="5-carboxymethyl-2-hydroxymuconate isomerase;
                     pfam02962"
                     /db_xref="CDD:427080"
ORIGIN      
        1 mphfiveytd nlekeadfhi llekanaili nqnglfpiag irsraikldn yviadgeedy
       61 afvhgsltva agrseddler vaeelfamit dhfreisrnr ylalslelke fsrptlkksn
      121 iherfqt
//
LOCUS       WP_457577797             764 aa            linear   BCT 27-JAN-2026
DEFINITION  serine protein kinase PrkA [Desulfomarina sp.].
ACCESSION   WP_457577797
VERSION     WP_457577797.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13393050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..764
                     /product="serine protein kinase PrkA"
                     /calculated_mol_wt=89681
     Region          21..647
                     /region_name="PrkA"
                     /note="Predicted Ser/Thr protein kinase [Signal
                     transduction mechanisms]; COG2766"
                     /db_xref="CDD:442049"
     Region          479..745
                     /region_name="PrkA"
                     /note="PrkA serine protein kinase C-terminal domain;
                     pfam06798"
                     /db_xref="CDD:429125"
ORIGIN      
        1 mrdltnamen lakhegrnns rpalsfadfl qeviarpeql irdvfqvyvd mintymcdee
       61 edcgddsesi gflkydctrl fvegsdrpff adrlfanrlm rhvesfkvgg kqnkififdg
      121 phgsgkstfl nnllrkfeey anspegsrye vvwrlkhdrl vggvhslnsl tnklawvfes
      181 egkseladel kcacndsrdl agtfdvpcps hdhplllipk dvrrrffddl fendeikwhl
      241 fteknyewif qdepcticss iydellkklq dptkvlecvf arpyvfnrkl gegisvfnpg
      301 dkplrhnvms nemiqrrlns aldgamrvsy lysryaktnn giyalmdiks hntdrlmelh
      361 niisdgvhkv edmeervksl lfalmnpedk kllkdlhafa drveyinipy vldlktevdi
      421 yrenfgkhid esflprvlhn farviiatrl rtkseameew idspekyemy cdkhlqllkm
      481 eiftghipew lseedienfn akrrlkiiae sekdgwkgls grdsirmfne fyttyakddk
      541 lidmsmlgrf frkfckqdrd ilpmgfldsl lrmynytvlq evkeslyyyn eeqisknlin
      601 yifgvnfevg avefceftge kleiteeffr rvesqlqiev edapafratt qkaytstalt
      661 qemlrdglpi tettlyshly ekyvhnlkgr vlepflknen frravkdfnq eefktydrki
      721 qddvtymmen lqkkhlysrq gakeiciyvi dnnlaeefsk ngvt
//
LOCUS       WP_457577791             474 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Desulfomarina sp.].
ACCESSION   WP_457577791
VERSION     WP_457577791.1
KEYWORDS    RefSeq.
SOURCE      Desulfomarina sp.
  ORGANISM  Desulfomarina sp.
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfobulbaceae; Desulfomarina.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Dunin-Horkawicz,S. and Lupas,A.N.
  TITLE     Comprehensive analysis of HAMP domains: implications for
            transmembrane signal transduction
  JOURNAL   J Mol Biol 397 (5), 1156-1174 (2010)
   PUBMED   20184894
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Hulko,M., Berndt,F., Gruber,M., Linder,J.U., Truffault,V.,
            Schultz,A., Martin,J., Schultz,J.E., Lupas,A.N. and Coles,M.
  TITLE     The HAMP domain structure implies helix rotation in transmembrane
            signaling
  JOURNAL   Cell 126 (5), 929-940 (2006)
   PUBMED   16959572
REFERENCE   6  (residues 1 to 474)
  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   7  (residues 1 to 474)
  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   8  (residues 1 to 474)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Desulfomarina sp."
                     /db_xref="taxon:2894769"
     Protein         1..474
                     /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=52896
     Region          5..462
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          <236..462
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mslklnredv swsrikralp lffllwsgga llatlllftv rgslqeiere atgkmlndyl
       61 atgnavdlhl gfipmgsrep lrglafirmv rgsdhvilvn ehgehldika lvdlspteeg
      121 vwlrigsgve qrvltivtgk ygdnvivqag adsranfrvy kmlekriivi vllssllllp
      181 lalfyvrlsl tplvsteksi selilrpkst llpeqgngpe ldrlykqins llvqnrqlvk
      241 emqdsldnva hdlrtpmtrl rsvaeyglqa dddceklrea lsdcleeser vlamlkimms
      301 vaeaesgtmr ldlqrcevge llaeivtlye yvaeekkvev sleaeeelhl ivdrtrisqv
      361 wanlldnavk ygraggwvki sagveggfcl vvfedngmgi seneqgriwe rlyrgdrsrs
      421 ekglglglny vravvethgg svsvrsvlhe gsrfevrlpl dqlsiqeksq tsge
//
LOCUS       WP_457578125             418 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Enterobacter kobei].
ACCESSION   WP_457578125
VERSION     WP_457578125.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter kobei
  ORGANISM  Enterobacter kobei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Enterobacter kobei"
                     /db_xref="taxon:208224"
     Protein         1..418
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47446
     Region          78..390
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mvyldylltf iesnpalaig fnlillvisg ffahlmckfl likivrkvff sshkqdvple
       61 kdrriaekls nfipviivyy vlqfmpnmpa slvtaintic gilffiflsv ffnemldivn
      121 ssylrktkrk nhsikgyiqi gkifihiiaa imilavmsnk spaiiisslg avaavlmlvf
      181 qhtllslvan iqlssndvlq lgdwiempdk nlsgevtdia lhtitirnwd ntisriptkn
      241 fltetytnwq amfssgarri mrsttidqhs vkfltqetla pmlalrgtne plaklidgrd
      301 pmgvadswfm dngltnltlf rhylmawlad rpdiikdmyi vvrtlkptps gipleiycft
      361 ssvlwmeyen tqsaifeyit avagqfslrl yqhpaghdfw rlsqeyslrd ripppgeg
//
LOCUS       WP_457578129             316 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Ensifer adhaerens].
ACCESSION   WP_457578129
VERSION     WP_457578129.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..316
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=34948
     Region          18..141
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(22,24,79..80,83)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            24
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(78,122..123,125..126,130)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(84,89..90,118,121..122,125..126,129,132)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(107..109,118..119,122..123,126,130,133,137)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(107,123,126,130,133,137)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(131,137..138)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mardaqnrts rrpqgrqigy arvstdeqat eaqeielhsa gcdvivqehg sgasrarpal
       61 arllreidag dtlvvvrldr larsvshlle vienltlkna hfrslrdpid tttpqgmfsl
      121 qvlgavaqle ralisertka gitaakakgr lpgnpgirek rpealakmta aqkaaygdri
      181 qasanqwlpt vrrmrpdhtw ddiarvlkqr gldwtperlr ravkwmvaer madpallrks
      241 pprlpedrlm tlvagihssn pdltlreiaa qlerlhertp rggskwspss vknlidralr
      301 mgllagasdt evplve
//
LOCUS       WP_457578132             230 aa            linear   BCT 27-JAN-2026
DEFINITION  SMC-Scp complex subunit ScpB [Ensifer adhaerens].
ACCESSION   WP_457578132
VERSION     WP_457578132.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     gene            1..230
                     /gene="scpB"
     Protein         1..230
                     /product="SMC-Scp complex subunit ScpB"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0051304 - chromosome separation [Evidence
                     IEA]"
                     /calculated_mol_wt=25131
     Region          39..208
                     /region_name="ScpB"
                     /note="Chromosome segregation and condensation protein
                     ScpB [Transcription]; COG1386"
                     /db_xref="CDD:440996"
ORIGIN      
        1 mvgsnaakve ragrktksed nvlidreldd lppdlrwrew mlrveavifa aaepvsretl
       61 trvvgkscsi dliiddlree lrsrpydiva vaggwqhrsr saygsviras qaptrsssvs
      121 lseheaavla aiaylqpvtr galsnmfgke vsrdtiaslr dagflgsgpr sptpgapyty
      181 vttrhflsaf gletlrdlpd lermeddgll srqaldetai gefdgdvled
//
LOCUS       WP_457578133             347 aa            linear   BCT 27-JAN-2026
DEFINITION  TniQ family protein [Ensifer adhaerens].
ACCESSION   WP_457578133
VERSION     WP_457578133.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..347
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=39002
     Region          26..156
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mttvdahapt isireryrdv vadrwpvtvv pqpeellssw lhrlayangv aprafarvlg
       61 lnpgmwsaal dlrlpadian llsaktgiap drfaamtlph dlprqfllpl rndgrhwast
      121 wlqfccrcla edaqpyfrrr wrlatrvsct ehgcrlrdrc pschgriavf dqgelvpqhy
      181 cvacgydlrr apipylspet rtldrcidni csveaiahap sgpvfvrrll gmpsvggyys
      241 tmiltslsta araycadrls rpdewlvdyt tddekdcker rlrrlipprs dhrawiella
      301 nalgrrrgrp tasegnepgi klpdllgaya rmnpgpgrre vqeligt
//
LOCUS       WP_457578138             158 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578138
VERSION     WP_457578138.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 158)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..158
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17688
     Region          9..136
                     /region_name="NUDIX_DHNTPase_like"
                     /note="dihydroneopterin hydrolase; cd04664"
                     /db_xref="CDD:467549"
ORIGIN      
        1 mieipvrcfa vsvvllrrvs agcevlllrr nhtlvgewcq iagaieegek aweaalrevs
       61 eetnltcdrl yaadiceqfy eadrdaisml pvfvgfvdad aavvinhehs efrwvsfeaa
      121 lamvpfagqr hvlkhveaef vlrepvphll ikadsrrs
//
LOCUS       WP_457578151             603 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Ensifer adhaerens].
ACCESSION   WP_457578151
VERSION     WP_457578151.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 603)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..603
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=65640
     Region          1..470
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrvarivvkn frtferldvn vendlcciig enntgktail raiqicldis lpstlrsllr
       61 edinanvdis tptqvligve ltgfegivne ealvstwktg adrarifyrf rpkpgvreql
      121 asgaiqpgsl tlddyaweir gggnpaidll dlewnedgvg eavrfadlqs flvvhlpalr
      181 dvegdlrnpr qspliklies fdiskdeqeg liqildeann liaksktisd vaqaidsrfk
      241 dvsgpafemg aklglsaatf railrnlkli lsdtslqefe pgrnglgmnn ilyisiliey
      301 lkrriaggns sgqlilieep eahlhpqlqy slisalnsig vqtvltshst hvtsqvplkt
      361 ivsltkrgda siaagnlaln akltsgevsd leryldstks sllyarkvml vegaaelfli
      421 paliesvhkv klervgislt aihgvhfdvy aklfahgsle kkcaivadad lipsdasald
      481 fnpddsspdl malendfvqv flgattfere ltskgllpmh iaaaealgap kihealssgy
      541 aklcsgsmsl ddevklrvel ggavlntakr fgkaryaqva arfadranel peyiqqafdw
      601 lse
//
LOCUS       WP_457578166             207 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578166
VERSION     WP_457578166.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10576085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..207
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22747
     Region          5..54
                     /region_name="Nudix_N"
                     /note="Hydrolase of X-linked nucleoside diphosphate N
                     terminal; pfam12535"
                     /db_xref="CDD:432618"
     Region          68..196
                     /region_name="NUDIX_CDP-Chase_like"
                     /note="CDP-Choline Pyrophosphatase and similar proteins;
                     cd04672"
                     /db_xref="CDD:467556"
ORIGIN      
        1 mestwlsrak rqqaiastgl hfckdefdre ryteiasian amladladvp varipglvsd
       61 fakgyatpki dvrgaviegg killvrersd grwtlpggfa dvgksaseni vaeireeagl
      121 qvcatqlysv rhkakaayep dardfyklff lcarsgeltm eagietsdvd ffapdslpel
      181 srnrvlqsdi ltafafrnge qhhvafd
//
LOCUS       WP_457578174             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ArdC family protein [Ensifer adhaerens].
ACCESSION   WP_457578174
VERSION     WP_457578174.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gonzalez-Montes,L., Del Campo,I., Garcillan-Barcia,M.P., de la
            Cruz,F. and Moncalian,G.
  TITLE     ArdC, a ssDNA-binding protein with a metalloprotease domain,
            overpasses the recipient hsdRMS restriction system broadening
            conjugation host range
  JOURNAL   PLoS Genet 16 (4), e1008750 (2020)
   PUBMED   32348296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Belogurov,A.A., Delver,E.P., Agafonova,O.V., Belogurova,N.G.,
            Lee,L.Y. and Kado,C.I.
  TITLE     Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa
            has a high similarity to the 'protein transport' domain of TraC1
            primase of promiscuous plasmid RP4
  JOURNAL   J Mol Biol 296 (4), 969-977 (2000)
   PUBMED   10686096
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..309
                     /product="ArdC family protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34504
     Region          1..308
                     /region_name="ArdC"
                     /note="Antirestriction protein ArdC [Replication,
                     recombination and repair]; COG4227"
                     /db_xref="CDD:443371"
ORIGIN      
        1 mssrkedkpr vdiyakitdr ivaelakgvr pwvkpwsaan ttgritrplr hnglpyqgin
       61 tlllwseava rgfvspvwmt fkqgvelggh vrkgetgttv vyasrltrte tdsrgeever
      121 gipflkaytv fcadqieglp ehyyrnlapa tdpveriaha dsffantgav irhggnqayf
      181 npaldvvqmp pfesfrdaps yyatlghelt hwvgsekrld rnlsryhkdr asraheelia
      241 dlggcflaad lgivpelepr pdhasylasw ltilknekrf ifaaaahaqr avnylhelqp
      301 adgqdrqaa
//
LOCUS       WP_457578179              92 aa            linear   BCT 27-JAN-2026
DEFINITION  HU family DNA-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578179
VERSION     WP_457578179.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..92
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9488
     Region          3..92
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mtttneiadk iaseqslska qakaivesvf khiadaaqsg aetsipsfgk fkvkdtpere
       61 grnpatgati kiaaskkltf tpgkavkdal ng
//
LOCUS       WP_457578196             393 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578196
VERSION     WP_457578196.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40515
     Region          4..392
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mstpsivias aartavgsfn gafgntpahe lgaavikgvl eragveaaev devilgqvlq
       61 agegqnparq aamkaglpqe ktawgmnqlc gsglravalg mqqiatgdad iivaggmesm
      121 smaphcshlr ggvkmgdfkm idtmikdglt dafygyhmgi taenvarqwq lgreeqgtfa
      181 lasqnkaeaa qkagrfadei ipfivkgrkg dvtvdqdeyi rhgatldqmt klrpafdkeg
      241 tvtagnasgl ndgaaatllm teaqaskrgi qplarivswa tagvdpqvmg tgpipasrka
      301 lakagwaigd velieaneaf aaqacavnkd lgwdpsivnv nggaiaighp igasgarvln
      361 tllfemkrrg vskglatlci gggmgvamca eam
//
LOCUS       WP_457578200             215 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578200
VERSION     WP_457578200.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..215
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23452
     Region          6..215
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 msdqswteyl pslmqgaqlt ilvtfismig gtvigiilam mkissskllq gcaaiygtlv
       61 rglpllvqvl lvyfalpalt gvrmpavvag tiaimlftga fmaeiirsgi qsvdpgqmea
      121 grsigfghwe tmrlviwpqa fwvmlpnvvn qfsitlkdts llsvigvvel tmagetiysm
      181 nfdtirvlai vgtmylviyl vaeriaawle wrisr
//
LOCUS       WP_457578203             295 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578203
VERSION     WP_457578203.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 295)
  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 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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..295
                     /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=33038
     Region          <138..276
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          219..273
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvnqdksatw isafnvdlsn aidhfdrpdg pllllnairg ivpfefamsv vyrrnatpvy
       61 vadtfanrmg kralelyiqg tfvlnpvyna flaglragvy rlrelapday fssdyylqfk
      121 vqqqseeeig yrtfgwpagr eevvvtielp hnhlaeisls rrtscggfad adcdrlraie
      181 plvgamyrri wqhrmrvskc dgrsfpfagl ladfgkgqls precdvahmi lkghssesig
      241 rnlgisittv kthrqnlyar lglssqqelf slflqsltks tdevgdkkld tattd
//
LOCUS       WP_457578206             256 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578206
VERSION     WP_457578206.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..256
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28038
     Region          8..226
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdgvnhmsks qsldrgleil eavnqaerpm gtrelarvle lspaivqrlv ntlaerhylq
       61 rdpdtkryti gyqtltfgas lmrrdnllie arkeleevtr klrvdsymaa lqgrraiylm
      121 clagdapvsv raepgevlsl hstaigkcil asfsdeqvle ilgpgplpai tsktvtdprl
      181 llddihltre rgfavvqhen idgiisvgal ikqpvsgprt aislsfspyf skdidveeaa
      241 aiivaaarrl sriavt
//
LOCUS       WP_457578207             391 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Ensifer adhaerens].
ACCESSION   WP_457578207
VERSION     WP_457578207.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 391)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..391
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42102
     Region          150..387
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mlespadqak lgtqcrerff ginaefdavi tddpvhigyl sgyrsilhdt gpypqaliat
       61 rekvalitga sdgaaalevl rdpeaiwryg tffvfnsgdm psyqgmpaaa qtaaealrta
      121 itvmaprvns iccdlhrpel raavenavpq arlgpaaeaf qrsraikisg eldllryvsg
      181 itdnaiegaa allrpgvnel eiaaeitrai avgggtarfv vvtsgerssr vdayarnril
      241 qdgdlvrldi gatvngyysd martyavgdp gilakdryaa llrgetrele lvrpgiaanv
      301 ifeaamkevr sgalpnyqrn hcghgiglys hefpligpns etllepgmvl cvetpyyeig
      361 wggmmvedtv ivtdngsell tntsrdlrra i
//
LOCUS       WP_457578209             245 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578209
VERSION     WP_457578209.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..245
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26517
     Region          1..229
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misardvhks fgslevlkgv dltvatgevv cvigasgsgk stflrclngl eransgeili
       61 gdislmaret dinklrqrvg mvfqhfnlfn hlsaldnitl gpirlksvpk aqaesdarkl
      121 malvglddra damprmlsgg qkqrvaiara lamkpeamlf deptsaldpe mvrevldvir
      181 nvarngmtmv ivthemgfar eiadrvafmh agmiheigpp rpdlrsaprk adagfslknf
      241 vgtar
//
LOCUS       WP_457578213             329 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Ensifer adhaerens].
ACCESSION   WP_457578213
VERSION     WP_457578213.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..329
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34781
     Region          <2..314
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 meeldavapn npvyisrccg hvgvgnslaf aaagvtenta dpngghiekr dgrltgqmqe
       61 naqrliftai paltleetvt aienaanqll kfgvasvmda gvgfdglmdm aafqtarrsg
      121 rlplraylai lagpdgilde chrlglvtga gdeflkigpa klfadgsigg ltaamsqpyl
      181 ndgvnrglfi ysdqdmnemv adymtrgyqv athaigdaai eqvlsayekg isaggsarlr
      241 hriehceftt fdqirrmksa gilpipqpcf lthfsdayaq avgaeataas splrtwieng
      301 mspatstdsp icpprhigel gshadaera
//
LOCUS       WP_457578220             392 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Ensifer adhaerens].
ACCESSION   WP_457578220
VERSION     WP_457578220.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..392
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43351
     Region          21..382
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msdkapcwpt etevservsc lkknmeaagl dalvitsqhn feyytgyrtl fwlsdtrpfl
       61 avvrldksgi sivlnqgerr dsfsrdnpnv hlvsyqgfte falqatanyl gdlprgssvg
      121 ldygrdlngr gslflidslr ntphnfalle aadliwrqrv ikskhelkak riacgiatda
      181 ffegladlrl gmteyefgqi lkvrmiglga dsidwlpvrf gqgemdyaap nsdrqlqadd
      241 fvwvdmgvrr gdqisdlnri akvgkvtpeq ddiygfvrdv tlrlaegirp gmtghdafav
      301 feklwsarnf sqrgklaiag rvghgsgial teppslmags seviiedmvl hvepkleiag
      361 gvfqveevfr vtpngpefls aispsnlpsv ef
//
LOCUS       WP_457578222             425 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578222
VERSION     WP_457578222.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..425
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46564
     Region          22..394
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqnfyeatas rptypelvgk ldtdvciigg glaglctaig liergvrdvt lieservgsg
       61 asgrnggfvf ggysldnael lrklgreear hlygltiqav ehirsrikqy eidcdivdrg
      121 vllanwfddp srlerlrsmm drdfgvewqq vsqgalrkql ntpryhgglf epnafhihpl
      181 kyvlglakav vdgganifeq spacsiersg qdfvirtska llkakhvvfa ggayargvtp
      241 riersvlpia tyvivteplg aglsevinaq faiydtrfaf dyyralsdtr vlwggrisif
      301 nrkpetiarl lhrdlvrvyp qlenvridya wgglmsyash kmpqigrdad gvwhalafgg
      361 hglaptsvag etiaeaiaeg eampkgfaaf gltrafgfvg laaaqliytg yqlrdgimsy
      421 rgsar
//
LOCUS       WP_457578223             263 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578223
VERSION     WP_457578223.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..263
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29100
     Region          26..261
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mafeftksat vaqfnekans qpavmiedvs kwfgtfqalh nvsltvaage rlvicgpsgs
       61 gkstlircin qleehqggri vvngtelrpg mkglanvrrd agmvfqqfnl fphlsvldnc
      121 tlalrrarki prdaanqiam eklervriae qankyprqls ggqqqrvaia ralcmtpkim
      181 lfdeptsald pemvkevldv mtalakegmt micvthemgf arevadrvvf mdkgavveea
      241 apqkffsspe hvrtqqflkq llh
//
LOCUS       WP_457578224             220 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578224
VERSION     WP_457578224.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..220
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23722
     Region          1..215
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mdfdfafalk iiprvlegag ntilvavlsf fgatllgffw emlrrshklv rpvtqfaida
       61 irstpalvqi yflffvlpyy givlpalfvg vfglsfyysg yisevfkagi daipagqsea
      121 alslglgrld tmlfvvapqm lrniaaplgs ysigilkstp llaviavpem lgsaldvasd
      181 tyryaepmfv agilflilal iaaflvaale rrlgvlstsh
//
LOCUS       WP_457578225             219 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578225
VERSION     WP_457578225.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..219
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23373
     Region          3..207
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 msfieivlgi lqgvgvtaev tvlgllyavp falvagvlqh fstgasrwti tiviefwrst
       61 svlvllyafy yslpafgiel savsvgamvl gmnagayasq svraalqsld rgqceaglal
      121 gldrlavlrm ielpqalrnm vptfvneaiq likgtalvsl itltdmtfra kqiaqlsydp
      181 vgiysglllc yliicypvsl fgryldrsag kaggringl
//
LOCUS       WP_457578227             239 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578227
VERSION     WP_457578227.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25954
     Region          7..201
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 minsptrpaa slheavreei iarirngtyq pealipsaam lgeefgvspi tikralrdlq
       61 stgalvavag kgtyvkkrtr vlrrldismp syegttiqlh sitrekisda amdsfnppsd
      121 amlcvrktvy adgapfmyda tylssdvsdd iieefgevfv ttalerrgie iantdliida
      181 apasgkveei fgippgypml rrfykfttns saitvfgvvq apfdqlacsi sipassklr
//
LOCUS       WP_457578228             159 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578228
VERSION     WP_457578228.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17707
     Region          2..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mmtldaidrn imrllrvdar msnaklagev glspsaclrr iklmeqagvi rgytavidtt
       61 qsettiavii nitlerqted yldrfeaavr khpeirecyl mtggsdymlr vdvenagafe
      121 rihkeilstl pgvlrihssf sirdvlaarp karrsvsts
//
LOCUS       WP_457578230             417 aa            linear   BCT 27-JAN-2026
DEFINITION  D-amino acid dehydrogenase [Ensifer adhaerens].
ACCESSION   WP_457578230
VERSION     WP_457578230.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..417
                     /product="D-amino acid dehydrogenase"
                     /EC_number="1.4.99.-"
                     /GO_function="GO:0008718 - D-amino-acid dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0055130 - D-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44897
     Region          1..415
                     /region_name="PRK00711"
                     /note="D-amino acid dehydrogenase"
                     /db_xref="CDD:234819"
ORIGIN      
        1 mkvivlgagi vgvtsayqla kaghevtvid rqegpalets fanagevsfg ycspwaapgi
       61 pqkaikwlfm ehaplilrpk idaamlgwla kmlanctsgr yainkgrmlr ladysrisit
      121 alrketgity dermqgtlql frtqaqldas akdvkalaad gipfevldrd gcvraepals
      181 yvrdkvvggl ltpkdetgdc fmftnalakk aeqlgvrflw rteikgldie gggvrgvvtn
      241 wethkadavv valgsyspll lkrygiklpv ypvkgyslti pitdasrape stimdetyki
      301 aitrlgdrir vggmaeisgy tndlgqarrr tlehsvmdlf pggdaskasf wsglrpmtpd
      361 gtpvigptki aglylntghg tlgwtmssgs arviadlvsg rkpeidatdl alsryaa
//
LOCUS       WP_457578248             329 aa            linear   BCT 27-JAN-2026
DEFINITION  carbon-nitrogen hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578248
VERSION     WP_457578248.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..329
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36527
     Region          44..308
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(86,169,173,177,202..203,205..206,227)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(86,169,202)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(170..173,176,183..185,203,205..209,212..213,
                     239..240,242..244,246..247,264..265,308)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mtqngnlkrr vraraaktge sytaalqhir qrphepairs irmavaqtal fndprdvsal
       61 hasgtemrgl mrhahqagar llhfpegttc wphkrimset gpreigpsdw trfewgalre
      121 eleatrrlas elklwtifgs vhqltsphrp hnslyvvsdr gelvtryder llsntkisfm
      181 yspgkkpvtf evdglrfgca lgmevhypei fveyenldvd cvlfstaget psnapafaae
      241 alghaasnty wvsfstlapq staapsgias pdgqwavqcp mtglpaiava diktnpqsla
      301 rpwrrkarsd lytphhiegd srsddrslf
//
LOCUS       WP_457578256             131 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578256
VERSION     WP_457578256.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..131
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14056
     Region          8..86
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpnpkapnev dvtvgrnvrr irnmlgmsqe mlamklgltf qqvqkyekgt nrisasklva
       61 mshaldcsig qfftdveast ttvpvpnvss aalklagqfd kiaspsqrda vfklvaslar
      121 hdathsalae e
//
LOCUS       WP_457578260             108 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578260
VERSION     WP_457578260.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..108
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11915
     Region          5..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtqptfgkri kelrtgkglt ldqlaietgs sksyiwelen kdpprpsaek laaiavalgv
       61 ttdyligree vtladaqdka ffreysqmdp dtrekirama rvlggkkd
//
LOCUS       WP_457578275             422 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerate kinase type-2 family protein [Ensifer adhaerens].
ACCESSION   WP_457578275
VERSION     WP_457578275.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Yang,C., Rodionov,D.A., Rodionova,I.A., Li,X. and Osterman,A.L.
  TITLE     Glycerate 2-kinase of Thermotoga maritima and genomic
            reconstruction of related metabolic pathways
  JOURNAL   J Bacteriol 190 (5), 1773-1782 (2008)
   PUBMED   18156253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..422
                     /product="glycerate kinase type-2 family protein"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43077
     Region          5..421
                     /region_name="GckA"
                     /note="Glycerate-2-kinase [Carbohydrate transport and
                     metabolism]; COG2379"
                     /db_xref="CDD:441946"
ORIGIN      
        1 mpaitdprrf lealftsava aadpekviaa nlparpkgrt vvvgagkgaa qmaaaferhw
       61 hgplsgvivt rygyaapcet ievleashpl pdengllask rllaevcglt addlvvalvc
      121 gggsallpsp ppgltledei avnrallasg apisamnavr khvsmikggr laaaaypakv
      181 vslivsdipg ddpalvasgp tladastred altlierysl dlpakvmawi nspdsaapsp
      241 ddprfarnev rliasasvsl eaaaaearaa gidaiilsda iegeardvgg vhaaiareva
      301 grgrpftkpv vvlsggettv tirgkgkggr nsefllalal gidgakgvsa laadtdgidg
      361 sednagafad dttiarlaaq rldaaaflqk ndswsafdal gdlfkpgptg tnvndfrail
      421 vq
//
LOCUS       WP_457578277             317 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578277
VERSION     WP_457578277.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..317
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34342
     Region          23..171
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mvepakpals wkplvvlpmp lvyrparade laatdalvvs sindltirhg fgpmaatspp
       61 nfqlfclrnd pdglwvaeeg ggivgcawsw tcgdlwflaq lfvdpaqqgr gignsllert
      121 leharksgaa hkalitftfn rvsqglymrh gffprtpiyf fdarreavrm lpeavlravp
      181 iepdaatmet latvdrcaig vsrdkhhryl lgdlatrgfl fyagsdpagy gyiganghig
      241 plavlrpdhv qdafaaalrl aaagtseris aflpgacdga lslavnqgmr itfpmllmas
      301 pgygdwtryl prnpgfm
//
LOCUS       WP_457578278             600 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Ensifer adhaerens].
ACCESSION   WP_457578278
VERSION     WP_457578278.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11114206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..600
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=65933
     Region          12..>121
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; pfam01321"
                     /db_xref="CDD:460159"
     Region          153..312
                     /region_name="Creatinase_N_2"
                     /note="Creatinase/Prolidase N-terminal domain; pfam16189"
                     /db_xref="CDD:465053"
     Region          315..539
                     /region_name="APP"
                     /note="X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also
                     known as X-Pro aminopeptidase, proline aminopeptidase,
                     aminopeptidase P, and aminoacylproline aminopeptidase.
                     Catalyses release of any N-terminal amino acid, including
                     proline, that is linked with proline; cd01085"
                     /db_xref="CDD:238518"
     Site            order(386,406,417,484,513,527)
                     /site_type="active"
                     /db_xref="CDD:238518"
     Region          538..598
                     /region_name="Peptidase_M24_C"
                     /note="C-terminal region of peptidase_M24; pfam16188"
                     /db_xref="CDD:465052"
ORIGIN      
        1 mdtrarpdis grigalrrkl aeagldgyvv prfdehqgey caphdhrlaf vtgftgsagv
       61 aivmrdraai fvdgryqvqv rdevdlgtfa iehlydaplk dwlknnlrng ervgfnamll
      121 pstwdadcsr svelaggvwt pvdgdlvdai wtdqpekplg kitafpvana gesvaekrrr
      181 iaamlaeqga dllieaqpdn iawflnvrgr dvafnpmpqs flifdragqt ewlvdhrklp
      241 ndlsdfeldd vaiaepgkll drvramaagr talidpgfap satahatraa ggtvqlaksp
      301 itlakmhkna telsgfrdch rldgaawvrf fawlerhaae reasgkpvte leaeerilay
      361 rqmaesfvep sfrsisaagg haamchyaat easnglirkd gvylldsggq yltgttdatr
      421 ttaigpvsde irraytavlk glismaslkf prgsfghqld afarrplwdl gldydhgtgh
      481 gvghflsvhe qpqrfdrrvn eielkpgmvt tiepgyykag aygirienqv evvddgdgfl
      541 sfrsltlvpi dlrladfgll taaertwida yhrrvaqeld gllepetvdw lsdrtapisa
//
LOCUS       WP_457578279             291 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578279
VERSION     WP_457578279.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..291
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32217
     Region          10..284
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtrndpikhf fiwpaliivl misifplvys lttsfmsmrl vpptparfvg fgnyldllqn
       61 prfwhvagtt tliafisvgl qyviglsval alnsrvpgeg ifrvsfllpm lvapvavali
      121 arqvlnptmg plnelmtaig fpnlpfltqt swalgsiiav evwqwtpfvi lmllaglqtl
      181 pddvyeaaal enatpwqqfr ditfpmllpi svavvfirli etykiidtvf vmtgggpgis
      241 tetltlfayq egfkkfnlgy tsalsflfli vitviglvyl ailkpylekh k
//
LOCUS       WP_457578281             246 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578281
VERSION     WP_457578281.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,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   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   4  (residues 1 to 246)
  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 246)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26981
     Region          3..243
                     /region_name="DppF"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1124"
                     /db_xref="CDD:440741"
ORIGIN      
        1 mtalslknld isygdvqith dvnldiadge sfalvgesgs gkstvlkaia glapewtgei
       61 tvlgsprghg idrafsrqcq mvfqdpygsl hprktvdatl gealtihgig drntrieevm
      121 tsvgldrkfr frfphqlsgg qrqrvaiara lmlkpkvlll deptsaldvs vqaeilnllk
      181 rlrreqnltf lmvthnlavv sflcdrlavm rqgriveiad vadlkrgdlk dpysrelmqi
      241 saahan
//
LOCUS       WP_457578287             608 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457578287
VERSION     WP_457578287.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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..608
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..608
                     /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=66725
     Region          29..278
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          242..596
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mkhrlvlafl llpllaamla wkgyavttds ylreagaqat talrlavtal dghlnryqal
       61 paliadhddv relvtrprdr rlreavdsyl kdingllqss diyvitpdgn tiaasnydgp
      121 tsfvgqnfsy rpyfqealrg eqsrfyalgt tslkrgyffg spirvgneir gvmvfkvdve
      181 rieaswqgge ykifvsdpeg ivfmsgdpew ryasilplts drlarteasr ryadatvhal
      241 tvservssdr hfltvsaens sreylmlsqr mpdadwtvnv lvdtasvrtq alttviaall
      301 llclaglgva iilqrrarln erlsmqaeaq aelerrvder tadlarvngq ieeeiaerrl
      361 tekqlrrtqa dliqagklag lgqmsaalsh efnqplaaak tyadsaalli ergrsdeatd
      421 nirrisglvd rmaaiskhlr nfarkpnekl grvpveevvr dtmeivsvrl kaaaatidid
      481 lgneplvvra gsvrlqqvlv niisnaadav eglddrtirl rakqedgkvv ltvsdrgpgi
      541 apaiaerifd pffstkgvgk glglglsisy niikdfggsl vatnlaegga efrielaaen
      601 snareaae
//
LOCUS       WP_457578288             382 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Ensifer
            adhaerens].
ACCESSION   WP_457578288
VERSION     WP_457578288.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..382
                     /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=42124
     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 mdvrvhnirk efgrfpaldd vsldirsgel iallgpsgsg kttllrlvag lesptegtif
       61 fgdedasqkt vqernigfvf qhyalfrhmt vldnvafglk vrpsnrrpps aeirkraldl
      121 ldlvqlsgld krypaqlsgg qrqrvalara mavepnvlll depfgaldaq vrkelrkwlr
      181 dihdrtghtt ifvthdqdea leladrvvvm skgvieqvgt pdeiydhpvs pfvygfigqs
      241 nclnvtlqng eiwfedrpig lrapsepdgp aklhfrphdi elvdgsggcl aglvaasrrv
      301 agtrhleldl grnhphveie lsperaaagd hsriafrptk wkifregrpe mkiapagatg
      361 sqrqtadeae smlaaqvswa tp
//
LOCUS       WP_457578289             168 aa            linear   BCT 27-JAN-2026
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578289
VERSION     WP_457578289.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..168
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19217
     Region          5..143
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mattliipgl fgsgsghwqr hwlndnpqav lveqddwdrp rldlwrdrle heifrhgtvd
       61 lvahslgcll vanlvrrpla rqvrsallva pcdlgptdrl hpgaidfgsm pdlplpfssl
      121 vvgslndpym pfdrlrhfst rwgepprrsw pcrahqhcqw fwplvawl
//
LOCUS       WP_457578290             182 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457578290
VERSION     WP_457578290.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..182
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18801
     Region          40..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrinlvdpv satgpcaell geirsafgva pnmfravans paalasmwgs fgalgkgrlg
       61 aklgeqiava vadrndchyc laahtalgrk agataeemta aqhgkssdpk taaaltfaqk
      121 lveargqvsd advrtlrdag fddedvveii ahvalnlftn yinvalavpv dfpgvklvre
      181 aa
//
LOCUS       WP_457578294             199 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578294
VERSION     WP_457578294.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..199
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21331
     Region          41..>166
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mdnlqmirna qfppalappa vqpqerfiag gegnpklrav vldpaperpn kpailhlhgg
       61 glvvgkpeva vpglqqlsae lgalivsvdy rlapehpfpa gfedayaalg wlhqaavelg
      121 vdrkriavmg esagaglaaa vslrardrge wpirfqllry pmlddrtvlr ffhrltseps
      181 sgtrsrmlla glpcsvasr
//
LOCUS       WP_457578295             596 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578295
VERSION     WP_457578295.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 596)
  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 596)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 596)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 596)
  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 596)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467931
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..596
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=65499
     Region          1..554
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
     Region          524..594
                     /region_name="oligo_HPY"
                     /note="Oligopeptide/dipeptide transporter, C-terminal
                     region; cl07097"
                     /db_xref="CDD:415039"
ORIGIN      
        1 mtedllrisd lavkfrgtpd galavkgidl aigrgevvai vgesgsgksv taksimrlve
       61 ymgaeivggr avlsektggs tdlltldetr mqglrgdria mifqepmtsl npvltigqql
      121 cevvvkhrki graeadgial nalqqvripe perrlkqyph elsggmrqrv miamailckp
      181 dlliadeptt aldvtvqaei lellkviqre tgmaillith dmgvvaeiad kvvvmlrgev
      241 vesgeihqif napkheytrr lldaapklqs rqegfpqtkh vpctqarqdk adpnvvlsvr
      301 nlvtrfavrq gmfervvanv havegvsfdl reketlslvg esgcgksttg ksimrlirpn
      361 ggevllqgrn legvnasemi emrkriqmvf qdpyaslnpr msveqivaep lrihrvgsps
      421 qirdrvysll ervgltraqa slyphqfsgg qrqriciara lalnpkviia depvsaldvs
      481 iqgqildlla eiqeefeisv lfishdmavv ervsdriavm ylgeiieigp rdavlgspah
      541 pytqqllsav pivhpdqrrs rtlgarelrs pirppgyvhq tpalkavgfe hyaria
//
LOCUS       WP_457578302             355 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotriesterase family protein [Ensifer adhaerens].
ACCESSION   WP_457578302
VERSION     WP_457578302.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Chen-Goodspeed,M., Sogorb,M.A., Wu,F., Hong,S.B. and Raushel,F.M.
  TITLE     Structural determinants of the substrate and stereochemical
            specificity of phosphotriesterase
  JOURNAL   Biochemistry 40 (5), 1325-1331 (2001)
   PUBMED   11170459
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Shim,H. and Raushel,F.M.
  TITLE     Self-assembly of the binuclear metal center of phosphotriesterase
  JOURNAL   Biochemistry 39 (25), 7357-7364 (2000)
   PUBMED   10858282
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Kim,G.J. and Kim,H.S.
  TITLE     Identification of the structural similarity in the functionally
            related amidohydrolases acting on the cyclic amide ring
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 295-302 (1998)
   PUBMED   9537960
REFERENCE   4  (residues 1 to 355)
  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
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Tuovinen,K., Kaliste-Korhonen,E., Raushel,F.M. and Hanninen,O.
  TITLE     Phosphotriesterase--a promising candidate for use in detoxification
            of organophosphates
  JOURNAL   Fundam Appl Toxicol 23 (4), 578-584 (1994)
   PUBMED   7867909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004443
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..355
                     /product="phosphotriesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39010
     Region          12..351
                     /region_name="Php"
                     /note="Predicted metal-dependent hydrolase,
                     phosphotriesterase family [General function prediction
                     only]; COG1735"
                     /db_xref="CDD:441341"
ORIGIN      
        1 mskelseghv rsgkvmtvng aidanqlgit lmhehilndc rcwwnapqtk erqylaegfv
       61 cmeilgelrq dpfvnkhnit lddeplaiae lqafataggr tvveptcngi grnplalrri
      121 skatglnivm gagyylassh paevadmsvd qiadgivrea idgvdgtgvk igligeigvs
      181 sdftpaeeks lrgaaraqvr tglplmvhlp gwfrlghrvl dvvaeegadl rhtvlchmnp
      241 shddfayqse laergafiey dmigmdffya dqqvqcpsde eaaraiarlv daghmdrill
      301 shdvflkmml shyggngyay vlrhflprlk rhgledgald rmmrdnprsv fqtga
//
LOCUS       WP_457578304            1059 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Ensifer adhaerens].
ACCESSION   WP_457578304
VERSION     WP_457578304.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..1059
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113489
     Region          1..1044
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mniprffvdr pifavvlsvl mligggltll klplseypqv tpptvqvtas ypgaspevia
       61 etvaapleqv ingvenmlym ssqaatdgrm tltvtfqqgt dpdmaqiqvq nrvsralprl
      121 pqevqrigvv tqktspdilm vvhlvspddr ydplylsnfa tlqvrdqlar lsgvgdvlvw
      181 gageysmrvw ldpakvaarg ltasdvvaai qeqnaqvaag svgqqpdasa alqvtvntlg
      241 rlsneeqfga ivvktgadgq vtrlrdiari elgadsyalr slldgkpala lqiiqspgan
      301 aldvassira tmedlqkgfp egieyriayd ptvfvkasle avvmtlleai vlvvivvvlf
      361 lqtwrasiip lvavpislvg tfalmymfgf slntlslfgl vlsigivvdd aivvvenver
      421 hialgetpke aarkamdevt gpiiaitsvl savfipsafl sglqgefyrq faltiaisti
      481 lsavnsltls palagvllkp hhgevkrdll trvidglfgw ffrlfnrffe rasnayvwsv
      541 rravrfsalv llvyaglvat twlgfhtvpn gfvpaqdkyy lvgiaqlptg asldrteavv
      601 kkmseialae rgvesvvafp glsvngmvni pnaaviftml kpfderkdps lsafaiagrl
      661 mgkfsqipdg fagifppppv pglgttggfk fqvedraglg faalaeaqga imgkamqtpe
      721 lagmlasfqv napqvqvdid rvkaksqgvp lntifetlqv nlgslyandf nrfgrtyrvv
      781 vqadapfrmq pedigrlkvr naagammpls alltvkhssg pdrvmhynsf psadisggpa
      841 pgysfgqata aieriaaetl ppgmtfewte layqekqagn tamyifplsv llaflilaaq
      901 ynswslpfav lliapmalls aiagvwftgg dnniftqigf vvlvglaakn ailivefara
      961 kedegadpls avleaarlrl rpilmtslaf iagvvplvia kgagaemrhv mgtavfagml
     1021 gvtlfglvlt pvfyvvvrkl airrekgrip egasleqra
//
LOCUS       WP_457578306             305 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578306
VERSION     WP_457578306.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32922
     Region          31..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mhshhridwe dlrfvlavae anslaaaara lgvnhttvlr rvgsfeqklg vrlfdrlpsg
       61 ymltaggeel lavarqmaet vtelerrltg qdlrlegslr itttdtlmas ilpsiladfr
      121 qrhpgvllev stsnalanls hrdadvairp avdspdalvg rriakvafav yaapsyldvr
      181 eltadtldia gehwiglgda lastsvarwm rttlvapavl rcdslvtare aakagiglaa
      241 lpcylgdttp glirigapva dmtrelwllt hedlrrtarv saftefvgqa lakhrplleg
      301 nkpst
//
LOCUS       WP_457578307             530 aa            linear   BCT 27-JAN-2026
DEFINITION  TolC family protein [Ensifer adhaerens].
ACCESSION   WP_457578307
VERSION     WP_457578307.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..530
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55521
     Region          169..523
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mmvsagarwv svgvialcrs mcraargsll lgalsipaac tsaalddlap psadrpavsg
       61 tgtkdaskvs agapdfslap npeipitiat psidpkhdys lpelvdiaqr tnpitraawq
      121 rarqaaiavg iteavylpll tadvlagleq tsatapgigg pipiapgtlt ttgaqfipsl
      181 tvkwllldfg grdagreaat qlafaanvtf ngthqklifd vsnayfvlta arvqlkiarq
      241 taqnaelvqa aakarmgrgi atsievaqan qqvaqarfnl tqsqgherna ymtlleavgv
      301 sptleiriad gsnralpkav pedlnrliat slqrrpdvqa afarlqadkn giaaaraefm
      361 pkvalvgnvn rnigslsved trfdqrstir vnqpnanlmi glsfpiydgg lrdarlqsam
      421 aqvgaaeqem aqlqntaare vvvaydllrt slagyaaase lttaaqttyd aavdyykqgl
      481 gtitdvsiaq tallqakvak ataysdtlva aaslafatgt ltnrnavnrf
//
LOCUS       WP_457578315             150 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Ensifer adhaerens].
ACCESSION   WP_457578315
VERSION     WP_457578315.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..150
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16735
     Region          51..137
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 maerltktga rnvfyggsif ffaifvglta hshyymrtts tdettltdav argkhvwekn
       61 scinchtllg egayfapelg nvwkrfggea dpdgardtlk awmaaqptgi egrrqmpqfn
      121 lteqelndla dflewtsrik tqnwppneag
//
LOCUS       WP_457578317             503 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiD family decarboxylase [Ensifer adhaerens].
ACCESSION   WP_457578317
VERSION     WP_457578317.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Mondal,A., Roy,P., Carrannanto,J., Datar,P.M., DiRocco,D.J.,
            Hunter,K. and Marsh,E.N.G.
  TITLE     Surveying the scope of aromatic decarboxylations catalyzed by
            prenylated-flavin dependent enzymes
  JOURNAL   Faraday Discuss 252 (0), 208-222 (2024)
   PUBMED   38837123
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Marshall,S.A., Payne,K.A.P., Fisher,K., Titchiner,G.R., Levy,C.,
            Hay,S. and Leys,D.
  TITLE     UbiD domain dynamics underpins aromatic decarboxylation
  JOURNAL   Nat Commun 12 (1), 5065 (2021)
   PUBMED   34417452
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Marshall,S.A., Payne,K.A.P. and Leys,D.
  TITLE     The UbiX-UbiD system: The biosynthesis and use of prenylated flavin
            (prFMN)
  JOURNAL   Arch Biochem Biophys 632, 209-221 (2017)
   PUBMED   28754323
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Jacewicz,A., Izumi,A., Brunner,K., Schnell,R. and Schneider,G.
  TITLE     Structural insights into the UbiD protein family from the crystal
            structure of PA0254 from Pseudomonas aeruginosa
  JOURNAL   PLoS One 8 (5), e63161 (2013)
   PUBMED   23671667
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..503
                     /product="UbiD family decarboxylase"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55850
     Region          11..496
                     /region_name="UbiD"
                     /note="3-polyprenyl-4-hydroxybenzoate decarboxylase
                     [Coenzyme transport and metabolism]; COG0043"
                     /db_xref="CDD:439813"
ORIGIN      
        1 mnrtfrpskg fatlqdfida leregdlkri srpvslvhev teihrrvlaa dgpallferp
       61 vdatgaaqpi plltnlfgse rriergfgla pggldalage laelrdprap qslrdawdrl
      121 pllrsamymr prkvtralcq evvwrdqeid lgrlpvqwcw pgepaplitw plvitrapdd
      181 pfdvnvgiyr mqvlgpdrai vrwlahrgga rhhrlwqrlg qdmpiavvig adpatilsav
      241 mplpdglsel nfsgllrrgr tqlvkaktvp lsvpanaeiv iegrvsaskt aeegpygdht
      301 gyynsvepfp vmrlsaitmr rnplylstyt grppdepsrl geamnrlfvp lvrkqfpeis
      361 dlwlppeacs yramvvaidk rypgqakrvm mglwsvlpqf sytkliiavd pdidvrnwsd
      421 vmwalatrfd asrdvtvieg tpidyldfas prsglggklg ldatnkigae tdrewgrvle
      481 mspevvgqvd aiwaglglgg ltr
//
LOCUS       WP_457578321             256 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Ensifer adhaerens].
ACCESSION   WP_457578321
VERSION     WP_457578321.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..256
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27828
     Region          64..>234
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mfntavlerv lvaslvaslv ggtafaqevg kspwgpkdei grlnlitpds raailsrieg
       61 sksydlavey figmpsweaa gdppyqmwmt htpngtlvsd pmkvgkemna hvsytgsavs
      121 myahmgthid alnhfglngk iwngyaaadh lgdqgwtitg aeklpaivar gvmidvaaak
      181 gmqmlpdnyr itrkdleeal ksqgvtlaeg dvalirtgrm qnyedkaaym snpprpqhrr
      241 gkvprrgrrr hgggrr
//
LOCUS       WP_457578322             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578322
VERSION     WP_457578322.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32586
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllaamrsf rrvielqsfn kaaeelgqsn asiskqvrql eerlgavliv rttrrmslse
       61 ngrayfsecc rlldeldhle rttsgeagei ngrlrlnapl sfgltvlapm larfmtlhpq
      121 lkvdmtlddh vldvvsegfd vsirvraalt dssliarrlg digqvicaap tyladngtpa
      181 tvadlkshhc ltyrladqpg swrlegpdga vmidlparfv adnslmlsem iqagigigvl
      241 psfiatplla egklcqvlpg hklaergiya vyptnrlllp kvkaftefla semrqael
//
LOCUS       WP_457578325             250 aa            linear   BCT 27-JAN-2026
DEFINITION  SURF1 family protein [Ensifer adhaerens].
ACCESSION   WP_457578325
VERSION     WP_457578325.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..250
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial respiratory chain
                     complex IV assembly [Evidence IEA]"
                     /calculated_mol_wt=26736
     Region          30..245
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mtggrdvkge gaksssrarf lltgallllc aifvalgtwq iqrlfwkldl iarvdarvha
       61 davpapsrpd wggitrende ylrvtatgtf shdksvlvqa vtergagfwv ltpmrradgt
      121 tvlvnrgfvp adrrdrtara egetpgttgi tgllrisepg gaflrsndpa gdrwfsrdva
      181 aiaaakgltd vapyfidada tpnpgglpig gltvvsfrns hlvyaltwfv lagmsvggvy
      241 ivrrrstssh
//
LOCUS       WP_457578327             432 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Ensifer adhaerens].
ACCESSION   WP_457578327
VERSION     WP_457578327.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..432
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46465
     Region          35..409
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mrprlsctal iaslvmstaa mawaaelprs geptfdrvie lvnanfydgk aldrfnttaq
       61 aeitdpvaal srtsassrvd aaiasvlasl gvshtgrfka dtinyfelad ifrfairddm
      121 rrlfppdgaa rypgigmvtt vkngqrfvsd vydgsaakka gllvgdqils vdgqayheig
      181 sfedkvgrtv elrlrrhrda eplslqvpve slrplqmfer aieesvalie tggrkvgyvr
      241 lwtlstrngl nlvaealssg rlkdaeglvv dlrgrwgggp adaaeflvgg tptfrliprr
      301 geatlanfrw qkpvvalidn gtrsglelfa ytlrqhgitl vgertagall agrayvlpdd
      361 sllevavsda vigdelrleg vgiapdvqma fplayaagkd pqreaaiaem vrvlhatpap
      421 etlpaqepaa tr
//
LOCUS       WP_457578330             385 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578330
VERSION     WP_457578330.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 385)
  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 385)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..385
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42104
     Region          10..362
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(22,198..200,260,282)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 mgvadlanar itiivsalga ggtehvvslv ashwarlgct vtvitleapt sepyyrldpr
       61 vtierldvpv qkagklraaw lvarrlyrlr stisrtrpdf vlsfltrtnv ltllatrglr
      121 lpvivsernn pavqpfgpfw kwlqlrlypr afalvtmtkg aldyfppnvr rsgrvianai
      181 nlpdgwqkkr gnnvltavgr lteqkgfdll leafakvasd hpewklviwg egearkalea
      241 qrnalgladr vempgvtakp glwvetadlf vlssryegwg ialleamavg lpvvsfacew
      301 gptdmiangd dgilvengdi nalaealsnl madetlrarl aanaeanvrr ydaehilsqw
      361 davalaareh sagrklksca npvfg
//
LOCUS       WP_457578332             508 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457578332
VERSION     WP_457578332.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 508)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..508
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54802
     Region          22..447
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mdkrsaassr veetldpkdw aelralshri vddaidylsq vrerpvwrnm pdmvresfsa
       61 plprtpkple eiyasvaenv lgypmgnihp rfwawymgsg nftgalgefl aavqgsnvgg
      121 gnhaaalmdq qvvnwckeml gfpttasgtl vsggsvaniv gltvarnvka gidvrahgig
      181 drplcfygsd qshschrkav elfglgdral rrvatdaelr idiaalrrai eqdrasgrlp
      241 iciianagtv ntgaiddiqa ladlaaefgl wlhvdgciga llriapenaw rvagierads
      301 ialdphkwlh apfeagcvlv rdaaahrgtf avtqeyldst vrglasapwl ydyglqtsrg
      361 fralkiwmsl mehgiekfgr lveaepqlel vaptniniac fryhpenmta erlkavntei
      421 mlrlqdegta visdtmghge hclrvainad geivagggig chkvlrgckr hrvaagscag
      481 rvsgagvaws mrtisviaas rcgsllav
//
LOCUS       WP_457578335             465 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457578335
VERSION     WP_457578335.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..465
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=49191
     Region          15..458
                     /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 madvrlgisw qpvirksdgp lylaiadaia adisegrlse gmrlppqrtl aealgidftt
       61 vsraynearh rglvegrvgq gtyvktrrir tgrtpaggli dmsmnlpplf ddpmlaarlw
      121 ddmaalqaeh glellmryqp pggtlhnraa gaawlkprlg evpaervlia agaqgallat
      181 lgsltkagdm icaeaitypg lralaahlgi rlhglamdre gllpeafeel caketpkaly
      241 cnptlhnptt ttlslerrqa ivtiarrhdv aiieddayga lpvstprpla alapdlvyyv
      301 gglakclspa lriaylvvpd srssvrvega iratvgmasp laaaiatrwi edgtadavla
      361 airsetaarq rivsellpag vaqthphafh awlqlpppwt rgelsarlqa agisvvasda
      421 falgappeav rlglgaaagh aelrrsllvi ndligqppaa ssfvv
//
LOCUS       WP_457578337             343 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578337
VERSION     WP_457578337.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37116
     Region          11..267
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtvipgpfpp vlevedlcia yadssgerra vhdvsfrinp gevvalvges gsgktttaqs
       61 iigllaangr vergtiklng tdiarwtdrq ldtvrgaris lvpqdpgssl npvktigsql
      121 gemfrihgal rsdeieaqvl sllarvglse palrarqyph elsggmrqrv liaiaialkp
      181 qliiadepts aldvtvqkri ldlidelrte ygtavllvth dlgvaadrad rivvlqggrl
      241 qeqgatgavl aaprspytkq llsdapsfta ppevgngstt rcggsgryrr rrgpcprirs
      301 qgrrvpatrr rrtelprpag ndpcnrrgir vweddddpqh rrl
//
LOCUS       WP_457578338             293 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578338
VERSION     WP_457578338.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30432
     Region          21..272
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mttfdtlhnd avaapraksd rrsgaasrll rvpvglalsw lilgsvflwa vapsfftgyn
       61 plegvggaql qrpsadhllg tdalgrdlya rivygavhsl tgafvavglg lavgtglgvv
      121 agsvrrrfdd aimrvvdvll sipplllsls iiillgfgtv naaiavgvts vagfarlara
      181 evvrvrrsdy veaafgsggt fasvlwrhil pnsltsvvaf aalqfgsavl qistlgflgy
      241 gappptpewg lliaegrnyi stawwlttap givvvlvvla anrvsqsfgr aaa
//
LOCUS       WP_457578339             338 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578339
VERSION     WP_457578339.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..338
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=36455
     Region          3..332
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 misaptttiy giqylravaa lgvvvfhaae rtghhfaiga agvdvffvis gfimwviser
       61 rpvsplaflr driqriapiy wlatavmvig glvglfpnlv lsnahvlssl lfipmrspss
      121 deiwpalvqg wtlnyemffy avfaltlllp rsrrlpaiag cfsalvaigf avdsdnalfv
      181 tytrpiilef vagmivaelw mrgrvpgams glvlvagafs gfaavavlrl pfdefilgpl
      241 avmlvlgtla leaqgwfrps rlpmmlgdas ysiylwhtfa isvvvkacgm mgiglltsal
      301 laviagtalg vfaylliekp latrlrsgff srpvqhta
//
LOCUS       WP_457578340             427 aa            linear   BCT 27-JAN-2026
DEFINITION  O-antigen ligase family protein [Ensifer adhaerens].
ACCESSION   WP_457578340
VERSION     WP_457578340.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..427
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O-antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46348
     Region          150..395
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkiskaslis sdrngvygtv aialslfvfa yssrfgqasi llyyslwlpl vlvdyrrvlg
       61 nygirlwilg faifaclsvf wsaapgmtar tgiqylshvi caliamrvvd irtlvrgaia
      121 gtgvvlvysl lfgvyhldpl dgtysfvgaf asknqlgfya slgiyfafva pialgerglw
      181 faasslvall sayslfasqs atsvlttvvi lglwlgmrlv gllspahrkg lflaaavccv
      241 mvavaaiygg gvdlvlglfg kdstltgrty lwqqgieaam ssplvgvgyq aywvqgfsep
      301 erlweefyia trsgfhfhnt fieamvetga iglvllsgil litvlghtkr lltqdhdtqs
      361 svlfgialll lvrsfveidi mnpyhigsfl lyfaagkltl pearthqsve drpapavsei
      421 plrlryq
//
LOCUS       WP_457578342             315 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide pyruvyl transferase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457578342
VERSION     WP_457578342.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..315
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35084
     Region          1..191
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 mkpyywesqh gnfgddlnlw lwdfllpgfr dvhddillvg vgtvlnrall pdgvrklvig
       61 sgfgygslpd mrdaaewdlr cvrgpltaek iglapergiv dpavmvadmp efrnlpkryk
      121 rsfiphwesa iagmwpvtcg tvgmhyidpr geaksvirei aqsefivaes mhgailadaf
      181 rvpwvavtts dsinsfkwnd waktvgveyr prhvpvssrt eamikgarfw gmgfeaqtvp
      241 eaanlrsadg evivaarepr qtflrsaakq vlaapstlal wqatraepql ssdsrlaerk
      301 erfqdalaav rrayf
//
LOCUS       WP_457578343             494 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Ensifer adhaerens].
ACCESSION   WP_457578343
VERSION     WP_457578343.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Hvorup,R.N., Winnen,B., Chang,A.B., Jiang,Y., Zhou,X.F. and
            Saier,M.H. Jr.
  TITLE     The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter
            superfamily
  JOURNAL   Eur J Biochem 270 (5), 799-813 (2003)
   PUBMED   12603313
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Soldo,B., Lazarevic,V., Pagni,M. and Karamata,D.
  TITLE     Teichuronic acid operon of Bacillus subtilis 168
  JOURNAL   Mol Microbiol 31 (3), 795-805 (1999)
   PUBMED   10048024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..494
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=52706
     Region          10..413
                     /region_name="MATE_tuaB_like"
                     /note="Uncharacterized subfamily of the multidrug and
                     toxic compound extrusion (MATE) proteins; cd13127"
                     /db_xref="CDD:240532"
ORIGIN      
        1 mpsnvnaksv trnvgwsvls ktgtfglkfv tvpilarilt peefgtvava ltvvqflami
       61 ggaglasali iqrdedmeli hsafwanlvv slmmalglfv fagplasllg apeaihllqi
      121 mslliplqla gdvaysllar rmnfskdavw tmlseilgal iavgaallgf gvwsllaqlf
      181 vsafirlagl yavsgyvprf vfsarrvlsl crfsfgmmgs eianfvtfqs pmvvisrylg
      241 lsdagaysaa nrfssipnqi vlsavmgvlf pafshmgedr qrrsqalmls tqvttvllap
      301 mmfglwalae pamlvlfgqq wasawpvlgl lalskglltp cstyipylkg igqgttlfww
      361 aviraiatta avayaaiggs lveamialcl vnlatlvgys wvvfradqlp flrgflisvr
      421 plvsafimav vvrllldhyg mllpsavlqv lvgatigali ylvlvlvter sllakltdmv
      481 rsrgasssvp aaae
//
LOCUS       WP_457578344             371 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578344
VERSION     WP_457578344.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=41063
     Region          9..332
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mnanissrin lmrivlisgi vfvhvpydpa tspyvgtygg idwlriflgd slfrvgvpcl
       61 saisgyllfr rglenfdygr tlktkartvl lpfllwnlaf lalvfvaqsk dissgylpki
      121 agasprewls fafalenlpi nlplyflrdl llcivlspal awlikrypaq tlavlfayav
      181 lpvpngiflk ksilfgfsag iymslhridv rsfdrfswpi tiaflsaavl lsillyqfgp
      241 nfpvwlemlr sliaisgivg swavsallvr tnigaqlsrg sglsfwifct hfpllvlfwm
      301 iwnrsdigyy pafycavpli tiaflagaya lsarwlpalt ailtgsrtgs ardmrartga
      361 vragpspqqr t
//
LOCUS       WP_457578346             326 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer adhaerens].
ACCESSION   WP_457578346
VERSION     WP_457578346.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10118577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..326
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35739
     Region          4..252
                     /region_name="Succinoglycan_BP_ExoA"
                     /note="ExoA is involved in the biosynthesis of
                     succinoglycan; cd02525"
                     /db_xref="CDD:133016"
     Site            order(10,12,95)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133016"
ORIGIN      
        1 msirvlivip clneaehlqg laeallpaar rlngailiad ggstdgtrei aarlaekdpa
       61 vlvldnpkri qsaainlava rhgacfdymi ridahgtypd dycerlveea lltgadsvvv
      121 amktvgftpf qkatayaqns klgnggakhr lgaashwadh ghhalmrisa fqaiggydei
      181 fshnedaefd yrfrqagyri wmtdrtsmvy yprakvgplf rqyfaygrgr arnvlkhraw
      241 pslrqllpla vapvavgall avvswlavvp vvlwavacig ygmwmalgqk npygplaais
      301 amvmhfawsa gfwrellttr nrrvap
//
LOCUS       WP_457578348             338 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer adhaerens].
ACCESSION   WP_457578348
VERSION     WP_457578348.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10455355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..338
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37381
     Region          9..172
                     /region_name="Glycos_transf_2"
                     /note="Glycosyl transferase family 2; pfam00535"
                     /db_xref="CDD:425738"
     Site            order(13,15,41,92,94)
                     /site_type="active"
                     /db_xref="CDD:132997"
ORIGIN      
        1 mtqrapdvsf viaaynaadt irraidsala qkgvdveviv vddcskdetc avveeladpr
       61 vrllrlaenr gpggarnagl eaalgdwiai ldaddtvspq rlsrmiglas steasivvdn
      121 idvlnldgrl ermfpeaele rrrtltlaaf igsnvlfrst fnfgymkpif errflnehrl
      181 rfeetirige dyillasala hggrcvvdps agycyhireg sisrvlelrh ieammkadre
      241 flvrhtldae alamqrrrek slveahaflr lvehlksksl agatqvaltn pralrhlrmp
      301 iavrlrrlla piarmkpaas tvaaerptsg esphvskg
//
LOCUS       WP_457578349             417 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578349
VERSION     WP_457578349.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 417)
  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 417)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..417
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45425
     Region          2..395
                     /region_name="GT4_ExpC-like"
                     /note="Rhizobium meliloti ExpC and similar proteins;
                     cd03818"
                     /db_xref="CDD:340845"
     Site            order(13,220..222,295,317)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340845"
ORIGIN      
        1 mhvafvhrrg fcqfaalash laqtgnevtl vtetvdqrip atrvirhrae pgpqansqma
       61 rhlgvpdhhv righrvaetf damarqgqvp dvivghigwg gmtfvkdvlp nvpalgycef
      121 fyraegadig fapddkpdqd trkrlrlrnt aqlltldaid ggfsptqwqr slypaehrar
      181 igvchegvdt rvfrpdpsas lklpdgrvlk agdppivtfv ardlepyrgf pqaleaaakv
      241 akrhpdalfv fvggdgvsyg apppgggswk dyllqsldip adrflfpgvv phgvlrqlfq
      301 isaahiylty pfvlswsvle amacgalvig sdtapmqevl ssgrngllvp ffdtdalaea
      361 isgalqqpek yselraaarr tveqrfrlgd ciarqmtlld kamgnpgstq ilrvssa
//
LOCUS       WP_457578351             750 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer adhaerens].
ACCESSION   WP_457578351
VERSION     WP_457578351.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 750)
  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 750)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..750
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82200
     Region          464..719
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mtaddrirsf gldftsaaaf rlgfdvavli wdapselsak tkyalsasrs lvplvsmalp
       61 raqggqrifw amrpgndrel geiaadgeil qtvvleptak lpfldlaaql sdlqpegrlk
      121 flnnlltvwr safrlsrdef figlvddvih alnlgqrpat iacrlahgry laettvnael
      181 geinaiyalg aeailplpqq faitgraerg qrrchfvles prapqalsli imgkrgiavr
      241 elsprgsryp nlqqwwpehg aapglrefvv rslsevpesg talaidlqlr salpakqagk
      301 salhpgaeid lalamsegll iggwtrdang vlagidylqe dgtalpldgn wyefpgwarg
      361 teegsktdvt gfvswlpmrd plgpllqprf qlrlasgavk plvpkpqpfd patqrnrilr
      421 avppqhandq afrtilapal rdveqrlgkt irvdqtkdfg pmmaaplisi vvplyrvldf
      481 lrfqlsglat dpfvaanaei iyvldspeih detehllggf hllhglsmkl vvmnrnggya
      541 racnagarfa rgsvivmlns dvvpcgagwl eklalpvlke ksigaigpkl lfedgslqha
      601 glyfarnkqd iwlnhhfykg mpgayapaqe mrsvpgvtga cqvmrkevwd lvggyaedfv
      661 igdyedsdlc lkirqagfdi vyepaaclyh lerrsisrsq dytrgvasqy nawlhterwn
      721 qdittlmpsy lgaeeaaaps trkpaarsaa
//
LOCUS       WP_457578352             281 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578352
VERSION     WP_457578352.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..281
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30999
     Region          48..248
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mnqpalhhad nlqpawqqne driegmlqtv ltnrflpqpd qnsvfvgdgn yravgaeflg
       61 hfirmgglqp kssvldigsg igrmavpltq yldsdhgryv gidpveggvt wcrqsvapvy
      121 pnftfqhvdi ahelynpsgr ingkalklpy pdrqfdfaim tsivthlppd evlvyfsein
      181 rmlkpggrlf vtafvvdsia akdehgrrdp rlafvrsgdg pcwfvpglpp laavgfddgf
      241 ldraleragf ttvlkslghw rgqsaghyqd vfvaerrsvs g
//
LOCUS       WP_457578354             433 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578354
VERSION     WP_457578354.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 433)
  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 433)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..433
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=48210
     Region          6..417
                     /region_name="GT4_ExpE7-like"
                     /note="glycosyltransferase ExpE7 and similar proteins;
                     cd03823"
                     /db_xref="CDD:340850"
ORIGIN      
        1 mseklrvlvv shghpthslg gaeiashglh kalnglsgve siylarvgsp vprhgasalm
       61 slrlamdevl yhaedfdhff lsngdtdair rdllrfvgdi kpdvvhfhhi lgfglealya
      121 vrdalpkari vvtfheylpi chnhgqmvkr psgqlcngas pischtcfpe ipvsrfvrre
      181 qflrgmlnla dafiapsafl anryvewgle aakifvieng ivmgdkapar elpsptarrn
      241 rfayfgqmtp fkgvhvlida vsrvpddiwg ddsslmifgg nlerqpndyq ekvaklieda
      301 grrvrfygay qnqdmprlmr svdwvvmpsv wwenspvviq ealhhgrpil csdiggmaek
      361 vrdrldgyhf ragsaqdlad rlidvlgapr awdnlratlr rptshvdcar ehvalyrkml
      421 kgeqpalpsa ava
//
LOCUS       WP_457578362             643 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer adhaerens].
ACCESSION   WP_457578362
VERSION     WP_457578362.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 643)
  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 643)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 643)
  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 643)
  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 11663208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..643
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71529
     Region          <238..339
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
     Region          358..609
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mrevdegech valvgaasly adrpivvsvh dpdhrfgrrp qllfkrrdrt pstvlrsfli
       61 dstgrgrfyg wtpvqldaia laidpetanh lstvepeiri rrlclielav liacrrtlif
      121 fqiirlflag nkkgaafrfv rqcdalsapd ysdwieaqal aeknearmdg qvsqrslrvl
      181 vsidggdalg vaetrdslna qswrcfqeat sadvaklief nkadkdtlwi rlpggvrlae
      241 ralerlvepf afsedvaicy sdedrisarg erfapffkpa wnaplvrsgw lplegavfrv
      301 vhiprgvave sassaeiala vaqartgdil hlprvllhrg qscyssptha evqprrerpa
      361 vsiiiptrdr aelleaclkg lfentapadl dvividnest epatlalfsr yqqsglirri
      421 alpgafnfsr acnigvdsaq hdlilllnnd vepidchwle clagelddpt vgaagnlllf
      481 pdgfvqhggv tlgagtvarh sfhfrdpkdg sdrgllrqrr dmsavtaacl ltrrdlwhrl
      541 rgmdeqnltv afndvdyclk lreagfriiw tpaaamlhre svsrgaddtp qklkrfaeee
      601 ramherwsda lkadpyynpn lsliaeefvl eahprtlaar ssa
//
LOCUS       WP_457578364             267 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578364
VERSION     WP_457578364.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29606
     Region          15..266
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mrraatpvgt sdrialirmi svmhavvlrd irsryfnhgl gflmgpimpv ahmlillliy
       61 sftgrnavfg edlalffatg lvpaltfsyi srymsisvva nknmlafpav klidimlars
      121 fleiigivla tlfigtilva tgsnvvprsp eqallamact aalsigvgii asviaaifpf
      181 famiyslfmv vvylssnapi yitsfpeevi yfcsfnpvfh lvewmrsayy lgyptqyldk
      241 tyvmmwcilt lpiglllerl lrpqimn
//
LOCUS       WP_457578366             323 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer adhaerens].
ACCESSION   WP_457578366
VERSION     WP_457578366.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..323
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36380
     Region          5..244
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mtryrcavvi ptknamhvlp tvmdkvrtqr tpwryeiivv dsgstdgtsd ylrglsdvrl
       61 veigpsefgh gktrnlgvgl adaefvaflt hdaepvdeyw llnlvssaeq dpaiagvfgr
      121 hiaqqtaspf tkseldkhfa gflahplvvs rdldpiryka dvgwrqmlhf ysdnnsllrk
      181 siwqqipypd vefaedqiwa kriieagysk ayspnavvyh shdygffeql crafdesrnf
      241 skyfgyqlsp npgralwtag efaiqalwqq vdesygnltl rhrfaraaqr ialvaghclg
      301 anhqkipaav asrlsldqkl fea
//
LOCUS       WP_457578373             546 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578373
VERSION     WP_457578373.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 546)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..546
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58208
     Region          39..540
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 mgevvgcggp gitlrqqrpf spwtgkevpt tplpvadvss ktalrlsris krfgplrand
       61 aisfelkqge viallgenga gkttlmnilf ghyvadegtv eafgkplppg dpraaidagv
      121 gmvhqhftla dnmtvqenia lgtqsiwrlr ldraaarrri drlsadfgla vdptatvssl
      181 svgerqrvei lkalyreari limdeptavl tpaetealfr tlkllvakgl siifishklh
      241 evmavsdrvl vlrsgqlvge retgstdrke laalmvgkev kpanvsplkl gapllaleqv
      301 satayngagl dkvsltltag eitgiagvag ngqavlaali agirrptsgs isiagrdvad
      361 wspraalahg varipedrha igsigdmsvt enviaeryrs prfsrmgfln wkaagrfaek
      421 liadydvkcp spearirlls ggnmqklilg raldadpavi lasqptrgld vgavayvhrm
      481 lllardrgaa illisedlee vlalsdrifv mfkgrlstps argersirel gelmaghsge
      541 rgdhaa
//
LOCUS       WP_457578377             448 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578377
VERSION     WP_457578377.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=47225
     Region          2..444
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mdlvirnggl itgdgktfhk raavyvrkgr iigvdaaaga eiaaretida aggivmpgli
       61 nahahgcirg psmpsgskpf agddvayfrn rhllqgtttl lnvcglamad eidvdnverh
      121 amdirvstah tpkniaaalv vdgkglsarh lsattddlla cgavalgeag ggqtlgggaq
      181 eyrfipqafl qefgvevtpa aarrlknavl gryldpaegl snlkltnele ccglsglada
      241 drvrdiitrs vmpsvalsla gfdeiareae rlgypaifhn aapsakrlia avekhpkarl
      301 vaghsnhpsf lpeeavsnaq nlrgkgaiid vstldcigtr wrndpsnlda lidagcvdti
      361 stdfagghwd gileaiqrmv rkkqlsaaea vvlatgnvar vftqmagdrg liekgkradl
      421 ivvdhvnlsr vrhvviagri vvrngrli
//
LOCUS       WP_457578382             131 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Ensifer adhaerens].
ACCESSION   WP_457578382
VERSION     WP_457578382.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..131
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14925
     Region          6..128
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 makaihsmir vleekrsidf yrvafgleia erlefetfvl iylsngesef eleltvnkdr
       61 tepyalgdgy ghlalsvddl daehqrltea glnpgkivdf nrdgallarf fflvdpdgyk
      121 vellqrhgry k
//
LOCUS       WP_457578387             178 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein [Ensifer adhaerens].
ACCESSION   WP_457578387
VERSION     WP_457578387.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Thomassen,E., Gielen,G., Schutz,M., Schoehn,G., Abrahams,J.P.,
            Miller,S. and van Raaij,M.J.
  TITLE     The structure of the receptor-binding domain of the bacteriophage
            T4 short tail fibre reveals a knitted trimeric metal-binding fold
  JOURNAL   J Mol Biol 331 (2), 361-373 (2003)
   PUBMED   12888344
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..178
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=18744
     Region          2..178
                     /region_name="MdpB"
                     /note="Phage tail collar domain [Mobilome: prophages,
                     transposons]; COG4675"
                     /db_xref="CDD:443711"
ORIGIN      
        1 mtepfigeiq lfsfnyapyg wafcngplmp iqqntalfsl igtsyggngq snfqlpnfag
       61 rapcnqgtgp gltprtigev fgaqnvtlls tempahthsl tiynqtdgtk rastpsagns
      121 lslptehtvm avstaqpdaq fapsmiglsg gnlphenrqp ylavnfcial ngnfpsfg
//
LOCUS       WP_457578389             407 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578389
VERSION     WP_457578389.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 407)
  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 407)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..407
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44846
     Region          47..401
                     /region_name="GT4_CapM-like"
                     /note="capsular polysaccharide biosynthesis
                     glycosyltransferase CapM and similar proteins; cd03808"
                     /db_xref="CDD:340837"
     Site            order(60,235..237,299,322)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340837"
ORIGIN      
        1 mlidasdfsp vrppphraia vtgsvlagav skqqiavlss ysrsltnfrf ellrclveag
       61 hsvlavgpeq dddvvrqlaa igvefvrspm artglnpltd latlwsywrl frsrqidvvi
      121 pytmkpivyg giaarlagvk rryflvtglg hvysdaagkr wvgrrikqls vllyrlalkg
      181 aggvfaynra dsadiesyrl isdhreltlv pgsgvdldhy afssppsgrp vfllvarllk
      241 dkgigefvea arlvrqqfpe aefrllgqfd pspaaisaet idewvkegsv tylgetndvr
      301 phlsdcsvfv lpsyyregip rsileamstg raivttdlpg cdetvidghn gylvearnvk
      361 qmaeamcrfl rspslipemg lrsrelaqak fdvhavnell lkrmslv
//
LOCUS       WP_457578390             222 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578390
VERSION     WP_457578390.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24697
     Region          4..221
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mgeqvlvfdl ddtlylerdf alsgfravda wlanhlgaeg faghcraata sghsgrvfdt
       61 alaamgiavd ealvgqlvav yrghrpeial addarryler ahvgrraiit dgpaatqqak
      121 vkalglealv drviftdlwg refwkpharg yeaietwael kpdnlvyiad npvkdfvtpr
      181 rrgwrtvmva rdarvhrmva pdrfhkadrq isnldeldda lr
//
LOCUS       WP_457578392             134 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Ensifer adhaerens].
ACCESSION   WP_457578392
VERSION     WP_457578392.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Gao,R., Bouillet,S. and Stock,A.M.
  TITLE     Structural Basis of Response Regulator Function
  JOURNAL   Annu Rev Microbiol 73, 175-197 (2019)
   PUBMED   31100988
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   3  (residues 1 to 134)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..134
                     /product="response regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14014
     Region          8..121
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
ORIGIN      
        1 mitpirtviv ddhplvivga ratiettndi vcvgsagtga ealglikete pgvavidial
       61 pdmsgltlae qilkqqlsay vvvmtiyper syaqqalqig vkgfiqkcsa pehlllairs
      121 vthggalsrs anrp
//
LOCUS       WP_457578393              72 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457578393
VERSION     WP_457578393.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..72
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7889
     Region          <9..68
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mktsgvpglt rreqdvlrlv algysnkeig aranvsvksi etykaratek lqlhtraqiv
       61 hfalthgwms vv
//
LOCUS       WP_457578397             416 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Ensifer adhaerens].
ACCESSION   WP_457578397
VERSION     WP_457578397.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..416
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46161
     Region          2..391
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mrvnygqsvy gqeeidavva vlrsstqmgk avrtmqerva tlfakrhgim vnsgssanhl
       61 aieiadlpkg sevitpaltf attvapivra glipafvdvv egtynidvda ierminrktk
      121 avmipslign lpdwdrirei adahkllvie dsadtlgati rdtstgarsd isttsfygsh
      181 vitaagnggm vcvnddelar kamlyrswgr tsslfveset ienrfnidld gfdydakfvf
      241 evlgfnieps emgaafglvq ldrlqqnida rernfakqra ffetyedwfv lpeqlplsrt
      301 gwlafpmtvr adapfsrrem qifleqrdiq trpvftgnil rqpamrgihs kveprgypva
      361 ddvmrggill achhgltqah ldhihqsfrd fatqftnsga skrrqqqaas feqpga
//
LOCUS       WP_457578398             326 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457578398
VERSION     WP_457578398.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..326
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35320
     Region          3..309
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msrvlitgaa gfigshltrt cldvghevhv vvrpgsddsr ldaldqsier hnfdlqseda
       61 mksclseisp efvfhlaarp rrreeaelsd akagikehlt allnllgaas svphpplkii
      121 rtgsiaeygt aprpyeedsr empataygae laaathligg lqrrlpfpvi tarlalvygp
      181 tqstefmipl fierclagqp civhhasdrr dllhvsdavd allrianapv strlvnvasg
      241 vaptmrevae livertgadp dlieyrlggm saganelras tarakdlfgw sariplregi
      301 trtvewhrqa palpssnagr wsreta
//
LOCUS       WP_457578399             337 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer adhaerens].
ACCESSION   WP_457578399
VERSION     WP_457578399.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 337)
  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 337)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..337
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38134
     Region          9..190
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(12,14,99)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(46,98..99)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            97..99
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mkqrpkisil vpafneesnv rrayeaivdv frslpgydre iifmdnhstd rtfpilteis
       61 redptvrvir fsrnigyqrs llvayksatg dcsvqidcdl qdpphlipgm lelwhdghqv
      121 vygirrtlkd gwlttrirra fywcinalse ddlplnagef rlvdrrilde lrkvddtspy
      181 lrglisamgf sqvgfeydre arvageskfp fkamlslavd gilnhsltpl rlasmaslvm
      241 gtatlvlllg yligkllfgq dwpagfattt illlisitln aiflgimgey vgrifmqskr
      301 rpapiieasl nddehrrpap ampdwrrgdv aahnkrr
//
LOCUS       WP_457578400             145 aa            linear   BCT 27-JAN-2026
DEFINITION  GtrA family protein [Ensifer adhaerens].
ACCESSION   WP_457578400
VERSION     WP_457578400.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8) (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..145
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15375
     Region          10..136
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mslpttkdas prqragetlt rfaavgavtt lldmalfntf yfagasptps nlvsyscgia
       61 vsymlnrawt fraahshvqa vkfvaatltg llistaivag lallipapva kvvsvpivfv
      121 wnylasrlwv frgseapste trniv
//
LOCUS       WP_457578405             402 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Ensifer adhaerens].
ACCESSION   WP_457578405
VERSION     WP_457578405.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..402
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43222
     Region          3..381
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 matwpvydee qiadvaavlr sgkvnawtgp hvaafeeaya ralgrkhaia langtlalel
       61 alfalglepg devivtprsf vasascvsfc ggvpvfadvd ensqnisaat iapkitsrtk
      121 giiavhlagf pcdmpeimal arqaglwvie dcaqahgaei dgkpvgsfgd iaafsfcqdk
      181 iittggeggl ialddealwk kawsrkdhgk sydaaflreh ppgfrwlhet igtnwrmtsl
      241 savlgsrqle rlpawhatrs rnaaildeva lelaalrvpt lpkgyrhayy ryyafvrpea
      301 lkpghdrdwi vaamnaagvp cfsgscsevy lekcfsdlgl spserlpvar rlgetsiall
      361 vdpaqsdeam tkaarflhav vteaslpalg qrapvlemea ra
//
LOCUS       WP_457578381             305 aa            linear   BCT 27-JAN-2026
DEFINITION  ArdC family protein [Ensifer adhaerens].
ACCESSION   WP_457578381
VERSION     WP_457578381.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Gonzalez-Montes,L., Del Campo,I., Garcillan-Barcia,M.P., de la
            Cruz,F. and Moncalian,G.
  TITLE     ArdC, a ssDNA-binding protein with a metalloprotease domain,
            overpasses the recipient hsdRMS restriction system broadening
            conjugation host range
  JOURNAL   PLoS Genet 16 (4), e1008750 (2020)
   PUBMED   32348296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Belogurov,A.A., Delver,E.P., Agafonova,O.V., Belogurova,N.G.,
            Lee,L.Y. and Kado,C.I.
  TITLE     Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa
            has a high similarity to the 'protein transport' domain of TraC1
            primase of promiscuous plasmid RP4
  JOURNAL   J Mol Biol 296 (4), 969-977 (2000)
   PUBMED   10686096
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..305
                     /product="ArdC family protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33863
     Region          5..304
                     /region_name="ArdC"
                     /note="Antirestriction protein ArdC [Replication,
                     recombination and repair]; COG4227"
                     /db_xref="CDD:443371"
ORIGIN      
        1 mtkdrrrqtq vdiyervtnq iiaaieagag dyrmpwhhdg saittpvnia ssrtyrgvni
       61 lslwaaahaa gyptgiwgty hqwqalgaqv rkgehghlvv fwkthdrdkt edqaddanrd
      121 eparsmfarg ysvfncaqvd gytppespvl peakridrae rfcaalgidi chggsqayyr
      181 pamdqvqipr facfrdavay yavllhecgh asgashrlgr dlsgrfgsaa yameectvel
      241 lsamicadlg lsveprpdha ryirswvdvm hsdkraifia sskaqeiadw mhaqqakqie
      301 argad
//
LOCUS       WP_457578406             227 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Ensifer adhaerens].
ACCESSION   WP_457578406
VERSION     WP_457578406.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..227
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24263
     Region          9..220
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mslietlgrt lviaphpdde vlgaggtmar laaqgsdvfv avvtegkppa ydrasveavq
       61 aeaheahril gvketrwlgf paaalsetsh salnaalfel vrsiapqtll vpfvgdmhvd
      121 hqliflssmv aarphqpgyp kvilayetls etnwnapyvt pgfapnvfvd isdhiarkla
      181 amkafksqvr aapherslet lnalatlrga tvlksaaeaf vmvrqvi
//
LOCUS       WP_457578408             449 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Ensifer adhaerens].
ACCESSION   WP_457578408
VERSION     WP_457578408.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..449
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49228
     Region          28..435
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 millesllkk trkyrlawqa eadlhgrlkn iahlltgnfa safiglagfa ltaralgpad
       61 ygllalsfay trgierfvsf rswqplikyg akalqvgetd dlkalfkfgl lidlatalag
      121 wglavlivlf agplfgisee msrfvliyca vlpfqvtgmp tavmrlygrf kivaygqvaa
      181 silrallcla gvylgwglfe fmllwmvsqi csslnrtawa frelrkqglt gvmwvpvgdi
      241 rtrfpgfwsf slwtnmalii qasafefdtl lvgyladpgs aglyhiakrv akiaqqageq
      301 vqavlypdls rvwategide frktvsqtgw llfafgvcal igahltiewv lrvtagpgfe
      361 aaaslvmvqf vavimflcgr tlysallamg hekillqsal lggvlflfta vvliprvgav
      421 ganlahivms gvwfvqmaia yrrkldskr
//
LOCUS       WP_457578409             671 aa            linear   BCT 27-JAN-2026
DEFINITION  GumC family protein [Ensifer adhaerens].
ACCESSION   WP_457578409
VERSION     WP_457578409.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..671
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=73686
     Region          12..665
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mlatlltaal lprtytaasa ivfdrndvrp yeaqvelrkl erdrsvmete ldvirsrvfv
       61 gvvvdalnlv ndpdfntylp parseyetfl qsffanisef ifgvseestq kerlisenvq
      121 rnraistlln syfvtrtges laltirvvqs nplkaatiad aiaeqylswt akkteeatnn
      181 tvaylrgema nsatriagme rdiaafards dltfdpqddv lrarmlqlne qyvtlrveea
      241 gavakyneak qlvsadgkel aggaltstql delrgeearl ertraqlgak fgknhplvld
      301 atnelesvrt migneaqrlv helannakva tvraekfqte lsalqdkvqg rnlaeirrre
      361 lardlqseqa iydqivlrlg alnpergeyk ptariasyae vptkptfpnn tlvivagsig
      421 avllavvgvi isdslesrly vprdaeqlln rpnlasvpdm rkrvrnssaf yhymlnnpes
      481 paatamrtlc mawltidhea ggkvvmlcsp algdgkttva lgmatmakvd glrpividld
      541 msaqsapnit ganttdtait aplegkvdik srivtspgyp hlefisvrpg lmnldvlcae
      601 lrdsydliiv dapaveeneg viwlashvds vilvcrsggt tdrqlanvqq rlslnhavil
      661 gsvmnycdrs e
//
LOCUS       WP_457578411             316 aa            linear   BCT 27-JAN-2026
DEFINITION  pectate lyase family protein [Ensifer adhaerens].
ACCESSION   WP_457578411
VERSION     WP_457578411.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wu,P., Yang,S., Zhan,Z. and Zhang,G.
  TITLE     Origins and features of pectate lyases and their applications in
            industry
  JOURNAL   Appl Microbiol Biotechnol 104 (17), 7247-7260 (2020)
   PUBMED   32666183
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Hugouvieux-Cotte-Pattat,N., Condemine,G. and Shevchik,V.E.
  TITLE     Bacterial pectate lyases, structural and functional diversity
  JOURNAL   Environ Microbiol Rep 6 (5), 427-440 (2014)
   PUBMED   25646533
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Marin-Rodriguez,M.C., Orchard,J. and Seymour,G.B.
  TITLE     Pectate lyases, cell wall degradation and fruit softening
  JOURNAL   J Exp Bot 53 (377), 2115-2119 (2002)
   PUBMED   12324535
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Yoder,M.D., Keen,N.T. and Jurnak,F.
  TITLE     New domain motif: the structure of pectate lyase C, a secreted
            plant virulence factor
  JOURNAL   Science 260 (5113), 1503-1507 (1993)
   PUBMED   8502994
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Linhardt,R.J., Galliher,P.M. and Cooney,C.L.
  TITLE     Polysaccharide lyases
  JOURNAL   Appl Biochem Biotechnol 12 (2), 135-176 (1986)
   PUBMED   3521491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..316
                     /product="pectate lyase family protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0016837 - carbon-oxygen lyase activity,
                     acting on polysaccharides [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34597
     Region          50..>304
                     /region_name="PelB"
                     /note="Pectate lyase [Carbohydrate transport and
                     metabolism]; COG3866"
                     /db_xref="CDD:443075"
ORIGIN      
        1 mkiqnfilrm rqsaarkmns lsywhftptt rrlvgpsrgl qllallsfls cgpafpvelp
       61 ptavpgaegh gkmarggrgg riilvtnldd agpgslreci egtgprncvf rvagvirlks
      121 slvigeenqs lsilgqtspg ggisltinqq naekkhtplv alrtqdvivr hlrirpalpn
      181 svknvdgvti edskrvyfdh nsvswatden intysnstdv tiansifaeg lnkhskcall
      241 gsdprvpqni tfwgnacisn ndrnpdnnhy atscidiinn vffnarsewg evfsqypggd
      301 adilrrqllq srtkhr
//
LOCUS       WP_457578412             295 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfotransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578412
VERSION     WP_457578412.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..295
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=33806
     Region          24..195
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msniawteqg skngvelsdi dfliigatks attwlqqslq qapyvympda elhffsrnyq
       61 kgdawyldqf erkphtrvig eksnsylesp eaprriqkal prarliaqlr npvdraysdy
      121 cmlyrrgevs kdiskyldpr qagggrfllg glyyrqlety ldlfpaeslk illyehirqn
      181 pqahldavrd flqlpsalkp vankvkdktv pvvppmlrrf lyplrpiaap frstpfvkgl
      241 rsmiarepdy tplpldlrnr lidfyapete rlgkllqqdl sgwldatsss klfpa
//
LOCUS       WP_457578416             406 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578416
VERSION     WP_457578416.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 406)
  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 406)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..406
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44381
     Region          17..380
                     /region_name="GT4_CapM-like"
                     /note="capsular polysaccharide biosynthesis
                     glycosyltransferase CapM and similar proteins; cd03808"
                     /db_xref="CDD:340837"
     Site            order(43,216..218,280,302)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340837"
ORIGIN      
        1 mitgafdrte kgarrlriav vasltaslvn frlellrglv qrgcdvyaig pdddtetttl
       61 letlgihfir ipmartetgp ihdlmtlvgl arvfrkirpd iilpytmkpi iygglaarlt
      121 gvphrfalvt glgyvfvdrt htvrtaalrw lsiklyrmal kgvervfvyn etdaaelqrr
      181 aivakdvltl vpgsgvdter fiacpppngt piflmvarll hdkglnefva aakilrarhp
      241 etrfkllgpf dsnpaaisrl evdrwvaega ieylgqakdv rphladcsvf vlpsyregls
      301 rtileamatg ravitsdapg caepvehgvt gyvtpvknva alaaamerfi adptliksmg
      361 aearrraedr ynvhvvnnal ftglgldrvk haehgtsftl qgasia
//
LOCUS       WP_457578417             430 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide sugar dehydrogenase [Ensifer adhaerens].
ACCESSION   WP_457578417
VERSION     WP_457578417.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..430
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=46031
     Region          9..416
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mssfqvqeri avvglgyvgl pvavafarva ddvvgydisr rrvealvagh ddtgeisgpe
       61 lsasrlkisd dpgclsnatl yiltvptpvd kaqrpdfgpl laacsaiapy lapgaivvve
      121 stvfpgatee icgpaleras glicgrdffl gysperinpg drvhrleaiv kvvagqnaat
      181 leriaaayga iipagihrag sirvaeaakv ientqrdini almnelamif erlgiptrev
      241 laaaatkwnf lhfvpglvgg hcigvdpyyl takaeevgyr pevilvgrsi ndrmgrfvaq
      301 kamklmvemg ialssarvgv lgltfkedvp dlrnsrvpdi vhelhtfgir plvhdphcsp
      361 qeakdnygiv lddlshfegl halilavphk aylatdggie rmlgrgavlv dvkgaladvr
      421 tpedirhwsl
//
LOCUS       WP_457578419             149 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457578419
VERSION     WP_457578419.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..149
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16728
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvarrrlked ycpsarslda igdwwslliv rdafddvrrf sdfqkslgia kniltdrlrt
       61 lvergiletv pageakarve yqltamgrdl fpvmvalrqf gerhlfqpge ehsllveket
      121 glpvkldirt qdgrpidaag tvlikvpea
//
LOCUS       WP_457578420             421 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457578420
VERSION     WP_457578420.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..421
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43953
     Region          36..406
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(44..45,48..49,52,84,133..134,136..138,141,161,
                     164..165,168,242,245..246,249..251,254,282,286,336..337,
                     341,345,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mdgiiaaapa gaanevpcpv gsarpasllt rpmmtlfafa aglavanayf ahplldvmaa
       61 dldlsetrag livgatqlgy alglillvpl gdlfdrrkii ifqsllsgaa lgfvalsdtv
      121 emllvsiaav gmlavltqal vayaaslshq aergrvvgfv tsgivigils aravagfltd
      181 lagwravyiv savltflial llykllpdqq retsklsylr lvastftlia qepvlrvrgi
      241 iatlifanvt tlltplvlpl svppfllsht qvglfglagi agalaasrag hwadlgfgqr
      301 ttgislalml aawlpialld qsllwlvagv lvldfglqav hvtnqaliyr vrpeaqnrlt
      361 aaymlfyslg salgssfsti ayayggwhgv clmgaalsli tllfwlmtep agpqggamln
      421 g
//
LOCUS       WP_457578424             472 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578424
VERSION     WP_457578424.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..472
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..472
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=52091
     Region          20..468
                     /region_name="COG3800"
                     /note="Predicted transcriptional regulator [General
                     function prediction only]"
                     /db_xref="CDD:443013"
ORIGIN      
        1 maigklyigr kvrelreank atqgqfaeri gistsylnqi ennqrpvsaa vllalaekfq
       61 idiselstge gdrllsalse alsdplfety saslqelklv aqnapglaha litchqayrr
      121 nseqlasidd tigrggpfve ttpyeevrdf fhfvdnyihe idilaerlas elglgegdnh
      181 aalasyleqr hgvrvvrgaa gdeairrfdp rariltlnay appatrdfqi alqiaqlhar
      241 eeidrvagsa gfrteeayei criglqnyfa galilpyqaf skaardlrhd iellaarfga
      301 sleqvchrls tlqrpgqkgi piffaridra gnitkrhsaa klqfarfgaa cplwnvhqaf
      361 etpgriirql aetpdgvryl clatqitkgg ggfraaqpry alalgceisy adafvyaddm
      421 dlgnraafdp igiscricer tkcasravpp lkrrlivdhd lrgalpyrls en
//
LOCUS       WP_457578428             230 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578428
VERSION     WP_457578428.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..230
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25288
     Region          11..204
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msaiqlnvik psvnnmtarv flraakldfs endvygqtrs peylarapsh ltpmietadl
       61 prgalwesca imqylcnkhg lddfyprepe aramidsamf yligtfypyl aratypalnf
      121 plyagevgcs dadaatkeia rkaavaalae pldvfrafyi gdkpfiggak psiadirlaa
      181 tleflaaidy dlpdwaktym asiertlgta yaepaadvrg yiayvksqrq
//
LOCUS       WP_457578433             328 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Ensifer adhaerens].
ACCESSION   WP_457578433
VERSION     WP_457578433.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34507
     Region          2..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkntvsiaci maavfgvaap aaafepdrpv efvvtagpgg gtdifartiq aiigkyelmk
       61 apvvvtnkgs aggaegfvyt atnkgdaykl afgtnnayll pvrakvpyka edltpvaala
      121 sdefvlwvng kasyntaadf aakakegglk iggsqskdvd qiltsminet tgstinyipf
      181 ksggeaavql agehldanvn npsenlgqwq agmvkplcvf ksvklsnetk vaggkawsdi
      241 ptckesgiai dnysmprtvw lpagvdqdvv kfyadlmrkv setpewakyl adtsqspayi
      301 agddfkaaie mdgaavgevl kregwlan
//
LOCUS       WP_457578438             267 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF899 domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578438
VERSION     WP_457578438.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..267
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30193
     Region          19..240
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtqtiekren gradaqstmq kppvvsaqaw eaarqemlvk ekahtrarda laaerrrmpw
       61 tavtknyvfe gsdgkaglld lfagrrqliv yrafyepgvh gwpdhgcrgc smvadqvahl
      121 shlnardttl vfasrapqad iarlkarmgw tmpwytitds fdadfdvgew hghnvffrdg
      181 eelfrtylvn srgdeqmgst wnylditplg rqevwedspa gypqtptykw wnwndsyveg
      241 aapdkrwvev sdageaamra sdtsakp
//
LOCUS       WP_457578442             380 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Ensifer adhaerens].
ACCESSION   WP_457578442
VERSION     WP_457578442.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..380
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41706
     Region          2..364
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(164,166,194,220,246,269,296,329)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mkivavrthl lehrlavpfe sasmrfdrra hvlveiecdd gtigwgeclg parpnaavva
       61 ayttwligqd prqteklwai lynalrdqgq rglaitalsg idialwdikg khyrasvsml
      121 lggrwresvr ayatgsfkrd gvdrvsdnal emaerraqgf hackikigfg idedlrvira
      181 vreaigdemr lmidanhgyt vteairlgka aadydidwfe epvvpeqlsa yravragqpi
      241 pvaggetwhg rygmwpaies ravdilqpdl cgcggfsema kitslatlhg vrivphvwgt
      301 gvhiaaalqf maamtpdpvr vnpiepilef drtenpfrqa vlkapieavd gvvaipdapg
      361 lgieidrdal arfkmpesaq
//
LOCUS       WP_457578443             228 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578443
VERSION     WP_457578443.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..228
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24454
     Region          4..228
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 makvtdalsg qigaghykpg drlpseaqlt qefgvsrtvv reaiaalrsg glvearhgig
       61 vfvlepgpst plpfhgidla rvssliemle lrtavegdaa alaalrrspa qeekiaeafd
      121 sfcesaaqgr ptaeadfnfh laiaqatnnp rfseflqmlg taliprravs esgeetvlas
      181 aelsrliaeh eailiaiqdg deeqarsamr qhlknsqvry rsmlraar
//
LOCUS       WP_457578434             347 aa            linear   BCT 27-JAN-2026
DEFINITION  4-hydroxythreonine-4-phosphate dehydrogenase PdxA [Ensifer
            adhaerens].
ACCESSION   WP_457578434
VERSION     WP_457578434.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Sivaraman,J., Li,Y., Banks,J., Cane,D.E., Matte,A. and Cygler,M.
  TITLE     Crystal structure of Escherichia coli PdxA, an enzyme involved in
            the pyridoxal phosphate biosynthesis pathway
  JOURNAL   J Biol Chem 278 (44), 43682-43690 (2003)
   PUBMED   12896974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..347
                     /product="4-hydroxythreonine-4-phosphate dehydrogenase
                     PdxA"
                     /EC_number="1.1.1.262"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050570 - 4-hydroxythreonine-4-phosphate
                     dehydrogenase activity [Evidence IEA]"
                     /GO_function="GO:0050897 - cobalt ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0042823 - pyridoxal phosphate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36501
     Region          12..336
                     /region_name="pdxA"
                     /note="4-hydroxythreonine-4-phosphate dehydrogenase;
                     Reviewed; PRK00232"
                     /db_xref="CDD:234696"
ORIGIN      
        1 mttngvaang arpvialamg dpagispelt akllalsdir eaahiitigd rrildegari
       61 agvtldlaas tlegldavgt erhvfvdlgh ldpadvvrge atlaggtfat rnfrvalela
      121 hagkaeavcf tpfnkkamrf aypgyddeir fvsdvlnftg kvrefnvlek vwnarvtshi
      181 pikevadnls veailaelel tqsclkeagy seakiavagl nphagdggsf gmeeidiiep
      241 avekakargf nvdgpfpadt vfgralkegy navmtmyhdq gqiamkligf dkgvtmmggl
      301 pfplctpahg taydiagkgi advgasreal llavrmakkk aalkaaa
//
LOCUS       WP_457578447             561 aa            linear   BCT 27-JAN-2026
DEFINITION  Na/Pi cotransporter family protein [Ensifer adhaerens].
ACCESSION   WP_457578447
VERSION     WP_457578447.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Tenenhouse,H.S.
  TITLE     Recent advances in epithelial sodium-coupled phosphate transport
  JOURNAL   Curr Opin Nephrol Hypertens 8 (4), 407-414 (1999)
   PUBMED   10491734
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Takeda,E., Taketani,Y., Morita,K. and Miyamoto,K.
  TITLE     Sodium-dependent phosphate co-transporters
  JOURNAL   Int J Biochem Cell Biol 31 (3-4), 377-381 (1999)
   PUBMED   10224663
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Werner,A., Dehmelt,L. and Nalbant,P.
  TITLE     Na+-dependent phosphate cotransporters: the NaPi protein families
  JOURNAL   J Exp Biol 201 (Pt 23), 3135-3142 (1998)
   PUBMED   9808829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..561
                     /product="Na/Pi cotransporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005436 - sodium:phosphate symporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0044341 - sodium-dependent phosphate
                     transport [Evidence IEA]"
                     /calculated_mol_wt=58919
     Region          3..547
                     /region_name="NptA"
                     /note="Na+/phosphate symporter [Inorganic ion transport
                     and metabolism]; COG1283"
                     /db_xref="CDD:440894"
ORIGIN      
        1 mnsgtfvile llgrvalllw gvrmvrtgvm rgwgdrlqrf veerlsnrlt afgggvlata
       61 vlgsatamal ivaglagaga isaqtglavl lgadigsalv sglfasgssl agvlaplfll
      121 tgyiafsvsg efrprnagri lmglglmlma lkvivsatap lreatlfhdv lqavatepvl
      181 gflvgamlaw lfhstlavil lvasllmngs levagavpli lginfggglp avsatldqpp
      241 sarklpvanl fcrgllavsl lpfarqivdi agrlptdplh vavglhvtfn lvvaavflpl
      301 ssfvvnlver lvppapvvgd pltsprylds msletpaial snattetirm sellermfrm
      361 altslqagrl enlkellpvd arlgnymasv haylgqltqd glpagetsra heimlfasnl
      421 ehagdvikls ladrirakik qniqftvsqr aaiealsevi vaslrllpaa lssrdvaaas
      481 rlaaqkdrfr eledeivrrh lggehvetaa gardnalfid lvrdlhrins diaaagyplv
      541 qaagllsssr ilnvgavaga r
//
LOCUS       WP_457578448             576 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578448
VERSION     WP_457578448.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 576)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..576
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60936
     Region          12..569
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtslsisaps gsrllrsgfl lpailvaiva ilvvapllri lfttltpegm aawkavlasp
       61 lsanlwwrpl lntmilgfsv gagclliggf lawlvvltdv pgrrflglma slpymipsfa
      121 aalawgtlfr nsrlggsagf fetsglaipd wlawglipta ivliahyysl aytiiaaals
      181 svgadlveag qmagakrpri ffgiilpvvt paliaaaslt fagavanfaa pallglpvrm
      241 qtlstrlfgm ietgqnergf vlallliavs alflwfsdri vsgrkafitv tgkggrtkrf
      301 plgawrwplf aiaviigflt tvlpvlvlaa sslapqsgal fsnwtlhfwi gegggemaqg
      361 qagifrnpvl idaiwntirl glvvafttml lglglaytiv qrrgsllatl lsqlaflpll
      421 vpsiafaaay ialfgapigp lpslygtfal lviaasahnl pfavqsgrsv lgqisadiee
      481 sarltgagli rrlfaiifpl airglfagai lvfvkmvrdl slvvllftat spvlsmvayr
      541 flqfanaitl vilvvclaas fvahslqnrv qkwkap
//
LOCUS       WP_457578449             340 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578449
VERSION     WP_457578449.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..340
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36894
     Region          13..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtmgtaeprg qalainnlsl efptfsgavk alddvsisvg kaeivgivge sgcgksvttm
       61 aatgllpkgr yritggtvrl fghstlsmdd nqlqdlrgkv vstifqepmn alnptirigk
      121 qltdvimrhe eidlaearrv ardiladmli gepervmnly pfelsggmrq rvliamafsc
      181 npgliiadep ttaldvtvqa vilrliqnra rrtgtsvifi shnvavvsql cdrlyvmyag
      241 rivehgatrt vletpqhpyt qallrclper vapkqeleai pgavpnllhp pagcyfqprc
      301 keaveqcrtr spqlvgasgq qvacwrrgva telveqggrq
//
LOCUS       WP_457578450             513 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578450
VERSION     WP_457578450.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 513)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 513)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..513
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55630
     Region          27..494
                     /region_name="PBP2_NikA_DppA_OppA_like_7"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08512"
                     /db_xref="CDD:173877"
ORIGIN      
        1 mngskwksig iallltstpl sgaiaaqdvl vlaraedppt adpgieisns gytltyaaye
       61 rlvaykgast evgpelaesw taddaglvwt fkiaaghkfd dgspvdaaav kfsfdrlmkl
      121 kagpsdafpv lkevevvdpq tvkfhlsapf apfistlavs gaaiinpkvm ehekdgdmak
      181 awlaehtags gpyriaswer nqsivldsne hyagaapalk qvvlrivgdv sarrlqltng
      241 dadiieqipl dqaealqkda svvvesnpsm yvnyiyinnr qpplddakvr qaisyavdyq
      301 giidgimlgq akqmrgavps gmwghdpqgf qysydiekak allaesgkgd ihltytfsqa
      361 dpawepvgla lqaslaeigv kldlqavadt tkrelvangk fdmapgawtp dfadpymfmn
      421 ywfdagkmgg pgnrsfynns kvtglvqeaa sivdeakrka lyieaqklst ddapylyime
      481 kndifarraa vkgyvynpml iqvynfgtms kte
//
LOCUS       WP_457578452             412 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578452
VERSION     WP_457578452.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..412
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44272
     Region          5..407
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mttsivlgag mvgvstalal qetghqvvli drkapgrets ygnagiiqte avepyafprs
       61 laeivrvglk rgndtdwrlg dmprlagplw ryftqsapat yartvaaysk lalrasddha
      121 rfiepanagd livregwrav yrspgkldaa vataerlkre ygvpsdvlts delaasepal
      181 ksrlagavhw tspwtcrdpg dlvsryaalf varggkvaqg damslhqtga gwrvlseggn
      241 ltaenavval gpwspmllar fgyrvpmvfk rgyhwhfggk egprismldi dssaliapmn
      301 agwrvltgah laplgtapas rqirhavsaa rtlfalrdpi eaapwsgtrp cmpdmlpvvg
      361 pcrhkglwfh fghghqgftl gpttalllae qvagnrnnpl alpllpstrd wa
//
LOCUS       WP_457578454             331 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578454
VERSION     WP_457578454.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..331
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34888
     Region          4..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..284
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mevrdleafl avmstgsitg aarlldrsqs qvtrliqdle tslgfalfer ngpriaptdk
       61 giafhedaer fvsgighlrn rakaiagkep epieiaatpa fasgiipial aalpehllph
      121 tinlrsmpae aavqsvfart adfcvtslpa dqpgldvqgf fegrcvaava phdplaakdv
      181 isiadlagrt lvtmsnpfrl rhsvdevlna agvrpnriia tnaannavqv aslglgvaii
      241 epatayglqs apivvrpldv qipflwails agsrplsagv rdliqriaqi asermpdltv
      301 hdpkqmaria ersfagrnag ngappdnpaa k
//
LOCUS       WP_457578457             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578457
VERSION     WP_457578457.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39235
     Region          1..356
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqpvvqfeni rksfgsfvav dnlnlnierg kfvtllgpsg cgksttlrml ggfetptegr
       61 illsgrdvtm vppnrrnvni vfqdyalfph msvakniafg lelkgvdnrq iqrrvselle
      121 lvqlqdfagr lpselsggqr qrvalmrala pdpdvlllde plsaldaklr qtmqielkai
      181 qeqtgktfmf vthdqeealt msdtivvmnn grieqmgdpa tlykrpgsaf vaiflgetnl
      241 lhsdvvgtda geaavrwngm tikasagals pkagdaiyvv lrpeaiqcsa qepgvanrvk
      301 grirqrvfkg nhtslkveig eghllnalvh pseveglsrd diwvgwssea ttliparnaa
//
LOCUS       WP_457578458             264 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578458
VERSION     WP_457578458.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28749
     Region          8..264
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mralfhdwpg lalksfywlf vlylflplsl mvavslkdas fisfplgnlt idwyakvikd
       61 kqfldaclyt imiaaattai atvigvwiam ligslrgaaq yvafavaclp avvpgmisai
      121 slrifittid lptgtvaiil ghvvhavpfv vvmvltrlrs mpgnlvdaar dlgadsivtf
      181 frvtlpylgp aifggmifcl llssddfvrt fflggyrptl pmlifarvqs gmspeinvma
      241 tlvlvvtavv glyaeyltrr srir
//
LOCUS       WP_457578451             485 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Ensifer adhaerens].
ACCESSION   WP_457578451
VERSION     WP_457578451.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 485)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..485
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52434
     Region          5..477
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 mklfiagldt etntfspmqt gieafrenli aygdatgkpl nccssqmfvw rnaaqekgwd
       61 vveslcavae pggrttravy esfratildd lkaampvsav mlalhgacva dgyddvegdl
      121 lahvrqvvgp dvpvaaeldl hchitdrmla natiistyke yphtdieeva eqlfrlvert
      181 lagevkpamg mhdcrmintf hphraplrgi vdrmkamegq dgvlsvsfgh gfpwgdvedv
      241 gakmlvvtdn dpekaarvar sfareifear eqmrgdylgi daaldravaa tsgpivladv
      301 sdnagggapg dstfilrrii ergiedvasc lywdpiavrm creagegatl alriggkvgp
      361 asgdpldltv tvrrvasgit qrfgptplai gdavwvssgs idivintvrt qtfhpecmta
      421 lgldpaqkki vvvkssnhfr agfepiardi hyvsapgalq ptfedlaftk lkrpywprva
      481 npfae
//
LOCUS       WP_457578459             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578459
VERSION     WP_457578459.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35701
     Region          44..326
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mavgthtagg glpvraahmk ystgvsrvin splyrytlga vaerrygril llagvpvvwm
       61 lmmhigpiye mlrisllssy ppqpgvgaef tfdnyalffs eklywmpllr sfiyasiata
      121 vtlvvvypva yyvakvvatg nrsralllll apfwageiir ifsvimllan rgavnvllre
      181 iglterpiqm lytsfsisfg lvymvclyml lplysaieki pkslldasad lgagpftrfr
      241 riilplsrdg ivsgcslvfl tcmgvfaapi llggpttsmf setissffhg assrwpagaa
      301 famimlaasl vtvglfmrvv ggskqrtf
//
LOCUS       WP_457578460             180 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578460
VERSION     WP_457578460.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..180
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19644
     Region          1..171
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mptapllvda fseahipeml dwfsslealv qwggpglsfp leaaqleaml agtkgaeper
       61 lmfagvvdgk laghaqvald wangvgrlar vainprmrgq glaqpfvsev trrffadlaf
      121 erlelnvytf neaairtyrs lgfyeegvrr ssakvgdarw dtaiygmlrg ewvervgaaq
//
LOCUS       WP_457578462             670 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-galactosidase [Ensifer adhaerens].
ACCESSION   WP_457578462
VERSION     WP_457578462.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..670
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=75526
     Region          18..630
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          625..670
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mhmpltrsnr fnakeqqtdm lelgvcyype qwprekweed arrmvelgla wvrigefawa
       61 kieprsgefh wewlddaiev lgkaglkvil gtptaappkw lidrypdilp vdvkgvvrkf
      121 garrhycfss rryrieaari seamaerygk nafvhawqtd neygdhdtiy sysdealraf
      181 rewlearygt vdelnrawgt afwamnylsf develpnnlv eepspthivd yirfssdqvk
      241 sfnkaqvdii rkhspgrpvt hnfmsqntdf dhykvgedid iaswdvypmg gllngrlsse
      301 dkgrylrvgd pdqpafnhdl yravgngrvw vmeqqpgpvn washnqspad gmvrlwtwla
      361 yahgvdmvsy frwrqvpfaq eqfhaglllp nseadqgyle vaqvaeemkr lpkgerreka
      421 kvailldyns rwatralpqg rtylasqial dwystvarlg vdvdiigqhl dlegyqlvla
      481 pdlvipeqaf veklaasgak vlfgprsgsk tedmhipegl ppgplaalid vsvarveslp
      541 efhgesvlyg netypagvwr etvrtnetvl atfegdyrng apalvgndka rymatgarge
      601 lldkvigdal gwasvealad lgdlritrrg kltfafnygk tavdvpasag atfhvggrkl
      661 gpvdvaiwse
//
LOCUS       WP_457578463             409 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578463
VERSION     WP_457578463.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..409
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44974
     Region          27..403
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(135,137,263,265,295..297,337)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mlnrksiigs lmvlaiagta taraeetlrf atwdtdesla iqqeiakkfe ekhpgvkvqv
       61 epyadgydqk liaafgagnp pdvmymwnfp qyytslkpld dliakdaaev kpddfpkglm
      121 ntvrvegkty gmpsgfttqv vfynkdmfar agveepkdgw twddlrakaa kfrdepnkvy
      181 gfavdakpdp ydfeqflwsn gtkyisddgk kidgymnsda aaqvldmfgd makkqeaitl
      241 nlgddtsgst lfkggkiamf qsamwsksgi dasgikygva plpkfgdkta hsalgvsais
      301 iakdaahpdl awefvkffss peavamrind lpvstsvaee kgmtkdpiyk pffdilatsn
      361 tethaflkna nwgkvqdnla raieatmidq gnakqhldea varskrlik
//
LOCUS       WP_457578465             514 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578465
VERSION     WP_457578465.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 514)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 514)
  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 514)
  AUTHORS   ter Beek,J., 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 514)
  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   6  (residues 1 to 514)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 514)
  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 10170708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..514
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56099
     Region          22..497
                     /region_name="PBP2_NikA_DppA_OppA_like_16"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08502"
                     /db_xref="CDD:173867"
ORIGIN      
        1 mktillagtm lmsaialgha rdltvaqssd irsnepgvnr dgntdsvifh iveglvgyae
       61 ngevkpllak sfevspdglt ytfklrddlk fhngkaltae dvvwnwnrym kpetkwtcag
      121 dfdgsksikv tsvaaadast vtmsiekpsa vflglmarpe cgytgivsqd svgadgayta
      181 pigtgpfkwa ewkkgeyvrl eknadyvspa ndgkpdgmvg skrplvdgik fmvipdastv
      241 ktgllsgald taevsadlia efkdsdtmql ivkrnngknl lyfqtrdkil snvavrrama
      301 ealdldqlva avsngtgean asmvsadsif ysdvqkkkip mdlekakknl adagyngepi
      361 tiiankrgnv psfpaavvaq ammqqvglnv qievldyatq vdrrrsgnyq visqsvsprl
      421 dpalmysfyv gnkdknaslm wdnpkavelm kaayveadqa krqaifdefh qlmldevpgi
      481 fmydmvdiwg atkklhgqpv wqsntrlwev tldd
//
LOCUS       WP_457578467             162 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578467
VERSION     WP_457578467.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..162
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17284
     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 mfqaatidtg dkrafyaela qqlesllhge pnlianaant salmfqtmps lnwagfyfle
       61 tddelvlgpf qgkpacvria vgrgvcgtav kearsilved vhafpghiac daasrselvv
      121 pvrrdgrvig vidldspepa rfdrddqigi eklaaifaaa ia
//
LOCUS       WP_457578469             208 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578469
VERSION     WP_457578469.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..208
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23244
     Region          24..200
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 maltevkrge gaaislferi arhplaqaer laeamqvrsv ragetvfhqd ephpyvyvie
       61 rglvkltylr angeewiksf aiegrffasl salvpagras fsaiaveesr leripfvtlq
      121 aladtdlgws rmirsalmml aerkerrerq fltldpeery rallveepev varvpqkdla
      181 gylgitpvgl sriakrvrae adttvnpg
//
LOCUS       WP_457578471             302 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578471
VERSION     WP_457578471.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..302
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33545
     Region          9..297
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mkkfsllstr agaiflapat alvgvfvivp ffwvifvsft nrtllgrtav dpdfvglqny
       61 falfnpatff trgqfgfsli ltiqfvllsa ligqallgll lawlsqtvtp tlksflqtav
      121 iaawilpevv igfawfafld ydngtlnmil rglglppgdw llqqpfwviv ffntwrgaaf
      181 smmlfnsafq sippsyfqaa dvagatswqk lrdialplir ghvvtdlili tmwtfnvftp
      241 fllthggpsy rteilsiyty riafkdfefg kgaavgvvim linlafalvy lrlahkkpve
      301 ae
//
LOCUS       WP_457578474             239 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578474
VERSION     WP_457578474.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..239
                     /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=26760
     Region          1..>222
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 marsdrlfrl lqalrtlpsp vtaarlaeet gvslrslyrd idslraagav idgergfgyr
       61 ltedialppq tftrleieal vlglaevqhm gepdlaaaar avlskitatl pdrlqrqalh
      121 avsqvyrfdr rgpptvdvsl lreaswqera viigyvdalg qrtdrqvlpl aivylervlv
      181 llawcclrqd yrkfrvdriv dvtmteesfr prrvpmlrdf vaylnagape tskmtlsgq
//
LOCUS       WP_457578476             270 aa            linear   BCT 27-JAN-2026
DEFINITION  anti-sigma factor family protein [Ensifer adhaerens].
ACCESSION   WP_457578476
VERSION     WP_457578476.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..270
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27247
     Region          1..>71
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msdtefsdei lmafadgeld eatmrrveaa letddelmar vamfmetraa asealkpvld
       61 epvpdelvak vramaaaagd aaraadapaa agdnvvafrr padqpaspng spsrflmama
      121 asllvvvgga ggyllrgggl adpggvpgam qvagtvgpal saildkaasg devavgegqg
      181 tvrlvsafel gsgqlcreye laqpgepglv svacrkastw qtrlavakpe ggdgyapass
      241 letvdaflts igagqpldad aekkalsgrk
//
LOCUS       WP_457578478             390 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerate kinase family protein [Ensifer adhaerens].
ACCESSION   WP_457578478
VERSION     WP_457578478.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ornston,M.K. and Ornston,L.N.
  TITLE     Two forms of D-glycerate kinase in Escherichia coli
  JOURNAL   J Bacteriol 97 (3), 1227-1233 (1969)
   PUBMED   4887503
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Doughty,C.C., Hayashi,J.A. and Guenther,H.L.
  TITLE     Purification and properties of D-glycerate 3-kinase from
            Escherichia coli
  JOURNAL   J Biol Chem 241 (3), 568-572 (1966)
   PUBMED   5325263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..390
                     /product="glycerate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0031388 - organic acid phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39525
     Region          7..377
                     /region_name="Gly_kinase"
                     /note="Glycerate kinase family; pfam02595"
                     /db_xref="CDD:460609"
ORIGIN      
        1 msltilvaps gfkeslsaee aadciekgvl racpsaevlk vpmvdggegf tkalvaitgg
       61 slheltvtgp lgepvashfg flggqserta viemaaaagl rlvprdrrnp clttsygvge
      121 liraaldaga rrillgcgds gindggagma aalgvklldr kgkplapgga alaslaridi
      181 sgrdprlaev ridaavnwhn vllgargvar vfgpqkgatp eqvellaaam etyaaaieta
      241 tgiavgdvag agasgglgaa vmgllggalh prydivmryl dldsmiarad lvitaegsld
      301 gqtpfgkvpa evghrakeag rpvialagti gkgvtlnfeh gidafasilk apctlddain
      361 aapkllvraa edavrmvrvg mllnerglaa
//
LOCUS       WP_457578479             492 aa            linear   BCT 27-JAN-2026
DEFINITION  SLC13 family permease [Ensifer adhaerens].
ACCESSION   WP_457578479
VERSION     WP_457578479.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..492
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50866
     Region          116..486
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mtispviase kdlvtlnaav aeridghmpv sqvrllvgam lvafaavlif laadglalpm
       61 rlslmvfatt licwtifdlp etpvalagaa alavtgavge eavyaalgnd ivwlmmaasv
      121 iaavlqasgl verlafrlla rfrdvsrlfw vvtltifvta fvipstsara aifmpvflgl
      181 astigrpgvt ralallfpsv illsaaaslt gagahlvavd firrsggeap gflgwallaa
      241 pfalltslla cglilrffld dadrnsrfdl paaptekrpf sardkailav taaivaalat
      301 sdlhgialpv valvgalvla sekisgmpfr kalkgvewnl llflagtlvi geallstgta
      361 tepadrliga fgqigkppaw lvvllaiava tfahivlasr taratvlipa valplagfgv
      421 spaslimvta igsgfcqtlm vsakpvalfg gmeppafsps dllrlalmla lpfiallalf
      481 alviwpavgl et
//
LOCUS       WP_457578480             278 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Ensifer adhaerens].
ACCESSION   WP_457578480
VERSION     WP_457578480.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..278
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29789
     Region          154..276
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtyktilavv gvdhsaddlr aaaqvcasan ahlsllivkl aasppigdfa aaisidwlne
       61 rqrevdkles cvasatdvlt regisfsvet kyteaawadd eigeraryad ltlvgdglil
      121 dpelrsrtid gtlfnsarpv lvlpkgkpar ldprtvvlaw nsrleaarav realdllkga
      181 kivhvtmvdp rsaygkngee pgadiagyla rhgvsvsver lpsgghrvdd vinrfasdva
      241 adlivmgayg hsrmrervfg gvtrsmlena vvpvlmah
//
LOCUS       WP_457578481             414 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Ensifer adhaerens].
ACCESSION   WP_457578481
VERSION     WP_457578481.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..414
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46049
     Region          8..398
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtqlpkqtlr vgfvgsgfia hfhmksmigv rnvevtgvfs rkaenrekfa nevealglgs
       61 crthesleal ltaddvdavw ilspnytrid vmrslhkavk dgrskvfava cekplartva
      121 earemlslae daglnhgyle nqvfctpvlr gkeiiwrraa tttgrpylar aaeehsgphe
      181 pwfwqgdkqg ggvlsdmmch svevaryllt apgaprnslk ikavngtvan lkwtrphyae
      241 qlrnrfgnev dyrnrpsedf aratvtledq dgnelmieat tswayvgagl riqlellgpe
      301 yaleynslst glkifmsrev kgsegedlve kqnaeqglmp vledeagvyg ytdenrhmve
      361 cfrkgekple tfedglavve mlmglyrsae inatlnfpap elehyvpvva rrga
//
LOCUS       WP_457578482             339 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457578482
VERSION     WP_457578482.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 339)
  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   2  (residues 1 to 339)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..339
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36382
     Region          4..338
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msdrpkikdi aeragvsvat vsralsgssl vtdetrqrin alarelnyrp nvsarnlrtr
       61 rsmsvllvvr dvgnpfylei lkgveatare agyavlmgnt endpdrevey fnmlrdghad
      121 gmilmtgklp ppepgesadl shlpvviale miegsgfphv qidnvaaaea avdhlialgh
      181 rriahiagpl pevmalrrrd gyraamkaag lavpegyevr gdyllesgea cvsdlfalpe
      241 pptaifaand emaygaihal rrlgrdvpgd vsvvgfddly lskafypplt tvsqpradig
      301 rtamsqllnv lsdgdaaaep aivlpttlni rgstapprk
//
LOCUS       WP_457578483             501 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578483
VERSION     WP_457578483.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..501
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=53540
     Region          4..501
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 msklrlngvs kaygatlalr rgdleiaage vhvlmgsngs gkstlckiia gsvrpdggqi
       61 lindkrvtis gpqaaraagi gifyqelsla shrsveenic lsalpvkagl fidraamkar
      121 aaryialfse vsgegfhaea lvgnlradqr qlveimkala seapilifde ptsaldraqv
      181 drffeilrdl kgqgrgiifi shrmdeitai gdrvtiirdg etietlklse tdpatvirlm
      241 vggasdmpaa rssapavvet gaqtaisvrs lsgkgfrdvs fevakgeilg lgglhgqgqs
      301 allraifgas tvssgevtig gerydaknpr dairrgcayv sgdrgrdgvi sgrpiienvt
      361 pihylrdrlm larpsslknk ampaleamht kfaslfhpin slsggnqqkv iiarwlidrp
      421 dvlllddptk gidlqakadl falirqlaae glgillysse daellgnanr ilvfnggsvt
      481 religddrtr ynlyqaayea a
//
LOCUS       WP_457578484             349 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Ensifer adhaerens].
ACCESSION   WP_457578484
VERSION     WP_457578484.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..349
                     /product="TonB-dependent receptor"
                     /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]"
                     /calculated_mol_wt=38502
     Region          <25..349
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 msralnennr gyfhpgrlgf rsymtniynp iyvpsdwvnt gglprsndlh afsdllatsv
       61 aisdtlsfae drfqltvggr yqemrvrgyn trpgavplgq qtyyyeegrf spavaalvnv
      121 tdsfsvygny vealtegpsa psnalnsdqi fppvvskqke igfkydlgev mlgaalfeir
      181 qpnglttggv favdglqvnr gielsaygep vdgvrllggi tfmdakldka ensrtgerfd
      241 gnrvpgvptt aislygeydt pwvedltltg rlvytgstyy dqrntqkvsd wtrvdlgary
      301 sferenakpv eiratvqnvf denywassar gflaagaprt fmvstafef
//
LOCUS       WP_457578485             391 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Ensifer adhaerens].
ACCESSION   WP_457578485
VERSION     WP_457578485.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Koebnik,R.
  TITLE     TonB-dependent trans-envelope signalling: the exception or the
            rule?
  JOURNAL   Trends Microbiol 13 (8), 343-347 (2005)
   PUBMED   15993072
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Nikaido,H.
  TITLE     Molecular basis of bacterial outer membrane permeability revisited
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 593-656 (2003)
   PUBMED   14665678
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..391
                     /product="TonB-dependent receptor"
                     /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]"
                     /calculated_mol_wt=41777
     Region          98..>385
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 margrfnsvs rrrakvvlag vsllamsava asaqearktn rveslaqaer ssggatqlap
       61 ivavgqaggq ppetgtigqp sapyaggqma tgarlgalgn rpvketpfsv tsytdklird
      121 qqartvadvt lndpsvrmda pafserdsff irgfsvtnld taydglfyit nprrsplegi
      181 ervevlkgps alvnggvgrv ggtinlvpkr atdepltrlt ttymsdsqlw shldvgrrfg
      241 pegewgvrfn gsyrggdtal dhneneigvl slgldyrgdr vrasldlnhs kqninapasl
      301 fnaaapgiki peapdgrint snpfeyhdse hnmvagrvef dvlenttvya aggisryred
      361 flstsytiqn pngdalaefg ynpqeiqggl g
//
LOCUS       WP_457578487             224 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457578487
VERSION     WP_457578487.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..224
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24687
     Region          1..203
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrlllvedel emaaalsaal srydmildha psidhamaal asqvhdgiil drqlpdgdgl
       61 sliprvralr sgipvivlta rsaidervrg ldmgaddyla kpfaveella riralmrrsp
      121 diapitarig qlifdfegrq arvdgrvldl prrellvlea larrqgrtvq rstleesvyg
      181 yddeiqsnsl dahvsrlrrk lsetaagvei hsirgvgyll rpsp
//
LOCUS       WP_457578491             362 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578491
VERSION     WP_457578491.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38975
     Region          1..359
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mskaaeidiv svskmygatt avhsislkip agsyccflgp sgcgktstlr miaghesiss
       61 gdlrlgnivv tdfpparrst ammfqsyalf phldlidnva fslkmkgvtr dirrakaldi
      121 lklmqmeayg trrpaqlsgg qqqrvalara litepealll deplsaldpf lkirmraelk
      181 klqktlgitf vhvthsqeea maladlivvm nngrieqaaa prtvferpat afvarfmgdh
      241 nvlsgkvrai sdnvvemeta ggqvftvrdi aqqvgrpidi girtdrvrla ppsekglgfq
      301 avvsnieyrg asvkltatga gsddftvivs dadhfrkpva vgdavslswt ledvvplgrl
      361 sa
//
LOCUS       WP_457578499             323 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578499
VERSION     WP_457578499.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34989
     Region          2..319
                     /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 mhtvaivafe gispfhlsvp civfgddllk lgapryrlvi agektgtvrt msgfsieveh
       61 dlaslteadt iivpawndag nrpsesllea lrdahargar lvglclgtfv laeaglldgr
      121 aasthwawad eferaypqva lnrnalylde gdiltsagta aaidcclhiv rsdhgaeian
      181 riarrlvvap hrhgdqaqyi eaplpapgsg dplsatitwa iehldeplsl erladhagms
      241 lrsftrhfrk ktgttftqwv laqrlavaqr lletgscsvd hvaemagfgs tvsfrqhftr
      301 alsispasyr rqfrnrpara sap
//
LOCUS       WP_457578488             208 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane protein [Ensifer adhaerens].
ACCESSION   WP_457578488
VERSION     WP_457578488.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..208
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21673
     Region          67..208
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mrqsskfsiw sgltllalcg aqpsqsadfs aptyqdppaf swsgayvgah gglgftgspn
       61 pfadrngval gvqagynmqa gpgivgaeie gsylgdtehk vnggklkekw rgaikakagl
      121 tfdqtlvygt agyamtsykk gsdvrndvgf kggyllgagv eqafagglsa kleynyittp
      181 dvrthtssgs sekdinshvi kaginmrf
//
LOCUS       WP_457578500             252 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Ensifer adhaerens].
ACCESSION   WP_457578500
VERSION     WP_457578500.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..252
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27360
     Region          104..240
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mteahepsss tadhktgitl trrslvvgva slfvtgcata rptpavvpaa vtpvrpsacr
       61 tvppmyyamp deqfpipevk iaevdpkfwr qevdyptser pgtlivdtpa kylyhvlpgg
      121 ramrygigvg regfawsgra ivaykrkwpr wtppdemvar qpklqpysia nggmppgikn
      181 plgaralyih kdgkdtlyri hgspeafsig kavssgcirl lnqdvvylhd qvrdgstivv
      241 ipdptkgdma ig
//
LOCUS       WP_457578505             561 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578505
VERSION     WP_457578505.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 561)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..561
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62416
     Region          <275..533
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mgvdwagpva avtrrnvlrl fsagvmanvl sgcrhdwppa aacelpypiv dvhchffnaa
       61 dvpveglvry valreklpea klsadplqsk rlenalvvfl vtalgdvapk akaedailkk
      121 rvprpsdaef erqkdeqlri avkqlvalag eqrasltars gaetpdyqgl leqiggtpgl
      181 pqglqrrsgs veetdvdala saakaheqig nylsfvrlmq dyrenlaety arifaskcrf
      241 smitpsildf eksiggrasp qhdqidvmde iqqlvikrhg ihmhsfvgfd phreaqkrgs
      301 slenvryaim ekgfigvkiy ppmgfkawgn adpaidaalk rlydwcrdns vpimahaens
      361 igagcgygnm aspaywkkll dtnryndlri nlahfgafde virpgaptgv mvscaqdkfs
      421 gpptwediig etighgrrpn lfadlsylse lvtdntpglh ekiralvdkw lrdydpdarh
      481 lmfgtdwsmm alekdynayv priaqqlkea nvseedqqni fwknasrylg ldrpgptrqr
      541 latycrkrgl daswlsqlei a
//
LOCUS       WP_457578497             503 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578497
VERSION     WP_457578497.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..503
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=54237
     Region          6..500
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mfgstsdtil eidnvtksfg qvaalkgmrl kvrrgrvhtl lgengagkst lmkilagvhe
       61 atsgeialdg rpyqprnpqd aaalglaivf qelslcsnlt vaenilatre prrfgfindk
      121 elvvraraiv adlglpidvs ekvgnlsiaq rqlveiakgl sheakvvild eptsslsdse
      181 aeilfdiiar lksrgvaviy ishrmeeimr lsdditvird geyvsthdrd dvtiealial
      241 mvgrrmdeiy ppaaheqkpd atpvlsvddl trdgefenis fdirpggilg ffglvgsgrs
      301 evmnalfgmr aatgtvrfeg kpvrfrspae aiargigfvt enrkeeglvl shsvgwnism
      361 aalsdftgpl gftrsraert aaaqevgrla ikthsldtps gslsggnqqk ivlakwlltr
      421 pkvlildept rgvdvgakfe iykiirqlaa egtailliss elpevlgmsd rvvvmhegvi
      481 gatlsgaeln petimahatg fks
//
LOCUS       WP_457578508             456 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457578508
VERSION     WP_457578508.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 456)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 456)
  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 456)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..456
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49436
     Region          153..451
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msgrashsfk wrlvgwlvlf etvatlvvia iavgllwvtg ylidgyengn vdvlkdaitr
       61 kadgglelqe tpelqrlrqq agkiwfivrd rqghrlsegt vpeefafava glermndarf
      121 rlspdknarp eavvkwlesp agmvqvfsgt egqltlgrll lsttgaflsi fvpmllllaf
      181 atvvvtpivv rrmlsglsha ashaahieyd qrgiqmpvtg vpneflplvt avndaltrld
      241 dgytrhkrfl aqaahelrtp vailgarias lppgpdktrl nedvtrlsil agqlldlerl
      301 daendefrpv dlaalaervi valaplgfga gyemtfeadq rpvmvtgdea sleraltnlv
      361 qnaidhggrr gtitvkvdpq gvievcddgd giprsetdri fepfqrlrkd gkgaglglnl
      421 vqkivhlhgg yvdvsrsasg gacmrivlpl aaavta
//
LOCUS       WP_457578510             239 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578510
VERSION     WP_457578510.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..239
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25280
     Region          156..232
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mplfspeitd fwnasfagdv lasadrftvv vnpdldeesp amvlhtaeng vivalspalg
       61 aalssaagqv lteaplrqgl cdagivlnga dnlfyftead kavllrensg ahvraltakd
      121 aaafalfqgs aseedldaay veldhwlvyg afdgdrlvca asmypwqerq iadlgvltlv
      181 sdrgkghark vvraisraal ekgyqpqyrc qldnhasval agavgvtlfg qweapsedg
//
LOCUS       WP_457578512             353 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578512
VERSION     WP_457578512.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..353
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37238
     Region          1..353
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mpllqfipaa afllslaasa qaddvgvrei dvaapkrerq lavtvwypak aggepvlvgd
       61 nrifegspaa knaplregry plvvlshgsg grveamswla aelaaagfiv agpnhpgtts
      121 gdstpantpk lwertadlsa lidtftrdpq wsaaidpgri avlgfslggs tameisgara
      181 sleayagycg sygkwdcawf vggrgyvddt pvdvdkldlr tvdkarfeqs nrdprikgav
      241 lvdpglaqay vedslkaiai pmhfinlgsk etiplavase plaaltpkgs yatvagadhf
      301 sflpickdga aellesfgev dpicgtterp radihaeisk ltrealqkil anr
//
LOCUS       WP_457578513             107 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Ensifer adhaerens].
ACCESSION   WP_457578513
VERSION     WP_457578513.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..107
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12285
     Region          1..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpyhstpldl afhalsdptr ravvsrladg empvsvlaep fdmalpsfaq hlkvledcgl
       61 iasekrgrsr wcrlergrfe eaatwmever rrwaerldrl eayldkt
//
LOCUS       WP_457578521             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578521
VERSION     WP_457578521.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..330
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34612
     Region          7..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtlvsqttet ggqntplkfl ktypmeiila alviflifva pgfastsnvl nvlrtvsmlg
       61 iiafgmtavi isgeidlsvg agaalagciv awfadrftdt fgdwgavtvg favalllgfs
      121 lgyltgrlrq wfnvptfitt lalfaalrgv anlitggfpm ssfplgfdfl gggylfgipf
      181 pvyifaltfa amhflmkyts fgrevyavgg nmeaarlsgi diwkvkaltl gltgaltavs
      241 gtliasqiga gtgttatgme ldviaaviig gtslfggkgr iwgtligvlf lgcisngmtl
      301 mnvseywqyv vrggiilgav llnqvlervr
//
LOCUS       WP_457578517             259 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578517
VERSION     WP_457578517.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..259
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28110
     Region          41..246
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mttrrqalgl laaaallpla priafsaapl stvanagyyr frfgkfevta lsdgtlalpm
       61 tkiyqnepeg elqrrldenf lgkephlsin aylvndgerl vlidagsgsl lgiaagkllr
      121 hltasgyrad qvdavilthv hadhsgglti dgkaqfpnae ihlaereyry wieregvtal
      181 teaqktdfqr ahdalapyia agkvkrfadd advlpnlgst lraghtpghs aivlkadngq
      241 rlvfwggrhs rrlhpvrha
//
LOCUS       WP_457578523             295 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578523
VERSION     WP_457578523.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..295
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32442
     Region          30..295
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mssfpdgaal pphwhgeapv kiarslftgg llaytglffa fiyiplvvia vysfnanpvn
       61 mmtwtgftte wyaqvlgfkt kvsesalyie stgqllqavw nslviaastt aiatvfgtai
      121 aialyrfefv gqrfyrvvmf mpmlmpdivl gialliffvn sgirlgltti iigqctflis
      181 yvfivvsarl agmdrtleha sadlganewm tfrrvvlpql fpaivggall afiismddlv
      241 ityfiagvdv ttlpmfifsm lrrgikpein aiammmltfs fvvaslglyl rsrqk
//
LOCUS       WP_457578518             286 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578518
VERSION     WP_457578518.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..286
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30250
     Region          11..279
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 msapataaqp sliskfigsr nltigatvtv ilvamalvsy vwtpysptam nfrdklqgps
       61 lahwfgtdnf grdilsmimv garnsisvsi vavlvgagig vplgawaaar ggfvdglvmr
      121 msdlafafpa lltaviitai fgpgatnami aigifnipvf arvtrgasmg lwkreyvqaa
      181 rcagrgdvai tflhilpnin hvllvqvtiq falaivaeag lsyvglgtqp pmpswgkmln
      241 daqtfiyqap wlaifpglai tfavlglnll gdglrdildp rvrrqr
//
LOCUS       WP_457578534             297 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578534
VERSION     WP_457578534.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32336
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdrldamgvv iaviengsls aasrhlkvpl atisrkvsel eahlgaqlit rtnrwiqlte
       61 agrvyveaak eilarveeae rvaageysti kgdltvsapi vfgrlhvlpv vvdflkahpe
      121 vdmrlalgdr fanlvddhid valrignlpd snlvatkigt vrrvvyaspd yvarhgvlrh
      181 pseladhdci tfenvtaahv wrfldggrel aapirsrliv ntaesavdaa isglgltrvl
      241 syqvarqvad gllvplledf ehpalpvqlv ylpqglvpmk lrafvdfaap rlravlr
//
LOCUS       WP_457578529             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578529
VERSION     WP_457578529.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39118
     Region          1..357
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 manivcsnvd kqygavdvik dfnldvadhe fivflgpsgc gkstllrmia gledisdgiv
       61 siggravndl pprdrgvamv fqnyalyphm tiydniafgl krmkvpkaei dtriravsat
      121 lglepylark ptelsggqqq rvaiaramik tprvflfdep lsnldaklrn hmrveiarlh
      181 qklktttiyv thdqleamtl adrivlmkgg aieqvgtpae iyerprtlfv agfigtpnmn
      241 fidvtaekte ggwllrsagg sfaisddrft lrhgqtlvlg irpadlapae sglnriegia
      301 dlvefhgnda lvtflfagke igalvkasgc prpgeavsft iepnglhlfd resglsvlst
//
LOCUS       WP_457578535             362 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457578535
VERSION     WP_457578535.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..362
                     /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=39990
     Region          15..360
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mkpeddarsv desayiasvr ratlwlgfly wfveflissi lwailgidpi msapgklllm
       61 scgmvfsygi aaamfgvrhq hialkivvgf ttalmaaian tgvdfllylf ivrpdpitpd
      121 wtsigytlvy smatfvgwsf ffvallysfe lrererrlai treealaaqm ralryqvnph
      181 flfntlnsit glieegqpla atrmvmslsn flrttleldp lhdvrladel alqagylhie
      241 gerycdrmrl rmdidtgled alvpslilqp lienavkhgv srspdqveiv isaakvghal
      301 eisvendiaa apeterrpgt giglknvadr vqarfpgvga cvsglvtpgr fraaitmplr
      361 la
//
LOCUS       WP_457578536             394 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457578536
VERSION     WP_457578536.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..394
                     /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=42840
     Region          24..339
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mvrghetvlp deagyaasvr ratlflglly qfmqfvisst lwaflgydpi aiapitlilm
       61 lngtlmsyam avalfrfrgr silfklllgs alalvaaain asvdllshgl iehgdpgpin
      121 wtnvgytliy cmalfhgwaf lyiallanye lrererrlav treealtaqm ralryqvnph
      181 flfntlnsia glieegastt arrmvlslss flrttleldp mqdvcladel alqlgylnie
      241 gerfsdrmrv kldiapgleq alvpslilqp lienaikhgv ggsigvveiv iraarqgetl
      301 elsvendman epprpankpa gtgtglrnva drikarfpev gafisglvap hrfraaigli
      361 aalrpttagk grksgpfckp ldladerqst svag
//
LOCUS       WP_457578537             254 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578537
VERSION     WP_457578537.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..254
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26142
     Region          8..236
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 miqlnetvav vtgagrglga slayalaeag calvlcgrsq salkdvakpi alnlgrrvqt
       61 valdladaks vaaavegiks engridilvn ngamwledsd edhpddavlg vvnaavtgtf
      121 lftqgllpll ahsprpdivt igsisglpna apqtvsvpfy aakraqaala dglrqklagt
      181 ptrsivvhpp yiedispldg aweaagsrrk geaatnrdia eavlfaltrp rhvtlsitvd
      241 addgglypsp arsa
//
LOCUS       WP_457578538             245 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578538
VERSION     WP_457578538.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..245
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27331
     Region          24..219
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mhsvsepift sgfplgssag lvtalewlgq pyrltrvdml gemrtdayer fngrvetpal
       61 vtdkgdvlte tmaialwleg rdqerrisfa pgtfeadrmh qfiaflntgf tgaffsmwva
      121 lesedateey retlrafgre fvakrhkqle ammgdsnyli gdrptladav fagvarwvdf
      181 heaidpkdya rnyprihalr qrieadpafr favaiedgep vtgsgamkgl vpledvlrmt
      241 galra
//
LOCUS       WP_457578541             180 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Ensifer adhaerens].
ACCESSION   WP_457578541
VERSION     WP_457578541.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..180
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19739
     Region          15..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 migsdtvvdi dtrhqvyfan rtalvayatr ivgsretaed ivqeafirfa pantgnppsa
       61 gpsglslayl ykivrnlsld llkrrkiear eeqseppfws mpievptped iilvsdeikr
      121 isgiledlpe evrvalemhr fggytleeia ahldisvata hrhvraammr vattlaggas
//
LOCUS       WP_457578544             578 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Ensifer adhaerens].
ACCESSION   WP_457578544
VERSION     WP_457578544.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..578
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64728
     Region          3..569
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mplpldlkgr pdervlrqlv aallfegive asehtdgdvt tfhwsiggrq frchgaigpf
       61 grlrlaagsv emrddadgwv vpplaqlvsv lpgsgptrgk llneltqtia fsawnerqvp
      121 arlrralsfa elegaleegh pyhpcykart gfsvadhaay gpemggafql vwllvarkhl
      181 rcaipgdeda fweaelgeet wselrakrqe rglspdafgl vplhpwqwre lrerqlsgwi
      241 aagealclgp agdrytatqs vrsllnrdrp laasvklpln ivntssrrtl ephsvctapv
      301 isrwiaemva gdpafrdryp ltvlqeyagi iadsdgplag qvaaiwrena eatlgsgeav
      361 ipfnalmmve adgrafaddw iqrfglmpwi nrlievavlp vwhllvhhgl aveahgqnml
      421 lvhrdgwpar lilrdfhesi efspgflrap ekapdflsle piyreaepdq fywtdnldsl
      481 relvmdtlfv ynlseishll dhcynlpetl fwqrvqtvla ayeaehgate rlaqlgcdqp
      541 rilteslmtr kllalkpeyh hevanalaar mlqrrrkp
//
LOCUS       WP_457578542             332 aa            linear   BCT 27-JAN-2026
DEFINITION  FecR family protein [Ensifer adhaerens].
ACCESSION   WP_457578542
VERSION     WP_457578542.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..332
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36094
     Region          13..50
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          112..325
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mtkdnhisea lleeamdwfl elkarpncrd tqarfrawlg qselhgqawq talrtwqllg
       61 evppvhehlw rgarpsvfve ppvrqrrrmg tgglvvgval alaaclvlfv slpsllvwwq
      121 adhvtetaqn rtitladgti iemgggsaia tdisagtrhv rllkgeayfn vardpsrpfv
      181 veaggvevsv lgtafdvqla stettvelah gtvavsysan ahkqnfelap gematvsnat
      241 gavlrsaiaa ddigawrsgr mfvndvtvaa aaerlqryhs awisipqpdl agrrvtgvyd
      301 lkdpdralqa lvqpfggkvr evtpygrilt rf
//
LOCUS       WP_457578548             159 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457578548
VERSION     WP_457578548.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17890
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrlnyaqq speffkkisd fshslkdsvi eqtirdlvnl rasqingcaf cvdmhvkeak
       61 ihgeselrly hvaiwresnl fapreraala wtevltklpe ggvpdelyer vrgqlsekei
      121 sdltfsimai nawnrvsvaf ksvpgsadkl yglhkagln
//
LOCUS       WP_457578550              78 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Ensifer adhaerens].
ACCESSION   WP_457578550
VERSION     WP_457578550.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15304352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..78
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=7899
     Region          <6..50
                     /region_name="M23_peptidase"
                     /note="M23 family metallopeptidase, also known as
                     beta-lytic metallopeptidase, and similar proteins;
                     cd12797"
                     /db_xref="CDD:410984"
ORIGIN      
        1 mivacdgmrv elahlrkgsv taligarvla gdpigavgns gnstephlhi havdagsgka
       61 vqlsfdgrvp srnaqfar
//
LOCUS       WP_457578556             214 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457578556
VERSION     WP_457578556.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..214
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=22906
     Region          7..166
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(10,12..17,52,54..56,59,109..111,115..116,119..120,
                     157)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(12,56)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(17,28,31..32,35,40,52..53,104,110..113,116,157)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 meqklsvima advvgysrlm eldekgtlat lmahrqelwd vavaahhgri vkligdgmlm
       61 efravedavl caveiqrgmq trnagtqrdr riefriginl gdilfedgdv ygdgvnvaar
      121 ieslakpggi svsasvhdtl ggrldirfed tgaqalknig rpvhiynivi ddggseggga
      181 dgatdtgdtg ksprqvepda slcvalcefe rqsr
//
LOCUS       WP_457578539             139 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578539
VERSION     WP_457578539.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..139
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15592
     Region          22..138
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtvenptevp afawrgafen kelntlhaec fehaltdddw wsqvnrfslg wvtmrisgal
       61 tgfvnvawdg gvhaflldam vtlplrrkgy atllveeavt hakasgcewl hvdfdphlre
      121 fyvdrcgfvp tdagliqlr
//
LOCUS       WP_457578561             115 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Ensifer adhaerens].
ACCESSION   WP_457578561
VERSION     WP_457578561.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 51693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..115
                     /product="SRPBCC family protein"
                     /calculated_mol_wt=13150
     Region          <2..114
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
ORIGIN      
        1 mkqvtllneg dehgvgavrr mrwstalpye lvfdiettkv epplfiegra lgeldgigrw
       61 tlqgeasacr vrydwivtvt kpwmvrlsfi lrpvfrwnhg vvmergrrgl skrla
//
LOCUS       WP_457578563             610 aa            linear   BCT 27-JAN-2026
DEFINITION  carbamoyltransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578563
VERSION     WP_457578563.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Parthier,C., Gorlich,S., Jaenecke,F., Breithaupt,C., Brauer,U.,
            Fandrich,U., Clausnitzer,D., Wehmeier,U.F., Bottcher,C., Scheel,D.
            and Stubbs,M.T.
  TITLE     The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic
            reaction
  JOURNAL   Angew Chem Int Ed Engl 51 (17), 4046-4052 (2012)
   PUBMED   22383337
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450873
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..610
                     /product="carbamoyltransferase family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016743 - carboxyl- or
                     carbamoyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68306
     Region          1..597
                     /region_name="COG2192"
                     /note="Predicted carbamoyl transferase, NodU family
                     [General function prediction only]"
                     /db_xref="CDD:441795"
ORIGIN      
        1 mrilgisafy hdsaaalved grivaaaqee rftrrkhdpd fparaieycl seagctmndi
       61 dhvvfyekpf lkferlvety latvphgfss frvampvwik eklfqkkmlr kdlgklvgkk
      121 ewdgsllfte hhqshaasaf fpspfasaav ltmdgvgewc ttslahghdn rldflkelhf
      181 phslgllysa ftyytgfkvn sgeykvmgla pygrprfaqt ildnlidlkd dgsfrldqhy
      241 fgyctglkmt spafhdlfgg eprkpesplt qremdlaasv qvvteeavmr laryarrqtg
      301 eknlclaggv alncvangkl lkagifddiw iqpaagdagg algaalsvwh eylgsarvvk
      361 esdsmsggyl gpafaqgeve qrlanaganf evlsdeeits stvsalteek avgwmqgrme
      421 fgpralggrs ilgdarsptm qkmlnlkvky resfrpfaps irredlsdwf didtdspyml
      481 lvgdvlesrr lhanhpqenl fgidllnvpr seipavthvd ysariqtvhr etnprywell
      541 trfkartgcp vlvntsfnvr gepivcnped ayrcfmgtei erlvvgncil kkenqpehlk
      601 qdykenfeld
//
LOCUS       WP_457578565             994 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter outer membrane beta-barrel domain-containing
            protein [Ensifer adhaerens].
ACCESSION   WP_457578565
VERSION     WP_457578565.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Veiga,E., Sugawara,E., Nikaido,H., de Lorenzo,V. and Fernandez,L.A.
  TITLE     Export of autotransported proteins proceeds through an oligomeric
            ring shaped by C-terminal domains
  JOURNAL   EMBO J 21 (9), 2122-2131 (2002)
   PUBMED   11980709
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Henderson,I.R., Navarro-Garcia,F. and Nataro,J.P.
  TITLE     The great escape: structure and function of the autotransporter
            proteins
  JOURNAL   Trends Microbiol 6 (9), 370-378 (1998)
   PUBMED   9778731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..994
                     /product="autotransporter outer membrane beta-barrel
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0046903 - secretion [Evidence IEA]"
                     /calculated_mol_wt=97536
     Region          94..994
                     /region_name="COG4625"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal beta-barrel porin domain [Function unknown]"
                     /db_xref="CDD:443664"
ORIGIN      
        1 mrqtplavls krlglftala slalstpala qsvwdggadn efgnganwap alpgasdaae
       61 vntgspqvnd grtirqlgvd ggnvtisntg altvtngsti nsgsvsinag galtsnveln
      121 ggslsidgnl ngrltlnngn vsvngrldsa svgsatslsn ngqvgdvnvs aggtfvnntg
      181 avagatvnag tasnagtmgs ltntqgnftn ntggtitgkt tvaggtvtnn fvvtdadvaa
      241 aaafvnndga tagaitnagt vsnagtiasv rndagsftnn fggevtgett vsggavtnng
      301 tlgtvtvgag gtftntsgas agavtnsgaa snagtiagln ntagnfanna ggtvtgkttv
      361 tggtvtnnfv vtdadvaaaa tfvnnsgava anvtnagtls nagtiasvrn dggsftnngn
      421 gtvtgkttva ggsvvnnaal adveigangt ftnnsgatag avsnagtgsn dgtiaslans
      481 gglfqntgti sgaanitgga lvnqgtvagt veifdgglls gsgivgsltv naggvvspgp
      541 giavatvngd ltfrsgsiyq vdvdaagqsd rlavsgtlsl eggrlavlag sgvydpstsy
      601 tiasagtvsg rfdavtsnla flsptltyga tgidlrldrn dvafadlaet angraaasav
      661 ealsvtsplt lavlslddat aasafsqlsg evhasvksal mwdsrfprda ileragstvs
      721 tlqetedavf wtsgfagagh lsgdgnaaai dnrtagilvg adaavsddwr lggilgyshl
      781 tvqpqarvda yhaglygygn igalnlagga iyshnevsse rdlafgsftd rltadydstv
      841 aqvfadlsft lsaddirlqp fanlayvyld tdafkenggs aalsaegatd damlttigvr
      901 wwanlpidqm pisasgmlgw rhaegdlsps arlafagasp ftiagvpiar dalvveagis
      961 arlsksarla itylgefgdg arssagranl ivdf
//
LOCUS       WP_457578566             464 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578566
VERSION     WP_457578566.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..464
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50929
     Region          36..408
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtqvrskala dvtmtpfwld rpdapeprer ltrhlkadll vvgggftglw gaiqakqrqp
       61 eidvilieks svangasgrp ggvvstsvmh glsnavrifp kdiatleklg qenmhgflkt
      121 leehaidcha ewggeltvav ddahiealhe ehelhlkygh qavfldqgav raeinspryk
      181 agvwskhicg tvhpallafg lkrvaltlgv rifenteltg ledlgdrmka haasgsvtap
      241 kvllatnafa aghrkiknrv vavrdrvlat eplsaeqmaa igwshrqgvy dtrtqmnymr
      301 ltkdnriifg grlayafagd pfpsidreld tyeplaaaff dtfpqleglr fshawsgpid
      361 lstrmavhfq ryhdekvvya ggysgfgvsa srfgariald ildgsktpes rldfatslpn
      421 tippepfrwl gaqitmyald tadksggwrk pwlkmvsamg fpls
//
LOCUS       WP_457578570             405 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Ensifer adhaerens].
ACCESSION   WP_457578570
VERSION     WP_457578570.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..405
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44068
     Region          2..369
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(164,166,207,233,259,282,309,334)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mkiaslktya vavppphvgg mywifvrltt acgiegigei yatsfhpkal tpliedvfer
       61 hllghdphqi erfwrsayss gftqrpdptm mgivsgleia cwdiigkaag rpvadllggt
      121 vheklrayty lypknaagef dfndpdlaag cavemvemgf tavkfdpagp ytnysghqls
      181 lgvmdrseef crkirdavgs sadllfgthg qmvpssairl arrlekydpl wfeepvppgq
      241 eaamaevara tsipistger lttkyefqrv lelkaasilq mnvarvggll eakkiagmae
      301 ayyaqiaphl yngpvgaaas iqlsaaspnf liheaildfs gfhadvlktk lavedgyiip
      361 srepglgtel nmdvvekhtp ytgerlhlqm dsrpadvkaf aparg
//
LOCUS       WP_457578568            1051 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Ensifer adhaerens].
ACCESSION   WP_457578568
VERSION     WP_457578568.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..1051
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114857
     Region          13..1023
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mttsssdekr pfnlsrwaia hpsmarflfg liilagvfgl mrmgqkedpd ftfrvmvvqa
       61 fwpgasieem qdqvvnkier klqetphldf vrsytragsa iitlqvegdt naeqvadafy
      121 qvrkkvgdis nelpegllgp yfndefgdtf itlhslsgeg ysypelkkfa iqardmlltt
      181 pgvekaviig dqpekiyidv ssnalaergl tlndlrstia gqnnidpaga vdtgtrsvri
      241 svegsldkve dlknlrlrag gqitrlgdia tvssgledpy srkfrfnged svqigvvmak
      301 gfkvtdvgna veatyqhfea slpygvkvdq vsnqpevvke avgefmkalg ealaivlvvs
      361 flsigwrsgl viaitiplvl aatfaimyel gidlqrislg aliialgllv ddamivvemm
      421 erkleeglvk veaasfayts tafpmltgtl ittagfipvg faastageyv rslfyvvgia
      481 lvvswfvavy ftpwlgnmll kqrshagnhh dvfdtrfyrr lrttvtwavr hriivlsttl
      541 alffvslwaf qfipknffpq ssrpeilvdl wlpegtsike vekqakalea rmmddedkrf
      601 iatyigegap rfflpldqql rnpnfaqllv makdeparer liakmrgila adfpsirakv
      661 drlflgpptg wpvqmrimgp drdevrriad rvkakfhenp llgavhddwl epvpgmklvi
      721 dqdraralgv tsqrirqilq asvtgapldn frdgeetvai varepaesrk llssvdsiyi
      781 ptdfggfvpl sqvakvvpvl eqgiewrrdr lptitvrgtl pdgvqpndva mkmfgemqpl
      841 rdslpagysi aiqggaedfa esqasiaaka pimlgvivil lmiqlqhfgk amlvlatgpl
      901 giigaaaall isgapfgfva ilgviallgi imrnsiilvd qidqdiaagm draeaiigsa
      961 vrrfrpitlt altavlalip isrgvfwgpl ayammggilv atvltilvlp agyalffgre
     1021 pkkssvepet pasleaedtk tvaypaavaa e
//
LOCUS       WP_457578574             660 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Ensifer adhaerens].
ACCESSION   WP_457578574
VERSION     WP_457578574.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 660)
  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 10101347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..660
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72285
     Region          59..540
                     /region_name="YtcJ_like"
                     /note="YtcJ_like metal dependent amidohydrolases. YtcJ is
                     a Bacillus subtilis ORF of unknown function. The
                     Arabidopsis homolog LAF3 has been identified as a factor
                     required for phytochrome A signalling; cd01300"
                     /db_xref="CDD:238625"
     Site            order(102,104,376,408,470)
                     /site_type="active"
                     /db_xref="CDD:238625"
ORIGIN      
        1 mptrrsflga asslalpalf psartagaqq tgdtsmtpdl ilhtglvttl dranptatav
       61 avkdglilav gddrtimala gsgtktidlk gkrvlpglnd nhthvvrggl nfnmelrwdg
      121 vrsladamdm lkrqvaitpa pqwvrvvggf tehqfaekrl ptideinava pdtpvfllhl
      181 ydrallnaaa lravgytrdt pnppggeitr dasgnptgll lakpnagily stlakgpklp
      241 fdyqvnstrh fmrelnrlgv tsvidagggf qnypddyavi qklsdegqmt vrlaynlftq
      301 kpkqekddfl kwtssvkykq gndyfrhnga gemlvfsaad fedfreprpd mppemegele
      361 evvrilaenr wpwrlhatyd etitraldvf ekvnrdiple ginwffdhae tisdrsidri
      421 aalgggiavq hrmayqgeyf veryghgvae atppvakmla kgvnvsagtd atrvasynpw
      481 vslswmvtgk tvgglqlypr ancldretal rmwtekvqwf sneegrkgri ekgqfadliv
      541 pnkdffncae deisfltsel tmvggkivya agefashden kvppampdws pvrtfggyaa
      601 wgepegagkr slrrtaitsc gcasdcgvhg hdhagawtsk lpiadlkgff galgcscwav
//
LOCUS       WP_457578576             215 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Ensifer adhaerens].
ACCESSION   WP_457578576
VERSION     WP_457578576.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..215
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=22787
     Region          <26..215
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtkppcagsa rsapttacsw sprippyksl geliaaykas ptdfsvaggg avgsqdwmkg
       61 sllakaagqe pkqmryvale gggavltale gghvkvgagd aaemskhhaa gkvrvlavma
      121 pdrlpgelae vptareqgvd iewpvwrgyy vgkdvsdady kwwadaftkl aatpefvker
      181 earglyeytq vgdafdqqvk advarfkiia keagm
//
LOCUS       WP_457578579             220 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Ensifer adhaerens].
ACCESSION   WP_457578579
VERSION     WP_457578579.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..220
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24327
     Region          8..182
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mkrdlpslil irhgetqwnv agrlqgrkdt pltangvrqa lavglrlaer iaeeeknltf
       61 wvsplgrarq tasiladtws ipfdrfaeaa alaersygaw eglahdeier dltdqydahc
      121 adpfdysmpg gesrtalsar lqawldtldr grrhvvvths gclralrgiy taasrdeila
      181 yrepqtasfl ltagretmld vplnilralg cdgagrtvwi
//
LOCUS       WP_457578580             366 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578580
VERSION     WP_457578580.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..366
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39027
     Region          18..366
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtvninsaal aagpakaisi sdvnlyygal hvlkninlei qpgeffaflg psgcgkttll
       61 rliagfnnar qgkvviggqd vldmpawkrd igmvfqsyal wphmtvaanv afgleerrla
      121 raevdrrvka aldlvglkhl adrrpsqlsg gqqqrvalar tiaiepkvll ldeplsnlda
      181 kmrvevrrel relqqrlqlt tifvthdqee antvcdriav fnegsiqqvg tpmglyekpa
      241 nlfvanflgt anildgkvag sgatrsfevv gggsipipag tevpagaklv frpqyatigs
      301 lepgavaleg iiahreflga tvrygvriga atvlidapfh sgdallepga tttlglkpss
      361 aqwlah
//
LOCUS       WP_457578581             446 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578581
VERSION     WP_457578581.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 446)
  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 446)
  AUTHORS   Studholme,D.J. and Dixon,R.
  TITLE     Domain architectures of sigma54-dependent transcriptional
            activators
  JOURNAL   J Bacteriol 185 (6), 1757-1767 (2003)
   PUBMED   12618438
REFERENCE   3  (residues 1 to 446)
  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 446)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..446
                     /product="sigma-54-dependent transcriptional regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=48912
     Region          7..436
                     /region_name="AtoC"
                     /note="DNA-binding transcriptional response regulator,
                     NtrC family, contains REC, AAA-type ATPase, and a Fis-type
                     DNA-binding domains [Signal transduction mechanisms];
                     COG2204"
                     /db_xref="CDD:441806"
ORIGIN      
        1 mrpeadiili dddasvleac cqvleledft vsphgsvvaa laglradsdt vivsdvrmpd
       61 hdgfdlvaav rkvdpdipiv lmsghgdipm alramregaw dflekpadpv hlietvrrar
      121 dhrrlllenr rlrlsvdkdg wetrlighsa pmvalreklq riaaasadvl iigdtgtgke
      181 vtaralhdfs grkgrfvavn cgaipetmle selfgheaga ftgarekrig kieyadggtl
      241 fldeiesmpi aaqvrllrvl qervierlgs nvelpvnicv vaatkadlhd aarrgefred
      301 layrldiarv elpplarrkg dvgllfqhfl slaakrqgrt appvgvdlla dlnarpwpgn
      361 vrelrnvaer fvlgleerpd teattagget leaqmdrler tiiinslarh egrvgatada
      421 lgisrktlyl kmrkfdidar adgdeg
//
LOCUS       WP_457578583             378 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578583
VERSION     WP_457578583.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..378
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39635
     Region          23..372
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mswigplplq qgllfvgvll lfaflgqnta esmhrmgltp gfaflshqan feigesvlpy
       61 aagdsyaral aagiantvkv alvgcllatv lgvalgifrl sgnlllatfa hgyvellrnt
      121 plllqlflws atiralpppr gaytflgsvy lsnrgvflps lsvdglpasv wlpavlltvf
      181 aalvisrrll agatfylpkt agtvlgalai fyfalvslgf sasvevpakg gfnirgglsl
      241 tpefaallig lvvnasasis eivrsgiqsv asgqweaara lglkpaqimr lvvlpqalrv
      301 itplmissfl dltknsslav aigypdlvsv anttanttgq aleaiiiigv vyltislavs
      361 almnlynrrv vlrgegkr
//
LOCUS       WP_457578584             343 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter substrate-binding protein [Ensifer
            adhaerens].
ACCESSION   WP_457578584
VERSION     WP_457578584.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..343
                     /product="amino acid 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=37024
     Region          32..266
                     /region_name="PBP2_BztA"
                     /note="Substrate bindng domain of ABC
                     glutamate/glutamine/aspartate/asparagine transporter; the
                     type 2 periplasmic binding protein fold; cd13692"
                     /db_xref="CDD:270410"
     Site            order(46,48,92,107,114,158..159,200..201,230)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270410"
     Site            order(54,58,182,185)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270410"
ORIGIN      
        1 mqqtsthrkl ftataalaag liatsalage tldkikargv ikvgvgttpg ffspdsngrw
       61 qgffvdfgra iaitvfndae kveftnsspq qrlpalqsge fdillsgvtq tvsrafklgf
      121 hfgpvvfydg qgllvrkdlg vakgeeldga tigvqsgttg elniadffrk tgkaftpvti
      181 eetgeflkal dsgrvdaltq datdlaakrt qlskpddyvl lperlskepl apairagddq
      241 wleivnwtvy atiqaeefgi tkenvdtfla sedpaikrfl gvdpslgeai gldpkfayni
      301 vktvgnygei fernvgkgtp lnfergynqp wtaggllysp pfr
//
LOCUS       WP_457578590             444 aa            linear   BCT 27-JAN-2026
DEFINITION  NfeD family protein [Ensifer adhaerens].
ACCESSION   WP_457578590
VERSION     WP_457578590.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..444
                     /product="NfeD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46064
     Region          15..439
                     /region_name="NfeD"
                     /note="Membrane-bound serine protease NfeD, ClpP class
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1030"
                     /db_xref="CDD:440653"
ORIGIN      
        1 mlrtltllfl lilsfafpas sraendrval vlhvngaigp ataeyvrrgl tkaqerrlpl
       61 vvlqvdtpgg ldtsmreiir ailgspvpva tyvapsgara asagtyilya shiaamapgt
      121 nlgaatpiai ggdmfgegkd gdkqpaaqsp aeakmvndav ayirglaelr grnadwgeka
      181 vreaaslsae aavrekavdf tatdvtdllk qangrtvrvg qreivldtag lttedfvpdw
      241 rtrllsvvtd pniavilmmi giyglifefl spgsvapgti ggiclllgly alsvlpvsya
      301 giglimlgig lmvaeahsps fgvlgaggsf alvlgaailf dtdtpgfgvs wsvlaalava
      361 slgfsllvar lafsssrhav vtgseqmigl agtvenwtga agyviahger wqavstetls
      421 rgenvkvigr ngltlevird gpkt
//
LOCUS       WP_457578588             549 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578588
VERSION     WP_457578588.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 549)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 549)
  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   6  (residues 1 to 549)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 549)
  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 10170725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..549
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60844
     Region          24..526
                     /region_name="PBP2_TmCBP_oligosaccharides_like"
                     /note="The substrate binding domain of a cellulose-binding
                     protein from Thermotoga maritima contains the type 2
                     periplasmic binding fold; cd08509"
                     /db_xref="CDD:173874"
ORIGIN      
        1 mkksllgaat alaliagpaa aqtvltanie pattwvrnfn pfnqtsarqs tldfiyeplv
       61 vfnrfdgnkp vfrlaesfkl sddlksiefk lrpnlkwsdg kpltatdvkf tydylkkfpa
      121 ldfvsiwtft tgveavdaet vrftlanpss laaeqlaqlp ivpehvwkdi aepvtyanea
      181 pvgsgpltei prftgqtydq crnphywdaa tlkvdcvrfp qladnnqilt atasgtldwg
      241 vsfipdienv yvakdpehfh fwyspssmva flfnqetane nnrkafndvk frraasmald
      301 rgtmvdvagy gyptlnedpa gmgelykswa dpsvaadfgk ygkydadaak alldeagyad
      361 kdgdgfrdnp dgskisfsii vpsswtdwid tvtiaveglq avgldgkiet peeavwtgnl
      421 ingtfdaain slpasaspyy pykrafsasd kgktrftsqr wfnpdveall teftqtadpa
      481 kqkeamnkaq rivaenmpmi pvfnnpnwyq yntkrfkgwa taenpfvnps itrnnparll
      541 hllalepvk
//
LOCUS       WP_457578591             744 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578591
VERSION     WP_457578591.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 744)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 744)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 744)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..744
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79682
     Region          162..718
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mehrnrrldl tlglglaafl avpwyriegg ffglgwlaef pgdpavapgl mqifahgkpw
       61 livalallgi cvaarfvrdp arrglllava gaagvlylal qglaigfsgw twtisetlfg
      121 tlsdgqpsmg agavlmaltf vllfafglae rgvlkgdafi vaaisllvtl vivfvfypvg
      181 smfaasvqdf dgsfkpdgfi rniqdasiws lscvvgegrc gvawrtlwla lmtasgstll
      241 glafalvatr trfpfkkgmr lltvlpiitp pfviglaltl lfgragvvte flsdafgvep
      301 grwlygltgi wiaqvlsftp isflvligvv egvspsmeea sqtlradrwr tfwtvslplm
      361 kpglanafli gfiesmadfg nplvlggshg vlsteiffav vgaqndpsra avlaiillcf
      421 tltafvaqry wlagknystv tgkgdsgahs alprsisigv haivipwmif tvvvysmilf
      481 ggfvktwgld nsltldhyak afsisfadga iawtgvawns fwttmeisli aapltamvgl
      541 ltaylivrqr fagrdvfefa lmlsfaipgt vigisyiiaf nlpplemtgt alilvacfvf
      601 rnmpvgvrgg iaamsqldks ldeasltlra tsfrtlrkvi lpllrpaiva alvysfvrai
      661 tsisavvflv saeynmatay ivglvengef gvaiayssal ilvmitvitg lqllvgerkl
      721 rrenrvlgaa pvrssntisq ekta
//
LOCUS       WP_457578592             697 aa            linear   BCT 27-JAN-2026
DEFINITION  two-component system sensor histidine kinase NtrB [Ensifer
            adhaerens].
ACCESSION   WP_457578592
VERSION     WP_457578592.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 697)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 697)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 697)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 697)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..697
                     /product="two-component system sensor histidine kinase
                     NtrB"
                     /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_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009399 - nitrogen fixation [Evidence
                     IEA]"
                     /calculated_mol_wt=74879
     Region          359..696
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 misrpflssi afrlpfaivf icvlvfslat vavfglqrar demaayglqa fsslakaslv
       61 srqvsdlvss apflmnatsp yrvssesrsv vaqvdvllqt mapetgktav egfasahive
      121 lldairtqtv tlaadadsaq qykadaaaal geiatgngia daevrqslna ivqsasnsds
      181 lfqlgelrrr yvavttprla pagpdsrisa akltpyervf eaqthyllem fairaavarl
      241 htvsrdlsha tetqseavar glnedlasts dalsrllviv avsallvlvm aifsirsvmr
      301 vsrgivslsk gmnalaqgrr dvdtpsykgt eteflrllea fsafresver vsrlrrtaea
      361 aartirstfr nmnegialfd pggkpitmnr rvmelvgwpg sarklplrrf vspmpeidpt
      421 llpadrdags lddrlvlrhr sdmgrvtevs lsrqpdrgiv llardvteid rqeaeaakaq
      481 rldgimrmth qvshevgnmi giitgslgll eretgfsdrq krhiarirka adrgrslass
      541 mlsvgsqhpl qpgaleigav lrgmadvlei avgekcrlaf eiadglpnah ldaalfeqai
      601 lnlclnaaaa mplggtilvr agcvesdvvv svtdagigms peavdkafep yfttrdqegg
      661 aglglavvyg fvrqsggdar ilsqpgrgtt velvfpr
//
LOCUS       WP_457578597             374 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Ensifer
            adhaerens].
ACCESSION   WP_457578597
VERSION     WP_457578597.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=41339
     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 mdvrvhnirk efgrfpaldd vsldirsgel iallgpsgsg kttllrlvag lesptegtif
       61 fgdedasqkt vqernigfvf qhyalfrhmt vldnvafglk vrpsnrrpps aeirkraldl
      121 ldlvqlsgld krypaqlsgg qrqrvalara mavepnvlll depfgaldaq vrkelrkwlr
      181 dihdrtghtt ifvthdqdea leladrvvvm skgvieqvgt pdeiydhpvs pfvygfigqs
      241 nclnvtlqng eiwfedrpig lrapsepdgp aklhfrphdi elidgcggcl aglvaasrrv
      301 agtrhleldl grnhphveie lsperaaagd hsriafrptk wklfreeqpn aaatleapae
      361 vetaepfela rtgs
//
LOCUS       WP_457578598             171 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Ensifer adhaerens].
ACCESSION   WP_457578598
VERSION     WP_457578598.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..171
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18653
     Region          16..167
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mesakrlsrk narrrkylar iceeattavl grlnaegflg ywsaaagdea aysrdrgyad
       61 rlvgaekvvf srmlteapwe rtriangsvm dvvsdlkasg egdilvnssa sliksllsad
      121 midrpyllic leiagggarl fedglpgttw rvahqetger gkialvydrv r
//
LOCUS       WP_457578600             341 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578600
VERSION     WP_457578600.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 341)
  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 341)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..341
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=36346
     Region          1..337
                     /region_name="CurA"
                     /note="NADPH-dependent curcumin reductase CurA [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG2130"
                     /db_xref="CDD:441733"
ORIGIN      
        1 mskntqvlla arpsekpvps dfrvvetaip epaegevllk ilylsldpym rgrmnagrsy
       61 akpveigavm eggtvarvlr srhpdfsdgd fvlshsgwqs yalsrstdlr kldpaaapls
      121 talgilgmpg ftayagllti gkplpgetvv vaaasgavgs avgqiarikg aravgiagga
      181 dkcafvrdtl gfdavidhra pdfaeqlaaa cpkgidvyfe nvgghvwdav fpllndfarv
      241 pvcgliahyn qpagaqagsd rlpgvmrevl srsllirgfi qrefadqrpl fyqemagwik
      301 sgevryredi vdglenapea figlldgrnf gklvirvaae n
//
LOCUS       WP_457578602             822 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578602
VERSION     WP_457578602.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 822)
  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 822)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..822
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=88602
     Region          1..80
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mrrltlaftl laiaavpara gpattsasvn fregpgtasn slgtiaegte vdvkecddag
       61 twcavsfngq ngfvsgkyln dadpkglgwp rayktdsgat itlyqpqina wkdfteldal
      121 iaaeykqsdd akpifgvvgv tgktdadsas gqvvvsdikm teinfsvldr keladltlev
      181 gklmpvgtit isedkltasl adyqrlgnve glkadappif iskkpailvq tdgkavfapv
      241 kgveglsftv ntnwdlfkve adatyylrnd kswlqskdla sgwqsasslp dilsklpddd
      301 nwkdakaaip pqadkvivpd viysdkpsel lafdgepkle qvpgtglkva tntesdafyr
      361 dvdsswyilv sgrwfastal dgpwtfatpk lpqdfqnipq daayytvras vpgtsenaea
      421 rlkasipeka rvsldgsvtv dvaysgdpkf ktidgtslty avntnetvik vgdkyfvlkd
      481 gvwfvgdapt gpfavakavp deiytippss piynatyvri ydtepdavwf gytmgylgay
      541 lawdtfvygt gwyyddywdy gwagggywpy yprpvtygvg afynpaigtf grygyaygpy
      601 rgiaagaayn prtgtyvrga agygpngdrg fvaaynprtg naamargghn vygswgtaav
      661 khgsdfaris ggstangagv nwrtsdgnhg fvaggkggdv yagrdgnvyr rddgqwqkrt
      721 pdgwqpvqkp liqdrtkage qfsanhpdaa eninqrietr qqagqgadre rapdhlaidn
      781 igrqlgnqrs ferqsfgqrp lnfptggggg fdrpggfggr rl
//
LOCUS       WP_457578604             414 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578604
VERSION     WP_457578604.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 414)
  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 414)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..414
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46019
     Region          6..407
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mptdrkiavv lkgyprlset fiaqellgle ragielvlis lrrptdgkrh pvhdeiradv
       61 hylpeylhee plrvlrglvr clpkpgfwrv lglflkdlpr dfsrnrfrrl gqalvlasew
      121 pgqprwlhah fihtpasvta yasviagtpw tcsahakdiw tspdwelsek lglarwtvtc
      181 trmgyehlrs lasdksrvhl syhgldldrf phfdgthsnr tgsdpadpvr ivsvgravgk
      241 kgydvllkal aklpaelhwr lehigagelt gqlktlatel gvsdrivwkg aldqtdvlah
      301 yrasdifala critadgdrd glpnvlveas sqrlacvsta isgvpelled gengrvvpse
      361 dpqalaaale elirnpalrh rfgdaaerkv rgqfdhhtsi eqlaglfase wraa
//
LOCUS       WP_457578606             516 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Ensifer
            adhaerens].
ACCESSION   WP_457578606
VERSION     WP_457578606.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..516
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56356
     Region          5..506
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mrfeqflign aarhaaktal vtdrkrlsyg efddlssrla aalakagvkr ndrvlvfmdn
       61 cweaavsifa ilragatfsp inastkadkl ayiiddceaa ailtqaklmp vvadaraqss
      121 gkadifvast aapngqspag avpfegclsa eatpvphggi dvdlamliyt sgstgrpkgv
      181 mmthrnidaa sesittylrn ehddiilnvl plafdyglyq llmairlgat lvleksfafp
      241 haiferiree gvtgfplvpt maamilqmrd lepgflpslr ylsntaaalp pphiarlrel
      301 fpgarlysmy glteckrcty lppeeldrrp gsvgiaipnt eafvvndegs rvppgvpgel
      361 virgphvmqg ywrndvater mlrpgpnpwe kvlytgdlfq tdeegflyfv grkddiiktr
      421 gekvapkeve tvlhahpgia eavvigmpdp vlghaiaalv vrtdpnltdk diirhctrhl
      481 edfmvpkiie frtelpktdt gkvsrrlate tmepaq
//
LOCUS       WP_457578607             359 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457578607
VERSION     WP_457578607.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 359)
  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   2  (residues 1 to 359)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..359
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36925
     Region          11..337
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 marsgpkltr iartlgvsaa tvsnalsgkg rvsaemveki rataaelgyv psqagralrt
       61 grtgvlglvl pdianplfpq iaqaielaas ssgygvliad srgdvstqtk aierlidrdv
      121 dglvivprrg triadvgcpv avidtpstpg ntvaadhwgg grqigehlka lghrrvliig
      181 nnpasnvqnd raggirsvfg egthtdtlwi eplekaagkg cplgladkva egytafacis
      241 dlhalralte lqraginvpe kasvtgfddl iwspvitpal ttarmdmtki aaiavaalvk
      301 aiserdpsdp aigapvtaat skvpmhlvvr qsaavppasq pilttataat svtegghqp
//
LOCUS       WP_457578612             340 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457578612
VERSION     WP_457578612.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Ravcheev,D.A., Khoroshkin,M.S., Laikova,O.N., Tsoy,O.V.,
            Sernova,N.V., Petrova,S.A., Rakhmaninova,A.B., Novichkov,P.S.,
            Gelfand,M.S. and Rodionov,D.A.
  TITLE     Comparative genomics and evolution of regulons of the LacI-family
            transcription factors
  JOURNAL   Front Microbiol 5, 294 (2014)
   PUBMED   24966856
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  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   3  (residues 1 to 340)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   4  (residues 1 to 340)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
REFERENCE   5  (residues 1 to 340)
  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 10428567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..340
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37592
     Region          3..61
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cl22854"
                     /db_xref="CDD:473980"
     Site            order(6,14..18,20..21,24,29..30,33,46,49,52..53,55..56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143331"
     Site            46..55
                     /site_type="active"
                     /note="domain linker motif [active]"
                     /db_xref="CDD:143331"
     Region          62..337
                     /region_name="PBP1_sugar_binding"
                     /note="periplasmic sugar-binding domain of uncharacterized
                     transport systems; cd06307"
                     /db_xref="CDD:380530"
     Site            order(74,152,205,281,301)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380530"
ORIGIN      
        1 mrptakdlae aaglslatvd rvlndrpnvs pravrsvnea ierigfirnp aavslarnks
       61 yrfrfvlpts gdlylaelih rveearvsmk gdlidldvvq ipiddphkva kyladidene
      121 fdgiammape spqvrdaigr liergvkfvq flsgqeklpt adfvgvdnya agataakiig
      181 rfvgrragkv livaetmqsl dsiqrrfgfd divnsqfphl qclpsvethg derratqilq
      241 rvlennqeva aiyvlssear iplegaasft dlqkitvvvh ertpfsergl rdasvdavia
      301 qdpghavrsa irimrartdf rephaaqdki rievllkenl
//
LOCUS       WP_457578614             117 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578614
VERSION     WP_457578614.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..117
                     /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=12947
     Region          <1..45
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mttlsetnir tmqpkgtfpw hlelsggrvg fpkevihawl enpkawklrn lqlmreafgi
       61 pdettadnsf navfeafark arsaeaammt aildrfgkla rgtehksdad nptdasi
//
LOCUS       WP_457578622             291 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578622
VERSION     WP_457578622.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32603
     Region          1..283
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mnlelidtfl dlldtrnfsr taerlettqs aisgrikale kavgtrlfyr grsgamatps
       61 glrfeqhars lkaawrharr dvgglehyeg tlrvsgqfsl mqslfldwie elhksnrrls
      121 lqleadsspk iisdlaegaa digvvfapqf lpdlsieeig terlvmvstd fenirdvtpd
      181 ryiracytay verthaellp hlahspmtag yeelavglik rlggtaylpe raisrlqdsg
      241 vdlrvvtdap emqqpvyval qrrrrhdpll nkairalkkv aeahfslpps k
//
LOCUS       WP_457578610              96 aa            linear   BCT 27-JAN-2026
DEFINITION  copper-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578610
VERSION     WP_457578610.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Loftin,I.R., Franke,S., Roberts,S.A., Weichsel,A., Heroux,A.,
            Montfort,W.R., Rensing,C. and McEvoy,M.M.
  TITLE     A novel copper-binding fold for the periplasmic copper resistance
            protein CusF
  JOURNAL   Biochemistry 44 (31), 10533-10540 (2005)
   PUBMED   16060662
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..96
                     /product="copper-binding protein"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10187
     Region          1..96
                     /region_name="CusF"
                     /note="Periplasmic Cu and Ag efflux protein CusF
                     [Inorganic ion transport and metabolism]; COG5569"
                     /db_xref="CDD:444311"
ORIGIN      
        1 mktvgkllaa lalvvstatf slpaqaaeft kgvvkkidtk akkvtidhed lknldmpamt
       61 mvfraddavl aklkegasie fvadrvngkl tvteik
//
LOCUS       WP_457578626             338 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Ensifer
            adhaerens].
ACCESSION   WP_457578626
VERSION     WP_457578626.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..338
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37283
     Region          3..328
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mfekkvhiwd efngriaavd sveirprvtg yidkvnyreg devkrgdllf tidqrpyraa
       61 lmsamarlar aealvgttkd rkergaalrk skfisdedan drsrdyeqaq advleaqaar
      121 diaelnlkft evrapidgkv gearltegnl avadqtlltt vvsqdtvyvd fdpdehsylr
      181 yaaqaretkt sisdllikvg lanedgfphs akisflnnev dpttgsirlr allankdkvf
      241 tpglyarvqi ardsensall vddkailtdq drrfvyildd knnavrkdis vgrlidglrv
      301 vdtglkpgdq vvvagfqkiy asgtpvspsa vamtsttd
//
LOCUS       WP_457578629             121 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457578629
VERSION     WP_457578629.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 121)
  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 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   3  (residues 1 to 121)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..121
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13086
     Region          6..>113
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 msskplvaiv dddiavreal vdfvrscgys aesfasaeey llsgrhaevn cilldimmpg
       61 ksglelqael nrtsrdkpii fissfdddrs rsiaedggav gflgkpidid allqylealf
      121 d
//
LOCUS       WP_457578635             340 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578635
VERSION     WP_457578635.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..340
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36829
     Region          4..335
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mptsasttpl lslralsiqf ekrrslsdtl arrpqqvvsa vngidlevmp getlgivges
       61 gcgkstlarl iaglhrptsg dilfegesvv glkgarrray nrrvqmmfqd pytslnprmt
      121 vrdtlreait vhrmrdgvai drrvdelldl vrlpegaadk fphefsggqr qrigiarals
      181 leptclvade lvsaldvsvq aqvvnlliel qdelgltvlf vahdlrlvrh vshrvaviyl
      241 gaiveigpse alfskpmhpy skgllaaaps ldpgarrrtp alsgelpspl aippgcpfhv
      301 rcphatercr rekpalrpvg sgmtachfae tigdasnstr
//
LOCUS       WP_457578636             149 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578636
VERSION     WP_457578636.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..149
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16401
     Region          49..138
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 maehdirdgv naffadyale qfttarfeei lgdrnetvwv sqnvvgidgy lrmsanspap
       61 vdiasdleit tlyvqphhhg rglgkallkt glqfcldtgq pgtwlavnae nekatafyla
      121 sgfemagqth ftigdqaypn hvlqfrldr
//
LOCUS       WP_457578638             174 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578638
VERSION     WP_457578638.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..174
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=18475
     Region          <47..171
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mpsrcrdtrp agievsstrp prtaksalkt cspgawersr yrssprggim tgsdiqavla
       61 kgasavqmgt aflktaeagt sapyraaleg terktrttra fsgrfargve nrfmnevdaa
      121 avmpfpaqnk ftrdiraast akgspdflsl wsgtgkgelw qgsasdliar lfpa
//
LOCUS       WP_457578631            1862 aa            linear   BCT 27-JAN-2026
DEFINITION  trifunctional serine/threonine-protein kinase/ATP-binding
            protein/sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457578631
VERSION     WP_457578631.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 1862)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 1862)
  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   3  (residues 1 to 1862)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 1862)
  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   5  (residues 1 to 1862)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 1862)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 1862)
  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   8  (residues 1 to 1862)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1862
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..1862
                     /product="trifunctional serine/threonine-protein
                     kinase/ATP-binding protein/sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=205362
     Region          37..1504
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          1493..1855
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mrhigkgnsi ddqglrdkpf dlssyalepl lqngefvisr arptgqardh csllvlshis
       61 drpspsqlrl lecefglrge lgsswalcpi dlvqhegris lvygdplaep lprllgafqt
      121 dtgfgatkpv psmevgrylk iasnvaaavr qmhqtgiihk diktahifvn ettdqvwltg
      181 fgiasrttre rqsqkppeal agtlaymape qtgrmnrsvd srsdlyalgv tlyeivtgsl
      241 pftaadpmel vhchiarqpv ppadrvsglp vpisaivmkl laktageryq taaglehdlr
      301 rclhqlgahg ridefvlgeh dvpdrlllpe klygrereae allhaferia dgappefvvl
      361 sgysgigkss vvnelhpvlv annglfaggk fdqvkrdvpy atlaqafqgl vrmllaksds
      421 dlgiwsaeir talgqngaiv vdlvpelkfv igepptapef saqdgqrqlh lafrrflavf
      481 arkehplvlf lddlqwldia tlalledllt qqdtkyilfv gayrdnevta shplmatltr
      541 lmrsgvivkd iglapltfqh tnsliadalr sdvdhthsls elvhekaggn pffviqflsa
      601 lteekllvls pdliwqwypd rigtkeysen vvalmtsklg rlphrtlqvl qqlacfgnnv
      661 dlvqlemvne nveedlqyal rselvfvsdg rcrfvhdriq eaayslipea eraelhlrig
      721 rrlaagtppe qlgenifeiv aqfnqgghli vsdterhqla efnlmaarra ksstvylsal
      781 gylerglall sddgwqrrpe lmfalaslqa ecefltgrla taeerlasls tlasnvadra
      841 siaslridly talsrndrai evclaylgkl gseipahpta daakreyqrt wsligsreie
      901 dlaalpqtqd sevvatmrvl grslspalft danllsvlvc qmtnlglehg haglscdayv
      961 wlgmiagphf gdyreglrfg elgyellqkm gpgqfrahil esfatliipw tkhlrtardl
     1021 mhsafdtats vgdlttasyc gsdifgilla agdpladiqd eavralefsr qvrfdmivdi
     1081 tsaqlalvqt lrgltptfgt ldhaefnees yelkvqaest valvacwywi rklqaryfag
     1141 dfatavhasf nakrllwtsp sfietaeahf ygalsqaaac dqtlpdwrer ylqvivehha
     1201 rlvewavhcp enfdcratli gaeiarlegq qltaqrlyea aiksarsnaf vhieaiasel
     1261 aarfhdacgl etishsylrn arqcylrwga dgkvrqldgl fpnlnlvase qapstttvas
     1321 pvdqldlatv lkvsqaisse ivfdslvntl mriameqaga erallilmrd aeprivaeat
     1381 tgretivvql hdkrptshdl pesvlqysqh tqelvildda svqnlfstdp ymaqrrprsi
     1441 lclpvssqak plgalylenn ltpgaftpar tavlkllasq aaisiensyl yrdlaerear
     1501 irrlvdadii gifiweftgr ileannaflr mlgydhddlv agrlswrnlv prawnetddh
     1561 lliqlraqgt lqpfeseyfh kdgtqvpvli gvatfggsdq gvayvldlte rkeaqealda
     1621 arnelahaar tmslgvltas iaheisqpls giitnastnl rmlaadppni egaretakrt
     1681 lrdgnrasev iarlralfsk kpaatedvdl ntaaravvel sshelqrnrv alaidlsdgl
     1741 pfvagdrvql qqvilnllln acdalssidd rprqitiktd ldevgeirlt vedngvgvdp
     1801 ntsdrlfnaf yttkdhgmgi glsvsrsiie rhdgriwasp nvgqgarfti tlpaarqfvt
     1861 ng
//
LOCUS       WP_457578632             233 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578632
VERSION     WP_457578632.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11417798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..233
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25253
     Region          1..233
                     /region_name="LivF"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivF [Amino acid transport and
                     metabolism]; COG0410"
                     /db_xref="CDD:440179"
ORIGIN      
        1 mlevddikaf ygssqalfgm tlkvdtgeiv tllgrngmgk tttvkaivgq vgvkggsirf
       61 sgrkiaglpa hrvarvgigl vpegrhifpn lnvrenliat arpgadgssp wtfaaimrlf
      121 prlgerlenm gdqlsggeqq mlaigralmi nprllildea teglaplire eiwnclkllk
      181 smgqsilvid knlshllpla drhyvvdkgq vvwegsseql kcdesvrnqy lgv
//
LOCUS       WP_457578642             202 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457578642
VERSION     WP_457578642.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..202
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21926
     Region          5..197
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtvpvylvdd ddavrralgl llstvgvkvi pfadpqaflg qlsrlepgcl ildirmpais
       61 glklqeklre ngvdwptivi sghgdieacr rafrngaidf lskpideedl idaihkgqei
      121 lartmqarae kaetlallaa ltqrerevld riaagfttrq iaeglglspr tveshraaig
      181 aklgstsqae mtriwlegth tp
//
LOCUS       WP_457578645             217 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457578645
VERSION     WP_457578645.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 217)
  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 217)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..217
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23603
     Region          1..208
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrvllveddq vlgealrdhv aaaghavdwf krildavaat dtvtyglill dlrlpdgegl
       61 tllrslrarg dgtpviilta hdqisdrieg lnsgaddylv kpfdlnelta rmlavsrryt
      121 gnatptvklp gieidqvhrk iavngdsqsl sarewavldk laahpgalvs kaqlhdalya
      181 fgaeiesntv evyisrlrkk igsdrietvr glgyclr
//
LOCUS       WP_457578647             234 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578647
VERSION     WP_457578647.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25463
     Region          <2..231
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 msfrvrrgtt haivgesgsg ktttirnivg fdrptagrie idgtnvsglt geglrqfrrk
       61 vqlvyqnpyg sldprqsvlq ivtepltnyp gllrsdreek arailgrvgl pedafarrph
      121 alsggqrqrv aiaralvldp qlvvldeavs aldvsvqari ldlldelqgd lgltylfvsh
      181 dlavvrqisd tvsvlkdgrl vdggtvsdvf enprsdytre linaipgrnr raaa
//
LOCUS       WP_457578652             367 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Ensifer adhaerens].
ACCESSION   WP_457578652
VERSION     WP_457578652.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..367
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39861
     Region          1..348
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(11,183..185,245,267)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 mfvlsglgag gaekvvnila rhrsargddv hvlalnaetp etyfaydrsv rvealgggss
       61 vpvfrtaerv arlrarlral spdlvisflt kvniivvlas rglrlrlvls ernnfntqdm
      121 nrlwrlarpl aarlaerlvm qtteavnslp ptlkakavii pnpitlqhvr dkqsgtntrv
      181 lavgrldrqk gfdllidafa gisgrapnmt ltifgegper pvleeqirrl glsnrvrlpg
      241 ttkspvewin agdifvlssr fegfpnvlle amsaglasia fdcpwgpsei idtpavgmlv
      301 pkedtrrlad aiaylaadat lrhqigamga ravaaryaiq svlkqwddvi aapketqaiy
      361 paarvsp
//
LOCUS       WP_457578653             179 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578653
VERSION     WP_457578653.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..179
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19524
     Region          62..167
                     /region_name="RfaB"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0438"
                     /db_xref="CDD:440207"
ORIGIN      
        1 msrpstrfia atqifrspas cserqtrpse dfdleaiela rklgiadkih lmgfrqpiap
       61 cmsgvdillv painepfgrt iieammygtp viatdhggnp eaiengvtgf lvepenpqaf
      121 vapmelllkn agewkhiseq arvsalatyg ikphvdgivs iyqrilerka tdgeqhcvd
//
LOCUS       WP_457578655             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578655
VERSION     WP_457578655.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..330
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33980
     Region          39..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtstatdiss pksgglrswl erypflpalv ilivllalng lfspnslsfr sltgllstym
       61 alimlaiaqt yvvsagdidl sagatlslvn vaivvlmerw gggagavlla lalgvligla
      121 cglvnglvva alrlqaivat fatsifftgl alyvmpvagt papalfwrty ggrllglpfv
      181 fyvlaalavl lyflsrtriv tellavgddq qaayqtglpv vavrikgyll cglfsalaaf
      241 cltgdtasgd plvggkmtly svaavvlggs alaggwttvv gsllgaltig lvnslvffmg
      301 tpsewqnfvq glailivlma gvlagrrara
//
LOCUS       WP_457578656             495 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578656
VERSION     WP_457578656.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 495)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 495)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..495
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53917
     Region          29..495
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 magsfmtaap afaagtltvs spqdpgswdp vdtflvnwas vatniydglt yrgpdlklvp
       61 glataweeld ggkrlrftlr egvkfhngep fnaeavkftf drllgeegsk gpqksnyavi
      121 ekveivdekt vdlvlktpdp vlptklagyg amivppkyiq ekgedyfnah pvgtgpfkfv
      181 syepkvgikl eafadhwgga pklsnlnyrf isepatavae lqagrvdlvi pptipigmip
      241 tiqgdsnlei vssagptvya lrfntrdgit kdpkvrkali lgvdrdtiiq silagqadpi
      301 asfqgklsfg fdpamkplpy dpeqakallk eagvapgasv qidvrgndat fnevvqaias
      361 ylqliginat ikpyetnvll ndiipagktg alfqqswggw tldydntays myhsgekwnp
      421 ydkdaeldkl lesqrsitdq akreeilkqi anyaadrsle mplynlnaif gvskrvknft
      481 pvpdsrlrlt dvtve
//
LOCUS       WP_457578658             271 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Ensifer adhaerens].
ACCESSION   WP_457578658
VERSION     WP_457578658.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..271
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28273
     Region          2..260
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 maafvagagw lfsihalaef ppllflgsrf viaglligll arfasfaelg ravrlllpaa
       61 lalavammaw ifglkqttnp gvaafitstg nllvpvfgll ffgwpvgral wisisvalag
      121 mgllflgpga rvevvsallw aasialvkrn steigavata aiqlvvagvv ilavslpveq
      181 mpaavpsiai wgwflasili stclrfvlqf rgqqmifaar asvimccepv wvlvfalafl
      241 gsplslsqil gcavillaml gqvvfrpnsa a
//
LOCUS       WP_457578660             321 aa            linear   BCT 27-JAN-2026
DEFINITION  formylglycine-generating enzyme family protein [Ensifer adhaerens].
ACCESSION   WP_457578660
VERSION     WP_457578660.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510263
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..321
                     /product="formylglycine-generating enzyme family protein"
                     /EC_number="1.8.3.-"
                     /GO_function="GO:0016670 - oxidoreductase activity, acting
                     on a sulfur group of donors, oxygen as acceptor [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35923
     Region          16..319
                     /region_name="FGE-sulfatase"
                     /note="Sulfatase-modifying factor enzyme 1; pfam03781"
                     /db_xref="CDD:397722"
ORIGIN      
        1 mspkmplvde tpaaisareq iwieggtflm gsdkhypeea pahpvkvdgf widvtpvtnr
       61 qfaafveatg yvteaektpd pkdypgalpe mmragsvifd ppkrvtsnsp sqwwnfkfga
      121 dwrrpygrqs nirgkldhpv vqvsyldaka yaawagkdlp teaewefaak gglegaefaw
      181 gdelvpeerf mantwhgmfp tenlkpdgfe rtspvasfpa ngyglydmig ntwewtsdyw
      241 strhpapaqk sccipanprg gdreasfdpr qptihiarrv vkggshlcap nycrryrpaa
      301 rhaheenaat thigfrcirr p
//
LOCUS       WP_457578663             824 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Ensifer adhaerens].
ACCESSION   WP_457578663
VERSION     WP_457578663.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534137
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..824
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85886
     Region          10..71
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(15..17,20)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          74..142
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          163..813
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(462,464,769)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(506..508,571,587..589,618,658..660,680,683,686,705,
                     708)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(770,798,802)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 msaaavsasi pvegmtcasc varvekaira vpgvteasvn lateradvrf dastksadiv
       61 kaienagyga aedtieltie gmtcascvar iekalktvpg vteanvnlat erasvritrg
      121 iataaaleea vrvagyaakr mtgdesvdre gekreqetrk laralliaav ltlpifvlem
      181 gshfipgvhe fvmnnigmqe swylqfaltt lvlfgpglrf yqkgvpalfr lapdmnslva
      241 igtsaawiys vvatfapdll pdgtanvyye aaavivtlil lgrflearak grtseaikhl
      301 mglqaktarv irngetvevp lsdvqtgdtv vvrpgdrvpv dgsvldgtsy vdesmitgep
      361 vpvekvagse vvggtinktg sftfratkvg adtvlaqiik mveqaqgakl piqslvdrvt
      421 awfvpaviai alltfgvwlv fgpdpaltfa lvngvavlii acpcamglat ptsimvgtgr
      481 aaemgvlfrk gealqtlrna aviavdktgt ltkgrpeltd letaegfdrd tvltlvaave
      541 trsehpiaea ivdaakakgl aiaeparfea ipgfgasaev sgrtvhvgad rlmtqlkldv
      601 safadqaarl gsegksplya aidgklaaii avadpikett pqairmlhdl glkvamitgd
      661 nrrtaeaiaa klgideviae vlpdgkvaal kklkqggrav afvgdginda palaeadvgl
      721 aigtgtdvai esadvvlmsg dllgvpnaia lskatirnik enlfwafayn avlipvaaga
      781 lypvygllls pifaagamal ssvfvlgnal rlrafrpvaa aqaa
//
LOCUS       WP_457578664             444 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578664
VERSION     WP_457578664.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..444
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49093
     Region          1..357
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrilvsstv mvgayfavag asgthasaae ltlcwaawdp analvelskd feaksgntmk
       61 fefvpwpnfa drmlnelnsg gklcdlmigd sqwiggaaen gqyiklndff dkegikmddf
      121 ipatvigyae wpknspnywa lpafgdvvgw tyrkdwfsrp elqaefkqky grdlgvpktf
      181 pelkdiaeff qkrqvdgktv ygaaiyterg segitmgvmd vlysygfeyg npkkayeldg
      241 fvnsadavkg lefykalydc ctppghsday msedidayks gqvalqmnfa ftwpgihada
      301 nvggdksgyf pnpagptgvq faqlggqgis vvaasdkqke aldyikwfaq peiqkkwwsl
      361 ggysalrsvv edpsfatsqp yaqtfldsma ivkdfwaeps yasllqasqk rfhdyvvanq
      421 gtakdaldgl sedwkdifed egky
//
LOCUS       WP_457578691             416 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Ensifer adhaerens].
ACCESSION   WP_457578691
VERSION     WP_457578691.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10315023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..416
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47158
     Region          122..203
                     /region_name="Phage_int_SAM_1"
                     /note="Phage integrase, N-terminal SAM-like domain;
                     cl12235"
                     /db_xref="CDD:472283"
     Region          230..406
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(263,359,362..363,394)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mtsgksvsde tgikaiwsah crqeflgrla aqgyarstqr kyeriigkfc aeiekrglss
       61 crldeaavdv lrqamltetn esartyakfc lnrfldhlvd agvaslpeqp vkeptpldrl
      121 reeydaylrq qralseatiy hclrflerfm afrfgktpgd lnaitpddiv aflgrlkvgs
      181 rpyrdktppt hlrnlfkflf wngktrrnla nsvprmvqaq panlprhlqp devqslvqav
      241 rsndpvgrrn yamlllmarl glrspeviai rledidwrtg eilirgkgrl hdrmplppdv
      301 geaivdyirn grkgesrllf vsskipyrpf ddaqilniil rsafektglk ppqkhvgshl
      361 lrhslateml rngasldeig dvlrhrsrmt ttiyakhdie alrsiaqtwp vaggar
//
LOCUS       WP_457578693             349 aa            linear   BCT 27-JAN-2026
DEFINITION  Fic/DOC family protein [Ensifer adhaerens].
ACCESSION   WP_457578693
VERSION     WP_457578693.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Veyron,S., Oliva,G., Rolando,M., Buchrieser,C., Peyroche,G. and
            Cherfils,J.
  TITLE     A Ca2+-regulated deAMPylation switch in human and bacterial FIC
            proteins
  JOURNAL   Nat Commun 10 (1), 1142 (2019)
   PUBMED   30850593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Kinch,L.N., Yarbrough,M.L., Orth,K. and Grishin,N.V.
  TITLE     Fido, a novel AMPylation domain common to fic, doc, and AvrB
  JOURNAL   PLoS One 4 (6), e5818 (2009)
   PUBMED   19503829
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..349
                     /product="Fic/DOC family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /GO_process="GO:0018117 - protein adenylylation [Evidence
                     IEA]"
                     /calculated_mol_wt=38439
     Region          9..221
                     /region_name="FIDO"
                     /note="Fido, protein-threonine AMPylation domain [Signal
                     transduction mechanisms]; COG2184"
                     /db_xref="CDD:441787"
ORIGIN      
        1 maeehpkgsy typnssddpd rtdvlrnrwg vethselrvk eyratavrml eiaegdgpkg
       61 nfdkahlkai hgyifqdvye waghtrnetp vvdgervepi gglskggtsf lpgsriemgl
      121 dealkairdq qalrnatpeq faeragqvla elnyvhpfre gngraqeafi aelgrhyghe
      181 idfsviskpr midasiettn npssdamkhv vqdaldssrr eairaafadl kdcgeeplhh
      241 nvrtaragee itgtvlgagd rlislvterg tvvadrgdlp erllddgeit fgaqsdfsrl
      301 grehparegq sqpapagqpq rdqnpdlkai qaqlaaqrgr grddddher
//
LOCUS       WP_457578702             642 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Ensifer adhaerens].
ACCESSION   WP_457578702
VERSION     WP_457578702.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..642
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=70526
     Region          3..254
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mteiinialn kldadpknvr ktysaegvea laanirvdgy rllqnlvvrr gdkkgryfvm
       61 aggrrlaaln llsdageiak dfaveckere geiateisla enimredmhp ldqyeafdal
      121 akqgkemadi aarfgtteiv vrrrlalarv spvllklfrd edmsfaqlsa ftvsddhqrq
      181 vtvwnslssw nrephsirra lteemipatd kriqfiggla ayeeaggpvk rdlfddrnag
      241 yaldaalvek lvaekleaaa atvraegwkw idcsatapvg yhtmkrhype gialseedqa
      301 aldsaqteyd dlaqsiengv addeaetklk evekridaln araeayspea leqagafvfl
      361 dyygrlaier gfvkadeiae tedrddeges lqdgkgkgep kvpaishsaa liedltahkt
      421 aalrielann pevalvavvh amllrvaypy hseqsalqls ltherlepsm kdaescrgla
      481 afndladnyg hhlpgnpadl fdwlmeqpqd tvlsllafga ahsvnavekk ftdrkkgieq
      541 anqlgyalkl hmpdwfettg dsyfkhvnrt tielavaeak gseaelsvra atkkseavti
      601 adrvvagsgw lpspvrltlp evgpeieagp npddnefpea ae
//
LOCUS       WP_457578711             339 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578711
VERSION     WP_457578711.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..339
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38130
     Region          107..299
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 myhnwldrwd errarrgeee kettdfvlda erafphakgv atleefcrla dqavadpaff
       61 depsgndqaf qkqdgwlrfp sgistdvden nvvstkites gsfdqvlvvf hhwnattrnr
      121 qiakffsrrg vtvveiampy hferrrpgss hadymlsanl grtiqsvrqa vwdgrkllrw
      181 lrsegyreia vlgmslgswv agliaahdpa vskaslflta gsladmvwtg ratrairdsl
      241 epaigltdlr rawaplnmen yahrlarpdl dlhvvlakrd kvvlpelser fmhglkvaga
      301 rpnilhlncg hyslarppyi llaglslkrf lsataksar
//
LOCUS       WP_457578713             444 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578713
VERSION     WP_457578713.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..444
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48350
     Region          29..>338
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 msklehaivv gagigglaaa salashfeki tvlerdelpn gssprsgvaq saqlhfllqg
       61 glaalceifp gldldlaiag avpirygldd rrelpgfdpf pqfdfgvqgy amsrpfveqv
      121 irqrinrlqn vtvrercrat dimvardglv sgvtwegang ssetlradlv idasgrgalt
      181 latlkssgrs qpeqttigvd ilyattvltl pessrdwkiv itvpnlnedt kagalipieg
      241 grwmavvaew haetpvidqs sflkftqclr tptiydaikg atsfgrverf gfpesywrhf
      301 erlddfpqgl ipigdamcrf npvygqgmsv alkeaallkt lldsrtctes plkeltsaff
      361 teasavista wsmaavpdli vpktrgerpa dlqallkrqq mlnqvaaldp eiykvtqeir
      421 hlvkpqsalh hpdivrrleg aftg
//
LOCUS       WP_457578723             197 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Ensifer adhaerens].
ACCESSION   WP_457578723
VERSION     WP_457578723.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..197
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21115
     Region          16..123
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(57,104..105,107..108,112)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(63,68..69,100,103..104,107..108,111,114)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(86,90..91,100..101,104..105,108,112,115,119)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(86,105,108,112,115,119)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(113,119..120)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          135..175
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(136..138,171..172,174..175)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mtsgvslpat sansakagve aekiyedsas gkkddrpgla aclkalrrgd tlvvwkldrl
       61 grdlrhlvnl vddltkrnig lkvlagegas idtstangrl vfgifaalae feralivert
      121 kagleaarar grnggrpfkm tpakirlara amgqpqtkva dlcaalgitr qtlyrfvgpk
      181 gelrhdgerl lkrkklv
//
LOCUS       WP_457578728             258 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578728
VERSION     WP_457578728.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..258
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29178
     Region          19..256
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 maettttsnm tvsttevaie ingmnkwygd fhvlrdinlk vmkgerivia gpsgsgkstm
       61 ircinrleeh qkgkivvdgi eltndlkkid evrrevgmvf qhfnlfphlt ilenctlapi
      121 wvrkmpkkqa eelamhflkr vkipeqanky pgqlsggqqq rvaiarslcm kpkillfdep
      181 tsaldpemvk evldtmvsla eegmtmlcvt hemgfarqva nrvifmdqgq iveqnspaef
      241 fdnpqhertk lflsqilh
//
LOCUS       WP_457578729             384 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578729
VERSION     WP_457578729.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..384
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41890
     Region          172..383
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mttneaslvr asmveaappp vleggiafwl rnnlfatpkd taltiisllv lawlvppalq
       61 wlfidaswmg dgrgvcatva qggsqpdgws gacwafvhak fsqflfgryp mderwraelv
      121 giffvvflvp mlmpkvpykr vnailllvvl pstatillpg gwfgltyvet slwgglmvtl
      181 alsfvgiavs lplgillalg rrsempvikm lctafielvr giplitvlfm asvmlplflp
      241 qgvtfdkflr aligvslfas ayiaevvrgg lqaipkgqye gadslglsfw qkmnlivlpq
      301 alklvipgiv ntfiglfkdt slvsiigmfd llgivrlnfs danwatavtp vsglifagfv
      361 fwffcfgmsr ysgfmervld ksqr
//
LOCUS       WP_457578736             413 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Ensifer adhaerens].
ACCESSION   WP_457578736
VERSION     WP_457578736.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..413
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45796
     Region          228..406
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(262,358,361..362,393)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mnatdylnrs alyrklvygp yrefarvyaa kmsneglgrq ctwrslslfr dlmdwhvgsg
       61 hasqdlsevh vdrflehrfk hwspdtgdrs alrrllsalr eedlipaalp verteheqiv
      121 dvfaaylsne rglaastvgs hkllslrflr evcpagangf aaltpeivig yverhaldgs
      181 adsgkamcgv vraflrylhl kgfismalad cvpsirrwrl aglptflppe kvqrvldacd
      241 rtsamghrdy avlmilaklg lrasevatln lddidwqsgt ifvhgkgrrq atmplrhdvg
      301 taivayirhg rpasacrrvf lrtlaphggf asgcaitmia kqaleragid gyahhgahlf
      361 rhslatdllr sgasfaeigq llrhrsidst riyakldiek lrelslpwpg gvq
//
LOCUS       WP_457578740             253 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Ensifer adhaerens].
ACCESSION   WP_457578740
VERSION     WP_457578740.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..253
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=28502
     Region          13..>217
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mmhekigphh lerkailyvr qssahqvlhn ressalqyam rdrlaalgws hietvdddlg
       61 rsaaggvtra gfdrmvaevc lgkvgavaar evsrfarnsr dwqqliemcr vvdtvlvdqe
      121 avyaprqgnd rlflglkgsl nayeldllrq rslsaryeka rrgelvvtvp vgfvkagdsi
      181 ekdpdrriqe aialvfnkva elgsarqall wfleqgldlp vryangdviw rrpnyatipd
      241 dckpdlrrsi rlw
//
LOCUS       WP_457578743             481 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578743
VERSION     WP_457578743.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..481
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51733
     Region          1..452
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
ORIGIN      
        1 mrigivgggp agiisaiava kvaqaqgrri tidifdpgap frgrsfntfs shmllntsig
       61 vsaldpdnpa gfvdylckee glsvtegdvv prdaasryle vefdkvkngh veltivparv
      121 ddvsldgcar awfhstvgsq aydaailatg lefrrlpdyf aigevispyp srqlaqvnpd
      181 dsvlvvgtrl aavdalvcla aqghrgsisv hsrsgifpgv rrsvikptnr pflneflgyg
      241 rdaekpvstf amflellerh isaagmrltd fvpsgqicga aqlnqdirlc etrenvwegl
      301 mmdvidglnl iwprlpdsek lrfrgeadwl grlahsmplr nariiqrmfs sgqlrsvsae
      361 eaqstsqqir wvvnttglcs anedpllmrv aeksllrfne sggvaveags lrtradlsiy
      421 angsvihgev ftansvysta qgaqhiardl lgggrvgatv sssseliaht sssgsriepv
      481 v
//
LOCUS       WP_457578744             309 aa            linear   BCT 27-JAN-2026
DEFINITION  type VI secretion system Vgr family protein [Ensifer adhaerens].
ACCESSION   WP_457578744
VERSION     WP_457578744.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..309
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=34623
     Region          14..>266
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mkmsgaesai atllaqnryt aivsaafskd evtlislegs eelgtsfhyr vtfvsrrrir
       61 nfadvigqpm tvglkladgk trffngivae fsytglddtr rpiyvadlvp ylnvlklrrn
      121 srvfqnanaa sivkqifsey qkcnfkdlts ttlaareycv qynetdydfv nrlleregiy
      181 yyflhyadrh elvlvdgpgg hkpctpaair tnlslendrf qddifwswre tvalrstevv
      241 lkdynfeipl aqltsaapva pvgtggvpil deelafdris tgegrrnkkd vvsandgpir
      301 qlfvfpggv
//
LOCUS       WP_457578764             420 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Ensifer adhaerens].
ACCESSION   WP_457578764
VERSION     WP_457578764.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..420
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46563
     Region          228..406
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(262,358,361..362,393)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mnatdylnrs alyrklvygp yrefarvyaa kmsneglgrq ctwrslslfr dlmdwhvgsg
       61 hasqdlsevh vdrflehrfk hwspdtgdrs alrrllsalr eedlipaalp verteheqiv
      121 dvfaaylsne rglaastvgs hkllslrflr evcpagangf aaltpeivig yverhaldgs
      181 adsgkamcgv vraflrylhl kgfismalad cvpsirrwrl aglptflppe kvqrvldacd
      241 rtsamghrdy avlmilaklg lrasevatln lddidwqsgt ifvhgkgrrq atmplrhdvg
      301 taivayirhg rpasacrrvf lrtlaphggf asgcaitmia kqaleragid gyahhgahlf
      361 rhslatdllr sgasfaeigq llrhrsidst riyakldiek lrelslpgre vsnepashra
//
LOCUS       WP_457578771             369 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Ensifer adhaerens].
ACCESSION   WP_457578771
VERSION     WP_457578771.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..369
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=40028
     Region          10..269
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(10,34..35,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(17..18,20..23,25,38,40,75,91..94,98,100,136,138,
                     140..141,143,153..154,157,173..176)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(17..18,20..23,25,38,40,75,91..94,98,138,140..141,
                     143,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(21,98,100,136,138,140,157,173..176)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(153..161,170,171..176)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mektpakigr ykvagkigag amgaiyqaed paiarnvaik virsdlpqgg ereqlltrfr
       61 nearaagqca hagivtifdy gqwrgnpyiv mervlgsdlq vlidegqlsl sestkivvqv
      121 ldalahihkq giihgdiksr nivlteagsp kimdfglatn ggeasvgsth ilgtpnymap
      181 eqlmglpidh radlysvgvl lhrmvvgrsp ygtenlaevl hkisdpfsie vletanlpts
      241 iaeviskalq kdvaqrfqsa tefsralrha lsegesrrsg yvghgaqaap dvheplmied
      301 slireitrql aqilgpitsl liqesllvsr sisellekls syvedplera gfvtkfqesl
      361 dklkvrsta
//
LOCUS       WP_457578789             297 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578789
VERSION     WP_457578789.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32274
     Region          8..>174
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          118..276
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 metklaaidl nlfvaleall acqnvsraaq rlgitqpams rslarlrelf gdellirggs
       61 gmqlttrgev lrkslrtamt hvrnavslqn mhsetkltva eglaptllpt llveftsptt
      121 slrastfsid qhaieqllag tvdfavgglh disdgissls vcsepfitvi sphhhgasve
      181 seraflrfkh vclmemghem fpqvnealsa rgvkfsrive lsnimsaall saegevaltv
      241 prsvarwlts tlslvpvapp lsmkpyqisv twadrslcpk rehilsriva tarerfi
//
LOCUS       WP_457578792             217 aa            linear   BCT 27-JAN-2026
DEFINITION  caspase family protein [Ensifer adhaerens].
ACCESSION   WP_457578792
VERSION     WP_457578792.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 217)
  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 217)
  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 217)
  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 217)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 217)
  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..217
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..217
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23128
     Region          50..>185
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mkpeglksis tehgsrdrer lrrllpkppt lrvdrrppgg ppsrsnrssa leksgfavtk
       61 vanakasdtl aaieafvkrl avaenpvvmv yfaghgvqla genyllpvda klgseeelrs
      121 valslgdlts rldalksslq ivvldscrnn pfeqtrglqr glassperlg rivaystspg
      181 nvatdkrrsa grpalvaqka vyafgheall ptpdagl
//
LOCUS       WP_457578795              35 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578795
VERSION     WP_457578795.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 35)
  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 35)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 35)
  AUTHORS   Rosinski,J.A. 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 35)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10596854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..35
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..35
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=3719
     Region          3..>31
                     /region_name="HTH_23"
                     /note="Homeodomain-like domain; pfam13384"
                     /db_xref="CDD:433164"
ORIGIN      
        1 msercriilr cadgiackvv agelgvhkht vgdrr
//
LOCUS       WP_457578799             367 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Ensifer adhaerens].
ACCESSION   WP_457578799
VERSION     WP_457578799.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 367)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..367
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39277
     Region          10..362
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mkeltksrfa alrrtmaesn vglvalapgs hmdwligyhp hpderpclll igpekeaflm
       61 palnaegtre htdiafhnwa ddvgpsdalt aaladvgaak pgrvvldetm radfalllid
      121 alpadtaref tpatlgalrm rkdkseyall kmnagiadra mqaafskirp gmtekelaad
      181 irahfasega apafwivgag gngafphhsa servieegda vvidiggrkq gfpsditrma
      241 ivgrapegyg qihtiverav qaalkaarpg vlakevdaaa rkvisdagyg eyfvhrtghg
      301 mgidgheppy itatsetvle egmvfsiepg iylpgrfgir ledivilrkd gpevlsslpr
      361 dvhvakv
//
LOCUS       WP_457578800             266 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457578800
VERSION     WP_457578800.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29022
     Region          1..252
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mtsifrkayf fliglflslp livvagvsvn qkqtlafppq gfslswygei flnpewrnal
       61 fasvtlavls aalavaialp lswflwrria pwanifqllg vapftlppvi talgmltfwa
      121 tvgfygqpwt avvshaiffv tlplvtlslg ftsidrslve aastmgader tifrtvvlpl
      181 ilpyivsgya fafvlslney ivaymtvgft vetlpikifn alrygytptm asvtvlfvtt
      241 aavifsfvar fgdlpkllga mssdgk
//
LOCUS       WP_457578801             187 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Ensifer adhaerens].
ACCESSION   WP_457578801
VERSION     WP_457578801.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..187
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19719
     Region          2..168
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtkilgisgs lrkasfntgl mraaaenppg gvefdtatlh giplydgdve kesgipdavt
       61 alkqkvmaad gvilftpeyn nsipgvfkna idwmsrpsad iakvfrgrpf alagsspgnf
      121 gtilsqnawl pvmrtlgael rsgkrlmlpk adtlfdeagt ltdtdardrl aafvkafadf
      181 agaegar
//
LOCUS       WP_457578802             136 aa            linear   BCT 27-JAN-2026
DEFINITION  sarcosine oxidase subunit gamma [Ensifer adhaerens].
ACCESSION   WP_457578802
VERSION     WP_457578802.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..136
                     /product="sarcosine oxidase subunit gamma"
                     /EC_number="1.5.3.1"
                     /GO_function="GO:0008115 - sarcosine oxidase activity
                     [Evidence IEA]"
                     /GO_process="GO:1901053 - sarcosine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=14691
     Region          <17..121
                     /region_name="SoxG"
                     /note="Sarcosine oxidase gamma subunit [Amino acid
                     transport and metabolism]; COG4583"
                     /db_xref="CDD:443640"
ORIGIN      
        1 mrrsphsptc pcgfrhrgew lvvseveaps glvrwleelc dggayvvdqs dgrvvfriag
       61 pnvrsilakg igldlhpsaf tvggstnalc ghipvnlart dedtfelivp rsyaeslfdd
      121 lmkmgrafdl taafsd
//
LOCUS       WP_457578804             324 aa            linear   BCT 27-JAN-2026
DEFINITION  2-hydroxyacid dehydrogenase [Ensifer adhaerens].
ACCESSION   WP_457578804
VERSION     WP_457578804.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..324
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=34735
     Region          5..316
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(11..12,14,54..56,77,105..106,109..110,112..113,116,
                     120,122,130,132,134,136..142,144..148,166..167,171..172,
                     272..273,280,286..292,294..297,299)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(55,78..80,103,243,290,293)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(79..80,107,156..160,179..181,184,213..215,219..220,
                     241..243,267..268,290,292..293)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 msskprillt rrwpaaveqv laerfdvtln egdvpltaae laealrtyda vlptvsdrlp
       61 adlfaggglr akilgnygvg ynhidvaaak aadivvtntp gvltdctadi amtlllavar
      121 ragegerqvr agewsgwrpt hmiggkvtgk tlgiigfgri gkamakrchf gfdmdvvfyn
      181 rsridpaeas rygarqldtv edvlkvadfv slhcpgggen rhlinadrla lmkkgaylvn
      241 targdvidep aliaalengv irgagldvfe aepnvperlr glenvvllph lgsateetrv
      301 amgmkvvdni taffdgrepp drva
//
LOCUS       WP_457578805              98 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Ensifer adhaerens].
ACCESSION   WP_457578805
VERSION     WP_457578805.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..98
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10777
     Region          2..86
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mvyiiaylta hpgkgdevvs laaplieatr reagcitydl yrkpaepdvl vfvetwkdka
       61 avdahfeeph lkafqaamad llvearlelv tpekvevl
//
LOCUS       WP_457578806             558 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457578806
VERSION     WP_457578806.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..558
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=60716
     Region          157..546
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mtiisanrrk rmhlvsgail gtfvlahffn hslglisiea metarrgfnl iwhslpgtvl
       61 lygalllhfv malesiyrrq tlrmpareal kivfglslpf llighvtaar veplltgvda
      121 dypdmlrmlw snsvnatrqs lalllvwghg clgawfwmrg rawfpryeil lytvailvpi
      181 fallgfvsga rsiedgyaeh ggygdrsysk pqfdltlled irlglyfgfg gliagtfllr
      241 ampkggrirv rypdgrvatv nlgfsvleas raadiahvsv cggrgrcstc rvriiqgled
      301 qpppedaela tltrigapdn vrlacqfrpv hnvtvvpild sdslgikkqi greggegrer
      361 riavlfcdlr gftsiaehkl pfdtvfllnr yfemvgeave dsggvidkfi gdgalaifgl
      421 kstyteacrq slaaavrisk gletlnqtfr geldeplria mglhagpaii geigygqats
      481 ltavgdtint asrleglake hdvqlavsae lvnraglvie gherldiglr grqatletwi
      541 vgdaagisea lqpapsna
//
LOCUS       WP_457578757             451 aa            linear   BCT 27-JAN-2026
DEFINITION  integrase catalytic domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578757
VERSION     WP_457578757.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..451
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - obsolete endonuclease activity,
                     active with either ribo- or deoxyribonucleic acids and
                     producing 5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=50397
     Region          92..187
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 mvlweasdrl cskrlkplip illpalerhg rlelnnglrd rlltvsaatm drllsevrvv
       61 arsgqrrrpg mssavrrsvp vrtfgdwndp lpgyvevdfv ahsgtsssgs faqtmvltdi
      121 atgwtecvpv rtresglvia aikqarsqfp fpllgvdfdn dsafmnelvv cwcrsqglev
      181 trsrayrknd qawveqknga ivrrlvgygr fvgseatsal arlyevvrlh gnlfqpsfkl
      241 qektrigacv ikryhppvpp varvlahsgv aepdkerlqa rleradpvml fagiravqee
      301 lgrrvdrrgl narseepvav dlhrftvslk tawqagekrp thrrpyrrtk pypkrqsmle
      361 pfelqirawl eadpavsaas vlerlmsadp sgftkkslrt vqmavkawrf etagqiildg
      421 dwmkraplss paaagedngh lsaqnfgnfr g
//
LOCUS       WP_457578823             395 aa            linear   BCT 27-JAN-2026
DEFINITION  PQQ-dependent sugar dehydrogenase [Ensifer adhaerens].
ACCESSION   WP_457578823
VERSION     WP_457578823.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12086000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..395
                     /product="PQQ-dependent sugar dehydrogenase"
                     /EC_number="1.1.5.-"
                     /GO_function="GO:0016901 - oxidoreductase activity, acting
                     on the CH-OH group of donors, quinone or similar compound
                     as acceptor [Evidence IEA]"
                     /GO_function="GO:0070968 - pyrroloquinoline quinone
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41624
     Region          60..385
                     /region_name="GSDH"
                     /note="Glucose / Sorbosone dehydrogenase; pfam07995"
                     /db_xref="CDD:429776"
ORIGIN      
        1 mrhtgagtsg ragkrsravg ilavsvalat fappsagaqd arefpsehgt vrvetlatgl
       61 ehpwsvealp dgglivserp grlrilrdgk lskpltgvpe vaergqggll dialdprfae
      121 trtlyltmaa ngkggygtvv vraklaadgt glidvkelfr msrftgkgqh fgsriaiapd
      181 gslffgigdr gegdraqdpr dhagailhin adgsvpgsnp yaggtgglpe iwskghrnpq
      241 giafdpkdgt lltvehgarg gdeinnpklg hnygwpvity gkdysgaeig egtakegldq
      301 plfywdpsia pgalavyrge mfpewdgdll vaalkyqlla rlerddsgai gseerlfdge
      361 fgrirdvvva pdgallmvtd eedgavlrvs kaatq
//
LOCUS       WP_457578857             254 aa            linear   BCT 27-JAN-2026
DEFINITION  competence protein CoiA [Ensifer adhaerens].
ACCESSION   WP_457578857
VERSION     WP_457578857.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Kramer,N., Hahn,J. and Dubnau,D.
  TITLE     Multiple interactions among the competence proteins of Bacillus
            subtilis
  JOURNAL   Mol Microbiol 65 (2), 454-464 (2007)
   PUBMED   17630974
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Desai,B.V. and Morrison,D.A.
  TITLE     Transformation in Streptococcus pneumoniae: formation of eclipse
            complex in a coiA mutant implicates CoiA in genetic recombination
  JOURNAL   Mol Microbiol 63 (4), 1107-1117 (2007)
   PUBMED   17233830
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Desai,B.V. and Morrison,D.A.
  TITLE     An unstable competence-induced protein, CoiA, promotes processing
            of donor DNA after uptake during genetic transformation in
            Streptococcus pneumoniae
  JOURNAL   J Bacteriol 188 (14), 5177-5186 (2006)
   PUBMED   16816189
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..254
                     /product="competence protein CoiA"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=28678
     Region          12..123
                     /region_name="CoiA"
                     /note="Competence protein CoiA, contains predicted
                     nuclease domain [General function prediction only];
                     COG4469"
                     /db_xref="CDD:443566"
ORIGIN      
        1 mkyalvegir leattgargt cpgcsspmip kcglkrlhhw ahkssiacdh wwepetewhr
       61 gwknqfpaec qeirhvanng dvhiadvkta sgmvlefqys aitpqerasr eafygrmvwi
      121 vngnrlkrdl psfqealtya psaetkaraw llsdqtsaii grwrggshpv fldfgdadfs
      181 spwlpstgll wwltyiprgr viatpvhrqs vvdhflsgap irgfakptpp lsrrsalpgf
      241 eayrarndar rwrf
//
LOCUS       WP_457578847             268 aa            linear   BCT 27-JAN-2026
DEFINITION  NYN domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578847
VERSION     WP_457578847.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181915
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..268
                     /product="NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28500
     Region          6..122
                     /region_name="PIN_LabA-like_N_1"
                     /note="uncharacterized subfamily of N-terminal LabA-like
                     PIN domains; cd11297"
                     /db_xref="CDD:350237"
     Region          195..264
                     /region_name="LabA_like_C"
                     /note="C-terminal domain of LabA_like proteins; cd10146"
                     /db_xref="CDD:199214"
ORIGIN      
        1 mstdtlalli dgdnaspkii tgllaeiany gtasvkriyg dwtqpslngw kecllehsiq
       61 pvqqfayttg knatdgamii damdllytgr fsgfcivssd sdfarlaari reqgvtvygf
      121 gerktprpfi tacdkfvyvd vlggagseaa hvanvekaks dkkpakaeaa ppkaeqgkhk
      181 aehggaasgk ldqvaigmlr kaveassded graslarvgg hlakqspdfd arnygyarls
      241 dlaeasgild vervgdqpkv vmvrlkkp
//
LOCUS       WP_457578819             481 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 9 protein [Ensifer adhaerens].
ACCESSION   WP_457578819
VERSION     WP_457578819.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10466057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..481
                     /product="glycoside hydrolase family 9 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51607
     Region          57..474
                     /region_name="Glyco_hydro_9"
                     /note="Glycosyl hydrolase family 9; pfam00759"
                     /db_xref="CDD:459928"
ORIGIN      
        1 mrypgstrke agsrsggaia gkayarsagh vgvapnqgdk avpclggaqa eavyggwscs
       61 yqldvtggwy dagdhgkyav tgalaaaqll aayergltfa ptsavmrdgl sripengngl
      121 pdildearwe lefllrmmvp dgeplagmvh hkihdtawta apmlpgddpq pralyrpsta
      181 atldvaavaa qgarlfaehn ptfsarllsa arkawvaana npallapksd gfggggdydd
      241 dsisdelfwa atelylttgn geylktlras plweadvfsp ggafnwrdva gfarlqlaly
      301 gralpavdqe tirnsvltsa qhllslqqae pfgivyrpne rrydwgsnql mlqnivvlsa
      361 aydlsgdrvf ldgaregmdy ilgrnamgls yitgygsrsp qnqhsrwyar qrdpqlpnpp
      421 vgslaggpns tfvddiarer lrgcapqtcy vddieaygsn eiainwnapl vyvasflada
      481 r
//
LOCUS       WP_457578811             184 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Ensifer adhaerens].
ACCESSION   WP_457578811
VERSION     WP_457578811.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..184
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=19660
     Region          5..130
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(10,12,68..69,72)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            12
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(67,111..112,114..115,119)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(73,78..79,107,110..111,114..115,118,121)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96..98,107..108,111..112,115,119,122,126)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96,112,115,119,122,126)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(120,126..127)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          142..180
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(143..145,174..175,177..179)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259843"
ORIGIN      
        1 manqifgyar vsttdqelsi qeaalraaga tiirsekksg tstngrdela tliefaragd
       61 tiivtridrl arsiadlsri vetltkkgvh lkateqpidt ssaagkaflq mlgvfaefet
      121 nlrkerqleg iakakaegvy kgrkasidgd tvnqmaadgk gaseiakelg igrasvyryl
      181 kvps
//
LOCUS       WP_457578821             367 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578821
VERSION     WP_457578821.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..367
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=39562
     Region          1..363
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mttpladkik alikthgpis vtdyfslcla dpehgyyrvh epfgkegdft tapeisqlfg
       61 emigiflvha wqqhgkpega viaeigpgrg tmmadmlrvv rrlapdlyas agvhlvetse
      121 rlrkvqsetl gahghkvewh tsfetlpegf lllaanelfd aipirqfvrt aqgfrermvg
      181 ldatdeltfa agvagidpel lptpaqgvae gtifeiapar davmsalcer lkisggtavi
      241 idyghmatgy gdtlqavrdh eydpplaspg radltshvdf eqlarraktd dvqinglahq
      301 gdflvglgll eraaalgrdk daltqetirq dverlagaga gkmgelfkvl avssppvpls
      361 pfrkpka
//
LOCUS       WP_457578863             338 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 26 protein [Ensifer adhaerens].
ACCESSION   WP_457578863
VERSION     WP_457578863.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Kaira,G.S. and Kapoor,M.
  TITLE     How substrate subsites in GH26 endo-mannanase contribute towards
            mannan binding
  JOURNAL   Biochem Biophys Res Commun 510 (3), 358-363 (2019)
   PUBMED   30717976
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Yan,X.X., An,X.M., Gui,L.L. and Liang,D.C.
  TITLE     From structure to function: insights into the catalytic substrate
            specificity and thermostability displayed by Bacillus subtilis
            mannanase BCman
  JOURNAL   J Mol Biol 379 (3), 535-544 (2008)
   PUBMED   18455734
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..338
                     /product="glycoside hydrolase family 26 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37933
     Region          24..305
                     /region_name="ManB2"
                     /note="Beta-mannanase [Carbohydrate transport and
                     metabolism]; COG4124"
                     /db_xref="CDD:443300"
ORIGIN      
        1 mpiavprsvl gagalallav agvtpgraqd svdgidrslt taaitpeare retrtveigv
       61 ydphdavass daltlehvfv ywqkpdraql krkfanaarq gralmlsvep ythaadwrag
      121 gnrlfadigr grfdreitdi ctraadfrgp vyvrwgheme epgerypwar rdsegyktaf
      181 ryfvskcrel apaaryvwsp kghrnlaayy pgddvvdaig ipvwglqkmd vdywgrerrf
      241 gealkekyqr vsrygkpviv aelgvsgsad ykrawyaeil dqqtyrqafp llttvvffnd
      301 kepykwplgy gapdwrldka alkaladrgp keaaelad
//
LOCUS       WP_457578865             194 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578865
VERSION     WP_457578865.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..194
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20576
     Region          11..167
                     /region_name="nicotinamidase_related"
                     /note="Nicotinamidase_ related amidohydrolases. Cysteine
                     hydrolases of unknown function that share the catalytic
                     triad with other amidohydrolases, like nicotinamidase,
                     which converts nicotinamide to nicotinic acid and ammonia;
                     cd01014"
                     /db_xref="CDD:238496"
     Site            order(16,90,123)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238496"
     Site            118..119
                     /site_type="active"
                     /note="conserved cis-peptide bond [active]"
                     /db_xref="CDD:238496"
ORIGIN      
        1 mpkmsvpdna vllpidmqqa fdsapwprrw neavdengla llaawrasgr pvvhvrhdsv
       61 mpgstlslga pgngfrpgfg pmgdealvtk gvnaafigtd ldlrlrrlgv etvvafgist
      121 dmcvstsvrv ganlgyrmil vedacdcfdq pdaeggvisa reihrahvat lraefaevls
      181 taklvealqr paaa
//
LOCUS       WP_457578866             664 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Ensifer adhaerens].
ACCESSION   WP_457578866
VERSION     WP_457578866.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..664
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73865
     Region          3..505
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 msereftvie newirlkdgt elaariwmpa gteadpvpav leylpyrkqg gtslrdesty
       61 pvfaaagiag vrvdirgsge segvidgeyt prelsdgcei vewiaaqpws ngkvgmmgis
      121 wggfnclqva alkppalkav isiastvdry nddihykngc hlsaqlswaa tmlgyqsrsp
      181 dpaivgdrwk qmwmerleke pffmeewleh qrrdefwqhg sicedfdrvg ipalviagwa
      241 dgyrntplka veglgdkaka ligpwvhkyp hfafpkprad fhgeairwwn rwlrdeenga
      301 engpqvrayi ldgprpslrr dsdpgrwvak dawatpemhl fgishdgrlt psaggtgige
      361 vylkspldtg tasgeyftlk pdaemagdqr iddagsltfe taplleaady lgqptltvdv
      421 tcqeptanla vrlvdvhpdg tstrvafgvl nlshrdgnaq pramepgrkt ritltldacg
      481 yrfragnrir vslstsywpl ilptptdpgl sidtaslsla lpqlgahrei avpepenpdp
      541 lpkyreltrg issrtverdm thgmthyriy edtglsehpd tglatqdird etwsiapddp
      601 ssmigtstwt cvakregwsv rtvststlhc tksewiteae vvayegetri fekhfkkrip
      661 rdfm
//
LOCUS       WP_457578870             267 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578870
VERSION     WP_457578870.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..267
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28476
     Region          28..140
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtssfnvqsa agyeqlmgrw srqlappfid fagvadgerv ldvgcgtgsl tfalphaadi
       61 seitaidfsp vfveatikan sdprievqqa dacalpfada sfdramallv lhfvpesgka
      121 vaemrrvvrp ggvvaaavwd hfggmpgmrm vldvaamldg naeqvrsryc fqpmmrpgem
      181 mqsfvsngla dvrqtsllir mdyqsfadfw epiaagegpl gkyagsldag mrtkldaair
      241 aayeagqpdg prsfaavawa crgivps
//
LOCUS       WP_457578871             312 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Ensifer adhaerens].
ACCESSION   WP_457578871
VERSION     WP_457578871.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..312
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32735
     Region          17..301
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mnarstvdgn qmsagtwall allgliwggs fffarvavah vppftlvflr lglaalalhi
       61 yirgrfgmye alagrwrefa lmglinnaip hafiflgqth igaglaailn attpvwtvii
      121 anmatedekl ssakiagcll glagtvvlig psavaglfgt tssvplwall lpvlaaisyg
      181 faatyckrfr dlappvtaag qltastlial pvaaftdtpw llpmppvevi lsilglalvs
      241 tayayilffr imraagatna slvtllvpps aillgylflg etlqaadfag mvlialglav
      301 ldgrilrfrr va
//
LOCUS       WP_457578872             263 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 25 protein [Ensifer adhaerens].
ACCESSION   WP_457578872
VERSION     WP_457578872.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Martinez-Fleites,C., Korczynska,J.E., Davies,G.J., Cope,M.J.,
            Turkenburg,J.P. and Taylor,E.J.
  TITLE     The crystal structure of a family GH25 lysozyme from Bacillus
            anthracis implies a neighboring-group catalytic mechanism with
            retention of anomeric configuration
  JOURNAL   Carbohydr Res 344 (13), 1753-1757 (2009)
   PUBMED   19595298
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Monterroso,B., Lopez-Zumel,C., Garcia,J.L., Saiz,J.L., Garcia,P.,
            Campillo,N.E. and Menendez,M.
  TITLE     Unravelling the structure of the pneumococcal autolytic lysozyme
  JOURNAL   Biochem J 391 (Pt 1), 41-49 (2005)
   PUBMED   15943581
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Fastrez,J.
  TITLE     Phage lysozymes
  JOURNAL   EXS 75, 35-64 (1996)
   PUBMED   8765293
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10157436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..263
                     /product="glycoside hydrolase family 25 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30232
     Region          53..245
                     /region_name="GH25_muramidase_1"
                     /note="Uncharacterized bacterial muramidase containing a
                     glycosyl hydrolase family 25 (GH25) catalytic domain.
                     Endo-N-acetylmuramidases are lysozymes (also referred to
                     as peptidoglycan hydrolases) that degrade bacterial cell
                     walls by catalyzing the hydrolysis...; cd06413"
                     /db_xref="CDD:119375"
     Site            order(57,81,110,112,142,144,183,203,224,239)
                     /site_type="active"
                     /db_xref="CDD:119375"
ORIGIN      
        1 mrrlllallp latllsgcss tdydlmqtas ipprfhdtdp qnfgdrtpqh hnihgidvsk
       61 wngdidwtkv kksgvsfafi kategkdrvd trfpeywqka raagipyapy hfyyfcstad
      121 dqadwfianv pksavylppv ldvewngesk tcrhrptpde vrvemkrfmd rleahygkrp
      181 iiytsvdfhr dnlvdqfkeh hfwvrsvakh pgevyverrw afwqytstgv ipgidgatdi
      241 nvfagsaknw knwvaavsqp kqn
//
LOCUS       WP_457578874             175 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457578874
VERSION     WP_457578874.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..175
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=18524
     Region          <55..156
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mrissvaava aclgmffagm gtsyagdvdk tiktssiptv trttgfpkpd lpqnvqytal
       61 iksyakqygv pvdlahavvk vesnfnpkar gsageiglmq ikpatarmmg ysgsskglyd
      121 petnikfgmk ylamahelsg gttcgtilky naghgakrmn pvskrycgkv qdiid
//
LOCUS       WP_457578876             699 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Ensifer adhaerens].
ACCESSION   WP_457578876
VERSION     WP_457578876.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..699
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=73663
     Region          97..600
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtaassplkr nlsvsqrlat lagaafvgfg svlgvawyeg rqandalqga laaqnglttv
       61 devrlattnl vlnamdsiid reegaiqpar aasiaeilkm letkstdika lagliggsda
      121 lstfdadvae lrqaigtdlk aliegkasad dfgkiddaid gagervatal aglseaattl
      181 vqtrvaeara tsdeafqlql asgliamatl lyllwfhgst lrrgilslrd gmqriqkgel
      241 stklealdrg deigamarsv dlfrlsaiek qsleqsaahs rreiekereq qqqereeavr
      301 riqaaidnlg raltqlaegd lavaidrpfd gnldqlrqnf nqtverlrvv lssvkdnals
      361 iesngrqmrt aaddlarrte rqaasleqts aaldeitvtv rtatqraeea sqmvdqtrtn
      421 aeesgrivgq aiaamarieg asneigkiin videiafqtn llalnagvea arageagkgf
      481 avvaqevrel aqraagaakd ikalvsrsgs evgtgvklvq atgealgrig tdvarinelm
      541 taivmaareq stglneista vgqldqmtqq naamveqtna sshtlaqdae rltdlvgqfr
      601 eghtmqramp taapapvtpa artaapvqtk tpavsavqrp aakgtseavp lrkigaakma
      661 sfptpspaka lmgklagafg nkpgsvpstt asgenweef
//
LOCUS       WP_457578877             416 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457578877
VERSION     WP_457578877.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Linder,J.U.
  TITLE     Class III adenylyl cyclases: molecular mechanisms of catalysis and
            regulation
  JOURNAL   Cell Mol Life Sci 63 (15), 1736-1751 (2006)
   PUBMED   16786220
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Linder,J.U. and Schultz,J.E.
  TITLE     The class III adenylyl cyclases: multi-purpose signalling modules
  JOURNAL   Cell Signal 15 (12), 1081-1089 (2003)
   PUBMED   14575863
REFERENCE   5  (residues 1 to 416)
  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 11450078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..416
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=44092
     Region          3..397
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Region          226..396
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(231,233..238,273,275..277,280,342..344,348..349,
                     352..353,388)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(233,277)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(238,250,253..254,257,261,273..274,330,333,343..346,
                     349,388)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 mswtsavrsl lelgaanaae gdregilvan vaacvivvtt tsfaliyaly gepsliplvy
       61 anlalavaaa mtplfhrfgr vasglwefgi cvvvlvwias yvgrdsgvll tllgvtpvaf
      121 ailgfqnial vtvlsamaai tviaasiafp qaragvygdt rflqllhsss iitvtlmcfa
      181 tiyyafqmar eaqgrlarlm tsimpdeiva rllrnereti idefehatvv lidivqfval
      241 snslgpertv nllnelfsef dclaaatgve kiktvgdayl avagvparhp tpekaaavfg
      301 fgaiaaarei gerhgvvlkl ragmasgsvt agvlgrakya ydiwgapvnl aarleaigkp
      361 gcitttaeir qrlgesflfi csgredikgf gpteiwttrm pdpdacvpgi rahtat
//
LOCUS       WP_457578878             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578878
VERSION     WP_457578878.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32439
     Region          11..291
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mpnllnetpg liafvrtves gsfsaaakil rtspsavsrs vgrleslvra rlflrstral
       61 vltfegqslf dkvapllrql dtsdevasre dtlagrirfs mpsdlaryfl tpifrdfasa
      121 fpaiklevgl adrqvdlnre dydvafrvgg ggqgelrvrk lanvnmviva spaylekhgk
      181 prsvdeasal pfaryivrgh pspmvfaggk qfspqgrvdc ytgqalraaa lhglgaallm
      241 kcvvqdelnd grlidistel dlppqplnvv hafgsmiplr vrrfcdfiad qtksipgl
//
LOCUS       WP_457578879             173 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Ensifer adhaerens].
ACCESSION   WP_457578879
VERSION     WP_457578879.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..173
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19737
     Region          9..166
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrghppasdr feedvlalvp alrryarslv rsdpdgedll qdcvekvlsr raqwrgvnlr
       61 awaftimtnl grnrhryvam hpqvaldedl gleaethesd plersrlera lnglstenrs
      121 vlmlvviegy ryqdvaemma ipigtvmsrl srarrqlaea mkddnvismr rpk
//
LOCUS       WP_457578882             404 aa            linear   BCT 27-JAN-2026
DEFINITION  multidrug effflux MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457578882
VERSION     WP_457578882.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..404
                     /product="multidrug effflux MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42371
     Region          11..389
                     /region_name="MFS_MdfA_MDR_like"
                     /note="Multidrug transporter MdfA and similar multidrug
                     resistance (MDR) transporters of the Major Facilitator
                     Superfamily; cd17320"
                     /db_xref="CDD:340878"
     Site            order(21..22,25..26,51,54..55,112,143,146..147,230,233,
                     353)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340878"
ORIGIN      
        1 miiqtsfrer ivlyalltsl tsisidallp glrqigadvg vapplstqhv islfilgmaf
       61 gelllgplsd amgrkralvl glgvyalgtv iamvanslem vilgrflqgv gvsgpkiatr
      121 amirdqfegd amarvmsfmf tlfilvpmla ptlaqgiitv agwrsifavy laaagvlglw
      181 lvmrqpetlp adkripfrlg lllsngrril shrrvtlliv atglvfgaql lylstaadlf
      241 fdaygigetf plyfamlamg iglasflnak lvqrfgaeam arrgfvglaa aglamlaasl
      301 ywggrpplam llvlgfaaff avgvlfgnln amamrslgqv aglgaslias gsslvatvfs
      361 iavgafydgt tlnlsagffl agvgalvlae lalradaspv eafr
//
LOCUS       WP_457578883             294 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457578883
VERSION     WP_457578883.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..294
                     /product="SDR family oxidoreductase"
                     /EC_number="1.6.5.2"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=30307
     Region          6..281
                     /region_name="TMR_SDR_a"
                     /note="triphenylmethane reductase (TMR)-like proteins,
                     NMRa-like, atypical (a) SDRs; cd05269"
                     /db_xref="CDD:187578"
     Site            order(9,11..14,37..38,41,55..58,76..79,145..147,178)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187578"
ORIGIN      
        1 mpdtllvtga tgqlgklvld qllasgiapa riiatsrdta kladyiargv qarvadfddp
       61 asldqafaga driliistda ldqpgkrlkq hlaavaaakk agakhivyts mpspetsvip
      121 fapdhlgten aikatgipyt ilrngwymen lfmalphale tgqwysssge grlahiargd
      181 takaaaaala astseshtyt ltggelrstd eiaalvakat gkslnvvhis dealagglks
      241 aglpdflipi vvsfdantrg ghidmvtgdv taltgatpvt laafleaska rlas
//
LOCUS       WP_457578885             490 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Ensifer adhaerens].
ACCESSION   WP_457578885
VERSION     WP_457578885.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..490
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53941
     Region          69..478
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(77..78,119,174,176,290,343..344)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(77..78,119,174,176,290,344)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mkafnyllsc slaasftlla ttshaqeakg wdrtvrtady lepaiprpaq eqtaadrlre
       61 fetrtgrkpn ilillvddlg ygdlgafggg amlgaptpni dklateglkl tsayatpvct
      121 psraalmtgr iparsgltrp llasdhptkn pwadevsaak llsdngyvtg lsgkwhigea
      181 kgmqpqdvgy defhgflsvv seytqymdsr kysqlmldpq rletfkslse yngvvegkkg
      241 gdlkivyple tqkqmgnvdq dfanwsvdfi kraakdnkpf ylihafakvh fdnyaadgye
      301 grspaklpyr davvevddiv grltktlqea gqadntfvff tsdngpeeds ypdsgftpfr
      361 sgkgttwegg vrvpgiaywp gmikagrisd glfdlmdlfn tslalagikd kipteryidg
      421 vdqssfllad dgqtsrqavf synqaefsai rwenfkgyfk vmqydqpfsn ismstfspvg
      481 vapldlryls
//
LOCUS       WP_457578887             282 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578887
VERSION     WP_457578887.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..282
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30623
     Region          6..279
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mnaggwadle lldhlvrgat lsqaarslgv dqttvsrrla alerrvgaal fdridgrltp
       61 tpvlspvver lrtiseeasl slatllrrta elqglvrvts igfvlsaila palarleqrh
      121 pgltldlvad nqmlsierre adiairmart gedsvrvksl gtlrfrlfrp rgqgegpcpv
      181 vrygpalahv pemqaldrlr pdarvaltad kleilmeaal slgaelmlpe vsasrdprfe
      241 vvdepgaaae rpvylmmhpe rarvpsvaav aafieeavrg wk
//
LOCUS       WP_457578888             185 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Ensifer adhaerens].
ACCESSION   WP_457578888
VERSION     WP_457578888.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..185
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20105
     Region          17..184
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtdapwhadp ltwgtgphlf evfleptdpy sakafgklda llaragadri tikirlqsqp
       61 whmysgvvvr cilaastlag gketaktvma avaahreefe fthhaggpnm dvtpntiier
      121 legysgvqlk aafaipdldr eikwhcryar qngihvsptf midgivrpdv ssgddvsawa
      181 aklla
//
LOCUS       WP_457578889             113 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578889
VERSION     WP_457578889.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..113
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12145
     Region          <17..86
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(38..40,50..51)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mptgssraaa issrsrgeaa aygvlthhff gqafiemlmv gtswrrrgla gtliahfqsm
       61 ssgaklfsst nmsnrpmqdl lvkagfrpsg yidnldendp eivfysppks svt
//
LOCUS       WP_457578891             193 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578891
VERSION     WP_457578891.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..193
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21484
     Region          14..180
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrpsaantgn rpavtlttdr lalrpttpad aqrafeiqsd wdvtrmlrma qfppdpddmt
       61 gwfgehrqew iagtafrfai drrgrmiglv dldeidgeeg elgywlekps wgqsyafeaa
      121 qavvsfafeq lglarlksgh aadnpasgkv llklgfrpek tmqkasrsrg eeilhqsysl
      181 aseawrnrsg adr
//
LOCUS       WP_457578895             217 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578895
VERSION     WP_457578895.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24383
     Region          7..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 maepfvvyga sgsgsvpiea vlsligvpyr veehapwegk qeadrlarin plrqvpalal
       61 ptgelmtesa ailiwladah pqsrlapait dpkrpaflrw mtfvsaaiya lywitddpsr
      121 iaereedhat vkarvfdrva hcwqrmgael qpgkyllgde lsvldlyvat asrwspgrrr
      181 fyevaptlad ivrrvdtdpk lvtlwterfp ftegwer
//
LOCUS       WP_457578898             512 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457578898
VERSION     WP_457578898.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 512)
  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 512)
  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 10612637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..512
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=56775
     Region          207..323
                     /region_name="HATPase_c_3"
                     /note="Histidine kinase-, DNA gyrase B-, and HSP90-like
                     ATPase; pfam13589"
                     /db_xref="CDD:433332"
     Site            order(211,215,218,241,243,245,247,274..277,290,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340391"
     Site            order(254,277)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340391"
ORIGIN      
        1 mkflilrvlk hselgmfhey rrqgkerskq rainfdgavv drvfptaldt driplelrye
       61 tdngiavkqq wltrqaknwr fegncpsdkv ydfvepgclf amevdagakp atgdwavfpa
      121 nnevttgvls dgataeltra gmialhgeeg vrvqgllnda kpemfgrdre tveimngggs
      181 vtgrkrlppr pkrlaeiigk tghslpsava dlvdnsisad ateiditfap pdsgngrwlt
      241 irdngdgmsg peldeamtlg sdveyesnsl gkfgfglkga swsqarvftv vtrrrggsls
      301 hltwdidnlg dwepsdaple ewernatalg eqgtailwke mtppaaapvv pgvspysaev
      361 melerhlglv fhrflegeak nrkrvtirin gvevrpnnpv ghplvepyel kpirmptnsg
      421 detiaigsgv alqrfhqicd aehdrrcddl isqtymrkrp qfhfgvslpr tpsseivgng
      481 pllalrrenq pqrvtvpiar shvlryrmek iw
//
LOCUS       WP_457578899             111 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578899
VERSION     WP_457578899.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..111
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12355
     Region          10..62
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mtlymlnerf lttkqaaahl sicektlldh vakgnlecvd vgtgtrafrr fspnqleqft
       61 rrlqklppcp strevrtagv ahtsvapafs diqkpttrre vfgplrnqtk s
//
LOCUS       WP_457578900             333 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Ensifer adhaerens].
ACCESSION   WP_457578900
VERSION     WP_457578900.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..333
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=38939
     Region          20..315
                     /region_name="XerC"
                     /note="Site-specific recombinase XerC [Replication,
                     recombination and repair]; COG4973"
                     /db_xref="CDD:443998"
ORIGIN      
        1 mkeqaaedlk rlsatgaapl tfddaagryw revgqywsrd kqyhavisrl vdhfgktrld
       61 qidhvavael ikkrrseprw gkaklkhaev rpvcnttvns hvlkplktif rrarvawgyh
      121 lpkepiwrel klkqpeevvr elddneksal drsvrddyqa wyqfthlsar rlaetlirwp
      181 dvnwaaneiv trgkgdrivr tpitrsirki ldgergrhpe fvftfvaern mprygivkgq
      241 rypityrgav trwrrdlaks evknfwlhgl rhdratkvlr tsgnlklvqr vlnhaqistt
      301 aryahvtddd vrralerstm srnesrrspd epd
//
LOCUS       WP_457578903             138 aa            linear   BCT 27-JAN-2026
DEFINITION  S24 family peptidase [Ensifer adhaerens].
ACCESSION   WP_457578903
VERSION     WP_457578903.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Luo,Y., Pfuetzner,R.A., Mosimann,S., Paetzel,M., Frey,E.A.,
            Cherney,M., Kim,B., Little,J.W. and Strynadka,N.C.
  TITLE     Crystal structure of LexA: a conformational switch for regulation
            of self-cleavage
  JOURNAL   Cell 106 (5), 585-594 (2001)
   PUBMED   11551506
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459250
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..138
                     /product="S24 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=15351
     Region          18..133
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 mpgeqlvghr dlpifaaaqg gdghvivtfd aveyvkrpsv legvkgaygi yltgssmipa
       61 yepgdmalvh phlpptrdkd vvlyhvppan daeaiikrlv sfndrewtlr qynpflefte
      121 srvewsfchr vvgkysar
//
LOCUS       WP_457578906             193 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578906
VERSION     WP_457578906.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..193
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20761
     Region          4..191
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 maevlvfhha qgltpgmhaf agdlraaghv vhlpdlfegr tfasieegva hieavgfeem
       61 rergvrlada lpenlvyagf sfgvlpaqkl aqtrpgarga llfyscipis gqwsfgpwpa
      121 gvpvqihgmd ndpifvgegd vdaareivek aedaelflyp gdqhyfadss lpsydaaata
      181 lamkrvlafl eri
//
LOCUS       WP_457578912             655 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578912
VERSION     WP_457578912.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..655
                     /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=72278
     Region          1..349
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          403..626
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mqyrpeidgl ralavvpvll fhagfglvsg gfagvdvffv isgylitaii hreisdgnfs
       61 iarfyerrar rlapalllvc avcipfalmw mlpeelnsfg kslyavnlfa snfffwdqtg
      121 yfapstallp llhtwslave eqfylvfpll llllhrfsra tllkvvaalv llsfaatqvf
      181 anldpaanfy llpsrfwelg vgallalvgv ekldlskgsr ellsalglla ivasylfvve
      241 safypgwttv pvvlgtalvl afgrsdtvvg rllslkplva iglisyslyl whqpvfafar
      301 lrsiedipae gyallialcf vlaylswrlv eqpfrkpgrf srravfgatl aagsaaiafg
      361 ftldgsdgla arnrelaqls epsvglgkkc davadlrcas npkpevavwg dsfarhlvdg
      421 iiaskpdvrl vqlaknncgp flnlspimpr lgrdwsddca ryneevrrfl lanrsiryvv
      481 lssqlsqylk eekvlvdgrs evttetklli dglratfawl rsngfepvfv aptphdgrdt
      541 glcvartrll glsdrhcepv lktvreydrd vlnvvadiad eypvvsfmdy lcdddsckie
      601 dkgvalfedf ghfskegsrq mgrafdfyra fieaakgrpv aeratdakaf dnaal
//
LOCUS       WP_457578913             197 aa            linear   BCT 27-JAN-2026
DEFINITION  methyltransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457578913
VERSION     WP_457578913.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..197
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21019
     Region          89..197
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 msttlpailm lvvglstlal ailrrvqsgr spvvltygdd aegfagrlfr livaalvihl
       61 lavamlpasv daalgripal dtpilhvvgl almtlggglt mlsqwamrhs wkigipekqd
      121 aplvtsglya fsrnpiyvgm vtaligtvla vpnvisvala lsawisisyq irmeethlak
      181 vfgdaygayc rrvrrwv
//
LOCUS       WP_457578919             392 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Ensifer adhaerens].
ACCESSION   WP_457578919
VERSION     WP_457578919.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..392
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41791
     Region          2..357
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtkelgvgii gcgnisttyf klaplfrgik vvacadinpa aaearaaeyg vkaesieall
       61 anpdvdivvn ltipdahypv skaileagkh vysekplvls leqgeelrai akakglsvgc
      121 apdtflggah qlarsyvdag kigrvtsgtc hvmspgmemw hpnpdffflp gggpildlgp
      181 yyianlinli gpvkrvaala tmanptrtit seprkgevip vktptnihal lefengatit
      241 lsaswdvwsh rhanmelygt egslyvpdpn ffggtveasg rdkkieplep wehpfgvanq
      301 ehpqgpmany rtagladmal ailegrdarc sldralhgvd vmvsilksge egrfielstt
      361 ctqpaalgie earallrete eemsgnrvaa as
//
LOCUS       WP_457578922             723 aa            linear   BCT 27-JAN-2026
DEFINITION  CHASE2 domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578922
VERSION     WP_457578922.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=77710
     Region          14..647
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mtrsqlfgvl igmtvvafft ilraqdpqll rqardvtfde yqriaprrfe pmpvkiidid
       61 easlrelgqw pwprdrlakl tdrlsemgaa aiafdvlfae pdrlsprtvv rdvggvdpsf
      121 laalpdndei faeairdkpv vlgfgltneg sylppvkagf altgestnea pprlraatpl
      181 rpqleanaag lghislnpgs ssavvrtapl flsdgqqfyp slamealrva qgastyvlaa
      241 apdvantlta vkigdfvvpl mstgevwlyv tpdtteryis arriladgep spdiragieg
      301 sivfigtsaa glqdvrttal gqnvpgvsih aqiveqilsg rylsrpdwan gleilsiala
      361 gtllvllttf vspvvalvcg mavtalalva swiafyyggr lfdplapila asithfaata
      421 yrflvtdrer revrqafgry lspsllyrie htrnalslgg ddreltvmfv dvrsftemse
      481 rmtptevvaf lntlldalsr hvlanegtld kfigdsimaf wnapvdvanh pqkavraalg
      541 mretlarlna dnafgfgadq evrigigiht glacvgnmga etrfnysavg dtvniaarie
      601 aackdvnidi lvseataqal pdhamldags lglkgkttrt rvyavagden laaspafadl
      661 rglhdrlvaa lgartqtsrs iinaaklkaa altpalagfy arigrradhf aqttdentkr
      721 pae
//
LOCUS       WP_457578923             584 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457578923
VERSION     WP_457578923.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 584)
  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   2  (residues 1 to 584)
  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   3  (residues 1 to 584)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   4  (residues 1 to 584)
  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 11573933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..584
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64851
     Region          6..167
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(10,12..17,51,53..55,58,109..110,114..115,118..119,
                     156)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(12,55)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(17,28,31..32,35,39,51..52,103,108,109..112,115,156)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          182..313
                     /region_name="TolBN"
                     /note="TolB amino-terminal domain (function unknown)
                     [Signal transduction mechanisms]; COG5616"
                     /db_xref="CDD:444347"
     Region          363..>557
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          414..442
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(415,418..419,422..423,425,449,452..453,456..457,
                     459..460,483,489..490,493..494,497)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          447..477
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          482..512
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          519..546
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 merklavila advagysrlv atdeegtlat latycetisg laaehggrvf gaagdslvae
       61 fqsavqavra avaiqrtlqr rnadlpperr mefriglnlg dvvvdggnll gdgvnvaarl
      121 qqvaqpndic isgalhdqie gklefpmqrl geralknipr pvlvhrvewr enpaggdlpg
      181 mplslpdkps iavlpfvnms gdpeqdffad gltediital slyrwffvia rnssfaykgr
      241 avdvkqigrd lgvryivegs vrrsgsrvrv tgqlieaetg nhlwaqryer efadlfaiqd
      301 eitqhvvaai epeiligenr raqlrgtdnl gayechmrgt llhnaqdsaa hfdeaiewqr
      361 raialdpefg rahmmlarsl farcffgfsk didrdsaelq aeaaravvid dhdpychyvm
      421 clanfaaqrp haaveeaqqa idinsnfala hmalgwariy igrfaesldp lhkalrlsph
      481 dpltylflnr malahyhlgn ydealrcaer alllrrtyfn lvmlitclgq ldridearkl
      541 lpeaianapn dvprywrfft ayvdpadhah fndglvkagl pmvp
//
LOCUS       WP_457578918             824 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-mannosidase [Ensifer adhaerens].
ACCESSION   WP_457578918
VERSION     WP_457578918.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..824
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=92029
     Region          17..666
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          743..811
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mlsedftrta irldlagdwq lssvdnshal amelpgdvhs allkagvidd pyvgrnendv
       61 qwvahkdwvi ertvtvgadd iagywyldle yldtvasvfv ndklvleaen cfrryrpdvs
      121 ktlvagenri rivlhssiae garrqaeqpf yvpyhpgnsp iangnmlrkp qchfgwdwnl
      181 aiaplgvyge ialcrleiar iehvtskqvw ledgsvdlvv tltlfadgpg ivpvhfslde
      241 drerldcavg kgetrithvf tvsepkrwwp agsgeqdlsr ltvevpqeqv trqigfrtve
      301 lltdkdeags rfafrvngre ifckganwip adalasrvtr egvedlltsa vdanmnmirv
      361 wgggfyepdw fydlcdrlgl mvwqdfmfac nlypstpdfl envaaevdyq akrlsshpsi
      421 avwcgdnelv galtwfdepr kdrdrylvsy drlnrtieva lkaalpeaiw wpsspasgyl
      481 dfgdawhadg sgdmhywsvw henksfdnyr tvrprfcsef gfqsytsmpv irqfsaekdl
      541 niaspviesh qknvggneri agtmfryfrf pkdfpafvyl sqvqqglair tavdywrslk
      601 phcmgtlywq lndtwpvasw ssldyggswk amhymvrrff qpvsvaaips adgkeiafsm
      661 vndtaepvtv elqtflvsld gqrtplaava ctcspdraat latiaafdip egdllfwsfe
      721 asngmrgegh hvngtykald lkpsgltldv apagegafdv tvkasglalh vmieadvagr
      781 ysdnafdlla getkvirftp kvplgagdlp rfsafdlesc qgkg
//
LOCUS       WP_457578925             511 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457578925
VERSION     WP_457578925.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 511)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 511)
  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 511)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..511
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55612
     Region          152..488
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msiaaststd kiivdksrsh rnkavsrtvr atrerlqtgs svpsgferem lnlyidsalh
       61 gaiaipvlvt liaavgiyls gnlgfvlwav mtlsahavtl ffarrarred isaekvpvwr
      121 rrfllgqvlm glcwatfvaq dcascgnvrf gffegtvllv alaatamgtf llrnallytf
      181 apvvaalafa slttgdviym gltgvislsl lflvlmtdrm nrasvhilsv qsekddliae
      241 levaksmsde arrraeeanl aksrflasms helrtplnai lgfsevmste vlgplsnpty
      301 keytndihrs gehllnline ildlsrieag rydlnedsvs lvdiaedcig mvqlkarakn
      361 itihqqfehg mpsvwideks mrqvilnlls navkftntgg evtfkvgwta gggqylsikd
      421 ngpgipeeei pivlsafgqg siaiksaeqg tglglpivqa ilakhngefi lrsklregte
      481 aiailparrv leslpaiedv aapvrrrksf a
//
LOCUS       WP_457578928             279 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-2,3-diacylglucosamine diphosphatase [Ensifer adhaerens].
ACCESSION   WP_457578928
VERSION     WP_457578928.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Bohl,H.O., Ieong,P., Lee,J.K., Lee,T., Kankanala,J., Shi,K.,
            Demir,O., Kurahashi,K., Amaro,R.E., Wang,Z. and Aihara,H.
  TITLE     The substrate-binding cap of the UDP-diacylglucosamine
            pyrophosphatase LpxH is highly flexible, enabling facile substrate
            binding and product release
  JOURNAL   J Biol Chem 293 (21), 7969-7981 (2018)
   PUBMED   29626094
REFERENCE   2  (residues 1 to 279)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..279
                     /product="UDP-2,3-diacylglucosamine diphosphatase"
                     /EC_number="3.6.1.54"
                     /GO_function="GO:0008758 - UDP-2,3-diacylglucosamine
                     hydrolase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31406
     Region          14..250
                     /region_name="LpxH"
                     /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxH
                     [Cell wall/membrane/envelope biogenesis]; COG2908"
                     /db_xref="CDD:442152"
ORIGIN      
        1 mmaaqqdnsa rklrtlfisd vhlgskaakt dylldflrhh eaetivlvgd ivdgwrlkrs
       61 wywpqncndv vqkllrkark garivyipgn hdeflrdfpg vhfggievaq rymhegadgr
      121 kylvlhgdef dvvvrnarvl aylgdwaydt aiainiglaa vrrrlgmpyw sfsswaklqv
      181 khavnfigef qkvvadearr hdaqgvicgh ihhavieeig diryinigdw vesctaiaeh
      241 hdgtmelitw hqmrggaseg easgeadkll aqlltqraa
//
LOCUS       WP_457578932             283 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578932
VERSION     WP_457578932.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 10007405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32119
     Region          1..283
                     /region_name="SbmC"
                     /note="DNA gyrase inhibitor GyrI/SbmC [Replication,
                     recombination and repair]; COG3449"
                     /db_xref="CDD:442672"
ORIGIN      
        1 meervawaty eqrlhrvsdy iyghldgdld ldrlseiacl sphhwhriyr avhretlagt
       61 vkrlrlqraa adlaqtdlpv atiaqrsgyp nlqsfnrtfk aayglppary rkegshvafe
      121 tastegipdm yevtlkdvea fdlvgvahtg symeigkafe tlygtlfsrq lfrpdmemig
      181 iylddpelvp aeklrsfacv sargpmpaea pltpqhldgg ryavlrhkgp yadmpkayqw
      241 lygtwlpqsg rdirdslmfe kylnnpreva ptellseiyl plk
//
LOCUS       WP_457578933             276 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA methyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578933
VERSION     WP_457578933.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Somme,J., Van Laer,B., Roovers,M., Steyaert,J., Versees,W. and
            Droogmans,L.
  TITLE     Characterization of two homologous 2'-O-methyltransferases showing
            different specificities for their tRNA substrates
  JOURNAL   RNA 20 (8), 1257-1271 (2014)
   PUBMED   24951554
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..276
                     /product="RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=30461
     Region          12..253
                     /region_name="TrmJ"
                     /note="tRNA C32,U32 (ribose-2'-O)-methylase TrmJ or a
                     related methyltransferase [Translation, ribosomal
                     structure and biogenesis]; COG0565"
                     /db_xref="CDD:440331"
ORIGIN      
        1 magtnserel laegpaiila ypqlgenigm varamanfgl aelrlvnprd gwpsekarsa
       61 asradhvida aklygsveea iadlnfvyat tardrdgykp vrspivaart lrqrfqtgek
      121 tgilfgrert gltneevala deivtfpvnp afaslnlaqa vllmsyewlk tgmefedqts
      181 fqaieqrpat kehlqglfeh veealearny frsadkkpkl venlravltr psfteseiqv
      241 lrgvissldr ftrenprgsg apgehsrkar dkgdse
//
LOCUS       WP_457578935             444 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Ensifer adhaerens].
ACCESSION   WP_457578935
VERSION     WP_457578935.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..444
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47208
     Region          261..435
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 msghqanrtf gkrkqnhvli lasgdkvrhm tvrpwmaaia vsfagvcsig ylaatsylvl
       61 rddliggtia rqarmqheye dritalraqv drvtsrqlld qqvveekvek llrqqmalts
      121 rngklgalve raessgvtta tdapaavepl ayekradasi sgsvkaiekl mglnvapvsa
      181 aavpalayaa pdagesssdr adrifskvtl slkdvereqm trvqrltdga aktsdairli
      241 vgrtgvdlpv ddvaelipan disgsaetai ggpfvepvnd ddfgrslaal dtalleldrt
      301 raevrklpfg npspasdits dfgnrldpfl grlalhagid fratvgtrir saapgtvtna
      361 gltggygnmv eidhgngvat ryahlstvlv kagdrvkage viaksgntgr stgphlhyei
      421 rlngnavdpm rfldastkla symn
//
LOCUS       WP_457578939             389 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Ensifer adhaerens].
ACCESSION   WP_457578939
VERSION     WP_457578939.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..389
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=43906
     Region          9..388
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 marnklsetk iktlskpgiy gdgdglylrv qkggsknwvf iyrrgdkrne lglggygqgt
       61 apvplalare kadvirqqla rgedprgdrv sikpktfkdc mddllkakes ewtndkhadq
      121 wvmtlrdyak plhdlpiadi vigdikdcli phwterpeta erlrariqav idygiahewr
      181 tagnparwkg llekvmpkrq kltrghhaam avkdapeava klrkskgkaa raveflilna
      241 nrtaevrgav wpefdfdekl wiipatrmkk krihrvplcq ralrileemk qkatsdlvfe
      301 gaksgkpisd smmtkalraa skdkaatlhg mrstfrdwag dftdharevi egalahiegd
      361 ateqayrrsd aiekrralls dwelyltks
//
LOCUS       WP_457578938             818 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Ensifer adhaerens].
ACCESSION   WP_457578938
VERSION     WP_457578938.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 818)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..818
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=92313
     Region          19..800
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mvspetasmk etasgksaap lsadelrlmd aywrasnyls vgqiylldnp llreplkreh
       61 ikprllghwg tspglnmlyv hlnrvikrdd ldmiyiigpg hggpslvaha ylegtytefy
      121 pniaedaegm qrlfkqfsfp ggipshvape tpgsihegge lgyalshayg aafdnpnlvv
      181 acivgdgeae tgplatgwqs nkflnpardg cvlpilhlng ykianpcfla riphdelkkf
      241 fegmgykpyf veghdpakvh qqladvldta taeirqiwdd arirgnlkrp awpmiifrtp
      301 kgwtcppeid gkkcedywra hqvpmgemdk pehirilekw mksyrpeelf tdegrlkpei
      361 aalapsghrr msdnphangg lllrdlkmpg frdyavdvps pgattveaar vmgkflrdvm
      421 knnmdaknfr lfspdennsn rwqdvlevtd rcymaeiype ddhlspdgri mevlsehqcq
      481 gwlegylltg rhgffscyea fihiidsmfn qhakwlkvcn eipwrrpvas lnyflsshvw
      541 rqdhngfshq dpgfidhvvn kkaevvrvyl ppdantllsv tdhclrsrny vnvvvagkqp
      601 gpqwltmeqa vrhcsmgvsi wdwasndans epdvvmaccg dtptletlaa vqllrehlpe
      661 vkvrvvnvvn lmklqpaeeh phglsdsdfd giftrdkpii fafhgypwli hrltyrrtnh
      721 gnlhvrgyke egttttpfdm vvlneldrfh lagdaidrlp qlgaraayfk qaiqaklieh
      781 reyiekhgdd mpsisgwkwg vngvqpakae tstegdnv
//
LOCUS       WP_457578940              67 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578940
VERSION     WP_457578940.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..67
                     /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=7234
     Region          1..66
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mspsndnyal islkdtcalt smsktmihrl rsegrfpaav algekriafs rqevqgwiaq
       61 klaaraa
//
LOCUS       WP_457578949             568 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Ensifer adhaerens].
ACCESSION   WP_457578949
VERSION     WP_457578949.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..568
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63260
     Region          7..565
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 meidvekhph vaaghayald vvagrisace yvkqacqrql ndlaraeegw ayyfdhdaaq
       61 kvctftcflp hikgplagqs ltlepwqsfi lttafgwlrh dngkrryrra ytevprgngk
      121 ttlsdgpaly cgfgekegga evysaartrd qakvafaaaq amlrratglr nalgidveah
      181 riiqmrsnsy fealsadads ldgknvhfal idelhahrdr svydaietga gkrnqsmvwa
      241 ittagadktg icyehrayti nllkgtaedd tyfgiiytid kdddwteeat wrkanpnygi
      301 svepehvaal crkamsspas qanfltkhln vwiqtnealy dmrawdrcfd edldiedfag
      361 epcrvavdla skvdiaavva lfgrdgkvyp fakfyvpeqa iidsrndsyk gweaegklia
      421 tpgdvididr ieadivdlst rfevleiayd pwqaqqmanh lveqganave yrqtvqnfse
      481 ptkeldalmr sgklahnsgp rdplswmign vvghydaken vyprkerpen kidgaialim
      541 vlglhlrafg gvqapspwen pdfriavv
//
LOCUS       WP_457578957             137 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF3168 domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578957
VERSION     WP_457578957.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10568396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..137
                     /product="DUF3168 domain-containing protein"
                     /calculated_mol_wt=14888
     Region          13..127
                     /region_name="DUF3168"
                     /note="Protein of unknown function (DUF3168); pfam11367"
                     /db_xref="CDD:431845"
ORIGIN      
        1 maessetelq kllfttltgn tsimalaggv ydrvptdpyk gktayvsfgp sdvvedgadc
       61 ifsgehtiql dvwskavgqv eakrlvfliy kalheqsltl tenalaeirv dfrrvfadpd
      121 plithgiasv tarieel
//
LOCUS       WP_457578985              63 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457578985
VERSION     WP_457578985.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..63
                     /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=6873
     Region          6..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mvnailismr dvcaltslsr tminrlrstg qfpaavelge rrvafvrsev lawieqkiag
       61 rng
//
LOCUS       WP_457578986             356 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Ensifer adhaerens].
ACCESSION   WP_457578986
VERSION     WP_457578986.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..356
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39195
     Region          69..316
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgsiahgfkg lakvkktlad gktiyycyaw rggpllkhkd gspiqpgdsl ikaqfdlahe
       61 nrrnpnpgtl sgliarflas tdytlksvet rreyaryldd ireafghltf nelqassarg
      121 kfkewrdgis chprsadyaw atlnrvlsfg vdrgelsanv arrggrlyrv drreaiwsss
      181 dilafnaiaa kelklalllg lwtgqrkgdl lslpwsaydg mafrlrqskt grrvyipaak
      241 avrealagsa rrsptiltnt rgkrwtsggf dsswrkacad agvrgltfhd lrgtavtrla
      301 lagcsiaeig avtghspkdi dailhihylg gqrdlaqqam tkwetagter slwtes
//
LOCUS       WP_457578987              78 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457578987
VERSION     WP_457578987.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     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 78)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..78
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7964
     Region          3..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 mtpaqcraar alvnwtqphl aeaagvspst lrdfesgkrv piannlsair aaleavgvtf
       61 ledgdvaagp gvamhpmi
//
LOCUS       WP_457578992             340 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Ensifer adhaerens].
ACCESSION   WP_457578992
VERSION     WP_457578992.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133569
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..340
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38039
     Region          2..325
                     /region_name="GT4_GT28_WabH-like"
                     /note="family 4 and family 28 glycosyltransferases similar
                     to Klebsiella WabH; cd03811"
                     /db_xref="CDD:340839"
     Site            order(13,174..176,232,254)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340839"
ORIGIN      
        1 mkvmhfhfgk dggaerffvh lvnalaergv eqtsvirhgr iwkkdiegat riiesnfrnl
       61 sldrillpmk vssmarrekp dalfawmpra srlmpnykgc ikisrlgdyp lrldyfrntd
      121 clvcntpgia ehvrkigwnr dvevisnftg tervapisra tldtpenvpv vmsmgrfvpr
      181 kgfhtliqai akvpdaylwl vgdgeeranl eklaadlgva krvrfagwqk dtrpflaasd
      241 ifvmasshep lgnvileswa qgtpvvssrs egpqwfmrdg englmvdigd adgfaqaidr
      301 iagdtslger laerghetlm nhfskqaitd aylklfaskr
//
LOCUS       WP_457578999             548 aa            linear   BCT 27-JAN-2026
DEFINITION  Na/Pi cotransporter family protein [Ensifer adhaerens].
ACCESSION   WP_457578999
VERSION     WP_457578999.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Tenenhouse,H.S.
  TITLE     Recent advances in epithelial sodium-coupled phosphate transport
  JOURNAL   Curr Opin Nephrol Hypertens 8 (4), 407-414 (1999)
   PUBMED   10491734
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Takeda,E., Taketani,Y., Morita,K. and Miyamoto,K.
  TITLE     Sodium-dependent phosphate co-transporters
  JOURNAL   Int J Biochem Cell Biol 31 (3-4), 377-381 (1999)
   PUBMED   10224663
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Werner,A., Dehmelt,L. and Nalbant,P.
  TITLE     Na+-dependent phosphate cotransporters: the NaPi protein families
  JOURNAL   J Exp Biol 201 (Pt 23), 3135-3142 (1998)
   PUBMED   9808829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..548
                     /product="Na/Pi cotransporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005436 - sodium:phosphate symporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0044341 - sodium-dependent phosphate
                     transport [Evidence IEA]"
                     /calculated_mol_wt=58505
     Region          1..540
                     /region_name="NptA"
                     /note="Na+/phosphate symporter [Inorganic ion transport
                     and metabolism]; COG1283"
                     /db_xref="CDD:440894"
ORIGIN      
        1 mqstivmvnl fgavalllfg lslvkdgvtr afgarlragl aqgtdgslrs fvtglvatla
       61 lqsstatalm tasfvekgli rsrmaqivll ganlgtamta wivatgiewl splviligvv
      121 lhrasrsnar qglgaafvgi glmllslhll gaatepmrds palgaflsml dsawpvalli
      181 aaglafasss slavvmlvls lsttgilsvg ltvalvlgan lggavppvma tlgsapsarr
      241 vtignlvvra igclialplt gmsveflqsl plprqnlpvd ihlafnlava ilawlfagll
      301 sqlmarfipd geaeetgpry ldettlntpv malsgatrev lrvgdlveam lmraanafnn
      361 ndlsdirdig kfekqvdqlq qevkiflsrl grdglsaedg rrsiviidya inlehmgdii
      421 ekglceqitk kvsnglkfse egyqelkslf nltidnlrva qtifvtrnad lakqlievkv
      481 nvrhmekrsa erhierlrdg lvqslqtssl hldmlrdlkr vnahiasvay pileenglls
      541 esrlrpga
//
LOCUS       WP_457579001             393 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579001
VERSION     WP_457579001.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 393)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..393
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42238
     Region          110..374
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtaqldlatv lllhkssfli gafcflyarw qsprdeglgi lasgflflal astlagygeq
       61 kllpptlwrl ssftlgiggy alfwigvrrl sggrrrladw lallvplaga lvglatdfhv
      121 vnvvrasvfn aaaflflaas avaviadrsk eplparamla aamavgaglc lavvigllkp
      181 givpitttya fflsiichfa ialfalvlvk eraeaelrrs adtdaltgvg nrrwflaqlp
      241 qaswqgdcll vmdldhfkri ndryghhtgd qvlvafadlv rtnlrrgdsf arlggeefgl
      301 ylprtsetqa faiaerlrra veelrvvsng qsvavsisig vatasgters weelfnrada
      361 alyaakrggr nrvasdaela dskplaaslh rag
//
LOCUS       WP_457579004             440 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Ensifer adhaerens].
ACCESSION   WP_457579004
VERSION     WP_457579004.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 440)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..440
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46584
     Region          2..435
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 madalkigia glgtvgaslv qilqdrheml attcgraiet tavtardrnr drgvdlskta
       61 wfddaislar eadidvfvel mggagdpays avkaalqrgi hvvtankall aahgielaki
      121 aeekgallny eaavaggipv ikalresmtg ntisrvygim ngtcnyiltk mekeqlsfea
      181 clkeaqrlgy aeadpafdie gndtahklsi ltslafgtai aaddiylegi tnisiddiha
      241 aadlgyrikl lgvaqrtesg ieqrvhptmv pydsviaqvd gvtnavaies dilgellmvg
      301 pgaggnatas avlgdiadia ksrpgaqhvp afgrptnall pykraqiqsh eggyfirlkv
      361 vdrtgvfasi atrmadngis lesimqhskh lmdtgepqti ilvthatseh svrdaikaik
      421 gegylvgepq virierpkan
//
LOCUS       WP_457579005             392 aa            linear   BCT 27-JAN-2026
DEFINITION  zinc-binding metallopeptidase family protein [Ensifer adhaerens].
ACCESSION   WP_457579005
VERSION     WP_457579005.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..392
                     /product="zinc-binding metallopeptidase family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44122
     Region          27..381
                     /region_name="COG4307"
                     /note="Uncharacterized conserved protein, DUF2248 family
                     [Function unknown]"
                     /db_xref="CDD:443448"
ORIGIN      
        1 matllqtlgd ligtnwkhrd vpkrysrtfv crcgshvffg nmfcnscqap lgylpgedal
       61 lpldpgpqpg iwaageerpl lkycgnrdtp aqcnwmlmas epgelciacr lnrtipnldr
      121 ednarywgll evakrrlvsq llalglpvks kvdedekhgl mfdflrsppn gprvltghad
      181 glitvnieea dsvqrekmrl elyepyrtll ghlrhevghy ywnrlvfngp wlepfrtlfg
      241 deradyaaal kanyengapp dwadryissy asthpwedwa etwahylhmi dslgtalgfg
      301 ldaedleaiv epferdalya pddtgadgfl sllnswiemt mvlnelarsm gqpdfypfvm
      361 skpsvaklqf vhmvieasrs agtefveagf lg
//
LOCUS       WP_457579006             280 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene/squalene synthase family protein [Ensifer adhaerens].
ACCESSION   WP_457579006
VERSION     WP_457579006.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=30609
     Region          12..272
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mhdnsaqila dlrdtdrdry lacllapadk qpalaalyaf saeiarirdl vhepipgeir
       61 mqwwrdlign dastgeghpl aeallgcirt hrlpvsvfen midarifdly ddpmedrsal
      121 egyagetasa liqlsslvld penaaksaev aghggvaqtv agllmllplh lrrgqvylpa
      181 elmratgldr etliagedsa aisqairafa gfgrdhlasa raqlaaiaps nfpafiplal
      241 vepilnraea agagllqkpi rpaqwqrqww mwraarrrrf
//
LOCUS       WP_457579007             487 aa            linear   BCT 27-JAN-2026
DEFINITION  phospholipase D-like domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579007
VERSION     WP_457579007.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..487
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=52493
     Region          112..487
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 midlvqnywp hilallsfal gipaavhaam tkddvraaag wvgvvllspi vgaliyavag
       61 inrirrssig sqrallrgqg pdqfgrfdvs dadisvqfge rfaamkilgd rvsrhrmstg
      121 nrisvlaggd aayaamleai agarrsille syifdrdvig lrfadaliaa vargvevrvl
      181 idavgarysv psivghleaa gvptavfngn iimglrlpya nlrthrkilv vdgqvafagg
      241 mnirvgftse iagqapaqdt hfrmagpvva difqvssedw qfssgealag pawaieeapl
      301 padgpsvlvr avpsgpdatn etnhkmlmga fsvaqknirv mspyflpdre lisalvtaar
      361 rgvevdiivp avnnlllvdr amtaqfdqvl kghcrvwrak gafnhskllt vderwayvgs
      421 tnldprslrl nfefdlevld hgfaeaingt isdilasaep vtlerlrkks fadrlanril
      481 wlgspyl
//
LOCUS       WP_457579013             517 aa            linear   BCT 27-JAN-2026
DEFINITION  caspase family protein [Ensifer adhaerens].
ACCESSION   WP_457579013
VERSION     WP_457579013.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 517)
  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 517)
  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 517)
  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 517)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 517)
  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..517
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..517
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54612
     Region          27..283
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mtvlcrtlla msllalpaap amastsalvv gvdkyphevs ldgavrdaqd vtqalkaadv
       61 apirqfineq atkdairaaw gelvaaaerg dtivftyagh gaqmpelvag seedgldefl
      121 elpgfdrara ektaseiivd nelsawfaea eakgihvlfv sdscysggmn rsisgktrla
      181 pmvraklppp skealsgakv rdvelsqvti laaslesqpt pevviggepr galswsfara
      241 legaadrdgd grisrveled yvfsnvklqs ealqvpnftp qlarsdkeiv lslprsakvg
      301 vaptvsgtkh alkspretgw tgklplsvvg dmpdlanigg dgvpyrweaa sgvfytpngd
      361 vaaehvapkr lqgvvdkfil vdflkalaaq spgavslkpv kdiyfagdrl nveapqggya
      421 nmlvfnlant geaqlldvqi agseshafkl rdlevvkpfg adhlvviatn apvdaiaaaf
      481 ansdldaaal lrlletrleg sestiavqpl ytrgqgq
//
LOCUS       WP_457579015             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin reductase family protein [Ensifer adhaerens].
ACCESSION   WP_457579015
VERSION     WP_457579015.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Carrillo,N. and Ceccarelli,E.A.
  TITLE     Open questions in ferredoxin-NADP+ reductase catalytic mechanism
  JOURNAL   Eur J Biochem 270 (9), 1900-1915 (2003)
   PUBMED   12709048
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Dym,O. and Eisenberg,D.
  TITLE     Sequence-structure analysis of FAD-containing proteins
  JOURNAL   Protein Sci 10 (9), 1712-1728 (2001)
   PUBMED   11514662
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..342
                     /product="ferredoxin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38158
     Region          2..342
                     /region_name="COG4097"
                     /note="Predicted ferric reductase [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:443273"
ORIGIN      
        1 mlclilvhyf lkpdfkglal tsglnqlaas agkyafygfv vllvlsivki iprtkieipy
       61 hlwrythrfi gllfvmvafh qmfikrpydg tallavylna faalgilsyt ytqllpwlrt
      121 rgyevfdvar edgatviaar plrralrakp gqfgflrvlk pglrephpft iagiepdgvv
      181 rfaikplgdy tqalrdgiav gdrlkleggy grfnhrrggk kqiwlaggig vtpflamarh
      241 lngdegqdih mvycvrdrre aigletfegq agklgnftfv lhdssvdgrl daaklangsa
      301 idpaeadlwf cgppplreai vkglkdlgkr pkrveferfq fr
//
LOCUS       WP_457579016             348 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579016
VERSION     WP_457579016.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..348
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37171
     Region          7..280
                     /region_name="AR_SDR_e"
                     /note="aldehyde reductase, extended (e) SDRs; cd05227"
                     /db_xref="CDD:187538"
     Site            order(12,14..17,37,68,86..90,127..129,158,162,185..188,
                     199..200)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(90,92,129..131,134,158,185..187,203,215,221)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(129,158,162)
                     /site_type="active"
                     /db_xref="CDD:187538"
ORIGIN      
        1 mnartatvav tgiggfvgrh valallregy pvhgtvralg raeeiersir aaggtdaarl
       61 tfgeadllee rgwaeafaev syvvhtaspf parlpanedd ligpardgtl rvlraahaag
      121 akrvvltssv aaviygagra pfteddwtdp qsslatpyyr sktfaeraaw dyaadsglel
      181 vvinpgmvlg pvlgheigts vavvrnllkg nypalpkfav pvvdvrdvad ahvqalsvaa
      241 aagerfliag ealsladita ilrrrfpeha grlprfvlpn wlaglaapfd aglrlivrel
      301 ghdpphfqrk gapcsrvaaa lcrrgrrglg eqpdfgrprl rrawrvsr
//
LOCUS       WP_457579017             243 aa            linear   BCT 27-JAN-2026
DEFINITION  rhomboid family intramembrane serine protease [Ensifer adhaerens].
ACCESSION   WP_457579017
VERSION     WP_457579017.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..243
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26596
     Region          31..226
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 merdqtatpp eaerdsaasp vrepafnlpa gltfillfli aihvlrtyvl ppaidqeiif
       61 nfaflparyd hplaeqglaw lwspvtysfl hgswehlifn ifwmvafgap vvrrigmgrl
      121 avfwclsaaa avalhtafhw gemivvvgas gvvsgfmgaa arfvfspsgr isrqfahlnr
      181 rldvgealan rsvvvfagiw fltnfliglg mftpggagsv aweahiggfl fgfllfslfd
      241 prd
//
LOCUS       WP_457579023             206 aa            linear   BCT 27-JAN-2026
DEFINITION  FMN-dependent NADH-azoreductase [Ensifer adhaerens].
ACCESSION   WP_457579023
VERSION     WP_457579023.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..206
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase (NADP+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21757
     Region          1..198
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mnvlhidsgi lgdhsvsrrl taalaaqvka drpdaqvtyr dlaasslphl tgaqimapad
       61 legvdaglaa dvklgrdmle eflaadtvii gapmynfgip sqlkawidri avsgktfryt
      121 engpeglakg kkiivastrg ghysagpaav mdhqefylkt vfgflgitdv efvraeglnl
      181 sadskqfaia eaektisegs vlrlas
//
LOCUS       WP_457579026             409 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Ensifer adhaerens].
ACCESSION   WP_457579026
VERSION     WP_457579026.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11482064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..409
                     /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=43959
     Region          27..404
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
     Region          207..270
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mvsrfaltas vvalllspat gfagsrgplq iivskdqqsl vvydgdavia tspvstgkag
       61 httpsgifsi lekrrhhksn iysnapmpfm qrltwsgial hgsnhvpdyp ashgcvrlps
      121 efaaslyklt ergvhvlisd rqitplevks allfrpapid lqpplsdvpl rpaisqarda
      181 pvevamrepp ggansarste epirilitrs dtrdtmrevq tsldflgyap gaidghagpa
      241 tiaalrafqa segidgdgkl tpdltdrllr kagrtppqng kilvrqgfkp lfeagltidk
      301 peealgthfl qfrhneeega egkwfgvsle nhlpastkkr lgisteadpf ayngiqrtla
      361 rmtisddvrk rveallaegs slsiadvesg letgqgtdfi titrtrpgd
//
LOCUS       WP_457579027             192 aa            linear   BCT 27-JAN-2026
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Ensifer adhaerens].
ACCESSION   WP_457579027
VERSION     WP_457579027.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Parey,K., Brandt,U., Xie,H., Mills,D.J., Siegmund,K., Vonck,J.,
            Kuhlbrandt,W. and Zickermann,V.
  TITLE     Cryo-EM structure of respiratory complex I at work
  JOURNAL   Elife 7, 39213 (2018)
   PUBMED   30277212
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 192)
  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 10012723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..192
                     /product="NuoB/complex I 20 kDa subunit family protein"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=20883
     Region          27..186
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 meltsgttlv apkpkgiidp stgkpigsnd aifgeinnel adkgflvtst delinwartg
       61 slmwmtfgla ccavemmqms mprydaerfg faprasprqs dvmivagtlt nkmapalrkv
      121 ydqmpepryv ismgscangg gyyhysysvv rgcdrvvpvd iyvpgcppta eallygvlll
      181 qkkirrtgti er
//
LOCUS       WP_457579029             612 aa            linear   BCT 27-JAN-2026
DEFINITION  HAMP domain-containing methyl-accepting chemotaxis protein [Ensifer
            adhaerens].
ACCESSION   WP_457579029
VERSION     WP_457579029.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Salah Ud-Din,A.I.M. and Roujeinikova,A.
  TITLE     Methyl-accepting chemotaxis proteins: a core sensing element in
            prokaryotes and archaea
  JOURNAL   Cell Mol Life Sci 74 (18), 3293-3303 (2017)
   PUBMED   28409190
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Dunin-Horkawicz,S. and Lupas,A.N.
  TITLE     Comprehensive analysis of HAMP domains: implications for
            transmembrane signal transduction
  JOURNAL   J Mol Biol 397 (5), 1156-1174 (2010)
   PUBMED   20184894
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Hazelbauer,G.L. and Lai,W.C.
  TITLE     Bacterial chemoreceptors: providing enhanced features to
            two-component signaling
  JOURNAL   Curr Opin Microbiol 13 (2), 124-132 (2010)
   PUBMED   20122866
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Parkinson,J.S.
  TITLE     Signaling mechanisms of HAMP domains in chemoreceptors and sensor
            kinases
  JOURNAL   Annu Rev Microbiol 64, 101-122 (2010)
   PUBMED   20690824
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11622275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..612
                     /product="HAMP domain-containing methyl-accepting
                     chemotaxis protein"
                     /GO_component="GO:0098561 - methyl accepting chemotaxis
                     protein complex [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=64934
     Region          3..169
                     /region_name="chemoreceptor_sensor"
                     /note="4-helix bundle ligand binding sensor domain of
                     chemoreceptors such as Tar or Tsr; cl00144"
                     /db_xref="CDD:444710"
     Region          89..593
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 msrlkishtl ialflvvavi vsalavsslg gikmmnernn eiattwlprv slsraletql
       61 sdtrmafarh lisltpfekk aaekvigetv ggfnkladey sslmvtdadk aaldnvrtay
      121 qaylsvaegm vklsnnlenm kaqsvfkvem retegkvdea ikemralnla gadaavaass
      181 athdqirmie igvialaavi vlgailyavr giarpiqiit rsmarlaegd tdssipygar
      241 kdeigemara vevfrqaaia nqhleadaqt qrakaeaerl rvteeaeaaa qrrlqeatag
      301 lasglrrlas gdlafqlnep fspdfeqlrh dlnqavaqla dtlaavssas gsidsgarev
      361 sqsaddlsrr teqqaaslee taaaldqitv nvgnsskrth earsvagqan esarksgaiv
      421 sgavdamgri ehsssqisni igvideiafq tnllalnagv eaaragdagk gfavvaqevr
      481 elaqrsanaa keikdlirns avevesgvrl vretgealrt iegfivtinq hmdaiavsaq
      541 eqsaglsevn tavnqmdqvt qhnaamveea naasatlaqe agrlreliar ftlaeagghg
      601 yaqstngarw aa
//
LOCUS       WP_457579032             143 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Ensifer adhaerens].
ACCESSION   WP_457579032
VERSION     WP_457579032.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..143
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15396
     Region          8..143
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtiepimtvd dlnrfldtdf pqvhtdgkvf hvtavgrgfa tmrldpnerh irpggtvsgp
       61 tlfaladvsa yialiahigp valavttnln inflrkpepe plectcrilk lgkrlavlda
      121 sivkvgdddl vahatatysi ppr
//
LOCUS       WP_457579033             367 aa            linear   BCT 27-JAN-2026
DEFINITION  COX15/CtaA family protein [Ensifer adhaerens].
ACCESSION   WP_457579033
VERSION     WP_457579033.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..367
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=41384
     Region          27..347
                     /region_name="COX15-CtaA"
                     /note="Cytochrome oxidase assembly protein; pfam02628"
                     /db_xref="CDD:460629"
ORIGIN      
        1 magvemateq mlrneigrtd rnrrqirgwl avvlftlfal vlvggatrlt esglsitewk
       61 pihgvipplt vaeweeefql yqripqyqqm nssmtvdefk tifwwewahr llartiglif
      121 alplayfwft gkverklrmp llgilalggf qgfigwwmvs sglvertevs qyrlathlvi
      181 aclifaacmw ifrglsahsn dtaptdrsrk masiiaifsl fqiylgalva gldagfsynt
      241 wplmdgaiip qdlflqqpww inlfenpktv qfvhrigayv lfafalmhmi aslraapett
      301 harravllfl lvsvqavigi ttlvlqvpvg wgvahqggal vvlgfaiahw rgfygeyprp
      361 taielrd
//
LOCUS       WP_457579034             246 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Ensifer adhaerens].
ACCESSION   WP_457579034
VERSION     WP_457579034.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 246)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..246
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27020
     Region          2..226
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrlaviadih gndlaleavl adidaqgitd ivnlgdhlsg plnaartadi likrailsir
       61 gnhdrylltm dphemrlsdr aaydqlqpqh rewlatlpva hvheetfflc hatptddety
      121 wlealtadgt vhmaqhsaie akavgvdypv ilcghthiqr avrlsdgrlv vnpgsvgcpg
      181 ydddqpvphk veagspdary aiieksasgw hvtfrnvpyd wmamsrlaas rnrlewakal
      241 atgfld
//
LOCUS       WP_457579036             196 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase [Ensifer adhaerens].
ACCESSION   WP_457579036
VERSION     WP_457579036.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Nebert,D.W. and Vasiliou,V.
  TITLE     Analysis of the glutathione S-transferase (GST) gene family
  JOURNAL   Hum Genomics 1 (6), 460-464 (2004)
   PUBMED   15607001
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Sheehan,D., Meade,G., Foley,V.M. and Dowd,C.A.
  TITLE     Structure, function and evolution of glutathione transferases:
            implications for classification of non-mammalian members of an
            ancient enzyme superfamily
  JOURNAL   Biochem J 360 (Pt 1), 1-16 (2001)
   PUBMED   11695986
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..196
                     /product="glutathione S-transferase"
                     /EC_number="2.5.1.18"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:0042178 - xenobiotic catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22318
     Region          1..71
                     /region_name="GST_N_3"
                     /note="GST_N family, unknown subfamily 3; composed of
                     uncharacterized bacterial proteins with similarity to
                     GSTs. GSTs are cytosolic dimeric proteins involved in
                     cellular detoxification by catalyzing the conjugation of
                     glutathione (GSH) with a wide range of...; cd03049"
                     /db_xref="CDD:239347"
     Site            order(11,13..14,16..17,20..21,64,67..68)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239347"
     Site            order(11,48..50,62..63)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239347"
     Site            order(48,61..62,64..65,68)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239347"
     Region          92..187
                     /region_name="GST_C_6"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 6 of Glutathione S-transferases; cd03205"
                     /db_xref="CDD:198314"
     Site            order(93..95,97..98,101,108..109,114,116..119,122,125,129,
                     132..133,136)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198314"
     Site            order(97,101..102,105..106,158,161)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198314"
ORIGIN      
        1 mkilyspasp ysnkvrmaah yagyaaesvl tdtnanppel idnnplgkip tlilddgral
       61 ydsrtimhfi dretkgklyp rnaekrtdve llealcdgvc dsllsivyek rshppekvhq
      121 pwidrqwekv ersldhlnan lpktgaklna ghfalaamlr yvelrfagew qkgraklknw
      181 pakfekhfpd ylkfka
//
LOCUS       WP_457579038             357 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579038
VERSION     WP_457579038.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 357)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..357
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37804
     Region          69..330
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnrqvpadas rsqarqaaii lkvahamsah giaalprnye lvyealsgrl pelsrelaal
       61 ghnpqqdald alglrhhlis haalaadrtr aagqealaei agklrlallq kqsfkdeldh
      121 fagrlatdpv agmsefadda arlreaagrl tneegalqqa letsmtrlae legelaesrr
      181 sltrdpatgl pnrlaltakl nsileaerad qpvalllasv eglremaehh ggtvaakals
      241 klstlfrksi kkddfvarvg qqefafvcrd vstenaeaia rrlrqsvkel tvtlpgraht
      301 aetlslaagi tlaqpastsa dlltqaeqal agardgagil cysaalgrgr gygqsaa
//
LOCUS       WP_457579041             347 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Ensifer adhaerens].
ACCESSION   WP_457579041
VERSION     WP_457579041.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..347
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38493
     Region          13..336
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(19..21,26,48,53,88,130,181..182,207,235..241,244,
                     246,255..257,291,308..312,316,320)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(48,53,88,130)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mryntlgrtg ikvseiclgt mtwgsqnsia eaheqldyaf dkgvnfidta elypttplsp
       61 etygdterfi gewlvrrgrr devvvatkva gpgrpyirng npttpegidq aidaslkrlk
      121 tdyvdlyqlh wpnrghyhfr nawsydpsrq dkdhvasdlr aildklgdlv kagkvraigl
      181 snetawgamk fidmaerhgl prvasiqney nqlyraydld lselshhedv gllaysplaa
      241 gllsgkyldg akpkgsrlsi ngdlggrftp hqepavegyv klarehgldp aqmaiafcla
      301 rpfmasviig atsmeqlktn lgavdltlsq divngirrlh riypmpi
//
LOCUS       WP_457579043             329 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579043
VERSION     WP_457579043.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..329
                     /product="glycerophosphodiester phosphodiesterase family
                     protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36047
     Region          9..316
                     /region_name="GDPD_GDE4_like_1"
                     /note="Glycerophosphodiester phosphodiesterase domain of
                     uncharacterized bacterial homologs of mammalian
                     glycerophosphodiester phosphodiesterase GDE4; cd08613"
                     /db_xref="CDD:176554"
     Site            order(36,85,87,100,167,198,275)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176554"
     Site            order(36,100)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176554"
     Site            order(85,87,167)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:176554"
ORIGIN      
        1 mkkafaifvl fvavvwlmnt slfvappagt akllahrgih qtypkdnvgr dtctatiirp
       61 pehpylenti asmqaafdag advveldvhl tpdrqfavfh dwtldcrtea kgvteetpmt
      121 slksldigyg ytadggktfp frgkgvgqmp tleevlaalp drkflinfks rradegaela
      181 tridaqpqwr eavfgvygge eptretlkrl qglrgydrts tmacltrylg ygwsglmpda
      241 ckntfvivpg nyapllwgwp drfaarmkaa gseiillgpy gggdfttgid tmqdlelvpp
      301 gfsgyiwtnr iemigpalak rqvadagtn
//
LOCUS       WP_457579047             553 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase [Ensifer
            adhaerens].
ACCESSION   WP_457579047
VERSION     WP_457579047.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..553
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60274
     Region          30..348
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          450..551
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mteqdlpere smefdvvivg agpaglaaai rlkqvnpels vvvlekgaev gahilsgavv
       61 dpigidrllp gwrdeadhpf ktevtddhfl flgpagsirl pnflmpplmn nhgnyivslg
      121 lvcrwlatka eelgveiypg faatevlynd egavigvatg dmgierngep gpnfargmal
      181 lgkytligeg vrgslakqli akfdlskdrd vqkfgiglke lwqvkpenhr pglvqhsfgw
      241 plgmktgggs flyhlednmv avgfvvhlny knpylfpfee fqrfkthpai rgtfeggkrl
      301 sygaraiteg gyqsvpklsf pggaligcsa glvnvprikg shnavlsgil aaeklaaaia
      361 sgrandepie iergwrdsai gqdlkrvrnv kplwskfgta igvglggldm wtnqlfgfsf
      421 fgtlkhgktd aqslepaaqh kkidypkpdg vltfdrlssv flsntnheed qpvhlqvkdm
      481 dlqkrsehdv yagpstrycp agvyewvekd grqvfvinaq ncvhcktcdi kdpnqninwv
      541 ppqggegpvy pnm
//
LOCUS       WP_457579048             662 aa            linear   BCT 27-JAN-2026
DEFINITION  heme lyase CcmF/NrfE family subunit [Ensifer adhaerens].
ACCESSION   WP_457579048
VERSION     WP_457579048.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Brausemann,A., Zhang,L., Ilcu,L. and Einsle,O.
  TITLE     Architecture of the membrane-bound cytochrome c heme lyase CcmF
  JOURNAL   Nat Chem Biol 17 (7), 800-805 (2021)
   PUBMED   33958791
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Stevens,J.M., Mavridou,D.A., Hamer,R., Kritsiligkou,P.,
            Goddard,A.D. and Ferguson,S.J.
  TITLE     Cytochrome c biogenesis System I
  JOURNAL   FEBS J 278 (22), 4170-4178 (2011)
   PUBMED   21958041
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Sanders,C., Turkarslan,S., Lee,D.W. and Daldal,F.
  TITLE     Cytochrome c biogenesis: the Ccm system
  JOURNAL   Trends Microbiol 18 (6), 266-274 (2010)
   PUBMED   20382024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..662
                     /product="heme lyase CcmF/NrfE family subunit"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015232 - heme transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=71320
     Region          2..653
                     /region_name="CcmF"
                     /note="Cytochrome c biogenesis protein CcmF [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG1138"
                     /db_xref="CDD:440753"
ORIGIN      
        1 miielghyal vlalataviq aalpilgarl ndrglmelas saavacfllv afafavltfa
       61 yvtsdfsvrn vwenshslkp liykisgvwg nhegsmllwl liltffsalv aafgrnlpet
      121 lkanvlavqa wiamafalfi lltsnpfarl mpapgegkdl npilqdvgla ihppllylgy
      181 vgfsvcfsfa iaaliegrid aawarwvrpw tlaawtflta gismgsyway yelgwggwwf
      241 wdpvenasfm pwlagtallh salvmekrea lkiwtvllai mtfslsllgt flvrsgvlts
      301 vhafatdptr gifilailvf figgaftlfa lrashlkagg ifapisrega lvfnnliltt
      361 atatvltgtl yplvlealtg dkisvgppff nmtfgllmlp llfavpfgpl lawkrgdlvg
      421 vsqrlfaava igllfgvtyy yfmnggpvla lfgialgvyv ivgsltdlal rsglgkvagn
      481 vawrrfsglp rsafgtalah iglgvtligi vavtafetet vvemkpgmtv daggytlrfd
      541 gmrngsgpny seesghftis rggvaiddvw sskrlyqarr mptteagirt fglsqlyvsl
      601 gdqiseggiv vriwwkpmil ciwggtlfmm aggfvslsdr rlrvgapara krpkavpvga
      661 ae
//
LOCUS       WP_457579054             400 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457579054
VERSION     WP_457579054.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Anderson,P.M., Sung,Y.C. and Fuchs,J.A.
  TITLE     The cyanase operon and cyanate metabolism
  JOURNAL   FEMS Microbiol Rev 7 (3-4), 247-252 (1990)
   PUBMED   2094285
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Sung,Y.C. and Fuchs,J.A.
  TITLE     Characterization of the cyn operon in Escherichia coli K12
  JOURNAL   J Biol Chem 263 (29), 14769-14775 (1988)
   PUBMED   3049588
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41263
     Region          39..391
                     /region_name="CynX"
                     /note="Cyanate permease [Inorganic ion transport and
                     metabolism]; COG2807"
                     /db_xref="CDD:442057"
ORIGIN      
        1 mataaafvre rtdwsgvmtv vaagvvaamq vgkgliagpl lqsdlglnls algwitsvfa
       61 vvgvvggmaa gafvtaagdr rllgigmall afgsftgaas paftllllsr iiegfgfllv
      121 vvagpailmr lvtqersdlv falwscfmpa gmaiamltgp afagwqaiww snglltlasl
      181 gsiflavsps rqtprvatrf rddaaetlts rgpvllfalf slyslmsftl ssflpillie
      241 rlqvslgtvg llsavitlvn vfsnlaaghl lsrgfargrl vasaalltgv sglwiflsps
      301 gghlilalcl lfsaigglip atlissvpll sprpalapma mgllmqgsnl gqlvgpvavg
      361 taiefygwts gaafigasav lcialtptle rtlresrper
//
LOCUS       WP_457579055             194 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Ensifer adhaerens].
ACCESSION   WP_457579055
VERSION     WP_457579055.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..194
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21353
     Region          2..188
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkvvagmqm sidglidgpd gytdwvdsws dtfdllpeid acvlgngmys gyeqywsaik
       61 rdphapleft gqlptpeeie yadfalgtph yvlsktrsdv ewenarivrd vseietlrqa
      121 pgrtiyvvgg artvsslmdh glidelrlti hplvvgkgka lfdtvaerhh vqfddakrld
      181 ggkvclvykv ggga
//
LOCUS       WP_457579057             637 aa            linear   BCT 27-JAN-2026
DEFINITION  HAMP domain-containing methyl-accepting chemotaxis protein [Ensifer
            adhaerens].
ACCESSION   WP_457579057
VERSION     WP_457579057.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Salah Ud-Din,A.I.M. and Roujeinikova,A.
  TITLE     Methyl-accepting chemotaxis proteins: a core sensing element in
            prokaryotes and archaea
  JOURNAL   Cell Mol Life Sci 74 (18), 3293-3303 (2017)
   PUBMED   28409190
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Dunin-Horkawicz,S. and Lupas,A.N.
  TITLE     Comprehensive analysis of HAMP domains: implications for
            transmembrane signal transduction
  JOURNAL   J Mol Biol 397 (5), 1156-1174 (2010)
   PUBMED   20184894
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Hazelbauer,G.L. and Lai,W.C.
  TITLE     Bacterial chemoreceptors: providing enhanced features to
            two-component signaling
  JOURNAL   Curr Opin Microbiol 13 (2), 124-132 (2010)
   PUBMED   20122866
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Parkinson,J.S.
  TITLE     Signaling mechanisms of HAMP domains in chemoreceptors and sensor
            kinases
  JOURNAL   Annu Rev Microbiol 64, 101-122 (2010)
   PUBMED   20690824
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11622275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..637
                     /product="HAMP domain-containing methyl-accepting
                     chemotaxis protein"
                     /GO_component="GO:0098561 - methyl accepting chemotaxis
                     protein complex [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67690
     Region          1..177
                     /region_name="chemoreceptor_sensor"
                     /note="4-helix bundle ligand binding sensor domain of
                     chemoreceptors such as Tar or Tsr; cl00144"
                     /db_xref="CDD:444710"
     Region          107..588
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtikarllvc lsllavamlv mivtafsalt siskrtesiv vdrllpvdhl ktvsdmyave
       61 ivdtthkvrs galdwaagak aidtalatid trwrtyeatr ltpeektlte ifdrariasd
      121 asirdlvqim qrqdkaeler fvdtklyssv dplaapisdl iklqlseang eleaanaekd
      181 nltlwqsvia gfallmlgat awfviagllr pltglreamr qlaagnlkal ifgegrrdei
      241 gqmagavavf rdnalererl eqeaeagrsl serereqrea qkakeaaevq aavsalgfgl
      301 drlaegdltf ridtplaerl dalrtnfnss vtnleealrs vgenarsina gaseirsaag
      361 dlskrteqqa asveetaaal dqiattvada srraeeagtl vtrtrgaaek sgeivgnavt
      421 amsgieassr eissiigvid diafqtnlla lnagveaara geagkgfavv aqevrelaqr
      481 saqaakeikv liatsgqqvk sgvtlvretg aalesiivev keinnhvtai vesareqaag
      541 iqqintavna idqgtqqnaa mveqstaash slareagaln dllmrfrtgn gssagprlva
      601 sgatesaaps paraltrkla gayrggarph edgwaef
//
LOCUS       WP_457579059             226 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Ensifer adhaerens].
ACCESSION   WP_457579059
VERSION     WP_457579059.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 226)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Rosinski,J.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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..226
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24678
     Region          2..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkegpdiali gslmgdpara nmltalmggr altatelath agitlqtass hlskletggl
       61 ltqrkqgrhr yfqlaedevg lmlenlmgfa asrgmnrhrp gpkdpalrka rvcynhlagd
      121 ygvrmydsli aekqievtgd dlaltpdgqn riealgidya alkksrrpic rtcldwserr
      181 shlagslgea lltlfidkgw akreansrai rftangekaf selfpq
//
LOCUS       WP_457579060             738 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Ensifer adhaerens].
ACCESSION   WP_457579060
VERSION     WP_457579060.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12982809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..738
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77887
     Region          60..210
                     /region_name="PDC1_MCP_like"
                     /note="first PDC (PhoQ/DcuS/CitA) domain of
                     methyl-accepting chemotaxis proteins and similar domains;
                     cd12913"
                     /db_xref="CDD:350338"
     Region          212..305
                     /region_name="PDC2_MCP_like"
                     /note="second PDC (PhoQ/DcuS/CitA) domain of
                     methyl-accepting chemotaxis proteins and similar domains;
                     cd12912"
                     /db_xref="CDD:350337"
     Region          309..720
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 milktatarn mfaivmtgll tsmvtaavvf wlsyqqlrer siaemtnaas asarsvetkf
       61 aeaktlanni rsalyavkgt gepsraeiet lmkrwivdnp lavgmstgwe pnafdgkdae
      121 fvgkpghdat grfvpyiars gdkviheala dydkpgpgdy yqipkktgld mvtepyvypi
      181 ngkdvlmtsi mvplkkdgtf igvvgvdmal gelstelakl kpfgtgfvsl lskdgsiish
      241 pdakvlgkvl kdtplagegw gdllshtgqa falkhtdgsg hlavavpvnl lpdtewyvvv
      301 svpeatvfag lshlamisia viavaaaimi ivgwtlasrf rkrvanvigv tgqiaagetd
      361 vdlseaerkd eigdlarslr vlrdatiakm qleseadanr slsererler eaqkardaae
      421 iqqavnglat glgrlaegdl ayridnpfad rldslradfn nsvaklhdtl cavganargi
      481 dagateirsa addlarrteq qaasveetaa aleeitttvk dsarraeevg alvartraga
      541 eksgevvana vdamhaieks sgeisniigv iddiafqtnl lalnagveaa rageagkgfa
      601 vvaqevrela qrsanaakei kalittsgnq vrngvtlvgd tgkaletiva evheinkhvs
      661 aivtatreqs tglqeintav ntmdqgtqqn aamveeqtaa shglaseaas lnallaqfnl
      721 gegqgsyagg gghrrraa
//
LOCUS       WP_457579063             325 aa            linear   BCT 27-JAN-2026
DEFINITION  magnesium transporter CorA family protein [Ensifer adhaerens].
ACCESSION   WP_457579063
VERSION     WP_457579063.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Guskov,A. and Eshaghi,S.
  TITLE     The mechanisms of Mg2+ and Co2+ transport by the CorA family of
            divalent cation transporters
  JOURNAL   Curr Top Membr 69, 393-414 (2012)
   PUBMED   23046658
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Niegowski,D. and Eshaghi,S.
  TITLE     The CorA family: structure and function revisited
  JOURNAL   Cell Mol Life Sci 64 (19-20), 2564-2574 (2007)
   PUBMED   17619822
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Knoop,V., Groth-Malonek,M., Gebert,M., Eifler,K. and Weyand,K.
  TITLE     Transport of magnesium and other divalent cations: evolution of the
            2-TM-GxN proteins in the MIT superfamily
  JOURNAL   Mol Genet Genomics 274 (3), 205-216 (2005)
   PUBMED   16179994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10191309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..325
                     /product="magnesium transporter CorA family protein"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36131
     Region          28..325
                     /region_name="EcCorA-like_u1"
                     /note="uncharacterized subgroup of the Escherichia coli
                     Mg2+ transporter CorA_like subfamily; cd12837"
                     /db_xref="CDD:213371"
     Site            order(31,64,76,78,92,106..109,111..112,141,144,203..204,
                     207,229)
                     /site_type="other"
                     /note="Cl binding site [ion binding]"
                     /db_xref="CDD:213371"
     Site            order(55,58..59,65,67,115,119,132,135,139,143,146..147,
                     150,153..154,156..157,160,182..183,185..186,189..190,
                     193..194,196..197,201,203..204,207..208,211..212,223..224,
                     226..227,230..231,233..234,237..238,240..241,243..245,
                     248..255,257..269,271..273,275..280,282..289,301..302,
                     305..306,318,321)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:213371"
ORIGIN      
        1 mitgycadgt avvltpadpp eslrsdliwl dlvepnkaed lmmekllgis iptrddlkdi
       61 epssrlyiee navfmtaslv frsdteipgl tdigfilags rlvtiryaep rsfalfkasm
      121 hrfpgncrdg avvltrllet iadrtaeile eavtkiddls iavfgekaag krrpphflea
      181 rlrdvaghhr lvaktrdsla slsrlltfvy tvpqvqddke trelcrsisr diqslsehag
      241 fisgnitfll daslglinve qnaiikifsi asvvllpptl vasvygmnfr vmpelewqfg
      301 ypwaiaamvi savipffffr wkgwl
//
LOCUS       WP_457579064             448 aa            linear   BCT 27-JAN-2026
DEFINITION  TldD/PmbA family protein [Ensifer adhaerens].
ACCESSION   WP_457579064
VERSION     WP_457579064.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..448
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46654
     Region          10..447
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 msdtidsadl ekraselvdl arkagadaad avvvrgrsrs vavrlgkvea teasesddfs
       61 lrvfvgrrva svsanpgfdl kllaeravam akaspedpfa aladadrlak sypdldlfda
      121 tavstetlae aalaaeeaal avsgvtnssg agasagmggl vlvtshgfsg symatrfgrs
      181 vsaiagegtk merdydydsr lffadlrdad eigrlagera varinprqvp taknvtvvfd
      241 priargfvgh lagaingaav arktsflrdm mgkqilksgl svtddplivr gsssrpfdge
      301 gvsgeklamv edgvlnhwfl stsaalelgl qtngrgvrgg ptvnpsstnl alepgsisrd
      361 dlirgvgtgf yvteligqgv nmvtgeysrg asgfwienge ltfavsevti asnlkdmfma
      421 ltpaddidrk fgvaaptlai egmtlagl
//
LOCUS       WP_457579068             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579068
VERSION     WP_457579068.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22050
     Region          5..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnrgrprnfs rdealasamq lfwdkgydnt slsdltramg lnppslyaaf gskaqlfiea
       61 vdlygrtdga giwdeletvp takaavhdll rrtaenftqr geprgcmvvl sapqmaggda
      121 eacdalkvrr lekqmaleqr feraveegel pvgvdcaaia ayvaslqhgm siqardgatr
      181 etlvaiadca aggwdamisa nirpd
//
LOCUS       WP_457579070             337 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579070
VERSION     WP_457579070.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..337
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37372
     Region          44..333
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mfyqlaaaag fmlagvlgca ayfwgtslvl dlifpskgks gvvasrnlri tnairpwlfl
       61 apalfalaty liypvfmslw ysvhdragqn fvgvsnyawm indgefrqsi ynnflwllvv
      121 palatffglv iaaltdriww gniaktlifm pmaisfvgaa viwkfiydfr pegaeqigll
      181 naivvafgaa pqawitlpfw nnfflmailv wiqtgfamvi lsaalrgipe etieaavidg
      241 angwqiffki mvpqiwgtia vvwttitilv lkvfdivlam tngqwqsqvl anlmfdwmfr
      301 gggdfgrgaa iavvimilvi pimvwnirna akemkgh
//
LOCUS       WP_457579071             544 aa            linear   BCT 27-JAN-2026
DEFINITION  GumC family protein [Ensifer adhaerens].
ACCESSION   WP_457579071
VERSION     WP_457579071.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..544
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=58603
     Region          1..>415
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mdiktvvrav wqlrkiilat talgavggvl lalstpsvfv sesklyvdpr evrltdsdls
       61 kqslategil aivdsqlevl rsrtvmekva asldlekdpe fagkgaggda sarvlkalge
      121 aiqvwrdpkt fivtieaktr dpeksalian rlvdtflgee taaqsgffqk ttvaldarik
      181 elkaeldaae kavedykasn divgaggeli adkqllslsd qvaaarnria eakakaeasg
      241 kvqltdvltg aypeeissla lselrkqyaa traqlsalda slgprhpqri avqqalessr
      301 seianelrri aaaagteldr aqrteqdlvq qlavqkarqi dssaefvelr elqrkaaatr
      361 eiyesflkra getreeeklt aknirviska epalqakgps rkiiliaatm agffaglglg
      421 vllgiyrsln glfpatrkae ddeapeppep dggpeptrrq qpqpdpasak lelppqfspa
      481 ahhaqslnaa yavarrsata gpvtaqpvpq tvdeddadia kvqeglralr srvehysrqk
      541 larr
//
LOCUS       WP_457579076             763 aa            linear   BCT 27-JAN-2026
DEFINITION  chemotaxis protein CheA [Ensifer adhaerens].
ACCESSION   WP_457579076
VERSION     WP_457579076.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 763)
  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 763)
  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 763)
  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..763
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..763
                     /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=81473
     Region          1..752
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmneikeif fqeceeqlae lesgllklnd gdrdpetvna vfravhsikg gagafglddl
       61 vsfahvfett ldcvrsnrld pgpevlkvml ksadvladlt naardggsvd earsrqlike
      121 lealangevp qasaapaepv akpvaavapp pvndegfqpv afsfddfdaa eepplmempt
      181 yeivfkpksd lyakgneatl llrdlsrlge msihcdmgal ptldrlspes ayffwkislk
      241 tdkgedairt vfefaewdcd leislvedea tqsgdelpmq pvpfdlsild depvvsvgvv
      301 eeeeqlasqq qdrdaavsaa gtasnvlqma qsaarapaek aapaasaaaq saaaqqaaas
      361 aatptirvdl drvdrlinlv gelvinqaml sqsvvendtn gtssinmgle elqqltreiq
      421 dsvmairaqp vkpvfqrmsr ivreiadmtg ksvrlitege ntevdktvid klaeplthmi
      481 rnavdhglet pekrlaagks aegtvrltak hrsgriviel addgaginre kvrqkaidnd
      541 liaadanlsd eeidnlifha gfstadkisd isgrgvgmdv vkrsiqalgg rinisskpgh
      601 gsiftmslpl tlavldgmvv tvanqtlvvp ltaivetlqp eaaaihsfgs nqrlisirns
      661 fcplvdvgri lnfraiqanp vegvallves egggqralmv daiqgqrqvv iksleanyth
      721 vpgiaaatil gdgrvalild vdaivaasrg hslkpemsla avg
//
LOCUS       WP_457579082             163 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Ensifer adhaerens].
ACCESSION   WP_457579082
VERSION     WP_457579082.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5) (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..163
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=17346
     Region          17..151
                     /region_name="Usp"
                     /note="Universal stress protein family; pfam00582"
                     /db_xref="CDD:425765"
ORIGIN      
        1 mvstqlsrle ghrrkfmavi ddtpecgrav hyagmrakns ngglvllyvi adgdfqqwlg
       61 veeimraear eeaeatlakv sqsvrerigi epevviregt ateqihaaie edrdiailvl
      121 aagsakegpg plvssiagka aafpipvtvi pdaltdeeid als
//
LOCUS       WP_457579087             183 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Ensifer adhaerens].
ACCESSION   WP_457579087
VERSION     WP_457579087.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..183
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=19659
     Region          5..130
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(10,12,68..69,72)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            12
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(67,111..112,114..115,119)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(73,78..79,107,110..111,114..115,118,121)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96..98,107..108,111..112,115,119,122,126)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96,112,115,119,122,126)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(120,126..127)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          142..180
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(143..145,174..175,177..179)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259843"
ORIGIN      
        1 mtgqlygyar vstndqdlsi qeaalkaagc tiiraekksg tatggrdelr tlldfarkgd
       61 tvlvtridrl arsiadlaai vkelesrgva lkateqpidt ssaagraflq mlgvfaefet
      121 airkerqleg iakakaegiy kgrkpsidte rvralaasgm gaskiartmr igrasvyrvi
      181 qrt
//
LOCUS       WP_457579097             496 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamylcyclotransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457579097
VERSION     WP_457579097.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Oakley,A.J., Coggan,M. and Board,P.G.
  TITLE     Identification and characterization of gamma-glutamylamine
            cyclotransferase, an enzyme responsible for
            gamma-glutamyl-epsilon-lysine catabolism
  JOURNAL   J Biol Chem 285 (13), 9642-9648 (2010)
   PUBMED   20110353
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Oakley,A.J., Yamada,T., Liu,D., Coggan,M., Clark,A.G. and
            Board,P.G.
  TITLE     The identification and structural characterization of C7orf24 as
            gamma-glutamyl cyclotransferase. An essential enzyme in the
            gamma-glutamyl cycle
  JOURNAL   J Biol Chem 283 (32), 22031-22042 (2008)
   PUBMED   18515354
  REMARK    Erratum:[J Biol Chem. 2008 Nov 14;283(46):32152]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..496
                     /product="gamma-glutamylcyclotransferase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55404
     Region          330..433
                     /region_name="GGCT_like"
                     /note="GGCT-like domains, also called AIG2-like family.
                     Gamma-glutamyl cyclotransferase (GGCT) catalyzes the
                     formation of pyroglutamic acid (5-oxoproline) from
                     dipeptides containing gamma-glutamyl, and is a dimeric
                     protein. In Homo sapiens, the protein is...; cd06661"
                     /db_xref="CDD:119400"
     Site            order(330,333,335..336,404..405,411,433)
                     /site_type="active"
                     /note="putative active site pocket [active]"
                     /db_xref="CDD:119400"
     Site            order(378..379,381,411..415,417,429,432)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119400"
     Site            405
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:119400"
ORIGIN      
        1 mlksteaeie evreyfewqa pdlevtfmqk vyseavlntr hdvwdihtnk drwwvitggt
       61 nlysqeqfpn mdlaltfhig lmlriprtee qqeddlrilp fgpvfekmee agtavaqahn
      121 lpgyqavgvr cretllelig vaqdaamwtd appqranfra wteiicndll psdtnkerrg
      181 alkcalesaw tfsnwlthsk satwidadma hsliqhavgm atslilralr gvpeecpkcs
      241 srhlepehge ntaapgvlwe rprcadcgws grpiplldle dgqpiisreg eetddcsimt
      301 vplrailkpg dptieplknt etgppehvvy faygsnmsta rlrermpsck plgiatlpgh
      361 alrfhkrstd gsgkcnaiat gdknsvigvl fsfdpaertk ldkaegvgsg yehatvtvin
      421 dkgrrrkvlt ylatpdyidd nlkpygwykd fvlaggrehd lppgyvaeyi eavepiddpn
      481 ktrdrkqrat lgspgr
//
LOCUS       WP_457579101             148 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Ensifer adhaerens].
ACCESSION   WP_457579101
VERSION     WP_457579101.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..148
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16245
     Region          1..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpdepttlpl dsqlcfsiys asiainrvyk pmldalgvty tqylvlstlw erdgltisai
       61 adrlglesst itpavkrlea agflgrhrsv sderqvevhl takgrglhvk tgcltdalle
      121 nsgftvpemi dlnervrklr dgmrdavk
//
LOCUS       WP_457579103             196 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579103
VERSION     WP_457579103.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..196
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=22062
     Region          2..196
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mrillvlahp ledsfaanva rearaalear ghsvdlldly redfdprlsv aergsyfsdt
       61 ydrsgaadwi grlqaadglv lvfpqwwfnf pailkgffdr vfapgiafdn dpaggriipr
      121 lhniklfwal tttgspwwvv hlymgnpvkr llkrgiaafc aeglnfrmla lhdmdratda
      181 krkahlqrvr rlassl
//
LOCUS       WP_457579108             570 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457579108
VERSION     WP_457579108.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 570)
  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 570)
  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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..570
                     /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=61794
     Region          77..564
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mtgvteegkr rasdglaami drarhrltrp fsfyltslll vaivpafifs lvvlkrsvda
       61 qeqvitsllq astgsvtriv erdiegmltt lkvlstsrai eddnlqafye rastalaqtd
      121 sylividrkh eqrlntrvpf gtqlgkgsda dsieraftns gaplvsnvff gktagkwvfn
      181 vylpaklstg eeyllaltqn aenmakavnr dtlspgwnaa lvdgagkvii ssdaavkage
      241 pffldkvpai sigvrniken gteyrvatef svitgwriia wapraivdap avwsflwlsl
      301 ggiifagiai agslaiarll sqgvklvaqd arrlgageri eprphmiaev eqvsaalara
      361 aaartkaese irflmrevah rsknqltviq smlnqsvysa esaadfadsf rkriaglars
      421 tdlmianaaq gvdfrelaqn qlqpftpddp rrvilsgppl rletqiaqtl gmalhelatn
      481 atkygalant sgvvklswsl edegiairwr eegadlagkp sdpirkgfgt lvlermlgma
      541 lnaglermmh adgiewritv prpaegddap
//
LOCUS       WP_457579109             412 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic murein transglycosylase [Ensifer adhaerens].
ACCESSION   WP_457579109
VERSION     WP_457579109.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Nikolaidis,I., Izore,T., Job,V., Thielens,N., Breukink,E. and
            Dessen,A.
  TITLE     Calcium-dependent complex formation between PBP2 and lytic
            transglycosylase SltB1 of Pseudomonas aeruginosa
  JOURNAL   Microb Drug Resist 18 (3), 298-305 (2012)
   PUBMED   22432706
REFERENCE   2  (residues 1 to 412)
  AUTHORS   van Asselt,E.J., Kalk,K.H. and Dijkstra,B.W.
  TITLE     Crystallographic studies of the interactions of Escherichia coli
            lytic transglycosylase Slt35 with peptidoglycan
  JOURNAL   Biochemistry 39 (8), 1924-1934 (2000)
   PUBMED   10684641
REFERENCE   3  (residues 1 to 412)
  AUTHORS   van Asselt,E.J., Thunnissen,A.M. and Dijkstra,B.W.
  TITLE     High resolution crystal structures of the Escherichia coli lytic
            transglycosylase Slt70 and its complex with a peptidoglycan
            fragment
  JOURNAL   J Mol Biol 291 (4), 877-898 (1999)
   PUBMED   10452894
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18638440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..412
                     /product="lytic murein transglycosylase"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44757
     Region          18..345
                     /region_name="MltB"
                     /note="Membrane-bound lytic murein transglycosylase B
                     [Cell wall/membrane/envelope biogenesis]; COG2951"
                     /db_xref="CDD:442193"
     Region          349..412
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mlrllslttl llcgwlglaq aatkadveaq frtwlqndlw peakkagisa gsfkaafsdv
       61 klnwdlpdla ppgfpkpkeq kqsqaefssp gnyfsekrlq glaatgrsla sthastlkki
      121 ertygvpgsv ivaiwgresg fgrakipypv vdvlatkafm strpdlfrre liaalhilds
      181 gdvdeaamrg swagamgqpq fmpssflqya vdfdgdgrrd iwnsvpdsla sianylvkkg
      241 wqrerdwgfe vsipeavsca qegpdlaqpl sswankgivr isgkafpshe lsassmmlvp
      301 agrhgpefiv tpnfyvlkey nnsdlyalfi gnladriatg ggafrstwgd vgnmlrsdvl
      361 kmqkalvakg ydvgkvdglp gyktrrslgd wqaksglaat cfpdaslkak lr
//
LOCUS       WP_457579121             297 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579121
VERSION     WP_457579121.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33027
     Region          14..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..292
                     /region_name="PBP2_GcdR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators GcdR-like, contains
                     the type 2 periplasmic binding fold; cd08481"
                     /db_xref="CDD:176170"
     Site            order(99..106,108..125,127..133)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176170"
     Site            order(105..106,108,225..227,247)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176170"
ORIGIN      
        1 mklsrrlvpd vttlqafeca arhgsftqaa aelnltqsav srqikdlenq vgvllfervr
       61 qrvilsdagq kflpevrrll nqteelmvra masaradstl siaslptfgs rwlvprlpdf
      121 lkrhpdtvin iasrsapfdf eeqnfdlaih ygqpvwarat csylcseiiv paaspamlat
      181 hpvaspediv tgpmlhlatr pklwaqwfea ndmdgrgayr gnrfdqfsmv ieaataglgf
      241 allprylieq eigagtlqiv ldrpmqtens yylavpegkl enpislafre witeqvg
//
LOCUS       WP_457579123             393 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457579123
VERSION     WP_457579123.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40663
     Region          4..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 msnpsivias agrtavgsfn gafgntpahe lgaavikgvl eragveaaev devilgqvlq
       61 agegqnparq aamkagvpqe ktawgmnqlc gsglravalg mqqiatgdae iivaggiesm
      121 smaphcshlr ggvkmgdfkm idtmikdglt dafygyhmgi taenvarqwq lsreeqdafa
      181 lasqnkaeaa qkagrfadei ipfivkgrkg dvtvdqdeyi rhgatldqmt klrpafdkeg
      241 tvtagnasgl ndgaaatllm teaqaskrgi qplarivswa tagvdpqvmg tgpipasrka
      301 laragwaigd velveaneaf aaqacavnkd lgwdpsivnv nggaiaighp igasgarvln
      361 tllfemkrrg vskglatlci gggmgvamcv erl
//
LOCUS       WP_457579125             167 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Ensifer adhaerens].
ACCESSION   WP_457579125
VERSION     WP_457579125.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..167
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18193
     Region          8..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpfkleseti gmlltdvsrl lrgafdrkvn amdlgirpge artliqvalt egikqaeiat
       61 rmgiepmtls ayldrleang lvarvpdpad rraknvvite kagplfnelm tglremmday
      121 tegldseara llcsnlrilr dnlrqldpcl agketaekae vrvgaap
//
LOCUS       WP_457579126             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579126
VERSION     WP_457579126.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30285
     Region          1..288
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 msliafwgav elglvyafva lgvflafrvl dfpdltvdgs fplgaavtav liiagvnpwl
       61 aacvamvaga aagivtamln vrfkilnlla siltmialfs vnlrvmgkpn valinadtml
      121 spfyglglrd fyvrplfigv lvvvaviivw rflesdagla mratganarm araqgvdtnr
      181 qiylgmaisn alvafggalf aqtngfadvt sgvgtivvgl aaviigetll gprgiliali
      241 gcvlgsilyr iaiqlalstd mlglqasdln fvtaalvtfa lvlprlrrgg aa
//
LOCUS       WP_457579128             850 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579128
VERSION     WP_457579128.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 850)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 850)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 850)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 850)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 850)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 850)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..850
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88989
     Region          21..850
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 migapsvrlr pllalrlalr emrgglkgfy iflacialgt aaiagvnsls qsitatiasq
       61 gqellagdir felnnrvatt eerayldglg tvaisaglrs marlpdgsnq alvelkavda
      121 ayplygtles epdrplhdli ardgdvfgav vapllldrld vkvgdeillg narvriagti
      181 trepdalsdg fgfaprlmvs dealaatglv qtgslvehty kvkladpagv aavrteaeks
      241 qpaagwsirt sgnaapalta nitrfsqflt lvgltalivg gvgvanavra yldakrsvia
      301 tfkclgapaa lvamiylaqi lmialigivi glalgalipf vaaqfladll pistafhlyp
      361 galglaalfg vltaltfail plgraraipa talfrqqgfd psgfpawpyl lgavaclaal
      421 aglaiftayd ryislvflga iafafivlra valaiawlar rsprvnspal rlaignihrp
      481 galtssvvls lglglallvt lalidgnlrr eltgslaera pnfffvdiqg seiegfrsvl
      541 nqaipkgkvi evpmlrgrit afngedvnsr nvppagqwvl rgdrgityak nkpenstlse
      601 gawwpadysg eplvsfssee agelglkigd tvtvnvlgrn itakianfrn veweslsinf
      661 vmvfspntfa gaphawlatv idpsatpeee aavlkavtna yptitsvrvk daldivngll
      721 gqlatairaa aavalvasvl vlagalaagn rarvhdavvl ktlgatrvtl ikafsyeyai
      781 lglatavfal faggiaawfv vnrimtlpss flpdvaivtv vaalvmtvgi glagtwrilg
      841 qkaapvlrel
//
LOCUS       WP_457579136             521 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Ensifer adhaerens].
ACCESSION   WP_457579136
VERSION     WP_457579136.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..521
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58393
     Region          8..508
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 madtlktlsr rsfllsagaa gfvassglat pfyargygrp efihgvqsgd vdtssgmiwt
       61 rvdrpskvsv eysttesfsn plrladltat pqtdcaikcs ldgllpdqdi fyrftatdly
      121 dvnrvsapvt grfrtaplrk rsirfvwsgd tagqgwgidd vgmktystmr qhepdffihs
      181 gdtiyadnpi pdeialrdgg vwknrvvthe krdvartlee yrgqwkynll dehvrqlnav
      241 cptfyqwddh evlnnwsast dlrddarype kdvavyaera arafhemtpi rmpatqpgrv
      301 frkigygpll dvffvdlrsy rganqgedgg galfgwrqvd wlkrelaasr atwkviacdm
      361 piglvvwddy tnrrgsdaia ngdngppagr erefadllrf vrdngidnlv wltadvhyta
      421 ahhydpgrga frdftpfwef vsgplhsgty gpkeldmtfg pevrfikasg ggidqnlpps
      481 aglqffgivd ingqtqqmtv rlmdrqdqel wrvtldpaai a
//
LOCUS       WP_457579139             361 aa            linear   BCT 27-JAN-2026
DEFINITION  TraB/GumN family protein [Ensifer adhaerens].
ACCESSION   WP_457579139
VERSION     WP_457579139.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007931
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..361
                     /product="TraB/GumN family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38561
     Region          83..359
                     /region_name="TraB"
                     /note="Uncharacterized conserved protein YbaP, TraB family
                     [Function unknown]; COG3735"
                     /db_xref="CDD:442949"
ORIGIN      
        1 mtafarpqqn lprhllarla dgalwlaall hvmlaacllv alvfvaeada tevecgganv
       61 ltalaksdpt klaaleaeaa aipnskgifw kiekdgvaps wllgtmhvtd prvlalptea
      121 paafeaastv ivesdeiide kksaaailmr pdltmlpdnk tiadflkpdd reqvetglka
      181 rgipltlvsr mkpwmiasfv alpacemsrk aagasfldkk iaedavsqgk tlkgletlve
      241 qlaamdslpt elhlraliet lalgktiddv fatmtdlyla gdtgmimpmm kavsdksaed
      301 fgyadfeqri ivdrnktmat raepilkdgg afmavgalhl pgkeglvell raqgftvtra
      361 n
//
LOCUS       WP_457579140             494 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleobase:cation symporter-2 family protein [Ensifer adhaerens].
ACCESSION   WP_457579140
VERSION     WP_457579140.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..494
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=51181
     Region          23..475
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 msdvssihpv derlpvgrla tlglqhvlvm yggavavpli vgralqlspq dvaflisadl
       61 fvcglvtiiq slglgrsigi rlpvmmgvtf asvgpmvsma amtpgqegar mifgaiigas
      121 lvalllapvm grllrffppv vtgtiilvig vslmrvgvnw ifgnpfgpta pklvdpshae
      181 wlaelkkaaa tggpavpdgl vlgasvpnpl yaepshiala gfvllsilvi arfgrglisn
      241 iavltgvvvg cvvaaalgmm hfdrvadagw favvtplrfg mpifdpvlia tmslvmivvm
      301 iestgmflal geitnrevsr qqltaglrvd glgtmigglf ntfpytsfsq nvglvgvtgv
      361 ksryvcvmgg vimialglip kmgalveavp tfvlggaglv mfgmvaatgv rilstvdfks
      421 srnnlfvvav svgfglipli apnfliwlph aihpiiesgi vlasisavvl naffnglsfe
      481 stasvnaakl adsh
//
LOCUS       WP_457579142             409 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457579142
VERSION     WP_457579142.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42000
     Region          49..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(64,119..120,122..124,127,147,150..151,154,228,
                     231..232,235..237,240,264,268,324..325,329,333,349,
                     352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpnpprdtlp pafkrigwsn lfaqfseqma laaaplaavl llaagpaetg wlqmaqtlpf
       61 lllsipaglv adrasrrrlm vssemlrals lvatlllmlg gllslpllav mgfvgaigtv
      121 cynvaapalv paivprhqla danrwlelar slaysggpai ggaivawtga slayvaatsl
      181 sllsvvlldg lgdqqqptap rrnllqdlae garflgghpl lrpilvtaiv fntawfvlqa
      241 vyvayaiqtl gltatgvgit lgiygagmmi gafaapaiar ripfglmial gplggltaaa
      301 vmlstiwvps galaglsffl fgagpvlwsi atltlrqavt pnamlgrvsa fittatfgar
      361 pigaalgavv atrfgveacl avaavgfliq flviiasgvp qlralpeaa
//
LOCUS       WP_457579155             285 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579155
VERSION     WP_457579155.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..285
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31015
     Region          2..257
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mldlvqlrsf valeqmgsft laaeklslgq stvsqhiqrl easlgrtlvd rdthrvslta
       61 dgqallahar smlaidgevr alfaesslrg rlrlgvsedf vmsrlpavle dfvrahpsvd
      121 leltvalsgv lyqmqdngei dlvlakrrlg dlrgelvyre plvwlardpe rikrdkvlpl
      181 iafpppsitr svalevldrh rlpwrivctc gslsgltaaa ragmgvlvqp rsmvpsglke
      241 ipagllpple dvefvlvpsk gvdqklsaal sveilanlrt lqgqs
//
LOCUS       WP_457579157             192 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579157
VERSION     WP_457579157.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21029
     Region          7..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msrksirenl lkagdqlvwn tgyagtgvrd iveaagarpg sftnhftske dfvievldry
       61 fayvsglvee algdrsvrsv drlrryidli tgkladadys rgcmignlsl easfdnerlr
      121 ahlsklfktw rgpfeaciae glekgeiapl gsaaeladfl lsawqgghaa hegrsqpgaa
      181 cnvqddrffn rv
//
LOCUS       WP_457579165             463 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Ensifer adhaerens].
ACCESSION   WP_457579165
VERSION     WP_457579165.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..463
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49431
     Region          27..433
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlpsalrhrl saiiagllpi ltssdaknaa rrmalvafsv rivsaaiafl sqiilarlmg
       61 efeygifvfv wvlvilfgsl scvgfhsvvi rflpeyqasa amdeirgvtt tvrifalssa
      121 ttvavlglag lwffsghiea yylvplylgl ftlpmislgd vmdgtarahg wpiaamsptf
      181 iirpllvlvf mvlavtagap htaqtammaa maaayvtsvs qflaltyrlr sryvpgprri
      241 elrrwlkvsi pvflvdgfgf lltnsdvviv glylepddva iyfaaaktma lvhfvmfavk
      301 aaagprvsna mardpgqipg iavesarwaf wpsllvgalv llagpfllsl fgpafvtglp
      361 lmmvlfagil akafvgpaet lltmvgqqtl cvilyagalv vnialnlsli plfglngaaf
      421 atagamfvea mllhlavrrt fgfalfafar aragnennga vhp
//
LOCUS       WP_457579171             484 aa            linear   BCT 27-JAN-2026
DEFINITION  argonaute/piwi family protein [Ensifer adhaerens].
ACCESSION   WP_457579171
VERSION     WP_457579171.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Thomson,T. and Lin,H.
  TITLE     The biogenesis and function of PIWI proteins and piRNAs: progress
            and prospect
  JOURNAL   Annu Rev Cell Dev Biol 25, 355-376 (2009)
   PUBMED   19575643
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Hutvagner,G. and Simard,M.J.
  TITLE     Argonaute proteins: key players in RNA silencing
  JOURNAL   Nat Rev Mol Cell Biol 9 (1), 22-32 (2008)
   PUBMED   18073770
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Hall,T.M.
  TITLE     Structure and function of argonaute proteins
  JOURNAL   Structure 13 (10), 1403-1408 (2005)
   PUBMED   16216572
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Carmell,M.A., Xuan,Z., Zhang,M.Q. and Hannon,G.J.
  TITLE     The Argonaute family: tentacles that reach into RNAi, developmental
            control, stem cell maintenance, and tumorigenesis
  JOURNAL   Genes Dev 16 (21), 2733-2742 (2002)
   PUBMED   12414724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..484
                     /product="argonaute/piwi family protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54011
     Region          11..472
                     /region_name="Piwi_piwi-like_ProArk"
                     /note="PIWI domain, Piwi-like subfamily found in Archaea
                     and Bacteria. RNA silencing refers to a group of related
                     gene-silencing mechanisms mediated by short RNA molecules,
                     including siRNAs, miRNAs, and heterochromatin-related
                     guide RNAs. The central component...; cd04659"
                     /db_xref="CDD:240017"
     Site            order(183,187,198..201,204,229,232,236,240,446)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240017"
     Site            order(264,266,339,462)
                     /site_type="active"
                     /db_xref="CDD:240017"
ORIGIN      
        1 mkftstifke pqlefgdkhq dpdprrglfl agplqtasgd aikiavvgsa ktvedtekfl
       61 aaasvgflgk sekhpnmhpd fpglgnqnpy rckfeiaqda taaipqakie kirkeplhgr
      121 avemavdevm elltaieegs srpdvaival pvaliervwn akvdsdgtve keddggsdap
      181 nfrgllkara mhlrfpiqiv wedvlderav iprkvkessa rkiqdeagrs wnimtslyyk
      241 gsgripwrrm pqegefsacy igisfyrevg gqqlftsaaq mfdergrgfi lkgrraqtet
      301 rgrhpymiqd dakalvaevl aaykshhkhf parvivlkts rfrdeeadgi mealeevgte
      361 mkdlvwvqet ssikvlrdgn ypvlrgtfve ldgkgllytn gsipyygtyp gmydprplll
      421 cphktsdstv aqiakevlsm tkinwnstqm nqklpipira arkvgevlky vgdgkvssdy
      481 trym
//
LOCUS       WP_457579163             350 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Ensifer adhaerens].
ACCESSION   WP_457579163
VERSION     WP_457579163.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..350
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37622
     Region          5..342
                     /region_name="CAD1"
                     /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283"
                     /db_xref="CDD:176186"
     Site            order(41..43,46,158,162,182..187,205..206,210,225,
                     244..245,247,267..268,291..293)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(41,43,63,89,158,293)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(41,63,158)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(94,97,100,108)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(107,165,169,261,266..268,270,279,281..282,285..292)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176186"
ORIGIN      
        1 maiargyaat daskpltpft ferreprddd vvieikycgv chsdihqarn ewgnsafpmv
       61 pgheivgivt avgskvtkfk vgdragvgcf vnscttcatr dldlehympg lvvtyngvea
      121 dgktptqggy sdsivvkegy vlsipenlpl daaapllcag itlysplrhw kagpgkkvai
      181 vgmgglghmg vklaramgad vtvlsqtlsk kedglklgad hyyatndpet ftalagtfdl
      241 iictvaaeid wnaylnllkv dgdlvlvgip enavpvhafs lvparrsisg smigsiketq
      301 emldfcgehn ivseietiri qeineayerv vksdvryrfv idmaslqdaa
//
LOCUS       WP_457579173              95 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579173
VERSION     WP_457579173.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 95)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..95
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9923
     Region          15..>46
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 matsdgyvrc lgsaraarel lglkqveaae aagisrrtiq rletgeldrt rasillqtcy
       61 edqgivfvrp aggqgwglid nsqgskaggq dsieg
//
LOCUS       WP_457579170             311 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579170
VERSION     WP_457579170.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..311
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=32251
     Region          32..308
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mvagglkrtr agnqerrntm sksksksisi iglgamgtal aktlidagnt atvwnrtpar
       61 adalvargar raatvaeaia asdvlilclt dyaavettla gvgtaiaskt vvnltngrpd
      121 evravaarle aygaryldgg imatppmigt pdafilcsgs adafektreq laafgqshyl
      181 gedpvlaavs dlallsamyg lfggylhata lagsvgftak qflplvepwl aammtalpdy
      241 aeridsgdhg rdvmsnlsmq svaitnivaa srslgidpaf mepierlakk rlaagfgsde
      301 asglieamrg k
//
LOCUS       WP_457579153             303 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579153
VERSION     WP_457579153.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32497
     Region          12..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 msrlsinrsg emavfakave lggfsaaakv ccmtpsavsk lvqrleerlg irlinrstrr
       61 lqltaegcaf yeravrilad ideaereags getpegrvrl nvsasyavhv lmpvlpefls
      121 afpsvsldil qtdavvdlma eradiavrag plksssliar klgstsmtiv gapsylqrfg
      181 mpesvgdlea mnrlshsyar sidgwpllsn gepftlapte qvrvsdgegl rqltlagvgl
      241 arlptftvke dircgrltav aehlnpgdie afhavfhgqg galparvrvv ldflakrari
      301 ssp
//
LOCUS       WP_457579158             604 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Ensifer adhaerens].
ACCESSION   WP_457579158
VERSION     WP_457579158.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12182596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..604
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=64565
     Region          38..179
                     /region_name="sCache_2"
                     /note="Single Cache domain 2; pfam17200"
                     /db_xref="CDD:435780"
     Region          166..591
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkniristri ylltamalvf maaamayktq vansevsder rqmlrnvtea aistiasfee
       61 qerngtlshe eaqsraisav mamrfgqdgy ffingfdgmm iahplakklv gtdvrglkdt
      121 ngkafnveli alaqnpgsgi vnyywdkpgh eepvekysyi qgfkpwgwgv gtgvyaddla
      181 akynasllmt iittaiaaia tlaaamaigr sisrpinrlk dvmlevsnnd trsevpdtdr
      241 rdeighmada lvvlrasvie rnalevrqre qqvaldgers aneemqqata rvqahvvsti
      301 ggalerlasg dltthvpdlg adyeklrqdf ntavaalrst vsaiadstsv vtgnaneisr
      361 aandlsqrte qqaasleeta aaldeitsav qnstnraeea trmvaearkg aatssevvrd
      421 aitamgrien ssskigeiig viddiafqtn llalnagvea aragdagkgf avvaqevrel
      481 aqrsataake ikglitasgv evsagvrlve atgsalgdie rrvneindri vaiataareq
      541 svglreinta vnqmdqmtqq naamveqtsa asqalagesn vlsgrlaqft veekawrpsa
      601 qraa
//
LOCUS       WP_457579177             551 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457579177
VERSION     WP_457579177.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 551)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 551)
  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 551)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..551
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58699
     Region          130..463
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 magrwtsrvd evaalwlprr easspadlrh akrlrtlaav sltalpvvpl alslampvss
       61 alplgtalwa sasllaaaga ivrgrapeev applepvvpd lsaaydlfag lvtvhdlrgn
      121 vlsvhgrdaa ehltlmrdpa grgfieqihi sdritflsai dilrqggdra tvdirierrt
      181 lpiegeqfvy mscelaplrd dngrlvaila qsrdvsqeag lraeaaarta eavsandakt
      241 rflaavshel rtplnailgf sdvlageyfg klendrqrey vglihksgeh llsvvntmld
      301 mskieagrye lmpepfgvae avsaceamls hqatekgvkl asritrgige inadqrafqq
      361 ilinlvgnai kftdqggvvt idaeaagaml klsvsdtgig iaadklallg qpfvqiqndy
      421 trryegtglg lslvkglval hggelsirsr egegtvivvt lprdgsgiac aeqeeartpv
      481 tvefpprlkd cdvapaaegg avrgeklerg tgiwhrasen sltgkrlrgk rpawpcagws
      541 lpdgvlglpv v
//
LOCUS       WP_457579180             128 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Ensifer adhaerens].
ACCESSION   WP_457579180
VERSION     WP_457579180.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..128
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13496
     Region          1..124
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mrtigaeltl veqgtveiel pfddkltqqh gflhagvisa aldsagtyaa ysvidpdasi
       61 ltiefkvnll spgrgerflf rgevtkpgst iivsdgrgya irsdgpakli asmtgtmmvv
      121 rgregieg
//
LOCUS       WP_457579184              92 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579184
VERSION     WP_457579184.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..92
                     /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=10809
     Region          35..91
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mkpmhcptdl sprrrggggr lfgvtamifn dtvgfytkre vcrmtkyspr slyryvkkgl
       61 fplpvplskr rkvwwipdvh qwfreqlgkp rk
//
LOCUS       WP_457579189             321 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Ensifer adhaerens].
ACCESSION   WP_457579189
VERSION     WP_457579189.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..321
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35311
     Region          7..320
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 msrgadnfyk sdrvtlekvt fktqyelnva gnlflpnnld pamrhpaivv ghpmgavkeq
       61 satlyatkma eqgfvamaid lpfwgesege prnavspdly aeafsaaidf lgtrpfvdre
      121 riggigvcgs gsfiisaaki dprlkaiatv smydmgaanr dalnkslsae qrkeiiaaaa
      181 qkryaefegg aievaggtdl eltatthpiq refydfyrtp rgeytpvgas dqrttkptvt
      241 sntkfmnfyp fndietispr pmlfisgdqa hskefsqday draaepkell wvkgaghvdl
      301 ydrvdlipfd klhsffgqhl a
//
LOCUS       WP_457579191             464 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457579191
VERSION     WP_457579191.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..464
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=50894
     Region          5..420
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mfwgrlaalg tlalgavlav pldrsglyva aivafgllna lafgfarssr fatvttwsfv
       61 vvdaailtyi fvtpspfave gwtsqlnlrl pnflylgvfl vsmalsyspa lvvwsgavti
      121 vvwtfaycwv atrpdtiayg rdlldgglsd aeiialvldp rsvslinlsy qtmflvlvti
      181 ilaisvwrsr rlvrkqvaae aqrsalsryf spnivrelss gtsgfgepsl qsaailfadm
      241 vgftriserl apedlvkllk eyharlatva fahggtvdky igdeimvhfg tprprkddaa
      301 ralacardml eqvrqwneqr lasgehaiev gigvhygevi vgnigderrl eytvlgdtvn
      361 vasrlerltr kigtslavsd dllvaaraqg snlgatieel rpdqmrfvrg rrrpvavwyl
      421 pqahragrrg srqhpvpsql kqvdrilpvt gtttfdisrr lppp
//
LOCUS       WP_457579192             148 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579192
VERSION     WP_457579192.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..148
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15342
     Region          1..136
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 meliingtkh qvdiepdtpl lwvlrdelam tgtkygcgla qcgactvlvd gqatrscvtp
       61 vesvagadim tieavaddpv gqkvveawvt nqvaqcgycq sgqvmaatal lkqtpkptde
      121 diagamvnlc rcgtynaiaa avrdaaqa
//
LOCUS       WP_457579193             124 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Ensifer adhaerens].
ACCESSION   WP_457579193
VERSION     WP_457579193.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..124
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13092
     Region          27..123
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mktlvlasla sllvavvvap aysqetdaap garlfqqrcg tchqiattrn gvgphlqgvv
       61 graagsdegf kyspalkasg vtwttetlet flanpgamvr gtrmtqrfnn aeerraiief
      121 lgsr
//
LOCUS       WP_457579197             308 aa            linear   BCT 27-JAN-2026
DEFINITION  XdhC family protein [Ensifer adhaerens].
ACCESSION   WP_457579197
VERSION     WP_457579197.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..308
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32915
     Region          23..308
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mndnpllvlp tparalltdd piellkfaae afkdsqvaia tlveirggaa rslgsqvivl
       61 sdgrfagyvs ggcveaavaa eallamaegr drtvrfgdgs pfldvvlpcg ggitvaihvv
      121 rrmeeveral eslrlrqata lrysparqsl alaepmerag wvggdfltiy rpstkvvisg
      181 qtievrsvar laecsgfevm vlapemgprf igdvvdpfsa ivllhhdleq empvleaalq
      241 tscfylgalg srrthqrrln rllrlghyep elarikapig lfgptrdsas lalsiladva
      301 asrsaafg
//
LOCUS       WP_457579198             289 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Ensifer adhaerens].
ACCESSION   WP_457579198
VERSION     WP_457579198.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..289
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31658
     Region          21..266
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(36,117,119,121..122,150,199,220,223,235,237,266)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mrrtqattdv hrasilsgea vkvgdlelcv vsagpldige pqkafdaass ddakvrelwt
       61 essvvveqnv lairsqgrva ifetgaptkd sntsplcsel tsagiepesv daiipthahl
      121 dhvggimrpd grrnfpnari hlhpsdaefw laderlgtra ersalvarrn lipnldrlvr
      181 hvddqetypg vtvmhtpght vghtsfivds gsdllflvgd vvhhpcqlah prirmlfdtd
      241 pdagvetrlk vleflasrtm paffyhfpfp gcgyversge gyrflplpm
//
LOCUS       WP_457579199             130 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579199
VERSION     WP_457579199.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..130
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=13265
     Region          1..>121
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnrfegrtvi vtgagsgiga acvrrlhaeg advvavdvtn eavdkivsef ggsarisgav
       61 ldvrdqhaae tlaiqtrarl grlnglinca gitgvasvld vepeklervm avnlgghcqh
      121 vpgvracgtp
//
LOCUS       WP_457579200             132 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579200
VERSION     WP_457579200.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..132
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=13620
     Region          <1..130
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mcqafvravr hdtgpraivn issgagvmgv pnrlpyvask favsgitksm spelgplgir
       61 vnavapgmtk tplveymlqd paaverikaa hpigrmgepe eiaavivfll tedasfmtga
      121 vvsvdggqta cl
//
LOCUS       WP_457579201             333 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579201
VERSION     WP_457579201.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..333
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36584
     Region          7..303
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mhlvhkidpk kllylatiie hgslksaara lnvsqpalsg smnrleselg irafertskg
       61 vfptplgeil ycharlirde iglaeralln awggapaavr lgslpslats vmplalqrwg
      121 qahpdrelqi vespqidllv gllrrefdfv igftecydle eglrqrvlfr dkllviarkg
      181 hplagqpdvd wrtlvsypwv fpsarrphav lgaalrstni sppenvtvcg svtllkavva
      241 nsdhlavlpl havneeldeg rlcnipidat aldrnialyf regyqmdeas rdliaiverv
      301 gqeicqrgla trtsavgpat rlhdsgeqde qsr
//
LOCUS       WP_457579204             328 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Ensifer adhaerens].
ACCESSION   WP_457579204
VERSION     WP_457579204.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34826
     Region          28..325
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mnwsqiarrr liatatalga lalttthasa adgqirwlvg yppggstdai arllaapisk
       61 tldqtiivdn rpgagssiaa aalakskpdg ltvmsvdngt lvinpvayrt lqydpdkdfr
      121 pvgvyaevnf llavgkdqpy ktveeflsqa ktasvpiaya spgigtplhl avermareag
      181 vklehvayrg mapalndala gvvpsividy ttaremirsg dlrplaifss trlpalpdvp
      241 tfgekalpgf savawqamvv phdtpddavn rlsdalakal edpavksrya llglgmppsd
      301 pqsfqkrwqe dkavwqplir dlgvtlge
//
LOCUS       WP_457579205             287 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579205
VERSION     WP_457579205.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Hong,H., Seo,H., Park,W. and Kim,K.J.
  TITLE     Sequence, structure and function-based classification of the
            broadly conserved FAH superfamily reveals two distinct
            fumarylpyruvate hydrolase subfamilies
  JOURNAL   Environ Microbiol 22 (1), 270-285 (2020)
   PUBMED   31657110
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Ran,T., Gao,Y., Marsh,M., Zhu,W., Wang,M., Mao,X., Xu,L., Xu,D. and
            Wang,W.
  TITLE     Crystal structures of Cg1458 reveal a catalytic lid domain and a
            common catalytic mechanism for the FAH family
  JOURNAL   Biochem J 449 (1), 51-60 (2013)
   PUBMED   23046410
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12105251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..287
                     /product="fumarylacetoacetate hydrolase family protein"
                     /EC_number="3.7.-.-"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30224
     Region          1..65
                     /region_name="DUF2437"
                     /note="Domain of unknown function (DUF2437); pfam10370"
                     /db_xref="CDD:463061"
     Region          64..287
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkvarfsnng kvllgvanda agtvhpfdsn ltsmadlirf sasgfsftaa sgpglplsev
       61 tllapiiper nifcvgknyy ehakefagsg feagavkgqe idaypaifsk ppstvigpda
      121 vvemhpqatq avdyeaelai vvgrpgrnia eadamqhvwg ytivndvtar drqrnhkqwl
      181 agkgldtfcp mgpwivtade idganldiec kvngevrqka ntsdlifkip qliaaisagl
      241 tlqpgdviat gtpagvgigf tpprflkagd rveitisgig slsntfa
//
LOCUS       WP_457579207             262 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579207
VERSION     WP_457579207.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..262
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26973
     Region          9..248
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 msepsvssan pllakmaagk ltvgmivrli rgveivaiak tagfdclfld lehnsfslet
       61 igqiciasnl agitplvrvv dsghasitra lecgamgvia pqvetakdav avvqaakfpp
      121 lghrsiapcl pllefrptpa veamqringa tmvvvmvesl aaldaideia avdgvdmllv
      181 gandlcnalg lpgqiehptv raafarvada ckangiylgv gglgsnpela kemislgary
      241 atagadvtff tnaamahark fq
//
LOCUS       WP_457579208             291 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579208
VERSION     WP_457579208.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..291
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30845
     Region          43..288
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtkitselet ravpasdesd vtvvhtpqds gvpgwardfs vvdrvvlitg agqgigrela
       61 rqfaasgatp ivadlnltna qsvrdeivas ggrasalqvd iadagsvdll vksviaehgr
      121 idvlinnaam fatldkrhfe mipldewdrv irvnvtgpfl caravaplmr sagwgriinv
      181 ssdavpkgvr nylhyvtsks aiigmtnala relgpdginv ncirpgpvat everavnptl
      241 dlrrlqlsqq ciqrgmvhtd lvglmiflat paagfitgqt iacdggyths s
//
LOCUS       WP_457579209             350 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579209
VERSION     WP_457579209.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..350
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38669
     Region          21..311
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mldefvwtei eevrlvsglr idpkkilyla tiiehgslks aaralemsqp alttsmnrle
       61 eelgmqvler spsgvvptat geilycharl irdeislaar allsaqggnp giirvgslps
      121 lassimpial srwrdiyrer elevvevpqi dlltgllrre fdfvfgftec ydlenglrqr
      181 vlfrdklcvi araghplase rnlqwevlvs ypwvcptarr shvildaalk kanvappeqm
      241 tvcgsvtllk slvvngdhla vlpahavrvd ldegrlcrld vtdpvldrni avffregyql
      301 depsrdlvsl vgsvgqelsa rekeraalei sappeddvtk laeeapvpap
//
LOCUS       WP_457579210             327 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Ensifer adhaerens].
ACCESSION   WP_457579210
VERSION     WP_457579210.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34689
     Region          1..324
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 miinrrnflv aasagaaltl plarsvfaqd nypshpvsfi ignppggddd tlsrflaeqi
       61 radlgqtiiv dnrgggattv agnlvassdp dgyrilcltt sgivqtvlrd nlpynldnfa
      121 pivgiggypm alvvsgqsdi ktmddlikva kspegitfgs agagtlahlt avrflkeigg
      181 ngvhvafknn peglqslggg fiqmmfpsar eaatlsangl lrvlavtspe rtsnlpdvat
      241 mselghpdid smlwygymap kgtpdavvqr lsdaiskgvq seafhqkfqp lafqeqlltg
      301 galrefmtvq aqrwqtvike nnvkftd
//
LOCUS       WP_457579212             247 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579212
VERSION     WP_457579212.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..247
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25179
     Region          12..245
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mneqnntggs rrlagrrilv tgaasgigka taelfagega lvacldrnas avtevasaig
       61 gyaiaaditd egdvakavnr ihdnlggidg lvnaagimat gsiqdmpval wrqiidvnli
      121 gtylvtkscv pflqrgetgt ivniasaqgl lpnvanhtay aaskgavvnl sralaaelsp
      181 qirvnavcpg mvdtpmavgn ggntdnyamk rvarpdeias ailfltswes syvtgaalav
      241 dggrsfh
//
LOCUS       WP_457579218             126 aa            linear   BCT 27-JAN-2026
DEFINITION  SOS response-associated peptidase [Ensifer adhaerens].
ACCESSION   WP_457579218
VERSION     WP_457579218.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..126
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=13835
     Region          <2..115
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mpadgfyewt kgedggkdpw fiylpdrkpf sfaglwaynq aldvvsctil tmaagqpmtq
       61 lhdrqpvilk peahdawlsq dtsvpdakal lqrnldgelq fhrvsrains skfegdpgin
      121 vafaga
//
LOCUS       WP_457579230             309 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579230
VERSION     WP_457579230.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33931
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 metlanlesf vrsaelgsfs saarrlgltp aavsrnvaal esnlklrlfq rstrslalte
       61 agerflhsvr dhleslqgai aeasneqtep agvlrlsmsp tfgieyilpk lpefmsrypl
      121 irpewmfenr qvdliaegyd aaigggfelt pgiiaktlas ahiiavaspl ymqnrvpphd
      181 psglteldgi vmrslrtgri rhwqmrnvag eeqsaalker ivvndpaamr saallglgva
      241 miakpdalpy lengelvrlt pawyadagpi siyyasrtll ptktrvfidf igevfqrerw
      301 perfagtlg
//
LOCUS       WP_457579231             250 aa            linear   BCT 27-JAN-2026
DEFINITION  3-oxoacyl-ACP reductase family protein [Ensifer adhaerens].
ACCESSION   WP_457579231
VERSION     WP_457579231.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481062
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..250
                     /product="3-oxoacyl-ACP reductase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25357
     Region          6..250
                     /region_name="fabG"
                     /note="3-ketoacyl-(acyl-carrier-protein) reductase;
                     Validated; PRK05557"
                     /db_xref="CDD:235500"
ORIGIN      
        1 mtnisqklsg ktalvtggsr sigaaiamrl aadgaavait ysaspekaaa vvkeienagg
       61 raiaihadsg npesvraava kteetfgsld ilvnnagial ggpiedikfe dyermiavnv
      121 tgvfvgtqea arrmksggri ihigssmvry aafptaslyt ltkgavagft rslvrdlgpk
      181 gitvntvhpg ptdtdmnpdg gpvskivgpg maigrygkdy evasvvayla speaafvtga
      241 divadggfta
//
LOCUS       WP_457579232             199 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent F420 reductase [Ensifer adhaerens].
ACCESSION   WP_457579232
VERSION     WP_457579232.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..199
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20485
     Region          13..190
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 msigiigage igsafarala qngiaatisn srgpetlrdf aaeltphita gtieeaaead
       61 lvlvaipwsk lpkaltglpd wagrividan npierplfqp aelngrlste vfadlvpgar
      121 vvkafnhlpp hllsgdprae ggsrilfysg ddarsraevg aliaklgfag idlgpvsvgg
      181 klvqfpggpl palnlvkfg
//
LOCUS       WP_457579233             396 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457579233
VERSION     WP_457579233.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..396
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39752
     Region          28..390
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,227,230..231,234..236,239,267,271,320..321,
                     325,329,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mdmpvspsht gtrahaplas wpavatvgig afalvttefl pvgllpqiaa eigisegqag
       61 lmvttpgvla aiaapltigl agrfdrkhvl vfllgllvls naivamatsf qalmfgrvll
      121 gigvggfwti ggslgprlrp gaeggratsl iysgvslgtv agvpagalvg nllgwrllfg
      181 lasgvaifvv aalllllpsi kpqqssglaq ipavlrnrkt qvgllaavli figqfaayty
      241 itpflnqvsh idaaalsall lgygvagfig nlfggwavgk hlsftlsgts alislsafgl
      301 aatgdsavaa tiwtlawgfg fgmlpiamqt ymfssapdql esvaalfvst aqlaigagal
      361 vgglavdyfg vasalviggg aglltvliva mssvsr
//
LOCUS       WP_457579235             112 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579235
VERSION     WP_457579235.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..112
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11971
     Region          4..59
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mdttsemmta lragrallgl sqeelaalag vsrqvvvrie kcegnvlvdt iekvrsalea
       61 egvvfidgeg trgpgggpya cssaadqcra vdrlrartrp hqmrygrldr kp
//
LOCUS       WP_457579238             265 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Ensifer adhaerens].
ACCESSION   WP_457579238
VERSION     WP_457579238.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..265
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=30306
     Region          <1..254
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mksrgakrqa reclkilrtf fgwamlphrr eaiglernpi adltprrmal pnitrsrhfg
       61 yleikayiaa aaridypygp faralielgq rrgevlkmrw snldlerkvw tipgktskpe
      121 sdhivflsdg mvgmlkllra gqaeghgdfv fsmshgqrpi anvsrfktsf ergfvtefgc
      181 iaptsvlrhw twhdvrrtvr tqlepivgrr evaaaaighg ksgmeriynl yayakeiraa
      241 fnawseklrk msdgtfrled wedse
//
LOCUS       WP_457579242             402 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579242
VERSION     WP_457579242.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=42752
     Region          2..381
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mreriliiga gfagmwsalg amrlldqqgk adgsvevavi apqpelhvrp rlyeknaaqm
       61 kaplseifan agvrfikgya tgisttdnvv tyqdgdgrhs titysklvla tgsvlfrpdi
      121 pgldhafnvd qladaakled hisdlgrlpe tharntvvia gggftgieta aemphrlraa
      181 lgdtakirvv ivergpaigp dlgpgprpvi eqallelgve tylrapivai desgvslstg
      241 erieaatviw tagaranpit sqidankdsf grlhvdrnlk vigqenvfat gdvacaatdd
      301 lgnrtmmscq haqnlgrssg hnvaadllgv apipysqeky vtcldlgpwg avytegwdrq
      361 iklsgaeakk lkttinttwi yppiadrtta laaadplriv va
//
LOCUS       WP_457579246             438 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579246
VERSION     WP_457579246.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15920060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..438
                     /product="epoxide hydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48004
     Region          50..154
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          121..>246
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          141..422
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mnlenkagdg pltrrsflfr gaaigvaaav lpgtgiaadi vkatatgdai qpfkadipen
       61 alidlrrrlv atrwpdsatv sdrsqgvqqr klrvlaqywq ssydwrraer klnafpqflt
      121 kidgldihfi hvrsrhenal plimthgwpg sifelldvid pltdptahgg kaedafhlvi
      181 psipgfgfsq kpdttgweaq riarawdalm krlgynsyvs qggdwgaiis dalarqapag
      241 llgihvnrve rsttlpadaa kalknggpap etmsadekkv fdeardflnn gfgyasilst
      301 rpetigygla dspvglaawl ldkiadwvft rgdaeqalgk daildnitly wltntgpssg
      361 riywenvkag akltparvpv avtvfpgevy rppkqwlska ypklvyynra lkgghfaawe
      421 epeifveeir agfksmrs
//
LOCUS       WP_457579250             299 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579250
VERSION     WP_457579250.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..299
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31541
     Region          5..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtptltisrl tkrfqsveal ksvslalepg rraallghng agkstmmkiv lglipfdsge
       61 vsvcgsapgs paartqvayl penvafhpal tgeeqlrhyl alrgenpkqa tellarvglg
      121 haarrrigty skgmrqrvgl aqtligrprl lvldeptsgl dpvsrrdfyd lldglaaegt
      181 aillsshvlt eveartdsil ilsggelvae gtladlrtsa alpvafsvrp apghapalaa
      241 tfpegveged gllrlrgsqs eklpllaria algsaiadld vippslediy shfsrrdgq
//
LOCUS       WP_457579251             291 aa            linear   BCT 27-JAN-2026
DEFINITION  glycine betaine ABC transporter substrate-binding protein [Ensifer
            adhaerens].
ACCESSION   WP_457579251
VERSION     WP_457579251.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..291
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31896
     Region          29..287
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(37,39,85,113,148,152..153,199)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mfktlatisl aasiaagtfg aaaaeekppv rigwaawsda efvtklaakl ikdelgqeve
       61 lvqtdiaply qgvgrgdlda mmmawlpeth adyfakvkgk vttlgtvydg arlgwvvpky
      121 ipedaiasid dlkkddvkek lkgriegidp gagltrlseq tvknyaldgy klqisseagm
      181 lttidramrk kdwfvataws phwmfgkyel ryiadpknal gkaervdvla rkdiekdnpe
      241 vsgllsrmkl pigdleaamf naqqtsyeka vdqyiadhpd qikawlakdg g
//
LOCUS       WP_457579253             217 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579253
VERSION     WP_457579253.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   3  (residues 1 to 217)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..217
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23589
     Region          1..>172
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 metrfletfl avvqhgslae asrrmgvtpa avaqriqale deiglpllar sgrrvkptea
       61 gvaileksrr vlaevrqlkg varddqafge lrlgaistvl tgllpnalrr vfdrtpgidi
      121 fllpgtsael ynsvaeekid aailvkppfp ipktlnwdli rserfvllap pgpfrdprrs
      181 ppsratvhsl rpkqlgwptg rylpsnpans psrvaga
//
LOCUS       WP_457579254             308 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Ensifer adhaerens].
ACCESSION   WP_457579254
VERSION     WP_457579254.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..308
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33523
     Region          8..299
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtfstqskgv yaiattpffe dgsidfnsid kltdfyeesg ctgvtilgim geapklepee
       61 sraivkrvvs rskipvivgv sapgfasmrs lardsmemga agvmiapppa lrtddqivny
      121 fagaveaigq dvpwvlqdyp ltltvvmapg viakiianhs sclmlkhedw pglekisklr
      181 amqkagelre fsilcgnggl fldfeperga dgamtgygfp dmltelmels aagkrdeahd
      241 lfdahlplir yeqqlgigla irkhvlkrrg viatdaqrkp aqmltptara evdyllarla
      301 rydrraaf
//
LOCUS       WP_457579256             307 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579256
VERSION     WP_457579256.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33895
     Region          6..296
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mhasilkyfv svarsgsirk aseelhvass avsrqikkle delgialfer lsnglrltva
       61 genvlrharv tlenfellrs dlgalqgkkt grvqmsclds laiqflpdmv nafhsihpgv
      121 sfhihtaghg nisslvaegd vdmgltfdla rpddtemlfr vpmplmafvg rehplarqrq
      181 vslaecaqyd lllqldtqpi rslieielsv fertgrpfvl snsqmmlkpf ilsgqgvaff
      241 tpigflaeir sgdlvaipls gsrlqnlhvg ilvqrrrqrt haaeaviefv gaelqrfsdq
      301 imeaihp
//
LOCUS       WP_457579258             541 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579258
VERSION     WP_457579258.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..541
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59453
     Region          4..541
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 marnpeydfi ivgagsagcv lanrlstdpa nrvllveagg kdrnplfrlp mlmgklfhsg
       61 iynwhyhtep ephlngrsly wprgkvlggt stingmiyvr gnrhdydrws qlglpgwsyd
      121 evlpafrrse thverkdafh sgdgeltvcr argnnplmdv fceagiqagy panddfnget
      181 qegfgrydft irkgkrwsts waflrpalgr knltvltgae ltrliiegdr argveylkdg
      241 vlgraraare vilssgvvns pkalllsgig padelralgi apvldlpgvg knlqdhvdcv
      301 mswecrepit lfsdlradkl ipavaqgmlf gegvtttfpy eagafirsnd gliapdiqlh
      361 fmpalektan lhfpnpfrmk qaveanhgft irvgpvnpvs rgeitlrsan atdkpkiqan
      421 ylrddfdvrt midairltrd ivgqkafdry rgkelapgpe alddatltrw lratamttfh
      481 pvgtakmgnd rmavvdarlk vrgieglrva dasimpviss gntnapaimi gekcaefiln
      541 a
//
LOCUS       WP_457579259             106 aa            linear   BCT 27-JAN-2026
DEFINITION  NIPSNAP family protein [Ensifer adhaerens].
ACCESSION   WP_457579259
VERSION     WP_457579259.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Fathi,E., Yarbro,J.M. and Homayouni,R.
  TITLE     NIPSNAP protein family emerges as a sensor of mitochondrial health
  JOURNAL   Bioessays 43 (6), e2100014 (2021)
   PUBMED   33852167
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Mukherjee,R. and Dikic,I.
  TITLE     NIPSNAP Beacons in Mitophagy
  JOURNAL   Dev Cell 49 (4), 503-505 (2019)
   PUBMED   31112696
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10546788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..106
                     /product="NIPSNAP family protein"
                     /GO_function="GO:0030674 - protein-macromolecule adaptor
                     activity [Evidence IEA]"
                     /GO_process="GO:0000423 - mitophagy [Evidence IEA]"
                     /calculated_mol_wt=12278
     Region          4..104
                     /region_name="NIPSNAP"
                     /note="pfam07978"
                     /db_xref="CDD:429767"
ORIGIN      
        1 milehrtytf kpgtvdkwmk kyeadglpvq krhlnrfvgl yvselgtlht tvlmwaydsl
       61 adrearrtam yadpdwqkfi sevwaldaiq kqevmimnpa sysppl
//
LOCUS       WP_457579260             526 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579260
VERSION     WP_457579260.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 526)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..526
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55366
     Region          4..504
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 mstsaqsale crnvtvkfgd vtalsevsas falgqihavv gqngagkttf arvaaglvqp
       61 tsgavnvmgq dirtgqvses raagvelvhq sfalppsftv aeamefgatg kggvfsrrgl
      121 lekwrahlag ldvqvdlnrr irdlpietqq gieiaralvt darvlildep tavlspagig
      181 mlfarvrrlk ergvtvilil hkirevlgia dtvtvlrggr kvegplpvae vsserlanli
      241 vgeavaksld rqdrdvlvgt kaptredadq qvhaagpail smksvstrpd sggialdgvd
      301 leirpgeivg iagvegngqk tlvraisala dleggtinlt ghdvtrqpla arrkiglrii
      361 pfernvegls ltsslwqnws arellqgsll kgirpvairq acdrslkaws vhynnsgqsa
      421 gslsggnaqk vilareidpd akliiaaqpt rgldigataf vwqalrqard rgaailliss
      481 dldelfdisd rvvvmlsgrl ngefhapfdi slvgaamtga aagasa
//
LOCUS       WP_457579261             345 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579261
VERSION     WP_457579261.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35637
     Region          5..344
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mkdslitvvr slifvtfali lcalvfqlag ynapvtlwav ldgaflrtga ieqslrwalp
       61 lfitavgvgi sfragffnig aqgqfyvgai saafaaeavr ggpaflvipt lllagmigga
      121 lwalwpgllr lrsgtdevit tlmgnfmagl llvyvtsgpl kdpsgsgqqa ssrpldpayr
      181 isdslglspt iiaiavavgi lmwllvnrta fgvlaslagr ngtmvewqga rlwklglssf
      241 lisgalagla gtiefmgpng riasgflpah gftailialv anlsvlgtam aavffgglas
      301 aalylpimag lpsaaidiin aaialfitar stvidkvlrl ggrkt
//
LOCUS       WP_457579262             502 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579262
VERSION     WP_457579262.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..502
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54782
     Region          4..440
                     /region_name="SsnA"
                     /note="Cytosine/adenosine deaminase or related
                     metal-dependent hydrolase [Nucleotide transport and
                     metabolism, General function prediction only]; COG0402"
                     /db_xref="CDD:440171"
ORIGIN      
        1 mreilirnat lvamdrthgt kpfaadilie gteirsigsg laagpdaqii dgrgklvmpg
       61 lvnahthsse tflrgryerm plelwllyay pllmndpige rllylrslll ameslrngvt
      121 tlcddffdpp rhdldrlatv frayddagir anvssaamnv htldalpfar evtplalqel
      181 ldfgppmsae ayadycraaf sslhgmsgrl rfmiapsapq rctpdlmaac mdlavenhvs
      241 fhthvletkt qavtglvgyn ksliaymhdl gllkrnttia hsvwvsdedi elmgragvsi
      301 ahnavsnlkl gdgiapirrl ldagvtvglg tdgvssndts rifdvmrvag lvhsaagpny
      361 erwlkadeil amatiggakt amleqvtgsl evgksadllv lnmrnypfqp lndiakhlvy
      421 sengssietv mvagrvvmqd grlttvdeqa vldeiselvp aylaehaele rrnaifeptm
      481 aqihrmatgm diplnryqgd mv
//
LOCUS       WP_457579264             469 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457579264
VERSION     WP_457579264.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..469
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50471
     Region          17..463
                     /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 mnrisparis rlignwrtlh gkvseqlsls igrlitarel pvggvlpser alatalavsr
       61 gtvvaaygsl rdagvldsrh gsghrivaaa apsgaahtrl ageiralpqd idmtsgalqp
      121 spilsemlta lkgadlasva aglgydasgl palrwaiary yadlglpthp dnilitsgaq
      181 qavwllanam vdasdavvve dpvyrgslea frrrnarivp iavtdegldi gqlekalknr
      241 prllylfpea hnptgrslnd qsrrelldli eryptflied gaqnelstia grtprpvagq
      301 anpelvatig tlsklfwggl rigwiraapp vvkrlasfka vndlgcsmfd qhlavgllen
      361 ireariyrhr eiaehleaae riiadhapgh whwsrpsggt amwihmpgid avalcqeaqr
      421 hrlflsagpg ysarenfgdv irlpfvrplq tmqfaietic slaggksag
//
LOCUS       WP_457579265             279 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579265
VERSION     WP_457579265.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..279
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28906
     Region          47..275
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgsfatrgeh aplavrqvap trshankryl vlggaggagk aaagllvaeg asvvigdvrg
       61 qaleeaiasl ghdskvlsgv vvdlsdassi aaaikeaear lgaidglvnc aaivrhvdpl
      121 etpwsdweri fsinvygafe aarlvakami akgikgaivn vaseagkkgh tqslaysask
      181 aaminftrvl sevlapqdin vncvcpggma tdmlrevava ygdlvkqapd evfkqlvssq
      241 lrrhidpvev artisfllsd daiiirgqai nadggdtpy
//
LOCUS       WP_457579266             339 aa            linear   BCT 27-JAN-2026
DEFINITION  BMP family ABC transporter substrate-binding protein [Ensifer
            adhaerens].
ACCESSION   WP_457579266
VERSION     WP_457579266.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 339)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (residues 1 to 339)
  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   8  (residues 1 to 339)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   9  (residues 1 to 339)
  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   10 (residues 1 to 339)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   11 (residues 1 to 339)
  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 10157009
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..339
                     /product="BMP 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:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35057
     Region          33..296
                     /region_name="PBP1_PrnA-like"
                     /note="periplasmic binding domain of basic membrane
                     lipoprotein, PnrA, in Treponema pallidum and its homologs
                     from other bacteria and Archaea; cd06354"
                     /db_xref="CDD:380577"
     Site            order(37..38,46,117,165,197,223,245,262)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380577"
ORIGIN      
        1 mttaskflhi clgsllalta ttasvraddt syvlvtpsri gvnkflglgk tgiekaaeaq
       61 gakarifegt dpstrrqnvq aaidmgapiv tvmgfefgdi iadlapenpe tkfviidtci
      121 peapenvyca vfreqeiayl agaeaaltsq sktvavigal dipflhrytd syelgakaan
      181 pdinvlptaw iggdnpfqdp vraqtqavlq lsngadriya vaagsnggvf kavaekpgam
      241 aigldvnqcg dapgaildst lkrvdvilpa tidgilkgta kpvesfglae gglelvamse
      301 dlaasgcmia kapdvigklt eiqakivsga itvpdpmaq
//
LOCUS       WP_457579267             556 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579267
VERSION     WP_457579267.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 556)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..556
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58944
     Region          1..499
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 mtllqmkgis krfgslvand eidlsvesge ihalmgenga gkstlmnily gllkpdagei
       61 ridgkamdfa splgaiaagv gmvhqtfrqf pdltvwenlv fqnepgqgpf vsaaaardvv
      121 rqlgekhgle inpdsrvrdl avgirqrlei lkalsrqaki lildeptavl tpqerdslfa
      181 amrhlasqgm alvlvthkip eviavtdeit vmrdgrvsgg lttrqtneae iiramvgrnv
      241 pptvadkvts taqpmlsvrn lsvrkggvav vndvtfdvrp geivgiagvs gngqpqlisa
      301 vtgleastge vviagrnvsg lsiadrravg isyvpedrhl tgtapaasia eniafgthrt
      361 aaassygflk kqairaqark lieqfkvkaa seevpigsls ggnmqkvvia reiehgspli
      421 vieeptrgvd vgaiefihkt liaerdkgra ilvvssdlte llalsdrilv mfegridasl
      481 sgkdmnedti grwmmggsgr gmtgvgletk srltaillsi avavvlggar rpfdrrqppl
      541 glsgnrprct rgagsg
//
LOCUS       WP_457579268             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579268
VERSION     WP_457579268.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30224
     Region          3..292
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mgrglgetls rsvpligmgl aaaiafragl inlggdgqml vgglaaalva lyvpapgavr
       61 avlaltaaic agglyawiaa vlqlglaipf litslllsyi argvtsylvr yplrdpstgm
      121 petyrvasaa rlpssifdlp vsfgmlimaa vaiavivndk rgvhgfewri tglnprfagy
      181 sgtnlprqtq rvaflsgala glvgallilg qqyrftdgal lapgytwsgl maavlamasp
      241 iatvvtaaff aalqvggfam eralglpavl twvlqaliil claarpvflk rr
//
LOCUS       WP_457579271             398 aa            linear   BCT 27-JAN-2026
DEFINITION  sialidase family protein [Ensifer adhaerens].
ACCESSION   WP_457579271
VERSION     WP_457579271.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..398
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016997 - alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43831
     Region          15..389
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 mdpeeitrrm ngrlqtvspe rmeallpspm iqnhaaflhl lsdgalacaw fggtlegksd
       61 isifasvlpk gatqwgppqr lsfdaahseq npvlftapdg glwlfhtsqp sgnqdecrir
      121 maevrrdasd plvlttsegr yldlprgcfi raplvvrgdg awllpifrcv qrpgqkwngs
      181 hdtaavgisl nqgetwqlee ldqsigcvhm spvslgegrl aaffrrrqad wvyrteslde
      241 grswsrpeas dipnnnssia alslkdgria micnpvsaad taerrtslyd elgeddnrpd
      301 adptggcvpi wgvrrapvsl clsqdggktf pvrlliedgp gtclsndstd grnkemsypw
      361 llegpdgamh laytyhrrai kyvrlapgwd hadqrrps
//
LOCUS       WP_457579272             539 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579272
VERSION     WP_457579272.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..539
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59189
     Region          1..523
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 madhllevrd lsvefhtavg vvkavrnisy hldrgetlai lgesgsgksv sssaimnlid
       61 mppgrissge illdgvdllt mpaqerrkvn grriamifqd plshlnpvyt vgwqirealt
      121 thgtdaakaa sealrlltrv gipdpersld kyphefsggq rqrvmiamal alrpdlliad
      181 epttaldvtv qaevlallee lqretgmavl iithdlgvva eiadrvvvme kgvlveagtv
      241 revyknpqhp ytkkliaaap gkgemhvpaa raehvlsvrd vrkrygsfea lkglsfdlmp
      301 getmavvges gsgkstlari llrldepdsg salwkgrdlf tmsptelykl rrdlqmvfqd
      361 ptqslnprmt vyqliseawv ihpdilpkak wrervadllv qvglgpehig ryphqfsggq
      421 rqriaiaral alepqliicd eavsaldvsv qaqvialldr lrqemgiafi fiahdlpvvr
      481 dfadhvmvmq kgnivelgtv revfdapqqd ytrallaagl dpdpdvqaah raarlqras
//
LOCUS       WP_457579273             491 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579273
VERSION     WP_457579273.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 491)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..491
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53567
     Region          23..487
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mgaytqpell atletldppd wssvsalahr iiddavghlg rvrerpvwqp lpeeiealyq
       61 apvpdrptpl edvyrqvkdt vlaypmgnih prfwswymgs gnftgalgdf laaiqgsnlg
      121 ggrhaaalvd qqvvgwlrdi igfpkaasgt lvsggsvanl vgltvarnam agidlreegv
      181 aalkepmrfy asdqvhschr kavetlglgn kalrriptds ryridlealr aaiaedrarg
      241 frpacvigta gtvnsgavdd ltalagiaae enlwfhvdgc igallsiape nawrvkgier
      301 adsvaldphk wlhapfevgc alvrdrakhr etfavspefl qgmprgiasg qwlhefgfqt
      361 srgfvalkvw malmehgiak farlidqnva qaafladlvr snpplelive peinivcfry
      421 apeglneerl ketnleimlr lqetgvaals dttirgkhcl raaicnhrtr pddlnllise
      481 vlrigseiaq s
//
LOCUS       WP_457579274             282 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579274
VERSION     WP_457579274.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..282
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30915
     Region          1..255
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklginllcl tdfveerhld nigrlrdlgy dgvevpvlsg kvnhyerlgr elnglglgrs
       61 ttsivptpea npvscdaevr arglshldwa ldcaialgae smggpfhapi gfftgrgase
      121 delkygadah halaeraaan gmhlslepln rfetyflntm eqarayvdrv ahpafkimyd
      181 tfhanveerr pesairmigq digvfhvsen drgipgrghi dfgamftvlk eigydgwltl
      241 eafgaglpai atatrvwrpl fpdfdtlfse satfirktwa aa
//
LOCUS       WP_457579275             504 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579275
VERSION     WP_457579275.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 504)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..504
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=53572
     Region          6..503
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mntkhpaiem rgiaksfpgv kalknvsfsa hcgevhalag engagkstlm kilsgiyrpd
       61 agavvvngee rhfthplaai ragiaviyqe fsllpertva qniflgrept rrglidhram
      121 ndearrvlal fgsahrieps tvvadldvas qqlveiakav sleakvivmd eptaalneae
      181 cevlyglvdt lkksgvaivy ithrmpeitr ladrvtvlkd gevavrfdhv pepeaivram
      241 vgrdlgdfya epaapqeigg vvlsvrnagn erlknvsfel rageivgfsg lqgagrvala
      301 qaifglspft kgeitlsgkp arftspreai ragvgllpgd rkaealvlmq svvdngmlts
      361 ralsglsgna natpfvsaea mekllreldv ragsfaqdik alsggnqqka ivarwlalap
      421 rllifieptr gidvnakagi yhlmrdlark gtaimmvssd lpevlgasdr vlvmrngelv
      481 aafsrgacea dvmlaatgee avaa
//
LOCUS       WP_457579278             187 aa            linear   BCT 27-JAN-2026
DEFINITION  dimethylarginine dimethylaminohydrolase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579278
VERSION     WP_457579278.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Shirai,H. and Mizuguchi,K.
  TITLE     Prediction of the structure and function of AstA and AstB, the
            first two enzymes of the arginine succinyltransferase pathway of
            arginine catabolism
  JOURNAL   FEBS Lett 555 (3), 505-510 (2003)
   PUBMED   14675764
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Leiper,J.M., Santa Maria,J., Chubb,A., MacAllister,R.J.,
            Charles,I.G., Whitley,G.S. and Vallance,P.
  TITLE     Identification of two human dimethylarginine
            dimethylaminohydrolases with distinct tissue distributions and
            homology with microbial arginine deiminases
  JOURNAL   Biochem J 343 Pt 1 (Pt 1), 209-214 (1999)
   PUBMED   10493931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..187
                     /product="dimethylarginine dimethylaminohydrolase family
                     protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016403 - dimethylargininase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20585
     Region          <2..181
                     /region_name="DdaH"
                     /note="N-Dimethylarginine dimethylaminohydrolase [Amino
                     acid transport and metabolism]; COG1834"
                     /db_xref="CDD:441439"
ORIGIN      
        1 mrhgeelavt rtlakqgmpv lrtlhgtama eggsfawlns rtavigrgir inddgisqia
       61 evlryqgvel lvvdlcgydi hidghflmid vdlaliwprg lsfvfleklr qlgirtiemn
      121 eddnpwivng laiapgrvim prglsdrtre alsrnnvtvl eidydkvqln gggihcstsp
      181 lirdsvd
//
LOCUS       WP_457579279             264 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579279
VERSION     WP_457579279.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29238
     Region          2..231
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mlwalpvill layvlpfagv tlwsvtrpel gvgnylrift gedfqaiflr tfwvcllsta
       61 itipiaylla yywvmgsarr srlieicifi pfwisvlvra fgwvvilrnn glasdvaaaf
      121 glsglstgrn vwsvitgmvh fmvpfailpm asvmrkidrr vllaalglgc rplgvfwriy
      181 lpmslpgvfs alamtfifsl gffvtpmilg ggrvvmtaes vfvqmfqtan wglgaalgvv
      241 llvvvfailw lsqrvmrieq lmsr
//
LOCUS       WP_457579280             392 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579280
VERSION     WP_457579280.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..392
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42698
     Region          36..390
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqraikhpdp rpraesnivp magcdpvqlp nsvaaevrsl rktynagtpq ahealkdvsl
       61 siranefftl lgpsgcgktt llrilggfem ltsgscrifg edvsrlppea rpvntvfqqy
      121 alfphmtvrr niafglemlg kpraevdrtv ermldlvhmr eyadrrpdtm sggqrqrval
      181 aralapqpkl llldeplsal dlklrqkmrl elkslqretg itfifvthdq eealamsdrv
      241 avisngllqq vgtpeeiyeq pqsrfvadfi gesnlieakv agtagseaal diegfglvha
      301 piaehvedgq evwlsirper lvlgvgqcgg qasatvadrt ylgnaveyhl ragghaltar
      361 sprgglrgrq dfapgdvvsl gfepgsikvl ls
//
LOCUS       WP_457579283             341 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Ensifer adhaerens].
ACCESSION   WP_457579283
VERSION     WP_457579283.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
REFERENCE   2  (residues 1 to 341)
  AUTHORS   McGraw,W.T., Potempa,J., Farley,D. and Travis,J.
  TITLE     Purification, characterization, and sequence analysis of a
            potential virulence factor from Porphyromonas gingivalis,
            peptidylarginine deiminase
  JOURNAL   Infect Immun 67 (7), 3248-3256 (1999)
   PUBMED   10377098
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..341
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0004668 - protein-arginine deiminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37637
     Region          14..340
                     /region_name="AguA"
                     /note="Agmatine/peptidylarginine deiminase [Amino acid
                     transport and metabolism]; COG2957"
                     /db_xref="CDD:442197"
ORIGIN      
        1 mknqtpreag frmpaeweph rrtwmmwpcr hevwddiaat rrdyaavaha irefepvtma
       61 arpedmaear aildpsidlv eadiddswar dagpcfltak dgrragarft fnawggkyhp
      121 fkgdaafsgv vlekagvagf vsnliaeggg vsvdgegtii ttetcfpnrn rnpgwsrddi
      181 erelldmlgg ekviwlpgnp iedetdghvd giavfvapgv vlmespgegg seeeeewnhy
      241 irlnleamqg qtdakgrpir ivtipeavda psdhpkfcrs yvnsylvngg vimpcygies
      301 dtvvrqmfrs lfpdrrvrev ridaiaiggg gihcitqqep l
//
LOCUS       WP_457579284             569 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Ensifer adhaerens].
ACCESSION   WP_457579284
VERSION     WP_457579284.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..569
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61462
     Region          29..563
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mapntrrtlq sltglllaas alcsgavgaa aetlvitdak vrtmnpaapl aeavaidddg
       61 vilavgdear vlekagadah vvklggrmll pgfqdahvhl ieagvnaslc efeafaslee
      121 tkdtvrdcik qsdnewvvgs gvsmtnllde tddpvgvlde ismdrpilil ddighgawan
      181 svaleaagyd kingnppggi ilrdqktgap ngivlenaqq klrnlafpdt penvkfayes
      241 mlptlktmae ngittvsdag gfwpqghlka wemaekndtl tlraanalyv ypdlpfdaqv
      301 eklaryysnd pnrllkfnqv kiyvdgileq rtgallapyn kgpgidhgfd sgflyfdeet
      361 ldryskvlse kgfklhyhvt gdrgarlald aiaqsdpepg phrlthiyll dkadygrfkd
      421 egvvadfqla psslsreyda firkfigdra dtmmpagsie ktgatvvmss dfdadelspl
      481 vkiqtalqrk kdgapdveta vkwmtinpak llnqddktgt iepgkfadlv vidkdifeip
      541 vkeigkaave atllqgepvy daeglfsgn
//
LOCUS       WP_457579287             198 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579287
VERSION     WP_457579287.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21480
     Region          6..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 magkreakke dlrsrliaag telireqglk nlrardiaer agaalgglyt vfddldglil
       61 hinsgtlkrl eaalnaavqp aadvqeafls lslaylrfal aernlwsalf ehrmpegapv
      121 pewhlaehgf ligliaapla qqfpeaaqed vavrartffa avhgvislsl egrfigitre
      181 vlereitala gllarrpn
//
LOCUS       WP_457579288             183 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579288
VERSION     WP_457579288.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19438
     Region          8..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkandkrrer gdraranilh hatqiasveg legltfgrva adagvargnv qvlfgdreal
       61 qlatiengva lyaetvvgpa malptaverl ialiegwytf veqrtlpggc lvhalsseyr
      121 trpgeirdrv ehhraearqr ivdlanaain agelqggidv gvlafeltsy qasanvaalm
      181 gga
//
LOCUS       WP_457579292             339 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457579292
VERSION     WP_457579292.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..339
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36012
     Region          62..314
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mdfvsvsvls gpssrriaat efrraaracr vglqrtnavk dlslepiata averevdatr
       61 ggtdamplqr ivaelglpse paavligsgq nsvayeldgr ilrlprhcga erdlvreaaa
      121 lravrpllpv pvpdlevrri dgqfvslhak ilgeplsdlt glrigaqrvl aadlaaflka
      181 lhslpidsve aepaeassse wngllaqcea vafpllspdv vtglrkrfsd flatcdalpq
      241 clihgdfgtg nilvdrgrls gvidfsgcgp gdpaydfasl aaglgdpfvd lvlahfspdt
      301 aardrmgfyr mtfplldily gvenrdpetv ragvhafaa
//
LOCUS       WP_457579295             623 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457579295
VERSION     WP_457579295.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..623
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=68187
     Region          3..623
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mstslshire iervasgaas prdepvvqsw lrclndykld ptiaqeayiv pgsklrehre
       61 qaeelirigr sgleglfnqv aeqnyvllls dargvtvdfm gdptfdnqlr kaglylgsew
      121 sesragtcav gacivsgqpv iihqddhfda shigltctaa pvfdtlgdlt avldisqlrs
      181 ptakasqqla lhlvsatarr ielanlmtrt rndwvlrlar spefldvdpd aaialdgsgr
      241 itgmthggfg alarsmnirg lqtrnflglp lsevfdidvd dlpnfmrgrp ngerllraks
      301 glvlfasaia pvvslrtpaa pearlpralr dlsqgdatme rvqtraakla trripiliqg
      361 etgsgkeyla raihdscgdn gnfvavncaa ipehliesel fgyapgaftg asqkgkrgli
      421 edadggtlfl deigdmpftl qsrllrvlse neiqpigalk arpislrvvs ashrdlaelv
      481 kqgrfredly yrlnaatlsl palrerqdls wlidqlrarv ekenhesyri dktaraalla
      541 hewpgnlrel snvlrvaaal senglidsec lpehlfseai hslpgeddal rqalrdcgdn
      601 vsalarklgv nrstihrrlk rln
//
LOCUS       WP_457579296             187 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Ensifer adhaerens].
ACCESSION   WP_457579296
VERSION     WP_457579296.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (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   4  (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 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..187
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20006
     Region          1..161
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 miriidfyff alkvaialll agmvvlvfgn vvlryafnqg itvseelsri ffvwltflga
       61 vvalrehghl gvdtlikrlp pvaakvavll ghvlmlyatw lmisgswtqt linlhvgapa
      121 tglsmgffyg aglafgvpaf lilladafai atgridvtta elvrdsedev aldpppaatl
      181 gplpvkr
//
LOCUS       WP_457579298             564 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor domain-containing diguanylate cyclase [Ensifer adhaerens].
ACCESSION   WP_457579298
VERSION     WP_457579298.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   5  (residues 1 to 564)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10542462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..564
                     /product="sensor domain-containing diguanylate cyclase"
                     /EC_number="2.7.7.65"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61494
     Region          169..373
                     /region_name="7TMR-DISM_7TM"
                     /note="7TM diverse intracellular signalling; pfam07695"
                     /db_xref="CDD:429600"
     Region          281..544
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mavfllllml thlgvgstha gdssnirnsc wasgrisenv itialaaerw scddrkfsid
       61 servllrfdl rpgesppryf lsrrsaleav hllaidqdga vrqasvsaaa lpssmaggyf
      121 kaplpvvtda trqvvvaidl pshrmtlera ylvpvdvavd siddmqllmf vaglagmlam
      181 llifnaafyr ilrepfvlwh saltlsllmt imtssslsvv ffdppamtls wmttllfgmt
      241 vasgamftys fiepglmhpa lrrllpycaa salflsafha afpfvarpiq staytaafap
      301 iliifilsvi dalrrgsraa kfqaagytpm iavglirlvt gvvpwfdsid atlafyagcl
      361 fealfttlgv adrfvtmkre rdrarieadl lerlsetdpl tgllnrraie gqfaqlradg
      421 fatlavidld hfksindvng havgdavlka vanafqtgpd vrayrlggee fvlllrgnda
      481 atlaerrrqa ipvivastvp glerpvtasm gvadtfgdeg feklyeradk llyeaksagr
      541 nrtrstikae tdleifvkeq afan
//
LOCUS       WP_457579302             359 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Ensifer adhaerens].
ACCESSION   WP_457579302
VERSION     WP_457579302.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..359
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38803
     Region          23..347
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maenfdpgal rqwwpkpakp rpivifgags ivgdahlpay rqagfpvagl ydpdrekaak
       61 lagawripaf ereedalava daifdlatpp aahaailakl pigaaaliqk pmgsdleaat
      121 ailelcrtrk lkaavnfqlr fapmmlalkd aiakgylgev vdfdawlala tpwglwpflk
      181 glprieiamh sihyldlvrg llgnplgvha ktighpnhev aqtrtaaild ygdrvrcvls
      241 vnhdhdfgrk fqacefrisg tsgaayvklg vnldypkgep delwirptga vewvsvpleg
      301 awfpdafanr manlqrfatg edheligsve dawqtmalve aayqssaapa taiaplpgr
//
LOCUS       WP_457579303             281 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579303
VERSION     WP_457579303.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..281
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29791
     Region          65..278
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkllryglpg qekpgildan gtlrdlsghv adfsgaaldp dklaeleald laglpavdgn
       61 qrlgpcvagt gkficiglny sdhaaetgat vpsepiifmk atsaivgpnd dliiprgsek
      121 tdwevelgvv igrkakyvte aealdyvagy ctvhdvsera fqierqgqwt kgkscdtfgp
      181 tgpwlvtkde vadpqnlpmw lkvngetmqn gssktmvygv ahlvsylsqf mslqpgdiis
      241 tgtppgvgmg mkpprylkag dvvelgiegl gsqkqsvrad d
//
LOCUS       WP_457579305             548 aa            linear   BCT 27-JAN-2026
DEFINITION  Na/Pi cotransporter family protein [Ensifer adhaerens].
ACCESSION   WP_457579305
VERSION     WP_457579305.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Tenenhouse,H.S.
  TITLE     Recent advances in epithelial sodium-coupled phosphate transport
  JOURNAL   Curr Opin Nephrol Hypertens 8 (4), 407-414 (1999)
   PUBMED   10491734
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Takeda,E., Taketani,Y., Morita,K. and Miyamoto,K.
  TITLE     Sodium-dependent phosphate co-transporters
  JOURNAL   Int J Biochem Cell Biol 31 (3-4), 377-381 (1999)
   PUBMED   10224663
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Werner,A., Dehmelt,L. and Nalbant,P.
  TITLE     Na+-dependent phosphate cotransporters: the NaPi protein families
  JOURNAL   J Exp Biol 201 (Pt 23), 3135-3142 (1998)
   PUBMED   9808829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..548
                     /product="Na/Pi cotransporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005436 - sodium:phosphate symporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0044341 - sodium-dependent phosphate
                     transport [Evidence IEA]"
                     /calculated_mol_wt=57613
     Region          1..539
                     /region_name="NptA"
                     /note="Na+/phosphate symporter [Inorganic ion transport
                     and metabolism]; COG1283"
                     /db_xref="CDD:440894"
ORIGIN      
        1 mstaivsinl fgavalllfg lgqvrdgmqr afgarlkagl aagtrdglrs ffsglvatia
       61 lqsstatall vasfverdli vprmaqivll ganvgtamta wivalglgwl spllllcgfv
      121 vgrgssstrk gsgaalvgig lmllslhlig gateplrtsa alsaffgmld nawpvalvis
      181 aglaalasss lavvvlilsl atsaslstgp lialvlganl ggavppvlat fkaaasarrv
      241 algnlivrav gclaalalag yisphidwpp vsrgnlpvdv hlafnlalal laaplarpls
      301 rltirllpde pkatdgplfl eqndlgtpva alagasrevl gvgdlverml veandalqqt
      361 dpsrlaaist legrvdrvqh eikvyvsrvg qseiaeeqrr hamdivdyai nlehigdiie
      421 kgllaelakk iarglafssd gheelsrlfa itidnlrmaq avfatrdnam arrlveaked
      481 vrrlerqsae rhlqrlrdgr aesietsslh ldmlrdlkri nahiatvahp ildqsgllid
      541 srirpaat
//
LOCUS       WP_457579306             616 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579306
VERSION     WP_457579306.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 616)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..616
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67056
     Region          30..609
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mallsetaka atlpgsamap tawqrwryrm kvasrepttl igvltallft ylivvpiisi
       61 vldavrvqfg herrlgkdfg eltlyyldra flspvsvdlf wrplfntlsv algaislsll
      121 igtvlawlis rtdmfgrrwf atalivpyml pawtfalawt tlfknrtvgg qpgwfeamgl
      181 tppdwvaygr fpiivilalh ytpfvillfg salrrfdsql edsarilgak ryqvamqiil
      241 plmrpallss mvlifakclg efgvpyvlgl pvkfevlsts lfrsiasrqt gvagvvaasi
      301 mligivtlmi darlvrearr fvtvgskgsm nrqsrlgkyr lpatgfaali fllsvglpll
      361 tlflstimkl paqftldnft ldywigrdlh tvalqtgvll spdlwaaakn tlvivglasl
      421 tsgilgllvg yvvirtpvkv lsvylrqvtf lpylvpgiaf aaaylslfav prgpmpalyg
      481 tvtilvlali adqmpyasra gisamtqlgk dpeeaaqisg agwfrrmmli vipiqkgslv
      541 tgvllpfisg ikglslfvil avpstdvltt yslrlvdyhy tqaanavvli iaaiaylgtl
      601 aaqkltktnl aeglgs
//
LOCUS       WP_457579309             632 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Ensifer adhaerens].
ACCESSION   WP_457579309
VERSION     WP_457579309.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=68539
     Region          1..632
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mpnahseavg prsgtqsflv lllgcigvvy gdigtsplya frealrpfln dgaqpdevig
       61 lislmvwtlt civtfkyvlf llradndgeg gtlsllallm kktgsfmpvl ffagligaal
      121 figdamitpa lsvmsalegm klvtpafsdy vlplaavimv alfavqskgt eavarffgpi
      181 tvvwflamaw gglihigddw tilqalnpin alwfithagw aglivlgavf ltvtgaealy
      241 adlghfgrkp istawfilvf palalnylgq galvlshpda vnnpfyllyp dwallpmvil
      301 atmatiiasq avitgafsla rqavhlgflp rllikftset ntgqiyvpav nallfvgvim
      361 lifsfgdses lataygisvt gamvvttvma fqflrsvwgy stvlaallla pllviesvfl
      421 lanlfkihdg gwvpvalalt imvvmwtwtr gsamlrekta rndipletfi rsieksthap
      481 qtvrgtaifl tsvgdktpav llhnikhnhv lhernviltv rtsehpyvaq edrvsmtels
      541 drftrlelcf gfmdepnvsk alslckkagf kfeimqtsfy lgrrtligdp nsglpgwqdk
      601 lyialaglgi dpssyfklpa nrvveigeqv ti
//
LOCUS       WP_457579312             151 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457579312
VERSION     WP_457579312.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..151
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16520
     Region          12..143
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrpsldsggd pvttafvggp ikredawrrm lsfighwhlr dfgffvveds ktgemagycg
       61 aqlpldklep elgwgiypqf qgrgyateam havldfaask lgwrtaisli tddnlasqav
      121 arklggaler hvdisgmryg vyrhvfgdss i
//
LOCUS       WP_457579314            1050 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Ensifer adhaerens].
ACCESSION   WP_457579314
VERSION     WP_457579314.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..1050
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111689
     Region          1..1020
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mplsefsirr piatvllsva lilagvfsyl ilpiaalprt dfpvinvsas lpgaspetms
       61 tsvaiplikq fatiagidti sttnalgsts isiefvlgrn idaaaadvqa aitrtlrllp
      121 qdmpappsyr kvnpadapvl llalksstvp lttldaiaqq visptlsvld gvaevsifgs
      181 qqyavriqmh pdalaargis vdqlrtavaa andnsplgta qtsdrqaaiv adtqrmnaas
      241 fadiivksvd grtvrlgdva tvidsvannq taswhdgsra iilaiqrqpd antvevvdrv
      301 qallpslrqs lpaaasietl sdrstsirga vhdvqftlil tvglvilvif afvrrlwatl
      361 ipalavpisi iatfaamypl gfsidnislm altlsvglvv ddaivmleni vrhmeedgid
      421 afsaaligsr eigftiiais lslvavfipv llmggvigri lnefaivvtv ailasafvsl
      481 tltpmlaarl partdreeka rwlqrldlaf ergfdgllra ydrllslcmk aralvfllfl
      541 ftvvitgyqi atipkgffpq edigqlqvtt qarqdisfaa msklqsnvea vfasspyvdh
      601 vastigsgga ssalnsgrlf velkpkserp pletvladlr rklaaipgiq afmspvqnls
      661 vgsrasasqy qlvlqsldqp lmnewaqklh damsadrtff tdvnsdlqin apqtrlvvdl
      721 dkaatlgvst selrttlygs fgteqistiy tagdsyevil eldpsmqwsa dkfdelrvgs
      781 angglvplga farvetvsgp ltinqlgqlp avtlsfnlpa kvalgdalae idrlkaeigm
      841 psevttrnyg ttqlfedaaa nqgllvlaai vtiylvlgil yeslihpltv lsglpsaisg
      901 allaiyfggf dlsiiaivgv lmligivkkn aimmidvalt lqragspaae aihkacvmrf
      961 rpimmtsvaa imstlpiaig sgasaelrqp lgvavvggll vsqlvtlfvt pviylymedf
     1021 mrvasrlvrr glqitrgerp tavddqpghg
//
LOCUS       WP_457579317             327 aa            linear   BCT 27-JAN-2026
DEFINITION  FecR family protein [Ensifer adhaerens].
ACCESSION   WP_457579317
VERSION     WP_457579317.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20752687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..327
                     /product="FecR family protein"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_function="GO:0016989 - sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34520
     Region          17..>46
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          85..323
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mksasattqc pardisdaal awvvrlhsge atsedqrayd awrgqsaehe aaaveaealw
       61 ddaahlrrdr qtglvypgrd tallsrrrll tgafgiavlg gglaasrpwl rilgsdyatt
      121 taetrsidlp dgsrvvlnar tamdvdfder arrvvlkegq affdvaadar pfqvasgeti
      181 vkalgtafdv danaadgslg iavtrhsvrv spmaggdvtg vtiaegervs vggdgaignp
      241 vvqdpaiala wqsgmyvaen rrlgdvvaal sryhggwivf shdrlkstlv savldlrtpd
      301 aslsalasgl pirvtrmtrf vtlisav
//
LOCUS       WP_457579319             432 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457579319
VERSION     WP_457579319.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 432)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..432
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47218
     Region          141..427
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlvlqlavll afglsfvtll vvadeggalv spapvetafr aikrsasgkl eladtaelar
       61 vrreqphfwf iarsdggeiv qsgdvpeiyr gmtvaldrmt ysdirddgpp snylavirrm
      121 tneegsftvf gqgtllsqps lilsfsrlfv apmlvllalv tifavprivn rairgisdla
      181 retdeinith rshrlaetav psevrplvrg insalhrldq sygqhqrfil daahelrtpv
      241 ailqarldll asgperdrli sdcerisala eqlldlqqle adarpftavd lvalcrnvva
      301 dlaplaideg ydlsfeqnte qsliqgdavs leravtnlvq naiehagnqg vivvrvepdg
      361 vievsddgpg ipeaerervf eafyrlkpre rgaglglnlv lqiaqrhkgr vsiltsqsgg
      421 acfrlafeng ri
//
LOCUS       WP_457579325             508 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579325
VERSION     WP_457579325.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..508
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55379
     Region          9..506
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mttehvdgap vvlsarrisk sfsgvqvlfs vdfelrqgei halmgengag kstlvkilsg
       61 feqptsgeil ldgkstklpa ngaaealgiv iihqefnlae hltvteslfl grevtrfgvl
      121 drkfmraetr rvldllgshv desamigsls iaekqmveia kaisrdarvv fmdeptavls
      181 reetnflfrl vrklrdkgts fvfvshklde vmeltdrvtv lrdgqwikts ptsildgeai
      241 aqlmvgrels slypaknepd vdedvvlrvd avstgyvrna sfevrrgevl gfsgmigsgr
      301 telmeaivgl rartagevlv rgepvpsgdv haankaglay mtkdrkakgl llnagmmanl
      361 tlqslgrhsr lgyldpgsee aalvkarrrf dirvrddriv agrmsggnqq klllakvmet
      421 dpsiiiidep trgidvgtkq qiyhfisala rdgrsiivvs sempeiiglc srvavmregh
      481 iagilegdei seqeimryaa glkkktaa
//
LOCUS       WP_457579326              99 aa            linear   BCT 27-JAN-2026
DEFINITION  PRC-barrel domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579326
VERSION     WP_457579326.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 99)
  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..99
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..99
                     /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=10315
     Region          19..76
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mdhtghvrla ateltpaile gatvygaddd kvgtvdhvhg vgtastvvid vggflgigak
       61 pvavpladld fmrdedgdvd avttwtkdql kempehyds
//
LOCUS       WP_457579327             120 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457579327
VERSION     WP_457579327.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..120
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13362
     Region          2..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkrlqqddcg fasalnaigg kwktlilwev nieprrfgel rrllpgisek vlaqqlreme
       61 adrlvrrevf paavqrveys vtefgktlne aitvlstwgk ehqarlaakg egcgadpgrn
//
LOCUS       WP_457579330             314 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579330
VERSION     WP_457579330.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..314
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33743
     Region          27..305
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttfavevle pagaagvagr ghafwarlar lawiapvlva livttlyptv fllalafsks
       61 tlgkpfrgfv gikhfatalq dpiflaaigr svayalatsl vqlalgflia llftsllkag
      121 rflmslvllp lmtppvmvgi awklifapag gllngtlity gfisepisfl ghptlawlai
      181 gaadlwqwtp fivilcfaal stvpdsvhea alvdgangwq rfwhitlplv aaplssiyll
      241 klilsfklfd liyiltfggp gfattsagfa iyrraieqfd vgraaaetmi yalviglvtl
      301 pvvrlhqhse rrel
//
LOCUS       WP_457579332             856 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579332
VERSION     WP_457579332.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 856)
  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 856)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 856)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..856
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=92782
     Region          1..90
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mrrllaylti asffstsafa dpailtanvn frvgpgtgfd amrvipqgee vdikecdaea
       61 swcavsyaga ngfvagkyln qsdatapawp rmfntekgat itlfqpqits wkdfkeleal
      121 vatelkpsad akpiygiigl saktvadeat envtltdvrt tqldfsaldr qqladlaldi
      181 gklvptdpiv vsqqrlaasl adfqrladip dikadpppif vsetpailvq tdgkpvtapv
      241 kgveglsfvv ntnwdlfkvd qaadyylrse knwlttktle sgwveaasvp dvfsklpeid
      301 nwkgvkaslp ptpfsdnqvp kvfysekpae llifegkpal epiagtgldw isntsssvff
      361 hrasktwytl vsgrwfssts legpwtfatp dlpddfvnlp ddasysavra sipgtsesam
      421 arlrasipkl arvstdgslk vdvhyngepk fepiegtsmf yavnaneqvi kvadkyfvlk
      481 dgiwfvgdtp tgpfavarav adeiytipss spvynatyvr iydtepdaiw ygytlgyfyt
      541 ylawdtvvwg sgwyyppywd yydddwpyyp ppisygfgas ynpaygtfgr ygyaygperg
      601 lvfgaaynpv tgtrfrggav agpggergfi saynprtgna mvarggqnvy gswgsvavkh
      661 ggefarisgg stgsagglrw rnsegdkgfi agskggdvya grdgsvyrrq dgqwqkhtpd
      721 gwqpvqrpdg enlrnaaqga asnrpqaaqr iqnraetrpa prrnqqvrqr apdhlsfdra
      781 grqfgnqnel srnygrlyqd sgrnfqsfdr grggysgggf qggnrggfhg gggrgggaaf
      841 rgggggrggg gggrgr
//
LOCUS       WP_457579333             405 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Ensifer adhaerens].
ACCESSION   WP_457579333
VERSION     WP_457579333.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..405
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43955
     Region          11..397
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msglakrqfd pdakgplvgt rvldlsrlva gnmlslqlad agadvikiep pagdplrdwk
       61 ddghslywkt ysrnkrsvvl nlrqeaamta lwalidtadv fienfrpgtl ermglspetl
      121 harnpnliiv risgfgqtgp yaqfpgfgti iegmsgfayr tgfpdrepvl pplaladmia
      181 gvygssatvt allardrgya kgqvidlsll epmfsvlgpe aaiyqttgki kervgsasnt
      241 aaprnvyrcr dgkyvalsgs tpqvarrife iigradmnqd prfatnserv knrdlvdeav
      301 ggwfarhdhd ealkimrdag atvgpiynia daasdphfae reiivdvedd efgrlpmhni
      361 vprlsqtpgv wrrpapalge htaevlaeag ldrgaietil qgkaa
//
LOCUS       WP_457579336             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579336
VERSION     WP_457579336.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..309
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34760
     Region          8..309
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mprsgnvpnv nrrsvtknvr qwwpyylmma pgliffvifh yfpiweakia feqlriippn
       61 iwvgikhfqt lfsspifwqv lintliistm kivfvfpvpi ivalllneir ggafrkfiqs
      121 aiylphflsw vviagvfiav lspsdgavnd iigffglqpv sfmtdtgsir wvlvfseiwr
      181 sagwdsllyl aaiiaidqel ydaaeidgan rwqkiryvti pgivptiatl filnagmfln
      241 adlnqvinfs ndvvrskidi idtyvyrigl qtgeyslata aglfkavlgm lmivaahlls
      301 krltgkgvw
//
LOCUS       WP_457579337             349 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457579337
VERSION     WP_457579337.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 349)
  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   2  (residues 1 to 349)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..349
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37283
     Region          6..335
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mkngprqrat iidvaeragv skstvarvla gsasisdear drvlkavaat gyernhlavg
       61 mrsgrsgmlg lvipditnpf waevargaqd raakddisll vfssdwdagt eathlralrr
      121 arvdgaiinp vadnfddldr fglpfvfigs saerfpdtls vgsdiaqavr lgmdilverg
      181 hpapalmlgp rsrlararfl ravhehciar didpdillve esdytveggr kamgrllagp
      241 wrgsravfva ndlmalgami avreaglrcp edisilgfdg ipagafswpg lttiekpgrq
      301 igiravecll dqiagrpehg riflpcrlve rgsladvsas vavraaagr
//
LOCUS       WP_457579339             122 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Ensifer adhaerens].
ACCESSION   WP_457579339
VERSION     WP_457579339.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..122
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12826
     Region          43..116
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mrgslattpk katdgipeac fdlgfhgvad fwppwcaaiv dgevaslaca arltdsgael
       61 glvtakafrg rgfgaaatag wsrlptlrsr tlfyrtdrdn asskrvasrl glrlrgaslr
      121 it
//
LOCUS       WP_457579351             410 aa            linear   BCT 27-JAN-2026
DEFINITION  benzoate/H(+) symporter BenE family transporter [Ensifer
            adhaerens].
ACCESSION   WP_457579351
VERSION     WP_457579351.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..410
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42573
     Region          7..396
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 msshvfpssl rfndlahpiv aglisvivny ggtfilvfqa akvaglspel taswvwsvsi
       61 gvgmtglwls wryrepiita wstpaaaflv talattpyae aigaymisal afvalglsgy
      121 fekvirlipp giaagllagi llqfgigafg gasvdpllvg lliiayvvlk rfsaryavvg
      181 ilvlgllfll aegrvdlsgl klefaapift mplfslnall svalplflit ltgqympgml
      241 vlrndgfkts anpivtttgf gslimapfgs hafniaaita aiaigkeahe dpsrrwiagi
      301 aagffyvlvg vfgvtlaavf mafpatfiat laglallgti ggslaaatad pacreaalit
      361 flasaanikl lgiggafwgl vigllayivl ngrlpqrrgs klplnegtak
//
LOCUS       WP_457579357             427 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579357
VERSION     WP_457579357.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..427
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45774
     Region          11..376
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 minrrhflrn aaffgagatl atmpafrafa edsmrlywwg tpsraertlg vaklfeaahs
       61 gakivgevgg sdywaklttm iaggnapdif qlepsrfady srrstnlpln dylgkvirtd
      121 klvpgvldlg tvdgkvtgmp lslnafamiy dadavtkagl ippsakttwd dfakfsidlt
      181 kaigkknvwa vgnasrytya feaflhqrgk klyteagklg yeasdaadwf gywesltkng
      241 gcvsaeiqal dkvlvdsnpl atgnaaiaia fsnqlpafqk iskstldits lpvssadgps
      301 glfyrpglhw siastaknpe laaqfidffv ndleagkilq vergvpvntd vqtavlpsid
      361 atakktvdyv ngiadrvgty ppavplgage ldervfrpla dkvafgqltp aeagnelvss
      421 adrilka
//
LOCUS       WP_457579363             504 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457579363
VERSION     WP_457579363.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 504)
  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 504)
  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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..504
                     /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=56223
     Region          29..500
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 msqrepaddt pwikkadele alfqltdgly raesetdafd atfdaieral gcsqasillf
       61 drhgvmrfva srglsedyrr avdghspwkp gdrdpipifv sdielsdepq alknairgeg
      121 irslafipvt vdgivvgkfm tyrdvahvyt adeatlclti arqlgfsier kqseeahqra
      181 eeglrrtner lrvildsase yaiitldadg riaswnsgae rllgyldsev lglsgsiffs
      241 pedraleipq qemrtaaetg raanerwhyr kdgsrfwgsg vmlrveesgp drylkifrdr
      301 teerraekrq kllvgelnhr vkntlatvns laeqtlksse tpeafaqafn trllvlakah
      361 dlltreawqa vnlsdiaqtv ltawiedgrv siqgaairid pkkalalsma fnelltnaik
      421 hgslsnqvgr valswqcqev csvlweergg pptsepdrqg fglrvlnrgl ahelgypvel
      481 rfepdglrct msmdfsskqp sgaq
//
LOCUS       WP_457579364             158 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Ensifer adhaerens].
ACCESSION   WP_457579364
VERSION     WP_457579364.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..158
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=17737
     Region          30..158
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mslflhqvis elpdeqqkmi rkarnrdall egrrilvved dirnvyaltn ileprgaive
       61 iarngreale vlekassgpg rpielvlmdv mmpvmdglva taeirrnptw kklpiialta
      121 kampddqerc ieagandyma kpldvdrlls lvrvwmpk
//
LOCUS       WP_457579367             406 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579367
VERSION     WP_457579367.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..406
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44555
     Region          35..406
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mekitrkrkl rsnrplwsnt rhikvvaqsr isvdkvdvli vgagiggalm awslakrdmk
       61 ilvvdrrwpv qgstlastam iqheidvplh rlttmigqdk arrawqrsar avetlitlid
      121 slgidcgfeq kkslylsgna ygaralrlei darqaagisa rflksaclre efglnrtaai
      181 esdisaaanp aqltaglwrk aqrdgvslig dteitdvrsv egwnaaatst geiilakhvv
      241 fctgyefldv vahqghrmvs twalatkphh prpdwlknyv vweasdpyly frstkdgrli
      301 vggedeesat afadpiklra ksknlrakls alleipigep dylwaapfgi tsdglplign
      361 vpglenvyav mgyggngity sqiaaeivss eilgyrdpds elfafr
//
LOCUS       WP_457579370             344 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA topoisomerase IB [Ensifer adhaerens].
ACCESSION   WP_457579370
VERSION     WP_457579370.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Borde,C., Bruno,L. and Espeli,O.
  TITLE     Untangling bacterial DNA topoisomerases functions
  JOURNAL   Biochem Soc Trans 52 (6), 2321-2331 (2024)
   PUBMED   39508659
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Bush,N.G., Evans-Roberts,K. and Maxwell,A.
  TITLE     DNA Topoisomerases
  JOURNAL   EcoSal Plus 6 (2) (2015)
   PUBMED   26435256
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Yang,W.
  TITLE     Topoisomerases and site-specific recombinases: similarities in
            structure and mechanism
  JOURNAL   Crit Rev Biochem Mol Biol 45 (6), 520-534 (2010)
   PUBMED   21087076
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Patel,A., Yakovleva,L., Shuman,S. and Mondragon,A.
  TITLE     Crystal structure of a bacterial topoisomerase IB in complex with
            DNA reveals a secondary DNA binding site
  JOURNAL   Structure 18 (6), 725-733 (2010)
   PUBMED   20541510
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Bugreev,D.V. and Nevinskii,G.A.
  TITLE     [The structure and mechanism of the action of type-IB DNA
            topoisomerases]
  JOURNAL   Bioorg Khim 36 (3), 293-311 (2010)
   PUBMED   20644584
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Forterre,P., Gribaldo,S., Gadelle,D. and Serre,M.C.
  TITLE     Origin and evolution of DNA topoisomerases
  JOURNAL   Biochimie 89 (4), 427-446 (2007)
   PUBMED   17293019
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Patel,A., Shuman,S. and Mondragon,A.
  TITLE     Crystal structure of a bacterial type IB DNA topoisomerase reveals
            a preassembled active site in the absence of DNA
  JOURNAL   J Biol Chem 281 (9), 6030-6037 (2006)
   PUBMED   16368685
REFERENCE   8  (residues 1 to 344)
  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   9  (residues 1 to 344)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   10 (residues 1 to 344)
  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 11466439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..344
                     /product="DNA topoisomerase IB"
                     /EC_number="5.6.2.1"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003917 - DNA topoisomerase type I
                     (single strand cut, ATP-independent) activity [Evidence
                     IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=38455
     Region          13..342
                     /region_name="Top1"
                     /note="DNA topoisomerase IB [Replication, recombination
                     and repair]; COG3569"
                     /db_xref="CDD:442790"
ORIGIN      
        1 msrrespqvg dgadliyvsd tepgytrfrs ssgfvyrrpn geqlkdsrvl ariqalglpp
       61 ayenvwicmq pnghlqatgy dargrkqyry hqawqemrsn akysqlpafa ktlprlrrri
      121 rkhmegpvdd pftvlaalaa lldhaplrig nstyvkengs ygastllkrh lkitddsiel
      181 sfkgkggqri rrrlrnprlq rllegiaelp grqlfvsvgq dgkpepiesg rfnrylaeis
      241 gapisaktfr twagsvaays aarqafaqgr rptikemcna aaealhntpa vcrksyvhpa
      301 vlalaqaeqk iprvrpnaka vpglrademq flrflnwlar haqg
//
LOCUS       WP_457579373             141 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579373
VERSION     WP_457579373.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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 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   4  (residues 1 to 141)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..141
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15238
     Region          17..>137
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mndqttlefl asqmsgdsge plyrrleeai kqaisastlr rgsvipserd lseglsisrv
       61 tvrkaieglv adglldrrqg aktvvssrve kslatmtsfs edmrsrglep gctwisreis
      121 rpspaemmal gipageknrt p
//
LOCUS       WP_457579374             105 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579374
VERSION     WP_457579374.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 105)
  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 105)
  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 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..105
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=11656
     Region          <2..105
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mrtandtpia ietaslparf vpdpdaigas lyeylaahga lpvralqrmq akpasdeerr
       61 llatpedtsl lvmerrcfla dgqiveftqt kyrgdvydfv ielmr
//
LOCUS       WP_457579376             326 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579376
VERSION     WP_457579376.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..326
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36630
     Region          3..314
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlilvtgatg kvgqhlistl ldrprfskar iralchnrvl npserleiir gsiadravad
       61 aaiagathiv hlatcketpa dvmdvtvkgl fwlleafrms ptarqfilig gdaavghffy
      121 rhegpitevt phraypgsya lskvleevmv eqysvqygmn vcclrapwim ekddfrhsls
      181 fgddvfggpd wktyfpphea rrhakagtvp llrdadggpl krnfvhvsdl vsailstidn
      241 phaerqrfni amdrpvdyge vasylertrg lpsvdvpshf hsnwldnska kflldwqpey
      301 dleklidqaf qyerppsdpr ivwypg
//
LOCUS       WP_457579377             260 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579377
VERSION     WP_457579377.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..260
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29048
     Region          28..254
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 maeqrpekrs agsgtaeaar atrrldaprm sgpsvhmsla ediglrivrg dyppgtilpn
       61 eaqwteifnv srtavreaik ilmakgllas rpkigswvep kerwnlldrd vlswyahspd
      121 riqflktvqe frhiiepeat alaairrsee qmaeitealr dmgqaatlqa rtqadtrfhl
      181 ailrasgndl liplgtlies alnhlfllvt rndstlvhal rlhenieksi rlqrpnaarn
      241 avrrllantd aliahsernm
//
LOCUS       WP_457579378             357 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579378
VERSION     WP_457579378.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38539
     Region          3..355
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mnaqielrnv nkyygayhal kdielsirkg sftalvgpsg cgkstllrsl aglesissgt
       61 lkiagevmna vpprkrdvam vfqsyalyph mtveenltys lrirgvaeae rkkaahevaa
      121 vtglthllar yprelsggqr qrvamsraii rhpkaflfde plsnldaalr vhmrkeiral
      181 hdrlgatsvy vthdqveamt madhvvimrd gvieqqgspl elydrpankf vagfigspam
      241 nflpavggpd grsiildvgt kqtialnrtv qpgqalsvgl rpehielaaa degilsapva
      301 miestgatcf ltmattpels vvfngrsvar agdrvglsfa pgsmhlfdad tqrrlad
//
LOCUS       WP_457579379             421 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579379
VERSION     WP_457579379.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..421
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45042
     Region          33..420
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrmtvkiaal asvaygalal ataahaaelr mawwggesrh vatqkaiaac gekyghtvkg
       61 eftgfdgyle klttqmagkt eadivqvnwp wlplfskngd gfadlrtlqa idlsnwsead
      121 laagsmngvl qglsvsttgr vfffnattfe kagvpipktw eeffattati keklgkdyyt
      181 fnavketaql lttlavvqkt gkdlvdpetn rvawtpeela egisflgklv etgairsqke
      241 eaadgnvnlf ekpswaegkv agsyewdsty skyadplkdg qvltpvpmlk ladavtdgvy
      301 rkpsmvfsis knskdpaaaa qivncllnep egidalgtsr glpaskaaat rlggkgepev
      361 raanaivlaa ggptvspfne hpeiraafid tleeyaygql dakeaaeqii dtvndvlakf
      421 d
//
LOCUS       WP_457579380             364 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579380
VERSION     WP_457579380.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39461
     Region          1..362
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 makvqlknle kvygnafkav hginldiedg efmvfvgpsg caksttlrmv agleeisgge
       61 vvigdqrvnd lppgkrsiam vfqnyalyph mkvrgnlafg lkiagkpkae idaaiahvak
      121 ileieplldr lpkqlsggqa qrvalgrali kkpgvflfde plsnldaklr atmrvritdl
      181 hrqlkaegls stviyvthdq teamtmgdri cvmqaghimq vaapkelynr panlfvagfi
      241 gspemnlvda elvdghlsig tqrlplgsnl qarlsgrpae avlgmrpqhl slatdgpaft
      301 akltnaefmg hevylhadle grklvsvvga aefealgrsd lirlrpdprk lhvfdktdgr
      361 nvsl
//
LOCUS       WP_457579381             378 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Ensifer adhaerens].
ACCESSION   WP_457579381
VERSION     WP_457579381.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..378
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41543
     Region          2..364
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(164,166,194,220,246,269,296,329)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mkivavrthl lehrlavpfe sasirfdrra hvlveiecdd gtigwgeclg parpnaavva
       61 aytpwligqd prqteklwai lynalrdqgq rglaitalsg idialwdikg khyrasvsml
      121 lggrwresvr ayatgsfkrd gvdrvsdnal emaerraqgf hackikigfg ieedlrvira
      181 vreaigdemw lmidanhgyt vteairlgka aadydidwfe epvvpeqlsa yravragqpi
      241 pvaggetwhg rygmwpaies ravdilqpdl cgcggfsema kitslatlhg vrivphvwgt
      301 gvhiaaalqf maamtpdpvr vnpiepilef drtenpfrqa vlkapieavd gvvaipdapg
      361 lgieidrdal arfkmpet
//
LOCUS       WP_457579383             417 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Ensifer
            adhaerens].
ACCESSION   WP_457579383
VERSION     WP_457579383.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..417
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46565
     Region          19..415
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
     Region          173..412
                     /region_name="RHO_alpha_C_GbcA-like"
                     /note="C-terminal catalytic domain of GbcA (glycine
                     betaine catabolism A) from Pseudomonas aeruginosa PAO1 and
                     related aromatic ring hydroxylating dioxygenases; cd08884"
                     /db_xref="CDD:176893"
     Site            order(191..192,196,199..200,203,205..206,210,336..337,
                     374..376,378..382,393..396,401,404,408)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,317,319,326,
                     328,358,361..362,368..369,372)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,317,319,326,
                     328,358,361..362,368..369)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176893"
     Site            order(206,211,372)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176893"
ORIGIN      
        1 mlqtfsspis slldaraegh slpaglytre dvfeadlevf frrhwicigl ecdvpepgda
       61 tvvdigktsl illrdddggi rvihnvcrhr garlldpgkt ivsklvcpyh twtyelsgel
      121 syaphmgksf dkecrslkpv ifksvgglvy vclsndpped ierlvgvmae rlapydiana
      181 kvayesdvie qgnwkltien nrecyhcsan hpelcvsfvd ldfgfdpdal spedraqaee
      241 hfslyeertr rweadgypsa aveqlvdctt nfrtqrliis gagesqtpda taasakllgt
      301 msrkdlgdmh lwghnswnhf mgdhavvsiv iplsadktlv rtkwlvhkda vegvdyelek
      361 ltnvwiatte qdaelvarsh agvedpayvp gpyspfsetn ldkfaswyid rmrahgy
//
LOCUS       WP_457579386             313 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Ensifer adhaerens].
ACCESSION   WP_457579386
VERSION     WP_457579386.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..313
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31585
     Region          3..312
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 maillladhd snhlsdqtak alsaaskias gteadvhvlv agagakvaae qaaklagvak
       61 vlvvddasla nnlaeplaal ivslagnydt ivsaatsvgk nvmprvaall dvsqvseiie
      121 vvssdtfkrp iyagnaiqtv qtteakrvit vrtasfasaa eggsaaiesv saaanpgvss
      181 fvadalsssd rpeltsakii isggralgss ekfrqvilpv adklgaavga sraavdagya
      241 pndwqvgqtg kvvapdlyia cgisgaiqhl agmkdskviv ainkdeeapi fqvadyglva
      301 dlfdalpelq kas
//
LOCUS       WP_457579387             254 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Ensifer adhaerens].
ACCESSION   WP_457579387
VERSION     WP_457579387.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..254
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27043
     Region          1..253
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvtvkrv vdynvkirvk adgsgvelan vkmsmnpfde isveealrlk eagkaeevvv
       61 vsvgpakaee tlrtalamga drailveted qveplavaki vkgvaeaeqp gliivgkqai
      121 dddsnqtgqm lsallgwaqg tfaskveigd gkapectarv trevdgglqt idiklpavvt
      181 tdlrlnepry aslpnimkak kkpldrhtpa dfgvdtaarl kvlkteepsg rkagikvksv
      241 aelveklkte agvl
//
LOCUS       WP_457579393             464 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY family carbohydrate kinase [Ensifer adhaerens].
ACCESSION   WP_457579393
VERSION     WP_457579393.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..464
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49111
     Region          3..462
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mrvaaidqgt tstrclvied gggwevagtr rhaqhhpapg wvehdpeell rniqsvlasa
       61 gavdaigisn qgesclawdg etgkplspvi vwqdartatd lsalppaaea rskavcglpl
      121 dpyfsaskla wlvkhvpavn aaleasrlrl gttdaffldr lcgtfrtela tasrtglldl
      181 stgnwseemc slhgvprqcl peiepvdagf gtidgtpvkv sivdqqaalf ghncrepgdc
      241 kitfgtgafl laiagtgrpp esdllptiaw qrqgetptfa leggvydags alewarnigl
      301 fsameelgsf egpsalargi vfvpalsgla apywdrqaap lfigmdhatd rrdlvravle
      361 giamltvgli eaaakvgelg ssisidggls qsayfaqfla saskrsitva pmheltalgl
      421 aelcgvdvng arsraitfhp ddtvnaddhl rfaraierar awrq
//
LOCUS       WP_457579406             626 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579406
VERSION     WP_457579406.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..626
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68370
     Region          214..608
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 msraehiasl adafpvvraw lehgpvaetk pprtaacela difrldafgr nilllcayva
       61 lepdgrdiva rllddpltsa ptlslaltrl pgahwkglsa eaplrraglv riegsgslvd
      121 arlrladtvl lrlvgapsld agasallrri prplslapnr atlareigsr lslpdtpvlh
      181 ltggdpegkl cafaeasagi naityalnsq llpqtavelv dfaagltrdm mlcagrlvlm
      241 hddmgetrta qlfaetyggp laiasvepmr vghrlalrle mprlkaseql avwhsvlsdd
      301 dtdlipalpr laatfcvape aahavaaems lernrdpkhl atcaweacrr aarprmddla
      361 hrvaspatwd dlilpprqkd vlesiiaqvr nrtqvydewg fgvrlqhkgl gvsalfsgps
      421 gagksmagev ignaldldvy rvdlsamvsk wvgeteknlr rvfdaaedgg vilqfdeada
      481 lfgrrsevkd shdrhaniev syllqrleay rglcilttnm rdniddaflr rlrfivdfrf
      541 pnlaerraiw mrifpdeqpr eqldydklaq lnlaggsirn ialgaaflaa drgcavsmae
      601 ilqaaqleyd kvgrpmtdae ragwlq
//
LOCUS       WP_457579407             474 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail sheath family protein [Ensifer adhaerens].
ACCESSION   WP_457579407
VERSION     WP_457579407.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Bock,D., Medeiros,J.M., Tsao,H.F., Penz,T., Weiss,G.L.,
            Aistleitner,K., Horn,M. and Pilhofer,M.
  TITLE     In situ architecture, function, and evolution of a contractile
            injection system
  JOURNAL   Science 357 (6352), 713-717 (2017)
   PUBMED   28818949
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Ge,P., Scholl,D., Leiman,P.G., Yu,X., Miller,J.F. and Zhou,Z.H.
  TITLE     Atomic structures of a bactericidal contractile nanotube in its
            pre- and postcontraction states
  JOURNAL   Nat Struct Mol Biol 22 (5), 377-382 (2015)
   PUBMED   25822993
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..474
                     /product="phage tail sheath family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=50684
     Region          182..469
                     /region_name="COG3497"
                     /note="Phage tail sheath protein FI [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442720"
ORIGIN      
        1 mgefnrrfgg lwsdsnvsya vddffanggg qclivrlfeq dggdgyaglt vgtlilraks
       61 pgawgnslsg kishpdvadp egaaaaakky gltvndifdl eivdtatdtr evlrtlsmrs
      121 dagqrrfdri laaqsnlvea ppaptfsnsr padaatgtat ggddgttlad atyqgdpalk
      181 tgmqalrkad ifnllcippd treatlpkav retaaalcae rralyivdpp newdanpdta
      241 attaknaqld atdqvlpltn arnaalyfpr llkrdplrgg qidafapcga vagvisrtdv
      301 nrgvfkapag laatlsntqg ltvkltdqen gllnpigvnc lrsfqnigrv vwgartlags
      361 dvlsddykyv svrrlalfie eslfrgtqwv vfegndeplw aqirlsvgsf mqrlfrqgaf
      421 qgaspkeayf vkcdastttq ddinrgivni vvgfaplqpa efviisiqqi rsas
//
LOCUS       WP_457579410             351 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579410
VERSION     WP_457579410.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..351
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38050
     Region          30..300
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(37,175,234,260,262)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 midqrltktt alallafvmq qnsasaetkt lyigmnggnf eraytehvlp pfekandvkv
       61 vvvpgtsadi lakataakdn pqmhvmlldd gvmvraiggg lcqkiaadpv ldqiqmaarl
      121 kddmaigvdm gmtglaynkk lfdekgwpap tswmdmadpk fenavvfqsa sassfglhaf
      181 lmfnriqggd etnvepgfdk fsdtigknvi efipssakis emvqtgeaai fpltptavnn
      241 lkdkgipvey aqpkegsvvl avtecviann sepelsqkla hyllspeaqs laldhgniip
      301 snvnakagtd aanaklstfk anmetakvld wdainqnrqe wnkrwnrmie r
//
LOCUS       WP_457579411             380 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579411
VERSION     WP_457579411.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..380
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39970
     Region          5..368
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mswrisvdva iiggglvgss aalamrkagl svalidrgyc gaqasgvnyg gvrrqgrape
       61 qlplsqrahg iwpqlkamvg idaeymrsgh lklartekdf akleayaetv rdyglglelv
      121 agsalahrfp wlsaqavgas lcpddghanp rlvapafara aeragamvle qtpvrdvaat
      181 gngfeilagd gieircqqlv nsagawsdrf aanfnepvpl triypsmvvt eplplrlpvs
      241 mgeqggsfyg rqvargnyvm gggrglplgd pdysrpsvta assvmqrait lfphlveaqv
      301 irfwsgteae mpdgnpvigp settsglfha fgfcgagfqt apavgevlae lvtdgrsttp
      361 idafsigrfr kvavetaasl
//
LOCUS       WP_457579414             324 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579414
VERSION     WP_457579414.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..324
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35704
     Region          105..322
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mlypdtvese ilvhkprfva smfaavliaf tafgltgttm gelmrpvige plesgfygrf
       61 atafvvavlf clnivligfa slrvqivvvw lellalflaf fqtfdlslpf ieeklpflit
      121 qglvttvyvs aisiviasai ailgavakls tngfayaias fytsffrglp llmqvyliyl
      181 glpqlgfiid avpagilals lcygaymtei frsgiqsidr gqweasrsig fgfgltmrkv
      241 ilpqalpvii pptgnqfism lkdsslvsvi gvwelmflar tlgqktfqhm emlisaamly
      301 wtmsivleli qsrierhyar skvr
//
LOCUS       WP_457579417             358 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579417
VERSION     WP_457579417.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..358
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40397
     Region          1..315
                     /region_name="Bac_luciferase"
                     /note="Luciferase-like monooxygenase; pfam00296"
                     /db_xref="CDD:425589"
ORIGIN      
        1 mkfavsltme rfspdipmeq vksnllqlar ladeggfetl wtaehhtlec tispnpfqtl
       61 vwlaqhtdri rlgtstlvap ywnpirlage salcdhltng rlefgiargs yqyefdrmag
      121 gipqqegvay mkemvpavkk lwsgdyaheg qywkfpvtaa vpkplqqphp piwvaardpg
      181 tfdwaianga silstplsap eaeihvlsek frkavadhpe vprprfmmqr rtcvydrpdg
      241 weravkhsmd ygrafenlmq nigtvhngfp eavpyeavkg kdnynpdnir knlmfgtpde
      301 aiekllvyea agvdqyclgl tfnlpfelqk rtlelfvsei mpffaareke qkriavga
//
LOCUS       WP_457579421             215 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579421
VERSION     WP_457579421.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..215
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23550
     Region          9..177
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mkaatrdlkv lavcigkpee rpgkkmktgi nkhptgetvf vgfegladda vcngkyhggp
       61 eqavyvegnl trlwwqraln kpinhglfge nlciagldnq ivsvgdrlli gdlvmevtap
      121 rmpcrvladr mgdhgfpkly kkvarpgfyc rvihpgyvta galvryvpya gervsmtema
      181 khhgkrgspe lialyqsvpv haklraflsn glikf
//
LOCUS       WP_457579423             360 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase [Ensifer adhaerens].
ACCESSION   WP_457579423
VERSION     WP_457579423.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..360
                     /product="fatty acid desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40437
     Region          38..302
                     /region_name="Delta12-FADS-like"
                     /note="The Delta12 Fatty Acid Desaturase
                     (Delta12-FADS)-like CD includes the integral-membrane
                     enzymes, delta-12 acyl-lipid desaturases, oleate
                     12-hydroxylases, omega3 and omega6 fatty acid desaturases,
                     and other related proteins, found in a wide range of...;
                     cd03507"
                     /db_xref="CDD:239584"
     Site            order(88,92,124,127..128,288,291..292)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:239584"
ORIGIN      
        1 mkntrvspls shgaaatvdr ekawlkilst yrqphigrst feltatlvpf vllwagawac
       61 lhfgywlgmv livpvaagfl lrlfmlqhdc ghgsffgrrs lddwtgrvis vltltpydyw
      121 rrahavhhas agnldergvg dittltvaey daltpggrvr yrfyrhplvm fgigpawlfl
      181 fkqrlpfgmm rsgalpwvst matnvaiaal sgiliwavgv apfllihlpi vllagaagvw
      241 lfyvqhqfed thwsrppewt fqyaamhgas hydlpqplrw itgnigmhhl hhlssrvpfy
      301 rlpevirdhp elgdmgriti rqslglvklv lwdeashrli sfreadaret varsalptpa
//
LOCUS       WP_457579426             308 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579426
VERSION     WP_457579426.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..308
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33476
     Region          54..283
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mhqsqskpsp alslsdlpap dvvirrlkhp grwisgglvi lllsvigraf avgqiqwtvv
       61 gefltagvii tgfgwtllis acalvlgvll gfafgimrls enpilrfaaw lyvwifrgtp
      121 vllqlliwfn ialifpklyi pglidarmvd vvtpfvaavl glgvnegsyl tevvrggigs
      181 vdkgqkesah tlgmtpgqtm rriilpqtlr lilpvlgnsa igmlkfssla atiamgemln
      241 aaqriyfing aviellfvca vwylagttvl sigqyylerh fgrdaatttt errwfkawar
      301 rpavtgea
//
LOCUS       WP_457579428             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579428
VERSION     WP_457579428.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21919
     Region          13..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnsernshrs vgrprefdmt qaldaairif sergyhgtsi aelkaemglt agslykafqd
       61 krdvfvaayd rykqvradll eqalssastg rekvarvvsf yamsacgetg rrgclaigaa
      121 velvlsdaei aakvaghnrk lvtrlegfir dgqldgsirh dadpastala lfsylqgvri
      181 agktgelenq llpsgeailr ild
//
LOCUS       WP_457579429             549 aa            linear   BCT 27-JAN-2026
DEFINITION  caspase family protein [Ensifer adhaerens].
ACCESSION   WP_457579429
VERSION     WP_457579429.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 549)
  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 549)
  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 549)
  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 549)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 549)
  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..549
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..549
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57869
     Region          16..250
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mnslraavll llffvgspvw aekrvalvig nsayrhapql anpqndaadm askltalgfv
       61 vvtgrdldlt gmrgvirefv gkvegadval ffyaghglqv nggnyiipid aqlksnndld
      121 fealpielvl aamernakvn lvfldacrdn plattlarsl gtrsvvvgrg lakldtgvgs
      181 liafatqpgn valdgagrns pftsallqhl gtpgqsitdd liavrravlq vtggkqipwd
      241 sssltgpvvl npakipetpt nsavvtsdtd rsvelsfwns ikdaternff eaylqqypsg
      301 afvtlaklki aaieardker etaelgqgdl kraalpkvtg vppelakleq ttpglkgssd
      361 ptsqmsagel tlitqrelvr vgcleqvdgk wgrgsqkalq ayaerkgikl asltpteelv
      421 sslkaaggrv cplvcgngle vrgnrcvaag lsvfngvwkl trhattdcgd wrelstsilv
      481 ndgvvssssg lagkvarngt inmtltfvhk grkggniltg mikndkgkgr fkgtgagsgc
      541 sgtvtmsrm
//
LOCUS       WP_457579430             654 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Ensifer adhaerens].
ACCESSION   WP_457579430
VERSION     WP_457579430.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..654
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=71482
     Region          37..381
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mlrfsrksgk epvnmaaelh pltlsratae ssklptlaai aatvavlyia rdvflplaia
       61 illtfalapv vsrlrragcp ravavtgtvt maflfltafg vivalqisev ardvpryqsn
      121 ivekvrslke agsdsqildr lsrvmerisi elsrpekdva vspvtapepk pllveifspq
      181 rpveilmsvi npllgplata glvivvvifm lferedlrdr firlvgygdl hrttealqda
      241 garvgqyllm qlvvnitygv plaiglwflg ipnallwgml aivlrfvpyi gpviaaalpl
      301 flafaaapgw slvvltlglf ialelvsnnv vepwlygsrt glsplaiiva aifwawlwgp
      361 vglvlstplt vclvvlgrhv rqfefleill gnepvlnpke rlyqrllagd pdeatdnaee
      421 mleemylvef ydtvaipall laesdrmrga lteeqgarva esagtlvanl eeiaveeede
      481 dksedpdrdt dekendyelp pgegrsvlcl ggrsalddvt ammllqvlrv qgadvnyfsh
      541 ealrpqkike lpiegrhaiv ltaldresmr hakflvrrlk rlapgarvgi vlwqdvdehe
      601 aakflveetq adfvvsaitd airealstep pqpfksahpg sagraavrgp ahda
//
LOCUS       WP_457579433             304 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579433
VERSION     WP_457579433.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..304
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33248
     Region          21..294
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mndiisavgf cnrtgkgdls tldaslreia etgadaceig iygeeivsgg riiedrvqhv
       61 aeitkrytfn klslhgqivs nfmdrqhhhl qrkvvramle lcdrlgagil vhhsgaaqla
      121 agenaadldk merdalaema eiakgygvri alenifttes gqyrqspsqv aetvraigsd
      181 nvvalidfsh ayieathrgl dfrdelrama pvtghlhvhd sfglpytmnr fyhpaeatal
      241 gigdlhlpig wgdiawddif seltflpdtt limeisaerf adqqlacleq arrlaagvgl
      301 rraa
//
LOCUS       WP_457579435             506 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing sensor histidine kinase [Ensifer adhaerens].
ACCESSION   WP_457579435
VERSION     WP_457579435.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 506)
  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 506)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18589008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..506
                     /product="PAS domain-containing 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=56454
     Region          14..269
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          143..503
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msnddglrkd ahfrehtrdi aelaldlldn tpghmwsmdt agrfiyrnrs mdayfgsslk
       61 dhgawlerih kddqrfvatt wrrsvetgep ldsahrlrga dgefrwfras grpsrdaqgr
      121 vavwhgqtid iehqkeaees lrarsvelsl lvdmvpsnlw rltpdgtttl vnrrmadylg
      181 ldlsnvsdia svmdtifhpd dadavyaelt rclatgerfs mryrllradg ayrwmsgrae
      241 plrdqdgniv qwfglchdie dqvqttaalg rsaeklarat qaanlsqlsa siahevnqpl
      301 aaiaadadac lrwlsadppn vnrgkraaer itldvaatve visrmralfk hqpqeraved
      361 vnrlvhevld lmsdeiaatt tridlaldqh lprvsldrvq vqqvlvnlir ngmqamdttn
      421 plrslkimss hdhpdtvris vedtgsgfkd pervfepfft tksngmgmgl picrsiveah
      481 ggrlwvanne algatvaftl pvastd
//
LOCUS       WP_457579439             156 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457579439
VERSION     WP_457579439.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 156)
  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 156)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..156
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16696
     Region          16..>155
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mpersnpien atdvnvvhii ddderirsal lelfgssgip aeafvdtadf dergdpeavg
       61 cllldvklpg msgieyqrkl sdagfdlpiv fmtgdgdvpt svtamkagav dfllkpfevd
      121 dllsavaaai eegrkqreva arrkharqca dsltpp
//
LOCUS       WP_457579442             568 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457579442
VERSION     WP_457579442.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 568)
  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   2  (residues 1 to 568)
  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   3  (residues 1 to 568)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   4  (residues 1 to 568)
  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 11573933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..568
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62885
     Region          11..171
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(15,17..22,57,59..61,64,112..114,118..119,122..123,
                     160)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(17,61)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(22,33,36..37,40,44,57..58,107,108,113..116,119,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          180..306
                     /region_name="TolBN"
                     /note="TolB amino-terminal domain (function unknown)
                     [Signal transduction mechanisms]; COG5616"
                     /db_xref="CDD:444347"
     Region          343..>516
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          405..431
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(407..408,411..412,414,438,441..442,445..446,
                     448..449,471,474,477,480..481,484)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          436..466
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          470..497
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtdqslqrrl aaivvadvvg ysrlmeadev atladlrklr sgviepavmr ytgrifkvmg
       61 dgfliefgsa vdavaaalem qrattaveas gdrrlllrvg vnlgdviddg sdvlgdgvnv
      121 aarletqaap ggicisakvh geivgkigdr ffdagerylk nltrpvhvwh wpdalqsilp
      181 lpecpsiavl pftntsgdea dapfvdglte dlitdlsrta glfviarnsv lgykgkpvdv
      241 rlvaqelgvr yvlegsarra kgrvrinaql idalggqhlw adrfdrtved vfelqdevna
      301 kivealigrl tiptqrnrpk nfeaydlcvr arllteespq tereaymllq ravelepsya
      361 ealgllaynr wlawthfgep edpnrqmaat faqkavdldp ndagcryvlg tilayerrwe
      421 eseaafakal eldpnhadtw aamsdmsvld grvadglaqi ekalrlnpyp acwylchlgq
      481 aqyaardyea atatlrrket yrtnsrkfla atlaqlgrre earreaelfl iahphftigh
      541 wlssqplrda svrdhfvdgf rkaglpem
//
LOCUS       WP_457579443             312 aa            linear   BCT 27-JAN-2026
DEFINITION  XdhC family protein [Ensifer adhaerens].
ACCESSION   WP_457579443
VERSION     WP_457579443.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..312
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33099
     Region          27..306
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mtiriaadpe tlspepraaf lsddaievls faarsleegq stalitlvei rggaaralga
       61 qmvvrsdgly cgfvsggcse aavaaetita lgkgldrtlr lgegspffdi vlpcgggitl
      121 aihvladaav lrqalstlqh rspvglryhp gkralslqhg seasgwyges fvrayrprpr
      181 vilagtplei davarvavaa gyetvvlerg qvpspdeldg dtavallfhd vdrelplldv
      241 altsnafyig algsrrthak rcqllrdcgg derllsrika piglfdkard arslavsvva
      301 diaharlrld wm
//
LOCUS       WP_457579444             457 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiD family decarboxylase [Ensifer adhaerens].
ACCESSION   WP_457579444
VERSION     WP_457579444.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Mondal,A., Roy,P., Carrannanto,J., Datar,P.M., DiRocco,D.J.,
            Hunter,K. and Marsh,E.N.G.
  TITLE     Surveying the scope of aromatic decarboxylations catalyzed by
            prenylated-flavin dependent enzymes
  JOURNAL   Faraday Discuss 252 (0), 208-222 (2024)
   PUBMED   38837123
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Marshall,S.A., Payne,K.A.P., Fisher,K., Titchiner,G.R., Levy,C.,
            Hay,S. and Leys,D.
  TITLE     UbiD domain dynamics underpins aromatic decarboxylation
  JOURNAL   Nat Commun 12 (1), 5065 (2021)
   PUBMED   34417452
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Marshall,S.A., Payne,K.A.P. and Leys,D.
  TITLE     The UbiX-UbiD system: The biosynthesis and use of prenylated flavin
            (prFMN)
  JOURNAL   Arch Biochem Biophys 632, 209-221 (2017)
   PUBMED   28754323
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Jacewicz,A., Izumi,A., Brunner,K., Schnell,R. and Schneider,G.
  TITLE     Structural insights into the UbiD protein family from the crystal
            structure of PA0254 from Pseudomonas aeruginosa
  JOURNAL   PLoS One 8 (5), e63161 (2013)
   PUBMED   23671667
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..457
                     /product="UbiD family decarboxylase"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49838
     Region          7..455
                     /region_name="UbiD"
                     /note="3-polyprenyl-4-hydroxybenzoate decarboxylase
                     [Coenzyme transport and metabolism]; COG0043"
                     /db_xref="CDD:439813"
ORIGIN      
        1 mtqyhkqdvr sfladyraeh pedvitidqp alddqdatal iwnlaergrh pmlhlkdvsg
       61 vgsevlcnif asrdriarll gstadrlhea yqaranrpft pevlkegpit eeivsgdavd
      121 lnalpmlkhf dtdrakyits giiigehpet gagnlsyhra mihsnnslat slhsrghlwr
      181 lmnmakekgr pmpvamvigg hplfmiaasa rlafgederd vagglmgepl qvvrtpkygi
      241 rvpahaeivl egvldpeahv degpfgeftg yssdrstnnl ftvetvmrrr nailvsvagg
      301 nsaehlnlgr vpreaevvek lkarfpsita vhypssgthf hayiamnqtr egearqvmlg
      361 llgwdqylkt vvvvdadvdi trdsevlwal athfqphkdv viieglpgna ldpsasgigt
      421 tsrmgldatr gpnfhgvrar isdeacaraa allksag
//
LOCUS       WP_457579445             307 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579445
VERSION     WP_457579445.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 307)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..307
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34737
     Region          1..284
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 miidlscypt dlvdlawrhd gppftgdkll kmmdgpyyvn gkprridkaf iqpsqgntiy
       61 thevmdlegk aairqymayt ekmvtehpdr flgcfvynpr ygtqngaeei eryakefdfk
      121 mvqlqanmha yrpdraldwl rpalkkcadl glmvkvhtgd gpysiptefy piirefpevn
      181 filahfgvqt ggvyvfepmq maldtpsvyv esgwclqsri vefakvlpkh kilfgsdtpp
      241 nepgmwinll evlcheppqg lnldedtled ylgnnvarmi gleatkppat veeaeaylrq
      301 hgvalaa
//
LOCUS       WP_457579448             350 aa            linear   BCT 27-JAN-2026
DEFINITION  septal ring lytic transglycosylase RlpA family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579448
VERSION     WP_457579448.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Jorgenson,M.A., Chen,Y., Yahashiri,A., Popham,D.L. and Weiss,D.S.
  TITLE     The bacterial septal ring protein RlpA is a lytic transglycosylase
            that contributes to rod shape and daughter cell separation in
            Pseudomonas aeruginosa
  JOURNAL   Mol Microbiol 93 (1), 113-128 (2014)
   PUBMED   24806796
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..350
                     /product="septal ring lytic transglycosylase RlpA family
                     protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0008932 - lytic endotransglycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=37955
     Region          73..194
                     /region_name="RlpA"
                     /note="Peptidoglycan lytic transglycosylase RlpA, contains
                     C-terminal SPOR domain [Cell wall/membrane/envelope
                     biogenesis]; COG0797"
                     /db_xref="CDD:440560"
ORIGIN      
        1 mvdgmgdgva atvevmrwla itmfcafgga ctttstpgmt slkahspatl hrvyvkmpda
       61 sgkrtsqrvg hytvgkpyvv kgkryypkee pgydrsgias wyargfqgrr tangetydpg
      121 rlsaahptlp lpsyvrvtnl tngssvvvrv ndrgpyhkgr lidisskaae mldmtrrgta
      181 svrvqyvgra alngddmafl masqrkrqgp lgvnrpigaq vagkpltsyg erstlfvgsk
      241 sagnflaasg lrgraasyvl wasqahhlap lgkasiaret aifaecclnk ervgeksvlq
      301 aflpaafdrk shrtgmtgrr sparrrrgdp etghirwcer cqsawracrg
//
LOCUS       WP_457579450              77 aa            linear   BCT 27-JAN-2026
DEFINITION  4Fe-4S dicluster domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579450
VERSION     WP_457579450.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Fujii,T., Hata,Y., Wakagi,T., Tanaka,N. and Oshima,T.
  TITLE     Novel zinc-binding centre in thermoacidophilic archaeal ferredoxins
  JOURNAL   Nat Struct Biol 3 (10), 834-837 (1996)
   PUBMED   8836097
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Beinert,H.
  TITLE     Recent developments in the field of iron-sulfur proteins
  JOURNAL   FASEB J 4 (8), 2483-2491 (1990)
   PUBMED   2185975
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Bruschi,M. and Guerlesquin,F.
  TITLE     Structure, function and evolution of bacterial ferredoxins
  JOURNAL   FEMS Microbiol Rev 4 (2), 155-175 (1988)
   PUBMED   3078742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..77
                     /product="4Fe-4S dicluster domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=8272
     Region          10..77
                     /region_name="PreA"
                     /note="NAD-dependent dihydropyrimidine dehydrogenase, PreA
                     subunit [Nucleotide transport and metabolism]; COG1146"
                     /db_xref="CDD:440761"
ORIGIN      
        1 mplalspttv pvvvdeakci adkgctvcvd vcpldvlris dltgkaymkf decwycmpce
       61 tdcptgavtv nipyllr
//
LOCUS       WP_457579452             247 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579452
VERSION     WP_457579452.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26594
     Region          17..247
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msalqahvre sdgglpvsls rveksfgqln vldsfnlevp agqflavvgr sgggkstllr
       61 liagldaata grvsiagqkv drtlasvrll fqearlvpwq rvienvgiar gqnwqetarr
      121 aladvglggr endwpsvlsg gqrqrvalar alvsapqill ldepfgalda ltriemhrll
      181 egiwtgrgft tvlithdvae avaladrvvv lregaialdi didlerprre ladpravdlq
      241 rqileav
//
LOCUS       WP_457579453             345 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579453
VERSION     WP_457579453.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..345
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37521
     Region          8..321
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtknaisqiw ytrcpvptpv glatqlglld kaftaegitl nsiidskdrs vrsshfdhhl
       61 dysfrhggnv ppirarsegn ptrlvgitwt defqaiitlp etgikttrdl vgrrfgiarr
      121 ppgivdfmaa talkglvsal slegltpsdv eivdiplses vldgregpql yglrnrqayg
      181 peaaallrge vdaiyvkgtp giavanlfaa htvaefgfhp dpkirinsgs prvltvderl
      241 aedrpdlvak liatlkqags waeehpdevr rfvarevgas eevvaaangp dlhkhlgvgl
      301 qpelvaaigh ykdflhewgf lasnfdidqw vdqrpwaeld arava
//
LOCUS       WP_457579455             185 aa            linear   BCT 27-JAN-2026
DEFINITION  AbrB family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579455
VERSION     WP_457579455.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sullivan,D.M., Bobay,B.G., Kojetin,D.J., Thompson,R.J., Rance,M.,
            Strauch,M.A. and Cavanagh,J.
  TITLE     Insights into the nature of DNA binding of AbrB-like transcription
            factors
  JOURNAL   Structure 16 (11), 1702-1713 (2008)
   PUBMED   19000822
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Daley,D.O., Rapp,M., Granseth,E., Melen,K., Drew,D. and von
            Heijne,G.
  TITLE     Global topology analysis of the Escherichia coli inner membrane
            proteome
  JOURNAL   Science 308 (5726), 1321-1323 (2005)
   PUBMED   15919996
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..185
                     /product="AbrB family transcriptional regulator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0010468 - regulation of gene expression
                     [Evidence IEA]"
                     /calculated_mol_wt=19898
     Region          8..>170
                     /region_name="AbrB"
                     /note="Uncharacterized membrane protein AbrB, regulator of
                     aidB expression [General function prediction only];
                     COG3180"
                     /db_xref="CDD:442413"
ORIGIN      
        1 mtrmkllaia tflltlsigg vggwvmwhfh mplawllgam ifcglaalag lplampkfar
       61 ppmtatigam lgtsfspavf ehagvwlrsl aglvffiaaa asvayvyfrk vgkfdhptaf
      121 fsampgglve mvtlgaergg dermisliha ariflvvlsl pfviqlisgg rdrservklr
      181 sifsr
//
LOCUS       WP_457579456             201 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Ensifer adhaerens].
ACCESSION   WP_457579456
VERSION     WP_457579456.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..201
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=20944
     Region          <6..200
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mgeadaivvp ansdiktmdd lvarlkadpa kvswaggsig gidhvaagli aktvgvdpkk
       61 inyvvhaggg evlastlggh atvgisgyee fraqveagql ralavtgdtr ipglevptlk
      121 eagvdlavmn wrgimahpkl sdedreglek avaalvktpe wkaalekrgw idtylpadaf
      181 aafladeqkr vegalkevgl l
//
LOCUS       WP_457579458             260 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579458
VERSION     WP_457579458.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..260
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29220
     Region          20..232
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msqiveipal pleellrsfp kegpgnttak vyrllrqliv evrllpgral pekevaailn
       61 vsktpvreai irlseeglvk vvpqggtfva tievqryiea cfirfrlesg aaaeaakrht
      121 ledlgrlels lnqqieavan edytrffeld edfhrvifst arlsgvwafv nqakgeidrm
      181 rhlkmvfgar rtgevihehr diidairaas pdeavaamtr hlgsleakit elsrdpklws
      241 yiesinattt ekrkprrslt
//
LOCUS       WP_457579460             482 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457579460
VERSION     WP_457579460.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50898
     Region          57..405
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(67..68,71..72,75,107,157..158,160..162,165,185,
                     188..189,192,259,262..263,266..268,271,299,303,353..354,
                     358,362,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 maergfrlgr rrasqaaigi tealprnptc pfhvgaiags cphgsscren vrmnpivvll
       61 afatfatgta eniivgivsd vagelgvsia lagqltavfs ivfaltapla lvltmkierr
      121 rlllcalglf vvsnlcaaas snfatlvvar igmamasatv cllatmlate lvakdmkgra
      181 igiifmgisg slvlgvpagi ficgligwrg vfialsllag lvwlaswrhv pvsarrkaal
      241 pryldhlrkp plvagqfvsi lmigghfvlf aflgpylvei asvaaeniai afavlgiagv
      301 sggylggwla drfsprnvll ltptayllal vtiplvedss wvmfsvlmiw aciswmispv
      361 vqsflisagp etadtgisln lstmhigvgl gtavggiala nlsvsdhcsa crgreflrvl
      421 vvevsrkttr thsrpsqkpc riigthgile yrlriwssvg rvqrvlrram aihvktagsv
      481 ea
//
LOCUS       WP_457579463             343 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579463
VERSION     WP_457579463.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 343)
  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 343)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..343
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37628
     Region          74..254
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtettfddla spdwrakiat lsgpararla erarnaplfa hayafhlnmr fgavtplqla
       61 efayeqrlvg lkvhvedgea aslagmsdaa lseygaaveq fglelhiets ttqetglfda
      121 vriaiatgat slrcypryeg rvseivsqti adlrrletfd pegrlrytle qhedlkseel
      181 igivkavanp rlgllfdfgn minayelplp alaaqapyvt evhvkdclvq qdrdgwahla
      241 cqtgtghlpl hamfvdllll gqdraqvlsf gleeeegyfa palrfpsees dpfiaarsas
      301 ftdigttdlg arlsqeaiaa hrqletvrtm lnqiaaealr ier
//
LOCUS       WP_457579464             262 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579464
VERSION     WP_457579464.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29005
     Region          1..252
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrerrvwswl avalgglyfl lplvgmfdfs mrmqrdgysf eayrvvladp qfqqtfgysv
       61 vlalltivlg illivptayf vrlrfpglrp vvefltllpl vippivivfg yiriyntssv
      121 lpltgswwgt nllllfgyat lslpymyrsv dtglrtidvg slteaaqslg sgwtrilavv
      181 ilpnvfvsvl sgafltfaiv igeyvfaall nvgsfgpymv wvggnrayep salavvafai
      241 twacmaliql vthfskfstv rr
//
LOCUS       WP_457579465             335 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457579465
VERSION     WP_457579465.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..335
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36136
     Region          <35..325
                     /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 matsqanwcf argspniwpc tgatlaipnr sssrpgghaa ftlsalalad pgdgiwfedp
       61 gpvttsnlfr tlglrlcpad vdadgmdvea amarypdarl afvmpsrhhp lgitlslprr
      121 lallewaras dawiieddyd sefrydgapl psmrsidsdd rviyagsfsk alypgirvgf
      181 lvlppqlvgt frtlsglihr svpvetqlal aefiggghfa shlrrmrgly aerreafmla
      241 grdalaglar idcsesglna lawlegsred qashravlda glqcyplsdy tiatpqpaal
      301 ilgyagvpad rmrpllfrla daiarsqgri grsgd
//
LOCUS       WP_457579471             245 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579471
VERSION     WP_457579471.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..245
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25309
     Region          4..244
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msarvlvtga yrgigaacal afaatgarva ladirkpdet aisavqagat etltlacdvs
       61 degsvaaige vvqqtfggld ivvhcagvih eaplletpva dfdrviainl rgsflvgkma
      121 lglmggtaee parlimiasd mayygretfs pyvaskhgvl glvrswakef aprvlvnaic
      181 pgpidtemlg aanmsaewra relaiplarf gkpeeiaela rflagsggry ftgqgigsng
      241 gsimp
//
LOCUS       WP_457579472             267 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579472
VERSION     WP_457579472.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..267
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29291
     Region          1..265
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mtqatisthm rhleerlglr lcsrgrsgfl ltdegrlvye atldlfgsle kfqsrvgeaq
       61 geltgsltfg tvdamitnrd ldlqgalaaf hrqaprvhle idvaapqvlh qgllnggyqi
      121 vlmptvgsat phlrtqpvfs evqklycaqg hplfdlpdda ltdavleaqs fagrtymlte
      181 ticgvnfqwa aatphmegtl llllsgayig flpdhyadew vrngrlrlla permtfedmf
      241 hiahprnkps raaetlaqai lasarpg
//
LOCUS       WP_457579477              92 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin [Ensifer
            adhaerens].
ACCESSION   WP_457579477
VERSION     WP_457579477.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     New connections in the prokaryotic toxin-antitoxin network:
            relationship with the eukaryotic nonsense-mediated RNA decay system
  JOURNAL   Genome Biol 4 (12), R81 (2003)
   PUBMED   14659018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..92
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0097351 - toxin sequestering activity
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045927 - positive regulation of growth
                     [Evidence IEA]"
                     /calculated_mol_wt=10037
     Region          4..66
                     /region_name="PhdYeFM_antitox"
                     /note="Antitoxin Phd_YefM, type II toxin-antitoxin system;
                     pfam02604"
                     /db_xref="CDD:460615"
ORIGIN      
        1 mtstvtaaav sknfgayqda avrepliitk ngrprtvlia yedylrlmrr errveltsal
       61 daddlaavet stmdpgldhl naeltkdkna te
//
LOCUS       WP_457579478             554 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase [Ensifer
            adhaerens].
ACCESSION   WP_457579478
VERSION     WP_457579478.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..554
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60157
     Region          31..349
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          451..552
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mskmsdlper esmefdvviv gagpaglaaa irlkqvnpel svvvlekgae vgahilsgav
       61 vdpigidrll pgwradadhp fktevkddhf lllgpagsir lpnflmpplm nnhgnyivsl
      121 glvcrwlatk aeelgveiyp gfaatevlyn degavigvat gdmgiernge pgpnfargma
      181 llgkytlige gvrgsiakql iakfdlsrds dvqkfgiglk elwqvkpenh rpglvqhsfg
      241 wplgmktggg sflyhlednm vavgfvvhln yknpylfpfe efqrfkthpa irgtfeggkr
      301 lsygaraite ggyqsvpkls fpggaligcs aglvnvprik gshnavlsgi laaeklaaai
      361 asgrandepi evergwrdsa igqdlkrvrn vkplwskfgt aigvglggld mwtnqlfgfs
      421 ffgtlkhgkt daqslepaaq hqkidypkpd gvltfdrlss vflsntnhee dqpvhlqvkd
      481 melqkrsehd vyagpstryc pagvyewvak dgkqvfvina qncvhcktcd ikdpnqninw
      541 vppqggegpv ypnm
//
LOCUS       WP_457579479             285 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579479
VERSION     WP_457579479.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..285
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30670
     Region          11..269
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrdfttdhsa lalntaslgh nldghgagws pervidacae rgfgsivfwr reigsraiei
       61 geraracgls iaglcrtpfi vgaeavdrqr videakaaid maaglgapvl tivvggvhpg
      121 tkgtgeslki vadrvgeiap yaagrnvkla leplnpvyag nrsclttlrd avdicdvvga
      181 tnlgvaidvy hvwwdseiqa qlqragaeri fgyhlcdwla dtrdvlldrg mmgdgvadlk
      241 slrrnieqag yagpceveif sannwwkrdp gevldvmver frtic
//
LOCUS       WP_457579481             419 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerate kinase type-2 family protein [Ensifer adhaerens].
ACCESSION   WP_457579481
VERSION     WP_457579481.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Yang,C., Rodionov,D.A., Rodionova,I.A., Li,X. and Osterman,A.L.
  TITLE     Glycerate 2-kinase of Thermotoga maritima and genomic
            reconstruction of related metabolic pathways
  JOURNAL   J Bacteriol 190 (5), 1773-1782 (2008)
   PUBMED   18156253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..419
                     /product="glycerate kinase type-2 family protein"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43191
     Region          3..418
                     /region_name="GckA"
                     /note="Glycerate-2-kinase [Carbohydrate transport and
                     metabolism]; COG2379"
                     /db_xref="CDD:441946"
ORIGIN      
        1 mksddkefla dlfraaieaa dpenalrahl pseprgrtvv igagkgaaql aaaferlwrg
       61 plegvvvtry gyaapctrir vleashpvpd aaglqatdal feavrdlted dlvvalicgg
      121 gsallpsppg qltleeevlf nqtllasgap isvmnairkq vsgikggrla aachpakvvt
      181 lvvsdvpgdd paqvasgpti pdmtdralar nlvktwgial parvaawleg neglaplpgd
      241 pvftrnevrv iasanlslea aaaraaslgv pavilsdsie geardvarvh aaiarevagr
      301 grpfsrpvvi lsggettvti kgggkggrnt efllslalaa dgigfsaiaa dtdgidgsed
      361 nagafadgqs marlrnlgcd psalladnda wtafhhlgdl fvpgptgtnv ndfrailir
//
LOCUS       WP_457579482             531 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579482
VERSION     WP_457579482.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..531
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57437
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msqgydyviv gggssgcvla arlsenpsar vclieaggrd shplihmpvg fakmtagplt
       61 wglktapqkh annreilyaq akvlgggssi naevftrghp gdydrwveeg aegwgfkdiq
      121 kyflrsegnt ilsgtwhgtd gplgvsnipe pqrmtrafvq scqelgipyn pdfngplqeg
      181 sgvyqtttrn nrrcsaavgy lrpalkrknl tvitgalvlr vvfegrravg vdyqvdgkrm
      241 taradsevll tsgaigtpkl mmlsgvgpaa alrshgidvi qdlagvgenl qdhfgvdiva
      301 elkdhdsldk ynklhwsfwa glqytlfnsg pitsnvvegg afwygdktsp ypdlqfhfla
      361 gagaeagvps vpkgssgitl nsytlrpksr gtvtlrsadp rdlpiidpnf ladpedvkis
      421 vegvkisqei faqpslekyi kirhfpsrdv rteadyiayt rqygrtsyhp tctckmgrde
      481 msvvdpqlrv hgldgiricd sstmpslvgs ntnaatimig ekaadmirgn a
//
LOCUS       WP_457579483             313 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Ensifer adhaerens].
ACCESSION   WP_457579483
VERSION     WP_457579483.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..313
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32383
     Region          10..311
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mdiqrlkphl pwitllvlva vvgitdpgfl rptnllgiag divplfimal gltfaiyigg
       61 idlsaqsman mvtviasvyl aslgawvavl cvvagfllgt lsgfvttrlf vpsfistlav
      121 ggvafsvaqw lsgqralnmd aaqrnetfgw mightwgipn elliaaglva lclfierrtt
      181 lgrvlkavga gelaaaasgi dvarykilaf aisgalasia gllfavklsg gaptiangfl
      241 lpaivavlvg gtpltggvgg vmntvvgtli vavirssmly feidatrqqi vfgvvliiai
      301 altidraklr tvk
//
LOCUS       WP_457579484             501 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579484
VERSION     WP_457579484.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..501
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55388
     Region          3..501
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 myelkavdkk fpgvhalkai dfhikrgeiv glvgengagk stlmkviyga yqpddgkvli
       61 ngtpvrfanp rqamekgigm vfqeqslipn ltvmeniflg yerqftrfgv vdwkvmakaa
      121 rrqlakvkld idpamvtskl sfaqrqlvel akvltleerv egdlvillde ptsvlskeev
      181 qllfklvrel vtrasfifvs hrmdevmels driyvmkdge vvdvvdrgaa paeaiqhkmv
      241 grnvdkqyyr ehlqkpfdaa kalvemdqvg lpgriqdisl klhagevlcl vgtegsgrea
      301 ilrtiygmlt pstgrlrikg gdatdlsprh avsrgvgyvp rerkiegiva gmnvyenmtl
      361 sqmkhrskgg vlrvgeeral arewikklsi kahsefadcg nlsggnqqkv vlakwrsags
      421 dimlldhptr gldigakedv ydmiramsaa gvgivlvadt leeaiglsht iivvkdgriq
      481 kqfacepgsk ptpydllhym i
//
LOCUS       WP_457579496             451 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor domain-containing phosphodiesterase [Ensifer adhaerens].
ACCESSION   WP_457579496
VERSION     WP_457579496.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Tchigvintsev,A., Xu,X., Singer,A., Chang,C., Brown,G.,
            Proudfoot,M., Cui,H., Flick,R., Anderson,W.F., Joachimiak,A.,
            Galperin,M.Y., Savchenko,A. and Yakunin,A.F.
  TITLE     Structural insight into the mechanism of c-di-GMP hydrolysis by EAL
            domain phosphodiesterases
  JOURNAL   J Mol Biol 402 (3), 524-538 (2010)
   PUBMED   20691189
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Schmidt,A.J., Ryjenkov,D.A. and Gomelsky,M.
  TITLE     The ubiquitous protein domain EAL is a cyclic diguanylate-specific
            phosphodiesterase: enzymatically active and inactive EAL domains
  JOURNAL   J Bacteriol 187 (14), 4774-4781 (2005)
   PUBMED   15995192
REFERENCE   6  (residues 1 to 451)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Zoraghi,R., Corbin,J.D. and Francis,S.H.
  TITLE     Properties and functions of GAF domains in cyclic nucleotide
            phosphodiesterases and other proteins
  JOURNAL   Mol Pharmacol 65 (2), 267-278 (2004)
   PUBMED   14742667
REFERENCE   9  (residues 1 to 451)
  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   10 (residues 1 to 451)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   11 (residues 1 to 451)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   12 (residues 1 to 451)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10482329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..451
                     /product="sensor domain-containing phosphodiesterase"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48651
     Region          41..166
                     /region_name="GAF"
                     /note="GAF domain; pfam01590"
                     /db_xref="CDD:460259"
     Region          208..445
                     /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 mlqcenrdvi sakavgakgy ppdesarlkr lrelsivstg pdpvldalvh aaclaadtpi
       61 glitlldger qwfkskrgie gdrsrradaf cdytirssrp fvvpdaardv rfaenpfvtg
      121 snrirfyagv pleiepglrl gslcvldqvp rrlgadvrgl ldrlarcave rllqsedryl
      181 lsridpgrld rakadkaala iaeealaqgl fvlhyqpkia ldtgrrvgfe allrlkkpdg
      241 svlgpatfaa alhdpilsrr igshvlksav aqaqawetag vdfghiavnv sssqfiafpg
      301 spclvdeila atrsaglspr hiqievtegv mlseqggdig vqlealraag fivafddfgt
      361 gfaslvhlke faydqikidg sfvramtaan adyaivkaii dmamalgkkv vaegvetvte
      421 fhalrelgch ygqgfffgrp vgasdvrffp a
//
LOCUS       WP_457579500             268 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphate/phosphite/phosphonate ABC transporter substrate-binding
            protein [Ensifer adhaerens].
ACCESSION   WP_457579500
VERSION     WP_457579500.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Metcalf,W.W. and Wanner,B.L.
  TITLE     Evidence for a fourteen-gene, phnC to phnP locus for phosphonate
            metabolism in Escherichia coli
  JOURNAL   Gene 129 (1), 27-32 (1993)
   PUBMED   8335257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..268
                     /product="phosphate/phosphite/phosphonate ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28413
     Region          14..259
                     /region_name="PhnD"
                     /note="ABC-type phosphate/phosphonate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG3221"
                     /db_xref="CDD:442454"
ORIGIN      
        1 mplaslamyv spppieeatr lfwkalgdrl rgygldarga ldetvaynea wfrpdllfgq
       61 tcgypyvqhl rgrvqlvatp vydlpgcdgp hkcsfiivna rssasslgdl rgmraainep
      121 gsnsgynlfr aavaphavdg rffssvietg ghrasidava sgaadvaaid cvtfgntlrf
      181 dpdrvaavrv laettkgpgl pfitsaltsa kdlmilrrtl aetigdpelg gvcdtlslkg
      241 isllgdsdye alaeldrdaa rhgypaiv
//
LOCUS       WP_457579502             236 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent F420 reductase [Ensifer adhaerens].
ACCESSION   WP_457579502
VERSION     WP_457579502.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..236
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24642
     Region          42..225
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mppiygangn spacrettss fpspttstdn lsisrrttmt tyaiigsgai gsalaerfha
       61 agidaviant rgaaslqtit dkfgstvkaa eleqalhsdv iilavpydav pqvakgksdw
      121 egriivdatn aidfpafkpr dlggrlssei vaelfpgael vkafntlpaa vlaadpvkes
      181 grrvlflsgn fqeartkvad liarlgfaps dlgsfktsgs lqhfgqplva lnllkd
//
LOCUS       WP_457579503             324 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Ensifer adhaerens].
ACCESSION   WP_457579503
VERSION     WP_457579503.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..324
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34550
     Region          45..297
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(60,143,145,147..148,175,229,250,253,266,268,297)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mqtrrsflin tavfgaaagt giglpatsfa kapmvgtqaa gfyrmklgdy eitalsdgtv
       61 klpmskiyqs maeseidtyl tdrfqsgaae vsvnaylvnt gerlvlvdtg tgdlmgpalg
      121 klvsnieasg ykpaeiddvi lthihadhsg glvsgddrvy knailhvnrr eaefwlkaka
      181 kakadqvlgp qiaqaerclg pyvdaeklet fddngaplpg fasvllaght pghsgiives
      241 kgekivfwgd vahgdvlqyd hpdvtvafdv dqnaaaatra tafaeaadgr ylvagahhaf
      301 pgighvrrde nnydwvplvy ravy
//
LOCUS       WP_457579505             542 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579505
VERSION     WP_457579505.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..542
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57997
     Region          24..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdqnthdinr renpaprhpe vpadfdfivc gagssgsvva arlaecgnar vllleaggdd
       61 taesvvnpsq wplnlgtnrd wgfvgepape lygrrlplsm gkglgggssi nvmvwarghk
      121 edwnhfasea gdeawgyesv lgyyrriedw rgtpdalrrg aggpvyvaqp rspqpiaeal
      181 lnaasamgip vfdtpngelm espggasiae lrirdgkres vfgsyvrplm slpnltvvte
      241 alvtrlifdg kratgvealv ngqrraftar cetvlslgai ntpkvlmqsg igpkdelkah
      301 gisvvqhlpg vgrnhqdhla fgctwayrkp egvggggcea klywksdsrl sqpdilqcql
      361 efavpsptet gletpahgwt mfsglaqpks rgrlrlsgpn tndpiliepn slsqpedmaa
      421 alaavelcre lgngdaftpl vtseaapgtr dragmidfir ksavtywhqs ctakmgrdsm
      481 svvnnelkvy gieslriada simprittgn tmapcvvige ragdlirkth gladlsgvap
      541 fa
//
LOCUS       WP_457579506             235 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Ensifer
            adhaerens].
ACCESSION   WP_457579506
VERSION     WP_457579506.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..235
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25992
     Region          52..153
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 manmptasts krrsivvvln prhqplrksf mlkltrkvar rncsgyiagm qrkafsemnc
       61 siaraldevg ewwslliire cffgttrfdq fqerlgiarn ilttrlrrli angvvervsl
      121 evhgrregyr ltakgeelfp vlvslqqwgd kwavgekgpp irmvehetds llgpvgpiss
      181 tgriisfrdv rlemgpgggp stakriadrn lailavadga stadksveld sksts
//
LOCUS       WP_457579509             398 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Ensifer
            adhaerens].
ACCESSION   WP_457579509
VERSION     WP_457579509.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 398)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..398
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=41897
     Region          7..394
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mltdakidsl rndtpgcaer shfnhagasl pprrvteaii ghlmlestrg pmeaaalvah
       61 elailranaa kfigadegev afggsgsalw gsvfaalpql rsgerilvgr qewggnvasm
      121 qraashagas ietipctedg svdpnalsam iddkvrmisl twlpanggli ndaeaigrva
      181 naaripyfvd agqalgqlpi dvsrigcdvl kaagrkyvrg prgtalvyvr snflekldpg
      241 fvdvssgplv ngkvelrkda rlfetseapi slllglgeai alaselgvea iqariallat
      301 rlreglkrip avevrdlgek qsglvsftve gisasvvrrr laeksisiga ngvpytpfdm
      361 targlqeiar asvsyfntag evdglihave hiakdaiq
//
LOCUS       WP_457579512             369 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Ensifer adhaerens].
ACCESSION   WP_457579512
VERSION     WP_457579512.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..369
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39913
     Region          2..364
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mdthvvivga gpaglavgac lrragldfvi lemaheiapa wrrhyrrlhl htvkvfsalp
       61 hmpfpkdypr yvprekmvay ldayaerfel rprfgetvks irrkdggylv etgtetfcag
      121 hvviasgsna epfvpslpei eafkggrlhs adyteaapfa gqsvlvvgmg ntgaeialdl
      181 aecgarptls vrngihivpr qlfgvpiqii aiatqplpra vndrlfptil dlalgkleky
      241 giarpkqgil eqinagripv idvgtvraik sgdikvasdi krftergatf vsgrhaefds
      301 vilatgyrps fekflpaalr pgksgvtrqa aalglylvgf hnpvtgllre igreaaavsa
      361 dierrsstk
//
LOCUS       WP_457579523             363 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457579523
VERSION     WP_457579523.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..363
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39655
     Region          <1..348
                     /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 mpaldifpyk qfgkiaanyw rrftvsdlgy geggglavlr qqlaiylsea rgirceadqi
       61 ivvgstlqaa nlvahvllda gdvvgvedpa yatllstlrs aglrlipvpv srdglnandi
      121 ahraadarmi lvspvgqfpa gatmseaaie rllawantsq rwifeddfns eirwrgtplv
      181 plaarkgger vihvssfnrv lapglrlayl vvprelitsf tavqdslscy aplthqhtva
      241 dfmasgelas hirrtralyr dratvmiasl keklgdvfdv peleaglhlt ltarepfddv
      301 elsrllrgaw idtpplssyc ierkdlfglv agfgnlster lagavqrmel vtrrflekag
      361 kss
//
LOCUS       WP_457579528             145 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579528
VERSION     WP_457579528.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..145
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15841
     Region          1..135
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdaldqkivr llrgngrrsv sdlaletgas ratvrarier meqdgtilgy tvmlradale
       61 dvvrgvmmve ieghvtdrvi rtlggfpeis qihttngrwd llvelsassl anfdavlrki
      121 rlvpgimgse tslllstprs trakl
//
LOCUS       WP_457579529             348 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579529
VERSION     WP_457579529.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..348
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37955
     Region          1..347
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvaidrvl kqygaasvih gvsvdiedge fvtlvgpsgc gkstllrmla gledisggei
       61 ridgrvvndv apkerdiamv fqsyalyphm tvkenmgfsl klqgrekati dklvkeaagi
      121 laleplldrl pkqlsggqrq rvamgraivr hpkvflfdep lsnldaklrv tmrseikelh
      181 hrlgttivyv thdqieamtm adkivvmrag rieqmgkpld lydrpdntfv atfigspsmn
      241 lfegnvgdgg ffidggvslp lptslghgea rtygirpedl elsetgipat vltveptgae
      301 thllvrvgtq tagivlhrrv dlkpeeqiyl qpknqkihlf caegarvn
//
LOCUS       WP_457579531             172 aa            linear   BCT 27-JAN-2026
DEFINITION  RES family NAD+ phosphorylase [Ensifer adhaerens].
ACCESSION   WP_457579531
VERSION     WP_457579531.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Freire,D.M., Gutierrez,C., Garza-Garcia,A., Grabowska,A.D.,
            Sala,A.J., Ariyachaokun,K., Panikova,T., Beckham,K.S.H., Colom,A.,
            Pogenberg,V., Cianci,M., Tuukkanen,A., Boudehen,Y.M., Peixoto,A.,
            Botella,L., Svergun,D.I., Schnappinger,D., Schneider,T.R.,
            Genevaux,P., de Carvalho,L.P.S., Wilmanns,M., Parret,A.H.A. and
            Neyrolles,O.
  TITLE     An NAD+ Phosphorylase Toxin Triggers Mycobacterium tuberculosis
            Cell Death
  JOURNAL   Mol Cell 73 (6), 1282-1291 (2019)
   PUBMED   30792174
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Skjerning,R.B., Senissar,M., Winther,K.S., Gerdes,K. and
            Brodersen,D.E.
  TITLE     The RES domain toxins of RES-Xre toxin-antitoxin modules induce
            cell stasis by degrading NAD+
  JOURNAL   Mol Microbiol 111 (1), 221-236 (2019)
   PUBMED   30315706
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..172
                     /product="RES family NAD+ phosphorylase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18752
     Region          7..164
                     /region_name="RES"
                     /note="Uncharacterized protein, contains RES domain
                     [Function unknown]; COG5654"
                     /db_xref="CDD:444375"
ORIGIN      
        1 mrfvgncyra hdprwafkpv sgdgaairga rfnpkgvpal ylalsvmtav keanqgfahr
       61 idpcvlcsyd vdcdditdls sevgrasnsv sveeiacswa ttlsegrrpp swsiydrlka
      121 rgtagiivps fapgaeegdr nlvlwnwgpn lphkvqvhdp sgrlqkdqls wd
//
LOCUS       WP_457579533             642 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579533
VERSION     WP_457579533.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 642)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 642)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..642
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70644
     Region          26..622
                     /region_name="PBP2_NikA_DppA_OppA_like_7"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08512"
                     /db_xref="CDD:173877"
ORIGIN      
        1 mkrtlalalc lglgiaaapa maetknpgtf vfmwtddiqs fdpayiantp ssygalniys
       61 rllnfngski sefvpslste vpslenglik qaadgsvsyt fpirkgvsah kvgikgadgk
      121 vtweyydklt daqkatiepg ygqitpedvr ysllrailqg qswmsnaite vitagkytdi
      181 akwveaegev ksindaspei lrmvydqlas qivvdgdnvt lklpksfpat lgvialpfgt
      241 svvdkewvas vggwdgsgdt wkahyrpelg anplfaeeng tgpfmleewd rtdrritlkr
      301 fdnyfmgpak lervvmrtvp ewttrrlqll sgdadfvtap vefidelskt egvkvidglq
      361 kvfsrgiffa wplddndnpa igsgkldgag ippdffadid vrkgfnyaqn ydalltqvll
      421 nktvqsrgpt vrgimgyrpd spvysydpak aeehfkkafd gklwdtgfaf tayvtegnpq
      481 ltaalsalqq glsrinpkfk mqiqalpwas vsdklnnrek paapltvmgw gpdysdpggp
      541 lgaasyylsp tglvggmvgq gyrdlmaekf kplldeawas vdpavrepiy aklqemsyey
      601 attqflwedf gyvvtrsnid gyvdnmilyg awdfypvtka nd
//
LOCUS       WP_457579542             178 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit C [Ensifer adhaerens].
ACCESSION   WP_457579542
VERSION     WP_457579542.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Hanazono,Y., Takeda,K. and Miki,K.
  TITLE     Characterization of the Nqo5 subunit of bacterial complex I in the
            isolated state
  JOURNAL   FEBS Open Bio 6 (7), 687-695 (2016)
   PUBMED   27398308
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..178
                     /product="NADH-quinone oxidoreductase subunit C"
                     /EC_number="7.1.1.-"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=20749
     Region          1..153
                     /region_name="NuoC"
                     /note="NADH:ubiquinone oxidoreductase 27 kD subunit (chain
                     C) [Energy production and conversion]; COG0852"
                     /db_xref="CDD:440613"
ORIGIN      
        1 msvepslnra lmlerfgeti edlgtahgid vfvvppekiv efcrflkdqp efrfnflsdi
       61 cgvdhypetp rfeavyhlys lpnrwrvrik crlgdppevp svtgvwrtan whereawdmy
      121 girfqghpdl rriymwegfe gfpqrkdfpl kgykdrlnpf gaegppptqp dlatrnip
//
LOCUS       WP_457579543             479 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Ensifer adhaerens].
ACCESSION   WP_457579543
VERSION     WP_457579543.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..479
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=50517
     Region          7..476
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mtaaallasi lvslpeiivi vgssilligg qllpkgkdal lvwasvavvl laalatftls
       61 ggaepayagm fvadpfsiff kslfylsill tfllsrnyad iegiggseyy vllllalagm
      121 mivasatdll siyvglelmv lctyvltgfl rrqqrsneaa lkyvilgavs tgiflygvsl
      181 vygltgttql drmaaavsnd pldpglllav vfivaglvfk igavpfhmwv pdvyegaptt
      241 itafmsvgpk aagfavilrv flnplvassn vwiilaviav vtmalgsfva lvqdnfkrll
      301 ayssiahagf ailgivagga dgiasvmlyl liytfmnlgi fgavimmrng nfsgeviedy
      361 sgfaklhpgl allmllylfs lagipptagf fakfyvlval vergfvllav iavllsavaa
      421 yfyirivmvm fmrepersfe paltplvgaa lavtaagtig iglfpawflk laqqsafgg
//
LOCUS       WP_457579551             220 aa            linear   BCT 27-JAN-2026
DEFINITION  OmpW/AlkL family protein [Ensifer adhaerens].
ACCESSION   WP_457579551
VERSION     WP_457579551.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..220
                     /product="OmpW/AlkL family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23480
     Region          5..220
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkvektaall afsvhvasva palafdakgp etpyayanig figvfydess dvylagaqap
       61 glglkvdndf tgglefgyrf sehlaasvti glpptakvyg ndllpieigs itygplvvsa
      121 hyhftalgpg fepyvgagla ymtvfneedg alkdldvdns igpvlqfgfe srlderwgff
      181 adfkkiwles tatgtingvp akadvridpf vtmigvsyrf
//
LOCUS       WP_457579552             552 aa            linear   BCT 27-JAN-2026
DEFINITION  hydroxysqualene dehydroxylase [Ensifer adhaerens].
ACCESSION   WP_457579552
VERSION     WP_457579552.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Pan,J.J., Solbiati,J.O., Ramamoorthy,G., Hillerich,B.S.,
            Seidel,R.D., Cronan,J.E., Almo,S.C. and Poulter,C.D.
  TITLE     Biosynthesis of Squalene from Farnesyl Diphosphate in Bacteria:
            Three Steps Catalyzed by Three Enzymes
  JOURNAL   ACS Cent Sci 1 (2), 77-82 (2015)
   PUBMED   26258173
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..552
                     /product="hydroxysqualene dehydroxylase"
                     /EC_number="1.17.8.1"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60849
     Region          1..505
                     /region_name="COG3349"
                     /note="Uncharacterized protein, contains NAD-binding
                     domain and a Fe-S cluster [General function prediction
                     only]"
                     /db_xref="CDD:442577"
ORIGIN      
        1 magrkvavfg ggiggltvah eliergyave iyddcdvpgg karsfgkpgs gtdgkddlpg
       61 ehgfrffpgf yqhvpdtmar iptlggtavd nlviarrcai aqetkplyvf qthapvtvdd
      121 walvlqdwfg rselglrpge aeyfvgrllk ymtmcdkrrl kemerltwwe yidagnksyq
      181 yqkllaaglt rslvamksev astrtiasil vqmfmcltel snsmdrvlna ptsdawinpw
      241 vsyltglgvq fnqrhrfvrf didgqlvssa rvqsptgelq itadyyvaaf pvevaqtllv
      301 ptlgpisqsi aklvnlkydw mnglqfylar dveicrghvi cadsrwavtl isqpqfwtgi
      361 nmgaygdgtt pgllsidiss wdtpgnkttl kpaknctehe ivaevwaqlk dhldattypl
      421 tnsdrvnhfl dpaivignpt vnrepllint cgswesrpra atelpnlfla sdyvqtntdl
      481 acmeganeag rraanailla dnsaashari fsfdepivfa plreidevlf nlglpnpgrt
      541 vagwlstarg wl
//
LOCUS       WP_457579555             290 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM-dependent methyltransferase [Ensifer adhaerens].
ACCESSION   WP_457579555
VERSION     WP_457579555.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..290
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31907
     Region          18..173
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msgltasaae qyasaviayy entkfdykav whsrdaaafh fgyydanvfs hnealvntnr
       61 viatlagigq gdrvldagcg hgatglwlae hrgcnvvgis pvttqveear rfaarsrfgd
      121 qlafevqsyt nttfsqasfd vvvaiesich avvkasfyee aarilrpggr lvvaeymhsg
      181 kplepllqrr mkewldgwsi pgletgeqhv ksaaaagfsn lqvlnnnpaa rrslrrlykl
      241 alvarpidyc lstlgfrnai qhgnvvaslr qyqllqkevw fygiltgtre
//
LOCUS       WP_457579557             423 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Ensifer adhaerens].
ACCESSION   WP_457579557
VERSION     WP_457579557.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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 423)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..423
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46375
     Region          8..278
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 msavpcmill genatgkssv leaitlallg taeataldrl ipaedvnptg lihrpdpvhw
       61 ddvsrdplsv kvgffggqls asltaaassa sfdgtdapsk ivlaygprry fpnkktrrfr
      121 apayralslf damatipnps dwllgcddrd fepavralre ilmldakdyf aregghivie
      181 ssggplrlee msvgyksiia matdiirell rfydnlefas atvlideiet hlhprwkmri
      241 msclrrafpq vqfivtthdp lclrgmhdge vfvlhrpdgd qriekienlp aikgmraeql
      301 ltseffglgs tdpetdakla lyhelasrke sldtsetekl trlkgeldqn lvvgdtpieq
      361 alvdvlrqae lktrtepvka lpkrasilsn alqrltgdfa apsivtraea stargtndgp
      421 aea
//
LOCUS       WP_457579561              84 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579561
VERSION     WP_457579561.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..84
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9262
     Region          7..59
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(7,11,36)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(10,35)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(17..18,29,32,36..37)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mnavqcrlar vamgwgirdl aaaagvssqt vsrlergerl rtrtldrmrk vfeaagidfi
       61 cdgdgfgimi rrphllplth petr
//
LOCUS       WP_457579546             166 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Ensifer
            adhaerens].
ACCESSION   WP_457579546
VERSION     WP_457579546.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 166)
  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   5  (residues 1 to 166)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..166
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=17667
     Region          5..164
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 mgqgffllfa agavvtaltv vlarnpvhsa lalmacflqi saifvlleap llaivqifvy
       61 vgaimvlflf vimmidvrea vlqrfvpgrn lpaltllvll gvemlalvlw sgrfsavepv
      121 asrggdqvrq lstvlfadyl lpfevasiil laalvgaivl arketg
//
LOCUS       WP_457579565             327 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579565
VERSION     WP_457579565.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..327
                     /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=36650
     Region          9..312
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msfskaqdli rlarlaatrr tgiglddicd efavshrtaq rmtdaletlf tnveavdgpd
       61 rrrrwrvadp mldrlqirqe savealeias rtargdgrlr havalddlrd gllarltpkd
      121 alrtetdvea vllgmgsvtr pgprvnlvpa vldavieglr gpfrlrlryr tedaperive
      181 phglllghrs ylvarqparg edtinfrmdq ilsaqcldes fslapgfsle dyaaqafgvy
      241 qnpaqydevi wrfapraaar aaefcfhpkq tievqedgsl ivqfraagwl emawhlyswg
      301 daveviapeg lrclvehhrr sdfdalp
//
LOCUS       WP_457579568             446 aa            linear   BCT 27-JAN-2026
DEFINITION  McrC family protein [Ensifer adhaerens].
ACCESSION   WP_457579568
VERSION     WP_457579568.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..446
                     /product="McrC family protein"
                     /GO_function="GO:0032067 - type IV site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=49286
     Region          1..426
                     /region_name="McrC"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, regulatory subunit McrC [Defense mechanisms];
                     COG4268"
                     /db_xref="CDD:443409"
ORIGIN      
        1 mpaytvrewd klaygagaaq ipdshanrla alaarsafag rggngvlehg rhalrargvv
       61 gilaagdvsl eilpkidvap getldhqnav irkrlvhmla valdlkidlg vitdlawqre
      121 tlleilirif cnkltealrk gmprryvtrd edlsilrgql ditrqftrha vnpsrlacrf
      181 dllsedtpln rimkaavvrl arlsrraanq qrlrelafvy aditeepvsa lrwdqvvidr
      241 tnrswqelfa marlflqdry qtttggvgeg tamlfemnal feeyvgrlia ralagtgltv
      301 slqagrlfcl saqdsgralf qtkpdilirq ggtvthvidt kwkrisarid dpkqgvsqad
      361 vyqmmayaql yraprltlly phhpglgaed avhacyritg hattletasi dvsnssqmla
      421 klrglviget npslteaetf nqnast
//
LOCUS       WP_457579569             310 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Ensifer adhaerens].
ACCESSION   WP_457579569
VERSION     WP_457579569.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Nemeth,E., Kozisek,M., Schilli,G.K. and Gyurcsik,B.
  TITLE     Preorganization of the catalytic Zn(2+)-binding site in the HNH
            nuclease motif--A solution study
  JOURNAL   J Inorg Biochem 151, 143-149 (2015)
   PUBMED   25898772
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Veluchamy,A., Mary,S., Acharya,V., Mehta,P., Deva,T. and
            Krishnaswamy,S.
  TITLE     HNHDb: a database on pattern based classification of HNH domains
            reveals functional relevance of sequence patterns and domain
            associations
  JOURNAL   Bioinformation 4 (2), 80-83 (2009)
   PUBMED   20198175
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Mehta,P., Katta,K. and Krishnaswamy,S.
  TITLE     HNH family subclassification leads to identification of commonality
            in the His-Me endonuclease superfamily
  JOURNAL   Protein Sci 13 (1), 295-300 (2004)
   PUBMED   14691243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..310
                     /product="HNH endonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34383
     Region          162..295
                     /region_name="COG3440"
                     /note="Predicted restriction endonuclease [Defense
                     mechanisms]"
                     /db_xref="CDD:442665"
ORIGIN      
        1 mttyllkinc elhlggaepr pssgfeweni rvtfpnpsri tggpgqqvkn gdqllvwahe
       61 dpgfgsglgl taegtaaqvt tegtltsatl tnvelinphf klrgwsggss gssaidhils
      121 hrhlrsyele eaelaefrav iaefvaakkr qlattaymse eekalladqs ailegferrf
      181 nrqearpdqv kfraalmrly ngrcvisrcg vpeileaahl vpfsesinfr ddprnglilr
      241 tdlhalfdkl llsihpmsgk vvlasrlqat tyrhfeghmv ehfaakeflr eqyqrfkgae
      301 esglknqvav
//
LOCUS       WP_457579587             362 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457579587
VERSION     WP_457579587.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 362)
  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 10009251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..362
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40201
     Region          1..337
                     /region_name="COG5397"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444156"
ORIGIN      
        1 mkqidlmyqt mlaelgqrsl daawtadfpp egrftpvtvk drrywyfdip dgtggrtrry
       61 vgpaddpdia krvethkrek ddlrarrrmv asltreggmi apdsmtgdiv ealsaaglfr
      121 lrgvligtva fqtyagilgv rlpmaalltg dadiaqdyai srevedtlpp mlellqsldp
      181 tfipvphrsg aasssafrta ngyrveflts nrgsddyldp pakmpalgga radplrfldf
      241 lirdpvrtml lhksgvpvtv paperyavhk livasrrhnn vqgaakrdkd irqaellfea
      301 lqqtrrasdl alvyneawer gpqwqeaira gagmmreegl drlrdcltyg aiqigeditm
      361 pf
//
LOCUS       WP_457579592             415 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system HipA family toxin [Ensifer
            adhaerens].
ACCESSION   WP_457579592
VERSION     WP_457579592.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=45771
     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 hgrtrpigla rsnrvrgaet imfeydrawl edpdrfslep alaltrgafa
       61 ppaglttfgs igdsapdtwg rrlmqrserr iaerdgravr tlaesdyllg vadetrlgal
      121 rfrwageepf qapiragvpa fielgrllqi terilrdeet dedlqlifap gsslggarpk
      181 asvidqhghl siakfpketd eysmetweei alrladqagi atplhelmdv agkkvmlsrr
      241 fdrdgtvrip flsamammga kdgergsype ivdalaehga qgrtdahaly rrvafnvlis
      301 nvddhlrnhg flwlgkvgws lspaydlnpv ptdvkarvlt tnidldegtc sldlleeaag
      361 ffaltlaqar tiikevatat atwretakvv garsaeinrm asafehddlq ralal
//
LOCUS       WP_457579593             232 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579593
VERSION     WP_457579593.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12044921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..232
                     /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=25697
     Region          17..155
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          <172..232
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mdsaldqlid asnvamneed irealcaftk rcafdwfayv dmtfpfgaaf tnfpeawqde
       61 ysacgylqid pvmaqaqrlm rpfawlnapt pgadrnvrqf wdgarrhgig ggvsipircp
      121 fgnfaaltfa ardwphiksp ldefkaiaav afvharivac rpttlkapdv nlsarevecl
      181 awaslgksma mtaelvgmrp gtvkfhldra rmklgaynlt navyqatrqr li
//
LOCUS       WP_457579595             219 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Ensifer adhaerens].
ACCESSION   WP_457579595
VERSION     WP_457579595.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 219)
  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 219)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..219
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24152
     Region          1..205
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 marvlvitdd pdffsllgyv lqaegflvsr aigpgdiaid ehvdpaviil dtsentleic
       61 rsivssnkqp aatialirst scelvarllp agvticvirp fglprlldil rraagslger
      121 qhppsrlrld rlertvtwkd rtirlspief glfadlhrhy grvrlrtdll aagwtqpglt
      181 vrcvdvhvcp lrrtlapfge tfietirssg yklvappdn
//
LOCUS       WP_457579596             443 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate aminotransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457579596
VERSION     WP_457579596.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Kafala,B. and Sasarman,A.
  TITLE     Isolation of the Staphylococcus aureus hemCDBL gene cluster coding
            for early steps in heme biosynthesis
  JOURNAL   Gene 199 (1-2), 231-239 (1997)
   PUBMED   9358061
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..443
                     /product="aspartate aminotransferase family protein"
                     /EC_number="5.4.3.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47376
     Region          12..441
                     /region_name="HemL"
                     /note="Glutamate-1-semialdehyde aminotransferase [Coenzyme
                     transport and metabolism]; COG0001"
                     /db_xref="CDD:439772"
ORIGIN      
        1 mmdsivaara qsrarsnaaf rearryfpdg tsratverdg gpiyvtrgeg ahlvdldgsr
       61 fldlnnnftt lihghafppv veavsrtvrd gtcfanpteh eialaallve ripaienirf
      121 vnsgteavmf aiktaravtg ktnvvrfega yhgasdwaev gqsnspanwg pvqrpssvpg
      181 yhgapasvad dvtvlpfndv dalehaigsv ggrtacilid vmpsraglie pepefiqaim
      241 elarrhsili vsdevlnlrq gyqgaserhg ltpdlitagk iigggfpiga iggssevmrv
      301 fsaehgrpav pqggtfsanp vsmvaglatm qamnedafsr lehfgdqvrl glrtaiarsg
      361 apfcvtgtas lfrihprsel prtyreafms gsqeetmrrl trhcvshgis lpigasacls
      421 tamtaadieh vievfddfls qtf
//
LOCUS       WP_457579597             297 aa            linear   BCT 27-JAN-2026
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Ensifer adhaerens].
ACCESSION   WP_457579597
VERSION     WP_457579597.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=32145
     Region          15..263
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mkievdvafa aenvvgesav wderqnklcw vdivgksihr lcpstgnhek wsfpdlvtsi
       61 glrndggaii glrksialwe fggelrhvae vepevpgnrl negvvapdga fwvgtmqdni
      121 aadgtpiams aktgrlyrya lgklrpvsed rfgitntliw tdggrlitad tednaiysya
      181 ldangllndr qtvlsgferg spdgscvdae gfiwncrvag ggcvirfapn gridrvvdlp
      241 cswptscafg gpqletlfvt sarftmsdeh laqnphegai falrpgtfgq tvnrfsq
//
LOCUS       WP_457579608             438 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Ensifer adhaerens].
ACCESSION   WP_457579608
VERSION     WP_457579608.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..438
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47073
     Region          17..391
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 mtlclfrnak ggvpswpflp svalcvtllp acagrptgvl apvaanpsta qvemlvtttr
       61 graekpgemf sgeralsptf aditvsippd tvrkagevaw prklppnpat dfaalkaeei
      121 drvaaekwln ihvrkspdgs vlvfihgfnn hfedavfrfa qivhdsgars vpvlatwpsr
      181 gsllaygydr estnytrnav erlfqylard pevkevsila hsmgnwlale slrqmairnd
      241 glpakfknvm laapdvdvdv fgsqiadmgk rrprftlfvs rddralavsr rvwgnvsrlg
      301 aidpeqspyk eelaadgitv vdltkikagd nlhhtkfaes peivqlignr lsggqtltds
      361 rlglgdhiva atagaaqtvg taaglvvaap aaivdqntrq nyahhvetlv gpsgrarsnt
      421 tdsacgkenq trsgkcnp
//
LOCUS       WP_457579610             168 aa            linear   BCT 27-JAN-2026
DEFINITION  YciE/YciF ferroxidase family protein [Ensifer adhaerens].
ACCESSION   WP_457579610
VERSION     WP_457579610.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Singh,M., Penmatsa,A. and Nandi,D.
  TITLE     Functional Characterization of Salmonella Typhimurium Encoded YciF,
            a Domain of Unknown Function (DUF892) Family Protein, and Its Role
            in Protection during Bile and Oxidative Stress
  JOURNAL   J Bacteriol 205 (7), e0005923 (2023)
   PUBMED   37367303
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Hindupur,A., Liu,D., Zhao,Y., Bellamy,H.D., White,M.A. and Fox,R.O.
  TITLE     The crystal structure of the E. coli stress protein YciF
  JOURNAL   Protein Sci 15 (11), 2605-2611 (2006)
   PUBMED   17001035
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..168
                     /product="YciE/YciF ferroxidase family protein"
                     /GO_function="GO:0004322 - ferroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18225
     Region          3..166
                     /region_name="YciE"
                     /note="Ferritin-like metal-binding protein YciE [Inorganic
                     ion transport and metabolism]; COG3685"
                     /db_xref="CDD:442901"
ORIGIN      
        1 mpaektlndl fldtlkdiyf aekqivkalp kmaraahsee gkarflqhrd etegqierle
       61 qvfeligksa rgktceaiqg liaegeeime eykgtaalda glissaqave hyeiarygtl
      121 kswaaqlgld aavplldanl qeeiatdqkl talgevaanp kaskraae
//
LOCUS       WP_457579622             264 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_457579622
VERSION     WP_457579622.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28277
     Region          18..237
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtigrdlinn hafhetdrrk vawvtgassg igkslalrla ldgwtvavsa rnsveldtla
       61 rsvenkihsf pldvtdreaa entvrdiemr lgpislavfg agtyrrdsls tfdaaaigem
      121 vglnimgtvn clqaimpamt trrsgriavm asvagytglp gaagygatka alinmcealy
      181 pelerqgvqm tiinpgfvdt pltrqndfpm pflissesaa eyimrglerg evrdripved
      241 esgleaiega sskpevrlda phva
//
LOCUS       WP_457579623             324 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Ensifer adhaerens].
ACCESSION   WP_457579623
VERSION     WP_457579623.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..324
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34177
     Region          <19..321
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mafchlalpg plcptppgga elstdyaert rvaafregat ligtlsaisl pfafgtagan
       61 nadglkavav lvavllpltg lmafvfvpep vnrstrefgl mqslvfmskn rpflrliaaf
      121 llngfanaip atlflyfvse rlgaaewrgp flllyfacav lgvplavkaa rrwskhkaws
      181 gamlvtcsif avsgflgdgd lvafgaicvc tglllafdlv lppsmqadvi dndtavsgsq
      241 rsgmyfaawa latklslata vgvtfpmlsl igfdpaqdrs spdalnglsl lyawapivpk
      301 laaiglmwgf pidrvaqrel igrt
//
LOCUS       WP_457579624             660 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Ensifer adhaerens].
ACCESSION   WP_457579624
VERSION     WP_457579624.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 660)
  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 10101347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..660
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72291
     Region          59..540
                     /region_name="YtcJ_like"
                     /note="YtcJ_like metal dependent amidohydrolases. YtcJ is
                     a Bacillus subtilis ORF of unknown function. The
                     Arabidopsis homolog LAF3 has been identified as a factor
                     required for phytochrome A signalling; cd01300"
                     /db_xref="CDD:238625"
     Site            order(102,104,376,408,470)
                     /site_type="active"
                     /db_xref="CDD:238625"
ORIGIN      
        1 mptrrsflga asslalpalf ssartagaqq tgdtsmtpdl ilhsglvttl dranptatav
       61 avkdglilav gddrtimala gsgtktidlk gkrvlpglnd nhthvvrggl nfnmelrwdg
      121 vrsladamdm lkrqvaitpa pqwvrvvggf tehqfaekrl ptideinava pdtpvfllhl
      181 ydrallnaaa lravgytrdt pnppggeitr dasgnptgll lakpnagily stlakgpklp
      241 fdyqvnstrh fmrelnrlgv tsvidagggf qnypddyavi qklsdegqmt vrlaynlftq
      301 kpkqekddfl kwtssvkykq gndyfrhnga gemlvfsaad fedfreprpd mppemegele
      361 evvrilaenr wpwrlhatyd etitraldvf ekvnqdiple ginwffdhae tisdrsidri
      421 aalgggiavq hrmayqgeyf veryghgvae atppvakmla kgvnvsagtd atrvasynpw
      481 vslswmvtgk tvgglqlypr ancldretal rmwtekvqwf sneegrkgri ekgqfadliv
      541 pnkdffncae deisfltsel tmvggkivya agefashden kvppampdws pvrtfggyaa
      601 wgepegagkr slrrtaitsc gcasdcdvhg hdhagawtsk lpiadlkgff galgcscwav
//
LOCUS       WP_457579625             461 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate aminotransferase family protein [Ensifer adhaerens].
ACCESSION   WP_457579625
VERSION     WP_457579625.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..461
                     /product="aspartate aminotransferase family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50484
     Region          1..458
                     /region_name="PRK06105"
                     /note="aminotransferase; Provisional"
                     /db_xref="CDD:180401"
     Site            order(117..119,151..152,154,225,258,260..261,287)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(118..119,151..152,225,258,261,287)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            287
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mndrpnslha ldrqslvhpy tnlavhqevg phvitggegi yvvddqgkry ieglaglfca
       61 glgfseprlv eaatrqlktm pfyhsfahks tepgirlaek llemapvpms kvffagsgse
      121 andtaiklvw yynnavgrpe kkkiisrrka yhgvtvatas ltglpfnhrd fdlpiakilh
      181 tdcphywrfa epgeseedfa trlvsnleam ileegpetva affaepvmvs ggvitppkty
      241 feklqavlkk ydillvadev icgfgrtgnm fgsetyglkp dmiscakqls aaympisalm
      301 inetisdvll dqsrkigtfs hgftygghpv aaavalealt iyqevdivsh vravgprfqe
      361 girklgehpl igeargvglv aglefvkdkv tkenfppawq vanhagkfat ergvltrglg
      421 dmvslcpami inekqiddlm armqlafddt lswarsqgyi a
//
LOCUS       WP_457579629             368 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Ensifer adhaerens].
ACCESSION   WP_457579629
VERSION     WP_457579629.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..368
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39073
     Region          21..351
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mldlrswigs llalgaltll fvgcalvlwp flsallwaav icfstwplyr qceravggyr
       61 aaaaaimtmv vvfalaapla flvtalvddi enlaeaitqv leegpsappn wvnglpiige
      121 gvaaywenla hdapafiael kkltgpitdi alsggaalrg vlielalsif itfflflhgr
      181 rmigfmrqis ervagprskr lltvigatvk gvvygmigta laqgllagtg fwiagvpqpv
      241 llgcltfals fvpggppflw vpvglwlllq gsmgwaifvg lwgfllvssi dnflrpylln
      301 qntnlpvlls lfglvggvla fgliglflgp tllavaynlf lewvaaeieg rvqaasglpv
      361 dletnskn
//
LOCUS       WP_457579639              78 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579639
VERSION     WP_457579639.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..78
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8179
     Region          14..>61
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 msnsaglrcg glhfpdavrd lrrgiglsqq efaeivgltr rqiaeievgg anprletlek
       61 vgrgglvvgf vakpepdp
//
LOCUS       WP_457579643             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579643
VERSION     WP_457579643.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33315
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 makedfndll wflavaeern ftkaaaklgi tqstlshtik rletrmglrl ltrttrsval
       61 teagdrlfhs lsprisairs dlaaltalrd tpsgtikitl sdhaletivw pklkpilsky
      121 pdikielsrd nglrnivddg fdagvrlges iekdmiavri gpdwrmlava speyladrsi
      181 pehpqdlmqh dcinmrqatg gglyiwefek ngqelrvrid gqltfntsyp mvdaalaghg
      241 iaflpedlat ehieagrlva llsdwsppfp gyyiyypsrh qnspafkvvv dalryqrs
//
LOCUS       WP_457579646             421 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Ensifer adhaerens].
ACCESSION   WP_457579646
VERSION     WP_457579646.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..421
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45683
     Region          1..372
                     /region_name="SsnA"
                     /note="Cytosine/adenosine deaminase or related
                     metal-dependent hydrolase [Nucleotide transport and
                     metabolism, General function prediction only]; COG0402"
                     /db_xref="CDD:440171"
ORIGIN      
        1 mpppvnahdh gygirtldfg naddalevwi pglrlrprte pylealvafs rlaqtgvgat
       61 mhchnslnid rlvdeagavm raacdagirl alscplldyd pwaydggpqr lrpyldpadw
      121 ddlsgsipsy aspsvqisaa davtaantsp lvdvqygpig pqwcsnalle aiaeashatg
      181 rrihmhlles prqrqwldrr fpqgvvryld eigflsprla vahgvqlrpd elellaargv
      241 qlvsnpsanl rlrsgvapva tippsgpafa fgldgtgfdd dqdlwrelrl ahllhggrdl
      301 trtftagrvf daaihvgakv vnapanedrv lvdyaaliad slmddldeae vlltrmtaah
      361 akalyvggqe imcdgrltrv dfeaaraell qqaradlprl taergrvtkl aaatrayyas
      421 w
//
LOCUS       WP_457579652             117 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579652
VERSION     WP_457579652.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12204063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..117
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12883
     Region          28..111
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpevraalrs glryaaeeim ardkyqqklt pakvalelgi svrqlhvlfe haeltfartl
       61 asmrtsqarr llverpalpv tevayacgfd slarcyrlft gaygmapgef raagslh
//
LOCUS       WP_457579653             224 aa            linear   BCT 27-JAN-2026
DEFINITION  substrate binding domain-containing protein [Ensifer adhaerens].
ACCESSION   WP_457579653
VERSION     WP_457579653.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..224
                     /product="substrate binding domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24925
     Region          17..213
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(27,31,70,84,86,148,165,192)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(28..29,33..34,36..37,40,44,46..52,113,142..146,
                     153..154,157)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddaefalaq rhqaprgrlr idvpialgrl hilpvlqrfl nrwpeveaev sfsdeyrdiv
       61 ddgidvavri ggptdsrlvr rvlashrlit caapeylkrr gtprtidelt rhdrigfkha
      121 ggpvpwhyrv gggdrdvgvq gnlrlgntea irdaclagtg laqlgaflvg rdiregrlvp
      181 lleeferdep pvcvvyptrk hvspkvrlfi eairaewaag apwa
//
LOCUS       WP_457579654             522 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Ensifer adhaerens].
ACCESSION   WP_457579654
VERSION     WP_457579654.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..522
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53661
     Region          236..486
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mgngtgaleg vinatpgadg ikvykidsvg glptgwtttg tgtgqvlvkd nfgtdiyrlt
       61 tnadgtyqle qlkerpgtqv tidaandfpn sptktydfgf akftalasss gqvtfnanta
      121 sgggnefgig npafstgekf kiefdkdvss vtlrfgtvkd pgsieftvrd gnstpytfsk
      181 tvvagqtsvt ilpsdvgfkf dyievlgkng invsfttvgy tetvaasdlt ltfgvtgedr
      241 dgdlsnsstl tfvsdgsttt aneisgsagh dvihggagdd tlnggdgndi iyasagdddi
      301 nggagvdlln fsdatgpvtf tlvqsswedd vdlssvglge edyrniegvi gsdfndklyg
      361 ssygdilagg egndtlsgng gadklygdag ndtlvggsgn dtlyggtgvd kltggsgddt
      421 fvldakdlql diadvitdyd gdddsvdlsa llgnlpsgtt ldgdylqvvq dgqnanlqvd
      481 tegnagsggw htvavlenfn vstevvkvlf nengtktsqd vh
//
LOCUS       WP_457579656             182 aa            linear   BCT 27-JAN-2026
DEFINITION  AbrB family transcriptional regulator [Ensifer adhaerens].
ACCESSION   WP_457579656
VERSION     WP_457579656.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sullivan,D.M., Bobay,B.G., Kojetin,D.J., Thompson,R.J., Rance,M.,
            Strauch,M.A. and Cavanagh,J.
  TITLE     Insights into the nature of DNA binding of AbrB-like transcription
            factors
  JOURNAL   Structure 16 (11), 1702-1713 (2008)
   PUBMED   19000822
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Daley,D.O., Rapp,M., Granseth,E., Melen,K., Drew,D. and von
            Heijne,G.
  TITLE     Global topology analysis of the Escherichia coli inner membrane
            proteome
  JOURNAL   Science 308 (5726), 1321-1323 (2005)
   PUBMED   15919996
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..182
                     /product="AbrB family transcriptional regulator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0010468 - regulation of gene expression
                     [Evidence IEA]"
                     /calculated_mol_wt=18941
     Region          <10..174
                     /region_name="AbrB"
                     /note="Uncharacterized membrane protein AbrB, regulator of
                     aidB expression [General function prediction only];
                     COG3180"
                     /db_xref="CDD:442413"
ORIGIN      
        1 mgrsgssyvp fsaveakdla wfaaaiwlgv aagiilrlpa ryllgpmivs aglhlsgvsd
       61 fqlpsvflaa aqvvigttvg crfvntapml ilrviglsvg stvlllsvsl gfallvstmt
      121 gdrfvgtvla yspggvaems lialslgiev pfvvfhhiir vllvvagsat vfrlridpfk
      181 tk
//
LOCUS       WP_457579662             233 aa            linear   BCT 27-JAN-2026
DEFINITION  toll/interleukin-1 receptor domain-containing protein [Ensifer
            adhaerens].
ACCESSION   WP_457579662
VERSION     WP_457579662.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..233
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24668
     Region          103..210
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 maqctapkeg hrsasaaanc pacrggsryr gyssynsghg sypsyspsyr assgsgggga
       61 grvrakwska gssvlytpte vraltpirqt aenraelpdl rdvflchawd drqgdaktlh
      121 dlleargvsv wfsekdvalg tsllreidkg lvksrvgivl vtpallrrlp aagvadkels
      181 allateqlvp ivhnttyeal rnvspllasr sglsteedtm avvadklael vat
//
LOCUS       WP_457579667             342 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Ensifer adhaerens].
ACCESSION   WP_457579667
VERSION     WP_457579667.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..342
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36930
     Region          3..250
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtmtkvnigi igtgfiakil apeiqssska rlaavssrtl akaedfvasy pgavavegad
       61 rliarddvea vyiaiptsak edvasralaa gkhvliekpl hssesfkrls alalkkglvl
      121 mdathfvhhp rtsamrqhla aligaprslh tmfyfpfsdr enirfdpsde pmgavgdmaw
      181 ysmravveyl apdafedikv faerdpqsga viratgvlkf dagktatfdv gytagaavmd
      241 ltvagtsgil tqddfvldwk sgfgfdnpdi ptgfihrsgm atrkdfafie tpgeksqhgl
      301 mvdsfadlir ndddaaretw lsataktqgf ldaiwrqiqa rg
//
LOCUS       WP_457579800             440 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer canadensis].
ACCESSION   WP_457579800
VERSION     WP_457579800.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19948164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..440
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47689
     Region          14..424
                     /region_name="cztS_silS_copS"
                     /note="heavy metal sensor kinase; TIGR01386"
                     /db_xref="CDD:273593"
     Region          221..439
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mslggissas wywpstlrar lflvlflgla iayglsfsil flerymsaka vmlgtletdv
       61 atsiaildrl paneragwld rlsrgsyrfv lgpglpgvpd lssrgaeiaa kieeaaghrf
      121 plrveaipgd dkrlqahltl sdgapltidv tprgvmpiae wlpyvlatqm allllcvwfa
      181 vgqvirplsn laaaadaldp nkkaeplsea gprevahaar afnamrdria hyleervqil
      241 aaishdlqtp itrmrlradm addtserdkl vqdlreierl vqdgiayars ahgnvektar
      301 idlasfidsl aydyqdtgks vsvvhaiegt vftkphalrr ilsnfidnal kfagaaeisv
      361 errengevai tvmdrgpgip ddmieasmqp ffrleqsrnr dtggtglgla iaqqlagaig
      421 gsvrlynrag gglaaevvir
//
LOCUS       WP_457580262             646 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer canadensis].
ACCESSION   WP_457580262
VERSION     WP_457580262.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..646
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71879
     Region          <240..>287
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
     Region          362..615
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mmvdasqvef kvplkaaled yadrpvvltv kdpghrlglr prlalhrkgr vpatvfrsfl
       61 vngkgrgrfy gwlpvqfega tlvadeatae msadvtpeis vrrlslleig itlvlrrplf
      121 ilrilrllma rnvkgatfrf arqvdalsap syddwidaqq aaervevpda lgdwptkpfv
      181 fvtigrgtdq avaetraslr aqtwrdyaem paseaarlkn edeqearpql wmripagmrl
      241 apralerlar pfafsssvva vysdedrvnk lgrridpffk pawnpplahs gwlpldgalv
      301 rladlpegld lentplgeli akaatgrrga vlhvprvllh rnapyqrtmr pvrlkadape
      361 vpkvsviipt rdrvdlleac lkglfestdg vdldvividn dssdpavlal mdryekagcm
      421 rrlplpdgfn fsracnlgve asrhelilll nndveplqpa wlsnlareld dpdvgaagsl
      481 lffpdgyvqh ggvtlgagtv arhsfhflhp qsgedngllr erreisavta aclltrkslw
      541 aqiggmdesn ltvafndvdy cvkvrhagct ivwtpdsaml hresvsrgad ntpeklrrfa
      601 reektvyqrw gdilrndpfh npnlsliaed fvlearprdl sprssr
//
LOCUS       WP_457580885             347 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Ensifer canadensis].
ACCESSION   WP_457580885
VERSION     WP_457580885.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..347
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38995
     Region          <9..76
                     /region_name="LptE"
                     /note="Outer membrane lipoprotein LptE/RlpB (LPS assembly)
                     [Cell wall/membrane/envelope biogenesis]; cl01125"
                     /db_xref="CDD:470086"
     Region          195..280
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 msqlqivfdg eslitpqsia teftssrsef ydeqfatgka elalilqiaq qqftqeldpr
       61 kiihrlaaal hetrakfhps vwqelipiaq khpvsefflq dpftrwssek prgysgdaql
      121 ldfiyghpsv areiakaspv gkalydytkd asssvavrer rdlltkhvde iaatrggeae
      181 iltiaaghlr eanqsvalqe rrikrwvald qdplsvgsit rdfrgtsvea idgsvrgilt
      241 rahklgkfdf vyaaglydyl phnvavkltr rclqmlkpng vflfanfatd igvdgymetf
      301 mnwalllrsq sdmwrivnes vdgtnfeshv tfgenrnvvy amlqkra
//
LOCUS       WP_457581024             120 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Ensifer canadensis].
ACCESSION   WP_457581024
VERSION     WP_457581024.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 120)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 139559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..120
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=12785
     Region          8..117
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(96..99,101)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
ORIGIN      
        1 mnggqpsvfv vedeyllaiq iqddllaagf svigpftslr ssiaaakrea pqaatldvnl
       61 ngefvypvad ellargipvl lltgyaasdl peqyrslprl skpfnsrdli rivegllagk
//
LOCUS       WP_457581952             208 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease D [Ensifer canadensis].
ACCESSION   WP_457581952
VERSION     WP_457581952.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Shevelev,I.V. and Hubscher,U.
  TITLE     The 3' 5' exonucleases
  JOURNAL   Nat Rev Mol Cell Biol 3 (5), 364-376 (2002)
   PUBMED   11988770
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Zuo,Y. and Deutscher,M.P.
  TITLE     Exoribonuclease superfamilies: structural analysis and phylogenetic
            distribution
  JOURNAL   Nucleic Acids Res 29 (5), 1017-1026 (2001)
   PUBMED   11222749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..208
                     /product="ribonuclease D"
                     /EC_number="3.1.13.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0033890 - ribonuclease D activity
                     [Evidence IEA]"
                     /GO_process="GO:0042780 - tRNA 3'-end processing [Evidence
                     IEA]"
                     /calculated_mol_wt=22958
     Region          14..>192
                     /region_name="Rnd"
                     /note="Ribonuclease D [Translation, ribosomal structure
                     and biogenesis]; COG0349"
                     /db_xref="CDD:440118"
ORIGIN      
        1 manairfheg disatdaary rgaiavdtet lglvprrdrl cvvqlspgdg tadviriaag
       61 qkdapnlvam ladparqkif hygrfdiavl fhtfgvtttp vfctkvasrl vrtytdrhgl
      121 kdnlkemldv diskqqqssd waaeilspaq leyaasdvlh lhalreklta rllrdgrmeh
      181 adacfaflpt rskldllgwd etdifahs
//
LOCUS       WP_457583362             268 aa            linear   BCT 27-JAN-2026
DEFINITION  M15 family metallopeptidase [Ensifer canadensis].
ACCESSION   WP_457583362
VERSION     WP_457583362.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 268)
  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 10610297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..268
                     /product="M15 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0071554 - cell wall organization or
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=29093
     Region          182..251
                     /region_name="Peptidase_M15_4"
                     /note="D-alanyl-D-alanine carboxypeptidase; pfam13539"
                     /db_xref="CDD:433291"
ORIGIN      
        1 mrrgsvracl gatvlllwtc vgnplaaelt lsgklellak aypdaiaeir dgalilrdgg
       61 aalpiddgrk kshaeklasg diedslsqiy rlgpcvnpph vdfdpgrirs ealmkrlygg
      121 saasvsrdlv avdwfgeslk vtsrngvara lqgvgaelag rpklkrylvp sagtfnwrki
      181 agartlsvhs fgaaidlntg yadywrwagk gksgaapfrn ryppeivevf ekhgfiwggr
      241 wyhfdtmhfe yrpeliaiar qagasacr
//
LOCUS       WP_457584366             117 aa            linear   BCT 27-JAN-2026
DEFINITION  EF-hand domain-containing protein [Ensifer canadensis].
ACCESSION   WP_457584366
VERSION     WP_457584366.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000101
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..117
                     /product="EF-hand domain-containing protein"
                     /calculated_mol_wt=12344
     Region          <25..109
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mrkvallmaa vfcqlapaaa qdkpaamyqg qmdrldrdgd gaisrpeyqg fmttafasld
       61 knkdgtlsaa eaapvlnaqq favinvnrdg kitqseflns vmadfkaadr ggdgslq
//
LOCUS       WP_457585307             114 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Ensifer
            canadensis].
ACCESSION   WP_457585307
VERSION     WP_457585307.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..114
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12421
     Region          9..113
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 maqdaasnle sansrtqqlm gdiapklael tddvlyadiw erpqlsqrdr slvtvsalia
       61 lnrpdqlrsh lvrakanglt eeqlvetith mafysgwpsa vsaiaiakev faen
//
LOCUS       WP_457585495             267 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Ensifer canadensis].
ACCESSION   WP_457585495
VERSION     WP_457585495.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..267
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29198
     Region          49..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          181..263
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnhkisvrpg agaaaqivqy nrlrysnili eqpvvivver gtkilrqgdf ecviapgeav
       61 alqqgqvfdv vnaaekdday larwiafdpe liaafhptkn vgapiekahl ltglqpafvd
      121 afgaatrvva epegiplpva rhrigellvw lnvlgcffrp vnatsfaqra rqnligdpgt
      181 pwtgsglgkr lgvseatlrr klsaegwsfq qlltdvrmsa amqmlqssdv pvlhiaqqvg
      241 yesqsrfaar frqrfgfpps airghrr
//
LOCUS       WP_457585960             268 aa            linear   BCT 27-JAN-2026
DEFINITION  M15 family metallopeptidase [Ensifer canadensis].
ACCESSION   WP_457585960
VERSION     WP_457585960.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 268)
  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 10610297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..268
                     /product="M15 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0071554 - cell wall organization or
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=29474
     Region          182..251
                     /region_name="Peptidase_M15_4"
                     /note="D-alanyl-D-alanine carboxypeptidase; pfam13539"
                     /db_xref="CDD:433291"
ORIGIN      
        1 mrrgskstcl raaflflsac vgetlaadpt lheklellar aypemiaevg kdkltlrdgg
       61 aalpiddgrq kshaekltsg diedslsqiy plgacarppa adfdpgrirs ealmkrlygg
      121 saasirrdlv svdwfgerlk vtrrhgvaka lqavegelaa rpklkrylvp sagtfnwrni
      181 agtrtlsvhs fgaaidlntg fadywrwsgg gksgaaayrn rypldiveif ekhgfiwggr
      241 wyhfdtmhfe yrpelisiak qasasacr
//
LOCUS       WP_457585972             275 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Ensifer canadensis].
ACCESSION   WP_457585972
VERSION     WP_457585972.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..275
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=30654
     Region          <8..61
                     /region_name="tolB"
                     /note="Tol-Pal system protein TolB; PRK01029"
                     /db_xref="CDD:234889"
     Region          40..194
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          123..272
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mrssvetydi ltgqtrvvwq tdrlveapnw spdarsliin gdgrlyrlal dgtepveidt
       61 gfahlcnndh gispdgstia isdktefgks aiyllpasgg sprlvtpnlp sywhgwspdg
      121 rsltycgird qvfdiytisv eggverrltq gegrndgpdw spdgawiyfn ssrtgrmqiw
      181 rvrpdgtdie risdspygdw fphpspdgrh llvlsydgdv fdhprdlnvr lrlmdmdggn
      241 ardlfelfgg qgtmnvpnws pggdrfafvr yepes
//
LOCUS       WP_457586825             208 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease D [Ensifer canadensis].
ACCESSION   WP_457586825
VERSION     WP_457586825.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Shevelev,I.V. and Hubscher,U.
  TITLE     The 3' 5' exonucleases
  JOURNAL   Nat Rev Mol Cell Biol 3 (5), 364-376 (2002)
   PUBMED   11988770
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Zuo,Y. and Deutscher,M.P.
  TITLE     Exoribonuclease superfamilies: structural analysis and phylogenetic
            distribution
  JOURNAL   Nucleic Acids Res 29 (5), 1017-1026 (2001)
   PUBMED   11222749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..208
                     /product="ribonuclease D"
                     /EC_number="3.1.13.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0033890 - ribonuclease D activity
                     [Evidence IEA]"
                     /GO_process="GO:0042780 - tRNA 3'-end processing [Evidence
                     IEA]"
                     /calculated_mol_wt=22898
     Region          14..>191
                     /region_name="Rnd"
                     /note="Ribonuclease D [Translation, ribosomal structure
                     and biogenesis]; COG0349"
                     /db_xref="CDD:440118"
ORIGIN      
        1 manairfheg disaadaary rgaiaidtet lglvprrdrl cvvqlspgdg tadviriaag
       61 qkeapnlvam ledparqkif hfgrfdiavl fhafgvttap vfctkiasrl trtysdrhgl
      121 kdnlkemldv diskqqqssd wgaatlspaq leyaasdvly lhalreklta rllrdgrmeh
      181 adacfaflpt rckldllgwd etdifahs
//
LOCUS       WP_457587941             644 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Ensifer canadensis].
ACCESSION   WP_457587941
VERSION     WP_457587941.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 644)
  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 644)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..644
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71058
     Region          <238..>285
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
     Region          360..613
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mmadasqvef kvplkaalen yadrpvvltv kdpghrlglr prlalhrkgr vpasvfrsfl
       61 vnskghgrfy gwlpvqfega tlfaddatae isadvtpeis vrrlslleig tilvlqrplf
      121 ilhilrllma rnvkgatfrf arqvdalsap sydewidaqq aaeraeasda pqdwptkpfv
      181 fvsigrgteq avaetrasla tqtwrdyaem pasevagmkd gnaarprlwm rlpagmrlap
      241 ralerlarpf afsssvtavy sdedrvnklg rridpffkpa wnpplaqsgw lpldgalvrl
      301 adlpegldle smplgeviak aakgrrdavl hvprvllhrd apyqrmmgpv rlkadatdvp
      361 kvsviiptrd radlleaclr glfestdgvd ldvividnds sepaalalmd ryekagrirr
      421 lplpggfnfs racnlgveas rnefilllnn dveplqpgwl snlarelddp dvgaagsllf
      481 fpdgyvqhgg vtlgagtvar hsfhflhpqs gedngllser reisavtaac lltrkslwmq
      541 iggmdesnlt vafndvdycv kvrqagctiv wtpdsamlhr esvsrgadnt peklgrfare
      601 eqtvyqrwgd ilrndpyhnp nlsliaedfv leacprdlap rtsa
//
LOCUS       WP_457588087             445 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Ensifer canadensis].
ACCESSION   WP_457588087
VERSION     WP_457588087.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 445)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..445
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48112
     Region          12..445
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          231..445
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mttsanhslk krliwhiltf qvlllvavia gfmallirad lggmildags asiaagavev
       61 gsdqklklkd tpelramrae tpgfwfvvrn ergetvqsgp vpdayrsige hldrvtfadi
      121 rdgmapymls aiarvvqter gtytvltggg rlwsasfavf fltnllllpi vlilvlipaf
      181 aipiivrraf aslaevadha ksidvdrrga rlpdgrvpge vrplveavng alqrldegye
      241 rrqrfimdaa helrtpvail qtrlegmdfg plrsrllvdt ariaglaeql ldleridrds
      301 ahfasidlvs lcrdvaadla plalsagcdi sfthgpeqvs ahgdagaler avtnlvrnai
      361 ehagglisih verggiievs dagpgipese rerifepfhr lqprdhgagl glhlvreivs
      421 rhkghisvvc pqtggacfrm tlpaa
//
LOCUS       WP_457588455             173 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Ensifer
            canadensis].
ACCESSION   WP_457588455
VERSION     WP_457588455.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..173
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18366
     Region          38..152
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mfqqirthla aagaasllgl fpdaalaqtt derrergaav irslnngmtq ptlegmrref
       61 pflaeateay algdvwsrpg ldnrtrqlaa vaafaaiget afmrvhagya lnigvseeel
      121 neiidmvtvp agfpkaiaas qvlsqlfeer rqpqrggpad qspamatgee agp
//
LOCUS       WP_457588946             233 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein [Ensifer canadensis].
ACCESSION   WP_457588946
VERSION     WP_457588946.1
KEYWORDS    RefSeq.
SOURCE      Ensifer canadensis
  ORGANISM  Ensifer canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1008387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Ensifer canadensis"
                     /db_xref="taxon:555315"
     Protein         1..233
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25105
     Region          78..>141
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mrrlligaav ivtlvyllgs igaerttlne trrpsariva qdqkpvaggg tqvsavapqh
       61 gqspesaesv gtekviatvf vrgkrvalre rpgkefaild rydagrpvgl lsvvgawsrv
      121 kdnltrregw iashllssdk prskpkrdtp asvepsreep vkvprisdal ivqriiaesi
      181 sgysgscpcp enrdragrrc grrsayskpg gaapicypgd vsremieafr arl
//
LOCUS       WP_457589543             364 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase, partial [Legionella pneumophila].
ACCESSION   WP_457589543
VERSION     WP_457589543.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Achari,A., Marshall,S.E., Muirhead,H., Palmieri,R.H. and
            Noltmann,E.A.
  TITLE     Glucose-6-phosphate isomerase
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 293 (1063), 145-157 (1981)
   PUBMED   6115414
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         <1..364
                     /product="glucose-6-phosphate isomerase"
                     /EC_number="5.3.1.9"
                     /GO_function="GO:0004347 - glucose-6-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0006094 - gluconeogenesis [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0051156 - glucose 6-phosphate metabolic
                     process [Evidence IEA]"
     Region          <1..349
                     /region_name="pgi"
                     /note="glucose-6-phosphate isomerase; Reviewed; PRK00179"
                     /db_xref="CDD:234679"
ORIGIN      
        1 irekkwlghs glpitdivni giggsdlgpr vcinalsnyi skefnyhfis dvdptsfndv
       61 iakinpqtal fivssksftt ketllnarka falyedrasi dqhfiavtah perahqmgik
      121 tvlpiwdwvg grfsfcsavn litaiaigye qfvellagah nvdthvqftd fknnipvlma
      181 ligiwnnnfl nihnllilty skkleyfvpy vqqldmesng ksidvngrmv dystgpivwg
      241 glgnqaqhsy fqllcqgthr cvgdfitlkt ndeheinsmc hykmkvlseg iqtienpygh
      301 ipgnmpmnhl ilsdcspytl galvalyehk ifvqsviwni npfdqpgies aksahreitl
      361 ssel
//
LOCUS       WP_457589807             150 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaX family transcriptional regulator, partial [Leclercia
            adecarboxylata].
ACCESSION   WP_457589807
VERSION     WP_457589807.1
KEYWORDS    RefSeq.
SOURCE      Leclercia adecarboxylata
  ORGANISM  Leclercia adecarboxylata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Ferrandez,A., Garcia,J.L. and Diaz,E.
  TITLE     Transcriptional regulation of the divergent paa catabolic operons
            for phenylacetic acid degradation in Escherichia coli
  JOURNAL   J Biol Chem 275 (16), 12214-12222 (2000)
   PUBMED   10766858
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         <1..>150
                     /product="PaaX family transcriptional regulator"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
     Region          1..>149
                     /region_name="PaaX"
                     /note="DNA-binding transcriptional regulator PaaX
                     (phenylacetic acid degradation) [Transcription]; COG3327"
                     /db_xref="CDD:442556"
ORIGIN      
        1 irryggeiwi gslirllref ghndqavraa vsrmskqgwi qaekrgnksy ysltargvkr
       61 meeaarriyk trpehwdgkw riliytipee krhlrdelrk elvwsgfgtm snscwmspnn
      121 leqqvydlid kydirpyvdf flaeydspht
//
LOCUS       WP_457589797             418 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Fusobacterium polymorphum].
ACCESSION   WP_457589797
VERSION     WP_457589797.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium polymorphum
  ORGANISM  Fusobacterium polymorphum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Fusobacterium polymorphum"
                     /db_xref="taxon:76857"
     Protein         1..418
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49525
     Site            order(43,46..47,49,73,76..77,80..81,83..84,107,121..122,
                     125..126,129)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          43..66
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..101
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..346
                     /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          187..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          226..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          287..317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          321..346
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          355..385
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkilkkelle kierldelwk yqeiidliet lpteqldtel igelgkaynn ienyekglkt
       61 lksieneegd nalwnwrvgy syfflkdyik aekyflkaye lepddeyard facdfligty
      121 talsklesrn gnsekaieya lesrkyayde egrvetdffl aslynrymky aeaeeilksi
      181 laetqkdeer lfelvyclfk qekyeeviqr lnhaleveek ekeivyiysl lvwcyhqlgd
      241 yekaleyqik fkekahsqig yqlgydpkkv eevlehsnra ielerndtwf fevkgvilld
      301 tgryeealdl fkkayelsnh gwylycmgrc lrglekyeea ikvllesrqi sidkndvvdg
      361 edfelaycyi gigdkenaqk yldsardsvt qrgllndylk ekieeiekgi lslnqfln
//
LOCUS       WP_457589869             309 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_457589869
VERSION     WP_457589869.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..309
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37085
     Region          2..183
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mqqtiqdfei ividdcstdk tieiiesfnd qrikiltkse nkglidslni gfkaakgkyi
       61 armdgddisd fmrfekqlhv lennptikvc gswlqafgke nkiikhkenh eqilvhmmah
      121 csmslgavmi drawvkdecf neekkhvedy dfwsrviwkg klyniqevly hyrfhetqvs
      181 nkynhiqrkg dipiklvffk klnynqekfq dsffekmflq keyftieefs lflawfsivq
      241 eqnkklkiyn qsdfnkvikk yktsliykiy fhsnfckidk kwritaltkl sfpdlffvfk
      301 lkikeklkf
//
LOCUS       WP_457589903             218 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Fusobacterium polymorphum].
ACCESSION   WP_457589903
VERSION     WP_457589903.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium polymorphum
  ORGANISM  Fusobacterium polymorphum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
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   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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Fusobacterium polymorphum"
                     /db_xref="taxon:76857"
     Protein         1..218
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25684
     Region          <2..185
                     /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          20..53
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(59,62..63,66..67,69,87,90..91,95..96,98..99,122,
                     125..126,129..130,133)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          59..86
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          87..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          121..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkyaeaeeil ksiltetqkd eerlfelvyc lfkqekyeev iqrlnhalev eekekeivyi
       61 ysllvwcyhq lgdyekaley qikfkekahs qigyqlgydp kkveevlehs nraielernd
      121 twffevkgvi lldtgryeea ikvllesrqi sidkndvvdg edfelaycyi gigdkenaqk
      181 yldsardsvt qrgvlndylk ekieeiekgi lslnqfln
//
LOCUS       WP_457590082             440 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide biosynthesis protein [Gordonia aurantiaca].
ACCESSION   WP_457590082
VERSION     WP_457590082.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aurantiaca
  ORGANISM  Gordonia aurantiaca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Yao,Z. and Valvano,M.A.
  TITLE     Genetic analysis of the O-specific lipopolysaccharide biosynthesis
            region (rfb) of Escherichia coli K-12 W3110: identification of
            genes that confer group 6 specificity to Shigella flexneri
            serotypes Y and 4a
  JOURNAL   J Bacteriol 176 (13), 4133-4143 (1994)
   PUBMED   7517390
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1903964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Gordonia aurantiaca"
                     /db_xref="taxon:3151852"
     Protein         1..440
                     /product="polysaccharide biosynthesis protein"
                     /calculated_mol_wt=44533
     Region          30..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mttdrmastp daprdddaan digaaslgrv tiatliaaas gylvlllaar hlgavgygvf
       61 avfwaayglv tgaqngqlqe ttravraaad agarsrpvlv nvgiglglav lvaatsplws
      121 davfgaergl svlllaagva sfavyahlcg alsgtlswss favlvsvdal lrlagaiiav
      181 aagwgttafl iitvigsvsw cvlllsssta rralgiggdv parrltantl tamaaaaass
      241 vlvmgfpvli nltanlrgtp daaearviga lvlavtltra pllvplnsfq gvlisrfver
      301 rhqpiaalaa plgivgvaga vgmvaawlvg pwllrtvfga dfdldglvva lltggatgla
      361 lltvtgaaav aagahrwyaa gwwvatlvav gmlllpvdvd lrtcvalivg pvvglavhvl
      421 gvlrhpsprk iagwdqnrel
//
LOCUS       WP_457590089             860 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Gordonia aurantiaca].
ACCESSION   WP_457590089
VERSION     WP_457590089.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aurantiaca
  ORGANISM  Gordonia aurantiaca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 860)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11905783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Gordonia aurantiaca"
                     /db_xref="taxon:3151852"
     Protein         1..860
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88818
     Region          33..860
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
     Region          612..860
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 migvppdegp trgarryvda flagltrirl lnlreirthr lrlftslavv vvssalliav
       61 lgtfgstses vrafnnavsg nadlevaaia dtgidaslag airrdvdgar avvpmirgsv
      121 vvddsavpli gsdqrvtals gglraavqqe nagsidfdkl rtgvfagpgl gltpgdaltv
      181 ngievevlev vdnrqasqln ngrfmfayld laqrlvgleg rldsilivte sgvnvgavrs
      241 qvekivdgra vvvnpdfrak qaevsssvtr datllvslvs lviaaflifn tmnmavasrr
      301 gslamiralg gkrthlvgdm lgeaaimgia ggvigipigi lagraviasl pdpppdtvgt
      361 vidyhlpwya pmvavlacii acvaatalaa ravfsvspve amapvevsds mvrrgpliai
      421 savvglagli aswvivatvp grpailagvv yligallvcf alskplswlv vrvarwfggp
      481 galasvnter aprrawatlm tvavaiavgm gtsgaldnlv ssmsksldgl gdpdfyvsss
      541 sesslplgpi lpsslrgeva ripgvtevvg gqwaavnige sraniqglep gsrapfmrka
      601 speavarvld gdgillsnvl arvldaktgd tvtlstptgp hdvvvrdtvd yvavdsgvaa
      661 msqellgewf erdgdtylqv itapdadpaa vqgslealva dvpttgnkpi nvytgaaala
      721 atqavveqag sftvaiqwiv agaaaialln tlllsvierr relgvlramg asrkfisrmv
      781 laeaaavaiv galvgivlga tmhllsdeil svttsltviy sprpsvamfv aiavalclvg
      841 aflpavrasr mnisesiqae
//
LOCUS       WP_457591953             312 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein, partial [Glaesserella parasuis].
ACCESSION   WP_457591953
VERSION     WP_457591953.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Plisson,C., White,H.E., Auzat,I., Zafarani,A., Sao-Jose,C.,
            Lhuillier,S., Tavares,P. and Orlova,E.V.
  TITLE     Structure of bacteriophage SPP1 tail reveals trigger for DNA
            ejection
  JOURNAL   EMBO J 26 (15), 3720-3728 (2007)
   PUBMED   17611601
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         <1..312
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
     Region          <4..158
                     /region_name="COG5412"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444167"
ORIGIN      
        1 lnlwttikpy fdnfsqfvsn lwngisgiws svwggisnwf sglwenlksl fsgnfsalgn
       61 iilsfnplal fttiftsvln wfgidlpakf snfgkniidg lvngisnawn lakekvselg
      121 ngikgwfaek lgihspsrvf kgygvnvveg lvigmdkaqp lateasqhls navtfepvln
      181 tvetifkptl ikekgffgsl wddiqfganm vgnllglnqp tdlrtpsfnp qakdgglfad
      241 yqplnrnevs ntatthnqgi tvhfspniti sgsapapdlk eqllqalndp amlygleqll
      301 nrvndqfgrr ay
//
LOCUS       WP_457592001             124 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein, partial [Glaesserella parasuis].
ACCESSION   WP_457592001
VERSION     WP_457592001.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Plisson,C., White,H.E., Auzat,I., Zafarani,A., Sao-Jose,C.,
            Lhuillier,S., Tavares,P. and Orlova,E.V.
  TITLE     Structure of bacteriophage SPP1 tail reveals trigger for DNA
            ejection
  JOURNAL   EMBO J 26 (15), 3720-3728 (2007)
   PUBMED   17611601
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         <1..>124
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
     Region          <7..71
                     /region_name="COG5412"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444167"
ORIGIN      
        1 akfsnfgkni idglvngisn awnlakekvs elgngikgwf aeklgihsps rvfkgygvnv
       61 veglvigmdk aqplateasq hlsnavtfep vlntvetifk ptlikekgff gslwddiqfg
      121 anmv
//
LOCUS       WP_457591996             224 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor, partial [Glaesserella
            parasuis].
ACCESSION   WP_457591996
VERSION     WP_457591996.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 224)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         <1..224
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [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          11..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 irkevtfess iaaigaamsd isrvkilsal mdgrawtate lssvanisas tasshlskll
       61 dcqlitvvaq gkhryfrlag kdiaelmesm mgislnhgvh akvstpvhlr kartcydhla
      121 gevavkiyds lcqqqwiten gsmitlsgiq yfhemgidvp skhsrkicca cldwserrfh
      181 lggyvgaalf slyeskgwlt rhlgyrevti tekgyaafkt hfhi
//
LOCUS       WP_457592031             435 aa            linear   BCT 27-JAN-2026
DEFINITION  NCS2 family permease [Lactiplantibacillus pentosus].
ACCESSION   WP_457592031
VERSION     WP_457592031.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus pentosus
  ORGANISM  Lactiplantibacillus pentosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Lactiplantibacillus pentosus"
                     /db_xref="taxon:1589"
     Protein         1..435
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45884
     Region          3..435
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 milehifhlr enrtsvrrel igglttflam syilavnpel lgsagmdkta vftatvlaai
       61 ggcllmglva nfpvdlapgm glnafftytv vqewhipwqt alagvfvagi lfilltlskl
      121 rdklinlips alkyavsagi glfiafsglq tsgiivadks navalgnlhn ptvllaifgi
      181 ivgimlvtan vtggifwgmf itaavgmifg iiplpsgivs gvpsvqplfg qaithigdin
      241 sfqmiivilt ffiiglfdts gtlvgvatea gmvdkesgev kgvgkalfsg alattlgaif
      301 gtspttayve stsgvavgar tglssvfvav lfaiaaffsp vltvitsavt asaliivgil
      361 mlsnvqyidw tkfeiavpaf ftmimmllty siseglavgf ifypitmtvk grwrevnalm
      421 wtmmvvfily fafva
//
LOCUS       WP_457592016             329 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Gordonibacter
            urolithinfaciens].
ACCESSION   WP_457592016
VERSION     WP_457592016.1
KEYWORDS    RefSeq.
SOURCE      Gordonibacter urolithinfaciens
  ORGANISM  Gordonibacter urolithinfaciens
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Gordonibacter.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Gordonibacter urolithinfaciens"
                     /db_xref="taxon:1335613"
     Protein         1..329
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36289
     Region          25..200
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(28,30,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(57,103..104)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            102..104
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mqetkdaqag aprtqnvpeq gsvavlipcy neavtigkvv ddfrrvlpea tvyvydnnss
       61 dgtgaiareh gavvrcerrq gkgnvvrqmm rdidadyylm vdgddtypae aapellaplv
      121 adeadmvvgd rlsngtygee ndrafhgfgn dlvrvlikwi ygfefsdvmt gyraynavfa
      181 ktmpvlspgf eietelsiha vdkrwriaev pidyrdrpeg seskldtfsd gckvllmils
      241 lfkdyrplal fswvallfcv lglvagvpvv wefaatglvp klpsallava lvfigilsft
      301 cglildtvvk gtrkqyelqv trayishkk
//
LOCUS       WP_457592042             128 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Hominenteromicrobium
            mulieris].
ACCESSION   WP_457592042
VERSION     WP_457592042.1
KEYWORDS    RefSeq.
SOURCE      Hominenteromicrobium mulieris
  ORGANISM  Hominenteromicrobium mulieris
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Hominenteromicrobium.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Hominenteromicrobium mulieris"
                     /db_xref="taxon:2885357"
     Protein         1..128
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14600
     Region          31..>124
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 meyskedlme akkqiwgvge nmgteeskki weenaqfwdn amgdesnefh revvrpkvte
       61 llspnpadyi ldiacgngny ssylaqrgas vvafdyskkm ielakrrqsq yakqiefcva
      121 datdrkvy
//
LOCUS       WP_457592527             285 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Hydrogenimonas sp.].
ACCESSION   WP_457592527
VERSION     WP_457592527.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31574
     Region          77..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          198..279
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtvtvpnyfl qekpesilsl sqglylkras asvrshrvrn tmhgllvvle gskrldtagg
       61 sveleapcga ffaqgnyfvs rnmrtyrala lyfddafaqs llkewggeeg asegsavsva
      121 vplpqesaal hlaeamwrda gggaevpapl lrlrtktlfm ellaidpagv agflhrivag
      181 rrgrfvkile enldivesvg dmqrllrmsp ahlhrrfmqe lgippkrwlt arrlekgaal
      241 llgsdrevaq iaaecgyatp swfiaafkry ygvtplqyrr ekrhf
//
LOCUS       WP_457592607             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Hydrogenimonas sp.].
ACCESSION   WP_457592607
VERSION     WP_457592607.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..360
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39989
     Region          2..>290
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          165..358
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mmkifsalva keliaffrsw glvaivlysf tldiyitgag iemqaknvav gyvdetaggm
       61 sekilsrlhm pefqkprlfl srealsrsiy nreimvglif esdfeknlkk ygtskidvll
      121 dsvaatqgfq alqylqnill dyadieipve lkihklfnpn attsqfmama emlsvitllg
      181 viltaavfvr ekengtweim llmpidpkli ilaksfsqvi vimggvviat givlfgvfdv
      241 pmngsiaaff llsffyafts agiglfvaav sksmlqvaql silimmplif lsgawtpiha
      301 mhpllqslsl isplryyieg sesiffrgtd fvdlwsyfag villgsvlyf ygfrkigrlf
//
LOCUS       WP_457592925             323 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Hydrogenimonas sp.].
ACCESSION   WP_457592925
VERSION     WP_457592925.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13299214
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..323
                     /product="peptidylprolyl isomerase"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=37492
     Region          39..>299
                     /region_name="PRK10788"
                     /note="periplasmic folding chaperone; Provisional"
                     /db_xref="CDD:182731"
     Region          174..320
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mkqrkssmkk lllllvtlas vslfassdtn ttengrviat vngyeitkae ldrqvgilmp
       61 rsffhstvtp eklkevekda lkelvkkhll lqyakkkgyk isdsiveree kkirkafgsk
      121 enfearlkrs nltydefrre lrndllmqkl ydkeirtdlt dedlsnyyek nkykfkvpek
      181 ikirliyvrn nptdpkgrek alkraqeale kikggkdfad iaakysnams rikggdmgfi
      241 hkgmldepie kvayslkkge msdivetpkg fyivkleeis psvqldfdqv kerlkkelks
      301 kyeeqkleki lkdmrqnaki vyk
//
LOCUS       WP_457593055             472 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Hydrogenimonas sp.].
ACCESSION   WP_457593055
VERSION     WP_457593055.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..472
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51289
     Region          15..411
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mirkhvteqt aiffsvtkwv vlssvvgvmi gaivtlflki lqlaensrsd fvfpyyymlp
       61 fallltvwiv rtfapsaegh gtekvieavh kkhgkiditv ipvklfatvm tifaggsvgk
      121 egpgaqigag aaswlsdllr fskedrkklv icgisagfas vfgtpiagai fgvevliigv
      181 ilydvllpsf iagfaaftta qflgieytyf dirfyqnvtl dlplifqvva aglffgfvsd
      241 ivvtavsmth kyikkvpvhp yiiafgggvv lialtfffge qylglgleti kdtlnpdpyf
      301 skdlpwyafl lktlftsvtl gvggsggiit pvfyigatsg hlfgqlagge hialfaalgf
      361 vsvlagstnt piaatimave lfgleiahya alsavisfli tghrsvfmsq ilamkkseml
      421 evkvgevien advdleetei grirnvkeri rrkreklkek kagrllskre dk
//
LOCUS       WP_457593231             259 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Hydrogenimonas sp.].
ACCESSION   WP_457593231
VERSION     WP_457593231.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..259
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27440
     Region          1..258
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msdilkigsy efksrlivgs gkypdfqttk datlasgsem itvavrrvni tspdeenlmd
       61 yfkdtdvkfl pnsagcttae eaitlfrltr eatgidlikl evigdtqktl ypdvietika
      121 cevlakegft vmaytnddpi iakrleeaga aavmplaapi gsglgvqnry nvvfvreavs
      181 vpvvvdagig qasdaaaame lgadavltnt aiaqakepiv maeamkhava agrlsylagr
      241 ipkrpyatas spvdgmiqf
//
LOCUS       WP_457593587             112 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Hydrogenimonas
            sp.].
ACCESSION   WP_457593587
VERSION     WP_457593587.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..112
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12185
     Region          9..110
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mgtytkklee iksligrlqk eapdqisafh qfmtavekps alerkqkeli nvalavaaqc
       61 ewcialhvkg aldagakree ildaamqavl mhggpalmym tpveealdef ts
//
LOCUS       WP_457593857             480 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook-length control protein FliK [Hydrogenimonas sp.].
ACCESSION   WP_457593857
VERSION     WP_457593857.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Aizawa,S.
  TITLE     Mystery of fliK in length control of the flagellar hook
  JOURNAL   J Bacteriol 194 (18), 4798-4800 (2012)
   PUBMED   22797757
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Mizuno,S., Amida,H., Kobayashi,N., Aizawa,S. and Tate,S.
  TITLE     The NMR structure of FliK, the trigger for the switch of substrate
            specificity in the flagellar type III secretion apparatus
  JOURNAL   J Mol Biol 409 (4), 558-573 (2011)
   PUBMED   21510958
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Waters,R.C., O'Toole,P.W. and Ryan,K.A.
  TITLE     The FliK protein and flagellar hook-length control
  JOURNAL   Protein Sci 16 (5), 769-780 (2007)
   PUBMED   17456739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13396646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     gene            1..480
                     /gene="fliK"
     Protein         1..480
                     /product="flagellar hook-length control protein FliK"
                     /GO_component="GO:0009424 - bacterial-type flagellum hook
                     [Evidence IEA]"
                     /GO_process="GO:0044780 - bacterial-type flagellum
                     assembly [Evidence IEA]"
                     /calculated_mol_wt=52757
     Region          280..>433
                     /region_name="FliK"
                     /note="Flagellar hook-length control protein FliK [Cell
                     motility]; COG3144"
                     /db_xref="CDD:442378"
     Region          371..433
                     /region_name="Flg_hook"
                     /note="Flagellar hook-length control protein FliK;
                     pfam02120"
                     /db_xref="CDD:460451"
ORIGIN      
        1 maslaltpll smlkemkidi dasslpknep glfkellell gsenpdpeal eslirrvksd
       61 svseegglsl afretagfrp mevrigpetk tshdqkedas alslpvpdiq ksrklsvkpl
      121 qtgvpseska segpkrhdri flanylshav lkreagdaka vhelrsshtl relvtradal
      181 glevvdlkvv tqketrpall petqkpplps pailqhteri sqsaaeviwr skegsparaq
      241 rpdkaavtlq nlltepkisd kkgeksvhak apkkpdsdfs allsnlqrvs gsassgtrha
      301 dktaplqgls mhdeaaepgv kpeygtgese gaewshsevr skaseqltqk iadakttlrh
      361 faqtlqerve nykppftrmq isldpkdlgs vevtmvsrgn nlhiqvhsnp taigimathg
      421 nelknqlvsm gftdvqmqfs mnqqqqqnrq qrhdfgdgya eseeipdfye sldliiphyv
//
LOCUS       WP_457593952             303 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Hydrogenimonas sp.].
ACCESSION   WP_457593952
VERSION     WP_457593952.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..303
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35116
     Region          <109..303
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          220..303
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meslffnigd krykttplye kgeehitrvd isngivffdf flkegkprsf eirnldrmvv
       61 isvvkegafs vfdniggrkf vceedearif cssrqdftlt ieakksdifv lfiadfflkr
      121 ylslnknepi dflyekiqge vgvelidtkp ldalslhlid kiidtrlqqr mhsitcehnv
      181 iefmihrfsl iclrdedidp delqialkaq kyllnhfvnp ptiphlahic atnetklkra
      241 fkkvfkttvg gyirklrlek anlllkdrvl sigevakevg yshqgyfgrl ffeaygiypk
      301 dlk
//
LOCUS       WP_457594044             477 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Hydrogenimonas sp.].
ACCESSION   WP_457594044
VERSION     WP_457594044.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 477)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..477
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54026
     Region          8..467
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          247..467
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mlkshfklsq ifylnfilll vgtllftsvi iyysiehiei kqytnqlrse layvrsrlde
       61 gkslglaare mgeimgrplr vtliamdgvp lfdneadvah menhanrpev maarregfgt
      121 avrysrtvgn driyvakkir wngrdavlrl svsldqvmkd faqlwvrial aflaaiaigf
      181 lisrliqrei daelgkvtdy lkaiaakqyn asfsagfsse fktiaallkk lakrleksek
      241 rkrkytaklr lasrqrseii saishefknp vaaimgytet ltddenlpvs irkkflsrie
      301 entkrisdmi drlsfitrle nseitprmsd fdlgeivqaa ahammqkypg rtvkvqirqp
      361 vaihadrtmm emvvvnlidn alkysdtvve vlvepdklav idrgegieah eieavtkkfy
      421 riekrswdns mglglaivky ilklhridle isskrgegtk vafalpavcp iinknev
//
LOCUS       WP_457594122             350 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Hydrogenimonas sp.].
ACCESSION   WP_457594122
VERSION     WP_457594122.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
REFERENCE   3  (residues 1 to 350)
  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 10657197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..350
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=40027
     Region          1..228
                     /region_name="PGA_cap"
                     /note="Bacterial capsule synthesis protein PGA_cap;
                     smart00854"
                     /db_xref="CDD:214858"
     Site            order(6,8,35,75..76,172,204,206)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:277327"
     Site            order(6,8,35,75,172,204,206)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:277327"
ORIGIN      
        1 mifcgdtvfq gkfddnifke cdesflkksk vinlesliei qsmkkissgi glisspdive
       61 flkamhvkac imannhitdf dvsidkqkrf lkdcdidscg agnnlssaie pciieenntk
      121 tailsfgwet isciaadets kgvnplrynh ilklvdsylt kypdtlltvv fhwnyeyeky
      181 pqpahrklaf kliemgvnai ighhphivqg aeiyrgrpif yslgnfyfra gihsgfkvtp
      241 ppeaydglcv eisddidktm lywthltsdg klllkkreel kqsakiaelt pfknmshqey
      301 iawfkanryk nrllpiyknp eskvetlind lwvgtrqqii dfmvrlksrh
//
LOCUS       WP_457594541             476 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook-length control protein FliK [Hydrogenimonas sp.].
ACCESSION   WP_457594541
VERSION     WP_457594541.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Aizawa,S.
  TITLE     Mystery of fliK in length control of the flagellar hook
  JOURNAL   J Bacteriol 194 (18), 4798-4800 (2012)
   PUBMED   22797757
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Mizuno,S., Amida,H., Kobayashi,N., Aizawa,S. and Tate,S.
  TITLE     The NMR structure of FliK, the trigger for the switch of substrate
            specificity in the flagellar type III secretion apparatus
  JOURNAL   J Mol Biol 409 (4), 558-573 (2011)
   PUBMED   21510958
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Waters,R.C., O'Toole,P.W. and Ryan,K.A.
  TITLE     The FliK protein and flagellar hook-length control
  JOURNAL   Protein Sci 16 (5), 769-780 (2007)
   PUBMED   17456739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13396646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     gene            1..476
                     /gene="fliK"
     Protein         1..476
                     /product="flagellar hook-length control protein FliK"
                     /GO_component="GO:0009424 - bacterial-type flagellum hook
                     [Evidence IEA]"
                     /GO_process="GO:0044780 - bacterial-type flagellum
                     assembly [Evidence IEA]"
                     /calculated_mol_wt=53303
     Region          242..>429
                     /region_name="FliK"
                     /note="Flagellar hook-length control protein FliK [Cell
                     motility]; COG3144"
                     /db_xref="CDD:442378"
     Region          367..429
                     /region_name="Flg_hook"
                     /note="Flagellar hook-length control protein FliK;
                     pfam02120"
                     /db_xref="CDD:460451"
ORIGIN      
        1 maslaltpll sllkemkmet ggpsvserdp glfkellqll qqsdpdpeav talmerletd
       61 gsspakrelp ltkekesfep vhikigegve rlpargdets serepppife lergerpktk
      121 egspppersl sgsgerifha ryasyssler kmedleavht irssrslkei irhaedfglt
      181 itdlkidrqk ekkstvppdt kkmplpspai lqrtehlsqs aaaliqqper rekgerstpk
      241 leavptlrtl laepkaevkg ekerlqkaen tapqkqksdf arllsglevl vkadkpstke
      301 elsirpttet dgvsapppad gdpeadfvdp lhtetkmkat ehltqkivea rstlrhfaqs
      361 lqeqvenykp pftrmqlsld pkelgnvevt lvsrgnnlhi qvhsnptaig imathgqelk
      421 sqlvsmgftd vqmqfnmnqq qqqqqrrgen ftgqytetee fselyesldl ivpyyv
//
LOCUS       WP_457594737             303 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Hydrogenimonas sp.].
ACCESSION   WP_457594737
VERSION     WP_457594737.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..303
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35082
     Region          <109..303
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          220..303
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meslffnigd krykttplye kgeehitrvd isngivffdi flkegkprsf eirnldrmvv
       61 isvvkegafs vfdniggrkf vceedearif cssrqdftlt ieakksdifv lfiadfflkr
      121 ylslnknepi dflyekiqge vgvelidtkp ldalslhlid kiidtrlqqr mhsitcehnv
      181 iefmihrfsl iclrdedidp delqialkaq kyllnhfvnp ptiphlahic atnetklkra
      241 fkkvfkttvg gyirklrlek anlllkdrvl sigevakevg yshqgyfgrl ffeaygiypk
      301 dlk
//
LOCUS       WP_457594760             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Hydrogenimonas sp.].
ACCESSION   WP_457594760
VERSION     WP_457594760.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..360
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39887
     Region          3..>290
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          165..358
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mirtffalva keligffrsw glvaivlysf tldiyitgag iemqakniav gyvdetgggm
       61 srkilsrlhm pefqkpvrfd srealsqsiy nreimvglif esdfekslkk rgtaqldlll
      121 dsvaatqsfq alqylqnill eyatfdipve lkihklfnpn attsqfmama emlsvitllg
      181 viltaavfvr ekengtweim llmpidprli ilaksfsqvl vimggvviat gailfgvfdv
      241 pingsifaff llsffyafts agiglfvaav sksmlqvaql silimmplif lsgawtpiha
      301 mhpllqklsl lsplryyieg sesiffrgta fadlggyfag vvilgsvlyf ygfrkigrlf
//
LOCUS       WP_457595063             285 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Hydrogenimonas sp.].
ACCESSION   WP_457595063
VERSION     WP_457595063.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31774
     Region          77..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          198..279
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtvtvpnyfl qekpesilsl sqglylkras asvrshrvrn tmhgllvvle gskrldtads
       61 sveleapcga ffaqgnyfvs rnmrtyrala lyfddafaqs llkewsgeeg asegsavsva
      121 vplrqesaal hlaealwrda gggaevpapl lrlrtktlfm ellaidpagv agflhrivag
      181 rrgrfvkile enldivenvg dmqrllrmsp ahlhrrfmqe lgippkrwlt arrlekgaal
      241 llgsdrevaq iaaecgyatp swfiaafkry ygltplqyrr ekrhf
//
LOCUS       WP_457595142             431 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Hydrogenimonas sp.].
ACCESSION   WP_457595142
VERSION     WP_457595142.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 431)
  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 431)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..431
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49397
     Region          <48..239
                     /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          74..102
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(75,78..79,82..83,85,109,112..113,116..117,119..120,
                     143,146..147,150..151,154)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <78..419
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          107..137
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..166
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          175..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msrylltila lllllagcsq ksgphpeaaq kksayrtfaq endyiihaly ykehkayara
       61 ytlfkelykk tsnpeyllea vkllirlkey aqarnelatl iekdpqksey yrllaitnik
      121 lgkkkealka anralqldpd nlgnadmias ihmmdgesek ayevykayyd rhhddtslir
      181 matilfhklg erkkaielle thskiigcse gvclflaeiy rqgndldnla svyarlyeat
      241 gkseyaqkaa eiytyekeye kaiaileash aderlllavl kqsrafkkal klakrlydet
      301 ldpiwqaeyg vlmyeaaekk ddpkllervv dalssafdkg vdeplylnyl gyllidhdld
      361 irrgmalver alkkspdspf yldslawgyy klgncdkarq imkkvvakmg lddpeikahw
      421 ekinqcrskk k
//
LOCUS       WP_457595393             305 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Hydrogenimonas sp.].
ACCESSION   WP_457595393
VERSION     WP_457595393.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..305
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35325
     Region          98..305
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          222..305
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meslffnigd rrykitrlye kgddhitrvd isngivffdi rlkkghtarr fdirnldrmv
       61 vlsvvkegrf tledrlgggv lrsrrdtsdi ycssrqdftl tleeggesdi fvlciadffl
      121 krylslnpne pidflyekiq gdigvalvdt kpldalslhl vekiidtrlq ermhsirceh
      181 nvielmihrf glidmvdesi dpdelqtarr aqryllnhfv spptipelar lcatnetklk
      241 rafkkvygtt iggyirklrl eranrllkdr lltigevare vgyshqgyfg rlffeaygiy
      301 pkdlk
//
LOCUS       WP_457595770             436 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Hydrogenimonas sp.].
ACCESSION   WP_457595770
VERSION     WP_457595770.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..436
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47422
     Region          2..409
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mpivariltl svvvgvvtgl aisffvlaar wlaemlfagh tlhtisslpw wylylvptla
       61 ifvvnwliek dagvreygvs eianavagne kfitlkglll kivasvlslg sgfavgnegp
      121 saaigamiay kvnalfkipq rfvrlvlsig assgiaavfv spitgivfav eniayefvqr
      181 ligpiilgav iafgvayqfi epiifrysvg rifqseyifa sllfvpvmlf flflylslkn
      241 rllhgfnaml lkrtgrwrnl ifallgglvt gtllnvapfa vfsghevvma lindklhisv
      301 ililmvvllr ifattvsiya navgglflpl msigaligyg ygellklngy gvepysfaai
      361 gaavfmgvvm rlpltavvla leitydynvi vptgiavila tyfanlnfni rklkatdiki
      421 sieekecqye kesres
//
LOCUS       WP_457596026             253 aa            linear   BCT 27-JAN-2026
DEFINITION  rod shape-determining protein MreC [Hydrogenimonas sp.].
ACCESSION   WP_457596026
VERSION     WP_457596026.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Martins,A., Contreras-Martel,C., Janet-Maitre,M., Miyachiro,M.M.,
            Estrozi,L.F., Trindade,D.M., Malospirito,C.C., Rodrigues-Costa,F.,
            Imbert,L., Job,V., Schoehn,G., Attree,I. and Dessen,A.
  TITLE     Self-association of MreC as a regulatory signal in bacterial cell
            wall elongation
  JOURNAL   Nat Commun 12 (1), 2987 (2021)
   PUBMED   34016967
  REMARK    Erratum:[Nat Commun. 2022 Jan 11;13(1):329. doi:
            10.1038/s41467-022-28008-1. PMID: 35017540]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..253
                     /product="rod shape-determining protein MreC"
                     /GO_component="GO:0005618 - cell wall [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=28294
     Region          <128..253
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional"
                     /db_xref="CDD:237560"
ORIGIN      
        1 mgprfytklp wllaalaaaa layyspavrt ffyafsvtve esyrrletsi srayerhmaq
       61 aetiarfere rraferellr crrdaaayra ladslgvrda nlsaiavrag gyaklgnfqq
      121 vwlepfesyd ptrnygvvrg gyavgivvee rgmplmilgg drgctfavyv gdarapgiat
      181 grdarhmvvr yipewmkvgp gdevftsgld rlfpmgipvg rvlsirkmqg fkdavielyg
      241 dtlhpdfvwv vsr
//
LOCUS       WP_457596189             224 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Hydrogenimonas sp.].
ACCESSION   WP_457596189
VERSION     WP_457596189.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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) (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 11459734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..224
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24437
     Region          52..224
                     /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"
     Region          149..223
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 meeknndldd liirsdkssn lkklllaaav lllvliviil vtksfvqsge kpqssvilpp
       61 epkvekraqa pkeplfeevp iqeeapartv pdkeaaspkp tpvetvspkp epapkpapkp
      121 apkqaaekpa pkkaaaakpa pkpeaapkgr yyiqvgaffr yppdrkflks iekegfgyti
      181 vegvkngtrf kkvlvgpyps rsaaakdlar ikrrinqnay vlkr
//
LOCUS       WP_457596315             259 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Hydrogenimonas sp.].
ACCESSION   WP_457596315
VERSION     WP_457596315.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..259
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27467
     Region          1..258
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msdilkigky eftsrlivgs gkypdfattr datlasgaem itvavrrvni tnpdeenlmd
       61 yfkdtdvkfl pnsagcttae eaitlfrltr eatgidlikl evigdtqktl ypdvietika
      121 cevlakdgft imaytnddpi iakrleeaga aavmplaapi gsglgvqnkf nvvfvkeavk
      181 vpvivdagig qasdaaaame lgadgvltnt aiaqaknpiq maeamkhavv agrmsylagr
      241 ipkrpyatas sptdgmiqf
//
LOCUS       WP_457596951             378 aa            linear   BCT 27-JAN-2026
DEFINITION  McrC family protein [Hydrogenimonas sp.].
ACCESSION   WP_457596951
VERSION     WP_457596951.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..378
                     /product="McrC family protein"
                     /GO_function="GO:0032067 - type IV site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=45297
     Region          2..374
                     /region_name="McrC"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, regulatory subunit McrC [Defense mechanisms];
                     COG4268"
                     /db_xref="CDD:443409"
ORIGIN      
        1 mvylyeneai hdeklhkait etpdlhahfr ndfgriypdn rcgflswdge eyfivpkivp
       61 edveanldif iymllyayev elsneslatf enrrerlfel fvrlfadrll delkrgvhre
      121 yrtmrenlkv lrgkyliern frnfhhqnly cefdefsmdn qlnrlflyai htlerfssya
      181 nlsrcetmld evsdvrfdpe rveisfdrln drfrhsyela tmllrklvpm prnsgersfa
      241 flfdmgevfe kfvarlvkai epqartqvrr hfgslhlkpd ivienrmiid tkyklvknre
      301 ellaadkyql yayginfgir dtmllyprhl edvkedmmlg egenavklkm rsldlrfegg
      361 yeeyiqevrs rikeaiya
//
LOCUS       WP_457597530             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Hydrogenimonas sp.].
ACCESSION   WP_457597530
VERSION     WP_457597530.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39909
     Region          1..313
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          164..357
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mkafwalvlk ellsffrswg lvavvlysft ldiyiagkgi elqaknvsvg yvdytgggvs
       61 rkilshlhap qfrdprpfts qkalynairn reimvgllfd sdfeknldag rpatldvlld
      121 aisatqsfqa lqylqnilld fskadfpvsl kihklfnpna rtewfmalae mlsnitllgv
      181 iltaavfvre kengtwdlml lmpldsrmvi laksfsqvlv lmfgvvlatg lvlfgafdtp
      241 ingslaaffl lsffysftsa giglfvaavs ksmlqvaqla ilimmplifl sgawtpiham
      301 spwlqklsli splryyiegs esiffrgtpw adlwpyfagv ivlggalyly gfrkigrlf
//
LOCUS       WP_457597537             112 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Hydrogenimonas
            sp.].
ACCESSION   WP_457597537
VERSION     WP_457597537.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..112
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11912
     Region          9..111
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mgkygqklae iekligelkk eapeqigafh rfmaavesps aldakqkeli nlalavaaqc
       61 ewcialhtkg alqagatrqe vvdaamqavl mhggpalmym tpvmealeef gs
//
LOCUS       WP_457597826             112 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Hydrogenimonas
            sp.].
ACCESSION   WP_457597826
VERSION     WP_457597826.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..112
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12241
     Region          3..110
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mgiyteklee iksligrlqk etpdqisafh lfmtavekps aldrkhkelv nvalavaaqc
       61 ewcialhvkg aldagakree imdaamqavl mhggpalmym tpvekaldef ms
//
LOCUS       WP_457598196             471 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Hydrogenimonas sp.].
ACCESSION   WP_457598196
VERSION     WP_457598196.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..471
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50873
     Region          15..411
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mirkhvteqt aiffsvtkwv vlssvvgvmi gaivtlflki lqvaeggrae lpfpyfyllp
       61 lalfltvwiv rtfapsaegh gtekvieavh krhgkiniav ipvklfatvl tifsggsvgk
      121 egpgaqigag aaswlsdmlk fskedrkklv icgisagfas vfgtpiagai fgvevliigv
      181 ilydvllpsf iagfaaftta qflgieytyf dirfyqnvtl dlplillvva aglffgfvsd
      241 lvvtsvalvh rmirkiplhp ylvafaggvl lvamallfge rylglgleti kdtlnpdpsf
      301 srdlpwyafl lktaftsltl gvggsggiit pifyigatsg hlfgqlvgge hialfaalgf
      361 vsvlagstnt piaatimave lfgleiahya alsavisfli tghrsvfasq ilamkkseml
      421 evkvgevieh aevdleesei grirnvreri rrrreklkek ragrglsrke k
//
LOCUS       WP_457598236             431 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Hydrogenimonas sp.].
ACCESSION   WP_457598236
VERSION     WP_457598236.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 431)
  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 431)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..431
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49441
     Region          <48..239
                     /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          74..102
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(75,78..79,82..83,85,109,112..113,116..117,119..120,
                     143,146..147,150..151,154)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <78..419
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          107..137
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..166
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          175..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msrylltila lllllagcsq ksgphpeaaq kkstyrtfaq endyiihaly ykehkayara
       61 ytlfkelykk tsnpeyllea vkllirlkey aqarnelatl iekdpqksey yrllaitnik
      121 lgkkkealka anralqldpd nlgnadmias ihmmdgesek ayevykayyd rhhddtslir
      181 matilfhklg erkkaielle thskiigcse gvclflaeiy rqgndldnla svyarlyeat
      241 gkseyaqkaa eiytyekeye kaiaileash aderlllavl kqsrafkkal klakrlydet
      301 ldpiwqaeyg vlmyeaaekk ddpkllervv dalssafdkg vdeplylnyl gyllidhdld
      361 irrgmalver alkkspdspf yldslawgyy klgncekarq imkkvvakmg lddpeikahw
      421 ekinqcrskk k
//
LOCUS       WP_457598359             285 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Hydrogenimonas sp.].
ACCESSION   WP_457598359
VERSION     WP_457598359.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
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   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31581
     Region          77..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          198..279
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtvtvpnyfl qekpesilsl sqglylkras asvrshrvrn tmhgllvvle gskrldtagg
       61 sveleapcga ffaqgnyfvs rnmrtyrala lyfddafaqs llkewggeeg aseggavsva
      121 vplpresaal hlaealwrda gggaevpapl lrlrtktlfm ellaidpagv agflhrivag
      181 rrgrfvkile enldivenvg dmqrllrmsp ahlhrrfmqe lgippkrwlt arrlekgaal
      241 llgsdrevaq iaaecgyatp swfiaafkry ygvtplqyrr ekrhf
//
LOCUS       WP_457598500             261 aa            linear   BCT 27-JAN-2026
DEFINITION  rod shape-determining protein MreC [Hydrogenimonas sp.].
ACCESSION   WP_457598500
VERSION     WP_457598500.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Martins,A., Contreras-Martel,C., Janet-Maitre,M., Miyachiro,M.M.,
            Estrozi,L.F., Trindade,D.M., Malospirito,C.C., Rodrigues-Costa,F.,
            Imbert,L., Job,V., Schoehn,G., Attree,I. and Dessen,A.
  TITLE     Self-association of MreC as a regulatory signal in bacterial cell
            wall elongation
  JOURNAL   Nat Commun 12 (1), 2987 (2021)
   PUBMED   34016967
  REMARK    Erratum:[Nat Commun. 2022 Jan 11;13(1):329. doi:
            10.1038/s41467-022-28008-1. PMID: 35017540]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..261
                     /product="rod shape-determining protein MreC"
                     /GO_component="GO:0005618 - cell wall [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=29592
     Region          1..250
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional"
                     /db_xref="CDD:237560"
ORIGIN      
        1 mnrfnrkitl lilfgivvlf slysasvrtf ftaftstvrs ayldlthsfd tawrnhlrqi
       61 rtierlqker dalekrllac qsdaasfrsm qealkimpet natfeavrpe gyamignfqq
      121 lwldrfenyd pmknygvirn gyavgivvek klhplmilag dpecmfavyv gevrapgiam
      181 gtdarhmvvk yipqwlklkp gdevytsgld hifppgipvg rllstqkmqg fqnayielyg
      241 dtlhpdfvwv tapargvesd s
//
LOCUS       WP_457598739             476 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook-length control protein FliK [Hydrogenimonas sp.].
ACCESSION   WP_457598739
VERSION     WP_457598739.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Aizawa,S.
  TITLE     Mystery of fliK in length control of the flagellar hook
  JOURNAL   J Bacteriol 194 (18), 4798-4800 (2012)
   PUBMED   22797757
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Mizuno,S., Amida,H., Kobayashi,N., Aizawa,S. and Tate,S.
  TITLE     The NMR structure of FliK, the trigger for the switch of substrate
            specificity in the flagellar type III secretion apparatus
  JOURNAL   J Mol Biol 409 (4), 558-573 (2011)
   PUBMED   21510958
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Waters,R.C., O'Toole,P.W. and Ryan,K.A.
  TITLE     The FliK protein and flagellar hook-length control
  JOURNAL   Protein Sci 16 (5), 769-780 (2007)
   PUBMED   17456739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13396646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     gene            1..476
                     /gene="fliK"
     Protein         1..476
                     /product="flagellar hook-length control protein FliK"
                     /GO_component="GO:0009424 - bacterial-type flagellum hook
                     [Evidence IEA]"
                     /GO_process="GO:0044780 - bacterial-type flagellum
                     assembly [Evidence IEA]"
                     /calculated_mol_wt=53202
     Region          242..>429
                     /region_name="FliK"
                     /note="Flagellar hook-length control protein FliK [Cell
                     motility]; COG3144"
                     /db_xref="CDD:442378"
     Region          367..429
                     /region_name="Flg_hook"
                     /note="Flagellar hook-length control protein FliK;
                     pfam02120"
                     /db_xref="CDD:460451"
ORIGIN      
        1 maslaltpll sllkemkmet ggpsvserdp glfkellqll qqsdpdpeav talmerletd
       61 ssspakrelp lakekesfep vhikigegve rlpargdets serepppife lergerpktk
      121 egssppersl sgsgerifha rytsyssler kmedleavht irssrslkei ihhaedfglt
      181 itdlkidrqk ekksavppda kkmplpspai lqrtehlsqs aaaliqqper rekgerstpk
      241 leavptlrtl laepkaeakg ekerlqkaen tapqkqksdf arllsglevl vkadkpstke
      301 elsirpttet dgvsapppad gdpeadfvdp lhtetkmkat ehltqkivea rstlrhfaqs
      361 lqeqvenykp pftrmqlsld pkelgnvevt lvsrgnnlhi qvhsnptaig imathgqelk
      421 sqlvsmgftd vqmqfnmnqq qqqqqrrgen ftgqytetde fselyesldl ivpyyv
//
LOCUS       WP_457598872             261 aa            linear   BCT 27-JAN-2026
DEFINITION  rod shape-determining protein MreC [Hydrogenimonas sp.].
ACCESSION   WP_457598872
VERSION     WP_457598872.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Martins,A., Contreras-Martel,C., Janet-Maitre,M., Miyachiro,M.M.,
            Estrozi,L.F., Trindade,D.M., Malospirito,C.C., Rodrigues-Costa,F.,
            Imbert,L., Job,V., Schoehn,G., Attree,I. and Dessen,A.
  TITLE     Self-association of MreC as a regulatory signal in bacterial cell
            wall elongation
  JOURNAL   Nat Commun 12 (1), 2987 (2021)
   PUBMED   34016967
  REMARK    Erratum:[Nat Commun. 2022 Jan 11;13(1):329. doi:
            10.1038/s41467-022-28008-1. PMID: 35017540]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..261
                     /product="rod shape-determining protein MreC"
                     /GO_component="GO:0005618 - cell wall [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=29597
     Region          1..250
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional"
                     /db_xref="CDD:237560"
ORIGIN      
        1 mnrfnrkitl lilfgivvlf slysasvrtf ftaftstvrs ayldlthsfd tawrnhlrqi
       61 rtierlqner dalekrllac qsdaasfrsm qealkimpet natfeavrpe gyamignfqq
      121 lwldrfenyd pmknygvirn gyavgivvek klrplmilag dpecmfavyv gevrapgiam
      181 gtdarhmvvk yipqwlklkp gdevytsgld hifppgipvg rllstqkmqg fqnayielyg
      241 dtlhpdfvwv tapargvesd s
//
LOCUS       WP_457599116             431 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Hydrogenimonas sp.].
ACCESSION   WP_457599116
VERSION     WP_457599116.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 431)
  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 431)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     Protein         1..431
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49427
     Region          <48..239
                     /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          74..102
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(75,78..79,82..83,85,109,112..113,116..117,119..120,
                     143,146..147,150..151,154)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <78..419
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          107..137
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..166
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          175..200
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msrylltila lllllagcsq ksgphpeaaq kkstyrtfaq endyiihaly ykehkayara
       61 ytlfkelykk tsnpeyllea vkllirlkey aqarnelatl iekdpqksey yrllaitnik
      121 lgkkkealka anralqldpd nlgnadmias ihmmdgesek ayevykayyd rhhddtslir
      181 matilfhklg erkkaielle thskiigcse gvclflaeiy rqgndldnla svyarlyeat
      241 gkseyaqkaa eiytyekeye kaiaileash aderlllavl kqsrafkkal klakrlydet
      301 ldpiwqaeyg vlmyeaaekk ddpkllervv dalssafdkg vdeplylnyl gyllidhdld
      361 irrgmalver alkkspdspf yldslawgyy klgncdkarq imkkvvakmg lddpeikahw
      421 ekinqcrskk k
//
LOCUS       WP_457599353             476 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar hook-length control protein FliK [Hydrogenimonas sp.].
ACCESSION   WP_457599353
VERSION     WP_457599353.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenimonas sp.
  ORGANISM  Hydrogenimonas sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Hydrogenimonadaceae; Hydrogenimonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Aizawa,S.
  TITLE     Mystery of fliK in length control of the flagellar hook
  JOURNAL   J Bacteriol 194 (18), 4798-4800 (2012)
   PUBMED   22797757
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Mizuno,S., Amida,H., Kobayashi,N., Aizawa,S. and Tate,S.
  TITLE     The NMR structure of FliK, the trigger for the switch of substrate
            specificity in the flagellar type III secretion apparatus
  JOURNAL   J Mol Biol 409 (4), 558-573 (2011)
   PUBMED   21510958
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Waters,R.C., O'Toole,P.W. and Ryan,K.A.
  TITLE     The FliK protein and flagellar hook-length control
  JOURNAL   Protein Sci 16 (5), 769-780 (2007)
   PUBMED   17456739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13396646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Hydrogenimonas sp."
                     /db_xref="taxon:2231112"
     gene            1..476
                     /gene="fliK"
     Protein         1..476
                     /product="flagellar hook-length control protein FliK"
                     /GO_component="GO:0009424 - bacterial-type flagellum hook
                     [Evidence IEA]"
                     /GO_process="GO:0044780 - bacterial-type flagellum
                     assembly [Evidence IEA]"
                     /calculated_mol_wt=53183
     Region          242..>429
                     /region_name="FliK"
                     /note="Flagellar hook-length control protein FliK [Cell
                     motility]; COG3144"
                     /db_xref="CDD:442378"
     Region          367..429
                     /region_name="Flg_hook"
                     /note="Flagellar hook-length control protein FliK;
                     pfam02120"
                     /db_xref="CDD:460451"
ORIGIN      
        1 maslaltpll sllkemkmet ggpsvserdp glfkellqll qqsdpdpeav talmerletd
       61 gsspakrelp ltkekesfep vhikigegve rlpargdets serepppife lergekpktk
      121 egssppersl sgsgerifha ryasyssler kmedleavht irssrslkei irhaedfglt
      181 itdlkidrqk ekksavppda kkmplpspai lqrtehlsqs aaaliqqper rekgerstpk
      241 leavptlrtl laepkaeakg ekerlkkaen tapqkqksdf arllsglevl vkadkpstke
      301 elsirpttet dgvsappptd gdpeadfvdp lltetkmkat ehltqkivea rstlrhfaqs
      361 lqeqvenykp pftrmqlsld pkelgnvevt lvsrgnnlhi qvhsnptaig imathgqelk
      421 sqlvsmgftd vqmqfnmnqq qqqqqrrgen ftgqytetee fselyesldl ivpyyv
//
LOCUS       WP_457599747             157 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Hydrogenivirga sp.].
ACCESSION   WP_457599747
VERSION     WP_457599747.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     gene            1..157
                     /gene="rimP"
     Protein         1..157
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17939
     Region          6..155
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mnvdstevsk kvrelvepiv nslgfrlfdv efkpergwvl rviidkkggv tirdceevsk
       61 risglldved iipfsymlei sspgltrsle kpehyeffkg rlvkvvlrep vsgkreatgy
      121 vkdvregiit lrerekgeel hipfsaiakg rleperw
//
LOCUS       WP_457600337             278 aa            linear   BCT 27-JAN-2026
DEFINITION  formate dehydrogenase accessory protein FdhE [Hydrogenivirga sp.].
ACCESSION   WP_457600337
VERSION     WP_457600337.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18656952
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     Protein         1..278
                     /product="formate dehydrogenase accessory protein FdhE"
                     /calculated_mol_wt=31681
     Region          3..274
                     /region_name="FdhE"
                     /note="Formate dehydrogenase maturation protein FdhE
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG3058"
                     /db_xref="CDD:442292"
ORIGIN      
        1 mnvfkqkere favarvrrlr dkfpetvqil dflervlefq stlienlseg gapiklsgae
       61 arikagkpal nlgsvdldif vkhvppfldl ieehgteeir egvrelrals rdklaslfkd
      121 ffedkdvgsl irlvvigvaq pvlyasvgdw efkhewwlrn tcplcgskps vsflmdteew
      181 egarflrcgl cltdwlyprt qcvncgnned dklsyfveqg igyielqtcs eckryiklid
      241 mrkdglavpd vddvaslsld lwvqsrgytk vernildl
//
LOCUS       WP_457600467             541 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Hydrogenivirga sp.].
ACCESSION   WP_457600467
VERSION     WP_457600467.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 541)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 541)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     Protein         1..541
                     /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=58665
     Region          6..535
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(50,53,373,376..377)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 meqfigyiiv fgivilfmai aiynrateaa efyvagrrip afwngmavaa dwmsaasfis
       61 magalyalgy dglayimgwt ggyvllalli apylrkfgky tvpdfiaery esnfarlval
      121 itaiiisfty mvgqvagvgi imgrlfgvsf elgiaigmvi iiattvlggm ksitwtqvaq
      181 yivlitayll pvsilatqwf gvplpqflyg qvlqnvvele tqygisphyv epfvkfnlaq
      241 flaltfvlma gtaalphvlm rffttpsvrd arisagwalf fiailyltap ayaafsrfvi
      301 lkdvvgkpid qlpawaqkwa etglfkvidk ngdgiiqwae lnihrdivvl atpeiaglaa
      361 vvgffvmagg laaalstadg lllviaaavs ndlyakmidp napekrvvkl gkiavaiagv
      421 iggfiaaqki afivqivawa fslatasffp alvlgvfwkr lnrqgaiagl vvgllvtiay
      481 iylnkyqgvs lwgiqhtasg lfgiianliv tivvtmvtpp pseriqkmve elrypkkihe
      541 v
//
LOCUS       WP_457600696             267 aa            linear   BCT 27-JAN-2026
DEFINITION  rod shape-determining protein MreC [Hydrogenivirga sp.].
ACCESSION   WP_457600696
VERSION     WP_457600696.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Martins,A., Contreras-Martel,C., Janet-Maitre,M., Miyachiro,M.M.,
            Estrozi,L.F., Trindade,D.M., Malospirito,C.C., Rodrigues-Costa,F.,
            Imbert,L., Job,V., Schoehn,G., Attree,I. and Dessen,A.
  TITLE     Self-association of MreC as a regulatory signal in bacterial cell
            wall elongation
  JOURNAL   Nat Commun 12 (1), 2987 (2021)
   PUBMED   34016967
  REMARK    Erratum:[Nat Commun. 2022 Jan 11;13(1):329. doi:
            10.1038/s41467-022-28008-1. PMID: 35017540]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     Protein         1..267
                     /product="rod shape-determining protein MreC"
                     /GO_component="GO:0005618 - cell wall [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=30594
     Region          21..266
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional"
                     /db_xref="CDD:237560"
ORIGIN      
        1 mtgrrfhlls vlvvvlglvl ffsdfsrfsy vravvkvvnt fvapliefke ntvaelreel
       61 taymhfvnte kenirlrrkl nslllmekel naclmeleal hnklkvpmsf krlryrvsrv
      121 iyydpsgfdl fvvieggedk gykegdlvvt esyvvgviet vfgstsrvit pfndkfsssa
      181 vvgtgpkkyi yrggypkgkl lhvsvedkvs kgeevymvdi kekvppfllg ridrvsrgkd
      241 pffkevsvkp evdprteeyv fvirrkr
//
LOCUS       WP_457600862             284 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF58 domain-containing protein [Hydrogenivirga sp.].
ACCESSION   WP_457600862
VERSION     WP_457600862.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1001782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     Protein         1..284
                     /product="DUF58 domain-containing protein"
                     /calculated_mol_wt=31678
     Region          115..>282
                     /region_name="YeaD2"
                     /note="Uncharacterized conserved protein, DUF58 family,
                     contains vWF domain [Function unknown]; COG1721"
                     /db_xref="CDD:441327"
ORIGIN      
        1 mrvkvkrsga ifigvtvflg vaaantgnnl lyilvssmla lmlisgtssi lnlkgielrl
       61 ipppevfanr rtpfrliark rgrlpsflir vssdidetlf pildsrerds vlhllfsrrg
      121 avekvrlvis sdfplgmfvr svevelevrf tvfpepiktp ltfvssgrer egssprftpt
      181 kgydevrgik dysgesmkli hwklsakrdr llvkemvgee repvilslns vsgdietrls
      241 klaylaidli drgypvglel dgkevpprgg nsqkliilre laly
//
LOCUS       WP_457601053             427 aa            linear   BCT 27-JAN-2026
DEFINITION  PDC sensor domain-containing protein [Hydrogenivirga sp.].
ACCESSION   WP_457601053
VERSION     WP_457601053.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Cheung,J., Bingman,C.A., Reyngold,M., Hendrickson,W.A. and
            Waldburger,C.D.
  TITLE     Crystal structure of a functional dimer of the PhoQ sensor domain
  JOURNAL   J Biol Chem 283 (20), 13762-13770 (2008)
   PUBMED   18348979
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1005487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     Protein         1..427
                     /product="PDC sensor domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49192
     Region          292..394
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
ORIGIN      
        1 mkaeeislld isisiptvph dlslkelkgi fdelgiykyl tvlkgnspvg lvyrdkveky
       61 snekliagdi atlccrlknt smkkeslsgi fdilpldrep viitdkrgty lgvltydtvl
      121 hyvthhrehv lpivqrvhss igkkeylcif glknlgnfks vfgteklesl qkifledvkd
      181 ffegditgvp ekgelwivtg kppakedike lfrefhreyt llfgefqhvh iygfcldmsl
      241 idseeklykl keelrdrtak iegsvfivhs lqptlilhdp tkqklitnik kkilsdfkdi
      301 vehvrsspkd mwehilydif eqypyfelfy iisekglqit nnivnpkvdy fvaqgkkgtd
      361 rsekpyfrea mkegsfisdv ylskatddfc itvseafsye gktyilagdi nfrqihrlvk
      421 nfkeatv
//
LOCUS       WP_457601312             849 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Hydrogenivirga sp.].
ACCESSION   WP_457601312
VERSION     WP_457601312.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp.
  ORGANISM  Hydrogenivirga sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 849)
  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 849)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Hydrogenivirga sp."
                     /db_xref="taxon:3050380"
     Protein         1..849
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=97803
     Region          232..>725
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          492..520
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(493,496..497,500..501,503,527,530..531,534..535,
                     537..538,561,565..566,569..570,573)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          496..783
                     /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          525..555
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          598..626
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          633..658
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mwkltglfsl iaflsitfga lnesislkvk vvgkileekp klippdritv srdvrpldls
       61 gelleapkgi eeprieipkg ggacgepkdk vyyraglkyy tegrlkkaeg kfldvlslqs
      121 safvpqseym lgliyaktnr ekealkffes scsaqhpfrq aaceslyale fklrgepiea
      181 qepelwkvvy eiknggevka pacegvvfkd yctyvqdfae grindeykds telrkaivli
      241 qagnfgeakl llkkhnrald rhrdvalyyl gviafregke keayryasll eisnrryaeh
      301 lylmlsgrdv lfskiayevt gakeallnsg vhsynrgnyd layaeltkag ehlfaayaai
      361 regdyerays slrkvkskdr eyylwlletl ywlgrdremd gvlaeireky telyreykgw
      421 lafkrenwke aykyfkdpyh ralalfnagr ygevikvlrd kndlrsrllk akaaismgkg
      481 alarefltee tpeeiylvgm sffiegeyak aigyferlls edslksrall riadshynlg
      541 nydrakelyk eiltfypdsp ealdatlala qielqkptkd lerlvrdfek kfpgspmitd
      601 lkyqlanlyi kegrksearr ilqellgnst yrakalikla elendpvrke ellkkamreg
      661 sgedkeratg mlmslylekk efekladfls kgdfddrkka lsiyisenie kaiklfnely
      721 eenpndeelk vkalelydkt kgkkylkiar esqnpkvrar alyllgliek kkdknkaley
      781 fvevvlsseg iqpyynrsil eavdillslk akkdasclla rldrryltkr dikkvkilkk
      841 klpkcevkk
//
LOCUS       WP_457601699             727 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601699
VERSION     WP_457601699.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..727
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84000
     Region          5..646
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mnrkedilrd lnedqleall yfdgplriia gagsgktrvl trkiaylinv lgihpsqila
       61 ltftnkaane mnervkqyvg edfdkaeist fhslcakilr veakhlgykn dfqiiddsdk
      121 kfilgeiyka hnlsaqelnf rnvittfsla knanlsadel lsklndlepe nyqtnvlivk
      181 mfeeynlmlq kqkyfdfddl iiqvnnlfnk fpaiatkwsq kydfilvdef qdtskmqyei
      241 vkklisknaq itivgdpdqt iyswrgadvn lilnfekdfs daktiilntn yrstksilna
      301 anklikynqk ryskdlvtdn segeeiefih afsveaearw vvqkinelkk kkiqlkniai
      361 fyrsnyysrs feeelikeni nykilngqkf fdrkeikdvl aflrviydss disllriint
      421 parkigevtl nkikakavee nltiyqtlir fvkeldiaye akknivdfln sinkhrhlil
      481 kgkhpftivl khflkevgyf dylnndpalk rtgeenvqel irsmetwetq nrnknladyl
      541 aeislysagd eydngtnyvt lmtvhsakgl efdnvflvgm seqifphykv llsddensle
      601 eerrlayvai trakdrlfis dsrgalninq kekkpsrfik emgidlnkfi lqtgsinldl
      661 lgetddekik einkkiipgd iishtmygeg tvlevnqdni rvkfvtsgse ktlsknhpsi
      721 rllknin
//
LOCUS       WP_457601692             902 aa            linear   BCT 27-JAN-2026
DEFINITION  cation-translocating P-type ATPase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601692
VERSION     WP_457601692.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..902
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=98723
     Region          10..891
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mdnnleqfkq ngltekevea kliefgentl tkskkvnpiv affrqfmdpm villliaaai
       61 slglaiyehi kshksqteli vsyiepaiil lvvslnsmlg ayqevksdqa vralaklnet
      121 natvkrdgiv kvipanllvp gdliilnagd visadcrile asnlavvess ltgeslavek
      181 ianfnkakds ilaqnnhllf sgtyvtngka laiveftgnk teigkinesl qnqkksstpl
      241 qdklnrlgkv fgiggivllf vslimqilln niytgvwdnw diytsslvta islavaaipe
      301 glitfttvll sigvkkmtkd kglvknllav etlgsvsiic sdktgtlten kmtvvdafyn
      361 nlllseaenk sefktlakyl tlandahinf dsknesfnev gdptetgllr faydlgiykd
      421 dllksmplls tltfdsdrkm msvlvdagdy nlmitkgapd vilkhskvnn lteieqinkn
      481 fatktyrvla vgikkvakeq ktinfadesn ldfvglvamv dpprknvaqs iekaklagvk
      541 tvmitgdhld takaiasnlg iynendlait glelsqmsdq elkekvklis vyarvnptdk
      601 lrivkawqsh nkvvamtgdg vndapalkas digcamgitg tdvskqaadl ilvddnfnti
      661 vnsiqngrli fdkikvviln llvsslteil vmligmvaff fayknhfnte fyifgasqll
      721 winllthgip aialglvdsg knvmnrppyd kkeslfargm gwnlifqsvv lstltliayv
      781 lgaefaiqnn lsvlvtastt afitmgvaas lnsinlmsdk sifisslkky wlvwlaalss
      841 tfltlfvvlv pdislvfrms gnlyqnsyll wmpillglgl tlanelwkli kltmkvyqsq
      901 ka
//
LOCUS       WP_457601705             513 aa            linear   BCT 27-JAN-2026
DEFINITION  phospho-sugar mutase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601705
VERSION     WP_457601705.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Shackelford,G.S., Regni,C.A. and Beamer,L.J.
  TITLE     Evolutionary trace analysis of the alpha-D-phosphohexomutase
            superfamily
  JOURNAL   Protein Sci 13 (8), 2130-2138 (2004)
   PUBMED   15238632
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..513
                     /product="phospho-sugar mutase"
                     /EC_number="5.4.2.-"
                     /GO_function="GO:0016868 - intramolecular
                     phosphotransferase activity [Evidence IEA]"
                     /calculated_mol_wt=59076
     Region          4..505
                     /region_name="PGM2"
                     /note="This CD includes PGM2 (phosphoglucomutase 2) and
                     PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2
                     is thought to be a phosphopentomutase that catalyzes the
                     conversion of the nucleoside breakdown products,
                     ribose-1-phosphate and...; cd05799"
                     /db_xref="CDD:100092"
     Site            order(7,9,12,106..108,116,267,269,271..272,318,339..341,
                     361,363,365,474,476..478,483)
                     /site_type="active"
                     /db_xref="CDD:100092"
     Site            order(9,106,272,318,339,341,361,363,365,474,476..478,483)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100092"
     Site            order(106,267,269,271)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100092"
ORIGIN      
        1 mqkldfgtag irgilgkepy qlnyfhvarv idayaqylkv qygkkasvvi grdnrkmscs
       61 fsklaayild syqikvwyvk diaatpfisy ltkikkanga inftashnpk nyngiklynh
      121 fgaqclpeei daikkyfkdy elyqtnfklp qninlahlkn lnwtskrdld nyvtevgnlg
      181 iniipnvkia ysplhgtgsk impllltklg ftkvnnqfvn aflspeqmki drhfktidyp
      241 npeyaeayny vkklglkhqa dllllsdpds drvglsvwng keyvnlngne tallifyfln
      301 qtnfyknknd lflvysfvss nlpsliatkh niksievptg fkwiakiine nkqdnfafgf
      361 eesygslins diandkdafq sialiikmas yyknqnlnll dvlnsiyeef gyvssetlnf
      421 diddnfdlnq tidkfinlnl keefniedyr nrndfmksqm iklkfndnsw iamrpsgtep
      481 kikfyifafg kneneatkkf nnfkiqisql mnk
//
LOCUS       WP_457601708             230 aa            linear   BCT 27-JAN-2026
DEFINITION  nuclease-related domain-containing protein [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601708
VERSION     WP_457601708.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  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
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..230
                     /product="nuclease-related domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26706
     Region          45..158
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
ORIGIN      
        1 mnfsklslem rwglilgsig mfiviilliv lyfwlklrkk qivskgvdfe rqinndlkny
       61 akaknfhfie ggwykyntnk ifnldgllit pfgvfvieik yllgklsgei enqeltltdn
      121 knkkrkvknp fkqnyrhiih lydlakfnfp ayslvimpng ttwnlneens wsliatenty
      181 haliedvint tkidgnfisk dqkkallyal knatvdsdeg ikkvrefqne
//
LOCUS       WP_457601720             413 aa            linear   BCT 27-JAN-2026
DEFINITION  NYN domain-containing protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601720
VERSION     WP_457601720.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..413
                     /product="NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48291
     Region          6..123
                     /region_name="PIN_LabA-like_N_1"
                     /note="uncharacterized subfamily of N-terminal LabA-like
                     PIN domains; cd11297"
                     /db_xref="CDD:350237"
ORIGIN      
        1 menkkialli dydnfndpkh ipllledlqe kkfniiskva yyslkasdkn kneiftkynl
       61 epksvavygk sknasdlila mdamnlmnqd fidgiciass dndfapvihr iksngkialg
      121 agderitedy iklfddfinm akidknnqns tlnnqqndnl sklfikidqi indlrsdsne
      181 eyvdlsqcvq ilkdnnrdfn pknygwknsk tvpffqsnlm tthydlkven kvwyikikqn
      241 nqklkkieni sdeitifktl lsklkrkdgg vefgsfirel gknshyknlp ilkkkrkfey
      301 fenkpfsdyf eidktkknsi sirvkedens dkltkkytns nsseieiykq tilnnktpem
      361 nfaafieqik knhkslsifn kkdkkwklfe qtplndyfev nkrnstvyik ikk
//
LOCUS       WP_457601729             330 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601729
VERSION     WP_457601729.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..330
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35950
     Region          1..329
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mekitvnnig althaldlmm erdksvviyg edagyeggvf ratqglqqky gvdrvwdapi
       61 sesaiagsai gaaiaglkpv ieiqfsgfsm yamgqifsna armrnrsrgt mtvpmvlrmp
      121 cgggvkaleh hseslealya hipglkvvmp stpydtkglm iaaiedpdpv vflehkrdyr
      181 afkqeipagy ykveigkasv vvpgedltvv ayghmvheti aalkllaekg ksysvevvdl
      241 rtikpldtat viesvkktgr vlvvseavey gsiatevlar vneyafddli skprrlngpd
      301 vtiplpalen yfmvdkekia tvieemldee
//
LOCUS       WP_457601739             545 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601739
VERSION     WP_457601739.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5) (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..545
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59880
     Region          19..478
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqqqetkfv aekstakkis ffsamlivig gsigagiffk sgnvlansqg slllaafswi
       61 iasfaviama lalieiasvr ndnlsligwn kvfnkkitan asknfmvyiy lpltyffmpl
      121 yvimslqdgl galldkdaav fgtnvdwliw tiislamsay fltiptlwsr vgdvqnkivt
      181 aikffplvfi aiigfvlait ktggqgdvti kvteditkti angkeelkni ggfgaflgif
      241 lsmtaiffay dgfyvaagis semkepkktp lalflglait tviyliiais msinggsffg
      301 mrdfmanlmg ataakwlfgi mniaiaigvl giingfsmwa pryvedllat gelpfwekvy
      361 kklnpnkpvi gviysiviti pvvllftiig aiayipnady diygsgmpsl yafadlmanw
      421 talftfafiv maifggivnr rtkrieipqk skyflvwawi svilifaali vsvlepavnl
      481 mlligfrgtt eelmpiligr imllvtlliy vilsygvtfi enevirrkyg svekfeeykk
      541 gvlki
//
LOCUS       WP_457601744             242 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA adenine methylase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601744
VERSION     WP_457601744.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Lobner-Olesen,A., Skovgaard,O. and Marinus,M.G.
  TITLE     Dam methylation: coordinating cellular processes
  JOURNAL   Curr Opin Microbiol 8 (2), 154-160 (2005)
   PUBMED   15802246
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Cheng,X.
  TITLE     Structure and function of DNA methyltransferases
  JOURNAL   Annu Rev Biophys Biomol Struct 24, 293-318 (1995)
   PUBMED   7663118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..242
                     /product="DNA adenine methylase"
                     /EC_number="2.1.1.72"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009007 - site-specific
                     DNA-methyltransferase (adenine-specific) activity
                     [Evidence IEA]"
                     /GO_process="GO:0032775 - obsolete DNA methylation on
                     adenine [Evidence IEA]"
                     /calculated_mol_wt=28147
     Region          1..233
                     /region_name="Dam"
                     /note="DNA-adenine methylase [Replication, recombination
                     and repair]; COG0338"
                     /db_xref="CDD:440107"
ORIGIN      
        1 mkpfvkwvgg krqlleqikk wmpekynnyy epfvgggall fevlpnkaii ndinqqlinv
       61 ykqikfnied lileinqids lnngkeyfyk lrdeynqnil nknlnariaa lfiflnkhcf
      121 ngiyrvnkng lfnvpyngki ttsidpdnlw kvhkflqnvk ientdfatvl knakkddfif
      181 idspyaplns tsfdaytntg fnlddhirla nlfkhldqkg ckilltnhnt plinpefpsy
      241 fn
//
LOCUS       WP_457601756             401 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601756
VERSION     WP_457601756.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..401
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43903
     Region          19..391
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 msigstikti ltaqglwgav iatvsfvaig ffatrkgyft ketngriskf iivfilpflc
       61 lwafmepakt ehlkdlgwvi gasvvyylvm gviswlvvky wpqlisknit akanalyeqk
      121 laagqieytk aahreyyldi ykqklitsqm mimygslqff ayplvaattg iifndfapal
      181 lqiwcipymi gtfshcklmy stdkeqkisv kavlksvfsp mmiilfislf lfliqfainp
      241 avqkhlatna naqkwllnfw asakgnlsal sgtvakavgv vsplawivig gslaasklke
      301 afkdvtvwit tarklivlpl viflitmglv agklisasag tllvllaatp patvcmvycv
      361 aynhphtaft aqvsslstll alvamplwlv ishvtflaia k
//
LOCUS       WP_457601757             455 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601757
VERSION     WP_457601757.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..455
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50916
     Region          11..421
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdllteilst qamwgaiiat isfvligyla tkknilsket ngrlskftin filpflcisa
       61 fmqkadaska ieigivlgls vafyvifsim swvitnyfpk lipnyinrka eelfheknln
      121 senpitkeya sqyivnnyra kltttqmmiv ygslqffayp likslsttpi fdsftlalaq
      181 twcipfmiga fsivpimysg ekfnrkhlap iaksllspmm iclyislilw siqfipffqn
      241 stnkyinnfw gnfgsnfpfi nktiqtgtsi vsplawivig gslaasnlke avkdkmvwit
      301 tarklivlpa fifvvtlilv ipftnklnvv nydvvsqeva qnaayafehn nqyylvksae
      361 nvglisrqtg vmlvllaatp pattcvlfat nykhpytgyt aevsslstll aiiamplwil
      421 isyltytsiv rvnidannft qakefiiqal qqvvv
//
LOCUS       WP_457601758             961 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601758
VERSION     WP_457601758.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 961)
  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 961)
  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..961
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..961
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=111071
     Region          591..911
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mqiekllekk enrsnnnffi nnffskknkg rsnetiltnd qvnlvngkfh isnlqenqfi
       61 semnvvaiak nfaslikeqq lenvtifigt dnvninkvya niaarvlsen nfnveilskn
      121 nlpfnlnfic nskwdfkiif nvseldaqfs qihfldvndl dikrvwlmkl faavrninnf
      181 anqipkseak lnisnvdsdy ktkmitkfkn lnigktkisi nfanvnnlnf yqnllnesnl
      241 nyelinyknk tinnaaeskf fkkqqlksmf khydlnflid tygqginvaa knksiykffk
      301 tdeiaalyln yllesgqlnk inknkifvak silcgsltee iafanqikvl nfldydevik
      361 keiaekkrai ftydeknrft tlngdkhdfd alnfliellk mydfykqnql tlfealnkin
      421 kkyskyfytl ktydfndena fkflqrissq ntlgkykiqr iqhfvsdkln sqeiviqlnl
      481 eqnikvllky sktlsqieim cetvgpvddl nqliinennv inailelked yknkkfsfwn
      541 ifkyltfigl figifvflfy svynvkteav snpnigqifn liwqtitynt aakwsfillv
      601 asflitilfn slilkrllqi qkekvnfghi ilanivgvva qnitpkaigg diatywflrr
      661 qginrsklis aiivntfmwq ivniilvvff vpigiyyyqe iltdftnrkt iiflimlilg
      721 ltidtiaatf flvltmskki qdgflngitw flewlpfvfi ynpeakkaky iyefyqirqg
      781 lktcfknvfs fieilfykgv vwvlapitfv aksanivqsd lqggwyfnil istlliksan
      841 sisptpggig tndfisqyif ksvfkanpei glnkaaesss iltaistiat vviptiigli
      901 fliivfigek ridahkqkrk ieslirndns letqkiktrf ypisitfasv fligltlwfl
      961 i
//
LOCUS       WP_457601770             442 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601770
VERSION     WP_457601770.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 442)
  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 442)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 442)
  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 442)
  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 10157724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..442
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51714
     Region          64..246
                     /region_name="EpsO_like"
                     /note="EpsO protein participates in the methanolan
                     synthesis; cd06438"
                     /db_xref="CDD:133060"
     Site            151..153
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133060"
ORIGIN      
        1 mqwdtnklsf tffwfflgit lflfliaiif hyfkfqyffy affnrkkaqn ifpkaekqhy
       61 ftyliparde skvienllks iknqtydsnk invvigvedl ndptvkiake ynfniylrqn
      121 feikgkgqlv neminfanqn nlltdafiim dadnlldanf tnamnnaynq gyevavgyrn
      181 nknwnsswvs acsgltfsrf shlenlkrtk ngttiqlsgt gfyiskkqie kfggwnfftl
      241 tedleltinm aldntkcayv sdaifydeqp iklndankqr lrwikghnql frkyrkslne
      301 alfkksqsnk vgcfelkfqa vsfasfilsi ifiiatislg iwtfyishln qkilitfisn
      361 liaillglii yyfsiviyta lsiyadprva mttkmkwkac fmqpiylfwy iplfikalck
      421 kevqwtkidh sinidlndlq nk
//
LOCUS       WP_457601760             270 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601760
VERSION     WP_457601760.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..270
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31437
     Region          186..263
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mqkatiqdkd kilnflaksp lynlfligdv eefgvendfi ksyikynnqn eilffilifq
       61 ttllfydpln qiqtnelsel iskhnitnif isdemfqnkk dffeqlkdfk inyqiiakan
      121 kkfngpinla qkatnleqik kivesrfqid efkdfrnenf atelnyyers flknisnnyf
      181 ieinnqvvah asvaaktnqa emiggvyclk efrnngyatq vtiallneii drnktailff
      241 hnpkagliyn kigfenfgkv ytlskvdnke
//
LOCUS       WP_457601774             300 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601774
VERSION     WP_457601774.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..300
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33826
     Region          2..254
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mskftaflrq tyiyfiliiv yiplvfatif sfnkesdrgf lstswnafsi eawktfgdgg
       61 rldalvnsvi iaiftalfvv sislvtvfam wrqrnkkygn ivrsvnnipl inpdnitaig
      121 lvlvfsilfg alantkegmv rgivghtvma lpygitlmyp rsekfnaslf easqdlgysk
      181 lrswfktyfi ymipsiifvs vvaaflsfdd fiilstttnv stlgtklyag qfrawglvvg
      241 afllfvifla niiyvsykii qvkknekimk qlskqnealn ktnrvnetip neveftlkne
//
LOCUS       WP_457601775             279 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601775
VERSION     WP_457601775.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..279
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31338
     Region          <59..260
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mnskiknala lnkrltllip faliaiflii lpiiliivna fipregfdsf qlvketktwv
       61 qiwrslkigi vssiicliig lpyayfvats knkflpiygi slilspmiif tiakiyaikg
      121 fflaitppen qdslnaewfm ilalvylnlp yivmplysvf rdmprniiea sldlgynriq
      181 tflkvvipys lkaiigglgl iflssattfv isdklllnkn qlqtigavin eytipsnefk
      241 lasgsvlvlv vsfifigsyf viytiprifi klkkgwtne
//
LOCUS       WP_457601776             459 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601776
VERSION     WP_457601776.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..459
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53403
     Region          6..446
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msqkqnqhii elknvvkefd gktvldnvnl kinkgefvtl lgpsgsgktt ilrllagfew
       61 vtrgeikfng ldikdlpshk rdlstifqdy alfphlnveg niryglklkr kpkeqindky
      121 eqilkekkii wdakaknkia kldklqkeye aemsklkpnt faynkrqkwl ddsdfhysyw
      181 enyvqqqteq fenryltrkl tseeideevk nitrlvgleg nenknisels ggmrqrvala
      241 rslviepeil lldeplsald akirqrmqvl lrsiqkklnl tfifvthdqa ealelsdrva
      301 vvrdgkieqy dtprniydyp inkwvatfig dsniyngtfn adgtvsvlnt tfktvheete
      361 fqpnqevdvl irpedidiye ynslvtkenk legvivdsay rgsyyylkik ltetqkiiyv
      421 etakkfnind kvllnwtids ihlmakdskw dyssdefkn
//
LOCUS       WP_457601788             567 aa            linear   BCT 27-JAN-2026
DEFINITION  M28 family metallopeptidase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601788
VERSION     WP_457601788.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 567)
  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 567)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..567
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008235 - metalloexopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=64145
     Region          237..459
                     /region_name="Iap"
                     /note="Zn-dependent amino- or carboxypeptidase, M28 family
                     [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]; COG2234"
                     /db_xref="CDD:441835"
ORIGIN      
        1 mkknvvltls ssiavfgtva iaascnkdke eskniisnvd yektdvrnfy nkfelenhgr
       61 iagnisnvsn ydestykfrd lqdpnkksld sndivfkydl nttiandvnn ygsyhaflwl
      121 keqvkqmnya nlnstdvity pelqdvqlqs esktyrgkty qnykmatnen vvnilkearf
      181 etqssfyetg itirkdeefk nqvienmlnk tgyqsqgflf hakdklrdgk ymannlgnnl
      241 ivsiqpenpg iteanknqlk dlyivahyds ttsstnhlsw gatdnatgva salsllkhys
      301 taenraklgt rlhvifvdae elgkygsiaf vkefmeskke tsgenevetn klllsaagmi
      361 nfdtvaggdn myvhspnsnp dvdvvkgnis ssirdqinai srirakdknd ieleleihpq
      421 feknsyrage tgdwsdhmpf yqyanipiay vestnfnvfs kfneydgyaq tnnpnawidk
      481 dgnkinlvpk akngsnivlw dlpegvsmen vviagdiwhs dldrydwvke nvgnkiykql
      541 dtvvetikey ltsvwhissn qtielti
//
LOCUS       WP_457601813             536 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601813
VERSION     WP_457601813.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..536
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60911
     Region          4..532
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mlevqslski fsdkklfenv nlkftegnty giigangagk stflkilage ieptsgqiii
       61 eknrrlsvls qdhnayddmi vtdvvvmgnt dlykikeekd aiyanpdate edyvragele
      121 ekygelggwt aendaqells glqipkekwd aqmstltanq kikvllakal fgnpdilimd
      181 eptnhldlra ikwlenflad ypnvvivvsh dsdfldnict hivdidynea kiytgnysfw
      241 kesselarel mkqsnakkev qieklkqfia rfsanasksk qatsrkksle kitldeikps
      301 nrkypyinwd inrepgkdil svenltyken gktlfenvsf tlskgekmvv igeddiaktr
      361 flecligkiq ptsgeikwgq tikftyfpnd nkeyfqedmt ildwisqwpl ensteetkdv
      421 sdsrmrgflg rmlfsndtvf kkvavtsgge karlmfsrmm lleanflild qpldhldaes
      481 idsvidglkk ykggaiftty nralvnqvan vileiapdks fiyhgtldey ekimdy
//
LOCUS       WP_457601819             591 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601819
VERSION     WP_457601819.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 591)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 591)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 591)
  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 591)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..591
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67496
     Region          1..588
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mfklfkllsk kvkgfafiti clsivqpfla mlipsitkqi iysvankelf diqilfwtlh
       61 tqstnqsily lilitistal llmlvayfss ffalrvaiyg skelreilfk hlltfsrany
      121 dkltsgtils rfsndmrkir dglntivrsl flspllfiwg lvfalntnly lsisifiiip
      181 flsigtfliv kklfplyake nrmidklndt ikediqginl iksynlenvr qnifeqknne
      241 aklialtnnk issfawpimd fislmgnafl ffviaflvqi lndqsisklv gdiyqfstyl
      301 tmtansiffm mftlnnlfrs sassrrywdl lntkseiplv tepifiesns itfknvsfky
      361 plaqknslen isfhikpnek igiigktgsg kttlfrliar eyliennngi ieignipiek
      421 insdnlyknv vpifqkpllf sgtikenltf snsqndyeea lfyadadfvy ektetfdfql
      481 sakasnlsgg qkqrlaiaqa iikkpkilli ddstsaldnk tdlkvrenif nnfqdstili
      541 iaqrinsikn cdrimvlddg kisdfnthen llksnliyqe ifnsqigenn g
//
LOCUS       WP_457601820             609 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601820
VERSION     WP_457601820.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 609)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 609)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 609)
  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 609)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..609
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69612
     Region          20..608
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 marhgfqtlf aknnnykklt fkdffnflkk ielnkskwil iiilsafvpi faniaiilig
       61 kitdtffnpi sfnknnfnyw lffgflgffi iciflqkflt tiqrlilnra iintgyklrv
      121 dlykkiqklp lnyfdnhqtg dlmsaltndi nnitdamvsm lgqlsliffq flltftlmfl
      181 yapilglial ilipsstlvi illiknnqky ffnqqkelgh fngfleeyle iqplvyvhqq
      241 qdkilkkfqk ynnnlvpndl ksssnmaftf pwfhfcrffn llviisigal fiineipsyg
      301 italtfgtli sfsiyitnvs enlskileia ntiqqglgsi arvneilelp eienqktlkn
      361 lnfikgeief knvsfaypsn pdklilknvs fkiksgesla lvgktgcgks tiakllskfy
      421 lptsgdilid gqsiyeikdk swrshidmil qdtyifnesv innllianpd lqkseltkil
      481 kytstenlin nlpngldtil esngknlsqg qkqlftilrs ivssreitif deatsdidti
      541 semhiqkaid ylfkqkttiv iahrlstive cdqillidng qiieqgnhqe llklngkyan
      601 lyaigfnnn
//
LOCUS       WP_457601828             423 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601828
VERSION     WP_457601828.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..423
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47371
     Region          <201..416
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 msvhlsneef nakyklnqnf sskihlaqdr nltnniagkp kilaveiikr ffknpvvvla
       61 tlaflalilt sviiyftspy laaqridans qekltfiksl pplfdaheis fdtlkiksyn
      121 vivdsqyyqy lrdagyglsf nteysasgsq fieynaydfy ttnrifttin sdhwnslvsd
      181 sdkivylqel gqavpklkty lgttengydi wttawvgviq smkvalivas iefligvtig
      241 aylgfhagkw idtvvmriie ifqsppsiiw llmfvsiwgt ndwvliggll fvgwtwpigt
      301 trmfiitvkd eeyitaaksi gastprqvyl halpaiigkl amnfvrrips vilsvaslaf
      361 lgffkddnsa nigkfmidni sqselnpwlm ilpasillvl slslqfiavg ihdaldpkiv
      421 kar
//
LOCUS       WP_457601805             294 aa            linear   BCT 27-JAN-2026
DEFINITION  UTP--glucose-1-phosphate uridylyltransferase [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601805
VERSION     WP_457601805.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kleczkowski,L.A., Geisler,M., Ciereszko,I. and Johansson,H.
  TITLE     UDP-glucose pyrophosphorylase. An old protein with new tricks
  JOURNAL   Plant Physiol 134 (3), 912-918 (2004)
   PUBMED   15020755
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..294
                     /product="UTP--glucose-1-phosphate uridylyltransferase"
                     /EC_number="2.7.7.9"
                     /GO_function="GO:0003983 - UTP:glucose-1-phosphate
                     uridylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009225 - nucleotide-sugar metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33484
     Region          3..294
                     /region_name="GalU"
                     /note="UTP-glucose-1-phosphate uridylyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG1210"
                     /db_xref="CDD:440823"
ORIGIN      
        1 mnkkvkklii paagwgtrfl pmtkiihkel vpilnkpvid llvneaiesg ieeiiiiisp
       61 rkkdllkyfa vdsdlqdelt hkhkeellki vketnksqii trviqneqhg lghalavakd
      121 yvnnepfavi lgddliksev pvikqmidfy nennqpnilg vqtveaenvh kygivkplne
      181 neknnkyfei esavekpkla napshkailg ryifnpeild ilsaieydgk neiqvvdafk
      241 klqnmynqki yafefegtry dlgsmegfvk anidyalanp eikdkiydfi knki
//
LOCUS       WP_457601829             362 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601829
VERSION     WP_457601829.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40754
     Region          16..339
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnlnqiktes lkddqllkvr nltvdfktsq kqtiriirgi dldikkgqiv glvgesgsgk
       61 svtskslinv ndgaiinade mqiadydltk igkhkklwqk irgqyigyip qdpltslnpt
      121 rkigkqllda lnlnnewknk tknekidylv slleqfgird arqvfyryph tlsggmkqrv
      181 vitmvvalnp kliiadeptt aldptvqasv lalfetirqk lgisiilish nisvvakfcd
      241 yifvmyagki iergtrkdif tkpahpytwa lisaipensq drlysikgtp pdlanlplgd
      301 pfaprndyal eidfykeppl ieidshhaaa twllhpdapk vqkpkdlqdk ldafkkvfkd
      361 ek
//
LOCUS       WP_457601835             227 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease HIII [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601835
VERSION     WP_457601835.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159551
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..227
                     /product="ribonuclease HIII"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0006401 - RNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016070 - RNA metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=26010
     Region          18..226
                     /region_name="RNase_HII_bacteria_HIII_like"
                     /note="Bacterial type 2 ribonuclease, HII and HIII-like;
                     cd06590"
                     /db_xref="CDD:260000"
     Site            order(22..27,57,95..97,123..125,159,161,175,198,224..226)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260000"
ORIGIN      
        1 mqikeldidl nsldnlsiig vdevgvgdyf gplvssavfi prekmyflse lgikdskkis
       61 dkkikelapi iqkntinqvf flsphgynql nvqynsnelk mfchlntisk vanetrsdfv
      121 lidqfstlks iknyyqkimv dnnwakipnf ntdisllkka enyslavaca silarnffln
      181 ymkrmneeyk infplgagnq vkefaqklfm dkninpkkia kihfkmn
//
LOCUS       WP_457601836             314 aa            linear   BCT 27-JAN-2026
DEFINITION  Cof-type HAD-IIB family hydrolase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601836
VERSION     WP_457601836.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..314
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35160
     Region          15..282
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
     Site            order(19..23,55..56,213,235..237,239..240)
                     /site_type="active"
                     /db_xref="CDD:319818"
ORIGIN      
        1 meeqnltkks dkkflfaidl dgtllasssq gsihevtfna ilrakaeghi vclltgrpwr
       61 stkpiyerld ldtvvsnyng aqihnpkden fipyikyldl nemlyvlgdp kvkseitnia
      121 iegpgwvqlq krdkdlesvf gfrestkfvv gldfnklplk ptgiifdvkh stdveelrsy
      181 lkrkfgdlge fsywskgkgl tpvfditnvs vnkgralsll sryygidldn tiamgdgfnd
      241 vpmfkvakis vavgnaskdv kkyatikltk nndegavghf insildnpek iiakseaarq
      301 kmmkhrssmd diee
//
LOCUS       WP_457601840             438 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601840
VERSION     WP_457601840.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..438
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50524
     Region          <17..384
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mpnyycekgk fgkkycrpvl pgteemlaae dkkvlveirn ldieygqgtk kftaikdmnl
       61 niydgevlgl vgesgsgkst tgraiigltp hsfgyikild tfvpknidkv trwgnkhkki
      121 ldfmvnkvqm ifqdptnsln pyknvekvvg egltnlknsk yiylitedqn ffielnkrie
      181 asnaeplven yqnqldwnft leesfdyvye klfnefqaky kylknfdell dfynkakelr
      241 itesnlteke ckkrliidil kqvgldesvl dryplefsgg qqqrlgicra vvlqpkllia
      301 depisaldvs iqaqvinifn dlkdkyhlti lfiahdlrmv eyisdriavi nkgvlleigp
      361 teeiiynpyh pytkslldav psieskkgsl lgyvydpnih nydeenqpkw qnlgnnhfvl
      421 atdkeletfk eikkekqy
//
LOCUS       WP_457601841             583 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601841
VERSION     WP_457601841.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 583)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..583
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66266
     Region          199..522
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mansrnkmtl deklameakn kskrnlndet nnsansfnen laaineqail rqankkvaee
       61 eikqiqkedl ssdellnnei ndfiveneky hldenlndne iinaegysqk fkkpiiwnlk
      121 pkpedllvvr kdinntlvrk fidfwktlfk nfvslgkkil qlvkilpkek nevleefqky
      181 idnakvetvf gkptkvaaei ediyltfknp anpkeknlvl rgsslkiyeg kvhaiigesg
      241 sgksvitsll ygltgsnaii esgkiklygl evqnfnaynw eksklrgniv savfqnpmsi
      301 ldptmkvgkq imegmlvnkl vknkkeayee alkylkltki nnpekvmkly phelsggmiq
      361 riaiasiisl kpkilvmdep ttaldptvqa lvldiirelq etfkiaivfi thdlavvssi
      421 sdfinimyag qiiesgtkee ilinpqhpyt wglivsmpdf nkdtrlqtik gavpsnlnki
      481 egdafavrnd yalgidfeee psfyqispth fvksnllnen apaykppkii qrlwakyens
      541 llkiygsknn eyvseeiyqk ylkeanqhnl eiestknkee tna
//
LOCUS       WP_457601842             325 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601842
VERSION     WP_457601842.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36603
     Region          53..321
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mafwnkrkea annvasqela pnriiqpfny qkwkiigdvl dyyesstlhk kqssmkeffy
       61 rfsrsfagvf glvtlliivl laiiipfftr dpnviteenk fwtfftngyi fgtddlgrdl
      121 warlwwglry slglsvavtm ievivglsig iamghfrlfd kimtfvikvi snvpsiiili
      181 vitivlkptf gvivfalsft swtgmanqmr sqvmraknfe winaskilgt ptikvlfnyl
      241 pvvvpilvtq ivfsipgvil setslafigl sipsiptlgn litdgsnlfv sypryvlips
      301 fmlvlvttsi qlmsasvqds llrqr
//
LOCUS       WP_457601853             455 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601853
VERSION     WP_457601853.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..455
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51275
     Region          1..453
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mnydliiigw gkggktlasq lpetwkiali ekdpkmfggt cinigclpsk slvndahlia
       61 klddfnfern yeinndffkq aiqhkndlvs flnqknyekl afksnvdiyv gnasfinenq
      121 iqikelngni lnisaskiii ntgaktrkln fdsswdtrni iyseealnln elpkkllivg
      181 agfiglefas fyanfgsevt ilqnnnlflp sedednahei lktlsnqnis infnsqildl
      241 sefneqtkvt ytnndevite ifdkilisig rianvedlnl aaanvelser keikvndylq
      301 tsnpniyaig dvkggtqfty islddsrivf nhlnndlsys lkernlipia tfisptyarv
      361 gltekeiink nipykkkfan vasipkarvi retkgfvkil idendyiiga slfmtnaeev
      421 inliavaikn kikskelknf iythptmtes lneil
//
LOCUS       WP_457601862             305 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601862
VERSION     WP_457601862.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..305
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=34994
     Region          10..88
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(11,22..23,25..26,28..29,32..33,35,42..49,51)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          77..289
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mirlevkyke ridkyisdns eitrndakal ilegaisvne iqvrkpnftv kendviniyk
       61 liekitnida kemeleiiye dndivvinkp snlvvhpapg hfddtlvngl lyhfknlsne
      121 ngllrpgivh ridkdtsgll liaknneahl klaemlkthe ikrsyvaivd gilenkflki
      181 nlplgrskkd rklisvqkdg keaitnvell ktfyyekqpy slvkcdletg rthqirvhla
      241 yikhpvygda sygkkvddfg qrlhayklef nhpitnqllt ifapipaefs isdydfsqlt
      301 qerkn
//
LOCUS       WP_457601873             365 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601873
VERSION     WP_457601873.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..365
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42227
     Region          238..>277
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mrirfkeiqk nlpnndkfyg flrflnvivt sdyeipftnk nlrytarilr nlyaiiiatf
       61 iilsfttfvf lkkntqfnks ivsvleivtf villsdiflr qityvirdpk kstfkiallr
      121 fyltgtfwim ficllpsfsl invwsgkeik ifeifgtlki lrilrlimll sifssfkmms
      181 qslkkqksii isafifilvi lilfsltiwy seyqfvlkel nlseeinsve nqnkinefyl
      241 qnsnlvsnfw dslyftaitl ttigygdfvp haemtkmiip iisligiaii slpgglfata
      301 lldslqnrkk vnkntnvndv skeqetvkti dlndealkkl idqevvkkln eilgklndnd
      361 qssnk
//
LOCUS       WP_457601895             148 aa            linear   BCT 27-JAN-2026
DEFINITION  23S rRNA (pseudouridine(1915)-N(3))-methyltransferase RlmH
            [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601895
VERSION     WP_457601895.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..148
                     /product="23S rRNA
                     (pseudouridine(1915)-N(3))-methyltransferase RlmH"
                     /EC_number="2.1.1.177"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0070038 - rRNA
                     (pseudouridine-N3-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17234
     Region          3..147
                     /region_name="SPOUT_MTase"
                     /note="Predicted SPOUT methyltransferase; pfam02590"
                     /db_xref="CDD:460606"
ORIGIN      
        1 mkkikiisvg nlspyfkqlf neyakniaif aefqnielke fseiknieek klretkkvle
       61 svdknsyvcl lslrgkqids tefatkldls dnwtfiiggs dglieellkp nlkisfskmt
      121 fphqlfkiml seqiyrafmi knnkkyhk
//
LOCUS       WP_457601900             266 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601900
VERSION     WP_457601900.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 266)
  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 266)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..266
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31341
     Region          23..260
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mkqeeiilkr nliknslgfd selfvyqdkt mfnysvdtim lgnfvslnrk vkkmleigtn
       61 ngalsifise rfselkidai eiqpeaieva kinveinnkq qqinlinddf nlfwmkkvkd
      121 ehfkkydsiv cnppfyrvdk tkiskkiseq fliatheikl tleqliygas kiieqkgyft
      181 vvipvermid ctflmrkynf epkriqfilp rmqdqpklvl iearyqagwg tkflpnlylh
      241 dpnnltehsy rkeikelykp kkvitk
//
LOCUS       WP_457601902             258 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601902
VERSION     WP_457601902.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..258
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28925
     Region          7..258
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mksnnnlkfg kftdigtkrl enqdrvaifc neqyyllilc dgmgghfgga laasttintf
       61 ettlhqlnvt qnltidetar wieqsvrkar kemeflslkd aalidmgttv tgvlinsvak
      121 tivvfnigds riytinkdns vnqitkdhnl ynsliekfny thkqaiaerg hraltsslgp
      181 tkktkinisd lskfydeief ifatsdgvhn fvsqsffeli finnkdddld nlaqdivqea
      241 llnksndnls igiiklkd
//
LOCUS       WP_457601818             194 aa            linear   BCT 27-JAN-2026
DEFINITION  diadenylate cyclase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601818
VERSION     WP_457601818.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Rosenberg,J., Dickmanns,A., Neumann,P., Gunka,K., Arens,J.,
            Kaever,V., Stulke,J., Ficner,R. and Commichau,F.M.
  TITLE     Structural and biochemical analysis of the essential diadenylate
            cyclase CdaA from Listeria monocytogenes
  JOURNAL   J Biol Chem 290 (10), 6596-6606 (2015)
   PUBMED   25605729
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Romling,U.
  TITLE     Great times for small molecules: c-di-AMP, a second messenger
            candidate in Bacteria and Archaea
  JOURNAL   Sci Signal 1 (33), pe39 (2008)
   PUBMED   18714086
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Witte,G., Hartung,S., Buttner,K. and Hopfner,K.P.
  TITLE     Structural biochemistry of a bacterial checkpoint protein reveals
            diadenylate cyclase activity regulated by DNA recombination
            intermediates
  JOURNAL   Mol Cell 30 (2), 167-178 (2008)
   PUBMED   18439896
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446911
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..194
                     /product="diadenylate cyclase"
                     /EC_number="2.7.7.85"
                     /GO_function="GO:0004016 - adenylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0106408 - diadenylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006171 - cAMP biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21753
     Region          <42..193
                     /region_name="DisA"
                     /note="c-di-AMP synthetase, contains DisA_N domain [Signal
                     transduction mechanisms]; COG1624"
                     /db_xref="CDD:441231"
ORIGIN      
        1 metqigiill sitlsllviv lititlpkii efskikfnkt kykklgrssq irlinqlret
       61 vetlsknkvg alitienndn idnlrtdgii lnanissall itifnkesll hdgaviirnn
      121 kiyyaatfyk itkksidnky garhraamgi selcdattii vseetgdvkf vkngvffdvs
      181 ldqfqeqlik ylkd
//
LOCUS       WP_457601916             243 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601916
VERSION     WP_457601916.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..243
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27593
     Region          6..239
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mqnklissvq nskikylkqv anfkysnlfl vegyhlvqea fknnlvietf elnenqlvyp
       61 nsilitsnvl ssitntktpe givalckitf ktelndkiif ldnvqdpgni gtiirtmkaf
      121 nfnslianin llnhkiirst qgaifnlnyy qykqndysii kklksegyki igtlldknsq
      181 pyfkndlftg kfvlimgneg ngisrelqql ldysvyipin feslnvavat givlnhiyqs
      241 ekk
//
LOCUS       WP_457601920             304 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601920
VERSION     WP_457601920.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34503
     Region          69..287
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mknekelnfp elkipkneki nsenvceiin kyangqkqli vnkkiaklln klskrkhskk
       61 nkvknsnhlv evknvtkyyv ngevinkvld dvsltidkge iilifgtsgs gkstllnlis
      121 gldrpnkgei yvnneslvnl ddrgltkfrr nnvsfifqsy nlltnlsayd naltgaylqk
      181 dkqkvlnide lfktfelsne knkypsqlsg gqqqrvsiir alvknseiif adeptgaldh
      241 attkivlktl felnkkektt iifvshdpqi tpiadrvfyv kngkiekivk ndkkkhpdef
      301 lkid
//
LOCUS       WP_457601925             713 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601925
VERSION     WP_457601925.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 713)
  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 713)
  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 713)
  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..713
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..713
                     /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 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=84023
     Region          258..685
                     /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 mdktnqkfig kftkilsgga skewkytfal feyegrkkip vyikgkeiel fieyeiycly
       61 nelketwnle eiklhelknt klevnilkkv egfgfkklel lknkygdnwi enseknnfya
      121 edlgnkiaek lkkelnkind nkiykyfien slisqhdkiv sltetedliq yfkkndifdl
      181 finfgfdfet nlkiafllke sslisissys fyrafiylyi yenfknnntl islsknminy
      241 vdteieklnt likvdrfdiy dvliemikrn eilqfksekg ilklttfkmy ekekyilnyv
      301 knlislsnnk keikefpksl sekqgeaylk ainknfsiis gfpgtgktyi lneiyntllt
      361 enkykksevq iltptgkags nittkfgilt ktihsflkid kdedlmnlkn yetnenvkvi
      421 iidefsmvni dlfyllltsc keiekvilig dhnqlpcigp gnmlsefvns dqiektklte
      481 ifrtdcvdic ehflniknni epnlntenvk fyeqnstefl nfieykyeee vkkysienvt
      541 ilcptnrfvd kineklqkwn neffhfpden fnvlfgdkpl figdkiiqiv nnyeknvfng
      601 eigyfkdfin gnfifeinnk eveytkaeik eniklayait vhkfqgsesn siiftvfkef
      661 dkmlknqlly tavsrakkel hifgdsylyi nkitdvknny kietnmklll een
//
LOCUS       WP_457601929             279 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601929
VERSION     WP_457601929.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..279
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32629
     Region          24..>122
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
     Region          25..258
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mlkkellinn eniifyeqne iddkpnvlfi hgfgdtgqrv lpliekknkn ynlyaldlpg
       61 nngtthkkel slnyyveivn elirtkfsnk piylaahsmg cfialkllri nknikfafli
      121 tpviystdln yqeklnnkkr ffipqnekdi idsqlalfdp dsyekfaqne kfkqailfnq
      181 khkiyenlnk fnklvneell nakflvselk plykekekil iiysefdnfl pknfveavik
      241 endlksilik naghaifyna tneinniiek qliieennv
//
LOCUS       WP_457601904             220 aa            linear   BCT 27-JAN-2026
DEFINITION  ribulose-phosphate 3-epimerase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601904
VERSION     WP_457601904.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Akana,J., Fedorov,A.A., Fedorov,E., Novak,W.R., Babbitt,P.C.,
            Almo,S.C. and Gerlt,J.A.
  TITLE     D-Ribulose 5-phosphate 3-epimerase: functional and structural
            relationships to members of the ribulose-phosphate binding
            (beta/alpha)8-barrel superfamily
  JOURNAL   Biochemistry 45 (8), 2493-2503 (2006)
   PUBMED   16489742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012464
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..220
                     /product="ribulose-phosphate 3-epimerase"
                     /EC_number="5.1.3.1"
                     /GO_function="GO:0004750 - D-ribulose-phosphate
                     3-epimerase activity [Evidence IEA]"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006098 - pentose-phosphate shunt
                     [Evidence IEA]"
                     /calculated_mol_wt=24652
     Region          1..219
                     /region_name="PRK05581"
                     /note="ribulose-phosphate 3-epimerase; Validated"
                     /db_xref="CDD:235515"
     Site            order(9,11,36,70,146..147,149..150,180,182,202..203)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238244"
     Site            order(16,19,39,41..42,44,46..49,73,77,97,99..100,122,125,
                     127,131,145,154,156,160)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:238244"
     Site            order(34,36,68,180)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238244"
ORIGIN      
        1 mtekfvtpsl lnvdegkrle madllinegi kwihydvmdg efvpniaiqf eeikeinekg
       61 kkhfkdihlm venpleylei yqnvgdiltv hfeaiknkse flsflknnkk taeftiglai
      121 kpntavseie kflpyvalvl vmsvepgfgg qkfipealnk isqlkqirek eqlhyliqvd
      181 gginnetgpq cfnagadacv agsfliknpn kdtidsilgn
//
LOCUS       WP_457601941             321 aa            linear   BCT 27-JAN-2026
DEFINITION  ribose-phosphate pyrophosphokinase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601941
VERSION     WP_457601941.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..321
                     /product="ribose-phosphate pyrophosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35286
     Region          6..315
                     /region_name="PRK01259"
                     /note="ribose-phosphate diphosphokinase"
                     /db_xref="CDD:234929"
ORIGIN      
        1 mnknnvilfg mpncyklakn isnrleipls eikritfadt esmlisqqtv rqkdvfvvas
       61 tsmpvnenlm ellifldslk rasansitvi ltyygyarqd rkesgrqpis aklvanllqt
      121 agatkiiavd lhnpaiqgff dipiddlkga fvlakpiids ketftvvspd hggtnrarkl
      181 aeliansiki ciidkrridt dkteilglig nikdqnavii ddiidtggti lkaaqalkds
      241 gakkiiiaat hglftkgfem fennpniekv iitdsinneh lvskfsklqv vsldkflagv
      301 idchingssi stlynrfqel i
//
LOCUS       WP_457601942             722 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601942
VERSION     WP_457601942.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..722
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82046
     Region          4..716
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mdfnfddfln ninnnqkdkk neddvlkkyg rnltdlaarn eldpvinrdd eirrmirils
       61 rktknnpvlv gepgvgktai veglarkive gqvpenlkgk dvieldlgsl iagasyqgqf
      121 eqrlkdilkr idesngeiiv fideihmlig agrnsdggmd aaniikplma rgkmhligat
      181 tfdeyrkyie kdaalerrmq kidvkepsig daitilrgik drfenfhnvk iqddaliaaa
      241 klssryisdr flpdkaidlv deaaatikte infqpeklek akqklaklem ekfalseedk
      301 tkhaerikni eqeiatinas inelqhkwdi eknrlnelsn lrhrldnlnh mltiyqnead
      361 yekasklmyd eipsvklkik elenlinhss ntlikdtvte eeiasivakw tnititklle
      421 tdrekllnlk hdleskvkgq deavtlvsqa virakanind pnrplasflf tgptgvgkte
      481 lartlayslf dsekqmirld mseymekhsv akiigappgy igydstgslt ekirrnpyti
      541 llfdeiekah rdvlnillqi ldngtitdsk griincrnli vimtsniase kilneledmp
      601 sikaellkfl spefvnride vitfkplske aikevvklel dklvkrvrsa kdinlayddk
      661 vaefiaekay dpnfgarpir ryvqnnlesv iaykiidgsi kkdhkykidi llnqfvinea
      721 tk
//
LOCUS       WP_457601945             509 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601945
VERSION     WP_457601945.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 509)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..509
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57407
     Region          1..503
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 msqnaiefrh itkefpgika nddvsfkvkk gtihaligen gagkstlmsm lfglyeptsg
       61 eilindkkvf fkgpndatny gigmvhqhfk lvkvfsnldn iilgsewtkn nfidrkiatd
      121 kiislqekyn lnfdlkmlsg dstvstqqkv eimkmlfrdn dilifdepta vltdeeiqgl
      181 lksfeifrea gktilfithk lreiqqvsdy atvlrhgkvi gtydvkttpm deivkamvgs
      241 nvvmaknnlp terkkvifel qnistknqvk nlqnlslkih ageifaiagv egngqreleq
      301 icsgmilpse gkiykanqng eliditkdkv lkrskngisf iptdrhahgl vldyniqens
      361 ilrrlwdkkf qtftwiknrs kkeftneiie kydvrgalng yaqsrslsgg nqqkfivgre
      421 ietphefiii mqptrgldvk ainnihqqii kekengkgil lisyeldevl aladtigvin
      481 egelvaikda keitrsqige fmaskkenk
//
LOCUS       WP_457601947             323 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601947
VERSION     WP_457601947.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (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   2  (residues 1 to 323)
  AUTHORS   Tomii,K. and Kanehisa,M.
  TITLE     A comparative analysis of ABC transporters in complete microbial
            genomes
  JOURNAL   Genome Res 8 (10), 1048-1059 (1998)
   PUBMED   9799792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..323
                     /product="ABC transporter permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=34648
     Region          9..322
                     /region_name="NupQ"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     subunit NupQ [Nucleotide transport and metabolism];
                     COG1079"
                     /db_xref="CDD:440697"
ORIGIN      
        1 mnisissgss lynlilvffc ilalgaisgm fsekvgivni gingtmifga igylmfsqta
       61 innnwgnspw lvipatlvam lfgfvssllf gfatiklkss qtisgfafnl laagialfvm
      121 rfygeqgstn lnntinhlhf aleptvdgvk gtfpiipfnl iitliiiigg yivlyktkwg
      181 lrfrsigenp qaadvagvkv nsykwqgifi sgiigsiaga ffaqktsdgs ftfngdvlgl
      241 gylalaimil gqwniliitg isfifsills lsfnqsmfpa ikdhagilei lpylltlisv
      301 mffagkkska paaagipydk sqr
//
LOCUS       WP_457601951             309 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601951
VERSION     WP_457601951.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..309
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34185
     Region          5..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnkvydviii gtgpgglnaa lygsraglnv aiidkgapgg klsqtakien wlgteiiegy
       61 elaikmfdha ikfgaeykyg nvksiqknne lfeiyfadef netmyaknvi vatgmknkep
      121 nwienyetyk ykgisfcatc dgpifkdqnv vvigggnsai eestflaniv dnvylivrdn
      181 qmiaeqklie dlkkhtnvyi hmnsevikil gdenqintfv iknnldnsif einangffpf
      241 igllpnnqlv nnfseilnes gfiktdenme tnvkglyavg direkhvrqi vtaaadgaia
      301 ikniadskn
//
LOCUS       WP_457601948             621 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease J [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601948
VERSION     WP_457601948.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..621
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=70530
     Region          1..553
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mnptriipig gvqeigkstl iveqdnhifi idagikfant attgikgiip nysylyenrd
       61 kieglfithg hedhiggvvh lvkqvpvkri fapriaiqyf klkfdehrin qkiefieiek
      121 navyhfgnck vdfwtaqhsi pdafgiritt pngslmctgd frfdynpigh sytdfarldq
      181 igkegltill sdstnamrpf hspsendilt diekymrqat kktiitafas nltrvkaiie
      241 lavklkkkvv tfgrsmvqgv kigrklgyin apndvfiekk einnypskdi vilttgsqge
      301 qlaalsrmsy nkhqsvkiek ndliifsssp ipgnrseiel linrlaklga iikengvdgy
      361 lhtsghaykh ehakifqltk pkyflpyhge yrmsmvhgqs avengvnphn iiipalghvy
      421 nmhkqnvyet deridfgpiy idgyttlstn atiikdrarl sesgfvalil nidktknniv
      481 grptlisrgs fyvknslelv eeakrishgc alfyirntpd wnvvelkqli terlenlfhn
      541 qkrrnpiivp iilftdeene nlfetspiqf nknevnkena lnntenqkvs ktskllnelk
      601 selldhyndi nddihdedde e
//
LOCUS       WP_457601954             346 aa            linear   BCT 27-JAN-2026
DEFINITION  SPFH domain-containing protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601954
VERSION     WP_457601954.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11556246
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..346
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39019
     Region          18..239
                     /region_name="SPFH_like_u1"
                     /note="Uncharacterized family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03408"
                     /db_xref="CDD:259806"
     Region          298..341
                     /region_name="DZR"
                     /note="Double zinc ribbon; pfam12773"
                     /db_xref="CDD:432773"
ORIGIN      
        1 mkngysvidf ngngeidwli ykhpitevwn nsklivnpgq vaivvrngqi dtifkegttk
       61 insntvpfls sveksfhkgk tpwpvefyfi ntrlkldakw gtsspieikd pvygiiirir
      121 grgqlgfeve nyqflyeklv gsisengyle fnfvldifrg kiqqyvktil lkkmneeqis
      181 ydllnlhlde fqaelenklr semtkfgfnl inlsldslni pvedrekins ylskkaelni
      241 lqddyrlvkg yniteklaen nngsanmilg vglgqslngs nsiippvetk tesqtalcyk
      301 csspisptsk fcnecgavnp tkcpncqnki tsnskfcsec gfklkd
//
LOCUS       WP_457601957             249 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601957
VERSION     WP_457601957.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..249
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28629
     Region          43..248
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msfkakmffl fpfflwhvwr irvyarkyrr tpeqytlqqr ndwllrkakr likwfninle
       61 vkgydelpka pvllvpnhks nldaililaa lakqtkeegv rnkiptflak nellkskvak
      121 atlelcdtff inrkdirdsf kqlakfgnfv kenltygvif pegtrikgde lgefkagafk
      181 taisnyisvv pvaihnsena dnknrkeklk itveflrpir andvitsnpe glakrtkeai
      241 sgalknakn
//
LOCUS       WP_457601959              99 aa            linear   BCT 27-JAN-2026
DEFINITION  Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC
            [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601959
VERSION     WP_457601959.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..99
                     /product="Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase
                     subunit GatC"
                     /EC_number="6.3.5.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0050567 - glutaminyl-tRNA synthase
                     (glutamine-hydrolyzing) activity [Evidence IEA]"
                     /GO_process="GO:0006450 - regulation of translational
                     fidelity [Evidence IEA]"
                     /calculated_mol_wt=11674
     Region          <51..99
                     /region_name="GatC"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit
                     [Translation, ribosomal structure and biogenesis];
                     COG0721"
                     /db_xref="CDD:440485"
ORIGIN      
        1 mekitkedik nivksiylep ktevieklwq ewqnlqtemk wlddlalddl epmthineeh
       61 lidclredvv dysfaiskee alknakeknd dfvlikkvv
//
LOCUS       WP_457601962             608 aa            linear   BCT 27-JAN-2026
DEFINITION  HsdM family class I SAM-dependent methyltransferase [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601962
VERSION     WP_457601962.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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 608)
  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 608)
  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
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416313
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..608
                     /product="HsdM family class I SAM-dependent
                     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70044
     Region          280..509
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mtrneiieii gkdkyvsnie ngewsyarql segernklld knakdnhkfl dirfenekli
       61 ilvetkdkik knlklnkaql qsyvnfeskl nkakkkiiai lastgedevl vyagdnnlkl
      121 ndstvlkdek niksfeyyed lffgvknnke evmkntyeln ellhkygire dirsqfvgtc
      181 llslkynlty knlstkqiss giesileqll ndninkagki wilkskiies qdvqdlkdfe
      241 fekilnfiem kilpfindks tqgqdllnlf ftafnkyvgk kdknqaftpd hivkfmceia
      301 einknstvld pccgsgsflv ramtmalddc nnenekkeik qkriwgieye egafglattn
      361 mlihgdgnsn iiqgscfdkt eewyndakin vvlmnppyna skkhsnpeyt ktwdkktsld
      421 pskgfhfvyd vakkvktgkl lvllptacai gtsedieqfk rkmldehtll avfslpqeif
      481 ypgasasacc mvfelgkkhe kaavketffg yfkddgfikr knlgrvekie ngvslweeis
      541 sewknlyfkr iekpglsvlk qvsyndewlp eaymetdysk lthedfekti refisykikf
      601 gddkngtn
//
LOCUS       WP_457601964             313 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidate cytidylyltransferase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601964
VERSION     WP_457601964.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..313
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35667
     Region          <144..312
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mnllkrriip gllfaiflfa tlipvsifap fhyqarivaf lfgftilsil lyelfnanrl
       61 kkyfsiplal ittslmffpl nafelhilnt snlssiqkiq ngsnqfqels ktmkligadw
      121 qsliiiltvs liffaielqt kiniswkdrl srvfilfisi yilqisikff yfsillnywy
      181 wlimiitavv sdvggfiggk lfskkwinkp fapaispkkt wegfifsisf giivtsglif
      241 gldlfphnia lktlfvafgt llavvgdlyf sylkrmngik dyskilldhg gvldrydsvs
      301 fvglfmfill vfa
//
LOCUS       WP_457601970              85 aa            linear   BCT 27-JAN-2026
DEFINITION  YlxR family protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601970
VERSION     WP_457601970.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Osipiuk,J., Gornicki,P., Maj,L., Dementieva,I., Laskowski,R. and
            Joachimiak,A.
  TITLE     Streptococcus pneumonia YlxR at 1.35 A shows a putative new fold
  JOURNAL   Acta Crystallogr D Biol Crystallogr 57 (Pt 11), 1747-1751 (2001)
   PUBMED   11679764
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10515383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..85
                     /product="YlxR family protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=10113
     Region          1..77
                     /region_name="YlxR"
                     /note="Protein of unknown function (DUF448); pfam04296"
                     /db_xref="CDD:427847"
ORIGIN      
        1 misnqiysts elirfnydkn nkeisldlnn lkknrgayfy pskenwekic ttkalnrvfr
       61 tnvsretyks iqeqleelvw tktke
//
LOCUS       WP_457601993             354 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457601993
VERSION     WP_457601993.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..354
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39944
     Region          4..341
                     /region_name="LLM_2I7G"
                     /note="probable oxidoreductase, LLM family; TIGR03858"
                     /db_xref="CDD:274817"
ORIGIN      
        1 mkielgistf gettplaetk kpishperir nmieeielad kvgldiyaig ehhredfavs
       61 mpeiilaaga vntkniklss avtvlsssdp iriyqafsti dalsngrsei mvgrgsftes
      121 fplfgyslkd ydelfeekld mlqainanek ldwkgrlthd vnnrgiyprv englpiwvat
      181 ggnphsivai arrelpivfa tiggdplrfk slvtiyrsaw ksfgndwskl riaghswgwi
      241 eeddqkakdn yfipvkqlvd tiakdrrswt gmtrkqydfe vseegaifag spetvakkii
      301 rimegleldr fmlhlpvgsm phkktlkaie lfgtkvapiv reyfknrefv reik
//
LOCUS       WP_457601931             326 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate--ammonia ligase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457601931
VERSION     WP_457601931.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Nakatsu,T., Kato,H. and Oda,J.
  TITLE     Crystal structure of asparagine synthetase reveals a close
            evolutionary relationship to class II aminoacyl-tRNA synthetase
  JOURNAL   Nat Struct Biol 5 (1), 15-19 (1998)
   PUBMED   9437423
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006461
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..326
                     /product="aspartate--ammonia ligase"
                     /EC_number="6.3.1.1"
                     /GO_function="GO:0004071 - aspartate-ammonia ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0070981 - L-asparagine biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38135
     Region          1..326
                     /region_name="AsnA"
                     /note="Asparagine synthetase A [Amino acid transport and
                     metabolism]; COG2502"
                     /db_xref="CDD:441996"
ORIGIN      
        1 myksklnike tqlaiqdlkf tfskslskal nlvrvsaplf vesktkindg lngetpvlfn
       61 alniesslei vhslakwkrh alqkykfnvy egiwtdmnai rreevldnth sfyvdqwdwe
      121 miiqkkdrnl sflksivkki yktirftehq lifnfpqlrk klpekltfis seeleelypn
      181 leaaereney akkhksffvy kigyplkdgi khskrafdyd dwtlngdlif ydyvnnkaie
      241 vssmgirvda kaletqqkfe nipnselsfy hekilndeyp ltigggvgqs rlsmfllekk
      301 higevqvgiw tkeekekaeq envell
//
LOCUS       WP_457602007             256 aa            linear   BCT 27-JAN-2026
DEFINITION  TatD family hydrolase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602007
VERSION     WP_457602007.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..256
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29279
     Region          5..250
                     /region_name="TatD_DNAse"
                     /note="TatD like proteins; E.coli TatD is a cytoplasmic
                     protein, shown to have magnesium dependent DNase activity;
                     cd01310"
                     /db_xref="CDD:238635"
     Site            order(9,11,127,150,200)
                     /site_type="active"
                     /db_xref="CDD:238635"
ORIGIN      
        1 msikyvdahc hpikqyykdn yqsiekaysk gvkvmmitgc nlaeneevik icshfdytfp
       61 vigihptevn gaidginlek qitkevkgig eigldyywkd ktpelqkesl isqikvaekf
      121 nlpvvihmrd ayedlydilk qfpnvkfmih tysgnldwak kfyelgcyfs fsgvstykna
      181 ketievldwl pvdriltetd apylspaakr gninysnyvi ftahfiagik kmpiekfadq
      241 vlknakglfk ldasrk
//
LOCUS       WP_457602010             331 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
            [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602010
VERSION     WP_457602010.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..331
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=36664
     Region          3..320
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mqkritfigt gawasglatv ltknnhfvtm wgidqkeidd innglntkyf gnskfnnpnl
       61 lqatndlkka legtdlivla vpsaafdsvi pkilensdsk klnilnvakg idsktkkffs
      121 evikkefgnr lencatligp sfavevfqnv mtmanivgin qiflewvaal fnndkfklvi
      181 ntneqgaelf aalknvlaig lginqysnpd lknpqaalls igvkeinkiy kalfekadde
      241 iafdlagigd ifltcsseks rnfsfglqvg eygvqkalem ntktvegyrt anifksilkd
      301 lkihvpffen iidvlfnnkp qselldfink y
//
LOCUS       WP_457602021             403 aa            linear   BCT 27-JAN-2026
DEFINITION  replication-associated recombination protein A [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457602021
VERSION     WP_457602021.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..403
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=45876
     Region          3..402
                     /region_name="PRK13342"
                     /note="recombination factor protein RarA; Reviewed"
                     /db_xref="CDD:237355"
ORIGIN      
        1 mknlandlrp qtlndiigqk qavnllkqia knklrtsfif fgeagtgkts saialandlk
       61 mkyglfnati nskndllnli enneiliide ihrlnkdkqd illsylefdk iivyattten
      121 pyfrvnpalr srmqiiqfnk lseveifdgl knviknnyan mkisdevlma lvrhstgdyr
      181 sslndlqlly llkndeeitf edikklipni nfysdmnssa hynnlsafhk slrgsdvnaa
      241 lyygtiilks gdyqglfrrl lahsyedvgl adpnlalrvn nafdvveklg fpeanlpvyy
      301 aiiasalapk snsvykamhk iidfvdagni yevpkhlrds hyksasklgd gigykyphdf
      361 pnsvvkqtyl pkeikdktff tysnndlski keyydflqkl nke
//
LOCUS       WP_457602043             355 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602043
VERSION     WP_457602043.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..355
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39301
     Region          41..289
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mfskssfwak lslkfgflsk ysakkqaetk aqslsgsiid krtpaiqplt iliptlliit
       61 lftvvplvln iknaffidlp dgtsqftfqn fenvindpaf avafrnsliy glivlpfvma
      121 isllisstia nvyrkwargi wqtifflpyv tnaiavslsf iqlfdpnglf nktfnlnvpw
      181 lesnnqfgfs allpiiiqgi wsglafnvli fttamlsvdk nlyrsasidg igtikqffti
      241 tlpsiksttt flitmgiing ikvfplaifn nqpadaiqng astlmifvyt ftkaanyaya
      301 saaalslfii gviystlirg gfntilkvsq nlgeynvwtr iknspvmiey qakkk
//
LOCUS       WP_457602044             336 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602044
VERSION     WP_457602044.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..336
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37559
     Region          75..336
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mfelglkirq wwsniklrkn rentahqvhe tnvfamafgl flktlvlvtl slvilfpfff
       61 mfmisfmgkq qalelssnfs lipqefspdn ytkamgiyaa gedveslkkg idylpslgft
      121 fanvvfsvvv kilvtmlagy afslktwrfk kllwsilisl lvlpevalls gqywmvtrld
      181 eaiklkqsfv gmvaavsvpf lasiftalmf rnafeaipkr lkevatvdga vgakyffkia
      241 vpmvtptilt vtiltalasw nsylwpalis dntftvlsvw ifsvgqdlsd panprpmpsl
      301 kmaaailaia pmfivyllar kwimrsisrq gstikg
//
LOCUS       WP_457602048             295 aa            linear   BCT 27-JAN-2026
DEFINITION  5'-3' exonuclease [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602048
VERSION     WP_457602048.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
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="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     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=33731
     Region          1..284
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 msnskfllid gnflmfqsfy asynpytmns lmkspegiyt ngvhvfllsl tklidfikpd
       61 ylfvafdaqg ktkrhenyeg ykagrtkape iifeqfdlik qiltglnikw feqigdeadd
      121 liatlaqnkn tenyifskdk dllqlvnent svishnkktg efelinldnf knligilpyq
      181 ipdfkglagd ssdnlkgveg igektaikll neyetlenly nsidlikgkt kekllldkes
      241 affckslail nrnvqmdkei lkyanfiyfn naegkellkk hnlkvaynfl fkvni
//
LOCUS       WP_457602052             222 aa            linear   BCT 27-JAN-2026
DEFINITION  signal peptidase II [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602052
VERSION     WP_457602052.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Paetzel,M.
  TITLE     Bacterial Signal Peptidases
  JOURNAL   Subcell Biochem 92, 187-219 (2019)
   PUBMED   31214988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..222
                     /product="signal peptidase II"
                     /EC_number="3.4.23.36"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25488
     Region          52..190
                     /region_name="Peptidase_A8"
                     /note="Signal peptidase (SPase) II; pfam01252"
                     /db_xref="CDD:460136"
ORIGIN      
        1 maeinglnpk rnfkeiinew wkkrvqnfqt kineakqnpk klafkylivl givfllvlid
       61 qltktylfnw nsdhtdgawt sigyydfgii girsighygv tiiplkksav vinivqtisi
      121 liilvllivp fysnnwnyli itafivagdf gnmldrfife ggmvkdilfl pflerwtskq
      181 lgtfnfadac iiigglylii ynlanffkek nsleetekke se
//
LOCUS       WP_457602055             296 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602055
VERSION     WP_457602055.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..296
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34736
     Region          3..275
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(27..28,30..31,34..35,70,74..75,78..79,126,130,137,
                     140..141,146,169,173..174,176..178,180..181,184..185,
                     188..189,214..215,217..219,221..223,225..226,228..229,233,
                     236..237,243,245)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(172,176,179..180,182..183,228,231..232,234..239,
                     242..244,248,250)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(193..200,216,219..220,223)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mntpfgsysn nntfvhrlda rlklivnili iimaffsdyf fsmflimipv mtayliatks
       61 fkallksfrm plligififf invytmkind piiqtyeyvw qrqvywdiyk giygiyygtv
      121 irtvalilri ytmilatsll vmttkpvllt kaiedllwpl kllfipvhii amiisitlrf
      181 iptlldeaqr iikaqasrgi dfrngkikek arsfttliip lfvisfsrae dlsnametrg
      241 ydpyekrtry rslkwewqdy lifilfvgll ifiivsqsky vpdflptwyk itksnf
//
LOCUS       WP_457602059             228 aa            linear   BCT 27-JAN-2026
DEFINITION  pseudouridine synthase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602059
VERSION     WP_457602059.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..228
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26140
     Region          1..219
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mkiekvisnf spysrseakt liktsqvkvn nliidksvdf dlnkdileik nqhfftcekl
       61 ylvmnkpknv vcshnqnegq tiydlipsky kyiknlqtfg rldkdttgli iisndgnlnh
      121 llmsnkkhie ktylatldkp fnsadliklt qgleiaknei tkpakahiin snlieltite
      181 gkyhqvkrmf qalnykvvel kriklnnlil ndlelgqvkk invenllk
//
LOCUS       WP_457602066             303 aa            linear   BCT 27-JAN-2026
DEFINITION  SPFH domain-containing protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602066
VERSION     WP_457602066.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..303
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33829
     Region          8..293
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mtdgaiigli lglffliilm iflaigikvv ketdfliier fgkyrttlqk ginfiiplid
       61 kirikdntke kvfdfpaqqv itkdnatilv dtvvylkiqd pklfaygaek pivairnlts
      121 ttlrnligel eldqsltsrd tinskltail drasdpwgik vnrielqnim ppkevqeami
      181 rqmqaerdrr akileaegir eseilkaqgy keslilkaea nkrkiileae aikeqltlea
      241 egkksalell nqspinesil qlkaieqlgt langnatkii lppnlkdvas smavaqamie
      301 kek
//
LOCUS       WP_457602067             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent 6-phosphofructokinase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602067
VERSION     WP_457602067.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..336
                     /product="ATP-dependent 6-phosphofructokinase"
                     /EC_number="2.7.1.11"
                     /GO_function="GO:0003872 - 6-phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006002 - fructose 6-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36715
     Region          2..313
                     /region_name="PRK03202"
                     /note="ATP-dependent 6-phosphofructokinase"
                     /db_xref="CDD:235111"
     Site            order(12,42,73,104..106,108..109,126,128,130,170..172,233,
                     260,263)
                     /site_type="active"
                     /db_xref="CDD:238201"
     Site            order(12,42,73,104..106,108..109)
                     /site_type="other"
                     /note="ADP/pyrophosphate binding site [chemical binding]"
                     /db_xref="CDD:238201"
     Site            order(22,26,55,60,63,136,148,152,155,183..184,186,222,
                     272..273,277,284,299)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238201"
     Site            order(22,26,55..56,59..60,155,186,188,220,222,225..226)
                     /site_type="active"
                     /note="allosteric effector site [active]"
                     /db_xref="CDD:238201"
     Site            order(126,128,130,163,170..172,233,254,260,263)
                     /site_type="other"
                     /note="fructose-1,6-bisphosphate binding site"
                     /db_xref="CDD:238201"
ORIGIN      
        1 mikkiailts ggdapgmnsa irgvykaars knievllvre gfkglcennf idasqidldf
       61 wncrggtcif tsrhldfrnp lihnqaikni kdndidalvv iggdgsfaga qllyenginv
      121 iaipatidnd inssdysigy dtalntivrs idsirdtsds hkrivivevm gnrcgdlaly
      181 sglatgaeii siseaplsye eiakrcaeyt lkyddkafns hkinrsiivv vseklydldk
      241 lrdliaskts wstrysilgy iqrggnptaq ervlaslmgi kaidllcdnq sgiaicarkn
      301 dllavpllka lsqksdskkk arkkaikfnd ihllna
//
LOCUS       WP_457602068             792 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602068
VERSION     WP_457602068.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..792
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89832
     Region          6..788
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mshnndydsk ayldklnaww raanylsvgq mylrknpllr qpitaddvkl ypighwgtis
       61 gqnfiyahln rvinkydlnm fyiegpghgg qvmisnsyld gsytelfpei tqdiegmtkm
      121 fkrfsypggt ashaapetpg siheggelgy amshatgail dnpeviaatv vgdgesetgp
      181 laagwfsnif inpvkdgavl pilyinggki snptifarks dkdielyfkg lgwdplfvsg
      241 sdhmlmheqm akvmdeaiqk ikaiqteark gqandakmgn wpviifrspk gwtgpatwkg
      301 eqvegsfrah qvpipvsakd mthidelvkw lesykpnelf dengrifadi qalapkgdkr
      361 mamnpitngg inpkplvmpk wedfalkiek pgaikaqdmi eagkyfadmi vknpdnfrif
      421 gpdetksnrl wevfkvtqrq wlqgtdkald ewigpegrvi dsqlsehqae gflegyvltg
      481 rhgmfasyes flrvvdsmft qhfkwmkkaa hvkwrkdyps lnviatstaf qqdhngythq
      541 dpgilthlad kspeyireyl padtntmlav fdkafqerev inlivtskqv rnqfytkeea
      601 kelvekglki idwasnvknn eepdlvmvas gtepnleala aisylhkayp elkirfvnvv
      661 dllrlrhpsi dprgysdeef daiftkdkpi vfafhayegl lrdiffhrhn hnliahgyre
      721 ngdittsfdi rlmsemdrfh maisaakavy gdkatdfine menkvaehka yiqeygydmp
      781 evvnweweni nk
//
LOCUS       WP_457602072             395 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602072
VERSION     WP_457602072.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..395
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43276
     Region          5..394
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mkkhiddlsl kgkrvlmrvd fnvpmkngii tsnkrivasl asikkvineg gklilfshlg
       61 rvkteedlas ktllpvaiel srllnksvtf vnqtrghele kavalmqdgd vilvqntrye
      121 dlnnkaeskn dsnlgkywas lgevfindaf gtahrahasn vgisqniees aigylvanel
      181 ntlnrlvnep qkpfyaivgg nkisdkilml eklihevdrm figggmaytf lkakgknigk
      241 sifeadqley akefydkyqd kiwlpidfkv atrfandvpv iqeveisdey egldigpktv
      301 tkftnalaka ktvvwngplg vvefsnykqg tleiakaiss ipnvysvigg gdsaaaiina
      361 gmenkfshis tgggatlefl kgvelpaiva iqdkd
//
LOCUS       WP_457602092             423 aa            linear   BCT 27-JAN-2026
DEFINITION  Y-family DNA polymerase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602092
VERSION     WP_457602092.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Yang,W.
  TITLE     An overview of Y-Family DNA polymerases and a case study of human
            DNA polymerase eta
  JOURNAL   Biochemistry 53 (17), 2793-2803 (2014)
   PUBMED   24716551
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Pata,J.D.
  TITLE     Structural diversity of the Y-family DNA polymerases
  JOURNAL   Biochim Biophys Acta 1804 (5), 1124-1135 (2010)
   PUBMED   20123134
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yang,W.
  TITLE     Portraits of a Y-family DNA polymerase
  JOURNAL   FEBS Lett 579 (4), 868-872 (2005)
   PUBMED   15680965
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..423
                     /product="Y-family DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=48199
     Region          7..344
                     /region_name="PolY_Pol_IV_kappa"
                     /note="DNA Polymerase IV/Kappa; cd03586"
                     /db_xref="CDD:176459"
     Site            order(10..11,13..15,43..44,47,50,105,158)
                     /site_type="active"
                     /db_xref="CDD:176459"
     Site            order(35,59,103,105..106,151,183..189,220..221,245..252,
                     278,301..304,306,335..336,340,343)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176459"
ORIGIN      
        1 mykktifhid fdsyfvsahr svepnlmnkp vavgrklsrs iatsisyelk nkgvktgwpv
       61 yrilqvepkt ifvepdfely ttisnqifqf vkekftdkme ifsidefwld vtdiinetdp
      121 lilatkiqkd ilykfkipat vgisenkfla kmasglgkpf glkvidntny kseiwplnig
      181 effgigkate sklkklgfnt igqlananpn dlelnnlfrs rlkivldean gkgssyvnna
      241 vteakslgad ytfpyynide fedllkmars latrvakqaq dknllahvva inlrdvdkhw
      301 hskqeklefp tnnldeimhh lvyllhslwn geglrgigvr lmnlvnasev giqlklfstn
      361 pyditidsfv enpkikkvks iiktinrqyh naslntadvl vkraktkhlr ffsiptledk
      421 kek
//
LOCUS       WP_457602093             384 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457602093
VERSION     WP_457602093.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 384)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..384
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=43046
     Region          1..377
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mkqirnffpl lkdivyfdns amaqkpsvai qkmnefytry avstrtsest igienknkit
       61 tlrnqvrnli nanendkvif tsgatdslnk ialmlknwiq agdeillsay nhssnigpwi
      121 nianekkakv vfsenifddi npktkiiafs qksnslyeti dmkaiyakak lnniliinda
      181 aqaiisepvd fkhsdvvafs ankfygptgf gilaikeels kqltpafvgg gvvdkidacg
      241 imqlknndss fepgtpdlaa iyffsesinf fnsyigydft qkklkelsny ayeklqtvpn
      301 ltlynpkddh iilftikntg tqdiahylat kniyvrsgif caqylrnlnn nesfvrvslg
      361 vynteeeidi lvealkeggd flvl
//
LOCUS       WP_457602096             249 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphonate ABC transporter ATP-binding protein [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457602096
VERSION     WP_457602096.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
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="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     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=28464
     Region          4..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 mpksvikfen vnlkypkseh nvlsnlnfel ksgemvaiig qsgvgkstif kaivrnlkpi
       61 sgqiklfnen innfkkskwr helqnigflt qkpnliafdn vyinikrniv nnysnrlfqf
      121 lgilnkkqkq aiynalekln ildkafirid elsggqqqrv eiakllikes kiiladepta
      181 sldfktanev lnilqkitke nqittivnih dlslindyfd rvlilskgkl ildsevenln
      241 lkqlqdyik
//
LOCUS       WP_457602104             449 aa            linear   BCT 27-JAN-2026
DEFINITION  replicative DNA helicase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602104
VERSION     WP_457602104.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..449
                     /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=52406
     Region          22..449
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mktktmtpme nnnginfisq lleeqvlslv lnypanletv vntlreedfy yrnnrelfiv
       61 fkkiyeeekp inddivliea nkmnftdsid vnflkhiyfc wafqnslnvy mrelmnltnl
      121 rflelkclet ldflqeqskn kkriesneiv ndikdwteff krdvfnieee npaskftefl
      181 ttltnepkdk ptltyiktld ekiggfkkgs liilaarpgv gktafaldia trisqrkkvl
      241 ffslemsyte lfkrvmanin nlplnelerv yqldketkak finknqalrk lklnifdktf
      301 efngivslik kefekekpsl ividylqlln iestrlkkdi nraqeisqit rslkllamel
      361 nvpilllsql nrnleqtnry prasdlkdsg sieqdadqii llhreirvet mtktptdsei
      421 inviigknrs getgkiellf kksitgfre
//
LOCUS       WP_457602113            1076 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction endonuclease subunit R [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457602113
VERSION     WP_457602113.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1076)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1076)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1076)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..1076
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=127074
     Region          28..925
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 miersivlqn gnetvvyeye ktkqtrktye seselenqfi kklqnlgyey lselndnskl
       61 kenlriqlqk lnnieltdse wktfydtylk sgdifekarr iqedyiysfs rengqiinfm
      121 lidkknlann klqvinqyka ekgsfknryd vtillnglpl ihielkrrgi dlkeafrqie
      181 ryqyesfwse dglfeyvqif visngtqsky ysnttrwnkv ngknkidynn kkrtgfqrns
      241 nsfeftsywa dqknnliedl vdfaeyffnk dtilniltky cvltvdekll vlrpyqivav
      301 ekiarkiama rnnkvqnrie aggfiwhttg sgktltsfka aqllsqdpqi dkvvyvvdrr
      361 dldyqtlkef nrfkegsvnh nvttkilqeq iednnpdkki ivttiqkldk yvksktfdri
      421 ktdnrefvli fdechrsmfg qmrrnifsff kksyifgftg tpilkenaik eeffrtteel
      481 fgqclhhyti ldairdknvl pfkvdysgsk dinlkegnfd knsfikhpqr issnvkyvle
      541 nynrkthrsi tykmnvitni hdvvknqnqn eekrikeing fnsifathsi enaiqyyqef
      601 krqqselaee kklkialiyt yhandikedk ydslvsegfa ieaptssqkd vlaaaikdyn
      661 emfktdfdlg amdgfqnyyk dvslrlknre ldmlivvnmf ltgfdapsln tlwvdkglry
      721 qgllqaysrt nrifneikna gnvvalwdlk entdeaitlf snkeaigivt lkpfefyyee
      781 gdekivsyvd tlkklkaefp ldtnfvdikn nvekskdfik tfnnylklkn llvtfdefde
      841 skefpvdnnn eeliteydiq nynsryldln davsrsyskr eaiqqesifd eeivflteli
      901 aqdeinvpyi lnllsklkkq lneqnkaqen rvesnnliln nkeninkkde kidvdkiwll
      961 vestpllrdk kgllsefmkq kdleiadwnk fvskqfkttv eklveeenlk eekvfellnk
     1021 cfekdsfvyk skeikdmqks gtfrfgvlww khneeknrii eklhkifktf ngayay
//
LOCUS       WP_457602130             235 aa            linear   BCT 27-JAN-2026
DEFINITION  B3/B4 domain-containing protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602130
VERSION     WP_457602130.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Roy,H., Ling,J., Irnov,M. and Ibba,M.
  TITLE     Post-transfer editing in vitro and in vivo by the beta subunit of
            phenylalanyl-tRNA synthetase
  JOURNAL   EMBO J 23 (23), 4639-4648 (2004)
   PUBMED   15526031
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Mosyak,L., Reshetnikova,L., Goldgur,Y., Delarue,M. and Safro,M.G.
  TITLE     Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
  JOURNAL   Nat Struct Biol 2 (7), 537-547 (1995)
   PUBMED   7664121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..235
                     /product="B3/B4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=26965
     Region          2..221
                     /region_name="B3/B4"
                     /note="B3/B4 domain (DNA/RNA-binding domain of
                     Phe-tRNA-synthetase) [General function prediction only];
                     COG3382"
                     /db_xref="CDD:442609"
ORIGIN      
        1 mkkikinekf feifptskig ilivnnlnnn ydgneiaytn mlknamneak khlqaevfsd
       61 npiiknwrea yskivtkkga rcsieallkr vnngneinni nplvdiynai slkyglpcgg
      121 edldkivgdf eltfakgdef fqtygseevd lprkdeliyk ddegaicrsw nwrealrtil
      181 ttetknailv ieindnkyek elisalkemk hlietqlngq vqeyifdinf qeaei
//
LOCUS       WP_457602131             193 aa            linear   BCT 27-JAN-2026
DEFINITION  chromate transporter [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602131
VERSION     WP_457602131.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Nies,D.H., Koch,S., Wachi,S., Peitzsch,N. and Saier,M.H. Jr.
  TITLE     CHR, a novel family of prokaryotic proton motive force-driven
            transporters probably containing chromate/sulfate antiporters
  JOURNAL   J Bacteriol 180 (21), 5799-5802 (1998)
   PUBMED   9791139
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..193
                     /product="chromate transporter"
                     /GO_function="GO:0015109 - chromate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015703 - chromate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21895
     Region          7..173
                     /region_name="Chromate_transp"
                     /note="Chromate transporter; pfam02417"
                     /db_xref="CDD:460551"
ORIGIN      
        1 mkkfwiiflf ilkvsfigfg ggnallpviq neavqkrkwl sqeefddivv vtnmlpgpsv
       61 iqsisyiaik elgkfwgslc tliailphvl fafalyiaat flpleylwtv avgvlstiig
      121 ilivfgwtym qktrkliklp lwiflflftf afcffvpvpg nlpilvmlav fliialialf
      181 sylkhkkekr kkc
//
LOCUS       WP_457602028            1470 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-directed RNA polymerase subunit beta' [Mycoplasmopsis
            gallinarum].
ACCESSION   WP_457602028
VERSION     WP_457602028.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 1470)
  AUTHORS   Chen,T. and Romesberg,F.E.
  TITLE     Directed polymerase evolution
  JOURNAL   FEBS Lett 588 (2), 219-229 (2014)
   PUBMED   24211837
REFERENCE   2  (residues 1 to 1470)
  AUTHORS   Werner,F.
  TITLE     Structural evolution of multisubunit RNA polymerases
  JOURNAL   Trends Microbiol 16 (6), 247-250 (2008)
   PUBMED   18468900
REFERENCE   3  (residues 1 to 1470)
  AUTHORS   Morse,R., O'Hanlon,K. and Collins,M.D.
  TITLE     Phylogenetic, amino acid content and indel analyses of the beta
            subunit of DNA-dependent RNA polymerase of gram-positive and
            gram-negative bacteria
  JOURNAL   Int J Syst Evol Microbiol 52 (Pt 5), 1477-1484 (2002)
   PUBMED   12361249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478913
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1470
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..1470
                     /product="DNA-directed RNA polymerase subunit beta'"
                     /EC_number="2.7.7.6"
                     /GO_component="GO:0000428 - DNA-directed RNA polymerase
                     complex [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003899 - DNA-directed RNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /calculated_mol_wt=166097
     Region          13..1403
                     /region_name="PRK00566"
                     /note="DNA-directed RNA polymerase subunit beta';
                     Provisional"
                     /db_xref="CDD:234794"
ORIGIN      
        1 msklikrntn vpiekitlsl tnqkrdvnew smgevtkpet inyksykper eglfdelifg
       61 pttdykcpic gtkykksden svcvktpmcq kyqpkilpki arrsrmghih lenpvvhfwf
      121 fkidhsiisk llglrvansn ipvtkadlek liyykshivl edgglkslrk ntiidisdaa
      181 iiyqdallel rdrfnkdned eadsyeiine aleqlqeyat skvgkdygid fyeyneiiee
      241 fsdakistgs haieyllshi dlekeveeie keitsinnqi aanssatkiq erqklykrla
      301 vlnafiksgq npldmliydl pvipadlrpl vqldggrhst sdinelyrri iirnnrlkkw
      361 aetaapmlim qneyrmlqes vdslidnark kpnpvqskdg rplksisdal tgkkgrfrqn
      421 llgkrvdysg rsvivvgpel kmhqvgipre maaklfepwi ikeliqskdn ninsikagkk
      481 avenldpiiw syvekaiegr pvllnraptl hrlsiqayep vlirgkaikl hplsctpfna
      541 dfdgdqmavh vpispqavre arelmlaskn ilgpkdgepi inpgqdiilg lyyltmeksg
      601 akgegsyfgt yedmltayen ntvdlharvv lpiselkkkf invpnnmqyi vstvgkfifn
      661 rvfpntfefi fgkyveiktk envdgsitkt ekeiihtsen veqlahytlp ygvnfkeaia
      721 lmpinlplak kdiakivkkv ynnyvsvinm eslasvieti denslkdifn kcaelkdhkg
      781 dtinishaei ldkliqeeyv kisqkvarky rnkeaiwdad dytalleivw fkytnivasi
      841 ldeikqlgyh fstisgttia vsdvlthpnt kerikegdky ieelkeyyed glltdderys
      901 ltirkwteik daiekdlkal tkeypnnplf mmftsgargn ssnfvqlagm rglmnnntki
      961 lkadaendrv vrstveipvk ssfldgltsy efyssthgar kgltdtalnt aksgyltrrl
     1021 vdvaqgitvr eedcgtdygf lvhdirdtkt ntiiesleer iegrftnkpv fdlngnliig
     1081 anelitpeia saiknagvee veirsvlscy tqngvckkcy gkdlalnrvv nigeavgvva
     1141 aqsigepgtq ltmrtfhtgg vagveditgg fgrlmelida ydspwgrpav iaenygvvtn
     1201 itdsngykli hvefedfdnk kqikiydgks drrirvkvgd kvvpgqklie gpiilnklle
     1261 vadtravqny llkeiqrlyr lqgitisdky ieiiirqmls kimitnpgds kffsgnlvdi
     1321 fvyqkesarl inegkkppfg evkikgakqt pllsssflsa asyqetpkil vnasiakqvd
     1381 nliglkenii lghkipagtn snyeiggkyd irdpheyfqs klsptdidln envndqedan
     1441 isdeiyellt fndneeqela defdsyenee
//
LOCUS       WP_457602132             225 aa            linear   BCT 27-JAN-2026
DEFINITION  chromate transporter [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602132
VERSION     WP_457602132.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Nies,D.H., Koch,S., Wachi,S., Peitzsch,N. and Saier,M.H. Jr.
  TITLE     CHR, a novel family of prokaryotic proton motive force-driven
            transporters probably containing chromate/sulfate antiporters
  JOURNAL   J Bacteriol 180 (21), 5799-5802 (1998)
   PUBMED   9791139
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..225
                     /product="chromate transporter"
                     /GO_function="GO:0015109 - chromate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015703 - chromate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25749
     Region          15..>146
                     /region_name="Chromate_transp"
                     /note="Chromate transporter; pfam02417"
                     /db_xref="CDD:460551"
ORIGIN      
        1 mlvgtllilv lviaislsvf gggqvfmpmf nwlwklsnel fktnisdnii nkvftisnat
       61 pgvvstkfaf ftgfiyfnye gaqfnwwgii fmlitylifc lpailimila mkylnkvknn
      121 syikkalili kpvvagimit igvqlllniw lpfitfneig tyfainwnks klsffrnwrl
      181 ialliyvpvn iiinlilykk mkiglfylml gsiissllvf epwln
//
LOCUS       WP_457602133             325 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602133
VERSION     WP_457602133.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..325
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39129
     Region          3..>99
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkkidlsili pchninklgf fslkhimkfr skyeieilvl ndysddntle ilnnlakkds
       61 rikifnlsdy tqkqgigfnr dflisqakge yfffiddddk lnlknfnfll dnflykydli
      121 sakhyctyav tkkmqmkvfn ipqykcktge yyshdlifkn llfawgkivr kniylqnkvq
      181 nniffkqkiy edldvvyswy lnqnikcfyl nknlieyrir knslstnlnk aydkfllaiq
      241 tyrnsfnkik elnwlnekel kqykfkaine llimiyalnl stkqnlflei knelrkline
      301 tnfqnyvfat kftkfftkqa lkklk
//
LOCUS       WP_457602134             453 aa            linear   BCT 27-JAN-2026
DEFINITION  M17 family metallopeptidase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602134
VERSION     WP_457602134.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11109704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..453
                     /product="M17 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50936
     Region          146..434
                     /region_name="Peptidase_M17"
                     /note="Cytosol aminopeptidase family, catalytic domain;
                     pfam00883"
                     /db_xref="CDD:459978"
     Site            order(150,152..154,199,201,230,236,240,243,246..247,279,
                     281..284,286,288..292,298,300,304,341..345,348,374..375,
                     377,382,384..385,391,393,403..404,406)
                     /site_type="other"
                     /note="interface (dimer of trimers) [polypeptide binding]"
                     /db_xref="CDD:238247"
     Site            order(226,231,238,248,307,309,311,336)
                     /site_type="active"
                     /note="Substrate-binding/catalytic site [active]"
                     /db_xref="CDD:238247"
     Site            order(226,231,248,307,309)
                     /site_type="other"
                     /note="Zn-binding sites [ion binding]"
                     /db_xref="CDD:238247"
ORIGIN      
        1 mnklefltkr dsnflliaan hnnlpfewvs kkegaitenl nkneayitik eiknydelve
       61 fikkyilnaq rafqidlksf ndvlnfsnee ilkafissiv fyqaklfnkk reeskknnfs
      121 llfsseneke lftkfnliae nrnkirnlqi mpenycnsvq lanyivedfs diknlkvtvl
      181 dknmieklkm glilsvnkgs theprvvive yngnkkskdk ivfvgkgitf dtggintkgy
      241 hmsgmkydms gsaivayavk tlaelkanvn vaavmmitdn rqdgdaslpe nvyesmsgls
      301 vevtdtdaeg rlvladglyy gatklkattl vdvatltgsv ltalghtysg iwstndekwt
      361 qfekagqish ekiwrmplhe dfhqfnlase vadlnnynns eksdsntaam flkqftnnvd
      421 yihcdvagta dvsgkpqgvl idtlvefall nqk
//
LOCUS       WP_457602143             223 aa            linear   BCT 27-JAN-2026
DEFINITION  LemA family protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602143
VERSION     WP_457602143.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..223
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24849
     Region          40..223
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 msnlfdqrnn qpnpegynpr pvnnyvkaqa sggekffygv iavlslgiyp irlknrlnam
       61 qnqvntaast idtqvakrtn iiislteaas sylkhereif eevakfrgmm gqmqnavsat
      121 esakigneln ngltgfmsrl iavsenypdl kadkvvrdlm eqsvylenei aaarrlynty
      181 vnefntsitt fptnvkaakm nlstlelfqa kasdyerpst kln
//
LOCUS       WP_457602152             600 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602152
VERSION     WP_457602152.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 600)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 600)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 600)
  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 600)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..600
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67545
     Region          8..599
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mktknkvstf tlfksifqfl dkedryfaii gmifaslssa atiigtyftg kaithfflpt
       61 ignpdsfdfn afiiysveig ilfllyavfg flqnkifvnl sfktamrmrk ismekllkmp
      121 isyfdkqktg diistlvndi nnfshsvstl maqffsglts iiltliimtf qsvvlmiviv
      181 llaillfsvt ifmlkqarpa linlqnefgn lnayveemlt nakvtqvldr qesaqvkfns
      241 iahniyshal kgdfwqkifd pwfifssnvi vlvtivlglv fktnnwnvyg idytkvdygm
      301 mvalislifg ltgniqtilt elfqvqlgva satrilkltn lnvpveqtvd idinkiqgli
      361 efnnvsfkyn pdsakyqikn asfyakpgqt iaivgptgag kttiinllsk fyeyqegqik
      421 idnidlktis khdlrdimav vlqdsflfnd tifnnlkiak pdatleevrh iakmvsvddi
      481 imrmkdgynt ivdnsdtsls qgekqllaia railgnkkil vldeatsnvd snteqiiqnt
      541 lqnvvmknkt siviahrlst iknadlilvv ndgeiiekgn hrelmdakgy ywnlytsqfn
//
LOCUS       WP_457602153             603 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602153
VERSION     WP_457602153.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 603)
  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 603)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..603
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68122
     Region          1..601
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mfklmkmipk rlkwffllgs ffilitvlin iffpnlisqf ikliivdnrt ettdiiffdg
       61 riafnnipin daknyliiai vlstlsnial vflgtfiiiy aaencskffr itlfekiqkf
      121 slkniadlks esiitrvsnd iaifweflvn gttilikgmf lvigtvilai wtdlslsivi
      181 aitipslsiv iaiaglstkn llrdtqktve fltknideni ngikviktyn lekqrkavfk
      241 ennqkwyqlq rkssiifmts asvffmlinf lvlgiyglia kefanpnatn lqeviaqqse
      301 slaklntfid ylynlsfgim mmmfflfsmf raivsakrin eiydykiddl yvadgvvlsq
      361 nydldikdln fkyyqeapel tlsninlklp fkhtlgiigp tgsgkstlan liihnylynd
      421 gsikignqel keinsknlhd svgivyqkal lysgtirsnl lwakenateq eiqealenac
      481 aaefvnkfed gldhpvamgg snlsggqkqr lsiarallrk pkililddst saldnlttkk
      541 vienikqnyd cstiiisqki galknannia vmeqgkivsq gkheelinls elynsiytkq
      601 ldq
//
LOCUS       WP_457602154             608 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family oligoendopeptidase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602154
VERSION     WP_457602154.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (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 10176314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..608
                     /product="M3 family oligoendopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=71422
     Region          33..597
                     /region_name="M3B_PepF"
                     /note="Peptidase family M3B, oligopeptidase F (PepF);
                     cd09608"
                     /db_xref="CDD:341071"
     Site            order(391..392,395,419,518,524,528)
                     /site_type="active"
                     /db_xref="CDD:341071"
ORIGIN      
        1 mkqykniqev pkkylfdles ilendtfenw lskyqevldl qiaikdskyd tldayleglk
       61 lnekgalisn kisnylsnns nrelnnplfk elenkvqqin ekfdekfgse tvrfyqniek
      121 ikvwindpkl anyrvslnqd ienynhkldd kieeflvkte sstpnyeepf vlltdsetdy
      181 gyvydqknkk lklnpvsrik flksddailr kntvkqwkka tsqfkqtlan llyqqfkgin
      241 veaklrnyks avsmltsndk vsdevlnklf tkvqslknev hkynqafakf ynlkfkekfn
      301 kkydslrelt nvksnysved aqklvlealn pfgkeymsiv nkafnenwid ymtienkmsg
      361 aysigstygi dkkfilmnfd gqfgsvetla helghslhsy fsdtyndlvn skypillaev
      421 asifneqmly nhilktsknr elkfqilgsm iegffgtvvr qtqwaeyeyn lyakianfev
      481 nssyesiskl yydvtknyvy kplkynpndl iasvsvphfy yhfyvykyai gqlvanyffa
      541 kyelegeeyl qyyinnflkk ggsdlplkil envgvnlldd efyeigfkyi kklikqyial
      601 gneifkkq
//
LOCUS       WP_457602174             786 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602174
VERSION     WP_457602174.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 786)
  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 786)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..786
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=91243
     Region          1..556
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mkltkvqeka vneivsyfnp lnkskvifka ptgagktfmi anvidriinq sngkklifvl
       61 atisdaslpq qlethirkyl pylnnsfeik yvvspssskt gnkikdytan iplmpnggll
      121 ifglasfgkn rifteegild tfidnvknsl dteliyirde ahrandtkre nslnkdteka
      181 neklknaahf yiemtatpkn idnsniveit ekelredetk llkerllyne gideikeeei
      241 ensqllekac qkfkeikedy idkdnkyglk ginpamliqv enktkeneee fnkqieliqt
      301 ilakyhlnwv tyfsddkkds sgreeisldk isknnsdidv iifkvgpsvg wdipracmlv
      361 qlrnvssetl siqtvgrikr npavkgvnne nwdtknpafs yyiysysrvp sieylasfsl
      421 kskyknidfi sgvidknqyy dfkrsseyrn kilnlisknq lqeqcdllie eykdkskiif
      481 esekllntnk riiskaifnt idlalanenl iekqknywnl nlknevlnql kqvaqelkin
      541 pelviyafft lkkseirqiy lnfqeqkhen qlgidykiik aklpdfvaie kddfnnnwnv
      601 fklennenln lksayenayi sketqwiaee stkenffvys snpeksflkk lrsflnkkpi
      661 esnsisvwai npvytgiyfe yidgdikeir ksfpdyliki kdhlvaievk stndydlkkt
      721 tkiekgykkf lhqknlkile dsftlvvykp eedefsgmst ienvnkkiae ydslslflnd
      781 iikeln
//
LOCUS       WP_457602175             576 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific DNA-methyltransferase [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602175
VERSION     WP_457602175.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 576)
  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..576
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..576
                     /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=67761
     Region          70..532
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mqqekdnlid senkekslkd eylekidnls tstfnkdqke lcrtiirnak eedvqniyql
       61 liqriklgfv fdiastpitt nkfitllken kelsfegnnf dlnnskekdv liigenfdvl
      121 nnlivierer ereragldfn ydviyldppy nteatekdgn nlandkenia askfiyrdkf
      181 srngwlnmir erlikartil kengvifvsi ddseqaylkv lmdeifgeen fvcnfiwkkk
      241 nsgsgsdskh irvlteyilm yaknqenlki nkekqdledg sykfydkwid srgkyklkql
      301 dmaslswsek ldyefeynne fyypggsken wlkrknglha ekdwrwrwsk ekllwgiknd
      361 fiefknekif tkqyqfvdne gnlilresvf snlilepngs lgtqeqknif yskvfdhpkp
      421 ielikflinl hakknarvld ffagsgttah avwdlnredg gnrsvtvvtn nendiaknvt
      481 yerlhrislg katdgssnfk wldknkpyen slkvyetkqf sidineslde kinlfiqeia
      541 dlanvylden edkerilyyl kqlyslkdnk eqnetn
//
LOCUS       WP_457602139             293 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide exchange factor GrpE [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602139
VERSION     WP_457602139.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Harrison,C.
  TITLE     GrpE, a nucleotide exchange factor for DnaK
  JOURNAL   Cell Stress Chaperones 8 (3), 218-224 (2003)
   PUBMED   14984054
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10470249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..293
                     /product="nucleotide exchange factor GrpE"
                     /GO_function="GO:0000774 - adenyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0051087 - protein-folding chaperone
                     binding [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=33766
     Region          99..263
                     /region_name="GrpE"
                     /note="pfam01025"
                     /db_xref="CDD:425996"
     Site            order(136..138,140,146..147,150..151,154..155,157..158,
                     161..163,165..169,171..172,190..191,193..195,198,204..205)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271355"
     Site            order(138,149,171,174,218,220..221,223..227,243,252,256,
                     258,261)
                     /site_type="other"
                     /note="Hsp70 (ATPase domain) interactions [polypeptide
                     binding]"
                     /db_xref="CDD:271355"
     Region          190..205
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
ORIGIN      
        1 mkfnfkngdy ikfnlfvrnl knelvedlnl knqelilghe nesfkfnlne ivigheltse
       61 iialqeyneq twklnleild ykssvemnlm qinnkflqel eiknkilsdl kteknnleit
      121 lkdtleilkt lrsenqnkal tlpkeeleka qkyalqkfvd dfsnpfsilk vavnagsnsn
      181 dqavknyvlg fnmvlnqved vlrnhgiief speigsifdp etskvieqie dyekpnntvl
      241 kvtssglklh drvikpaivv vskgkilenq esnkkknafk kkhhfkskkq skn
//
LOCUS       WP_457602188             515 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Mycoplasmopsis gallinarum].
ACCESSION   WP_457602188
VERSION     WP_457602188.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis gallinarum (Mycoplasma gallinarum)
  ORGANISM  Mycoplasmopsis gallinarum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Mycoplasmopsis gallinarum"
                     /db_xref="taxon:29557"
     Protein         1..515
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=57958
     Region          31..488
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mknwkfirkw knsrfysffs flhnkrkkgl kvrfvfiiyl livlagwlfl slpfsqtgne
       61 kvsisdafft aisafsdtgl vtsptystwt itgqaiiail ifigglgifa lkifiinfif
      121 lqrkrtslte lelvsterss snsrmikkvi vdsilfllit fvlfsfilsi yfyfatpwad
      181 nlinkqdigd yispqgnwal sfrygffhsi salnnagfdi igknslsayy gnytlqtifl
      241 ilfligglgy pvihdisnyf rhklankprk yhwslftkls lstyfivtcl gfltmltfeg
      301 lhknpsgfwk vddptlgtyg qklwallfls fssrsagfat fnlaklstpa lfmitmlmfi
      361 gaapsstggg irtttfgili itlfskilgh pqprvfkrri sqnsinnsfm vffislalvi
      421 aigfgistss vdyfgggkvp adtpymhyif etasafgtsg ltvgitdnmn lfskiiisil
      481 mfigqlgits tiliwgkkrn ysryyeyise divtg
//
LOCUS       WP_457602215             155 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Mycobacterium
            intracellulare].
ACCESSION   WP_457602215
VERSION     WP_457602215.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10452013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..155
                     /product="acyl-CoA dehydrogenase family protein"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16325
     Region          11..149
                     /region_name="Acyl-CoA_dh_1"
                     /note="Acyl-CoA dehydrogenase, C-terminal domain;
                     pfam00441"
                     /db_xref="CDD:395354"
ORIGIN      
        1 mpgdnllgpl nggwnvalss lqherqmiwi mnwveikrgl eavrtagagv sgddvytelg
       61 sliadaealr atgyralgne lagrpspead tmkllgsltl qrvwelsaaa agpesagdpd
      121 llferqdala atiyggtsev qrniiaerll glpkg
//
LOCUS       WP_457602628             451 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein, partial [Nitratifractor sp.].
ACCESSION   WP_457602628
VERSION     WP_457602628.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         <1..451
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          37..429
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 vfgdrdvdir grlirmcrkd lcsmnirids isiifflgrw lplsiaigit mgviasmmdl
       61 lvikinglls tqivllflyp llvaaitgyv ikynhevsgp gigfsilhlk tkkylqlhsi
      121 laklfisvlt lsggfiagre gpsfflgigi gewigkaygf gkkfknmlgl igggaftgal
      181 lkaplgssif amelenmydf dyrpfipmiv asivsyltfs ffrgnhafir lthkavwnle
      241 sipyiiamgf avsmviyayt lffhfflkls kmipigrrpl igtiaaipfm vllylisqdp
      301 dilsapvnmn ilsnlaqsgf pigvniaiiv ftivitsltl gfgipgglil pvliigaamg
      361 nifghifpnq lvmftlagmg aglsagaktp laaivmitem shddvvipmt aavitsylts
      421 fgyslylgqe nifrsslkdf rsytqhpkes e
//
LOCUS       WP_457602637             243 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Nitratifractor sp.].
ACCESSION   WP_457602637
VERSION     WP_457602637.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..243
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=27923
     Region          <6..50
                     /region_name="DUF1062"
                     /note="Protein of unknown function (DUF1062); cl01786"
                     /db_xref="CDD:470343"
     Region          58..238
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mekaykllae qegisnkkak elidrglvyv gdqkvkiara elpddtrfri ekpeqiriiy
       61 qddeivavdk pafidsyeie eaiegaqllh rldretsgvl llarnedfar raieafrrrk
      121 vrkeyvawve gvlvepmeid lpihtirkgk aisridkkrg kpaltrvwpd evqgkkskvr
      181 ieietgrthq irlhlahagh pivgdeqygs ptrakrpllh akkitllgrs yeapepkdim
      241 ryk
//
LOCUS       WP_457602671             266 aa            linear   BCT 27-JAN-2026
DEFINITION  3'-5' exonuclease [Nitratifractor sp.].
ACCESSION   WP_457602671
VERSION     WP_457602671.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Rothwell,P.J. and Waksman,G.
  TITLE     Structure and mechanism of DNA polymerases
  JOURNAL   Adv Protein Chem 71, 401-440 (2005)
   PUBMED   16230118
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Shevelev,I.V. and Hubscher,U.
  TITLE     The 3' 5' exonucleases
  JOURNAL   Nat Rev Mol Cell Biol 3 (5), 364-376 (2002)
   PUBMED   11988770
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Zuo,Y. and Deutscher,M.P.
  TITLE     Exoribonuclease superfamilies: structural analysis and phylogenetic
            distribution
  JOURNAL   Nucleic Acids Res 29 (5), 1017-1026 (2001)
   PUBMED   11222749
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Taft-Benz,S.A. and Schaaper,R.M.
  TITLE     Mutational analysis of the 3'-->5' proofreading exonuclease of
            Escherichia coli DNA polymerase III
  JOURNAL   Nucleic Acids Res 26 (17), 4005-4011 (1998)
   PUBMED   9705512
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..266
                     /product="3'-5' exonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30620
     Region          2..219
                     /region_name="DNA_polB_like1_exo"
                     /note="Uncharacterized bacterial subgroup of the DEDDy
                     3'-5' exonuclease domain of family-B DNA polymerases;
                     cd05782"
                     /db_xref="CDD:99825"
     Site            order(6..9,103..104,107..109,169..170,205,209)
                     /site_type="active"
                     /db_xref="CDD:99825"
     Site            order(6,8,109,205,209)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99825"
     Site            order(7..9,103..104,107..108,169..170,205,209)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99825"
ORIGIN      
        1 micifdceti pdielirrnf svegltdaaa iakaqsdfae thngstflpi pyhrvvalsa
       61 viaddfgtfl kvgdfgngsd eeeaiirhff dyieernprl vsfngrgfdm pmlliramky
      121 nlsfpawfdq nnpqlnktkw enyrqryaee fhtdlletlg nfgavrnlkl dllctmagip
      181 gkydvsgdqv tdlyfagele kireycqsdv lntywlwlky ellkgkltpe dyarslgemr
      241 ekmphdrgyy dpftraidde lgrlei
//
LOCUS       WP_457602933              35 aa            linear   BCT 27-JAN-2026
DEFINITION  M15 family metallopeptidase [Nitratifractor sp.].
ACCESSION   WP_457602933
VERSION     WP_457602933.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 35)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 35)
  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 10610297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..35
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..35
                     /product="M15 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0071554 - cell wall organization or
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=4212
     Region          <4..32
                     /region_name="Peptidase_M15_4"
                     /note="D-alanyl-D-alanine carboxypeptidase; pfam13539"
                     /db_xref="CDD:433291"
ORIGIN      
        1 mpqdpavraf kkrgwrwggd whsikdyqhf dknkr
//
LOCUS       WP_457603249             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Nitratifractor sp.].
ACCESSION   WP_457603249
VERSION     WP_457603249.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..360
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40479
     Region          2..305
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          165..358
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mmrtflslvn keiigflraw glvavvlyaf tldiyiagkg ielqaknvsv gyvdesggvv
       61 slkilerlha pqfkppvrfr sqeeldralr nreimvgllf dndfsrdyer nghsrlnvll
      121 dataaaqsfq alqylqhill dfskihfpve lkihklfnpn attswfmsla ellsmmtllg
      181 viltaavfvr ekengtwdmm llmpvdprli ilaksfsqvl ilslgiviat glilfgafdv
      241 pihgsiwaff llsffyafts agiglfvaav sksmievaql aifimmplif lsgawtpiha
      301 mapwlqklsr isplryyieg sesiffrgta wmdlwpyfvg viglgalvyl ygfrkigrlf
//
LOCUS       WP_457603320             258 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Nitratifractor sp.].
ACCESSION   WP_457603320
VERSION     WP_457603320.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..258
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27296
     Region          1..258
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msdilkigky eftsrlivgs gkypdfqttr datlasgsem itvavrrvni tdpdeenlmd
       61 yfkgtdvkfl pnsagcttae eaitlfrltr eatgidlikl evigdtaktl ypdvietlka
      121 cevlakdgft imaytnddpi vakrleeaga aavmplaapi gsglgiqnrf nvvfikeavn
      181 vpvivdagig casdaaaame lgadgvltnt aiaqaenpie maeamkhavl agrlsykagr
      241 ipkrpfatas spvdgmif
//
LOCUS       WP_457603362             113 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Nitratifractor
            sp.].
ACCESSION   WP_457603362
VERSION     WP_457603362.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..113
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12133
     Region          1..113
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 metytkklee ikkligdlqk eapeqikafd afmaavekps aldrkskeli nlalavaaqc
       61 ewcialhtkg aldsgasrae iidaamqavl mhggpalmym tpviealdef gak
//
LOCUS       WP_457603459             299 aa            linear   BCT 27-JAN-2026
DEFINITION  M15 family metallopeptidase [Nitratifractor sp.].
ACCESSION   WP_457603459
VERSION     WP_457603459.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 299)
  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 10610297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..299
                     /product="M15 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0071554 - cell wall organization or
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=34547
     Region          188..253
                     /region_name="Peptidase_M15_4"
                     /note="D-alanyl-D-alanine carboxypeptidase; pfam13539"
                     /db_xref="CDD:433291"
ORIGIN      
        1 mkkvkwmmwv lifsmlgtaa ygkcdanaqr lvraypdhlk ecrdnrivwr dgtkmlyddg
       61 kkksfeslln qadiedmfrf rypkgasgys rsrgpsknyd pgrirnekff rkmygnsaae
      121 vrshliripw lprssggryr itvtringvd ralaavsrdl drlvarnpsl kkylappggg
      181 fywrtiagth rlsvhsfgaa idinvkhsay wrwggkhyry rneiplsive iferhgfiwg
      241 gkwyhydtmh feyrpellgg erstpptgks daeaqrqkvh hsspglmeki eelndgrsl
//
LOCUS       WP_457603500             284 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603500
VERSION     WP_457603500.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30919
     Region          88..284
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msdtaittgr apsvympsae alatvlapae rparpsalsa sltfgwrall kikhvpeqlf
       61 dvtafpiimv lmftylfgga ladspraylq fflpgimvts vvmitmytgi glnsdiekgv
      121 fdrirtlpvw rpsalvgmif gdvlryvlaa vviltvgvvl gfrpdggllg vlagigllvv
      181 fsfafswvwt ffglvlrsek svmgtsmmvl fpltflsnvf vdpstmpgwl qafvkvnpit
      241 qlvtsvraam agsmdgpstm wmllwsalfv vvfgtltmyr ynrr
//
LOCUS       WP_457603497             317 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603497
VERSION     WP_457603497.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..317
                     /product="S41 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33546
     Region          9..299
                     /region_name="Peptidase_S41_IRBP"
                     /note="Interphotoreceptor retinoid-binding protein; serine
                     protease family S41; cd07563"
                     /db_xref="CDD:143479"
     Site            order(68,212,269)
                     /site_type="active"
                     /note="active site triad [active]"
                     /db_xref="CDD:143479"
ORIGIN      
        1 mdpdqitaiv eraaalvade yvlpdvadrv aghlrerlra gayagagdpa tlgalvtadl
       61 qsanrdlhlr lkhhdqplsd raddptgehf arlaalgmgg vtrvqrlpgn vglleiqpyv
      121 fppdlagdal taalrllagt dallldlrrt eggspdgval lcgwffaept hlhtmhersg
      181 atrqfwsaaw lpvpryapek pvhvltgpat fsggeelayd lqqfgratvv geptrggahp
      241 rvghrlhphl eltvpvarpv haasgtnweg cgvtpdlasp adgardlayr rsleallaad
      301 pdrptaaear talaals
//
LOCUS       WP_457603507             484 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603507
VERSION     WP_457603507.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..484
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53480
     Region          76..483
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mprlpafehp sappsgvamn rpmdsgmdtt tvlpyagsra strtrwlraw mvtapidvaa
       61 lltpllltqn ywrgtlfnaa ltvglfaagg lyrprrhisi ldelpslggr llasgavgai
      121 iaalrhdsvp yvsgfmrgva lsaglvivgr alnsrlilla rkrrwvehna ivigggpigg
      181 elarllrryp qyglrfvgav dapsrpriga lpligtiddl eklaemlece vlviadpdcs
      241 eadlmesllr passrcdlwa vprlwgsrsq ggypdhigai pivkigdttl tgprwrlkra
      301 sdvvfavtal lvlsplllfc vvatfldggr gvffrqerig rygkpfhvik frsmrpadel
      361 esqttwsiah dervgpigrf mrrtsldelp qlwnilrgem svvgprperp yfvekfsmey
      421 pryamrhrvp vgltglaqvs glrgdtpisd rarfdnyyve nwslwldiki vlrtvtevfr
      481 gggr
//
LOCUS       WP_457603505             246 aa            linear   BCT 27-JAN-2026
DEFINITION  YveK family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603505
VERSION     WP_457603505.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Mijakovic,I. and Deutscher,J.
  TITLE     Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year
            retrospective
  JOURNAL   Front Microbiol 6, 18 (2015)
   PUBMED   25667587
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Elsholz,A.K., Wacker,S.A. and Losick,R.
  TITLE     Self-regulation of exopolysaccharide production in Bacillus
            subtilis by a tyrosine kinase
  JOURNAL   Genes Dev 28 (15), 1710-1720 (2014)
   PUBMED   25085422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..246
                     /product="YveK family protein"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0061097 - regulation of protein tyrosine
                     kinase activity [Evidence IEA]"
                     /calculated_mol_wt=25900
     Region          1..>127
                     /region_name="YveK"
                     /note="Capsular polysaccharide biosynthesis protein YveK
                     [Cell wall/membrane/envelope biogenesis]; COG3944"
                     /db_xref="CDD:443144"
ORIGIN      
        1 mdlahflrdt igrrwpivla ltllcgaftg vlaerrppvy raetqmvvtf aveksaapqp
       61 rppadeagrl mqrrvktyat mmntprltrp vidslglpyt tddlagrvva sstvnslaid
      121 vavtdrsagt aaaiaaalaa elqriaerdl ppaglglkah vavvraavpp prsepvrwqw
      181 yalggalggl avgvgvalvl gyrragtpvs vdvralwttt vrraagvpgq tdgrvadasv
      241 kerqas
//
LOCUS       WP_457603508             355 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603508
VERSION     WP_457603508.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..355
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=38231
     Region          90..348
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 msdrhqltds dpraqgsdve pggpaeeerp rrrrgrrial ivllvvvlls ggtalaggly
       61 yrsvdksier vdafegvpee srpqveakga mnimilgsds rdpestggsr sdtiilahlp
      121 kdrssaqlis iprdtwtavp kskegrggrd akinaayawg gvplmvqtve kfsgvrvdnv
      181 amvdfagfke iidalggvei dvekgfttky sligtrtfek grqtmdgaaa ldyarerhaf
      241 pdgdfarirh qqqvikaild kaasggvmtn paklnsfvra tsdsvavdks lslvdlamem
      301 rglrgdnltf ftcpvkgtgr vgsesvvfpd parsktlfda vrrdsvpeil aisgk
//
LOCUS       WP_457603501             299 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603501
VERSION     WP_457603501.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..299
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31014
     Region          2..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mievdqltkr ygphtavedv tfrcepgsvt gflgpngagk sttmrmicgm tpptsggatv
       61 ggrpyrhlpn pgreigvlld asahhagrtg retltlaart mgvdrgrvaa vldqvglndt
      121 aarrrvgays lgmrqrlgla lallgdprvl ildepangld pegifwmrgl lrdfadrggt
      181 vllsshllre veavadrlvv igggrvvaqg gkdellagag tlvrardpha lrltldraal
      241 patagtdggf vvraepgrvg qaaadaglvl telrpagsgg leqlfltlta gastkeavr
//
LOCUS       WP_457603509             244 aa            linear   BCT 27-JAN-2026
DEFINITION  YcnI family copper-binding membrane protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603509
VERSION     WP_457603509.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   de Oliveira Silva,Y.R., Zheng,D., Peters,S.C. and Fisher,O.S.
  TITLE     Stabilization of a Cu-binding site by a highly conserved tryptophan
            residue
  JOURNAL   J Inorg Biochem 253, 112501 (2024)
   PUBMED   38342077
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Chillappagari,S., Miethke,M., Trip,H., Kuipers,O.P. and
            Marahiel,M.A.
  TITLE     Copper acquisition is mediated by YcnJ and regulated by YcnK and
            CsoR in Bacillus subtilis
  JOURNAL   J Bacteriol 191 (7), 2362-2370 (2009)
   PUBMED   19168619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..244
                     /product="YcnI family copper-binding membrane protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24510
     Region          5..179
                     /region_name="YcnI"
                     /note="Uncharacterized conserved protein YcnI, contains
                     cohesin/reeler-like domain [Function unknown]; COG4549"
                     /db_xref="CDD:443613"
ORIGIN      
        1 mirlrrpati aaltltavat avlglagpvs ahvtinpaea kqggygrfaf rvpnesdtas
       61 tvkvevnlpe napvgsvstm pvagwtvave krkvdppiev hgsqlteavs kltftaapng
      121 gvkpgefqef pvsmgplpqa dtmvfkvlqt ysdgnvsrwi eeptpgaeep enpapvlkla
      181 aaapasagas apaaaaaddd dddddagsga avalgvaglv aglgglalgg lafartrrep
      241 aaks
//
LOCUS       WP_457603513             244 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603513
VERSION     WP_457603513.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..244
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26886
     Region          33..128
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mnvfgtvadl yerarpgypp eiaesilayh ggapasvvev gagtgkgtev larlsapltc
       61 vepdermaar laerfpeari eattferwsp padgvdvlac amawhwldpa trnalarral
      121 apggtlavfg hrydyadadq qaavraalrs vdptvrerpv dwfhrdvlds gqfddvrrev
      181 frrelpldke rylalmrtfg pylsrtpdqq rrgiaaldrl vddfggtvvl dlrttlvlgr
      241 adar
//
LOCUS       WP_457603517             483 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603517
VERSION     WP_457603517.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..483
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48638
     Region          28..>319
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mgldpglrrl algtllaayp gpvppdwavd lladglaght lfgtnihdpa qvaastaalr
       61 agrpdvivai deeggdvtrl ahatgspypg naalgavddp dltrqvyaai gaelaalgit
      121 vdlaptvdvn tadenpvigt rsfgadpkrv avhsaaavag lqstgvaaca khfpghgatv
      181 adshhelptv dvppavlrer dlppfaavvd agvravmtah irvpaltgdg patfsravlh
      241 dllrveygft gaiitdalem kgavlaaggv gagavralaa gadllcigar vdaelvesva
      301 aeivaaitdg rlarerveea agrtaalaat gpadapppaa dglgyaaalr avrvegdlvr
      361 dtaplvvqvh atstiaegrv pwglgphlaa gveqaravag dtdpdqlrrl agdrpvvlvg
      421 rhlhrlpgar elvealaath qvtvvemgwp gawrpagara fvathgasha ngraaadalg
      481 lta
//
LOCUS       WP_457603518             223 aa            linear   BCT 27-JAN-2026
DEFINITION  class F sortase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603518
VERSION     WP_457603518.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Bradshaw,W.J., Davies,A.H., Chambers,C.J., Roberts,A.K., Shone,C.C.
            and Acharya,K.R.
  TITLE     Molecular features of the sortase enzyme family
  JOURNAL   FEBS J 282 (11), 2097-2114 (2015)
   PUBMED   25845800
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Spirig,T., Weiner,E.M. and Clubb,R.T.
  TITLE     Sortase enzymes in Gram-positive bacteria
  JOURNAL   Mol Microbiol 82 (5), 1044-1059 (2011)
   PUBMED   22026821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..223
                     /product="class F sortase"
                     /EC_number="3.4.22.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22942
     Region          77..221
                     /region_name="Sortase_F"
                     /note="Sortase domain found in the class F family of
                     sortases; cd05829"
                     /db_xref="CDD:320678"
     Site            order(134,201,215)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:320678"
ORIGIN      
        1 mtvrnrgala amaagaaalt lagvvacgse paedvggdev talagatptp tpaatatggg
       61 svpvnpgtlp adseivppvk lsippirvta tvnpvgvner tdefevppsv dqvgwyrygp
      121 gleagagsvv iaghvdsaeq gkgaffrlre lgrgdeltat gsdgrersyr vvareeyrks
      181 kipleryfar dgkprltlit cggpfdaktr syrdnivvta vpa
//
LOCUS       WP_457603520             845 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603520
VERSION     WP_457603520.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 845)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 845)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..845
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=89680
     Region          17..823
                     /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 metgdprnsv ppgrsgpffg fvgaigvval avsagplval adrwselpaa fwtmaalava
       61 cdarpfvppg rrqtsavfps tcftfaillg wgfgpavavq avavavsgwr lgyapwrtgf
      121 naaqyacala aayavtrlgp gelfdggrlh wtdvaavgga tvawfvvnyg lvssavrlrf
      181 gdrwwpsvrs glayellatg sllllapvlv aaarasaali plvlvplfav yrmarlsaer
      241 eqladvdplt glpnrkallt evaeqvhlhg draargapda hlalllldld rfkhvndalg
      301 havgdrllve vsarltgavg agdmvarlgg defaivvprl tdidqarera drvvaalaep
      361 vpldglpldv ggaigialyp ehgedfatlm rhadvamyda khrndtvavy apesdhnsae
      421 rlslladlrr vlesgpsaqg getvgvrggd gaaltpalpv radrparnqr pardggrrsg
      481 dganrwlrrr rerveerhdd dlieriltga dpirrraara gagpvagplv vgdaefapet
      541 etadadvtqd aeaavstgap gvigptadgs tvagpdeqag hpgeitmyyq pqiaiatgev
      601 vgveallrwr hprrgmvdpg eliqvaeqsa vmrlltrrvv ddvveqlakw saagltlraa
      661 lnvsvrdlht geiadqiadr larygvpper lqveitegal madprrvlas itqlhrigvg
      721 ialddfgtgy sslqhlrrlp lsevkvdrsf vlgmaedpdd aaivrsmiel agalglrvva
      781 egvedertwr mlhaagcdva qgwfharpmp aedlvawlsr yrpvrpaeag srsgpapege
      841 skass
//
LOCUS       WP_457603523             815 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603523
VERSION     WP_457603523.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 815)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..815
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90271
     Region          10..757
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 msrrtllheg wtlraepgpa vppeiagtav pasvpgcvht dllaaglipd pylddnenrl
       61 twigrtdwvy ettfagqpgd dervdlvcag ldtvatvtln gvevgrtenq hrsyrfdvra
      121 llrpdgnala vrfdspyrya eahrdrlgdr pnaypepfhf irktacnfgw dwgptlvtag
      181 iwrdiglhaw starlasvrp ivtvaddvgr velhvqvera gdepltvraa vagvtadvav
      241 pagertavvt ltvadpalww pigygdqpry dldvtlhgad greldaaarr igfrsvrldt
      301 tpdahgtpft lhvndvpvfv kgvnwipdda fpnrvtrerl agrfgqaada nvnllrvwgg
      361 gryesddfyd lademgllvq qdflfacaay peeepfrtev eaeareqvtr laghpslvlw
      421 tgnneniwgw hdwdwqepla grtwgrgyyl dllpaivgel dptvpywpgs pwsgsedvhp
      481 ndpahgtthi wdvwntddyt ryrdyvprfv aefgyqappa yatlrralsd dplthdspgm
      541 ahhqkaadgd gklrrgldah lpppadfddw hyltqlnqar aiqlgvehfr shrpvctgtv
      601 vwqlndcwpv tswsaidgdg rrkplwyalr rayadrlltv qprdgglalv avnetaraws
      661 gpatvtrlal tgepraktsv dldvpayssv vlalpaelar pddgraellv adagdtaera
      721 lwffaedrdv rwpaaqwdat vepvdggrrv rvtartvlrd ltlfpdrldp aaqldralvt
      781 llpgesatft vhapgpldad altrrpvlrc vndlv
//
LOCUS       WP_457603524             112 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603524
VERSION     WP_457603524.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..112
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12108
     Region          4..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msvplyqaka elfrtlghpv rirvlellqd gpkpvrdllt aidveasnls qqlavlrrag
       61 mvtsyrdgpl vmyalstpdv adllaagrri lgavltdrda lldelrasgt dr
//
LOCUS       WP_457603528             246 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603528
VERSION     WP_457603528.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10595285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..246
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26666
     Region          10..246
                     /region_name="Y_phosphatase3"
                     /note="Tyrosine phosphatase family; pfam13350"
                     /db_xref="CDD:463853"
ORIGIN      
        1 msdvdapqsp fpalfnfrdv ggyaardgrt vrrgrlyrsd slhridetdr saftalgirt
       61 vidlrrpsev erdgrvpdyd gltyrhihpe hadwganrfd asgvslaryl adryadlart
      121 gtaglaeavg liadsanapv vvhcvagkdr tgivcaltla vlgvpdedvv adyalstaas
      181 rrftewvrat lpdaeepppp flespaeame lflaelrtgy gsvegyltha gvteaqvesl
      241 rthlld
//
LOCUS       WP_457603531             286 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603531
VERSION     WP_457603531.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..286
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28155
     Region          111..>285
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mavqtglgep rgpwfvspel dpdgrryrdv pgggpeagrr slrhrllsva avvalstvsg
       61 aaagtwaadr gapgpaaasa apvpaelita agktvpgvvs vmvggrsgas asgsgfaidn
      121 eqhivtndhi larggsgvvt vetsdgrrfp aevvgrepas dlavlkvpas aglpplplak
      181 anstrvgepv lavgsplgla gtvtagivsa lnrqvrigng rhtavqtdas inpgnsggpl
      241 vnargevvgv ntaiatidgn gsigigfaip idqvqqtadt iigrgg
//
LOCUS       WP_457603537             335 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603537
VERSION     WP_457603537.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..335
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=34973
     Region          4..330
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 msghvavlga gswgtafaki ladagrdvtv larraavaea irtgrhnpey lpgirlperv
       61 tatgdaaeai egaevvvlsv psqtlrgnla dwtpylapda tlvslmkgie lgttkrmsqv
      121 itetagvpdd rvvvvsgpnl apeiaaeqpa atvvagtdsr rtalvqasir tpyfrpytnd
      181 dvigcelgga vknvialayg iatamgfgdn tramlmtrgl aetarlgval gadpitfagl
      241 agmgdlvasc sspmarnrtf gehlgrgetl eqaqaatrqt aegvksclai rdlarahgve
      301 mpiteqieri chegmdprla vdalmsrtak pesye
//
LOCUS       WP_457603540             737 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603540
VERSION     WP_457603540.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..737
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77103
     Region          14..716
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mgrrpvavrl arwsaehpwr aialwvvfva vcfvggsaag lneatdedqa igefgraqli
       61 vdsggfdrpa tenvlitars gsldqaaaka aaqdaadrlr qvdgvasigt pmpsrdgsal
      121 lvpitmsgdp gtagdrvqpl rdttakvqda hpqlrveqvg gpsidkaldd tlgkdfkrae
      181 llslpvtlai liiafgalia agvpvllals svaaamglst lashlvpatd ttasvillig
      241 mavgvdyslf yvrrereera kgrsgldave iaaetsghav vvsgtaviis mgglllaqda
      301 ifsslavgsi lvvavavigs ltvlpallak lgrwvdrprv pllwrltapr dgqparprfw
      361 pavlkpalra pvatllisva lllaltapal gmklkfpgpe dvprttaamq aydrltaafp
      421 sngtshtvav rapaeqadrv raaltdlagr taadplfapa egdgpeiqvs adrrvsvlev
      481 atphasrsde asrslhelre dlvpatlggi pgveyavggg vaasedyaah iwaklpivaa
      541 fvlaltflvm awtfrsmvva ltsivlnlls agaaygllvl vfqstwaegl lgftsmdaiv
      601 twlplflfvv lfglsmdyhv fvvsrireav drgmptreav ahgitssagv vtsaavvmva
      661 vfsifatlsm idfkqlgigl aaailldati iravvlpsvm tllgdanwwa prfmrrrtpt
      721 pavepppapa pelvgar
//
LOCUS       WP_457603542             311 aa            linear   BCT 27-JAN-2026
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603542
VERSION     WP_457603542.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..311
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32261
     Region          33..>225
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mktlpaaaaa vltavtvgvp rpaptdvhpd tyvvsrapgv lpeglavtas gtmyvtssat
       61 gavyrgdtrr aglrpflapg adgrtsaagv rvdrrgrvlv agwttgtlfv yapdgtllar
      121 raaapgaaln dlavtedtvy vtdsatgtvw ragltggrvg alvpwvgpdd fpavpvflng
      181 ivvdpsgrva lvaeqggerl frvdladrsv tevevsggrm gadglllegd rlygvvnepd
      241 dadgtrflvn larldqelrt aqvvdrsrpv giqrsptsva rdagrllwvd sqlfattpap
      301 pftvtevpgl r
//
LOCUS       WP_457603544             529 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603544
VERSION     WP_457603544.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..529
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54999
     Region          27..424
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,286,289..290,293..295,298,326,330,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mtqatapara tavdmshrqi lealsglllg mfvailsstv vsnalpriit dlrggqsayt
       61 wvvtstllat tattpiwgkl sdlfskkllv qlslvvfvlg svlagqaqtt geliacrvvq
      121 gvgaggltal aqvimatmia prergrysgy lgavmavgti ggpliggviv dtswlgwrwc
      181 fyvgvpfavl alivlqrtlr lpvvkrevki dwwgatlita avslllvwit lagdrydwis
      241 wqsgvmvaga allgalaarv ekraadpmip phlfrnrtit laviasiavg vgmfgasvfl
      301 gqyfqisrga sptmsglmtl pmiggllvss tvvgriitst grwkswlvig svlltagfal
      361 mgtmradtpy whlavfmali glgvgmsmqn lvlavqntvr pdelgaassv vaffrslgga
      421 igvsalgall ghrvtgymad glsrlgipas gsgggglpdv htlpgpirtv veaayghaag
      481 diflaaapfg llalvavvli revplrrsna epvpagreta eaipagtkd
//
LOCUS       WP_457603545             193 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603545
VERSION     WP_457603545.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..193
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21862
     Region          1..163
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtaapilper hewtvddlge lpkdlpyelv ngrlivpspt alhqeicvel llalrvncpp
       61 eflvsidlsm rvdrrneprp dvvvirrkha grspvpveda llavevvspt shfrdlydka
      121 kvysrsgvrs ywvvdpqher ialteytldg aareyeqlah tedlfvterp wkvsvdlpal
      181 tarrndllav eed
//
LOCUS       WP_457603547             368 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite oxidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603547
VERSION     WP_457603547.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Hsiao,J.C., McGrath,A.P., Kielmann,L., Kalimuthu,P., Darain,F.,
            Bernhardt,P.V., Harmer,J., Lee,M., Meyers,K., Maher,M.J. and
            Kappler,U.
  TITLE     The central active site arginine in sulfite oxidizing enzymes
            alters kinetic properties by controlling electron transfer and
            redox interactions
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (1), 19-27 (2018)
   PUBMED   28986298
REFERENCE   2  (residues 1 to 368)
  AUTHORS   McGrath,A.P., Laming,E.L., Casas Garcia,G.P., Kvansakul,M.,
            Guss,J.M., Trewhella,J., Calmes,B., Bernhardt,P.V., Hanson,G.R.,
            Kappler,U. and Maher,M.J.
  TITLE     Structural basis of interprotein electron transfer in bacterial
            sulfite oxidation
  JOURNAL   Elife 4, e09066 (2015)
   PUBMED   26687009
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Barber,M.J. and Neame,P.J.
  TITLE     A conserved cysteine in molybdenum oxotransferases
  JOURNAL   J Biol Chem 265 (34), 20912-20915 (1990)
   PUBMED   2249998
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Campbell,W.H. and Kinghorn,K.R.
  TITLE     Functional domains of assimilatory nitrate reductases and nitrite
            reductases
  JOURNAL   Trends Biochem Sci 15 (8), 315-319 (1990)
   PUBMED   2204158
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Neame,P.J. and Barber,M.J.
  TITLE     Conserved domains in molybdenum hydroxylases. The amino acid
            sequence of chicken hepatic sulfite oxidase
  JOURNAL   J Biol Chem 264 (35), 20894-20901 (1989)
   PUBMED   2687265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..368
                     /product="sulfite oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40071
     Region          48..363
                     /region_name="SO_family_Moco_dimer"
                     /note="Subgroup of sulfite oxidase (SO) family
                     molybdopterin binding domains that contains conserved
                     dimerization domain. This molybdopterin cofactor (Moco)
                     binding domain is found in a variety of oxidoreductases,
                     main members of this family are nitrate...; cd02110"
                     /db_xref="CDD:239028"
     Site            order(49..50,52,54,98,163,192,197,205,208,210..211)
                     /site_type="active"
                     /note="Moco binding site [active]"
                     /db_xref="CDD:239028"
     Site            98
                     /site_type="other"
                     /note="metal coordination site [ion binding]"
                     /db_xref="CDD:239028"
     Site            order(248,284,288,290,299,301,333,338..340,358)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239028"
ORIGIN      
        1 mttvddvsrp srvagpdeai saeelqlaar nhgiplealr ydvtpaglhy llihydipdv
       61 dpaayalsvs galerplrld laalrdrprv thrvtlecag ngrallhprp vsqpwlveav
      121 gnaewtgtpl apllreagls gdavdvvftg adhgvergve qdyqralpva dalreevlla
      181 yemngapllp qhgaplrliv pgwygmahvk wlrditvtte pfdgyqnava yrlrrdaadp
      241 gvpvtriepr alvrppgfpd fmsrtrvlrp gpctldgraw sghapvtsve vtvdggetwt
      301 pavldepagg ewawrrwsvr wtatpgryvl garatdasgr tqpveqpwnr ggfannlvqr
      361 vevvvpae
//
LOCUS       WP_457603550             272 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603550
VERSION     WP_457603550.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..272
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28841
     Region          34..152
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mieereqdaa vkarhramwa mgdyaavaaq vipelgatlv raagvapgmr vldvaagtgn
       61 aalpaaraga evvagdltpe llaigraeae regltltwee adaealpyag aafdavlscv
      121 gvmfaprhra aadevlrvcr pggtiglvnw tpegfvgqlf aamrpyappp ppgaqppplw
      181 gdeehvrelf gdrvdaftsa rdavvvdrfa tpaefreffa trygptvavy ranagdpert
      241 agldraltdl aarhldggvm rweyllitar ra
//
LOCUS       WP_457603553             321 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603553
VERSION     WP_457603553.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..321
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36026
     Region          8..321
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 msgaqfsaet sgggafvrqp nrftgrvtph stspegggpd eqgrwpleag ryrliwcrac
       61 pwahrarivr gllgldevis lgtvdpirde rgwrfaldpd gfdpvlgigf lseaylstdr
      121 dytgrvtvpa lvdtltgrvv tndypqltld fstewrrfha pdapdlypve lrpqmdalma
      181 eihrdvnngv yrcgfatsqe aydeaftalf arldalserl agrrylmgda iteadvrlft
      241 tlvrfdvayh ghfkcnerkl tempvlwaya rdlfqtpgfa etvdfdhikr hyyathdmin
      301 ptrivplgpd lsgwttphgr g
//
LOCUS       WP_457603554             716 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603554
VERSION     WP_457603554.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 716)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..716
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=77529
     Region          37..714
                     /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 mrapdsdggd vsrpgaaaya aewaravrri gfvplsaaet erllvplter lgeallaptf
       61 sarpaeevgr alvqahltep gvldwsvqal gdrflpwvlp srtespelre rvallqgafa
      121 agfaralrdr vfsqqeriar sawqardtve qalrdsearf ravftgaaig igiagvdgqi
      181 ievnqsfadm lgyavaemrr mnvsalfhpd daagmwelyq eliegkrdsa rvekryyrkd
      241 gsvvwtdlav slirhddgrp rftvamvedi tqryelqqrl rfqalhdplt glpnrtlffe
      301 tlgdvfdgag pdqrvglcfi dldgfkavnd slghdlgdrl lkviarrlsd cvagrghlva
      361 rmggdefvil vdsdggidda vevaelalaa vsapvhvgdq qlavsasigi vecpaaetsv
      421 gdlmkaadtt lywakaegrg rwavydpers aadiarsala anlpaaldrg efvlhyqpiv
      481 slldgtmvav ealvrwqhpe lgligpdrfi glaeetgliv rlgawvlrqa crdaeswrra
      541 ypdttpvvsv nlaarqaddp aivetvaeal qhtglpaell qleltesavm gsageplrtl
      601 hqlaglglrl aiddfgtgys nlaylrrlpi hcvklagpfv egirgdggda vadhrderiv
      661 dalvrlahal elsvtaeave tevqaerlra lrcdtgqgrl fgapmpaegi rarlgg
//
LOCUS       WP_457603556             193 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603556
VERSION     WP_457603556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..193
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21786
     Region          21..176
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtppppvtfd rrrpdeltsv vdaladlyar vyaeppyleg paqvarfrtg lpdeaarpgf
       61 rlvlawegee ligaaygwtm aagtwwsrak deppaevrdr dkfavlewiv hprhrsrgvg
      121 aelmrrllqg rqeswatlas dprsrangiy rrngwivagh selpwgpsme llvrdlrive
      181 earagtprpd qrr
//
LOCUS       WP_457603557             347 aa            linear   BCT 27-JAN-2026
DEFINITION  TRM11 family SAM-dependent methyltransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603557
VERSION     WP_457603557.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 347)
  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
REFERENCE   2  (residues 1 to 347)
  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   3  (residues 1 to 347)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..347
                     /product="TRM11 family SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37263
     Region          110..344
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 miryalllap sanrvyadaa arlaraelav fagsgvldvv paaaevtgig gveyltftta
       61 epglgerdla hlanlsaaya lfervgddll rpvplrplar ydsdlitipk yagktneqft
      121 rlllnvtvla saaaprmldg pvvvldplcg rgttlnqalm ygydgigier dsqdvdayaa
      181 flrtwlrrkr lkhttdstsv rrdrklvarr feavlapsrd ehragaaqrv ivlntdttra
      241 realrprcad vivtdapygv ahgsrtghgl srsplellta avpvwrellr pggalglswn
      301 thvapraqae avladaglrv ldgpgfgdfa hrvdqaierd vlvavap
//
LOCUS       WP_457603558             516 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603558
VERSION     WP_457603558.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Bone,R., Fujishige,A., Kettner,C.A. and Agard,D.A.
  TITLE     Structural basis for broad specificity in alpha-lytic protease
            mutants
  JOURNAL   Biochemistry 30 (43), 10388-10398 (1991)
   PUBMED   1931963
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Olson,M.O., Nagabhushan,N., Dzwiniel,M., Smillie,L.B. and
            Whitaker,D.R.
  TITLE     Primary structure of alpha-lytic protease: a bacterial homologue of
            the pancreatic serine proteases
  JOURNAL   Nature 228 (5270), 438-442 (1970)
   PUBMED   5482494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15340045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..516
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52466
     Region          199..378
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(228,252,287,290..294,296,304..308,311,315..318,320,
                     328,333..338,353..355,360,364)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(228,316,318,320,333..338,353..355)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mdrrrmtaig vlvaaaglta avtvpsfage eprraapaad gvapevldam grdlaltrdq
       61 avkrlrterw aagtvtrlrg elgagyggsw lsadgatltv avadpagear vraagavpkr
      121 vargvaelda vksrldaaga daspdvagwy vdvadnavvv iarpgaeadg rrlaaaagsk
      181 aamvrvrtad eaprplfdvr ggdaylinna grcsvgfsvv ggfvtaghcg rpgdrttgsn
      241 rvaqgtfaas sfpgddwafv rvnadwtpqg vvtdfndggt vavngsteap vgasicrsgs
      301 ttgtrcgliq aknatvnype gtvtgltrtn vcaepgdsgg awlsgdqaqg vtsggsgdct
      361 rggttffqpv neilqrnnlt lvtagdqpap tqppaggget tppvtaeptp paddtecsgq
      421 vsrtgrvaag rtqvqpdgrf yrvpdgtqea clsapdgarv vlelqrftgg afrtvaraat
      481 adgtarltae tqagayryrv vglsgsgeyt lafsar
//
LOCUS       WP_457603565             213 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603565
VERSION     WP_457603565.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 213)
  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   3  (residues 1 to 213)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..213
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22811
     Region          9..151
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtepawlvet raaydavaed yarllpdvve ppldrallaa yaemvgpgra vlevgcgtgr
       61 vtahlhrlgl diggvdlspg mvavarrtyp dlrfevgslt elsapdrsla glvswyslih
      121 lppellpevf vgfhrvlvpg ghlllavkag drldrreqay gqpvgydvyw lspqrlaaql
      181 aaagfavtat tvrapadger qpqafllaqr pad
//
LOCUS       WP_457603567             202 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603567
VERSION     WP_457603567.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..202
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22563
     Region          29..200
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtnkirraea herghsgagp pdepsdddvi rasvaeperf aplfdrhavp vhrylarrig
       61 ppaddllaet flvafrrras ytsdvgvrpw lfgiatnlvr rhvrteerry ralarlaage
      121 vappviedai drldagalrr dlalalaslh rrdrdvlllt awadlsyeqi aavldiplgt
      181 vrsrlhrarr ltrlalalee pt
//
LOCUS       WP_457603572             398 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603572
VERSION     WP_457603572.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..398
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42221
     Region          1..380
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msarsarrvr ptlrlrltll ngvllvgaga ilvllawllv rdalrptdel lpgttvvltd
       61 grtldagqwq rqlvdaasqe llvkgllalv aisvvgvaga ylvagralrp lhqvtatarr
      121 lgeatlderi gwsgaddeva elaetfdaml drisgafeaq krfvanashe lrtplavmrt
      181 eidvtlsddd adlaeyrrma gvvrdasera nglvdallvl arseaqtgrr larraesdla
      241 igtanalsav sreveriglk vhtslrpapv vgdpglldrl agnlvenavr ynhlhgriwi
      301 rtgtdgersw lvvgntgfev apadvpglfe pfrrggqert gargsglgls ivravsdahg
      361 gtvkavaqpg gglevtvtlp sdgpgrrppd rrpgpsgr
//
LOCUS       WP_457603581             782 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603581
VERSION     WP_457603581.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11706914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..782
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82867
     Region          24..619
                     /region_name="HAD_like"
                     /note="Haloacid Dehalogenase-like Hydrolases; cl21460"
                     /db_xref="CDD:473868"
     Site            order(323..327,471..472,499,516..517,520..521)
                     /site_type="active"
                     /db_xref="CDD:319763"
     Region          642..769
                     /region_name="Hr-like"
                     /note="Hemerythrin-like domain; cd12108"
                     /db_xref="CDD:213983"
ORIGIN      
        1 mgteprecvp eqpararrwa waewaplvll tvavlagaal wftgahdaar lvwaavtvva
       61 lvpaawttlr qlwlrqfgvd viavlallga llvreflaga viavmvatgr aleeyaqrra
      121 trdlraller aprqarrrtp dggievvpld rvavgdrlvv gpgdvvpvdg vveesatlde
      181 svvtgesqlv traageevas gvvnagagfg lrarrnaaes tyagivrlag eatarkapmv
      241 rladryaaaf vpftlvlagl awllsgeftr avavlvvatp cplllatpia vvsglsrvar
      301 rgvlvrdggs leqlgrartl lldktgtlta grpraaevvv apggdrdevl rlaasveqls
      361 phvlaaalvr qarerglpla eptqvteepg hgvsgrvdgr mvhvgqlage ppewagrlge
      421 raeragrsav wvsddhgplg ailledpvrp darrtvrrlr eaglerlvmv tgdrpgtarq
      481 vaqivgvddv iarcspqeka drvrqesara vtvmvgdgvn dapalaeahv gvamgatgat
      541 asadvadavl tvdrldrlad aveiaryarr iavqsatvgm glavlamlva aagrlppvag
      601 aflqegidvl vilnalralg gglrrrdlpa htrelldrya gehggvrdvl arlrdtadmv
      661 atrpddpacl palrevhrrl vdevlpheaa edrqlypala gplgsdeats tmsrahveiv
      721 rlverigghl taqpdgrlrr devpdllaal ygldavlrlh laqeeedyfs lnpeegstap
      781 gr
//
LOCUS       WP_457603584             327 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603584
VERSION     WP_457603584.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..327
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33958
     Region          22..325
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mprparagtr ggrlataacw lavapvaawa lvrltglerg plvqavaftp yaaavapvva
       61 vaalalrrrt pavvavlaal aligtvapra vpgdrpaadg ptlrlltanl rlgsadpaal
      121 vdlvrtrrvd vltvqeltpp laaeldrlgl aellphrslt pevgstgsgv yarhplrdtg
      181 hrrnkgffft qayatvtvpg applrvesah paapyaphvv pdwwtdqraq ppatpdggls
      241 vlagdfnatl dhaalrdlia tgytdaadaa gagfggtwgp ydgdpippvt idhvlvdrri
      301 avraartypv pgsdhralla elrlptg
//
LOCUS       WP_457603591             186 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603591
VERSION     WP_457603591.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 186)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..186
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19205
     Region          1..135
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mspltwavaa vvtdgsgrll lcrrsegarr walpggrlrh despadavvr avraetgwav
       61 tpvdlvglyr vigpqapppp agrcggrpdv lvhvfraapv dagpagdpva gclprwwppq
      121 elpgvltpat raaiadalag ragvlrhtta adaltppgdg qsrsrmidts sakwrgpgvy
      181 dhassa
//
LOCUS       WP_457603592             599 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603592
VERSION     WP_457603592.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 599)
  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 599)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..599
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63861
     Region          22..597
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mstttaette ttetteates twrtlrrgla lspelrtgla gtlalalvym vgrvavpvav
       61 qrgidhgivg gldlnvislt vaitagvlvv ttacgylmmr rlftvsetal agvrtrafrh
      121 vhdlsmlhqq serrgslvsr vtsdvdqitq flqwggvili vnlgqllvtt avmlayswql
      181 tlvvlvafap avlvirqlqr rlagayglvr qrtgtllgai gesvvgapvi raygvagrta
      241 rrldtaidgq rvaqqrairi simgssvgel aaglalagvv vvgvslgvdg tltvgqltaf
      301 lflvtlfiqp vqiatevlne aqnaiagwrr vldvldvspd vadpgeqgre lppgpldarf
      361 agvtfaypgg ppvlhdvtld ipaksrvavv getgsgkttf aklltrlmdp tegqvllsgv
      421 dlrqvrfdsl rsrvvmvpqd gflfdatvge nvrfarpdlt derltaafae lglsdwldgl
      481 psgldtpvge rgealsvger qlvalarayv adpdllvlde atsavdpate vrlqrtldav
      541 trgrttlaia hrlstaqaad evivvdrgri vqrgpheelv rdadsvyall yaswleqtr
//
LOCUS       WP_457603593             622 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603593
VERSION     WP_457603593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 622)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 622)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 622)
  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 622)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..622
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65735
     Region          12..599
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 masgtsrdvl grglrvlgra ireqprifav avsgsvlfgl lviasayvvg gvvgdvvvpa
       61 vergevarga lalaatalfg isvlrvvgif grrlgagymq yrlqaayrrr vtrrylelpl
      121 awhhrnstgt llsnansdve aawypiaplp favgtlvmli gavaslfftd walalvglav
      181 fpalfalnvv ysrrmaprqa raqrlraevs giahesfdga lvvktmgrea qetarfasra
      241 gelrdalisv grlrgvfdpm letlpslgtl avlvvgalrl regaitvtel vsvaflftvl
      301 afpvraigwv laelprsvag wdrvrrvlda tgempygttt ldpatrepat lafddvhfay
      361 epaeahlpga qvlgevtftv pagktvalvg ptgagkstia slavrlvdpg agritldgvd
      421 vreltaasla ataalvaqvp fvfddtvran ialdragigd devwaalrla eadgfvaalp
      481 dgldtmvger gtslsggqrq rltlaralag rprllvldda tsavdprvea ailaglrapa
      541 dggapasilv vayrratial adeviyveqg rvvargthte llstvpgyad lvtayeqaeq
      601 ereqnrtyde vtpltsglev dr
//
LOCUS       WP_457603597             557 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603597
VERSION     WP_457603597.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..557
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=58179
     Region          7..341
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 msgvpqrtll lwcpdwpvla aeivdgvpat dpvvvlhanr viacserara egirrglrrr
       61 eaqgrcphlt vvdhdpgrdv rafepvvaav eevvagvevi rpgacataar gpsrylggee
      121 aaaerivehv aqscavesqa giadgvfaag laaregriva pggtreflaa rpvealgrpa
      181 ladllrrlgv rtlgefaalp agdvlarfgf dgalahrlag grddrplavr qppadltvta
      241 dydepvdrvd aaafaarmla erlherlagy glactrlgie avtahgqelh rvwrhdgllt
      301 aaaiadrvrw qldgwlsgsn grggtrparp tagivrlrlv pdgvlaqagl qpglwgetge
      361 ererahrals rvqgilgpea vvtavlgggr spadqvrlvp wgderaparp gppplppvga
      421 apgaasapvv vpagggagrr agrgravaep pwpgripppa pavvlptplp advrdaagep
      481 vvvsarlavs aaparltvgd grpveitgwa gpwpvderww apaearrrar fqvsladgaa
      541 lllaveggmw lveaiyd
//
LOCUS       WP_457603601             275 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603601
VERSION     WP_457603601.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29589
     Region          34..268
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mtaaeqvrvv rswewarper parrevlaal pereeakppl lfvpgfghga wafaehwlgh
       61 aagrgfpaya lslrghggse papeatlrsy thdvtqvaas lprqavlvgh gagarvvaha
      121 maryparaav lvapvlggwg tfgtalrrnp vgtvpavfga glrlnrrqlf srelpdadar
      181 rhlarlgrag rraqwqlltg rspepavgrp pvlvlgspdd rvlpaaaltr aarryasapl
      241 lfpgmghdlm ldarwrepid aildwldkdp apaqg
//
LOCUS       WP_457603608             974 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603608
VERSION     WP_457603608.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..974
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103145
     Region          <4..961
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mtvraastvl vgrrpelaal gdalarsrtg epatvlvgge agvgktrlle efgtqvdaag
       61 arllvgqcle lgeaglpfap faaalrdvlr hdgpaafagy eaefarllpe larmpagvaa
      121 pagpaladtp rgylfdlvae lfrriaeerp lvlviedlhw adrstrdlig flvraaratr
      181 llvvctyrtd elhrghplrp flaeldrvrg vdrielgrld rdgtaavlad llgteqvart
      241 vddvhertqg npffieelaa aggpvgcaai petlrdllla rvdrlpepaq rvlriaaagg
      301 trfahellae vaglpeaale dalraavagq lvvadpdgdy efrhalvrea vhddllpgeh
      361 arlharyaaa ieaqphlvaa grapaeiahh wyaahdhpra lttarvaaea aaeryayaeq
      421 srllervlel weqvpdaadr lgmdhlrvle dtltaavtag dlsraltltr aalaevdsda
      481 eplraarlld hrgrlfallg ksdgaaelre ayrlaagaph gperlgvlad iashlmkvdp
      541 reaasvatea aagasevgtd lvllptrial lhridgtpel glaelrrvea raraaddswa
      601 lvsalvflsd vlyelgryde seqaaaagvs earrvgisrs igayllsnra ealialgrwd
      661 eadatcaeaa ridppgvsgl hwlqlraglh larahpgade vvgralaflg rpylwpnhrl
      721 plhelrveaa laaddkpeav raaraalada hladlpregw pvlnalarta altgdatlaa
      781 dvsavaaalp arhpaehaha ahvtailggt altgpadala awratvaawr aagqpyplgr
      841 allglaeaaa aagerdevaa avretaelaa rlgatplgeq aatlarrvgl rgtgrpgpdl
      901 ltsreqevlr lvaeghsnsr iaerlfispk tasvhvsrii akldvtnrve aaalahrlgl
      961 ldppppapaq rrar
//
LOCUS       WP_457603616             372 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603616
VERSION     WP_457603616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 10008453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37393
     Region          20..197
                     /region_name="COG4279"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]"
                     /db_xref="CDD:443420"
ORIGIN      
        1 mspgfddygp pvrvegglra rstrgaigqs wwsrrfvevl esfalgsrlt rgrayarrgq
       61 vlrldvspge vtaevqgsrp rpypvrigla aypskvwrrl eselagqaff sarllagdlp
      121 aeleelfaea gaplfpaaig eldqrcgcpd favpckhlaa tfyllaeafd adpfhllhwr
      181 grsraelldr lrtlrgadag ssggtggasg aggaggagga ggagssggtg ssggtggagg
      241 aggaggagga ggnggagaep vpgagpqsga gpeppgttgv pvvgaarala glppveaeae
      301 pdrfwlspvp lpdrpptlat gselllrqlg spgamiggpg laerlrrayr efgrgeaasp
      361 refgrgeaag er
//
LOCUS       WP_457603618             152 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603618
VERSION     WP_457603618.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..152
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16686
     Region          5..134
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mstpdlsyll dhtshvlrtr vaaalaeigl tarmhcvlah alpeertqiq laemgdmdkt
       61 tmvvtvdale raglaerrps rtdrrariia vteegarvaa rsqeivdrvh aealaslpdd
      121 erkvflrale rltaghlatp vqspkparra rq
//
LOCUS       WP_457603623             184 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603623
VERSION     WP_457603623.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..184
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20418
     Region          29..180
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mttplqvtta rlripvterd hvrgpvdapv tvveygdfqc rfcgaaytnl aevlrqrtdm
       61 vrlvyrhfpi tnvhpyaeta aetaeaaaar grfwemydwl yqhqdqldqv hlslgveqig
      121 lspeeiaaev grqeyadrvr qdfvggirsg vngtptlfvn dvrhdggydl aellavvdaa
      181 tddg
//
LOCUS       WP_457603626             199 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603626
VERSION     WP_457603626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..199
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=20862
     Region          1..>152
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mtgalllalt agmlgavnpc gfamlpayls llvagpdggr gavgraltat agltlgyvlv
       61 fgafglalap aadwlrprlp wltvtlgvll alagcwllag rklptprplr vaprltrtwp
      121 smalfgaaya ltsltcaiap flaivvtslr agrrcaawrc sartrwgwrs wsawprspwr
      181 ccaagswrgc aarargcrg
//
LOCUS       WP_457603631             411 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603631
VERSION     WP_457603631.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Weyler,W.
  TITLE     Monoamine oxidase A from human placenta and monoamine oxidase B
            from bovine liver both have one FAD per subunit
  JOURNAL   Biochem J 260 (3), 725-729 (1989)
   PUBMED   2764901
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12024463
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..411
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43439
     Region          24..405
                     /region_name="Amino_oxidase"
                     /note="Flavin containing amine oxidoreductase; pfam01593"
                     /db_xref="CDD:396255"
ORIGIN      
        1 mpdtdvvivg gglaglaaar rlhragvpwr lleagdrlgg rvatdrvdgf lldrgfqvln
       61 tayprltglv dvgtltmgwf tsgvlvrrgd rlerlvnplr epagapgtlt agigsltdrl
      121 rfatlaagya tvpvgrlldt petsaekalr raglsdaiie ellrpflsgv lldrelatss
      181 hvlavvmrsf argriglpad gmqalpkala aplpaeliel ntpvtdvapg rvrtpsgeit
      241 cravvvavdp ptaatllpgl skvrmhaytt yyhrtdtapl depillldgd rreliantvv
      301 vsraaptyap dgqhlvatsv vgpqappepv irreldrlyg rsaadwthlt tvavpdalpa
      361 arppqgrlrk pvalgdglyv agdhrdspsi qgalasgwrt vgavlaelrr g
//
LOCUS       WP_457603632             336 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603632
VERSION     WP_457603632.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..336
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37677
     Region          4..318
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marpitlftg qwadlpfdev crlaaewgyd gleiacwgdh fevdkaladd syverkratl
       61 akhnlqvfav snhlvgqavc dhpiderhqd ilpariwgdg epegvrqraa eeikdtaraa
      121 aklgvntvvg ftgssiwhtv amfppvppav iergyqdfad rwnpildvfd evgvrfahev
      181 hpseiaydyw ttkrtleaig hrgafglnwd pshfvwqdld pvnfifdfad riyhvdckda
      241 kvrtgdgrrg rlsshlpwad lrrgwdfvst ghgdvpwedc fralnaigyd gpisieweda
      301 gmdrlvgape alqfvrrlaf dapsaafdaa fsssrd
//
LOCUS       WP_457603633             355 aa            linear   BCT 27-JAN-2026
DEFINITION  polyprenyl synthetase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603633
VERSION     WP_457603633.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wallrapp,F.H., Pan,J.J., Ramamoorthy,G., Almonacid,D.E.,
            Hillerich,B.S., Seidel,R., Patskovsky,Y., Babbitt,P.C., Almo,S.C.,
            Jacobson,M.P. and Poulter,C.D.
  TITLE     Prediction of function for the polyprenyl transferase subgroup in
            the isoprenoid synthase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), E1196-E1202 (2013)
   PUBMED   23493556
REFERENCE   2  (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
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Chen,A., Kroon,P.A. and Poulter,C.D.
  TITLE     Isoprenyl diphosphate synthases: protein sequence comparisons, a
            phylogenetic tree, and predictions of secondary structure
  JOURNAL   Protein Sci 3 (4), 600-607 (1994)
   PUBMED   8003978
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..355
                     /product="polyprenyl synthetase 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=37358
     Region          33..353
                     /region_name="IspA"
                     /note="Geranylgeranyl pyrophosphate synthase [Coenzyme
                     transport and metabolism]; COG0142"
                     /db_xref="CDD:439912"
ORIGIN      
        1 mtvtvaptdp allrgrfdaa laafldarep drpddgtgav htalrwfvlt ggkrmrplfc
       61 ywgwrgfggp daspivvaaa slelfhafal ihddivdrsd rrrgaptlhr ffaelhaasg
      121 wpgdpaaygr qaavlcgdlc atwsaqmfhg cglpperlrr ghvllarmrs eviageyldv
      181 vgaagdgsva naltvvrlkt arytvtrpvq igaalagaap eevaalagfg dplgdafqlr
      241 ddllgvfgdp svtgksnldd lregkptvll alarasaspa gaarlgelvg dpgldqsaaa
      301 evrgiveesg areavermir tradaalval dalplaepar rvlatlaera vdrhe
//
LOCUS       WP_457603634             464 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603634
VERSION     WP_457603634.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..464
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50122
     Region          3..341
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msrrlvvldv vgltprllah mprlravaea gfaaelgtvl pavtcsaqst fltgelpagh
       61 gvvgngwyfr dlgevllwrq hhalvggekv wqaarrvepg yrvanvcwwy amgadvdwtv
      121 tprpvyhadg rkepdcwtdp pelrdtltda lgtfplfsyw gpgaglpssa wisraaqril
      181 adhapdltlv ylphldydlq rfgpsgpqaa aaaaeldtvl gplldaarer datvvalsey
      241 gitdvsrpvd vnrmlraegl lrvytqagme yldpwtsraf avadhqvahv yvedpadvpa
      301 vaklcaslpg vaevldaagq agygldhprs gelvlvaepd awftyyywld darapdfarl
      361 veihrkpgyd paelffdpaa pgaakrraav alarkklglr ylmsvvglda garavrgshg
      421 rlpadpadgp vllcsdraai rprveatdvk alllelagla reap
//
LOCUS       WP_457603637             363 aa            linear   BCT 27-JAN-2026
DEFINITION  YihY/virulence factor BrkB family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603637
VERSION     WP_457603637.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          60..340
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 maarddahdv hedtrdgred apatrddara ghdrpdgrkh agpvgpddgp dspadlsatg
       61 wmatlkrtvr efqddsltdw aaaltyygvl sifpgvlvli svlgllgdra tegvrdtvgq
      121 avpeenirri iesaidqagq sgglasiaai vglvaafwsa sgyvaafmra snsiydvpeg
      181 rpiwktlpvr lgvtavigvm llisavivvf tgglaeqagn aiglgetavt vwniakwpvl
      241 lvlvslmfai lywaspnarh ggfrwvspgg vlavvlwlvv sglfalyvsn fgsynktyga
      301 vagviiflvw lwlsnvaill gaefdaeler sraiaaghpa deepyvelrd drklrkkgra
      361 hsr
//
LOCUS       WP_457603638             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603638
VERSION     WP_457603638.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20063
     Region          1..176
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mfatdrvrlr tptpddapdm frlhsdpelr lvtddepflp hhvgqvrarl ekraaeqpea
       61 aapvsllaet vadgtflgtg vlwginafng yahlgitllp eargqgygte virllcrygf
      121 rnrnlrrlei etlagntamr rtaercgfvh egtqrdreyd gdgftdlviy gllrrdwtp
//
LOCUS       WP_457603639             573 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603639
VERSION     WP_457603639.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..573
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60980
     Region          63..551
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mptnpaapet gpeptdtrpt spssdvpavp lpgvpapaae lardaagraa ealagpapvr
       61 lgdvvpapeh vrpdpaddft lsadavlrvs pagrdvaeql agwlrpatgf plpvadtged
      121 gpltltlsaa vparpgepdd arlgdegyrl dvttggvrit aatpaglfhg aqtlrqllpa
      181 piesptavaa rwavpggtiv drprfpyrga mldvarhffa vedvlrvvdh laryklnhlh
      241 lhltddqgwr iavdswprla evggttavgg gpggwytrdd yrrivayaar rhvtvvpeid
      301 lpghtnaalv aypelapgki apppytgtev gfsfvdpade qtyafvadvv gevaastpgp
      361 wlhlggdeaf kvpadsyrsf veraqrlvaa tgktvvgwhq lapaahvdgr vlqwwgtngd
      421 dpetadavrr garlilspgn hayldmkyap dtpighdwag lidvrrayew dpgshvrgvp
      481 aeavlgveap lwtesittpa evefmlfprl pavaelgwsp rethdwsrfr srlaahgprw
      541 stagiafhps peipwpttpa qiptqptptp tsp
//
LOCUS       WP_457603641             477 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603641
VERSION     WP_457603641.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 477)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..477
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50201
     Region          1..470
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 msgvvlrgfg wrhggrkrwa lrgvdlrves gervlllgps gagkstllaa lagllpedsg
       61 eqegtveidg ldprkarerv givfqdpetq lvmarsgddv afglenrgvp ageiwprvde
      121 alhrvgfpyd rdrptaalsg geqqrlalag tlalrpglll ldeptanldp agatlirrav
      181 analdpdttm vlvehrvtea lplvdrvvvl epgggvradg ppeavfaahg dalaaagvwv
      241 pghvapprha ttppgdvllt aerlglpprl dptdlrvrag ealavlgpng agkstlalll
      301 ggllkpgtga vtasaelagr dartpphrwr apalvrrigs vfqdpehqfv tatvrdelal
      361 gprrtgrpes avtatvdell hrlrldrlag anpytlsgge arrlsvatal ataprllicd
      421 eptfgqdrrt wlelvdllae lrdgghgvva vthdedfvaa ladttltlhr spagvap
//
LOCUS       WP_457603644             391 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603644
VERSION     WP_457603644.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..391
                     /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=42319
     Region          3..317
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrnryldllr flailrvvty hvtgyatltl vfpamsvmfa lagslmaasl drsgvravgr
       61 rlrrllpslw vvaavfvpam lltgltfspk vllwlfpisd ppanywggla lspiwylrdy
      121 lwfvlaspfv lwlfrraplp tlaapylllv aieigvlanp ptvlrefgly fgawllgfah
      181 hdgllrrmrn rvllpvaavv gaaglvwivt hpgprgfdin diplgnalws aafilvaigr
      241 apggvtwvdr vpalgravtv vnrraltiyl whmpfvvllt plvglvgwsp rdpvglwlrv
      301 glvfalvgvv tllvgwvedv aarrtpelvp gkprrtvadr aaaapaspap agaedalvsv
      361 garvpaprrp vedpgrgdgv raarrdtpgg d
//
LOCUS       WP_457603645             458 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603645
VERSION     WP_457603645.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49155
     Region          1..303
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtdvsdrlgr mvrqaqatgr ipavsaalhr adrplwtcav gdtgndtplg petvfrigsv
       61 tktftavlvm qcrdeglldl ddpigrhldl pahgdatvrr llshtaglqr ephgdvwdsl
      121 rapavdella dlarvervlp tgrrfhysnl glallgeava rlrggtwaev ladrvltplg
      181 ltatgpypte raatgflvda ysdeahpepp adfgavapaa qlwstatdma rwaafladpa
      241 avdpdgavla attveemrwp ltptdesvws agfglglili pqpervihvg hdgampgfla
      301 avygrrggqg aagamgvavl gssgtgvevf dlshrllaaa aehdpaeiep wrpgppapdh
      361 lrgvpgrwwg egfeyvfswh dgtlrargad dpagkppavf aplpdrpdvf rtvsgrevge
      421 llrltrderg vvvrmhwaty rftrtqetfd gydfragd
//
LOCUS       WP_457603646             190 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603646
VERSION     WP_457603646.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..190
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..190
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19953
     Region          <27..61
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mkqallatkd lgkneravai aiaahanneg nawpsvatla dyagcsertv qralaklvql
       61 grlvvtkvag iatrvyrlvt gqgvtnngpg vtnqpegvtn raaggdsqgd trsvedqekl
      121 ktrasardwr rflpknkntn patngypype rrgaalpmta ggdrchkpgh vgqpasgcip
      181 crsealagdr
//
LOCUS       WP_457603651            1155 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603651
VERSION     WP_457603651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1155
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1155
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=124460
     Region          24..1154
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mdltcghcar tagpddrfcg gcgrplaaac pgcghandsg anfctncgqp lrdhavtvqe
       61 drrqvsvlfi divdfttyae radpeqarsl qqvyfatvrr lvhqyggvve kyigdavmal
      121 fgapvatdnd alrcvragle lqrslarqpa gphpplgfrv giatgealvd laaardggqa
      181 fvtgdvvnta srlqglapvg gvvvdestwa atrremeydd qppvtlrgrs svsriwlavr
      241 arprrdgqta eltpmvdrdh ergllvsalh rtltertsql ltvfgpagvg ksrllrelar
      301 haaslpgtrv twltgqcppf genvtyaala divrswaglt gaddpatird rlrerlghla
      361 dphavrlaea lgplvgvsge rltsaeteaa wrrflltlaa tgptvlvfed mhwadeamls
      421 fveqlgaaar nvpllvvata rpelrerhpa wtgtisgams isvppmhdgd idtlyslllg
      481 qatlpqdara pliefadgnp lyaqeyarml ldgglaerta glalvdpagg aemprtvqav
      541 ianrldlldp adravlqaas vvgvqfwaap valalgrpae wveralhhlq rrdlvyelpv
      601 stmpgqaeyr frhvlvrdvc yqrlpraerv arhqrtadwl eqladgrqhd laevlanhrw
      661 aaheiartvg ldqtphaaat rsalhraarr aydlhaleta atlvdralsv ecgpdpalel
      721 fqaelafyrd rdgfldgggt allttlagrl adagdrpgaa kawrllataa faradrselm
      781 rcldraiglh atlpdsedkv gvllelarah mldaetepac vaartaaela erlelreara
      841 naritlavvr yqagaeeaya eladvteecr verltsrrra vhnlawvlqe egdltgsarl
      901 vdeqrsldla gehaltvsfs dqwarsyysg dwtsalrmae gstrrptdew dlhivavsgw
      961 iralgddpag pgtgedlvdq alvaarrsgf qrvlrstlah aalcravqgr rdeamallte
     1021 ldedwrqtkm ipfaewvpav ghvaallggd aavlvrdlla haprvtrwar eagrsaeaal
     1081 argdgdaara grlltsaaeg yaemtdvtdq miasalavgp lteadppaaa atlarvrafa
     1141 grhaatgllr iagag
//
LOCUS       WP_457603655             146 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603655
VERSION     WP_457603655.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  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 146)
  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 146)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12153064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..146
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16306
     Region          <4..112
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
ORIGIN      
        1 mtkdewvkal yglanppsas dviegrliei alralelgvn vvidfglwgr dersalrqaa
       61 adlgasvtmr yfqltpaeqr qrldrrqaee phttwhmsde elatwaavms iptpgeldgs
      121 epvddppagf atwdewrrhr wpavis
//
LOCUS       WP_457603669             322 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase enzyme family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603669
VERSION     WP_457603669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..322
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35198
     Region          41..267
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 midkpdider llaaevaaaw svdvvdlafm pvgldghawa yrveasdggr yflkvrrgdf
       61 spaavllpgf lrtqglrqvv apldlrldgg varrfgdyrl llypfqdgds lwgrgltdrq
      121 wteygdflgr lhrvtpsaev aavlpvetyr ssagdrlral ggqaaasetl gafwkrygaa
      181 lrrlaetvdd lasrvtpgqh vichadihpg nliadgdgtl hvvdwdapil aprerdlmfv
      241 hsadfgdhpi nahraelfre gygalepdpv llsyyrgerh lddvaaflgs ilgpeasaes
      301 randlhwlir iaeavadpgy ap
//
LOCUS       WP_457603677             576 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603677
VERSION     WP_457603677.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 576)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..576
                     /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=63411
     Region          <151..319
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtdepprppa pearpgerat rrprsidpre lgftprrpvp wlaplllist glrtllamlf
       61 gayldkrelq nafsdgtfrq vgpdgglwld yvadlgdgfd atysvaylla qpeltvdght
      121 lpraqtlvmg gdqvypaagy eayedrckgp yqaalpvapp eqpklfavpg nhdwydglta
      181 flrlfvrtrd rhfagwgtgq srsyfavelp agwwllgldd qsgsylddpq ltyfdevark
      241 ltpeskvila vpaptwvkav dhpnaydsid yfirtlvapt gaqvrvlvsg dlhhyaryag
      301 tdrqlitcgg ggaylypthr lpeklevppr dtltrrasnt reydlaaryp dkarsrrygw
      361 gifarlpfrn pgfttllgtl htllmlamag vavqqvgtte qrlfsvplai mlvvammgav
      421 ffakpptagg krharhwilg vahglaqial aaggtwvwlq lpfydwpwpl pavaavvlyg
      481 plsglvasql valyllvaga fgvnlnelfa aqgiedskaf lrfridpdgt ltiypiavdk
      541 vshdwqlnpd qsptaawltp ktpltprlae ppivir
//
LOCUS       WP_457603685             724 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603685
VERSION     WP_457603685.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..724
                     /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=76658
     Region          33..393
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          475..709
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mtsppltkva dregspaeep agtatgrepg reatpsrfra dvaglravav glvllyhagl
       61 pfipggfvgv dvffvisgfl itgqliseie rsgrvsltgf yarrakrilp aatvvlaata
      121 vavrlfvprg ewqviggdia aaatyvvnwr fadravdyla edvapspvqh fwslaveeqf
      181 yllwpllivl ailaarrlrr anvrpvlwvg lavlavpsfv wsivetansp eraffvsttr
      241 lwelavgaav allavraarm prsvavvlgw lglaaivvaa llvsgktawp gyaaalptlg
      301 aaaviaagaa agsrgpvlvl gmrpfqwigd lsyslylwhw pmlvvaaahf gdlsvteglv
      361 valasvipaw ltfrlvenpl rysrkistsp rlalslggnf tlagicaglv lvlmgawaaa
      421 atttkgryap gaallstapg tapigpvper fdaitpdplq irqgfmdvpd tnrdkcfqqv
      481 egaevlscty gvpngsttva lvgdskmdqw lpafqvlaaq ndwkllimak agcaftsaqv
      541 lkgdgsgkpy tdciewnral ldrlvqerpd yvvtsqsast aldsggerat vaamvsgvra
      601 swkkldsvgt kvvvlannph pgaavacadk nrkrlsacaf drekhdqdpa yrmqrqavag
      661 apkvkmidlf davcptdrcp vvfgnvliyr ggshigaayv kttaphlara lsdvgvparf
      721 tpag
//
LOCUS       WP_457603695             318 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfotransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603695
VERSION     WP_457603695.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Gunal,S., Hardman,R., Kopriva,S. and Mueller,J.W.
  TITLE     Sulfation pathways from red to green
  JOURNAL   J Biol Chem 294 (33), 12293-12312 (2019)
   PUBMED   31270211
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kakuta,Y., Pedersen,L.G., Pedersen,L.C. and Negishi,M.
  TITLE     Conserved structural motifs in the sulfotransferase family
  JOURNAL   Trends Biochem Sci 23 (4), 129-130 (1998)
   PUBMED   9584614
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..318
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050656 - 3'-phosphoadenosine
                     5'-phosphosulfate binding [Evidence IEA]"
                     /calculated_mol_wt=35354
     Region          131..276
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msspspvfva gtgrsgtsri advigqhpli hripmetkfl vepgglrdla daltdrydpi
       61 vgedalhrls dfltvrvpgr rddrgktvpe lvgerryrda vhrlwpqvia hafeepapae
      121 gfgdgdrpag pfgpasrrrv vpryfrdrse ligvlrglvd tlfggaaada gkptwcektp
      181 fnlfyldflw elvpeativh ikrhpisvla shlaqpwaps tvdgvlayll pvydrwlawr
      241 naadltsrry vevkaedlaa dwpgqrralf erlgvedavt astfqadkla hrddqfdagt
      301 rayverelge iipamgye
//
LOCUS       WP_457603697             302 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603697
VERSION     WP_457603697.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..302
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31752
     Region          8..231
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msgepvavea rdlsrrygav walrecsfal panrvvalvg angagkstll siiagtlaat
       61 ggtvsvhgrq vvrggsadgg srvailaqdk plyrdftvsd mlrfgrstnr vwdqrralsw
      121 ldrfavpldr rcgklsggqr aqvalavalg srpavlllde planldplar vevtgellae
      181 vadddmivml sthivaelsg vgdhllllda grpvltgdve elldshvrlt gpradqppgp
      241 gtvvqaqhtg rqstfvlrrp atpaahavva pgwtaqpitl delilthlra saaapherea
      301 aa
//
LOCUS       WP_457603699             250 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603699
VERSION     WP_457603699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..250
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26147
     Region          10..243
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlglpahvna clfdldgvlt qtakvhnaaw aetfdaylrr rsaetgepfh pfdsgpdynr
       61 yvdgrpradg vrtflasrgi tlpegspddp peadtvnglg nrknvvllqr iehdgvevye
      121 gsvryleaat taglrravvs asancaavvh aagldrwlea rvdgvvaran glrgkpapdt
      181 flegarllgv epsqaavfed alagvaagra ggfgyvvgvd rvgqadella hgadvvvtdl
      241 adllapelaa
//
LOCUS       WP_457603701             790 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603701
VERSION     WP_457603701.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..790
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88660
     Region          9..764
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mireraypve pwhvremqld mdvlaqsesv falsnghigl rgnldegeph glpgtylnsf
       61 yelrplpyae agfgfpesgq tivnvtngkl irllvddepl dvrygellah ervldmragt
      121 lqrelhwrsp agrevkvrtt rlvsftqrsv aaihyevepv dgplrlilqs elvaneslpp
      181 qsrdprvaav lesplqaeee lttddggqli hrtkvsglrv aaamghdvdg perttieseg
      241 yedwvrttig cvlkpgqtlr vvkyltygws srrslpalrd qvgaalaaar ldgwdglcra
      301 qreyldafwd aadvrvegdp evqqavrfgl fhvlqagara errpisakgl tgpgydghaf
      361 wdtemfvlpv ltytqpgavr dalqwrydtl aqaqerartl nlegaafpwr tiegpessay
      421 wpagtaafhi aadvadalrr yvlvtgdeal ereiglelli etarlwrslg hhdragrfhi
      481 dgvtgpdeyt avkndnvytn lmaqrnlrta adcamryrdq aldlgvteee aaawrdaand
      541 mhvpydaete vheqvegftr fqewdfehtp pekyplllhy pyfdlyrkqv vkqadlvlam
      601 hwrgdafsaa eklrnfvyye rrtvrdssls actqavlaae vgylelahry lreaalmdlh
      661 dlnentrdgv hmaslagawi alvagfgglr dhdgmlsfap rlssrlsrle fslqwhgmrl
      721 rvdvrphqtt yslrnggpdt vvelrhhgep lqvtsaqpvt vavppthprg pqpeqpqgra
      781 plmhlperme
//
LOCUS       WP_457603709             113 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603709
VERSION     WP_457603709.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..113
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11979
     Region          1..98
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(17,19..21,27,50,52..54,56..58,61..62,84,88..89,91)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            53
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mttrqgrvgp vievagdldm asapqlrdrl levvetgart vvvdltqvgf vdssglgalv
       61 lvyknlrecd gwlglavvrq sirnvfsits vdrviplfgt vrdaedgspa avr
//
LOCUS       WP_457603713             322 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603713
VERSION     WP_457603713.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..322
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33795
     Region          6..319
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtapalltvd rltvrfrlrd avvhavtdls ltlrpgella vvgesgcgks vlahallgll
       61 prnatvtgqa rlhapgreea dligagerhl arhvrgrgvg lvpqspatal tpvrtgrkll
      121 eetlrahghs rrdapaaaar iaadvgldpa dlnryphels ggmaqrlata lalapdppvl
      181 ladepttgld rplvdhtldl lrrrcdtgaa vllithdlta arrvadtvav myasrivehr
      241 ptealfdgpa hpytagllda lpdrafvpvp ghppaltdlp ggcafaprca ratgtcdalp
      301 rlaadgegrv achhplreev pa
//
LOCUS       WP_457603715             236 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603715
VERSION     WP_457603715.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  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 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   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   4  (residues 1 to 236)
  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 236)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24401
     Region          25..235
                     /region_name="DppF"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1124"
                     /db_xref="CDD:440741"
ORIGIN      
        1 mtltvpgatd aaapgaapaa glaahqvcva yggqrvldrv dlhvapgetv glrgpsgsgk
       61 stlarvlall hapdgghvti dgqplggvrh rlpahlrtrv ailfqspraa tdprlsladi
      121 iaeplratgt sreqaaarta eladlvglta dlltrrphav sdgqlqracl aralvhrpdy
      181 llcdeataml dastqahvaa vvtdyqrrqg agvlvithdp almarwatrv vdlpaa
//
LOCUS       WP_457603717             158 aa            linear   BCT 27-JAN-2026
DEFINITION  TspO/MBR family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603717
VERSION     WP_457603717.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Campanella,M. and Turkheimer,F.E.
  TITLE     TSPO: functions and applications of a mitochondrial stress response
            pathway
  JOURNAL   Biochem Soc Trans 43 (4), 593-594 (2015)
   PUBMED   26551698
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..158
                     /product="TspO/MBR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=16272
     Region          31..155
                     /region_name="TspO"
                     /note="Tryptophan-rich sensory protein TspO/CrtK
                     (mitochondrial benzodiazepine receptor homolog) [Signal
                     transduction mechanisms]; COG3476"
                     /db_xref="CDD:442699"
     Site            order(48..49,51..52,92,140,143..144,147)
                     /site_type="lipid-binding"
                     /note="lipid binding site [chemical binding]"
                     /db_xref="CDD:320706"
ORIGIN      
        1 mrvptlvkta aavtataaag aaatstgtss rwyrclrkpa wqppsaafpl vwtplyglia
       61 vagaraldrs egperaafar gyalnlalna gwtalffgar rpgaalaeia alnasnlvll
      121 rraartdrpa gaalapyvaw tlfatalnga ivglnrgr
//
LOCUS       WP_457603719             292 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603719
VERSION     WP_457603719.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..292
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32172
     Region          34..89
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..277
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mssphpyare lgaflrarrg rlrprdvgle pggrrkvtgl rreelallag lstdyyqrme
       61 qgrevrpsdd vldalagalg lddterrhlf tlaraarrpv pasvdreper vpdgtrrllr
      121 vmdtpavvlg rhldlldwnp maqallgdpa dhppgrlnml lllfddaltg grscpdwerq
      181 aldyigmlra avaddpthpr ataivgelsi rsaefrrlwa rhdvrasvsg tktfrvpglg
      241 divldwdtyp lpgspgpvml vftaepgspd adrlrllasw ratrpasadg rp
//
LOCUS       WP_457603725             397 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603725
VERSION     WP_457603725.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..397
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=42822
     Region          4..390
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mserdalrgl lrqshharpe dlpgmarraa rqlgaddmil yvvdheqrql lalpgpdapr
       61 rvslaiegtl agrafsmlrp fggpvddgar lwlpllygle rvgvaevvaa aavpdsevaa
      121 feavasllae lvitrshhsd tiervrrrep mrlpaemlra qlppltfstg gviisgilep
      181 cydvggdafd yavngdiahl alfdavghgs gggmravmla slalaayrna rrggfdlvet
      241 yhhidtaard hdrrglitgv laeldqrtgr lrvisaghpg glvlrrgrva avlptptalp
      301 valgdrrppm vveealepgd dvlfytdgii earsadgerf gterlvdftv raladglplp
      361 etarrlvhai layqddrlqd datvlmvrfr eptagra
//
LOCUS       WP_457603732             160 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603732
VERSION     WP_457603732.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..160
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17049
     Region          16..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msaapveesa rrsgplldhl arrmrlrses vlaplglrpr hlvaltvlrd aggisqqala
       61 gtlqidstnv vgllndlead glaerrrspe drrrhevrlt eagtkrlrea ecalagaeee
      121 vlgalapger dllydllrra tqgrsstcge viaeggpgac
//
LOCUS       WP_457603738             501 aa            linear   BCT 27-JAN-2026
DEFINITION  leucyl aminopeptidase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603738
VERSION     WP_457603738.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..501
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51657
     Region          14..500
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mlvirlvsgp agpdalvlpv rpggpdspds lasldptvsp astarlvpta vplgddvpae
       61 aaavlpatrl tgaagevreh lrpggsparl wllgvgegae rdwrtagaal araakdetqi
      121 tialpgeata alrglaegll lgsyrfrlte agkrpalaev svlvddpdal agtldaarat
      181 aettrlardl tnmpsstknp ewfaaqvaea asgrpglhlr vrgpeelaae gfggllavgg
      241 gsasgprlve ldwrpdgart hvvlvgkgit fdtggisikp vpamklmrkd magaaaviaa
      301 tlgaaelrlp vrvttlapla enmvsgsafr pgdvirhygg ltsestnsda egrlvladal
      361 ayavrelkpd llidlatltg anavalgkrh aalysendal aaglldaita agerawrmpl
      421 addyveylas eiadlhsspa qgagsvvaal flreftgdlr drwahldmsa pswsddthge
      481 lvkgatgwgv rgllrwlatl g
//
LOCUS       WP_457603740             318 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603740
VERSION     WP_457603740.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..318
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31901
     Region          45..275
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mptvphrppl daltvgafal avasvsssap lvafaaasal avafwrtals vavlgpvalt
       61 rrraelralt vgpgrregly cvlsgvalaa hfatwmpsaq ltsvaaatal gatqpvwqgl
      121 iargqgrrlp tavwagiava vlgavlatga dfgvsgrafa gdllavvggl faavytafge
      181 rarasisttt yttvcygvca aillvvclvg gvrlhgfdga twlailglva gaqllghsmf
      241 nyalhrvsat tvsvlillea pgaaligwvw lgqlprplal pglalllagv avvvlggara
      301 grratpvaap adptplgd
//
LOCUS       WP_457603744             218 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603744
VERSION     WP_457603744.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  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..218
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..218
                     /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=22907
     Region          22..215
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mrdllpaeva vavadaadwa gellpaelaa lgeravpgrr rdftagrvca rralgalglp
       61 ampvpagadr apiwppgvvg aithtrdyca aaaaratdvr avgidaeryr plspgvrrkv
      121 crpdeeadla rlppgtpwpt vlfsaketvy kvwhplvgtw lgfadarvvl dpetgtfhaa
      181 iaparlaaap vpdppsavtg rfavdddlvr taavllrr
//
LOCUS       WP_457603754             416 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603754
VERSION     WP_457603754.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   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   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Domain dislocation: a change of core structure in periplasmic
            binding proteins in their evolutionary history
  JOURNAL   J Mol Biol 286 (1), 279-290 (1999)
   PUBMED   9931266
REFERENCE   6  (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   7  (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 11450659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..416
                     /product="sugar 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=43011
     Region          1..416
                     /region_name="MalE"
                     /note="Maltose-binding periplasmic protein MalE
                     [Carbohydrate transport and metabolism]; COG2182"
                     /db_xref="CDD:441785"
ORIGIN      
        1 mrirtagvva vlglalaasg cgdsgsdkpa adesakatgg klviwaddkr taalkpfaee
       61 fgkengvtve vqavskdlqt nfvtasqqgs gpdvvvgahd wignlvqnga idpvqlpaeq
      121 kagfnetavk avtfngqlyg vpyatenial irntelapea pktiedlvaa gkklkaekka
      181 seilclqsgq ngdayhiypl ytsgggylfg taangdydpk dlgvgkpesi aafqkiaklg
      241 ekgegalkrs itgensiatf tgkkcaflvs gpwavadakk anisydispv pgfaggkeaq
      301 pfvgvqafyv aakgknkala qefvtnyvtk pelavalyka eprppaltaa fdqvkgedpd
      361 lakfseagkn gqvlpaipam aaiwdpfgka eaaiiggadp aktitaaskt iqgqik
//
LOCUS       WP_457603762             224 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603762
VERSION     WP_457603762.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..224
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23229
     Region          15..190
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtgvalaeel lllayddetg katmprisld lgmaaavlve lalagrvaya dgnlavvdpa
       61 ptgepiadav lakiaadtph tpsswvqrlr hglrdrilsd lcgrgvvrdv detelgfihv
      121 hrypvadasv eadirqrlad altsgqlpde rtaalatlva vlrmepalgl tgpaaedagr
      181 rleeiaagag fsgtvsrdds vvrpsislvi talgqavdaa lgkr
//
LOCUS       WP_457603766             577 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603766
VERSION     WP_457603766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 577)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 577)
  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 577)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..577
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62278
     Region          2..574
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mlirllrshl hpyrrwlaav vafqfvgtia slylpslnad iidrgvavgd tdqilrtggw
       61 mlvvsllqia csiaavyfga ktamafgrdv rgsifrrvns fsarevarfg apslitrntn
      121 dvqqvqmlvl lsctmlvaap imsvggvvma lredvglswl mlvcvpvlav algliirrmv
      181 pgfrlmqtri dtvnrvlreq itgirvvraf vrepyetdrf rvantdlttt alrigrlqal
      241 ifpivmlvln vssvavlwfg aarvdsgqiq vgaltaflqy lmqilmavmm atfmlmmvpr
      301 aavcaeriee vldtdssvvp atdpvtevtg rgelelrgag fqypgasapv lhdisfraep
      361 grttaiigst gagkttlltl iprlvdptag avlvdgvdvr nlapnelwrr iglvpqrpyl
      421 ftgtvannlr ygnpdatdad lwaaleiaqa rdfvtempgg leapiaqggt nvsggqrqrl
      481 aiaralvrkp eiylfddsfs aldlgtdarl raalkpvtad aavvivaqrv stiidadqii
      541 vledggvvgm grheellesc ptyaeivasq qtaevaa
//
LOCUS       WP_457603768             171 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603768
VERSION     WP_457603768.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..171
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18044
     Region          10..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 megvpstges apgpppssea sralrdvlri agdtraalar rlglnatdaa aidhlvsspe
       61 plgpvelgnr lgirsasatt lvdrlvqagh vartphpydr rrlslqvtes avsevlealr
      121 pmlvgvdrav arltpeqaea ttaflrevte vmreyvatap depsraradr g
//
LOCUS       WP_457603770             583 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603770
VERSION     WP_457603770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..583
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61049
     Region          1..459
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglasvav yadsdrdalh atladeayal ggdtaadsyl
       61 ridklidvaa rsgadavhpg ygflsenadf aqavidaglt wigptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvgna devmafavdh glpvaikaaf ggggrglkva rtmeeiphlf
      181 esatreavaa fgrgecfver yldkprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltdaq raqihdsaka icreagyhga gtveylvgvd gtisflevnt rlqvehpvte
      301 etagidlvre qfriadgekl rftedptprg haiefringe dpgrnflpap gtvtalrlps
      361 gpgvrvdtgi sagdviggnf dsllakviiv getrtealer arraldemvv dgmatalpfh
      421 rlvirdeaft aepftvhtrw ietewdntvp aftatagaad epaeretvvv evggkrlevv
      481 lpaglgagta aaapaakkpa rrggggkaga avsgdtltsp mqgtivkiav adgdevaegd
      541 lvvvleamkm eqplhahkag tvgglaaevg avitagaaic tia
//
LOCUS       WP_457603774             661 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603774
VERSION     WP_457603774.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..661
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69356
     Region          12..268
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(12,36..37,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msnalpqlva dryrlltplg qggmgrvwka rdevlhrdva ikelvpppgl tpeerremre
       61 rslrearaia rlnnvnvvri fdvlrtdgdp wivmeyvask slqdtiaedg pvsvakavei
      121 glgvlnalka ahkagimhrd vkpgnvllge dgrvvltdfg latipgdpnv trtgmvlgsp
      181 ayisperard gtagpeadlw slgatlyaav egkspyarps aiatlaalat epmppprnag
      241 plkpvlqgll rkdpderita evaermlrka agrraksisl ldgvrrpgpn gprvprpplv
      301 paprpadqae raasgvaatg gtaaaadpta kvpaptsdag ptakvtpppa dptakldpap
      361 sadetlvdde arvdgvdpal detrldgepv tdtpapvspa asgsapvspa pasadpapst
      421 gratvlpvek sapnrrnlli galvllllvg lvvavpllns gddgdggept agtsasaapp
      481 papsesasps apaasasasp tpsaspsasg aalpagwrly tgpngfkvpi penfqarvgg
      541 dnvvlyevgg srrvlfiqwt sdpkpdaytd wqkqepyras rvrgyklvgi tecdpyfrtc
      601 adwdwletrn gdtrfhvrnr gvatagnrgf alrwevpakd wdanlanwei itkgfvpdrk
      661 n
//
LOCUS       WP_457603778             303 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603778
VERSION     WP_457603778.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..303
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31777
     Region          83..303
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mveyrtvfda evvfsngggl rtdgfrldvp hpdvtddeva allvrhlgll mvgevritnr
       61 tvveephkgg rgvtaptggg grrvvelshv itdglvtlpg wpapaitewl treasrsrya
      121 pgvefqvgri dmiantgtyv dtpshrfadg pdltgvpldr ladlpglvvr vpagtravdr
      181 lmlapydvag cavllhtrwd ahfgtdayaa pdapyltgdg aqwlaesgaa lvgidsinid
      241 dmtaaaagqr pahtgllaag vpivehltgl dalpptgfrf taapprvagm gtfpvrafav
      301 vda
//
LOCUS       WP_457603786             252 aa            linear   BCT 27-JAN-2026
DEFINITION  Bax inhibitor-1/YccA family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603786
VERSION     WP_457603786.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Guo,G., Xu,M., Chang,Y., Luyten,T., Seitaj,B., Liu,W., Zhu,P.,
            Bultynck,G., Shi,L., Quick,M. and Liu,Q.
  TITLE     Ion and pH Sensitivity of a TMBIM Ca2+ Channel
  JOURNAL   Structure 27 (6), 1013-1021 (2019)
   PUBMED   30930064
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Watanabe,N. and Lam,E.
  TITLE     Bax Inhibitor-1, a conserved cell death suppressor, is a key
            molecular switch downstream from a variety of biotic and abiotic
            stress signals in plants
  JOURNAL   Int J Mol Sci 10 (7), 3149-3167 (2009)
   PUBMED   19742129
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Zhou,J., Zhu,T., Hu,C., Li,H., Chen,G., Xu,G., Wang,S., Zhou,J. and
            Ma,D.
  TITLE     Comparative genomics and function analysis on BI1 family
  JOURNAL   Comput Biol Chem 32 (3), 159-162 (2008)
   PUBMED   18440869
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Reimers,K., Choi,C.Y., Bucan,V. and Vogt,P.M.
  TITLE     The Bax Inhibitor-1 (BI-1) family in apoptosis and tumorigenesis
  JOURNAL   Curr Mol Med 8 (2), 148-156 (2008)
   PUBMED   18336295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..252
                     /product="Bax inhibitor-1/YccA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26903
     Region          3..252
                     /region_name="COG4760"
                     /note="Uncharacterized membrane protein, YccA/Bax
                     inhibitor family [Function unknown]"
                     /db_xref="CDD:443793"
ORIGIN      
        1 mrsanpvldr lddvgraerq vlgvgtadtm tvadvisrtv glllvtgvta avswvvvpqa
       61 awisaalags alaslalvlv islkqitspp ivvgyavlqg lllgvasraf emvypgivaq
      121 avigtfgvfl gmavlyrarl vratprlarl vigtlvgiva iglvnlvayl ftgrqgvvvy
      181 slsdrvgwlp ylfsvvaiia galsfildfd lversaanrl prryawycaf gllvglifly
      241 wqilrllsyv rr
//
LOCUS       WP_457603788             494 aa            linear   BCT 27-JAN-2026
DEFINITION  CYTH and CHAD domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603788
VERSION     WP_457603788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Lorenzo-Orts,L., Hohmann,U., Zhu,J. and Hothorn,M.
  TITLE     Molecular characterization of CHAD domains as inorganic
            polyphosphate-binding modules
  JOURNAL   Life Sci Alliance 2 (3) (2019)
   PUBMED   31133615
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Tumlirsch,T. and Jendrossek,D.
  TITLE     Proteins with CHADs (Conserved Histidine alpha-Helical Domains) Are
            Attached to Polyphosphate Granules In Vivo and Constitute a Novel
            Family of Polyphosphate-Associated Proteins (Phosins)
  JOURNAL   Appl Environ Microbiol 83 (7) (2017)
   PUBMED   28130300
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Martinez,J., Truffault,V. and Hothorn,M.
  TITLE     Structural Determinants for Substrate Binding and Catalysis in
            Triphosphate Tunnel Metalloenzymes
  JOURNAL   J Biol Chem 290 (38), 23348-23360 (2015)
   PUBMED   26221030
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Bettendorff,L. and Wins,P.
  TITLE     Thiamine triphosphatase and the CYTH superfamily of proteins
  JOURNAL   FEBS J 280 (24), 6443-6455 (2013)
   PUBMED   24021036
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Kohn,G., Delvaux,D., Lakaye,B., Servais,A.C., Scholer,G.,
            Fillet,M., Elias,B., Derochette,J.M., Crommen,J., Wins,P. and
            Bettendorff,L.
  TITLE     High inorganic triphosphatase activities in bacteria and mammalian
            cells: identification of the enzymes involved
  JOURNAL   PLoS One 7 (9), e43879 (2012)
   PUBMED   22984449
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The catalytic domains of thiamine triphosphatase and CyaB-like
            adenylyl cyclase define a novel superfamily of domains that bind
            organic phosphates
  JOURNAL   BMC Genomics 3 (1), 33 (2002)
   PUBMED   12456267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18995808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="CYTH and CHAD domain-containing protein"
                     /EC_number="3.6.1.25"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050355 - inorganic triphosphate
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=54513
     Region          6..179
                     /region_name="CYTH-like_Pase"
                     /note="CYTH-like (also known as triphosphate tunnel
                     metalloenzyme (TTM)-like) Phosphatases; cd07374"
                     /db_xref="CDD:143620"
     Site            order(6,8,10,43,57,59,61,72,82,119,121,140,157,159)
                     /site_type="other"
                     /note="putative active site"
                     /db_xref="CDD:143620"
     Site            order(6,8,138,157,159)
                     /site_type="other"
                     /note="putative metal binding residues [ion binding]"
                     /db_xref="CDD:143620"
     Site            order(6,8,10)
                     /site_type="active"
                     /note="signature motif [active]"
                     /db_xref="CDD:143620"
     Site            order(8,10,43,57,61,72,82,121,157)
                     /site_type="other"
                     /note="putative triphosphate binding site [ion binding]"
                     /db_xref="CDD:143620"
     Region          209..487
                     /region_name="CHAD"
                     /note="CHAD domain, binds inorganic polyphosphates
                     [Function unknown]; COG5607"
                     /db_xref="CDD:444338"
ORIGIN      
        1 matvvererk ysgdegfrlp dltgcggvvt msdatvsdld avywdtddll llrsghalrr
       61 rtgghdagwh lkvgavggar vehqfpagas ddgpppelva lirgasrgrp vapaarvvnr
      121 rrehrlldad grvlaevaed dvrsedlvdg aartwheiei elvegdeell dalgerlraa
      181 garevtvsks hravagrier fddrepdgpa apvlayvrvq rdaivgnhaa gyqgnedavh
      241 dmrvatrrlr atlrtfrglw drreseavra elrrlggelg rvrdtqvmaa rlteavhelp
      301 delvlgpvaa rigerfaadl aeattalrsa ldsdrypall trldrladap padvgrrwtd
      361 rrirkavrra dtrldralat tgpdgdaalh earkklkaar yavevrepaa gkraarlvkr
      421 fkalqdllgt hqdsvvtrev lrrqalqaya dgentftygl lharqaeaag hdrpavlrar
      481 drsrhrkvrr wlkp
//
LOCUS       WP_457603803             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ion transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603803
VERSION     WP_457603803.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..292
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32544
     Region          11..228
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 maghcariva srpfevaivv limangvvlg ietypnlgaa gpvlrwtewm fravfvveis
       61 irvlaygrrp qdffrhgwnv fdllvtaaif vpglhgdsav lrfirvarvl rlvrfspglr
      121 tivaalwrsl pgvagflala avtlyvygma gwlifgdryp eqygdigrsl vtlfvllsle
      181 tlpdlleqgl evspwtllyy vsfvmiavnl llniliaviv nsmeearrle mteglaadyd
      241 sdgdgipdev driaisqrld dlrmviaele relridreep pgaprrrqps dh
//
LOCUS       WP_457603805             301 aa            linear   BCT 27-JAN-2026
DEFINITION  TatD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603805
VERSION     WP_457603805.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..301
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32103
     Region          36..298
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlaamteqte trkqraarra gefppapepl pvpvpdshth lditvgefgt ppggttgddp
       61 vaaaidvaar agvdrlvqvg vdadssrwsa dvadryapvl atvalhpnea prladldeal
      121 reietlagrd rvrgvgetgm dffrtgddgr aaqeesfrah iaiakrhgka lvihdrdaha
      181 dvlrivddeg apetvvmhcf sgdadfarec vrrgfllsfa gtvtfgsaaa lreaaavtpp
      241 eqmlvetdap yltpmpyrgr pnasyliplt vrflaettgt dvdalcaals tngerafgpw
      301 r
//
LOCUS       WP_457603815             340 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603815
VERSION     WP_457603815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..340
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35102
     Region          1..321
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrtcrvglvg aggvaqrhar vltgfadvel lgvtdvapda agalagtygg rvfrdvdell
       61 aagpdavyvc vppfahgpve eavvaagvpm fvekpvaldl etaervaalv qqqglltgvg
      121 hhwrylhvve earrllagrp vrmvngawld kvppvawwar rdrsggpvve qaahvldlvr
      181 llageavevt aygdgspppv dgadidsvta atlrfgsgav gtlaascvlg wkhragveil
      241 adglalwlae dgltvrdadg erhvpadpdg arvavdrafv davcglgddv rvpyaealrt
      301 hrlalavaes artgrpvalp tgpasrlsap vadagvsvda
//
LOCUS       WP_457603819             348 aa            linear   BCT 27-JAN-2026
DEFINITION  iron-containing redox enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603819
VERSION     WP_457603819.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilks,A.
  TITLE     Heme oxygenase: evolution, structure, and mechanism
  JOURNAL   Antioxid Redox Signal 4 (4), 603-614 (2002)
   PUBMED   12230872
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Ryter,S.W. and Tyrrell,R.M.
  TITLE     The heme synthesis and degradation pathways: role in oxidant
            sensitivity. Heme oxygenase has both pro- and antioxidant
            properties
  JOURNAL   Free Radic Biol Med 28 (2), 289-309 (2000)
   PUBMED   11281297
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Maines,M.D.
  TITLE     Heme oxygenase: function, multiplicity, regulatory mechanisms, and
            clinical applications
  JOURNAL   FASEB J 2 (10), 2557-2568 (1988)
   PUBMED   3290025
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..348
                     /product="iron-containing redox enzyme family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37415
     Region          144..312
                     /region_name="Haem_oxygenas_2"
                     /note="Iron-containing redox enzyme; pfam14518"
                     /db_xref="CDD:434009"
ORIGIN      
        1 msvvadrryg paplpaargp vsaallaalr dtprelpagl gaafdavaap ltdedlqltl
       61 flcyelhyrg wsgvdeawew epsllalrar aerpfeaalr elagpqpavl pagvpgalad
      121 lvaaddgppl avtlqrradl drfrefvthr siyhlreadp hswalprlgg pakaalveiq
      181 tdeygngrld rmhaelfrtt mdrlgldtgy aahldrvpav tlatnnlmsl fglhrrlrga
      241 llghlaayem tsslpnrryg nglrrlgfda vatrfydehv eadavheqia aydmcgglvr
      301 aepalasdvl fgaaaalavd alfaahllda wsagesslrp ptqilaaa
//
LOCUS       WP_457603825             807 aa            linear   BCT 27-JAN-2026
DEFINITION  ArnT family glycosyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603825
VERSION     WP_457603825.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 807)
  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   3  (residues 1 to 807)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..807
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80488
     Region          36..>273
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mnrtdsppta ptagppgtep apapvpeetr tgrdprwarp alagllvata llylwglgas
       61 gwanafysaa vqagsqswta ffygssdaan sitvdktpas lwlmalsvri fglsgwsilv
      121 pqallgvasv gvlyatvrrw ygpaagllag avlaltpvat lmfrfnnpda llvfllvaaa
      181 yatvraveta strwivltgv lvgfgfltkm lqaflvipvf agvyllaapt glgrrirqll
      241 laglavvvsa gwwvaivela pasarpyigg sqnnsilelt lgynglgrit gdevgsvggg
      301 ggrpggggsg pfsgqtgllr mfdtevggqi swllpaalil lvaglwlagr aprtdrtrag
      361 lllwggwllv tglifsfmsg ifhayytval apavgalagi gvtllwrars apveavaaap
      421 vpavadapvv agasvvaapg rrralvatlv lagtlavtaw wswhllgrta dwhpwlrsti
      481 lavglttaal latsalikef asgngvqsda nslvdsetgv aagpgvgfag rvvrwvvpvv
      541 svagiavala gpaayatqta atphsgsips agptgaggfg gpggpggrmp gggngqfpgf
      601 pggpngtgsd gtgsdgsgpg gtgqdggana ggfpgfpggg sapgapggtg qdggtapggt
      661 pgqggfpgqd ggtgqegrgq rgggmgglld arepsaemta lltadaddyt wvaatigsnn
      721 asgyqlatgr pvmpiggfng sdpsptlaqf qryvadgrih yflggggfra dggsnasaei
      781 aawvtetfta ttvdgvtvyd lssgkqg
//
LOCUS       WP_457603833             590 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603833
VERSION     WP_457603833.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..590
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63496
     Region          21..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maaeeathrp pttprpaaps rpdvsvvvpv yntlrylrsc ldsvlrqtig pgrmeivavd
       61 dgstdgsgrl ldryaakhpg tvrlvhqpns ggpaspcnrg ldlatgryvf flgsddrlgp
      121 ealerlvaaa drygsdvvlg kvvgvngrhv fsdvfadgna vdvslfdsal pwslantklf
      181 rrdlvdrlgl rfpedmpvls dqpftlaacy harrisvlad ydyyhavrrl darnityhsr
      241 veqrlvsver lfayvadlip agarrdavlr rhaglelanl vgddfrhldr aaqervhatv
      301 arlvrrhvtd glrdrldiea rlrlgavtag gvddllavie qdsgrgvpat vfagdrwhag
      361 ypgaparwtd vtdvradwla rldtvdvswv dghtltvttr spyprfatea gpvrmlagpv
      421 vgatrmdagd ptgrtlrtdf aldrllaass asgqrhpvra evdgghgrgg aavraprlaa
      481 grprllrhga rlygvaatvd prngqlvlsv vpvtvgqlvg rlrrrggrgp ataqtsgrgp
      541 eallgrhghl evrgaaqvqp gplrradqph hhpgaggaap dqargvrvdv
//
LOCUS       WP_457603760             335 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome d ubiquinol oxidase subunit II [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603760
VERSION     WP_457603760.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Borisov,V.B., Gennis,R.B., Hemp,J. and Verkhovsky,M.I.
  TITLE     The cytochrome bd respiratory oxygen reductases
  JOURNAL   Biochim Biophys Acta 1807 (11), 1398-1413 (2011)
   PUBMED   21756872
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..335
                     /product="cytochrome d ubiquinol oxidase subunit II"
                     /EC_number="7.1.1.7"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0006119 - oxidative phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=33827
     Region          1..328
                     /region_name="AppB"
                     /note="Cytochrome bd-type quinol oxidase, subunit 2
                     [Energy production and conversion]; COG1294"
                     /db_xref="CDD:440905"
ORIGIN      
        1 melawyallg lffatylvlg gydygvglll arrgpapgnr atltalgpff lgnevwlvaa
       61 ggilfgafpr legellsgfy pavlaalagv vlvtagvqlr srpasaaara rwdrvvvvgc
      121 llaalgwgav lagllqgvpl sadghvvgvg hlatpfvaaa glallalvav hgatfltlrl
      181 paaeapalar lasglvpaal vavgaatvlg vlsdrvraav arpavavllp lalvaallaa
      241 raalrrgrag vafaatatal alpapligaa lwprilvsta dpaasltvae aaagrptlal
      301 lgwlalpllp allgfqamcw wvfrgridgr apvyw
//
LOCUS       WP_457603835             398 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603835
VERSION     WP_457603835.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..398
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41160
     Region          6..398
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mvtrvtnqgp ltgvrviela gigpgpfasm mladlgadvv rvdrpggggf gafpgdllnr
       61 nrrsiavdlk qpegrdlvld lvagadalve gfrpgvterl glgpddclaa npklvygrmt
      121 gwgqdgplaq raghdidyla ltgalhgvgr agerpvppmn llgdyggggm mlalgvvaal
      181 yavrggapgq vvdaaivdgv svlatqihal rgiglwqdpr gvnlldggap fydtyecadg
      241 ryvavgalep qfyaelvrlt gfppdggdgp qdagaaagge aldrddpanw palraawarl
      301 frtrtrdewt ellagtdacv apvldwaeap ehphlrarev fvapdgvtqp apaprfsatp
      361 tsvrrpppsp gehtdevlag agidagriaa lrnagvig
//
LOCUS       WP_457603837             453 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603837
VERSION     WP_457603837.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..453
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48052
     Region          86..>188
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mqpspvrrrl lavgaalalt lgltgaapaa attgrddgsg plpgytivnp plpplvvgga
       61 attvrqgvha nagyvieipa rwngelvmwa hgyrgqgtel speppgfdlr qrlvaqgyaw
      121 asssydrngy dvrsgvrgtr aladlfsrtv rrphrvliag vsmgghvigr sleqypgyys
      181 galpmcgvlg dqelfdffld ynlvaqalag vrayptppdy ltsavpriqv tlglagltpg
      241 gadttnalgk qlravtvdrs ggprpgadaa favwkdflfg iavgeadgsp arrpgqlatn
      301 lftrytpnqp vnlnatvqrv apenlrqrla pgltevpria grptvpvlsl hglgdlfvpl
      361 rmeqayardv arhgrsrllv qravrtaqhc efspaeagaa wddlvrwvrt gkrpagdavt
      421 drravaapdf gcrfsdhaar aagagtrply ppc
//
LOCUS       WP_457603843            1816 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603843
VERSION     WP_457603843.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1816)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1816)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   3  (residues 1 to 1816)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   4  (residues 1 to 1816)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 1816)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 1816)
  AUTHORS   Keatinge-Clay,A.T. and Stroud,R.M.
  TITLE     The structure of a ketoreductase determines the organization of the
            beta-carbon processing enzymes of modular polyketide synthases
  JOURNAL   Structure 14 (4), 737-748 (2006)
   PUBMED   16564177
REFERENCE   7  (residues 1 to 1816)
  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
REFERENCE   8  (residues 1 to 1816)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 1816)
  AUTHORS   Keating,T.A. and Walsh,C.T.
  TITLE     Initiation, elongation, and termination strategies in polyketide
            and polypeptide antibiotic biosynthesis
  JOURNAL   Curr Opin Chem Biol 3 (5), 598-606 (1999)
   PUBMED   10508662
REFERENCE   10 (residues 1 to 1816)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18690430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1816
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1816
                     /product="type I polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="4.2.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016218 - polyketide synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=188930
     Region          12..1359
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1362..1633
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Region          1718..1793
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mqndipaddg vepiaivgla arlpgaadvd efwrnlvdgv estteltree qlargaqpqe
       61 vddpgwvnra plvdgydqfd aglfgmtare aeitdpqhrl fletcytalq dagydpgryd
      121 gavgvyagtg gntylhrnvf rnkrvggnph gavslatgns pnyvatnvsy rldlrgpsmt
      181 vhtacstslv afhlacealr ngecdmalag gvnielphvg ylgmdgftsp dgrcrpfdag
      241 angtvwgsgv gvtllkrlsd aiadgdtira vvlgnainnd gagkvgftap sidgqmeava
      301 qavelagvdp rsisyveahg tgtalgdpie vaalsavytk dtdergwcgi gsvksnighl
      361 sqpsgivsvi ktvlamehgl ipptinyetp npaidfadtp fyvantltkw dtdggprrag
      421 vssfgiggtn ahvvleeapa agrhepsarp ahllqvsakt ptaldtavrr ladhlesgsd
      481 valadvahtl rvgrqvyahr aavvagdpas aaaalrerrk ghrgvadgpa prvaflfsgq
      541 gsqyagmgae lygqdsayaa avdecaellr pelgldirdl ilgrdpeaad kltetrytqp
      601 alftveyala aawraagvtp aamighsige yvaatvagvl dladalrvva argrlmhslp
      661 agsmlavtld esevtgklpe glsvatvngp gtcvvageta lveefaaslg gknkskllrt
      721 shafhspmtd pildeftalm atvplrapav pfvsnvtgtw iteaqatdpa ywaahlrrpv
      781 rfgacvatll aegtwalvec gpgrqlanla rmqiakagea qraltplgsl pgpgeqtgdv
      841 aallgtagal wcagvpvsvp adpharrvpl ptypferrry widpdpeqel aaapaetgpr
      901 plpewfavpa wrqappvrta eplgrclvla dgprgealva alraagddpv evrageafta
      961 tangfrlrpg vradaeelva algadlprri vhafaldgdp agtdaaaawa aqergffgal
     1021 hlvqalagag vtadeagvrl dlvtagigdv rgddltrpeh atlaglarvl paelpgltvr
     1081 lldtdpaarg vaalvaelrs pvdaehpeva lrgdrrwlag yeqvtvaaed epgvlreegr
     1141 ylitgglggi gvtlaedfar rvraklvlla rsglperdew dahlavhgga dragraiaai
     1201 rrmeaagaev lvlaadvtda ddlrrvrdea errfggldgi vhaaglpggg maevkdrdea
     1261 rrvlapklag tlalarvfgd lpldfvvlcs sitaviggfg qvdycaannf ldafarsgtg
     1321 frapvvsqnw ggwaevgmav etaapaafra agrdtvttav thpvlttmva gpdgtvlhgl
     1381 vsadthwlld ehriggvpvv pgtahlesvr aavvaalpap gpdaavelrd vvflepfsvp
     1441 dgtvaqyrve ltpaedgtdf avaslaagqa rthvrgtagw ttdaappaav pavagrrvdd
     1501 dasfgrgrts mltfgprwaa laehhladge elarvqapaa avgdlpswgm hpalldvata
     1561 fgrgqgsgty lplsygrivv rgalpatfhs hlrhrpaatd evvaadlslr dpdgrelvai
     1621 sdfvlrrvdq davtgnltea paadadaaap vtedirpvdg aeafrrslaa glgaqvvitt
     1681 rtvadirrra arvttdslae etdapagpag vtgggsaapg telektiaqv wrdglgvtdv
     1741 gvdddffalg gnslvavqli aamrkatgvr lpmrslfetp tvaglaarie elraeapada
     1801 paapaaipai prlprg
//
LOCUS       WP_457603851             319 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603851
VERSION     WP_457603851.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..319
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34967
     Region          27..289
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtttapeagr spaperprrp grrpltlrrr esraglalvt ptllvvvavi gipivwtvvl
       61 afqrvrlatl rktglfgelt ldnidrvlht pgfadtlwtt vlysvggtag sivvglvaal
      121 avrgpfrgrt lvrasmllpy vapvvamtfv wqvmldpqlg ivndwgrrfl gwdspvpfls
      181 qestalwtvi afeawryfpf aflfllarlq avpgeleeaa rvdgatptqr frhillpqlm
      241 pvialigvlr fimtfnkfdd vylltggaag tevvsvrvyq fltarteiga aaaqavvlav
      301 vllvfvaiyl rffgarrea
//
LOCUS       WP_457603855             396 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603855
VERSION     WP_457603855.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..396
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41225
     Region          5..368
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(6..7,10,43,98..99,101..103,106,126,129..130,133,210,
                     213..214,217..219,222,246,250,307..308,312,316,332,
                     335..336,339..340,343)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mstygtwlaf gafpliavrv ldssafavsl leaaglavaa vlavplgpwv ayrrklpvmi
       61 atdlvrfaal asvpaayalg vlsygqllvv avvcgtaait ftaasgaylk slvrgdrlla
      121 angrfeatnw aataagpplg galvgllgpv vtitadavsh llsalavrri rsgdtvaprd
      181 pagasrvadl gagwrfvrrd pvlwrlflns vlvgglimat apllavlllg gyrvaawqyg
      241 lvfgvsalgg vlgarlsprl vrrygrhrvm tvsgwlrstv plglafthpg tsglltviav
      301 ewvlitcmgv fnpiyaterl rrtpqahtaq vltawsvtgr ltqaalmtvw gvlatvvgpl
      361 aaitvsgvll lgtplllptr rhtrdpepar pavavs
//
LOCUS       WP_457603859             193 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603859
VERSION     WP_457603859.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..193
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20867
     Region          39..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mnaaflpepp qspaakaaye ddlasdgyvn nltrvwcwrp dvlmsfqntr tellsestls
       61 srevavlvaa taaargdsyc slawgarlag msdeetaaav lrgdeadlse retaladwsr
      121 qvvtdpnatt etdtrrlrea glsdreifea ttliafrlaf stvndalgar pdaqlaekap
      181 rlvretvtfg rpv
//
LOCUS       WP_457603861             218 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603861
VERSION     WP_457603861.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..218
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23262
     Region          2..210
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 miravffdvg gtildetref atwadwlgvp rhtfsavfga viargldyqe vfrafrpdfd
       61 ltaelarrva agdpesfgad dlypdaracl aalreqglrv glagnqpeha eatlraldla
      121 vdvigtaaaw gvakpapeff drvvregggd asailyvgdr pdndaapama agmtaclirr
      181 gpwghildmp dvaerclfri dsldelpalv arhnaagg
//
LOCUS       WP_457603874             248 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603874
VERSION     WP_457603874.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..248
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26399
     Region          21..212
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrfvsdqrla dgvrereftl geipgilwtp asaptsapli llghpgglrr myprlvarar
       61 dctaqgfaaa tlelpgggdr pasaaaeqar adlrralaag epvaddmvdr lvlplvekav
      121 pewravldal lalpeiggpv gysggvisig vrlavvepri vaavlfagsf vpramfaear
      181 rvtvplhvll qwddegndrq maldlfdafg saektlhanm gghtgvprfe gesanrffgr
      241 hlrtppss
//
LOCUS       WP_457603880             606 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603880
VERSION     WP_457603880.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10575293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..606
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66011
     Region          5..36
                     /region_name="AcylCoA_DH_N"
                     /note="Acyl-CoA dehydrogenase N terminal; pfam12418"
                     /db_xref="CDD:463571"
     Region          43..467
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(134,164,166,198,200,449..451,453,455)
                     /site_type="active"
                     /db_xref="CDD:173838"
     Region          478..601
                     /region_name="Acyl-CoA_dh_C"
                     /note="Acetyl-CoA dehydrogenase C-terminal like;
                     pfam12806"
                     /db_xref="CDD:463716"
ORIGIN      
        1 msssdlllsr rdlafllhdw ldvarlterp ryaehsretv devldlaarv aaerfaphnr
       61 aadtgeptfd gqrvrtipqv kaaleafaet gllaatmdes vgglqlphtv aaaafawfqa
      121 anvgtsaypm ltlgnanlll ahgsaeqidt wvrpmiegrf fgtmclsepq agssladltt
      181 raepqddgty rivgtkmwis ggdhelaeni vhlvlaripg appgvkglsl fivpkvlldd
      241 dgnlgprndv vlvglnhklg yrgttntlln fgegvhrpyg ragavgylvg qphqglavmf
      301 hmmnearigi gagatalgyt aylksvayar qrpqgrpvad kdpttpqmpi vahsdvrrml
      361 laqksyvega lalvlycgrl ldeqktapae adreraqlll dlltpitksw paqwclaand
      421 laiqvhggyg ytrdydveqh wrdnrlnaih egthgiqald llgrkvtmrd gaalelllet
      481 irgtvtrawk aegfaselag qlgaavdria vvtrrlwapg dpelalanas vyleavghvv
      541 iawmwleqvl avealgspdg aegeflagkr qaaryfyrwe lpkvgaqfdl legldrttld
      601 mreswf
//
LOCUS       WP_457603882             486 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603882
VERSION     WP_457603882.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 486)
  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 486)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 486)
  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 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..486
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51791
     Region          152..485
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mtevrpdeet vpllgaevri tdaagllaaa vdgpvdllsg gdfpapvrev rctvrantaa
       61 eppvhcfeay lrveaapagl ialglagpvg lllaerlaar ggdgpaaavg riaaeagrri
      121 wprpvatlva pprdpagrev lrtaeeaglr prvdqdngtv riradvpsae vdpahlraml
      181 glllqavrel sgdseepavl rgrtylvgrr pvavtgprsa avtldqvggl pdvvarfrev
      241 avsfrhpqam arwgarrpqg ilmygppgtg ktmlaralan evgadfveir tpeildkylg
      301 gsernikrif rearryrrpt vmlfdefdsi isyagaggda asqavnavag ifkqemntlf
      361 eenpdvivva ttnfpqrvda slirsgrfdl kiaipvpdea graeilskmv relidrherp
      421 gfkmfaddld paalaadtag ltgadlrevl rrvqlakalr eaaegappap igqddlreav
      481 aglrrg
//
LOCUS       WP_457603886             363 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin reductase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603886
VERSION     WP_457603886.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="ferredoxin reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38366
     Region          30..267
                     /region_name="FNR_iron_sulfur_binding_2"
                     /note="Iron-sulfur binding ferredoxin reductase (FNR)
                     proteins combine the FAD and NAD(P) binding regions of FNR
                     with an iron-sulfur binding cluster domain.
                     Ferredoxin-NADP+ (oxido)reductase is an FAD-containing
                     enzyme that catalyzes the reversible electron...; cd06216"
                     /db_xref="CDD:99812"
     Site            order(80,94..97,112..114,116,120..122,161,164,265,267)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99812"
     Site            order(94,96..97)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99812"
     Site            order(119,122,125,132,140,142)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99812"
     Site            order(156,160..163,165)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99812"
     Site            order(161..162,185..187,241..242)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99812"
     Region          279..363
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mtttasrrpq kvtfrdrllr lagtvttpvl pddyldliap lragaplrgk ivairpetrd
       61 aatlviqpgr awqghtpgqy irlgvdvdgv rqwrayslts ppdaadgris vavkaipdgk
      121 vsnhlvrrlr pgtivhldqa qgefvlpaat pervlfltag sgitpvmgml rsgladradv
      181 vlvhsaptrd dvifgtelra ladrgalrli erhtdtdgll dvaelaglvp dhldretwac
      241 gpigmldave gywssnglve rlhterfrpt vitpgeggtv tftgagvtve sdgattllda
      301 genagvlmps gcrmgicfgc vvplrqgavr dlrngdvtta vpgdgvlvqt cvsaaagtcd
      361 idi
//
LOCUS       WP_457603890             422 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603890
VERSION     WP_457603890.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..422
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45470
     Region          37..411
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mhngselpeq lalhggqpvr rtpwptydkg avfvhseded aairavrshl yfrydhrppn
       61 etecgrfede lcryfgtrha lavssgtaal alalmgagvp pgslvacpgf tfvatpsaiv
      121 lagcrpflve vdddlrmdld dlrrrwhpei ravmvvhmrg faadvealsa faaemgvpli
      181 edavpalgae lngrklgtfg aagafstqsd kalncgeggf litddstlfa ravalsgaye
      241 grlrrhfpdg eppltgldlp llslrmdeir aallraeltr lpqrlalfhr nyahvsgala
      301 glpgiavrrp vapgaylgea fvfrvpggda gwfaralrae gvdarnigad ddlnvrafwn
      361 wrflydsadp geiratlprt arlltetvdv plssnltpgd cddlvravrk vaaaretalv
      421 gs
//
LOCUS       WP_457603898             360 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603898
VERSION     WP_457603898.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..360
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40497
     Region          <297..360
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtghrfervt grrglrdfla ltdrlyadep ryvptprqqi rrwwrdgvpm yvlrdatgav
       61 vgrttlhtda dfdaelgrrc qlfgltefta paarplfdai gayvtpgrdl lfgpvallpn
      121 qaggvitsgy adrgfvdsaw nppyypdaye engftgrfvs dtwicpvppp vepppalgvq
      181 pdgarlelhr gntrrldeql dllrrmlnds faqlgyytpi saaqlrrqtd glaylldesl
      241 llyltrdgrp vafvlcvpdi sdflvavrgd lnpvnqlrll atrrryrrea vlivkgvvpe
      301 fqgrgyqrll sahlhhnlhd ggytalrsty vgrdnpasaa qyrrlggrpl hgytfyarer
//
LOCUS       WP_457603900             323 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603900
VERSION     WP_457603900.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..323
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34351
     Region          1..321
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mpltdldlag clayrpeldv padldafwar tldgggdpaa avyepvdtgl tqirtyaati
       61 pgfggepvrg wlhlpagadg plpclveylg ygrgcglahe klfwaaagfa hlimdsrgqg
      121 wsaatggtpd phpypagtvp gfltrgvadp adhyyrrlit dtvrfaeaar rhpavdparv
      181 avtgfsqggg lalaagalcp dvaavmpdvp flcdirrgvr vagpdspyae vvdylalhrd
      241 radqvfrtls yldaavlapr atapalfsia lrdqvcppst cfaayhrygg dkdvrvyefn
      301 dheggeaehq reqltwlrgi lgg
//
LOCUS       WP_457603902             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603902
VERSION     WP_457603902.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..309
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=29867
     Region          7..307
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mpevsttalv aaldiggtkt taalvtaage vvgrrtaptp grsgaaavld taaglveklr
       61 adapgvvral gvgsagvids gsglvlsatd vltgwtgtdl rgdlsrrlgv pvavindvha
      121 halgearhga aagydtvlyv avgtgvgasf vlgdtvlaga hsaaghaghq psayagtlpc
      181 tcggrghlea iaagpalaae yvrrtgrpva dlravaalaa dgdeaarevv rlggaaagsa
      241 vgglvnvldp aavvigggvt glgepwwral rdavraetlp glagvpvlas tlgpdapllg
      301 aaslawkvs
//
LOCUS       WP_457603904             312 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603904
VERSION     WP_457603904.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..312
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32409
     Region          7..312
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mttpaprfag vvppavtplt degevdvhsl erlvewllda gvdgifalgs sgetvfltdr
       61 qrnlaletiv ktaggavpvi agciepttrr vveraeastr lgadglvvta pfyaivgphe
      121 ierhfravaa avelpllayd ipvcvhskls vdlltrlaad gvlagvkdss gddvafrqla
      181 lavaehaper dfslltghev vvdammlagg sgsvpglgnv dpagyvrlhr acvagdwaaa
      241 rreqdrltrl frivdaadpa tsagatrgvg afktalsllg viagnavslp lrpldaaetg
      301 rvrtqlelag ll
//
LOCUS       WP_457603906             652 aa            linear   BCT 27-JAN-2026
DEFINITION  dipeptide/oligopeptide/nickel ABC transporter permease/ATP-binding
            protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603906
VERSION     WP_457603906.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 652)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 652)
  AUTHORS   Monnet,V.
  TITLE     Bacterial oligopeptide-binding proteins
  JOURNAL   Cell Mol Life Sci 60 (10), 2100-2114 (2003)
   PUBMED   14618258
REFERENCE   6  (residues 1 to 652)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..652
                     /product="dipeptide/oligopeptide/nickel ABC transporter
                     permease/ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69264
     Region          8..281
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
     Region          336..642
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mrrslttrls rpgmafarlg laarfalgfv alivvvgvla plllrhdptq tglgpaltgp
       61 ngdfwfgldk lgrdvfsrlv agtrrslivg fgaagialvl gailgavags srtvvdeiim
      121 rcldvvmafp tivlsallii sfgknsllvl viaigfvftp svarivranv lsqygedyva
      181 aeriigarrp hilwrhvlrn caapilvfvt vmvadaivfe aslsfigggl apqeaasswg
      241 sviafgkemv qiggwwatff pgllilltvl alnvlsegms dawaapaarr atsttsgdal
      301 eqakpgtgev velpglaeaa qrlrerarpl pqgkpvlqvs dlsigfegrh rgvdivdgls
      361 fdvrpgevvg lvgesgsgks lsvlavmgll pqgarvrgei rfqdtnllkl nargrralmg
      421 reiamvyqda lsalnpalrv gaqlaqmirr ggtrsaeelm rlvgldpqrt laayphelsg
      481 gqrqrvviam alsrdpklii adepttaldv tvqaqvmkll ldlrerlgfa lilvshdlal
      541 vsdvsdrvvv myggqivetg vtadvmeapa hhyargllgs vlsletgaer ltqirgvvps
      601 padfpkgcrf sdrcpmatei crdtapaleg tdghgyachh pavtvsekel ar
//
LOCUS       WP_457603916            1768 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase/MFS transporter [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603916
VERSION     WP_457603916.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1768)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1768)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1768)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   4  (residues 1 to 1768)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 1768)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 1768)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   7  (residues 1 to 1768)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   8  (residues 1 to 1768)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   9  (residues 1 to 1768)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18492676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1768
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1768
                     /product="non-ribosomal peptide synthetase/MFS
                     transporter"
                     /EC_number="1.14.-.-"
                     /EC_number="6.2.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=189180
     Region          18..1315
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
     Region          1334..1711
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(1344..1345,1348..1349,1352,1384,1439..1440,
                     1442..1444,1447,1467,1470..1471,1474,1549,1552..1553,
                     1556..1558,1582,1586,1640..1641,1645,1649,1665,1668..1669,
                     1672..1673,1676)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtesrhdvtp vddvytvpas yaqeriwfta qlspgqplft mtdavtlpag agpeqalaal
       61 rtvtdrheam rttlrlhdgr lyqdihptvp velpvtdlsa lpgperdaar arivaeyarl
      121 dlpmdaaplw rarllrldpd twwllfaghh vildgtsllh lraeltelca aavagrapdl
      181 pelpiqyady aawerdrldg prwdelrdhw realtglpav halttdrprp atltfdgadv
      241 rrtlpgpvta alpelsqqaa atpfmvqlaa yvallhrlsg sddvvvgmpv agrdraelep
      301 llgmfmnmlv lrvdvsgdpp fltlvrrvrr vvldawdhqd mpfqklveel avrrdpgvpp
      361 lyqltfhhlp tgrgeafgga mddlsleiag delrleyrta lferaameaf adrylllfaa
      421 avaaprtrvs alpvmpdaeh aavvtgwnat aapvrrttla elfdaqarrt pdavalvdgd
      481 trmtyaqlsd aaeqvasrlv ahgvgpesvv aiheprsrrl iagllgihra gaaylpldpd
      541 hppqrlafml adagagvlla delpdgltvp gtvlpltapd rprtaggtaa gpgnaayviy
      601 tsgstgrpkg vvnehaaivn rldwmqdafa lgpddavlhk tpigfdvsvw evfwpllvga
      661 rlvlaapggh rdpaylreli ererittvhf vpsmldafls tagpadparc gslrrivcsg
      721 eelpadlarr avaaipsaal hnlygpteaa idvtawaatp ealtgvtrvp iggpirnvrt
      781 yvldeamrpv pagvagqlhl ggvqvargyl nrpgltaasf vpdpfgepgg rlyatgdlar
      841 wrtdgtlefl griddqvklr glrielgeia avlreqpgvg saavvvrgat paeqrlvayl
      901 tgeapdpael raalkrrlpe ymvpsafvtl dalplsangk ldtaalpaps sgvapaqrrp
      961 pvtpveqtva atwrdvlgvp evgldddffe mgghsllair mlallreayg qvdvgvmdvf
     1021 ahptvqglaa lidapadgdr qrpllyeltr pvpadqrvrs yvcvpygggl asiyqplada
     1081 lpaghtlfsv aipghdvgvr dtelpfdelv ercvteiqer vdgplvlygh cvggalltgi
     1141 arrlhergrp ieaiyaggvf ptarpdnmlg rlvdwadsrg adrryetflr sigaeladld
     1201 qaqvdrfvhh vrreaaeaqe rftewldgep vrvpapvisv vgthdvltey yeeryrewsf
     1261 lgestalvvl deaghyfvkq raealaevlt rthprlaeps aaprqlagng walaatstdp
     1321 vtaetgvqpg vrrflaitas qlisstgsal tqwavpvwvy letgsmlwfg lsgviaylpa
     1381 llalpvagav adrfdrrrvl laacatavta egllalllwt drlglaavyt lvcvlgaasv
     1441 fqritylaai pqvvpkrylg hangiaqlav glsslavpll aagllaaigl agvlvidivs
     1501 yvvaigvlaa vrfpdllgrr rkepflaeli ggarmtwaep gframlgffs lynlclasll
     1561 lvppmvlafg tmgqvgtvaf aealgavlgg laiavwggpt rrrmpaliai afgvavslvl
     1621 sgvrpslllv algsfgvglg lglhngiyls iiqvkvpqrf hgrvlaiiqt ltwatlplgf
     1681 avlvplsgsl lepmfapgga lagsvgalig tgpgrglgfa fvvsglalav valgaygirr
     1741 lrlfdtetpd apadatewlp hlrrvddl
//
LOCUS       WP_457603918            1445 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603918
VERSION     WP_457603918.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1445)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1445)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   3  (residues 1 to 1445)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   4  (residues 1 to 1445)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   5  (residues 1 to 1445)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1445
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1445
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=150248
     Region          6..1374
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1355..1426
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mnetvepiai vglslrvpga asaeefwrnl vvgaesltrf traellargv paeqlddpay
       61 vpvaavldgv drfdaelfgl sprdaeltdp qqrlflehah aaltdagcdp arydgeigvy
      121 aggnadlyqw lnvrrnpral adagelrvsl gnkpdylast vafrlglrgp amtvqtacss
      181 slvavhlaae alrsgecdta laggvcvelp hgvgyvadeg ytsadghcrp fdadadgtvy
      241 gsgvgvvvlk rlsdaladgd diralvigna vnndgsakas ftapsvtgqv evvtqalava
      301 gvaprsvgyv eahgtgtvlg dsielaalst aygrrtaerg wcgvgstkan ighlsaaggv
      361 igliktvlsm rhrlipptvn hdrphpdidv easpfyvvst ltkwepedqr plragvsslg
      421 lggtnahlvl qeapprvppe pdhgggellq vsaatpdala aacarlaerl tgapdvelrd
      481 vaytlregrp ayrhraavva vdrgraaaal tdpkrratgd aaapprvgll lpgqgaqhpa
      541 mgahlaatep vfaaavdeca ailgwdangm ifdagpgade rlagpavaqp alfaveyala
      601 tlwrhwgvtp aamighsvge lvaatvagvf dlpdalrlaa argrlvqaap egrmlavqrg
      661 adeiaallpd gvavaisngp htcvvggape pvaaaevllr ergigctplr spyamhvpll
      721 aavrdefaal vaavprrapd lpvfsaataa pftdeqitdp aywadqlcrp vrfgatvaal
      781 aatgaaddwl llecgpgrql aglarlslpa garaplrtlp apgerltdrq tayeaagrlw
      841 tagvpvrlpa sgtprrvplp gypyqraryw idpepvaapa epatderydd gvvevpawrq
      901 lpdlapveap gplllfaage rgttladrlr ergadvtvvr pgpafavrpd gyrlrpasva
      961 dhqrlldeca ddgraarivh awaldgdpag pdadavaaaq ehgylalltl lealpaadva
     1021 ldvvtagtad vtgsdllrpe hatvagvvrs vplerpglrc hwvdadpaep gadaladell
     1081 gaeraeaval rlggrrwtrg faaaparrrt gpavrdggcy litgglgrig gafaaelarr
     1141 garlvlvgrt arpdlveale ragaqvrhvr advtdvdalr avradieddl ggldgivhaa
     1201 rlpdtglstg srpaeatael lpkvtgtlal ravfgdmpld fvllsssvta ltgglgradd
     1261 taanaylday arsphgwrsp vlsvawgawr eegvpdhdgl apdaavraac rvlaegrtgs
     1321 vaigaytvea vagherrlaa ttaatastvt aadgdlqdtv ariwrdvlgv tevgphddff
     1381 rlggtslvaa qlvlrirqav garlsmrvlf daptvaamaa rieslraapp aeapiprlrr
     1441 pgrpg
//
LOCUS       WP_457603930             499 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603930
VERSION     WP_457603930.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..499
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52750
     Region          6..499
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mstellhdll drtagarpda pavgdgtvef tyrqvradsl rlagwlrgqg vrrgdrvlva
       61 lpadaalpal lyavaragav fvvlrtpape valahvldda epglvltddp vlaglsrarg
      121 vpvrgavear raasgvaigg apagpaplav dpvcliytsg stgmpkavvs thaqvtfavr
      181 aiqselryrp ddvvhvllpp sfdyglyqif lstvagarlr lgdpgdtggr llatlvesga
      241 tvlpcvpsla inllrllgra gaprpplrll tntgaamppe vlaglrrllp glsvqlmfgl
      301 teckrtaimp pdadlrrpga cgralpgtei ftvdaegrrq ppgvrgelvv rgphvmagyw
      361 rrpeltaqrf rrahglfpql htgdhghvda dgyvhfagrr ddvykekgtr vsateveaaa
      421 yrvdgvdaag vlppadgrdg atlfvvaelt padvlrrlre qleemkvpar cvvlpdlplt
      481 gngkvdrral arlagehrg
//
LOCUS       WP_457603944             157 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603944
VERSION     WP_457603944.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..157
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17200
     Region          24..157
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mgrrgdaggr gggdpaggvm tgwyvyrhvv tldetnmvgn vyfahflhwq ghcrerflad
       61 hapavldqlr rgeltlvtvs camdyyeecf gleeievrms adgreghrls mhfeflragr
      121 evargrqtva clrptpagpv pvdppvdlra alaafta
//
LOCUS       WP_457603962             463 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603962
VERSION     WP_457603962.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..463
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50538
     Region          <175..>290
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          366..456
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mavalaaltv laglpgaara glpsqrlvwt ecaddlpdvp pdprvrcarl rlpvdwarpn
       61 gpafdlavar rfarlpeqrv gtlvfgpggp gdsgverirr gdrfsdelld rfdlvsfdpr
      121 tvartaapvc tpdpalrrpp vplagqadfd aavaynralw srcrptspvf dhadtlsttr
      181 dldalrralg errlsfhgss ygtllgqqya erypghvrav vlegvfdhsl dvrsfvrtqa
      241 aalqdafdef vswcdrsadc vlherdvrsv warvlaradr geyaprtafd vtavalgmla
      301 gprwpqlaai vrdmdagtpp pevnlsisva afcadwpaev rdyaeyvglv rearaaapdv
      361 rygagllavq tclgrpspvr npphelnvht rtpllllnar hdprtgyawa vnvarqlgrh
      421 grlvtyegwg hgtyqrndct tavvdrylvd ltvpapgtrc pas
//
LOCUS       WP_457603966             338 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603966
VERSION     WP_457603966.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..338
                     /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=35219
     Region          97..338
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mviglyalla gaavgalgvg alrlvrhrsi lahiavllav tiasvtagvt avaqamflsa
       61 hdlqvvlvtv aasaalslav gvafarrlaq aavwadqarq rerqleagrr elvawvshdl
      121 rtplaglram aealedrvvd epaavaeyhr rirvetdrmt rlvddlfels ritagalrpa
      181 lspvplgdvv sdaiaatapl aadrrvrvla petgwptvra aeaelarvvt nllinsvryt
      241 ppdgtvrida grddadawla vsdtcggipe adlprvfdva frgtrartpa pagadeaapa
      301 ggglglaivr glveahggrv hahnvtggcr fvvrlpaa
//
LOCUS       WP_457603934             487 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiD family decarboxylase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603934
VERSION     WP_457603934.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Mondal,A., Roy,P., Carrannanto,J., Datar,P.M., DiRocco,D.J.,
            Hunter,K. and Marsh,E.N.G.
  TITLE     Surveying the scope of aromatic decarboxylations catalyzed by
            prenylated-flavin dependent enzymes
  JOURNAL   Faraday Discuss 252 (0), 208-222 (2024)
   PUBMED   38837123
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Marshall,S.A., Payne,K.A.P., Fisher,K., Titchiner,G.R., Levy,C.,
            Hay,S. and Leys,D.
  TITLE     UbiD domain dynamics underpins aromatic decarboxylation
  JOURNAL   Nat Commun 12 (1), 5065 (2021)
   PUBMED   34417452
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Marshall,S.A., Payne,K.A.P. and Leys,D.
  TITLE     The UbiX-UbiD system: The biosynthesis and use of prenylated flavin
            (prFMN)
  JOURNAL   Arch Biochem Biophys 632, 209-221 (2017)
   PUBMED   28754323
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Jacewicz,A., Izumi,A., Brunner,K., Schnell,R. and Schneider,G.
  TITLE     Structural insights into the UbiD protein family from the crystal
            structure of PA0254 from Pseudomonas aeruginosa
  JOURNAL   PLoS One 8 (5), e63161 (2013)
   PUBMED   23671667
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..487
                     /product="UbiD family decarboxylase"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51977
     Region          9..487
                     /region_name="UbiD"
                     /note="3-polyprenyl-4-hydroxybenzoate decarboxylase
                     [Coenzyme transport and metabolism]; COG0043"
                     /db_xref="CDD:439813"
ORIGIN      
        1 mtggrapvdl rhalatldpl pgelvrvaee lparygvsah yarwagapaa pptgpgpavl
       61 fdrvrpahgp travlmglyg trrraagllg vtpaelphrl ldavaaprpp vpatdparwp
      121 rhrlpldlta lpvpvftded agpyltlgav latdpdtgvr nlsvhrmcvq gpdtltiwmv
      181 pgrdlelahq aalrrgaalp vaihlglgpa vllssccpts lvppdldela vagalagrpv
      241 ellpcttvda efvahaeyvi egellaehap esrhgavatp eflgyqgrah pslplirvta
      301 itarespilq avsgpgheqs vllgfgmeaa vldllrrrgt palaahchta gggqlmvvlq
      361 wpakrgpadd davrdaaeav ldgfrmaklv lcvdedvdme sdqdlwwamv trfqadqdlr
      421 vladregfpl dpsqhtgysr slsadgrtak avfdctvpya qrdrfrrprf tepslpvprr
      481 paaplpr
//
LOCUS       WP_457603972             391 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603972
VERSION     WP_457603972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=41366
     Region          52..294
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mhlyltalnp tdavlegflp aanalglpat vltdrpaewp advpvrhcav rdpaaivaat
       61 taespaalls nsdhlqeata vaagklglpg kdpeaarrck dkaamrrala aagldpvrai
      121 tldpgatpav padlfpavlk prggvaseda ylvtdrrela aqvtairrrr pevvliveey
      181 lagelrtydt lgdsgsltvl ggwrtglgap ptftevsldw appppahdar lralldalgv
      241 gfgachteyv vrpygirlie vndrligdrm dliltgllgv plfahvirlh lgeplaaldl
      301 pdpaalnrya rveyvcadqs grltaapgpv dtvhdgvrls crpmrevgrv aertgtnrdy
      361 laalhgigpd pdtvraalta frddlswtit g
//
LOCUS       WP_457603974             530 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603974
VERSION     WP_457603974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..530
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57095
     Region          7..526
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtstglrpra awhthpadla aahavfgcla revatpadvt itgdvvqvwl pstgvtlrct
       61 aarlspvgth rytgpvrhrp dggpwrdlda eglaslvaae ltartghnnp effdqvrasr
      121 dtvahllagr paadptptsd paidayvase qslvlghphh ptpkwrsgdp dewqayapel
      181 rtefrlhwla vpddlvaeag pvdpmlaale pprppaghrv lpvhpwqvtl vppthprvrr
      241 lglagapvrp tasvrtlysp dadlfvktsl hvritnclrk naryeltaav altrllagip
      301 lsdgvamlae payrtidaag adeaygtilr tglrahlrpq qtavlaaala aaplsaadpv
      361 awwrryvgll vpavldawlr hgvvhephlq nvlvvrdadg cpvrmllrdl egvkldisrw
      421 tswppglprq vgydalqarq rvvyclfvnh lagisgalad arpgiepalw revrdvvaav
      481 aadlgeppel rallageplv akanllvrwr rdadraapfv pvpnplggra
//
LOCUS       WP_457603979             240 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603979
VERSION     WP_457603979.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..240
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26439
     Region          30..240
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mvhkvltpre gaehmcaemr khfgvdfdph elpdgeflsl drlsltshtg thvdapshyg
       61 srttygdgtp rhidsmpldw ffrpgmvldl tdagtgvidv ariekefarv grrpdpmdiv
      121 llhtgadara gtpeyftrfa gldgpatrll ldlgvrvigt dafsldapfg diidryrrtg
      181 drsvlwpahv vgrereycqi erlanlgelp tpygfrvacf piriagagag wtravalidd
//
LOCUS       WP_457603981             423 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457603981
VERSION     WP_457603981.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 423)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..423
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=44662
     Region          4..417
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 msqrrvvitg igvvapgglg akafweriva gtpmtrlita fdstgfrsri aaecdfdpfq
       61 ygfsehdigr ldraalfalt atreamsdsg lvvdrddahr vgvslgtavg atlrleeryr
      121 avshegrdwl vdhrlagpdl ydyfvpssma aevawaagae gpnavvsagc tsgidavgha
      181 wdlirdgsvd mmiagatdap iapitvacfd aikatsntnd dpgtaarpfd rtrngfvlge
      241 gsavlvleel qsarrrdahi yaeirgyasr gnafhmtglr pdgqemaaai raaldtarip
      301 atavdyvnah gtatrqndrh etealkrglg mhaydvpiss ikpvighslg avgaievaas
      361 amaiefdvvp ptanlhhpda eldldyvpre arqrklstvl tvgsgfggfq samvlaapea
      421 vaa
//
LOCUS       WP_457603983             414 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603983
VERSION     WP_457603983.1
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   Manikandan,P. and Nagini,S.
  TITLE     Cytochrome P450 Structure, Function and Clinical Significance: A
            Review
  JOURNAL   Curr Drug Targets 19 (1), 38-54 (2018)
   PUBMED   28124606
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Guengerich,F.P., Waterman,M.R. and Egli,M.
  TITLE     Recent Structural Insights into Cytochrome P450 Function
  JOURNAL   Trends Pharmacol Sci 37 (8), 625-640 (2016)
   PUBMED   27267697
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Pochapsky,T.C., Kazanis,S. and Dang,M.
  TITLE     Conformational plasticity and structure/function relationships in
            cytochromes P450
  JOURNAL   Antioxid Redox Signal 13 (8), 1273-1296 (2010)
   PUBMED   20446763
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   5  (residues 1 to 414)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Degtyarenko,K.N. and Archakov,A.I.
  TITLE     Molecular evolution of P450 superfamily and P450-containing
            monooxygenase systems
  JOURNAL   FEBS Lett 332 (1-2), 1-8 (1993)
   PUBMED   8405421
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Nelson,D.R., Kamataki,T., Waxman,D.J., Guengerich,F.P.,
            Estabrook,R.W., Feyereisen,R., Gonzalez,F.J., Coon,M.J.,
            Gunsalus,I.C., Gotoh,O. et al.
  TITLE     The P450 superfamily: update on new sequences, gene mapping,
            accession numbers, early trivial names of enzymes, and nomenclature
  JOURNAL   DNA Cell Biol 12 (1), 1-51 (1993)
   PUBMED   7678494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10800858
            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="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=43655
     Region          10..412
                     /region_name="P450_rel_GT_act"
                     /note="P450-derived glycosyltranferase activator;
                     TIGR04515"
                     /db_xref="CDD:275308"
     Site            order(117,121,128,170,250..251,254..255,258..259,262,295,
                     304,306,329,361..363,366..367,370..371)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410651"
     Site            order(191..192,250,253..254,258,302..305)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410651"
ORIGIN      
        1 mtatstddal gstlmtlrgf qwvygarqdp yalllraesd dphelgrrvr angaltwssa
       61 eawvtathal avrllrderl glrkppptds apswamptld dvlplddvgl rldrtdcerf
      121 grsvaaalaa prlkkahtei tvridrlaag lngtfdltsd yavpvatmat svllgvpaah
      181 qeefarlcag aataldatlc pprldtarll ldsiaglrel lvslptgagd dllgeltrte
      241 pdsvlpvall hcavgadlta tliantmcal laepgrwtav atepglaaaa vretlrfapp
      301 vrlqrlvart dldldgtait agsevvvlle aanrdpaafa dpdhfdpgre paaeilwahp
      361 ampagvvaet vrrhatvavs alaahlptlr aagegyrrlr spvtgsplsr pvva
//
LOCUS       WP_457603985             533 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603985
VERSION     WP_457603985.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..533
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=57403
     Region          58..526
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtpltrrrll ggsivaggsa lvggigapgg aaaagcapef gavsvgrddp ryqeltirga
       61 nrrftgtpds vrlvntpaqv veavrdarrt garlavrsgg hcfedfvdsp evrlvidvse
      121 mrgisydpvh raisvqsgat lgqlyrtlyl awgvtlpagv cpsvgigghl agggygtlal
      181 rhglaadhly gvevvvvdas grvrtvvatr apndpnrdlw wahtgggggn fgvvtryllr
      241 spgatgasaa allprppatl lhaavnwnws dineqiflrl vhnfcrwhee hggdgttdtg
      301 idagiflyhk ingqiqlgvn vdgtrpdada lltgylaals dglgitntee rsvtpwlkat
      361 lsmppagdys fkakdaflrt gwtgeqlstl yrylsegsye fygsnafigy fggkvntvda
      421 astamahrda rfasviqsvw ftpeqetkll twarecyrdv yastggvpvp geaysgtyin
      481 ypdvdiadpa wnrsgvpwha fyyrdnyprl qrvkrtydpl dvfhhglsvr twe
//
LOCUS       WP_457603988             328 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603988
VERSION     WP_457603988.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35197
     Region          1..244
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgvlgcadia irrlmptiag ldgvevvava srsrskaeqv agqfgcaavt gyrdllkrdd
       61 veavyiplpp rlhyewvaea lqagkhvlae kplctthvet velmavarer grvlaenfmf
      121 lhhsqhdavr amvaanaigr lqvfsssfgv ppldragfry qpalgggall dvgvyplraa
      181 qlflpelevl aatlrydett gvdvagsall aapdgvavql afgfdhsyrc eyalwgstgr
      241 iavdraftpp dqlkppvrve rqdqatelam padpqvrnav rafvqavrsg vdgpieerat
      301 lrqaqlveav rdvarvtgsp armlraag
//
LOCUS       WP_457603989             204 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457603989
VERSION     WP_457603989.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..204
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21379
     Region          13..178
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mpgplhrsnh papqvvligg slcassrtgr lavwcagrca eegavvtclr gadlelpfyr
       61 phrgdgpqrv privaalara dgvvllspty hgtvsgllkn aldyandlad arepflsdrp
      121 igcvaissge qgahstlatl rtiahalrgw ptplglalsg eraeldttga padprtraal
      181 eilldqvlva arrrvrptva garr
//
LOCUS       WP_457603990             250 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603990
VERSION     WP_457603990.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 250)
  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   3  (residues 1 to 250)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..250
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27139
     Region          1..>147
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mttsvpaagm ygeeqaevye lvhrargkdy deeaafvaeq arellpgaat lldvacgtga
       61 hlrafarlfd rveglelspa mveaartntp gavvhhgdmr sfhlgerydv itcmfgsvgy
      121 ltdveelnaa lrrfaahlsp ggvvaidpww fpdtyldgyv saslveadgt tvvrvshskr
      181 dgdasrmevh yivarpaggv hhfveqhrit lfprdtyeka frgaglsvry legsqsgrgl
      241 fvgcaghqed
//
LOCUS       WP_457603992             410 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603992
VERSION     WP_457603992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..410
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44277
     Region          6..369
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mlapvskegq afldllavhi pyvrevsgah drdgtfpfev fdrfrtsgvl aatvpaelgg
       61 lgvshmhdva lalrtlaefd asvalalhmq lsrgltltye wrygapeaqs laerlmrsig
      121 ereaiicgav kdaprattrl tpapgggwll ngrktlvsla paathfavya evhvdeeplr
      181 laapvltrqt pgltvldnwd glgmrgsgtv divfdncpia aedvlpratv garqdavlag
      241 qtvssvtmlg iyagiasaar nvavdwtvrr rvdpgaavrt llaeiearlf alrssaaaal
      301 rnadelafdf svdadergrr mmtpfqcakl mvnqlasdiv drcmtvvgga sfsarhplar
      361 hyrdvragry mqpytyvdai dylsgqvlcf dqdndyvsar airarrepsp
//
LOCUS       WP_457603994             592 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603994
VERSION     WP_457603994.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 592)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 592)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 592)
  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 592)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..592
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63606
     Region          1..586
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 matlraalrl gcadrralaa tvalvvigaa ppigvawftk llfdevgrgr sadpstatwy
       61 avaiavlgal aaiasrvsgy fttalqnait iaadvrlyrk lntfvglgpf eqpalrdrla
      121 laqqaatqap yvvvmfavdv aqnvvtiggf aviltslwpp agllllavav pdfliqlrls
      181 rrtaravees aslfrarflf qtvltdlraa revrlyhlgr ffhdrligav rsaagielaa
      241 arhtttvqac walagaavtl tatvfavnat vrgrlslgdl tlllaaftaa hsglagiaaq
      301 lgeagaamrl frhyvavlds ptdlvdgtlp applrtairf edvwfryded gpwvlrgvdl
      361 titagqavgl vglngagkst lvkllcrfyd pdrgritwdg vdlrelriet vrrrmgavfq
      421 dfmcydltae envgigrlph tteqvveaaa haeihdrlra lphgyatlls rtfagqdgep
      481 gvtlsggqwq rvalarslmr adadllilde pssgldadae trvhasltqi rhgrtgllis
      541 hrlstlrdar rivvldagrv vesgthdelm aadgeyarlf rlqadgyqla at
//
LOCUS       WP_457603996             513 aa            linear   BCT 27-JAN-2026
DEFINITION  copper resistance CopC/CopD family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457603996
VERSION     WP_457603996.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   van Sorge,N.M., Bonsor,D.A., Deng,L., Lindahl,E., Schmitt,V.,
            Lyndin,M., Schmidt,A., Nilsson,O.R., Brizuela,J., Boero,E.,
            Sundberg,E.J., van Strijp,J.A.G., Doran,K.S., Singer,B.B.,
            Lindahl,G. and McCarthy,A.J.
  TITLE     Bacterial protein domains with a novel Ig-like fold target human
            CEACAM receptors
  JOURNAL   EMBO J 40 (7), e106103 (2021)
   PUBMED   33522633
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Lawton,T.J., Kenney,G.E., Hurley,J.D. and Rosenzweig,A.C.
  TITLE     The CopC Family: Structural and Bioinformatic Insights into a
            Diverse Group of Periplasmic Copper Binding Proteins
  JOURNAL   Biochemistry 55 (15), 2278-2290 (2016)
   PUBMED   27010565
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Cooksey,D.A.
  TITLE     Molecular mechanisms of copper resistance and accumulation in
            bacteria
  JOURNAL   FEMS Microbiol Rev 14 (4), 381-386 (1994)
   PUBMED   7917425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17591615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..513
                     /product="copper resistance CopC/CopD family protein"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0046688 - response to copper ion [Evidence
                     IEA]"
                     /calculated_mol_wt=51302
     Region          6..128
                     /region_name="CopC"
                     /note="Copper-binding protein CopC (methionine-rich)
                     [Inorganic ion transport and metabolism]; COG2372"
                     /db_xref="CDD:441939"
     Region          330..>510
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; cl42370"
                     /db_xref="CDD:478162"
ORIGIN      
        1 mrgvarwvll vwlawcpalf vvfgfaspaa ahfklvkavp adgarvsgav gevrltfsap
       61 gtptgagfrl srdgeavavt shtpdggrtw lvhpaapltg gefalrwsva apdahpltgd
      121 vaftvvpsaa apgatatprp tagspghagh gvpglpsasp sahagghavg htadaeqgav
      181 rfvgvagrwl sygaillgvg glvfalttlv gtrrdiqlvq vwvraagltv aagavlelaa
      241 laavfsadgg lasaagtqal talsrtpvaa glglrlagaa gllvagslea alirgrhavg
      301 rhaaatvagi ptdpqplvvp tvgeapddda hrvraravrp vllgvtvall vgsflldght
      361 vtarprmivv aadvahtlaa avwvggvlll aalllgrarl gaptgaaema vrfsvpataa
      421 vtltgvagva ltvaildrpg hlvstswgrv llvkvalvav vaviglynsr rvvprlddpv
      481 pggtrrlrrt vlveavlmva vllvtailvn agt
//
LOCUS       WP_457603999             432 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457603999
VERSION     WP_457603999.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..432
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44374
     Region          32..353
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mttaphhtgs hhssrpatew aaaralahrl paplpaesvp lasaagrtla aplvaavplp
       61 gfdnsamdgy avrgpgpwrv vgqilagrth avaplvegta vevatgapvp gradrvvpye
      121 iadrigdvlr avpgdrrhir cageyaargq elvpagspvt pavlglaasv gldhltvrar
      181 prarllisgd evvhagrppw grvrdaigpm lapllsawga dllgprmvgd qpdwfaeaia
      241 dstrdadvtv vcgassvgpa dglhaslrhl gavahvdgvr crpghpqvla qagarwivgl
      301 pgnpyaalvs tltlidpllt glagrppadl dtavlttdpl rlderntriv pvrrgapglr
      361 lvdgahpgyl gaaadadala vvppgwrpgt pvglltlpwq vgrppgpglp alpgwvgsse
      421 artgeadrri pl
//
LOCUS       WP_457604000             317 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604000
VERSION     WP_457604000.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..317
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33287
     Region          4..314
                     /region_name="MDR1"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08267"
                     /db_xref="CDD:176228"
     Site            order(40..42,45,130,134,152..155,157..158,176..177,180,
                     195,212..213,234..235,262..264)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176228"
ORIGIN      
        1 mkaivydryg spdvlriedv skpsptgrqv lvkiaatsvn lsdwetlrgs plysrigglr
       61 sparrtlgsd iagrvdavgp avtrfrpgda vygdnlmlkg gfaeyaiape svlahkpaal
      121 tyaeasaipq agviawqgtq gaaagkrvli ngagggsgsf aiqvakrfga evtgvdnagk
      181 ldfmrsvgad evidyrsqdf trsgpydlil dlvahrsvfd yrralapggr yrcvggsvpa
      241 llrvltigaa agrlthrrlg vlavkegpth fepvadlcat gdltihidrt ftldevpeal
      301 ahvgegralg kvivtvv
//
LOCUS       WP_457604003             567 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604003
VERSION     WP_457604003.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 567)
  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 567)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..567
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=61407
     Region          267..305
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          311..339
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(312,315..316,319..320,322,346,349..350,353..354,
                     356..357,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          317..567
                     /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          344..374
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          379..407
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          447..475
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(448,451..452,455..456,458,482,485..486,489..490,
                     492..493,515,518..519,522..523,526)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          480..510
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          514..542
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtdgaerydc hrdhgpyagv saflgrvaad rprlaarhav elhaiapqld paarpaaeee
       61 pirfhparrt aclaygaael vaawagtlrr pvtvrfdhva gadettaell dalarrlgpa
      121 pvrldlrddg apdpapgert pqalrralgd slargyyhha arvarrgraa vapdgdlrhw
      181 wafttglata laalnraaea ldlydearav tddpkitmsa ayatamlhar hlpaadqdpa
      241 larhwleval rlaaeladpr rrllstvfye qglalldsra grpdralrlv ddgltrltaa
      301 lgpgerpqdl arlrhnraqv hlalgdpara ladldtviah dpdnceyyvd raalhraagr
      361 traairdyda airlgphlpe ayynravlqq ergrperara dlervlaiep ghldarialv
      421 nlhvergald aaeagaragl agapqepall ctlglvlaer grpaeadell tralsgdpel
      481 veawtnraaa rfergdvaaa ladldraval seapvprynr gtalarlgrw deaardfaqa
      541 laqpgldral rrdlraeltr crralav
//
LOCUS       WP_457604008             346 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604008
VERSION     WP_457604008.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34271
     Region          1..199
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          114..344
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mgtvivlitl lvgllsglta glgrqnvsai tglpadriaf qtpgegqgvs ysnstvtekq
       61 wqqwaeapgv tgaeplgiat tratagnrsa gvsafgvrpg shlapgsgri dgrsavlstr
      121 aaddlgvkag dsvtlagqrl tvaavrgdas fshtpvvwis ldvwqkiapp tgtgggspaa
      181 tvvaltttsg adlvatdrqa gtktvsvdds lsaigsytse ngslqlmrgf lfaisalvig
      241 afftvwtiqr sgdvavlkal gastatllkd aigqavvlla ggtllgtgia aalgalvags
      301 avpfvltpvt vllpaavmvv lgalgaalai rritsvdplt algsar
//
LOCUS       WP_457604009             227 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604009
VERSION     WP_457604009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23981
     Region          3..221
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mslnltditl typdgegrlt aldrvtldvp kgsltavigp sgsgksslla vaatlitpdt
       61 gtvtvdgtpt tglvraelad lrrrkigivf qqpnllpslt aaeqlqvmaq idgrpparar
      121 travelldav glagqadrrp hqlsggqrqr vniaralmnn ptvllvdept saldhergaa
      181 vidlitrlth qqatatvlvt hdrthltavd qiaevhdgrl hvpapar
//
LOCUS       WP_457604012             547 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604012
VERSION     WP_457604012.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (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   4  (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   5  (residues 1 to 547)
  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   6  (residues 1 to 547)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (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   8  (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 10194399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..547
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60649
     Region          56..541
                     /region_name="PBP2_AlgQ_like_4"
                     /note="Periplasmic-binding component of alginate-specific
                     ABC uptake system-like; contains the type 2 periplasmic
                     binding fold; cd13583"
                     /db_xref="CDD:270301"
     Site            order(174,183,236,318,442,446..447)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270301"
     Site            order(190,193..196)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270301"
ORIGIN      
        1 maqlsrrqvl lasgaaavaa lagcgddtpd kkdldrnrtg amekygigdq fkatepvtfs
       61 ilynnhpnyp lkpewlfwae larrtnvkld pvavplsdye qkrsvlvgsg dapliipkty
      121 hpqessyvss gailpvsdyl dlmphfkdkv erwglqpemd tlrqedgkfy llpglhekpw
      181 qdytlavrtd vleqlkipsp ttwdevyaml kamkaahpdv ipfsdrfgkp npagnllnml
      241 alahglpgag wnyqptswda gagkyvftga sdgyrqvvay lhklvaegll dpetftqtdd
      301 qarqklasgk sfvistnaqt lvndyrpdia kinpnarlgk ilfpvgpagp vnaasrleng
      361 vmisskareg knfvammqfv dwlwysdagq efakwgvegt tytkdasgkr alapdvnvig
      421 lnpkgskhlq kdfgfyngvf ayggkldlvq sffspeelef qkemnarkpa pwvtpppapl
      481 sdeereqttl watalkdhvt qntlkfalgq rplsewdayv selkgknaqa ytdlvnkaye
      541 ryrkshg
//
LOCUS       WP_457604013             301 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604013
VERSION     WP_457604013.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..301
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32924
     Region          6..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 maghsdlgrf lrqcradltp eaagiaavaq grrvrglrre evallagvsv dyytrleqgr
       61 htspsaavvd alarvfrlda aarahladla rparrssrqm paqrvrpamh qllasmtehp
      121 alilgrrtdv lasnalgral ltdwtllppr hrnyirwvfl dpgardafld wpavaadvvg
      181 tlrlyagrnp ddpqlselvg elsikspefr awwngrhvhe rthgtkrmhh pavgpitlry
      241 ealvlpgdpd qtlflyttdp gspsydnlrl lgslaaraap apgrasstpl pdasrtepnp
      301 s
//
LOCUS       WP_457604015             494 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604015
VERSION     WP_457604015.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52468
     Region          10..492
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msvptsavvv pdllrhrtgl mpeqeaisvr gktaityrdw drrsnavara vldrlggtgr
       61 garvallfgg ddwidyavay lgvlkagata vhvndtmpav elrrrfdqca vagvirgaal
      121 ppwrddagrw svvvadldqg dsaavdtgvt pedisdilyt sgttgpakpf tnphgnltyg
      181 rgsaalgqlv dpapllapmp lgttssattv avlatttpsp livcspddpe eiarllathg
      241 catliltpwt airlaairpq drydlgsvkt ignasaimpp riardllaam pnatianaya
      301 qseavpaiil gnvdpdrpmw lgrpgrgtem rvvdpqgepl ppgelgevwl rceapkrlyl
      361 dqalnarvha ggwtrtrdlg ratadgelfl fdrmtdvitt dgklvsslev eaalydhpsv
      421 reatvvalpd pehgeivaav vaadpaldda tlaaflaerl ephqvparih rldalprggt
      481 gkvlkyqlrq rfgg
//
LOCUS       WP_457604020             624 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604020
VERSION     WP_457604020.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10347689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..624
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=65803
     Region          19..526
                     /region_name="AFD_class_I"
                     /note="Adenylate forming domain, Class I superfamily;
                     cl17068"
                     /db_xref="CDD:473059"
     Site            order(178,181..186,188..189)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(181,297..298,322..327,413,424,427,438,520)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(181,221..222,271,273..274,277,297..298,322..327,413,
                     424,427,435..438,501)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(221,273..274,277,297,435..437,496,501)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Region          550..604
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mpvtdclhti fsrraaeqph riavtcgdhr lsyseldrls gelaerlrgy gvgpgvhvgv
       61 cvdrsvdlvv cvlavvkagg ayvpvdaehp aarvaavlag srvpvtvavt rtadslaews
      121 gpvlwaddse ddddtddedg egtaaeaaag agpadravga davrepagea gpddpayvih
      181 tsgstgapkg vevshrsvva llehgaerfg fggddtwtlf hsigfdfsvw elwgallsgg
      241 rlvvvpgrva rtpalmldlv rreqvtvlnq tpsafrqlaa ayladegpdd lrlvvfgger
      301 ldvamlapwi arrgddrpel vnmygitevt vhaterriva adldrpsvsp igrplpgvri
      361 elrdetgapv pdgtpgelyv agaglargyl hqpeltaerf aesggerwyr sgdravrtdg
      421 dlvylgrvdr qlkvrgyrie pgeveaavla hpgvgtalvt aqdfgdgdvr lvayvapppg
      481 adpsaltead lavtvadlpg ylrpsrfhvv adipltvqgk advavldrla epaeqaeqae
      541 qagddavsgv kaiadevlrr dvpvdgdlfd lgatslaltr ivamvndrfg ialtgaemee
      601 ptvgclaevv dasrrhhslq qvgg
//
LOCUS       WP_457604023             512 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604023
VERSION     WP_457604023.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..512
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55060
     Region          5..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mhrtlydvlt ttvdshpdkl aliagphrlt yrdlaarvag lagrlqadgv rpgdrvvica
       61 gnrvetvtaf waalaaggva vvvgheqrpe rvrhvladca atvllalepm arsltglglp
      121 asvravlpvg aedtrfagtp apvdvisedl aalvytsgst gdakgvmlsh anmltaldsl
      181 neylrngped vflcalplaf dyglyqmima fsqgatlvle rdmslplqvv kdiaryrctv
      241 vpgvpvlfel veqfsrfgmp dvssvrcltn tgaallprhi aairrlfpga diysmygvte
      301 ckrctylppe lldakpgsvg qaipntqilv vdeqdrpcpp yqvgqlvvrg gtvmqgywgl
      361 pdetarkire hpvrggrcly tgdygylded ghfffkgrid evikvrgrkl iprdveevlr
      421 svpgvaeasv vctalddgdh diaafvaadp aavdasalra acrsgletwq rptryevlat
      481 lprnsngkvd kpellrrypv ptaalapaga pc
//
LOCUS       WP_457604029             507 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604029
VERSION     WP_457604029.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 507)
  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 507)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1017701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..507
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=56320
     Region          <203..504
                     /region_name="PRK06922"
                     /note="class I SAM-dependent methyltransferase"
                     /db_xref="CDD:180751"
ORIGIN      
        1 mtdlptrfvl fpgrhhlltr fqadylrrla gdeatvvwav tsanhentrr npvayhrrea
       61 aierfsvlsg lrslavpifd taytdafaev tlksiavatg leltpadtvv acstpevakl
      121 yerlgfgial veadpdlpgt perpwdvllr laagdeswrt lthpatidvf eryrlveair
      181 svvndplvgd eggltvtrdy rtyveafasa aqrkwdsvrr yvtpgrivdi gcgagavlel
      241 adreaalres dligvevarh lyqeclhkka qgvfrnanvy ffhrnvlgga vfkdrsvdtt
      301 ltfaltheiw sygrqresll qfarrihdht vpggvwlnsd vcgpdepdrp vilrlttddg
      361 anpasprrdl adltsaevrr yvsglstrar ldqfavdfaf gfayepladg avrlglgaam
      421 dyltrkdytd nwlsetreqf cglsfadwte llteagfeig pasapvrndw vidnriapva
      481 sltdldgrpl dwptthvltv ahrprna
//
LOCUS       WP_457604030             347 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604030
VERSION     WP_457604030.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..347
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35494
     Region          5..341
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgeprvlvvg agvsgvllar rlrdagadav ligphgggaa grpadataas gglvrafepd
       61 paarslaaas laelladpsl ataagwrrtg slylldaraa agvdgaeilt raevadrfgf
      121 aglpdgtvgv werragyldp drlrrtvlrg lgrtettpva rlddrvvelr dgrrltgdlv
      181 vvaagawtpr llgaaglpts lrtkhiqyah hvtgraelpc fvdetsglyg rpagpgrmll
      241 glpsdrwdvd ppspepdaal aarvltvaar rlpgldprpa gppvsatdcy sepaglalrh
      301 vagavhtftg gsggaaktvl aasrlaatal lntrtaipvp hgqtead
//
LOCUS       WP_457604031             224 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604031
VERSION     WP_457604031.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..224
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24225
     Region          26..148
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mtdtdgrlsa tprttlrrmk ekghrdraal fdvlraafvc hlgvlvdgdp mvvptvygfd
       61 drhlylhgsv asrslttdae vcvtvtvvdg lvlarsvfeh ginyrsamvy grprwvtdae
      121 ekvyglrllt ehvapgqwdh arrpnrrela atallalpla easvktrsgp pddgdgpdaa
      181 lglwagelpl varwqqpvtd palppttpvp ahvaardgtr adqg
//
LOCUS       WP_457604033             435 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604033
VERSION     WP_457604033.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..435
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45200
     Region          57..>242
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mdtitnaphp lrstvrgrvl lpgdegfdva grawnlavaq spaavveaad addvaalvry
       61 arpaglsiav qpnghgatgr adgaillrtg rldtveidpa arrarvgagv psgrlqaaaa
      121 pygltglpgs spvvsvtgva lggglswfgr aygwvsdavt afdvvdaear hrrvtaetdp
      181 dlfwalrggg gdfaivtale lalhpapely ggrmmwaaah apdvlrafrr itatapeelt
      241 vwmdllhlpg adpmvaldvt ylgdgtgard llapldrlpa pisdsrrimp vtelggitae
      301 ptapspgisr aelltrlddd aagalladpi apllsvqlrh lggalarysd sphgpltepy
      361 alylfgvatd paavtarqra laaalpvsgr kpvtflnpde tvadaftpav ltrlravkrr
      421 hdpdglvrsn fpvag
//
LOCUS       WP_457604034             382 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604034
VERSION     WP_457604034.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=39398
     Region          24..62
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          82..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 msdkaptspv srersreikr lsvilaarqa rrlsrvdlae mtglsaatvt alvrelvaeg
       61 yliergpgap ttgrpremle fnpraelvaa vsleplrisc eiadsegavi ahrvarlgan
      121 vvetvcefvl dlvgdnlpsl rgvaiavpgv ssngavrlap svglveawpi gesvqrrlgv
      181 pvvvdndvnl maagecvaga gadvanllli hvadgigagl vldgkvrrga sgaagevgfl
      241 plggaterry sgvgefearw svnaiaervv alnpgrrpes pvrelsglaa tsapareyld
      301 evlgawagli lscacvvdpg lvllsgaaae lddaaldqlq tlvsartpap tevrratlgd
      361 qavlhgaisy alsaavprps lp
//
LOCUS       WP_457604035             286 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604035
VERSION     WP_457604035.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..286
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29482
     Region          1..267
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 maavarsyly vpgdradlld kaagrgadal vldledavtp arkaqaretv agylgaaaaa
       61 gpelwvrins dqveadvevl spaaagvwvp kaepdllaev daaltrvqrr lgpdapafrv
      121 valietargv ltaprvaaaa rvlrlglgea dlagelglqp gperaefapi rsqvvvasaa
      181 agitppvgpv ettlrdperl eqttrallrq gfrarsaihp gqiatvnevf tpteaevasa
      241 ravlealera erggsgvatd aggrlldrav vraaaevvrr aeasag
//
LOCUS       WP_457604040             924 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604040
VERSION     WP_457604040.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 924)
  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 924)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Rosinski,J.A. 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 924)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..924
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=97715
     Region          <4..887
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          861..917
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mgsgpapaga vgtatdtggd allgradecr rlgalladav dghggalvvr gaagvgktal
       61 lehcaarstg mrvlratgap feaelpfsal hqlarpllhr lgdlpaqqad alrtvfaigg
      121 gsrpvnrlaa yvatlslltt aaedtpvlcl vddahwidpa saeallftar rlladrvavv
      181 faardapafp apglpelplt glprddairl amragldprv aadlaaatag nplaltelpa
      241 tlseehrngw lplreplvlv eriemtvlah arglpddtwr alvacavtea stpalleril
      301 aadglrlgvl dpavdaglir vtdrevtfrh pltraavhsv agpgrrraah lavaaaltgd
      361 dtadrrawhl aaattvpdeg vaalladsae raqrrggvva earayersar ltpdpdvras
      421 rlaaasrawa nagasrhait lgeeaigltr radlrcrvkp llahlaqqhc dtagaeayla
      481 daqayaqadp lgaarlmsar vnqfwarldv tgmvplcarv aelaaadaga twpkgpirla
      541 aaqvlaglpe gvasaralvt acaghadgsa aelaevfcwi gdhdtarall epeidrarat
      601 ddvfllayal prlaglewrt grlhaayqaa aeavriaeqv alpvlraeal avlalveall
      661 geepealanv edarrllpge freievrlry atgiaavvga rwhdavtele rvrraqrdgg
      721 iaepgwlpva aelaeayahl sdpqrsarrl rdlagtggaa araasarveg llagepdlde
      781 vfaaalarcd pavvplerar tllsygqrlr rarrrrdarv qlhaalrlfe algaqgwarr
      841 crteidatgr rppepgdrtv drltgqerli alhvaegltn reiaarvfls pktveyhlgn
      901 vyrklrlrsr pelirhlsgp paag
//
LOCUS       WP_457604046             226 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604046
VERSION     WP_457604046.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>226
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          28..>226
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mgrseavpsg epdrpevpeq rsgdgpylqv rdlrvrfdte dgvvravdgv sfavergrtl
       61 givgesgsgk svtslailgl hnakrttisg eisvggrqlv glgeeevrrl rgrdmamvfq
      121 dplsalhpyy svgrqiaeay rvhhpragrr eartravdml grvgipqpar rfdqyphefs
      181 ggmrqramia malvndpdll iadepttald vtvqaqildl ladlqe
//
LOCUS       WP_457604047             473 aa            linear   BCT 27-JAN-2026
DEFINITION  TldD/PmbA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604047
VERSION     WP_457604047.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..473
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48519
     Region          11..469
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 msergmnael eiaagvvdlv rhtagpaaea evlvtrsdla ltrfansfih qnvsetgvav
       61 hlrlhvdgrt atgsgsrvda dglaalvert raaarlappd pawpgltapt pvpsgpavde
      121 dtafaspder aervrafvda vegleaagyc rtsyrsgafa nsaghtaagr aaeaamdgia
      181 raggadgvar lcadrladld gaalgaraaa karaaadpve lppghyevvl epaavadllq
      241 nlawygfngk hyaerqsfae pgtaqfdpav tlvddplhag tlpfdlegtp rralplvegg
      301 ttgavaydrr ggaeagagst ghgmpgsatf gpiphnvrll tgtagvagaa vaagpvsagv
      361 tgavgdpdta alvagmrrgl lvsdfwytrv ldpkqlvvtg ltrngvwlve dgvptravrd
      421 frftesypra lgpgrvlglg rtavrqpari dgswyetpal rlsswhftgg asg
//
LOCUS       WP_457604051             606 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604051
VERSION     WP_457604051.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 606)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 606)
  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 606)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..606
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65323
     Region          16..588
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mpassdgnpa ahsgarsqpl rnlwrlrpyl rpyatefawl lvaalaataa slavplvvqr
       61 vvdgpvarqd eagllrlgal alllgvaeav lifirrwtqs sssvgmeaai radiyahlqr
      121 lpagfhdrwq sgqllsrits dlsvirrfls fgllflvlnl vtyaavvall irlhqwlgll
      181 vaasavplfl isrrfarhyh aasrrmqdqq gdvatlveet alglrtmray grgpelaarf
      241 avgarrlhdt gigkarllar tsalfdlvpn ltlgavlvag aaavadgvls igelvafvsl
      301 qlmliwpvqs lgwiiangqe aataadriqe vldtpptivd alharqldrg evrgrlrfeg
      361 vgfrypgtsa pvlrdldltv epgetmalvg atgcgkstll slvprlhevt rgritldgyd
      421 vrdlrleslr rlvavafeep tlfsmsvwen lalgrpdase devraaltla qaefayelpw
      481 glstrvgeqg lslsggqrqr lalaravlgr pavlvlddpl saldvhteal veaalrrvlr
      541 dtatttllva hrpstvalad rvallddgri vavgthsell arvpayravl saeperrsdg
      601 vglvrs
//
LOCUS       WP_457604053             318 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604053
VERSION     WP_457604053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33402
     Region          35..314
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 msdfetvaat enqaarrgvs gepgtpgrag rpdrarslag dawrdlrrnp vfwislllvv
       61 lvaamavapg lfaandprdc mlsrqhagps ggaifgydfq gcdtfaravy garasllvga
      121 fsalitgvia lvvgmlagyf ggwvdavlsr vidivlgipl llaaivllkr vstsgetvrl
      181 favilvlall gwttaarvvr ssvitareqd yvaaarmlga gngrimwrhi lpnalapaiv
      241 vltialgsfi aaeatlsflg iglkaptisw gididagrvh mresatpliv pstflaltvl
      301 afimlgdair dafdpklr
//
LOCUS       WP_457604056             303 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604056
VERSION     WP_457604056.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 303)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..303
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31764
     Region          1..134
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          163..297
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 meqlrrvgay gvlrdsdgrv llargsvrcp ypgvwqlpgg gvehaehpad tvvrefaeet
       61 gltvapgair aavadvaafa dlgialhtdr lvfeveargg rlrpepaggs devgwftpde
      121 aaarqlmpft aellglpvtp lpadlpralp aepagpsvdr rqrfaayglv tdpadrvllt
      181 miadgypgag rwhlpgggtd hgeqpaagll relveeagql grvvdliavd nlhnpaalgp
      241 egrpldwhgv rviyrvcvda ptdavvtela ggstaraawf apeqvtglsm tdvaaratgq
      301 rvs
//
LOCUS       WP_457604057             464 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604057
VERSION     WP_457604057.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..464
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48943
     Region          49..455
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(159,161..162,294..298,319,322..323,326,341,345,395)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mgrgrvwaag lvtaalalsg ctggddngfr pgaadagdpy vpgagnggyd vghyaldvry
       61 dpasdrltgt atltvtatra lsrfqldlag ldvervrvdg avvkhrhdga elivtpaggl
      121 psgrrftvev ayggvpkplp naelgdggfh atpdgaialg qpesastwyp vndhpsdkat
      181 ydlavtvpdg laalsngvpe grtssggwtt wrwserapma sylstlvigd yrvssgthag
      241 kplvtavaaa lpadgpaaas vartgevadf laarfgpypf eayggvvvad eriryaletq
      301 srpvygpaff rgdrpntevv ahelahqwfg dsvsvarwsd iwlnegfaty aewlwaehdg
      361 grtvaqtvve ryaatdwsrp tvdpgragmf gdavyqrgal avhalrravg deafyrvlrg
      421 wlaqhrdgnv ttadfigyae rtsgrplral ldawlvggtp pglp
//
LOCUS       WP_457604062             236 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604062
VERSION     WP_457604062.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  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 236)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..236
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24832
     Region          72..147
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 msvadafdav agsydqarrr lvpcfdafyg tavevaappl raalaagrtp evldlgagtg
       61 llsllltaav sgvrltlvdg apgmlavaag hldargvphr tvhadlagpl pagrydavvs
      121 alaihhldde gkralykraa dalvpggvfv naeqvagptp aldrrydevw taritelgsd
      181 aeeiagarer mrhdrpapva eqcrwlteag lvdvdcffke wrfavfggqr pdgsar
//
LOCUS       WP_457604064             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604064
VERSION     WP_457604064.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28603
     Region          1..254
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mirlsgvsrt fdgrsgrvea lrgidldvae gefvavlgrs gcgkstllrm iagllpvtgg
       61 eitvggtpit kprrdvamlf qrpallpwrs vldnvllpve ifgwrraehr drarqllema
      121 glggfekrlp helsggmqqr vslcrsligs prvmlmdepf saldaltree lsgelqrvhm
      181 etkativfvt hsideavlla drvvvlsprp grirevvevn vprprtlgrh ehledvaris
      241 aelhellmer dapsvpvggr
//
LOCUS       WP_457604066             257 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604066
VERSION     WP_457604066.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..257
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26337
     Region          1..256
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msaleiggva fgsrlilgtg gaanlhvleq airasgtelv tlalrrvdtt pggsgglldl
       61 vercgvrllp ntagcrtave avktahlare afdtdwvkle vigdertllp dgvellraae
      121 elvadgftvl pytsddpvla rrladlgcaa vmpagspigs glgignphhi rliraavdvp
      181 vvldagigta sdaalamelg cdavllasav traadpvama tamryaveag hlaygagrit
      241 rrfhalpstp degrpdl
//
LOCUS       WP_457604072             482 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604072
VERSION     WP_457604072.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49219
     Region          18..436
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(28..29,32..33,36,71,126..127,129..131,134,154,
                     157..158,161,271,274..275,278..280,283,307,310,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtpaillpyr pvlgqpvlrr llpglatsal gdglalvavt wlalqlapag qrgtwtafav
       61 aaytlpgaag tlllgrwlga rsgaqlagwd atvraaalga ipvahlagvl dvglyvalla
      121 vssllhpwgs agrftlvael lpqrhhlaan allgvfgqaa tivgpplagl liawtgpvwv
      181 iavdaasfav lavsyrlvvr dreaaavser dtaavrdrea aavrdgdtat vherdtngry
      241 rngpagagps rmsgfriigr drsllgllsl sfaffflfgp fyvampvhvt ddlhasagtl
      301 aayytafgvg sllgglltgh lrgwplrttl agivalfgaa llplglgapv vlslpafala
      361 glvwapyqpt atalfqrrag tadlprvlaa ngavtvlavp lgtmlggpat allgarptll
      421 acavtilalg lvaavsaarp gaqntertgp agphdrpgpq ttgphdrpgr vkapdrvrpg
      481 as
//
LOCUS       WP_457604073             168 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604073
VERSION     WP_457604073.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..168
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18890
     Region          5..155
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mdgpedfdaf ytatarrvvh hvyalcgdla eaqdvtqeay arawqrwsrv gayedpegwv
       61 rtvawrltan rwrglrrwfa ararlgretp tpgpnpdrva llaalrrlpd aqrlvvvlhh
      121 lhdlpvaeia rttgmpegtv ksylsrgraa lavlltddke evdvgthw
//
LOCUS       WP_457604074             488 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604074
VERSION     WP_457604074.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..488
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=48601
     Region          72..488
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mslvqpvdnv amlpaylaag tavlvllvdl lvarpavtva vaalgaagta vgaalvgaag
       61 trrtfcvgdd cswvwngraa lvgaviallt lgvlalsgpl lragrtpvge ycfllacamt
      121 ggvvlgaagd litlivalet ltlplyvlvg lrrgslagae aavtffvvsv vattvtllga
      181 allyavtgtl hldrlgatla arddltdlpl ttvavalvva glafkvaavp fhawapatyd
      241 gaplpvaayl stasklggvv allavvqral pgdltgpvla alavltmtvg nlvalrqrrt
      301 vrllawssva qagyilaplg alaltagrtg daraaayaaa vayaiffvll elaafaavva
      361 lrpadgdggt ladlrgaarr hpwvggafal aliglaglpp glaglfakvt vvrallagha
      421 gwlalvvaln aviglayylr vtaslyatpa gvatvrpart vvlalgaatv aavvigfapq
      481 lvldvaar
//
LOCUS       WP_457604075             501 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 4 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604075
VERSION     WP_457604075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=50864
     Region          <156..470
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mtfgqvllvs vvavpalgal atavvpgdra grvvgtaaaa ltllatlplv ggdhgwfgyg
       61 prpavqpwhq ldlqwvpgld lrfhlgvdgi swplvvltal ltllccaytl wrvppgggsg
      121 ralvalllvv evgilgtfla ldlvlfflff evvllpmyav iagwggadrr raarkfalyt
      181 lfgsvlllvg vyvvvaaagt adlvaltgga glsrgtqlaa ftllalafav ksplwplhsw
      241 lpdahtqapt vgsvilagvl lkmgtyglir vavgvapega rwaapvlgvl avaailvggl
      301 vclaqddlkr liayssvghm gfvllgvatl tatgiqaali gniahgvitg llfflagavk
      361 drahtgslae lsglretapr lagllgfaav aslglpglag fwgeafavva avqrggplwl
      421 tlavlaalgg altaayflrl lrrvthgrps pavaglapgl agaeltawap lvllalavgl
      481 apalvlsyas gpveallgvv p
//
LOCUS       WP_457604076             641 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit 5 family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604076
VERSION     WP_457604076.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Desmarais,J.J., Flamholz,A.I., Blikstad,C., Dugan,E.J.,
            Laughlin,T.G., Oltrogge,L.M., Chen,A.W., Wetmore,K., Diamond,S.,
            Wang,J.Y. and Savage,D.F.
  TITLE     DABs are inorganic carbon pumps found throughout prokaryotic phyla
  JOURNAL   Nat Microbiol 4 (12), 2204-2215 (2019)
   PUBMED   31406332
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Efremov,R.G. and Sazanov,L.A.
  TITLE     Structure of the membrane domain of respiratory complex I
  JOURNAL   Nature 476 (7361), 414-420 (2011)
   PUBMED   21822288
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Nakamaru-Ogiso,E., Kao,M.C., Chen,H., Sinha,S.C., Yagi,T. and
            Ohnishi,T.
  TITLE     The membrane subunit NuoL(ND5) is involved in the indirect proton
            pumping mechanism of Escherichia coli complex I
  JOURNAL   J Biol Chem 285 (50), 39070-39078 (2010)
   PUBMED   20826797
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Brandt,U.
  TITLE     Energy converting NADH:quinone oxidoreductase (complex I)
  JOURNAL   Annu Rev Biochem 75, 69-92 (2006)
   PUBMED   16756485
REFERENCE   5  (residues 1 to 641)
  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 11436849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..641
                     /product="NADH-quinone oxidoreductase subunit 5 family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=65647
     Region          65..618
                     /region_name="NuoL"
                     /note="Membrane H+-translocase/NADH:ubiquinone
                     oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+
                     antiporter, MnhA subunit [Energy production and
                     conversion]; COG1009"
                     /db_xref="CDD:440633"
ORIGIN      
        1 mstptlwlaa vlpaaplvag llglllppap rqdraaarrs avalgvagaa vsllaalall
       61 vrvdapveas ttwvdlgglr vtlglrldgv avlvatavaa valavqvysi gylrrgphdd
      121 vdvdhryppy aaqlslftaa mltvvvsgdl imllvgwevm gvcsylliah drrlpeapga
      181 avkaflvtrv gdvgfllgia llgvgagsfr iadvlahdyg tgtltaacll llagvagksa
      241 qfplhtwlpd amagptpvsa lihaatmvaa gvyavarlfp lferapaala vlgvmaaitm
      301 llgafaataq ddikrvlaws tvsqigymtg alavgapaaa lfhllthaaf kallflaaga
      361 vihavgttlm srmgglrtam pvtfwcmvvg lgalagvppl sgfwskdgvl aaaeaaaldg
      421 agptaawvgw lvwlaglvgv avtawyatrl llrtflgrtr tpllrphdpp allrwpvlll
      481 tvpaallgla afapwfadrl rvpgddtaea velvhlapnl ilpfllllag agvawagwrr
      541 dpaadparfl gplrpvfara frlddvqhal vvrpagalar vvrtgdelgv dglvegsgra
      601 avevggglaa lhraalpraa agvlagalli glavaligvt s
//
LOCUS       WP_457604077             347 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604077
VERSION     WP_457604077.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..347
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38854
     Region          19..321
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgsddevldr tggkyvepgg eftrdqryia tritadgsng wpvepgryrl avsracpwan
       61 rliivrrllg ledaismava gpthdkrswt fdldpdgkdp vlgierlada yfarfpgyer
      121 gitvpalvdv ptgqvvtndy aqmsldltte wtahhrpgap dlypeplrge idevngvvfa
      181 dvnngvyrcg fagsqeaydk ayhrlfdrld wlserlagqr ylvgdtitea dvrlfttlvr
      241 fdpvyhghfk cnrqklsemp vlwayardlf ttpgfgdtid fdhikrhyye vhrdinptgi
      301 vplgpdlsnw liphgreelg grpfgdgtpp pppppservd pshtplr
//
LOCUS       WP_457604080             492 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604080
VERSION     WP_457604080.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 492)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..492
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50325
     Region          9..371
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtdtadvgal pargmpaadv lgeiralraa drpthggrlf ayvydpgvag ldelaqaaya
       61 esahvngldp tafpsllame nalvgaaarl lgggpgtgap dvvgsvtsgg teslllavka
      121 ardarpdlte privapasah aafakaahyl rvtldtvpvd avtlrpdpav vaaairpetv
      181 lvvasapsya hgvvdpvtei aavaqaadvr chvdacfggw alpwlrrlga pvppfdfavp
      241 gvtsisvdlh kyayapkgvs vllhrdpalr apqffayadw pgytmvnpvi astrsggpia
      301 aayatlrhlg edgylrlaaa trdavtglad avratgglrl maepettvvc ftsddpgldl
      361 fvlvdeltar gwhtqpqlty adlpasvhlt vtaavaprva efgpalaeav aaaraagpvv
      421 lppellalag sltpealtpd lvaglagglg laggagvpdr mavvntllda aparlrerll
      481 aefvgllqrp aw
//
LOCUS       WP_457604083             372 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604083
VERSION     WP_457604083.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38434
     Region          62..362
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mtevksaeap appaavpdel spgrarwhgl rpylplvalv vaailpystl hlpgifegpl
       61 nspgtlqlla iclvfgglaa gydllfgrtg mlsfghalyf aagvygtdil vtkaglplwq
      121 aavltviggt tlaallgava lrtvgiafam vtlafaqvga ilvardfggl tggeeglpld
      181 vsglpsalvg vtntvnlywl alaylaivvl vvhrvsaspt grvlaglrdd errigvlgld
      241 pyrfklvaft lagglasagg vvyvlivgga sphitsselt lsllvmvvlg gpgtrwgpvl
      301 ggvlymyldh rltafgssda vnslpaflsh plsqplfvlg tvfilavyff pgglaslrsr
      361 vtpllaalrr pr
//
LOCUS       WP_457604085             222 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604085
VERSION     WP_457604085.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..222
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24179
     Region          <11..207
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 msarhpeetg iaviglgrfg trlaeslsrl gyevlaidrd parvqhwsae ldrvvqadst
       61 eevvlrqlgl adfrrvvvai gasleasvlt vlalaelrie qiwaratsek hakilhsvga
      121 hhvvfpeaet gervahlivs rmldfiefdd dfaiakvkvp aplvgrslrd iapqdrygvm
      181 vvgekqsgqp fryagpdtvl qadsvliveg aitqvqrfsa lt
//
LOCUS       WP_457604086             294 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604086
VERSION     WP_457604086.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30085
     Region          7..291
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mntnpdksvt vlglgpmgra lagaflsagv pttvwnrtpg kdrelverga msartaeeav
       61 aasgltvvcv vnydasdail rreavaaalt grtvvsltad tpdrardtar waaghairyl
      121 dgaimtpttt igtpdavliy sgpaglyqeh qpvldalggt hthlgeeigr aaaydialld
      181 ifwtamagya halavakaeg vtagelapfa agiaailppi feegaaemdt gifpgdgnpi
      241 tsavssmahi vhtseahgid agvmraaegm arravglghg adgflrvaev lgrr
//
LOCUS       WP_457604089             320 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604089
VERSION     WP_457604089.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..320
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35189
     Region          18..319
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 madvievgaa rdgapppaar trrrgaterg nrttpylfla pylilfgvfg lapivfgvwi
       61 slhqwdlqlp nrpfvglgny rdlfssdsai ygdwwssvra tgvftlfsvp llvvvplgla
      121 lllnrsfpgr tffraaffap yvlgvavigl lwrflldanl glvnrllgvv glpsdtpwvt
      181 dvpwawvslv gvtvwwtcgf naviylaglq dipaelyeaa kvdgagawdr frhvtipglr
      241 pvmlfvfttt llasanvfgq aflitqgapg eqtrtvvwri vdeglrdyda graaamsvff
      301 almlavvsvv nfrlfryred
//
LOCUS       WP_457604090             274 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604090
VERSION     WP_457604090.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 274)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..274
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30121
     Region          2..274
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mrnmraaary gvlllitaif vtplvwmllt svktyddaqr vppgwlpnpf stygyqqivd
       61 naanpvlrwf vnsmlaatlh tllvlvtasm aayalarkrf rgrkvlfali vgtlflppts
      121 liipnfiiae rlnwidtltv vivpgaasaf gvfflrqffl sipaeleeaa vldganhwqv
      181 frrvllplsk palatlavls fltnwndflw pvyvlfsper ltlpaglgll qgayvtdypv
      241 ivagavlasv pvlilfvfaq rhviqgvsrs glkg
//
LOCUS       WP_457604091             337 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604091
VERSION     WP_457604091.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..337
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35359
     Region          <12..329
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mlvlgvvavv giresarvtn llvlvkvaic afviiaglff vkaanlspfi psaepagagd
       61 dgvkqpvtqa ifglepsvfg fagvltaaav vffaytgfea vanlgeetrk pkrdlplgll
      121 gtllistvly igvslvvvgm vkyteidega piasafravg agwaavlvsi aavagltsvi
      181 lvdlvamgri gfaiardgli ppaiakvhpr wgtpyriagi mtvavallag flplsaladl
      241 vsigalcaft lvaiavpilr rrrpdlerpf kvpfspvlpi vtavaclyls lnlsvetwlr
      301 flawmllgav iyfgyghrkn rlarrehsdt pepaptp
//
LOCUS       WP_457604095             226 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604095
VERSION     WP_457604095.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..226
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24094
     Region          74..>117
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mtdiadtepe agaaagtatg ahsgtataaa tgartgtgtg acaapgvpaa aaggdgpall
       61 tepfdvpfpa pgivravrrr adasqrelar farvhpstig rieagtltps ltmlsrivgt
      121 agfrlvvvde agrvlkpmrd radlrdgaer rypshldvit dpepgewwad ryglarppet
      181 fyrnrevrdw lrrrsqwevr varyrsvppp pdpqrcgyrg gppirp
//
LOCUS       WP_457604098             289 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604098
VERSION     WP_457604098.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..289
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29820
     Region          1..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtvpaveavd vwrtyeldgv svsalrgvsl tidqgeyvav igpsgsgkst lmhllggldr
       61 psggrlvigg rdvttmtape latlrnetig fvfqafhlla rtsavdnval plvyrgvgar
      121 qrreraaaml grvglghwlh hrpnqlsgge qqrvaiaral vtepavllad eptgnldsat
      181 geavleller lnaesgvalv mvthdqevaa rahrriavrd glirsdslhd rppsdgsgvp
      241 atldpapsae prsasgsgpg hppggpggat gatgrlpraa ggrqrgdag
//
LOCUS       WP_457604099             465 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604099
VERSION     WP_457604099.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..465
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46475
     Region          78..464
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mgrvartpsp rlpaarrprl vtvvlavval tgttaascgd dapavtvaev grapvsevid
       61 apatvtaraa atltapadgt larlrvqpgq rvtrgqvlav idspsardrl akardalraa
      121 kragrgagtg dlggsrrgtd raadeafaaa raaagkvgdp qvraelllqv qsaqrqyesa
      181 araadravaq vqrgvaglns avgalsaaqr lqaqqaydla katvdaltlr apiagvvqpg
      241 gtrsaapadl agllgaagga avpgldpsal gtggqggppp gvddaipagg rvtagtpvlt
      301 vvdigrlgll aevdetdvll vragvpasve ldavtgatyd atvrsvdvlp tssarggvty
      361 rvrldlgagr lgeaeaapap rpgmnavvrl rvreaadava vpasavfsad grdavwvlrd
      421 gragrvpvtv gvqgqdlvqi vdgvragdrv vvrgadqvrd gqelp
//
LOCUS       WP_457604102             189 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR-like C-terminal domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604102
VERSION     WP_457604102.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..189
                     /product="TetR-like C-terminal domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19609
     Region          95..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mpragltpat vvreaaalad evgyekltla alaarlgval pslykhvrgv dslhqklavl
       61 ataeiadvlt aaaagraggd alravaaayr ayarqhpgry paaqrapdpa dpdhlaager
      121 avgavraill gygldgdaat dairmfraav hgfvaleaag gfglprdtdr sfdqmiagld
      181 rayrswedr
//
LOCUS       WP_457604105             388 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathionylspermidine synthase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604105
VERSION     WP_457604105.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Sui,L., Warren,J.C., Russell,J.P. and Stourman,N.V.
  TITLE     Comparison of the functions of glutathionylspermidine
            synthetase/amidase from E. coli and its predicted homologues YgiC
            and YjfC
  JOURNAL   Int J Biochem Mol Biol 3 (3), 302-312 (2012)
   PUBMED   23097746
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Pai,C.H., Chiang,B.Y., Ko,T.P., Chou,C.C., Chong,C.M., Yen,F.J.,
            Chen,S., Coward,J.K., Wang,A.H. and Lin,C.H.
  TITLE     Dual binding sites for translocation catalysis by Escherichia coli
            glutathionylspermidine synthetase
  JOURNAL   EMBO J 25 (24), 5970-5982 (2006)
   PUBMED   17124497
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Bollinger,J.M. Jr., Kwon,D.S., Huisman,G.W., Kolter,R. and
            Walsh,C.T.
  TITLE     Glutathionylspermidine metabolism in Escherichia coli.
            Purification, cloning, overproduction, and characterization of a
            bifunctional glutathionylspermidine synthetase/amidase
  JOURNAL   J Biol Chem 270 (23), 14031-14041 (1995)
   PUBMED   7775463
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..388
                     /product="glutathionylspermidine synthase family protein"
                     /EC_number="6.3.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43753
     Region          1..383
                     /region_name="Gsp"
                     /note="Glutathionylspermidine synthase, CHAP domain [Amino
                     acid transport and metabolism]; COG0754"
                     /db_xref="CDD:440517"
ORIGIN      
        1 mrreastprp gwdetiraqg lvyvdtelpd geimsywdet aaysftldev lrleeateel
       61 hrmsvaaaeh vvarrryaef gipewaaeav arslrenppt lygrfdlwyd gsgppkmley
      121 nadtptalve asivqwywle htrpdadqwn slherlvgaw akigaglhep rahvlwssee
      181 esgedqitag ylaetarqag ldvtlmpiqr vgwdgrrfvd addrpittcf klypwewmla
      241 epygrpaldp gtpttwiepa wklllsnkal lavlwemypg hdyllpayld sprgmteyva
      301 kpllgreggs vrivtgdrei tnpgiygdeg fcfqefralp efegnrtvlg swivdgesag
      361 agvresesli tdgyarflph yidaprvl
//
LOCUS       WP_457604118             319 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 9 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604118
VERSION     WP_457604118.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 319)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..319
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32391
     Region          2..310
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 milvlralgv gdlatavpal rglraglpgr elvlaapgwl aplaeltgav drvlptagpd
       61 riawtgpppe vavnlhgrgp qshralaavr pgmllahsnp gaghpdgpaw dddehevrrw
      121 crllhayglp adpgdlalrr paltgvpagv tllhpggkip akrwpadrfa glarelaarg
      181 hrvavtgspd eralaervar daglppeavl agrtglaema alvagarlvv sgdtgvahla
      241 tgygtasvvl fgpvpaahwg pppdrprhra lgaieptpvn pdstgsggvg thptldaigi
      301 devvaavadv ervsgavaa
//
LOCUS       WP_457604120             477 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604120
VERSION     WP_457604120.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..477
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=47923
     Region          23..469
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mytvaqligg vwgaggegge lvvhdpadgs pvtrtpvata devakaveaa rgvaaewaat
       61 apaaraaalh raadaveaaa delaeattae mgkplddarg gvaagvgtlr qyaelaplrg
      121 grtlhgahga ldfmapeprg vvaaitpwnd pvavscgllg aalvtgnvvv ykpsertpat
      181 gwllaralds alpagvlsli tgggevgaal agqeldviah vgstatgrvi aaagartgak
      241 vllenggsdp lvvdadvdpi waaeqaalgc fanagqicva veriyvhrdv aegfldalva
      301 raealtvgpg rdpgtqlapl vdrrhrdhvh gqvtaaladg arvraggvlp dgpgafypat
      361 vvegcrhdma lvreetfgpv apvvvvdsfs gglrcaadsp yglaatvltg smshaqrawr
      421 elpvgtvkin svfggapgga aqprrgsgqg fgygpellde fstvkavhle apggghw
//
LOCUS       WP_457604124             834 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604124
VERSION     WP_457604124.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 834)
  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 834)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..834
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92111
     Region          1..820
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtltaalpkt adpdtlydaf aswasergld lyphqdeavi eivsganvim ntptgsgksl
       61 vaiaahfaal addrttfyta pikalvsekf falcevfgae nvgmltgdas vnadapiicc
      121 taeilanlal regrradvgq vimdefhfya epdrgwawqv plielpqaqf vlmsatlgdt
      181 trfvddltrr tgrptavvrs aerpvpllfs yattplhetl eelletkqap vyvvhftqaa
      241 aleraqalms vnvctraekd miaqaignfr ftsgfgktls rlvrhgigvh hagmlpkyrr
      301 lvetlaqagl lkvicgtdtl gvginvpirt vlftglskyd gtrtrllkar efhqiagrag
      361 ragfdtlgrv vvqapehvie nekalakagd dpkkrrkvvk kkppegsigw geptfqrlve
      421 aepepltssf qvshsmllnv igrpgdafas mrhlltdnhe dpaaqrrhir raiaiyralr
      481 aggvveelpe pdetgrrvrl tvdlqldfal nqplsplala tvelldresp syaldvlsvi
      541 esilddprqv lsaqqfkarg eavaamkaeg ieyearlell devtwpkpla elldsayemy
      601 rqghpwvadh qlspksvvrd myeramtfpe yvqfyglsrs eglvlrylad ayktlrqtvp
      661 edakteelvd liewlgelvr qvdsslidew erlrnpsdva evaaslddrp pavtrnaraf
      721 rvlvrnamfr rvelaalrrw dllgeldagd gwnadawada lepyfeayds igvgpdargp
      781 allmieqgre rwtvrqildd pdgdhdwgis aeidlaasde tgaavvrvtd vgql
//
LOCUS       WP_457604125             394 aa            linear   BCT 27-JAN-2026
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604125
VERSION     WP_457604125.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 394)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..394
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42579
     Region          1..394
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,254..256,294,311..313,336..338,380)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkaltwhgkr dvrvedvpdp rieeptdaiv ritstaicgs dlhlyevlgp ylkpgdilgh
       61 epmgvveevg pgvtrlkkgd rvvipfnisc gscwmcerql yaqcettqvt sqgkgaslfg
      121 ytslygsipg gqaeylrvpq aqfgpitipd sgpderwlyl sdilptawqa vkyadtppgg
      181 tlavfglgpv gqfsarigrh lgagrvigld lvperlemar rhgievldvs qlddvpgali
      241 dlvdgrgpda vidavgmeah gaplgkmaqt aagllpdkla qamtdkagvd rlvvlhaalk
      301 avrrggtvsi sgvyggeqdp mplmemfdrg iqlrmgqchv rrwvdeiipl lerdddplgv
      361 edlrthrlpl tdaprayemf qkkedgcvkv vlap
//
LOCUS       WP_457604127             815 aa            linear   BCT 27-JAN-2026
DEFINITION  Tex family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604127
VERSION     WP_457604127.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Fuchs,T.M., Deppisch,H., Scarlato,V. and Gross,R.
  TITLE     A new gene locus of Bordetella pertussis defines a novel family of
            prokaryotic transcriptional accessory proteins
  JOURNAL   J Bacteriol 178 (15), 4445-4452 (1996)
   PUBMED   8755871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..815
                     /product="Tex family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /calculated_mol_wt=87049
     Region          1..727
                     /region_name="Tex"
                     /note="Transcriptional accessory protein Tex/SPT6
                     [Transcription]; COG2183"
                     /db_xref="CDD:441786"
ORIGIN      
        1 mtqsvhqria eelgvaerqv raavelldgg atvpfiaryr keatglldda qlrtleerlr
       61 ylrelderra avlesirsqg kldealeaqi laadsksrle diylpykpkr rtraqiarea
      121 glepladtll adpaqdpktv aagfadpdkg vadaaaaldg arailierfa edadligtlr
      181 eqmwsrgrlv srvregqeta gakfadyfdf aepypklpsh rilavfrgek egvldltmdp
      241 eaegdadaat gpsryeaava grfgisdqgr padrwladtv rwawrtrili hlgadlrmrl
      301 wqaaeeeavr vfatnlrdll laapagarvt mgldpglrtg vkvavvdatg kvvatdtiyp
      361 heprrqwdas lhtlatlaaa hgvelvaign gtasretdkl agdlikqhpe lkltkvvvse
      421 agasvysasa yasqelpgld vslrgavsia rrlqdplael vkidprsigv gqyqhdlsev
      481 klsrsldavv edcvnavgvd vntasapllt rvsgigagla enivlhrdan gpfrtraelk
      541 kvprlgpkaf eqcagflrip ggddpldsss vhpesypvvr rilsstgqdl raligrsail
      601 rglratdfvd dtfglptvtd ilaelekpgr dprpefrtat fvegvekisd lqpgmilegv
      661 vtnvaafgaf vdvgvhqdgl vhvsamshtf vkdprdvvks gdvvkvrvld vdvprkrisl
      721 tlrlddeapa ggrpaaggpg geerggrrgg gqrgdgggqr gdrggqrgda garrggqger
      781 ggsrggqspr qgrgggaaap vndamaealr ragla
//
LOCUS       WP_457604136             317 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604136
VERSION     WP_457604136.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..317
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=33509
     Region          14..313
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mgvmtkadvv vvgggvigmt taltlqrrga hvtvltahdp adtvstvaaa vwypshteed
       61 prvlrwardt haelrrqaad gvpgvvdrpt rmwlrhrytg ppwwadacgd ltaepaeppy
      121 tallrftaps vemtpylawl rqrleagggr vvrralgtla eayevapvvv natglaagrl
      181 aadpavypar ghvllvanpg ltvsvrdedd pagvtyvhpr rhdvvlggty eagvghtrpd
      241 peeaaairrr cvalvpqlad apvlgerigl rparhggprv evdaadvrlv hayghggagv
      301 tlswgcaaev adlalgv
//
LOCUS       WP_457604141             204 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604141
VERSION     WP_457604141.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..204
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21852
     Region          2..182
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 matvistlfi sadgvaeidp dwhfpyfden mgravtedyd tsdvlligre tydsfagawp
       61 dreaaggeda pfakqlgdmr kvvvsrqple fswrnseliq gdlvdavral kadagikgll
      121 ipgsisvvqq llaaglvdel rllvhpvaar kgrrlfdegg apyhlrvaat eayptgvirv
      181 iytpapapga vgyddvkdqv pags
//
LOCUS       WP_457604142             158 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604142
VERSION     WP_457604142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..158
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16999
     Region          5..140
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mraaterhgd eliarrhlpa lpdrvwhaft sptgiaafwg gshatvpqas vtvdlrpgge
       61 faldtrapdg rtgrlrfvyv rveppselvf depvtglrtt vtlrpaghgt dltvhqrklp
      121 pelrtdqatd glasildala ahlrhhddgd ssdpsnpa
//
LOCUS       WP_457604147             772 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604147
VERSION     WP_457604147.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..772
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=82298
     Region          1..767
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 maehrlttlt gpggsgktrl atetgrrmtg dlpdgvwlve faavsaggdv vqatisglgl
       61 rdallgdags aepadrlvaa irdremllil dncehvvdqa aalahrllge crrlrilats
      121 replgitgea lwpvaplglp dgdapiaeve sspavrllrd raaavrrdla fdaraattma
      181 ricraldgmp laielaaarl rtmsvdqlat rlddrfrllt ggsrtalprh rtlramvdws
      241 wellsdaera vlrrlsvfsg gasldaaerv caggavepgd vldlltaltd ksllvaagdv
      301 aphyrmlgti keyaaqrlae vgeadlarra hlayftelae taeprlrrad qltwlarlea
      361 ehdnitaavr galaagegre amrlaagagw ywwlgghrte gmeliiaate apgdvpddir
      421 avvyglvvlf lssgpgdaqh aaewihkayr lsgeghgghp elalvvpmer mlrepdallp
      481 aweslldhed pwvralarlh lgklrvilgv eaaqaeaclr qalaefravg erfgisfals
      541 elaeliavrg dvaaacayye qaaaavtevg avedvirmra rlawlyrlgg detasaaala
      601 eahrlaagva wpgalaelal vraylarhdg dadeayaqlr svsallgdea dlasvragtq
      661 dllgylaedv eqarthraaa craareggya pltaqvlvgv adlavrldrp dhaarllgaa
      721 tavrglpdra hpdvprieaa ardrlgdaef aeavaqgret gwerlveitl as
//
LOCUS       WP_457604157             247 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604157
VERSION     WP_457604157.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26068
     Region          4..207
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mpdrvvvlsd ihgvlpalea vlaepdvaaa dlivltgdla agpqpvevld rlaalgdrac
       61 wvggnadrel vqaragrssp iavsnwaagq lrddqvarla alppyvtlpv tglgdvlfch
      121 atprddeevv lvdsrldrwa evfaglpaev gtvvcghthm pftrladrrl vvnpgsvgmp
      181 yggagawwal lgpgvqlrrt rfdvdaacar vaaestfpda aawadeyvrs rhsdadaltv
      241 faprdgr
//
LOCUS       WP_457604163             248 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604163
VERSION     WP_457604163.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..248
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26445
     Region          17..134
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtdptaalsf gaaaaeydrf rprypeaalr waldglldaq vvdlgagtgi ltrgllaltg
       61 pvaqvvpvep dpgmraqlaa atpgatalag saeavplpdg sadavlagqa yhwfdrerah
      121 aeaarvlrpg gtfapvwnir dervgwvael triahlgdna gdvtqryadf gaaftavevg
      181 efphattltp devvgmlhtr sfwltadtde rrrvdaelae lfaghpdlag rdavelpyrt
      241 mvlrarrr
//
LOCUS       WP_457604166             161 aa            linear   BCT 27-JAN-2026
DEFINITION  CarD family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604166
VERSION     WP_457604166.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Kaur,G., Dutta,D. and Thakur,K.G.
  TITLE     Crystal structure of Mycobacterium tuberculosis CarD, an essential
            RNA polymerase binding protein, reveals a quasidomain-swapped
            dimeric structural architecture
  JOURNAL   Proteins 82 (5), 879-884 (2014)
   PUBMED   24115125
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Stallings,C.L. and Glickman,M.S.
  TITLE     CarD: a new RNA polymerase modulator in mycobacteria
  JOURNAL   Transcription 2 (1), 15-18 (2011)
   PUBMED   21326904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..161
                     /product="CarD family transcriptional regulator"
                     /GO_function="GO:0140110 - transcription regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0009303 - rRNA transcription [Evidence
                     IEA]"
                     /calculated_mol_wt=17690
     Region          3..157
                     /region_name="CdnL"
                     /note="RNA polymerase-interacting regulator,
                     CarD/CdnL/TRCF family [Transcription]; COG1329"
                     /db_xref="CDD:440940"
ORIGIN      
        1 mvfsvgetvv yphhgaalie aietrvikge preylvlrva qgdltvrvpa enaeivgvre
       61 vvgeeglgkv fdvlraphte eptnwsrryk anleklasgn plkvaevvrd lwrrerergl
      121 sagekrmlak ardilvgeva laekstkgea etlldkvlte a
//
LOCUS       WP_457604177             199 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604177
VERSION     WP_457604177.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..199
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22216
     Region          7..182
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrddggvlle tarltlrrft mddvdrlval dadpevmrfl tggaptpaat yrdevlprvl
       61 aqyaqhpglg rwatldrftg eflgwhsldp sddggeaelg yrlrratwgh glategaral
      121 vrhafdtvgv crvwaqtmav ndrsravmar aglryvrtfh lafddpipgt ehgeveyelr
      181 rdawpatrqe wdaaalrar
//
LOCUS       WP_457604182             203 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604182
VERSION     WP_457604182.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..203
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22017
     Region          6..185
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mpsrllylvr hgeqdrpeee adtglsergr rqatllgerl rgtrfaavhh gparraaeta
       61 alvaaslpgv pvreddragd hmphdtdpag lpesyaafla gfsererrdg prvtaesvar
      121 fatapaegdv relvvthnfl vawlvlhavd aparrwigln qqncgltvir yssggppali
      181 afndvahlpp elratglpdd yri
//
LOCUS       WP_457604183             146 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604183
VERSION     WP_457604183.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..146
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16108
     Region          62..120
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mdavlvvnad lgplhrvtvk hairmlcrrv aeiheaepdr vigvfplprv vrlvryvvtr
       61 wrfsagpaws ragvlardrr kcaycdgaas tidhvlprsr ggrntwgntt aacyacnqrk
      121 gdrtpaeagm plrrepvtps waalar
//
LOCUS       WP_457604186             594 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604186
VERSION     WP_457604186.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..594
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=62952
     Region          263..559
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 maeplrdrar ratgwrlrmn gderphyvvc gsdplaywvv rsllatdsad grvrvtlvvp
       61 grrrsegpdg rdvpgvrvvt aerldeaafr raglagaagl allhqddvgn mhaalcaqev
      121 esrlrlvvrm fntnladglr qlfpdsavls dasiaapafv aaalgevapt hfrhagrtly
      181 varrddvrpq dvvcglavtt dpdlvrvlpa deaaadvvla eatgrpagte vaarrlvrar
      241 rrrqpvavll ravrhfatrk igiavlvllg viaalgwlna raadvswsea vyltlvttlt
      301 gqdpdvnkpv aaqvmqvvln laglalipli taavvdgivn arlalhagrv qpdrsghvvm
      361 vglgnigtrv maqlhdfgve vvaidknada rgaplarrlg vplivgdagr eetlrsasvd
      421 tcqalvvvst ddgtnlraal iarsldpdlr vvlrlfdgdf aeriqqafgi gisrsvsyla
      481 apafaaalld ravvatipvd rhallvtevp vvagspldgs plsavarpge vrllahtrpn
      541 qkadwsadpr mviqagdrlt vvarraglta llrettpapp paptgppaar rpqe
//
LOCUS       WP_457604193             417 aa            linear   BCT 27-JAN-2026
DEFINITION  FUSC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604193
VERSION     WP_457604193.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..417
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44511
     Region          44..240
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 maregrlrfl rrgnlregla drdgqriasa meelrhrgka tlhdrlhrvr tafglavqag
       61 laaglaylva hrllknpqpv fapisavgtl aasvgqrfrr tvelivgvav gvlvgdaliy
      121 fvgtgawqla lvvtsaills ifagasvaiv iqaaatavli vtlspstenl efprfidall
      181 gggiallvta illplnplrv inraarpald llagqldaca davrsrdrda aqqalfrlre
      241 nkeelaalse aiegaketst lsparwhrrs elthyaeaad pidramrntg tlirravtmi
      301 edsepvpepm pdaighlaes vrllrqefaa gqepqearer slravseagr ayaegvgfsg
      361 svviaqvrtt asdlmvasgi eqeeanrlvr qafgenrqge paarnpaahp ptappvg
//
LOCUS       WP_457604194             423 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604194
VERSION     WP_457604194.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 423)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..423
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=43561
     Region          54..422
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mtvtlvpslp vlpvlpapar pdplgvlgvp geinldhaas apcaraaada vagllpwyas
       61 vhrgagalsr rctlayerar qtvgdflgar pddhviftrn ttdalnllar alpagttvit
      121 fgaehhanll pwprgsvrlp vpdspagavr slaaalgela rdarpglpvl vavtgagnvt
      181 gecwpvaela rvahrhgari lvdaaqlaph apvdltaldv dyvalsghkl yapfgagvla
      241 gradwldaap pylagggats hvgaathevr wtagparhea gtpnllgava laavcealga
      301 adrdalhare qallarlrtg laalpdvvel rmfspeaprv givsfvvagr dsaevaahla
      361 srhrigvrdg lfcahpltrr llaeasartg rtdlpptalr aslglgttep evdtlltalt
      421 hlp
//
LOCUS       WP_457604195             503 aa            linear   BCT 27-JAN-2026
DEFINITION  PrsW family intramembrane metalloprotease [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604195
VERSION     WP_457604195.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Ho,T.D. and Ellermeier,C.D.
  TITLE     PrsW is required for colonization, resistance to antimicrobial
            peptides, and expression of extracytoplasmic function sigma factors
            in Clostridium difficile
  JOURNAL   Infect Immun 79 (8), 3229-3238 (2011)
   PUBMED   21628514
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..503
                     /product="PrsW family intramembrane metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54106
     Region          56..325
                     /region_name="PrsW"
                     /note="Membrane proteinase PrsW, cleaves anti-sigma factor
                     RsiW, M82 family [Signal transduction mechanisms];
                     COG2339"
                     /db_xref="CDD:441909"
ORIGIN      
        1 mrpdqwvagd yadrmadtpp gaapppphap aappgaptpr mplrrlgwrr flvlagvvll
       61 iaagalfmvf tlgeslgaea lligviaail pvpvlvfcfl wldryepepl kylifcfawg
      121 afvstaisll vntasaglfe drglpvalta vlvapfieel tkaagpllvl ifrrrefsgi
      181 tdglvycgls avgfamveni lylgghgyra gadeygpatg aqqviaifiv rillfgfahp
      241 lftsmtgvgl gvaartadrr vrvlaplagl llamilhgtw nllpslaqat gevvivlygy
      301 igvmvpiffa mvglavwlra wegrltertl pdyvragwlt ppevaalgsl grrhaartwa
      361 rrvagdggvr amrgyqfaat rlallrdgmr rgldrkpeer ertareerel ldaitayrsf
      421 fvgrdpqapv gvwdgqryhl rfpdgsqrpv eapddpvvpi pvvlaqppaf pqggygpggw
      481 hggpgghgpg gwhdpgapwh pgr
//
LOCUS       WP_457604197             239 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604197
VERSION     WP_457604197.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..239
                     /product="winged 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=25559
     Region          28..207
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
     Region          134..221
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(153,172..173,191,194,202..203,213,218)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mivellllvt aragepsavl paldllphsv rtaprdvrtl vsgptpdavl vdarselsea
       61 ratcrmlhat glgvplvavv teaglialna dwgvddvila gagpaevear lrlavgrlsn
      121 atagaggsir agelnidpdt yaaklkgrpl dltykefell kflaqhpgrv ftrdqllrev
      181 wgydyfggtr tvdvhvrrlr aklgseyesm igtvrqvgyk fvvppsrslp epeptplpv
//
LOCUS       WP_457604199             277 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604199
VERSION     WP_457604199.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 277)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..277
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30145
     Region          2..276
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtrlwsasrl tylaltlsai lsifpiywmf vvasrtsdtm gqvpppltpg gnlgtniarl
       61 fdntdayflt glinsaivat tvtisvvffs tlagfafakl rfrgrnalll vivatmmvpt
      121 qlgviplyll mtklnwndrl pavivpalvt gfgvfmmrqy agqavsteli eaarmdgcnt
      181 ariywnvvlp alrpaaavlg lltfmttwnd flwpyavlnd penptvqlsl ralsdgyyqd
      241 msqvftgtai atlplllvfv vfgrqiiggi megavka
//
LOCUS       WP_457604203             605 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604203
VERSION     WP_457604203.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..605
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64949
     Region          42..562
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 msrstagrls aerraddlrr lraerfdvlv igggvtgaga aldaasrglk valveardya
       61 agtssrsskl ihgglryleq lefhlvheal tergllatrl aphlvrpvpi lvplpaegga
      121 gdlprrffrr syygigvaay dafagifggg rgmplhrhlt regtrrifps lrpdklagai
      181 ryydgqvdda rlvvtlarta aslgatvvts aravgltrqa revtgvrvrd leapagspda
      241 efevrartvi aatgvwsddm srmlndvglr pklrvraskg vhlvvprsai vgetglilrt
      301 atsvlfvipw gghwiigttd tdwqldrshp aatasdidyl lsqvnmvldr plttadiegv
      361 yaglrpllag eadstsklsr ehavvepmlg lllvaggkyt tyrvmasdvv dramhrlgrt
      421 rssrtadlpl lgadgyaamw rdradlarrh gvavgvvehl lerygsltle llalvdadpl
      481 lgsplagape ylaaevtyaa raegalhled vltrrtrisi etshrglesa ehaaelmgav
      541 lgwdaatrdr evahyrarvl aeresqlmpd diaadaarlg apdvrgfaad rgtdgpgvel
      601 paspr
//
LOCUS       WP_457604204             551 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 27 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604204
VERSION     WP_457604204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Bhatia,S., Singh,A., Batra,N. and Singh,J.
  TITLE     Microbial production and biotechnological applications of
            alpha-galactosidase
  JOURNAL   Int J Biol Macromol 150, 1294-1313 (2020)
   PUBMED   31747573
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19064013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..551
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58667
     Region          44..327
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(51,86..87,128,169,171,205,227,231)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          339..413
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          429..550
                     /region_name="beta-trefoil_Ricin_XLN-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in Streptomyces olivaceoviridis
                     endo-1,4-beta-xylanase and similar proteins; cd23418"
                     /db_xref="CDD:467297"
     Site            order(440..443,453,455,458,462..463)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(449,480..481,482,492,494,497,499,501..502)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(467,471,473,480..481,492,494,497,501)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(523..527,536,538,545..546)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mrrwtrrtla vlgvaavala atvtdqavap rparaldngv artppmgwnt wntfgcnine
       61 tlirqtadai vsnglrdlgy kyvvvddcwf dpnrdsqgnl qahpqrfpsg mkslgdylha
      121 rgllfgiyqv pldktcaqvg gafpgatgsl nheyqdarqf aawgvdylky dwcsstgtin
      181 dqvarfgimr dalastgrpi vysinpnsyh aktgpqrnws dvanlwrtte ditnawntgq
      241 tngypmgiqn ivdvtvplag yaapggfndp dmlevgrggm ndtemrshfa lwavlaaplm
      301 mgndvrsana atlailrnan lvainqdtlg rqaaqvsfdg trrvlakpla ngdvavalfn
      361 qgsstttvst taaaagksgs sftlrdawtd atststgtis asvpahgtvv yrvsgggttt
      421 pppvpttfrl rsessgrcld vdnagtangt gtliwdchnn anqqftangq alqvlgkcld
      481 vptnatagtr vqiwdcnggt nqqwtingng tvsngrfpsl cldvdnagta ngtrvivwtc
      541 hgnanqrwsr a
//
LOCUS       WP_457604207             405 aa            linear   BCT 27-JAN-2026
DEFINITION  Dyp-type peroxidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604207
VERSION     WP_457604207.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Sugano,Y. and Yoshida,T.
  TITLE     DyP-Type Peroxidases: Recent Advances and Perspectives
  JOURNAL   Int J Mol Sci 22 (11) (2021)
   PUBMED   34074047
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Colpa,D.I., Fraaije,M.W. and van Bloois,E.
  TITLE     DyP-type peroxidases: a promising and versatile class of enzymes
  JOURNAL   J Ind Microbiol Biotechnol 41 (1), 1-7 (2014)
   PUBMED   24212472
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Sugano,Y.
  TITLE     DyP-type peroxidases comprise a novel heme peroxidase family
  JOURNAL   Cell Mol Life Sci 66 (8), 1387-1403 (2009)
   PUBMED   19099183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..405
                     /product="Dyp-type peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43006
     Region          62..392
                     /region_name="EfeB"
                     /note="Periplasmic deferrochelatase/peroxidase EfeB
                     [Inorganic ion transport and metabolism]; COG2837"
                     /db_xref="CDD:442085"
ORIGIN      
        1 mtgrrvsrrg lltggamaag galagagalt avrsgtpgvr pddavpvaqv gsaaepfhga
       61 rqsgvttdpq ahaafvaftl rpgtdraale rmlrllsdda arltqgrpal adtepelsvl
      121 parltvtfgf gpglyaaagl dgrrpasvad lpafgidrlq prwsggdlll qicaddpltv
      181 ahtqrvlvkd srpfavvrwv qqgfrraaga epgrtqrnlf gqldgtanpk pgtpadtavw
      241 vtdgpdwlrd sttlvvrris mnletwdllg rtdrelavgr rldtgapltg raehdepdfa
      301 algpdgltvi pdfshltrar vtddrqkilr rpynydgvpt pegtadsglv fasyqadiar
      361 qflpvqrrla erdllnewtt pigsavfavp pgcpeggwig sqllg
//
LOCUS       WP_457604212             349 aa            linear   BCT 27-JAN-2026
DEFINITION  endo-1,4-beta-xylanase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604212
VERSION     WP_457604212.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Chu,Y., Tu,T., Penttinen,L., Xue,X., Wang,X., Yi,Z., Gong,L.,
            Rouvinen,J., Luo,H., Hakulinen,N., Yao,B. and Su,X.
  TITLE     Insights into the roles of non-catalytic residues in the active
            site of a GH10 xylanase with activity on cellulose
  JOURNAL   J Biol Chem 292 (47), 19315-19327 (2017)
   PUBMED   28974575
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Xie,H., Flint,J., Vardakou,M., Lakey,J.H., Lewis,R.J., Gilbert,H.J.
            and Dumon,C.
  TITLE     Probing the structural basis for the difference in thermostability
            displayed by family 10 xylanases
  JOURNAL   J Mol Biol 360 (1), 157-167 (2006)
   PUBMED   16762367
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007844
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..349
                     /product="endo-1,4-beta-xylanase"
                     /EC_number="3.2.1.8"
                     /GO_function="GO:0031176 - endo-1,4-beta-xylanase activity
                     [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38609
     Region          1..331
                     /region_name="XynA"
                     /note="Endo-1,4-beta-xylanase, GH35 family [Carbohydrate
                     transport and metabolism]; COG3693"
                     /db_xref="CDD:442908"
ORIGIN      
        1 mgtavdmaal ndaaepryre laasefstvt aenvmkwesl eptrgtynwg padelidfar
       61 knnqrvrghv lvwhnqlpaw ltsgvadgsi skaelrqilr nhitavvthf kgkiwqwdvv
      121 neavsdpwdt pstlhykgfw aqnlgpsyia dafrwaraad pkallfyndy nieafgsgnp
      181 addktqfvyd mardlrakgv pidgvgaqgh lgtqygnfst lqvaaalrkf aglglatalt
      241 evdvrsqite gveagdsaei nprlqasaan fsvlmqacla erhclsftlw gftdkhswvp
      301 gafsdppegl atvydenyqp krayhemkad lifsgppyvl pripqhprr
//
LOCUS       WP_457604214             436 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604214
VERSION     WP_457604214.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..436
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46297
     Region          3..360
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mvmkrragav lalfvtsall asacsgggde ekaaeselyk kpvtltwwhn asqdgpgkty
       61 wekvakdfst ahptvkieie aietnqlqrt rlpaallsnd ppdifqawgg gemreqvead
      121 ylkditdqvk gevadignaa eiwqvegkqy glpyrmgieg iwynkdmfak agitappttf
      181 eelnaavtkl ktinvipial gagdkwpaah wwynfalrac svdtlkkatk drnfddpcfv
      241 kagqdlkafi dtkpfqnnfi atpgqndpts angllangka amelmgdwnr gtldtvatdk
      301 aalgkflgwf pvpaisgsag dpkaalgggd gfacsknapa ecveflkylv spevqkgyaa
      361 tgtglpvakg aadgvtdpal ksilqatsda tyvqlwldta ygstvgtamn daivaifagn
      421 gtpekvvsam kaaask
//
LOCUS       WP_457604220             180 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA 2'-phosphotransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604220
VERSION     WP_457604220.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Yang,X., Wang,J., Li,S., Li,X., Gong,J., Yan,Z., Zhou,H., Wu,C. and
            Liu,X.
  TITLE     Structural and biochemical insights into the molecular mechanism of
            TRPT1 for nucleic acid ADP-ribosylation
  JOURNAL   Nucleic Acids Res 51 (14), 7649-7665 (2023)
   PUBMED   37334830
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Banerjee,A., Munir,A., Abdullahu,L., Damha,M.J., Goldgur,Y. and
            Shuman,S.
  TITLE     Structure of tRNA splicing enzyme Tpt1 illuminates the mechanism of
            RNA 2'-PO4 recognition and ADP-ribosylation
  JOURNAL   Nat Commun 10 (1), 218 (2019)
   PUBMED   30644400
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Spinelli,S.L., Kierzek,R., Turner,D.H. and Phizicky,E.M.
  TITLE     Transient ADP-ribosylation of a 2'-phosphate implicated in its
            removal from ligated tRNA during splicing in yeast
  JOURNAL   J Biol Chem 274 (5), 2637-2644 (1999)
   PUBMED   9915792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..180
                     /product="RNA 2'-phosphotransferase"
                     /EC_number="2.7.1.160"
                     /GO_function="GO:0000215 - tRNA 2'-phosphotransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003950 - NAD+
                     poly-ADP-ribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006388 - tRNA splicing, via
                     endonucleolytic cleavage and ligation [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=19323
     Region          1..178
                     /region_name="KptA"
                     /note="RNA:NAD 2'-phosphotransferase, TPT1/KptA family
                     [Translation, ribosomal structure and biogenesis];
                     COG1859"
                     /db_xref="CDD:441464"
ORIGIN      
        1 mehrdlvrvs krlslalrhr pdtfglrldr agwvpvadvl aglrisraql davvvgndkq
       61 rfaveagpdg adriranqgh sipvdlgltp aappprlfhg tgeavldair aqglrrggrh
      121 hvhlspdvat arrvgarrgg avvvltvdaa amaeagylfy rsanwvwltd tvpppylstt
//
LOCUS       WP_457604221             434 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite oxidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604221
VERSION     WP_457604221.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Hsiao,J.C., McGrath,A.P., Kielmann,L., Kalimuthu,P., Darain,F.,
            Bernhardt,P.V., Harmer,J., Lee,M., Meyers,K., Maher,M.J. and
            Kappler,U.
  TITLE     The central active site arginine in sulfite oxidizing enzymes
            alters kinetic properties by controlling electron transfer and
            redox interactions
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (1), 19-27 (2018)
   PUBMED   28986298
REFERENCE   2  (residues 1 to 434)
  AUTHORS   McGrath,A.P., Laming,E.L., Casas Garcia,G.P., Kvansakul,M.,
            Guss,J.M., Trewhella,J., Calmes,B., Bernhardt,P.V., Hanson,G.R.,
            Kappler,U. and Maher,M.J.
  TITLE     Structural basis of interprotein electron transfer in bacterial
            sulfite oxidation
  JOURNAL   Elife 4, e09066 (2015)
   PUBMED   26687009
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Barber,M.J. and Neame,P.J.
  TITLE     A conserved cysteine in molybdenum oxotransferases
  JOURNAL   J Biol Chem 265 (34), 20912-20915 (1990)
   PUBMED   2249998
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Campbell,W.H. and Kinghorn,K.R.
  TITLE     Functional domains of assimilatory nitrate reductases and nitrite
            reductases
  JOURNAL   Trends Biochem Sci 15 (8), 315-319 (1990)
   PUBMED   2204158
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Neame,P.J. and Barber,M.J.
  TITLE     Conserved domains in molybdenum hydroxylases. The amino acid
            sequence of chicken hepatic sulfite oxidase
  JOURNAL   J Biol Chem 264 (35), 20894-20901 (1989)
   PUBMED   2687265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..434
                     /product="sulfite oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46804
     Region          104..425
                     /region_name="SO_family_Moco_dimer"
                     /note="Subgroup of sulfite oxidase (SO) family
                     molybdopterin binding domains that contains conserved
                     dimerization domain. This molybdopterin cofactor (Moco)
                     binding domain is found in a variety of oxidoreductases,
                     main members of this family are nitrate...; cd02110"
                     /db_xref="CDD:239028"
     Site            order(105..106,108,110,161,229,260,265,273,276,278..279)
                     /site_type="active"
                     /note="Moco binding site [active]"
                     /db_xref="CDD:239028"
     Site            161
                     /site_type="other"
                     /note="metal coordination site [ion binding]"
                     /db_xref="CDD:239028"
     Site            order(317,347,351,353,360,362,394,399..401,405,421)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239028"
ORIGIN      
        1 msqspspaea vhdadrsrqw lagqahgpgv drdrllevga amaavtaaaa erepvavasa
       61 pvgvdpgapi vkplpadllr pldtnaemrw psmagqgyvv pidrffvrnh tvtphldaat
      121 wrlrlfgdgl rgaptrdnpv efdldelrrl paeehaalle cagngrryfa eqqdeptpgv
      181 awglgsvgva rwrgvrlgtv lrlaglrdea vdvmpegldp dyvsggvnlg rvrrpmpvak
      241 alddvllaye mngeplppdh gfpvrvvvpg wvgissikwv gaievsttpl fspwntqfyr
      301 mfgpghpadg tvltaqpvrs afelpwdarv pageemlltg rswsgngpia hvevdtgdgw
      361 rpadlvaadr ggawqrwtvr wcppaagrhv lraratdctg avqpdraapn dlaylfdavv
      421 ahpvtacwpq lrwc
//
LOCUS       WP_457604223             225 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan recognition protein family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604223
VERSION     WP_457604223.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Dziarski,R. and Gupta,D.
  TITLE     The peptidoglycan recognition proteins (PGRPs)
  JOURNAL   Genome Biol 7 (8), 232 (2006)
   PUBMED   16930467
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Guan,R., Roychowdhury,A., Ember,B., Kumar,S., Boons,G.J. and
            Mariuzza,R.A.
  TITLE     Structural basis for peptidoglycan binding by peptidoglycan
            recognition proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17168-17173 (2004)
   PUBMED   15572450
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Steiner,H.
  TITLE     Peptidoglycan recognition proteins: on and off switches for innate
            immunity
  JOURNAL   Immunol Rev 198, 83-96 (2004)
   PUBMED   15199956
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Dziarski,R.
  TITLE     Peptidoglycan recognition proteins (PGRPs)
  JOURNAL   Mol Immunol 40 (12), 877-886 (2004)
   PUBMED   14698226
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..225
                     /product="peptidoglycan recognition protein family
                     protein"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0016019 - peptidoglycan immune receptor
                     activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045087 - innate immune response [Evidence
                     IEA]"
                     /calculated_mol_wt=23879
     Region          69..206
                     /region_name="PGRP"
                     /note="Peptidoglycan recognition proteins (PGRPs) are
                     pattern recognition receptors that bind, and in certain
                     cases, hydrolyze peptidoglycans (PGNs) of bacterial cell
                     walls. PGRPs have been divided into three classes: short
                     PGRPs (PGRP-S), that are small (20...; cd06583"
                     /db_xref="CDD:133475"
     Site            order(76,113,196,202,204)
                     /site_type="active"
                     /note="amidase catalytic site [active]"
                     /db_xref="CDD:133475"
     Site            order(76,196,204)
                     /site_type="other"
                     /note="Zn binding residues [ion binding]"
                     /db_xref="CDD:133475"
     Site            order(77..78,109,113,127,144..145,150,196,202..204)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133475"
ORIGIN      
        1 msvpvprrtv lrgavllgaa aagvgaltqi gsgpgaraaa trvdqptian catwgarpps
       61 spvsvvtsrp nkiivhhtaf pnttdyslaq ayrnsrdiqn lhmdgngwld sgqhftnsrg
      121 gyltegrhgs lyallhgqtm vqgahcvgqn sqaigiendg iyvdvqppqa lwnslvtfca
      181 ftcqqygiap teiyghkdfn ntqcpgllhd rlpelrrtva arlgg
//
LOCUS       WP_457604224             447 aa            linear   BCT 27-JAN-2026
DEFINITION  pectate lyase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604224
VERSION     WP_457604224.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wu,P., Yang,S., Zhan,Z. and Zhang,G.
  TITLE     Origins and features of pectate lyases and their applications in
            industry
  JOURNAL   Appl Microbiol Biotechnol 104 (17), 7247-7260 (2020)
   PUBMED   32666183
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Hugouvieux-Cotte-Pattat,N., Condemine,G. and Shevchik,V.E.
  TITLE     Bacterial pectate lyases, structural and functional diversity
  JOURNAL   Environ Microbiol Rep 6 (5), 427-440 (2014)
   PUBMED   25646533
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Marin-Rodriguez,M.C., Orchard,J. and Seymour,G.B.
  TITLE     Pectate lyases, cell wall degradation and fruit softening
  JOURNAL   J Exp Bot 53 (377), 2115-2119 (2002)
   PUBMED   12324535
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Yoder,M.D., Keen,N.T. and Jurnak,F.
  TITLE     New domain motif: the structure of pectate lyase C, a secreted
            plant virulence factor
  JOURNAL   Science 260 (5113), 1503-1507 (1993)
   PUBMED   8502994
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Linhardt,R.J., Galliher,P.M. and Cooney,C.L.
  TITLE     Polysaccharide lyases
  JOURNAL   Appl Biochem Biotechnol 12 (2), 135-176 (1986)
   PUBMED   3521491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..447
                     /product="pectate lyase family protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0016837 - carbon-oxygen lyase activity,
                     acting on polysaccharides [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47188
     Region          65..445
                     /region_name="PelB"
                     /note="Pectate lyase [Carbohydrate transport and
                     metabolism]; COG3866"
                     /db_xref="CDD:443075"
ORIGIN      
        1 mrtrtaavaa laaalvltta apapaapgkp sraaeligrq tlpandgwaa agtgttggsa
       61 aapdrvhvvr traelvaalg gdnatnaada tpkivyvagt vdgfegpdgt lldcadladp
      121 eyslpaylaa ydpatwgrvn psgpleaarv rsvaeqtrqt qinvgsntti vglrgarltg
      181 ltlmidrvan vivrniefad ardcfpawsp tdgdtgnwns qydqisvrrs ehvwidhntf
      241 tdgdnpdsaq pvyfgrpwqv hdgsvdvtht aslvtvswnr ftgrdkvmli gssntvgpdv
      301 grlnvtvrhn lfdgtlqrlp rvrfgqvdvh enhyqlggpg fayalgvgvq salyaennff
      361 tltgdtgpad llydwggtal tergswvrqg drlprpvdll aaynaahdpd lggdagwtpt
      421 lraarplpap lvpfvvdafa gagrlpl
//
LOCUS       WP_457604226             388 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604226
VERSION     WP_457604226.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..388
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40801
     Region          4..271
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msgndpprva liganghgrw hrrtiaelha agrarlvalv dvrplehepe apvppetgvl
       61 tdhrdmlaes rpdvvvictp phthlpiald vlaagadlll ekppvldlae hrtlaeaaaa
      121 agravqvnfq algsaaltel tgalgrlgpv tgiatlaawq rpdayyarsp wagrlsvdgh
      181 paldgalanp lahalmqcla vaesvtgapv rparievery rvrpievddt tvlrltpnag
      241 ppvlaaltla aeehvpgevl vtgehgrall eyptdrlrlp gddaprpvpg rrgllanlld
      301 hrtdgtplia plartepfta vldalrdapv ptlldgdlvr eagdgpqrvr mvrgvgavlr
      361 aaaetgalps eagvpwavkp yvvdlpvq
//
LOCUS       WP_457604227             494 aa            linear   BCT 27-JAN-2026
DEFINITION  mannitol dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604227
VERSION     WP_457604227.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="mannitol dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=51394
     Region          7..491
                     /region_name="MtlD"
                     /note="Mannitol-1-phosphate/altronate dehydrogenases
                     [Carbohydrate transport and metabolism]; COG0246"
                     /db_xref="CDD:440016"
ORIGIN      
        1 maltpdrlgl atlrhlppes rplvrpgtvp agivhlglga fhrahqavht eaavgaaggd
       61 wgiigvaprs tdvvealdaq dclfsvttla aegaatrvvg alagvrhaas dpdavvglla
      121 dpairvvtlt vtekayrldp vtaaltvdad ltadlttgrp prtvpgllvr gllaraaada
      181 gpialvscdn lpangrrlrg lveqglalar vpdataervl aavtcpgtmv drivpastde
      241 trdtarqalg vtdlaavaae pwsqwviedd fpggrpawer sgailtgdag pwerlklral
      301 ngvhsatayl galagaetva ealtlphlda vlrrllaeei apsftpppga dvaeygeqvl
      361 arfgnpairy rttqvamdgs qklpqrvlht vadlraagrs arwsalvvaa wlrfllgyad
      421 dgrplplddp ladrlraala agahtpagvv davfalrevf padlaaddef radvtgwlta
      481 lerhgvratl agar
//
LOCUS       WP_457604230             442 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604230
VERSION     WP_457604230.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..442
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48503
     Region          7..>227
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mspparervr halvgagara emfvralald hadtaelval advnqirmda hnrwlaelgh
       61 ppvptyaaad vtamlakerv dvvlvtsvda thdeyvtaal ragcdvvvek pmtvdaercr
      121 rildavaetg rrvtvafnyr ynplheqfrr lladgavgei gsvhfewlld vrhgadyfrr
      181 whrdksvsgg llvhksghhf dlvnwwldar pvevhaygrl ffygedgrrh gyardydrah
      241 gspaadgdpf alrladhprl relyldaeae dgyhrdrnvf apgvtieddl avlarydtga
      301 tmtyhltaya pwegyrvmvn gsrgrlelev tesdhvspsv agalkgaalh gdeaaveqga
      361 arltlrpfwa ppqeipvegw trrghggada rmtrvllgge pdplgraata rdgalalltg
      421 laanrsletg apvrvadllt lp
//
LOCUS       WP_457604232             120 aa            linear   BCT 27-JAN-2026
DEFINITION  fluoride efflux transporter FluC [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604232
VERSION     WP_457604232.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..120
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11924
     Region          2..119
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mtvllialga aigaplrylt dravqsrhgs pfpwgtltvn vagslllggl laapvgpgvt
       61 alagtgfcga lttwstlsye tlrlartgkr rlayanvals vvaglgaafl gyalvaalsg
//
LOCUS       WP_457604231             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604231
VERSION     WP_457604231.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41346
     Region          23..382
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(33..34,37..38,41,73,127..128,130..132,135,154,
                     157..158,161,236,239..240,243..245,248,276,280,329..330,
                     334,338,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msstidapag krppapravl tarngvavvf alnglavasw fsrvpaarea ldlspsrlgl
       61 lllcvsagsl lamptaglva qrlgpartva vsvvlvtlgl tgagfaasla gsvvgvgfgl
      121 aafgfgsglc dvamnvegaa vekrlgrtil prfhaawslg svagaglgag aarldvpvgv
      181 hlpvlsvlvl vgtllgaraf laapaeaagd gqpaarrral laawreprtl lvgllvlvma
      241 ftegsandwl avafvdgygv deavgaavfg vfvvgmtlgr tvgtvaidrw grvpvlyati
      301 atasagaala vlagsgplav vgvalwglga slgfpvgmsa aaddedkapa rvsvvavigy
      361 taflagppll gflgdhfgvl salgvvplll lptlalvpvl rerpaapdaq agapaakag
//
LOCUS       WP_457604235             218 aa            linear   BCT 27-JAN-2026
DEFINITION  CatB-related O-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604235
VERSION     WP_457604235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..218
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23452
     Region          56..186
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(67,81..82,87,89,91,120,122,125,144,160,168)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(80..81,83,92..93,122,125,142..143,148,156,158..159,
                     161,165)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(81,83,112,122,125,130,142..143,148,156,158..159,161,
                     165)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 mtpdprtvhp lpafdrvvfl kplvrspkiv vgdytyyddp ddatgfehrn vlyaygperl
       61 vigkycaias gtrflmagaa hpgmgvstyp ftmfggewae qtldivtamp srgdtvvgnd
      121 vwfgfgslvm pgvrigdgav iatgpvvtad vppytivggn parpirqrfd dadivrlrra
      181 awwdwptglv tahartimag tpaeiariaa ehgveqpg
//
LOCUS       WP_457604237             210 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604237
VERSION     WP_457604237.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..210
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21597
     Region          5..210
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mtgpvdaivf dmdgtlvesh avvpaayraa vragggpsyt daeviagysi gspadllahl
       61 lrrpasgedl dryhteldvl agrvrvypgv adalaeiaar vpvgvftgas hraaeilldr
      121 agllghfevv lggdqvdrpk papdgveaac rrlgvppgra ayvgdspldv raarrsgava
      181 vaaawghqyd pdepadlsls rpgellallg
//
LOCUS       WP_457604238             520 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604238
VERSION     WP_457604238.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55348
     Region          18..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtdrpnyvhe alelfagfgd realvgggrr ltypqvaaqv rglaaalrhh gvrpgaavlv
       61 mlgntvegpl lqlalhllgc rsmwvapvts rrevdefval sapeafvhdp rdaqavevaa
      121 glsgvpvlcl gpggagpdlt tevagpaael paevpapesi lqtsgttgtp klvhhresfy
      181 rqvlalaadf rgagfpllrh lshspmwlas gqittlinlf tggvlflreq wdpaafvatv
      241 daerltstfv tppmlyevld hpdlpgadfs amfmfnvgag paaparlrqa iarfgpclri
      301 vyglseavvi calpgltedp ehperlrscg rpygdvsvei rdaggrvlpa gedgevwvrt
      361 klsfagyhgq peltaetlvd gwvrtrdigh ldadgylylv drlqdriltr qrswpiysrp
      421 iedvlaghpe vraaavigvp dpvagelpha yvvpapgasv tgeelialvv relsetwapg
      481 avefvdalpl nqsakvdkra lraryaaahp agadpigspa
//
LOCUS       WP_457604239             367 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-hydroxy acid oxidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604239
VERSION     WP_457604239.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 367)
  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 12014085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..367
                     /product="alpha-hydroxy acid oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37194
     Region          29..322
                     /region_name="FMN_dh"
                     /note="FMN-dependent dehydrogenase; pfam01070"
                     /db_xref="CDD:426029"
     Site            order(32,114,136,164,171,239,263,266,318)
                     /site_type="active"
                     /db_xref="CDD:239203"
     Site            order(32,136,171,263,266)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239203"
     Site            order(114,136,164,239,263,266,318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239203"
     Site            order(136,171,263)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:239203"
ORIGIN      
        1 madpadgfvp paslaelaal aravlpadvw dfvdggsgte talaanraal drvavlprml
       61 agvddpstea tlpggraalp vavapmayqr llhpdgepal aaaaraagvp yvastlsstp
      121 ieeiaatgat vwfqlywlrd ralvadlldr aeaagcaavm vtvdvpvlgr rlrdarngfa
      181 lpphvtaanl pggrddlahq gtpgvsavav htgavfapal swadlewlra rtrvpllvkg
      241 ildprdavra adagsdavvv snhggrqlda apasaavlpe vvaavdqrca vlldsgvrgg
      301 vdvlralalg adgvllgrpl lwalaaggra gaeaalalla aelrdalils gcpdpasarr
      361 lrtrigg
//
LOCUS       WP_457604241             447 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604241
VERSION     WP_457604241.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..447
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47756
     Region          <26..426
                     /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 mepvdlavsa lhgsvgdpal nsmnflneva qhypdavsla agrpyeeffd sallhthldr
       61 frrhlaeevg ldragvdrtl lqygrtkgiv hhliarhlav degltvdpes ivvtvgcqea
      121 mflvlralrt gpadvlfava ptyvgltgaa rlvdlpvrpv aggpdgvdla dlragvrrar
      181 aeglrprgcy vmpdfanpsg vsmdteqrrr llelaaeedl lliednpygl fpadgtdrrp
      241 tlkaldtarr vvylgsfakt vlpgarvgyv vadqrvgead gtvvpfadhl akiksmvtvn
      301 tspisqavig gallahdcsl vaanvreraa yarnlrhlad glarrfpagg pvswtvpagg
      361 ffvvvsvpfa vddallhrsa reygvlwtpm ahfydagtpv dalrlsvsav tpesidlgld
      421 rlaalvtdtm adrvtpecqg sgtvrvs
//
LOCUS       WP_457604253             491 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604253
VERSION     WP_457604253.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..491
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51021
     Region          78..491
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mvhadqvllh rlllvtgrpr aalspstrtt darfdtpgrv npagsgvrrr vrrhrvvvvg
       61 agfsglacal aldaagaevr vleardrvgg rtlsrplpgg gwldlgaqwi gptqdrmyal
      121 vaayglttfs spahgaaall lggrpatgep pglsallgtl demaggldpa apwrvddaar
      181 wdritlggwl dasaadpvta gyagrmlagg llaaspdevs llhmlfylrs gggtgsllrm
      241 aggaqqdrlv ggpaalaerm aaalppgslc lrapvdgvaq dgdgvrvrag reayrgdavv
      301 ialaptlagr irydpplppl rdgltqrmpm gvalkvhaly pepfwradgr sgvsstdtgp
      361 ltetvdnslp dapggvltaf sygaqaralr rlpqdarrda lcealaaifg paaarpddlv
      421 eydwsadewt rgcfcgvlpp gawcaygpel rapvgrvhwa gtetatrwsg ylegavtage
      481 raaaealaql g
//
LOCUS       WP_457604256             711 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604256
VERSION     WP_457604256.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 711)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000903
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..711
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73742
     Region          28..325
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
     Region          371..670
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
ORIGIN      
        1 mppstdpapa eptaadrker iirsvalfvm pflmvtmmfa tyvgtmhsph prqmpvavig
       61 sgaeaqgvvd alnaaagepv earlvasrda avellrdrei sgalqlpvag sdqatiitas
      121 aagasragta qqllapvavq qqwasttedv aplpdddrag isvlfaamgm mlagyvplsm
      181 llmatphllr lrrfvplaag wsaltstiiw lilgpgvgav dghyltflgv gmlttgavgl
      241 aqllftkvmg plavllgmlf fvvlgmpasn lalpvdtmpg ffqflhgvlp lpaagealrs
      301 alyfdgrgig vhlltlaawi vaavllcllk erggapipqa pqvdgpdtpl palaggpprs
      361 krfryvtvaa fplsilvavv glmsfsmhkp ephdipvavv aavpeqaeqv aaglraglgg
      421 vadvsvaasv dearerilaq dlvaayvlpa tpggeatlys ssaagssqhm ivqtmfrqva
      481 agqqtplavt dvaplsrtdt mgsnslyvgm swimsgflml avlrggaphl rrlrqflpil
      541 ggwaigmatw lwllfdviig avdgsalemi gfgaltifav ssvtgvftrt fglaaivpmm
      601 vvlmmagvpa sggglsiymv peffrtlqgv lplpaavdta rsltyfdgvg vgrnlavvai
      661 waavglllnl gvdwwlrrre rtaggtgphp apdtsggldg ivgepapaga r
//
LOCUS       WP_457604259             269 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604259
VERSION     WP_457604259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..269
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28257
     Region          53..265
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mastltrrtl lgaaagvaga avvgglaarq lsgprpgpap alpdapagde rliriasgar
       61 grevdfwtav pegygdgrgl pvclvlhgas atprdygrfg larfltdavr rgappfalag
      121 atggrlswra agdddpqrmv reevptwcar rgfdssrlav wgwsmggfga lllaetypkw
      181 lrmtaafspa vsagdavftg verlrgtpvg lwcgrqdnfl kdvralaral peepvraawa
      241 dgrhnfgywg tvipdafali gaalnpprt
//
LOCUS       WP_457604265            1081 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604265
VERSION     WP_457604265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1081
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111700
     Region          4..981
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msllarfsla nrglialval vttafglfav pslkqqllps lefpaafiva typgaapeiv
       61 esqvaepien slqgipgldk vtstsregaa tvqvqyefgt dlddvvnkme talnridsql
      121 pegvdpqvia gstddlpavv vaatgdgder alaeklrnav vpelealdgv rsvdvtgarn
      181 qvvtitpdpa klaaakvapt aiasalksng vavpagalad gdrslpvqvg tpirtiddlr
      241 givlttapaa pvrlgdvaav eqqlapatsl trtngkpslg iavtaapdgn avdishdird
      301 rldelgdaag aeltvvfdqa pfveksiesl ttegllglvm avvvilvfll svrstvvtav
      361 siplsvlval ivlwagdysl nlltlgalti avgrvvddsi vvlenikrhl eygepkrdai
      421 ltavrevaga vtastlttva vfapialvgg fvgqlfapfa itvtvalias llvsltvipv
      481 laywflrprg gaddaaarra aeekelrnpl qraylpvidf atrsrktrwa tvglgllvll
      541 gtfglaqkle tnflddsgqd tlairqempa gtslagtdra aarveevlrr tpgvetyqvs
      601 agggdnpfag ggsdqatwsl slsddtdaaa vrqglrkefd algpevgelt fgggqnasan
      661 qvevvvqaad qetltraaea vrgamagtpg vedvtsslat qvprvevtvd rvaaaraglt
      721 eaavgqlvaq tyrgaplgqv tldgtaqsvv lssgarpplt vdelralrvg avpldaiadv
      781 eqvdgpqqvt ridgersvsv tgtatgsnlg attqelqkrl daldvpgaty viggvsadqa
      841 dafadlglav laaiaivfli mvatfrsltq alillisvpf aatgaiglll vtgtplgvpa
      901 ligvlmlvgi vvtnaivlld linqyraqgm dvteavvegg rrrlrpilmt avatifallp
      961 malgltgegg fiskplaivv iggllsstll tlvlvptlyt mvehtkgsfr nrgrggapep
     1021 vepqpepdpv pvavgggert eergvvappp arpsgalvdg tdqfevlrlp ksrqsplppt
     1081 e
//
LOCUS       WP_457604266             131 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604266
VERSION     WP_457604266.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 131)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..131
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14553
     Region          4..117
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mfvfrldtrs gvppylqlvq qvrqavllgf lqpgdrlpli revvedlain pntvakayrq
       61 meqenlatgr pgqgtfvneq qsaamsasty tslrrgletw lrrayaagld eqavdalfts
      121 vrqqtrnedv a
//
LOCUS       WP_457604269             298 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604269
VERSION     WP_457604269.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..298
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31216
     Region          1..298
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrfglfgtgy waaethaaai eahpraqlag vwgrnpakae elatrhgvpa ftdvdalida
       61 cdavavalpp dvqadiavra atagrhllld kplaldlada drvvdaaqas gvasvvfftq
      121 rfhpnvtgfl astaaaggwq haratmfasi fqpgnpygds twrrergalw digphalsli
      181 lpvlgrvtrv aamdgpsglv hlllthdgga tsslsltlda pseavtrdfv ffgengteiv
      241 ppgdgsalqa fgaaldqlle evdagtrdhr cdvrfgrevv avldaaqtar aqgrtvem
//
LOCUS       WP_457604273             248 aa            linear   BCT 27-JAN-2026
DEFINITION  YidC/Oxa1 family membrane protein insertase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604273
VERSION     WP_457604273.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Hennon,S.W., Soman,R., Zhu,L. and Dalbey,R.E.
  TITLE     YidC/Alb3/Oxa1 Family of Insertases
  JOURNAL   J Biol Chem 290 (24), 14866-14874 (2015)
   PUBMED   25947384
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Keil,M., Bareth,B., Woellhaf,M.W., Peleh,V., Prestele,M.,
            Rehling,P. and Herrmann,J.M.
  TITLE     Oxa1-ribosome complexes coordinate the assembly of cytochrome C
            oxidase in mitochondria
  JOURNAL   J Biol Chem 287 (41), 34484-34493 (2012)
   PUBMED   22904327
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Funes,S., Kauff,F., van der Sluis,E.O., Ott,M. and Herrmann,J.M.
  TITLE     Evolution of YidC/Oxa1/Alb3 insertases: three independent gene
            duplications followed by functional specialization in bacteria,
            mitochondria and chloroplasts
  JOURNAL   Biol Chem 392 (1-2), 13-19 (2011)
   PUBMED   21194367
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ravaud,S., Stjepanovic,G., Wild,K. and Sinning,I.
  TITLE     The crystal structure of the periplasmic domain of the Escherichia
            coli membrane protein insertase YidC contains a substrate binding
            cleft
  JOURNAL   J Biol Chem 283 (14), 9350-9358 (2008)
   PUBMED   18234665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..248
                     /product="YidC/Oxa1 family membrane protein insertase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0032977 - membrane insertase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25714
     Region          38..244
                     /region_name="YidC"
                     /note="Membrane protein insertase Oxa1/YidC/SpoIIIJ [Cell
                     wall/membrane/envelope biogenesis]; COG0706"
                     /db_xref="CDD:440470"
ORIGIN      
        1 mlafaplhsa aaaaatvvtw ladvlapltg gaataaaivl ftvavrllis pltvaqvrge
       61 rrrtalapev relqrryadd parlqselfa lyrnagaspv agclpallqa pfflvmyrlf
      121 atgdgapell gerlagvplg whlgdglagp vplvfgvlla allalawwss rrmrraaaat
      181 gtvagtpaeg pgaavlgrvl pllpygtvlv alvvplaavl ylvtttawta leqvvlrrpq
      241 paaaidkr
//
LOCUS       WP_457604275             269 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604275
VERSION     WP_457604275.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..269
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=28963
     Region          2..267
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtihrl aarhaelfag dkvhadspqg rfaegaarls gtvldgteay gkhllhhyag
       61 eltlhvhlgl ygkfadgpge ppapvgqlrl rlhsdrhwle lrgptacell tppevaalrd
      121 rlgpdplrad adpdrayari rrsptplaal lldqsvvagt glifvtealf raglppllpg
      181 reltpagwae lwadlvmlmt ravergridt vrdadlpeat graprvdrhg gevyvyrrpg
      241 apchvcgtav srgalagrnl ywcptcqag
//
LOCUS       WP_457604281             370 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate/propionate family kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604281
VERSION     WP_457604281.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=39086
     Region          2..369
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msrilvlnsg sssvkyrlyd gddvldkgtv ervgepgggp adhesavrei igrldltglt
       61 gvghrvvhgg rkfsapvrid davvaaiedl vplaplhnpa nlagirvare alpdvpqvav
      121 fdtafhhtlp eaaatyaidk aiaeqygvrr ygfhgtshay vsrrvadlld rpydqlntit
      181 lhlgngasac avqggrsvat smgmsplegl vmgtrsgdld ptvifhlrre ggmvvddidd
      241 llnhrsgllg ltgvndmrev larrdagdpd atlafdvycr ritgyvgayy allgrvdaia
      301 ftagvgehaa pvraaslagl erlgvavdpa rndghgdrlv spdgaevavl vvgtdeerei
      361 aretrevlgv
//
LOCUS       WP_457604282             321 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604282
VERSION     WP_457604282.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..321
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32923
     Region          56..301
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrrrpaalit aavlgaaltg cseqptapag rpapdvppts atpaprvpag kaptesfavg
       61 vrqvklnrdg drplpvtlwy paagaaggav ersapaadgr fpvvlfshgl sarpedyqal
      121 ltrwaaagfv vaaprfphts rgtdgnpldv lnqpadvsyv ltrvlalgek agdplrgrld
      181 pervaatghs aggvttiglf tagrderlda givfagtalg vgtafsgaaa pqlfvhgead
      241 evvsyaagka vydvvpwpka mlslpkgdhg rallgdgkal gvvadttvef lrwtlygdpa
      301 akkrlpadaa rgnlatlddr l
//
LOCUS       WP_457604283             391 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent malic enzyme [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604283
VERSION     WP_457604283.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Alvarez,C.E., Trajtenberg,F., Larrieux,N., Saigo,M., Golic,A.,
            Andreo,C.S., Hogenhout,S.A., Mussi,M.A., Drincovich,M.F. and
            Buschiazzo,A.
  TITLE     The crystal structure of the malic enzyme from Candidatus
            Phytoplasma reveals the minimal structural determinants for a malic
            enzyme
  JOURNAL   Acta Crystallogr D Struct Biol 74 (Pt 4), 332-340 (2018)
   PUBMED   29652260
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tao,X., Yang,Z. and Tong,L.
  TITLE     Crystal structures of substrate complexes of malic enzyme and
            insights into the catalytic mechanism
  JOURNAL   Structure 11 (9), 1141-1150 (2003)
   PUBMED   12962632
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Xu,Y., Bhargava,G., Wu,H., Loeber,G. and Tong,L.
  TITLE     Crystal structure of human mitochondrial NAD(P)(+)-dependent malic
            enzyme: a new class of oxidative decarboxylases
  JOURNAL   Structure 7 (8), 877-889 (1999)
   PUBMED   10467136
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Goward,C.R. and Nicholls,D.J.
  TITLE     Malate dehydrogenase: a model for structure, evolution, and
            catalysis
  JOURNAL   Protein Sci 3 (10), 1883-1888 (1994)
   PUBMED   7849603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..391
                     /product="NAD(P)-dependent malic enzyme"
                     /EC_number="1.1.1.40"
                     /GO_function="GO:0004471 - malate dehydrogenase
                     (decarboxylating) (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0004473 - malate dehydrogenase
                     (decarboxylating) (NADP+) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=39901
     Region          14..369
                     /region_name="SfcA"
                     /note="Malic enzyme [Energy production and conversion];
                     COG0281"
                     /db_xref="CDD:440050"
ORIGIN      
        1 mssstpdpad pvfrlhvggk mavastvplt sredlslayt pgvarvceai aadpglvdty
       61 twvshtvavv tdgsavlglg nigpraalpv megkavlfkq fagvdavpvc ldtqdvdeiv
      121 atvkalapsf gginledisa prcfeverrl dealdipvfh ddqhgtaivv laalrnaaal
      181 lnrklgdlrv avsgagaagv avtkmliagg vdpdrvvvcd srgiigrhre ltgtkaelae
      241 ltnaegrqgd itealrdadv lvgvsggqip eaavagmapg givfalanpt pevhpevaar
      301 hvavvatgrs dypnqinnvl afpgvfrgal dagatritds mkvaaadaia gvvaesltad
      361 aivpspldpr vapavaeava eaarrdgvar r
//
LOCUS       WP_457604284             623 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 39 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604284
VERSION     WP_457604284.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 623)
  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 623)
  AUTHORS   Ernst,J.F. and Prill,S.K.
  TITLE     O-glycosylation
  JOURNAL   Med Mycol 39 Suppl 1, 67-74 (2001)
   PUBMED   11800270
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 623)
  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 623)
  AUTHORS   Gentzsch,M. and Tanner,W.
  TITLE     The PMT gene family: protein O-glycosylation in Saccharomyces
            cerevisiae is vital
  JOURNAL   EMBO J 15 (21), 5752-5759 (1996)
   PUBMED   8918452
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474915
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..623
                     /product="glycosyltransferase family 39 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65281
     Region          1..>168
                     /region_name="COG5305"
                     /note="Uncharacterized membrane protein PF0508, contains
                     N-terminal glycosyltransferase domain of PMT family
                     [General function prediction only]"
                     /db_xref="CDD:444104"
ORIGIN      
        1 mrrfapasvr srpgpvvwvi pglltlavtl tgighaqpwr delatwsaav rpvpdlvrmt
       61 rtidaatgpy yllmhgwtal agasptalrl psalamavaa altarlgaml vgsragllag
      121 llfavlpvts rygqearpya latlfavlat lllvealrrp twrrwagyal avaalallhl
      181 ialtllaaha vvvlltaarg paavvdppgr sraempdasr pcrrhpwrst qprdrapver
      241 hgchgapqtp aalhpatrss aggtprvsph pgsrehgtda peaerqdvtg earegsapgr
      301 rvlagwllal vpvvvlvtpl alvargqrgr qldwvdparl pdlaalpgal aqsgvvggfv
      361 lalaalgaar lgrrallpva avllpvvlvf aagtivplwv trylvftvpf acvlagaala
      421 aarvtpapar tpgtatpaep ertatpaaag rtaapaeaeq gptsprgrta agiavvvlag
      481 llglpdqval rrthewprsa pvdyagaagi iraeqrpgda ivysprdgwl fpdlgmayhm
      541 grrlprdvlv vrdqrqdasl wavecddpar clagvdrvwl vvtgrrpdpp aavpgakgda
      601 lragytvrqv wprpgitval lvr
//
LOCUS       WP_457604291             711 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase UvrD2 [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604291
VERSION     WP_457604291.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..711
                     /product="ATP-dependent DNA helicase UvrD2"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /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:0008094 - ATP-dependent activity, acting
                     on DNA [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000725 - recombinational repair [Evidence
                     IEA]"
                     /calculated_mol_wt=76841
     Region          11..573
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          628..695
                     /region_name="HRDC"
                     /note="HRDC domain; pfam00570"
                     /db_xref="CDD:425755"
ORIGIN      
        1 mgvhsaaerv lagldpeqrs avtapagpvc ilagagtgkt ravtsriayr altgdiagrh
       61 vlavtftara aaemrsrltv lgvqgvqart fhaaalrqvr yfaprllagr ampelldskv
      121 rvvtlaaakv glradraaar dlsaeiewak sslvepgeyv vaaakalret pyeparvadv
      181 fdayerlkrg ngvidfedml raavwgieeh pdvaeqvrnq yrhfvvdeyq dvnplqqrll
      241 eawlggrddl tvvgdasqti ysftgatssy lvdfprlhrg atvvrlvrdy rstpqvvgla
      301 navisqargt earlrlelhg qrrpgpepel riftdepaea navaarcral vaggtparei
      361 avlfrtnaqs eayekalsea gvpyvlqgae rfferpevrq amialraatr sadagtplpa
      421 avvealtavg wapdapppgg aarerweala alvqlaeeya aqaeeepglt gfteelarra
      481 aqqhvptveg vtlaslhsak glewdavflv glaegtlptt yaktmeqvee errllyvgit
      541 rarewlwlsy atarspggra rrpsrflpql drsgggerag gggparraer raerrrpqvv
      601 scricgatll agadrklgrc ptcpsdidee lyerlrewrq rvagaqkvpa yvvftdatlt
      661 alaerkpgrt eelvaiagig prkvglygdt vlalvagatv devcpqktse n
//
LOCUS       WP_457604293             436 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604293
VERSION     WP_457604293.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..436
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47671
     Region          1..435
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mptrrakipa tkypverftl dnglrvvltp drsapvigva vvydvgirse pegrtgfahl
       61 fehlmfqgse nleklahfrh vqgaggtfng sthldytdyf etlpanaler alfleadrmr
      121 gprlteenlr nqvdvvkeei rvnvlnrpyg gfpwltlppv mfdtfpnahd gygsfvdles
      181 atvadaadff rryyasgnav lavsgdidva eattlierhf gdvparpapq rpdfaepdlt
      241 aerrstytda laplpavaga wrvpdpisdf agylpyvvla evltdgdasr lverlvqrdr
      301 svtglggylg fmgdpfdvrd ptalllqahl ppggdvdkvl rtvdeeldrl aadgltdgel
      361 artqarmath llrdtdavlg ralrmavleq qrgepgllnd lprlvgevte eqvraaaaal
      421 rperraavev vpggar
//
LOCUS       WP_457604294             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604294
VERSION     WP_457604294.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (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   4  (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   5  (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   6  (residues 1 to 353)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (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   8  (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 10194283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..353
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37018
     Region          43..261
                     /region_name="PBP2_NrtA_CpmA_like"
                     /note="Substrate binding domain of ABC-type
                     nitrate/bicarbonate transporters, a member of the type 2
                     periplasmic binding fold superfamily; cd13553"
                     /db_xref="CDD:270271"
     Site            order(50..51,84,129,151,157,187,204..205,208,235)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270271"
ORIGIN      
        1 mrglplrrlv tlatlaavga atlgttaacg edsdaaagsg pvtlrlgyfp nithapavvg
       61 vekgifkekl gsdveletkt fnagpaaiea vfsgaldaty igpnptvnaf skskgeavrv
      121 isgaasggva lvvkpgitsv eqlrgkkiat pqlgntqdva lrfwlkekgl ettkegggdv
      181 kivpqenaqt vetfgsgaid gawvpepfvs rlvnaggkvl vderdlwpdk kfvitnllvs
      241 tkflkahpdv vkklvegqva anefvntkpd eaqqaisdhi gkitgkpldl klikqawptl
      301 eftndpipss lktgldhava vgltqpvdln glydlkylne vlktqgkaev sqp
//
LOCUS       WP_457604296            1134 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604296
VERSION     WP_457604296.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1134)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1134
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=122335
     Region          42..908
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          930..1134
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mtvqpalfga satpaprtad agprytpvel arllrlpapt reqaaiiaap vepllvvaga
       61 gsgktetmaa rvmwlvansy vrpehilglt ftrkaagela hrvrtrldql irrlgrqgrd
      121 phddplagep tvstyhsyag rivtehglra gyepttrllt easrwqlvdl lvrnydgdms
      181 evdrmpstit davlalagel dehlvdpdel aawtgrffad vqsrpgrvya dvrkalqlqr
      241 trlkllplvr ayarrkddfe amdfadqlar aarvardhpg vgvierdrfr vvlldeyqdt
      301 shaqvvllna lfggghpvta vgdpcqsiyg wrgasagtld rfpaefartd gspadvlslt
      361 tswrnrpeil gvantlsvpl raagarvpel haalsvrdpi phrtpggqag gtvhcallet
      421 yadeadwiad svlaawrgaa gmpgalpehi padrrpttav lvrlrsqipa ieaalrargl
      481 pvdvvglggl ldtpevrdvv ctlrvladpt dgaallrllt garwrigprd lvalhrrara
      541 iarsrreltg degpeitvda ldeatlveal adlgpaqays aegyarlrsy gmelallryr
      601 ldqslpelia diertigldv evavragrdg agdaglarah ldalgdvaar fsgetpgatl
      661 agflaylaaa edeerglapg evevvagavq vltahaakgl ewdvvavagm trgvwpgpvr
      721 nsdhwlgglg vlpfplrgda dglpelalpe aedqrgvara ltdftdawra hdereerrla
      781 yvavtrprrl llcsgywwge gtkrfrgpsv flrevhdacl aggdghvvda wtpepagdav
      841 npttetvlra ewpadplgtr rqalteaaal vrrhladpet arreaavlat tgaaddaeva
      901 rwrreadlll aeraelarqa eavevelpgq lsvtqlvalr rdpealartl rrpmptepnp
      961 yarrgtafha wleqrfgtdr lldvdelpga adedaapdea laelqerfla gewadrvpve
     1021 vevpfatvia gvvirgrmda vfarpggryd vvdwktgrqp agreadaaav qlaayrlawa
     1081 elagvpvdrv gaafhyvrds atvrpadlld aeglaalvaa vpeipgdlpe ranp
//
LOCUS       WP_457604300             188 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar O-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604300
VERSION     WP_457604300.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="sugar O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19856
     Region          14..181
                     /region_name="LbH_MAT_GAT"
                     /note="Maltose O-acetyltransferase (MAT) and Galactoside
                     O-acetyltransferase (GAT): MAT and GAT catalyze the
                     CoA-dependent acetylation of the 6-hydroxyl group of their
                     respective sugar substrates. MAT acetylates maltose and
                     glucose exclusively at the C6...; cd03357"
                     /db_xref="CDD:100047"
     Site            order(16,25,70,82,84,90,92,102,104,110,112,114,116,
                     123..124,126,138,140..141,146,158..159,162,164..165,
                     174..177,179)
                     /site_type="active"
                     /db_xref="CDD:100047"
     Site            order(16,25,70,82,84,90,92,102,112,114,123..124,126)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100047"
     Site            order(26,29,33,40,66,68..69,85..86,100,102,106,108,110,
                     114,116..118,120..121,127,129,136,138,141..143,146,154,
                     156,159..160,164,176)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100047"
     Site            order(110,112,114,116,138,140..141,146,158..159,164..165,
                     174..175,177)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100047"
ORIGIN      
        1 mtsmkdrmla geqyiaddpa iiadleraar lgerfnrssa ddpagrlaal rellgslgdd
       61 awvrpplycd ygfqthigpr tfvnfnavll dvaritigad vqigpnvqll tathpvepea
      121 rrakwesalp itigdnvwlg ggvivlagvt igentvvgag avvtrdlpan vvavgnparp
      181 irnlgqps
//
LOCUS       WP_457604304            1230 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604304
VERSION     WP_457604304.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1230)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1230)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1230)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1230
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1230
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=129292
     Region          108..914
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          970..1218
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mqayrlvrrp ggaeagvthd agagqgvgrp ggpadaeprs ggsagdaahp etitppadat
       61 tpatpgtgtr gaappattpd aggeeartgd etretgagqg lsrvravdpv qaeviahtdg
      121 pmlvvggpgt gktttlveav aarvaegvdp erilvltfgr rgatelrhri eariaegghr
      181 vireplvrtf payafgllrr aaaergepsp rlltgpeqdl iirelldvvg eepgddpvgw
      241 pedlrpalrt rafaqqlrdl lmraaergvg pvelarlgek lgradwpaaa rflreyvavl
      301 alrdvsnrgs vaydpaelvr aatgmlldds ellaaerrrl thvyvdelad tdpaqldlla
      361 vvagggrslv afadpdssty afrgadpagv ttfphrfrta sgapaaqvtl ttsyragpel
      421 laatarlarr lrgpaghrrl rplpgvpagt vevrtfrsat sesawlahal reahlldgvp
      481 wsrmavlvrs tgrqlpslrr alhtagvptv vhgedlplhl qpavapllll lrcalepdrl
      541 deeaavallh splggadpla errlrqglra lalaagdrrp sgellvealr dpaelatver
      601 rwaapaqava hllatareta grpgatvedv lwavwresgl aerwagaitr graatgehet
      661 aqrwraeaad rdldavlvlf daaarftdrl pgartevfld hvlgqelpad tlaaaadrgd
      721 avrlltahaa kglewdlvav agvqegvwpd lrlrgsllgs erlvdvlagr adgaglrasl
      781 vgqtsallde errlfhvais rarrrllvta vasaavggdd heeqpsrflh elaaadppat
      841 ggggaaptgp apngpnpngp nptgngptrt atrggivdgp vphgdehpqd gppaalpvtl
      901 pprgltlsal vaelrtavtd patpitrrha aagelarlaa agvpgahpdd wwglrglsdd
      961 rplvdegepv rvtpsamesa lrcslrwlle rhggsgpasa aqgvgnlvha aamlaedasv
     1021 drealleyva arfdaielaa rwmagperqr aeamvdkllr wlagnprrll aiehefavrl
     1081 ddpsrpielt grvdrlevdd egrlvvidlk tgkstavter evaehpqlga yqaaveaggf
     1141 aefgeepgga alvqlgtgar dakeqtqaaa gegpeagwat alvrrtadtm aastfaavan
     1201 skcrvcpvrt scpvsgqgrq vvepppenqp
//
LOCUS       WP_457604320             245 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604320
VERSION     WP_457604320.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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 245)
  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 245)
  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..245
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..245
                     /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=26923
     Region          2..184
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mfallvaran rlvtvhdlvd elwpdapprs aianvrtyaa nlrrslgsga ddearivrep
       61 ggyrllidek lidlhrlnvr srrarelmre grsaqavpvl vevvgaaapl laglavgpal
      121 taqreavsqe rqaalellte ayldlgrpes avsllrdhvs hqplreraqc llmraliqtg
      181 dagapwpsta plarrcpiss gchparrwnd fvwrppgrda gfrnrrarwr rsgvvlisai
      241 gcrgr
//
LOCUS       WP_457604321             746 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604321
VERSION     WP_457604321.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..746
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=82130
     Region          47..743
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          577..605
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(578,581..582,585..586,588,618,621..622,625..626,
                     628..629,658,661..662,665..666,669)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          616..656
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          657..685
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          697..724
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 metirsgahk rnwlprtvmd fvgreemvdr llcevreasg qgptirvidg magcgkttla
       61 lhvasrsaer fpdgqlfvdl rghstrtrmr pavaldtllh qlgvpagrip lelpgrqemw
      121 rrelaarsvl vvldnaadsr qvepllpvsg savvlvtsrr rllalterpp vslavlaeae
      181 alellatlig sgrvaaepea arqlvdicgc lplavrlagt rlahrpdwri adlvdrlshr
      241 siflpglrae arsvveafae syepldeacr kafrsfglaa gnhldtamva altdlplrda
      301 advldelvdr hlvqetsagr yrlhdlmrry aaelarqede pttgrpairn lldhvlhsvv
      361 rasasiedgr vlaqhlrlge plrpdllagr vdrdldwlee qrsnldafvr qaadqghepm
      421 awrlaragwr ffyirgyfdd isathalgla aaqrcgdrha valmhnylas acvrtgayqd
      481 asahlhevvs iltglgdesg aqrarfnlga vhwltgrlhq sleanrmtlr scaldtlpvl
      541 pnlgltlryl grydestavh rlhlfaarik qdpfhmsnal ghlgglryrl gqnaaaerll
      601 raslalrdrt gngfgraetl sdlagtyrql gryddalrhh eaaieaaaas gerhvqaqar
      661 nelavtlgat gradeavavf eealaiatri ghpyeqaral dglaghlaek epaqarryrq
      721 ralaifermg aperhdlrrq lvetpa
//
LOCUS       WP_457604322             156 aa            linear   BCT 27-JAN-2026
DEFINITION  MogA/MoaB family molybdenum cofactor biosynthesis protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604322
VERSION     WP_457604322.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Kanaujia,S.P., Jeyakanthan,J., Shinkai,A., Kuramitsu,S.,
            Yokoyama,S. and Sekar,K.
  TITLE     Crystal structures, dynamics and functional implications of
            molybdenum-cofactor biosynthesis protein MogA from two thermophilic
            organisms
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 1), 2-16
            (2011)
   PUBMED   21206014
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Bevers,L.E., Hagedoorn,P.L., Santamaria-Araujo,J.A., Magalon,A.,
            Hagen,W.R. and Schwarz,G.
  TITLE     Function of MoaB proteins in the biosynthesis of the molybdenum and
            tungsten cofactors
  JOURNAL   Biochemistry 47 (3), 949-956 (2008)
   PUBMED   18154309
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Schwarz,G.
  TITLE     Molybdenum cofactor biosynthesis and deficiency
  JOURNAL   Cell Mol Life Sci 62 (23), 2792-2810 (2005)
   PUBMED   16261263
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..156
                     /product="MogA/MoaB family molybdenum cofactor
                     biosynthesis protein"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=15768
     Region          2..156
                     /region_name="MoaB"
                     /note="Molybdopterin biosynthesis enzyme MoaB/MogA
                     [Coenzyme transport and metabolism]; COG0521"
                     /db_xref="CDD:440287"
ORIGIN      
        1 mirarvivas nraaagvyed tsgpllvagl relgcevdap vvvpdgepvg dalraaradg
       61 vdvvltsggt gitptdrtpd vtralldyei pgiaeairah srdtvptaal srglagvtgr
      121 tlvvnlpgsr ggardglavl gpilrhavdq lrggdh
//
LOCUS       WP_457604325             257 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdenum cofactor guanylyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604325
VERSION     WP_457604325.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Guse,A., Stevenson,C.E., Kuper,J., Buchanan,G., Schwarz,G.,
            Giordano,G., Magalon,A., Mendel,R.R., Lawson,D.M. and Palmer,T.
  TITLE     Biochemical and structural analysis of the molybdenum cofactor
            biosynthesis protein MobA
  JOURNAL   J Biol Chem 278 (28), 25302-25307 (2003)
   PUBMED   12719427
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Lake,M.W., Temple,C.A., Rajagopalan,K.V. and Schindelin,H.
  TITLE     The crystal structure of the Escherichia coli MobA protein provides
            insight into molybdopterin guanine dinucleotide biosynthesis
  JOURNAL   J Biol Chem 275 (51), 40211-40217 (2000)
   PUBMED   10978347
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   5  (residues 1 to 257)
  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 10002369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     gene            1..257
                     /gene="mobA"
     Protein         1..257
                     /product="molybdenum cofactor guanylyltransferase"
                     /EC_number="2.7.7.77"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061603 - molybdenum cofactor
                     guanylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=26059
     Region          15..254
                     /region_name="MobA"
                     /note="Molybdopterin-guanine dinucleotide biosynthesis
                     protein A [Coenzyme transport and metabolism]; COG0746"
                     /db_xref="CDD:440509"
ORIGIN      
        1 mtgyaailla ggaarrmggv dkparavggr pmlhrvldav adadqrivvg ssgplprgvr
       61 tareeppggg pvaataagla lldpgtttva vlaadlpllt taavaelrra laachsrddp
      121 ppaldaaaag pedapatagp edapatarse dapatagped apaawretld grsaalacyv
      181 dgdgrrqhlc alwqvpalrs aldrlaatrg gsldgapvrg lladvavrev swsgsgpppw
      241 fdcdtdedvr raeewtr
//
LOCUS       WP_457604327             275 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604327
VERSION     WP_457604327.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28189
     Region          30..240
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlsdprevlt rpspppdatv sygdhpdqca dlrlpagdgp prplvvvvhg gfwraeydra
       61 htgpmaaala alghpvaqie yrrtgrpggg wphtltdvra giaalpelaa aalpgrvapv
      121 ppilvghsag ghlalyvath apdtvggvla lapvadlaqa yrldldegav aallgggpdd
      181 vpdryaaadp stlvpirtrt vvihgdqdvq vpiaisrswv aadraaggsa tlvelpeceh
      241 fgliapgsta wpqvvaalrs lhddlpgida asstr
//
LOCUS       WP_457604331             557 aa            linear   BCT 27-JAN-2026
DEFINITION  solute symporter family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604331
VERSION     WP_457604331.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..557
                     /product="solute symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015123 - acetate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58051
     Region          6..556
                     /region_name="ActP"
                     /note="Na+(or H+)/acetate symporter ActP [Energy
                     production and conversion]; COG4147"
                     /db_xref="CDD:443318"
ORIGIN      
        1 mntvlaaeag sttarnltit lflvfvaitl aitvwasrqt ktatdfyagg rsfsgfqngm
       61 aiggdymsaa sflgiagiia lygydgflys igflvawlva lllvaellrn sgrytmadvl
      121 afrmrqrpvr taaavstitv sifyllaqmv gagalvalll gikpgttflg mdadiakvat
      181 iimvgalmii yvtvggmkgt tyvqivkafl lmggalamtl lvlakykfnl ssllgdaasa
      241 sgkgaaflep glrygvetpg dalktfyskm dllslgialv lgtaglphil irfytvptar
      301 aarksvlwai giigtfyllt lalgfgaaai vggseitaqd kagntaapql aeklgeqflg
      361 gdlggatlla iiaavafati lavvagltla sssslahdfy anvvkngqas erqevtvari
      421 salvigavsi vlsiyaqnln vaflvalafa vaasgnlpai lyslfwkrfn tsgavwaiyg
      481 gllaavvlvf fspvvsgapt amfpdhdwqw fplsnpgiis ipfgflcgwl gtilskesde
      541 ekyaelevrs ltgagah
//
LOCUS       WP_457604346             418 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604346
VERSION     WP_457604346.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41756
     Region          14..389
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,141,
                     144..145,148,221,224..225,228..230,233,257,261,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msfttdesrw pdvwlaatar gisscgdfla aatltlalqs agagglavsg lllaatlplv
       61 vlapltgrla drvdsrlllv aaglaqaavc lalayardpv lvialvalla tglavtqpai
      121 aalvpvmvrp edlpragaln qtagtlgala gpalagllvg qfgtrvpllv dafsylalva
      181 agllirtrrg grrtpaavaa avapawrlrr dplltvmvgs vaavigavga vnvievffir
      241 etlgssttvy glvtgswtlg ivlgawlfar varrladdga llgaglvllg gcclavlvsa
      301 avpsawllvp iwlaggvang gnnvfdqlll arrvpeasrg rafavfgaaa qgaamggylv
      361 gglllevagp rvliagcgva gllvvvallg pvrravraer aaartaapaa vsvaaksv
//
LOCUS       WP_457604338             159 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604338
VERSION     WP_457604338.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..159
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16649
     Region          1..155
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mrwtvldspi gefsvgtddd avrgahfgrv dgaagepgda varlavaelr ayfageltef
       61 tvpvsaprgs eferavwrem tripygetkt ygevakavgd pggaravgma cnrnpvpviv
      121 pchrivgagg klvgfggglp rkvtllelea svalrraws
//
LOCUS       WP_457604350             491 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604350
VERSION     WP_457604350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..491
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50060
     Region          40..487
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 madaarstdr lealditrkl aaicgtpfar fagpadevag rtarwvavpg gphaaaevlr
       61 laaahdltvv prgagtkidw gaapaqvdim ldtgrlagvw heprdaavae igagtplrav
      121 qatlartnrr lpvdapspga tlggvlaade sgplrhrhgs pcaqlvgvry ldadgelvsv
      181 gesgtealgr atpgsgggra sgrgpaggag gdpgrgggda ilgrgevpgl dvarllcgsq
      241 gglgvlvsat mrvhavpagr lwvsrpvwtp levhdlvrav laagvepaav eldlpvpvpl
      301 prrrippthp svvnrpdhpa vtgrpaagsl vvlleggpad vteraerlta vlgaeaivsh
      361 hapewwgryp fapgdtalri evpindlhaa vyalrdatgg pvpvrgsags gtvhaalsga
      421 lppervasil tavrsvliar rgrcvvvaap aavrravdlw gelptlprlr sakahldphh
      481 rlapgrlpgg l
//
LOCUS       WP_457604354             384 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604354
VERSION     WP_457604354.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 384)
  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 384)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..384
                     /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=40179
     Region          126..369
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msswhwarta lvpavalval lglvvqsegi dtsaelvall vvlassaaly lrrrhpvavg
       61 lvalaavaay gallhrpgpi mlvfvvalyt vvdegylava vglglasvvs favadsytrt
      121 gvsgngatll hagwlvaviv gvtrnrrayl aevqarvlaa eqrkeeearh rateerlria
      181 relhdllghh lslisvqasa alhrpdpers aealtvikqt sretlrelra algvlrqest
      241 tpnrpapgld rldelvtaag rcgltvrtev tergplppev dlsayrivqe altnvsrhag
      301 sttavvrvvp dgdevlveva ddgagpagpp gngilgmger aralggslst gpgpdggflv
      361 rarlplrpap lpvpaprtaq gett
//
LOCUS       WP_457604356             304 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604356
VERSION     WP_457604356.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..304
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30820
     Region          7..302
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(45..47,50,135,139,161..166,185..186,188,213..214,
                     230..231,250..252)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mgtrtfraav vrtpggpdti eiidvperep gpgevrvdva aapvnpadlg vvggffhslg
       61 lihqphhtgl gwdfagvvaa agpgvdlavg trvaglvggf drdfgtyaeq lvvaaadvav
      121 vpddldlvaa atvplngqta aqivdllgdp padgrllvtg aagavggyvv plardrgwrv
      181 tglaragdek fvrglgadfi taaepgwdav adaagwqdqa lalvgdggvf vgvrpnahpp
      241 aergvtvrav evhadgarla dllartaage lparvhavlp ldrvadahra vaeggvrgry
      301 vlrp
//
LOCUS       WP_457604363             301 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604363
VERSION     WP_457604363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..301
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31617
     Region          8..216
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtgdrlaiea sgltkrygdv tavrdltftv rpgavtgflg pngagktttm rmltglvtpt
       61 sgaatiggqp ygrlaqpsrt vgavfdgnaf hpghtardhl gvyaamagcp dsrvaelldl
      121 lglaqaadrr trefstgmrq rlslatallg dprvllldep sngldpegms wlrgllrrla
      181 degrtvlvss hvlhevqqvv ddvvvirrge lvaagpwsrl tgpptvlvts pdatdlaaal
      241 tagagsvepa gpgrlrvrgl daprvadlaa dhrlrihelv tettsleqlf ldlttdtaea
      301 r
//
LOCUS       WP_457604364             153 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604364
VERSION     WP_457604364.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..153
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16660
     Region          20..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdnpepdlvp trlaglpswl itrtavragr lvsdglaavd argyhfrlla tldefgpasq
       61 aalgrrsgih vsdvvaalne laerefvtrs pdpadrrrnv vtitaagrrq lrrlekrlaa
      121 vqddllapls pderadltrl lsrvlahhnr ppa
//
LOCUS       WP_457604365             363 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604365
VERSION     WP_457604365.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40726
     Region          2..107
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          69..>188
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 miepfrvhvp qadlddladr lartrwpdel pdagwdygip lsrvrelaeh wrtaydwrea
       61 eaelnrypqf tttidgqnih flhvrsadpd alplilthgw pgsvvefldv igplseqfhl
      121 vvpsipgfgf sgptrergwd vdrvarawae lmrrlgyrry gaqggdwgsv istrlggidp
      181 ehvvgvhlny lptppppgwt geaglsgedr drldrirrlk tqrhphqvly asrpqtvsya
      241 lndspvgqla wiaekftewt dpgsavsvdr iltdvsvywf tgtaassarl vresafggpp
      301 apcppplgva vfahditrsv rpiaeltyti rqwsefdrgg hfaalevpel fvgdvrsffw
      361 nlr
//
LOCUS       WP_457604367             789 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604367
VERSION     WP_457604367.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 789)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..789
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85986
     Region          5..759
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mphgddgwri rrtsadldrl getesvfala ngwvgwrgtl degepcgmpg sylngfheqh
       61 eltypesgya fpersdtvis apnaalirlw vddepldlst gtirrhhqel dlragvvrre
      121 tewvspggrg vrirstrlvs ltrrpvaavd wavepldepv rlrvgadlla nqrvperadd
      181 praasvihdp ltgeirredg ldgvlvhrtg rsgqrvavav ahrveapdei atdteltadr
      241 frlalsgpvr pgerirvtrf aayecadvdg tpageladlv vaeaatardd gfdallteqr
      301 aaldvawtta dvelegdpel qlavrfsvfh llqsgradgd rtipakgltg ngydghvlwd
      361 tegyvlpvlt ylapelarsa lrwrhahlpe ardraaelrl tgatypwrtl sgrecsgywp
      421 agsaglhvna diadavlryv aatgdtafla ecgaevliet arlwhgyghf ddggafhltg
      481 vtgpdeysal vddnvftnlm arrnlrgaad aaedcpevaa rlgvdaaeva gwraaadamf
      541 vpydgkrgvh eqsagftaqp ewdfagtged dyplllhfpy qelyrkqvvk qadlvlamlr
      601 cpgeftaeek trnvayyear tvrdsslsas aqailaaevg hldlaydlfa etafqdladl
      661 gdktadglhl aslagawlvv aqgfgglrdd rgvlafeprl prpitrlafh lrrhghrlrv
      721 tltgrearye lpdagpgdav elwhhgeqlr vtgdgpvtrp mppvpdpgpe pqappgrrpe
      781 rraqeaggd
//
LOCUS       WP_457604371             494 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604371
VERSION     WP_457604371.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51028
     Region          22..493
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 maepelvdvv vvglgvggee vagrlaeagl tvvgierdlv ggecpywgcv pskmmiraan
       61 alaeahrvne lagsaqvrpd wapvakrira eatdtwddkv avdrftgkgg rfvrgsgrld
      121 gpnrvrvgdq vfqarygvvl gtgtrpsvpp idgladtpyw tnhqaievee lpasllvlgg
      181 gaiglelaqv farfgvrvtv ieaadrvlav eepeasalaa dalradgvei htgvkagrvs
      241 hdgttftvha dgaeftgekl lvvtgrkahl eelgldtvgv dagqrylpvn drmhvtdgiw
      301 avgdltgega fthiamyqag ivvadvldhm rrtkggpdas gtasvvggaa gvvsavggam
      361 saggstaapg svpvadyral prvtftdpev gavglteqqa rergvnvqvg yadltssarg
      421 wihktgnagf ikliadadqg vlvgatsagp aggevlsalv vavhaavpis qlrhmiyayp
      481 tvhraiedal ralk
//
LOCUS       WP_457604372             366 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604372
VERSION     WP_457604372.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..366
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39101
     Region          1..366
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mharftpvrd cfrdlfttgr etgaslsvwh dgvpvvklvg gttaavppgt vvpaagadqp
       61 wrpdtlvdvy svgkpvvalc llllvdrgrv dldapvsayw pgfrapatvr qvlthtaglp
      121 afpvprpaaa iadwdllcad laaaepewmp gavaaehawt yghlvgelvr rvdgrpvgrf
      181 laeeiagpwr ldlafglgea drrrcadlsy adpawpdamr gepgslrara ldnppggrdv
      241 amvnsdlwra aeipavnlha taaglarlya gllargtldg vrlfspelvt eatrvqysgp
      301 dllldrpvdw tlgmqwepdg swgmggiggs sawadpergy afayatarla dhdrveelvd
      361 alhscl
//
LOCUS       WP_457604374             440 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604374
VERSION     WP_457604374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..440
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49788
     Region          5..429
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtgrtavvlf trdlrvhdhp alaaacsafd rvvplyvldp alqklspnrt rflhqsladl
       61 realrkrggd lvirrgdpva etvklarkvg aegvglsadv sryahrrerr lraecdrhrm
      121 flrlfpglti vepgalrpgg gdhyrvfspy frawqgvrwr delaapkrvr lpdgvdpgrl
      181 pdppkgdspd aavggetvar rrltawlptl dryddihddm agdetsrlsp ylrfgcvspl
      241 avanragdrd gpfvrqlcwr dfyhqvvagf pdlstvayrr garedwrddp hafdawaegr
      301 tgmpvvdagm rqlraegwmh nrarlitagy ltkhlgldwr pgleiffrwl ldgdrvnnsg
      361 nwqwvagtgn dtrpyrgfnp vrqaerydpd gayvrrwvpe lasvagkavh qpwrlpdevr
      421 rtldyppple vpgadpvwlr
//
LOCUS       WP_457604376             306 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604376
VERSION     WP_457604376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..306
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32182
     Region          15..>294
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          226..>295
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 millsgcgrv sglldrvslf hpvwaadgwv yylrevtsts gsgvaevwrq rpdgsaekpv
       61 lrhapavstc eaglfsflfa gpggdlgval ecgwdgtell syspadrtfe plastrflae
      121 aalvnrgggg yveaprecgp ggvqlladgk ayefgspvtv ggvtfnlsgg dtdcestvla
      181 rspaalgerl ffitapdslg rlplppevsp ddltwhltew avgsatarfi telpgladla
      241 vspdgrsvia avasdhvggv wsvdvrtgkk triaggaray hpsfspdgkr fvyveklerl
      301 kfaear
//
LOCUS       WP_457604405             335 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604405
VERSION     WP_457604405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..335
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36250
     Region          5..332
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdqvleirg lcvdygvgad avravrdvdl tlhrgevlgl agesgsgkst laygltrllp
       61 ppgvvsggqv iyhpgdgppv dvltlspakl refrwaetsi vfqgamnsln pvhrvstqll
      121 dviraherrs taasrsarak ellrlvgisa drldsyphql sggmrqrvmi amalalepqv
      181 vimdepttal dvvmqrqilg qlaelrerls favlfithdl sllvefsdri aimyggrive
      241 eapatrlyre plhpytegll hsfpalhgpr reltgipgsp pdlrampsgc afhprcpkaf
      301 dgcdeqvpvl gaprvddpar avacrlhpav aplsr
//
LOCUS       WP_457604398             655 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604398
VERSION     WP_457604398.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 655)
  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 655)
  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 655)
  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 655)
  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..655
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..655
                     /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=69284
     Region          2..247
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mpvgfgvlgp vtawddagap vdlkgprhra vlarlvaarg rtvpvgqivd dlwddpppgg
       61 vgavrtfvaa lrrrlephrp preparllvt dgpgyalrad pdtvdawrfe dtvtaaadal
      121 praaldrlde algwwrgpay adfdqpwaha ersrldqirl taverraeal laldraadav
      181 pdldahvaah pwredgwall asalyragrq adalavlrra rellrdqlgl dpgprlrrle
      241 tdllrqaepe ptgparvwae taaayersvv pgararlest vgllrslavt gpggleaard
      301 qreaaitaae qlgdpeftar viggydvpai wtrsddpaqa arvvaaaera laglgpdape
      361 atrarllatv aiesrgtasp rpaeaareae aiarrvadpa llaqalngvy mqtfhragla
      421 aerdgigael valaarhgla tveilghlir vqarsaladf taadahadaa drlaarhesp
      481 lvgvftggyr amrtaatgaa ypdaeaayrs watglagcgm pgverglapl allclrvwhd
      541 lpavfpadtd wgpyapwarp lllladgrre eaakalrrtp apprdllmea lwcltgraav
      601 algdrdamlr arsalapaag elagagsgll tvgpvavhld rldaalgmtg gqdrs
//
LOCUS       WP_457604409             372 aa            linear   BCT 27-JAN-2026
DEFINITION  FUSC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604409
VERSION     WP_457604409.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38885
     Region          15..206
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mapaarrevr eayerlrryf ivalqaglaa glawyvastl lknpqplfap aaaagtiaaa
       61 ignrirrtae llggvilgvl vgdlliklig agpvqtglvv alaislavvi rgsgavmvqa
      121 gstavllgtv epnapdlavp rtanalvggg vavvvallll plnpvrvvhr aagptldlfa
      181 neltaaakal aardagaaea slgrleaaev erkqtteiva aarevtslsp wrwrrraqlr
      241 ryenaavhle laytnsrnmv rrvvallear epvppalpag veafgqslrl lhrdflagrp
      301 pdiararare aaqdagrara vglgfsgtiv asqllivvge llqasgmtki eadrtagvce
      361 hrpdsradpn dr
//
LOCUS       WP_457604401             375 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604401
VERSION     WP_457604401.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 375)
  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 375)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..375
                     /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=38103
     Region          <173..375
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 materltrva ataglavvll aaigvqavav aaswglrywl pggaaavvvg vlalvrhrqr
       61 vvtataglav agsavaaarl fdlptepgpa lalasavlvg savralpplp agliaagglv
      121 vaagawaaar pgaggsgvva ldglcwlggv vagltlrlld eraraaaerv rrderlelar
      181 elhdvvahhv tgmvvqaqaa hlvgrrdpar ateslagiea aggealramr rlvgvlrdta
      241 dappasagte qiaelverfr rqgppvrlrl pgetawppev tstvhrivre altnvarhap
      301 hagqvtvdvs qepdavvvev tddasgvsgv saeqrggygl iglrerveal ggtlragprs
      361 gagwsvravv phgra
//
LOCUS       WP_457604412            1036 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604412
VERSION     WP_457604412.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1036
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=108007
     Region          123..1031
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          835..863
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(836,839..840,843..844,846,876,879..880,883..884,
                     886..887,918,921..922,925..926,929)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          874..904
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          917..944
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfgvlgatq ayaadgsvlp vaggrlrall vlllldadrt vapqrlvdgv ygdrppeqat
       61 nalqsqvsrl rrllpgahie fgpagyrlav dpqrvdvhrf tglaaagraa laagdpagaa
      121 allrdalglw rgepladvtd apfadaeaar lrqarlaave drveaelala pagapliael
      181 rdlvaahplr erlhgqlmra lhgagrraea lavyadarrv laeelgtdps aelvalhtal
      241 lrddaappar lpspltsfvg repelrrvhe llgaarlvtl hgpggagktr lattvasghd
      301 gpvclvelaa vapgapvapa vlaaldlrda glrtpggpad ltgrlvaala drrlllvldn
      361 cehviddaar ltgrllaaap glrvlatsre plgltgealc pvgglpapdg paappaaaay
      421 pavrlftdra advspgftld dattpavlri crtldglpla lelaaarlra lpvtqvaarl
      481 ddrfrllcrg drtaaprhrt leavvgwswd lldeperrla armsvfagaa dlaavqavca
      541 pdaddvldvl tglvdkslve atggryrmle tirefaaarl aehgetrrmr dahaayfldl
      601 aqagdvalrg ggqerwlrrl daarddlhaa lrhaetttgl rlvaalafyw wlrglrgega
      661 alarrlvdrl dgppdgvaee yalglliaal agggersevd aasrilwtla rpprhpflly
      721 lsgmasgpps pqdaaalheq avrdrllgtd pwsralgllg tamvsllhgr haqaradldg
      781 alagfralsd rwgmivtlst haeaayrtgd vasaaapmae alelaeqlgs tldlaellrt
      841 radgrlaagd ltgaaedfrr vrriagpaga pelvaaaylg lgeiarrdgd pqrartlcer
      901 avaecpsgwf gadvvrlaal vtlgqladat gdpaaarahy rqvltagvgv wdvpvvaaaa
      961 dglagpllrd gdpesaarll gaaaallagt gaadapagtp tavtlrerlg eaafatayar
     1021 gadlprqral alvdgr
//
LOCUS       WP_457604416             435 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604416
VERSION     WP_457604416.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..435
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46921
     Region          16..405
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 matprvavvg agaaglatlk aladagvpav afeaadtlgg lwvygapgsp ayrtlhlnts
       61 kgrtefadhp mpadwpdypd harvagylgd yadrfglrea vrlrhtveqv trtgdgwrvr
      121 atgpdgpvev dveavvvang hnrvpkrpep ypgecaaeqm hshdyrgpeq lagrrvlvvg
      181 ggnsamdiav dasyaaartl lslrrgvwvv pkyllgrpsd tlngalarrl pwrlrqrisq
      241 tmittavgpp tryglpapah gflqdhptls dallsrlthg diqarpgiar fdgdrveftd
      301 grhdevdlvv wctgyrvevp fldpallgdg adrlplyrhv fhldapglaf vglmqstgaa
      361 fplveaqarl vaarlagtwt ppdparqaaa crdelraata rwgqrrphmr vdfdvylgel
      421 grelaagrrr agaar
//
LOCUS       WP_457604417             725 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 95 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604417
VERSION     WP_457604417.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Wu,H., Owen,C.D. and Juge,N.
  TITLE     Structure and function of microbial alpha-l-fucosidases: a mini
            review
  JOURNAL   Essays Biochem 67 (3), 399-414 (2023)
   PUBMED   36805644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..725
                     /product="glycoside hydrolase family 95 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=77896
     Region          6..228
                     /region_name="Glyco_hyd_65N_2"
                     /note="Glycosyl hydrolase family 65, N-terminal domain;
                     pfam14498"
                     /db_xref="CDD:405224"
ORIGIN      
        1 mtahrihdta paddwtdafl tgngelglmv hgrphaeriv vnhhrlvlpn gtrdarapel
       61 agrmphiral vlagrraeaa rlltggrele wtqsfhpgya ltvdaapgpv rdyrrdtdft
      121 tgevtvewsg grrrcfasra dgvavlhldq gdcvvgatge lpgkpadvvy ehaayrsdgl
      181 vflrvraryp daggaygfeg ltllrgdvtv dgdrvrvrgp allttlvdrp gappwrtrvs
      241 egrlaaltgd ydtllarhvp rhlgpytrvg ldlgvpaadr alpvgellar qaaapdrldp
      301 allerlfhag ryllfsasgv lpprltglwl gswdaawagd fttdanlnlq laganvgalp
      361 evtaaharlv aaqvdhwran ahavygargl lapsrtdgeh ghlfhvhpdw pftawlagad
      421 wllhplhehh lvtgeplgev agwlaevadf fadvltvvdg rpalvpsysp etgpyddtgr
      481 vapvavnatm dvaaarhalr laaevtgtdr wagvrppgyl vdgrgalaew awpgstgded
      541 hrhvshlypv wplheidpdd tpelaaaahr altlrgdenr pahgslhral aaarlrdgel
      601 vaanlrkilg admffrslms ahnpgrttyn adaahalpav lieslvqsrp gtlrllpapl
      661 pglssgtlrg itcrgrvtve eltwapgrvr arlvspvaqr vvvhapgghr avalapdrpy
      721 evafg
//
LOCUS       WP_457604418             258 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604418
VERSION     WP_457604418.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..258
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27333
     Region          13..134
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mdedarrrhs ssfgaaatay aehrpdyaha alrwalepap gvrvldlgag tgkltatlae
       61 vsddvtavep dpamlaelrr tlpdvralag saeaiplpds svdavvagna mhwfdmavag
      121 peiarvlapg gvlaglwnvv ddrvdwvagl aavsgsaaig prdtpaswra atatmhlpkt
      181 gearfgspeq aefphgqrrt adslvatlat ragmlvmper ertetldrir aylasrpeta
      241 dgeftlpmlt cvlrvrrr
//
LOCUS       WP_457604422             153 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604422
VERSION     WP_457604422.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..153
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16346
     Region          5..50
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 msndmysveq vadllglhvr tvrgyirsgr lratrigkqy ritradldal tgrpappsap
       61 gaevssvvrl dgvdraavdr latlvlagvn thhdpdrplr vqtvhdeerh rmtimilgdl
      121 tatadllrll dgvldgvldg gngllgggeh srg
//
LOCUS       WP_457604421             151 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604421
VERSION     WP_457604421.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..151
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16463
     Region          16..140
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mlreymaemv rrwygrperp gevdaalaed psddlapptg llvlarrdgr lagcaglrwq
       61 pdwaeltrvy vrpehrgagg gaaliaaiea yatgggatri rldtrsdlve aralyarhgy
      121 reipaftsgp haqhwfekal agrvddaaqa r
//
LOCUS       WP_457604428             315 aa            linear   BCT 27-JAN-2026
DEFINITION  formylglycine-generating enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604428
VERSION     WP_457604428.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510263
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..315
                     /product="formylglycine-generating enzyme family protein"
                     /EC_number="1.8.3.-"
                     /GO_function="GO:0016670 - oxidoreductase activity, acting
                     on a sulfur group of donors, oxygen as acceptor [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33543
     Region          47..315
                     /region_name="FGE-sulfatase"
                     /note="Sulfatase-modifying factor enzyme 1; pfam03781"
                     /db_xref="CDD:397722"
ORIGIN      
        1 mstepvdpgd gggtpppspc caprrppaag tgaaagasav rsphggtddl ialpggtflm
       61 gtddpedleg pvrpvavapf aiaatpvtnr qfarfvdatg yrtdaerygw sfvfhlllap
      121 sahryvldas vpqapwwlav egthwaapdg pgsdvrgrer hpvvhvshrd aeayclwsgt
      181 rlateaewey aargglsqar yawgdeltpd grhmcniwqg afpavntadd gfagtspvta
      241 fppngyglyd vagnvwelta epwrdhrgri spgesvirgg sylchdsycn ryrvaarsrt
      301 tvdsstgntg frvar
//
LOCUS       WP_457604430             425 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604430
VERSION     WP_457604430.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..425
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45009
     Region          3..418
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mtvqqfrlpd vgeglteaei vtwrvapgdp vglndvivdi etakavvelp spyagvvdrl
       61 laaegqtvev gspiiairtg ddadapdaap aaaspaaeep aeertavlvg ygvsaqartr
      121 rprratpsvr padtsrpaht srppvltkpp lrklakdlgv kltevrgsgp ggritrqdll
      181 dhttgpapat darrderlpv rgvrkataaa mvasaftaph vtefltvdmt gtvefvdrlk
      241 qdpafqgvkv spllvaslav ldavrrhpdv naswdeenqe ivrfadvnlg iaaatprgll
      301 vpnikaaqnl pvrdlavaln elastaregr trpadlsggt ititnigvfg vdagtpilnp
      361 geaailclga lrrmpwvvde qvvprwtaql slsfdhrlvd gelgsrvlah vgrfledplw
      421 glalr
//
LOCUS       WP_457604437             555 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604437
VERSION     WP_457604437.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..555
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=57811
     Region          114..552
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtaarrggva gpvsggghas rkrprrvaea alpaddrlar elldglaeav vtvdhagvvt
       61 lvnamaadll pevapgvdla acrvpalada aaagsdafet ehhgrrlrgl rrpladdrsa
      121 wyvrdvteeh artdallaer srtaflaeag srlglslhre qtlrtavtlp vpyladaavv
      181 vhrppppded qphwiryatg dpgpvtglag whtvesvpgl vealegdlte pspwldaela
      241 dlaevlpagf grpgtvlisp mpsaggpaga lvlarrrerp gfdkreigla refagragaa
      301 laaaelygeq ahlarvlqns llppalprlp gmtlaggyra agdslriggd fydlfptgdg
      361 glfalgdvcg kgvgaavltg rvrqslqtlr lveqrprell ellnrallda pdaarraqft
      421 tlllgalrre pdggllirva ggghpaplvv ragggvetir vggmpvgalt darfadaevr
      481 lapgdlllay tdgvteargg ptepamfgda rlrqalatgt glppaalvdr vlqlvdewld
      541 gqphddiaml avaag
//
LOCUS       WP_457604449             182 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604449
VERSION     WP_457604449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..182
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=19451
     Region          7..>164
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mieqhlppri gslctgyggl dmavelvlgg qltwyaevdr hartvlehhw pgvpnlgdir
       61 tvdwatvprv dvltagfpcq disnagkrag iggkhsslws avadavralr pplvfvenva
      121 allrrgfdvv eadlaaigyd tswtclrasd igaahrrdrl fllatpaepl gegadvadtv
      181 rp
//
LOCUS       WP_457604461             197 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604461
VERSION     WP_457604461.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 197)
  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 197)
  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 197)
  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
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Bujnicki,J.M.
  TITLE     Phylogeny of the restriction endonuclease-like superfamily inferred
            from comparison of protein structures
  JOURNAL   J Mol Evol 50 (1), 39-44 (2000)
   PUBMED   10654258
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..197
                     /product="restriction endonuclease"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21244
     Region          63..184
                     /region_name="COG1787"
                     /note="Endonuclease, HJR/Mrr/RecB family [Defense
                     mechanisms]"
                     /db_xref="CDD:441393"
ORIGIN      
        1 marrkrrrgk rsdamtlaai gggllavsav vqvvrehpvi aslvalaava svsawaylrw
       61 agarqlaehe rnvavtdhms gpefeqfvar lmrasgyrnv tvsggsgdmg advigqspcg
      121 rrvvvqckry kgnlgsphvq rfagtardih rahvallvtt grptaqarev alrcrimlvd
      181 rpalaqwvst qvlhleh
//
LOCUS       WP_457604470             434 aa            linear   BCT 27-JAN-2026
DEFINITION  CpaF family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604470
VERSION     WP_457604470.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..434
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46231
     Region          14..423
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mtapaasant vapelvarlr vrvserlagh gaqlpdaqrd aviagyiaee llahareais
       61 agraplapqa eaalaralrd sftglgglqr liddpqvedi fangcdnvwi rttdgqtrrv
      121 ppvaasdedl idlvrvaaar sgqeerrfdr gspalslrlp ggqrlfavma vskrpsvsir
      181 rnvlhrvtld dlvrrgelta glqelitamv rarknlvicg gtgagkttll raaagaigph
      241 erivtvedaf elgldedata hpntialqqr epnlegvggi dmatmvkwgl rmrpdrvivg
      301 esrgaeavpm llamsqgndg smctlhasss kqaltrlamy vmqapeklaf daanvligqa
      361 vdfvlhldia adgtrvlssv rqvletdgtq vpsneiyrpg pdrraipaap iradtldelt
      421 aaglnpslla qdrw
//
LOCUS       WP_457604476             123 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604476
VERSION     WP_457604476.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..123
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13150
     Region          23..111
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mddvgttktd tppisplage pikradaerl agvlkavadp arlrllsliq sapegeasvs
       61 dlteplglsq ptvshhlril teagllerek rgvwayyrlv psaiaaiadl ltpprkratk
      121 rvr
//
LOCUS       WP_457604482             128 aa            linear   BCT 27-JAN-2026
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604482
VERSION     WP_457604482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Gordon,B.R., Li,Y., Wang,L., Sintsova,A., van Bakel,H., Tian,S.,
            Navarre,W.W., Xia,B. and Liu,J.
  TITLE     Lsr2 is a nucleoid-associated protein that targets AT-rich
            sequences and virulence genes in Mycobacterium tuberculosis
  JOURNAL   Proc Natl Acad Sci U S A 107 (11), 5154-5159 (2010)
   PUBMED   20133735
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18741]
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Gordon,B.R., Imperial,R., Wang,L., Navarre,W.W. and Liu,J.
  TITLE     Lsr2 of Mycobacterium represents a novel class of H-NS-like
            proteins
  JOURNAL   J Bacteriol 190 (21), 7052-7059 (2008)
   PUBMED   18776007
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Oshima,T., Ishikawa,S., Kurokawa,K., Aiba,H. and Ogasawara,N.
  TITLE     Escherichia coli histone-like protein H-NS preferentially binds to
            horizontally acquired DNA in association with RNA polymerase
  JOURNAL   DNA Res 13 (4), 141-153 (2006)
   PUBMED   17046956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10570331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..128
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13309
     Region          1..123
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 makqiihkli ddldggdade tvrfgldgvq yeidlsaana gklrevfspy tahgtkvgrg
       61 gvagggrafr gavgvaggra vhagvgatad reqnkairaw akkagkdisd rgripqeivd
      121 eyhtkagr
//
LOCUS       WP_457604492             146 aa            linear   BCT 27-JAN-2026
DEFINITION  very short patch repair endonuclease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604492
VERSION     WP_457604492.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Tsutakawa,S.E. and Morikawa,K.
  TITLE     The structural basis of damaged DNA recognition and endonucleolytic
            cleavage for very short patch repair endonuclease
  JOURNAL   Nucleic Acids Res 29 (18), 3775-3783 (2001)
   PUBMED   11557809
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Tsutakawa,S.E., Jingami,H. and Morikawa,K.
  TITLE     Recognition of a TG mismatch: the crystal structure of very short
            patch repair endonuclease in complex with a DNA duplex
  JOURNAL   Cell 99 (6), 615-623 (1999)
   PUBMED   10612397
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Tsutakawa,S.E., Muto,T., Kawate,T., Jingami,H., Kunishima,N.,
            Ariyoshi,M., Kohda,D., Nakagawa,M. and Morikawa,K.
  TITLE     Crystallographic and functional studies of very short patch repair
            endonuclease
  JOURNAL   Mol Cell 3 (5), 621-628 (1999)
   PUBMED   10360178
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..146
                     /product="very short patch repair endonuclease"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006298 - mismatch repair [Evidence IEA]"
                     /calculated_mol_wt=16878
     Region          6..141
                     /region_name="Vsr"
                     /note="G:T-mismatch repair DNA endonuclease Vsr, very
                     short patch repair protein [Replication, recombination and
                     repair]; COG3727"
                     /db_xref="CDD:442941"
ORIGIN      
        1 mpeqswassp atrramqgnr srdttpelal rralhakglr yrvcaqplpn lrrkidivfr
       61 parvavevyg cfwhgcpqhh rqptannkyw rekltknmdr drrtrqaled agwllivvwe
      121 hedldaaarr iaesvrarrg ftapea
//
LOCUS       WP_457604493             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GIY-YIG nuclease family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604493
VERSION     WP_457604493.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..237
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26665
     Region          24..81
                     /region_name="GIY-YIG_SF"
                     /note="GIY-YIG nuclease domain superfamily; cd00719"
                     /db_xref="CDD:198380"
ORIGIN      
        1 mldaalnard ehgrqwadar wgcyafydyd gepiyvgqtn erlrvrvrrh ltnqrtdava
       61 mrildvfeva emelwplwef eevagkrhpd yaaaqqklna veytaylkai resrfkailn
      121 ekippvsptv dlpasgrfpl isdatrrerg hpdiriarra etisrlaava hergevsdgl
      181 rrvlviqgvr layiaavrla yaegrptpdp saidvtglvg svlfehddtp dlfdtdg
//
LOCUS       WP_457604494             392 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604494
VERSION     WP_457604494.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..392
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=42789
     Region          15..374
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtqlalipsd agtakptaae ffagiglvrl gledagfkvv wsndiepdkk emyvrhfndp
       61 egahdyergd iadvkgpqma dglslawasf pctdlslaga rrglagsesg tfwhfvrvlr
      121 emgdrrppvv alenvvglat srggedlaaa iralndldys vdvltldarr fvpqsrprlf
      181 lvgaleppad epvpnselrp dwlqapfgdp slrthrallp appppmttgl teladkvpps
      241 sdlwwdeqrk aafvsslspi qaerletlrk grgisrrtay rrtrggkptw eirpddisgc
      301 lrtarggssk qavveagqgk vrvrwmtpre yaklmgaady rldglrtnqa lfgfgdavcv
      361 pvvawlgrey lmplvrgelr ssesprlavv va
//
LOCUS       WP_457604515             282 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604515
VERSION     WP_457604515.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..282
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=29208
     Region          74..262
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mellpillgl gcaaglvlva dglrrrppgt ptrrprrvwt aadrsrllaa vvgglaaaal
       61 trwpvaalla aaavwalprv lgpdrehtra varieavatw aellrdtlss aagleqaita
      121 tapvtpqpir lqvqalaaav rggarlpdal rvfaadladp tadlvvralt qaagyhggql
      181 sqcltslaat arelsgirmr vatkraatrt aarvitgtav amvaglilln rgflapyqtl
      241 agqlvllvvg gvfaggfwwl arasrvpqpp rvlatdggwv ap
//
LOCUS       WP_457604520             371 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604520
VERSION     WP_457604520.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..371
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38266
     Region          1..363
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrqlglpgr llaaqalvvl vgagtlglva avvgpaifrs hlrrvtgpvd pgtahhveqa
       61 yasasalalg vaiavsllaa lavsaylarr larpvtqlat aaadvsrgdy aarvngpglg
      121 pefdtvaaaf ntmaarlada eatrrrllad lghelrtpla tieayvdaae dgiavegedt
      181 wtvlraqttr lrrlaedvva vsraeehqld lcprpvavge lvsaavaaar pryaakgltl
      241 heqvapdvgv vdadpvrmgq vlgnlldnal rhtpptgrvs vhatraadev rvsvtdtgdg
      301 idarhlphvf erfyradaar drehggsgig lavaraivtq hggritaase gpgrgamftv
      361 alpgagpaag s
//
LOCUS       WP_457604521             733 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604521
VERSION     WP_457604521.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..733
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77884
     Region          49..711
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mpsprsplsr lftvllagll aglvlalaal pggllggfaa raalgayadl pdalrtpvqp
       61 qrsylyandg ttlittfydv nrtdvsldei apvmrqaiia aedrrfyshg gadlrgiara
      121 lvanvkgggt eqggstltmq yvrnvlktdp nrtpeerqaa teqtvgrklq eiryanaleq
      181 slskdeilnr ylniayfgsg aygvaaagqr yfgkapadlt lgeaallagl vqspdayspi
      241 dgdkdqalar rgyvldamae tgaitaqqaa aaktepltlr ptaqpngcta taqghddwgf
      301 fcdylrrwwl tqpafgstpe ereqalrrgg yrvvttldpe iqqtaqeqat kvygygnkra
      361 lpiaavepgt grvlamavnr hysldanpdg qanhpntvnp lisggasvdg yqagstfkmf
      421 tmlaaleagk plstgfdaps rlptryasdd egncdgtwcp ananpqwmdg yrmmwdgfgr
      481 svntyfvwla eqvgedkvve maqrlgitfr adsdaafard naanwgaftl gvaattpldl
      541 anayatvaae gtyctplpvv svtapdggav dvaqpsckrv lepdvaraat daarcpvgqq
      601 safdqcnggt atavdrivgr pvagktgsse rnatetfvgy tpqvavagia anpddvtdlv
      661 gsavqakvid avartiktal agkpvadfta psralvgdpq rpqpprrtep drreqrqese
      721 lpsdvlrwlr grg
//
LOCUS       WP_457604524             251 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604524
VERSION     WP_457604524.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..251
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26491
     Region          44..192
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtvpsppspa pvplpgarhg rdpdraikrg prrvpaeeva atqrdrlfdg lvrevatrgy
       61 dsarvsdich aagvtrpafy alfsgkqdaf laayrhgiav vshlmedayr dagpdwpeaa
      121 raalrtlldv lasvpafarm alvevdaagp darrerdall ssfrrffada gpdpagvdrd
      181 allsivvggi hatirervaq graeelplll paltyaatap flgpreagrv araaraddgp
      241 aatapcapsq p
//
LOCUS       WP_457604526             238 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604526
VERSION     WP_457604526.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..238
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25296
     Region          7..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          131..235
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mavhlyavsl dagdprrlar fwsgvlgrei lddpregval ggdahsdfri rflpsdvpkt
       61 vqnrihfdlt saspqaqrdt vdraltlggq hidigqgpdd dqvvladpeg nefcvieagn
      121 nflagcgpvg avncdgtraa glfwsealgw plvwdqdeet aiqsprggak vtwsgpplmp
      181 sggrdrvhld lvadgdrdae vdrllalgat ragtgrhtad dvvladpdgt efclltpr
//
LOCUS       WP_457604529             268 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604529
VERSION     WP_457604529.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..268
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27337
     Region          1..224
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnltdrvvvi tggaggigaa lgrrfaaega aaivladlaa daaraaadai gpvasgvgld
       61 vtdeaavhal veeterrhgr idlfcanagv atgggidapd adwdrawrvn vlghlhsara
      121 vlpgmlsrgq ghllltcsaa glltavgdap ytatkhaavg laewlaityr dagirvsalc
      181 pqgvdtpmla dglaeghlga rviaasgail tpdqvadvvv aglaeerfli lphpevadya
      241 rrraedpdgw qaglrklvrk lranspqs
//
LOCUS       WP_457604530             425 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604530
VERSION     WP_457604530.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..425
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43642
     Region          10..382
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(20..21,24..25,28,60,113..114,116..118,121,142,
                     145..146,149,231,234..235,238..240,243,267,271,324..325,
                     329,333,349,352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mviwirnrrf rllwtstlls nlgnwlmiva vpvhvytmtg stlssgfafv aqtlpaivfa
       61 plagvladqw drravmvgad llrmavvlal vvvddpgmlw llytvmffes aighvfqpaa
      121 ravvpaivgr ggdleaansw ntvasgvvrl agaplggaly alvgfdalvl idsatylasa
      181 vlifgmgrlr vaddghrpgt sswlaafrgq ireglaflfg hpvlrttlgv ssiflmanaa
      241 lnvllvpyvi svlggdagdv gvlmaalggg flasayvgnv lsrsgllrls ftgclaaitl
      301 cfaglflihh faaalvfial aglpggallm lvqvqvqrht pdrqlgrvgs afsaaemaat
      361 vvgasagsia gqqlplittv wlvigvlaag aavaalllpt rsgppaaepv vtatppatag
      421 tggdg
//
LOCUS       WP_457604536             508 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604536
VERSION     WP_457604536.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..508
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52363
     Region          14..408
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mssdpffsdg glrrgrlgta hlvfftvaas apltvlgggv ttmyavsgni gaalgyvlla
       61 avlavfatgy aamsryvana gafyayiang lgraggvags avalaaynai qiglygllga
      121 ilgdfmdakt gisldwwvwa llawvfigal gvlridlnat vlavllilec vavlifdlva
      181 fanpdggtvt tagispghlf gagfgavlaf tiasftgfes gaiyseevkd prrtvaraty
      241 iavaftglfy afsawaltvl tgpenapaas aeagpgiifg aldqytgavv adianvlfit
      301 svlaallsfh ngvarylfal grervlpgfl gatssrsgap vagslvqsvl avvvflafam
      361 tgrdpvidlf twlsgaaavg vvllmtltsa svvgffrgrp gpesawqrai apalgtvllt
      421 avllvllfnf dallapdtas ylkwllpaip vaagvvgliw gailrtsrpd tyrrigqvte
      481 eglhepglhe pglhpapead rwagahhr
//
LOCUS       WP_457604541             281 aa            linear   BCT 27-JAN-2026
DEFINITION  carbon-nitrogen hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604541
VERSION     WP_457604541.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..281
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28985
     Region          11..268
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(47,126,130,133,158..159,161..162,183)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(47,126,158)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(127..130,132,139..141,159,161..165,168..169,
                     194..195,197..199,201..202,223..224,266..268)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mtapparqlt vaavqaqpvp gdvagnagaa arlvaraega rvvvlpelfl payhpptlga
       61 dpdatdvaad adgrvtdarl dplrsaaada gaavvigaav rhpdrrrtis slvvdpagtv
      121 taaydkqqlw sgerelfdag rrgatievdt wrlglgvcyd gcfpeharaa agdgahgylc
      181 psgylagsah rrdlyyaara ldntmyvvfa nsvggtdpwr fnggaavydp egrplargad
      241 tgedvlvatl dpdalaatra ahtmlldrpl dagadravlv a
//
LOCUS       WP_457604545             238 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604545
VERSION     WP_457604545.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..238
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24574
     Region          147..228
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtapltdtar dtrrfsyldm alvlavgvgl ansavadlla rgparlgmpe taastiawal
       61 ingtqlavgl avvrhrfgei arplrlvrpa grqvgaavgw glakaaltlv lvvalpaalv
      121 esgggeggyp agsplaqfaf afafgavvsp lyeeilyrgv fyqglaarlp avaavvlsaa
      181 ffavvhlprv fntvsalfag llfawllhrh rnlwvpilah avsngtlval afaaeasa
//
LOCUS       WP_457604547             424 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604547
VERSION     WP_457604547.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43594
     Region          24..374
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,75,130..131,133..135,138,158,
                     161..162,165,242,245..246,249..251,254,278,282,338..339,
                     343,347,363,366..367,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtatartsgp vdappgglfr hrdfrllwta htvsavgnnm tvvalplvav avldattfqv
       61 avltaaawlp wllaglpvga wvdrvrrrpv miaadlvaaa lfasvpvaal lglltvghll
      121 vvalgaglar vffetadqvh lptllrpgqv peanarlhat qtasylvgpg laglvaqlvg
      181 avaavaldal sfllsalclr riraaeprph rpagttslrr evaaglrfvv rdpylrvltv
      241 fgaasniglt gyqavlvvfl vrsaelpagl vglliglasl ggvigaalaa rlsrrlgsar
      301 tllvagaltg ppalliplag pgertgwlvl ggvlvslgva vgnvvkgsfr qtytphrllg
      361 rvtvsmqlln ygtiplaall agalgaawgp ggairvmtaw laltplilla gplrkrrdlp
      421 aapf
//
LOCUS       WP_457604548             549 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604548
VERSION     WP_457604548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..549
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60155
     Region          15..544
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mrlvtraata alrlpaartg rvtvtrdipv rvrdgvtlrt dhyapglpaa pcvlirtpyg
       61 rggpirllgr liaergfhvv iqscrgtfgs ggefaplvhe rddgldtldw lrrqrwwtga
      121 fgmfgasyqg fvqwalaaea gdelramvav vtasatrdst yagesfaldt vltwaellqa
      181 qtvpwlarqw elkrgqprla ralahlplae adrvatgvtv pffqewlrhh tpdadywrtr
      241 vfgdritevq apvamvsgwq diflpaqldd yarlraagtr trlvvgpwth gspglllasl
      301 regldwldth lagrpgpera pvrvhvggdg ggwrdlpdwp ppatparwhl rsagglapep
      361 qergapdriw ydpadptpsl ggpllvaqra gavdnrpvea rpdvltytse plrdpvevag
      421 pvraeihlrs elsyldvfvr lcdvdrrgrs wnvcdglvrv epgrfprdps gvvtvpvtlw
      481 ptayrfasgh rlrvqvsgga hpryarnpgt geplgtavtl ragwreilhd rehpsvlvlp
      541 lvpapstag
//
LOCUS       WP_457604549             221 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604549
VERSION     WP_457604549.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..221
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23133
     Region          6..137
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mttplyddia dwyeeyaset ssvymdrvrs vladllgdgp grcvdlccgt gahaaelrrl
       61 gwtpvgvdls ggqlrharar lpvaradata lplatgtvpa vvcvlahtdm pdypaavaea
      121 arvlapggrl lhvgvhpcfv gafadrsepe rividggyas rdrtvrswna tgvrarvgaw
      181 hlplagllda vaaaglrltr vvesgsgpip dvlaleatkp h
//
LOCUS       WP_457604551             265 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604551
VERSION     WP_457604551.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..265
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28726
     Region          7..265
                     /region_name="Oca4"
                     /note="Protein tyrosine/serine phosphatase Oca4 [Signal
                     transduction mechanisms]; COG2365"
                     /db_xref="CDD:441932"
ORIGIN      
        1 magrewelvg apnardlggl pttdgrrvra grlirtpalg rltdedlpvl gklgpacvvd
       61 lrdvheqava ppdrlvgepr tvhlpvydaa hpvftyvsav lqghdldaya alaregmpva
      121 mtaiyrwfvt gesaragfga avrlaaegan lpllfhcsag kdrtgwlsvv lltalgvede
      181 airadylvhn elteslrevl lsamiqrrpd ldpavarpll evrpeyldaa ydevrrahgs
      241 fdaylrdglg vtdadraalr erlle
//
LOCUS       WP_457604553             172 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604553
VERSION     WP_457604553.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..172
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19043
     Region          6..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 myrrrddprg rmvaditndl rrysvdaqhi ghafaglhgl natdlyalia vmeaelvgdp
       61 itpgrlgeal nlssgsvtal vdrlergghi rrdrdtadrr killhyadrg atlaqsffgp
      121 lgrrtdevmd rfsddelavv hrfmaemvhs mrthrdeira aprrggasgp ad
//
LOCUS       WP_457604560             305 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604560
VERSION     WP_457604560.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 12204063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..305
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32824
     Region          197..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmvttgqpsp atrtglpelr pgtdeivtgv lgdlaaepgw prpvlldrdl lilvthghgt
       61 aeldfrpvpc rpgtllrahp gqalrfvgaq ldatvvswrp dalrgldvdp davpahrqla
      121 gededavise vsqlavdadr halvpaaaal lrhqlavlll rlsllphpgd gatpraetet
      181 frrlcrever gyrhtrrved yaaqigcsvr tltraclavt grsakqvide rvalqacrll
      241 aatdesiaai grelgfpept nfgrfftrev gvspgtfrae rerplavrlv rprppadspv
      301 pggqa
//
LOCUS       WP_457604561             187 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604561
VERSION     WP_457604561.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..187
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19777
     Region          26..176
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mttvdrpgaa tvelrpvdvd sfrgllrrqa stvtvvttpg lrgnrmrpdl ppagftatsf
       61 tsvsldpplv svclgrasss wptveqaehv avhllasgqq eiaqifatsg idrftahpgw
      121 tigpfgvpli gdalavllcr vvrrieagdh tillgeplal gagedgdpll hhrdgytttl
      181 gdwpeaw
//
LOCUS       WP_457604562             467 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604562
VERSION     WP_457604562.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 467)
  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 467)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..467
                     /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=49403
     Region          152..463
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msrwirgplp rlglrarlla lgvlglavgf afggtlllga lgwtlqrsvd eealrtadav
       61 allaaedalp dplpvaggql rvqvvdaqgr iraasidadr lvpmlgpdel rpgqrqrlvv
      121 dgrragmpgp vrvvtvpagt aqeprtvlva ksltdvrhsl hvvrnlllvg fpllvaglgv
      181 vawrvvgatl rpveqlrsga aeitgragae rlpvpagqde ihrlavtlnd mldrlaasrd
      241 rqrafvadaa helrspltnm rtelevarrl ggdtdwpava ddlladterl srlvddllll
      301 arldeqdarp spvgpvelge llrgvaaryp sppvrltppd aprwvegdag elrrvlvnlv
      361 dnalrhassa velavsgpdg ayhlitvtdd gpgipaadre rvfarftrld darardagga
      421 glglaivrel vrraggtvel adatpgaaap glratvrlpa laepdae
//
LOCUS       WP_457604563             669 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-galactosidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604563
VERSION     WP_457604563.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..669
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73790
     Region          4..613
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          605..660
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mrnwhgdgiw ygadynpeqw peqtwaedve lmrragvnlv svgifswall epapgryvfd
       61 wldraidllh dggisvdlat ataspppwla hrhpetlprr adgtllwpgg rqaycpsspv
      121 frdhslalve avarryarhp avvlwhvsne lgchnvhcyc dvsaeafrgw lrerygdlds
      181 lnaawgtafw sqryhdwaei npprtaptfa nptqqldflr fssdeqraql raerellnrl
      241 vpqpvttnfm igtgikyldy hswasdvdvv sndhyltaad pqpqvnlala adhtrgvagg
      301 apwllmehst savnwqprnv aktpgqmrrn slahvargad gvlffqwras ragaekfhsa
      361 lvphagpdtk vfrevcrlga dlralaevrg srvdadvail fdyeawwgae ldshpsvdvt
      421 ytdrlsalha alwragvtad vvhpsadlsr yrlvvvptly lvrdadadal rrfvetggta
      481 vvtyfsgivd ehdhirlggy pgafrdllgv rveeffplre getvrlddga radvwtewlh
      541 aegaevlaay tdgplpgvpa ltrhavgaga awyvgtrldd eatdrlvarl laetgvrppv
      601 napagvevvr rrsadrswlf vvnhttepar lavsgvellg garcdgelev pagevavvre
      661 epapvpata
//
LOCUS       WP_457604564             318 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604564
VERSION     WP_457604564.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..318
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34778
     Region          58..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdlpliqed ravpppaatt tnggrgrrlr llsrtdrvvi tlmvlvplll vtglvwlpav
       61 atvllsgtnw dgigpiseie wvgaknyddv vniyppfvpa vqnnllwlaa lfvvatpfgm
      121 flavlldkei rgsrfyqtal ylpvvlslal igfvwqliys rdqgllngvf ggdtdwygdp
      181 dvniwavlva agwrhvgyim llylaglkgv dpslreaaav dgssetstff rvvfpvlrpi
      241 niivlvvtvi eslrafdlvw vinkgrngle lisalvtqnv vgeasrigfg salatimlav
      301 slvfitiylw tvmredkr
//
LOCUS       WP_457604569             363 aa            linear   BCT 27-JAN-2026
DEFINITION  mannose-1-phosphate guanylyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604569
VERSION     WP_457604569.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Pelissier,M.C., Lesley,S.A., Kuhn,P. and Bourne,Y.
  TITLE     Structural insights into the catalytic mechanism of bacterial
            guanosine-diphospho-D-mannose pyrophosphorylase and its regulation
            by divalent ions
  JOURNAL   J Biol Chem 285 (35), 27468-27476 (2010)
   PUBMED   20573954
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 363)
  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
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Shinabarger,D., Berry,A., May,T.B., Rothmel,R., Fialho,A. and
            Chakrabarty,A.M.
  TITLE     Purification and characterization of phosphomannose
            isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A
            bifunctional enzyme in the alginate biosynthetic pathway of
            Pseudomonas aeruginosa
  JOURNAL   J Biol Chem 266 (4), 2080-2088 (1991)
   PUBMED   1846611
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="mannose-1-phosphate guanylyltransferase"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0004475 - mannose-1-phosphate
                     guanylyltransferase (GTP) activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0009298 - GDP-mannose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38127
     Region          1..356
                     /region_name="CpsB"
                     /note="Mannose-1-phosphate guanylyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0836"
                     /db_xref="CDD:440598"
ORIGIN      
        1 mfyavipagg sgtrlwplsr aghpkflhpl tgtpasllqa tvdrlspltt pertlvvtga
       61 ahaaavarql aglpeenilv epsprdscaa ialaaaviaa rtpdavmgsf aadhligdpa
      121 rlaevvrqai rgaeqgllmt vgitptrpet gygyletgep agdgplrpvr efkekpaaev
      181 aevyvrsgrh lwnasmfvwr vdvflselar qqpelhagit aiaaawgtpe qddvlgriwp
      241 tlprisvdya vmegaatagr vatvpgdfgw ndvgdfhtlg evlpadgagn vvlggdakpg
      301 vllhdttgtv vvphsgrlva tvgvhdlivv dtpdallvcp rdraqdvkki vdelkergee
      361 glv
//
LOCUS       WP_457604573             473 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604573
VERSION     WP_457604573.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..473
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51170
     Region          36..418
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtlphtgral adaapvsywl drparpdplp plagthtadl lvvgggyagl wtallakead
       61 pdrdvllvea gtcgwaasgr nggfcaaslt hglangverf pgeigelerl grenldaiaa
      121 tvakydidcd fertgelava vepyqldgla adadlarryg hdvrlldrde vraevaspty
      181 lggmwdrdrv alldpaklaw glrraaldlg vrvhehtrvt glagdgaalr attaggadaa
      241 pgavrarqvv latnafppll rrlrswivpv ydyalmtepl tgaqrdaigw rhrqgladag
      301 nqfhyyrlta dnrilfggyd avyhygnrva paleqreatf ttlashffat fpqldglrfs
      361 hrwggvidtc trfcaffgta ysgrlayaag ftglgvgatr fgarvtldll sgtdtpltrl
      421 dlvrrkplpf ppeparsvgi nltrwslara dardgrrnlw lrtldrlglg fds
//
LOCUS       WP_457604585             413 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604585
VERSION     WP_457604585.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 413)
  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 413)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..413
                     /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=42511
     Region          195..409
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtvrgvfapl vrastwrrav flllggvlal pyallavvfa qmlgnatapr plvlgllvva
       61 aglavvpvfl agsraleiaa arallavdlp epapghridr etrlraalwi alhlgtgavv
      121 wfaaisafpm alvfvaglag mdtgavadqr fgpvdpahpv qaglaglavl aglgyavagl
      181 galaasmapv llgpaqaeri aaleahavrl aernrlarel hdsvghaltv atlqagaare
      241 lldtdpefsr raltaieets rramddldhv lglireagaa tapapqstla gldrlvaaar
      301 aagldvesrv dgaldalpav vsregyrivq egltnaarhg rgpvalrvav ppeglaielv
      361 nsvrgaagpa rggrgldgmr ervlllggrl dagpdgdrwr vratlpvprg evr
//
LOCUS       WP_457604603             372 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604603
VERSION     WP_457604603.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40863
     Region          1..106
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          72..361
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mtpfridvpe avlddlrarl srtrlapaap gepwaagtdp gyladlvryw ldgfdwrave
       61 ralnrypqfv ttvrgtpihf vhvrsaspda talilthgwp stytemlplv srladfdlvi
      121 pslpgfvfsg plaegpttea avadvwaelm trlgydrfga yggdvgsgvs twlgarhadr
      181 vigvfsqhik fppadrrgel spaeeafiam ldakaqddwg ygiiqetrpd tlaaalsdsp
      241 sglaawiiek yqrwsdcggd isrrfgfdel lttvmlywvt ncistsfrpy rddhlaphlp
      301 mvtvpagitv svedaglprs faertyanlt hwrepsvggh flaqeepdll aadlraffna
      361 lrcsrsptgd vv
//
LOCUS       WP_457604607             325 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604607
VERSION     WP_457604607.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..325
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35658
     Region          6..276
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtrtflqpdd lhdlvsdqfg sdrrlaaldr ltggtkkgvy rlrlddrttv mlyvwaagen
       61 ywppspavpd dpftdasgad lfdaahaalt gagvrvphll midrdgshld adialvedag
      121 alrlealveh dpaaavtpls algdalrrmh tafgphygkv aaiargeasq trrtedvivd
      181 ralghldaaa ardarladah hrvaahvrhl rsavtpreey glvhgelgpd hvlvtpvgea
      241 vmidfeglty fdvewdhawl qmrfgetypa lrpvaldphr lalyryaqtl sliegplria
      301 dtdfpdrkwm ldlaewnitk alaai
//
LOCUS       WP_457604616             562 aa            linear   BCT 27-JAN-2026
DEFINITION  hydantoinase B/oxoprolinase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604616
VERSION     WP_457604616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Watabe,K., Ishikawa,T., Mukohara,Y. and Nakamura,H.
  TITLE     Cloning and sequencing of the genes involved in the conversion of
            5-substituted hydantoins to the corresponding L-amino acids from
            the native plasmid of Pseudomonas sp. strain NS671
  JOURNAL   J Bacteriol 174 (3), 962-969 (1992)
   PUBMED   1732229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..562
                     /product="hydantoinase B/oxoprolinase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60662
     Region          2..562
                     /region_name="HyuB"
                     /note="N-methylhydantoinase B/oxoprolinase/acetone
                     carboxylase, alpha subunit [Amino acid transport and
                     metabolism, Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0146"
                     /db_xref="CDD:439916"
ORIGIN      
        1 mttldgaqve vvrsyllsaa eemratlirt sfnpviyevh dfglsmydad lrlvaeatgl
       61 tfflgandfs lrkgveyvgr enlhrgdvvl lnypywnaah afdatlfapv frpdeadpda
      121 dgdlvgflcv rahwmdlgak dpgyvldstd mhqeglifpg tkvvsrgepv reihelirfn
      181 srmpdavlgd lhaqiaalrt gerrmleiie kfgrdtvnqa idriiadgea raraalatlp
      241 qgtwtaedwv dddgisddpv kmrvtvtiad grfvvdfags apatrgpinm pfgateaick
      301 vvlksvtsrd epsnagtvap levraepgtl fhavypqptf tlwtgivave lilkalaqgm
      361 pdllpassgg dvpgfmmvgl hpdtgkmfav snndlvgwgg taqhdgmdaa thvsgstgrg
      421 tpievmeakt gmfferweir edsggagrfr ggcglrrdir fvtpgefltv ikktksapwa
      481 ldgglqpepn qivvfpgtdr ehrvstkrtt vavgdrvtll tagggghgdp rgrdpeavrr
      541 dvaegyvspe aardvygvdv dg
//
LOCUS       WP_457604614             376 aa            linear   BCT 27-JAN-2026
DEFINITION  SPFH domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604614
VERSION     WP_457604614.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11213143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..376
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=40349
     Region          26..236
                     /region_name="Band_7_1"
                     /note="SPFH domain-Band 7 family; pfam13421"
                     /db_xref="CDD:433193"
     Region          313..362
                     /region_name="GYF_2"
                     /note="GYF domain 2; pfam14237"
                     /db_xref="CDD:464112"
ORIGIN      
        1 mglmdklrge lidivewldd srdtmvwrfp ryqneikmga klvvresqta vfvnegkiad
       61 vfepgtytle trnlpilstl kgwkygfnsp fkaevyfvnt rqftdmkwgt qnpvilrdae
      121 fgvvrvrafg afaarvvdas rllrelvgtd pqfrteevqe ylrqlmvgrl ggalatagvp
      181 lldlaahqda igrrlaavlt eelaevgiai pkfvienvsv ppeveqaldk rtsmgavgdl
      241 drytrfqaan ameaaannpg geagagiglg lgmamgqqma rsmgggaatq ppqpapaqpa
      301 aaeppplpgq aqwyvgvggq rqgpydlgal aeqanagald adtlvwrtgm aqwqpagqvp
      361 elasvlasvp pplppq
//
LOCUS       WP_457604619             363 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604619
VERSION     WP_457604619.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37867
     Region          130..363
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mrltvlvgpg lvadaallas staatcaeld vagevvtaas ademrallat adqpvvvlpg
       61 ptaaaralig aqpsgvvwyd ltvepsvpga vhlagrglwg ltwairhavh rlrapatria
      121 ygpdpdqwgd lrlpstpdag papvavllhg gfwrsiwgad lmdalavdla rrgyaswnle
      181 yrrpdrhgwd attqdvqagl lalrepardr lvdldrivvl ghsaggqlal raaadlaart
      241 sgprvalavs lagvldlteg errylgdgav aaalggspvt aprryaesdp mlrlptgvpt
      301 llvqgtedsl dlvdanrrya aaaaaagdei rhleqpgdhf avidpasavw qdtmtavdar
      361 lgr
//
LOCUS       WP_457604623             221 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604623
VERSION     WP_457604623.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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 221)
  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 221)
  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..221
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>221
                     /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..209
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mqigllgpfq vttdggvpad vpgarlrgll aalalqpgrv vpkatlvdwi wgeqppadaa
       61 nalqrlvsrl rkalpagavd glpdgyrlav epdavdavrf erlvrrardg dgpqrvrllr
      121 ealglwrgda lrdiglpdsp aldaaatrle rlrltatedr ydaeiglgre adlipeltdl
      181 vaahpvrerl atalmralva agrptqarrg ehrppparah p
//
LOCUS       WP_457604626             294 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604626
VERSION     WP_457604626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10218577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..294
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016208 - AMP binding [Evidence IEA]"
                     /calculated_mol_wt=29842
     Region          4..140
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
     Region          152..287
                     /region_name="Usp"
                     /note="Universal stress protein family; pfam00582"
                     /db_xref="CDD:425765"
ORIGIN      
        1 mnrpvvagvd glpsslaaad laaatavars rplllvhgyl hpmgygvpln pydlgvpapt
       61 aesekmlesv aadlaerhpg lrvqvrqvag gpgatmvees rraelvvvgs rgvggfagll
      121 lgsvsgqlaq hghcpvlivr peeqpipvdg pvlvgvdgsd saayaielaa deadrrdael
      181 vlmhvrsper gavapevaae astaaraeaa gllaeaaarv raahpdlrva eravtaaspe
      241 talreasgea slvvvgsrgr ggfaglllgs vsqalvqhsh cpvlvahrpe padd
//
LOCUS       WP_457604634             695 aa            linear   BCT 27-JAN-2026
DEFINITION  primosomal protein N' [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604634
VERSION     WP_457604634.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Bhattacharyya,B., George,N.P., Thurmes,T.M., Zhou,R., Jani,N.,
            Wessel,S.R., Sandler,S.J., Ha,T. and Keck,J.L.
  TITLE     Structural mechanisms of PriA-mediated DNA replication restart
  JOURNAL   Proc Natl Acad Sci U S A 111 (4), 1373-1378 (2014)
   PUBMED   24379377
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Manhart,C.M. and McHenry,C.S.
  TITLE     The PriA replication restart protein blocks replicase access prior
            to helicase assembly and directs template specificity through its
            ATPase activity
  JOURNAL   J Biol Chem 288 (6), 3989-3999 (2013)
   PUBMED   23264623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11487457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..695
                     /product="primosomal protein N'"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006270 - DNA replication initiation
                     [Evidence IEA]"
                     /GO_process="GO:0006302 - double-strand break repair
                     [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=72023
     Region          2..695
                     /region_name="PRK14873"
                     /note="primosomal protein N'"
                     /db_xref="CDD:237844"
ORIGIN      
        1 mdvplphldr pfdylvpeal dadarpgvrv kvrfagqlvd gwlleraess ehpklaylek
       61 vvspvpvlsp evarlarava dryagsladv lrlavpprha raekavttdt pptdepapgg
      121 tepdgspadg tepdgspadg tepdgspadg tatadgtapg gvpseaadag arpggraevd
      181 prgwrdypag pallraltdg rparavwsal pgedwadrya davaatvagg rgavvvvada
      241 rdldrldaal tavlgagrhv rlaaadgpar ryrafltart ggvdvvigtr aamfapvrrl
      301 glvaiwddgd dlhaeprapy phardvlltr aqlgdiaavv ggyartaeaq llvetgware
      361 vvadravvra rtpsmaptgd dpqlardpga asarlpslaw ttardalrad lpvlvqvprr
      421 gyvpsvacad craparcphc agplalpsaq gtpacrwcgr vaaayacpec ggrrlrasvt
      481 garrtaeelg rafpgvpvrt sgreevlatv pggaglviat pgaepvaegg ygavllldsw
      541 alltradlra geealrrwma aaalarpgta ggrvvvvadg alapvqallr wdsawfaare
      601 laerrelgfp pavrmasvtg aaeavadlla garlpgdaev lgpvpadegr ermlvrvprs
      661 raaamaealh aaagqrsark aadpvrlqvd pltlf
//
LOCUS       WP_457604644             216 aa            linear   BCT 27-JAN-2026
DEFINITION  GIY-YIG nuclease family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604644
VERSION     WP_457604644.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..216
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24079
     Region          71..>120
                     /region_name="MUG113"
                     /note="Meiotically up-regulated gene 113; pfam13455"
                     /db_xref="CDD:372608"
ORIGIN      
        1 mkgcgysgcs ntsavnkygv elclehgivl hntvrveafs kkvsrlyeng dltqhsagit
       61 yiiqlpnhni kigttkngrt lysrlrnlsn eqrgkvtlla tlpggetqea vlharfseyr
      121 rydlfveqfs paaelfyfak etgleseglw akqafdlwef tpgtivepte edrkylavac
      181 tscgaevdep cswkvdtaea ihasrksrld ylltsr
//
LOCUS       WP_457604662             610 aa            linear   BCT 27-JAN-2026
DEFINITION  NHL domain-containing thioredoxin family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604662
VERSION     WP_457604662.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Kumari,P., Aeschimann,F., Gaidatzis,D., Keusch,J.J., Ghosh,P.,
            Neagu,A., Pachulska-Wieczorek,K., Bujnicki,J.M., Gut,H.,
            Grosshans,H. and Ciosk,R.
  TITLE     Evolutionary plasticity of the NHL domain underlies distinct
            solutions to RNA recognition
  JOURNAL   Nat Commun 9 (1), 1549 (2018)
   PUBMED   29674686
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10221804
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..610
                     /product="NHL domain-containing thioredoxin family
                     protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=64440
     Region          8..132
                     /region_name="Thioredoxin_like"
                     /note="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold; cl00388"
                     /db_xref="CDD:469754"
     Region          209..535
                     /region_name="NHL-2_like"
                     /note="NHL repeat domain of NHL repeat-containing protein
                     2 and similar proteins; cd14951"
                     /db_xref="CDD:271321"
     Region          229..278
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          296..334
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          350..391
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          403..443
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          446..484
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          494..535
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
ORIGIN      
        1 msarvrapel rgrawlntgg kavtladlrg kivlldfwtf ccinclhvld elrpledkyg
       61 dvlvvigvhs pkfehekdpa alaaaveryg vhhpvlddae mdmwqqyaak awptlavvdp
      121 egyvvatmag eghaeglarl ideliaghea kgtlhrgegp yvppaepdtv lrfpgkalpl
      181 dggnllvsds arhslvelaa dgetvvrrig agsrgrtdgp asaatfaepq glcllpphva
      241 evagydvvva dtvnhllrgv rlssgevvtv agtgrqwrst vddhahdara vdlsspwdva
      301 wyddrvvvam agihqlwwfd pikrtagmya gttvealrdg plpdvwmaqp sglsvsadga
      361 rlwvadsets airwvsdgvm htavgqglfd fghvdgpadq allqhplgvc alpdgsvlia
      421 dtyngavrrf dpetgqvgtv adglaepsdl vltgegdvlv vesaahrltr lapgaltsag
      481 antvdgprhr lerkptdvaa geltldvift papgqkldet ygpstrlvvs asppellveg
      541 agtttdlsrk lvvsgdvaqg vlqvtaqaat cdadvehaac hltrqdwgvp vrvvtggatr
      601 vplvlrgmda
//
LOCUS       WP_457604664             210 aa            linear   BCT 27-JAN-2026
DEFINITION  septal ring lytic transglycosylase RlpA family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604664
VERSION     WP_457604664.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Jorgenson,M.A., Chen,Y., Yahashiri,A., Popham,D.L. and Weiss,D.S.
  TITLE     The bacterial septal ring protein RlpA is a lytic transglycosylase
            that contributes to rod shape and daughter cell separation in
            Pseudomonas aeruginosa
  JOURNAL   Mol Microbiol 93 (1), 113-128 (2014)
   PUBMED   24806796
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..210
                     /product="septal ring lytic transglycosylase RlpA family
                     protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0008932 - lytic endotransglycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21046
     Region          101..210
                     /region_name="RlpA"
                     /note="Peptidoglycan lytic transglycosylase RlpA, contains
                     C-terminal SPOR domain [Cell wall/membrane/envelope
                     biogenesis]; COG0797"
                     /db_xref="CDD:440560"
ORIGIN      
        1 maarhlrtrk fsspaaiaat aavgvalavg gtvgavrlts aeppaepavv etlpstpapt
       61 saapspsasa spsaslspsp katpspkasr tqaasrskar taspsptakk tsspkvvdsg
      121 scgasfyaeg qmtangetfn pnaltaahkt lpfntkvrvt npdngksvvv rindrgpfid
      181 grcldlsraa fatiaatslg hvnvryevlg
//
LOCUS       WP_457604666             188 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604666
VERSION     WP_457604666.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19969
     Region          4..156
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mpelerlaah hapavlrfer enrayfaryv pdrgddfftg yaarhaalld eqergtchfh
       61 vlvgdhgavl grfnlvdvag gsaelgyrva ehaagrglag egvrrvcela rteyglrrlv
      121 asaalanpas lavlkragfv ldgsergdsv hdgsvrsgsv sgcevdldge pglrhvldlr
      181 apyaaasp
//
LOCUS       WP_457604674             343 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604674
VERSION     WP_457604674.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..343
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36409
     Region          38..>205
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          <236..343
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 malhaprpss srsvdrsttv prtrwsrftt alaalvgtav vltggataah aepsvaeiea
       61 qidrdwnkle pvieqvnavr eqlaarrkqa dalgrqiapl qarvdaalgq vgglaadvyk
      121 gdnlstvnal lgsrspgdlv nglelldrfa hrqheqvrsv aalrdelaak kkpldemiag
      181 larteaqlaa kkkqidaeia rlqklrlkvy gnggggplrp apcpagypgg aagaavkfac
      241 aqigkiyvwg aagpdhfdcs gltmaawakg gvslphnarq qhgmtkrvsr aelragdlvf
      301 yysdlhhvam yvgdgwvvha sqsgkpitmk rvddgdinsy grv
//
LOCUS       WP_457604680             489 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604680
VERSION     WP_457604680.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..489
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50613
     Region          4..486
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 msrikefnlp dlgegltege ilawlvkvgd dielnqpive vetakaavei pakwagrvqa
       61 ifhpegstve vgvpiiaidt dpnagpiees ttatpasdlp apsaaslaav qvapaegmve
      121 pgliggvapg grtavlvgyg prnapakrrp rkgdapaaap iqaaapvapa pvapapvapa
      181 papavngngr vsgpvlakpp vrklakdlgi dlatltgsgp lgsitredvq raasatpaaa
      241 epltvaapaa saasfgadre qripvkgvrk ltaenmarsa ftaphvtefl tvdvtramka
      301 ldrlrdrrew rdvrvsplll vakavllavk rhpmvnstwa gdeivvkeyv nlgiaaater
      361 glivpnikda grlslrelad amtelvqtak sgrtspadms ggtltitnvg vfgvdtgtpi
      421 lppgesaila fgavreqpwv hkgkvkprlv ttlglsfdhr iidgelgskf lrdigdflad
      481 peaallawt
//
LOCUS       WP_457604684             126 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604684
VERSION     WP_457604684.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..126
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13293
     Region          8..109
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mhrsrlyali idaprdeage taafwsaalg aslrtdpaep eftgladvvp glvtavqsvd
       61 daprhhldie tddvaaever lcglgaapvs rwldchvlra pgghllcvip vasdsalfes
      121 tatrwp
//
LOCUS       WP_457604690             110 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604690
VERSION     WP_457604690.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..110
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12316
     Region          2..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mifitakfrv rpedadrwpq iaadftaatr aepgclwfdw srslddptey vlveafrdde
       61 agaahvqseh frtaqrtlpp hlaetprivn vtvpqqdwsr lgelavpgda
//
LOCUS       WP_457604694             289 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604694
VERSION     WP_457604694.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..289
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29367
     Region          4..266
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mtgpelaeag rllaaarrpv vftgagmsae sgvptfrdaq tglwqrydpl elatpaafra
       61 dpalvwgwye arrhgvrral pnpghravaa irarcpetvv itqnvddlhe rggvpapvrl
      121 hgslfaprcs acarpapipe daaapgddap pgdaaapdgm pephagpltp pacagcgapv
      181 rpgvvwfgea lpsaaldaav eaasgcdlll tvgtsalvhp aaeiplvaar lgapvvqvnp
      241 vptpldaica vnlrgpagev lpalvraawp dadaawpdad aawpdadag
//
LOCUS       WP_457604696             250 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604696
VERSION     WP_457604696.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..250
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26290
     Region          1..245
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mqpttvdvpt pdgtadayla tpgtggpfpa vllfmdafgl rprvaemaat iaergyvvla
       61 pnlfhragra plidlgalad dsrrgalfes igpmmaaltp davardtaay ldflaarpdv
      121 apgpavitgy cmggtnalra iealpdriaa vaafhagrvv tdapdsphla vgavtgelyf
      181 ghadadpsmt aeqiatleka ldaagvtyrs evyagarhgy tqsdtpmyde qatkrhwtal
      241 fdlldrtyrr
//
LOCUS       WP_457604698             432 aa            linear   BCT 27-JAN-2026
DEFINITION  FUSC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604698
VERSION     WP_457604698.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..432
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45246
     Region          73..236
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 madrradtvr spldraverg glalsrarae ggaagrnrlr qlevtvvisa qaglaaalaa
       61 lladellgsg ahvfapaaav gtiataigqr arrtfellig vglgilvgdl lrallgsgsw
      121 qtglvvtlai atallvagrg galvgqaggt avliatlapv qpglelprif dalvgglvgl
      181 fvvalllpvn pirvldrave pvvarlteql davahaltrr dadaaqrale dlrgiepdig
      241 rlndalsgae evvtiaparw hrralfhrya datqhlerlv lyarsiarrs atalqydepi
      301 ppalpdavar lgeavreler acksgedler trelvrqgae lagrawsqgv rtygeamisd
      361 lrtgqsellr atgcrpedan gtvrraagag eaearppvra rmsrpvprrp agrhqpkatg
      421 relaparagp ag
//
LOCUS       WP_457604704             544 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604704
VERSION     WP_457604704.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..544
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=55634
     Region          8..259
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,67,72..75,87)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,70,86..89,93,95,132,134,
                     136..137,139,149..150,153,167..170)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,70,86..89,93,134,136..137,
                     139,149..150)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,93,95,132,134,136,153,167..170)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(149..157,164..170)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msgwelsgyt pvrrlgagas gsvvlathda tgtpvaikyl irdlgedsaf rtafrtearl
       61 lgeiddpnvs rlyeyvespy gaaivmelvd gvslrqmlre hgpttpeaal cvlkgslagl
      121 aaahthgvvh rdykpenvlv tgtglsklad fgiampigqg sdttvsgtpr ymapeqwtga
      181 pagpacdvya atatffeclt grppyqgpdl lslrdqhasa pipaeaappp vhellrhgma
      241 krpderppsa eaflellerv agtgygpewe erglrelarr alllaalwpf pdraegatav
      301 ahtelgtttt grsgrfrkgr trtvlaagal aaavlaggag ysyaahddts aagptgpasa
      361 apattgapvp dptgaetpsp sptpspstvs atppppapsa tpdptgtptr tgtptpsasr
      421 ttsppppdvt apvvdgvsad pgeldpkgcp ygaksstvta tvtddrsgpa altvtfgytv
      481 dgatgtirma aagrgvftgt lgplstpkrs aripirvtaa daagntttst spvyvtlyhd
      541 ctpg
//
LOCUS       WP_457604709             226 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604709
VERSION     WP_457604709.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..226
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23608
     Region          15..225
                     /region_name="Oca4"
                     /note="Protein tyrosine/serine phosphatase Oca4 [Signal
                     transduction mechanisms]; COG2365"
                     /db_xref="CDD:441932"
ORIGIN      
        1 mitrgatada ttggsgvrnl rdaggvgslr rgvlyrsgal hlltpegare ledlglrtvi
       61 dlrsirevad rpdrcaglgv ehchfpvftd qswpddqval ypymaeqagr vtvaiirqli
      121 tpgalpalvh casgkdrtgv vvaviqtlln asdaevtqdf lrsnaaldlt gspagaaigh
      181 gtrpvtaahl lhamvwirsh hgsvsaylqa agateaelea lrgvla
//
LOCUS       WP_457604710             333 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604710
VERSION     WP_457604710.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..333
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36071
     Region          10..276
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msvsptqrvl dpdqvrrhlt asfgsgaeva gcgpltgggf aavwwvrltd grevvlkvgp
       61 aphvpllrye rdmigaeahy lrlvadrapg vptpallhhg tdpdlgdwll marlpgrtlw
      121 dlsragadvg plraefgral aalhgvtger ygydgdrasg atwrdaytam vddmladaad
      181 wavplpapat rirelvarha evldavrrpa llhfdgwagn vlavdgpdgt prltglvdge
      241 rylwgdplmd lvspllfrra edepddplvr ayraaapfpf dagarrrlgl yrlylyllmt
      301 vempsrnita dndpgrvell aellgaelad lad
//
LOCUS       WP_457604713             262 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604713
VERSION     WP_457604713.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10595285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..262
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28231
     Region          5..241
                     /region_name="Y_phosphatase3"
                     /note="Tyrosine phosphatase family; pfam13350"
                     /db_xref="CDD:463853"
ORIGIN      
        1 mttppdfatl cnfrdlggwr tgdgrtvarg rlyrsdslak lagedlerfa algvrtvidl
       61 rypweiadrg rapeslgvtw lnlsiehrpy vqadidpdvd pwryladrya evaedgvael
      121 rqaieviadg ehplvfhcas gkdrtgllaa lvlsllgvde dqiaadfalt eqatdrlvae
      181 wrdrnggatp gwpaygrapa eiirlvlaal raahgsvhgy vtgrlgvgqe tiaalrarll
      241 tgdtnplptq gttgstptpa ar
//
LOCUS       WP_457604717             381 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604717
VERSION     WP_457604717.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..381
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41118
     Region          3..375
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdevalrsli pgvlgvlvrr gadfaaaeda vqdaliealr vwpadqprdp rgwlvtvawr
       61 rfldvvrada arrrredlvd eepppgpvpa vddtlrlyfl cahpslspss avaltlravg
      121 glttrqiaqa ylvpeatmaq risrakrtvs gvrfdragdv gtvlrvlylv fnegysgdvd
      181 laaeairltr qlaaaidhpe vagllalmll hharragrta pdgslvplae qdrsrwdttl
      241 iaegvgilqt alsrdrlgef qaqaaiaalh adapaaaetd wvqivewyde lvrltgspia
      301 rlnravavge adgpraglaa laalddtlpr ytavaaylhe rdgdpdraaa lyaeaarras
      361 slaerdhlhr qaarlnsrrp g
//
LOCUS       WP_457604734             339 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604734
VERSION     WP_457604734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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   2  (residues 1 to 339)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..339
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35777
     Region          1..339
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mshvtledva raadvslata sralngrrvt phlhdrvlaa aarlaytpna haralagasr
       61 rsvgvvchdv tdpyfaavag gvmrvaadnd llvmlastfr dpereiayvs mlraerapai
      121 lligsgfedp rweramaael apyldgggrv avvsrhrtlk vdsvlpenra gaaelarall
      181 glghrrfavl sgppelttva drlggfrdel aaagvtldpg evaeaaftrd ggyramtell
      241 drgldatcvf actdvmavga yaalrdrgls vpgdvsvagf ddipvvrdlt pplttvalpl
      301 hrlgeeamkl altenagrrr rivrlpgevv mrastapva
//
LOCUS       WP_457604735             313 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604735
VERSION     WP_457604735.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..313
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34576
     Region          59..311
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mcyghdghaa lrqsldrrdl lrgslaalag iglatglgat aaqagghhhg rrpvpkelis
       61 lqlwtvrdal ngspgydatl ahlarigypr velalgyfgr tarelrrfld gigikasssh
      121 dgiaadaaal eqkianartl gqrfmvvpyl nsdreddwkr waeqmnveaa aarkaglryg
      181 yhnhahefti dfgngrrpwd vlteeldprl vhleidiywa vtgginsgeg vddpegftld
      241 virsapqrvl qyhvkdrdpa tgdmadlgtg midfarifrg hqvmeyiven dtpdvtpqqt
      301 vavgyrylrr lrf
//
LOCUS       WP_457604736             243 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604736
VERSION     WP_457604736.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..243
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25351
     Region          29..134
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mariayadad aeafaatrhl tddgltawra avarhlvprp gmrlldlgag tgswahaftd
       61 wfpgvevvav epsaamrarc gfaplvagda ghlpladgsv ggawlstvih hvpdlaaaac
      121 elrrvlrpga pvlirsafag rheaitlfdy fpeairvldt ypgiadveaa faaagfataa
      181 veqvpqvtas slreaaaglr reahtplqli tdaeyaagvq rlheaaqads gpvidaldll
      241 vlr
//
LOCUS       WP_457604745             258 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604745
VERSION     WP_457604745.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26222
     Region          21..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msplsyvvtg ggrgvgravv erlaadggtv vvierdtgal gwlarhplad rlhavtgdag
       61 detvtgraad raeasaplag wvnnaavfrd adlhrapage vvdlialnlr pavagaatav
      121 rrflaagtgg aivnvsshqa rravpgalpy atakaalegl tralavdygp rgiranaval
      181 gsihterhaa ylagldpeea ahvdaemarl hpagrigrtd evaevvafll sdrasfvnga
      241 tvpvdggrav lgldpear
//
LOCUS       WP_457604751             150 aa            linear   BCT 27-JAN-2026
DEFINITION  phage holin family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604751
VERSION     WP_457604751.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Saier,M.H. Jr. and Reddy,B.L.
  TITLE     Holins in bacteria, eukaryotes, and archaea: multifunctional
            xenologues with potential biotechnological and biomedical
            applications
  JOURNAL   J Bacteriol 197 (1), 7-17 (2015)
   PUBMED   25157079
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Young,R.
  TITLE     Bacteriophage holins: deadly diversity
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 21-36 (2002)
   PUBMED   11763969
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Wang,I.N., Smith,D.L. and Young,R.
  TITLE     Holins: the protein clocks of bacteriophage infections
  JOURNAL   Annu Rev Microbiol 54, 799-825 (2000)
   PUBMED   11018145
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Young,R. and Blasi,U.
  TITLE     Holins: form and function in bacteriophage lysis
  JOURNAL   FEMS Microbiol Rev 17 (1-2), 191-205 (1995)
   PUBMED   7669346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10538267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..150
                     /product="phage holin family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15860
     Region          32..142
                     /region_name="Phage_holin_3_6"
                     /note="Putative Actinobacterial Holin-X, holin superfamily
                     III; pfam07332"
                     /db_xref="CDD:462148"
ORIGIN      
        1 mtvptqdpgy qaagapphad evrgsslgdl mrqvttdlst lmrqevelak aeirqegrka
       61 gkaaglfgga gfggymvalf vsiaiwqfld nvmdsglaal ivaviwaava avlysmgkkn
      121 aerirglkqt ndsvqripda lkphpegvir
//
LOCUS       WP_457604769             121 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604769
VERSION     WP_457604769.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..121
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12750
     Region          15..100
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(23,25..27,33,56,58..60,62..64,67..68,90,94..95,97)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            59
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mpaslpsppe savphvrvdi tdeldlaglp evahvldril alrpreltid lagcrhvdaa
       61 avallldvhr rlarqggllt lsnphprirr ilansglgav pvvdtprpaa rgrarvasas
      121 r
//
LOCUS       WP_457604770             483 aa            linear   BCT 27-JAN-2026
DEFINITION  cellulase family glycosylhydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604770
VERSION     WP_457604770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..483
                     /product="cellulase family glycosylhydrolase"
                     /EC_number="3.2.1.4"
                     /GO_function="GO:0008810 - cellulase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030247 - polysaccharide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51317
     Region          40..139
                     /region_name="CBM_2"
                     /note="Cellulose binding domain; pfam00553"
                     /db_xref="CDD:425748"
     Region          189..440
                     /region_name="Cellulase"
                     /note="Cellulase (glycosyl hydrolase family 5); pfam00150"
                     /db_xref="CDD:395098"
ORIGIN      
        1 mfsiprpsrr hllvggavga lalaatavlp spdamaatgc avtyttnswq ggftatvavr
       61 nlgdpvsnwm lgftfpdggq rvvqgwsatw qqsgsavtar sldyngalgt gasttigfng
      121 swtgsnpspt sftlngtvct ggtstpppst pppstppppt tpppttpppt gttpvaingq
      181 lqvcgvnlcn qygrpiqlrg msthglqwfa ncytdasldv lanewrsdll rismyvqeqg
      241 yetnpagftn qvntlvdkae argmyalidf htltpgdpmy nldraktffa nvsarnaakk
      301 nviyeitnep ngvswstirn yaeqvipvir andpdavviv gtrgwsslgv seggnsdeiv
      361 nnpvraqnim ytfhfyaash rdnyrnevqr aasrlplfvt efgtvtytgd gavdtassna
      421 wldlldrlki syanwtlsda pegsaalrpg tcasgsfggt svltesgafm rerirtadnf
      481 pts
//
LOCUS       WP_457604762             463 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604762
VERSION     WP_457604762.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..463
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48602
     Region          22..461
                     /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 mndgsaidrv vrhlgalaad aapgtrlpsv reltthhhvs pvtvaeatrr lvadglvetr
       61 pgrgayvatr raappradls wqtvalgsrr ggedemqall alppsgaipl tggyldpdlq
      121 paaalgaala raarqpaawq rgpvegradl rawfareagg glraedmvic pggqaalsst
      181 lraltipgdt ilvesptylg alaaaraagl rvvpvpadad gvrpdqlaaa fartgarlfy
      241 cqplyanphg atlaaarrge vaeavreaga flveddyard ltvdgdappp laaddpdghi
      301 vylrsltkst apglriaaig argpagarlr aarllddlfv agplqqaale fltapawdrh
      361 rrslrvqlra rreallaald rhlpsltprd vprgglhlwv rlpdntddva vttaaaaagv
      421 tvfpgrpwya aeppaphlrl tyaaappeqm deairrlsta lph
//
LOCUS       WP_457604774             541 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604774
VERSION     WP_457604774.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 541)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..541
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59737
     Region          6..479
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(62,65,102,105,150,173,177,209,260,321..322)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(209,260,322)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          460..536
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 madnspwwrs aviyqvyprs fadgdgdgig dvagirsrld hlaalgvdai wfspwypspm
       61 adagydvsdy rdidpvfgtl aevealiaea halgirsivd vvpnhcsdvh pwfraalagg
      121 pgaperdlfw fragrgpggd lpptdwtgef ggptwtrttd pdgtpgdwyl hlfapqqpdf
      181 nwdhprvrae fedilrfwfd rgvdgirids agllvkdgtl pevhpdqphp frdqdgvhdv
      241 yrawrriads ypggralvge vwlpdrqrfa nylrpdelht afnfdflgca wdatslresi
      301 dgtlaahapv gapatwvlsn hdvtrhvtry gradtrfsfa akregiptdl elgtrraraa
      361 allslalpga ayvyqgeelg lwevedipyk lrqdpmwers grvdpgrdgc rvplpwqgdt
      421 ppfgfspdga taapwlpqpa dwkdrtvraq tgdphsmlel yraaltlrra epalgdgtlt
      481 wlpapdgvla farepgftcl vnlgdaavpl pthdrlllas gpldddrlpp dtavwlrtrs
      541 a
//
LOCUS       WP_457604780             295 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604780
VERSION     WP_457604780.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..295
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33248
     Region          73..197
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mfenlkiagr airtvftadp itrvrrfyei qspdvefaar rthymnvgyw sdgvtdidta
       61 adaladklaa aaglkpddtv ldvgfgygdq dfkwlrerqv akvyglnitp hhveaaqrra
      121 qeegladrtd frlgsatelp fedntfdrvv alesafhfyp rsaffaealr vlrpggvlat
      181 adiipvsgdv vraaiqsgpl sfvkfsipke nwhdrdtyrq elveagfanp evrsikdrtw
      241 egwraymaer tndpafravv kpavrksmaa hwknqdlmkr elaqldyvia vghkr
//
LOCUS       WP_457604782             520 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid
            hydroxylase MhpA [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604782
VERSION     WP_457604782.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Diaz,E., Ferrandez,A. and Garcia,J.L.
  TITLE     Characterization of the hca cluster encoding the dioxygenolytic
            pathway for initial catabolism of 3-phenylpropionic acid in
            Escherichia coli K-12
  JOURNAL   J Bacteriol 180 (11), 2915-2923 (1998)
   PUBMED   9603882
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Ferrandez,A., Garcia,J.L. and Diaz,E.
  TITLE     Genetic characterization and expression in heterologous hosts of
            the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia
            coli K-12
  JOURNAL   J Bacteriol 179 (8), 2573-2581 (1997)
   PUBMED   9098055
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482118
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     gene            1..520
                     /gene="mhpA"
     Protein         1..520
                     /product="bifunctional
                     3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid
                     hydroxylase MhpA"
                     /EC_number="1.14.13.127"
                     /GO_function="GO:0008688 - 3-(3-hydroxyphenyl)propionate
                     hydroxylase activity [Evidence IEA]"
                     /GO_process="GO:0019622 - 3-(3-hydroxy)phenylpropionate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=56029
     Region          1..520
                     /region_name="mhpA"
                     /note="bifunctional
                     3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid
                     hydroxylase; PRK06183"
                     /db_xref="CDD:235727"
ORIGIN      
        1 mlrtdvlivg ygpvgemlti llaqrgltvt averwatpyn fpravsydge asrvlaaagv
       61 adrlgpvves sgeytfkngf grtllhvkvt gdgpmgwpds vsfyqpglea llaergaelp
      121 gvtvlrpyqv tglvehddgv evtiagpdge evraarwvig cdgansfvre hlgsgvtdlg
      181 ftydwlvcdv vphearefkp nnlqvcdpar prtavsagpg hrrwefmrvp gesreefesa
      241 esvwrllglf ditpdnatle rygvyttqac saerwrsgri llagdaahvm ppfmgqgmss
      301 gfrdalnlaw kldlvhrgla dealldtyqe ercahvqhai rmsidsgtvi cetdraaaag
      361 rdaamlaelr rrtarprtrs lleplsggvr hsgceaagap mpqgrvevdg raglfdevvg
      421 tgfvllcaed pddlldadar afldalgarv vrivpagapa pgagaaptaf dlddvylahl
      481 krydavavlv rpdfyvfgta adpaavpalv edlrrqirrg
//
LOCUS       WP_457604786             889 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604786
VERSION     WP_457604786.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>889
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <37..876
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mwparaasvh rvlpawpsrv tpaghvvvag lvavlarwtg qdevvlglap aggvvarvdv
       61 sgdpgfgela arvglawtap vavpdrpdpv aveladgpva etgpaavdvd mvvrvaadgs
      121 vlrvdyaveg fsaqfvqglv dqvvvlvsag taapqvalsr lplldaaere rlltwgrgpv
      181 reipgepihe lvlgwaqrsp eavagvagde vltygeldrr sgllaaylrs vgvragdvvs
      241 valerglwsl vaamgvlrag aaytpmdvsw paermrvlla dhgarvvltv gavapripag
      301 dgvtvvaldd gwpavparaa adlpvvpvda pafviytsgs tgtpkgvvls herltnflaw
      361 mtdecaigpg srmlhsaapv fdaafgemfa altgggcvvv cprddlldar rltdlvnshg
      421 vthtfgpatn iapldpaacp glrciifgge avpprlaqrw ltagtrvvna ygpaeiavac
      481 twfdasagwg gayvpigwpm pnrqvrvvda nldlmpvgvp geiliagfgv adgylnrpel
      541 taqrfvtdpy ggglayrsgd lgrwnsagal eilgrmdhqv kvngirielg eiesilaqhp
      601 evetavvvrr edrgvarlva yvtgrdgrtp atgdlrdhaa ahlpsymvpa avvtldrfpl
      661 ggtgkidrna lpapgaqrpd lgvpyvepat egerlvaevf asvlgiervg ardgffhlgg
      721 tslqsaavat gideaadvvv pvsqihrtpt ahelarwlat aprrtdtgst agqtrqrpgp
      781 vplaqqvakc lmsplevvvp vtwwiegeld lralmaalgd lhhrhqalha ryrrtdppta
      841 iippnpgmpq lrlladaate hdaldqlaea vqqpldytqg rnwraalir
//
LOCUS       WP_457604788             215 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604788
VERSION     WP_457604788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..215
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22239
     Region          18..201
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mdestgalts msgftpepip tarlvllplg vehaeemaav ladpalhtfi ggepatpaal
       61 raryerlvag spdpaeswcn wviqlrdggr ltgfvqatvt eahgpvtdaa tagaravghr
      121 hldeaapaaa gpvaevawvv gtrwqgrgia teaargmvgw lgrrgvrtlm ahihpdhras
      181 aavatacgla ptdvwhdgev rwtgpaalsp ppars
//
LOCUS       WP_457604790             299 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604790
VERSION     WP_457604790.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..299
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31556
     Region          216..297
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtaaptlhfc tdpgeflaaa eayleadpvv gtvvatvaqr maarraegva lpeddwwlvv
       61 rdasgavvga amrtapfppr ppfllpmpea aavalagawh rrgervravn galpaaraca
      121 devarldggr vavaqhtrlh vldqlappap vpgalraatt ddvdlvaawf gaftadadeq
      181 agrppgtsah etpdraellr rirdgrvwfr tdgsgrpvhl taahptsfgv arvgpvytpp
      241 eqrgrgwagn avaevcrllt aegarvclft dqanpvsnrl yarlgfrpvv dmanlalvd
//
LOCUS       WP_457604793             135 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604793
VERSION     WP_457604793.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..135
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15266
     Region          3..123
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 maarqlklgl rvrdldrshr lylrlgfkei pqtdqtnlry ltfghtwlil sdlhrhghhn
       61 aererevkag ppglgvvltv ptadldatya lrrdeglpvt lepedvgwar ifygldpdgy
      121 evmceqfhpp sraas
//
LOCUS       WP_457604795             213 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604795
VERSION     WP_457604795.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..213
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22221
     Region          8..203
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mstseargrv rafvtvsldg yvtgpddhag qglgvggerl hhwvmggpwt ydtprepgtg
       61 mtgedrayfd ellagvgaal cgrgmydsag awggsnpfea plvvlthrta dqpdpdagfl
      121 mvdgfdaala aarrtagdga vvigggadvi rqalaagvvd elglstapvi lgrgkrlfeg
      181 fdrdvdleir avhhsrhavh vryavgrras dnd
//
LOCUS       WP_457604797             426 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604797
VERSION     WP_457604797.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..426
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42819
     Region          74..339
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrtwgpfval aaalllpvpa tpavaavrap vrrlpaappc pnvpapsarp pqpppapdpa
       61 aravggaald taglvvppas sappavtats wvvadldsga vlggcgphey gvpasvqkll
      121 laatmlprld phrevtvtag dlavepgssa vglveggryq ietiwlglll rsgneaanal
      181 arlgggpdgl aggvramnee ahrlgarqth avtpsgldgp gqftsaydla liaracfadp
      241 afrryattri aqipaqpaqr akgfaisndn mlldhypgal ggktgftdla rhtyvgaaer
      301 ggrrlvvtll gaevttqrgw qqgaalldwg faqprdaavg rlvepgeldr pappaggaas
      361 alagqaglrg ggaapgprpg tgvtvavgav ltaggallla rrrrnaaava lsagsalrep
      421 eipeqd
//
LOCUS       WP_457604799             428 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604799
VERSION     WP_457604799.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..428
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43836
     Region          75..344
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mraralavat avtllatgtp apaaaapatt paapvaapgv apvpcprlpa pkvsrpprpa
       61 ppattpeqaa vggealagag lvvppgspap pavtattwlm adldtgevlg acgahvpgtp
      121 astqklllaa tmlsrldpkh vavatradld iepgssavgl lvggrysvet lwlglllqsg
      181 ndaanmlarl gagsaqagva emneqarrlg agqthavtps gldgpgqfts aydlaliara
      241 cfadaafrry altertqipa qpalkkggfq iqnenqliyr ypgalggktg ftelarhsyv
      301 gaaqrdgrrl vvtllgaear pvrgwqqgaq lldwafrlpr dasvgrlvep gerdaeaaep
      361 rqaaaaearr tasppwrgpa gtalhrigdg dwrvivpvag llaltvggva avlaarrgrs
      421 rrrgrrra
//
LOCUS       WP_457604800             410 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604800
VERSION     WP_457604800.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  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 410)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..410
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44513
     Region          2..390
                     /region_name="GT4_WbuB-like"
                     /note="Escherichia coli WbuB and similar proteins;
                     cd03794"
                     /db_xref="CDD:340825"
ORIGIN      
        1 mrvgiltyhy ppepafvpgs laeelvargh evrvltgfpd ypgghvypgw rqrwrhqths
       61 erltvrrvpr yaagdgsara raatwlsfag saalagrgll rdvdvlyvcg hpavtfaatg
      121 llrllgrtpt vlhvqdvwte rsaqdsgwpa rleaatrrly resavvavgs pfmadlvrag
      181 gadpgrvraa pnwtderifr ptqagpavrr lvrrddrcvv mhagtigarq dletavraaa
      241 algdrmdlvl vgsgpqerrv rglaadlgad nvrflerrsa vdmpqlyaaa dyqlvaqrdl
      301 pelrgrvpgk lqaalscaap vvasaageta evveraragl scppedwaal adrfwlaaai
      361 ppaarldmgr rgrdaylrdm smragvdrie allheaaerp snrtkfahss
//
LOCUS       WP_457604802             657 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604802
VERSION     WP_457604802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 657)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 657)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 657)
  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 657)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..657
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70608
     Region          <261..639
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mlktdqrtpv ppvpahdsvl pelremwwet gvraraqagl favftelprl vwsavsvswr
       61 adrvrssvva attvgagvms afgllaaqrv lvevfaggpt adkviaalpa lvalaavtal
      121 ragmatamgy aqngltpkvd reverglfel ttavrleafd adafaddmer asrgadsttg
      181 lvqssmnlla giagiagvla vavavvvihp llllallvat vpngwaslra ghlryqtyaa
      241 gsvrrrrlwl lhrlmaerds apelrsyglr gflldqydrv mgvetdiqla larrvttttt
      301 vgamiggvat avvyvllgvl lvngqiplaa aatcviavqt aqrslavvtf qvdrvytegq
      361 hfrdytgfmt raadylspta tptartaahe rlhkitveav slrypdrdts avdgvtltik
      421 agqtvafvge ngsgkstlat miatlrtptg gtiryngrpl qdwnidalra riavvtqdyh
      481 kwpftaatni aigdittkpd qdrieaaaar avahnmiqel phgyetlldr tfangqdlsg
      541 gqwqritaar gflrdadlli mdepssaldp raedalfqai rdrqgratti lithrlanvr
      601 hadriyvlhh gtlvetgthd dlmtadgrya elftlqaagy dttpstpapl prqtata
//
LOCUS       WP_457604807             458 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604807
VERSION     WP_457604807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..458
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45938
     Region          51..406
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtapatmlpa taatratacp vsapgwrlga lygpavygvs aaavalpdaa rhlhtgglal
       61 twvltayaag vgvgavtagr lidqwgsrpv lfiaatllag gallcvlapt laalvtgrvl
      121 lavgsgavka ialsgtarlp tahrpaglaa fgaclagfga taplagamaa hwfwpaalal
      181 pvlsvavipl cwhlttrrpr papvdwtgag llaavaagll ltaqtaahyt svlttlliaa
      241 ataaaavwla grtrkhpggf ltgqvlsagw frhaaaagac vyaalfavly ggphllsqyg
      301 yssmqigvll lpgavigall artaaqaarr mparhvlaav cllfaavlcy tathpqpwai
      361 avvstaafta savaqtllta ettrhappdm rgavtglltl aiflgggcgt vlcvalwqsw
      421 gttialaata ilpaagavaa wrlgiperrs cswwatts
//
LOCUS       WP_457604808             115 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604808
VERSION     WP_457604808.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..115
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12548
     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"
ORIGIN      
        1 maesrralgr vladarrsag vtqdrlavlv rwsrstvanv evgrqcapre fwvacdaalg
       61 legallaawg rtdvlarrlr eqeaeaqirq llvqpspgcv crelhrllae sgwss
//
LOCUS       WP_457604820             362 aa            linear   BCT 27-JAN-2026
DEFINITION  segregation and condensation protein A [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604820
VERSION     WP_457604820.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Kamada,K., Miyata,M. and Hirano,T.
  TITLE     Molecular basis of SMC ATPase activation: role of internal
            structural changes of the regulatory subcomplex ScpAB
  JOURNAL   Structure 21 (4), 581-594 (2013)
   PUBMED   23541893
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Volkov,A., Mascarenhas,J., Andrei-Selmer,C., Ulrich,H.D. and
            Graumann,P.L.
  TITLE     A prokaryotic condensin/cohesin-like complex can actively compact
            chromosomes from a single position on the nucleoid and binds to DNA
            as a ring-like structure
  JOURNAL   Mol Cell Biol 23 (16), 5638-5650 (2003)
   PUBMED   12897137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..362
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=38142
     Region          40..283
                     /region_name="ScpA"
                     /note="Chromatin segregation and condensation protein
                     Rec8/ScpA/Scc1, kleisin family [Replication, recombination
                     and repair]; COG1354"
                     /db_xref="CDD:440965"
ORIGIN      
        1 mtappldpph gpgdpavaae laaevdgvvp aepgtgeqts gftvrldnft gpfdlllqli
       61 skhkldvtev alhkvtdefi aylramgdqw dldetsefll vaatlldlka arllpsaeve
      121 deedlallea rdllfarllq ykaykeaaah iaeleavggr rypraatlep ryaealpdlv
      181 lgigperlrt lavkamspkp vpevsiahvh mvrvsvreha giiadrlrra giatfsllca
      241 dcemtlevva rflallelyr qglvafvqeq aleeltvrwt gpadgdaelt vdeyagspep
      301 tttsvpaapp ddsaapaeda aavagdaaes agatvpgdva aaaasdaavp ieaadepapt
      361 qe
//
LOCUS       WP_457604822             542 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604822
VERSION     WP_457604822.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18102377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..542
                     /product="GNAT family N-acetyltransferase"
                     /calculated_mol_wt=59513
     Region          97..238
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          178..245
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mgkrssrsrr repirrpipt arlsasagrv tdltgqhlvd gwpvseqvrv rlargadmaa
       61 vrrltalagv aledevvedv dagaggaalr lgldgghdaf vrhmaekfag pqgmdprrvl
      121 ppvtlvlvae hdqhgvvgav vayppngviq qlvehqrrag vsgqqlfqlv msgvmfmvri
      181 kaiavdetmr ghgigsallh rcqqiyahcg ymisygqmad spalerfyrd hgfdvlards
      241 gfdpwvvlgv haevrpdpge rtfvrhqktg anrrpgrvpt prrgnrqfdp gtlalhddhl
      301 pallmhgsge flaiqflpml wikmaegqra nacidacaql rhayqqfgir aeilpvgvvi
      361 hhpdgsrtqy atdeprwhge stlvghtill lpeherlvdp tieqvpeira lrqgpvigrl
      421 aeqnrhalhd grtsfavqra dllieyqpvq pehrdrllrg plltrnddqy rraavnlaam
      481 alhafrdaga adrirqstaf prltalldai gdapidvdes tgdvlihlpg gpvrldqvpv
      541 pa
//
LOCUS       WP_457604826             207 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604826
VERSION     WP_457604826.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..207
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22244
     Region          20..150
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(25,27,81..82,85)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            27
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(80,131..132,134..135,139)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(86,91..92,127,130..131,134..135,138,141)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(110..112,127..128,131..132,135,139,142,146)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(110,132,135,139,142,146)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(140,146..147)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          162..203
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(163..165,197..198,200..202)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mttaptvapt gttrphnrir vgyarvstrg qdhqaqldal agahcrevvt etastrgdrp
       61 klratlerlq pgdtlvvykp drvarsmkel lvfvedelhg rgivleilsg vcagvhrpdg
      121 atiadrllfa vaalaaeler elirertldg lraaaaqgrr ggrpvaitad qldvararla
      181 rgesvtaiaa hlrvgrstly ralkpdd
//
LOCUS       WP_457604844             239 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604844
VERSION     WP_457604844.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..239
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24269
     Region          55..206
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(85,130)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(90,93..94,98,102,126,128..131)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(120,149)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mgargkvtei gggmkatrll lpalgalsva ghlwaawtvr ahrarlaeah rlavtdpltg
       61 lvnraglaaa ladlagepyd vaivdldgfk qvndmfghaa gdavlvevaa rlsaaidevd
      121 gavvarlggd eivlvcpspa piahllgtev vralaapvvl pggqelavra svgavsamvg
      181 deparvlraa dlalyqakan ggdqvaeygr vldlpvvetr pvvrlremte aaralggaa
//
LOCUS       WP_457604847             244 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604847
VERSION     WP_457604847.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..244
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26506
     Region          2..243
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 merplppylq itqhyrdliq sgelrdgdrl psarqlveqw gvahataakv latlraeglv
       61 kttsggaggt vvsvqdvgqs prdrvlavrr wgriyppgeh arivsaelvd apehvaaalg
      121 vepgsavirr rrvtfreeap vsastswyag elaevapgll iierlkqgtp gyieqqtgrv
      181 arlgrdqfta aladaavsad lgvpegspvl vgrnwfrdad gevleygeyv stperwqtye
      241 yele
//
LOCUS       WP_457604852             307 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604852
VERSION     WP_457604852.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..307
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32721
     Region          14..300
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mfdsqfarta amdrivamvn dkggvgkttl vsnllgqlaa agykvlgvdl nrqanmsddl
       61 gyrdrpgidd qgeqlyeair rpgknplvah evrpnlwvvp ggrelaaltp litmnmqqeg
      121 raaylglaaa lapmaadydl ilidsppeni vlvdlalaaa rwtimptrsd tggligmklt
      181 aerfrtarei nptlgllgvv lfatlsgara ihaevkedva aafggqspml astiryserv
      241 ardarragkl aheleieaaa qpafwealrq grkpgrhsta tasvsadfra laaevldiia
      301 aqeatqa
//
LOCUS       WP_457604863             203 aa            linear   BCT 27-JAN-2026
DEFINITION  suppressor of fused domain protein, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604863
VERSION     WP_457604863.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Das,D., Finn,R.D., Abdubek,P., Astakhova,T., Axelrod,H.L.,
            Bakolitsa,C., Cai,X., Carlton,D., Chen,C., Chiu,H.J., Chiu,M.,
            Clayton,T., Deller,M.C., Duan,L., Ellrott,K., Farr,C.L.,
            Feuerhelm,J., Grant,J.C., Grzechnik,A., Han,G.W., Jaroszewski,L.,
            Jin,K.K., Klock,H.E., Knuth,M.W., Kozbial,P., Krishna,S.S.,
            Kumar,A., Lam,W.W., Marciano,D., Miller,M.D., Morse,A.T.,
            Nigoghossian,E., Nopakun,A., Okach,L., Puckett,C., Reyes,R.,
            Tien,H.J., Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T.,
            Xu,Q., Yeh,A., Zhou,J., Hodgson,K.O., Wooley,J., Elsliger,M.A.,
            Deacon,A.M., Godzik,A., Lesley,S.A. and Wilson,I.A.
  TITLE     The crystal structure of a bacterial Sufu-like protein defines a
            novel group of bacterial proteins that are similar to the
            N-terminal domain of human Sufu
  JOURNAL   Protein Sci 19 (11), 2131-2140 (2010)
   PUBMED   20836087
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Merchant,M., Vajdos,F.F., Ultsch,M., Maun,H.R., Wendt,U.,
            Cannon,J., Desmarais,W., Lazarus,R.A., de Vos,A.M. and de
            Sauvage,F.J.
  TITLE     Suppressor of fused regulates Gli activity through a dual binding
            mechanism
  JOURNAL   Mol Cell Biol 24 (19), 8627-8641 (2004)
   PUBMED   15367681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>203
                     /product="suppressor of fused domain protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
     Region          58..202
                     /region_name="SUFU"
                     /note="Suppressor of fused protein (SUFU); pfam05076"
                     /db_xref="CDD:461543"
ORIGIN      
        1 mdesrgsgvl rhqslhdgfv paqgpqqafa daidrhieeh fgpvefvyhe iashlvgvhv
       61 yvvaptekrp yrtlitsgms elpmtvpegh dispyaelml slpadwplae vaglgdetgw
      121 plrilkqvar lpheygtwig ewhsvpngdp aqpyatdtpf agvvvtpmlr vppeartidv
      181 ggglrialla liplhpkeia vkv
//
LOCUS       WP_457604865             192 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604865
VERSION     WP_457604865.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..192
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=20635
     Region          16..>185
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 msprsstrrr cvidhrpapr igslctgygg ldmavelvlg gqltwyaetd rhaatvcahh
       61 wpgvpnlgdi rtidwtdvpp vdiltagfpc qdisnagkra gitgvhsnlw tsvahavral
      121 rppvvfvenv aalrtrgldv vhadlaalgy dtswlclras digaphrrdr lfllattgeg
      181 rrdtnaadtl cp
//
LOCUS       WP_457604869            2489 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase, partial [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604869
VERSION     WP_457604869.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 2489)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 2489)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 2489)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 2489)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..2489
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>2489
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
     Region          2..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          32..1419
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1237..1690
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1445..1446,1448,1469..1472,1497..1500,1524..1526,
                     1547..1548,1570..1571,1585,1612..1613)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1548,1572,1585,1589)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1706..1791
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1809..>2489
                     /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 madeaklldy lkrvtadlhq vrqrlrevea geqepvaivs mscrfpggvr spedlwevva
       61 sgrdvvsdfp tdrgwdlgsl ydsdpeqagt sytrqggfvh dladfdpgff aisprealam
      121 dpqqrwllet swealeragi dphslrgsrt gvfagstgqd ygtvlmgaaq gleghlmtgn
      181 agsvvsgria ytfglegpav tidtacsssl valhlagqal rqqectlaiv agvtamctpa
      241 afvefsrqrg laadgrckaf aaaadgtgws egvgvlvler lsdaqrnghp ilavvrgsav
      301 nqdgasngls apngpsqqrv iqqalanagl aaggvdvvea hgtgtrlgdp ieaqallaty
      361 gqergdsapl llgsvksnig haqaaagvag vikmvmamrh gvvpptlhvd eptpevdwsa
      421 gdvslvteat pwpavdrprr savssfgvsg tnahtileqa papqpapsaa apvverpvvp
      481 vpvsardaag laaqaarwaa riaadetlrp ldvafssvts rstldhravv hatgredlla
      541 glralaagqp sgavvagqag grgslavlfs gqgaqragmg relyagfpvf aatldevcvy
      601 ldallprplr evlfalegsa eaalldrtvf tqaglfavev alfrlvesfg iapefvgghs
      661 igevtaayva gvlsladaca lvaargrlmq alpagggmla vaadevavve siagstdrvg
      721 iaavngptsv vvsgavdald evervwrdrg vrtrrltvsh afhsplmepm laefravldg
      781 ltfsapslpv vsnvtgalad ademrtadyw vrhvreavrf adgvtalraa gadtfleigp
      841 rsvltamvad ilpaddavla vaaqrkdrpe vhgllaglae lhvhgvavdw rqwfadtgar
      901 rvdlptyafq hqrywpeaga gwtgdvtavg lrpaqhpllg aavgvahaeg flftgrlarr
      961 thpwicdhvv fdtvllpgtg fvelalqaga hvgadhvrel tlesplilpe tggvdiqlwi
     1021 gpadetgcrs vslhsaqdge ptegtgeraw trnasgvlas gpavpsgpag wsdlttwppl
     1081 gaievgtddl ylnlaaqgyd ygpsfialrs awrrgddlfa elalpeapaa eaagyglhpa
     1141 lldaalhtlg lttpagepsg agmppgfgrl pfswndvalh gagaaaarvr vshtgpdsis
     1201 llltdvtgap visvgslvlr pvsadqlrta sgggteslfr vewaplalpa gpatvdwavi
     1261 gdaaaltdav aatgtavaay pdlaalatam dggtdapgvl vlplldppas agvpravaea
     1321 thrvlavlqq flaeeryavs rlvvltsgav atdrdtdltd lagaavigll rsaqsenpdr
     1381 fvlvdvddva gcaaalvpav atdepqvvir agvaagarlt rvaapteppa apfdsdgtvl
     1441 itgatgtlgr lmsrhlvsty gvrhliltsr rgraaegvae lcaelealgv svtvaacdva
     1501 drgavaella gipaehplta vihaagvrdd gvissltper mdgvlrpkvd aawhlhelta
     1561 dldlkafvsy sslaataggp gqgnyaaana fldglaqhrk arglaaltla wglwadrsgm
     1621 ttelddvhln risrsgvaam eaeeglalfd aacrttdaal vparldlatm kvqfaggtip
     1681 plyralirtp araaaastga slvqqlaglg daeraaalve ivrgqaaavl gypdpaaiep
     1741 rrafsefgfd sltavemrnr lnnafgmrlp atlvfdyptp hdlaaflgte iagtpvpvrp
     1801 tttavsvgdd eplaiigmac rlpggvwspd dlwrlvvdgv daisdlptdr gwdldslysp
     1861 dpdapgtfya rgggflsgvd rfdpnffgis prealamdpq qrlllettwe sfesagidpt
     1921 dvrgsstgvf vgtsgqdygs llayspeaae gymltgmtss visgrvaytf glegpavsld
     1981 tacssslval hwagqalrrg ecdmalaggv mvmatptafv efsrqrglaa dgrcksfaas
     2041 adgtgwsegv gmllvqrlsd arrqgrtvya vvrgsainsd gasngltapn gpsqqrvirq
     2101 alasarltta dvdvveahgt gttlgdpiea qallatygre rpadrplllg siksnighaq
     2161 aaagvagvik mvqairhglv patlhvdeps phidwtsgav elatqsrpwp avdrprraav
     2221 ssfgisgtna hviieqadel svapaepgpg lvasdavlwp lsgrskgala gqaarlaeyv
     2281 rergdidaaa vgwslattrs afghraavvg sgteellagl davasgtpag nvvadtttsh
     2341 gagpvfvfpg qgaqsarmaa glvgrvpvfd arlaecqral apyldvdlvs vltgddeswl
     2401 arvevvqpvl wavgvalaav wqhagvtpaa vvghsqgeig aacvagilsi edaakavalr
     2461 sraltvlrgt gtmasidlsa eavgerlpa
//
LOCUS       WP_457604873             427 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604873
VERSION     WP_457604873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..427
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42015
     Region          22..337
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 msegrpgqqp adgrrtglga agvavtlagv lvnglaylvp vlaarkldad dlgalatalg
       61 lvaiagvpgl glqlavavhh arhgpsdtrr ltvltaalca gallvatpvl vaaldlpavv
      121 pallavttas vvlssrslge lqggqrflrl aaamallaaa ryggvivgll lgagltgala
      181 igaltaalap palawltgtp rrpsaaprlt vaqvtagcga tlamlvvsya dlllarqllp
      241 psgsgaysvg tvltkgalwa pqvaavlalp rlargdrrsr tvalavtgac glvlvgasav
      301 agglafrlvg gpdytalgry aplfaavgal yavtfvllnd rlaggvrwpa aplwlgtgal
      361 vtvaaivrpr tvgglvvaal atavvttllm avpatrrpas hpatgdrssp pgpatdrtrs
      421 apaappg
//
LOCUS       WP_457604888             331 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604888
VERSION     WP_457604888.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..331
                     /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=36098
     Region          14..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsil lllqahgrlt aadlaarlqv sartiyrdve alhaagiply geaghdggyr
       61 lvagwrtrlt gltaeeadrl lfaglpgpaa elgyqsvvaa vqlklraalp apladraarl
      121 eqrfhldtpg wysdgdpsph laeaaeavwr qhrlrvryrg wrgettrlle pyglvlkggr
      181 wylvaarpdr adpatyrvnq ildltpldep ferpefdlpa wwrahvvefr aglhrdeari
      241 rlsprgfarl revgsdvvva aaeasagppd atgwvhavip ieslthahgd llrlgaevev
      301 lapealrtrl setaaalaal yhppsapplp g
//
LOCUS       WP_457604889             209 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604889
VERSION     WP_457604889.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..209
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21807
     Region          23..188
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(64,66,68..69,128..129,147,188)
                     /site_type="active"
                     /db_xref="CDD:293792"
     Site            order(64,66,68,128,147,188)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mtarvghavt sgtfsldgqt fdvdnnvwvi gddsecvvld aphdvaaire vigdrrvlai
       61 iathahddhv rvapelarat gapvllhpad rvlwdmvhpd tapdgeltdg qtiaaggttl
      121 rvlhtpghsp gacslyapdl gavftgdtlf aggpgatgrs ysdfgtives irtrlltlpp
      181 etvvhtghgd dttigaeaph ldewiargh
//
LOCUS       WP_457604890             611 aa            linear   BCT 27-JAN-2026
DEFINITION  VirB4 family type IV secretion system protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604890
VERSION     WP_457604890.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..611
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=65645
     Region          39..610
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mifvrrrral hddnpsaspp saglaaavap asvevtprfl rvgdgyaatl vvtgypaevg
       61 pawlepllsw pgrldlalhi dpipapmaas rlrnqrarfe ssrradaekg kladpyveaa
      121 addaadlaer largaaklfr vglyltvhar teaelldaca qvkaaaastl ievqpatwrh
      181 lpgwtttlpl atdslqmrrt mdtqalaaaf plasadlpap lpgdpattgg vlygvnpdsq
      241 givwwdrwaq enhnsvilar sgagksyfvk ldilrqlyqg vqvavvdped eylrladavg
      301 gtivrlgapg vkinpldlpa gdgrpdvltr rglflhtlis vllgqvpppa eraaldrail
      361 qvyrragita dpathhrpap llkdlaatlr dddnpaahel aarlapwvag sfsdlfdspt
      421 ttrpdghlvv wslrhlpdel rtvgtllald eiwrqvdlpp qhrrrspegs hpqgrrlvvv
      481 deawllmrdg egarflfkms kagrkrnagl svitqdvadv lgtdlghavv anaatqvllk
      541 qapqaidrva dafgltager rmllsarvgh gllisgtnrt afesissqae hllatttpsd
      601 ladlddgeed l
//
LOCUS       WP_457604896             329 aa            linear   BCT 27-JAN-2026
DEFINITION  TRM11 family SAM-dependent methyltransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604896
VERSION     WP_457604896.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  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
REFERENCE   2  (residues 1 to 329)
  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   3  (residues 1 to 329)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..329
                     /product="TRM11 family SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33805
     Region          63..262
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 makhraetag dpneqstpta atidpigghr aapgpeglsv wataqatgpv qrrgryvres
       61 vqhparmlpa iaahavtayt qpgdlvldpm cgigttlvea ihagrdaigv eyesrwsdia
      121 danikhahtq gatgragvir gdatsilslv paaltgqial vvtsppygpt vhglvrpgad
      181 gvakfdnayn dgtdrgnlay rdltgladgf aqiltgchtl lkpggvvvvt arpwrkhgel
      241 idlpsaviga giragltpvd rcvallaavr dgglvarpsf fqlqavrkar aagtpmhlia
      301 hedvlvftkn htgsgagtsk dtgeggava
//
LOCUS       WP_457604897             100 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604897
VERSION     WP_457604897.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..100
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11119
     Region          32..>69
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mrdnpprprr rppppptpah atghhdeqep rlytpaeaaa llripeswlr rragrrqipc
       61 tflgkhlrfs aadlaaliaa saepatgrrt hrrhrppapt
//
LOCUS       WP_457604898             378 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604898
VERSION     WP_457604898.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..378
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42620
     Region          60..355
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mawveqrgmk frvrlrmtdg tvttdsthdr radavirake idvevardtf idprggripl
       61 aewvpiwest hqaspatwaa yrshlrlhil ptlgplplvd irrqhiktla vvlgkrlapr
      121 svadvimvls mvlqeavedr ripfnpcrgi ripkgiraer phataeqvaa ivarqarpsd
      181 glmiltaayt gmrwgelagl hrdnldltlg siyvhpdtga lhevegklyl gppktndsvr
      241 hirlprfltn llathladhp hhtvfpgarg yhqrrsnfnr rawtpavtgd pqrdippilp
      301 gmhfhdlrht hktwliedgi peiaqarrlg hrlagvrgiy shvtepmitn lvdalqkrwe
      361 ttqpdlpdst lrhlrpva
//
LOCUS       WP_457604900             406 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457604900
VERSION     WP_457604900.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..406
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45412
     Region          68..400
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpgrarange gsifpyrngl aayvwvtkpd grrtrkyvyg ktrdavhdkw iklhqqakqg
       61 pvattvptvg tfltywltei iqpnraplty atyetfvrly itpglgakrl drlqsrdvqt
      121 winqvartcq ccaqgkdaar pnhkrrccai grccqaipst rtvsdiraal raalthaqae
      181 dlitknpavp vtlatvrrrr gkswssdear rflesaradd dplyaayalv lvtglrkgea
      241 lgltwedvdl dageltigrq lqrvrgqllh rdtktqasda tlplpdiclt alklrgeqrn
      301 eaeaaagkaw hetglvfttr ygtpieprnf qrswqtrcek agvkpitvhd arrtcatlla
      361 dldvhprvam qvlrharfsv tmeiytqvts tktrealkrl geslsr
//
LOCUS       WP_457604904             173 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457604904
VERSION     WP_457604904.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..173
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19137
     Region          1..171
                     /region_name="COG3981"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443180"
ORIGIN      
        1 mptlisptts lyaafqdcrd dwgpglhedg fgigpeddld spdgfadwvr rrvrldhgag
       61 vpcpderhas crwiledgqv lggiamrhwq dddlgqigyg vrpsarrrgl aswalgemlr
      121 eartvlglhr vlipclednl asartiesqg gvlqgildtg hvrvrrywit lsr
//
LOCUS       WP_457604910             865 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457604910
VERSION     WP_457604910.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>865
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <69..865
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 msvgivgaqa tdvagpgfei ldlmgdlrrp aawparaasa yrpvdlpvpa garspgavll
       61 agllgvlary tgqaevavgl ssggvlrvdv adepgfgelt srvaaaltgp vtrdtgaagp
      121 vviglvdapv aevgpdvvdv divvtvagdg salrvdyaad gfsadwvrgl vdqtvsllsa
      181 gvrepgvplg alpllgater erllawgrgp arpvpgeplh elvlewarrt pdavagvaag
      241 evltyaelar rsgalaaqlr smgvrpgdvv slaldrsmwt lvatlavlra gaaytpmdvs
      301 wpadrmrmll adhgarvvlt vgevaprvpr pdgvrvvsld vdwptlaaae aadlpvvaps
      361 rpafviytsg stgtpkgvvl thehltnfvt wmreecavgp dsrmlhscsp vfdvalgeiy
      421 taltsgarvv vssrddllda rrlteliake qathafcppt nlaavdpadc psltcvtlag
      481 epipprmaqr wtaagarlin aygpaeasva ctwfdaskgw pgayvpigrp mpnrqirvvd
      541 anldlvpmgv pgeilitgag vadgylnrpe ltaqrfvtdp ygggtayrtg dlgrwnaaga
      601 leilgrmdhq vkvngiriel geieatleqh pdvgtavvtr redqgtarlv gyvtgrdgrv
      661 pvtadlraha aavlppymvp avimvldrfp tggtgkidrr alpepgsrrp dldvpytepa
      721 tdserlvagi fatvlgldrv galdgffhlg gtslqsaava valdeaadva vpvsqihrtp
      781 tpqglarwla taprrpgaep apsvtgrpgp skpvpltpsv akcvvlpfel vcpttwwieg
      841 eldlralmaa lgdlhhrhqa lhary
//
LOCUS       WP_457604918             376 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457604918
VERSION     WP_457604918.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>376
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
     Region          74..>371
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mgpveswspt lrttveltlq trfavttfwg pelimvynea yvpligdkhp aalgapaaav
       61 fpeiwdtigp mltgvlaggp atwsqdlelf ldrrgfaeqc yftfsysavr gsdgrvegvi
      121 diaaetteqv vlqrrltllt rltdalsmsd dpqrillaav gvlraaprdl pqadvlwpgv
      181 saagarlpav ppsvfgrqdl vvedwsgrtv awlrlptasp wrqqpvlvae lsphlpvdea
      241 ytrflrlvga aigqafdraq arqverrfve lerqmsealq rsvltepaqp erlqvavryr
      301 aaveqtrigg dwydsfllpd gglaltigdv tghdqraaaa maqirnllrg vavtlrkpps
      361 avlgeldtam rtlavt
//
LOCUS       WP_457605010             480 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605010
VERSION     WP_457605010.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48784
     Region          24..418
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(29..30,33..34,37,69,119..120,122..124,127,147,
                     150..151,154,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtapapalrt gsaagrgtll aailasgmvf ldstvvnval prlgaeldat vaglqwtvng
       61 yllmlaafvl lggalgdrfg rrrvfllgvv wfavasvlcg laqdtgwlva arflqgagga
      121 lltpgslsvl qasfhpddrg raigtwsgls gvstalgpll ggwlidtlsw rwiffvnlpl
      181 avgvvlaalr wvpesrdeei srtgggrrfd vagallgala lggvtyalid apargldspa
      241 vlaaavlgvv avvvfvlver rrgdtamlpt glfssrlfsv lnvftvvvya alggftffla
      301 vylqnvvgws alltglatvp mtvlllvgsp ragalsarig prlpltvgpv iaavgllllr
      361 rvgpgasywv dvlpgvtlfg agltlvvapl ttsvlgavsd rfagvasgfn naasraggll
      421 avaalpllvg lsgtgyeqkg aladayrgal awcaglllag avlaavlihr pgrgegraps
//
LOCUS       WP_457605013             580 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605013
VERSION     WP_457605013.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 580)
  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 580)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..580
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60049
     Region          37..559
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msvtgmrrra avglaalaat aftavavtpd qaearpkpvd vqllaindfh gnleppsgss
       61 gtidgqpagg aeylashlks mraeakrqgk gtvtvaagdl igaspllsaa fhdeptieem
      121 nlaglefasv gnhefdegaa ellrmqrggc hpvdgcadgt pfggakfsyl sanafktstg
      181 lplmqpfgik ivkgvpigfi gmtlegtpni vsqqgvaglr ftdeadtank yakilrllgv
      241 ksivvllheg gvqngggind ctgfsgpivd ianrmdpsid vivsghthaa yncninnklv
      301 tsassfgrlv tqidlkidpr trdvvsasan nvvvtrdvek dpastelinr yktalgpvad
      361 rvvgettaai tktqenlyqt gvdangkpty qtgesplgnl iadaqlaatd teqnavaafm
      421 npggvradld agpvtyaeaf tvqpfannlv tldltgaqly cmleqqftva rvlyasstvn
      481 yvvdvngtta pagtpcagtr vvrgslting tpvtdtatyr vtvnnflagg gdgfsvltgg
      541 tnavtgqidl daftayltek spvsppaldr irtttevaag
//
LOCUS       WP_457605014             224 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605014
VERSION     WP_457605014.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23534
     Region          5..>173
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mprpvvfdlf htlvhgadde rdrvvgemal vvgvdpaalv aayhatwrdr lvrwnaaetv
       61 rilagrlgga ptdeqvaraa ahrltlahrv lgrvspatld vldalrergh rlalisnats
      121 etaeawpggp larrfdvtvf sceaglakpd paiyraaaqr lgvapadcvy vgdgadgela
      181 gaaaagmtvi rttehqdtdp gwigpvianl gdlpahleqp asae
//
LOCUS       WP_457605016             491 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605016
VERSION     WP_457605016.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..491
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=51748
     Region          24..271
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(24,26..29,31,44,46,78,95..98,101,103,139,141,
                     143..144,146,156..157,160,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24,26..29,31,44,46,78,95..98,101,141,143..144,146,
                     156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,101,103,139,141,143,160,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,69,75,80..83,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,169..172,176..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtetppgalr lpivpgltdl qvfarggyat iyratqisvg revavkienr tldserdqar
       61 flrearaagr msshphvvdl fdvgvtvdqh pylimelcdg syaermrtsp lgpaetrdlg
      121 vkiadalahs haagvlhrdv kpanilhsef nsavladfgl avlaefrdss vmlealtpay
      181 appetfnhsp ptpavdvysl catlyalmyg rpprwhsern pslvtvlemf qqpipglpgv
      241 pgelidvlrl gmsndpgarp savelrgllt slpldgapat ggrfddgtgd rfhrtggpnp
      301 rppadddhpt vasrgrrwpk rwflggagvl alaasagggw vagghtpavt ptpatsgvag
      361 vapvpgcasa dvrlpagarc atelecfgpv rlrrdraeas rvpcdgqhtw etyaagdlpa
      421 alagarhetv aadpavgrvc nadtfrlvsg gksasgwnle vlppeaeadr tyrclagrgv
      481 nalagptltg r
//
LOCUS       WP_457605019             247 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605019
VERSION     WP_457605019.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25882
     Region          4..207
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mpdrvavlsd ihgvlpalea vlaepdvaaa dlivltgdla agpqpvevld rlaalgdrac
       61 wvggnadrel vqaragkssp iavsnwaagq lrddqvarla alppsvtlpv sglgdvlfch
      121 atprddeevv lvdsrldrwa evfaglpaev gtvvcghthm pftrlvdrcl vvnpgsvgmp
      181 yggagawwal lgpgvqlrrt rfdvdaacar vaaestfpda aawadeyvrs rhsdadaltv
      241 fgprdgr
//
LOCUS       WP_457605020             230 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605020
VERSION     WP_457605020.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..230
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24628
     Region          35..190
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mtrrppgwfd pllgrlgtar aedftrivtp esggresavl vllgeepgag pdvlvlqraa
       61 tlrnhagqpa fpggaadped adaratalre aneevgldpg svtvlaelpr lwipvsdfvv
      121 tpvlawwhdp hpvhprepae vahvarlpvt elvdpdnrmr vrhpngwvgp afsargmlvw
      181 gftagvidrl lemggwsrpw phsrvvdlpp vdatpapsag teaadespvr
//
LOCUS       WP_457605021             263 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatase PAP2 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605021
VERSION     WP_457605021.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..263
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=27892
     Region          48..219
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(131,138,155..157,201,207,211)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mdttgatvth rswrhrrldr dhslglrltl tvvaaflvlv pfaliallvl gawppllrld
       61 asitdafhgy aqdhpawvav mtvwthvfgp gplrvaavvv vvwlvrrgap rlavwvvvtm
      121 vaggllgall kllvgrdrpd lldpvaraag ysfpsghaln atlaagvlll vflpfvrdsr
      181 pgrialwtaa llvtvvtgis rialgvhwts dvvggwvlgt avvaataaaf atwhsgsgrp
      241 strplregve peladqrpeg gra
//
LOCUS       WP_457605028             240 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605028
VERSION     WP_457605028.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24430
     Region          17..222
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mnpveqavvw lndplnwtnp ggvldrlgeh lsmsalavll gclvawpvgl wlghsgrggg
       61 lvllvsnvtl aiptlallti lpltflgfgr pavvvalavf aippllanaf tgvrqadpea
      121 rdaargmgls ggqvlrrvel plavpylaag frtaavqvva taalasfvng gglgqiirag
      181 fgldiaaggg qiiaggvlva glallvegvl alvervvtpr plrrertran rrataattgs
//
LOCUS       WP_457605033             248 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605033
VERSION     WP_457605033.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..248
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26598
     Region          17..134
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtdptaalsf gaaaadydrf rprypeaalr waldglhdar vvdlgagtri ltrgllaltg
       61 pvaqvvpvep dpgmraqlaa atpgatalag saeavplpdg sadavlagqa yhwfdrerah
      121 aevarvlrpg gtfapvwnir dervgwvael triahlgdna gdvtqryadf gaaftavevg
      181 efahattltp devvgmlhtr sfwltadade rrrvdaelae lfaghpdlag retvelpyrt
      241 mvlrarrr
//
LOCUS       WP_457605037             346 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605037
VERSION     WP_457605037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..346
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36846
     Region          6..342
                     /region_name="CAD1"
                     /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283"
                     /db_xref="CDD:176186"
     Site            order(41..43,46,158,162,182..187,205..206,210,225,
                     244..245,247,267..268,291..293)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(41,43,63,89,158,293)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(41,63,158)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(94,97,100,108)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(107,165,169,261,266..268,270,279,281..282,285..292)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176186"
ORIGIN      
        1 mltvnayaat sateplaptt ierrdlgpdd vlidirfsgi chsdihtars ewgptrypiv
       61 vgheiagvvr evgsavtkfa vgdrvgvgcl vdscrecdnc rkgleqyclk gstgtyggvg
      121 rdgkptqggy sqaivvtedf vlripdgiel daaapllcag ittysplrhw nagpgrrvav
      181 igmgglghma vklahamgae vtvlsqslkk redglrlgad hyyatsdedt ftelagsfdl
      241 iintvsatld mdaylrllav dgtlvnvgap ekplsvhafs liparrsfag sniggiaetq
      301 emldfcaehg lgaeievipa ekineayerv ldsdvryrfv idastf
//
LOCUS       WP_457605042             320 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605042
VERSION     WP_457605042.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..320
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32268
     Region          4..308
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mrersgvglg lallsaitfa tsgtfarpli tgewsavavv iarvgiaalv lavpavlalr
       61 grwsvlrrna gsvvlfgllg vataqacffn avrylpvgva llleylgivl vvgwmwlvhg
      121 qrprlltvag svialcglvl vldltgagrl dpvgvlwglg agvglagyfv iagridaglp
      181 svvmasggma vgavallllg glgalplaag tadvtfgghr vswlvpiagl sliaavvayl
      241 agvagtrllg arlssfvglt evmfavliaw lvldelpsli qlaggvlilg gvalvradel
      301 rgtpsvpeaa qaepvltgdr
//
LOCUS       WP_457605043             232 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605043
VERSION     WP_457605043.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..232
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24086
     Region          7..224
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 msgprgavvf dadetlvdlr pavtgalvav leemrrrtpa aaavaladle gdwgavfgal
       61 saapvqeirr aalarslara gleadldefa alffarryal srpfpdvlpa laalrqhhvl
      121 gfatngnsra ercglagqfa fevyaheggl pkkpvpeffa avvaasglpa arivhvgdsp
      181 ehdvaaaqra glravwlnra glprprglep daevstlagl stvlatltsa na
//
LOCUS       WP_457605045             215 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605045
VERSION     WP_457605045.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..215
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21501
     Region          8..>150
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdtaartget aqtldrglrl lhlvadapgg ltvteaahrl gigraavyrl vgaltghgml
       61 rrdgegrlri gvgvlhlarr aqpllaegal palrrlaedt gatahltvve ggegvalavv
      121 epswtsfhva yrtgtrhple rgaagravla gragdpgpvs tsgelqsgay gvaapvlgvp
      181 glegsvgvvs ltpldmadvg aqvtaaaeav aaals
//
LOCUS       WP_457605047             363 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605047
VERSION     WP_457605047.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39470
     Region          1..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtyakas riypgterpa vnqldlqigd geflvlvgps gcgkstslrm lagledvddg
       61 aiyiddrdvt hlppkardia mvfqnyalyp hmtvyenmaf alklrktsks eidrrvkeaa
      121 gllqleefls rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvqtrtqias
      181 lqaklgvttv yvthdqveam tmghrvavml dgvlqqvdtp ralydtpanv fvagfmgspa
      241 mniktvklte qggafaemiv pltreqvqaa gaeggdgkvt vgfrpedcdl vspseggmpv
      301 vvelvedlgs danvyghaal eghnerfvvr tdrrsmpnmg dtvfvkprtg rshvfhaatg
      361 qri
//
LOCUS       WP_457605053             207 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605053
VERSION     WP_457605053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21878
     Region          3..125
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprprsltpa qladaalavl drdglpgltm ravgaqlgts tmglyryvad rdelealvve
       61 rvlepvdtrp ppdvpwadgi rdlaervrra vglhpavvpl lpayrhrspt ilrwgeavla
      121 mltragftgt grviafrall gyvvgaiqme hlgalsgpgt aviaalprde fpllaatare
      181 agavapedef gggldllldg larrlds
//
LOCUS       WP_457605056             413 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605056
VERSION     WP_457605056.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..413
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41328
     Region          1..413
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 meqlarrlgv pdavvvglgs mlgagvfvvf apaaaaaggp gllvalavag fiaycnatss
       61 arlaarypes ggtyvygrer lhpfagflag wgfvvgktas caamaltvga ylwpgrarlv
      121 avlavvavta vnlrgigkta tatrvlvavv lavlavvavt gapqvaadrl tapaglgvgg
      181 vltaagllff afagyariat lgeevrdpeh tipravplal gavlaiyltl avvalgvlga
      241 drlastdapl vevvtaaghp glawlvraga avavtgvlls llagvgrttl amarrhdlpg
      301 alaavhprhl vphraelava avviavvavg dvrgaigfss ctvlvyyait nasaltlgpd
      361 pdrrlpvrll aalglvgclv lavnlplpsv lagfgvlalg algyavrrrr rpa
//
LOCUS       WP_457605068             466 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605068
VERSION     WP_457605068.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..466
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47838
     Region          1..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 maahpllddl raalgdaavl tdpdllsghe rdeadlcdsg tplavvrprd tdevvavvra
       61 agrhgvpvvp qgartglaga anavdgavvv stvamdavre idpvgriavv qpgvvnaala
      121 ravrehglwy ppdpgswess tiggnvatna ggmccvkygv tseyvlglev vlasgevlrt
      181 grrtakgvag ydltrlfvgs egtlgvitev tvalrpapee sltlvavfpt vataggavag
      241 iaergltpsl lelldrthlr aieayrpmgl rtdaeallla avdtgtraad dlarlaevct
      301 aagadevyaa tdaaeaaall qarrlahpam erfaaetfpg gngglviddv avprgrlael
      361 ldgvariaea crvpigvvgh agdgnmhpni vvdradpasl argrrafdei mrlgldlggt
      421 ctgehgvgll krdwlareig pvgvrvhqai kaaldpagll npgkvf
//
LOCUS       WP_457605070             211 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605070
VERSION     WP_457605070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..211
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22564
     Region          24..211
                     /region_name="COG4339"
                     /note="Predicted metal-dependent phosphohydrolase, HD
                     superfamily [General function prediction only]"
                     /db_xref="CDD:443480"
ORIGIN      
        1 mddltarwrn aaraagatdp aaadragarl lagwrephrr yhdeahlrav ldvvdtyagl
       61 ardadlvrla awchdavygp raagdanera sadlavella aaglpaatvt gvrrlvllta
      121 ghaagpddpd gallcdadla vlaapperyd ryaaairaey ahvpepdfrt graavlrhll
      181 dlpalyrlpe pharwedrar anlsrelaal t
//
LOCUS       WP_457605071             714 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605071
VERSION     WP_457605071.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..714
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74641
     Region          33..712
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtpsrtatgp avpkkrrrgr agagelltaa vgavpggaar pgqqqmaeai ersiasgehl
       61 lvqagtgtgk slaylapalt vdgpvvvsta tlalqsqlve hdlprladav epvlgrrptf
      121 avlkgrhhyl clarldssve depddalfda pragnsggtk wlgeagrlgk qvqrlrdwae
      181 etatgdrdel dpgvddqvwr svsmparecv gasrcpfgqe cfaeasrara readivvtnh
      241 sllavdmlag rhivpphrll vvdeahelad rvssaaqael vpelidrstr rarpllrpdv
      301 aerlteagda lavglaeapa grltaglppa lreactllds atraalegig dvkaddpdpv
      361 rkqqakavld elsttaqrll eeadhdvawv ekpdngsrra lvvaplsvag tlathlyder
      421 tvvatsatla lggrfdtvar algldapppa ppspaaaaia taaaagrspv tpvaaaegsr
      481 asigtvpate gpgwssldvg spfdyarqgi lyvaahlprp svsglpgpag eellalveal
      541 ggrtlglfss rraaqqaael vrartdlpvl lqgeealpll vrrfrevres clfgvmslwq
      601 gvdvpgdacq lvvidrlpfp rpdeplaaar aaavdagggs gfaavsvpia avrlaqgvgr
      661 liratgdrgv vavldsrlet argygpflrr slppfwyttr pevargaler laks
//
LOCUS       WP_457605075             253 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605075
VERSION     WP_457605075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..253
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27589
     Region          32..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtdldnqagy wnstgsaktf ghpvarqwld gidrrarvld ygcgygrlag llvrwgfenv
       61 egvdvaprlv nraiqeqpga rftvltspph ldhpddsvdl vllfavltci pgdagqrell
      121 telgrvlrpg gllyvsdlcl qeddrnrsry erfaakygty gifetddgav crhhttdwld
      181 qllgdfdvva srdvavetmn grparasqrl vakpqpgasr aghrgvgdss grrqcppsha
      241 dprstsgqpd htg
//
LOCUS       WP_457605076             275 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605076
VERSION     WP_457605076.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 275)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29413
     Region          32..235
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mtidgfaapp alveharrfr aegavpavpr vaatvlllrp agdgfevymi rrvaamtfgg
       61 myafpgggvd rsdseahlgw agpepavwge rlrldpsdaq avvcaaarev feeagvllag
      121 pdpdtvvgdv sgddweaarq dlegrrvgfa dllagrgltl rsdlllpwsr witpefeprr
      181 fdtyffvall pegqrtrdvs geadhtlwlr padalaraea geltmlpptm vtlaevaaag
      241 dlaavaraaa erepgtpilp hidgldgdep lfrlr
//
LOCUS       WP_457605083             214 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605083
VERSION     WP_457605083.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..214
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21839
     Region          4..>65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 matskdlpdv ggfirdlrrn akislrqlae qagvsnpyls qierglrkps aevlqqlasa
       61 lrvstpamyl ragllddkeg qgvlaaiavd peltmaqkqs ltqiyetfrr enarlaeate
      121 aattaetaga tepasapeap atvaaaatgp vtpegtptea vlesvavtea gaapapttap
      181 apttapaptt aapqdttarr aarkaagaae eeqs
//
LOCUS       WP_457605084             149 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605084
VERSION     WP_457605084.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..149
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16085
     Region          7..148
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mardwklvid cadpiglarf waealgyqve dnsvlierla aagavppeay vevdgrkawr
       61 elaavrhpdd pvdpasgtgl grrflfqavp epkrvknrlh vdlhvgpegr aaevkrltal
      121 gatvlaevad rggehttmad pegnefdvq
//
LOCUS       WP_457605094             605 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605094
VERSION     WP_457605094.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..605
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=65059
     Region          42..562
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 msrstagrls aerraddlrr lraerfdvlv igggvtgaga aldaasrglk valveardya
       61 agtssrsskl ihgglryleq lefhlvheal tergllatrl aphlvrpvpi lvplpaegga
      121 rdlprrffrr syyglgvaay dafagvfggg rgmplhrhlt regtrrifps lrpdklagai
      181 ryydgqvdda rlvvtlarta aslgatvvts aravgltrqa revtgvrvrd leapagspda
      241 efevrartvi aatgvwsddm srmlndvglr pklrvraskg vhlvvprsai vgetglilrt
      301 atsvlfvipw gghwiigttd tdwqldrshp aatasdidyl lsqvnevldr plttadiegv
      361 yaglrpllag eadstsklsr ehavvepmlg lllvaggkyt tyrvmasdvv dramhrlgrt
      421 rssrtadlpl lgadgyaamw rdradlarrh gvavgvvehl lerygnltle llalvdadpl
      481 lgsplagape ylaaevtyaa raegalhled vltrrtrisi etshrglesa ehaaelmgav
      541 lgwdaatrdr evahyrarvl aeresqlmpd diaadaarlg apdvrgfaad rgtdgpgvel
      601 paspr
//
LOCUS       WP_457605098             590 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605098
VERSION     WP_457605098.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..590
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63761
     Region          21..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maaeeathrp pttprppats rpdvsvvvpv yntlrylrsc ldsvlrqtig adrmeivavd
       61 dgstdgsgrl ldryaakhpg tvrvvhqshs ggpaspcnrg ldlttgryvf flgsddrlgp
      121 ealerlvaaa drygsdvvlg kvvgvngrhv fsdvfadgna vdvslfdsal pwslantklf
      181 rrdlvdrlgl rfpedmpvls dqpftlaacy harrisvlad ydyyhavrrl darnityhsr
      241 veqrlvsver lfayvaelip agerrdavlr rhaglelanl vgddfrhldr aaqervhatv
      301 arlarrhvtd clrdrldiea rlrlgavtag gvddllavie qdsgrgvpat vfagdrwhag
      361 ypgaparwtd vtdvradwla rldavdvswv dghtltvttr spyprfatea gpvrmlagpv
      421 vgatrmdagd ptgrtlrtdf aldlllaasa asgqrhpvra evdgghgrgg aavraprlaa
      481 grprllrhga rlygvaatvd prngqlvlsv vpvtvgqlvg rlrrrgrrgp vtaqtsgrsa
      541 eallgrhghl evrgaaqvqp gllrrpdqph hhpgaggaap dqargvrvdv
//
LOCUS       WP_457605103            1041 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605103
VERSION     WP_457605103.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1041
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=110214
     Region          10..1035
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mstsqewtfp asyaqervwm anqldagspv fnvsfpwlfp advdadtaad vvnrviarhe
       61 alrtrlrtdd galvqvvrah epaplpvtdi thlpageqra eferirgema rtpipldaap
      121 lwrarlirme eglalalvvh havfdshsav lfhaelvafc eaartgaepa vpelpiqyad
      181 favwqrqqlt gaeldrqlaf wtghlagapp vtglpldrpr paqlgfagde vrftlpdgll
      241 drvgvlatga qatpymvlla gfaallsris gdadvvvgvs tagrdnpelt pligmfvnpv
      301 alrcdvsgdp tfaallgrvr nglidamehg qtpfqkivea vdpqrdpsvq pifqtalnwi
      361 pdsgldpvel gttkddlafd ittgdcrlvy rtelfdrata etvvrryvrl laaavaeper
      421 tvgalplltd tereqvlgaw ndtardvpvt tvvdevqrqa aatpdaaalv cdgvtlryge
      481 lntaanrlar llvargagpe trvalalprs cdlvvamlav lkagaayvpv dtaypagria
      541 ylladaapal vvtapdtaal vpgdalvldg eigsdqsgdd ltdadrvapl rpehpayvly
      601 tsgstgrpkg vvvehravta ylawaratyp glagvallhs pvsfdltvtg llgtltaggt
      661 vrlaaidepa araggrpafl kvtpshlpll dgelsptadl viggealtge qlaawraahp
      721 dvavineygp teatvgcvaa riapgepvpa gpvpigtptw ntrallldga lrpvppgvvg
      781 elyvtgtqla rgyhdrpalt aerflpcpyg ppgarmyatg dlarwradgt ldylgrrddq
      841 vkvrgmriel geveaallah pdvraaaaav rtdggepmlv gylvgpahed svraelarel
      901 pahlvpaalv rldalpltpn gkldraalpa patteaaqds yvaprteaea lvaevyaeil
      961 rvekvgahdd ffalggnslr gmramarira evdvdlpmra lfsspvvadl aaqieqriaa
     1021 eldglsdtev aallaaeegt n
//
LOCUS       WP_457605104            1814 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605104
VERSION     WP_457605104.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1814)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1814)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   3  (residues 1 to 1814)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   4  (residues 1 to 1814)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 1814)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 1814)
  AUTHORS   Keatinge-Clay,A.T. and Stroud,R.M.
  TITLE     The structure of a ketoreductase determines the organization of the
            beta-carbon processing enzymes of modular polyketide synthases
  JOURNAL   Structure 14 (4), 737-748 (2006)
   PUBMED   16564177
REFERENCE   7  (residues 1 to 1814)
  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
REFERENCE   8  (residues 1 to 1814)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 1814)
  AUTHORS   Keating,T.A. and Walsh,C.T.
  TITLE     Initiation, elongation, and termination strategies in polyketide
            and polypeptide antibiotic biosynthesis
  JOURNAL   Curr Opin Chem Biol 3 (5), 598-606 (1999)
   PUBMED   10508662
REFERENCE   10 (residues 1 to 1814)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18690430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1814
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1814
                     /product="type I polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="4.2.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016218 - polyketide synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=188819
     Region          12..1365
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1362..1633
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Region          1716..1792
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mqndipaddg vepiaivgla arlpgaadvd efwrnlvdgv estteltree qlargaqpqe
       61 vddpgwvnra plvdgydefd aglfgmtare aeitdpqhrl fletcytalq nagydpgryd
      121 gavgvyagtg gntylhrnvy rnkrvggnph gavslatgns pnyvatnvsy rldlrgpsmt
      181 vhtacstslv afhlacealr ngecdmalag gvnielphvg ylgmdgftsp dgrcrpfdag
      241 angtvwgsgv gvtllkrlsd aiadgdtira vvlgnainnd gagkvgftap sidgqmeava
      301 qavelagvdp rsisyveahg tgtalgdpie vaalsavytk dtdergwcgi gsvksnighl
      361 sqpsgivsvi ktvlamehgl ipptinyetp npaidfadtp fyvantltkw dtdggprrag
      421 vssfgiggtn ahvvleeapa agrheppsrp aqllqvsakt ataldtavrr laghlesgsd
      481 valadvahtl rvgrqvyahr aavvagdpas aaaalrerrk ghrgvaegaa prvaflfsgq
      541 gsqyagmgae lyaqdsayav avdecaellr pelgldirdl ilgrdpeaad kltqtrytqp
      601 alftveyala aawraagvtp aamighsige yvaatvagvl dladalrvva argrlmhalp
      661 agsmlavtld esevtgklpe glsvatvngp gtcvvageta lveefaaslg gknkskmlrt
      721 shafhspmmd pildeftalm atvplrapav pfvsnvtgtw iteaqatdpa ywaahlrrpv
      781 rfgacvatll aegtwalvec gpgrqlanla rmqvakagea qraltplgsl pgpgeqtgdl
      841 aallgtagal wcagvpvnvp adpharrvpl ptypferrry widpdpeqel aaapvetgpr
      901 plpewfavpv wrqaaparta eplgrclvla dgprgdalva alraagddpv evrageafta
      961 tangfrlrpg vradaeelva algadlprri vhafaldgdp agtdaaaawa aqergffgal
     1021 hlvqalagag vtadeagvrl dlvtagigdv rgddltrpeh atlaglarvl paelpgltvr
     1081 lldtdpaarg vaalvaelrs pvdaehpeva lrgdrrwlag yeqvtvdaed epgvlreegr
     1141 ylitgglggi gvtlaedfar raraklvlla rsglperdew dahlavhgga dragraiaai
     1201 rrmeaagaev lvlaadvtda ddlrrvrdea errfggldgi vhaaglpggg maevkdrdea
     1261 rrvlapklag tlalarvfgd lpldfvvlcs sitaviggfg qvdycaannf ldafarsgtg
     1321 frapvvsqnw ggwaevgmav etaapaafra agrdtvttav ahpvlttmva gpdgtvlhgl
     1381 vsadthwlld ehriggvpvv pgtahlesvr aavvaalpap gpdaavelrd vvflepfsvp
     1441 dgtvaqyrve ltpaedgtdf tvaslaagqa rthvrgtagw ttdaappaav pavagrrvdd
     1501 dasfgrgrts mltfgprwaa laehhladge elarvqapaa avgdlpswgm hpalldvata
     1561 fgrgqgagty lplsygrivv rgalpatfhs hlrhrpaatd evvaadlslr dpdgrelvai
     1621 sdfvlrrvdq davtgnlaes paaddaaapv tedirpvdga eafrrslaag lgaqvvittr
     1681 tvadirrraa rvttdslaee tdapagtaat gggsaapgte lektiaqvwr dglgvtdvgv
     1741 dddffalggn slvavqliaa mrkatgvrlp mrslfetptv aglaarieel raetpadapa
     1801 apaaipaipr lprg
//
LOCUS       WP_457605116             463 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605116
VERSION     WP_457605116.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 463)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 463)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..463
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48731
     Region          7..345
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msspstrrla islilalagt gvaacsddgq ksdssqitvw sledvadrva atktiiadyt
       61 aktgvkvnlv tvnedqfpsl iassaaagdl pdvvgsvsla gvrtlsanel ldtdandavi
      121 drlgrdtftp raleltsdgg tqlavpsdgw gqllvyrkdl faaaglpapd tyekiaaaaa
      181 klntggvagi taatspgdvf tqqtfehlal andcrltdds gnvtldspac veafrfygdl
      241 mrnnsvkgaq dvdttratyf agkaamliws pfildelagl radarptcpq cqsdpawlak
      301 nsgfvtaikg pngtepaqyg evsswavldg aadpaksfve ymlsdgyprw fgmspegrfp
      361 vrtgtredkq kfrtawntsp agvdtkkpls evygedvlat lrkspdtfqr wgltenqgkl
      421 vgailgelpv pkaladvvgg rsdaraaaer arkdveaiak gvn
//
LOCUS       WP_457605119              89 aa            linear   BCT 27-JAN-2026
DEFINITION  metal-sensitive transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605119
VERSION     WP_457605119.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Porto,T.V., Hough,M.A. and Worrall,J.A.
  TITLE     Structural insights into conformational switching in the copper
            metalloregulator CsoR from Streptomyces lividans
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 9), 1872-1878 (2015)
   PUBMED   26327377
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Dwarakanath,S., Chaplin,A.K., Hough,M.A., Rigali,S., Vijgenboom,E.
            and Worrall,J.A.R.
  TITLE     Response to copper stress in Streptomyces lividans extends beyond
            genes under direct control of a copper-sensitive operon repressor
            protein (CsoR)
  JOURNAL   J Biol Chem 287 (21), 17833-17847 (2012)
   PUBMED   22451651
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Sakamoto,K., Agari,Y., Agari,K., Kuramitsu,S. and Shinkai,A.
  TITLE     Structural and functional characterization of the transcriptional
            repressor CsoR from Thermus thermophilus HB8
  JOURNAL   Microbiology (Reading) 156 (Pt 7), 1993-2005 (2010)
   PUBMED   20395270
  REMARK    Erratum:[Microbiology. 2014 Dec;160(Pt 12):2820]
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Liu,T., Ramesh,A., Ma,Z., Ward,S.K., Zhang,L., George,G.N.,
            Talaat,A.M., Sacchettini,J.C. and Giedroc,D.P.
  TITLE     CsoR is a novel Mycobacterium tuberculosis copper-sensing
            transcriptional regulator
  JOURNAL   Nat Chem Biol 3 (1), 60-68 (2007)
   PUBMED   17143269
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..89
                     /product="metal-sensitive transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=9729
     Region          5..>64
                     /region_name="FrmR"
                     /note="DNA-binding transcriptional regulator, FrmR family
                     [Transcription]; COG1937"
                     /db_xref="CDD:441540"
ORIGIN      
        1 mnlrpemtge altrlkrarg qlnaviemme ngedcraalt qlaavskaid ragfkiiasg
       61 mrycdaarqa geepemteee lerlflsla
//
LOCUS       WP_457605126             255 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605126
VERSION     WP_457605126.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..255
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27802
     Region          37..131
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mpnralsfga aarayerfrp gypeeladlv layadrpvrt aleigagtgk atrlfarrgi
       61 avtatdpdpa mlaelrrhvp advrvrqaaf eqlraderhd lvyaaaalhw tdpdrrweri
      121 agllasggvf asfggplria dpalrdavaa arsafladde ipspdgtppe aamqwpgtel
      181 rasewftdvr qsqiarriti saddyvglls tvsaylelpp pvreqvfrrv rdvlpgtvev
      241 tadvtvhlar rtsqp
//
LOCUS       WP_457605130             247 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM-dependent methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605130
VERSION     WP_457605130.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26419
     Region          <40..139
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdrqrlssia hshhpiaapl sgvnvnrllr ragrrpaari ldlgcgeaaw alqalahypd
       61 ghadgvdlnp yaleraaeaa avrglaerlt lherdarsyv pdgdydlvlc vgsthafggf
      121 ggtlelagrh vnadgilmvg egfwqvpptp ealtalgakp ddhtdlaglv aaaeragwtp
      181 vyahvsdtae wddyewswtg sltewaldnp ghtdaadala aagehrdqwl rgyrgvlgfa
      241 tlvlrrt
//
LOCUS       WP_457605132             468 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605132
VERSION     WP_457605132.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..468
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50755
     Region          <180..>295
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          371..461
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mfrrtvaval aaltvlaglp gaaragsppp rlawgecadd lpdvppdprv rcarlrlpvd
       61 warpngptfd lavarrsarl peqrvgtlvf gpggpgdsgv erirrgdrfs delldrfdlv
      121 svdprtvart aapfctadpa lrrppvplag qadfdaavay nralwsrcrp tspvfdhadt
      181 lstvrdleal rralgerrls fhgssygtll gqqyaerypg hvravvlegv fdhsldvrsf
      241 vrtqaatlqd sfdefvswcd ssadcvlhgr dvrsvwarvl aradrgeyap rtafdvtava
      301 lgtlagprwp qlaaivrdmd agtpppavnl sisvaafcad wpaqvrdyae yaglvrdaaa
      361 aapdvrygag llavqtclgw pspvrnpphe lnvhtrlpll llnsrhdprt ghawavnvar
      421 qlgrhgrlvt yegwghgtyq rndcttavvd rylvdltvpa pgtrcpas
//
LOCUS       WP_457605133             129 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605133
VERSION     WP_457605133.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..129
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13551
     Region          11..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mpplplgrlh hlivdcpdpm aearfwsavl gdpityaddd ftvvsastaa sglafqrapg
       61 lvpptwpdpa vpqqvhldvm vddqdaagea vlalgarrlp gdhvyadpag hpfclirrpt
      121 waspvdgsa
//
LOCUS       WP_457605137             291 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605137
VERSION     WP_457605137.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..291
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=29677
     Region          1..279
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mdvlryaaft adpaggnpag vvldatgagd aemqqvaaev gysetaflvp tgeggrftvr
       61 yfspkaevpf cghatiasav ayaqrhgpgv lhldtraglv evatsvqadg attatltsva
      121 prtvplaagd laallaalrw spddldatlp prvayagawh pivaaatrrr ladldydmaa
      181 lsalmaerdw ttidlvhrep plvfharnpf ppggvvedaa tgaaaaafgg ylrelglvrp
      241 patvtvrqge dmgrpsllti gipaapgagi avtgtavpip addvrsgaar s
//
LOCUS       WP_457605142             127 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605142
VERSION     WP_457605142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14325
     Region          22..119
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msaslrdhrl pmpvpageyd rcpvtdllrr msdkwtllli tllgrhphrf nelhravegi
       61 sprmltrtlr tlesdglver evfptlppsv eyrltplgvs lleplsalad wavahyaeiv
      121 avrqrpv
//
LOCUS       WP_457605148             249 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605148
VERSION     WP_457605148.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..249
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27288
     Region          15..222
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mriaehiaal deegvrlaea adragldapv ptcpgwqvrd llrhvsgvhr warghvmtgr
       61 rqpystrega effaavddde lldwfreghr aladtlaaad esvecwtflp apsplafwar
      121 rqahetavhr adaesavstv pywepsfaad gidellngff grpggrlvad pprsmalvpt
      181 didaawtfsi epagrrvvag empaqltivg saselylllw nrngsgrlel rgdaavldlw
      241 raratitwn
//
LOCUS       WP_457605143             250 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605143
VERSION     WP_457605143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..250
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25960
     Region          183..249
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mdariqqsvv vnlsrrpapv evgpfvigld ptttspyiny atprpgaavt aadvaalvaa
       61 fhaadrrprl eyvtscapdl ealltaagft learhtylvc vpsmpasppv pdhfslcepg
      121 tdsqraalis vqneafggdp vasetdvarl rrqqdaggvv vmavtedggc aggggaaapv
      181 gavsevagia vraphrrrgl asaitadvtr rlfsagaeva wleaggedsw rvyqrvgyrp
      241 agqrlylamn
//
LOCUS       WP_457605152             396 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605152
VERSION     WP_457605152.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..396
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41841
     Region          1..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maskadtiga rirywrmrrg gmsqavlagl agvsqsyisq vesgrktidr rstlvavaaa
       61 lqitvadllg qgtetgdpar eraaecvpai wsalieiedg errpstrthe elaagiarse
      121 qlrhrsnfpa maqmlpglll eaaaaggpal aqvayqasac lrhlgyrhla lnaarvavta
      181 aedveeaawl gatrfayaqs lpiesaslaa raadrslael qsaasdervr qmlgqlhlsa
      241 alastvsgrp daardhltea areaatlgdp adgmgfngcg fgptnvtlwe msiaaesgep
      301 grvielsrrv rpqvlaasir qmsywldlgr aladsgrrdn eaiaafvrae qaapvpfsln
      361 plaqdavvam aqrakrravp nelrllagrl gislaa
//
LOCUS       WP_457605153             194 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605153
VERSION     WP_457605153.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..194
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20626
     Region          10..152
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 mtddphagam sfifeagvlk raartgwwfa gvkhpesiae hsfrtaligm mlaamegadp
       61 grvsmlcvlh dtqetritdi phiakrylta apntavtadq vaacppavad vitavvaeye
      121 asetleaiva rdadkleclv qaveyrhqgv advqrwidss raalktssah rladvaltga
      181 pmawlnppas ppvt
//
LOCUS       WP_457605156             606 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605156
VERSION     WP_457605156.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10575293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..606
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65999
     Region          5..36
                     /region_name="AcylCoA_DH_N"
                     /note="Acyl-CoA dehydrogenase N terminal; pfam12418"
                     /db_xref="CDD:463571"
     Region          43..467
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(134,164,166,198,200,449..451,453,455)
                     /site_type="active"
                     /db_xref="CDD:173838"
     Region          478..601
                     /region_name="Acyl-CoA_dh_C"
                     /note="Acetyl-CoA dehydrogenase C-terminal like;
                     pfam12806"
                     /db_xref="CDD:463716"
ORIGIN      
        1 msssdlllsr rdlafllhdw ldvtrlaerp ryaehtretv devldlaarv aaerfaphnr
       61 aadtgeptfd gqrvrtipqv kaaleafaet gllaatmdes vgglqlphtv aaaafawfqa
      121 anvgtsaypm ltlgnanlll ahgsaeqidt wvrpmvegrf fgtmclsepq agssltdltt
      181 raepqddgty rivgtkmwis ggdhelaeni vhlvlaripg appgvkglsl fivpkvlldd
      241 dgnlgprndv vlvglnhklg yrgttntlln fgegvhrpyg ragavgylvg qphqglavmf
      301 hmmnearigi gagatalgyt aylksvayar qrpqgrpvad kdpttpqvpi vahpdvrrml
      361 laqksyvega lalvlycgrl ldeqktapae adrerarlll dlltpitksw paqwclaand
      421 laiqvhggyg ytrdydveqh wrdnrlnaih egthgiqald llgrkvtmrd gaalelllet
      481 irgtvtrawk adglaselag qlgaavdria vvtrrlwapg dpelalanas vyleavghvv
      541 iawmwleqvl avealgspdg aegeflagkr qaaryfyrwe lpkvgaqfdl legldrttld
      601 mreswf
//
LOCUS       WP_457605161             442 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605161
VERSION     WP_457605161.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..442
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47544
     Region          52..431
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mdgnndapap spsrpvqngs elpeqlalqg gqpvrrtpwp tydkgavfvh sededaaira
       61 vrshlyfryd hrpphetecg rfedelcryf gtrhalavss gtaalalalm gagvppgslv
      121 acpgftfvat psaivlagcr pllvevdddl rmdlddlrrr wrpeiravmv vhmrgfaadv
      181 ealsafaaem gvpliedavp algaelngrk lgtfgaagaf stqsdkalnc geggflitdd
      241 stlfaraval sgayegrlrr hfphgepplt gldlpllslr mdeiraallr aeltrlpqrl
      301 alfhrnyahv saalaglpgi avrrpvapga ylgeafvfrv pggdagwgda gwfaralrae
      361 gidarnigad ddlnvrafwn wrflydsadp geiratlprt arlltetvdv plssnltped
      421 cddlvravrk vaaaretalv gs
//
LOCUS       WP_457605157             486 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605157
VERSION     WP_457605157.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 486)
  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 486)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 486)
  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 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..486
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51838
     Region          152..485
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mtevrpdeet vpllgaevri adaagllaaa vdgpvellvn gdfpapvrev rctvradtaa
       61 eppvhrfeay lrveaapagl ivlglagpvg lllaerlaar ggdgpaaavg riaaeagrri
      121 wprpvatlva pprdpagrev lraaeeaglr prvdqdngtv riradvpsae vdpahlraml
      181 glllqavrel sgdsdepavl rgrtylvgrr plaaagprsa avtldqvggl pdvvarfrev
      241 avsfrhpaam arwgarrpqg ilmygppgtg ktmlaralan evgadfveir tpeildkylg
      301 gsernikrif rearryrrpt vmlfdefdsi isyagaggda asqavnavag ifkqemntlf
      361 eenpdvivva ttnfpqrvds slirsgrfdl kiaipapdea graeiltkmi relieryerp
      421 gfrmfaddld paalaadtag ltgadlreal rrvqlakalr eaaegappap igqddlreav
      481 aglrrg
//
LOCUS       WP_457605166             276 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605166
VERSION     WP_457605166.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..276
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27424
     Region          4..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlglkgrva lvaggtsgig lacakefaae gahvavcgrd pqrlaaaere ltavasgrvs
       61 atgvdltdtg aaarwvdrva gelggvdvll vsggsppvgt atgfdaddyr savdrvllpa
      121 vavslaalph mraagwgrll lvasetacvp igplvlsgvt raalvrfaqg lavdvgrdgi
      181 tvnvlapggv rtppmeraaa rlagadgdve arlaamghhs avgrlarpee vaavaaflag
      241 erasyvtagv hlidggaaat gpdlphltgv rkdtya
//
LOCUS       WP_457605167             279 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605167
VERSION     WP_457605167.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..279
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30696
     Region          45..177
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 msttsrfter dvseffdqtt qtylsfwdse gvlhtgyftg eddgdyhaaa drtsdilaad
       61 agidasanvl dvgcgcgnfl lrlaertgcr gegldlsier vrlaeqrrae rgaalpvsfr
      121 hgsatalpyd dgtfthvvsq dalflvpdkp rshaemfrvl apggvlavsd flqpterige
      181 aarrhvydrv rwndgysldg yrralteagf vdvvarslda hirqtyrvlg rtareraett
      241 adeaartwil gfadscdeiq aaidrgefgw gmfvarkpa
//
LOCUS       WP_457605168             426 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605168
VERSION     WP_457605168.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..426
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44797
     Region          22..420
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mttpgrtdpd vlvvgagvvg lccawflrra glsvtvvdrg evgdpaacsa gntgfvgtqg
       61 saplaepgvp atgirwlfsp qspfavrprl dgallawlwh frrhcterha ragfetllal
      121 kqrslallre icaedelagt ltergmilac hteqgyakar rtipaatarg vplreldrse
      181 larlepgvdf avagtllnee gaalripafl valaaalrar gvdvvtgaev rdfevtgrrv
      241 ravhtsrgel rpaevviaag vwsavcarml gvaltlqpak gytvtlpagp gtptrpvlls
      301 egkvavmplg drvrvggtle lsgldtsisp rrvdgilhta rrylpaldtg rrldvwsglr
      361 pctpdslpli grasgydnvs vatghghigm glapaggqll aqlvsgaepd lpletfavdr
      421 fqrgis
//
LOCUS       WP_457605169             237 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605169
VERSION     WP_457605169.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..237
                     /product="aspartate/glutamate racemase family protein"
                     /calculated_mol_wt=25604
     Region          7..225
                     /region_name="Asp_Glu_race"
                     /note="Asp/Glu/Hydantoin racemase; cl00518"
                     /db_xref="CDD:444951"
ORIGIN      
        1 mndrpeigvl cldtsfdkip ghirnpdtfd fpvryrvveg atpqrlvrea dptllrpfvd
       61 aardleaagv agitgacgfl vlfqaelaaa vrvplwsssl vqlpmvhrmv grpvgllvad
      121 eaaltsrhla aigaadvpva vtgmagqpef revmlegrrd aldverlaae vdervdalag
      181 ahpdlgalvv ectdlvpfah riqarlgvpv fdivtlttma yasltrrpyr rkrrgpq
//
LOCUS       WP_457605171             351 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605171
VERSION     WP_457605171.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..351
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37309
     Region          1..348
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mrfaftpeql alaetarryl aeqqppdaag vpetdparre aawktlgtlg wldadlgave
       61 wgvlaeecgy glhrepwltt valagpalra agqppagpva lawaeapagr arldeahlpg
      121 cravpdrdav rlhgrkervv dglaatsavv vargpdgpgl yladlaatrr vplpapwdat
      181 raecrvdlag apaedlwlda rrvladtrrl alalfaceav giarraheia vahardrvqf
      241 grpiganqav shplaqayar ietarslayr aawcvaerep gvepevvaaa laareaalta
      301 teaaiqtlga agftwahpah rwyrralwhq dfagtasdlr aelaamvlav a
//
LOCUS       WP_457605173             534 aa            linear   BCT 27-JAN-2026
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605173
VERSION     WP_457605173.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..534
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56579
     Region          1..530
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mlkgcvawpe tdaeryraag iwtgellgei gregarrhpg rtavvdaggr mtyaeldaaa
       61 drfaaglhrl glraedrvvv qlpntaafvv valglfrlga vpvfalpshr eaeltylarh
      121 tearalvvpd rfggydhrpl aatvaasaag ldhiivagep gphlalsevr deprdlpapd
      181 pgdvafflls ggttglpkli prthddyayq lrrsaealgv dehgvylasl paahnaalgc
      241 pgvlgtlrag grvvlsptps pddvfplita egvtlttlmp pllavwldla gdygvdlsgv
      301 llevggaplr pevareilsr glrlshwfgm aegplwytrl ddppetiatt qgrplipade
      361 yrvvdehdrd vppggvgefl vrgpttlrgy ydapeynata ftadgylrtg dlvrltpegn
      421 lmvagrikdv inrggekiga aelesqieah pavraaavia vpdpalgeki cavvvrrdeg
      481 ggldlaelra fltgrglaay klpdrlevvp afshtgagkv dkralrrslt gdga
//
LOCUS       WP_457605174             160 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605174
VERSION     WP_457605174.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..160
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17241
     Region          21..142
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mavrrldehs gplethcfvc spinehglri pfsydderae vlasftfaqr hsgaptyvhg
       61 glslavlnea mawavvggar rfavtvdtta rfvrplriga dyrvrariat tapdrlgttg
      121 tivdgtdrvc veataefrvl sestasrlsa rvaarrdpsa
//
LOCUS       WP_457605175             364 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605175
VERSION     WP_457605175.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..364
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38385
     Region          159..282
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mepsssparq aqalsmrlfl hslgaaelmt mylghrlgly rvlgdgpvtg aelaaragvg
       61 arhatewleq qaaagvvepa gdgrfrlpeg hrqaltdats pfavlslavl pvaglapmld
      121 rlveayakge gvgydeygee fraaqagmnr pvfthelprw irtalpdvha rlsrpgavvi
      181 dvgcgtgdss lalaqaypfa tvhgvdlgaa aigaardraa saglaervvf tvadvaerpg
      241 aergdlvcvf dalhdmsrpv rvltaardll rpggcvllme prvgerftap ageverfmya
      301 vsvlhclpvg ltgdgddgga pagtgtvmrp dtvrryaera gfaattvlpv ehrfhrlyrl
      361 dppa
//
LOCUS       WP_457605192             405 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605192
VERSION     WP_457605192.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 405)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..405
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=41003
     Region          2..403
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mnrvvitgvg pvsnigigar afeqglregr vgvgpirsfd ttgfprtmag evrdfvpvdl
       61 lrrldvaawg rsslfaaaaa rlavrdagld aaldagalap drvgvvvgtt sgesklteef
      121 grrvvdagfa avdpallagl pagrlafavn eelgvtgesv tlatacsasn yaigyaydai
      181 aagdaevmlt ggadsvcrwa hagfvrlgav aetacapfdl nrsgmvtaeg gamlvlesad
      241 haaargarpy aevlgyalnc dashmvapna atiaacmrla fdnagispsd vdyvcahgtg
      301 taandateae alfeafdgkv ppvssiksml ghtmgaasaf gaiasavaia rgflpptvnw
      361 aspdpamswl dpipnrarpa pvrvaqnngf afggnnaivl lgaps
//
LOCUS       WP_457605216             418 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605216
VERSION     WP_457605216.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..418
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44660
     Region          16..405
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mdkagfyrea rhdvdgplhg vrvleiskvw agpmtgavla dlgcevirie mpgnregrmp
       61 pdipgtglsw fretvhrnkr svaldlrrep areaflrlvv tadvvvenyr pgtldgwgvg
      121 yaqcrrvnpd ivfvsisgwg qygpratdag fdpiaqaaag wmglngepdg tpmkapsfla
      181 ddlaglhgai galaalrhrd rtgegqhvdv slldallans ggyltlgatg vplrrwgdqa
      241 dfvvpagtyr crdgwlylav aldkhwrsla aamdrpelar apgfatneer rarrdevnal
      301 vgawceartv aeaaaglaaa gipaepvrdf adaaadphvr erdmvqtvpl cngttgpltg
      361 paakfsrtpt rvrhgapavg adtealltea gvdwaelarl racgatdrqe apacirph
//
LOCUS       WP_457605226             380 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylate-amine ligase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605226
VERSION     WP_457605226.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18585821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..380
                     /product="carboxylate-amine ligase"
                     /EC_number="6.3.2.2"
                     /GO_function="GO:0004357 - glutamate-cysteine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0042398 - modified amino acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41121
     Region          19..379
                     /region_name="YbdK"
                     /note="Gamma-glutamyl:cysteine ligase YbdK, ATP-grasp
                     superfamily [Posttranslational modification, protein
                     turnover, chaperones]; COG2170"
                     /db_xref="CDD:441773"
ORIGIN      
        1 mrprptttat ttpqiptvlt lgveeeflll dpatgesmpv adrvrgalsg tareqsrqef
       61 rhsmvemvtp vspdlgelre hlvtlrraaa raadaagarl vavgatpvce ahrtvpdeqr
      121 yhdmsrrfgp vahdpavcgc hvhvgvpdre lavqvcnhlr qwlpvvqalt ansplhdgrd
      181 tghaswrsmq lerwpsigpt phfdsaadyd atvadlitag imldaamvyw yarpsasypt
      241 vevrvgdvcp tvddtvlvag lvralvatli ddvragvpap rirdclvaaa hwraahdgvd
      301 gelvdlrtgr srpawdlvdd lvvtvtpalt rhgdldlvrr eldrvrrdgt gatrqrqvma
      361 dtggdirvvl ahlaaqtvst
//
LOCUS       WP_457605253            1901 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605253
VERSION     WP_457605253.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1901)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1901)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1901)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1901)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11463197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1901
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1901
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=197179
     Region          7..1408
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1442..1708
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
ORIGIN      
        1 mtgtrapivv vgmacrypda tdpgqlwqtv lgrrrafrpl pperlpvady hrpgrdevdh
       61 tyvdraavls dwvfdrsrfh vpgevfravd lthwlaleva adaladagcp agaglpndrv
      121 gvmlgnsmtg efsranglrl rwpyvqrlla etlagldlsd aerekllata edrfkepfpp
      181 pgeetlagal sntiagricn hfdfhgtgyt vdaacasslm avataarmla dgdldvalag
      241 gvdlsldple lvgfarvgal atgdmriyds rptgflpgeg cgilvlcred faaehglrpy
      301 arlhgwgtss dgnggltrpe pagqllalrr aydragltpe qvsfveghgt gtavgdetel
      361 salrdlhagr rlpavlgsvk anightkaaa gvagmikavl aihhqvippt tgcesphpal
      421 aaagsplvvt deptpwpgpd ryasvsamgf gginahvvlg gispttrrvv tdaerraarp
      481 lpshevvvca aadraalaar ltdladlagr lsraelgdla atlaaepvaa gavrfaavvr
      541 dpdglvhaar ravtaladad telfdpeagv flgagaapri gylfsgqgsp vrpdagalge
      601 lldgplagyd seveiaaggv pdtavaqpai lraslaglaw lrrlgveaea aaghslgeig
      661 alcwagaldd kealdlvrvr grlmsdapgr gamaavagpa drvrellrpg plvvagensa
      721 eqctvsgpaa evarfvagap aaglratalp vshafhsplm apaslalrdh ltglagrapr
      781 rpvcstvtgd wlgtgtgtdl adlltrqlve pvrfrdalar laartdllie vgpgavlagl
      841 aadlpdarvv aldsgapgph giatvtaalf atgagpdvga yyarracrrl tpdwrpvflr
      901 npcegtggpa rtpqpprprp apvtptpapp vvtaddtdll savtrrvaam veldaatlrp
      961 dtrlvadlhl sslrvsqlav daaaavgrsa pavpaalada tidqlaamla tlpaagevda
     1021 ppagiaswvr aftdrfvesa aptarpgarr gwtvlgtedh plskgvaehf pladtpdarl
     1081 lllppgltvp aelvvtalra taadglplvv lhhggvgaav grsiamerpg aavmvaetpv
     1141 ddrclklvae asvdwtgyve avydedgvrt trvaaplals rrderiplas gdvllvtgga
     1201 kgiglecaae vcqatgatav lfgrspgtdp evragldrlt algitagyha vdvsdgqavt
     1261 aavtaaqery gpvrgllhaa ghntprried vtveglratl apkadgfdhl vaalgddlrf
     1321 avafgsvigr tgltgqseya vanewlarrc aeltrerprt rwltvqwsaw sgvgmgvrlg
     1381 vldalvrdgl episvpagtd lllrllaapd tgpcvlaagr lpagptlryr dddrtggrfa
     1441 ervlaltpgv esvlgatlta gtdpylsdhv vdgvpllpav lgleamtqaa taltgapgtp
     1501 vrltgvrler pvtvtdrrdi rvaalvhddg rvetalrsdd tgfavdhfaa vvttgavpap
     1561 dppapavrlg epglpaagly gglyfhgpaf rrvrgyhals ayrcvfsvra epgtawfgmy
     1621 ldaslrlgdp gardavlhgl qgcvpdrrvl pvsveritvw hrpsgvltvt arqraedgae
     1681 fvydvlvtde sgrpveewtg lvlrsvaeig wsempaflag pavarrlrhr hpgidaavlp
     1741 atrgdggptl rladwlagaa lgepagarha gdgrvtapgg ggvsashldd lvlvtvapgp
     1801 vgvdwervdd rpppleerhr alavrlaaes gedeavaavr vwtaievtrk lglgpsaplv
     1861 ftgrepsgtl glrsgdhvls svllrtagda rqvavcvgtp a
//
LOCUS       WP_457605261             453 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605261
VERSION     WP_457605261.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..453
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49301
     Region          102..446
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mlvdnavegd srvqkaarsa adagwdvtli gcahidaerr wrlgdaevrv lplaaspavv
       61 agprggsasg gragprdgfa slggvsglra rlvargglpl raarlarrpv ehaqvrywra
      121 rlrdgawrrl epglwdyerv agpvidelrp elihahdfrm lgvaaravdr artagrdvkl
      181 vwdahewlpg arprsdnarw lpahlgyvre yvghadavvt vsdtladllv rdhalperpt
      241 vilnapvaat temsapglre rcglspgtpl lvysgamavq rgvdtvveal pllpgvhlal
      301 vvadpdaayv rqvvaraarh qvgdrvhvlp yvphrrlvaf latadiglip lhhwpnheia
      361 litkffeyah arlpivvsdv rtmsetvrat gqgevfrard aadlaravrv vladpdryra
      421 ayegpdsplp gwtweaqaar ldalyrrllt ptr
//
LOCUS       WP_457605252             152 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605252
VERSION     WP_457605252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 152)
  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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..152
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16770
     Region          1..145
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msapvyryrh rvtfdetnlv gnvyfahyah wqghcrehfl aeqapsvlaa lsdglalvtv
       61 smsvefyaes hafdtveiem slvelngnri tmgfdyrrvh pdgapaelia rgrqtvavme
      121 rvdgqlqpap vpadlaaala vyrrsaagvw vr
//
LOCUS       WP_457605272             545 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605272
VERSION     WP_457605272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..545
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56227
     Region          25..424
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 msaptmtaea apmskrktle alsglllvlf vamlsstvvs talpkiigal ngsqtqytwv
       61 vtatlltata ttpiwgklad lfnkklliqi aivvflvgsv aagfaqsagq liaarafqgi
      121 gvgglqalvq vaiaamippr ergryngylg gvmalatvgg pllgglivdt swlgwrwcff
      181 vgvpvaaval fllqitlnlp tvrrdnvkid ylgatliaag vsvlliwisf vddsfawlsw
      241 qtgamvggav lllalavwve araaepvvpl hivrerttal ailgslavgm amfggavflg
      301 qyfqigrgys pteaglltip mmagvlissi vagrmitatg kikpyivvga vmlvigfaml
      361 gtidhetslv fvglamfivg vgvgmtmqnl vlavqntval kdigaasasv affrslggti
      421 gvsvlgavla rrvtdrithd laaagiptsg gggstlnlda lpepvrqivr aaygdatghi
      481 flisaaiavv givaalllrp vtlrssldlp dtgrsvavga davdgapafd evsvdsagre
      541 ertrr
//
LOCUS       WP_457605299             279 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605299
VERSION     WP_457605299.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..279
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29610
     Region          9..260
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtadprlarl slnqrttqrw svaqavdgcv ragipaiglw repvaeigvp aavrlaadag
       61 lrvsslcrgg fltaadeagr aaaladnrra ideaaelraa clvlvvgglp pgsrdlagar
      121 qrvadalael apyaaargvr laleplhpmy cadravlstl gqaldlaeaf paeqvgvvvd
      181 tfhvwwdpdv wrqiaragar iasfqvcdfl tplpadvllg rgmmgdghid fpplrravea
      241 agytgdveve ifnaevwatd pdlvlttmia ryaervltd
//
LOCUS       WP_457605305             339 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605305
VERSION     WP_457605305.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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   2  (residues 1 to 339)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..339
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35713
     Region          1..339
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mshvtledva raadvslata sralngrrvt phlhdrvlaa aarlaytpna haralagasr
       61 rsvgvvchdv tdpyfaavag gvmrvaadnd llvmlastfr dpereiayvs mlraerapai
      121 lligsgfedp rweramaael apyldgggrv avvsrhrtlk vdsvlpenra gaaelartll
      181 glghrrfavl sgppelttva drlggfrdel aaagvpldpg avaeaaftrd ggyramtdll
      241 drgldatcvf actdvmavga yaalrdrgls vpgdvsvagf ddipvvrdlt pplttvalpl
      301 hrlgeeamkl altenagrrr rivrlpgevv lrastapva
//
LOCUS       WP_457605303             383 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605303
VERSION     WP_457605303.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..383
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42358
     Region          1..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mertsvgiil ngvtgrmgyr qhlvrsllai rdqggvpard gsriwpeltl vgrdenrlaa
       61 iaarhgltay ttdldaalad dahqiyfdaq vttqrekair aaieagkhvy tekplaegfl
      121 aslelarlaa akgvrngvvq dklflpglrk lkrlvdggff grilsvrgef gywvfegdwq
      181 aaqrpswnyr aedgggitld mfphwhyvle qiiapvtavt avtathiper vdesgtryra
      241 taddaaygif elaggivaqv nsswavrvhr delvefqvdg thgsavaglr dcriqhrgat
      301 pmpvwnpdlp vtepfraqwq tvpdngehdn afkvqweafl rhvvddepfp wdflagargv
      361 qlaeaglrsa regrrvtiee ipr
//
LOCUS       WP_457605308             137 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605308
VERSION     WP_457605308.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 137)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..137
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14706
     Region          5..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18882"
                     /db_xref="CDD:467593"
ORIGIN      
        1 maaydvalvl lvdptgailm qhrdgntsvs pyqwglpggs iepgetpeqa arrelreetg
       61 ltagelhllw sgprphedgf phtvtvyvfr gatdarqedv vlgegqamvf vprdqvldre
      121 lavsaakvlp lhlaeta
//
LOCUS       WP_457605310             296 aa            linear   BCT 27-JAN-2026
DEFINITION  arginase family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605310
VERSION     WP_457605310.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Dowling,D.P., Di Costanzo,L., Gennadios,H.A. and Christianson,D.W.
  TITLE     Evolution of the arginase fold and functional diversity
  JOURNAL   Cell Mol Life Sci 65 (13), 2039-2055 (2008)
   PUBMED   18360740
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Ash,D.E.
  TITLE     Structure and function of arginases
  JOURNAL   J Nutr 134 (10 Suppl), 2760S-2764S (2004)
   PUBMED   15465781
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Cederbaum,S.D., Yu,H., Grody,W.W., Kern,R.M., Yoo,P. and Iyer,R.K.
  TITLE     Arginases I and II: do their functions overlap?
  JOURNAL   Mol Genet Metab 81 Suppl 1, S38-S44 (2004)
   PUBMED   15050972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..296
                     /product="arginase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016813 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear
                     amidines [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29971
     Region          7..290
                     /region_name="Arginase-like_1"
                     /note="Arginase-like amidino hydrolase family; cd09999"
                     /db_xref="CDD:212523"
     Site            order(96,119,121,123,136,225,227,270)
                     /site_type="active"
                     /db_xref="CDD:212523"
ORIGIN      
        1 mghrqwtvvg apssagahtp gierapaalr aaglldllga daedagdvpg frwrpdpayp
       61 rgqnagavaa vasavadrva aalgrgrapl vlggdctvtv glvagcarag lspalvyvdg
      121 gpdlytpetr angnldamgl ahmlglpgtl pevagvgpdv pllspervvv ygdslprgdh
      181 erelvaelgl ayvpadevha dawaaarrar svaegaadrf vvhvdvdvls fvdapladvp
      241 epfglslgea aatlaelvas prfaglsvte inpdhlpdde llprfagvla galtgr
//
LOCUS       WP_457605312             243 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605312
VERSION     WP_457605312.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..243
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25642
     Region          29..134
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mariayhdad aeafaatrhl tddgltawra avtrhltprp gmrlldlgag tgswaraftd
       61 wfpgvevvav epsaamrarc vfaplvagda ghlpladgsv dgawlstvih hvpdlaatar
      121 elrrvlrpgg pvlirsafag rheaitlfdy fpeavrvldt ypsiadvega faaagfataa
      181 veavpqvtaa slreaaaglr reahtplqli tdaeyaagve rlreaartvd gpvvdaldll
      241 vlr
//
LOCUS       WP_457605321             653 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction-modification system subunit M [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605321
VERSION     WP_457605321.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 653)
  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 653)
  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 653)
  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 653)
  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..653
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..653
                     /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=73270
     Region          8..141
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          154..418
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mstkhqelan fiwsvadllr gdykqseygr vilpltvlrr ldcvleptkd avlarhqqlk
       61 dagvqnmdpv lrraaglsfy ntsemsfrkl lgdqdhvaln lrayiggfsp gavdvldkyg
      121 fdaqisrlae agllyqvvak fadidlhpdv vsnhqmgyvf eelirrfsei snetagehft
      181 previrlmvn lllapdeddl vtpgivrkiy dpacgtggml teaqehiqah nphatvevyg
      241 qelngetyai crsdmmlkgg dptkiafgns fnqdgheger fdymlanppf gvewkkvekf
      301 vkdeaargha grfgaglpri ndgsllflqh miskmkrped ggsrlaivfn gsplftgaag
      361 sgeseirrwi lendllegiv alpdqlfynt gistyfwilt nrkdparark vvlldgrdyw
      421 tkmrkslgdk rkvltdehia dltrtyvnal aiaddpehpq hakvkvfktt dfgyqritve
      481 rplrlrfevt eetvallaea kavlkyaere tllataksli gtssatraef amklnglgkl
      541 paavekavwe afsvsdpege vqtdrkgnpl pdpdlrdnen vpldedihdy lkrevlphvp
      601 dawidetrtk igyelpfirh fynyrpprpl aeidveikal eaeiqtllge vie
//
LOCUS       WP_457605334             294 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605334
VERSION     WP_457605334.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32339
     Region          13..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          99..286
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maedigstvp rrqlgrllrq frneagvtld aaaealeysr qkiwriecgl gpvrmldvka
       61 mcelygvsae mteamrglaa etkskgwwha ygdavpswfe lyvglesaaa hlreygdnli
      121 pgllqtraya lglyqpgsrl sveererave vrlqrqsllt rrlpqpprld tvlseavlrr
      181 tvhgpgvmtg qltrllevse lpnvslrvvp faagphpgsv agsfvildfp iskggraaep
      241 svvysesltg alyldkpdel rayenawtgl dalalseaes rdmikrvige trhd
//
LOCUS       WP_457605326             949 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction endonuclease subunit R [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605326
VERSION     WP_457605326.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 949)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 949)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 949)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 949)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..949
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=105682
     Region          20..879
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 maqrqfaqyl akqidergpl dvlrrgvkdk gvlirlayfk pahaitedal klyranrltv
       61 trqlaystsn nntldlvlfv ngiplatael knpltgqtve dakeqyrktr dpkelifarr
      121 tlvhfavdpd lvfvttklag ektrflpfnt gsngpgvsgg agnppatdkg yrssylweqi
      181 wrpdvfmdlv rrflhydket kalifpryhq whavtqltdh aarhgsghny lvmhsagsgk
      241 sntiawlahr lsslhtapdi trdglrpnep vfdkviiitd rvvldrqlqd tvfqfehvpg
      301 vvqridkdsa qlaaalqget akvvittmqk fpyvlnqvqg lkgkrfaviv deahssqsgd
      361 saaalkkvll klgsddvdes gdlltasala rgrhetlsyf aftatpkpkt lelfgtphpv
      421 tgnpqpfhty smrqaidegf ildvlrnylt yksywklana npddpevdpk kagaqlarfa
      481 slhptmqaqk aeiivehfrk htaprlggra kamvvtgsre aavrlhtair kyvemqgyvg
      541 cdslvafsgd levdgvehte aringfsege lpgrfgytaa ddkyagtpka kqhteykilv
      601 vaekyqtgfd qpllttmyvd kllknvaavq tlsrlnrthp lktqgdvfvl dfvneagdia
      661 eqfkpyfeta attptdpnll ytaqntvtgy pvlvdsemqa yaealleaer kattetglqr
      721 ahaalyrfte pavqrfnala addpeaadgf rsalrdytrm yaflsqvvpy hdeelerlyl
      781 ygrallnrlp rrqdpsvdig evqlthlrvs ktgehdasls pegeqmlpgf vgggagsqhd
      841 pekvalsdli dafndrfgig lgeadkvwve qqivalaedg tleaaalvnd esnfgvvcdk
      901 riedvilsrh ddngklmqry lddeslrsql nqfarrqayq mirrrkgia
//
LOCUS       WP_457605338             263 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605338
VERSION     WP_457605338.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..263
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27753
     Region          13..155
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 matgfggeva tyyarhrrgy pppvldalaa afrlgaddtv vdlgcgtgql sipladrvga
       61 vigmdpepdm lviarrtavd rgtanatwvl ggdsdvpals rllgggsvga ltvavaihfm
      121 drdalfqaar plvrpgggia vvtngeplwt qdtewsralr gclermlghp vtgrcqtded
      181 grrrnrealv ragyryeets vrydapltvd dmvggvlsam saerlptlqq raalaadvrd
      241 alggvdvvte rvtvrlqcgi lgs
//
LOCUS       WP_457605350             133 aa            linear   BCT 27-JAN-2026
DEFINITION  YbaB/EbfC family nucleoid-associated protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605350
VERSION     WP_457605350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Cordeiro,T.F.V.B., Gontijo,M.T.P., Jorge,G.P. and Brocchi,M.
  TITLE     EbfC/YbaB: A Widely Distributed Nucleoid-Associated Protein in
            Prokaryotes
  JOURNAL   Microorganisms 10 (10) (2022)
   PUBMED   36296221
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..133
                     /product="YbaB/EbfC family nucleoid-associated protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14201
     Region          27..106
                     /region_name="YbaB_DNA_bd"
                     /note="YbaB/EbfC DNA-binding family; pfam02575"
                     /db_xref="CDD:460599"
ORIGIN      
        1 mwadeaalda aarrldewes sltdraarar dlsartqalt gtarsadglv evivdasgll
       61 tglrldervr qhsaahtarq ilavtrdara dllrqlteat tetlgaddpa araiveshqr
      121 rlgpdpdapd aar
//
LOCUS       WP_457605364             269 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605364
VERSION     WP_457605364.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28433
     Region          65..265
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtaivtparr aslagdgltl tgralahwrr epgplagslg fdilmvlmfa ylfggalqvp
       61 gggsyreflm pgmfamtmvf gismttmavs adlergvtdr lrsmpvsrla pllgravadl
      121 mfavvtlavm llvglavgwr argdlgdtla alglilllrf alvwvgvflg ltvkgqsavt
      181 avqtlefplg flssafvaps tmpawlgava ewnplsatvg atrelfgnpg wggdswvaah
      241 hpllavlwpl vlvavflpls lrryralsr
//
LOCUS       WP_457605375             275 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605375
VERSION     WP_457605375.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29727
     Region          4..274
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mavrlasvhl ypvkslggvd vdraevepwg lrhdrrwlvl rpdgrklgss vlpallglta
       61 vpgsgsvtli ardgssltva epvdgppvpt dvsrldtvrl aadeahdwls arlgrpvrla
      121 wlddphrrpm saehgggpgd plnlsdagpl lvattpslrr lrdwivegal ergepapepl
      181 amarfrptvv ldgpvepfae dgwtrvriga vdfrvsdrcd rcsvtlidpd tlargkepir
      241 tlarhrrddg ktwfgvrlvp lttgevrvgd pvvvs
//
LOCUS       WP_457605380             340 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605380
VERSION     WP_457605380.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..340
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36320
     Region          21..339
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtertdrmps qrrdsatdat vlsvddltvt vgtrrgpvra vagvswqvrs getfalvges
       61 gsgksmtlla atglapraat vtgrvrlldt eltalpderr rkvrgrhvgf vfqdpmtsln
      121 pvlpvgrqvt eaaeehlglt rraardrave llemvgipsa arrvdayphq fsggmrqrva
      181 iamalacepd lliadeptta ldvttqaqii elvadlqarl gtavvwvthd lgvvagiadt
      241 vavmyggriv eqgpvdavfd tpthpytral laarpdpsrr gedlvaipgs ppspldlpag
      301 cafwprcpvr adprcehelp pltpvgnght vrtfyrgeag
//
LOCUS       WP_457605383             345 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605383
VERSION     WP_457605383.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..345
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36775
     Region          3..327
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 msadtpdvva elddlkvhfp tpagtvravd gvslavrrge tlglvgesgs gkstaglall
       61 rlvdptagrv rvagedvtrw srrrlratrr hvamvfqdsq asldprrtvg dsiaeplivh
      121 rlagsaaarr arvaelldlv glradtagry phelsggqrq rvgvaralag epdlivldep
      181 iasldlsvqa qimnllrhlq rdlgltylfi ahdlaavehm sdriavmylg rivetgpper
      241 iyrhpahpyt aallsavpva dprvererrr ivltgdipsp vdppsgcrfr trcpqarpac
      301 aetdpalaev gpghhaaclf pldgerdggp geegattrad aagta
//
LOCUS       WP_457605402             335 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605402
VERSION     WP_457605402.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..335
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35988
     Region          5..332
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdqvleirg lcvdygvgad avravrdvdl tlhrgevlgl agesgsgkst laygltrllp
       61 ppgvvsggqv iyhpadgppv dvltlspakl refrwaetsi vfqgatnsln pvhrvstqll
      121 dvirahepks taasrsarak dllrlvgisa drldsyphql sggmrqrvmi amalalepqv
      181 vimdepttal dvvmqrqilg qlaelrerlg favlfithdl sllvefsdri aimyggrive
      241 eapaarlyae plhpytegll hsfpalhgpr reltgipgsp pdlrampsgc afhprcpkaf
      301 dgcdeqvpvl gaprvddpar avacrlhpav aplsr
//
LOCUS       WP_457605405             348 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605405
VERSION     WP_457605405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..348
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36935
     Region          35..294
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtlspssieq vipgqgamaq psararrrrf rfvanakaat glsvlgvyvl lavigpwiap
       61 ydpdarsadv lqapsarhwf gtthlgqdif sqilvgarsv mvvgliagvl atilsiligv
      121 tsgylggaad eglsavsnvf lvipalplii ivtslvdqag dmlvaliigl tswawgarvl
      181 raqtlslrrr dyveaaratg ertwriigfe ilpnltaiia sgfvgtvifa vmseitlafi
      241 gissmtswnw gtilfwaqgq qalaqgawww fvpaglaial lgtalalinf gidefvsprl
      301 rtggrtrirt adgrvvamrv gftpvlapnp apvpmqrpad ptredats
//
LOCUS       WP_457605411             558 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605411
VERSION     WP_457605411.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 558)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 558)
  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 558)
  AUTHORS   ter Beek,J., 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 558)
  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   6  (residues 1 to 558)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 558)
  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 10170725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..558
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60667
     Region          38..536
                     /region_name="PBP2_TmCBP_oligosaccharides_like"
                     /note="The substrate binding domain of a cellulose-binding
                     protein from Thermotoga maritima contains the type 2
                     periplasmic binding fold; cd08509"
                     /db_xref="CDD:173874"
     Site            order(43,254,436,518)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:173874"
ORIGIN      
        1 mrrrqllalt lagamvtgaa acgdspnank ksgqaatvln vgmpngpqae nnnpflttsa
       61 aaslgyrwqi yeplmmwnpv kpaepfkpwl atkaewssdy rtvkvtvren atwsdgqkvt
      121 aedvaftynl vkkfpalndq gvpytdavas gnevtismas pqfvnqqkvl wrvpivpkhl
      181 wekiadpatd pvkqpvgsgp ytlksftpat ttlsvrdsgy wqdppkvkel rytsytdnsa
      241 qttalanges ewsfvfipny qtvfvakdqk nhkmwappvl gihglyvntt kkpfddpalr
      301 kamnmvidra difttaeagy fhpevksitg lpspagdsfi apeykgqehk vdvegakall
      361 tgagykldgt tlkdksgkpv tirltdpagw sdyqtsleiv kgnlakigia atidkanqda
      421 wfrnveqgnf eatfrwtesg atpydiyrti mdgrvlkpig taspagnfgr fqskeatdal
      481 vsyanatdda trttamatlq kifveqvpmi pvgadnigga ystknwtgwp ddanpygalq
      541 ptqpnavdvv lhlkpaag
//
LOCUS       WP_457605423             523 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605423
VERSION     WP_457605423.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..523
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53482
     Region          4..519
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mtnpstlyrg gvlhcpadps atallvrdgr iawlgtdaea pradrvvelg galvtpafvd
       61 ahvhatdtgl alsgldlsav rsagelleav safaaglpgd avvlghgwde sgwadpvlpd
      121 aaaldraagg rrvylsqasi hsalvsaall aacpevgsaa gyeasgwlrr dahhvvrsaa
      181 fasvsraqrv aaqrraleha aslgvaavhe cggpdisdee dftgllaisg agvpevygyw
      241 gellgaakar elgavgaggd lfadgalgsr tahvsaayld geagacghgy vsaeqvrdhl
      301 ldcaahglqg gfhaigdaai gtvlegfgla arslgvdrlr aarhrvehae imskaliagf
      361 veygivasmq pafdrlwgga grmyesrlgl arslesnpmg amhgvgvala fgsdspvtsi
      421 dpwgsvraaa ahhnpaqrms vraafaahtr ggwravhldn egvlalgapa tfavwdspag
      481 verglpvvla edpelrgadd ptplpvcrat vlrgdviyqe gss
//
LOCUS       WP_457605434             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605434
VERSION     WP_457605434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  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 260)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27630
     Region          55..229
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mraltdgwlm agrnmrhvvr apeeiiiyfs lpimfvlvfg yvfgsgmsvp gagsyrefll
       61 pgvfvmtmly glgatasaia vdtgrgvvdr frslpmarsa llsgragadl vraclemttl
      121 vvcgllvgwq wregtgpala avalilllrv amtwvgilfg llvpnpdtva vvvfplafpl
      181 talsnvfvap elmpdwlgai aawnplsatv aaardlfgnp glsgdswpar halelaiawp
      241 laliavaapa avrryrrlgr
//
LOCUS       WP_457605440            1036 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605440
VERSION     WP_457605440.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1036
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=107722
     Region          123..1028
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          835..863
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(836,839..840,843..844,846,876,879..880,883..884,
                     886..887,918,921..922,925..926,929)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          874..904
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          917..944
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfgvlgatq ayaadgsvlp vaggrlrall vlllldagrt vapqrlvdgv ygdrppeqaa
       61 nalqsqvsrl rrllpgapie fgpagyrlav dpqrvdvhrf tglaaagraa laagdpagaa
      121 allrdalglw rgepladvtd apfagaeaar lrqarlaave drveaelalt pagapliael
      181 rdlvaahplr erlygqlmra lhgagrraea lavyadarrv laeelgtdps aelaalhtal
      241 lrdepapavr lpspltsfvg repelrrvhg llgaarlvtl hgpggagktr latavasghd
      301 gpvclvelav vatgapvapa vlaaldlrda alripggpad ltgrlvaala drrlllvldn
      361 cehviddaar ltgrllaaap glrvlatsre plgltgealc pvgglpapdg paapeaaaay
      421 pavrlftdra advspgftld aattpavlri crtldglpla lelaaarlra lpvtqvaarl
      481 ddrfrllrrg drtaaprhrt leavvgwswd lldeperrla armsvfagaa dlaavqavca
      541 pdagdvldvl tglvdkslve atggryrmle tirefaaarl aehggtgrvr dahaayfldl
      601 aqagdaalrg ggqerwlrrl daarddlhaa lrhadtatgl rlvaalafyw wlrglrgega
      661 alarrlvdrl dgppdsvaee yalavliatl agggdrsevd aasrilwtla rpprhpflly
      721 lsgmasgpps pedaaalheq avrdrllgtd pwsralgllg tamvsllhdr haqahadlng
      781 alagfraldd rwgmivtlst haeaayrtgd vtsaaapmae alelaeqlgs tldlaellrt
      841 radgrlaagd ltgaaedfrr vrriagpaga pelvaaaylg lgeiarrdgd prrartlcer
      901 avaecpsgwf gadvvrlaal vtlgqladat gdpaaarahy rqvltagvgv wdvpvvaaaa
      961 dglagpllrd gdpesaarll gaasallagt gaadapagtp taaelrkhlg eaafatayar
     1021 gadlprqral alvdgr
//
LOCUS       WP_457605455             435 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605455
VERSION     WP_457605455.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..435
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47070
     Region          16..405
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 matprvavvg agaaglatlk aladagvpav afeaadtlgg lwvygapgsp ayrtlhlnts
       61 kgrtefadhp mpadwpdypd htrvagylgd yadrfglrea vrlrhtverv trtadgwrvr
      121 atgpdgpvav dveavvvang hnrvpkrpep ypgectaeqm hshdyrgpeq lagrrvlvvg
      181 ggnsamdiav dasyaaertl lslrrgvwvv pkyllgrpsd tlngalarrl pwrlrqrisq
      241 tmittavgpp tryglpapah gflqdhptls dallsrlthg diqarpgiar fdgdrveftd
      301 grhddvdlvv wctgyrvemp fldpallgdg adrlplyrhv fhldapglaf vglmqstgaa
      361 fplveaqarl vaarlagtwt ppdparqaaa creelraata rwgqrrphmr vdfdvylael
      421 grelaagrrr agaar
//
LOCUS       WP_457605458             280 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605458
VERSION     WP_457605458.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..280
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28669
     Region          10..251
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msapgrsggl agrrvlvtga rgtfgqhlga altaagahvv gldlhadpda tppvlgvdlt
       61 dpaatppava avverlggld llinnagvgg papaelppde vvrrqievnl laawrttaaa
      121 mpaleasrgr vifvasrmav lplplaaayg vskralvaya dalrhevgth vgvsvvypsm
      181 vaspihdstv aaglslsgvs rpepvegvvs ailraatarr aprdlattrr grielalarh
      241 apaladrmvr rtvatrlaag dldgaalaeg mvrrhrqdrr
//
LOCUS       WP_457605461             169 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605461
VERSION     WP_457605461.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 169)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..169
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18037
     Region          5..144
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mavspyitrl rrhvghdllm lygvsgvvtd dagrvllarr gdngrwsvpa gtvdpgeqpa
       61 dalvrevhee tgvnvaidrl agvathpvvy pngdaceyln iwfrcravgg aptadgdesl
      121 avawfapdal pdlddwarlr igtaltddap pwyaapgesh palhqpdnl
//
LOCUS       WP_457605464             725 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 95 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605464
VERSION     WP_457605464.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Wu,H., Owen,C.D. and Juge,N.
  TITLE     Structure and function of microbial alpha-l-fucosidases: a mini
            review
  JOURNAL   Essays Biochem 67 (3), 399-414 (2023)
   PUBMED   36805644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..725
                     /product="glycoside hydrolase family 95 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=78059
     Region          6..228
                     /region_name="Glyco_hyd_65N_2"
                     /note="Glycosyl hydrolase family 65, N-terminal domain;
                     pfam14498"
                     /db_xref="CDD:405224"
ORIGIN      
        1 mtahrihdta pagdwtdafl tgngelglmv hgrphaeriv vnhhrlvlpn gtrdarapel
       61 agrmphiral vlagrraeaa rlltggrele wtqsfhpgya ltvdaapgpv rdyrrgtdft
      121 tgevtvewsg grrrcfasra dgvavlhldq gdcvvgatge lpgkpadvly ehaayrrdgl
      181 vflrvraryp daggawgfeg ltllrgdvtv dgdrvrvrgp allttlvdrp dappwrtras
      241 errlaalagd ygtllarhvp rhrgpytrvg ldlgvaaadr alpvgellar qaaapdrldp
      301 vllerlfhsg ryllfsaagv lpprltglwl gswdaawagd fttdanlnlq laganvgalp
      361 evttaharlv aaqvdhwran aravygargl lapsrtdgeh ghlfhvhpdw pftawlagad
      421 wllhplhehh lvtgeplgev agwlaevadf fadvltavdg rpalvpsysp etgpydgtgr
      481 tapvainatm dvaaarhalr laaevtgedr wagvrppdyl vdgrgalaew awpgstgded
      541 hrhvshlypv wplhdidpdd tpelaaaahr altlrgdenm sahgslhral aatrlrdgdl
      601 vaanlrkilg admffrslms ahnpgrttyn adaahalpav lieslvqsrp gtlrllptpl
      661 pglpsgtlrg vtcrgrivve eltwapgrvr arlaspvaqr vvvhapgghr avdlapdrpy
      721 evafg
//
LOCUS       WP_457605467             339 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605467
VERSION     WP_457605467.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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   2  (residues 1 to 339)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..339
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35302
     Region          10..339
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msgrtpgeqv tiadvarhag vaastvsyvl sgkrtisatt rgrvlasvra lgyhphagar
       61 alasrkanvi alvlplrtgm qvpvvmrfat avvttarrhd hdvllvtade gpaglhriag
      121 salvdgvllm dveledsrvp llrelalpgv lighpadstg lacvdldfrr agelcvehla
      181 aaghrriall gapaavydrg tgfahrtrsg vraaaerlgv davtrpceeg paavrrdlea
      241 lladhpdvtg lvvqnesavg pvlatlpllg rrvpcdvsvv aicpdelaeq sgltcvpvpa
      301 eevgkqaval lmrrlsgegv pevtllephl tvrdtsaar
//
LOCUS       WP_457605468             258 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Nitratifractor sp.].
ACCESSION   WP_457605468
VERSION     WP_457605468.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..258
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27367
     Region          1..258
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msdilkigky eftsrlivgs gkypdfqttr datlasgsem itvavrrvni tspdeenlmd
       61 yfkdtdvkfl pnsagcttae eaitlfrltr eatgidlikl evigdtaktl ypdvietika
      121 cevlakegft imaytnddpi vakrledaga havmplaapi gsglgiqnrf nvvfikeavs
      181 vpvivdagig casdaaaame lgadgvltnt aiaqaenpil maeamkhavi agrmsykagr
      241 ipkrpfatas spvdgmif
//
LOCUS       WP_457605480             197 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605480
VERSION     WP_457605480.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21400
     Region          <28..62
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          73..185
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mtpqptrrne qsrrailaaa lelltetgyp altveaiaar agvgkqtiyr wwrgkgavil
       61 daladdmpev ialpdtgdlr adlrqvlrat vaefadprls attraitiet lvdedlggqa
      121 rdrllrpqln avrdrleaar eagqvrpdaa ldqvvellfg plyhrwllrn gpltddyadg
      181 ivdlvvaavt pstrtsg
//
LOCUS       WP_457605511             267 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605511
VERSION     WP_457605511.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..267
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28128
     Region          177..261
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mdggliavav raehdravla gllgrdpvlh ayqlgdlddf fwpytswfrr gdqvvllyhg
       61 velptllafa apdrvpdlag llaeaapvlp armwahlspg leaavgrwfv vseaaahhrm
      121 altdpgrlaa vpavgaplgp adaaelagly avaypgnwfd prmldtgqyv gvrehgrlva
      181 vagvhvfspr wrvaalgnvt thpdvrgrgl gagvvaalca rlrtsvdhvt lnvradnaaa
      241 vrlyerlgfs rvagftecal tsaaaag
//
LOCUS       WP_457605541             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Nitratifractor sp.].
ACCESSION   WP_457605541
VERSION     WP_457605541.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..360
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39934
     Region          1..305
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          165..358
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mnrvfwaila kelliflhsv glvavvlysf tadiyiagsg iqlkprnvsv gyvdetgggl
       61 slkilsrlha pefkpprrfp sqealsraif nrevmvgllf dnrfakdyrr gaparldvll
      121 dataasqaft tlsylqnill dvarlhlpve iashklfnpn anthyfmsls emlsvitlli
      181 viltatvfvk ekeegtwdlm llmpvdarli ilakslsqvl vvmggilial gfvvlgtfdt
      241 plngsfwgfi llslfysfss agiglfiaav srnimqvaql sivimmpmif lsgawtpiya
      301 mhpffqwlsl lsplryyieg seslffrgts lidllpdfgg vfllgillyg ygfrkigrlf
//
LOCUS       WP_457605542             397 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605542
VERSION     WP_457605542.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38744
     Region          9..327
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtetvsraap pasrhavtvg agatlttivc vlpvflvggl avqladelrf spaglglavs
       61 iyfgvsalas vpsgalverf gsapvaraai llsaasllav aglarsypil vallalsaaa
      121 nalgqlasna alaehvpahr qglsfgvkqa avpaatllag lavptvalta gwrwafvaaa
      181 vaalavlpav pragrdrrar aasgrrpggt gplvviglaa tlaaaaanal gtflvdsaaa
      241 rglspglagl tltlgsvvcv larvgvgwla drrtsghvgl iagmlltgsv glillavags
      301 aplvagvvlg fglgwawpgl mnfavvrlhp qapaaatsit qtgvyaggcl gplglgalag
      361 aagypamwlt aaaamllaaf lmllgarllr rgespsg
//
LOCUS       WP_457605564             681 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605564
VERSION     WP_457605564.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..681
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73343
     Region          10..681
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpatdldatp gldaeltaer ahldasraal krmreraeal fatgdkvagd sytaeqlgrh
       61 marrvkelad dpttplffgr ldfggddpdh agrdyhvgrr hvtdelgepl vldwrapvsr
      121 sfyrasardp qgvavrrrfg fsagtltsfe dehldrgeel gtasriltae ierprvgpmr
      181 divatiqpeq delvradlad sicvqgapgt gktavglhra ayllylhrer lrrsgvlivg
      241 pnraflsyia avlpalgeve veqatvedlv arvpvravdd paaaalkhdv rmaevlrrav
      301 eahigtptep imvsdgsyrw rigldplhrl vtetrqeglp yatgrervra rvvgllqrqa
      361 earraespsd awlrrmsrik pvtdlldtvw paltpdgllh rlrtdadala aaadglltpe
      421 eqelfrsgki grtakatrwt aadavlidev agllerpagf ghvvvdeaqd lspmqcraia
      481 rrsehgsitl lgdlaqgtap waatdwresl ahlgkpdaav vplsvgfrvp aavvafanrl
      541 lpalavdvpp arslrndgal dvrtaedlta atvaevraal ahdgsvgvia addavdrlra
      601 aladagveta taddveaaar vtvvpatlvk gleydhvvvv epaaivaaep rglhrlyvvl
      661 travsrlavl hreplpaplt a
//
LOCUS       WP_457605571             446 aa            linear   BCT 27-JAN-2026
DEFINITION  C39 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605571
VERSION     WP_457605571.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Kanonenberg,K., Schwarz,C.K. and Schmitt,L.
  TITLE     Type I secretion systems - a story of appendices
  JOURNAL   Res Microbiol 164 (6), 596-604 (2013)
   PUBMED   23541474
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Lecher,J., Stoldt,M., Schwarz,C.K., Smits,S.H., Schmitt,L. and
            Willbold,D.
  TITLE     1H, 15N and 13C resonance assignment of the N-terminal C39
            peptidase-like domain of the ABC transporter Haemolysin B (HlyB)
  JOURNAL   Biomol NMR Assign 5 (2), 199-201 (2011)
   PUBMED   21347827
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Schwarz,C.K., Tschapek,B., Jumpertz,T., Jenewein,S., Lecher,J.,
            Willbold,D., Panjikar,S., Holland,I.B., Smits,S.H. and Schmitt,L.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            an oligomeric species of a refolded C39 peptidase-like domain of
            the Escherichia coli ABC transporter haemolysin B
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 5), 630-633
            (2011)
   PUBMED   21543878
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10609171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..446
                     /product="C39 family peptidase"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48773
     Region          237..386
                     /region_name="Peptidase_C39_2"
                     /note="Peptidase_C39 like family; pfam13529"
                     /db_xref="CDD:379241"
     Site            order(260,368,385)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:239109"
ORIGIN      
        1 mfgrpmraaa lagltaltll gtsapvqaqa prpgvthdeq itfqefsrfp dwrtgthqgt
       61 ravpgrhpal tiarpagtte ftdehtgttr tweyatwtsp errigfdate mvaswnaatp
      121 agtwiqvelh gtyntgaqtp wyvmgrwasg dqdikrstld gqgdpwssiw tdtfsvddad
      181 agvllrsyql rltlyrapgq aaapqvrmlg amasnvpdrf tvtpsrggia wgtelavpry
      241 sqnvhigeyp eydgggeawc sptstemvve ywgrkpsaed tswvdpsypd ptvdhaarmt
      301 ydyeyegagn wpfntayaas fpglearvtr lhsldeaerf ikagipvvts qsflaseldg
      361 anygtsghlf vivgftadgd vivndpasss ndavrnvykr eqfeqiwlrt kryrangtva
      421 sgsggiayli kpadrpwpvv pgstnw
//
LOCUS       WP_457605585             280 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605585
VERSION     WP_457605585.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..280
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28682
     Region          9..252
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtssergaav vtgaagglgr aiaaalhadg wnvlltdvda aavsaaaapl ggwsrpldvr
       61 desacadvaa eaaaapgglg lwvnnagvlv tgpswahdap arralvevna lgamngtlaa
      121 vavmreqgrg hvlnvvslag liaapgetvy aaskhallaf slgtlsdlrm agvrgvhvsc
      181 lcpdgiwtpm lhdklddpga lasftgallt pervaaravr larrprpvvs lprwrgaqvr
      241 lldafprlal altpviratg ragqrrqahr vrenpspprl
//
LOCUS       WP_457605593             530 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605593
VERSION     WP_457605593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..530
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54579
     Region          33..528
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mstltgtrhl vrlilrrdrl llplwvlvla vlpityaasf felfptaaer aaylegtarn
       61 psivallgpa ygdsvgalta qrsgfllliv alaslltvir htrteeeagr rellggsvlg
      121 rhagltaall vtygadlvlg lltaaglvst glpvggslay glvtvltgav fatlgglaaq
      181 ltetaggarg vglaglgaaf glrlagdtag ndwpswlspl gwaarvrpye gerwwvlllp
      241 laatvllaal aypisvrrdl gagvlpprlg pagaggalsg pfglawrlhr gqilwwsvgf
      301 gllglilgga aeaagrsveg sprmeeivar lggasgmada ylgvtlslag laaagygiqa
      361 alrmraeeaa ghaepvlatg trrstwllsh vafallgpvv vlgvtglatg ltyglstgdv
      421 prqlgrmlaa glaqvpaawv laglavllyg llprlasaaw vvlavcvllg qlgavleldq
      481 wlldvspfth tpqvlrdtwt atplyvltal avtlatagll tfrrrdipiv
//
LOCUS       WP_457605598             517 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605598
VERSION     WP_457605598.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..517
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51834
     Region          40..513
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 madaarstpr lgalditrkl aaicgdpfar fagpadevag rtarwvavpg gphaaaevlr
       61 laaaydltvv prgagtkidw gaapaqvdim ldtgrlagvw heprdaavae igagtplrav
      121 qatlartnrr lpvdapspga tlggvlaade sgplrhrhgs pcaqlvgvry ldadgelvsv
      181 gesgtealgr aapgggggrp ggrgpagdgd ggagsgpaca vggpgwgagg pvggaggdpg
      241 rgggdaipgr ggtagldvar llcgsqgglg vlvsatmrvh avpagrlwvs rpvwtplevh
      301 dlvravlaad vdpaaveldl pvpvplprrr ipathpsvvn rpdhpavtgr paagslvvll
      361 eggpadvter aerltavlgs eamvghhape wwgrypfapg dtalrievpi gdlhaavyal
      421 rdatggpvpv rgsagsgtvh aalsgalppe rvasiltavr svliarrgrc vvvaapaavr
      481 ravdlwgelp alprlrsaka hldphhrlap grlpggl
//
LOCUS       WP_457605606             481 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Nitratifractor sp.].
ACCESSION   WP_457605606
VERSION     WP_457605606.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..481
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51869
     Region          13..409
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mkfgvehssi llsvakwlll ssvigviigs ivtlflnila wgegasatlp fhyyyllplg
       61 lvlsvwltkt fapeakghgt ekvieavhkr sgkidvavip vkllttvitl vtggsagkeg
      121 pgaqigagta saiadllrfs pkdrkklvic gisagfatvf gtpiagaifg ievlivgavm
      181 yevllpsfva gfsafftaqy fgvkytyydi syfqhyfidl vliakvvlgg vffglvayli
      241 iatlrqteka vervpmnpyl kafgagllli avstflgdry fglgldtisq tmsigsdvas
      301 ntpwyaflak ifytaitlgs ggsggivtpi fyigatsghw fgglfgehhq lalfaalgfv
      361 svlagatnap iaatvmamel fgmdvahyaa vsivisflvs ghrsvfpsqk ivmsksdllq
      421 veygediehs rvdlderpqr qirniyrnvq lkrarhqkrr ekkssaekli eevneqeske
      481 s
//
LOCUS       WP_457605604             448 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605604
VERSION     WP_457605604.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 448)
  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 448)
  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 448)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11620702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..448
                     /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=48394
     Region          19..115
                     /region_name="HATPase"
                     /note="Histidine kinase-like ATPase domain; cl00075"
                     /db_xref="CDD:469604"
     Site            order(46,50,53,75,77,79,81,90..93,105,107,112,114)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340391"
     Region          127..446
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtepllhlal rveqdiflvr qrgrevaaav glehqdqvri atalsevare llhgadgadv
       61 tfaldrdavg rpilqvdlsp lrplpggrye pqsgavarlv dtlrvvaveg dtvvrmsrrv
      121 pdhaeeltad raaelraela erapgsalde laaqnaqlia aldevrsqrd elavlnselq
      181 etnrgvmaly nqlteeleet nrgvvalyae ldeksaqlra asesksrfla nvshelrapv
      241 taiiglarll adsasdpltg eqarqvglir ssagdllglv nelldlakae sgriepdwse
      301 vdlravfgql rgtlralasr pevelvveep papatvrsde vllaqvlrnl lhnglkfter
      361 gevrlraerr gdqwtlsvtd tgvgippelh erifeefyqv pgttrvggtg lglpyarrlv
      421 tllggtlelt seagrgstft vvlpvgga
//
LOCUS       WP_457605610             207 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605610
VERSION     WP_457605610.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..207
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23318
     Region          26..190
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtdikgtaal tpgstdsdal reaeaarlka lhdrefaefa essyyrveri lratcrdrqa
       61 vddalqeayl hgrvewpklr ehvkpagwii starfkmlkd hdrrqreaav apedlppssh
      121 sdiadvweaq etlrgwlhql parhaevfqm sregfsnqei asilgltens vrsyktaakk
      181 rlgelaeeag ftraerdrrq gagrgpr
//
LOCUS       WP_457605613             399 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605613
VERSION     WP_457605613.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Green,K.D., Biswas,T., Chang,C., Wu,R., Chen,W., Janes,B.K.,
            Chalupska,D., Gornicki,P., Hanna,P.C., Tsodikov,O.V., Joachimiak,A.
            and Garneau-Tsodikova,S.
  TITLE     Biochemical and structural analysis of an Eis family aminoglycoside
            acetyltransferase from bacillus anthracis
  JOURNAL   Biochemistry 54 (20), 3197-3206 (2015)
   PUBMED   25928210
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Lella,R.K. and Sharma,C.
  TITLE     Eis (enhanced intracellular survival) protein of Mycobacterium
            tuberculosis disturbs the cross regulation of T-cells
  JOURNAL   J Biol Chem 282 (26), 18671-18675 (2007)
   PUBMED   17449476
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..399
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43744
     Region          1..399
                     /region_name="Eis"
                     /note="Predicted acetyltransferase [General function
                     prediction only]; COG4552"
                     /db_xref="CDD:443616"
ORIGIN      
        1 mhirrlaade rlttsfplqa yafeaspiga trtdqfrayl pynagnttlv aeedgvtaaa
       61 vsaipmrqnl rgavlpmagv agvathplar rrghvrtlmq qlldgvrdeg hqltalhpfr
      121 asfyerfgyi glprrrtaif npadlapllr aelpdelvwe rigagyprwr ayterclrer
      181 hgfavfpdfr avglrdrddr wlisvvrgge tvgavtyrid dhagtlfadd mlvddayara
      241 svlqffarhv dqvarisvqv tpdelpelwl tdldvqvear varpdptapm arllsldala
      301 dqpvgvgrvl ievvgdrwla grhlldgttg klavlpaqta aegsvptarl taaglsalay
      361 gvldpaevvl rglgevpvds agelrrlfpr elphlfadf
//
LOCUS       WP_457605619             388 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605619
VERSION     WP_457605619.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  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 388)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..388
                     /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=40382
     Region          130..373
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msswhrhglk akaalvpava lvallglvvq sdgidttael lallvvlass aalylrrryp
       61 vavgvaalaa vaaygallhr pgpimlvfvv alytvvdegh lavavglgla svvsfavads
      121 ytrtgvngng atllhagwlv avivgvtrnr raylaevqar vlaaeqrkee earhrateer
      181 lriarelhdl lghhlslisv qasaalhrpd persaealav ikqtsretlr elraalgvlr
      241 qegtspsrpa pgldrldelv taagrcgltv rtevtetgpl ppevdlsayr ivqealtnvs
      301 rhagattavv rvvpdgdevl vevaddgagp agppgngllg mgeraralgg tlttgpgpdg
      361 gflvrarlpl rpaplpvpap rtaqgett
//
LOCUS       WP_457605631             188 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605631
VERSION     WP_457605631.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 188)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21258
     Region          49..177
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mteeltdrst rwtihgervv dgsrrsrlsi advelpdgir feqyvirapr samvavldgq
       61 erlllmrrhr fvfdrwvwel pggyvdeged pakcavreve eetgwrpeav epllsfqpwv
      121 atadaenllf fareaehiga pvdvneterv awipleearr lvsegeivga gtviavlelv
      181 arrargel
//
LOCUS       WP_457605638             304 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605638
VERSION     WP_457605638.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..304
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30925
     Region          7..302
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(45..47,50,135,139,161..166,185..186,188,213..214,
                     250..252)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mgtrtfrtav vrnpggpdai eiidvperep gpgevrvtva aaavnpvdlg vaggffhslg
       61 lidqphhtgl gwdfagtvda vgpgvdltag tpvaglvvgf drdhgtyaeq lvvpatglav
      121 vpddldlvaa atvplnglaa aqvvdllgep padgrllvtg aagavggyvl alasargwrv
      181 tglaragdek fvrslgagft taaepgwdav adtaawqera ltlvrdggvf vgvrpnaqpa
      241 aergvtvrvi etradgvrla dllartaage lparvhavlp ldraadvhra maeggvrgry
      301 vlrp
//
LOCUS       WP_457605641             330 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605641
VERSION     WP_457605641.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  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..330
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..330
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34963
     Region          <246..317
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mdpaladlpt drvvalpgad adavamtiah ghaelaavvh rpvsactmpa dfvhavldrl
       61 ervavellpa wlpeathdvr pdtsglaavr aaaaarsrrd rypgaflsdl avfavtgrrs
      121 gattlplraq aaalarlvad afgrrkvvll aepvhgdgav taagaawlvq hggpavwlag
      181 agavgldglp afrvappaap vgqapvagrp hpgsdaekrl eaalaaqswa agrrwnqsyq
      241 shrlaapvrl dllwpdercv veidgpehcr pvrfeadrqr dvqlqldgya vlrftnarvi
      301 hdvgtvvtqi gtylrarrrd laeglhhgrr
//
LOCUS       WP_457605645             301 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605645
VERSION     WP_457605645.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..301
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31641
     Region          8..216
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtgdrlaiea sgltkrygdv tavrdltftv rpgavtgflg pngagktttm rmltglvtpt
       61 sgtatiggqp ygrlaqpsrt vgavfdgnaf hpghtardhl gvyaamagcp drrvaelldl
      121 lglaqaadrr trefstgmrq rlslatallg dprvllldep sngldpegms wlrgllrrla
      181 degrtllvss hvlhevqqvv ddvvvirrge lvaagpwsal tgpptvlvts pdatdlaaal
      241 tagagsvepa gpgrlrvrgl daprvadlaa dhrlrihelv tettsleqlf ldlttdpaea
      301 r
//
LOCUS       WP_457605648             153 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605648
VERSION     WP_457605648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..153
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16603
     Region          20..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdnpepdlvp trlaglpswl itqtavragr lvsdglaavd argyhfrlla tldefgpasq
       61 aalgrrsgih vsdvvaalne laerefvtrs pdpadrrrnv vtittagrrq lrrlekrlaa
      121 vqdellapls pderadltrl larvvahhar ppa
//
LOCUS       WP_457605650             363 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605650
VERSION     WP_457605650.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40923
     Region          2..107
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          69..>188
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 miepfrihvp qadlddladr lartrwpdel pdagwdygip ltrvrelaeh wrtaydwraa
       61 eaelnrypqf tttidgqtih flhvrsadpd alplilthgw pgsvvefldv lgplseqfhl
      121 vvpsipgfgf sgptrergwd vdrvarawae lmrrlgyrry gaqggdwgsv istrlggidp
      181 ehvvgvhlny lptppppgwt geaalsgedr drlarimrlk tqrhphqvly asrpqtvsya
      241 lndspvgqla wiaekftewt dprstvsvdr iltdvsvywf trtaassarl vresafggpp
      301 apcppplgva vfahditrsv rpiaeltyti rhwsefdrgg hfaalevpel fvddvrsffw
      361 nlr
//
LOCUS       WP_457605654             791 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605654
VERSION     WP_457605654.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 791)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..791
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85945
     Region          5..759
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mpqgddgwri rrtsadldrl getesvfala ngwvgwrgtl degepcgmpg sylngfheqh
       61 eltypesgyg fpersdtvis apnaalirlw vddepldlgt gtvrrhhqel dlragvvrre
      121 tewvspggrg vrirstrlvs ltrrpvaavd wsvepldepv rlrvgadlla nqrvperadd
      181 praasvihdp ltgeirrddg ldgvlvhrtg rsgqrvavav ahrveapdei atdteltadr
      241 frlalsgpvr pgerirvtrf aayecadvdg tpageladvv vaeagtardd gfdvllaeqr
      301 aalgaawata dveldgdpel qlavrfsvfh llqsgradgd rtipakgltg ngydghvlwd
      361 tegyvlpvlt ylapelarsa lrwrhahlpe areraaelrl tgatypwrtl sgrecsgywp
      421 agsaglhvna diadavlryv aatgdttfla ecgaevlvet arlwhgyghf ddggafhltg
      481 vtgpdeysal vddnvftnlm arrnlrgaad aaegcpdvaa rlgvdaaeva gwraaadamf
      541 vpydgkrgvh eqsagftaqp ewdfagtged dyplllhfpy qelyrkqvvk qadlvlamlr
      601 cpgeftaeek trnvayyear tvrdsslsas aqailaaevg hldlaydlfa etafqdladl
      661 gdktadglhl aslagawlvv aqgfgglrdd rgvlafeprl prpitrlafh lrrhghrlrv
      721 tltprearye lpdagpgdav elwhhgeqlr vtgdgpvtrp mppvpdpgpe pqappgrrpe
      781 rraqeaaggd d
//
LOCUS       WP_457605658             160 aa            linear   BCT 27-JAN-2026
DEFINITION  TadE/TadG family type IV pilus assembly protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605658
VERSION     WP_457605658.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Tomich,M., Planet,P.J. and Figurski,D.H.
  TITLE     The tad locus: postcards from the widespread colonization island
  JOURNAL   Nat Rev Microbiol 5 (5), 363-375 (2007)
   PUBMED   17435791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17599729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..160
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=16541
     Region          39..>131
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
     Region          41..82
                     /region_name="TadE"
                     /note="TadE-like protein; pfam07811"
                     /db_xref="CDD:462276"
ORIGIN      
        1 mqrpartvrs rpasagrpag ppgpgrfaaa lrarlaeger ganpvelavv mpvilvmlfg
       61 siqvavwfva rstalnaaqt avnaqrtida gpdagrerai sflqqsgdwl vgweetgptc
      121 vesatgvtct vqghslsvip gvsfavtqta hgpaerwttg
//
LOCUS       WP_457605666             494 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605666
VERSION     WP_457605666.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51127
     Region          22..493
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 maepelvdvv vvglgvggee vagrlaeagl tvvgierdlv ggecpywgcv pskmmiraan
       61 alaeahrvne lagsaqvrpd wapvakrira eatdtwddkv avdrftgkgg rfvrgsgrld
      121 gpnrvrvgdq vfqarygvvl gtgtrpsvpp idgladtpyw tnhqaievee lpasllvlgg
      181 gaiglelaqv farfgvrvtv ieaadrvlav eepeasalaa dalradgvei htgvkasrvg
      241 hdrgaftvya dgaeftgekl lvvtgrkahl eelgldtvgv dagqrylpvn drmhvtdgiw
      301 avgdltgega fthiamyqag ivvadvldhm rrtkggpdas gtasvvggaa gvvsavggam
      361 saggstaapg svpvadyral prvtftdpev gavglteqqa rergvnvqvg yadltssarg
      421 wihktgnagf ikliadadqg vlvgatsagp aggevlsalv vavhaavpis qlrhmiyayp
      481 tfhraiedal ralk
//
LOCUS       WP_457605669             440 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605669
VERSION     WP_457605669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..440
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49950
     Region          5..429
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtdrtavvlf trdlrvhdhp alaaacsafd rvvplyvldp alqklspnrt rflhqsladl
       61 retlrkrggd lvirrgdpva etvklarkvg aegiglsadv tryahrrerr lraecerhrm
      121 flrlfpglti vepgalrpgg gdhyrvfspy frawqgvrwr delaapkrvr lpdgvdpgrl
      181 pdppkgdspd atvggeavar rrltawlptl dryddihddm agdetsrlsp ylrfgcvspl
      241 avanragerd gpfvrqlcwr dfyhqvvagf pdlstvayrr garedwrdda hafdawaegr
      301 tgmpivdagm rqlraegwmh nrarlitagy ltkhlgldwr pgleiffrwl ldgdrvnnsg
      361 nwqwvagtgn dtrpyrgfnp vrqaerydpd gayvrrwvpe lasvagkavh qpwrlpdevr
      421 rtldyppple vpgtdpvwlr
//
LOCUS       WP_457605673             262 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605673
VERSION     WP_457605673.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..262
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28263
     Region          80..253
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(83..86,136..141,176,178..179,200,206..207,230,232)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(85..86,136,140,178..180,200,230,232)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mrprvlsala lglvllvtgc geagkspeka aapppasasp sptpvtkpsp thttpakpkl
       61 rpvpkklpag lhrasgssgv altfddgpdp rytpqilaql raarvkatfc vvgkqakryp
      121 elvarivreg hqlcnhswhh dvnlgrrsaa eirsdlertn eaihaaapka pitwfrqpgg
      181 rwtaeevtia kqmglrplhw svdpqdwdhp paktiikrvt gatrhgsvvl mhdaggdraq
      241 tmaacrhlip dlkrrygial pr
//
LOCUS       WP_457605675             274 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605675
VERSION     WP_457605675.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..274
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=26876
     Region          1..266
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkiiavlgtg rmgtpiarrl laggnrvrvw nrspersepl avagatvaas psaavdgadi
       61 vvvmladaga vetvlfgpdg aatalrpgtv vvqmstigpd dvravagrlp tgvslldapv
      121 ggsvdaartg tlailaggpa dvveraapvl eqlgsvrhcg pigaaaavkl vantglvtav
      181 aalhdalava aalgvdrqta ldvlsrgalv gavgratapg asfavalaak darlalrrpv
      241 papvleaald lmqaapdqda dlsslvsadf lkgc
//
LOCUS       WP_457605683             247 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605683
VERSION     WP_457605683.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26361
     Region          13..244
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msglrieela drlvvtldrp ekrnaidadl vgelhavcae learprllll tggtagifag
       61 gadiaqlrer grldalaain qgvfariral pmptvaavdg palgggaela yacdlrvctd
      121 ravfgqpevr lgilagagat yrlpaligea rakellftgr rvdaeealri glvnrvvadp
      181 eellptahgl ldemakgsal alrltkmavd apaaahpqld llsqavlfed eekhrrmtef
      241 ldrrrar
//
LOCUS       WP_457605685             285 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605685
VERSION     WP_457605685.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..285
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=29927
     Region          7..279
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 msgrfvvvga gtmglgiayv aagagyavel vevdpargae avrrlgelwd rgvqrgklte
       61 daatanrerv tlraglaevt egadviveav perldlkrav lreaesrrpv llgsntssip
      121 iaelaagldr padfvglhff npvwamalle vvvgpatapa tteaavalat rlgkdpvvvr
      181 dmpgfatsrl gvtlgleair mvadevaspa didkamvlgy rhpigplelt dlvgldvrld
      241 iartlqaayg drfapppllv emvaagklgk ksgqgfytwk dgvkq
//
LOCUS       WP_457605698             171 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605698
VERSION     WP_457605698.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..171
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19430
     Region          1..159
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mtgrdeefrd yvtarleplr rtayllcrdw htaddlvsit lgklyrnwrr alganniday
       61 vrgmltnawl derrrpwrre hstdevpera dlaagepsvg eremlldllg glaprrravv
      121 vlrfycdlsv eetaqilgvs tgtvksqsar aletlrllas hhsavesgrr r
//
LOCUS       WP_457605706             380 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605706
VERSION     WP_457605706.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..380
                     /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=39466
     Region          125..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mttwpgavrr vapyspvlla ltvavatwas atgglgarsp lppvvivlia latgasvlsa
       61 rhwvlpaaaa acwlvlvawa pvvlaswrag tglrgrqlaa yligtfpvml agmavgnalg
      121 gqrrllvagp gnammsyawl viapalvglw igarrdalta lrdraerler ereahaervr
      181 aqerariare mhdvvahrvs lmvvhagale vttadpatae aaavirstgr aaltdlrevl
      241 gvlrqepplp vagwdgidel isesraaglr vdrvddgtpg pvpdavarta yrvvqegltn
      301 arkhapgaav gvrvrhlpdg ievavrndrs dgagpvlpga glglvglrer veltggrlaa
      361 gptpdggfll ralvpvgeat
//
LOCUS       WP_457605708             225 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605708
VERSION     WP_457605708.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..225
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23697
     Region          10..166
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdaalellhd tisspwvyla lfaiavvdgf fpvvpsetav itagvfaatg qpdlplvisv
       61 aalgalvgdh vsyaigrhgg arlldrlpre srrraavdra rrgiavrggl vltvaryvpg
      121 grtavtltmg atrfprrrfl afdalaaatw gtysasvgyl gglaferdpv rgllfglgla
      181 ltvtlvvevv rwargrrapq vlrgnpcstg dvkkgpfltp padar
//
LOCUS       WP_457605718             119 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Nitratifractor
            sp.].
ACCESSION   WP_457605718
VERSION     WP_457605718.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..119
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12674
     Region          9..112
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mgkysdklee ikrligdlqk eapdqiqafh qfmaavekpg amdakakelv nvalavaaqc
       61 ewcialhvkg aldagasrae vidagmqavl mhggpalmym tpltealkef edgkefggk
//
LOCUS       WP_457605727             288 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605727
VERSION     WP_457605727.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30746
     Region          182..286
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mttdvstagr hpragsvvll aglglvavaa lllvatgntg irysadhdgt vpmwsrwipa
       61 lagialirli ppapdptwpd pvapyreavp lllagitfaa vmpllggepa ytvvklalll
      121 gvplvvflaa rrraprwrpg papadaahrw gpalpvavwl vlsyatplav pasdwgrtvt
      181 pvelavtllv afavnallee vfyrrwlqtr wesllgrwpa ivlaslvwaa whvaiqgsgr
      241 pavdlasviv nqgvtglflg ylwsryrrmw pllvvhgavn ampvvlgl
//
LOCUS       WP_457605743             530 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605743
VERSION     WP_457605743.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..530
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56370
     Region          1..527
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 meefdyvivg agaagcvlan rltedpgtrv llleaggwdr spyvrvpkaf srlmdderta
       61 whypattgpg rqeiwqrgrm iggstsvngm iwsrgaardw daleplgwgw svmgrvfpql
      121 edhplgpaph rgtggpvrls iatgtdplae emvatgaelg wrhaddldah dderigypta
      181 tiragrrvsa adaflhpvrr rpnltvevga vvlrvlvegg ratgvrvarg ggettyraag
      241 evilaagala tphllqvsgi gpadtlraag vpvlldrprv gaglrehrsm vlqhrlaerg
      301 ghnmtigspl gqaratlrwl ltgggplalp vldvaahlks rpdldrpdah llmapfsaap
      361 prpgkalele repglmclgt vtrpdsegsl titdadprtp paivanylat ahdrrvavdl
      421 frrmreffgt gpiakrirae tvpgtatttd aeiveaavar gycgyhaigt camgtgddhv
      481 vdprlrvrgv dglrvadasv lpvmvagwts apvtalawra advirgrdad
//
LOCUS       WP_457605732             269 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605732
VERSION     WP_457605732.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..269
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29358
     Region          20..268
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mteltvpaqa tsptaesglm vraeqvhksf gplevlkgid levrsgevcc llgpsgsgks
       61 tflrcinhle kidagriwvd gdligyrerg gklyemrdke vaaqrraigm vfqrfnlfph
      121 mtvlqnvtea pvllrqakka harehaaqll drvglgdklg aypgqlsggq qqrvaiaral
      181 amrpklmlfd eptsaldpel vgevldtmkd lardgmtmiv vtheigfare vgdhlvfmdg
      241 gvvveqgdpr evisapqher tkaflakvl
//
LOCUS       WP_457605753             197 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605753
VERSION     WP_457605753.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21422
     Region          17..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 madvdvsgev farrpkrada rrnydaliaa arevfgerga gasleeiarr agvgigtlyr
       61 nfpqrrelfe avyveevral sasaadlade ppwdalvgwl hrfvayvatk ralaeelvhd
      121 sevfrscrte iyatgepllr raqqagaart dagfddvirl isglaayqfp dpaqrdrvla
      181 ialdglrppt gagsprv
//
LOCUS       WP_457605759             261 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605759
VERSION     WP_457605759.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..261
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=26743
     Region          31..258
                     /region_name="SEST_like"
                     /note="A family of secreted SGNH-hydrolases similar to
                     Streptomyces scabies esterase (SEST), a causal agent of
                     the potato scab disease, which hydrolyzes a specific ester
                     bond in suberin, a plant lipid. The tertiary fold of this
                     enzyme is substantially different...; cd01823"
                     /db_xref="CDD:238861"
     Site            order(39,81,109,239,242)
                     /site_type="active"
                     /db_xref="CDD:238861"
     Site            order(39,239,242)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238861"
     Site            order(39,81,109)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238861"
ORIGIN      
        1 mprrvrtvfa allaavlgav llpgaaraat vnyvalgdsy ssgvgagpyd lstclrsqks
       61 yaplwaaahs vtsfrfpacg gavtadvlnn qvgqlssstt lvtitiggnd agfadvmtsc
      121 rfggtssces avneskafat atlparldat ytairnrapn arlvvlgypr lfetgscgll
      181 amssykrtil nqaadtlngv isgraaaagg tfvdarpffa ghgvcaadpw irdvsgviea
      241 yhpnangyry gylaaltaai g
//
LOCUS       WP_457605755             486 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605755
VERSION     WP_457605755.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49524
     Region          17..456
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide)-like multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17504"
                     /db_xref="CDD:341047"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,141,
                     144..145,148,272,275..276,279..281,284,318,322,372..373,
                     377,381,397,400..401,404..405,408)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341047"
ORIGIN      
        1 mihssgrgsr rltflvlaag tgffamlqsl itpvlptiqh dlhtspntvt wvltayllsa
       61 svftpiigri gdmvgkektl vfslaalalg cllaavapsi gvliaarvvq gvggavfpls
      121 fgiirdefpa arvssavasi savvavgggl gvvlagpiva tlgyrwlfwi plvvvgltal
      181 aahrfvprsp vrtpgrinwl savllsgwlv alllpvskga awgwgsgrvv glltlaavla
      241 aawlateara anplidlrmm rlpavwttnl vgllygasmf avyaflpqfa qiptsagygf
      301 gasvtqagll mlpmlvgmfv agllagrlqs rfsakaqlst gavfnvaaaa mltvahdtrw
      361 qvgiagglvg lgiglafasm anlivanvpa gqtgaatgmn anirtiggai gaalasavit
      421 anpqpsglpr eagftagfll ltgisvaaal aalavpsgrr rwprrrigpa vpdlapapaa
      481 elvpar
//
LOCUS       WP_457605761             511 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605761
VERSION     WP_457605761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..511
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55180
     Region          63..476
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(171,173..174,310..314,334,337..338,341,356,360,415)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mrraltaaia altlttagtt vtgspgqaap tgwgrpqpaa atptpgspgl gdsyfpdygn
       61 ggydvghydi rlryepatdr lsgtttilat atkdlsrfnl dfaldvesvr vngwaagfar
      121 agdhelvitp arpltkgqql tvvvryagvp sqttvygyta wtrtadgala vnepesawww
      181 ypsndhpkdk atwdvsvsvp tgvevisngv qprdplpeag nrtrwswrsv kpgatyqafl
      241 aigqydivtg tapngqpvvn aysttlgerl paarasiert aeivewesgl fgpypfeaqg
      301 gvagpvdgig faletqtrpv ygpgfwrrga ntyvvvhena hqwfgdsvsv adwrhiwlne
      361 gfasyaewlw seeqgegtaq elfdftydsy padsefwqvr pgapgpsgif daavydrgam
      421 alhqirlavg daafyrilrt wtakrqygtg tvaqfqalae risgrdldav fttwlftpgr
      481 pavataartt aapaqpaswa kiraahdllg r
//
LOCUS       WP_457605767             183 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605767
VERSION     WP_457605767.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 183)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..183
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18716
     Region          1..135
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mspltwavaa vvtdasgrll lcrrsegarr wglpggrlrh despadavvr avraetgwav
       61 apadlvglyr vtdpqvpapp aglcggrpdv lvhvfragpa dagpagepat gclprwwppq
      121 elpdvltptt raaiadalag ragvlrhttt adaltppgdg qpgdgqpapp gqraseqads
      181 ssr
//
LOCUS       WP_457605773             240 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605773
VERSION     WP_457605773.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..240
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25136
     Region          5..236
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mddavsvrel vvdrggrrvl hgiscavprg tvtgllgpsg sgkttlmrav vgvqtvdsgt
       61 vdvlgrpags anlrrrvgyl tqapsvyadl tvrenaryfa vlqgrgraea dravadvgla
      121 eaadqlvgtl sggqrsrasl acalvgepel vvldeptvgq dpvlradlwa rfhamaangt
      181 tllvsshvmd eaarcdrlll iregrlvadd tpaavraatg tddleeaflr lirdaegear
//
LOCUS       WP_457605777             622 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605777
VERSION     WP_457605777.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 622)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 622)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 622)
  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 622)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..622
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65531
     Region          12..599
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 masgtsrdvl grglrvlgra ireqprifav avsgsvlfgl lviasayvvg avvgdvvvpa
       61 vergevagga lalaaaalfg isvlrvvgif grrlgagymq yrlqaayrrr vtrryldlpl
      121 awhhrnstgt llsnansdve aawypiaplp favgtlvmlv gavaslfftd walalvglav
      181 fpalfalnvv ysrrmaprqa raqrlraevs giahesfdga lvvktmgrea qetarfasra
      241 gelrdalisv grlrgvfdpm letlpslgtl avlvvgairl rqgaisvtel vsvaflftvl
      301 afpvraigwv laelprsvag wdrvrrvlda tgempygttt ldpatrepat lgfddvhfay
      361 epaeahlpga qvlgevtftv pagktvalvg ptgagkstia slavrlvdpg agrvtldgvd
      421 vreltaasla gtvalvaqvp fvfddtvran ialdragigd devwaalrla eadgfvaalp
      481 dgldtmvger gtslsggqrq rltlaralag rprllvldda tsavdprvea ailaglrapa
      541 dggapasilv vayrratial adeviyveqg rvvargthte llatvpgyad lvtayeqaeq
      601 ereqnrtyde vtplasglev er
//
LOCUS       WP_457605786             333 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605786
VERSION     WP_457605786.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..333
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34889
     Region          1..333
                     /region_name="CurA"
                     /note="NADPH-dependent curcumin reductase CurA [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG2130"
                     /db_xref="CDD:441733"
ORIGIN      
        1 msgtnreihl asrpegwptp enfrlvttev ptpgpgqvvv rnrfmsvdpy mrgrmndvks
       61 yvppfaldap ldggaigevv ageaggvkpg dtvlhglgwr eyalvdakgv rkvdpglapv
      121 taylgvlgmt gltaytglld vaamkpgetv fvsgaagavg smvgqiaklr gagrvigsag
      181 saakverlta lgfdaafdyh dgpvskqlra aapdgvdvyf dnvggdhlea aigamnlhgr
      241 aaicgmiaqy nateppaapr nlalvigkrl tlrgflvgdh ghlreqfvqe vagwlregrl
      301 sydetivdgi eqapeaflgl lrgenlgkml vrl
//
LOCUS       WP_457605811             469 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605811
VERSION     WP_457605811.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..469
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48404
     Region          2..460
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mipltlaeva aavdgrlvga dpdarvtgtv efdsrkvnrg glfvafpger vdghdyaaga
       61 issgavavlg trevpdvpmv lvgdaldamg rlaravvdrl pgltvigltg ssgktttkdl
      121 iaqlavrlgp tvappgsfnn elghpytalq atpetrylvm ekgargvghv rylcdvvppr
      181 isvvlnvgva hlgefgsvea ialakgelve alpsdglavl naddprvdam asrtgarvvr
      241 ygeseradvr avdvtvdgrg rpsytlvtpe gsapvrlglt grhqvsnsla aaavgrelgl
      301 plpdlaaaln elglvstrrm dvferpdgvt viddsynanp astgvalral asmrgdgrtv
      361 avlgymaelg dfelqghqqv grlaaelgvd rllvvgepaa pihegatavg nwggesvllt
      421 dqaaavevlr selrpgdvvl vkgsryrtwe vadalradap egateggaa
//
LOCUS       WP_457605819             821 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605819
VERSION     WP_457605819.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..821
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87715
     Region          51..401
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          <427..547
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          688..758
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 mtphrnigfv aaaatllsaa plsaiferwt wliqaavvva vvagsaalsr lgrmplwgqv
       61 lamlagltlg ltwvfpggte llafvptpat fahfgdllqt slqdmrsygv kvpdvdsllf
      121 lavlgigava vvvdvlavgl rrpalaglpm laiysvpvav yvdsvpatpf vvgaagylwl
      181 lvtdnvdrvr rfgrrftgeg rdvdvweasp laaagrrlav vgvivavalp lavpgmtggl
      241 lnnvgagpge gngrpgqggs sgrvdlfaal sgqlnqseei elvkvstnet apfylrlgvv
      301 ddlrpsgfqa rvptgrsvar slsdpgddap rgvdrqryra tvevtknlnm pllpvytepv
      361 ktedlngnwl ydtnqqvvfs nrdnargksy sfdyvrstfs paalraarsl psdspvmrqq
      421 terpsvpave elvaelvkdk sndydkvrai ydyfsvdngf tyalstrngs sgeditdfla
      481 tkvgycqqya aamawlvraa giparvavgf tngskadngt yvltnrnlha wtevnfngig
      541 wvpfdatpaa avpgsvrsaw apdidapeev tpsagstsap dtagpsagpn eadrldkdtd
      601 qgltlnqggp aeespvwpww lagalallal lavpalrrsa lrrrrrvrav ppaatalpvp
      661 gqrgetravv vgvdaeaara dahaawdell dtlvdfhvrv drtetprata erlarealae
      721 rgdaatgvrl lgraeerary ardpltdael qpalrtvrga laagadrrtr llaallppsv
      781 lqrwraalae rsarvvttsg qvrqqmtrws prrllahrpt r
//
LOCUS       WP_457605823             395 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605823
VERSION     WP_457605823.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..395
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40320
     Region          49..392
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mtgpapdptp gpapgpldrv aprydggalt dvlpsalall gvpgaadrlg laprlagvrr
       61 iavllvdglg wyqiptaapy aptlaglaat agrplttgfp sttptslvsl gtgtpsgahg
      121 vlgftvrvpg tdrvlnhvdw agdpdpaswq pvptwyqrar avgvavtvvs rpefagsglt
      181 laanrggdyr gaagvdalaa rmlaalaagd gpalvsgyhp dldrhghlsg vdsapwrtaa
      241 advdtllarl vdglppdaal lvtadhgqld vpaghridld tdprlragvr vvageprvry
      301 lhvepgaead vvaawtevlg paaqvltrae avatgwfgpv peahltrigd vvvvcrdtya
      361 vvatrseppm asrlvayhga dtaaemtvpl lvvrg
//
LOCUS       WP_457605826            1116 aa            linear   BCT 27-JAN-2026
DEFINITION  error-prone DNA polymerase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605826
VERSION     WP_457605826.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481461
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1116
                     /product="error-prone DNA polymerase"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=121245
     Region          63..1116
                     /region_name="dnaE2"
                     /note="error-prone DNA polymerase; Validated; PRK05672"
                     /db_xref="CDD:235553"
ORIGIN      
        1 msfhnpkmpw skleqvlsgr aggerhlhvv dplavdadgg dspawsrkrq eyqppeldrp
       61 dgvvpyaelh ahsnfsfldg ashpeelaee aarlgltala vtdhdgfygv vrfaeaaral
      121 rlptifgael slglpgpqng epdplgrhll vlahghegya rlaatisraq lrggekgrpv
      181 ygeleeiaae lrdhvlvltg crkghvpaal ltegvdaaar eldrltalfg aetvaveltd
      241 hghpvdadrn daladlaaaa glptvatnnv hyatpgrrrl attvaavrar rsldeidgwl
      301 paaatahlrs gaemaarfaa ypgavaraae ygaelafdlq lvapqlpayp vppghtemsw
      361 lrrltmdgar erygppeahp eayaqlehel rmisdlgfpg yflvvydiva fcraqdiycq
      421 grgsaansav cyalritnvd avrhrllfer flaperdgpp didvdiesdr reeviqhvya
      481 rygrehtaqv anvisyrprs avrdvakafg fspgqqdaws kqidrwgsva avdvadipeq
      541 vvayanelqt fprhlgihsg gmvicdrpvi evcpvewgrm pgrsvlqwdk ddcaavglvk
      601 fdllglgmls alhygydlig srldlgdmtl ddpevydmlc radsvgvfqv esraqmatlp
      661 rlkprefydl vvevalirpg piqggsvhpy irrkngqepv tyahplmrna lektlgvplf
      721 qeqlmqlaid lagfdaagad qlrramgakr svermaqiad rlyagmaerg itgeladdvy
      781 rkltafasyg fpeshamsfa ylvyasswlk ryhpgpflaa llnaqpmgfy spqtladdar
      841 rhgvevrrpd inasgakavl estpetrwgs vpgepphawg lggpavrlgl gsvrtlgedv
      901 aerieaeraa hgayrdmpdl arrvgltaaq lealatadaf acfgltrrqa lwaagaaaqd
      961 rpgrlpgtvt gadpptlpgm aavdrlvadv watglspesh parfirdrld elgavpiarl
     1021 gqvppgqrir vggivthrqr pataggvtfl nledetgmln vtcspglwqr yrrvartsga
     1081 lvvrgrlqrh egvtnltadr ldaieppvtp asrdfr
//
LOCUS       WP_457605830             465 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin reductase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605830
VERSION     WP_457605830.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Carrillo,N. and Ceccarelli,E.A.
  TITLE     Open questions in ferredoxin-NADP+ reductase catalytic mechanism
  JOURNAL   Eur J Biochem 270 (9), 1900-1915 (2003)
   PUBMED   12709048
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Dym,O. and Eisenberg,D.
  TITLE     Sequence-structure analysis of FAD-containing proteins
  JOURNAL   Protein Sci 10 (9), 1712-1728 (2001)
   PUBMED   11514662
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..465
                     /product="ferredoxin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50269
     Region          52..465
                     /region_name="COG4097"
                     /note="Predicted ferric reductase [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:443273"
ORIGIN      
        1 mtaavtgrra prrplptapa wwadvagala alsllvvaal waadrgvqel lagaatglts
       61 lgrlaglvsa dlmliqvvlm arvpllerrf gqdriarwhr lagftsfhll lahvlltvlg
      121 yagtarrgvp aeaanlvlty pgmllataal alltlvvvts vraarrrlry eswhllhlya
      181 ylgvalalph qlwtgadlla splaraywwt vyllalasvl vwrlglpawr slrhrievaa
      241 vvaeapgits vwlrgrdlhr lpvragqfll wrfldgpgws rahpyslsap pqgnllritv
      301 kdlgdgsarv galrpgtrvl iegpygrltg qhwrgggitl lacgvgltpl lallwelpya
      361 pgeavlvhrv rtaddlvfsa eldrlvaerg lvvhrlvgpr aarpswlpay aeglsdaeal
      421 rrlspdvagh dvflcgpdgw vdavraatra agvpdahvhh erfaw
//
LOCUS       WP_457605845             289 aa            linear   BCT 27-JAN-2026
DEFINITION  deoxyribonuclease IV [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605845
VERSION     WP_457605845.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Asano,R., Ishikawa,H., Nakane,S., Nakagawa,N., Kuramitsu,S. and
            Masui,R.
  TITLE     An additional C-terminal loop in endonuclease IV, an
            apurinic/apyrimidinic endonuclease, controls binding affinity to
            DNA
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 3), 149-155 (2011)
   PUBMED   21358045
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Garcin,E.D., Hosfield,D.J., Desai,S.A., Haas,B.J., Bjoras,M.,
            Cunningham,R.P. and Tainer,J.A.
  TITLE     DNA apurinic-apyrimidinic site binding and excision by endonuclease
            IV
  JOURNAL   Nat Struct Mol Biol 15 (5), 515-522 (2008)
   PUBMED   18408731
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Ivanov,I., Tainer,J.A. and McCammon,J.A.
  TITLE     Unraveling the three-metal-ion catalytic mechanism of the DNA
            repair enzyme endonuclease IV
  JOURNAL   Proc Natl Acad Sci U S A 104 (5), 1465-1470 (2007)
   PUBMED   17242363
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Mol,C.D., Hosfield,D.J. and Tainer,J.A.
  TITLE     Abasic site recognition by two apurinic/apyrimidinic endonuclease
            families in DNA base excision repair: the 3' ends justify the means
  JOURNAL   Mutat Res 460 (3-4), 211-229 (2000)
   PUBMED   10946230
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Hosfield,D.J., Guan,Y., Haas,B.J., Cunningham,R.P. and Tainer,J.A.
  TITLE     Structure of the DNA repair enzyme endonuclease IV and its DNA
            complex: double-nucleotide flipping at abasic sites and
            three-metal-ion catalysis
  JOURNAL   Cell 98 (3), 397-408 (1999)
   PUBMED   10458614
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Barzilay,G. and Hickson,I.D.
  TITLE     Structure and function of apurinic/apyrimidinic endonucleases
  JOURNAL   Bioessays 17 (8), 713-719 (1995)
   PUBMED   7661852
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..289
                     /product="deoxyribonuclease IV"
                     /EC_number="3.1.21.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29870
     Region          9..287
                     /region_name="Nfo"
                     /note="Endonuclease IV [Replication, recombination and
                     repair]; COG0648"
                     /db_xref="CDD:440413"
ORIGIN      
        1 msgcdgrrrv gshtptsggl araalpyada agsevvqvyv snsrgwalps gdpaqdasfr
       61 dwcgerglpv fihasllvnl gsptpatvtr saetlahalr rgraigaegv vfhagsavda
      121 ghadaalrqv reallpllde vaatggpmll vepsagggrs lasrvehlgp yldavdrhpm
      181 lgvcfdtcha waaghdlaae ggmtatldtl vatvgadrlr lvhandskdl cgstrdrhen
      241 igkgtigepa faelmrhpat agvpvlvetp tekhvghaad iatlkrlhp
//
LOCUS       WP_457605854             162 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione peroxidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605854
VERSION     WP_457605854.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Arthur,J.R.
  TITLE     The glutathione peroxidases
  JOURNAL   Cell Mol Life Sci 57 (13-14), 1825-1835 (2000)
   PUBMED   11215509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..162
                     /product="glutathione peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004602 - glutathione peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17102
     Region          1..160
                     /region_name="BtuE"
                     /note="Thioredoxin/glutathione peroxidase BtuE, reduces
                     lipid peroxides [Defense mechanisms, Lipid transport and
                     metabolism]; COG0386"
                     /db_xref="CDD:440155"
ORIGIN      
        1 mtvfdvqida ltggpadlgs yrgrallvvn vasrcgltpq yaglqeladt yagrgltvlg
       61 vpcnqfagqe pgsaaeieef cqvnygvtfp ltekvdvngp drhplyaelv stpdadghtg
      121 dvrwnfekfl vapdgtvaar fspqvtpeap elraaiekvl pa
//
LOCUS       WP_457605860             364 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605860
VERSION     WP_457605860.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..364
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39615
     Region          8..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          189..288
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mvddsdwttv geqirqarlg vglsqaelat rigldrtmia kveagarrvd alelvrlata
       61 ldvtidyllh rrpavishra allaeddnve aarrslrldi alsawvgdvr qmieagtlrp
      121 ntpmrypgpv eseadartaa rwlreahrlg gepittlmef sercgqyvlv idlpgdgasl
      181 idgdiavavv sakgdpgrrr ataahelghl vlgdeyssdl avhlsradre sminafaael
      241 llpvaafsgp apegnpreqi irlaamyrts wslalrqael agwldatrrr slsqvtptqa
      301 efmdavgwap qpdlngvrvp pgyshavmqa wrrdlvtgsr avellhgqit sddlprrdda
      361 dlpl
//
LOCUS       WP_457605866             261 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605866
VERSION     WP_457605866.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..261
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28339
     Region          32..236
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mhktltfsdh lrlidersta fraavaaaps ldmqvpthpe rtlfdlvrhv gtgrrkaaai
       61 vaagpadgpp eksawddaad apqerealla wwtesveqlt stlraagpdr gcwtwwddsp
      121 spqtagawar rqvpeiavht ydvqltvgap qplpeevald gfddcqftlc attvawphrp
      181 avvdyhaveg rswrlrlsag gaqvahltpp adgapdtadv sawgtasdlv lffygripld
      241 sltfegdrri fdqlaawdps v
//
LOCUS       WP_457605869             560 aa            linear   BCT 27-JAN-2026
DEFINITION  ammonium transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605869
VERSION     WP_457605869.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, 57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..560
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57658
     Region          2..414
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 msapnagdta wvlvcaglvl fmtpglaafy ggmvrtrnvl amlqqnmial gvvsltwvlv
       61 gytiafgdda gsglfgnlel fgltdlkvpp apnlhvidgr itiptlafvl fqmmfavitp
      121 alvtgatagr lrfggwvlfl avwsivvyap iahwlwhpgg wlakfgtqdw agglvvhasa
      181 gaavlavllv vgrrrdwpht aappnsiplt ivgagilwfg wfgfnggdgl qanglaaqav
      241 lnthlaaaaa mlvwlalerv tdghstvvga vsgavaglat vtptagyvna asavaigala
      301 glvchfalkl kyvlrlddal dvlavhfvgg mlgtlllglf gnrgvnplga dglflggggg
      361 llwrqlvgvv svvafsfvlt wliaagvqal iglrvppadq erldqaqqga dayhlggvts
      421 ltapgaprrr aaaapagepa appgepsvpp gepaappgqr vrvvtallep dpaansadlr
      481 dallragais vivsdaavat ttpqasllpr gywqdqplsa rlrvtvlvgt dgvgavldel
      541 drmgarrsdt fvqeaervqs
//
LOCUS       WP_457605875             225 aa            linear   BCT 27-JAN-2026
DEFINITION  urease accessory protein UreF [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605875
VERSION     WP_457605875.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..225
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23950
     Region          5..225
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtealkllqf gdsvfpvgaf sfsngletav eqgavhdrst lqefvrtvtr aaatgdgval
       61 lvahraarag dldgiraadq avhlrkinee trtmtvrmgr klaeaaervv gesllrkrva
      121 esgggvpvty pvalgvlfae lgvgeadafa ahqygaasmv lgaavrlmrv dhldtqsilf
      181 avnervgedy eevrtagldd mqsfaphldv lagahqhahv rmfms
//
LOCUS       WP_457605892             275 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605892
VERSION     WP_457605892.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29647
     Region          34..268
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mtaaervrvv rswewarper parrevlaav pereeakppl lfvpgfghga wafaehwlgh
       61 aagrgfpaya lslrghggse papeatlrsy thdvtqvaas lprqavlvgh gagarvvaha
      121 maryparaav lvapvlggwa tfgtalrrnp vgtvpavfga glrlnrrqlf srelpdadar
      181 rhlarlgrag rraqwqlltg rspepavgrp pvlvlgspdd rvlpataltr aarryasapl
      241 lfpgmghdlm ldarwrepid aildwldkdp apaqg
//
LOCUS       WP_457605901             564 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605901
VERSION     WP_457605901.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 564)
  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 564)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   3  (residues 1 to 564)
  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   4  (residues 1 to 564)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..564
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59086
     Region          209..329
                     /region_name="GAF_3"
                     /note="GAF domain; pfam13492"
                     /db_xref="CDD:433253"
     Region          343..545
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpastsrqps tqplaaaara vllalvaalt lfatrdatql wwiallgvag lpavlapqhr
       61 llapisrfae vlvlglaasq vaadthlsgv tggvgasavl pylavpvtvt alsrrfrega
      121 allavaaatl lasaaftqvd ggpqlgqvgy lavcaqwlil aglglytagt lqrvmrvrge
      181 gkpqpyaeat rlltqlrtva rqlpgatldp ggisehllee lrvvaktdrg avlsasgggr
      241 lvvlaqigad rvdwettlda dsaiadawat qqptvsarsq arsrhsgevs alivplvagv
      301 rtvglvviea dtaaaypppv vsrvtaltgp aalrleaall fdevrslatn eerqrlarei
      361 hdgvaqelvm vgygidnala tvhedaeeta dslrtlrqev trvitelrls lfelrsevdr
      421 hgglaaaiae yartvgasgg lrvhlsldes tarlpaatea ellriaqeav tnarkhagas
      481 nlwvtcevdp pytrievsdd ghgigdqrpd ghyglaimae raerirgrle irprqpsgtt
      541 vavvlgsspr rdkvrgsaaa aege
//
LOCUS       WP_457605903             419 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605903
VERSION     WP_457605903.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..419
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44379
     Region          <93..405
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(277..278,281,355,359,400)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(277,281,355,400)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mtprawallt lgglvvallv avallvpwsr ppapradqla alrdlpaeqv srgrafhgal
       61 rpaawsalav glvvalllgl tplggrlvel vgrpfgghwv aqavlgglav mfladlltlp
      121 faawrrtvlv ryglstqswg gwavdllksy avsavigalv llgfytvvrl aprwwwafga
      181 agaaalvvvl sfvlpvlvep vfnrftpmep gplrteltam aardgvpvrd vlvadasrrt
      241 savnayvsgl gptrrvvvyd tllreaepae vtsvvahelg hakdrdvwtg tvlgalgaaa
      301 avvalyligs wtpllrlasv dsiaqprafp llialvtvag llatpaqalv srriearada
      361 halaltgdpa tfeamqrrla gvnladpdpp rwerlwsath pstvermaaa rayaresgr
//
LOCUS       WP_457605908             291 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605908
VERSION     WP_457605908.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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..291
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..291
                     /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=29822
     Region          17..223
                     /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 mstpyaataa pgvevcavvl aagegtrlrp ltermpkalc pvgnvplldr alarlaglgl
       61 tgpervavna cylgdqvvar vgdrahlsve pdaplgtagg vgrlrdwidg rgvlvgnada
      121 yladpqappg pdiaalldgw dghgvrllgr pagdphapgt fdghefvgfs llpwrlvrdl
      181 patfgdlvrt vwrpaeaaga ltvvpyrgtf ydtgtpadyl aanlhaagpd glvdpaatvt
      241 grvtvsvvga galvhgdvdr svvwpgasva agerlrevir agddltvpat r
//
LOCUS       WP_457605917             324 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605917
VERSION     WP_457605917.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..324
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33597
     Region          1..323
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mreamaaaev gddvygedpt vtaletevaa lfgheaalfa psgsmanqla lqlhvppgde
       61 llcdadahvv tyevgaaaay ggissrtwpa vgaeldpdvv agmirpdgyf avptraiave
      121 qthnrggggv iplptlrrmr evadehgval hcdgariwha hvsdgvplae ygvlfdtlsv
      181 clskglgapv gslvvgsaek iararflrkr mgggmrqvgi laaagryala hhvarladdh
      241 vkaarlaeav aphgvlasav rtnivpldlt khpldahala aaaraeglli svlgprtarl
      301 vthldvtdaq idraatilnt alra
//
LOCUS       WP_457605920             558 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605920
VERSION     WP_457605920.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 558)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..558
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60396
     Region          2..544
                     /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 mtqsqleeml qrltdrlaqa lraepfdlri gqqvgaelvq ahiasaeglg rtveviqlrl
       61 vrdldlvvdd vedrmarlla tvatgyaral rdrtldeqes irraammara qaeralrdse
      121 arfrhqathd pltglpnrtl fterltaait apgrgadrvg vcfldldrfk vvndslghqi
      181 gdsllvtvaq rlhralgehl varlggdefv ilvertagtd dvvkvaeaal aavrepalvd
      241 gheltvsasi giverpvagt spmdlmraad stlhwakaag garwslfdad rnrrelarya
      301 lsaaipaald rgefyldyqp ltslrdgrvl gmealvrwrh pelgvlrpds fislaeetgl
      361 ivrlgswvla eacreagtwp gadgdapfvs vnlavrqlhr tdlvtevrgv lgrtglpphr
      421 lqleitestm mstvvepvra lrvlgdlgvr vaiddfgtgy cnlaylrdlp vdelkvagef
      481 vtglrapgcg tderilaslv slahaldltv taegvetadq adrlraigcd agqgwhfgrp
      541 gpaaphlgrv pahvdaas
//
LOCUS       WP_457605926             318 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605926
VERSION     WP_457605926.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..318
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32309
     Region          1..264
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 mtqpaireip ltgpgsgpys itvgpddalw lalagsggva rlgldgevrt yrddppgsrp
       61 liivggpdga lwytrsgddr lgritvgget gsvalppgcg pcglavgadg alwyagmsdd
      121 tigrvsvdge vtsfplpvdk gfpsmlaagp ddalwltlnq anaiarvdld gtvavhplpt
      181 eaagpvgitr ggdgalwfve ivagqlgrit pdgridefpl pdraarphai vadpaggcwf
      241 tewganrigh idpdghhtah dlptpaseph gltltpdgav waaleigava hltpsppspp
      301 sppsppspps ppsppspr
//
LOCUS       WP_457605946             407 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605946
VERSION     WP_457605946.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..407
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42602
     Region          12..374
                     /region_name="MFS_YfmO_like"
                     /note="Bacillus subtilis multidrug efflux protein YfmO and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17474"
                     /db_xref="CDD:341027"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,138,
                     141..142,145,213,216..217,220..222,225,249,253,303..304,
                     308,312,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341027"
ORIGIN      
        1 mdrrsepnrs aiyattlvaf laiagiavvd pilpaigeai gvtawqvell ftayiavmav
       61 gmipatlasg rfgfkpvlvt gvsvvglaai lasfsndivq lsvlrgvwgl gnamffatam
      121 vvlvnlandr ewvvglfeta lglgfavgpl iggllgevsw rlpffvcgvf mvlalgvaar
      181 klrepvnkqq pvrlgqifat yrkpafvtlc vvtaaynfvf fvvlgytplf lrldviplgl
      241 aftgwglgla agillighrl ahrigavqtv gvallgllvc mvlfatstgt amslvvlvva
      301 glfmglanan ltdlalglgs adrrvatgaf nlvrwgaaap apiisgklae hslalpfwvg
      361 fgvlaagvla ylafghlmaa gygerviwnr aarraehape epvgeay
//
LOCUS       WP_457605953             369 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457605953
VERSION     WP_457605953.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 10008453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..369
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37555
     Region          20..197
                     /region_name="COG4279"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]"
                     /db_xref="CDD:443420"
ORIGIN      
        1 mspgfddygp pvrvegglra rstrgaigqs wwsrrfvevl esfalgsrlt rgrayarrgq
       61 vlrldvspge vtaevqgsrp rpypvrigla typskvwrrl eselagqaff sarllagdlp
      121 aeleelfaea gaplfpaeid eldqscgcpd favpckhlaa tfyllaeafd adpfhllhwr
      181 grsrtelldr lrtlraadag ssggagglgg agglggaggl ggaggageag etggtggtgg
      241 agrtggagrt rgaggvggag aepvpgaepe sagttgvpvv gaaralaglp pveadaepdr
      301 fwlspvalpd rpptlatgpe lllrqlgspg agiggpglae rlrrayrefs rgeaapsgef
      361 grgeaager
//
LOCUS       WP_457605966             563 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605966
VERSION     WP_457605966.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..563
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60484
     Region          24..537
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mnnldnistq sgllpaghra hvradgvrva rggrvvlsdv svtvsagsrl avvgengrgk
       61 ttllhvlagi llpdqgtver lgtigvarqn lesrhgetvg tlvhgatres eralraldda
      121 aaalaagrag addayaaald aatrldawda qrrvdvalag ldacpdrerp latlsvgqry
      181 rvrlacllga rvdllmldep tnhldaasla fltarlrehp ggvvlvthdr allrdvatef
      241 ldldpsadgr prryagdyaa wqdgrrrdfa hwvrdheaqq aehqrltdav reaqgrlstg
      301 wrpekghgkh qrqsrapglv qalrrrqeal dehritvpep pqplrwppld traglpilrc
      361 hdvtvagrlr trvtltldgg drllvtgpng agkstllsvl agdlvpstge vrhpsgarva
      421 ylgqevpdwp plmlahdlye qhvgrlrstg rlgsgtplpl gatnlldaea rrtpvgrmsh
      481 gqqrrlnlal rlaecpdlli ldeptnhlsa plvddltaal lttraavvva thdrqmlhdl
      541 aawptlplta gpsghtgscl seg
//
LOCUS       WP_457605974             156 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605974
VERSION     WP_457605974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..156
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16798
     Region          21..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mahstvpaar draglagetv rrilhvaaam rhhqhegiaa lgltpavara lheldpdrpl
       61 pardlaeqlg cdrsnitgla dkleqaglve rrtdpadrrq kalvvtgrgr qvrdrvrqvm
      121 sdsrlldals teelatlrdl vlkvsdggcp qecgqv
//
LOCUS       WP_457605976             547 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605976
VERSION     WP_457605976.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..547
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60304
     Region          31..499
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 malsrrtill sgaalgaaga aaglpvaaaa spgplrrdpf tlgvasgdpd hegfvlwtrl
       61 apeplaedgl ggmptrtvpv awevaaderf rhvvrrgval arpdsahsvh velggllpgr
      121 ehfyrfraer wvspagrtrt apapwlmpsa lamafascsq yehgyftayr rlaetepeli
      181 lhlgdyqyey akdtynvpgg nprdhegpet rtlanyrqrh aqyktdtdlq aahavapwvv
      241 vfddhevenn wadevpeapd pdfparraaa fqayyenmpl rrtsiprgid mrlyrrvrwg
      301 rlatfhmldt rqyrddqacg dgykscaeas dparsitgaa qeawlldgfr rsearwdllg
      361 qqvffaqrdn nsgpltvtsm dawdgyaasr dritrgwtaa gvrnpvvltg dvhahwasdl
      421 kldyadptsr tvgselvcss itstgdgads ptgshpwlaf nphlrfqnnl rgyvrttitp
      481 teltadfdvl pyvsrpdapa ytrarfvied rlpglnltyd rppaaartaa pgadqgrqtv
      541 eaetvrp
//
LOCUS       WP_457605987             207 aa            linear   BCT 27-JAN-2026
DEFINITION  carbonic anhydrase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605987
VERSION     WP_457605987.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..207
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21876
     Region          8..205
                     /region_name="CynT"
                     /note="Carbonic anhydrase [Inorganic ion transport and
                     metabolism]; COG0288"
                     /db_xref="CDD:440057"
ORIGIN      
        1 mpstspraal aellagnrrf vsgwpvhghd vtaaaavasg dqqpyavvlg cidsrvplea
       61 ifdqtfgsic virtgghvld ravrgsieyv veqlgvrlvm vlghercgav gstvealrtg
      121 rrpggdlayv vdriapavtd vgvddpdahp lairrhirrt vaalrrddrl agpvdagela
      181 vegalydlat gevtllprer trnrppg
//
LOCUS       WP_457605992             304 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457605992
VERSION     WP_457605992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..304
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31420
     Region          1..294
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mgaghdhsga vtnaahrhrg rlwaafglla almvveavaa fttgslalls daghmftdvl
       61 gigmalaait atrragtdpq rtfglyrlev laalanavll gavaiyvlve avrrfgeppe
      121 vlagpmlvva vlgllaniva fallragake sinlrgayle vlgdllgslg viaaalviav
      181 tdwwwadplv avgiglfilp rtwrlgraal rilvqaapeh lqvtavhdrl aavpgvaevh
      241 dlhvwtltsg mevasahltt dpgadpagvl aaaraalhed fsidhatlqv epgasagvcg
      301 ktew
//
LOCUS       WP_457605990             704 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605990
VERSION     WP_457605990.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..704
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77110
     Region          5..701
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdqttldre iaaeqrhldr vyarlaelrr saadaeregy rlarvgnfga lverdamvfh
       61 aaqrrhvlda eheglvfgrl dlrtgqvlhv grlgvrgvda etlvvdwrap aaaafyqatp
      121 aeprgvvrrr tiqsasekvt rieddlldpe aappdmavvg dgallatlsr atgrgmrdiv
      181 atiqreqdea irspgngvti vsggpgtgkt avalhraayl lysdrgryag ggilvvgpsg
      241 vfveyiasvl pslgeetatl hslgslfpgl sasrtdppdv aavkgslrmr rvleravrda
      301 vpdspaelrl lyrgellrle rpaldairdr tlargarrne vrraafdavl aalyaqartl
      361 rvgrlpeqpa fedeiierpe freflkawwp rlhprhvldw larpdrlrry aggilssaei
      421 rllgdayrtl ategltvadi alldeldall gkpvrrtrpk rdpyqlaggv relstyadrq
      481 raaraaarer pddyrdyahv vvdesqdvsp mqwrmvgrrg rlaswtvvgd paqtawtgdp
      541 qeldrardqa lgrrkrhrye lttnyrnsae ifavaaaeir rlypdlplpd avrstgvppv
      601 ertvpaadlp aatveaaeal laqvegtvgv itpvprrdev agwlgglgag rlqvvtslqa
      661 kgmeydgvvl vapseiradp gsgvrtlyva lsratqrltt ldpv
//
LOCUS       WP_457605985             574 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457605985
VERSION     WP_457605985.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..574
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57355
     Region          65..567
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 msisprrsav alaaltallv sgcsdgpdrp rpaptspaps saapapsdpp atdpaaraaa
       61 lvgtlsdedl vgqvlmpyay gssatqvsag saagnralag vdtpaemvak yrlggvilvg
      121 fsaddptsgn qattnvdnpk qvraltdglr aaagklpaga apfligtdqe ygvvtritdg
      181 vtllpsplaa gaagnpalte aawraagael aamginldfa pvadvlatrs avigsrsfga
      241 dpataspqva gavrglqaeg vgaavkhfpg hglsaedsht elpvikqsra eldrlafppf
      301 rsgigagama vmsahldvka vdpgtpatfs rklltdvlrg qlgfqgvvit dgmnmapakk
      361 wspgeaavra lnagndlilm tpnvtqaydg lraalkdgsl prarlveavt rvltmkfrla
      421 grdtpalstl dgaahrkaad dlataavtvl rgkcggavtg pvsvtssggr ertrklltea
      481 ltaagvkvvp sggtvvhlvg ygdgakdlsa gaavtvamdt pyvlsgaksp tlmatysstr
      541 asmtglaavl agkarpagrs pvpvsglpat tcrt
//
LOCUS       WP_457605995             184 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457605995
VERSION     WP_457605995.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..184
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20293
     Region          29..180
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mttplqvtta rlripvtdrd hvrgpvdapv tiveygdfqc rfcgaaypnl aevlrqraev
       61 vrlayrhfpi tnvhpyaesa aetaeaaaar grfwemydwl yqhqdqldpv hlslgveqig
      121 lspeeiaaev grqeyadrvr qdfvggirsg vngtptlfvn dvrhdggydl aellavvdaa
      181 tddg
//
LOCUS       WP_457606002             391 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606002
VERSION     WP_457606002.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..391
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41692
     Region          3..390
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mradrpydlv lfgatgftgg ltadylarha pdrlrwalag rnpdklaavr drlaaidpal
       61 aelplltadv tdpaslrava esarvvattv gpyvhhgepl vaacaaagtd ylditgepef
      121 vdrmyvrhha eavrtgarlv hacgfdsiph dlgvwytvkq lpadgpiavd gyvraggrfs
      181 agtyhsalta fsrtgemsra ararramepg pdgrrvravp grvgrvrefg qwavplptid
      241 pqvvrrsaaa rpeygpdfry rhfaamkrlp tvlvagvgla gvvglvkvap trrwllgrla
      301 sgqgptaeqr arswfrvrfv gtgggrrvvt evaggdpgyd etakmlaesa lclafddlpe
      361 tagqvtpaaa mgdalldrlv ragitfrtls s
//
LOCUS       WP_457606004             317 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606004
VERSION     WP_457606004.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..317
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=32194
     Region          1..168
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mtgalllalt agmlgavnpc gfamlpayls llvagpgggr gavgraltat agltlgyvlv
       61 fgafglalap aadwlrprlp wltvtlgvll alagcwllag rklpaprplr aaprltrtwp
      121 smalfgaaya ltsltcaiap flaivvtslr agsplrglal fgayalgmal vvgvaalava
      181 llrgrvvarl rgagawvprl sglvllvagg yvawygwyev rlaqgrydaf tdpiirtaar
      241 iqqsvvsavd mlgpavlaal laalllavsr prslsrdlav garaegvkrt sdgpevqdrg
      301 raagaagtaa gervsag
//
LOCUS       WP_457606009             481 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-amylase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606009
VERSION     WP_457606009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 481)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..481
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52217
     Region          38..387
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(82..83,86..87,122,125,180..183,213,215..216,
                     218..219,241,243,248,304..305,310)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(124,185)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(215,241,305)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          394..479
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mhrrrcraaa lalglaasll vpltaaappa aaatpgakkv ivqlfewnwt svaaectstl
       61 gpkgygyvqv sppqehvnss pwwvsyqpvs yriesrkgtr aqfqsmvntc haagvkvivd
      121 avvnhmsgqe nggtgwagss yghynypgty ssadfhycgr ngnndianyn dryevqncel
      181 vnladlktes eyvrsrlaay lndllslgvd gfrldgskhm paadiaaika klnrsaylvq
      241 eviygagepi qpteytgngd vhefrygkdl armfnnerla ylknfgeswg ylssakavvf
      301 tdnhdtqrdg gvltyrdrgt yalanafmla wpygtpavms sftysgrdqg ppadgsnrit
      361 nvtcysgwec ehrwpvianm vgfrnatega gvsnwydngy qhiafsrtgk gyltindedg
      421 avngrsyytg lpagrycdvi hgtfsngscs gpvitvdssg wfaanvpahd aiaihigakl
      481 s
//
LOCUS       WP_457606011             296 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606011
VERSION     WP_457606011.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..296
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=31347
     Region          172..291
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlfdrfatrr ppgwliaala vplllvtall vgraltvtpe rqaappaaap sattaapsps
       61 pvesvppaap apddlpvvty dpaprgfppd pdpadtrpls eglrpnrnva aydapggrpl
      121 aflaptisgv rltvpivdrr sgwtavllps anrtiawlps ggwttvvlrd qivverrthr
      181 ltwsrdgram rtwpvslgms gqltplgrtf vlgrtpppea vyggvdifal gaipddpgav
      241 ptglrgahig lhswynddtl grnvtngcir ltrsaqrlll tevepgtafv vvdrlp
//
LOCUS       WP_457606027             309 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606027
VERSION     WP_457606027.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..309
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33506
     Region          2..232
                     /region_name="F420_Rv1855c"
                     /note="probable F420-dependent oxidoreductase, Rv1855c
                     family; TIGR03560"
                     /db_xref="CDD:274648"
ORIGIN      
        1 melriftepq qgatydqlla varraeetgf aaffrsdhyl kmgsvsgepg ptdawttlag
       61 lardttrirl gtlmtaatfr lpgplaitva qvdqmsggrv elgigtgwyt eehtaygipf
      121 pslgerfdrl eeqlavitgl wstpegstfd fpgtyypvsd spalpkpvqr prppillggm
      181 gpkrtprlaa ryadefnlpf asvedtvaqf grvrdacaai drdpstmtws nalvlccgrn
      241 eaevkrraea igrdpdelra ngaagtpaev vetlgryaea gssraylqvl dltdldhlel
      301 vaaevmpri
//
LOCUS       WP_457606038             194 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606038
VERSION     WP_457606038.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..194
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20824
     Region          22..193
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 msfplstpsa vpagtlttgp qptlstadgl vlrpwadeda pavlsayrdp eirrwhtrrp
       61 tspeqvlqwf ahsrrawqee tgaswavtrg devvgrmalg gfnlddgeag caywvvpaar
      121 gtgvasgalr alsawalgdg rlhrlwldhs tgnaascrva vkagfrlegt krsaavhddg
      181 rhdmhlharv rgdd
//
LOCUS       WP_457606048             224 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606048
VERSION     WP_457606048.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23855
     Region          6..188
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtatpvttvl fdfawtlfar dserwvgnaa asigrtlavg eahriagdfa ellrktatdp
       61 ahiardldpr vwdrailtvl eripgvdral asamhgthae aiepyadtva tlsalrdsgv
      121 rigvvsnvgw dirkcfarhg ldghvdafvl syevgfvkpd priwgaalea lhaapgqtlm
      181 vgdhptgdsg svsagilali lpmvespaqk rgfeyvlrla qvas
//
LOCUS       WP_457606054             711 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606054
VERSION     WP_457606054.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..711
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74782
     Region          14..696
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 maagrsrwta tliavavvlg wlivggiagp ysgklgevst ndnasflpad aeatraqdla
       61 ggfvdrettp alvvyerpgg ltptdqqriq adaarfaevp gvvgplpppv vsqdkqaaqv
      121 ivpidsaege qirsvverlr diagpdrdgl tvdvagpagl lgdlievfsa idgplllvtl
      181 tvvlvillvv yrspvlwifp llaagmsysl aavfvyllad hdivklngqa qgiltvlvfg
      241 agtdyallli aryreelhrh erpwdamrta wkgaapaiia sgatvivsll clllsslnsn
      301 ralgpvsavg iaatllvmlt flpallvlgg rwafwprrpr ydqadprteh giwgriagfv
      361 arrartvwvv tavvlaalai gvtqlgattl gqsqlftqrt dsvagqevid rhfpagtgsp
      421 atifttqdta rqvaqvaqgv pgvasvlplg ergenappdp nappkvvdgr vqlnvtlada
      481 pdsngaerti rdlreavhrv pgadaivggf tainvdtada svrdrdviip vvllviavil
      541 alllralvap vlliatvvls flatlglcal lfryvfdfpg vdqsfplfaf vflvalgidy
      601 niflmsrvre esvrrgtrag vlaglavtgg vitsagivla atfsalavlp lvvlvelgva
      661 vavgvlldti vvrsllvpal aydigpkiww pgrlsrshre gdragagvdr a
//
LOCUS       WP_457606052             411 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606052
VERSION     WP_457606052.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pawelek,P.D., Cheah,J., Coulombe,R., Macheroux,P., Ghisla,S. and
            Vrielink,A.
  TITLE     The structure of L-amino acid oxidase reveals the substrate
            trajectory into an enantiomerically conserved active site
  JOURNAL   EMBO J 19 (16), 4204-4215 (2000)
   PUBMED   10944103
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Weyler,W.
  TITLE     Monoamine oxidase A from human placenta and monoamine oxidase B
            from bovine liver both have one FAD per subunit
  JOURNAL   Biochem J 260 (3), 725-729 (1989)
   PUBMED   2764901
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12024463
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..411
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43478
     Region          24..405
                     /region_name="Amino_oxidase"
                     /note="Flavin containing amine oxidoreductase; pfam01593"
                     /db_xref="CDD:396255"
ORIGIN      
        1 mpdtdvvivg gglaglaaar rlhragvpwr lleagdrlgg rvatdrvdgf lldrgfqvln
       61 aayprltglv dvgtltmgwf tsgvlvrrgd rlerlvnplr eptgapgtlt agigsltdrl
      121 rfatlaagya tvpvgrlldt petsaetalr raglsdaiie ellrpflsgv lldrelatss
      181 hvlavimrsf argriglpad gmqalprala aplpaeliel ntpvtevapg rvrtpsgeit
      241 cravvvavdp paaatllpgl prvrmhaytt yyhrtdtapl depillldgd rremiantvv
      301 vsraaptyap dgqhlvatsv vgpqappepv irreldrlyg rstadwthlt tiavpdalpa
      361 apppqgrlrk pvalgdglyv agdhrdspsi qgalasgwrt vgavlaqlrr g
//
LOCUS       WP_457606057             336 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606057
VERSION     WP_457606057.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..336
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37837
     Region          4..318
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marpitlftg qwadlpfdev crlaaewgyd gleiacwgdh fevdkaladd syverkratl
       61 akhnlqvfai snhlvgqavc dhpiderhqd ilpariwgdg epegvrqraa eeikdtaraa
      121 aklgvntvvg ftgssiwhtv amfppvppam iergyqdfad rwnpildvfe evgvrfahev
      181 hpseiaydyw ttkrtleaig hreafglnwd pshfvwqeld pvnfifdfad riyhvdckda
      241 kvrtgdgrrg rlsshlpwad lrrgwdfvst ghgdvpwedc fralnaigyd gpisieweda
      301 gmdrlvgape alqfvrrlaf daptaafdaa fsssrd
//
LOCUS       WP_457606062             464 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606062
VERSION     WP_457606062.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..464
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50126
     Region          3..449
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msrrlvvldv vgltprllah mprlravaea gfaaelgtvl pavtcsaqst fltgeppsgh
       61 gvvgngwyfr dlgevllwrq hnalvggekv wqaarrvepg yrvanvcwwy amgadvdwtv
      121 tprpvyhadg rkepdcwtdp pelrdtltda lgtfplfsyw gpgaglpssa wisraaqril
      181 tdhapdltlv ylphldydlq rfgpsdpraa aaaadldgvl gplldvareq gatvlalsey
      241 gitdvsrpvd vnrmlraegl lrvytqagme yldpwtsraf avadhqvahv yvrdpadvpa
      301 vaklcaslpg vaevldaagq agygldhprs gelvlvaepd awftyyywld darapdfarl
      361 vdihrkpgyd paelffdpaa pggakrraav alarkklglr ylmtvvglda garavrgshg
      421 rlpadpadgp vlicsdraai rprveatdvk alllelagla reap
//
LOCUS       WP_457606068             291 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606068
VERSION     WP_457606068.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..291
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30587
     Region          13..284
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtaagplpgp galrfgygtn gfanhrlgda lavlaelgyq gvaltldhdh ldpfapglpr
       61 rvaavrrrld alglavvvet garylldpwh khaptllhdd aahrveflrr avrigadlga
      121 eavsfwagvr ppgvppdvaa drlvagcatv caeaaeagvp lgfepepgml vediagwrrl
      181 raalgappgf gitldighcr cleplpvpqc vsevaahlvt vqiddmrrgv hehlefgtge
      241 idfppvlral adagyrglva velprhshaa pavaarsldf lraaasrgeg r
//
LOCUS       WP_457606071             526 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606071
VERSION     WP_457606071.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 526)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..526
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=56634
     Region          23..519
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mseigqsear plveapadav agevvlrltd vvktfpgvra ldgvqlevra gevhcllgqn
       61 gagkstlikv lagvhrpdsg evlwrgepas fanpqaamra giatiyqeld lvddlsvaen
      121 aflgheprrf gfvrrghmar rtrqilarlg hpeippgrlv rhlpaagkqi vsmaralshe
      181 arliimdeps avlahdevan lfriirelta qdiaviyish rmeeireigd rvtvlkdgrt
      241 taaslparet ptrdlvarmt grtieyvfpq rpadhgggae llrvdgltrp gefadvslgv
      301 rageivgiag lvgsgrsell etifgarrah agtvrvngrt lrpgsvgaav ragmgmapee
      361 rksqalllge piyrnvtlat fsryarlgft dtgreraead riaaslelrp rdvrrpvrtl
      421 sggnqqkvvv grwllgdtrl llldeptrgv dvgaraelyq virdlaargv gvllvssevp
      481 evlgladrvl vmregrvvre apageldent vldlvmagsl megapa
//
LOCUS       WP_457606073             363 aa            linear   BCT 27-JAN-2026
DEFINITION  YihY/virulence factor BrkB family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606073
VERSION     WP_457606073.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38819
     Region          60..340
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 maarddahdv hedtrdgrdd apamrddtra grdrpdgrkh agpvgpddgp dspadlsatg
       61 wmatlkrtvr efqddsltdw aaaltyygvl sifpgvlvli svlgllgdra tegvrdtvgq
      121 avpeenirri iesaidqagq sgglasiaai vglvaafwsa sgyvaafmra snsiydvpeg
      181 rpiwktlpvr lgvtavigvm llisavivvf tgglaeqagn aiglgetavt vwniakwpvl
      241 lvlvslmfai lywaspnarh ggfrwvspgg vlavvlwlvv sglfalyvsn fgsynktyga
      301 vasviiflvw lwlsniaill gaefdaeler sraiaaghpa deepyvelrd drklrkkgra
      361 psr
//
LOCUS       WP_457606075             778 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606075
VERSION     WP_457606075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Shu,C.J., Ulrich,L.E. and Zhulin,I.B.
  TITLE     The NIT domain: a predicted nitrate-responsive module in bacterial
            sensory receptors
  JOURNAL   Trends Biochem Sci 28 (3), 121-124 (2003)
   PUBMED   12633990
REFERENCE   2  (residues 1 to 778)
  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 778)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20592222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..778
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=82252
     Region          75..308
                     /region_name="NIT"
                     /note="Nitrate and nitrite sensing; pfam08376"
                     /db_xref="CDD:462453"
     Region          411..635
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mplphparvr rhhrsadrtg rlrsvrvqll apilvatagl vvlgaaqtga aldasadadr
       61 arvlagtata tvrlvheler elgetaalrq rggtsgrplv daqrrrvdta veryrsaqdd
      121 arraapdlgg vlddvggrla qlaptrdlal agdrgdpayv slvesllava dalpsqlrda
      181 elanqareva avaaqehlsa lerdllravf vrgglqsgel arlgrlrgar eqrqaeflri
      241 asapassawy rlvdgtdvtt arrirdavld sdgapgtvkt dgdawyvaqs gairrynllg
      301 rdltdrldrd aadlagaarl ravltagats tvalgslvta vllavrtsrr lrrlrvaalt
      361 manrelperi taiaagertp aegpatrmtd girrgrdeva qvaeafdtvn raalrlagqq
      421 aelrldvtrm aealarrirt litrqlrlld dfereetdpd alarlfaldh laarlrrnge
      481 nllvlaggep grghegalll ddvvraaase iedyprveid vptaavhgta agnlvhllae
      541 llenatvysp peapvlvdgr rtvdglvlrv rdqgigvses rlteinerla apatlssaaa
      601 gsmglhvvah laarhgirvq lhnpgtgtva qvdvpesvlt rvesvasrpa aerrpraaaw
      661 fksgpaagrs lvtsattvgp argvaavrtp ggallapsta rirpvsvppt pvpttaaglp
      721 rrqvgghlpe pmpdttappp atdlldpevv rarlsalaeg vasatrrapn ttpngrrp
//
LOCUS       WP_457606078             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606078
VERSION     WP_457606078.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19834
     Region          1..176
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mfatdrvrlr tptpddapdl frlnadpelh litddgpflp qhvgqvrarl ekrageqpda
       61 gaavsllaet vadgtflgtg vlwgidtfsr lahlgitllp eargqgygte virllcrygf
      121 rnrnlrrlei etlaantamr rtaercgfvh egtqrergyd gdgfgdmviy gllrrdwtp
//
LOCUS       WP_457606084             124 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606084
VERSION     WP_457606084.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Daines,D.A., Wu,M.H. and Yuan,S.Y.
  TITLE     VapC-1 of nontypeable Haemophilus influenzae is a ribonuclease
  JOURNAL   J Bacteriol 189 (14), 5041-5048 (2007)
   PUBMED   17496075
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..124
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=13723
     Region          4..122
                     /region_name="PIN_Sll0205-like"
                     /note="VapC-like PIN domain of Sll0205 protein and
                     homologs; cd09872"
                     /db_xref="CDD:350220"
ORIGIN      
        1 mtllldthva lwaitgdatl gvefldrlrh dpdvflspvs lweitvkqqa gklsgppdla
       61 ervrdmgfre lpvthdhait agrlpphhrd pfdrmlvaqa itenltlatr dasiplyevd
      121 vlkv
//
LOCUS       WP_457606108             487 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606108
VERSION     WP_457606108.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  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 487)
  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 10612637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..487
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=54359
     Region          23..158
                     /region_name="HATPase_c_3"
                     /note="Histidine kinase-, DNA gyrase B-, and HSP90-like
                     ATPase; pfam13589"
                     /db_xref="CDD:433332"
     Site            order(29,33,36,56,58,60,62,92..95,108,110,119)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340391"
     Site            order(69,95)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340391"
ORIGIN      
        1 mneeelppep qlmeslravg ysleaavadl idnsitaqan rvevffsaea epylaivddg
       61 tgmnadeara amclagtsaa rsrrpddlgr fglglktasl sqcreltlvt krdgvvtalr
      121 wdldyltrsr rwalltlsea easilpryge ieanpsgtlv vwrhfdrlps asqaifakaf
      181 neqmlsarah lslvfhrfls gedgkpkvtm alngvrlkvv dpfltahrat qrgpaeslav
      241 agaeidvqpf tlpyiskltq aeketaqiag rlrdsqgfyi yrarrlviwg twfrlvpkdd
      301 lgklarvrvd ipntldhlws ldikksaavp pteirdqlkr lvdrivhpsq raqlyrgrps
      361 aasdrvvrmw nlidergsfr yelnrehpll aaldeqldng arrllsellr niessfpved
      421 aynrlggdnv hapqhsdege lldyaatlws vfsqtgesad dfvarlryve pftlsknpea
      481 llrraas
//
LOCUS       WP_457606113             499 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606113
VERSION     WP_457606113.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..499
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51696
     Region          19..499
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mssvlsavvq prlsrpswls pkvfrtevla glvvalalip eaisfsilag vdprvglfas
       61 ftmavtiaic ggrpamisaa tgaialvvap larehgldyl iaavilggai qillaalgva
      121 klmrfiprsv mvgfvnalai lifaaqiphl lgvpwlvypl vavalaimvg lprltravpa
      181 plvaivvltv vtvvagvavp tvgdegalpd slptlglpqi pwtmdtltlv apyavgialv
      241 glmeslmtak lvdditdtps nktreswgqg vanivtgffg gmggcamigq tminvkasga
      301 rtrlstflag vfllvlvval gdvvavipma alvavmiiva vstfdwhsvt patlkrmpyg
      361 etivmlatvg ttlathnlai gvvagvlaam vifarrvahl vevtsvldpd gttriysvhg
      421 elffassndl vgqfdyandp dtvvidmtha hvwdassvaa ldaittkyaa rgkaveiiel
      481 nqpsarihds lagqlgvgh
//
LOCUS       WP_457606118             350 aa            linear   BCT 27-JAN-2026
DEFINITION  sporulation protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606118
VERSION     WP_457606118.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Sonoda,Y., Mizutani,K. and Mikami,B.
  TITLE     Structure of Spo0M, a sporulation-control protein from Bacillus
            subtilis
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 12), 1488-1497 (2015)
   PUBMED   26625291
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Han,W.D., Kawamoto,S., Hosoya,Y., Fujita,M., Sadaie,Y., Suzuki,K.,
            Ohashi,Y., Kawamura,F. and Ochi,K.
  TITLE     A novel sporulation-control gene (spo0M) of Bacillus subtilis with
            a sigmaH-regulated promoter
  JOURNAL   Gene 217 (1-2), 31-40 (1998)
   PUBMED   9795118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..350
                     /product="sporulation protein"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /calculated_mol_wt=37301
     Region          1..256
                     /region_name="Spo0M"
                     /note="Stage 0 sporulation-control protein Spo0M [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG4326"
                     /db_xref="CDD:443467"
ORIGIN      
        1 mvfkkmlgaf gvggpsvdtv lsnpstrpgl mlggqvnltg gshdveidhi tvglvtrvei
       61 dgaeeeydal vefhrvqvag glrlregqql slpfqvampw etpvtdlygq nlhgmtmglr
      121 tevairsaid kgdldpvyvh plpvqerile afgrlgfgfk gadlerghis glhqslpfyq
      181 eieyyaapqy ahgvnevelt fvanehgvdv vlefdkrggl ftgghdsygr yhaahadadr
      241 vdwaaqvdtw vrqaldgyqs lhaghgyapp aqgygapgyp ppppgyghaa yghpgghyke
      301 ehhqerhggp gmgavaagvv ggaalgfagg mvadevfdsf gedeggdeea
//
LOCUS       WP_457606123             165 aa            linear   BCT 27-JAN-2026
DEFINITION  TspO/MBR family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606123
VERSION     WP_457606123.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Campanella,M. and Turkheimer,F.E.
  TITLE     TSPO: functions and applications of a mitochondrial stress response
            pathway
  JOURNAL   Biochem Soc Trans 43 (4), 593-594 (2015)
   PUBMED   26551698
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..165
                     /product="TspO/MBR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=16997
     Region          31..155
                     /region_name="TspO"
                     /note="Tryptophan-rich sensory protein TspO/CrtK
                     (mitochondrial benzodiazepine receptor homolog) [Signal
                     transduction mechanisms]; COG3476"
                     /db_xref="CDD:442699"
     Site            order(48..49,51..52,92,140,143..144,147)
                     /site_type="lipid-binding"
                     /note="lipid binding site [chemical binding]"
                     /db_xref="CDD:320706"
ORIGIN      
        1 mrvptlvkta aavtataaag aaatstgass rwyrrlrkpa wqppsaafpv vwtplyglia
       61 iagaraldrs egperaafar gyalnlalna gwtalffgar rpgaalaeia alntsnlvll
      121 rraartdraa gaalapyvaw tlfatalnga ivglnrggag lrrrs
//
LOCUS       WP_457606127             236 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606127
VERSION     WP_457606127.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  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 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   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   4  (residues 1 to 236)
  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 236)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24501
     Region          25..235
                     /region_name="DppF"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1124"
                     /db_xref="CDD:440741"
ORIGIN      
        1 mtltvsgptd aaargaapaa glaahqvsva ygrqrvldrv dlhiapgetv glrgpsgsgk
       61 stlarvlall hapdgghvti dgqplggvrh rlpahvrtrv ailfqspraa tdprlsladi
      121 iaeplratgt sreqaaarta eladlaglta dlltrrphav sdgqlqracl aralvhrpdy
      181 llcdeataml dastqahvaa vigdyqrrqg agvlvithdp almarwatrv vdlpaa
//
LOCUS       WP_457606129             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606129
VERSION     WP_457606129.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33496
     Region          6..317
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtapalltvd gltvrfrlrd avvhavtdls ltlrpgella vvgesgcgks vlahsllgll
       61 prnaavtgha rlhaagreav dligagerhl arhvrgrgvg lvpqspatal tpvrtgrkll
      121 eetlrahght rrdapaaadr iaadvgldpa dlnryphels ggmaqrlata lalapdppvl
      181 ladepttgld rplvdhtldl lrrrcdtgaa vllithdlaa arrvadtvav myasrivehr
      241 paevlfddpa hpytagllda lpdrafvpvp ghppaltdlp ggcafaprca ratdtcatvp
      301 claaasrvac hhplreevpa
//
LOCUS       WP_457606145             251 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM-dependent methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606145
VERSION     WP_457606145.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..251
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27846
     Region          <27..144
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtspdlprqf tiregelril npfddvklat lgrairlrpg delldlcsgk gellctward
       61 hgitgtgvdi stvftaaare raaglgvadr vrfvhgdaaa yiperpvdva acvgatwigg
      121 gvpgtlellg ralrpggmal vgepywrrep pddeavtgsh arsrdefrdl pglveqfgec
      181 gwdlvemvla dqdswdryaa ahwlnlrrwl danpddelap elrreltedp vryvrfqrey
      241 lgwgvfallr r
//
LOCUS       WP_457606152             416 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606152
VERSION     WP_457606152.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..416
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44971
     Region          2..412
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtspavedll rtlapqvlgv lvrrhgqfsa cedavqeall aaalqwpeqg lpdhprswlv
       61 tvatrrltde wrseharrer evavavrqpa yaavappade eppsgddtlk llflcchpal
      121 pvsgqvaltl ravgglttae iaraylapea tmsqrirrak qrieasgarf tlpspadrde
      181 rlaavlrvly lifnegytas sgealrrael tgeairltre lrrllpddge vagllalmll
      241 tdshraartg pdgelvplae qdrsrwdrda vaegvalvte altwsapgpy qvqaaiaavh
      301 aeaptaedtd wrqivalyrv larvapnpmv tlnqavavam vdgpraglal latldgddrt
      361 aghhrlaavr ahlldlagdr aearaaylaa arattslper rylevraarl tgdrpr
//
LOCUS       WP_457606166             202 aa            linear   BCT 27-JAN-2026
DEFINITION  C39 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606166
VERSION     WP_457606166.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Kanonenberg,K., Schwarz,C.K. and Schmitt,L.
  TITLE     Type I secretion systems - a story of appendices
  JOURNAL   Res Microbiol 164 (6), 596-604 (2013)
   PUBMED   23541474
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Lecher,J., Stoldt,M., Schwarz,C.K., Smits,S.H., Schmitt,L. and
            Willbold,D.
  TITLE     1H, 15N and 13C resonance assignment of the N-terminal C39
            peptidase-like domain of the ABC transporter Haemolysin B (HlyB)
  JOURNAL   Biomol NMR Assign 5 (2), 199-201 (2011)
   PUBMED   21347827
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Schwarz,C.K., Tschapek,B., Jumpertz,T., Jenewein,S., Lecher,J.,
            Willbold,D., Panjikar,S., Holland,I.B., Smits,S.H. and Schmitt,L.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            an oligomeric species of a refolded C39 peptidase-like domain of
            the Escherichia coli ABC transporter haemolysin B
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 5), 630-633
            (2011)
   PUBMED   21543878
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10609171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..202
                     /product="C39 family peptidase"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=21559
     Region          42..176
                     /region_name="Peptidase_C39_2"
                     /note="Peptidase_C39 like family; pfam13529"
                     /db_xref="CDD:379241"
ORIGIN      
        1 mnpiirkcvl svaglaaagg avagpaaaha apvkgkgdra adyeyqaqpn yfycgpastr
       61 ialsaegrdv sqdelatklg ttengtdsai ditrvlneyt ggkyktteir ddvatrdqie
      121 rlradirtav dddrpvvani lggardidgv ehsypghyvt vvryegdgdr vliadparpd
      181 eptywmdvte lanwiagrgy ss
//
LOCUS       WP_457606170             217 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606170
VERSION     WP_457606170.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..217
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22399
     Region          2..195
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrevsvpvvd gglvgdvvvp aeaqgvvlfa hgsgssrhsp rnmavgraln erglatmlvd
       61 lltadeeard eitaelrfdi gmlaerlagi vdwmgadpel grlpiglfga stgaaaalva
      121 aaarpdrvga vvsrggrpdl agssltavra ptlllvggld eqvialneqa rdalgevael
      181 rivpgathlf eepgtleqva dqagtwftth lrqphpa
//
LOCUS       WP_457606168             365 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606168
VERSION     WP_457606168.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..365
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37977
     Region          <112..362
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdddvgitgr aptagprqtw aglpwpvrta vtwsacllvv taglwllgqi avllaplava
       61 lagtlflaal ldpvlvrlrr lrvpaglaal lsillllgil ggagvlvwnl tasqfgelsq
      121 qldeglqrtr dfvtsslpvt dqqldrlveq irqglssgap dpvagarkva evagavllal
      181 vllffllkdg rsmwrwvlrr ltgprrelta eagragwrtl gaysrgtmii aaidaigigl
      241 alvvlrvpla lplalitflg gfvpiigatv agavavlval aangpttall tlaaviavqq
      301 iegnlleplv mrrqvqlhpa vilvvvtagt lvagvagafv svpiaavlwr vldtvqrhra
      361 aeaag
//
LOCUS       WP_457606173             791 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606173
VERSION     WP_457606173.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 791)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..791
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88791
     Region          9..764
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mireraypve pwhvremqld mdvlaqsesv falsnghigl rgnldegeph glpgtylnsf
       61 yelrplpyae agfgfpesgq tivnvmngkl irllvddepl dvrygellah ervldmragt
      121 lqrdlhwrsp agrevkvrtt rlvsftqrsv aaihyevepv dgplrlilqs elvaneslpp
      181 qsrdprvaav lesplqaeee lttddggqli hrtkvsglrv aaamghdveg perttieseg
      241 yedwvrttig cvlkpgqtlr vvkyltygws srrslpalrd qvgaalaaar ldgwdglrra
      301 qreyldafwd aadvrvegdp evqqavrfgl fhvlqagara errpisakgl tgpgydghaf
      361 wdtemfvlpv ltytqpsavr dalqwrydtm aqaqerartl nlegaafpwr tiegpessay
      421 wpagtaafhi aadvadalrr yvlvtgdeal ereiglellv etarlwrslg hhdragrfhi
      481 dgvtgpdeyt avkndnvytn lmaqrnlrta adcamryrdq aldlgvteee aaawrdaand
      541 mhvpydaetd vheqvegftr fqewdfehtp pekyplllhy pyfdlyrkqv vkqadlvlam
      601 hwrgdafsaa eklrnfvyye rrtvrdssls actqavlaae vgylelahry mreaalmdlh
      661 dlnentrdgv hmaslagawi alvagfgglr dhdgmlsfap rlssrlsrle fslqwhgmrl
      721 rvdvrphqtt yslrnggpdt vvelrhhgep lrvtsarpvt vavpppahps gpqpeqpqgr
      781 aplmhlpert d
//
LOCUS       WP_457606175             250 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606175
VERSION     WP_457606175.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..250
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26049
     Region          10..243
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlglpahvsa clfdldgvlt qtakvhnaaw aetfdaylrr rsaetgepfh pfdtgpdynr
       61 yvdgrpradg vrtflasrgi tlpegspddp peadtvnglg nrknvvllqq ieqhgveaye
      121 gsvryleaat taglrravvs asancaavvh aagldrwlea rvdgvvaran glrgkpapdt
      181 flegarllgv epsqaavfed alagvaagra ggfgyvvgvd rvgqadella hgadvvvtdl
      241 adllaaepaa
//
LOCUS       WP_457606182             437 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606182
VERSION     WP_457606182.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..437
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47108
     Region          1..347
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvalkdvt kvfpdgtvav dtinldvndg efmvllgpsg cgkstvlrmv agledpssga
       61 imlggeland lpprdrkiam vfqdfalyph mtvgdnigfp lrlsgvepgp rgeriqdvas
      121 algigdvlgr kpsqlsggqr qrvamgraiv rrpglflmde plsnldsglr aelraeisgl
      181 trelgvttiy vthdqaealt madrvaimrk gvlqdvgtpt qvygrpatly vaaflgsprm
      241 nlleasvyvh ldryvalnlg eqslylpwdd irsravahyh gerivvgmra ealtpvapdt
      301 agdvlhgrir ylehhghesl afldigatai vvdemgtpve qaapgqrglr rfnqvmqrlt
      361 gratessaps pevgggggnr tsvlpdpgrh hrrpaelavr lapypqvspg hplavqvrmd
      421 alhffdergd ridvgwr
//
LOCUS       WP_457606184             727 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606184
VERSION     WP_457606184.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..727
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=82509
     Region          1..214
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          367..723
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mtlisfvvpa fkvqgylrec ldsildqpfg dievigvdda spddsgeila eyalrdprvr
       61 pvrlaenvgl gparnigldr avgeyvwfvd gddwlvpgcl phvadrlrdt apdvlivdhv
      121 rahwnnigtr samrdvfpdp pgattftlrd rletlkllht awnrvvrref lierglrfep
      181 gwyedvsfsy palmaagrig vldriclnyr qrrtgaitkt rgdrhvevfa qwhrvfglmd
      241 rwrvtglrpa vfermiwhyl tvlgngdria pelrapffaq mhadyvrflp pegypvppgp
      301 eglkhrlvaa grwrtfsalr eahqagetar rtarrarrrv apvvrrtarl ardlalgeyy
      361 raelhrpidp tlavyaaywy rgyscnpaai yeaarrlapq vrgvwivrrd rvatlppgve
      421 yvvagsreyh rvlararwlv nnvnfpdfvr krpgsvhvqt hhgtpvkvmg ldqqrypvga
      481 mgmnfagllr rvdrwdysit snsfstqmwe raypadyttl evgyprndrl alataedrgq
      541 vraalgiapd eyvvlyapth rehlpgwrpp fdpdrmldvl gprgrllmrs hyfhdrerhp
      601 rgpaaggvld vsayervedl ylaadvlvtd yssamfdyav ldrpivvyap dwdayrvarg
      661 vyfdllaepp gtvaldfpgl ldvfrsgavd deaaesaraa frsrfcaldd ghaaervvrr
      721 vflgetp
//
LOCUS       WP_457606190             200 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606190
VERSION     WP_457606190.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..200
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22690
     Region          19..194
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mefaevvrrr rmvrnydpdr pvppevvdrl ldhavrapsa gfsqgwgflv leepedrerf
       61 waattpgggg rerwlagmrr aplivvphan rdayldryae adkgwadrae drwrvpywyv
      121 dtgfaallml ltavdeglga cffgippqri gayreafgvp pelhpigait vgyravdhrs
      181 pslrrgrrpv qdvvrrgrwt
//
LOCUS       WP_457606192             430 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606192
VERSION     WP_457606192.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44729
     Region          27..379
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(37..38,41..42,45,77,132..133,135..137,140,160,
                     163..164,167,248,251..252,255..257,260,283,287,340..341,
                     345,349,365,368..369,372..373,376)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtdvtqarrr garrwaidlr plrvpayrrv wtgnaiamfg fqftavavpv emfdltggsl
       61 wvgllgiagf vplllfglwg gavadardrr rvllvggcvl wastlgllvq slagvrspll
      121 llllvalqst afaitspars ailprlvpae lvpaattlnf ttftaaavfg plaaglifaa
      181 wqvevalpia yaadallyta alwatlrlpa mpptpdpdgg vrkagfasiv dgfrylattr
      241 vlllsfaidl iamilampra lfpelaqerf ggasavgwly ssiaigamlg gltsgwigrv
      301 rrqglaltva vvgwgvaial aglagqlwva vvllgvagaa dlvsatlrqs mllvyapdrm
      361 rgrlqgvntv vvaggprlgd lragataaaf gtgfamvggg laaavlaval vvafpallry
      421 rsttpaeerh
//
LOCUS       WP_457606204             433 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Nitratifractor sp.].
ACCESSION   WP_457606204
VERSION     WP_457606204.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..433
                     /product="tetratricopeptide repeat protein"
                     /calculated_mol_wt=50407
     Region          <90..416
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          135..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(136,139..140,143..144,146,170,173..174,177..178,
                     180..181,204,208..209,212..213,216)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          168..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          203..232
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msrnpvihal wavlltmgva gkpvmqklpg edslivrall aeergdypks eallltlydk
       61 tgkveyllha aretmvqgtl yaevvdrlea wlrkhrkkhk dlrpsrvlaa lyardgepdr
      121 alkiarnwls rsedpedlkl laslliskrr yteaskllek ayekskdpel llrnvalmek
      181 ylgrrqqair llethlrmnr esplglyfgl ielyakekrf dkvleiykkl yerdprevvl
      241 kkivqlslyl kdfdglekfl aahpgneell yllykrsgrf dkaialaqrr yeetrrpkwl
      301 aeeailtyeg pkkekkltpe vlkrfrelfd ralkegadds lylnyygytl idhdldidrg
      361 ialvrkaleq qpdnayylds lawglykkge ctqaykvmkr vfdggapeep eirdhyraie
      421 acmkrqsnnq egk
//
LOCUS       WP_457606205             327 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606205
VERSION     WP_457606205.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..327
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34495
     Region          4..325
                     /region_name="MDR1"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08267"
                     /db_xref="CDD:176228"
     Site            order(40..42,45,131,135,156..159,161..162,180..181,184,
                     199,217..218,239..240,273..275)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176228"
ORIGIN      
        1 mkaivqdryg ppetlvladv etpapgpgdv lvrveaaaln aydwhvmrgd prlsrlalgl
       61 arprarirgr dvagrveavg tqvrhvrpgd avfgdlgead gafaeyvcvp ehlaaprpan
      121 ltpaqaaalp lagvtalqgl rdagqvrpgh hvlingasgg vgtlavqlak algatvtgvc
      181 rtrnvdlvrs lgadhvvdyt redftrdgrr hdvvfdlvgn rsltalrral tpdgtlvlsg
      241 ggvyrggsll gpigllargr llapvisqrv vvlatspgra hldvlrehae agrltpvvdr
      301 thplrevpea vryletehar akvviti
//
LOCUS       WP_457606213             291 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606213
VERSION     WP_457606213.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..291
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..291
                     /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=30409
     Region          99..155
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          177..285
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(241..242,245,258..261,263)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mqrvrflara aalavvvlvg vgacaldpqa egaggstpgp vgltegasga sasptpeqpv
       61 tspsaqpsrt aspkpsrspe atkttkpkpk psasagcpqg ehqravetyl trlggfgtlt
      121 vdgeqsatdc aaikkfqiry gispssgrag pttydvakrl aatdtarcra gsrltfcvdl
      181 trqtvwamrg gkvvmgptvt rtgmsgyatp agtysvgrkn prewsnpyev wlpywqqfng
      241 gigfhettty lhngaigshg cvnllhrdav rlwelgsvgt rvvvigrrpg t
//
LOCUS       WP_457606234             386 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 9 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606234
VERSION     WP_457606234.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 386)
  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 386)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..386
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40115
     Region          28..379
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtspssdsds prrdlgpsal gpvgervpdv eriavlrana lgdfifvlpa ldalrsayps
       61 aeivllgapw haalwrdrpg pvdrvlvvpa apgirdpgpg espgdvpafl aaaraerfdl
      121 alqvhggggn snpfvaglga rvtaglraeg appldrwlry vyyqheviry levaalvgap
      181 attitpalav taadraeava vlgeptrprv alhpgatdtr rrwpperfge vareltgdgy
      241 evlvtgtpae qetvdavvaa agvpvrpqvg tlslgalaaa yadcalvvsn dtgplhlaaa
      301 vgaptvgvfw vgnlingasp lrgrhrpiaa wtthcpvcgv dctpgiyphr pgdgecphrv
      361 sfvadvpvae vveaarellt pqpatr
//
LOCUS       WP_457606237             724 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606237
VERSION     WP_457606237.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..724
                     /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=77104
     Region          33..393
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          475..709
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mtsppltkva dregspseep ggtattrepg reatpsrfra dvaglravav glvllyhagl
       61 pfipggfvgv dvffvisgfl itgqliseie rsgrvslvgf yarrakrilp aatvvlaata
      121 vavrlfvprs ewqvvggdia aaatyivnwr ladravdyla edvapspvqh fwslaveeqf
      181 yllwpllivl ailaarklrr anvrpalwvg lavlavpsfv wsiietadsp qraffvsttr
      241 lwelgvgaai allavraarm prsvavvlgw lglaaivaaa llvsgktawp gyaaalptlg
      301 aaaviaagaa agsrgpvmvl gtrpfqwigd lsyslylwhw pmlvvaaahf gdlsltegll
      361 valasvipaw itfrlvenpl rysrkistsp rlalslggnf tlagicagmv lvlmgawaaa
      421 atttkgqyap gaallstapg tapigpvper fdvikpdplq irqgfmdvpd tnrdkcfqqv
      481 dgaevlscty gnpnaattva lvgdskmdqw lpafqvlaeq ndwkiliaak ascpftsapa
      541 vraddpskly tdcidwnrsl mrklveerpd ylvtsqgaar afdsdakept veamvagvrs
      601 awkkldavgt qvvvlannpg pgpavtcadk nrkrlsrcaf drerhdqdpa yrmqrqavsg
      661 apkvkmidlf davcptdrcp vvfgnvliyr ggshigaayv kttaphlara lsdvgvparf
      721 spag
//
LOCUS       WP_457606263             160 aa            linear   BCT 27-JAN-2026
DEFINITION  very short patch repair endonuclease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606263
VERSION     WP_457606263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Tsutakawa,S.E. and Morikawa,K.
  TITLE     The structural basis of damaged DNA recognition and endonucleolytic
            cleavage for very short patch repair endonuclease
  JOURNAL   Nucleic Acids Res 29 (18), 3775-3783 (2001)
   PUBMED   11557809
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Tsutakawa,S.E., Jingami,H. and Morikawa,K.
  TITLE     Recognition of a TG mismatch: the crystal structure of very short
            patch repair endonuclease in complex with a DNA duplex
  JOURNAL   Cell 99 (6), 615-623 (1999)
   PUBMED   10612397
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Tsutakawa,S.E., Muto,T., Kawate,T., Jingami,H., Kunishima,N.,
            Ariyoshi,M., Kohda,D., Nakagawa,M. and Morikawa,K.
  TITLE     Crystallographic and functional studies of very short patch repair
            endonuclease
  JOURNAL   Mol Cell 3 (5), 621-628 (1999)
   PUBMED   10360178
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..160
                     /product="very short patch repair endonuclease"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006298 - mismatch repair [Evidence IEA]"
                     /calculated_mol_wt=17812
     Region          1..130
                     /region_name="Vsr"
                     /note="G:T-mismatch repair DNA endonuclease Vsr, very
                     short patch repair protein [Replication, recombination and
                     repair]; COG3727"
                     /db_xref="CDD:442941"
ORIGIN      
        1 mawvttaqgs hlrgrrtrdt apeialrrav halglrfrlg rtlfnrcrpd lvfpgpavav
       61 fvngcfwhgc pqhgpsqfrg pnadkwetki amnrardqrv dnelgaagwh vvrvwecevr
      121 rdvveaarrv gvevrgrscv atdrrisvar taagqqltah
//
LOCUS       WP_457606265             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ion transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606265
VERSION     WP_457606265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..336
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37305
     Region          55..272
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mqcrhgypps pvrrpdpasr rqaligdtvp aprggrrtsd gkrgpaghca rivasrpfev
       61 aivvlimang vvlgietypn lgaagpvlrw tewmfravfv veitirvlay grrpqdffrh
      121 gwnvfdllvt aaifvpglhg dsavlrfvrv arvlrlvrfs pglrtivaal wrslpgvagf
      181 lalaavtlyv ygmagwlifg drypeqygdi grslvtlfvl lsletlpdll eqglevspwt
      241 llyyvsfvmi avnlllnili avivnsmeea rrlemtegla sdydsdgdgv pdevdriais
      301 qrlddlrmvi aelerelrid reeppgaprr rqpsdh
//
LOCUS       WP_457606285             294 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606285
VERSION     WP_457606285.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..294
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31270
     Region          14..293
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mvnpvpadet havgvaalir qrlgecspae rrvarallas ypsaglgtva alaeradvsa
       61 ptvlrflsrl gfggypefqr alrdelaere tspltayrat ersgapphga lsraaaalpe
      121 avagtladlp qgeldaavrl ladqqyrita aggrfsalfa nylvlhlmqv rgnsrllpag
      181 pveradmlvd vgrrdlvvlf dfrryeeptl alarevtgrg arvvlftdrw lspvaglaev
      241 vlparvdsps pydsfvptla lvetlvaali drlgpmagar lkamegaqqa fgvr
//
LOCUS       WP_457606302             543 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606302
VERSION     WP_457606302.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   2  (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   3  (residues 1 to 543)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..543
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56800
     Region          1..525
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mitfdrvtvh yaeggppplr dvtlrveege lclvagrtga gkstllrain glvphftggt
       61 lhgavtidgr dtrthpprdl advvgvvgqd plagfvtdtv eeelaygmeq lalspavmrk
      121 rveetldllg iadlrdrplr tlsggqqqrv aigavltahp rvlvldepts aldptaaedv
      181 latvtrlvhd lgvtvvlaeh rlervlqyad rllylpgdgr vhdgtpatal thidiappli
      241 elgrlagwtp lplsvrdarr rasglrhrla gvapppvpag adtgptltar kivvrypgtv
      301 avagvdldlr agrvvalmgr ngsgkssllw avqgsgprhg gtvavtgseg tadpkalpag
      361 qarrhvglvp qnsgdllyle tvdaecaqad retgvpagtc ralvdqlvpg lpgdrhprdl
      421 segqrlalal avqltaappv vlldeptrgl dyhakrqfaa vvrmlagsgr avvvathdve
      481 lvatladrvi vmaegeivsd gttaevmlas pafapqvaki lapapwltve qvaaaltptr
      541 apa
//
LOCUS       WP_457606314             191 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606314
VERSION     WP_457606314.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 191)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..191
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20803
     Region          43..>185
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mstrartrap avrprgprpt agyrvfqvvn avvltgvvvv tlypfltiva rslsdnayiv
       61 agevnlvprg fnltayrvvt sdptfwisyr ntvfytvvat lisvvlttcy ayvlskkhlr
      121 grtalvgiav ftmfftggli pnyvlvtslg lkntvwaial pnainvfnll vmkaffeslp
      181 veleepppst g
//
LOCUS       WP_457606328             208 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606328
VERSION     WP_457606328.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..208
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22214
     Region          <76..176
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mtterprgsr lprvllivgv lavlaavaav vvplvrppgp rpdfqlpvac getwrlstyp
       61 ghddydidlf ptsgeawgrp vlasadgtvt vagingslgg rtpqdpdgpr grgggywvki
      121 dhggkwetqy lhlleppsvq agqrvargdq lgrvgstgns gaphlhyeqr rgwekvethf
      181 dgvpsgitsd dreysvrlts ancapprq
//
LOCUS       WP_457606349             293 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606349
VERSION     WP_457606349.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..293
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=31339
     Region          12..101
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 misnnpggrl wvdpdgvegl gkayeshvql yesylsqlta lrsryanawg dddmgeqfst
       61 kflqgldnle aiiggvkgtl hytaqglkes grayreadea aldvsrrmak dfdgldgpay
      121 arravagpvl eptaegeaqr phllsrrlaa gepvaerarl lpqqqgtpml plepaepltp
      181 ltaahpaiss yfmgpeyata hvggrplpee yrlialnpfe dgstrvdanl ydsitpltga
      241 pvttpdgtai dpgqgrffvv kenpavdptv pgyqplylsy apdgtptpii pga
//
LOCUS       WP_457606399             414 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Nitratifractor sp.].
ACCESSION   WP_457606399
VERSION     WP_457606399.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 414)
  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   4  (residues 1 to 414)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19948164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..414
                     /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=47465
     Region          1..391
                     /region_name="cztS_silS_copS"
                     /note="heavy metal sensor kinase; TIGR01386"
                     /db_xref="CDD:273593"
     Region          197..411
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maalillfst llyfyirhnv ekelqhslve qasylfghyd rleetlaqqk gllrqtlgie
       61 aeivtrpdag wkphhfesfk rdhrfylrgl fpydfdrhsy llltrditqp mrmveqvfra
      121 ivflnlvaml liilyayils kmliapisff skklarmdgn vletintrei peefrplahs
      181 vnqlvsrikn yilynkelfv gaahelktpl avlktrsqva likrdknses lqkvieenit
      241 tvddmsemvr tilefgraeg aqldqakrld ikaflqqkie efrllahteg keihsrlklg
      301 rleillqptl ltqilqnllq nalrytpegg ivhlyayrkg drlivkirde gpglddsfdp
      361 fapfkrgkds pgaglglflv rnavdslgge itlqnredrr gaiatlllpi egnd
//
LOCUS       WP_457606407             296 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606407
VERSION     WP_457606407.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..296
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31558
     Region          3..294
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msriavigat gsvgrqicar faedgqevla varghaarvg pypfvardva addaaelarf
       61 lrshdlrvvv naagrwgptr aemlrshlgv aqrlaearsv mddpprlihl gtvheygpap
      121 agvdlderqp vdpgtpyamv kvacsmavla aggvvlrcan mfgphppeet ffaavlrrlr
      181 aasrdrsvve ltvadarrdf vdvrdvagav laaastaveg qvlnigsgha hplrelvdgl
      241 iaeagvpasr vriteqdvps hgggwirvds raaqrltgwr prytareslr amwaqv
//
LOCUS       WP_457606414             309 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606414
VERSION     WP_457606414.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..309
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32379
     Region          6..304
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mgsvsrvavm gasgcvgrqv caafahaghp vvavsrrpas hlaayrfrsl dlasvpperl
       61 arvldeercd vvvnvtggwg stpeamrhdh igltgrlvra vaaaargprl vhlgtiheyg
      121 pvpdgavide svppapvtey artklagsrs vldatargei dgvvlravnl cgpypaepsf
      181 pgfllrrlra aaagddvlel tvasahrdyl dvrdaadair raattdaavt gqvvnigrge
      241 avpmrelvrm avaaagippa rvrlvaqpvd skggdwtlag irraeqlikw rpriglaasl
      301 samwgsest
//
LOCUS       WP_457606444             465 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606444
VERSION     WP_457606444.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..465
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46469
     Region          78..465
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mgrvartpsp rlpaarrprl vtavlavval tgttaascgd dapavtvaev grapvsevid
       61 apatvtaraa atltapadgt larlrvqpgq rvtrgqvlav idspsardrl akardalraa
      121 kragrgtgtg dlggsrrgtd raadeafaaa raaagkvgdp rvraalllqv ssaqrqyesa
      181 araadravaq vqrgvaglns avgalsaaqr lqaqqaydla katvdaltlr apiagvvqpg
      241 gtrsaapadl agllgaagga gvpgldpsal ggggqggppp gvddaipagg rvtagtavlt
      301 vvdigrlgll aevdetdvll vragvpasve ldavtgatyd atvrsvdvlp tssarggvty
      361 rvrldlgagr lgeaeaapap rpgmnavvrl rvreaadava vpasavfstd grdavwvlrd
      421 gradrvpvtv gvqgqdlvqi vdgvragdrv vvrgadqvrd gqelr
//
LOCUS       WP_457606447             394 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606447
VERSION     WP_457606447.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   2  (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   3  (residues 1 to 394)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..394
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41035
     Region          5..394
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mrlaeawrva sdalranrmr slltmlgvii gvasvvilva igtgtkqqve qqveglgsnl
       61 llvvpgriev gtapvvspld lsdadavsrv vgdpgrvavt vasgatarag nrsdfttvqg
      121 vlettpsvft rslsrgrylt gadvdtsrrv avlgdsvara lfpdrdplgq qvtlagvrfr
      181 vigvfaplgq slgvdrddev hvpvtaaqrl wgtqridgia vkapdrerid elgdrivael
      241 trrhpdtefs avtqrqilgv lgdilgvltg vlaaiagisl lvggvgvsni mlvsvrertr
      301 eiglrkavga rprdigvqfl leavlltsvg gltgmalgvg tallvdafsp ipaaitwwsl
      361 alafgvsaav givfgvvpaq ragrldpvva lrae
//
LOCUS       WP_457606462             205 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606462
VERSION     WP_457606462.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..205
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..205
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22469
     Region          <52..96
                     /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 mtdiadtepe aptapgvlta pgvpgvpasa aadggpallt epfdvpfpap givravrrra
       61 dasqrelarf arvhpstigr ieagtltpsl amlsriigta gfrlvvvdea grvlkpmrdr
      121 adlrdgaerr ypshldivtd pepgewwadr yglarppetf yrnrevrdwl rrrsqwevrv
      181 akyrsvpppp dpqrcgyrgg ppirp
//
LOCUS       WP_457606479             332 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606479
VERSION     WP_457606479.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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   2  (residues 1 to 332)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..332
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35278
     Region          5..332
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mrhrlkdvae ragvsvktvs nvvngyqhvr adtrarveea iaalnyrpnl sarnlrkgrt
       61 gvialavpel dipyfaelar hvvtaaadhg wtvlidqtgg rseqerkaas gigdhmidgl
      121 ilsplaltad dlaalaglpm vllgervdhg ladhvmidnv aaareitahl iglgrrriaa
      181 igsqptpega sarlrlagyt aalteagiay derlvapapa whradgaaav rhllttgvrp
      241 davfcfndtl algalralhe mglrvpedva vagfddiedg rfsiptlttv apdkeriarl
      301 avellagrlg pdrdapprel vaphhvalre sa
//
LOCUS       WP_457606484             545 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606484
VERSION     WP_457606484.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..545
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58152
     Region          7..545
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msatliakdl taghgdrllf edldlvvapg dvvglvgvng agkstllrtl aglvpreqgs
       61 vslspptatv gylpqeperr pgetvrefla rrtgvsaaqa aldaataalt agaagadday
      121 analerwldl ggadlderaa qvaaelgldv gldhpmtgls ggqaaragla slllsrydvf
      181 lldeptndld lagldrlerf vtglragtvv vshdrefltr tvtriveldl hqrqvnhygg
      241 gyaayleere varrhareey eeyadtkadl earartqraw mekgvknarr katdndkigr
      301 kfraestekq aakakqtarl ierlevveep rkewelrmei aaapragavv aslrgavvrr
      361 ggftlgpvdl qidwadrvai tgangsgkst llaallgrlp ldeghaalgp gvvvgevdqa
      421 rglflgdqpl ldafgaavpd lapadvrtll akfglradhv lrpaatlspg ertraalall
      481 qgrgvnllvl deptnhldla aieqlesala sypgtlllvt hdrrmldavs vnrrlrvadg
      541 riaeh
//
LOCUS       WP_457606495             539 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606495
VERSION     WP_457606495.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10196530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..539
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=56186
     Region          15..275
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(15,39..40,69,74,79..82,98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,43,45,77,97..100,104,106,143,145,
                     147..148,150,159..160,163,180..183)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,43,45,77,97..100,104,145,147..148,
                     150,159..160)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,104,106,143,145,147,163,180..183)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(159..167,176..183)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          377..476
                     /region_name="CBM_2"
                     /note="Cellulose binding domain; cl21579"
                     /db_xref="CDD:451319"
ORIGIN      
        1 mggpvrngvq llgeryrlve qlgaggmsvv wrgydevlgr qvavkvlasr lasdkafrhr
       61 irveaqaaar lchpnitnvy dygesvqvgl tvpyvvmelv dggplsgrlg rdgqlpwrea
      121 mtigaevasa laaahargvv hrdvtpgnvm ltptgvkvvd fgisalvges dkgpdgallg
      181 tpaylaperl dnghvspatd vyavglllyr mltgrlpwqa stttemlrah myrdpdpmpa
      241 vpglpepvaa lvqrclakrp edrpataeva rtlaeaagia aivpvspafg rtdpalaena
      301 gttilpwsae tdalpfsvvr trtrraaarr rkveagvaav glvavtvtmw gltsrspasg
      361 gveptearms mpepipcavd yslrrdtgkd fsaeltltnt gdrelrgwtm nftfpgkqtv
      421 ttaqpparqa grtvsiaapa tgpalapgas tkltlagryt gsntlpveft lggstcgvqv
      481 sgiagsaptt appvktpvkp atkttaksgp akakpapakp kpkaapkpkg kengkgkaq
//
LOCUS       WP_457606497             222 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606497
VERSION     WP_457606497.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..222
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24022
     Region          <11..207
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 msarhpeetg iaviglgrfg arladslsrl gyevlaidrd pnrvqhwsad ldrvvqadst
       61 eevalrqlgl adfrrvvvai gasleasvlt vlalaelgie qiwaratsek hakilhsvga
      121 hhvvfpeaet gervahlivs rmldfiefdd dfaiakikvp aplvgrslrd iapqdrygvm
      181 vvgekqagep fryagpdtvl eadsvliveg gitqvqrfsa lt
//
LOCUS       WP_457606499             444 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606499
VERSION     WP_457606499.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..444
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47155
     Region          8..439
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mrrllrkpvr lvplgflavi lvgagllmlp watseqrytp fvtalftsts avsvtgmavt
       61 dtpnywngfg lvmitvltql gglgiltgas lvilavsrql glrnrllvqa etaefglgdv
      121 rrlllriaat vfvtealmta viatrlflay dyrpgralws avfhsvqafn nggfalysdg
      181 liafsrdgwv alplsigaii gglgfpalfe avrewrqpar wavatkltvw gsvvltvfgv
      241 ayllmaewgn pftigtydvp gkllasftqi alsrtggfdv isvghltdes ypmliglmfi
      301 gggsastagg ikvstffllg faiwaelrge pdttvgrrrv aaasqrqalt vallsvalva
      361 ggtvglialt shisfsaalf evtsafsttg ltvgvsgqls ppgqyvltal myigrigplt
      421 lgsaialntr rrlyrypeeq pivg
//
LOCUS       WP_457606501             372 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606501
VERSION     WP_457606501.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Van Der Rest,B., Rolland,N., Boisson,A.M., Ferro,M., Bligny,R. and
            Douce,R.
  TITLE     Identification and characterization of plant glycerophosphodiester
            phosphodiesterase
  JOURNAL   Biochem J 379 (Pt 3), 601-607 (2004)
   PUBMED   14750903
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tommassen,J., Eiglmeier,K., Cole,S.T., Overduin,P., Larson,T.J. and
            Boos,W.
  TITLE     Characterization of two genes, glpQ and ugpQ, encoding
            glycerophosphoryl diester phosphodiesterases of Escherichia coli
  JOURNAL   Mol Gen Genet 226 (1-2), 321-327 (1991)
   PUBMED   1851953
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Larson,T.J., Ehrmann,M. and Boos,W.
  TITLE     Periplasmic glycerophosphodiester phosphodiesterase of Escherichia
            coli, a new enzyme of the glp regulon
  JOURNAL   J Biol Chem 258 (9), 5428-5432 (1983)
   PUBMED   6304089
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171238
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.46"
                     /GO_function="GO:0008889 - glycerophosphodiester
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40384
     Region          44..362
                     /region_name="GDPD_ScGlpQ1_like"
                     /note="Glycerophosphodiester phosphodiesterase domain of
                     Streptomycin coelicolor (GlpQ1) and similar proteins;
                     cd08602"
                     /db_xref="CDD:176544"
     Site            order(49,76,78,91,185,222,317)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176544"
     Site            order(49,91)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176544"
     Site            order(76,78,185)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:176544"
ORIGIN      
        1 mrrtlsalgv agallaaavv vpavaaqagp dhgaaeqara tqrpivighr gasgyrpeht
       61 leayrlairq gadfiepdlv atkdgvlvar heneisgttd vaarpefaar katktidgvt
      121 vtgwftedft laelktlrak erlpqvrvan aafdgrfqip tfqevidlar aeskargrti
      181 gvypetkhpt yfasigrale eplvavlrrn rlthradpvf vqsfetanlr kldtmidvrl
      241 vqlmdasgap ydfvaggdkr tyadlatpag lawisryadg vglnknlivp rdsagrllap
      301 tsvirdahrq klvvhawtfr aenqflpvdf rigtdpnarg ditseyelff dlgldgvfsd
      361 hpdtavaara gr
//
LOCUS       WP_457606509             369 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606509
VERSION     WP_457606509.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..369
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38191
     Region          59..359
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mtnsvvdapp aqvpdeltpg rsrwhglrpy lplvalvvaa vlpystlnlp gifegplnsp
       61 gtlqllaicl vfgglaagyd llfgrtgmls fghalyfaag vygtdilvtk aglplwqaav
      121 ltviggttla allgavalrt vgiafamvtl afaqvgailv ardfggltgg eeglpldvsg
      181 lpaalvgvtn tvnlywlala ylaivvlvvh rvsasptgrv laglrdderr igvlgldpyr
      241 fklvaftlag glasaggvvy vlivggasph itsseltlsl lvmvvlggpg trwgpvlggv
      301 lymyldhrlt afgssdavns lpaflshpls qplfvlgtvf ilavyffpgg laslrsrvtp
      361 lltalrrsr
//
LOCUS       WP_457606520             552 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606520
VERSION     WP_457606520.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..552
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58847
     Region          22..390
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mseqisgqpl aptapvppea ptfaalgarq etvealaaag itrafaiqey alpialrgvd
       61 ligqaptgtg ktlgfgipll ervfapsegs dgvpqalvvv ptrelgiqva kdldaagrtr
      121 gvrvlpiygg vayepqieal rkgveilvgt pgrlldlqkq khlrldrvra lvldeadrml
      181 dlgflddvek ilamlpedrq tmlfsatmpd pivtlsrrfl rrpvtihagh taetgpspqt
      241 kqlayrthsl nkveivaril qaegrgltmi ftrtkraadr vaedldfrgf avaavhgdlg
      301 qgareralra fragkidtlv atdvaargid vtgvthviny dcpedqdtyt hrigrtgrag
      361 atgsavtfvd wddmprwrii dktlgldmpe ppetyhtsah lytdldiptd vsgtlptaer
      421 traglsaeve edlggggrsr rgarrgdsrg rergdrdrgr grggeggssa gstsaqadag
      481 ddeaprtprr rrrrragetv ageptaviga egaaetaaap qaaegeaask prrrrrrrgg
      541 stgapaeasn ad
//
LOCUS       WP_457606527             271 aa            linear   BCT 27-JAN-2026
DEFINITION  M15 family metallopeptidase [Nitratifractor sp.].
ACCESSION   WP_457606527
VERSION     WP_457606527.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 271)
  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 10610297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..271
                     /product="M15 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0071554 - cell wall organization or
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=32153
     Region          175..241
                     /region_name="Peptidase_M15_4"
                     /note="D-alanyl-D-alanine carboxypeptidase; pfam13539"
                     /db_xref="CDD:433291"
ORIGIN      
        1 mkkklryslf lpfllllpag lqakcdsnar rlvnaypqls acrnnrivwk dgttmlyddg
       61 rrktftqrlk kpdiqdmfhd rypksfsipq kdfdpgryry epffrhmygn speevrrhlt
      121 tidwfgqkir vtrvnnvdrq lraverdlkr llkkkpgyrk yltpiggtfk wrkiagtnrl
      181 svhsfgaaid invkhsaywr wnkgayryrn qipheivrif ekhgfiwggk wfhydtmhfe
      241 yrpelpgmgk gsshsaaskl rkgrqesmdc f
//
LOCUS       WP_457606532             472 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606532
VERSION     WP_457606532.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47245
     Region          1..442
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mtasglpcrv hlgyalgslv tgafgtvpgl lllpyltdtl gvaaglaall vllpkawdvl
       61 vnpvagrisd rtrsrwgarr pyllggglal avlfasifaa pfadgpaaaa yvalaflata
      121 tafaffqvpy vampaeltad paertrlmtw riavlalail vsgavapavv saggdgvpgh
      181 rwmglfvavl ivagtvgvfl gtrsaptgtv gesepslraq lavatgnrpf rvllicfviq
      241 sagvatvlag vkyfadqvlr epdsgptllf acfvapallv mplwsragar lgkraslaaa
      301 slifavgala lvaapalpaa aayavvavig vgyagqqvfa lamlpdciay dtartgrrqa
      361 gvftglwtag etfglalgpg iyglvlqlsg yvssstgtaa vqsgsarlgv llgftvlpal
      421 lvaiplvllr gytltsaqla avpdaaasga aapgagspga tgsgadapvt ra
//
LOCUS       WP_457606534             492 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606534
VERSION     WP_457606534.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 492)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..492
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50264
     Region          7..371
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mtdtagggal pargmpatdv lgeiralraa drpthggrlf ayvydpgvag ldalaqaaya
       61 esahvngldp tafpsllame nalvgaaarl lgggpgtgap dvvgsvtsgg teslllavka
      121 ardarpdlae privvpatah aafakaahyl rvaldtvpvd pvtlrpdvaa vaaavrpetv
      181 lvvasapsya hgvvdpvpei aavaqaagvr chvdacfggw alpwlrrlga pvppfdfavp
      241 gvtsisvdlh kyayapkgvs vllhrdpalr apqffayadw pgytmvnpvi astrsggpia
      301 aayatlrhlg edgylrlaaa trdavaglad avratgglrl maepettvvc ftsddpqldl
      361 fvlvdelter gwhtqpqlty adlpasvhlt vtaavaprva efgpalaeav aaaraagpvv
      421 lppellalag sltpealtpd lvaglagglg laggtgvpdr mamvntllda aparlrerll
      481 aefvgllqrp aw
//
LOCUS       WP_457606541             280 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit C [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606541
VERSION     WP_457606541.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Hanazono,Y., Takeda,K. and Miki,K.
  TITLE     Characterization of the Nqo5 subunit of bacterial complex I in the
            isolated state
  JOURNAL   FEBS Open Bio 6 (7), 687-695 (2016)
   PUBMED   27398308
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..280
                     /product="NADH-quinone oxidoreductase subunit C"
                     /EC_number="7.1.1.-"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=29155
     Region          1..165
                     /region_name="NuoC"
                     /note="NADH:ubiquinone oxidoreductase 27 kD subunit (chain
                     C) [Energy production and conversion]; COG0852"
                     /db_xref="CDD:440613"
ORIGIN      
        1 mtpeevgrrv vallapveat asvsggqgya ratvdvppts wadavraard daeldldfld
       61 wlsavdelad gfdvvlhlws vrhrhglllr trvprdtpvv asvvglfpga awherethem
      121 fgidfaghge lrplllppef eghplrkefv lasrvakpwp gakepgesea gggrrpvrpp
      181 gvpapgewgt tptpagaaga gegprggtpa rparerparp aaaerparpa perpvsgeae
      241 agsavapaad dvgplgrplp gerptgpprq epepgaages
//
LOCUS       WP_457606538             186 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit B [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606538
VERSION     WP_457606538.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Friedrich,T. and Weiss,H.
  TITLE     Modular evolution of the respiratory NADH:ubiquinone oxidoreductase
            and the origin of its modules
  JOURNAL   J Theor Biol 187 (4), 529-540 (1997)
   PUBMED   9299297
REFERENCE   4  (residues 1 to 186)
  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 10001254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..186
                     /product="NADH-quinone oxidoreductase subunit B"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /calculated_mol_wt=19999
     Region          10..157
                     /region_name="NuoB"
                     /note="NADH:ubiquinone oxidoreductase 20 kD subunit (chain
                     B) or related Fe-S oxidoreductase [Energy production and
                     conversion]; COG0377"
                     /db_xref="CDD:440146"
ORIGIN      
        1 mqvpavlgep irfvlnwgrr yslwvfnfgl accaiefiat smgrhdfmrl gvipfahgpr
       61 qadlmvvsgt vtdkmapavk rlydqmpepk yvisfgacsn cggpywdsys vtkgvdqlip
      121 vdvyvpgcpp rpeallhgil rlqekiaaeq sglggvprpd altspadava rpvealtapp
      181 vrppvg
//
LOCUS       WP_457606543             347 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606543
VERSION     WP_457606543.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..347
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39004
     Region          19..321
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgsddevldr tggkyvepgg eftrdqryia tritaderdg wpvepgryrl avsracpwan
       61 rliivrrllg ledaismava gpthdkrswt fdldpdgkdp vlgierlada yfarfpgyer
      121 gitvpalvdv ptgqvvtndy aqmsldltte wtahhrpgap dlhpeplrge idevnavvfa
      181 dvnngvyrcg fagsqeaydk ayhrlfdrld wlserlagqr ylvgdtitea dvrlfttlvr
      241 fdpvyhghfk cnrqklsemp vlwayardlf ttpgfgdtid fdhikrhyye vhrdinptgi
      301 vplgpdlsnw ltphgreelg grpfgdgtpp ppppeservd pshtplr
//
LOCUS       WP_457606548             501 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 4 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606548
VERSION     WP_457606548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=50813
     Region          <156..470
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mtfgqvllva vvavpalgal aaavvpgdra grvagtaaaa ltllatlplv ggdhgwfgyg
       61 prpavqpwhq ldlswvpgld lrfhlgvdgi swplvvltal ltllccaytl wrvppgggsg
      121 ralvalllvv evgilgtfla ldlvlfflff evvllpmyav iagwggadrr raarkfalyt
      181 lfgsvlllvg vyvvvaaagt adlvtltgga glsrgtqlaa ftllalafav ksplwplhsw
      241 lpdahtqapt vgsvilagvl lkmgtyglir vavgvapega rwaapvlgvl avaailiggl
      301 vclaqddlkr liayssvghm gfvllgvatl tatgiqaali gniahgvitg llfflagavk
      361 drahtgslae lsglretapr lagllgfaav aslglpglag fwgeafavva aaqrggpfwl
      421 tlavlaalgg altaayflrl lrrvthgrps pavaglapgl agaeltawap lvllalavgl
      481 apalvlsyat gpveallgvv p
//
LOCUS       WP_457606550             488 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606550
VERSION     WP_457606550.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..488
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=48605
     Region          72..488
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mslvqsvdnv amlpaylaag tavlvllvdl lvarpavtva vatlgaagta agaalvgaag
       61 errtfcvgdd cswvwngraa lvgaviallt lgvlalsgpl lragrtpvge ycfllacamt
      121 ggmvlgaagd litlivalet ltlplyvlvg lrrgslagae aavtffvvsv vattvtllga
      181 allyavtgtl hldrlgatla arddltdlpl tgvavalvva glafkvaavp fhawapatyd
      241 gaplpvaayl stasklggvv allavvqral pgdltgpvla alavltmtvg nlvalrqrrt
      301 vrllawssva qagyilaplg alaltagrtg darsaayaaa vayaiffvll elaafaavva
      361 lrpadgdggt ladlrgaarr hpwvggafal aliglaglpp glaglfakvt vvrallagha
      421 gwlalvvaln aviglayylr vtaslyatst gaatvrpart valalgvata aavvigfapq
      481 lvldvasr
//
LOCUS       WP_457606556             168 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606556
VERSION     WP_457606556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..168
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18732
     Region          5..155
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mdgpedfdaf ytatarrvvh hvyalcgdla eaqdvtqeay arawqrwsav gayedpegwv
       61 ravawrltan rwrglrrwfa ararlgretp apgpdpdrva lltalrrlpe aqrlvvvlhh
      121 lhdlpvaeia rttgmpagtv ksylsrgraa lavlltddke evdvgthw
//
LOCUS       WP_457606573             268 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606573
VERSION     WP_457606573.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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..268
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..268
                     /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=27431
     Region          4..>65
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 midqdladrl cavdgvvava lggsrargdh rpdsdwdlgl yyrgtpdlag lravaasiad
       61 gpvdltapgg wgpwvdgggw lrvggvavdw iyrdldrvhr vwadcragry tveaqaghpl
      121 gfyshayage valgrvlgdp tgeltalrae tvdyppalga alvaggwetg llldgaakga
      181 aggdagyvag clfrvvgvlv halhgragrw lvnekgmias agrlpgappd faertqallg
      241 avgrtpsela atiaaartla aevlplsg
//
LOCUS       WP_457606575             103 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606575
VERSION     WP_457606575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=11407
     Region          <28..96
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrlllldagl gpltaqhevr aggrfvarvd lawpalrlav eydgdhhrer ahfrrdvarl
       61 nalraagwvv lrftaddvlr rpdatvalvr qalaerrata adh
//
LOCUS       WP_457606586             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606586
VERSION     WP_457606586.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28825
     Region          24..268
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mtqstearpe vpprpavrrg iavrpaavgl palglviava awwlvtsgln lvhpaalppp
       61 qavgkslagt tevllpalgi ttwmtvfgfv lssvagvlig malaassrve rmfapllvav
      121 navpkiafgp llvvavgwgq kpiltmvfll cffpivlsta tgltttpadl aelgrslnas
      181 wwqsfrkvrf paalpqifvg lkvamplaai gavigefysd rpglgyqilq yngvgdtata
      241 waaivlvalm sialyaalsl verlalpwvr attsar
//
LOCUS       WP_457606599             319 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 9 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606599
VERSION     WP_457606599.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 319)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..319
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32545
     Region          2..310
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 milvlralgv gdlatavpal rglraglpgr elvlaapawl tplaeltgav drvlpttgpd
       61 rigwtgpape vavnlhgrgp qshralaavr pgrvlayrnp gaghpdgpaw dddehevrrw
      121 crllhayglp avpgdlallr paatgvpagv tllhpggkip akrwpadrfa glarelaarg
      181 hrvavtgspd ertlaervar daglppravl agrtglaema alvadarlvv sgdtgvahla
      241 tgygtasvvl fgpvpaahwg pppdrprhra lgaieptpvn pdstgsggvg thptldaigi
      301 devvaavadv ervsgavaa
//
LOCUS       WP_457606601             230 aa            linear   BCT 27-JAN-2026
DEFINITION  D-sedoheptulose-7-phosphate isomerase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606601
VERSION     WP_457606601.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Harmer,N.J.
  TITLE     The structure of sedoheptulose-7-phosphate isomerase from
            Burkholderia pseudomallei reveals a zinc binding site at the heart
            of the active site
  JOURNAL   J Mol Biol 400 (3), 379-392 (2010)
   PUBMED   20447408
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Seetharaman,J., Rajashankar,K.R., Solorzano,V., Kniewel,R.,
            Lima,C.D., Bonanno,J.B., Burley,S.K. and Swaminathan,S.
  TITLE     Crystal structures of two putative phosphoheptose isomerases
  JOURNAL   Proteins 63 (4), 1092-1096 (2006)
   PUBMED   16477602
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Eidels,L. and Osborn,M.J.
  TITLE     Phosphoheptose isomerase, first enzyme in the biosynthesis of
            aldoheptose in Salmonella typhimurium
  JOURNAL   J Biol Chem 249 (17), 5642-5648 (1974)
   PUBMED   4606909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..230
                     /product="D-sedoheptulose-7-phosphate isomerase"
                     /EC_number="5.3.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008968 - D-sedoheptulose 7-phosphate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:1901135 - carbohydrate derivative
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=23706
     Region          34..191
                     /region_name="GmhA"
                     /note="Phosphoheptose isomerase [Carbohydrate transport
                     and metabolism]; COG0279"
                     /db_xref="CDD:440048"
ORIGIN      
        1 mtagtpaaga tvledhlsll aaallplrea eqmlarwgee laqrlaaggr llvagnggsa
       61 aeaqhltael vgklrhdrqp lsaialhaet savtaiandy gydetfarqv rahgrphdhl
      121 llmttsgtst nlltaahaah qtgmrcwaft gpapnpladl chehlaidsp dgqvvqelhl
      181 vashvlceyv elalpaalaa rpaagpvrag vevvvgepdp tapagrgdaa
//
LOCUS       WP_457606612             329 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606612
VERSION     WP_457606612.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465281
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..329
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34491
     Region          17..328
                     /region_name="COG3380"
                     /note="Predicted NAD/FAD-dependent oxidoreductase [General
                     function prediction only]"
                     /db_xref="CDD:442607"
ORIGIN      
        1 mpsaaydhlv taeragvvvv gagiagvaca telaragipv rvrerarvtg grmaskrfdg
       61 rpadlgaayf tvddadfaav vdrwrdagla rewtdtlvay gsrgreqvtg pmrwaaprgl
      121 rslvehlaad lpvthdrlvm tvgpgprvdg taaeavvlam pgpqaallld palaeatrav
      181 aaqrwssalt gvlhfparrw adfrgafvnd hpvlslvcdd gdrrgdgapv lvahttagfa
      241 aghllqptaa rpaieqavrd llglpepavs shvhrwtyas pdahsgsatf hldddgigla
      301 gdaygrprvq tawrsgrdlg ralaarlgg
//
LOCUS       WP_457606648             192 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606648
VERSION     WP_457606648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20453
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 maraglnrgr liqagaelad evgfdqvtvs alarrfgvtv aslyshvrns hdlrvgiall
       61 algeladeaa dalagragke altafanvyr dyahrhpgrw aaaqlrldpq taagsagirh
      121 sqmmrailrg yhlpepeqth avrllgsvfq gfvglemggg fdhsapappe swervldavd
      181 allrnwptad at
//
LOCUS       WP_457606656             382 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606656
VERSION     WP_457606656.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..382
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41710
     Region          115..357
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mreptgrepd rtrggrvwkl aglaavagla waardvpaql ggrltgarad raarsprfrd
       61 gtfhnpagas atmvadpgrn llrelvfgkq krrpgspvpl lrpgaaptaa dparelnvvw
      121 yghastlvei egqrvlldpv wsdrcspsgl vgprrihepp vrltdlppld avlishdhyd
      181 hldmdtvrtl adlqsapfvv plgvgahlar wgvlehrive ldwseshrag gltltataaq
      241 hfsgrglrrd gtlwsswtit gthrkvfytg dsgyfdgyaa igaehgpfdl tlmqigaydr
      301 awphihmfpe eavaahldvr ggllvpvhwg tfnlalhdws epvdrlwaea kardvrlavp
      361 rpgervvvde ppavdgwwqs va
//
LOCUS       WP_457606660             828 aa            linear   BCT 27-JAN-2026
DEFINITION  Tex family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606660
VERSION     WP_457606660.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Fuchs,T.M., Deppisch,H., Scarlato,V. and Gross,R.
  TITLE     A new gene locus of Bordetella pertussis defines a novel family of
            prokaryotic transcriptional accessory proteins
  JOURNAL   J Bacteriol 178 (15), 4445-4452 (1996)
   PUBMED   8755871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..828
                     /product="Tex family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /calculated_mol_wt=88532
     Region          15..743
                     /region_name="Tex"
                     /note="Transcriptional accessory protein Tex/SPT6
                     [Transcription]; COG2183"
                     /db_xref="CDD:441786"
ORIGIN      
        1 mqggnhprrr mtivtqsvhq riaeelgvae rqvraavell dggatvpfia ryrkeatgll
       61 ddaqlrtlee rlrylrelde rraavlesir sqgkldeale aqilaadsks rlediylpyk
      121 pkrrtraqia reagleplad tlladpaqdp ktvaagfadp drgvadaaaa ldgarailie
      181 rfaedadlig tlreqmwsrg rlvsrvregq etagakfady fdfaepypkl pshrilavfr
      241 gekegvlelt mdpeadgdad atgpsryeaa vagrfgisdq grpadrwlad tvrwawrtri
      301 lihlgadlrm rlwqvaeeea vrvfatnlrd lllaapagar atmgldpglr tgvkvavvda
      361 tgkvvatdti ypheprrqwd aslhtlatla aahgvelvai gngtasretd klagdlikrh
      421 pelkltkvvv seagasvysa sayasqelpg ldvslrgavs iarrlqdpla elvkidprsi
      481 gvgqyqhdls evklsrslda vvedcvnavg vdvntasapl ltrvsgigag laenivlhrd
      541 angpfrtrae lkkvprlgpk afeqcagflr ipggddplds ssvhpeaypv vrrilsstgq
      601 dlrgligksa ilrglratdf vdetfglptv tdilaelekp grdprpefrt atfvegveki
      661 gdltpgmvle gvvtnvaafg afvdvgvhqd glvhvsamsh tfvkdprdvv ksgdvvkvrv
      721 ldvdvprkri sltlrlddea paggdgagrd radgggqggr grgrlggdrg gpqgggrtgg
      781 gpgggcgsgg rnrqhrdqgs gpqqrpsrga papvndamae alrragla
//
LOCUS       WP_457606644             155 aa            linear   BCT 27-JAN-2026
DEFINITION  cytidine deaminase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606644
VERSION     WP_457606644.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Navaratnam,N. and Sarwar,R.
  TITLE     An overview of cytidine deaminases
  JOURNAL   Int J Hematol 83 (3), 195-200 (2006)
   PUBMED   16720547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..155
                     /product="cytidine deaminase family protein"
                     /EC_number="3.5.4.5"
                     /GO_function="GO:0004126 - cytidine deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009972 - obsolete cytidine deamination
                     [Evidence IEA]"
                     /calculated_mol_wt=16135
     Region          3..127
                     /region_name="Cdd"
                     /note="Cytidine deaminase [Nucleotide transport and
                     metabolism]; COG0295"
                     /db_xref="CDD:440064"
ORIGIN      
        1 mrdtdralvq aatavaklrc rsdnhtvasa vrstdgrvfs gvnvyhftgg pcaevvalga
       61 aatqgagele aivavgdrgr gvlppcgrcr qvlldyfpsi kvivgppdgl ravpiadllp
      121 etyvwsdqqv evpagprapl wptpvvpgvr qaaed
//
LOCUS       WP_457606666             400 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606666
VERSION     WP_457606666.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 400)
  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 400)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..400
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44118
     Region          10..388
                     /region_name="GT4_WbuB-like"
                     /note="Escherichia coli WbuB and similar proteins;
                     cd03794"
                     /db_xref="CDD:340825"
ORIGIN      
        1 maptstasrr vlvvnqyakp laeaggtrhv elfgrlsgwd ytiiagdldn ysrtrnyqpd
       61 prfvrvwspg ysgnnhrrvl nwlgysmaal laglrqprpd vvyassphil apvagwllar
      121 lrrarfvlei rdlwpesmvs tgylrsgsrt hrlltalesw lyrradrivv vaggwrgylr
      181 drgvdpakvc wvsnsaepsd fvprpdryap lrdrvpvagr lvvyagahgp angldlllda
      241 aaelpehtfl ligdgldkar lverartqgl tnvhflgtvp krelagiigg advgvhvltn
      301 aeifrlgasp nklydylaag lpvvtncpde pteivhttga giavepadiv pglrkllded
      361 tatlramger grryiedhrs rtvmaarlqr lldevrppvq
//
LOCUS       WP_457606672             394 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606672
VERSION     WP_457606672.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..394
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43285
     Region          32..386
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtqqalrtrp lrvlqvtttp eggdwfyyqv vglarrghdv tavlpgegtl tervrtagvr
       61 teivplsgwr pqqmprvaaa elklirlihg lrpdvvhthl lkaavacrla tltdrralhv
      121 nqlpgaahlr nrllrrldla tlrradmvig scsdfaeryr rfgaravats hygfdvhryd
      181 patpagpfrs efgldpatpv vgmvahmyps klkafreigi kghevlidav prllsrvpea
      241 hvfivgdefv gdgsyrrale eraqrlgvtn rthftghrtd iphvmaaldv lvtpslddsa
      301 sgasvqallm etpvvasdvg glpdtvqhge tgllvppvdp aaladaaadl lldpqrrwam
      361 grlgrircle rydaertvad verlyrtala grnr
//
LOCUS       WP_457606668             404 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606668
VERSION     WP_457606668.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 404)
  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 404)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..404
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43379
     Region          21..339
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 msdpsrdhae palvllgaan sihvrrwata laarghrvav aswvaadpip gvellvpara
       61 granagrwqa vrrmvrsaww lrrqvarvrp dvlhvhsvst agalslavpr gvprvvtpwg
      121 sdlrfavssr prgwvaraal lradlvvpts gavrgevtqr yrvppdrsvt lswgvddeli
      181 rdrdvvdraa vrarfgipgd atavlsirsa spvyrtadil aafagaargr pdlhlvllgg
      241 ltpaeaaagr arrecldeaw alaralpgrv tvldgalppa elfglmrase vavsvprwdq
      301 rsttvleaal agcrlvladl ppyrelvadg lvadlvpepl tagltgllla adalppadqr
      361 rnltlittae swshqvdamr glyrrvvgrr rrpaeehagq rvph
//
LOCUS       WP_457606676             214 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyltransferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606676
VERSION     WP_457606676.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wang,W., Zhang,Y., Wang,L., Jing,Q., Wang,X., Xi,X., Zhao,X. and
            Wang,H.
  TITLE     Molecular structure of thermostable and zinc-ion-binding
            gamma-class carbonic anhydrases
  JOURNAL   Biometals 32 (2), 317-328 (2019)
   PUBMED   30895492
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Smith,K.S. and Ferry,J.G.
  TITLE     Prokaryotic carbonic anhydrases
  JOURNAL   FEMS Microbiol Rev 24 (4), 335-366 (2000)
   PUBMED   10978542
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..214
                     /product="acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22400
     Region          4..213
                     /region_name="NeuD_NnaD"
                     /note="sugar O-acyltransferase, sialic acid
                     O-acetyltransferase NeuD family; TIGR03570"
                     /db_xref="CDD:274656"
     Site            order(125,127,131,133,143,149,151,161,166..167,169,179,
                     183,185,187)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100050"
     Site            order(161,163..164,169,181,187)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100050"
ORIGIN      
        1 mtndivivgc gghgretlgi irainraapr ppwrilgfvd ddpsdlnlkr vhrldaaylg
       61 athrlvdlpp sthlilsigd prtrkavger idryglpaav lvhpsaeige dtvagegllv
      121 fagarvttnv rlgrhvhlnq nvtighdctl adyvsvnpla avsgdcrias gvmigtnatv
      181 lqalevgads ivgagacvvr svpertvvkg vpar
//
LOCUS       WP_457606678             203 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606678
VERSION     WP_457606678.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Miyake,K. and Iijima,S.
  TITLE     Bacterial capsular polysaccharide and sugar transferases
  JOURNAL   Adv Biochem Eng Biotechnol 90, 89-111 (2004)
   PUBMED   15453186
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..203
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22899
     Region          24..172
                     /region_name="Bac_transf"
                     /note="Bacterial sugar transferase; pfam02397"
                     /db_xref="CDD:460547"
ORIGIN      
        1 mkrvldvvla tvlllllspl lalvataill tlgrpvlfrq vrpgrygqpf vlykfrtmre
       61 plpgenpwts ddarstrlgr llrrtsvdel pellqvlsgr mslvgprplv maylpryrdd
      121 harrhevrpg itglaqvsgr rsltlgqrld ldvryvdews lgldlrillr tlaepfrrge
      181 irgqslaeid dvgllppale evr
//
LOCUS       WP_457606680             212 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606680
VERSION     WP_457606680.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..212
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23398
     Region          1..172
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mltgrivvlr pmcladlgff aelgnvtrvr shvvgwdwpv spdaqrdwye racrdwrsrr
       61 ltvadpvsde pvgvtglwev dwhnlsalta iklmpglapp gagsdaiklt mawsfyevgl
      121 rrlhstildf naaslgayvr kcgwriegre reavfrrggw hdllkvaalr gdfdgladsa
      181 eyvervcgsp pvpawpgadg gtrerrlspa ns
//
LOCUS       WP_457606686             376 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606686
VERSION     WP_457606686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..376
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39503
     Region          4..373
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtgrihlspp digrleesyv laairsgwva plgpdvdafe seisarvgtr halatssgta
       61 alhlallavg agpstvvvip tltfaatana avytgaepvf vdcepatgnv dvallaemld
      121 rlraagrrva avvavdmfgl cadygtllpv ceaagvpvve daaealgatr ggraagsfgr
      181 vgalsfngnk vmttsgggml lsddgelvdy crylatqarq pvvhyehtdi gynyrlsnll
      241 aalgraqlnr ldgmlarrra vrdryaklfa phagvrllgd gdltgncwlt tivvdpartg
      301 wtaaqlgahl rdldiearpv wkpmhlqpvy rtaeslvtga aqhlfehglt lpsgsaltag
      361 qldrvcrave qfvasr
//
LOCUS       WP_457606688             307 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(+)/NADH kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606688
VERSION     WP_457606688.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..307
                     /product="NAD(+)/NADH kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006741 - NADP+ biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0019674 - NAD+ metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=33022
     Region          1..269
                     /region_name="NadK"
                     /note="NAD kinase [Coenzyme transport and metabolism];
                     COG0061"
                     /db_xref="CDD:439831"
ORIGIN      
        1 maglgmvlhp trdvsevvai ierwasrhrk tllvraedah rvptgvepvp agtladrada
       61 lisiggdgtm lgalrmavrd pkpvlgvhlg rvgflvevep pdlpralerl vehdftvesh
      121 aclacdvcgd dvvafndial vrqpgagfvt atlavdgqry gyyrcdalvv stpsgstays
      181 yaaggplisp ateamvvtps apmagisrsv llsahetvhl elradsapva vemdgllirq
      241 aategsvhir yvkdagrvvr ldprryqern qlklslldlp llpdqlrell pdglreqlnr
      301 relpppr
//
LOCUS       WP_457606694             263 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606694
VERSION     WP_457606694.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..263
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28700
     Region          15..152
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpdaifshpr lapvydafdg drddldayla iadeldarvv ldlgcgtgnl alllarhgrt
       61 vvgvdpagas lavarskdre grvrwihgda ttlpplradl avmtgnvaqv frtdddwart
      121 lrgvraalrp gghlvfetrr perraweewa adtapvtrdv pgegpvqrrl eitavelpfv
      181 sfrftyrfpa dgavvtsdst lrfrdrdeve asltaagyrm rdvrdapdrp grefvfvarr
      241 adqprgegas gtqpsargsr avg
//
LOCUS       WP_457606722             405 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606722
VERSION     WP_457606722.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..405
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=44509
     Region          8..352
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtsaptvtra prlpsltglr wvaallvfgf hagtmgivae phlkplidka fslglsgvef
       61 ffilsgfvlv wsyrdgeraw tflrrrfaki ypnhvvtfva alavaawfad pvvpwaaian
      121 fflvqawipv ggyfysvnnv swslscelaf ylclplvvpw lrrartgvlr tvlvaaplli
      181 lalwpgqqlv peeqrwwftq ifpvtrslef wmgvaaaelm rrhrwrgpnl aaatgifvtt
      241 wvvaalwipa efwaallava yllviaaaad advrgrptpw rsramvwlge vsfafylvhv
      301 lvmvtvlrlt ghwgtglpgw rgplavlgfl vvtlalaaal hrwvetpmmr llgpsrrara
      361 asrapavpap rtpaeaatvp aadggaasvt gpvedieyag rrrpd
//
LOCUS       WP_457606739             420 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606739
VERSION     WP_457606739.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  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 420)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..420
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45641
     Region          6..412
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mptahlvprh aaaqvnaala dtrvvlisga rqagkstlvr lvagdrlaer rdldraqdra
       61 aaiadpvgfv dssellvide iqrapellla ikaavdedpr pgrylltgss rlfgmvaapd
      121 alpgrmetve lwpfsqgeld galdgfvdav falgpnlrhe sdvtradyaa rivrgglpea
      181 tartdprrrq rfldayvqal idrdvrqlsd iqhkgelrrl vrllaarsat iiaanslesa
      241 lglsrptivr ylhaleeifl ikripgwsrn lgtrataapk lifvdsgiaa neiatdaral
      301 lrpgapfgpl lesfvlsels rqltwseqfv dlshyrdqsr yevdavlenr agqvvgievk
      361 aastvgpddf rglrrladrl gddfivgivl ytgtatlpfg drlrampvsa lwqvsastad
//
LOCUS       WP_457606763             502 aa            linear   BCT 27-JAN-2026
DEFINITION  leucyl aminopeptidase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606763
VERSION     WP_457606763.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Drinkwater,N., Malcolm,T.R. and McGowan,S.
  TITLE     M17 aminopeptidases diversify function by moderating their
            macromolecular assemblies and active site environment
  JOURNAL   Biochimie 166, 38-51 (2019)
   PUBMED   30654132
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415720
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..502
                     /product="leucyl aminopeptidase family protein"
                     /EC_number="3.4.11.-"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0019538 - protein metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51616
     Region          14..501
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mlvirlvsgp agpdalvlpv rpggpgspds pgsltspdst aspepglvpt avpigddvra
       61 eaaavlpatr ltgaagevre hlrpggspar lwllgvgdgd erdwrtagaa laraakdetq
      121 itialpadat aalrglaegl llgsyrfrlt eagkrpalae vsvlvddpda lagtldaara
      181 taettrlard ltnmpsstkn pewfaaqvae aasgrpglhl rvrgpkelaa egfggllavg
      241 ggsasgprlv eldwrpegar thvvlvgkgi tfdtggisik pvpamklmrk dmagaaavia
      301 atlgvadlgl pvrvttlapl aensvsgsaf rpgdvirhyg gltsestnsd aegrlvlada
      361 layavrelkp dllidlatlt ganavalgkr haalysenda latglldait aagerawrmp
      421 laddyveyla seiadlhssp aqgagsvvaa lflreftgdl rdrwahldms apswsddthg
      481 elvkgatgwg vrgllrwlat lg
//
LOCUS       WP_457606766             434 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606766
VERSION     WP_457606766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..434
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43243
     Region          161..431
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mggtdvtdgw dwrrpggspv pggpasgrpp qdasgqtasp wwsdaladpw rdpyapaavv
       61 vpavpapgag epepvtdpdl parsgmrqvv lislitalla gslgsaltya flrggdvpti
      121 gaqsgqapal aqrkpeslag vaervlpsvv tirvvslggt segsgfvvts eghivtndhv
      181 vadgsgkatv vfndgstaag tvvgqdpesd lavikvsrsg ltpvqfgdsd alavgdpvla
      241 igsplslant vtagivsald rtmqagepgg ptryyaaiqt daavnhgnsg gplvdgagrv
      301 vgvnstiksl vadgqeagni glafaipinq akritediig tgkarrtvig aqvggtgatg
      361 ggvrlnavep agpaaaaglr tgdvvlrldg hpmtdptdlv alvrkyapgs vvtveyrrgs
      421 arqnasvtla adak
//
LOCUS       WP_457606779             711 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606779
VERSION     WP_457606779.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..711
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75860
     Region          127..519
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mgadrddaae tgtvvtpsae fpplgdeera algrigerwr gprraddlpv dptlgrhdhh
       61 pvptrfgrlt pidmftvaqp delvatgaad lpgdrtgraa artrrallgp plssasvlye
      121 rmrklvalpv lssdllssva ygpeamlavl vlagsaalgl alplaavlvl lmvavglsyr
      181 qtipayphga gsyivagdnl grtpglaaaa glmldyvltv svsvaagvha vtsalpgldp
      241 wavplgvlvi vvllagnlrg vrtagnifvl ptyafvvvlv avlaigyaka asrgfapvpp
      301 psvpaaeglg lllvlrafss gavsmtgiea vsnavpafrp tewrnarttl gwmvamlvtl
      361 fagliglihl dglvpradet llsqlgrvtf psgpwyailq attalillla antafndfpr
      421 llffmardgh aprrylhmgd rlafsnglva laltaavvfv afgghterli plyavgvfla
      481 ftlsqtgmvv hwrrrrgagw rrrlavnavg aalsglvllt aavakfaega wvvvlavpll
      541 vllfrrihrh ydrlhralal hpppsappae cdelpqqvrh lvivpvarln raslralaya
      601 tslgrptlav hlapeeaead rfreqwrawg dhlrletivs pyrsvigpla hylealhaan
      661 pdltltvivp evvlrrrryr llhsraeqrl raalralpgv vvtsvpvhvs r
//
LOCUS       WP_457606781             211 aa            linear   BCT 27-JAN-2026
DEFINITION  M15 family metallopeptidase [Nitratifractor sp.].
ACCESSION   WP_457606781
VERSION     WP_457606781.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 211)
  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 10610297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..211
                     /product="M15 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0071554 - cell wall organization or
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=24321
     Region          125..209
                     /region_name="Peptidase_M15_4"
                     /note="D-alanyl-D-alanine carboxypeptidase; pfam13539"
                     /db_xref="CDD:433291"
ORIGIN      
        1 mklslfflis cgllfasgpk qispidkkie qrmrsghsyr ngcsiplkdl rylripyrgf
       61 dgkrhlgemi vhkdvarevv rifdelyrqg ypirrmqlvs dyggsdwksi eadntsafnc
      121 rpvtggkkws rhaygkaidi nplenpyisr srriahkasl pyrkrvggss pqrkavilpn
      181 spvvrsfksr gwrwggdwht ikdyqhfdkk k
//
LOCUS       WP_457606788             398 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606788
VERSION     WP_457606788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43192
     Region          10..397
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 marlaqtpgl tdvqrsilet vrefadkeii phaqrlehad eypsdildgm remglfglti
       61 deeygglges lltyalvvee lsrgwmsisg ivnthfivay lisqhgsadq ktrllprmat
      121 gevrgafsms epecgsdvsa ikskavrdgd dyvlngqkmw ltngayssvv atlvktdtga
      181 dsvygnmstf llekepgfge tapgltipgk idkmgykgve ttemvldgvt vpasavlgge
      241 ekvgrgfyqm mdgievgrvn vaaracgisi rafelavaya qqrhtfgqpl akhqavafkl
      301 aemgtkieaa halmvnaarl kdagqrndve agmakllase ycaevvqeaf rihggygysk
      361 eyeierlmre apflligegt seiqktiisr gllkqykq
//
LOCUS       WP_457606792             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606792
VERSION     WP_457606792.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23217
     Region          2..197
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkrvdhrer raliadalmr vaaeqgleav slrhvaaaae vspgmvqhyf rtrdemmvfa
       61 lavvrdrnea rvrraveplg atpaprallr amlaellpld edrradgrva laflaytavr
      121 pavaaalhde taallafvag qiaagsplva dgrvdperaa vgllavmegl giyvlgghyp
      181 petalaalda qldlifgtep apgavsrdes grrrparr
//
LOCUS       WP_457606840             218 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606840
VERSION     WP_457606840.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  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..218
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..218
                     /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=22747
     Region          18..215
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mrdllpatva vavagpadwt gellpaelsa lgeravpgrr rdftagrvca rralaalglp
       61 atpvpagadr apiwppgvvg aithtrdyca aaaaraadvr avgidaerdr plspgvrrkv
      121 crpdeeadla rlpagtpwpt vlfsaketvy kvwhplvgtw lgfadarvtl dpdagtfhaa
      181 iaparlaaap mpdppsavtg rfavdddlvr taavlprr
//
LOCUS       WP_457606876             603 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606876
VERSION     WP_457606876.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   4  (residues 1 to 603)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..603
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66396
     Region          6..109
                     /region_name="E_set_CDase_PDE_N"
                     /note="N-terminal Early set domain associated with the
                     catalytic domain of cyclomaltodextrinase and
                     pullulan-degrading enzymes; cd02857"
                     /db_xref="CDD:199887"
     Region          123..529
                     /region_name="AmyAc_CMD"
                     /note="Alpha amylase catalytic domain found in
                     cyclomaltodextrinases and related proteins; cd11338"
                     /db_xref="CDD:200477"
     Site            order(204,206,246,287,325..326,362,364,444..445,488,492)
                     /site_type="active"
                     /db_xref="CDD:200477"
     Site            order(289,328..329,338..341,344,364..365,387,428)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200477"
     Site            order(325,362,445)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200477"
ORIGIN      
        1 mslqphhdgs atyvpeqepa lgqtvpvfvr vpagtgvsqv hvrttgdgep rfaearidrt
       61 dggdvwwrad vevrnpvsny rflldgergt rwlnaaglsg hdvpdngdfk lvsyapppaw
      121 ardaviyqif pdrfarsaaa dgrtvpdwai gcdwdtpvig rgpetprqfy ggdldgvteh
      181 ldhldrlgvn tvyltpvfpa rsnhrydass fdtvdpllgg daalarlada vhargwrllg
      241 ditsnhtgda hdwftaavsd vnaperelyy fdlpgsdyes wngvkslpkl nwgsaelrrr
      301 fataedsllr rwlrppygld gwrvdvanmt grrgadayth evarllrevv adtrpdglll
      361 aehghdhtgd ldrdgwhgtm nyvgftdpvw swlrhgddpv pnflgtpggv rrrdagavla
      421 tmntyrslvs wrsythswql lgshdsarir tvvgdaarqe vaagllatmp gtpvvfagde
      481 lgltgtngeg srtpmpwhrp eswdrrtfea yrslltlrrd epalrhgglr wvhadadtlv
      541 flreaptstv lvlarraagt pvhltgvgaa envygnapal hpdaegrvtl padgptfqvw
      601 rlr
//
LOCUS       WP_457606919            1158 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606919
VERSION     WP_457606919.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1158
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=128798
     Region          172..1130
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mprrsslsyr dalrllapgs tritetdkvv sagilgagal shgtalallg pknalvqlvr
       61 datgnqagri rttggksyye lleashtvla lsaffdgfrd evgpgfdrle ltdeekvgmv
      121 paerrhhtlp qeidggyfpl pssvygmddt rrdveaayvr lydatiafce glaawpsvrr
      181 gldltslrsr vvsramshyq drfdrlatdl pefgfrmmrq aiehnlrdnr tlttevsarl
      241 dalaqlyrnl aelsgpvatd rpdllresld rltgslaavf rqpllrikdv dfhlrlpnvd
      301 sgfispdfra aeygkhtspe reswwddqpr rgdlvgflsr yltdpaslhr pllllgqpga
      361 gktlltrvia arlpasrfta ivvplrrmsg dtspaeqiea aieqvmderi rwadlrratq
      421 httvvvifdg fdelvqvtgt ahsqyidrva efqetqwdlg ysiipiitsr ilvmdrasvp
      481 qgtvlvrled ltdaqvtawl tavnaanedr pgyrrlsage llshgelarq pllltllaiy
      541 ynehwadrrp gtaisrsdlf tglltafirr qvsekaptal ahhereareh qlrrdlaita
      601 famfnrnrel vnraalrldl dcfgsrsgdg srfelgdvlg peqlvtaaff vvygpddvqg
      661 edarrtyefl httigdflia eyvvgalrsl aelrrhtrsp agfgyqldtg qfrallshqp
      721 lvkrealvef ardlssrhpq erdaivetis gllaearqrt dlagvngyrp apydpvrlla
      781 aytanlvala alvspdgvrh tdlmdeatwv stvrlwragl dekgqlamis wlnrdadgri
      841 iaerrrerrg etvnvaaeea rllgdittyg qlqagartwr gqqpdsfeag rfhadlvsla
      901 trrwpvpslh qlilydersy rrlwaraves peavsstsat vlleclaedg aqlprevvcg
      961 ltrvalsrlp dsptappeli iscpylidef pelvdslgst ddhavlhali lrhglhrlpq
     1021 ryvprvrrvl adiedrlael pledgvvsae maeqfaaara dnrtalwllm aldeyadlaw
     1081 pkippktmha llahrlpdef ldeaslcrll ldylrahdrv paevslasal dtlrvlaasd
     1141 dhagqpghag pipaaeav
//
LOCUS       WP_457606940             390 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606940
VERSION     WP_457606940.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 390)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..390
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40178
     Region          1..390
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msdavivgav rtpvgrrkgs lagvhpvdls ahvlralaer tgidpgqvdd vvwgcvsqvg
       61 eqswnvarna vlaagwpesv pgttldrqcg ssqqalhfaa atvlsgqadl vvaggvesmt
      121 rvpmgasvag gmpfsaaile ryrgvegvae dsplpfnqgv gaeliaqrwr fsrtqldefa
      181 lasqekaaaa qdagafeael apvaladggk fsadegirrd tslaklgela tpfradgvvt
      241 agsasqisdg aaalavttae wasrhglrpl arvhtavvaa ddpvtmltap ipatakalrr
      301 aglgieeigv yevneafapv plawlaetea dperlnprgg aialghplgg sgarimttml
      361 qhmrdngiry glqtmceggg manativell
//
LOCUS       WP_457606953             422 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606953
VERSION     WP_457606953.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 422)
  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 422)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..422
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44724
     Region          2..412
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mrivvahnry reaqpsgent ivdaeiaqlt aagvevlpfl rssdeipsms kpakallpis
       61 piwapkaqhd ldrlltehrp dvlhlhnpyp llspwvvrta hkrgvpvvqt vhnyrqvcss
      121 glyfrdgvic qdcrgralgv paivhrcyrn sraqsalmat tlavhrptwk svdryialtt
      181 avadhlrdyg ipderivvkp navpdpgtpa pagngflfmg rlspekgldl llsawrrhpv
      241 galgplriag dgelrplaea aaaerpdvly lgqldrpgvr aaladssvvl atstwhdvlp
      301 tviiealasg rpvlgtalgg ipylvgadgp repagtgpae vataapgdgp valpsgvqrg
      361 eagwvvapev ealaaalpla aaeagtlags arsryertfh pdvitkrlid iyaglaggra
      421 ar
//
LOCUS       WP_457606966             275 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606966
VERSION     WP_457606966.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28147
     Region          30..240
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlsdprevlt rpspppdatv sygdhpdqca dlrlpagdgp prplvvvvhg gfwraeydra
       61 htgpmaaala alghpvaqie yrrtgrpggg wphtltdvra giaalpalaa aampgrvapv
      121 ppilvghsag ghlslyvaah apetvggvla lapvadlaqa yrldldegav aallgggped
      181 vpdryaaadp salvpirtrt vaihgdqdiq vpiaisrswv asdhaaggsa tlvelpeceh
      241 fgliapgsta wpqvvaalrs lhddlqgida asstr
//
LOCUS       WP_457606972             239 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdenum cofactor guanylyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457606972
VERSION     WP_457606972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Guse,A., Stevenson,C.E., Kuper,J., Buchanan,G., Schwarz,G.,
            Giordano,G., Magalon,A., Mendel,R.R., Lawson,D.M. and Palmer,T.
  TITLE     Biochemical and structural analysis of the molybdenum cofactor
            biosynthesis protein MobA
  JOURNAL   J Biol Chem 278 (28), 25302-25307 (2003)
   PUBMED   12719427
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Lake,M.W., Temple,C.A., Rajagopalan,K.V. and Schindelin,H.
  TITLE     The crystal structure of the Escherichia coli MobA protein provides
            insight into molybdopterin guanine dinucleotide biosynthesis
  JOURNAL   J Biol Chem 275 (51), 40211-40217 (2000)
   PUBMED   10978347
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   5  (residues 1 to 239)
  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 10002369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     gene            1..239
                     /gene="mobA"
     Protein         1..239
                     /product="molybdenum cofactor guanylyltransferase"
                     /EC_number="2.7.7.77"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061603 - molybdenum cofactor
                     guanylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=24463
     Region          15..236
                     /region_name="MobA"
                     /note="Molybdopterin-guanine dinucleotide biosynthesis
                     protein A [Coenzyme transport and metabolism]; COG0746"
                     /db_xref="CDD:440509"
ORIGIN      
        1 mtgyaailla ggaarrmggv dkparavggr pmlhrvldav adadqrivvg ssgplpsgvr
       61 tareeppggg pvaataagla lldpgtttva vlaadlpllt taavaelrra laawhprddp
      121 ppaldpaasg pedapaaagp edapatwret ldgrsaalac yvdgdgrrqh lcalwrvsal
      181 rsaldrlavt rggsldgapv rglladvavr evswsgsgpp pwfdcdtded vrraeewtr
//
LOCUS       WP_457606978             304 aa            linear   BCT 27-JAN-2026
DEFINITION  fructosamine kinase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457606978
VERSION     WP_457606978.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Shrestha,S., Taujale,R., Katiyar,S. and Kannan,N.
  TITLE     Multi-omics reveals new links between Fructosamine-3-Kinase (FN3K)
            and core metabolic pathways
  JOURNAL   NPJ Syst Biol Appl 10 (1), 64 (2024)
   PUBMED   38830903
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Shrestha,S., Katiyar,S., Sanz-Rodriguez,C.E., Kemppinen,N.R.,
            Kim,H.W., Kadirvelraj,R., Panagos,C., Keyhaninejad,N., Colonna,M.,
            Chopra,P., Byrne,D.P., Boons,G.J., van der Knaap,E., Eyers,P.A.,
            Edison,A.S., Wood,Z.A. and Kannan,N.
  TITLE     A redox-active switch in fructosamine-3-kinases expands the
            regulatory repertoire of the protein kinase superfamily
  JOURNAL   Sci Signal 13 (639) (2020)
   PUBMED   32636308
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Gemayel,R., Fortpied,J., Rzem,R., Vertommen,D., Veiga-da-Cunha,M.
            and Van Schaftingen,E.
  TITLE     Many fructosamine 3-kinase homologues in bacteria are
            ribulosamine/erythrulosamine 3-kinases potentially involved in
            protein deglycation
  JOURNAL   FEBS J 274 (17), 4360-4374 (2007)
   PUBMED   17681011
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..304
                     /product="fructosamine kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32795
     Region          8..264
                     /region_name="FN3K"
                     /note="Fructosamine-3-kinase [Carbohydrate transport and
                     metabolism]; COG3001"
                     /db_xref="CDD:442239"
ORIGIN      
        1 mdlaylrahp ehlptflthq riretpvsgg dicaasrltl ddghsvfakt wperaarplp
       61 egffaaeaag lrwlreagsv pvpdvfvalp dllaldwvep geptpeaaea fgrdlaglhr
      121 agapafgadw pgfigalpqd ntpdlgpwpd wfarrrllpy lrlsvdggal dgagaalveq
      181 vvdrigefgg depparlhgd lwpgnllwga ddrvwlvdpa ahgghretdl aqlalfggpp
      241 hldrimaayr eawpladgwr ervplhqlhl llvhtaifga ayadavgsta raalrgldra
      301 tvdr
//
LOCUS       WP_457606987            1011 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457606987
VERSION     WP_457606987.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1011)
  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 1011)
  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   3  (residues 1 to 1011)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1011)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1011
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=111286
     Region          1..233
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          130..1008
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(807,810..811,813,843,846..847,850..851,853..854,883,
                     886..887,890..891,894)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          807..830
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          841..871
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          882..910
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          915..951
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          956..989
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdirllgvpe vwqgavplpl gtpkqqtala vlvlhggqlv tvdtlvdelw pddpprsala
       61 nvrtyvgnlr rtfdrhhgpt lvrlsggyrl dvddervdvr rfehltgeaa sawsdgqher
      121 vdellgqger lwrgplvagl rvgpvltarr aaleeqrlaa ielrarldva lgrtraaial
      181 ltdhvnshpy reqahallas alkadgdagg alaviqraes ilirqlgvep gtellslrrs
      241 llgrtaghsp saarkggper ggavtssarr vhprhlprnt adfigrrelv ermlaeigas
      301 gdeaptvrvi dgmagsgktl falhlahlls drypdgqlfi dlrghtegap vepgdaltvl
      361 lrqlevpagr ipsdheerae lwqrelrgrr vvlvldnaad gqqvrpllpv gsgsavlvts
      421 rrrlsvsdig ppvslpvmts deavellart agteriskep daatevarrc ghlplavrla
      481 ggwlahrpaw rvadlarrle aggtvlrrla veqqtvagaf sasyehlsep vkwlfrligl
      541 hpgdsfdarm aaalaalpld rtermlddll dqhlieevap gryrmhdlmr qysaelfres
      601 tdpaqrhqag nrlldhvlhq vavrassldq qvlathlrle aplradline tdnsdiewle
      661 qerlnliali rfalqeeghs gyawrlaram wrfcymrgyf gdivathqtg ltaaersgdr
      721 aaqavmhnyl asaytrtgsy ldslrhleva vsisrdlhdr rnehryranl vvvhwltgss
      781 ersvslgrql lredtrgavd pivalpnlgy aliavgryre alrahrqhlf larcqgnwfh
      841 msnalghias venrlgnhrk aarlivaslr lraqnghrfg eaearnelgi ayrhlgrlae
      901 arsqhelald lardssdrhv qaaasndlgl tlaaaghvdq aasahrealg lasriahpye
      961 qgralsalad hlagtdaaea dryrqralai fermgaperh dlrrqlaetp a
//
LOCUS       WP_457606989             844 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457606989
VERSION     WP_457606989.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 844)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 844)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..844
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=89902
     Region          135..788
                     /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 mtrahardng tdrrllllvg lvvfvaglat lvsirliaag dlatqknitr aatiaflvav
       61 aatvnvriri ratthgvswt daasviglav apvpwviiat glgvaitrli grltpiklvf
      121 gvakemtlaa aggvvliaag wswpwsgpid rslpalvlay vtvvvldell tfpvlafatg
      181 tpirkhfreq ldlrlaivla rfsvilctll ilridptfli vvpplvlslh layssrlrnr
      241 aereawqrla rttdalnvvd ldrvlttavt qatelfsade veielreeal vvrgvggait
      301 yrgpagepsa iegsvltnrl eghdktvdvg vlrlrfagpv elsereqytl rtfasalcta
      361 vrnaqayael ariaedhaya athdaltgls nrrhlldegs aqltsrhadg vtalvlidln
      421 hfkevndtlg hgagdqvliq vaerlrgaar pddlvarlgg defavllrgl papavaahra
      481 eallaalhdp ldldgmrisv easggiavap atggmaellr radvamyqak ragqrvatya
      541 pardtadlsr ltlggelpra vadheftvnf qpivdlgsge vigaealarw hhpthglidp
      601 lrfleavers gllpafaeai ldqaliaags wrdagfdlpv svnvsprsll darfpgavla
      661 rlrahdlppd rlvleltetl tlsqldvvdr vlsrlrdsgv rlalddfgtg ysslsllsri
      721 pvhelkidrs fvgametape aaavirstld lgrsldltvv aegvesepqr ralwelgcaa
      781 gqghlfarpl paaallaalq rgnggrtgal apalhdtgav irlpgrrtgr trpappaasd
      841 arqp
//
LOCUS       WP_457607009             247 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607009
VERSION     WP_457607009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=26672
     Region          1..241
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mlivhvpagm rqaylisvpr dllvalppap gfpggqdkvn aayehgggge ggarllsttl
       61 nrltgirfdg aalvdfsgfk evidqlggir mcvdtpvrsi htryqfeagc qqmdgartld
      121 yvrqrydlpg gdfdrqrhqq qmlravldra getrlrsdpv kldrvlraag galtvdtngv
      181 pldellfalr glpadalrgv qvpsypqtid gvsyvvlddg gaglfgalrd trvpewagan
      241 prwvnrl
//
LOCUS       WP_457607006             480 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607006
VERSION     WP_457607006.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 480)
  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 480)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..480
                     /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=50165
     Region          248..470
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpttaptqpt vptpptgpvr pgrrpgrtlt aravvatcav alvsvlvtal vavplavrga
       61 errdqealaa qarlaadvlr vrpvrqrdga gdrlirqlrq qqidvyvird gradrpglpr
      121 plvtrvagge nvsgrrlvdg errlvearal pggdgvvltr arsaapwrqv lrglwlplla
      181 glaagaaagl llarrlarpi rtaataaarl ragdravrvp vespdevadl ayalnglaaa
      241 latsegrqre fllsvshelr tpltairgya ealadgviea davpatgrtv laeaehldrl
      301 vrdllalarl eavdfplepv pvdlaglaad aerawsgrca algvpfrlet pgapvpaytd
      361 pgrirqvvdg llenalrvvp pgapvvlavr adgpagggml evrdggpgft dddlrvafer
      421 galheryrgv rkvgsglgla laaglvrrlg gdiaarhape ggaaftvrvp pdpyaartsa
//
LOCUS       WP_457607012             829 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA gyrase/topoisomerase IV subunit A [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607012
VERSION     WP_457607012.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Nollmann,M., Crisona,N.J. and Arimondo,P.B.
  TITLE     Thirty years of Escherichia coli DNA gyrase: from in vivo function
            to single-molecule mechanism
  JOURNAL   Biochimie 89 (4), 490-499 (2007)
   PUBMED   17397985
REFERENCE   2  (residues 1 to 829)
  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 829)
  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 829)
  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 829)
  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 11415135
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..829
                     /product="DNA gyrase/topoisomerase IV subunit A"
                     /EC_number="5.6.2.2"
                     /GO_component="GO:0009330 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) complex [Evidence
                     IEA]"
                     /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=89017
     Region          27..816
                     /region_name="GyrA"
                     /note="DNA gyrase/topoisomerase IV, subunit A
                     [Replication, recombination and repair]; COG0188"
                     /db_xref="CDD:439958"
     Region          574..631
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          637..680
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          684..731
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
ORIGIN      
        1 marrkddrak adlaafdqag arvfdnplvt evsdsyleya fsvihsralp dardglkpvh
       61 rrilwsmyeq ghrpdrshvk sarivgdamg kyhphgdtai ydamvrlaqd fslnvplidg
      121 hgnfgspddg paaarytear msreamllvg elgedtvdve pnydgsltqp tvlpaafpnl
      181 lvngasgiav gmatnmiphn lgevvqaarw linhpdatld klmefvpgpd lptgglllgl
      241 devrrayetg rgvvrmrgrv eigplegsrg rqaitvtelp ygvgaekvia aitnevnktk
      301 rltgiadvkd ltdrengtrl vveckvgvnp qalladlyrl tpleqsfgvn nlvlvdgqpr
      361 tlglkelldv flahryevvt rrsayrkrkr eerlhlvdgl lialldidrv vkliraseda
      421 qaakdglmqk fklseiqasy ildtplrrlt kydrleleae qeklrgeiae lskilddpkv
      481 lrkvvsdela avvkqfgapr rttlvdgdlk evlaasvpag plevaddpcq vilsatglva
      541 rtaaeseeaa earrrsgrvk hdavraivhs targrvllvt sagrafkidv lplpvlpeqs
      601 gtvslrggms aaelvplepg etvvglaplg psaqgspgla lgtragvvkv capdwpvrsd
      661 efevislrdg devvgatwlt dgaetlafvs seasllrfaa svvrpqgpkg ggmaginlpg
      721 darvvffgai rtddakhgep mvvtstgatv kvtpfkaypa kgratggvra qrflkgelel
      781 svawigprpv gatatgdpve lppadprrdg sgfavmlgpt vvghhidrd
//
LOCUS       WP_457607014             685 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607014
VERSION     WP_457607014.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 685)
  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 685)
  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 685)
  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 685)
  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 685)
  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..685
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..685
                     /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=74460
     Region          4..679
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaqpetlyg addlthlegl davrkrpgmy igstdsrgvg hlvneildns tdegvaghat
       61 tvdvilhadg svqvdddgrg iptdvhaksg isgvelvltr lhaggkfggs gyktsgglhg
      121 vgasavnals rrfdvtvrrg gkvhamsfrh gvpgvfdgdg pdapftpgpg lqivgamkrg
      181 qrtgtsirww hdpryfetga aldtetvrlk lrntaflvpg vayrlrdetg eqsveesfhf
      241 pngltdmvef laptgdrpvs gtllvtgegt yrenaadang vmqsnvqrra evevafrwgt
      301 gyertvecft ntirnahggt hrkgferala rtlaeaarna rgllkpkeda ptlddvlegm
      361 tavvhvripe pqftsqtkde lstagitkvl qglveahlks wlddrrtkae artvlqkivd
      421 aarvrltqkq qkdaarrkta legaampakl vdcraagier selfivegds algtgrlars
      481 seyqallpir gkilnvqkas lqqvldnaec aaivqvlgag sgrtfdlstl rygrvlimad
      541 advdgahirt llitlfarym rplieagrly aampplhkit tkgrnpqtvy tytqaemeat
      601 vrklekagkq ivtpiprfkg lgemdadelw ettmnpatra vrritlddve aaerilellm
      661 gekveprrnw lidsadrvdr daida
//
LOCUS       WP_457607054             189 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607054
VERSION     WP_457607054.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   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 189)
  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 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   5  (residues 1 to 189)
  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..189
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..189
                     /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=20185
     Region          90..178
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(109,128..129,146,150,158..159,170,175)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mttdgtnaan sgtdpserpf slvigvtssp aerlrltell dgvapllmva dldelrelit
       61 dapasarapa pavapaapvp rakpapdgal vidaarstar wgdretaltr lerdlltclt
      121 vepvrvwsya elhhavwhda pthgradvqs lvkrlrrkld elgtgvtiaa vrgvglrltd
      181 hrhprvrgd
//
LOCUS       WP_457607069             314 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607069
VERSION     WP_457607069.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..314
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=33201
     Region          11..310
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mtkadvvvvg ggvigmttal tlqrrgarvt vltahdpadt vstvaaavwy pshteedprv
       61 lrwardthae lrrqaadgvp gvvdrptrmw lrhpctgppw wadacgdlva epaeppytal
      121 lrftapsvem tsyltwlrer leagggrvvr ralgtlaeay evapvvvnat glaagwlaad
      181 psvyparghv llvanpgltv svrdeddpag vtyvhprrhd vvlggtyeag vghtrpdpee
      241 aaairrrcva lvpqladapv lgeriglrpa rhggprvevd padgrlvhay ghggagvtls
      301 wgcaaevadl alsv
//
LOCUS       WP_457607080             245 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607080
VERSION     WP_457607080.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..245
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26408
     Region          7..119
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          134..242
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 matrlvqinm kahdevalgg fwakvlgwgi sseapgvtnl epedltypdp ralyidlvvs
       61 tepktaknrv hvdlattsaa hhaelvarlt algatpadig qgdvpwtvla dpdgnefcvr
      121 epnprhaetg piaevvvdca dprgmadfwg ratdwtvhev tdrqavlrsa qgvgpylrfa
      181 rtadaktgwn rvhldvcpyp sddldaetar lrslgatdad lggadipwrv lvdpegnefc
      241 vltpr
//
LOCUS       WP_457607083             158 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607083
VERSION     WP_457607083.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..158
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17003
     Region          5..140
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mrarterhgd eliarrhlpa apdrvweaft spsgiaafwg gshasvppgs vtvdlrpgge
       61 faldtrapdg rtgrlrfvyv svdeprelvf depvtglrtt vtlrpagygt dltvhqrklp
      121 pelrtdqaad glasildala ahlrhhddgd dsdpsnpa
//
LOCUS       WP_457607098             421 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607098
VERSION     WP_457607098.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 421)
  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..421
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..421
                     /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=44567
     Region          5..414
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 msaayspeqp svllgnctvl darvvdgmap vtgagvwvrg driaavgpya evaeqaraag
       61 rltevdldga yvtpglvnmh thfslslpgs agegvkgmga ydlahymadg arrtlhsgvt
      121 tvrcvaekdh adfalrrain agrvpgpriy tagralvctg ghghesndtl ecdgpvgfrh
      181 gvrsqikaga dlikvmisgg iagehesiht pqlfademsa vietahawgr kvtahagpad
      241 vigaavelgl dcvehgyqlt pqvaarmaer gtalvptllv trckeffdel gvpewmqcrs
      301 lgagprhles fdtaiaagve vllgsdmppf wefegttasi releymseri gtaraihagt
      361 lgpirwlgae sdlgtvevgk ladliatdad pladtsafrd vrwvmkggri arddrnqeet
      421 r
//
LOCUS       WP_457607100             556 aa            linear   BCT 27-JAN-2026
DEFINITION  hydantoinase B/oxoprolinase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607100
VERSION     WP_457607100.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Watabe,K., Ishikawa,T., Mukohara,Y. and Nakamura,H.
  TITLE     Cloning and sequencing of the genes involved in the conversion of
            5-substituted hydantoins to the corresponding L-amino acids from
            the native plasmid of Pseudomonas sp. strain NS671
  JOURNAL   J Bacteriol 174 (3), 962-969 (1992)
   PUBMED   1732229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..556
                     /product="hydantoinase B/oxoprolinase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59966
     Region          3..555
                     /region_name="HyuB"
                     /note="N-methylhydantoinase B/oxoprolinase/acetone
                     carboxylase, alpha subunit [Amino acid transport and
                     metabolism, Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0146"
                     /db_xref="CDD:439916"
ORIGIN      
        1 mgeptvdgat vevvrshlvs aaeemraalv rtafnpviye vydfgisvyd rrlrlvaest
       61 glsrflgand yslrkgveyv gvenlhrgdv vllnypywna ahtydatmfa pvvlpdseel
      121 igylcirahw mdlgakdpgy vldstdmhqe giifpgtkvy argepvpeih elirfnsrmp
      181 elvlgdlnaq iaalrtgerr vtelyrhygp avvdavvdrv idaaaqraea avaalpqgsw
      241 taedwldddg vsddpilmrv tvtiadgaft vdfagsspav pgpvnlplga tiatcrvafk
      301 gvttpheqtn aghfaplrvr aepgtlfhaq ypaatftqwt gtvalelilk alaqgmpdrl
      361 aassggdvpg fmmvgrhpdt gdmfavsnnd pvgwggtprh dgigpanhlc qtqarntpve
      421 vlesktgmff erleirtdsg gagrfrggcg lrrdirfvtp geflsvikkt rsapwalagg
      481 eqpepnqvvv fpgtdrehrv strrtavavg drvtlltagg gghgdprsrd peavrrdvae
      541 gyvsaraard vygvit
//
LOCUS       WP_457607113             138 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607113
VERSION     WP_457607113.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..138
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15485
     Region          10..127
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mskpplpepa vamlgkpnpa viatlrdgqp vsaatwylwe ggrvlvnmde grrrlahlrs
       61 dprvsltvld egnwythvsl igrvvelrdd egladidris qhytgkpypr rdrarvsawi
      121 eierwhgwga hkdnsqtg
//
LOCUS       WP_457607119             333 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607119
VERSION     WP_457607119.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 333)
  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 333)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..333
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37168
     Region          5..186
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,95)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            93..95
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mrlsvvvpcf neeasverlh emlsvafael tdvdvevvyv ddgsedgtla alrrlaaadp
       61 avcytslsrn fgkeaamlag lrratgdavv imdadlqhpp rllpemvmly rqgfdqviar
      121 rdrrgdrfir mvasrsfyrl vnwwidvrll dgagdfrlls rlavnailam peynrfskgl
      181 fswigfrtav vahrnetrqa grsrwtfgkl fnyafdglls fnnrplrlai ygglfltlia
      241 vgymawvvad avekgidvpg yttiivsvig lggiqmmilg vigeyigriy yetkrrphyl
      301 vqetervvda pgrtsripeq rvatgesmag etg
//
LOCUS       WP_457607122             373 aa            linear   BCT 27-JAN-2026
DEFINITION  SPFH domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607122
VERSION     WP_457607122.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11213143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..373
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=39991
     Region          23..233
                     /region_name="Band_7_1"
                     /note="SPFH domain-Band 7 family; pfam13421"
                     /db_xref="CDD:433193"
     Region          310..359
                     /region_name="GYF_2"
                     /note="GYF domain 2; pfam14237"
                     /db_xref="CDD:464112"
ORIGIN      
        1 mdklrgelid iiewlddsrd tmvwrfpryq neikmgarlv vresqtavfv negkiadvft
       61 pgtytletrn lpilstlkgw kygfnspfka evyfvntrqf tdmkwgtqnp vilrdaefgv
      121 vrvrafgafa arvvdasrll relvgtdpqf rteevqeylr qlmvgrlgga latagvplld
      181 laahqdaigr rlaavlteel aevgiaiptf vienvsvppe veqaldkrts mgavgdldry
      241 trfqaaname aaannpggea gagiglglgm amgqqmarsm gpgaatqpaq papaqpaaae
      301 ppplpgqaqw yvgvggqrqg pydlgalaeq anagalgadt lvwrtgmaqw qpagqvpela
      361 svlasvpppl ppq
//
LOCUS       WP_457607142             415 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607142
VERSION     WP_457607142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..415
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=44986
     Region          4..409
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mststdfsva isgaglsglc laqyltragi dvhvyerdpg pfvrrqgyri ildryglaal
       61 reslprplyr lalatgdepg ghlrftdrrl rdaftitfkd dphetrqvdr ltlrsilqsg
      121 ldgrihydke avavdsggpa glrlrfsdga aaaatvvvga dgvgsalraq lmpdadpvdt
      181 pmagiygrsp lrrdgasvip dalrtsgvla iadrpgsaff ftsmrfgesp reaftrlapg
      241 syaptgddyv mwalllrrde lppgvrgdlr alwhvaarks idfhplvrrl vdtaeldatv
      301 lnlfatgrrp hrwavpratm mgdavhvmpp fgahggntal rdaallghkl vearrngtsv
      361 eeaiagyqde mvpyafhavd naarlmhrlt ggaaaphwvl trvlprlhrv tvpea
//
LOCUS       WP_457607139             127 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607139
VERSION     WP_457607139.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 127)
  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 127)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..127
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13614
     Region          14..102
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mgsasrpalr epsyfvlaal lggplhgyav ikrvtelsgg rvtlaagsly svidrllgeg
       61 lvtadgeeiv ngrarryyrl tdegcrvlte eadrlaqaar vvmdrlprre asqagarhps
      121 tvrirpa
//
LOCUS       WP_457607155             249 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607155
VERSION     WP_457607155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26251
     Region          6..227
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mgqtvepavr ierlsrvygt grnqvtalag vdvgfgrgtf tavmgpsgsg kstllqiaag
       61 ldrptkgrvv vggtdlsgls etrltelrrt rigfvfqafn ligaltveen ivlplrlagv
      121 rpdrawlthv vervgladrl hhrpaalsgg qqqrvaiara latrpevifs deptgaldsr
      181 taaevlallr avvdehgqtv vmvthdpiaa scadrvlvla dgamvadlpq lgavriaehl
      241 asldgrvlr
//
LOCUS       WP_457607164             227 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607164
VERSION     WP_457607164.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24060
     Region          3..221
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mslnltditl typdgegrlt aldrvtldvp rgsltavigp sgsgksslla vaatlitpds
       61 gtvtidgtat tgmtrgelad lrrhkigivf qqpnllpslt aaeqlqvmaq idgrpparar
      121 travelldav glagqadrrp hqlsggqrqr vniaralmnd ptvllvdept saldhergaa
      181 vielitrlth qqttatvlvt hdrthltavd qiaevhdgrl hlpaqar
//
LOCUS       WP_457607167             363 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607167
VERSION     WP_457607167.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..363
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36635
     Region          18..191
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          128..361
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvawrdlkf akgrfalmgt vivlitllvg llsgltaglg rqnisaiadl pvdriafqap
       61 gegqdvsysn stvtekqwqq waeapgvtga eplgitttra tagnrsagvs afgvrpgsrl
      121 apdsgriddh savlstkaad dlgvqagdsv tlagqrltva avrgdasfsh tpvvwislgv
      181 wqksapptgt gdgsptatvv altttsdvdp aatdrqagtr tvsvsdslsa igsytsengs
      241 lqvmrgflfa isalvigaff tvwtiqrsgd vavlkalgap tanllkdalg qavvllvggt
      301 llgtgiaaal galvagstvp flltpvtvll paavivvlga lgaalairri tsvdpltalg
      361 sar
//
LOCUS       WP_457607172             255 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607172
VERSION     WP_457607172.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..255
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28380
     Region          4..>63
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..253
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mivrtvgell rqwrqrrgls qldlaiaadv sarhvslvet gkskpspdmi lrladqlhvp
       61 lrdrnrllla ggfapryaer sldhnalsav hdavrrvlra hepypavvfd rrwnivmtnr
      121 avepffaqva pdllrppvnl vrlgldprgl acmvvnladv ravfrtrisr qlatapdpel
      181 talyeellap epentssqri eadvvipmil rvggrelrlf stittfgtpm ditideiaie
      241 syypadaasa ayftt
//
LOCUS       WP_457607177             128 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607177
VERSION     WP_457607177.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..128
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13939
     Region          10..126
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mwtfrspqlv lfsddltrav afynrlgfre tfrvptdgep ihvdlvldgy kigiasvast
       61 redhgldpva egqrvavilw tddttaayeg lvadgapala pphvwlgrll iawtadpdgn
      121 piqivqsr
//
LOCUS       WP_457607182             316 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607182
VERSION     WP_457607182.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..316
                     /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=34084
     Region          2..314
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrptarvla lleilqaggg ftvadlagrl gvdertvrry aahladlgip vearrgrygg
       61 yrlapgyklp plmltdeeav avmlglvaag raglvtaega avesatakir rvlpavlarr
      121 idslletvdf tararkpapa gievllvlad aarhqqpvti tyttwrgesa errldpyglv
      181 fhagrwyvtg hdhhrravrt frldrigtah ptpgrfeipa gfdpttqvlt glaavpyahe
      241 isvvlhtsle qaqrripqsv gtlievsggv rltaraerld gaaqmlaglg wsftidrpde
      301 lkdevralan rllada
//
LOCUS       WP_457607192             362 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607192
VERSION     WP_457607192.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..362
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39802
     Region          1..106
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          72..361
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mtpfridvpe avlddlrarl srtrlapaap gepwaagtdp gyladlvryw ldgfdwraae
       61 ralnrhpqfv ttirgtpihf vhvrsaspda talilthgwp stytemlplv srladfhlvi
      121 pslpgfvfsg plaegpttea avadvwaelm trlgydrfga yggdigsgvs twlgarhadr
      181 vigvfsqhik fppadrrddl spaeeafiam ldakaqddwg ygiiqetrpd tlaaalsdsp
      241 sglaawivek yqrwsdcggd isrrfgvdel lttvmlywvt ncigtsfrpy rddrlaphlp
      301 mvtvpagitv svedaglprs faertyadlt hwrepsvggh flaqeepdll aadlraffsa
      361 lr
//
LOCUS       WP_457607205             398 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607205
VERSION     WP_457607205.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..398
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42893
     Region          7..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 massvdprfg valrefrerr glslrslgql ahrskshlhe leaalkaptv dtarhldril
       61 daggvlarlv dapidhaaea gelrarvavs dvsndtleri eqgvddlass yptmapadll
      121 plvrrhlsyv vrlldgrvtl aqqrrllvag gwlavlratv hidlrqrnaa aahlraardl
      181 aehaehpeiq awcletrawd vltqgdyrsa ldlsqqaqrv apqgssariq ataqearawa
      241 rigdvaatrr tldrversaa nlpiperaeh hyrydpakaa aytattlawa gdpgaeqvar
      301 avladldpyg dggarprrsa sarldlglal vaagqpdeav algaqavasg rvvpsnwwra
      361 aellakvedl gvpeaamfhe lcveyapgrr stadstpg
//
LOCUS       WP_457607234             349 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607234
VERSION     WP_457607234.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..349
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35658
     Region          8..336
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mgsagvpvvv gldnggtsdn atvltvdgrf lvdglleiss dvgagpeaav ealvrafdgv
       61 lahtgvprdl vravgldtpg pasatgviss rgstnfsqpa wrgfdvrtal errlglpvvy
      121 andgnaaaly ahhvyfgaea marssvsaiv gtglgggvve sgrvvggaag magefghvhi
      181 pldgliepdq aapvcacgft gdaesvaslt airrnllpyw larhpehpla aeepdraakl
      241 lrgygergda larlvfaqqa kalgrlftia anftdphayf vgggvveaap efrdwflaav
      301 aehtvlreeq ravatfalvp drdmagargv aiaaleavrg aataaapla
//
LOCUS       WP_457607252             190 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607252
VERSION     WP_457607252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..190
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20939
     Region          8..180
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 midfsvkptl tgervvlrpf hdddlpalae iladpevvrl tgspagetfe psrlrawygt
       61 rnsqddrldl avvdrasgtc vgevvlnewd rvnascnfrt ligpggrdrg lgteavrliv
      121 gygfeqlglh riglevfafn prarrayekv gfvaegtlrq vlrdgddwad atvmsilape
      181 wnrhrghpeg
//
LOCUS       WP_457607259             330 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607259
VERSION     WP_457607259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..330
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34091
     Region          25..328
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mitlprppra gtrsgrlatv acwlavapva awalvrltgl ergplvqaia ftpyaaavap
       61 vvavaalalr rrapamvavl aaltligava praipgdrpa adgptllllt anlrlgsadp
      121 aalvdlvrar rvdvltvqel tpplaaeldr lglatllphr sltpevgstg sgvyarhplr
      181 dtghrrnrgf fftqayatvt vpgappvrve sahpaapyap dvvpdwwtdq raqppatpdg
      241 glsvlagdfn atldhaalra liatgytdaa daagagfggt wgpydgdpip pvtidhvlvd
      301 rriavraagt hpvpgsdhra llaelrlpag
//
LOCUS       WP_457607224             418 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607224
VERSION     WP_457607224.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 418)
  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   4  (residues 1 to 418)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..418
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44020
     Region          69..333
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          343..417
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mdldlgreql vvvgasfgsl swfdqelppg svvlveepdv iarrdlagfa erlpmigrlv
       61 aaeyqtgfdp dallarepgl adarlvlpgl eyavgatarl aerlglpgag veaadvfsdk
      121 hrmrlladri glanpayelv ddparavefa qahggrcvlk ptrrsgslgv qlitdaaevp
      181 arwaasatpp dpaeatergl ptgvlveell vgsehsvell vaegevvfgn vtdkriaggr
      241 ypvetghtvp salpadahda lraaavrlae aagfrsgmlh sewiladgvp tlvecaarmp
      301 gdmitalisi ayerdvieay lrilrgerpa mparatgaaa iefliappgr vtavdgrrda
      361 lrvpgvldvq vetkvgqtvp ellssahrsg hlmtwgatpd eaadaarraa sqiritvg
//
LOCUS       WP_457607282             846 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607282
VERSION     WP_457607282.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 846)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..846
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=89877
     Region          17..824
                     /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 metgdprnsv ppgrsgpffg fvaaigaval lvsagplval adrltelpaa fwtmavlava
       61 cdarpfvppg rrqtsavfps tcftfaillg wgfgpavavq avavavsgwr lgyapwrtgf
      121 naaqyacala aayavtrlgp gelfgggrlh wtdvaavgga tlawfvvnyg lvssavrlrf
      181 gdrwwpsvrs glayellstg sllllapvlv aaarasaali plvlvplfav yrmarlseer
      241 eqladvdplt glpnrkallt evaeqvhlhg eraargapda hlalllldld rfkhvndalg
      301 havgdrllve vsarlmgavd ggdmvarlgg defaivvprl tdidqarera drvvaalaep
      361 vpldglpldv ggaigialyp dhgedfatlm rhadvamyda khrndtvavy apesdhnsae
      421 rlslladlrr vlesgpsaqg getvgvrggd gaaltpalpv radrparnqr pardggrgrs
      481 gdgpnrwlrr rrdraeerhd ddlieqiltr adpirrraar agagpgagpl vvgdaefape
      541 tetadadltq daeaavstga pgvigptadg staaeadepa ghpgeitmyy qpqiaiatge
      601 vvgveallrw rhprrgmvdp geliqvaeqs avmrlltrrv vddvveqlak wsaagltlra
      661 alnvsvrdlh tgeiadqiad rltrygvppe rlqveitega lmadprrvla sitqlhrigv
      721 gialddfgtg ysslqhlrrl plsevkvdrs fvlgmaedpd daaivrsmie lagalglrvv
      781 aegvedertw rllhaagcdv aqgwfharpm paedlvawls ryrpvrpaea vsrggpapeg
      841 eskass
//
LOCUS       WP_457607299             484 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607299
VERSION     WP_457607299.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..484
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48677
     Region          28..>319
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mgldpglrrl algtllaayp gpvppdwavd lladglaght lfgtnihdpa qvaastaalr
       61 agrpdvivai deeggdvtrl ahatgspypg naalgavddp dltrrvyaai ggelaalgit
      121 vdlaptvdvn tadenpvigt rsfgadpkrv avhsaaavag lqstgvaaca khfpghgatv
      181 adshhelptv dvppavlrer dlppfaavvd agvravmtah irvpaltgdg patfsravlh
      241 dllrveygft gavitdalem kgavlaaggv gagavralaa gadllcigar vdaelvesva
      301 aeivaamadg rlarerveea agrtaalaaa tgpadapppa adglgyaaal ravrvegdlv
      361 rdaaplvvqv hapstiaegr vpwglgphla agveqarava getdpeqvrr lagdrpvvlv
      421 grhlhrlpga relvealaat hqvtvvemgw pgawrpagar afvathgash angraaadal
      481 glta
//
LOCUS       WP_457607302             221 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607302
VERSION     WP_457607302.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..221
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23745
     Region          148..221
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mldrrvflhl atwlgqwpag pglhvvrshr rarpawdgrl rpavavtagg stvlsvaadr
       61 veavrtlvrd rplgewlpdl pgavgtpefv ahtsvfrwct dpaplpevge wvpptlpglp
      121 pwlrlfdrev lvvrgadgay ragvgikrhd ayghelavgt vptargrgla rrlvaqaarr
      181 vldegaipty lhdpgnvasg rvaeaagfpd rgltafgvfp r
//
LOCUS       WP_457607340             319 aa            linear   BCT 27-JAN-2026
DEFINITION  formylglycine-generating enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607340
VERSION     WP_457607340.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510263
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..319
                     /product="formylglycine-generating enzyme family protein"
                     /EC_number="1.8.3.-"
                     /GO_function="GO:0016670 - oxidoreductase activity, acting
                     on a sulfur group of donors, oxygen as acceptor [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33856
     Region          47..319
                     /region_name="FGE-sulfatase"
                     /note="Sulfatase-modifying factor enzyme 1; pfam03781"
                     /db_xref="CDD:397722"
ORIGIN      
        1 mstepvdpgd gggtpppspc caprrppaag sgaaagasav rapfggtddl ialpggtflm
       61 gtddpegfpd dlegpvrpvt vgpfaigatp vtnrqfarfa datgyrtdae qygwsfvfhl
      121 llvpsahpyv ldasvpqapw wlavegaswa apdgpgsdvr greqhpvvhv shrdaeaycr
      181 wsgtrlatea eweyaarggl sqaryawgde ltpdgrhrcn iwqgvfpavn taedgfagts
      241 pvtafppngy glydvagnvw eltaepwrdh rgrispgesv irggsylchd sycnryrvaa
      301 rsrttvdsst gntgfrvar
//
LOCUS       WP_457607328             226 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607328
VERSION     WP_457607328.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23775
     Region          1..218
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mspmieardv tyafgetpal rgaslavaag evvavmgpsg sgkstllhcl agilrpdsge
       61 vrfdgtridt lgeadrstlr rdsfgfvfqf gqlvpeltaa envalplllr gvrrtpalra
      121 aqgwferlgl aglehrrsge lsggqaqrva larglvaepr vlfadeptga ldsltgeevm
      181 tllvdaarer gttvvlvthe ariaayadre vmvrdgrvna pagvas
//
LOCUS       WP_457607344             414 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607344
VERSION     WP_457607344.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427748
            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="M20 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42976
     Region          16..402
                     /region_name="ArgE"
                     /note="Acetylornithine
                     deacetylase/Succinyl-diaminopimelate desuccinylase or
                     related deacylase [Amino acid transport and metabolism];
                     COG0624"
                     /db_xref="CDD:440389"
ORIGIN      
        1 mtsdthaslr aghlvdahav vtltqdlvri pstwdagrgr seqpvadlva evmrgfgwrp
       61 evtdvvpgrp nvvavvdggl pgptlmfegh tdvvtegape ewtvdpfggd ivdgrlygrg
      121 sadmkagvaa mihatravel agpfpgrivv aalvdeegqm lgakhfttta larevdaaii
      181 cepeaeeica vakgavrllv tctgkmahga mpqhgrnpvp avaelvaalg ryqkelqaap
      241 gehehlglty ltptvldags adqlnvipgr avlgvdcrtv pgvdhaalaa rvradaeaig
      301 arhgvtfave vvddrpcavt pedhpislav adahravtga epvfggvpga tdgtilwrds
      361 gipnvvygpg pkwiahqpde yvevddivrk tkvyaeaala fltgatgart gaas
//
LOCUS       WP_457607348             766 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607348
VERSION     WP_457607348.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..766
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84593
     Region          34..530
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(44..45,82,140,142,235,341..342,402)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(44..45,82,140,142,235,342,402)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mtgpladppy egtigrtyde stehwsapps aaagtpnvvy vllddvgfad fgcfgaeidt
       61 ptidrlaasg lrytnfhtsp lcsptrasvl tgrnhhsvgm rmlsnfdsgf psgrgritha
      121 aatvaemlad agfntmavgk whvapldqtt psgpydqwpl grgferyygf leaetdnfyp
      181 elvydnhqvd ppatpeegyh ltedltdrai gfvrdqtsft pekpfflyla yaaahaphqa
      241 ppeylakyrg rydagwdvvr adrhrrqigl giippdaplp phnpgvvpwd dvppeqrrlf
      301 armqeayaam vdhtdaqlgr lvdfleridr lddtifvvms dngaspegtp lgtlnptafq
      361 nrvpenlqds ldrideiggp raqsnyplgw aqvsntpfrr ykqhtheggv rvpfvlswpa
      421 gdvpggevrt qfqhsidvta tvldlvgvrp pavrrgipqm plhgrsfrdg lrdpaappsr
      481 drqyfemfgh rgiyhqgwka vafhergtsw dedrwelyri dedptesrdl aaehpevlrr
      541 lieefwieaa rydvlplddr gfairarvpr pgsvrdrldf tylagvptis gaavpptmnr
      601 shaitarvhr taatqggviv vlgnvsggyv lhikdnhlvy eynhlgtryv lgsegelplg
      661 pveltfeltk tadcqgvgrl yvdgeaagea lfprllpffh gfagmdvgrs ihspvspsyp
      721 arhefsgele yvrfrlaase evgepiapag gvaprpsvgv gfevvd
//
LOCUS       WP_457607350             428 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607350
VERSION     WP_457607350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..428
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45431
     Region          3..421
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 msvqqfrlpd vgeglteaei vtwrvapgdp vglndvivdi etakavvelp spyagvvdrl
       61 laeegqtvev gapiiairvp gdgpatpsad epptgdepaa hepavertav lvgygvsaqa
      121 rtrrprratp svrpagparp ahtsrppvlt kpplrklakd lgveladvrg sgpggritrq
      181 dlldhttgpa pvaahrrder lpvrgvrkat aaamvasaft aphvtefltv dmtgtvefvd
      241 rlkqdpafqg vkvspllvas lavldairry pdvnsrwdee nqeivrfadv nlgiaaatpr
      301 gllvpnvkaa qnlpvrdlav alnelaatar egrtrpadls ggtititnig vfgvdagtpi
      361 lnpgeaailc lgalrrmpwv vdeqvvprwt vqlslsfdhr lvdgelgsrv lahvgrfled
      421 plwglalr
//
LOCUS       WP_457607352             322 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607352
VERSION     WP_457607352.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..322
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34563
     Region          2..321
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mltlsqalns glrrameddd kvllmgedvg rlggvfrvtd glqkdfgear vvdttlaesg
       61 ivgtaiglal rgyrpvceiq fdgfvypafn qivsqlakmr artggrtalp vvvripvggg
      121 igavehhses neayfahtag lrvvycaspd dahwmirqav agddpvifye pkrrywvkge
      181 vtpagpplpl drartvrpgt dvtvltyggt vatcvaaaea aaregrdlev idlrsispld
      241 vatieesvrr tgravvvhea ptfagfgaev vaqvtsrcfy sleapvervg gfnlpyppak
      301 veeeylpdld rildavdrvl aa
//
LOCUS       WP_457607372             345 aa            linear   BCT 27-JAN-2026
DEFINITION  cobalamin B12-binding domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607372
VERSION     WP_457607372.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Krautler,B.
  TITLE     Vitamin B12: chemistry and biochemistry
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 806-810 (2005)
   PUBMED   16042603
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Marsh,E.N.
  TITLE     Coenzyme B12 (cobalamin)-dependent enzymes
  JOURNAL   Essays Biochem 34, 139-154 (1999)
   PUBMED   10730193
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472039
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..345
                     /product="cobalamin B12-binding domain-containing protein"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36101
     Region          12..220
                     /region_name="MtbC1"
                     /note="Methanogenic corrinoid protein MtbC1 [Energy
                     production and conversion]; COG5012"
                     /db_xref="CDD:444036"
ORIGIN      
        1 mtppppdrpt paagrrigpd rlaayldrld aadragaval arglladgfs vadvlvdlva
       61 vaqrevgrrw ltgswsiaqe haathvseqv vdalgatvgp prrghvvmac vegewhalaa
      121 rivtevvraa gwrvtflgas vparhlvsyl hqtgpdavll scvqpnrlvr aarmveasra
      181 agvpvlaggp gfgpdgrwat aigaagwgas ardaveller plsaahtgap ppppddayva
      241 vlhrrrelvr lalaavdppp esaedvaagi ahlvdaliaa vrvdddrllr dfvgwqeeal
      301 tsrggralld rvlgtleral tehprvvarl raareaapdd pgpag
//
LOCUS       WP_457607385             429 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607385
VERSION     WP_457607385.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..429
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46217
     Region          9..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpdsgfpwpi ettrldnglr vvvsedrtap avavnlwydv gsrhepagqt gfahlfehlm
       61 fegsvnvakt ehmkliqgag gslnattnpd rtnyfetvpa ehlelalwle adrmgglvpa
      121 ltqetldnqr dvvknerrqr yenvpygdaw lrllpllypp ghpyhhatig smadlnaadl
      181 atfqefhsty yapnnavltv vgdttaaevf gladkyfggl aaradipaap dgrtvpatgr
      241 pavetvtadv paprvyvahr thpfgtpgyd vttvlatvlg sgrgsrlyqr ladgeriaqp
      301 dlvgaygvdl ahapapliat atarpgvsae rlrdgladvv delatvpvta aeldrakall
      361 stmwwrqmst vdgradtlgr yatqfgdpar aadrlpawla vtaeqiaeqa aellgaadrv
      421 iltylpeek
//
LOCUS       WP_457607391             266 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607391
VERSION     WP_457607391.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..266
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28040
     Region          37..154
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpahrpaepd vsryytevyv eadrldgspq grlearrtrd llarllpaap advldvgggp
       61 gayagplata gyrvhlvdlv pahvaaarsa yplvtasvgd aralpspdaa adatlllgpl
      121 yhlprqadrv aalreaarvt rpggtivaaa isrhaalidl tvqgrldddn rqllraeyet
      181 gvndprtgft taffhrpeel aadfvaaglp tpevygvegp lwpvlnalgt gpderlfadv
      241 vacaerferd aailgasahl laaarr
//
LOCUS       WP_457607405             547 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607405
VERSION     WP_457607405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   4  (residues 1 to 547)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..547
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60230
     Region          14..490
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(69,72,109,112,157,175,179,211,273,334..335)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(211,273,335)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          471..544
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mntdatqqtp gtgwwteavi yqvyprsfad sdgdgigdlp gitsrldhla elgvdalwls
       61 pfypspqada gydvsdyrdv dplfgtlada dkliaeakar glrvivdlvp nhtssahrwf
      121 teavaaapgs perqryvird gkgpdgaepp ndwvsvfggp awtrlpdgqw ylhlfdsgqp
      181 dlnwdnpevr aefldvlrfw ldrgvdgfrv dvahglikqa dladwqepqe ilsgsevdkp
      241 rppmwdqdgv heiyrewrrv ldsypgeril vaeawvepae rlaryvrpde mhqafnfeyl
      301 laawtapaqy avitrsleat dsvgapttwv lsnhdvvrha srlglgtggg rangvgvddp
      361 qpdaalglrr araasllmla lpgsaylyqg eelglpehtt lpdearqdpt wkrsghterg
      421 rdgcrvpipw eadapsygfg ptdaswlpqp pvwaeyaldr qrgvpgstye lyrtalrlrr
      481 ehalargplr flssgdevlm ftnggltvlt nfgadpvslp agaevlvssa pldadavptd
      541 vtvwfrv
//
LOCUS       WP_457607409            1014 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607409
VERSION     WP_457607409.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Shu,C.J., Ulrich,L.E. and Zhulin,I.B.
  TITLE     The NIT domain: a predicted nitrate-responsive module in bacterial
            sensory receptors
  JOURNAL   Trends Biochem Sci 28 (3), 121-124 (2003)
   PUBMED   12633990
REFERENCE   2  (residues 1 to 1014)
  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 1014)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   4  (residues 1 to 1014)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20592222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1014
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=107361
     Region          81..316
                     /region_name="NIT"
                     /note="Nitrate and nitrite sensing; pfam08376"
                     /db_xref="CDD:462453"
     Region          457..650
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mstgpttlpg spnaeqrnrr rrlprlrdar irsklalilv vpvaaviala tirlvsvgqg
       61 ayeadrvrsl savsvdiaal tqdlhkerma aavfladpnq kpdaynlrvr qtderiaayq
      121 dergklgdvs gaissqlnvi dahlstlngt rqevldrlqm pvaeaslryg ivlddlvays
      181 dalaqqpgad sladarrava afahakaeva eeqavaftal dggqvdeeqf ssfvatltgq
      241 qealltfsrs atpgqralvd rtvsgdavql adrvagdvsr sigrpalvtr deasaaigav
      301 ddlmrwaeiq lldemladad earadvirqa ivesllvllt lavavtlavv larslndslr
      361 rlregalava nhdlpdavsr lqnvnaigdg gvdeivqqvr dpiklsnrde vgqvavafnv
      421 vhreavrvaa eqaalrtsvs amflnlarrs qslvdrmige ldaierseed pkrlaqlfel
      481 dhlatrmrrn denllvlaga dsavprrdda llvdvlraaq sevelynrie fgtvdtdisv
      541 aahavndvvr lvaelldnat rfsppnttvv adgrrirdyv liqiedrglg lsddqldsln
      601 rrlaapptvd vaafrlmgla vvrrlasryg irvelrrnve ggtvaqvtlp nstvvlpanr
      661 gqapltrprq plaveqspls qvgagdalag agrgaatatl adqwrgatta ppsrwqtpae
      721 trdttpavql ggatgalptv aapapvaaap aapapvsgag wsaggptvay paldplpkrt
      781 pgvestqpat qaappayqpl aaapavestp atpvvarpeq raeapifrem eavwfrshge
      841 dettiftrpt fdeppapaqp avappaasar pklptrtpga qasglttptt ppaysppevp
      901 stppaaatpp paaepaptpp idpeawrtaa degwsrasra aepttggttr sglpkrvpqa
      961 qlvpggiepk sgrdrsrrtp devrgllsay hrgvqrgrta gadlnststk etnr
//
LOCUS       WP_457607426             242 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607426
VERSION     WP_457607426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..242
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26900
     Region          4..>62
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtesrlgrev artlrrereq agltqqalaa rsglsqaaia riergdrlps lttadrllaa
       61 lgrqlrieve pldshldaal demagtvlae rievlrldri tealgdlpyv lsggtaallq
      121 gaplpvdave iavrwrdspq fsalldrtya qrwnarwqew ggihtepeep gehrwltryg
      181 elrarmcnel pepievrlge rtypveplve vevtdrrtae llsryrrrla aatgeapdgs
      241 ag
//
LOCUS       WP_457607438             465 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607438
VERSION     WP_457607438.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..465
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48930
     Region          50..456
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(160,162..163,295..299,320,323..324,327,342,346,396)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mrrgrvwaag lvaaalalgg ctggddgngf lpgaadagdp yvpgagnggy dvghyaldvr
       61 ydpasdrltg tatltvtatr alsrfqldla gldvervrvd geaakyrhdg aelivtpsgg
      121 lpsgkrftve vayggvpqpl pnaelgdggf hatpdgaial gqpesastwy pvndhpsdka
      181 tydlavtvpd glaalsngvp qgktssggwt twrwserapm asylstlvig dyrvssgtha
      241 gkplvtavaa alpadgpaaa svartgeiad flaarfgpyp feayggvvva deriryalet
      301 qsrpvygpaf frdglpntev vahelahqwf gdsvsvarws diwlnegfat yaewlwaehd
      361 ggrtvaqtva eryadtdwsk ptvdpgragm fgdavyqrga lavhalrrav gdetfyrvlr
      421 gwlaqhrdgn vttadfvgya ertsgrplra lldawlaggt ppglp
//
LOCUS       WP_457607440             366 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607440
VERSION     WP_457607440.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..366
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=38870
     Region          69..354
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mtrrrllgla alvaallvat gavvttrlva nrpaapaagp stappasptp apttasptpp
       61 pgadlngpln lllvgvdtrv sipgwephad avlllhvpag ldraylfslp rdlvvdipay
      121 pkarypggrt klthamsygs rvpgdkrnps taqgyellrt tvsrytglri dagavitfgg
      181 fdklvdtlgg vdlyvdqrve srhrrpdgtm rtltgggytg pqmvyekgtr hltgwqaldy
      241 arqrytaggd ytrqrhqqql lralarkild qgtardpqrv eqvvaalgkt lvyagggrkl
      301 idyayvlggl padrltlvvl pgagvssgga yrgeqlkplg rdfltalrgg radaflaahp
      361 alrvrn
//
LOCUS       WP_457607463             532 aa            linear   BCT 27-JAN-2026
DEFINITION  peptide ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607463
VERSION     WP_457607463.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 532)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 532)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 532)
  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..532
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..532
                     /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=57790
     Region          16..523
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrvrrlaawa alplavtlgl tacgsggggg gagdsdaavr ieiaepqhlv ptntnetsgs
       61 qvlsalfspl vdydeankph evaadsvtts dnkvwtiklk pgytfhngek vtadnyidaw
      121 nygayapngq nssyffekva gyddlqgekp kattmsglkk vddltftvtl sqpyvdfksm
      181 lgytafyplp kaafsapgvl aegyeqapig qgpfkmkgsw qhdakvever ydafpgqqpk
      241 vggvefriyq qptaayadvl sdnldvikti ptenlstaat dlgdrfqqsp asslqvlafp
      301 tfqeefskpe vrkaismaid rdeitksifk dsqqparsfv spvvagyren tigtagafdp
      361 vkakamyeaa ggpkkielsy ngdgghkdwi datcnqlkan lgvecvgtae pkfadlltkl
      421 kqkqpvglfr mgwvmdypsm enylgplyss tgssnyygys npefdkllae garaasedea
      481 ikkyqaaedl laqdmpvipl rygqnnfghs tkvknvhvdl fdrvdllkie ra
//
LOCUS       WP_457607483             170 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607483
VERSION     WP_457607483.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..170
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17423
     Region          7..170
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mstvdstvid tpagplsvla gpggavraag ftadptvllp lihpslrgel reradlgpvt
       61 aavrayldgd laaidaiave qhtggaflth awqvlrdvkp gdpvtytgfa alagrpaair
      121 aaaaacarna aalfvpchrv lrtdgtlggy rwgldvkkwl lghegrvtas
//
LOCUS       WP_457607480             606 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607480
VERSION     WP_457607480.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 606)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 606)
  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 606)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..606
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65061
     Region          16..588
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mpassdgnpa ahtgarsqpl rnlwrlrpyl rpyamefawl liaalaataa slavplvvqr
       61 vvdgpvarhd eagllrlgal alllgvaeav lifirrwtqs sssvgmeaai radiyahlqr
      121 lpagfhdrwq sgqllsrits dlsvirrfls fgllflvlnl vtyaavvall irlhqwlgll
      181 vaasavplfl isrrfarhyh aasrrmqdqq gdvatlveet alglrtmray grgpelaarf
      241 avgarrlhdt gigkarllar tsalfdlvpn ltlgavlvag aaavadgals igelvafvsl
      301 qlmliwpvqs lgwiiangqe aataadriqe vldtpptivd apharsldrg evrgrlrfeg
      361 vgfrypgtsg pvlldldlav epgetmalvg atgcgkstll slvprlhevt ggritidgyd
      421 vrdlrlgslr rlvavafeep tlfsmsiwen ltlgrpdase devraaltla qadfayelpw
      481 glatrvgeqg lslsggqrqr lalaravlgr pavlvlddpl saldvhteal veaalrrvlr
      541 dtatttllva hrpstvalad rvallddgri vavgthsell arvpayravl saeperrsdg
      601 vglvrs
//
LOCUS       WP_457607513             182 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607513
VERSION     WP_457607513.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..182
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20260
     Region          1..168
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtaavfghdg pwteekylal gethghleff dgslhvtpaa tprhqriqrn lgnlleaaar
       61 hvglelldtv nvrlrpgria ipdlvvtepi dfdqpmiear dvrlvcevis pgnaatdkvl
      121 kmhyyaaagi ewyllveqet gtlhlhrrqg rhyrevsvtk pgsvleltep vratirpedl
      181 vp
//
LOCUS       WP_457607509             467 aa            linear   BCT 27-JAN-2026
DEFINITION  TldD/PmbA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607509
VERSION     WP_457607509.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..467
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47762
     Region          13..463
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 msaelevaag vvdlvrrtag agaeaevlvt rtdlaltrfa nsfihqnvse tgvavhlrlh
       61 vdgrtatgsg srvdadglaa lvertraaar lappdpawpg ltaptpmpsg pavdeatafa
      121 spderagrvr afvdavdgle aagycrtayr sgafansagh taagraaeaa mdgiartgga
      181 dgvarlcadr ladldgaalg araaakaraa adpvelppgr yevvlepaav adllqnlawy
      241 gfngkryaer qsfaepgtaq fdpavtlvdd plhastlpfd legtprralp lvqggttgav
      301 aydrrggaea gtgstghgmp gsatfgpiph nvrllaagad agagsaaaav sagvtgavgd
      361 pdtaalvsgm rrgllvsdfw ytrvldpkql vvtgltrngv wlvedgvptr avrdfrftes
      421 yplamgpgrv lglgrtavrq parvdgswye tpalrlsswh ftggasg
//
LOCUS       WP_457607524             364 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607524
VERSION     WP_457607524.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39211
     Region          28..353
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mnvvangqvp vvggsgagnd pgdaarlage pllsvrgltk hfpvrqglra tgavravdgl
       61 dfdvrpgetl glvgesgcgk tttgrmlvrl leptagsiaf agrdithakr gelrglrqdl
      121 qiifqdpyas lnprhtvgri vamplqvnri tppggvkhrv qellelvgln pehynryphe
      181 fsggqrqrig iaralalkpk livadepvsa ldvsiqaqvi nllrslqhdl dlafvfiahd
      241 lavvrhfchr vavmylgkiv eigdrdtiyt rpqhpytral lsaipdvttl gpagrirltg
      301 dvptplnpps gcrfrtrcwk atdhcateep alttrddgrq qtachypesg pvgvstgepv
      361 evsq
//
LOCUS       WP_457607541             188 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar O-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607541
VERSION     WP_457607541.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="sugar O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19985
     Region          14..181
                     /region_name="LbH_MAT_GAT"
                     /note="Maltose O-acetyltransferase (MAT) and Galactoside
                     O-acetyltransferase (GAT): MAT and GAT catalyze the
                     CoA-dependent acetylation of the 6-hydroxyl group of their
                     respective sugar substrates. MAT acetylates maltose and
                     glucose exclusively at the C6...; cd03357"
                     /db_xref="CDD:100047"
     Site            order(16,25,70,82,84,90,92,102,104,110,112,114,116,
                     123..124,126,138,140..141,146,158..159,162,164..165,
                     174..177,179)
                     /site_type="active"
                     /db_xref="CDD:100047"
     Site            order(16,25,70,82,84,90,92,102,112,114,123..124,126)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100047"
     Site            order(26,29,33,40,66,68..69,85..86,100,102,106,108,110,
                     114,116..118,120..121,127,129,136,138,141..143,146,154,
                     156,159..160,164,176)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100047"
     Site            order(110,112,114,116,138,140..141,146,158..159,164..165,
                     174..175,177)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100047"
ORIGIN      
        1 mtsmkdrmla geqyiaddpa iiadleraar lserfnrsaa ddpagrlaal rellgslged
       61 awirpplycd yghqthigar tfvnfnavfl dvaritigsd vqigpnvqll tathpvepea
      121 rrakwesaqp itigdnvwlg ggvivlagvt igentvvgag avvtrdlpan vvavgnparp
      181 irnldqps
//
LOCUS       WP_457607550            1134 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607550
VERSION     WP_457607550.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1134)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1134
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=122244
     Region          42..912
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          930..1134
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 msvqpalfga satpaprtad agprytpvel arllrlpapt reqaaiiaap vepllvvaga
       61 gsgktetmaa rvmwlvansy vrpehilglt ftrkaagela hrvrtrldql irrlgrpgrd
      121 phddplagep tvstyhsyag rivtehglra gyepttrllt easrwqlvdl lvrnydgdms
      181 evdrmpstit davlalagel dehlvdpdel aawtgrffad vqsrpgrvya dvrkalqlqr
      241 trlkllplvr ayarrkddfe amdfadqlar aarvardhpg vgvierdrfr vvlldeyqdt
      301 shaqvvllna lfggghpvta vgdpcqsiyg wrgasagtld rfpaefartd gspadvlslt
      361 tswrnrpeil gvantlsvpl raagarvpel haalsvrdpv phrtpggqag gtvhcallet
      421 yadeadwiad svlaawrgaa gmpgalpehi padrrpttav lvrlrsqipa ieaalrargl
      481 pvdvvglggl ldtpevrdvv ctlrvladpt dgaallrllt garwrigprd lvalhrrara
      541 iarsrreltg degpeitvda ldeatlveal adlgpaqays aegyarlrsy gmelallryr
      601 ldqslpelia diertigldv evavragrdg agdaglarah ldalgdvaar fsgetpgatl
      661 agflaylaaa edeerglapg evevvagavq vltahaakgl ewdvvavagm trgvwpgpvr
      721 nsdhwlgglg vlpfplrgda dglpelglpe aedqrgvara ltdftdawra hdereerrla
      781 yvavtrprrl llcsgywwge gtkrfrgpsv flrevhdacl agadghvvda wtpepagdav
      841 npttetvlra ewpadplgar rpalteaaal vrrhladpet arreaavlat agaaedaeva
      901 rwrreadlll veraelarqa eavevalpgq msvtqlvalr rdpealartl rrpmpteptp
      961 yarrgtafha wleqrfgadr lldvdelpga adedaapdea lvelqerfla sewadrvpve
     1021 vevpfatvia gvvirgrmda vfarpggryd vvdwktgrqp sgpeadaaav qlavyrlawa
     1081 elagvpvdrv gaafhyvrds atvrpadlld aeglaglvaa vpeipvdlpq rtnp
//
LOCUS       WP_457607556             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607556
VERSION     WP_457607556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (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   4  (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   5  (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   6  (residues 1 to 353)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (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   8  (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 10194283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..353
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36962
     Region          43..261
                     /region_name="PBP2_NrtA_CpmA_like"
                     /note="Substrate binding domain of ABC-type
                     nitrate/bicarbonate transporters, a member of the type 2
                     periplasmic binding fold superfamily; cd13553"
                     /db_xref="CDD:270271"
     Site            order(50..51,84,129,151,157,187,204..205,208,235)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270271"
ORIGIN      
        1 mrglplrrlv tlatlaavgt atlgttaacg edsdvaagsg pvtlrlgyfp nithapavvg
       61 vekgifaekl gsdveldtkt fnagpaaiea vfsgaldaty igpnptvnaf skskgeavrv
      121 isgaasggva lvvkpgitsv eqlrgkkiat pqlgntqdva lrywlkekgl ettkegggdv
      181 kvvpqenaqt vetfgsgaid gawvpepfvs rlvnaggkvl vderdlwpdk kfvitnllvs
      241 tkflkahpdv vkklvegqva anefvnskpd eaqqaisdhi gkitgkpldl klikqawptl
      301 eftndpipss lktgldhava vgltqpvdln glydlkylne vlkaqgkaev sqp
//
LOCUS       WP_457607559             444 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607559
VERSION     WP_457607559.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..444
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46968
     Region          27..430
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mssatttvrp lpalgpnrrl kvpkqaertl angltviavr rssvplvelr lwmpfgrthl
       61 argamlaqtm lsgteahsat elaaelqkvg ggltagldpd rlmlsgaglv tgldrmlell
      121 aevltgatyp adwveterdr lvdriqvaqs qpshlartal lkrvygrhpy aeqtpdpdqv
      181 ravrpaalrr lhaervhpag avlvlvgdva peraldaaek alagwrgdgh vaelppappl
      241 epgplllvdr pgsvqssvrl alpavprthp dhaalqlanl ifggyfssrw veniredkgy
      301 tygphslveh svagsllvag aevatevtaa alvettyelg rlatvppktd eleqarqyal
      361 gtlqlgmstq aglasltsay agnglrldfl aeyaarlaat tvddvaevaa rylaparavt
      421 vvlgdaarva dslaaltpvr tesa
//
LOCUS       WP_457607502             237 aa            linear   BCT 27-JAN-2026
DEFINITION  SanA/YdcF family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607502
VERSION     WP_457607502.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Chao,K.L., Lim,K., Lehmann,C., Doseeva,V., Howard,A.J.,
            Schwarz,F.P. and Herzberg,O.
  TITLE     The Escherichia coli YdcF binds S-adenosyl-L-methionine and adopts
            an alpha/beta-fold characteristic of nucleotide-utilizing enzymes
  JOURNAL   Proteins 72 (1), 506-509 (2008)
   PUBMED   18393394
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Rida,S., Caillet,J. and Alix,J.H.
  TITLE     Amplification of a novel gene, sanA, abolishes a
            vancomycin-sensitive defect in Escherichia coli
  JOURNAL   J Bacteriol 178 (1), 94-102 (1996)
   PUBMED   8550448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..237
                     /product="SanA/YdcF family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=25841
     Region          31..231
                     /region_name="SanA"
                     /note="Uncharacterized periplasmic protein SanA, affects
                     membrane permeability for vancomycin [Cell
                     wall/membrane/envelope biogenesis]; COG2949"
                     /db_xref="CDD:442192"
ORIGIN      
        1 mrgltarwra wrgdhrravr llrrllvlat aavvllgaat vasatwvrga aegrlfdaad
       61 apetpvalvl gtkvepdgtp apflaarlei arqlyaagkv rvlllsgdhm nwdydepdam
      121 rrwlvdrgvp aektvldhag fdtydscvra yrvfgvrrat vvtqsfhlpr avalcrdagi
      181 dtvgvgddta rryadqwris svreygacvk aaadvltgrd pvhlgrretg vddalra
//
LOCUS       WP_457607565             707 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase UvrD2 [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607565
VERSION     WP_457607565.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..707
                     /product="ATP-dependent DNA helicase UvrD2"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /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:0008094 - ATP-dependent activity, acting
                     on DNA [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000725 - recombinational repair [Evidence
                     IEA]"
                     /calculated_mol_wt=76211
     Region          11..573
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          624..691
                     /region_name="HRDC"
                     /note="HRDC domain; pfam00570"
                     /db_xref="CDD:425755"
ORIGIN      
        1 mgvhsaaeqv lagldpeqrs avtapagpvc ilagagtgkt ravtsriayr altgdiagrh
       61 vlavtftara aaemrsrlgv lgvqgvqart fhaaalrqvr yfaprllagr ampelldskv
      121 rvvtlaaakv glradraaar dlsaeiewak sslvepgeyv vaaakalret pyeparvadv
      181 fdayerlkrg ngvidfedml raavwgieeh pdvaeqvrnq yrhfvvdeyq dvnplqqrll
      241 eawlggrddl tvvgdasqti ysftgatssy lvdfprlhrg atvvrlvrdy rstpqvvgla
      301 navisqargt earlrlelhg qrrpgpepdl riftdepaea navaarcral vaggtparei
      361 avlfrtnaqs eayekalsea gvpyvlqgae rfferpevrq amialraatr sadagtplpa
      421 avvealtavg wapdapppgg aarerweala alvplaeeya aqaeeepglt gfteelarra
      481 aqqhvptveg vtlaslhsak glewdavflv glaegtlptt yaktmeqvee errllyvgit
      541 rarewlwlsy atarspggra rrpsrflpql drsgggerag gagparraer rrpqvvscri
      601 cgatllagad rklgrcptcp sdideelyer lrewrqrvag aqkvpayvvf tdatltalae
      661 rkpgrteelv aiagigprkv glygdtvlal vagatvddvc pqktsen
//
LOCUS       WP_457607575             996 aa            linear   BCT 27-JAN-2026
DEFINITION  UPF0182 family membrane protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607575
VERSION     WP_457607575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Keefe,B., Leestemaker-Palmer,A. and Bermudez,L.E.
  TITLE     The ability to detach from biofilms in the lung airways prior to
            transmission to another host is associated with the infectious
            phenotype of Mycobacterium abscessus
  JOURNAL   Front Immunol 16, 1508584 (2025)
   PUBMED   40124375
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Gannesen,A.V., Ziganshin,R.H., Zdorovenko,E.L., Klimko,A.I.,
            Ianutsevich,E.A., Danilova,O.A., Tereshina,V.M.,
            Gorbachevskii,M.V., Ovcharova,M.A., Nevolina,E.D., Martyanov,S.V.,
            Shashkov,A.S., Dmitrenok,A.S., Novikov,A.A., Zhurina,M.V.,
            Botchkova,E.A., Toukach,P.V. and Plakunov,V.K.
  TITLE     Epinephrine extensively changes the biofilm matrix composition in
            Micrococcus luteus C01 isolated from human skin
  JOURNAL   Front Microbiol 13, 1003942 (2022)
   PUBMED   36204611
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..996
                     /product="UPF0182 family membrane protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=108531
     Region          13..960
                     /region_name="COG1615"
                     /note="Uncharacterized membrane protein, UPF0182 family
                     [Function unknown]"
                     /db_xref="CDD:441223"
ORIGIN      
        1 mrssplprms rrgrvtigvl igvfilftll gwgvnawtdw lwfdevrytq vftgvlatrl
       61 llflvvgagm allvggnlwl ahrlrpkmrp hsaeqatler yrmllsprlg twialaaavv
      121 glfaglsaqs rwgqwllfrn ggdfgvkdpe fgvdvgfyvf qlpfwryvlg vgftavvlsl
      181 lgalavhyif ggvrlqgvgd rmtnaarahl sslvavfvll kavayvldrr amlleynega
      241 klygagyadv nallpakeil awisivvala iivfsnavmr nlvwpgisla llgvsavaig
      301 giypwavqtf evkpsardke apyiersika trsafglega kttpyaasnl vppaslatdt
      361 svvsnirlld pqlvsetytq lqqvrgfydf gskldidrys vkdktsdyvv gvreinygel
      421 tdqqsnwinr htvythgygl vaapanqvvc ggqpyfvsgf lgekaqeacs apteeipaqq
      481 priyygerme andyaivgqt gdrnvefdrp tstggeqyyt ytgeggvkig sfprrllyai
      541 keqesnflls eavnenskll yvrnprdrve kvapfltldg dpypavvngr vlwiidgytt
      601 aatypyaerv nlqaetadel tgrgtfqlar envnyirnsv katvdaydgt vklysyddtd
      661 pvlkawnkaf ggdlvlpkgd ipaelaehfr ypadlfkvqr nlltkfhvtd pgdfysgqdf
      721 wqvpnvpdap dsgqkqppyy lftqfpgqdg prfqltsavt pngrqnlaal vsgsyvdgqp
      781 klevlelpdq trisgptqvh qqmtnngdir qqlnllssnq aqvqygnlls lpfadgmlyv
      841 epvyvksssq daypllqkvl lsygdggsyv vlannlsdgi kqlveqgkra pntnpppstd
      901 dnptppptgg dnnntpppms gelaqaaarv qtaigevkaa qasgdferyg ralkaldeam
      961 safqqaqaaa ngsgnpapsg svsppaptsp apspgg
//
LOCUS       WP_457607596             170 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607596
VERSION     WP_457607596.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17466
     Region          6..164
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtglrvrrae ladfpvvarl tvaayeadgq lkdesgyapv ladvagraet gevlvavdda
       61 tgqvlgavtf vlpgtpyael agpgeaefrm lavdpaaqgr gagaalasac varatelgct
      121 avvicvragm aanahrlyer lgfvrypekd wtplpgidlr glrldlsaag
//
LOCUS       WP_457607609             316 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607609
VERSION     WP_457607609.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..316
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34523
     Region          1..316
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mravlvvnpk atttsersrd vlvralrsev dlsvrytrrr ghamdlarea aqegvdlvvt
       61 lggdgtvnev vnglmaaepp tfrtgqtsae rlpalatvpg gstnvfaral glprewpdgt
      121 smileglrlg rsrtiglgra ddryftfcag fgldaavirr veqarkkgrv stpalyfrst
      181 agqyfvgsdr rhpsvtlerp geapatelat aiiqntapwt ylgdreinpn peasfdlgld
      241 vlalrrlrva startavqff skrpdphgkq vlrlhdvaef tlvserplpf qldgdylger
      301 ekvrftsvpa alrvic
//
LOCUS       WP_457607604             569 aa            linear   BCT 27-JAN-2026
DEFINITION  nitrite/sulfite reductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607604
VERSION     WP_457607604.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Lu,Z.J., Cao,Y.Q., Long,W.J., Long,Z.D., Chen,G., Ma,Q.S. and Wu,B.
  TITLE     Isolation and characterization of an operon involved in sulfate and
            sulfite metabolism in Sinorhizobium fredii
  JOURNAL   FEMS Microbiol Lett 282 (1), 89-99 (2008)
   PUBMED   18336549
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Schnell,R., Sandalova,T., Hellman,U., Lindqvist,Y. and Schneider,G.
  TITLE     Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium
            tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in
            the active site
  JOURNAL   J Biol Chem 280 (29), 27319-27328 (2005)
   PUBMED   15917234
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Zeghouf,M., Fontecave,M. and Coves,J.
  TITLE     A simplifed functional version of the Escherichia coli sulfite
            reductase
  JOURNAL   J Biol Chem 275 (48), 37651-37656 (2000)
   PUBMED   10984484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..569
                     /product="nitrite/sulfite reductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050311 - sulfite reductase (ferredoxin)
                     activity [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=63329
     Region          37..569
                     /region_name="CysI"
                     /note="Sulfite reductase, beta subunit (hemoprotein)
                     [Inorganic ion transport and metabolism]; COG0155"
                     /db_xref="CDD:439925"
ORIGIN      
        1 mavsstptrp dtpapaarap rrprgegqwa lghreplnpn erikkdddpl nvrdrieniy
       61 ahrgfasidp qdlrgrfrww glytqrkagi dggrtavlep heledeffml rvrvdggqln
      121 laqlrviadi srefardtad itdrqniqyh wirvedmpei wrrleavglq tteacgdcpr
      181 ivlgspvagv ardevldptp aideivrryv gdkaysnlpr kfktsiswlv dtpyeandia
      241 flgvehpehg pgfdvwvggg lstnpmlakr lgvwvplnev pdvwagvvgi frdygyrrlr
      301 nrarlkflva dwgverfrev lekeylgrtl ldgpaanlpa kpvdhigvhr qsdganyvga
      361 apvvgrvsgt qlaqladvve ahgsdrvrlt pyqkllvldv apertdslvt alrgiglear
      421 psawrrgtma ctgiefckla ivetkrrgee lvarleerlr dfdadisihl ngcpnacart
      481 qvadiglkgq lvvgpdgrqv egfqvhlggg lgiaqgqtag fgrklrglkt taeelpeyve
      541 rlarrylagr tegetfanwv iradeeelr
//
LOCUS       WP_457607621             332 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607621
VERSION     WP_457607621.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..332
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34373
     Region          10..309
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrgqrlvaal mtallagcgp avatsgpvpa gvgpapersy avgmrqftld pdgrrplpvt
       61 vwypaapssp gpptsasatp sgspravpas papargprvr pgapfaagrf pvvlhshglr
      121 slpalhaalt srwaaagfvv vaptyprtnq rarpftredv rnqpadawrl irhlvrlgar
      181 pgdplgahla vdrfaaaghs agghttlgmf asgqssplra giviaggrmv agpsrplapm
      241 lfvhgsadri vpesigraay arclgpaafl sltgqghgey ltpgrpgfpq vldtttdflr
      301 wtlyadraal hrlptdatap ntttftaral pt
//
LOCUS       WP_457607624             370 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate/propionate family kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607624
VERSION     WP_457607624.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=39116
     Region          2..369
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msrilvlnsg sssvkyrlyd gddvldkgtv erigepgggp adhesavrei igrldltgls
       61 gvghrvvhgg rkfsapvrid davvaaiedl vplaplhnpa nlagirvare alpdvpqvav
      121 fdtafhhtlp eaaatyaidk ataerygirr ygfhgtshay vsrrvadlld rpydqintit
      181 lhlgngasac avqggrsvat smgmsplegl vmgtrsgdld ptvifhlrre ggmvvddidd
      241 llnhrsgllg ltgvndmrev larrdagdpd atlafdvycr ritgyvgayy allgrvdaia
      301 ftagvgehaa pvraaslagl erlgvavdpa rndghgdrlv spdgaevavl vvgtdeerei
      361 aretrevlgv
//
LOCUS       WP_457607637             496 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607637
VERSION     WP_457607637.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..496
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=51574
     Region          13..273
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,67,72,77..80,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,75,96..99,103,105,141,143,
                     145..146,148,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,75,96..99,103,143,145..146,
                     148,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,103,105,141,143,145,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 matlqagrll arryrlidpi gaggmsviwr ardevldriv avkvlapsla adarfrdmvr
       61 eearsaaqld hphvtavhdy getvapdgti tsfvvmells geelehrlte gplpwpaave
      121 tgaqvaeala aahrlgivhr dvtpanvmmt gtgakvldfg iatrigapdd dedggtfgtp
      181 ayvaperldg apaqpatdvy slgvllfetl tghppypaet weqlsaalad cpeptlddvp
      241 glpgpvadic lrcldrdprr rptahrvaav lrdqllpadp qaatmlaptm tlpaltpppt
      301 rpepagppap gpapaaqprp epgqepaaqp vpsrrrtltl aalgvtvvaa aallvpalmp
      361 drttgprvlp tagpvrpspa dppvaeapat tppaaptsvp psggarppat gqadaaervd
      421 glieaglteg qiredvgvdl rnllrnavaa ngegevtaav drlrgkider rregsispgy
      481 arrldaaaae lvagrt
//
LOCUS       WP_457607648            1203 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607648
VERSION     WP_457607648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1203)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1203
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=126134
     Region          90..871
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          943..1191
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mqayrlvrrp gglgagvthd agagqgvgrs ggstdaeprs ggsagdaahp qtaappegas
       61 pqnetgaspp saasagigag egtnvsrpad pvqaevvght dgpmlvvggp gtgktttlve
      121 avaarvaegv dperilvltf grrgatelrh rieariagdg hrvvreplvr tfpayafgll
      181 rraaaergep sprlltgpeq dliirelldv vgeepgddpv gwpedlrpal rtrafaqqlr
      241 dllmraaerg vgpvelarlg eklgradwpa aarflreyva vlalrdvsnr gsvaydpael
      301 vraatgmlld dpellaaerr rlahvyvdel adtdpaqldl lavvagggrs lvafadpdss
      361 tyafrgadpa gvttfphrfr tasgapaaqv tmttsyragp ellaatarla rrlrgpaahr
      421 rlrplpgapa gtvevrtfrs atsesawlah alreahlldg vpwsrmavlv rstgrqlpsl
      481 rralhtagvp tvvhgedlpl hlqpavapll lllrcalepd rldeeaaval lhsplggadp
      541 laerrlrqgl ralalaggdr rpsgellvea lrepaelati errwaapaqa vahllatare
      601 tagrpgatve dvlwavwres glaerwagai trgraatgeh etaqrwraea adrdldavlv
      661 lfdaaarftd rlpgartevf ldhvlgqelp adtlaaaadr gdavrlltah aakglewdlv
      721 avagvqegvw pdlrlrgsll gserlvdvla gradgaglra slvgqtsall deerrlfhva
      781 israrrrllv tavasaavgg ddheeqpsrf lhelaaadpp atgggggpap tgngpagngp
      841 tgtatrggta dgpvphgdeh pqdgpsaalp vtlpprgltl salvaelrta vtdpatpitr
      901 rhaaagelar laaagvpgah pedwwglrgl sddrplvdeg epvrvtpsam esalrcslrw
      961 llerhggsgp asaaqgvgnl vhaaamlaed asvdrealle yvaarfdaie laarwmagpe
     1021 rqraeamvdk llrwlagnpr rllaiehefa vrlddparpv eltgrvdrle vddegrlvvi
     1081 dlktgkstav terevaehpq lgayqaavea ggfaefgeep ggaalvqlgt gardakeqtq
     1141 aaagegpeag watalvrrta dtmaastfaa vanskcrvcp vrtscpvsgq grqvvepppe
     1201 sqp
//
LOCUS       WP_457607672             270 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607672
VERSION     WP_457607672.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..270
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=27458
     Region          60..247
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(70,110,139,233,236)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(70,233,236)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(70,91,139)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 msergevarw graaalslla gtvggaavla gqaiaartre yaqpelglvl ratvgradap
       61 plrlvllgds salgvgvdrf edtiggqlan llaegptgrr vqlssvgvsg sratdlatqv
      121 arallgerpd vavvligand atamsrpgda aaylgsavrr lreahvevvv gtcpdlgavr
      181 avaaplrqvl gwsgrrmara qtaavldagg tvvdlgtetg pvfradagtl chdgfhpsad
      241 gyrvwahall paveaaaava frhhrqppag
//
LOCUS       WP_457607674             494 aa            linear   BCT 27-JAN-2026
DEFINITION  CYTH and CHAD domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607674
VERSION     WP_457607674.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Lorenzo-Orts,L., Hohmann,U., Zhu,J. and Hothorn,M.
  TITLE     Molecular characterization of CHAD domains as inorganic
            polyphosphate-binding modules
  JOURNAL   Life Sci Alliance 2 (3) (2019)
   PUBMED   31133615
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Tumlirsch,T. and Jendrossek,D.
  TITLE     Proteins with CHADs (Conserved Histidine alpha-Helical Domains) Are
            Attached to Polyphosphate Granules In Vivo and Constitute a Novel
            Family of Polyphosphate-Associated Proteins (Phosins)
  JOURNAL   Appl Environ Microbiol 83 (7) (2017)
   PUBMED   28130300
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Martinez,J., Truffault,V. and Hothorn,M.
  TITLE     Structural Determinants for Substrate Binding and Catalysis in
            Triphosphate Tunnel Metalloenzymes
  JOURNAL   J Biol Chem 290 (38), 23348-23360 (2015)
   PUBMED   26221030
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Bettendorff,L. and Wins,P.
  TITLE     Thiamine triphosphatase and the CYTH superfamily of proteins
  JOURNAL   FEBS J 280 (24), 6443-6455 (2013)
   PUBMED   24021036
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Kohn,G., Delvaux,D., Lakaye,B., Servais,A.C., Scholer,G.,
            Fillet,M., Elias,B., Derochette,J.M., Crommen,J., Wins,P. and
            Bettendorff,L.
  TITLE     High inorganic triphosphatase activities in bacteria and mammalian
            cells: identification of the enzymes involved
  JOURNAL   PLoS One 7 (9), e43879 (2012)
   PUBMED   22984449
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The catalytic domains of thiamine triphosphatase and CyaB-like
            adenylyl cyclase define a novel superfamily of domains that bind
            organic phosphates
  JOURNAL   BMC Genomics 3 (1), 33 (2002)
   PUBMED   12456267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18995808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="CYTH and CHAD domain-containing protein"
                     /EC_number="3.6.1.25"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050355 - inorganic triphosphate
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=54409
     Region          6..179
                     /region_name="CYTH-like_Pase"
                     /note="CYTH-like (also known as triphosphate tunnel
                     metalloenzyme (TTM)-like) Phosphatases; cd07374"
                     /db_xref="CDD:143620"
     Site            order(6,8,10,43,57,59,61,72,82,119,121,140,157,159)
                     /site_type="other"
                     /note="putative active site"
                     /db_xref="CDD:143620"
     Site            order(6,8,138,157,159)
                     /site_type="other"
                     /note="putative metal binding residues [ion binding]"
                     /db_xref="CDD:143620"
     Site            order(6,8,10)
                     /site_type="active"
                     /note="signature motif [active]"
                     /db_xref="CDD:143620"
     Site            order(8,10,43,57,61,72,82,121,157)
                     /site_type="other"
                     /note="putative triphosphate binding site [ion binding]"
                     /db_xref="CDD:143620"
     Region          213..487
                     /region_name="CHAD"
                     /note="CHAD domain, binds inorganic polyphosphates
                     [Function unknown]; COG5607"
                     /db_xref="CDD:444338"
ORIGIN      
        1 matvvererk ysgdegfrlp dltgcggvvt msdatvsdld avywdtddll llrsghalrr
       61 rtgghdagwh lkvgavggar vehqfpagas ddgpppevva lvrgasrgrp vapaarvvnr
      121 rrehrlldad grvlaevaed dvrsedlvdg tarswheiei elvggddall dalgerlraa
      181 gsrevavsks hravagrier fddrepdgpa gpvleyvrvq rdaivgnhaa ayqgdedavh
      241 dmrvatrrlr atlrtfrglw drreseavra elrrlggelg rvrdtqvmaa rlteavhelp
      301 gelvlgpvsa rigerfaadr aeattalrsa ldadrypall arldrladap padvgrrwvd
      361 rrirkavrra darldralai tgpdgdialh earkklkaar yavevrepaa gkraarlvkr
      421 fkalqdllgt hqdsvvtrev lrrqalqaya dgentftygl lharqaetag hdrpavlrar
      481 drsrhrkvrr wlkp
//
LOCUS       WP_457607686             302 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607686
VERSION     WP_457607686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..302
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31818
     Region          82..302
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mveyrtvfda evlfsngggl rtdgfrldvp hpdvtddeva allvrhlgll mvgevritdr
       61 tvveephkgg rgldvpasgg rrlvelshvv tdgmvtlpgw pgpaitdwlt reesrnryap
      121 gvefhvarid miantgtyvd tpshrfadgp dltgvpldrl adlpglvvrv pagtravdrl
      181 mlapydvagc avllhtgwda hfgtdayaap eapyltgdga qwlaeagaal vgidsinidd
      241 mtaaaagqrp ahtsllaagi pivehltgls elpptgfrft aapprvagmg tfpvrafaiv
      301 ga
//
LOCUS       WP_457607689             381 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA recombination protein RmuC [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607689
VERSION     WP_457607689.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..381
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41371
     Region          72..353
                     /region_name="RmuC"
                     /note="RmuC family; pfam02646"
                     /db_xref="CDD:460637"
ORIGIN      
        1 msfatlavvv lclaaggavg wlaararaaa diarleatla atqtgegrle qsmralsyea
       61 taqsqeavar avaplhdtlr ryeqrvaele rdrvdayael reqvrsmsav sgelrtetkq
      121 lvaalrapqv rgrwgehqlr riveaagmle hcdfseqvta atdhqgvrpd lvvrlhggrt
      181 vvvdakapfd ayltameard ergrdthlda harhlrahvd glaaksywsa fdqtpefvvl
      241 fvpadpfldv alqrdpslle hafarnvvla tpatlvallr tvayswrqea larnaatvhs
      301 larelygrls tlgdhvgklg sslsgavtay nravgslear vlvsarklae lgvsddelaa
      361 paqvelaprq pqapelrhhe f
//
LOCUS       WP_457607697             326 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607697
VERSION     WP_457607697.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..326
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31987
     Region          21..168
                     /region_name="ydcZ"
                     /note="Uncharacterized membrane protein YdcZ, DUF606
                     family [Function unknown]; COG3238"
                     /db_xref="CDD:442470"
     Region          189..321
                     /region_name="ydcZ"
                     /note="Uncharacterized membrane protein YdcZ, DUF606
                     family [Function unknown]; COG3238"
                     /db_xref="CDD:442470"
ORIGIN      
        1 msragtaapp apptlstgrr vagvglatas gvmvavqsri ngelgvrlad giaaavvsfg
       61 vgllillvlv patpggrrgl aalrgalrag tlrpwqclgg vcgaflvatq gltigalgva
      121 vftvavvagq sgssllvdra gigpsgrqpv tpnrligavl tvlavllavg drlgdpealv
      181 lallplaagv giawqqavng rvraaagsam tatlvnftvg taallvtlav dlavrgrpdg
      241 afpsepwlyl ggplgivfia laaalvrftg vlllglatia gqivgavlld lvlptaashp
      301 gldtllgaal tmvavlvaaf gparrp
//
LOCUS       WP_457607683             266 aa            linear   BCT 27-JAN-2026
DEFINITION  3'-5' exonuclease [Nitratifractor sp.].
ACCESSION   WP_457607683
VERSION     WP_457607683.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Rothwell,P.J. and Waksman,G.
  TITLE     Structure and mechanism of DNA polymerases
  JOURNAL   Adv Protein Chem 71, 401-440 (2005)
   PUBMED   16230118
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Shevelev,I.V. and Hubscher,U.
  TITLE     The 3' 5' exonucleases
  JOURNAL   Nat Rev Mol Cell Biol 3 (5), 364-376 (2002)
   PUBMED   11988770
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Zuo,Y. and Deutscher,M.P.
  TITLE     Exoribonuclease superfamilies: structural analysis and phylogenetic
            distribution
  JOURNAL   Nucleic Acids Res 29 (5), 1017-1026 (2001)
   PUBMED   11222749
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Taft-Benz,S.A. and Schaaper,R.M.
  TITLE     Mutational analysis of the 3'-->5' proofreading exonuclease of
            Escherichia coli DNA polymerase III
  JOURNAL   Nucleic Acids Res 26 (17), 4005-4011 (1998)
   PUBMED   9705512
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..266
                     /product="3'-5' exonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30558
     Region          2..219
                     /region_name="DNA_polB_like1_exo"
                     /note="Uncharacterized bacterial subgroup of the DEDDy
                     3'-5' exonuclease domain of family-B DNA polymerases;
                     cd05782"
                     /db_xref="CDD:99825"
     Site            order(6..9,103..104,107..109,169..170,205,209)
                     /site_type="active"
                     /db_xref="CDD:99825"
     Site            order(6,8,109,205,209)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99825"
     Site            order(7..9,103..104,107..108,169..170,205,209)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99825"
ORIGIN      
        1 micifdceti pdidlirrnf dveglgdaaa iekaqslyae ghggstflpl pyhrlvalsa
       61 viadefghfi kvgdfgngsd eeeaiirhff dfieaknprl vsfngrgfdm pmlliramry
      121 nlsfpawfdq nnpqlnktkw enyrqryaee fhtdlletlg nfgavrnlrl dllctmagip
      181 gkydvsgdqv tdlyfagele kireycqsdv lntywlwlky ellkgrltlq dyarflatmq
      241 ekmprergyy apfseaidae larlel
//
LOCUS       WP_457607708             167 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607708
VERSION     WP_457607708.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..167
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18280
     Region          4..156
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mpdsdgfdef yrgsrqrllg fvyvltgdla eaqdavqeay irawqrwstv rgyddpeawv
       61 rvvasriavs rwrslrsrar aylrhgavad vpapstetld vvaalrrlpe aqrtaiamhy
      121 llgmpvaeva reteapvgtv karlsrgrta lagllavvdl eegaada
//
LOCUS       WP_457607710             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ketopantoate reductase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607710
VERSION     WP_457607710.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..327
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33731
     Region          1..311
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryviigaga vggtigvlla daghdvtlva rgahldalre rgltlrtpdr evtgrlpava
       61 gpdgpplpad tvlvltvksq dtvaaldvwa dapvegggta gerlpvvlaq ngvanepaal
      121 rrfarvhpvc vwlpathlep gvvvanghph pgmlhigryp sgaddtsrav atdltaagfv
      181 apvrddvmrw kygkllanlg nglqallgrd vpealstrvr aegeaalaaa giahttvqee
      241 aaergdrvsh rpvggeersg gstwqslarg agsvetdhln geivllgrlh gvptpanaav
      301 qtavrravrd ripaggfpls elekllg
//
LOCUS       WP_457607712             182 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607712
VERSION     WP_457607712.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..182
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19763
     Region          15..172
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mdpvggssvt plaeadylaa dygrhrvelf drglivspap dlrhqrvarr lanavesaaa
       61 pagllvyhgv nvrldvdrvm ipdlvvtdar degtvldakr valvgevvsp rnagvdrvlk
      121 mqlyaiarip wyllveqdgd shslrlhrld gahyvedava kagetlsvte pfrwaidpsa
      181 lr
//
LOCUS       WP_457607718             218 aa            linear   BCT 27-JAN-2026
DEFINITION  Maf family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607718
VERSION     WP_457607718.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..218
                     /product="Maf family protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009146 - purine nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=22950
     Region          8..183
                     /region_name="Maf"
                     /note="7-methyl-GTP pyrophosphatase and related NTP
                     pyrophosphatases, Maf/HAM1 superfamily [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0424"
                     /db_xref="CDD:440193"
ORIGIN      
        1 mstsvavrlv lasqsparrk llqaagiepd vlvsgvdesq vvsdqaedlc lelarlkaqa
       61 vrdrlrpspd ertlvlgcds vlafdgeilg kpddaadatr rwqrmrgrsg vlhtghclld
      121 vthesraeav asttvhfadi sddeiaayva tgeplavaga ftidglggaf ltgiegdpgt
      181 vvglslpllr rllaevelsi vdlwtkiapg gqeiehlg
//
LOCUS       WP_457607720             217 aa            linear   BCT 27-JAN-2026
DEFINITION  O-methyltransferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607720
VERSION     WP_457607720.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..217
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23623
     Region          48..217
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttkplpltp elhaylvahg sapdeivqel aeetraalpa eavmqvapeq aafltfltrl
       61 lgvrqavevg tftglsslai arglaeggrl tcfdiseeyt gvarrywqra gvqdrielri
      121 gpaaetlrel preryldfaf idadkvgypv ywdelvprmr pgaviavdnt lrdgrvlapr
      181 naddraiaaf ndaviadvrv eavmlpiadg vtlarvl
//
LOCUS       WP_457607722             450 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607722
VERSION     WP_457607722.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44401
     Region          1..445
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mprltrdrit wltyaqlglw gfflygfgpv vpllrdeqgt saavaglhst giavgalagg
       61 alfapvarrl grgpaiwlgl agvaagvtal gllrplpatl aavaviatfg mmvvsgvsvv
      121 ltarhgptap aalteanaac agmgilaplt igatvdaglg wrplmavevg litlvalaal
      181 tfrvrgpkra tadaaagtpv pvaaatrvpa vpasgvseav vpapvvpapv vpapvvpapa
      241 vpapvvppsg epgssgsgaa grlpraywia wvlmsvtgsi evclslwtad vlrthaglsa
      301 ggasaavaai vcgmfagria ggraalrwap vplllgalav smagftlfwg stvgwlavtg
      361 lvvlgignal hyplaisial avagpaadka agwsaysmgv gfgiapvalg wvadgvgphp
      421 aflllpafia vavlltvrmg ralpapvrta
//
LOCUS       WP_457607725             147 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607725
VERSION     WP_457607725.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Moukendza Koundi,L., Ekomi Moure,U.A., Boni,F.G., Hamdi,I., Fan,L.
            and Xie,J.
  TITLE     Mycobacterium tuberculosis Rv2617c is involved in stress response
            and phage infection resistance
  JOURNAL   Heliyon 10 (5), e27400 (2024)
   PUBMED   38495141
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..147
                     /product="DoxX family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14893
     Region          24..133
                     /region_name="COG4270"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443411"
ORIGIN      
        1 mapliallag talariagll gvdaldgwhp alrvglalmf vltgvahfas rradliamvp
       61 pslprpdllv tvtgvlelag alallfpata rpaaaglall mlamfpanvs aarrrltlar
      121 rpvtplgvrt vlqvvfvaaa lavtlgg
//
LOCUS       WP_457607727             171 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607727
VERSION     WP_457607727.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..171
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18089
     Region          10..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 megvpstges arvsppssea sralrdvlrl agdtraalar rlglnatdaa aidhlvsspe
       61 plgpvelgnr lgirsasatt lvdrlvqagh vartphphdr rrlslqvtes avgevlealr
      121 pmlvgvdrav arltpeqaea ttaflrevte vmreyvatap deppraradr g
//
LOCUS       WP_457607734             320 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607734
VERSION     WP_457607734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18662006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..320
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35017
     Region          173..301
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          241..311
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtlpagwsar rptlddvpai lavvhaadtf avgypdfdde dvrsaltapf vdpardswlv
       61 tdpdgtavaw silanpsgvg rewvdvlvdp drgadlrapl larllervae raaerglpal
      121 taragvyape trwagelaea gftrikryir msrsladlpa epapppgvtv rplraddedd
      181 lrlfhriydt afrdtpdhdp ldfaqwrdll psygkvwdew flaevdgepa galqssdqal
      241 dqdrgwvrtl svlpayrrrg vgaallrraf svyaakgrtg aglgvdlanp tapvtlyrsv
      301 glveehwadm yersvpasrv
//
LOCUS       WP_457607747             518 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 87 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607747
VERSION     WP_457607747.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Morita,Y.S., Sena,C.B., Waller,R.F., Kurokawa,K., Sernee,M.F.,
            Nakatani,F., Haites,R.E., Billman-Jacobe,H., McConville,M.J.,
            Maeda,Y. and Kinoshita,T.
  TITLE     PimE is a polyprenol-phosphate-mannose-dependent
            mannosyltransferase that transfers the fifth mannose of
            phosphatidylinositol mannoside in mycobacteria
  JOURNAL   J Biol Chem 281 (35), 25143-25155 (2006)
   PUBMED   16803893
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..518
                     /product="glycosyltransferase family 87 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56367
     Region          70..495
                     /region_name="COG5650"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444371"
ORIGIN      
        1 mstqspagid epgaseaapr taetinhpsr sdwfvrgasg liggplgdha aaldrpagre
       61 srfwtagriv lalvcltlal hwvqkspcqd gawqnniqyt rmcytdvlal yyaeglnegk
      121 vpyadhpvey pvltgyfmga lglpvhalga dnpainqgqw fynlnalvlg alavatvavi
      181 lslrrrrpwd aalfalspal vltatvnwdl laiglaafgl lawararpdr yalllpgvag
      241 vliglggaak mwplfllgpi lvlalragkm laglvatata lvtlvavnlp vaipyrenwe
      301 rffdlnttrp idwgtlwyig ryldgrisps apgqlgpfew lnaniptlnw lsyllfglac
      361 lgvaglalla prrprlaqla flvvaaflif skvwsqqfvl wllplavlar prwgaflawq
      421 vaevgyfaaf ygellgtams rpvfpegvfv lasslrlitv vvlcgfvird imrpeldvvr
      481 htyaddpdgg vldgapdapw hqrwfrarsh nmplpnpr
//
LOCUS       WP_457607758             437 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607758
VERSION     WP_457607758.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..437
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46844
     Region          15..406
                     /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 mtgttlddyt dryarrvrgm taseiralfa vanrpevvsl aggapyiaal pldavgemlg
       61 rlgsehgatt lqygvgqgap elrericevm slsgidascg aspedvvvtv ggqqaldlva
      121 rlfldpgdvv laegptyvga lgvfqaaqaq vahvpmddeg lipealevai adlaragrrv
      181 kflytiptyq npagvtlsee rrervldice ragllvvedd pygqlgfege aprplrarrr
      241 dgvfylstfs ktfapglrvg wilaphavrd klviaseaqi lcpsayaqsa vstylgtmpw
      301 rqqlkvyrev yrerrdalld amadlmpegt twttpqgglf vwatlpdgld skammprava
      361 arvayvpgtg fyadgtgagn mrlnfsfptp eriregvrrl agvmeqeiam rkvfgavgga
      421 gprrrqggsd apgpdla
//
LOCUS       WP_457607763             346 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607763
VERSION     WP_457607763.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..346
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36761
     Region          75..337
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mknrprgglg rglgaliptg pvpgaepaat epessavaas psapaagata aitggvattp
       61 spaaepepql spvpgarfae ipvdaivpnp kqprhvfdee aleelktsiq evgflqpivv
      121 rqldpdkfel vmgerrwraa qavgretipa ivrdtkddam lrdallenih ranlnpleea
      181 aayqqlleef gatheelarr igrsrpqisn tirlmnlppa vqrrvaagvl sagharalls
      241 ldnaeaqeal aerivregit vrgaeelvhl alaeepaksa aakrrpkpha paltdladrl
      301 sdrfdtrvkv digrskgkit iefatvddle rivgiigmge dgtpea
//
LOCUS       WP_457607798             257 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607798
VERSION     WP_457607798.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..257
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27237
     Region          52..161
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtgdatasar atsqyatttg nltarmalha ygtnpqswfa wlgerlplag dvlevgagtg
       61 elwqrvshrg rltvtdfspa mcarlhevpd agvlrcdath lpfragavda liansmlyhl
      121 ddpdaalref arvlrpggrl avavngrdhm aelnalgpai gcpdlavrfh dkndvtaeat
      181 pariaahfdd vtverypdel vvpaaepila yvasmigplt aaqeaaaraa vearldaega
      241 frvrkhtvli satrgar
//
LOCUS       WP_457607802             267 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607802
VERSION     WP_457607802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29984
     Region          12..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          83..261
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meneptaeli raqlrrlrvr aelsqeefgr lvhfsgsqvs avelghrpld rfflaradev
       61 lgtggllmsl lklaerdgqp swfrpwleae rqaqqlrtyq ptlvpgllqt enyaramirt
      121 ddlitddeve rrlgvrldrq silsdpgrpk yiavieesvl rradegyrgl maeqiahlve
      181 caerphvdih ivpasvtvhv glvgpfalar gtdggwvghl enqlggvvvd kdedvaills
      241 rwesvrseal prrqsvelmk dvmtsws
//
LOCUS       WP_457607810             256 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607810
VERSION     WP_457607810.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..256
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=27923
     Region          5..190
                     /region_name="SGNH_hydrolase_like_1"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01832"
                     /db_xref="CDD:238870"
     Site            order(12,171,174)
                     /site_type="active"
                     /db_xref="CDD:238870"
     Site            order(12,171,174)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238870"
     Site            order(12,54,83)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238870"
ORIGIN      
        1 mrwrsyvavg dsftegmdda ypdgsyrgwa dlvatrlave agpdfgyanl airgrlfpnv
       61 vaeqvpsala mkpdlisfaa ggndvlrrsf dpdtfvprfd svvqrlrsgg sdvvlfrfad
      121 vmarlpgqrl vaprvallnr avgevaerhg ailvdlyadd tylnpllwst drlhlsaagh
      181 rrvaaqvlta lgvgcdeewl mvpphpaptp wlaaraadlr wvgrhlapwi krrltgrssg
      241 dfitakrpvl gpvdad
//
LOCUS       WP_457607814             300 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607814
VERSION     WP_457607814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..300
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33373
     Region          26..290
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mpvpsdphpr lqsyadpqrl vttewlaehl gdeglvvves dedvllydtg hipgavkvdw
       61 htelndqvtr dyldaasfae lcaakgigrd dtvvfygdnf nwwaayalwv fslfghqdvr
      121 lldggrqkwi aegreltrdk vsrprasypv perndapira yreqvmahva agrplvdvrs
      181 pgeytgemlh mpdypqegal rgghipgavs kpwksaandd gtfksadelr avyadqlgls
      241 psddvvaycr igersshtwf vlhhllgfpq vrnydgswte wgnlvrapvv kgdqpggltr
//
LOCUS       WP_457607818             199 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607818
VERSION     WP_457607818.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841242
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21419
     Region          20..66
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          82..187
                     /region_name="TetR_C_16"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17920"
                     /db_xref="CDD:465568"
ORIGIN      
        1 mdvtepatrt rrsdatraai lraarerfaa dgydratira iaadaridps mvmryygske
       61 glfaaaaefd lrlpdltevp pdrlgetltr hfvrrweadg tlvallraaa tnpgaaermr
      121 gifagqlava vartgadpat agrraglvas qilglaltry vvrlppvadl dpeeladwvg
      181 ptiqryltqp lppsrasgr
//
LOCUS       WP_457607826             855 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607826
VERSION     WP_457607826.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..855
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89882
     Region          4..855
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhdrarg pdgrtglsdl lrghrlavgl tqaelagrag vgvrtvrdle rgravrpqrt
       61 tvdlladalg lsgderrefv dtarpaasrl pgpgtddppv alpqpvpllg rerdvaevsg
      121 lldaypvvsl vglagvgkta lavtvahava arhpagvagv lvgegsdspd vlaasasmfg
      181 vnrladlscr igdrralllv davdrapdav aealrvltaa vptlrvlvtg rrpvglpgel
      241 vrpvapldvp pagavpadra dldrwpaaal faarlaqvrp epptpvelpa laalvrrlgg
      301 lplaielmaa rgrildvtel ldrygdrvld lsggrpgwep agpsagpsag psagpsagtv
      361 tlrdavatsy rllapadraa lrrlsafrnr wsvelaedll adggrrwdaa pmldrlrelg
      421 llsvrgsgpf rfrlldavrd faaeqadadg etarirmrha vvvaglvhrt apglvgaqms
      481 gavrlldeat sditaalays aehapetall laaslprwwr lrgrdvsgrh rlrelladpr
      541 tagarptlra wamlgaarla aehgagaeei pgvraalvif teagdvtgel sarsvlcall
      601 pglgahdear eqaeaalaaa trhhrvrema vaqahltwhd vrearlagar rrlatvdrla
      661 aqcgdqrlrv laradqaelt rlegryaeaa eqgrrvaaal aelgdpgrrr rtigavglal
      721 ahagrtdeal atvaelwpsg avpgrrrppa vemldlpgsg gdvrtedalr glieghvalh
      781 rgdrevaaew faaaadaaeg vagrrdlvea lvglavstad pavldrldaa rqvtgvsllp
      841 qeeellfsls arrrr
//
LOCUS       WP_457607850              84 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607850
VERSION     WP_457607850.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 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 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=8878
     Region          <34..82
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 maeltvpelm rvmrecaged esvtfaddvg gadfadlgyd slavlevtsr lshdygvtlp
       61 edgvaglrtp demvrfvnar lasg
//
LOCUS       WP_457607866             277 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607866
VERSION     WP_457607866.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..277
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29146
     Region          18..269
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 msapwrlsvd wpasgptrvf dlaqqmytgi phhpnhppys ftltkrhgei mypdgvsaaa
       61 emittgghvg thvdglahvs rlgrvyggvd vtasqsyagg vpdvsvhelp pmlapghlvd
      121 atvalgrplt padgvgadlf erwfadrarp rpgdvvlvrt gwdekwtdna aylgvttgap
      181 gvdvsgarwl tdhgvvaaga dtiafehmps palavhchll vdhgvpimea mnlaplaaee
      241 vwdfffiaap lsirggtgsp irplavvpdt tapetta
//
LOCUS       WP_457607868             384 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607868
VERSION     WP_457607868.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..384
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41261
     Region          8..378
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msviweprld degrhwrdla rdvaarhftp laeeldreqr ypwesvrvlv eeglagllve
       61 rehggrgasf vtacavieev sracpstgai ltayalgatp lvlagtpeqr erylgglarg
      121 eaisfaltee gagsdaarir ttaeregtgw rlrgekiyig nggasryyvv faltdpqagt
      181 rgitaflvdk dadgvvidry edkmgirgtl tsnlkldtwv pdgdvlgdln rgmrlamhtl
      241 sagrisvaaq slgvalagfd vasreaarre tfgrpiidnq gisfpladva tgitaarmit
      301 feaarthqeg gdvgvlgama klyasevahr avdtavqvfg gdgfckpcpa erlyrdqril
      361 eiyegtseiq rlvlgraika svaa
//
LOCUS       WP_457607873             369 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607873
VERSION     WP_457607873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Wilkens,S.
  TITLE     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   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 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   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   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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   9  (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 11449010
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..369
                     /product="sugar ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38656
     Region          2..267
                     /region_name="RbsB"
                     /note="ABC-type sugar transport system, periplasmic
                     component, contains N-terminal xre family HTH domain
                     [Carbohydrate transport and metabolism]; COG1879"
                     /db_xref="CDD:441483"
ORIGIN      
        1 mrrrsfasaa lvvalgmtat acstegaapa apaegkalea kdvrigfanf aepaspvlga
       61 idvgmrkeae krgweilvln ndrdgptava naetmvsrgv thvvefqgdg kvapqimdif
      121 nkagipviai diahpgahff ginnvesgrl sgraggtyak ekwgckpdlv tlleneesgd
      181 vallrtegil kglkevcpdi dgvitrrnsp ttpdgaqgva rdilvskpda kkilalggnd
      241 nmiigtinaa eqlsrageiy gyglgadlml fgvdtpglgg stafwyegya kqiytildrm
      301 vagekipvvd spkdpnalfn pvcafpkdav ssipplkeri dalyakdapa ksaaeqycpa
      361 gtetyglgk
//
LOCUS       WP_457607887             370 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607887
VERSION     WP_457607887.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..370
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38329
     Region          55..339
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkrkwallpa alatalvlsa cgggsddega ggegkeaklt maiasavigp keevavyava
       61 kelgyfaeek ltvdtintdg svaalqavas gsgditpada gsvlgaaekn vpikaigglv
      121 qnwpwvmavk pdspitggad lrgkkigvis lasgsapyar ayvkaagldp akdvellpvg
      181 vgaqaaaaln dgkvdmlaly tqayaviena gtelkyltnp dvfsgirslt fsvgardfda
      241 kkdsyerflr aaykamlfsa knpeaamkig ykvfpqilag ksaderlkad aesltawlkt
      301 atpasgdpeq fgdwgaisde ewaktqaytk eagqitgevd lkklwdpsll sgannfdkaa
      361 vlskaanyta
//
LOCUS       WP_457607891             376 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607891
VERSION     WP_457607891.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..376
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37957
     Region          18..227
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          134..374
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflairelgf arlrfalmga vialisvlmv mlsglsvglv rdgvsglqnl pvtsfafahg
       61 vqhdsafsrs vvdasavdtw rdqpgvaeas afgntlingr tdggtevdla lfgvetgsfl
      121 spavsegdrl gpadgivvsp taidaglrvg dtvtvdrlgt rlrvvgvteq qdtfghvdva
      181 yvplatwqav ksgtpagtqv paqaaqeita vavraadgas vdlaagdeaa gtesltldes
      241 ygaspgytae tttlqliqgf lyaisalvag affavwaiqr kqevavlral gastgwvlrd
      301 altqalilla vaiavgmgig lglgallsgg nvpfalhpqs iaaaaagllv lglvgaaaav
      361 vrltsidpat alagnr
//
LOCUS       WP_457607895             404 aa            linear   BCT 27-JAN-2026
DEFINITION  dipeptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607895
VERSION     WP_457607895.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..404
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44519
     Region          58..404
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 msrpvqepap ryagyrsfdy lvphvdykvf elapqigrvp ehdlglsdeq rarvsrllre
       61 hmaislhehp kilpadvtql rdynrtgrna fgfeglarsg mtavfdnfmn gtgcvtseha
      121 wkwddviydi glrfadvakq dhvvvattle qifeakrngq ialvagleaa tmieneldri
      181 dilygfgvrq mgiaysqanm lgsglsedrd gglthfgrra vdrmnklgia idishsgdqt
      241 sldvieasrv pvfithagar svwntprmkp deviracaer ggvigieaap httlsgdhph
      301 hsiesvmdhf tycvelvgid hvafgpdtnf gdhvglhdsf tqhlaigkah gvvdhprvpy
      361 vsgmenpaec fsniagwlvt hgysdeeiak viggniirvl qevw
//
LOCUS       WP_457607900             393 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607900
VERSION     WP_457607900.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..393
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42731
     Region          14..385
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mrlpesfyhs vrsrlteale qrgldgflat spaevaflsg ffyiaterpv ylwlpregdp
       61 llviprldee yaaqqgvtvp tityfeypgv vtaeetlasa lsrpggpvrr igvgaglsvg
      121 afralsraig gaelettdav aalrlckfpe eipfheaaar icdemlaagr alieealaag
      181 rplpredeia rhvigygtdr myaeydlvvy ttklagglvy agpnsalphg lptrrrlqpg
      241 dtlilslgaa vasrfveser tfvigeptae qvryyeadre aqevgtqami agrtcaevnr
      301 icldvlrdrg lgdyirhrqg hgiglqnhea pwvsdgddtv lapgmllsse pgvyvpghag
      361 yrisdtvlvq ddgprrltry prdlasniie gir
//
LOCUS       WP_457607905             251 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607905
VERSION     WP_457607905.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26969
     Region          14..238
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 marretalqa ahgrlrqlig sefrsgeklp nerdlaerle vsratvrevl gqlvaegvvt
       61 rtwgigtfvh ddaervpvsi gdvtalrdri tasghrptlq daavsrakcp adcarvlgle
      121 pdspvwrvdr lfavdgvpaa wirdhlplrf dgrdldpsgl lsidldmfef lagatgmpvr
      181 raeielsavl adeeaterlg vaighplvta tqvgygtgga plfhghitvr tdvltlrisr
      241 ggepepaspa e
//
LOCUS       WP_457607921             339 aa            linear   BCT 27-JAN-2026
DEFINITION  polyprenyl synthetase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457607921
VERSION     WP_457607921.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wallrapp,F.H., Pan,J.J., Ramamoorthy,G., Almonacid,D.E.,
            Hillerich,B.S., Seidel,R., Patskovsky,Y., Babbitt,P.C., Almo,S.C.,
            Jacobson,M.P. and Poulter,C.D.
  TITLE     Prediction of function for the polyprenyl transferase subgroup in
            the isoprenoid synthase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), E1196-E1202 (2013)
   PUBMED   23493556
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Chen,A., Kroon,P.A. and Poulter,C.D.
  TITLE     Isoprenyl diphosphate synthases: protein sequence comparisons, a
            phylogenetic tree, and predictions of secondary structure
  JOURNAL   Protein Sci 3 (4), 600-607 (1994)
   PUBMED   8003978
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..339
                     /product="polyprenyl synthetase 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=35732
     Region          14..336
                     /region_name="IspA"
                     /note="Geranylgeranyl pyrophosphate synthase [Coenzyme
                     transport and metabolism]; COG0142"
                     /db_xref="CDD:439912"
ORIGIN      
        1 mtvagstryp pfiddlarse sgrllraelg rrwpetpdrl daivryallp agkmlrpmmt
       61 lhaaeavggs prdvlaaalg teylhvatlv hddiidadtl rrgrpavpva ygipgaivag
      121 dhlifhafqa ivegsraapa asvvaavtal aeagqdlcrg qaleerlvgd ldagarwype
      181 mirlktgalf ravchigall ggadplvsaa larygehlgt afqirddlls ylstpeqtgk
      241 patsdlnngr ptlplllayd aigdaarvel lavlhrrgag pgdvewvtal lddvgavaga
      301 rrrmvehaer araelavlnp sasadvltgi aawmtsema
//
LOCUS       WP_457607930             424 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607930
VERSION     WP_457607930.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..424
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=44361
     Region          19..381
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtadvvvaga gagglacaha lgalglrvlv ldrqraptsi akgeilqpet vrildswgal
       61 dalratgarp vgrlairdas gepllcldya glpgayrqil cadygdlrav lagrlpatve
      121 vrwgvrvtgv rrdsggridg vrvvadgter dvaaplvvaa dgmssplrra agigverrey
      181 phglvafdvd gaevadevsa yrtarglclv yplpggrcrl yaqvtpgefr grvdleawcg
      241 rlladvpair plgqalrasl hrrqllavyr lrsarlgvpg lalageaaha vhpmaaqgvn
      301 sslgdaetla aclaaeggtp epaavdralr afeaarrprl dhvatvshna srmitavsgl
      361 pkllgarmmr rtaanprllg ltagnlsgth vrplsavdrl yqlglladrh ahtpsppvps
      421 eser
//
LOCUS       WP_457607943             550 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457607943
VERSION     WP_457607943.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..550
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=58852
     Region          72..547
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mgadnfratl aadmelgagn vllrlaehga dmdmprvtfd advdgipawt plslatltdr
       61 vaaraawfra rgvrradpia vyvtsapdvf lnflaltwlg aipalmngnm pvplaaefvr
      121 rlrgagvvvd adhaalaehd lgapilgdaa qtgtgdpaqa pphhrhhpee pvvithssgt
      181 trvpaaivhs hhglfaaira vrltesrpyg evremsalpa ahaagiitln qalcngyqll
      241 clsaqggpfa hsaetilsai erwrptgvfg favtwselar vdlttrdlss vrnwfntgdc
      301 aheahvrrlv avgshpaytr dgmvdvpgsk fvdmlgstem ghgafrithr lgsdrydrcv
      361 grpypfaeia lldvdtgeev ppgqvghvgl ksptlalgyw ndsvttyrtr lggyyltgdl
      421 myrdeagayh hvdrasdavd lgggtwlyta lseerilrhc pdvrdctvla atgedgttvt
      481 dvllllaada dpahdrtdrv raalgpsvaa tlrrvvtvpd ddvvtgptgk vrkflmrqrl
      541 ladagaprtg
//
LOCUS       WP_457607977             246 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457607977
VERSION     WP_457607977.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..246
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25970
     Region          165..246
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mitvdesltg rdalldaagh hpyarhalrr dqaargwrha gtvgwllppg ewsaggavga
       61 pgpaldvfaa hradgtlrag qsinlsradp devaarlpva rliewdflwt tappphqpeq
      121 ervvrltaad hpalaaliee afpattsrpg epgiadwygi rdgdrllacg adrsrgdigf
      181 lagltvapgh rgrglgaalt agmtcalfgr ydvvalgvyp dnvgairlyr rlgftaaerr
      241 tsvtla
//
LOCUS       WP_457607994             280 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607994
VERSION     WP_457607994.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..280
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=29041
     Region          104..275
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mtstrdrqra aaraklerem aeragrarkr rqtqaivgaa avlvlvvagt vwlvaalgdd
       61 dekqggttav agavqcayte vpkegrpaqi kdvglppaqq sgkgtqtmti dtnlgpitak
      121 idrakvpcta gsfthlaskg ffdntkchrl vtegikvlqc gdpsatgkgw rdtdgtggps
      181 ynlaeenlpt dkrppypegv iamansgqpg stgsqffivy gdspldpnyt vlgtitggmd
      241 vvkqvaaagd dgafakqagg ghpkkeitmt kvtmspvegg
//
LOCUS       WP_457607997             823 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457607997
VERSION     WP_457607997.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 823)
  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
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..823
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=90152
     Region          100..821
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mshdvvppve gtvhptgdad gsvtersgnp paratgatgg asdatadgga vvvpfpteas
       61 testpgsgfa lsnaptgrrv rarlarfnap wqtsqvsevl epliathren hpkadarllq
      121 rafdtaarwh sgqyrksgdp yithplavat ilanlgmdtt tlvaallhdt iedteytlda
      181 mradfggeva llvdgvtkld kvklgdaaka etirkmvvam akdprvlvik ladrlhnmrt
      241 ltflprpkqe qkaketleil aplahrlgmn tikweledla fgtlfpkrfe einrligehq
      301 pqreallrqv tqkvstdlka akikaettgr pkhlysiyqk mivrgrdfnd iydlvgvril
      361 vdtvrdcyaa lgvihanwqp vpgrfkdyia mpkfnmyqsl httvigptgk pvemqirtya
      421 mhrtaefgia ahwkykehkg tpvvgppahi demtwlrqll dwqreaadps efldalrfdl
      481 ssqevyvftp kgdviplptg stpvdfayav htevghkcig arvngklvpl estlsngdvi
      541 eiftsksdta gptqdwlgfv ksprartkir qyfnkerree aieagkdaiv kamrkqgmpl
      601 qrmltsdalm aiardlhlad vaslyaavgd sqvsaqsvvq klmasyggee gaaediaeta
      661 vatrpprsrq ssadpgvvvr gvsdvwikla rcctpvppds vfgfvtrsgg vsvhrddcan
      721 aedlraqper vvevswklts astflvaiqv ealdrhklla dvtrvlseer vnilsatvtt
      781 trdrvavsrf sfemadpkhl ghllaavrkv dgvfdayrvt sga
//
LOCUS       WP_457608016             253 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608016
VERSION     WP_457608016.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27112
     Region          3..252
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 magqailsar gltrdfrgfr avdrvdldva petvhalvgp ngagkttlfn lltgflppse
       61 grieldgrdv tglppervar lgvarsfqit slfpqlgare hvelalqsgs glgwrfwrsa
      121 klmrryrdra dellamvgla dlaeapaeal aygrkralel aialaldpkv llldeptagm
      181 gledvdrtvd liaavrtgrt vvmvehnmsv vgrladtvtv lqagkvlveg pyeqvrader
      241 vitaylgaad aah
//
LOCUS       WP_457608021             626 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Nitratifractor sp.].
ACCESSION   WP_457608021
VERSION     WP_457608021.1
KEYWORDS    RefSeq.
SOURCE      Nitratifractor sp.
  ORGANISM  Nitratifractor sp.
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Nitratifractor.
REFERENCE   1  (residues 1 to 626)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 626)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Nitratifractor sp."
                     /db_xref="taxon:2268144"
     Protein         1..626
                     /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=67097
     Region          7..617
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,444,447..448)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mdlqtliyif vgatfalyiv ialwakaast kdfyvagggv hpiangmata adwmsaasfi
       61 slagiiaykg sdggaylmgw tggyvllall lapylrkfgk ftvpdfvgdr yhsdlartva
      121 viavifisft yvagqmrgvg ivfsrflqvd vntgvvigmv ivfiyavlgg mkgitytqva
      181 qymvmiiayl ipaiflslmv tdtflpqmgi fgtttfafnd gvkeipagty lmhaldqavt
      241 dlgfnaytmp gnlwnmfmlt valmvgtagl phvivrfftv pkvkdarasa gwallfiail
      301 yttiasvaaf srvniidrvq nvpykqwvte gvkqadgrin hggwfktwee ghllawndrn
      361 gdgkiqyaag kafddpkgkp hyngkvapdg hlltsnplpa egkkpgpfyn evyidrdiiv
      421 lanpeianlp nwvialiaag glaaalstaa glllvisssi shdllgrvmf kdpvtgkskl
      481 tdkqellaar iaavaaivva gylginppgf vaqvvafafg laaasffpti ilgifdkrmn
      541 kagaiagilt gliftfsyiv yfvfmggdpk dylfgvapvg igtigmvlnf ivsllvsrvt
      601 epppahiqem veniriprga geahdh
//
LOCUS       WP_457608025             217 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608025
VERSION     WP_457608025.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22943
     Region          5..127
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          74..201
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mprprqallt rdrivetala lidadgldal strrlaaalg vrgpslynhf atkeeildav
       61 adgvaatvdi svfdedewld alrrwarsyr aalaahpniv pylaqgpgrr paalamadav
      121 ygalvragwp parathigaa mryfvagsal gsfargfved pslyaahphl nqahrlaghq
      181 rsvdegafal gldallhgla aeyaatvapl ervggpe
//
LOCUS       WP_457608028             390 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608028
VERSION     WP_457608028.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..390
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43623
     Region          1..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfalsdeer airdtvrtfv trevmpleae vlrrerahqp gldrselrel qlkakkfgfw
       61 glatpeeygg mdlpavmqsl iwtelgrsfv pfrfggeadn ilfhateeqk refliptieg
      121 eriscfaite pgagsdaani klrarrdgdd wildgektfi tngndadfai vvavtdpekg
      181 arrggatafl vdramgwrse fiqtmgeggp aslifdgvrv phrnilgeig qgftlgmewi
      241 gkgrytipsh avgiaeralq maidhantre tfgapiatnq aiqwmiadse teleaarwli
      301 lrsawtvdqg ldprhassmg klygagmvnr vvdrvlqihg gmgytrelpi erwyrqvrly
      361 rifegtdemq rliisrdllr gytkigghla
//
LOCUS       WP_457608037             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608037
VERSION     WP_457608037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..353
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36679
     Region          1..347
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 mntfqatrlv aareikvkvr dktflystli flllavvatv vpalmssgps tvavtaagae
       61 plraagldvm lvaddgaaeq avrdgdadaa vvagplvvad erapddvvsa lsaapqvkll
      121 dpdavdplva ylvpfafafv fffmsqtfgl qiaqsvteek qtriveilva avparallag
      181 kilaagalal gqitliaava ligmrltdgg dllgliapai gwfvpfflcg flllaamwaa
      241 agalvnrqed iagastpvql avmapffavi flndnaaamr ilsylpisap tampvrlftg
      301 daapwepivs lallllaaag fllagariye gsllrtngrt svraawrqre pig
//
LOCUS       WP_457608061             387 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608061
VERSION     WP_457608061.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11111798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..387
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41919
     Region          16..380
                     /region_name="DegT_DnrJ_EryC1"
                     /note="DegT/DnrJ/EryC1/StrS aminotransferase family;
                     pfam01041"
                     /db_xref="CDD:395827"
     Site            order(64..65,161,164,185,189..190,322)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99740"
     Site            order(64..65,89,161,164,185,190)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99740"
     Site            190
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99740"
ORIGIN      
        1 msgqpstvse fpewpqygde ertglirale qgqwwrmggs evdsferefg dyhgsphala
       61 vtngthalev alevlgvgpg tevivpaftf issslaaqrl gavavpvdvd ldtycvdpaa
      121 veaaitprtk vimpvhmagq fadmdaldkl aadagvallq daahahgaqw rgrragalgs
      181 vaafsfqngk lmtageggav vfpdeelrer aflvhscgrp rtdreylhst tgsnyrmsef
      241 taavlraqlt rldeqialre qrwpllssll aeipgvvpqa tdprtdrnph ymamfripgi
      301 gierrravvd aliargvpaf vafraiyrce gfwmaaapde saeaiaarcp nteqihsdcv
      361 wlhhrtllgt eqqmheiaav ladvlag
//
LOCUS       WP_457608068             596 aa            linear   BCT 27-JAN-2026
DEFINITION  substrate-binding and vWA domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608068
VERSION     WP_457608068.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20696117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..596
                     /product="substrate-binding and vWA domain-containing
                     protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=64536
     Region          51..360
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          320..589
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
ORIGIN      
        1 mtpsvtrtqq wlpytaavta glvviagafv fvqqrdagse vprtdcattl qvnsstekaa
       61 llvdlaeryn rssrsidggg caqvhvsaln sgqatealat gwtrtglpqp qvwlptsslw
      121 tgqlrlldqa agrapqtpdr ypsiansplv iampqpkael irrrgplgwg eilglsgrdg
      181 wagfgkpewg rftfgkdnpn lstsglaati atyyaavqrs sdltrsdlad pavtqfvrri
      241 eanvshysdd svdllrslae adlaggagst ddmsaivlqe elvdlyntga lsprqdgqer
      301 grrpnvplva vhpeegtfnl dhpfvvlpsa derqraaatd flafltedaq qesfarlgfr
      361 dherrasael lanvgaeptg glsyfeppdp qvvgamldgw rtlrkkanil ialdtsgsmq
      421 amvgtrtrfq vasaaagkgl allntedrvg lwsfssetpk rpkspyreei plgefdqkri
      481 nskiaglhvd ggtalyatvr aahrelldry dpqrinaivv ltdgkneyrq dndlarllte
      541 valdprrpvk vfciafdres dfatldriak assgkafdat dpakideafv klvssf
//
LOCUS       WP_457608075             227 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608075
VERSION     WP_457608075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..227
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24006
     Region          14..203
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mttapserpa pptlvedlll llfqpasgtv agentlfyvl ggavladlal gdhlttaarg
       61 risvvgsppp dgllrpawdy laekprgvqt vlaaigptlr epvlqrliar gdidrqphkv
      121 lglfrstalr egrterraql ladvrqalvd gvqptarvaa laallsasgt lpqfhreipw
      181 tssvitrake lergdwgada taqavtrtvt atvvnsviva itvlprs
//
LOCUS       WP_457608092             336 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar-binding transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608092
VERSION     WP_457608092.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..336
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35579
     Region          26..330
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mtsdsgnlre paiggvattq lrlltkvarm yhehglrqpq iaeqlhisqp rvsrllkqat
       61 vlgivrttvv tpagvhaele eeierrfglr dvvvadtghs spdeqstlka igaaaavyle
      121 ttltggdrig isswsstlls tvdamrprpn pvaeqvvqvi ggvgsstsqi yatrladrla
      181 iltgaravfl papglasspa arevlmadph inevmgtygg ltmllaglgs lepspllmes
      241 gnaiadaeqq alrklgavgd iclrffdeng dlvksalder vlgidshtlr siprvvaiag
      301 garkftaira alrgdwvdvl vtdldvarrl aeepar
//
LOCUS       WP_457608089             188 aa            linear   BCT 27-JAN-2026
DEFINITION  RICIN domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608089
VERSION     WP_457608089.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19729
     Region          44..177
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(48..50,61,63,76..77)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(101..102,114,116,125..126)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(155..157,168,170,177)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mklrefaaal aalvgvvagg avapsaafaa dngpwevfpa savdkcvevq ggstassaqv
       61 qvytcatwgg gvtplhqrwi frptssgyqr ivngktgmca nikgstdvns tkivqyncgg
      121 sgtlndqwyp qfvrkiggfd fyqfksrlnp akclnvqgst tsdgsdlily pcsttnnaif
      181 swtpavqa
//
LOCUS       WP_457608096             374 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608096
VERSION     WP_457608096.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38165
     Region          38..349
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtirttlpap agpatdtata telatkarrl sllngvfelr afialavliv vfsllsdsfl
       61 tltnvitmtk hvainaiial gmllvilkgg idlsvgsvvg lsgvvagell qglrlgfldt
      121 vayppvwavi vlcvavgmvv glvngilitr frvapfiatl gmlyvargla llisdgttyp
      181 nlagspelgn tgfdilgsgr plglptsiwl mvilaaaval vlikspfgrw lyatggnera
      241 aelsgvpvrr vktivyvvag acaavaglii aseltsaapq agetyelnai aavviggaal
      301 sggrgtvrgt lvgafvigfl adglvllgvs tfwqilikga vivlavmldq gqqrfqrrqg
      361 avasaaaatk asps
//
LOCUS       WP_457608098             512 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608098
VERSION     WP_457608098.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..512
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=54362
     Region          1..503
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mtpilracav tkvyggthal kgvdfgiaag rvtalfgeng agkstlmkil agieqpttgh
       61 ieldgapirp gsarqaadqg isiihqelsl cpnlsvqdnl flarevrtrg vvdraaqrea
      121 tlavlrrlee dlnpdqpvge lrlgqqqive iarallqdar vlimdeptsa ltapevavlf
      181 rlireltagg vavvyishhl dealeiaddv avlrdgtlva tdtarevtlg wivqhmvgrd
      241 pdalfperep vvgapvlsad rivvadpqnp hrlavdgvsl tlregeivgi yglmgsgrte
      301 llealagrit paagtitldg aplgnagirr riaqgialvp edrqrdglvq smsvgqnlsl
      361 aglsrfvrrl lvtrgaerea vertisevtv ktsgagasig slsggnqqkv vigkalltrp
      421 rvllldepsr gvdvgakadi felmavqarr glsvlfatse aeealhipdr llvlargvvv
      481 gefrrgqitr edlmslsdgr vaapttrkep aq
//
LOCUS       WP_457608104             323 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608104
VERSION     WP_457608104.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..323
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33384
     Region          10..313
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mtvveqatfd crqafadelr alarlddriv avcndsvgss nlvgfreefp qrlvnvgiae
       61 qdlvgvaagl anagkipyvc aaapfltgra leqikadvay snahvvlcgq spgmaygelg
      121 pthhsiedls wmravanldv ivpadpdqtr aavrwaatag rpcylriprf kvpavtppda
      181 pfapgtavrl tdgddvtvia igsltsrald aadrlraegi avrvlnmpfv dpidtravla
      241 aaaetrgivt aeeatvtggl gaaiaaivaa arpapmrilg iprvfaptgd taflldhfgl
      301 tadgiaaaar dlfdasgpgg grg
//
LOCUS       WP_457608106             304 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608106
VERSION     WP_457608106.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..304
                     /product="transketolase"
                     /EC_number="2.2.1.1"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32919
     Region          41..302
                     /region_name="TktA1"
                     /note="Transketolase, N-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3959"
                     /db_xref="CDD:443159"
ORIGIN      
        1 mtdlldevap vklsadpdrc arygelsarl rvsdadvaav elrrisrevr rsiirmidra
       61 rmghiggdls vtdilvtcfw galsldpqrp awherdrfil skghcaaaly stlahcgffp
      121 aseldtfmap msalnghpnr lkvpgvetnt galghglpva tgcaiaaqlt gatwrtvvvl
      181 gdgemqegsn weaamtaahh glssltavvd rnrlqqgart eetkrlepla dkwrsfgwev
      241 revdghdhaa llralgpsst gqpvavvant ikgkgvsfme drvewhhkvp tpdqterala
      301 elvg
//
LOCUS       WP_457608108             339 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608108
VERSION     WP_457608108.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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 339)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..339
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37490
     Region          59..298
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msdqaridmp lpvfgagiwh fgryvdryat dgygppvntl eainlaskvd dlsvvdltyp
       61 fdpsglavad vagvltmngl ravavtpeiy trrfnrgaft npdaevrraa ielvseaaev
      121 arelgcdyvk lwpgqdgwdy pfqadhrqlw qysvdavrel aaafpdlrfa ieykpreprn
      181 amvfssvart llaiediglp nvgilldfgh slyggespad aarlaisrgr lfaidvndny
      241 rgwdddmvvg smhpietfef fyalveagwq gvwqldqfpf redsvqaatd girvmkrihr
      301 aigavdreal haaqqaqdal aaqriiqnal ygtyeggrt
//
LOCUS       WP_457608126             266 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608126
VERSION     WP_457608126.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..266
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27157
     Region          1..224
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnltdrvvvi tggaggigaa lgrrfaaega aaivladlaa daaraaaeai gpvasgvgld
       61 vtdeaavral veeterrhgr idlfcanagv atgggidapd adwdrawrvn vlghlhsara
      121 vlpgmlsrgq ghllltcsaa gvltavgdap ytatkhaavg laewlaityr dagirvsalc
      181 pqgvdtpmla dglaeghlga rviaasgail tpdqvadavv aglaeerfli lphpevadya
      241 rrraedpdgw qaglrklvrk lraadr
//
LOCUS       WP_457608142             362 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608142
VERSION     WP_457608142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..362
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37753
     Region          11..336
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msaaddrsia rrtliviglv latgvglalv watrrvlvwg lvavffaval kplvdrlerr
       61 vrrralatll vflaafalls avaalivvpl vdevgrfadr apdlvreaqa gqgplgrlld
      121 rfhllryaep gqlrrygarl gdptvgvvrs vaqavaalvt vvvlaylmvl eapkivaatl
      181 rltgdgaaar lrrigrdssr ivtgylsgnl lisvicgglt fvvlfllgvp faavialtva
      241 vfdliplvga tlgalaaaga aflhsptagl vvlvffvvyq qvenhllqpv imgravrlnp
      301 ltvlvsvlls velaglvgal laipaagivq vllrefapag rqalpqpadg dpagsrhppa
      361 gg
//
LOCUS       WP_457608144             262 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608144
VERSION     WP_457608144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..262
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27768
     Region          20..215
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mdhddtetle ivvdparpsg rtlladgveq syvdvadary lhfeyvrria aaidlaaprg
       61 aaltalhlgg galtlprwla strpgsaqrv ierdpgvvel vrrrlprlpp evvvalgdar
      121 eavagepsgt ydvvvadvyr aarmppqvaa vefaaqvarv lrpdglylin ltdlpplaht
      181 raqvatlrav fadvclvadr rmlrgrrygn vvlaatpttg ripvirlatr vaadpvpgtv
      241 lhgatldafa agahpvtdad lg
//
LOCUS       WP_457608154             312 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608154
VERSION     WP_457608154.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..312
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32629
     Region          37..312
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mtermvderp sgprsrrgtl vvvcavllal llaghrlvpn vnglgslvds vtpllgiavp
       61 alalaallrr srpallavll paliwaglyg rawlppaaga dgatvrvvsq nlrvsnpdpa
      121 atvgaltgda pdliglqeva dggrvapvla gryphravvs tvalwsrwpi reahgvdtgl
      181 gwdralravv aaprgdltvy vvhlgsarag htatrdqtva aladavradp adrlvvlgdl
      241 ntattdrvfd pltrllgdaq aeagqgfgft wpaelpvtrp dhvlyrgltp ttagvlrtpd
      301 sdhravtagf rw
//
LOCUS       WP_457608156             315 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608156
VERSION     WP_457608156.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..315
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33239
     Region          7..267
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(7,31..32,61,66,71..74,91)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,35,37,69,90..93,97,99,135,137,
                     139..140,142,151..152,155,172..175)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,35,37,69,90..93,97,137,139..140,
                     142,151..152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(18,97,99,135,137,139,155,172..175)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(151..159,168..175)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mrtlggryel eqraglggms evwrahdrvl drtvavklis paldgdagsv driraearsa
       61 arlvhpnvas vhdfgtatlp dgrpvpyivm elaegetlaa hlrggpldwr iavrvcaevc
      121 aalaaahahg ivhrdvkpan viltpcgvkv ldfgiatpag apdhtpdgvv vgtpaylape
      181 qldrqpatpa admyalgvll yycltgelpy eagsttqllg srrrrpprpl pevpglpsev
      241 aelcrrclda dpcarptspm aalllaeavd arvyvpmtat lprqrepqvs pwtsraaaea
      301 teamavdaat sgrvg
//
LOCUS       WP_457608160             805 aa            linear   BCT 27-JAN-2026
DEFINITION  ArnT family glycosyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608160
VERSION     WP_457608160.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 805)
  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   3  (residues 1 to 805)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..805
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80484
     Region          36..>273
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mnrtdslptv ptaappgtep apapvppqtr tgrdprwarp allgllvvta llylwglgas
       61 gwanafysaa vqagsqnwta ffygssdaan sitvdktpas lwlmalsvri fglsgwsilv
      121 pqallgvasv gvlyatvrrw ygpaagllag avlaltpvat lmfrfnnpda llvfllvgaa
      181 yatvraveta strwialtgv lvgfgfltkm lqaflvipvf agvyllaapt glgrrirqll
      241 laglavvvsa gwwvaivelv pasarpyigg sqnnsilelt lgynglgrit gdevgsvggg
      301 gggrpggggg gpfsgqtgll rmfdtevggq iswllpaali llvaglwlag raprtdrtra
      361 glllwggwll vtglifsfms gifhayytva lapavgalag igvtllwrar sapvaadaaa
      421 pvpavadapv vagasvvaap rrrralvatl vlagtlavta wwswhllgrt pdwhswlrpt
      481 vlalgltaaa llatlavike fvsgngvqsd anslvnsetg vkaragagia grvvrwvvpv
      541 vsvagiaval agpaayamqt aatphsgsip sagpagaggf ggpggpggrm pggangqfpg
      601 gpgggngqfp gfpggpngtg sdgtgsngtg pggtgssgtg pgdtgqdgga naggfpgfpg
      661 ggsapgapgg tgqegrgqrg ggmgglldar epstemtall tadaddytwv aatvgsnnas
      721 gyqlatgrpv mpiggfngsd psptlarfqq yvadgrihyf lggggfradg gsnasaeiaa
      781 wvaetftatt vdgvtvydls sgkqg
//
LOCUS       WP_457608162             407 aa            linear   BCT 27-JAN-2026
DEFINITION  dolichyl-phosphate beta-glucosyltransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608162
VERSION     WP_457608162.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 407)
  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 407)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 407)
  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 10135784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..407
                     /product="dolichyl-phosphate beta-glucosyltransferase"
                     /EC_number="2.4.1.117"
                     /GO_function="GO:0004581 - dolichyl-phosphate
                     beta-glucosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42941
     Region          24..230
                     /region_name="DPG_synthase"
                     /note="DPG_synthase is involved in protein N-linked
                     glycosylation; cd04188"
                     /db_xref="CDD:133031"
     Site            order(27,29,113)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133031"
     Site            order(61,112..113)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133031"
     Site            111..113
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133031"
ORIGIN      
        1 mtdtyapraa vqarpaagsa vldvvvpvyn eeadlgpcvr rlhahltahf pypfritvad
       61 nasvdgtpav araladelpe vgvlrldekg rgralraaws aspapvlaym dvdlstdlaa
      121 llplvaplis ghsdlaigtr lartsrvvrg akrevisrgy nlllrgalaa rfsdaqcgfk
      181 airadvaael lplvrdtgwf fdtellvlaq raglrihevp vdwvddpdsr vdivatalad
      241 lrgigrlgra lvtgalplaq lraqlgrgpl pappaqvpig lprqlarfaa vgvastlayl
      301 llflaargpl gaqpanllal lltavantaa nrrltfgvsg rrhvgrhhlq gllafalgla
      361 ltsgslatlh atttpnrale ltvlvtanla atalrflllr lamhhrp
//
LOCUS       WP_457608183             348 aa            linear   BCT 27-JAN-2026
DEFINITION  iron-containing redox enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608183
VERSION     WP_457608183.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilks,A.
  TITLE     Heme oxygenase: evolution, structure, and mechanism
  JOURNAL   Antioxid Redox Signal 4 (4), 603-614 (2002)
   PUBMED   12230872
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Ryter,S.W. and Tyrrell,R.M.
  TITLE     The heme synthesis and degradation pathways: role in oxidant
            sensitivity. Heme oxygenase has both pro- and antioxidant
            properties
  JOURNAL   Free Radic Biol Med 28 (2), 289-309 (2000)
   PUBMED   11281297
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Maines,M.D.
  TITLE     Heme oxygenase: function, multiplicity, regulatory mechanisms, and
            clinical applications
  JOURNAL   FASEB J 2 (10), 2557-2568 (1988)
   PUBMED   3290025
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..348
                     /product="iron-containing redox enzyme family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37297
     Region          144..312
                     /region_name="Haem_oxygenas_2"
                     /note="Iron-containing redox enzyme; pfam14518"
                     /db_xref="CDD:434009"
ORIGIN      
        1 msvtadsryg paplpaargp vsaallaalr eaphalpagl gqhlnavaap ltdedlqltl
       61 flcyelhyrg wsgvdeawew epsllslrar aerpfeaalr elagpppavl ptgvpgalad
      121 lvaaddgppl aatlqrradl nqfrefvthr siyhlreadp hswalprlgg pakaalveiq
      181 tdeygngrld rmhaelfrtt mdrlgldtgy aahldrvpav tlatnnlmsl fglhrrlrga
      241 llghlaayem tsslpnrryg nglrrlgfda vatrfydehv eadavheqia aydmcgglvr
      301 aepalasdvl fgaaaalald allaahllta wsagesslrp raenlaaa
//
LOCUS       WP_457608193             238 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF and ANTAR domain-containing protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608193
VERSION     WP_457608193.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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   2  (residues 1 to 238)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 238)
  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 238)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10588662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..238
                     /product="GAF and ANTAR domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24987
     Region          24..162
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          <187..229
                     /region_name="ANTAR"
                     /note="ANTAR (AmiR and NasR transcription antitermination
                     regulators) is an RNA-binding domain found in bacterial
                     transcription antitermination regulatory proteins;
                     smart01012"
                     /db_xref="CDD:198080"
ORIGIN      
        1 midnlgvlet aallreltag ligaagfdea ldrlvriard avpgvdccgf talragepag
       61 vaasdpdrae lddlrhgpdt pamtaihrre miiagglpde trwpawsera ralgvhgvis
      121 apvdvdeqvi gainlyaeap daltprhqlt amllaehagl llaaardrer aasrageidd
      181 sllaegvvgq avgvimtqrg cpapealrvl rsaassldip lrevaerlvl tvsrprdn
//
LOCUS       WP_457608190             362 aa            linear   BCT 27-JAN-2026
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608190
VERSION     WP_457608190.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..362
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38766
     Region          65..360
                     /region_name="2-desacetyl-2-
                     hydroxyethyl_bacteriochlorophyllide_"
                     /note="2-desacetyl-2-hydroxyethyl bacteriochlorophyllide
                     and other MDR family members; cd08255"
                     /db_xref="CDD:176217"
     Site            order(66,68..69,72,136,141,174..179,198..199,203,220,
                     245..246,248,268..269,295..297)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mrdrvvvvgg pgrvelaeld apelregtfr vetlysgvsa gtelsfvkgt npylhvtwda
       61 alglfrpgea stpypvtrlg ymqvgrvvas rtpavavgev gamtyghrsg wvadplterf
      121 vplpddldpl lgvyvahmgp icangllhaa adlcgadvrt lgdgvrgrrv avvgggvval
      181 ltalfarrhg aasvvvvdpt parrqvaeal gldtldpdad dpavvlktrw nhaagdrgad
      241 vvfqcrgqdw alqlalrllr pqgtvidlaf yqagadavrl geefhhngls lrcaqigrvp
      301 rglaptwdre rlsaetvell rqygdvirkh lisavvplde aptlltdlae rrrselqvvl
      361 tp
//
LOCUS       WP_457608202             247 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608202
VERSION     WP_457608202.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26621
     Region          16..239
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mtqpepltpl tedwqralav vahpddlefg aaaavarwtg qgkevvycll tsgeagidgm
       61 tperarvvre eeqrasaavv gvseveflgl pdglleygvp lrraiaavvr rhrpdvvltn
      121 nfretwdgay alnqadhiac gratldavrd agnrwifpeq ltdgtqpwsr vrevwaagsp
      181 varhgvdvtd tfdrgvaslr ahgaylsglg dggfdaeefl egmarpagsr lgarfgatfe
      241 vfpinlq
//
LOCUS       WP_457608204             425 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608204
VERSION     WP_457608204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..425
                     /product="cupin domain-containing protein"
                     /EC_number="1.14.11.47"
                     /GO_process="GO:0043687 - post-translational protein
                     modification [Evidence IEA]"
                     /calculated_mol_wt=45343
     Region          33..327
                     /region_name="RoxA"
                     /note="Ribosomal protein L16 Arg81 hydroxylase, contains
                     JmjC domain [Translation, ribosomal structure and
                     biogenesis]; COG2850"
                     /db_xref="CDD:442098"
ORIGIN      
        1 mstthvdppg ghgrpavpfs atealgrcva vepakfaadh wgrspllsra aelpnadgft
       61 dllspddade llsrrglrtp flrvakdgql vpaarftggg gagaeigdqv ldekvlalya
      121 dgatlvlqgl hrtwpaivdf ardlgtalaq plqvnayltp agsqgfathy dthdvfvlqv
      181 egrkhwrihp pvladplerq pwggradevs ataegrpeld vvlepgdaly lprgwlhsaq
      241 aqessslhlt vgiraltrya vveellalaa edarlraslp fgldladpda iepeltetve
      301 alrdwllrad paavagrlra rvwpaarpap irplaqaqal arltaaseva vrgglrwqlt
      361 paadgrvtlr vpdrtltlpg tceaalrall tgevtrvgdl pgldddadrl tltrrllkea
      421 vlvpa
//
LOCUS       WP_457608219             385 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608219
VERSION     WP_457608219.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..385
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41170
     Region          7..364
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkgqqtpagd lrlvdltkrf gvftavddlt ltipqgsffa llgasgcgkt ttlrmiagle
       61 qptsgqvllg eqdiaglrpy krpvntvfqs yalfphldih envafglrrr girnvgdqve
      121 rmlalvqleg ygrrrpaqls ggqqqrvala ralinhpqvl lldeplgald lklrrqmqie
      181 lkriqtevgi tfvhvthdqe eamtmadtva vmnagrieql gapadiyeyp atafvanflg
      241 qsnllaaead graaddvlvt ahgsrfsvpa grarltdgpa flgvrpeklh lvdgpdrvpa
      301 ghqhvggvvt dasyvgvstq ylvrtawgse lsafaansgl ggqlpvgaav tahwdprhaf
      361 llpraagedd qtaplldepp vgalp
//
LOCUS       WP_457608222             473 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608222
VERSION     WP_457608222.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..473
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51388
     Region          36..418
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtlphtgral adaapvsywl drpvrpdplp plsgthtadl lvvgggyagl wtallakead
       61 pdrdvllvda gtcgwaasgr nggfcaaslt hglangverf pgeigelerl grenldaiaa
      121 tvakydidcd fertgelava iepyqldgla adaelarryg hdvrlldrde vraevaspty
      181 lggmwdrdrv alldpaklaw glrraaldlg vrvhehtrvt glagdgaalr attaggadaa
      241 pgtvrarqvv latnafppll rrlrswvvpv ydyalmtepl teaqrdaigw rhrqgladtg
      301 nqfhyyrlta dnrilfggyd avyhygnrva paleqreatf ttlaehffat fpqldglrfs
      361 hrwggvidtc trfcaffgta ysgrlayaag ftglgvgatr fgarvtldll sgtdtpltrl
      421 dlvrrkplpf ppeparsvgi nltrwslara dardgrrnlw lrtldrlglg fds
//
LOCUS       WP_457608224             400 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608224
VERSION     WP_457608224.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..400
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42902
     Region          25..399
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrillvgagg vgsaavsiaa rrtffeimvv adhdparaar avaglgdrfv aatvdassad
       61 avaalcrehr ithvlnavdp rfvmpifdga faagadyldm amslsrphpe rpyaetgvkl
      121 gdeqfavaer waaagrlalc gigvepglsd vfaryaadel faeideigvr dganltvagy
      181 efapsfsiwt tieeclnppv iweagrgwft tepfsepemf dfpagigpve cvnveheevl
      241 liprwvpakr vtfkyglgae fievlrtlhk lgldstepvr vrgvdvsprd lvaaalpdpa
      301 tlgdrmsgkt cagtyvtgtg pdgrprrvyl yhvvdnewsm aeyghqavvw qtavnpvval
      361 ellatgawsg tgvlgpeafp ptpfldlltg ygspwgmeer
//
LOCUS       WP_457608263             162 aa            linear   BCT 27-JAN-2026
DEFINITION  anthrone oxygenase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608263
VERSION     WP_457608263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Lin,Z., Zachariah,M.M., Marett,L., Hughen,R.W., Teichert,R.W.,
            Concepcion,G.P., Haygood,M.G., Olivera,B.M., Light,A.R. and
            Schmidt,E.W.
  TITLE     Griseorhodins D-F, neuroactive intermediates and end products of
            post-PKS tailoring modification in Griseorhodin biosynthesis
  JOURNAL   J Nat Prod 77 (5), 1224-1230 (2014)
   PUBMED   24786728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..162
                     /product="anthrone oxygenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16786
     Region          6..157
                     /region_name="COG5500"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444251"
ORIGIN      
        1 mrlvqqltlv gatvgaglma glfaafayav mpalrgaedr tfvdamqrin vtivngwfll
       61 aflgtpvlaa laavlawrga trpalpwiva glalylvmfv vtvavnvpln dalaaagtad
      121 lgaarerfes awvtwnvvrt lasnagfgal cwalvlagra tg
//
LOCUS       WP_457608269             298 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608269
VERSION     WP_457608269.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..298
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /EC_number="1.14.99.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31178
     Region          31..249
                     /region_name="COG3397"
                     /note="Predicted carbohydrate-binding protein, contains
                     CBM5 and CBM33 domains [General function prediction only]"
                     /db_xref="CDD:442624"
ORIGIN      
        1 maarrafaal aavaatvplt aapaaahgap tsplsraaac gpeggraqtp acraavaaga
       61 avrewdnirv aridgrdrer ipdgelcsgg lsayrgldla radwpattlt agarhtfryr
      121 ttiphrgtfr yyvttgsysp rrvltwadle ekpflevtdp piragayemr grlpagrtgr
      181 hlvyviwqns dtqdtyyscs dvifraarge pdppsaapka gaspprtlag paaddepavp
      241 vatvtdggpl srplvagaaa lvvallaaav iglrraggpp pgrpcgvrnh ragrrrvw
//
LOCUS       WP_457608265             314 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608265
VERSION     WP_457608265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 314)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..314
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33584
     Region          2..172
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          224..304
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdavsglldg prargafllr siltppwsml irdeapltlv avvrgdgwiv pedgdaarlt
       61 sgdvaivrgp apytvaddpa tapqvvvhpg qtcttpdgre lfamtrwgvr twgngpggrt
      121 vlltgtypvr gtvgrrllda lpplavvrre swdtplvpll adeivkddpg qealldrlld
      181 llliaalrew farpgaaapa wylayadpvv gralrmlhdd parqwtvasl aaevgmsraa
      241 larrftalvg eppmayltgw rlalaadllr epgatvgava rrvgygssfa lsaafkrryg
      301 vsprrhvdpd rlag
//
LOCUS       WP_457608275             459 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608275
VERSION     WP_457608275.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..459
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=49362
     Region          28..412
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtdyrhlsyw lsgldepltp rpglpgdtda dvaivgagyt glwtayylar adptlrvvvl
       61 ereiagygas grnggwcsal fptslpaltr rhgrdralam qramhdtvte vgrvaaaegi
      121 dcdwraggtv mlargeaqla raraevaqah ahgltdddlt lldageaaar caaegvrggt
      181 ytphcaavhp aklvrglara verrgvrihe rtpvtalrpg aavtaagvvr apvvvrateg
      241 ytpglpgrrr tvapvyslmv atpplpeetw ariglaeret fsdyrhvivy gqrtadgrla
      301 fggrgapyhy asrvrpdfdr eprvfvalrr algelfpvlg pevpvthawg gplgvardwa
      361 asvgldrrtg lawaggyvgd gvgtsnlagr tladlirgve sdltalpwvg hrsprwepep
      421 lrwlamnagl kimssadkse hrtsrpsrra dlftrflgh
//
LOCUS       WP_457608288            3650 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608288
VERSION     WP_457608288.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 3650)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 3650)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 3650)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 3650)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3650
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..3650
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=378214
     Region          2..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          32..1422
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1237..1692
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1445..1446,1448,1469..1472,1497..1500,1524..1526,
                     1547..1548,1570..1571,1585,1612..1613)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1548,1572,1585,1589)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1706..1791
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1809..3200
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          3007..3465
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(3218..3219,3221,3242..3245,3270..3273,3297..3299,
                     3320..3321,3343..3344,3358,3385..3386)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(3321,3345,3358,3362)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          3484..3569
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 madeaklldy lkrvtadlhq vrqrlrevea geqepvaivs mscrfpggvr spedlwevva
       61 sgrdvvtdfp edrgwdlgsl ydsdpeqsgt sytrqggfvh dlpdfdpgff aisprealam
      121 dpqqrwllet swealeragi dphslrgsrt gvfagstgqd ygtvlmgaaq gleghlmtgn
      181 agsvvsgria ytfglegpav tidtacsssl valhlagqal rqrectlaiv agvtamctpa
      241 afvefsrqrg laadgrckaf aaaadgtgws egvgvlvler lsdaqrnghp vlavvrgsav
      301 nqdgasngls apngpsqqrv iqqalanagl atggvdvvea hgtgtrlgdp ieaqallaty
      361 gqdrgdsapl llgsvksnig haqaaagvag vikmvmamrh gvvpptlhvd eptpevdwsa
      421 gevslvteat pwpavsrprr savssfgvsg tnahtileqa papqqspsad gallverpvv
      481 pvpvsardaa glaaqagrwa ariaadetlr pldvafssvt srstlehrav vsvtgredll
      541 aglralaagq psgavvarqa ggrgslavlf sgqgaqragm grelyagfpv faatldevcv
      601 yldallprpl revlfapdgs aeaalldqtv ftqaglfave valfrlvesf giapefvggh
      661 sigevtaayv agvlsladac alvaargrlm qalpagggml avaadevavv esiagstdrv
      721 giaavngpts vvvsgavdal devervwrdr gvrtrrlvvs hafhsplmep mladfravld
      781 glefaapslp vvsnvtgala gdeictpeyw vrhvreavrf adgvtalraa gadtflevgp
      841 rsvltamvgd vlpaddavla vaaqradrpe ahgllaglae lhvhgvavdw rrwfadtgar
      901 rvdlptyafq hqrywpeaga gwtgdvtavg lrpaqhpllg aavgvahaeg flftgrlarr
      961 thpwicdhvv fdtvllpgtg fvelalqaga hvgadhvrel tlesplilpe tggvdiqlwi
     1021 gpadetgcrs vslhsaqdge paegagertw trnasgvlas gpaapsgptg wsdlttwppp
     1081 gatevgtddl ylnlsaqgyd ygpsfialrs awrrgddlfa elalpeapaa eaggyglhpa
     1141 lldaalhtlg lttpagepsg agmppgygrl pfswndvalh gagaaaarvr vshtgpdsis
     1201 llltdvtgap visvgslvlr pvsadqlrta sgggteslfq vewaplalpa gpstvdwavi
     1261 gdaaaltdav aatgtavaay pdltalatam ddgtdapgvl vlplldppas advpravaea
     1321 thrvlavlqq flaeeryavs rlvvltsgav atdrdadltd lagaavigll rsaqsenpdr
     1381 fvlvdvddva gcaaalvpav atdepqvvir agvaagarlt rvpapaeppa apfdsdgtvl
     1441 itgatgtlgq lmsrhlvsty gvrhliltsr rgraaggvae lcaelealgv svtvaacdva
     1501 draavaella gipaehplta vvhaagvrdd gvissltper mdgvlrpkvd aawhlhelta
     1561 dlglkafvsy sslaataggp gqgnyaaana fldglaqhrk arglaaltla wglwadrsgm
     1621 ttelddvhln risrsgvaam eaeeglalfd aacrttdaal vparldlaam kvqfaggsip
     1681 plyralirtp arasaattga slvqqlaglg daeraaalve ivrgqaaavl gypdpaaiep
     1741 rrafsefgfd sltavemrnr lnnafgmrlp atlvfdyptp hdlagflgte iagtpvpvrp
     1801 atttvpvgdd eplaiigmac rlpggawspd dlwrlvvdgv daisdlptdr gwdldslysp
     1861 dpdapgtfya rgggflsgvd rfdpgffgis prealamdpq qrlllettwe sfesagidpa
     1921 dvrgsstgvf vgtsgqdygs llayspeaae gymltgmtss visgrvaytf glegpavsld
     1981 tacssslval hwagqalrrg ecdmalaggv mvmatptafv efsrqrglaa dgrcksfaas
     2041 adgtgwsegv gmllvqrlsd arrqgrtvya vvrgsainqd gasngltapn gpsqqrvirq
     2101 alasarlsaa dvdvveahgt gttlgdpiea qallatygre rpadrplllg siksnighaq
     2161 aaagvagvik mvqairhglv patlhvdeps phidwtsgav elatesrpwp avdrprraav
     2221 ssfgisgtna hviieqgdep vdaarvdtrp glvdsgvvaw plsgrsreal tgqaarlarh
     2281 vrehgevdaa avgwslattr stfdhraavv gssteellag ldalasgspa gnvvagtams
     2341 hgagpvfvfp gqgaqsarma aglvgrtpvf darlaecqra lapfldvdlv svltgddesw
     2401 larvevvqpv lwavgvalaa vwqhagvvpa avighsqgei gaacvagils lgdaakaval
     2461 rsraltalrg tgtmasidls aeavaerlpv fpgvgvaavn gpstvvvsgp pqpvadlvea
     2521 cqadgvrarl ipvdyashsa avqevaerlr adladvtprp ghvrmvstlt gdwvdpasmd
     2581 agywydnlrq tvrfdpavrv avaaghttfv eisphpvltm pvtailddag vtghtlgslr
     2641 rgdddptrll tnlatahtig lpvdlttvla etdvvalpty afdhqrywve ppahraqdvs
     2701 saglqdaghp llsatltfpd sermvftgrl svrthpwlge hrvmdnillp gtafvelaty
     2761 agaqagcptv eeltllaplv lpelgalqvq ltvgdrdddg rrtvqlysrp yrdgsdeila
     2821 dvawtchatg llgpqpadaa pafdlgvwpp pgatrvesdd fysgieatvf gygpafrglr
     2881 aawirddevf aevelpaghh aeagrfgvhp alldgalqam siggflgrmg dgadadvprl
     2941 pfawtgvsll aagatalrvr vaaagevgvs fqvadatgap vlhvdslimr rvsgdslgaa
     3001 rsgrheslfq vdwpvlpvpt grvpaairwv algddlvlsa aceaagarvr tdvgldtlgd
     3061 llaggepape lvivpvgdag npsdpelaaq araathrtla alrtwladdr fadsrlvlvt
     3121 rdavaageqe pvnlrqapvw gllraaqleh pgrcqlvdld dapdsaaala aaiasgepql
     3181 avrdgqvrtp rlgrvpagve plpggidpag tvlitggtgv lgrilarhla tshgvrhlll
     3241 agrrgaaaeg igdlvgelag tgtevtvaac dvadpdalsa llagvpaahp ltavvhaagv
     3301 lddgvlesmt pervdavavp kidaawhlhr ltadanlaaf vlfssaaatl gsagqsnyaa
     3361 snafldalaa hrrarglvgi slawglwaqa sgmtghlgdd dvrrmaeqga tglateqaln
     3421 lfdaawrlda aavlpmrldv gtlrgqaetg tlapmlralv rvplrrsmda agarsggvql
     3481 grrlaglaap erlkvmldvv raniaavlgh agsdavdpnr lftdlgfdsl tavdlrnrln
     3541 slsglrlpat lvfdyptpta laekltseia adaapstqpl fqgidtvesl lnaipldpaa
     3601 rarftarmqd llakasdlaa gpavepdrpd ldsasddeif dfiskefgis
//
LOCUS       WP_457608298             220 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608298
VERSION     WP_457608298.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 220)
  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..220
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..220
                     /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=23099
     Region          14..215
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mieqilpptv avsesftdpa gvtlfpeeea lvarsvekrr refttvrhca rlalgelgla
       61 papivsgarg aplwpdgvvg smthcdgyra avvgrtaafa slgvdaepha plpdgvlgai
      121 alpaersrtv tlgavrpavc wdrllfsake avykawfplt gkwldfsead ivfdpagtfk
      181 arllvpgpvf ggaevrafag rflverglvv taisipavas
//
LOCUS       WP_457608323             190 aa            linear   BCT 27-JAN-2026
DEFINITION  copper resistance CopC family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608323
VERSION     WP_457608323.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   van Sorge,N.M., Bonsor,D.A., Deng,L., Lindahl,E., Schmitt,V.,
            Lyndin,M., Schmidt,A., Nilsson,O.R., Brizuela,J., Boero,E.,
            Sundberg,E.J., van Strijp,J.A.G., Doran,K.S., Singer,B.B.,
            Lindahl,G. and McCarthy,A.J.
  TITLE     Bacterial protein domains with a novel Ig-like fold target human
            CEACAM receptors
  JOURNAL   EMBO J 40 (7), e106103 (2021)
   PUBMED   33522633
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Lawton,T.J., Kenney,G.E., Hurley,J.D. and Rosenzweig,A.C.
  TITLE     The CopC Family: Structural and Bioinformatic Insights into a
            Diverse Group of Periplasmic Copper Binding Proteins
  JOURNAL   Biochemistry 55 (15), 2278-2290 (2016)
   PUBMED   27010565
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Cooksey,D.A.
  TITLE     Molecular mechanisms of copper resistance and accumulation in
            bacteria
  JOURNAL   FEMS Microbiol Rev 14 (4), 381-386 (1994)
   PUBMED   7917425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..190
                     /product="copper resistance CopC family protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0046688 - response to copper ion [Evidence
                     IEA]"
                     /calculated_mol_wt=19193
     Region          4..123
                     /region_name="CopC"
                     /note="Copper-binding protein CopC (methionine-rich)
                     [Inorganic ion transport and metabolism]; COG2372"
                     /db_xref="CDD:441939"
ORIGIN      
        1 mtrvrwasav vvglavllgw tgaawagsga assvpadgav ltsapsavel vftgrpvaad
       61 shvavrdaag rslavgeprp sgdrslvqtv rsaergdvvv ayhvvladgs eksgtlwfsv
      121 gtgvrparas dpggeaaapl hehgidplsa vlllvnavvv fvavamlvlr prrsvepppa
      181 aaqqpemssr
//
LOCUS       WP_457608327             348 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608327
VERSION     WP_457608327.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..348
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36344
     Region          192..305
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 msgqqsaarw rtsvtgpqrd rwatvlghvt saipagtayv lvdgnerdat vladrlaaal
       61 rdagrprirl sraicagpad lrggltpgsv viaagpawra qlpaghwhlt irvrgasper
      121 grrhrsdaad ivvdladpaw pvirhigawf thtdawyrte tqaffaaraa twdtgsgadl
      181 aayaaavtea aipagasald vgcgtgralp alrdavgptg tvlgvdltpa midvarsrah
      241 aadaalalad vrrlplpgca vdavfaagll lhlpdtdagl relarvtrpg grlvlfhpsg
      301 radlagcgtq pgdpltetsl rlaahrtgwh ltgyddpphr flalatrr
//
LOCUS       WP_457608334             336 aa            linear   BCT 27-JAN-2026
DEFINITION  3-oxoacyl-ACP synthase III family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608334
VERSION     WP_457608334.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=36134
     Region          <66..335
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msfglvsfge algdpapvad vvaqytddvn rvlgygyrlv hraapdiglt dlaeraarra
       61 ldaatlpaar vdllvlavtd ltehlywdaa adlayrlgaa gaeavlltqa cttgvlsldt
      121 vagkfathpe yatalvvaan rtceaywnrm dtqpmvfsdg avatvarrgh prlrwqvtea
      181 atdgryagfy rldgggaaap fapgaeppaa rdvwhvmeff dydpeqfaqy arhldermvr
      241 vteracerag vtvadlarli lvadneramt slaeahkvpp ertnralaae yghlgaadqm
      301 fglsrlldag elhdgdrval islgrgthwa ctiiev
//
LOCUS       WP_457608340            1768 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase/MFS transporter [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608340
VERSION     WP_457608340.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1768)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1768)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1768)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   4  (residues 1 to 1768)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 1768)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 1768)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   7  (residues 1 to 1768)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   8  (residues 1 to 1768)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   9  (residues 1 to 1768)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18492676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1768
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1768
                     /product="non-ribosomal peptide synthetase/MFS
                     transporter"
                     /EC_number="1.14.-.-"
                     /EC_number="6.2.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=189192
     Region          18..1315
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
     Region          1334..1711
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(1344..1345,1348..1349,1352,1384,1439..1440,
                     1442..1444,1447,1467,1470..1471,1474,1549,1552..1553,
                     1556..1558,1582,1586,1640..1641,1645,1649,1665,1668..1669,
                     1672..1673,1676)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtesrhdvtp vddvytvpas yaqervwfta qlspgqplft mtdavtlpag agpeqalaal
       61 rtvtdrheal rttlrlhdgr lyqdihptvp velpvtdlsa lseperdaar arivaeyagl
      121 dlpmdtaplw rarllrldqh twwllfaghh vildgtsllh lraeltelca aavagrapdl
      181 pelpiqyady aawerdrldg prwdelreyw realtglpav halttdrprp atltfdgadv
      241 rrtlpgdvta alpelsqqaa atpfmvqlaa yvallhrlsg sddvvvgmpv agrdraelep
      301 llgmfmnmlv lrvdvsgdpp frtlvrrvrr vvldawdhqd mpfqklvedl avrrdpgvpp
      361 lyqltfhhlp tgrgeafgga mddlsleiag delrleyrta lferaameaf adrylllfaa
      421 avaaprtrvs alpvmpdaeh tavvtgwnat aapvrrttla elfdaqarrt pdavalvdgd
      481 trmtyaelsd aagqvasrlv ahglgpesvv aiheprsprl iagllgihra gaaylpldpd
      541 hppqrlafml adagagvlla delpdgltvp gtvlpltapd rprtaagtaa gpgnaayviy
      601 tsgstgrpkg vvnehaaivn rldwmqdaft lgpddavlhk tpigfdvsvw evfwpllvga
      661 rlvlaapggh rdpaylreli ererittvhf vpsmldafls tadpggpgrc gslrrivcsg
      721 eelpadlarr avtaipsaal hnlygpteaa idvtawaatp ealtgvtrvp iggpirnvrt
      781 yvldeamrpv pagvagqlhl ggvqvargyl nrpgltaasf vpdpfgepgg rlyatgdlar
      841 wrtdgtlefl griddqvklr glrielgeia avlreqpgvg saavvvrgat paeqrlvayl
      901 tgeapdpaql raalkrrlpe ymvpsafvtl dalplsangk ldtaalpaps sgvapaqrrp
      961 pvtpveqtva atwrdvlgvp evgldddffe lgghsllair mlallreayg qvdvgvmdvf
     1021 ahptvqglaa lidapadgdr qrpllyeltr pvpgdqrvrs yvcvpygggl asiyqplada
     1081 lpaghtlfsv aipghdvgvr dtelpfdelv ercvaeieer vdgplvlygh cvggalltgi
     1141 arrlhergrp ieaiyaggvf ptarpdnmlg rlvdwadsrg adrryetflr sigaeladld
     1201 qaqvdrfvhh vrreaaeaqe rftewldgep vrvpapvisv vgthdvltey yeeryrewsf
     1261 lgestalvvl deaghyfvkq raealaevlt rthprlaepa aaprrlagdg walaatstdp
     1321 vtaetgvqpg vrrflaitas qlisstgsal tqwavpvwvy letgsmlwfg lsgviaylpa
     1381 lltlpvagav adrfdrrrvl laacatavta eallalllwt drlglaavyt lvcvlgaasv
     1441 fqritylaai pqvvpkrylg hangiaqlav glsslavpll aagllaaigl agvlvidivs
     1501 yvvaigvlaa vrfpdllgrr rkepflaeli ggarmawaep gframlgffs lynlclasll
     1561 lvppmvlafg tmgqvgtvaf aealgavlgg laiavwggpt rrrmpaliai afgvavslvl
     1621 sgvrpslllv algsfgvglg lglhngiyls iiqvkvpqrf hgrvlaiiqt ltwatlplgf
     1681 avlvplsgsl lepmfapgga lagsvgalig tgpgrglgfa fvvsglalav valgaygvrr
     1741 lrlfdtetpd apadatewlp hlrrvddl
//
LOCUS       WP_457608343            1449 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608343
VERSION     WP_457608343.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1449)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1449)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   3  (residues 1 to 1449)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   4  (residues 1 to 1449)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   5  (residues 1 to 1449)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1449
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1449
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=150519
     Region          6..1388
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1355..1426
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mnetvepiai vglslrvpga asaeefwrnl vvgaesltrf traellargv pveqlddpay
       61 vpvaavldgv drfdaelfgl sprdaeltdp qqrlflehah aaltdagcdp arydgeigvy
      121 aggnadlyqw lhvrrnpral adagelrvsl gnkpdylast vafrlglrgp amtvqtacss
      181 slvavhlaae alrsgecdta laggvcvelp hgvgyvadeg ytsadghcrp fdadadgtvy
      241 gsgvgvvvlk rlsdaladgd diralvigna vnndgsakas ftapsvtgqv evvtqalava
      301 gvaprsvgyv eahgtgtvlg dsielaalst aygrrtaerg wcgvgstkan ighlsaaggv
      361 igliktvlsm rhrlipptvn hdrphpdidi easpfyvvst ltkwepedqr plragvsslg
      421 lggtnahlvl qeapprvppe pdhgggellq vsaatpdala aacarlaerl tgapdvelrd
      481 vaytlregrp ayrhraavva vdraraaaal tdpkrraagd aatpprvgll lpgqgaqhpg
      541 mgahlaatep vfaaavdeca ailgwdanei ifdagpgadd rlagpavaqp alfaveyala
      601 alwrhwgvtp aamighsvge lvaatlagvf dlpdalrlaa argrlvqaap egrmlavqrg
      661 adeiapllpd gvavaisngp htcvvggape pvaaaevllr ergigctplr spyamhvpll
      721 aavrdefaal vaavprrtpd lpvfsaataa pftdeqitdp aywadqlcrp vrfgatvaal
      781 aatgaaddwl llecgpgrql aglarlslpa garsplrtlp apgerltgrq tayeaagrlw
      841 tagvpvrvpa sgtprrvplp gypyqraryw idpepvavhv epatderydd gvvevpvwrq
      901 lpdlapaeap gplllfaage rgtaladrlr ergadvtvvr pgpafavrpd gyrlrpagvt
      961 dhqrlldeca ddgraarivh awaldgdpag pdadavaaaq ehgylalltl lealpaadvt
     1021 ldvvtagtad vtgtdllrpe hatvagvvrs vplerpglrc hwvdadpadp gadaladell
     1081 gaeradaval rlggrrwtrg faaaparrrt gpalrdggry litgglgrig gafaaelarr
     1141 garlvlvgrt arpdlveale ragaqvrhvr advtdvdalr avragieddl ggldgivhaa
     1201 rlpdtglsag srpaeatael lpkvtgtlal ravfgdlpld fvllsssvta lagglgradd
     1261 taanaflday arsphgwrap vvsvawgawr eegvpdhdgl apdaavraac rilaegrtgs
     1321 vavgaytvea vagherrlaa ttaatastvt aadgdltatv ariwrdvlgv aevgphddff
     1381 rlggtslvaa qlvlrirqav garlsmrvlf daptvaamaa rieslraaps asapaeapip
     1441 rlrrpgrpg
//
LOCUS       WP_457608349             549 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl [acyl carrier protein] synthase domain-containing
            protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608349
VERSION     WP_457608349.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Heath,R.J. and Rock,C.O.
  TITLE     The Claisen condensation in biology
  JOURNAL   Nat Prod Rep 19 (5), 581-596 (2002)
   PUBMED   12430724
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10093619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..549
                     /product="beta-ketoacyl [acyl carrier protein] synthase
                     domain-containing protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0033818 -
                     beta-ketoacyl-acyl-carrier-protein synthase III activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55729
     Region          5..420
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(174,310,347)
                     /site_type="active"
                     /db_xref="CDD:238429"
ORIGIN      
        1 mseddriavv glacrvpgad dapalwrnll sgvdsvrrvp agegapggpd wvsafgrldd
       61 legfdadlfg ypaaaaalld pqhrlfleva whaledaaid pdrdpaqigv fagcapsryl
      121 hhhllgnpal apaagtlaed wddaltgsgc dylptrtafa lglsgpavav qtacstslva
      181 vcqagqslld yrcdvaiagg aavvstrqag yrlrpgglla tdgvcrpyda aatgqvfgng
      241 agavvlkrla daradgdhvy avlagwavnn dgadrpgftv pgvsgqaavm aealasvgwd
      301 aadvgylegh gtgtpvgdai evdalarvrr garaplllgs vkgnlgnlda aagvlslika
      361 vyavrtgqvp gtahftaahd didlaaagad vgaesrswtg erragvssfg lggtnahvlv
      421 epapapdaad agapgpvvlg lsagspaalr elarrlalrl adgdlavadv ahtlavgrrr
      481 layrdavaca dageavaglt alaagdpvdg deavrawrag adlpvppgrr vplpgypfrr
      541 trhwiearr
//
LOCUS       WP_457608361             254 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608361
VERSION     WP_457608361.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..254
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27203
     Region          15..250
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 msqvtasrwf gpagsstgda qvfvfpyagg vaaafapwrd laapelsvqv almpgrgarl
       61 heppvddlge lvdalatava erasgpfllf ghslgalvaf evtrelrrrg apaplallvg
      121 gaeapgtrlv rrrvhdldda glidalrdfg atpaalladr dlmelilpgv radfalsery
      181 ayrqgpplev pvhvllgdrd ehvdpdraag wsrecvtepq whvfpgghff ltdhlpeiid
      241 lmrhivasht pvae
//
LOCUS       WP_457608364             545 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608364
VERSION     WP_457608364.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..545
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58761
     Region          8..538
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msdsfvvcsn ltfswpddtp vfqnlsftlg ggrtglvapn gagkstllkl iagqyrpaag
       61 svtvdgvlgy lpqslplaad ltvaevleia pliaalhaie agdaderhft tigadwdiee
      121 rtraqldrlg lgdlafdrrl gtlsggqvvs lglaaqllkq pdvllldept nnldlgarhr
      181 lydvleqwhg clllvshdra lldrmdriae ldrgemrfhg gdftsyeaav raaqdvaekn
      241 vrsaeqdlkr ekrelqeare raarragnas rnlknaglar ivagglkrda qvaagkanem
      301 hsgrvddara rldeaeralr nektitvelp attvpagrtl ltaervrvrh gerslfagdg
      361 vdltirgper iallgdngag kstllrlidg dlepesgrit radgriayls qrldlldldr
      421 tvaenlaafa pqapdaqrmn llarflfrgp rahlpvgvls ggerlratla cvlgaepaph
      481 lllldeptnn ldlvsvgqle salhayrgal lvvshderfl aaidvgrwlr ladgrlvetg
      541 ppdaa
//
LOCUS       WP_457608374             296 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608374
VERSION     WP_457608374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..296
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=29879
     Region          41..294
                     /region_name="SEST_like"
                     /note="A family of secreted SGNH-hydrolases similar to
                     Streptomyces scabies esterase (SEST), a causal agent of
                     the potato scab disease, which hydrolyzes a specific ester
                     bond in suberin, a plant lipid. The tertiary fold of this
                     enzyme is substantially different...; cd01823"
                     /db_xref="CDD:238861"
     Site            order(48,90,129,275,278)
                     /site_type="active"
                     /db_xref="CDD:238861"
     Site            order(48,275,278)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238861"
     Site            order(48,90,129)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238861"
ORIGIN      
        1 mnrprlpllr tagrmtalva aaagmlltva apavaaapag ryvalgdsyt saplvptqvd
       61 lnclrsnrny pslvaasags ssfadvscsg attedilygg dgalgialpp qvnavtsata
      121 lvtvqiggnd igfsgiigdc aeasvssplg spckdrftag gtdqlraria atapkvtavl
      181 ravrqaapna rvvvlgypai lpdsgygcwp vvpiayqdvp ylrgvqkaln tmladtaaaa
      241 gasyadvytp sigrdackss gtrwveglvp qnsaapfhpn argeqgmata llahls
//
LOCUS       WP_457608380             407 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608380
VERSION     WP_457608380.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..407
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44790
     Region          13..117
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          84..>208
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mavktmtrtg tdirefrvdv peedladlra rlaatrwper qtvddqsqgv pletsqalar
       61 ywateydwrk vkarlndlpn fvteidgldi hfihvrsrha dalplivthg wpgsvieqlk
      121 ivgpltdpta hggsasdafh lvipsmpgyg fsgkpekpgw dpqhiarawt elmrrlgytr
      181 fvaqggdwga litdmlgvqa ppelagihtn mpcvvppdvd allqtgitgv nnpladlpsg
      241 lsaeeraace ridffwkhsa yalimttrpe tlmaladspv glatfmldhd aasldlicaa
      301 fagrpgglsr ddildnitly wltntgvssa rlyaqnalsf faakgvqvpa avsqfpdeil
      361 laprswaera ypnlihynml drgghfaawe qpelfaqemr aafrslr
//
LOCUS       WP_457608390             678 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608390
VERSION     WP_457608390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 678)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..678
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73103
     Region          4..668
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mthvdrdqwg vpqlwagdvd alarlqgrva aldrawqisv erwraegrla ahvgpaelaw
       61 drfarrvrld dtarrcyerl dpdtrrwvga yvdgvnsgla egaaaapefa atgtapepwr
      121 pwsplgvflv qhvlfstfpn klwhahvart lgpgaaglfa vegpassgsn awalpadpat
      181 grgpliagdp hrllelpgvy qqvrlacpef dvvglafpgv pgvphfghtg hvawavtnam
      241 adyqdlyrer lrrdgdrvlv rdadgwtpat rhveeievrg gapetvevie tprgpvidhd
      301 rvtgeaialr tpsrvegrlg feallpllra rrtgdvadal rhwvepvnsv laadtgggvr
      361 rlvaglvpvr dercrrepvp awepayrwrg dylplvdegv dgvavcandr rddvaahgtd
      421 fapphrarri ralladgtep atvhtddrlp agplyrlldr ldpgrldepa ralllrlrgw
      481 dramaagsae agayaawraa larrlrvhpg lraldvpcgf delfapwtdp aariglaldh
      541 laaaldlaep aaealaevaa gpapgewggr hllhpvhlgv apavtdavta mrrrvalagd
      601 tdcvlatssv pgvsdacwrg pvaryvwdlt draasrwivp fgasgrpgda hfadqltrwa
      661 agtlipvpag pltgdett
//
LOCUS       WP_457608393             518 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608393
VERSION     WP_457608393.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 518)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..518
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55085
     Region          35..502
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mssigsptga apadtaraaa tardhlfnag slgryrdvla rgvdrvarrv aeadrpftgv
       61 tpeelaplvg aidldrplgd tdaaldelhd vwlrdavyfh hprylahlnc pvvipallge
      121 avlsavnssl dtwdqsagat lmerrliewt agriglgaga dgvftsggtq snlqalllar
      181 eeayrtvvgg adgrpdrpqv lsrlriltsa aghfsvqkaa kllglaadav ltvptdadrr
      241 mrtdelarai dgchrdgqvv mavvatagtt dfgtvdplpe iadicaaagv wlhvdaaygc
      301 gllvsptrrh lldgieraas vtvdyhksff qpvsssallv rdgrtlrhat whadylnpar
      361 aveqgipnqv dksiqttrrf dacklwltlr imgpdaigal fdqvvdlaaq awrrldadpr
      421 fevaapsqls tvvfryrpag laadlvdean lharealaas gaalvagtrv dgahhlkltl
      481 lnpettaddv ahvldliadh aawyvrtata aelscpvg
//
LOCUS       WP_457608396             194 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608396
VERSION     WP_457608396.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..194
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20860
     Region          20..164
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mtaftrvdda lgeftlrpld pdadaallhr wvthpksafw lmqdadvaav aaeyrriagh
       61 phhdaylgsw rgtpaflaer ydpahvelag lydpepgdvg mhflcapadt pvhgftravi
      121 ttvmawlfad patrrvvvep dvrntavhal naavgftvvg pirkpekeal lsactrdqfr
      181 aatgaptgee gapa
//
LOCUS       WP_457608399             594 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608399
VERSION     WP_457608399.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..594
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65653
     Region          10..589
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnasasvdhl tpeawatanr llvrkalaef aherlitpep dgpgrwlvrs ddgaveyrfa
       61 aqrlaldhwe vdadsivrrr dgadlppdav dlcvelrgal gltdailpvy leeitstlag
      121 tayklakpav saaelaaagf qaietgmteg hpcfvanngr igfgvheyha yapeaaapvr
      181 liwlaahrdh ttftcaddld ydtlvraeld eqtragftat ltglgldpad ylfipvhpwq
      241 wwnklavtfa gevaarrlvc lgegpdeyla qqsirtffnv sdpakhyvkt alsvlnmgfm
      301 rglsaaymea tpaindwlag liegdpvlkr tglsiirera aigyrhrqye aatdryspyr
      361 kmlaalwres pvpglepgrr patmasllhl drdgrslaaa lidesglapa dwlrrylday
      421 lvpllhslya ydlafmphge nvilvlrdgv vervvfkdia eeivvmdpda dlpervrrvr
      481 aaipetekil siftdvfdcf lrhlsaalht rgvldqdefw rtvaacaady aatvphladr
      541 mrrhdlfape ftlsclnrlq lrnnqqmvdl sdpsaalqfa gtlvnplapy apra
//
LOCUS       WP_457608432             499 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA carboxylase biotin carboxylase subunit [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608432
VERSION     WP_457608432.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Chou,C.Y. and Tong,L.
  TITLE     Structural and biochemical studies on the regulation of biotin
            carboxylase by substrate inhibition and dimerization
  JOURNAL   J Biol Chem 286 (27), 24417-24425 (2011)
   PUBMED   21592965
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Mochalkin,I., Miller,J.R., Evdokimov,A., Lightle,S., Yan,C.,
            Stover,C.K. and Waldrop,G.L.
  TITLE     Structural evidence for substrate-induced synergism and half-sites
            reactivity in biotin carboxylase
  JOURNAL   Protein Sci 17 (10), 1706-1718 (2008)
   PUBMED   18725455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..499
                     /product="acetyl-CoA carboxylase biotin carboxylase
                     subunit"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52933
     Region          1..466
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
ORIGIN      
        1 mfdkvlianr geialrvlra crelgvrtvv vhssadadsl pvrladeavr igpaasrrsy
       61 lnaaaiveaa rqtgaqavhp gygflsedad faeicaengl vfvgpppqvm aaladkstar
      121 almsnaglpl ppgsvrtlpt vgeaqevaae vgypvivkaa aggggrgmtv vrsaaelpra
      181 yartraaaqv afgddrvyve ryladarhve vqvlcdghgn gvhlgtrdcs vqrrhqklie
      241 eapapalrqa tldtvaeval rgalsvgftg agtveflvde aerchflein criqvehpvt
      301 emvsgidlvq eqlhvaygtp lrlrqsdvrl sgvaiecrvn vedpdrdfap apgrldrfrp
      361 pggpftrvdt hghvgylvsp hydsllakva vwapdrdaal drldralaef dvagpgvrtt
      421 ipfarrvlrd pafraarhtt alverllapp tddtppagdg ppaeaaravv pdprgaaepg
      481 grtpvsavpa agpttwrnr
//
LOCUS       WP_457608437             465 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608437
VERSION     WP_457608437.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..465
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48677
     Region          70..464
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtahpvaedp asttvnwvdd ilftgrdtdv clrlpepvdk gtlrrlvgea qdrlagaglr
       61 aggaaalrlp pslayvayll atwrtgaqav lldhrltdhe vdqalrrlsp qvvvaptrtg
      121 ggalrifvdv tagvsaysdr pagsphaviq lssgstgpsk vigrtaadlv aevhrytrid
      181 gvalpgerii llpsmvhvlg lvggllyglh agvelcpper lsgdailaav aaqdtpatvl
      241 gvpfhiglla sttpagplpq lkrmttggel vsaavanaft drygvplgnm ygmtevgvig
      301 tdlygrhrpa iapapgievr eragelwvsc pdnpyvglad ptrwadgwlh trdagvvdpd
      361 tglvtikgrl dsqvsvgglk vdlteveatv aglpgvvaav vvwddgitay vqtdgslted
      421 tldkliaerl agfkrprtlr lldqmprttt gklvrsvpal rdaas
//
LOCUS       WP_457608446             420 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608446
VERSION     WP_457608446.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 420)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..420
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=42167
     Region          4..406
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mtavitgmgl ftpagrgvad tfdalltgrs glrrppeghp aagslevagv lpdidprsva
       61 sgpetkvldr vvllalitaa ealadagiev grdvdperia vivggvggms tlegqvlara
      121 argraavspy lltgilpnmp sariaiahgi rgysssvgta casgaqavad gvrliragea
      181 dvvvcgasea plfgtfadtf gnaralargw depteasrpf dkrrngfvla egaallvler
      241 aghadgrgvr gyaevagfga ntdayhptap rpdgvgaaac mrralaaggv epadvgyvna
      301 hgtgtklgdv aetialaevf gtggvpvsst kaltghllga sgvleaaata laldsgllpp
      361 tyhlddpdpe ceadhvravp rptraghalt nsfgfggqnv slllrrlsgp arraatpaag
//
LOCUS       WP_457608440             376 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608440
VERSION     WP_457608440.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 376)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..376
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=37913
     Region          7..374
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 maeretvrit gtyalsalgr gadallagvl tgtpaftpvr rfdttgrrvt vaatvpdvgt
       61 lageladaid taalaagldr agraesalfl athggpyslp vprgweeptv palaghlaar
      121 cglggrtriy ttacvsassa vadaaalirr gdlervvvaa gylvepdqya lfdagralaa
      181 dgavrpfsag rkglllgdgv aavvlesaga aarrgaetla vvagwgragd ayhpcqphpd
      241 glglaravea alrrgglppe aigyvnanat gtpfsdasea aaltrvfged agrlpvsstk
      301 svhghaleas gllellvtvl alrhgklpvt agwlgpdpqc pldvirdapr partghaltl
      361 naafggadta llvsts
//
LOCUS       WP_457608452             323 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608452
VERSION     WP_457608452.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..323
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          7..313
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtgsdplrly rtvrlirrfe eraielvrag eivggihpyl gqegiaagvc aalgaedlvt
       61 gthrghghvl akgadparml aelcgrvtgl nrgrggsmha adfgvgvlga naivgaagai
      121 ltgavwerrr rgagivgatf fgdgavnegm lleafnlaal wripvlfvce nngyattmpv
      181 dgavagtiag raaafgmpaa vvdgqdpeav revtaaavar mragggpelv eartyrfdah
      241 htfehqvrld yrppeevaeg rsrdpvdiag arldpavrae vdaaveaeld aavdyalagp
      301 hpdpataldh lyasgltart ggg
//
LOCUS       WP_457608455             321 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608455
VERSION     WP_457608455.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..321
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33766
     Region          1..315
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mprlsyrral tralademar desvvvlged irvaaanvtt gllkkfgper vrdtplseqa
       61 ftsfatgaal agarpvvefq ipsllflvfe qivnhahkfp lmtggqcavp vtyvvpgsgs
      121 rtgwagqhsd hpyalfahvg vttvvpatpa daygllvsai rcddpvvvfa pagaldlrad
      181 vtdpapvplg rgivhragtd vtvvavghlv hdalavaeel agqasvevfd prtlypfdwd
      241 glvesvsrtg rlvvvddgnr scgiageiia tvaervrlaa pprrvtrpdg avlpfapald
      301 ravqpgrdql taaiqltlkd g
//
LOCUS       WP_457608460             520 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608460
VERSION     WP_457608460.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55509
     Region          18..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtdrpnyvhe alelfagfgd realvgggrr ltypqvaaev rglaaalhhh gvrpgaavlv
       61 mlgntvegpl lqlalhllgc rsmwvapvts rrevdefval sapeafvhdp rdaqaveiaa
      121 glsgvpvlcl gpggtgpdlt araagpvaep pagvpapesf lqtsgttgtp klvhhresfy
      181 rqvlalaadf rgagfpllrh lshspmwlas gqittlfnlf tggvlflreq wdpaafiatv
      241 daerltstfv tppmlyevld hpdlpgadfs amfmfnvgag paaparlrqa iarfgpclri
      301 vyglseavvi calpgltedp ehperlrscg rpygdvtvqi rdadgrvlpv gedgevwvrt
      361 rlsfagyhgr peltaetlvd gwvrtrdigh ldadgylylv drlqdriltr qrswpiysrp
      421 iedvlaghpe vraaavigvp dpvagelpha yvvaapgasv tgdelialvv relsetwapg
      481 avefvdalpl nrsakvdkra lraryaaahp agadpigspa
//
LOCUS       WP_457608465             367 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-hydroxy acid oxidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608465
VERSION     WP_457608465.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 367)
  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 12014085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..367
                     /product="alpha-hydroxy acid oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37367
     Region          21..360
                     /region_name="FMN_dh"
                     /note="FMN-dependent dehydrogenase; pfam01070"
                     /db_xref="CDD:426029"
     Site            order(32,114,136,164,171,239,263,266,318)
                     /site_type="active"
                     /db_xref="CDD:239203"
     Site            order(32,136,171,263,266)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239203"
     Site            order(114,136,164,239,263,266,318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239203"
     Site            order(136,171,263)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:239203"
ORIGIN      
        1 madpadgfvp paslaefaal aravlpadvw dfvdggsgte talaanraal drvavlprml
       61 agvddpstea vlpggraalp vavapmayqr llhpdgepal aaaartagvp yvastlsstp
      121 ieeiaatgat vwfqlywlrd ralvadlldr aeaagcaavm vtvdvpvlgr rlrdarngfa
      181 lpphvtaanl pggrddlahq gtpgvsavav htgavfapal swadlewlre rtrvpllvkg
      241 ildprdavra adagvdavvv snhggrqlda apasaavlpe vveavdgrca vlldsgvrgg
      301 vdvlralalg adgvllgrpl lwalavggrp gaeaalalla aelrdalils gcpdpasarr
      361 lrtrigg
//
LOCUS       WP_457608463             322 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608463
VERSION     WP_457608463.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..322
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33742
     Region          79..284
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtldpqvvaw raaraaagtv plytqtlaea raadlaaira gsgavepvte vrdttvpgpa
       61 gplpvrihrp dgdgplptlv yffgggwtlg svdtadgicr rlvnlaavqt vtvgyrlape
      121 hpfpaavedc haalrhlaah aaefrvdadr lavggdsagg nlaaavtlla radggprlaa
      181 qllvypntdq rpghrpgdde dpmlfnrhsv gwyrghyltd pgdaahplas pllaedlsal
      241 ppafvvtagh dplreeglry aerlresgvp tetddypgmv hgffampgvf dagrqaqera
      301 aaflrrvlgl dpahaatgad hg
//
LOCUS       WP_457608480             677 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608480
VERSION     WP_457608480.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..677
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..677
                     /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=72180
     Region          269..439
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mhlsappsgr rillaaavat atalattgpv taapdtsapa sdrqeqyaaa aaeygvpqnv
       61 llgvsylesr wdthtgqpst sggygpmhlt daahilampg sahvdededp rgddsrplkl
      121 dpataaaper etplppaslq tldaaaaltg ldagtlrtdp aanirggaal lasyqkalgg
      181 pvgagtdpaa wygavarysg adtsdaaaaf adevydqlgq gasrttddgq rvtlaataat
      241 pdrsrlarlg lrnaerpdgl ecpvrlacew ipapyeqlsd dpgdygnhdl adrpkqqkie
      301 yivihdtegy fgpsvdlvkr adylgwhytl rsvdgyiaqh iktkdvgwha gnwyvnaksi
      361 glehegfagq gtwyteamyr tsaklvrhla lklgipmdrq hiighdnvpg itaanvggmh
      421 wdpgpywdws hyfdlmkapf rstgtprtgl vtidpdfatn rpaftgcnqq ppgvptprpp
      481 aepcpsrgss avilrtapsp daplvndlgl rpdgtpdtmy isdhgarasa gqtyalagrq
      541 gdwtaiwylg qkawflnpas aptakwatgf vvtprpgkat ipvygraype qaaypdtipy
      601 qtisplqytf aagqryavgg vlpgeyyrav sfdgsapgdr tvvrgknryv qvqfghrimf
      661 vnlddvlvlp spvgtpr
//
LOCUS       WP_457608477             225 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608477
VERSION     WP_457608477.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..225
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23693
     Region          14..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mdgllltdel vllaydddga nrlgsphlgy glagavllel alagrvevtd krltvtdpal
       61 tgvplldeal atvgsgrprk pkdwigklak glpdrvlggl vdagvlrres drvllvfprt
      121 rypsptgaep avetaarqrm ttalttdgpv dartaalltl travgldrki frelpkervk
      181 arieeiaagd wasaatkkai eemqaalmia mtagtsaaim tttts
//
LOCUS       WP_457608482             343 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608482
VERSION     WP_457608482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..343
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36249
     Region          38..>205
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          <182..343
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 malhaprpss srsvdrstav prtrwsrftt alaalvgtav vlsggataah aepsvaeiea
       61 qidrdwnkle pvieqvnavr eqlaarrkqa dalgrqiapl qarvdaalgq vgglaadayk
      121 gdnlstvnal lgsrspgdlv nglelldrfa hrqheqvrsv aalrdelaak kkpldemvag
      181 larteaqlaa kkkqidaeia kleklrltvy gkggggplrp apcpsgypgg pagaavkfac
      241 aqigkiyvwg aagpdhfdcs gltmaawakg gvslphsarq qhgvtkrisr aelragdlvf
      301 yygdlhhvam yvgdgwvvha sqsgkpitmk rvddgdinsy grv
//
LOCUS       WP_457608491             203 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608491
VERSION     WP_457608491.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..203
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21661
     Region          2..190
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mgklivtefl tldgvaqapg epdedreggf nhggwqmpll ddksgavmfq qassmdalll
       61 grktydifag fwpkapadip ftgllngvsk yvasrtltep lawansslvs gdlaervtem
      121 karhdevhvi gsldlvqsll rpglvdrlnl wvypvvlgtg krlfgegtvp salrltesvt
      181 hahgtlqlty epagaptygd aaa
//
LOCUS       WP_457608494             188 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608494
VERSION     WP_457608494.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 188)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20726
     Region          48..180
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mrdeiralve elppgdqlev rhreaaltwl agtedifrra kprtpsphlv ayfllrdpad
       61 gavllvdhrl agmwlpsggh vepgehpadt vrrelreelg vsavfappfg ecpafltvte
      121 tvgppehrht dvslwyvlsa drgrrftpdp vefagirwwt paevneapag tvephlgrml
      181 aklaattp
//
LOCUS       WP_457608503             135 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608503
VERSION     WP_457608503.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..135
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14966
     Region          7..124
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mskaeydafl agcpsrqlld ritdkwvtlv laalrsdgsh rfgadcagdp rprryselfr
       61 tlpgvsqkml tqtlralerd glvtrtvept vpvtvtyelt plglsllkti qglklwaeth
      121 mddvfanraa ydsrv
//
LOCUS       WP_457608505             178 aa            linear   BCT 27-JAN-2026
DEFINITION  SixA phosphatase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608505
VERSION     WP_457608505.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..178
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18718
     Region          11..175
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtdgrngqrt lvllrhakae qsadgpdaer sltarghada atagawlarq gllpdvvlcs
       61 parrtrqtwh dvamgmtgsp peggpagsrp avryeatayd ahpdqllell rtveptagtv
      121 llvahnpgvs llsalldpqr adpdglrttd lvvhrpttrw aelapggapl tarhtara
//
LOCUS       WP_457608510             287 aa            linear   BCT 27-JAN-2026
DEFINITION  5-oxoprolinase subunit C family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608510
VERSION     WP_457608510.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..287
                     /product="5-oxoprolinase subunit C family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29388
     Region          1..283
                     /region_name="PxpC"
                     /note="5-oxoprolinase subunit C/Allophanate hydrolase
                     subunit 2 [Amino acid transport and metabolism]; COG1984"
                     /db_xref="CDD:441587"
ORIGIN      
        1 mievlragal ttvqdqgrpg wahlgvprsg aldpaalrla nrlagndeda agleitmtgc
       61 alrftravav altgapadvv vewrtgdlrp gdvgrplslp agavlrvapa ragvrtwlav
      121 sggiavepvl gsratdtlsg lgppplrdgd rlplgtpagp papvdlavtr pvpdelrlsv
      181 rpgprqdwft pealdllcra aytvspdsnr vgarlagaal travpgelps eglvlgavqv
      241 ppdgrplvfl adhpttggyp vigvvddvta laqarpgttv tfhgpqr
//
LOCUS       WP_457608512             249 aa            linear   BCT 27-JAN-2026
DEFINITION  LamB/YcsF family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608512
VERSION     WP_457608512.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Oke,M., Oni,O., Bello,R., Samuel-Omoyajowo,K. and Senbadejo,T.
  TITLE     Structure-function relationships of the 5-oxoprolinase subunit A:
            Guiding biological sciences students down the path less traveled
  JOURNAL   Biochem Mol Biol Educ 47 (6), 620-631 (2019)
   PUBMED   31520514
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..249
                     /product="LamB/YcsF family protein"
                     /EC_number="3.5.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0017168 - 5-oxoprolinase
                     (ATP-hydrolyzing) activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26086
     Region          1..248
                     /region_name="PxpA"
                     /note="5-oxoprolinase subunit A [Amino acid transport and
                     metabolism]; COG1540"
                     /db_xref="CDD:441149"
ORIGIN      
        1 mdlnadlgeg fgswrlgddh alldlissan vacgfhagda vtmhrvcaga aergvavgaq
       61 vgyrdlagfg rrhiaydfae lrdetiyqlg aldafcrlyr trvrylkphg alyhaaarde
      121 gqaaalvaai sgydhelpvl cqpgtvlaql aagaglrvva egfadrnylp ngtlvprssp
      181 dalvtdpeqv avravrmave rtlvavdgtv ipapvesicl hgdtpgavrc aelvraalid
      241 agvtltpfa
//
LOCUS       WP_457608536             350 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608536
VERSION     WP_457608536.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..350
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=36751
     Region          97..341
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 miedelraaf arleestppv gpvraavdra viirrrrrrr vrlagtalav aaialvgfta
       61 maprppapta apapatpape tggalnllll gvdqpvgsrr adsvllvhlp adrsrlylvs
      121 fprdllvpvp pqggteklna tfsraagsgt dltagyratr eavarltgvr vdagavltyp
      181 gareltdavg gvpvclpapv rsvhterrfp agcqrldgpa avdllrqryg lrdggldrdr
      241 naaryaagll rqlreqgtat dpaqlgrlll rigpavtidt gdlslpalta asgraavaep
      301 aalafpvrde wngrgyepdp elapgfldal radrlaqwaa ahpgqvtalr
//
LOCUS       WP_457608514             610 aa            linear   BCT 27-JAN-2026
DEFINITION  NHL domain-containing thioredoxin family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608514
VERSION     WP_457608514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Kumari,P., Aeschimann,F., Gaidatzis,D., Keusch,J.J., Ghosh,P.,
            Neagu,A., Pachulska-Wieczorek,K., Bujnicki,J.M., Gut,H.,
            Grosshans,H. and Ciosk,R.
  TITLE     Evolutionary plasticity of the NHL domain underlies distinct
            solutions to RNA recognition
  JOURNAL   Nat Commun 9 (1), 1549 (2018)
   PUBMED   29674686
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10221804
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..610
                     /product="NHL domain-containing thioredoxin family
                     protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=64472
     Region          8..132
                     /region_name="Thioredoxin_like"
                     /note="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold; cl00388"
                     /db_xref="CDD:469754"
     Region          209..535
                     /region_name="NHL-2_like"
                     /note="NHL repeat domain of NHL repeat-containing protein
                     2 and similar proteins; cd14951"
                     /db_xref="CDD:271321"
     Region          229..278
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          296..334
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          350..391
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          403..443
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          446..484
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          494..535
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
ORIGIN      
        1 msarvrapel rgrawlntgg kavtladlrg kivlldfwtf ccinclhvld elrpledkyg
       61 dvlvvigvhs pkfehekdpa alaaaveryg vhhpvlddae mdmwqqyaak awptlavvdp
      121 egyvvatmag eghaeglarl ideliaghea kgtlhrgegp yvppaepdtv lrfpgkalpl
      181 dggnllvsds arhslvelaa dgetvvrrig agsrgrtdgp asaatfaepq glcllpphva
      241 evagydvvva dtvnhllrgv rlssgevvtv agtgrqwrst vddhahdara vdlsspwdva
      301 wyddrvivam agihqlwwfd pmkrtagmya gttvealrdg plpdvwmaqp sglsvsadga
      361 rlwvadsets airwvsggem htavgqglfd fghvdgpadq allqhplgvc alpdgsvlia
      421 dtyngavrrf dpetgqvgtv adglaepsdl vltgegdvlv vesaahrltr lapgaltsag
      481 antvdgprhr lerkptdvaa geltldvift papgqkldet ygpstrlvvs asppellveg
      541 agtttdlsrr lvvsgdvaqg vlqvtaqaat cdadvehaac hltrqdwgvp vrvvtggatr
      601 vplvlrgmda
//
LOCUS       WP_457608539             403 aa            linear   BCT 27-JAN-2026
DEFINITION  LOG family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608539
VERSION     WP_457608539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..403
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42755
     Region          171..403
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mptpppadvi ephaphvnei etrtafeqrl aggtlagltv qglrldldpv pdlrdvdvtg
       61 tlfvgcrfag revgadlvrr ganvvppfsg lpyptqpshl ytadelaagf aeggfaemyd
      121 trvyahfrah ggalpdvrea lgqrlhdhgv dnaladatrs wlaahgpqsv vgvmgghavp
      181 rgsvayrmaa vlgwelarad rlvvtgggpg vmeaanlgaf laawpaeels aaidvlavap
      241 dftdhdryta aavavrkrya dgtslpsprp sapgtewars gglaiptwly ghepanlfag
      301 riakyfsnai redtilrlar ggivfapgka gtvqevfqaa tktfygtdga sgayvfldrt
      361 ywttelpves llrplfaasp fgdlshtihl tddvheavrv lvq
//
LOCUS       WP_457608544             147 aa            linear   BCT 27-JAN-2026
DEFINITION  copper resistance CopC family protein, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608544
VERSION     WP_457608544.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   van Sorge,N.M., Bonsor,D.A., Deng,L., Lindahl,E., Schmitt,V.,
            Lyndin,M., Schmidt,A., Nilsson,O.R., Brizuela,J., Boero,E.,
            Sundberg,E.J., van Strijp,J.A.G., Doran,K.S., Singer,B.B.,
            Lindahl,G. and McCarthy,A.J.
  TITLE     Bacterial protein domains with a novel Ig-like fold target human
            CEACAM receptors
  JOURNAL   EMBO J 40 (7), e106103 (2021)
   PUBMED   33522633
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Lawton,T.J., Kenney,G.E., Hurley,J.D. and Rosenzweig,A.C.
  TITLE     The CopC Family: Structural and Bioinformatic Insights into a
            Diverse Group of Periplasmic Copper Binding Proteins
  JOURNAL   Biochemistry 55 (15), 2278-2290 (2016)
   PUBMED   27010565
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Cooksey,D.A.
  TITLE     Molecular mechanisms of copper resistance and accumulation in
            bacteria
  JOURNAL   FEMS Microbiol Rev 14 (4), 381-386 (1994)
   PUBMED   7917425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>147
                     /product="copper resistance CopC family protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0046688 - response to copper ion [Evidence
                     IEA]"
     Region          <28..123
                     /region_name="CopC"
                     /note="Copper-binding protein CopC (methionine-rich)
                     [Inorganic ion transport and metabolism]; COG2372"
                     /db_xref="CDD:441939"
ORIGIN      
        1 mrtrsvtall aaaltallla patpaaahns lqeatparda rltaaptqvt lrfmqglnps
       61 yttitvsdag qrqvptsapa vngatgtvti deplgngtyt vayrvvsrdg hpvqgsyrft
      121 vadpaapaps aaasssapps saapaaa
//
LOCUS       WP_457608546             410 aa            linear   BCT 27-JAN-2026
DEFINITION  Dyp-type peroxidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608546
VERSION     WP_457608546.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Sugano,Y. and Yoshida,T.
  TITLE     DyP-Type Peroxidases: Recent Advances and Perspectives
  JOURNAL   Int J Mol Sci 22 (11) (2021)
   PUBMED   34074047
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Colpa,D.I., Fraaije,M.W. and van Bloois,E.
  TITLE     DyP-type peroxidases: a promising and versatile class of enzymes
  JOURNAL   J Ind Microbiol Biotechnol 41 (1), 1-7 (2014)
   PUBMED   24212472
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Sugano,Y.
  TITLE     DyP-type peroxidases comprise a novel heme peroxidase family
  JOURNAL   Cell Mol Life Sci 66 (8), 1387-1403 (2009)
   PUBMED   19099183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..410
                     /product="Dyp-type peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43363
     Region          67..397
                     /region_name="EfeB"
                     /note="Periplasmic deferrochelatase/peroxidase EfeB
                     [Inorganic ion transport and metabolism]; COG2837"
                     /db_xref="CDD:442085"
ORIGIN      
        1 msdspatarr vsrrglltgg amaaggalag agaltavrsg gpgvrpgnav pvaqvgdave
       61 pfhgarqsgv ttdpqahaaf vaftlrpgtd raalgrmlrl lsddaarltq grpaladtep
      121 elsvlparlt vtfgfgpgly aaaglddrrp asvaelpafg idrlqprwsg gdlllqicad
      181 dpltvahaqr vlvkdsrpfa vvrwvqqgfr raagaepgrt qrnlfgqldg tanpkpgtpa
      241 dtavwvtdgp dwlrdsttlv vrrismnlet wdllgradre lavgrrldtg apltgraehd
      301 epdfaalgpd gltvipdfsh ltrahvtddr qkilrrpyny dgvptpegda dsglvfasyq
      361 adiaaqflpi qrrlaerdll newttpigsa vfavppgcpe ggwigrqllg
//
LOCUS       WP_457608559             332 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608559
VERSION     WP_457608559.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..332
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36703
     Region          25..322
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtpasqtrtp avgaqappag lrpgaraasr raetrrkwye iiglttpaiv iyvmfvlvpm
       61 gfafyyslfr wrgvgpptey vgfrnytlaf qdpifldalr nnaiivfgsl liqgpvalgi
      121 alllnrrfrg rsafrllvfv pyvlaevtvg imwklilten gtldallqsi glgglvqawl
      181 adldvviwtl lfvltwkyvg faiilllagl snvpqelnea aeidgaswwq iqrhvtlpll
      241 gptiriwmfl smigslqvfd mvwvtsvpav rslgasatma tymvdngffa rlwgygnava
      301 vilfaisfva allfqrfllr rdiegaitrk gk
//
LOCUS       WP_457608572             408 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608572
VERSION     WP_457608572.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 408)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..408
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44751
     Region          20..406
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,87..88,95,99,106,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,81,83,86,88..89,171..172,184,238..239,242..243,
                     247,290,293..295,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtddvmpase lytdgfaadp ypalarlrad rpvcpvgspr fdswlitrfd dartaltdpr
       61 lskdlygpgq hylkifgpns eglnrnmlns dppehtrlrr vvsqafaprr iealrprias
      121 tveqlidkma phgeadlmhe faiplpmtvi cellgvppad hdrvldwtqv irtsgstsrp
      181 peqeraavqe aqlrlhhyla glvrakrddp addiigalik avdrdgtlae aelvtttfll
      241 lfaghqttad flgnavlall thpeqmellr dsprllpaai eellrfdgpl pvaspritte
      301 dvdyqgvrip rgaivgvain aanhdpahfa dpdrldlrrv rgphlgfghg vhyclgvsla
      361 rmeaelalga llrrlpglrl gvplaevrrl paaspfrgll elpvtfta
//
LOCUS       WP_457608580             345 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608580
VERSION     WP_457608580.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  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 345)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..345
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36051
     Region          15..308
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtvvhvvlpg diddpadpsg gnaydrrvcr glsargwtvr ehqvpggwph pgpreradla
       61 gllgglpdgv pvlldglvas tvpdvlapha arlrlvilvh lpiegetear slaaatavva
      121 tsawtrdrll dryrlrperv tvappgvdaa pvadgtaggg rllcvaavtp vkghdvlaaa
      181 ltevddldwt cdwvgppdrd rafadrlrgr liatglagrv rltgprtgpg laatyaaadl
      241 lvqpsrrety gmvvtealar gvpvlasdtg glpdtlghap ggdrpgllvp pgdpgataaa
      301 lrrwltdpgl rdrlrraarq rrhtltgwpv tvdrlatalk eataa
//
LOCUS       WP_457608591             301 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608591
VERSION     WP_457608591.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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..301
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..301
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30344
     Region          26..295
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mrpllglavl aalvasvgtg pflaglrlid apalaaalgi gvittvccaw rwslvagglg
       61 vrlpmraava hcyravflns tlpggvlgdv hravrhgrda gdvargvrav vwertagqvv
      121 qvviavalla afpspvrryl palaavlavv alalvlaara vprsgasrla rvartavadv
      181 rsgvlgrrtw agvvvastvv faghlatfvv aartagadap lshllpltll allamavpln
      241 vggfgpregv aawafasagl taaqgvatgt vygalvlvas lpgaavllar rlprrepgnc
      301 r
//
LOCUS       WP_457608593             439 aa            linear   BCT 27-JAN-2026
DEFINITION  MSCRAMM family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608593
VERSION     WP_457608593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Foster,T.J.
  TITLE     The MSCRAMM Family of Cell-Wall-Anchored Surface Proteins of
            Gram-Positive Cocci
  JOURNAL   Trends Microbiol 27 (11), 927-941 (2019)
   PUBMED   31375310
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Foster,T.J.
  TITLE     Surface Proteins of Staphylococcus aureus
  JOURNAL   Microbiol Spectr 7 (4) (2019)
   PUBMED   31267926
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Deivanayagam,C.C., Wann,E.R., Chen,W., Carson,M., Rajashankar,K.R.,
            Hook,M. and Narayana,S.V.
  TITLE     A novel variant of the immunoglobulin fold in surface adhesins of
            Staphylococcus aureus: crystal structure of the fibrinogen-binding
            MSCRAMM, clumping factor A
  JOURNAL   EMBO J 21 (24), 6660-6672 (2002)
   PUBMED   12485987
REFERENCE   4  (residues 1 to 439)
  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   5  (residues 1 to 439)
  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
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Patti,J.M., Allen,B.L., McGavin,M.J. and Hook,M.
  TITLE     MSCRAMM-mediated adherence of microorganisms to host tissues
  JOURNAL   Annu Rev Microbiol 48, 585-617 (1994)
   PUBMED   7826020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471690
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..439
                     /product="MSCRAMM family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=45856
     Region          10..>387
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mevpagdyki aitpvygdgq ddevlrqwvp grsswaqagt vrvsagdtte vserllapsg
       61 stlrardavt gaevdglcvf ldprrnpcgd trvtvpplip gpqevwvytr ddthlpryat
      121 vnvladgsgt avvvltpaan vvsrvvdaat gapvagacvt papagtgelp dnpgrycsda
      181 sgnvrvglva agswnlfarp aggsaygaqw vgstggtgda kqarvvtlra gqtvtvppir
      241 ldragvvtgt vtsaatgrpa tsgtvtlape sgffpdwgve ldaqgryrid wlgpyawpll
      301 fttadnatqw sggfalrgka vpvtvragat tvynlavrrg vlvtgrlvdp egrpvvaelt
      361 vrnartrevi gwtldrdgey alrvlgpqpv tvawlwtppy vnyagwydga trpadatevt
      421 lpgtgtlrld vavdrfpag
//
LOCUS       WP_457608598             271 aa            linear   BCT 27-JAN-2026
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608598
VERSION     WP_457608598.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..271
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28270
     Region          60..214
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mvsalrtdpf agailqvgvl aalagtvgls aygwlagllf gvvtvaalgy glrrsgadrl
       61 gpadwvtltr atlaggvaal tvdsfrepiv vpvlvalsav alsldwvdgq varrtgtvsa
      121 lgarfdmevd sflvlvlcgy vadqvgawvl vigamryvfv aagwvlpwmr gslpprywrk
      181 vvaatqgial avvaagvlpr llavavllga lamlvesfgr dvawlwrhrv rpvpralpaa
      241 pvspapaghh sgwapdvria rqpaevggrh r
//
LOCUS       WP_457608626             281 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608626
VERSION     WP_457608626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..281
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29417
     Region          19..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnessaaapd rlldlfhgar ltptqrriah clvrhagaaa ylsaaevael agvsqpsvtr
       61 famalghdgy palrrrlrel tvtgsaepaa gnalqravha erdnldrlaa qladagrvae
      121 vgkllaasrp lpvlglraaa plaayfayfa akvhpdvrvl ddggsmlvdr ldqaaaagat
      181 amlafvlpry pretldalre ardagltvva itdspvspat ehaevvlpaa vgadlvfdlh
      241 tapmtlamvv lqaicdaapa etqnrleafe ssaarrqlfl g
//
LOCUS       WP_457608634             253 aa            linear   BCT 27-JAN-2026
DEFINITION  YveK family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608634
VERSION     WP_457608634.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Mijakovic,I. and Deutscher,J.
  TITLE     Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year
            retrospective
  JOURNAL   Front Microbiol 6, 18 (2015)
   PUBMED   25667587
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Elsholz,A.K., Wacker,S.A. and Losick,R.
  TITLE     Self-regulation of exopolysaccharide production in Bacillus
            subtilis by a tyrosine kinase
  JOURNAL   Genes Dev 28 (15), 1710-1720 (2014)
   PUBMED   25085422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..253
                     /product="YveK family protein"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0061097 - regulation of protein tyrosine
                     kinase activity [Evidence IEA]"
                     /calculated_mol_wt=26482
     Region          1..>126
                     /region_name="YveK"
                     /note="Capsular polysaccharide biosynthesis protein YveK
                     [Cell wall/membrane/envelope biogenesis]; COG3944"
                     /db_xref="CDD:443144"
ORIGIN      
        1 mdlahfrdti grrwpivlal tllcgaftgi laerrppvyr aetqmlvtfa aetsaapqpr
       61 ppadeagrlm qrrvktyatm mdtprltrpv idslglpyst ddlagrvvas stvdslaidv
      121 avtdrsagta aaiaaalaae lqriaerdlp paglglkahv avvraaappp rpepvrwqwy
      181 alggalggla lgagialvlg yrragtpvsa dvralwattv rrrpadavae pagvpgqsdg
      241 rvssasvker qas
//
LOCUS       WP_457608638             484 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608638
VERSION     WP_457608638.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..484
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53430
     Region          76..483
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mprlpafehp sappsgvamn tpmdsgmdtt tvlpyagsra strtrwlraw mvtapidvaa
       61 lltpllltqt ywrgtlfnaa ltvglfaagg lyrprrhisi ldelpslggr llasgavgai
      121 iaalrhdsvp yvsgfmrgva lsaglvivgr alnsrlilla rkrrwvehna ivigggpigg
      181 elarllrryp qyglrfvgav dtpsrpriga lpligtiddl eklaemlece vlviadpdcs
      241 eadlmesllr passrcdlwa vprlwgsrsq ggypdhigai pivkigdttl tgprwrlkra
      301 sdvvfavtal lvlspllllc aaatfldggr gvffrqerig rygkpfhvik frsmrpvdey
      361 esqttwsiah dervgpigrf mrrtsldelp qlwnilrgem svvgprperp yfvekfsmey
      421 pryamrhrvp vgltglaqvs glrgdtpisd rarfdnyyve nwslwldiki vlrtvtevfr
      481 gggr
//
LOCUS       WP_457608647             150 aa            linear   BCT 27-JAN-2026
DEFINITION  OsmC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608647
VERSION     WP_457608647.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..150
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16068
     Region          14..138
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 msddtfrsve iertsvgryv arnarggels mgtgedatft pvelllaalg gctavdvdhv
       61 tsrraeptrf avtvsgdkir dpetgnrmen ltvtfavtfp dgadgdrare mlprslrqsh
      121 dwlctvsrtv elgtpvsivd andpgsadpr
//
LOCUS       WP_457608651             271 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608651
VERSION     WP_457608651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..271
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29662
     Region          21..261
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mtalgagrar prglgvrvae nvlfavglpv ltvalwavws trstnrflvg pgtlldafrq
       61 twigpafvdd vlpslyrlli glfasillgv vagvvigrfr plreilepll effraipppv
      121 lipvamlllg itdtmkvvvi tsgaiwpill ntiegvratd svmietassf risrwdrlwr
      181 lilpaaspri mtgvrqalsv alilmvisem fassaglgyr iayfqrnyli aemwsgilll
      241 gligvalavv fgvverrvlr wyhgmkevtr a
//
LOCUS       WP_457608653             270 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608653
VERSION     WP_457608653.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29536
     Region          1..263
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mpdgspllrv ehlrkvytsg rgeveaigdi nftmdpgell cvvgpsgcgk ttllkclagl
       61 lrptsglvem egspvtgpsp amavvfqeyg rslypwltvr gnvelplrhk klsraerart
      121 vadaldavgl sqsarshpwq lsggmqqrva iaraiayqpd vlimdepfaa vdaqtradle
      181 dlvrelhltr gistvfvthd idesvylgqr vlvlsnsptr vqedlvidlp rerdqlttra
      241 lprftelrth vyeqiqrakr gpaatsqpap
//
LOCUS       WP_457608643             239 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter permease [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608643
VERSION     WP_457608643.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Rempel,S., Stanek,W.K. and Slotboom,D.J.
  TITLE     ECF-Type ATP-Binding Cassette Transporters
  JOURNAL   Annu Rev Biochem 88, 551-576 (2019)
   PUBMED   30485755
REFERENCE   2  (residues 1 to 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   3  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Rodionov,D.A., Hebbeln,P., Gelfand,M.S. and Eitinger,T.
  TITLE     Comparative and functional genomic analysis of prokaryotic nickel
            and cobalt uptake transporters: evidence for a novel group of
            ATP-binding cassette transporters
  JOURNAL   J Bacteriol 188 (1), 317-327 (2006)
   PUBMED   16352848
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..239
                     /product="energy-coupling factor ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0000041 - transition metal ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23913
     Region          6..212
                     /region_name="CbiM"
                     /note="ABC-type Co2+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG0310"
                     /db_xref="CDD:440079"
ORIGIN      
        1 mdtlamhisn giingpvaai faalalaala fcvlrgradl ddrlapmagl vaafifavqm
       61 lnfpiftagv sghllggala allvgpwvga lcvavvlivq alvfgdggva mlglnitnma
      121 llgtaaayll ialllrvlpr tpvglaitaf vsalvsvvva sqgfvlqywl ggttdlggnl
      181 tglagtmafa hlligigegl itattvvtva kvrpdlvyal ralkpatpap avpvaggar
//
LOCUS       WP_457608656             800 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608656
VERSION     WP_457608656.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..800
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88473
     Region          12..797
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mtaveselrt laelddtela rldawwrann yltigqiylq gnpllrepls aehikprllg
       61 hwgtspglsl iyahvsrlir htgqqtiyla gpghggpalv aagylegtys eiypdvsqde
      121 agmlrlfrqf sspggipshv svttpgsihe ggelgyvlvh afgavmdnpd llaiavvgdg
      181 eaetgplegs wkgvsflnpe rdgavlpilh lndakisgpt vlgrkdpeev rhllrghgyd
      241 vievegsdlp gmhhrfaaal aaawtrirdi qtaardgswd gtrptwplii lrspkgwtgp
      301 dtvdgvtvtg twrshqvpls gvkdnpehla llerwlrsyr peelfdstga pvalvrdqap
      361 dgdlrmsasp hangglltrd ldlpdfrsya ievsqpahqr aestrklgem mrdiyarnad
      421 rfrlfcpdet nsnrlggvfd vsdrafmerv tpddvaisrd grvmevlseh nchgwlegyn
      481 ltgrhgmfat yeafamvsas qtvqhgkwlq eakhlpwrak vpslnvllts tawrndhngf
      541 shqgpgliqv vltqrgdvar vylppdantl lsvadhcfrs rsyinlivid kqpqlqylsm
      601 deaiehcarg agiwewagtd dgtsdpdivl acagdvvtme tvaaaqilrd rlpglkvrvv
      661 nvvnlmtlvr pkdhphgmse tlftelftdd vdvvfsfhgy pgaihqlvhg rpdadrfrvr
      721 gfieqgtttt pfdmtvrnka sryhlvmdai nnakrlprga adlktwcrsq ldrheayvve
      781 hledmpevrd walgdwaarg
//
LOCUS       WP_457608660             418 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608660
VERSION     WP_457608660.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..418
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44994
     Region          20..327
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrvrttaav iaavalllag cggsdgksds ktfefwsfan inqkadvdvy tkahpdvrvk
       61 ltevgtttet aqaltaalag gkvpdlvliq addlpkfmqs pdnfvdlttl gandikgnyl
      121 dwvmaqsttk dgkiigvptd vgglavayrt dlfkaaglpt dresvsklwp twdefinvgk
      181 tyvqktgkpf vdntptsvff qavnqgsqry ysadrrldyd neqvkaafdv tlkafsagis
      241 akqgsfssgw taamkkgdya vvcspswmls qmktnapetn gkwdiatipg gsgnwggsfl
      301 aipkraknak aawnyisemq spkgqldhfl mqgslpttps vytdpqlvgk tdpffsnapi
      361 gkiytqsvvg ikpfyfgpqd gpigteflnt ltsveqgkvd pakawdtalt nvknavre
//
LOCUS       WP_457608670             410 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608670
VERSION     WP_457608670.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..410
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45725
     Region          5..410
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtpdvehllr aetpqvlgal vrrfghfeia edavqeallv asrawptdgv pdnprswlir
       61 igyrrmvdll rtdqarrrre rhagmselas rtrqadpale tddsltllll cchpalspta
      121 qvaltlravg glttteiaha hgttentmga risrakqqla ragarftppt dadrdsrmna
      181 vmqvlyliyn egytastgde ltrvdltrea irltrmlhds qpddpevtgl lalmlltesr
      241 raartdgdel vpldeqdrtr wdpelirega dlidsvwrrr evgtyqlqaa iaavhaaaas
      301 pdqtdwpqia alylglerls ptapvrlsrv vavahaygpd rglallddln rsyhldenpl
      361 trqreraira hllemtgdta caaaryreaa eltenqveqr ylqrrahrlg
//
LOCUS       WP_457608662             298 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608662
VERSION     WP_457608662.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..298
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30760
     Region          49..242
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mgsrchvgtr rraicveifr qipataqglr ptgvsgnqpm rtgrgsvmki vviggsglig
       61 sklverldaq gheavpaspk tgvntltgeg vadvlsgadt vvdvsnspsl eggaaleffe
      121 tstrnllaaa adagaghyva lsvvgserlp dsgylrakva qekliaasgl pyslvhatqf
      181 feflqgivda atdgdtvhla pvliqpmaad dvaaavaevv tgvptngvve vggpeqfrld
      241 elgrsvlvar qdprsvvsds garyfgaals erslvpadga riagtrlddw rmrathgr
//
LOCUS       WP_457608686             403 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608686
VERSION     WP_457608686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..403
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44695
     Region          75..368
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 marpelaigt sgklrieklg pkrfrararf rdydgitrdi eatdttgpaa eralkvklrd
       61 ratptddeit retrisalae lwveeitaee riapqtihry atsvrtsilp algnlrirea
      121 svgcldrflr diakdrpsaa kgvkvvlsqm falavrhgai ptnpvrdtgr lrkprrtvvv
      181 lsaeqlqavr tairewqrpi pgkpgprhsg dladvvdlml atggrigeil alrwedldla
      241 aerptlticg tlvfiksqgf frqpwtksda gyrrvvlprf avgmlmarkl taadnphdai
      301 fasrrgtwls pnnvrrqwrq araeadldwv tphtfrktva tlikeeidtk saaaqlghss
      361 eevtdtyyia kpvqapdvsg ilerlgshps tqgsppgend ahr
//
LOCUS       WP_457608693             565 aa            linear   BCT 27-JAN-2026
DEFINITION  murein biosynthesis integral membrane protein MurJ [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608693
VERSION     WP_457608693.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     gene            1..565
                     /gene="murJ"
     Protein         1..565
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=57077
     Region          19..522
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 mtkpaplaaa grvagaaali avltvlsrla gfgrtavftw mlgptdlgga ylvanyvpnf
       61 ifeivaggal aslvvpllag aveagdrrav aattgalltw tlsllvplav llavfadplp
      121 glignglsea qqasgarmlr vfapqlplyg vgivltgvlq ahrrfawpvi apllssltvi
      181 avylgftaae grqatigeag rggelllsag ttlgvvmlsl sllipvrrlr lrirpgyrfp
      241 adararvggl alagvvtvta qqialvvaln qvtygrtgdv vvynlaqtvy flpwavlavp
      301 lavaayptlv aaratgdera yretlapavr gvvllsllga aalvgtaipv ghfffadpld
      361 artaavgiag fapglvgygl favltralya rgetraatva talgwlsvpa lavvsaqvap
      421 ladrvlavtl atsagmlllg alliaavrra aggealagig ragtagllaa vvagaggaav
      481 aaglaglgdg tpttpwalaq gmlsgvvvgv lflavawltd ardlrpllat vtrrlrrrrp
      541 aggddgppaq qhpgergdgr etvss
//
LOCUS       WP_457608708             502 aa            linear   BCT 27-JAN-2026
DEFINITION  copper resistance CopC/CopD family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608708
VERSION     WP_457608708.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   van Sorge,N.M., Bonsor,D.A., Deng,L., Lindahl,E., Schmitt,V.,
            Lyndin,M., Schmidt,A., Nilsson,O.R., Brizuela,J., Boero,E.,
            Sundberg,E.J., van Strijp,J.A.G., Doran,K.S., Singer,B.B.,
            Lindahl,G. and McCarthy,A.J.
  TITLE     Bacterial protein domains with a novel Ig-like fold target human
            CEACAM receptors
  JOURNAL   EMBO J 40 (7), e106103 (2021)
   PUBMED   33522633
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Lawton,T.J., Kenney,G.E., Hurley,J.D. and Rosenzweig,A.C.
  TITLE     The CopC Family: Structural and Bioinformatic Insights into a
            Diverse Group of Periplasmic Copper Binding Proteins
  JOURNAL   Biochemistry 55 (15), 2278-2290 (2016)
   PUBMED   27010565
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Cooksey,D.A.
  TITLE     Molecular mechanisms of copper resistance and accumulation in
            bacteria
  JOURNAL   FEMS Microbiol Rev 14 (4), 381-386 (1994)
   PUBMED   7917425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17591615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..502
                     /product="copper resistance CopC/CopD family protein"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0046688 - response to copper ion [Evidence
                     IEA]"
                     /calculated_mol_wt=50191
     Region          1..115
                     /region_name="CopC"
                     /note="Copper-binding protein CopC (methionine-rich)
                     [Inorganic ion transport and metabolism]; COG2372"
                     /db_xref="CDD:441939"
     Region          325..>500
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; cl42370"
                     /db_xref="CDD:478162"
ORIGIN      
        1 mwlaccpavf vvlgfaspaa ahfkllkvvp adgarvdgtv teirltfsap gtptaagftl
       61 srggaavpvt thtpdggrtw lvhpsaaltd gkftlrwsva apdahpltgd vtftvvpaaa
      121 ppgatatprp tagshghtgh ggpavpsasp pahsgghavg htadadqgpv rfvgtagrwl
      181 sygaillgvg glvfalttlv gtrsdirlvq vwvriagltv vagvllelaa laavfggggl
      241 asavsaqalt algrtpvatg lglrfagaag llvagsleaa lirgrhavgr havvtvaaip
      301 taprplvvpp tgdvsgdevq rvraravrpv llgvtvalll gsflfdghtv tagpraivva
      361 advahtvaaa vwvggvllla alllgrarlg vptgaaemav rfsvpataav tltgvagaal
      421 tlaildrpgh lvstgwgrvl lvkvalvavv avvglynsrr vvprlddptp egmrrlrrtv
      481 laeavlmvav llatavlvnt gm
//
LOCUS       WP_457608713             381 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608713
VERSION     WP_457608713.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..381
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=41166
     Region          80..365
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mlvggkggad rgkrsmwrgv prwarvctil givmvvlsgs vligsralva ryegsvgkad
       61 lfgdqaagan ekksdikgpl nillvgvdpr tatarplads imvlhvpatm drgylfslpr
      121 dlrvdipefp kadysgandr lnaamshgsn vpgqnpstaq gfellaktvq evtgikrfda
      181 gaiinfsgfk kivdamggvd myierevrse hlqpdgtprq lkpggggylg pqavyekgna
      241 hlkgwqaldy vrqrypkngv pdadygrqrh qqqfvkamvs qafsadvvan pikldrvlra
      301 agkslvfngr gnsvvdfgla lkdirpeaie tiklpggpig sgsnyrgeql lepaedffta
      361 lrteqldafl lehpdfkqkt k
//
LOCUS       WP_457608733            1081 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608733
VERSION     WP_457608733.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1081
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111919
     Region          4..981
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msllarfsla nrglialval vttafglfav pslkqqllps lefpaafiva typgaapeiv
       61 esqvaepien slkgipglde vtstsregaa tvqvqyefgt dlddvvnkme talnridsql
      121 pegvdpqvia gstddlpavv vaatgdgder alaeklrnav vpelealdgv rsvdvtgard
      181 qvvtitpdpa klaaakvapt aiasalksng vavpagalad gdrslpvqvg tpirtiddlr
      241 givlttapaa pvrlgdvaav eqqlapatsf trtngkpslg iavtaapdgn avqishdird
      301 rldelsktsg aeltvvfdqa pfveksiesl ttegllglvm avvvilvfll svrstvvtav
      361 siplsvlval ivlwsgdysl nlltlgalti avgrvvddsi vvlenikrhl eygepkreai
      421 ltavrevaga vtastlttva vfapialvgg fvgqlfapfa itvtvallas llvsltvipv
      481 laywflrprg gaddaaarra aeekelrnpl qraylpvidf atrsrktrwa tvglgllvll
      541 gtfglaqkle tnflddsgqd tlairqempa gtslagtdra aarveevlrr tpgvetyqvs
      601 agggdnpfag ggsdratwsl slsddtdata vrqdlrkefd algaevgelt fgggqnasan
      661 qvevvvqaad qetltraaea vqgamagtpg vedvtsslat qvprvevtvd raaaaraglt
      721 eaavgqlvaq tyrgaplgqv tldgtaqsvv lssgarpplt vdelkalrvg avpldaiadv
      781 eqvdgpqqvt ridgersvsv tgtatgsnlg attqelqkrl daldvpgaty viggvsadqa
      841 dafadlglav laaiaivfli mvatfrsltq alillisvpf aatgaiglll vtgtplgvpa
      901 ligvlmlvgi vvtnaivlmd linqyraqgm dvteavvegg rrrlrpilmt avatifallp
      961 malgltgegg fiskplavvv iggllsstll tlvlvptlyt mvehtkgsfr nrrrggapep
     1021 vepqpepdpv pvaagggera eergvvappp arpsgalvdg tdqfevlrlp ksrqsplppt
     1081 e
//
LOCUS       WP_457608740             131 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608740
VERSION     WP_457608740.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 131)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..131
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14489
     Region          4..117
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mfvfrldths gvppylqlvq qvrqavllgf lqpgdrlpli revvedlain pntvakayrq
       61 meqenlvtgr pgqgtfvteq qsaamsasty tslrrgletw lrrayaagld eqavdalfas
      121 vrqqarnedv a
//
LOCUS       WP_457608744             299 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608744
VERSION     WP_457608744.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..299
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31772
     Region          8..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtatgfalrt dgvgkryrkg walrdctlal paggvialvg pngagkttll rlvvgllaps
       61 tgtvevlgrd vtastpqtls rigflaqdhp lykrftvaem lrfgrscnrr fdqelaerrl
      121 aklgipldrr tgtlsggqqa qvalalalak rpdllvldep vasldplarh eflqvlmgav
      181 aeggvtvlfs shvvhelerv cdhlvvlnqg rvtltgdidt llaehrllvg prtandldra
      241 gavveavhsd rhttllvrdg glpaapgwqt qpialedlvl aylrrpsepg aavtpgvpa
//
LOCUS       WP_457608764             290 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608764
VERSION     WP_457608764.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..290
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31347
     Region          1..289
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 mrcdipeglr wverteagra wlaelpgrla hcvarweltv gppfayafas lalpatlpdg
       61 trvvlklqyp dddsvheata lahwngrgai rllahdadrr allvercdpg tplhalaadt
      121 aldvavgllp klavpagapf tplaeeaagw aermpgnwrr agrpyerrll dtalglladl
      181 apsqgeqvlv nqdlhagnil aagrepwlvi dpkplvgere falvplvrga elghspaavr
      241 hrldrlsael gldrervrgw aigqtvawsv ggdqvfpgnv eaarwlldvm
//
LOCUS       WP_457608769             409 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent RNA methyltransferase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608769
VERSION     WP_457608769.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  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 409)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..409
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=42636
     Region          10..404
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 merpgleeae rveltvdava pgghcvarvg gqvvfvrhal pgerviaevt elhrgfarad
       61 aveildaspd rvtppcpyar pggcggcdlq hvapaaqldw klavvreqlt rlggltaeqi
      121 dalgvrveal pggplgwrsr vryavdaagr tgllkhrshe vvpidrclia hpaiqdlpvl
      181 pptgarwpha davetvastg gdvavvaytd gvpaavsgpe rvretaagrs ftlpasgfwq
      241 vhpaaadalt gavldlldpq pgetawdlyg gaglfaaala erldgarvtl vesapdgvaa
      301 arqnladlra vevvaarvea alsrrritgp vdlvvldppr sgagapvvra vvaagprava
      361 yvacdpaafa rdvrtfteag wrlaalrgfd lfpmtqhvel vglflppqg
//
LOCUS       WP_457608780             388 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608780
VERSION     WP_457608780.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..388
                     /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=40921
     Region          24..384
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msapatrrvr ptlrlrltll ngvllvgaga ilvllawllv rdalrptdel lpgttvvlsd
       61 grtldagewq rqlvdaasqe llvkgllala aisvvgvaga ylvagralrp lhqvtatarr
      121 lgeatlderi gwsgaddeva elaetfdaml drisgafeaq krfvanashe lrtplavmrt
      181 eidvtlsddd adlaeyrrma gvvrdasera nglvdallvl arseaqtgrr lgrraesdla
      241 igtanalsav sreveriglk vhtslrpapv vgdpglldrl agnlvenavr ynhlhgriwv
      301 rtgtdgersw lvvgntgfev apadvpglfe pfrrggqert gargsglgls ivravsdahg
      361 gtvravaqpg gglevtvtlp sadpaaat
//
LOCUS       WP_457608802             241 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608802
VERSION     WP_457608802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..241
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25303
     Region          17..240
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtdqtvvlpa epgtavddvv rvegvsrtfg rgehavhavr dvsftagrge lvavrgrsga
       61 gkttllnlvg gldrpdagri rvaghdvtaa gerellslrr gtigfvfqtf glvpilsaae
      121 nvgvplrlak vpaaereqrv avllelvglg ghaaqrpyel sggqqqrvav aralanepdl
      181 liadeptgql dsdtgrsimd llravvharg mtalvathdp alieladrtl tlrdgrlvse
      241 d
//
LOCUS       WP_457608813             304 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608813
VERSION     WP_457608813.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 304)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..304
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=32742
     Region          29..285
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtspdarrtl rppagyrlap svraltfspy dpcariaagt fwwatrtpdg patlalrpea
       61 geltaegygp gagwvverad riaglcddlt gfaalaaahp lvarlahthh glrmpatgqi
      121 fprllravfe qkvtgkeayr ayaatvrhfr epapgplqpl llppepaava atpywvfhpf
      181 gveqrradtl rraaavadrl ercadsaeat rrltaipgig pwtaaevvri aygdpdavsv
      241 gdyhvpntva walageprgd darmlallep frghrgrvcv lleaagirap kygprapirs
      301 fary
//
LOCUS       WP_457608815             450 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608815
VERSION     WP_457608815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 450)
  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 450)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..450
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=49955
     Region          8..388
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtaaprkkrk frtvslfsga ggldvgvdqs glfdllacve lqprfcetlt lnrdnglfgt
       61 edtriiqadl skldpyelmd elglkpgeld llaggppcqs fstagrrrtv edprgtllwd
      121 flrfveafkp kyflmenvrg llsaalrhrp iadrpdkggp pltaeerqgs vielwaddma
      181 kvdngiyrvd cfevnavnyg apqlrervlf ignrvnqqve fpepthgpid patgqpqpgl
      241 lphctlrdal aafrdddpvl mdfsprkkhy lamipaggnw rtlptevaqe smgkaffakg
      301 grsgwwrrls wdlpcptivt lpnhastsmc hpdevralsv gefarvqefp dgwsfagsam
      361 eqmaqvgnav pvrlglvaah tiarylerps dlqategdlp rfrrvylnsh vrtrqwykag
      421 qafvwdgigg sahygrrtpa qqeplplfda
//
LOCUS       WP_457608817             205 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608817
VERSION     WP_457608817.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..205
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21881
     Region          7..188
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 msreratall vdfdgvlrrw dpavaagver eygltegvlg eiamswgllq pvltgqvsha
       61 qwmvsvadal tpavgadrar aavqewqsyr gevdpdvltf lrevraagiw vglgtnatdl
      121 ldadlaalgl teeldvivns svvgvhkpak eyfqaaceal etppgrvlfv ddedravaga
      181 rvaglsahrw sgpadlrylr aalay
//
LOCUS       WP_457608819             162 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608819
VERSION     WP_457608819.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..162
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17204
     Region          28..161
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mdaaereryg pqtrplpyer gtdgprvvlv gvdgsrtsmr aaayaaglar rqgatlvavf
       61 vsspasysam lsgvvagavq qthdeladel raecrrgaee ldlpvtflcr rgdaytelcr
      121 aadehradiv vvgsseqagh klvgsvatrl vrtgrwpvvv vp
//
LOCUS       WP_457608822             155 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608822
VERSION     WP_457608822.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 155)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..155
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17043
     Region          8..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtvytprraa rvllvdasdr vllfegsdpa rpghrywftp ggglepgesp adgairelae
       61 etglrlapae lgtpvwsdtv efpfdgvwyr qeqqfylvrv tvwdvdtagf ndverasvhg
      121 hrwwpvtela ataeryyppd lpgrlgtvla ggtac
//
LOCUS       WP_457608823             368 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite oxidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608823
VERSION     WP_457608823.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Hsiao,J.C., McGrath,A.P., Kielmann,L., Kalimuthu,P., Darain,F.,
            Bernhardt,P.V., Harmer,J., Lee,M., Meyers,K., Maher,M.J. and
            Kappler,U.
  TITLE     The central active site arginine in sulfite oxidizing enzymes
            alters kinetic properties by controlling electron transfer and
            redox interactions
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (1), 19-27 (2018)
   PUBMED   28986298
REFERENCE   2  (residues 1 to 368)
  AUTHORS   McGrath,A.P., Laming,E.L., Casas Garcia,G.P., Kvansakul,M.,
            Guss,J.M., Trewhella,J., Calmes,B., Bernhardt,P.V., Hanson,G.R.,
            Kappler,U. and Maher,M.J.
  TITLE     Structural basis of interprotein electron transfer in bacterial
            sulfite oxidation
  JOURNAL   Elife 4, e09066 (2015)
   PUBMED   26687009
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Barber,M.J. and Neame,P.J.
  TITLE     A conserved cysteine in molybdenum oxotransferases
  JOURNAL   J Biol Chem 265 (34), 20912-20915 (1990)
   PUBMED   2249998
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Campbell,W.H. and Kinghorn,K.R.
  TITLE     Functional domains of assimilatory nitrate reductases and nitrite
            reductases
  JOURNAL   Trends Biochem Sci 15 (8), 315-319 (1990)
   PUBMED   2204158
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Neame,P.J. and Barber,M.J.
  TITLE     Conserved domains in molybdenum hydroxylases. The amino acid
            sequence of chicken hepatic sulfite oxidase
  JOURNAL   J Biol Chem 264 (35), 20894-20901 (1989)
   PUBMED   2687265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..368
                     /product="sulfite oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39921
     Region          48..363
                     /region_name="SO_family_Moco_dimer"
                     /note="Subgroup of sulfite oxidase (SO) family
                     molybdopterin binding domains that contains conserved
                     dimerization domain. This molybdopterin cofactor (Moco)
                     binding domain is found in a variety of oxidoreductases,
                     main members of this family are nitrate...; cd02110"
                     /db_xref="CDD:239028"
     Site            order(49..50,52,54,98,163,192,197,205,208,210..211)
                     /site_type="active"
                     /note="Moco binding site [active]"
                     /db_xref="CDD:239028"
     Site            98
                     /site_type="other"
                     /note="metal coordination site [ion binding]"
                     /db_xref="CDD:239028"
     Site            order(248,284,288,290,299,301,333,338..340,358)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239028"
ORIGIN      
        1 mttvddvsrp srvagpdeai saeelqlaar nhgiplealr ydvtpaglhy llihydipdv
       61 dpaahtlnvs gaverplrld laalrdrprv thrvtlecag ngrallrprp vsqpwlveav
      121 gnaewtgtpl apllreagls gdavgvvftg adhgvergve qdyqralpva dalreevlla
      181 yemngapllp qhgaplrliv pgwygmahvk wlrditvate pfdgyqnava yrlrrdaddp
      241 gvpvtriepr alvrppgfpd fmsrirvlrp gpctldgraw sghapvtsve vttdgggtwt
      301 aavldepagg ewawrrwsvn wtatpgrfvl garatdasgr tqpveqpwnr ggfannlvqr
      361 vevvvpae
//
LOCUS       WP_457608828             301 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608828
VERSION     WP_457608828.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..301
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=32736
     Region          <36..281
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mspsagdpal drpawevava vaqvlvnrrl ygdvvervrr rlpmqvaaet vwgllppltf
       61 atddlvitai lepcydvggd ifdyalngdv lsvglfdtcg hgikasamas lvvsayrnar
      121 rtgldlvdta isidrwvrse hpglfatall aeldrrtgvl rtinaghpga mllrdgkavr
      181 alpgptalpl glgnlsarrp rvheealhpg drvlaytdgi tdargddger fgldrlvdfv
      241 eralndrlps petmrrlvra vlayqqdqld ddatalflew qpphlplghl ehltarvegs
      301 r
//
LOCUS       WP_457608830             209 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608830
VERSION     WP_457608830.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 209)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..209
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20566
     Region          <46..190
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mllflvvclp galgpplsss rvgvyslaag pppaasargp dgpasagala sgpsaadgsa
       61 agrrgapggr frwplpgapr vvrrfdpppq pwlsghrgvd laaapgapvl aagagtvlfa
      121 gtvagrpvlt vghsgglrtt yepvrpglta gtpvdagtpv gdllaghqgc aeaaclhwgl
      181 rrdaeyldpl allglgrvrl lplhpvpag
//
LOCUS       WP_457608831             334 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine recombinase XerC [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608831
VERSION     WP_457608831.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..334
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35401
     Region          1..334
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(186,280,283..284,315)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mreavddfad hlsrvrnrsv htvrayvtdl vslldhavrm gcaelpeldl avvrswlakq
       61 rtmgaarttm arraaaartf sawahrtgll addvaaplas prarrelptv lradqaaalv
      121 eapsrqrpgp aeadrptahp dgvglgddhg tvaepasaep agdgpagavl lrdrlllell
      181 ygtgvrisea cglnvtdvdq arrvvrvlgk ggrersvpyg vpaqraldaw lrdgrpallt
      241 pgsgralllg arggrlnptt arrivsgwag aagvprvtph glrhsaathl leggadlrav
      301 qellghssla stqiythvsv erlraayrqa hpra
//
LOCUS       WP_457608833             120 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608833
VERSION     WP_457608833.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 120)
  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 120)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..120
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12805
     Region          <8..115
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mnlicgkdmf ipdiavlrss gggrsavdia eavllgeivs pgnrckdvid rpreyaaagv
       61 pyvlrvdlrn rvpalalyel vdgeyrplsa aaagttfvmr qpfefsvdpa dlldeeapqa
//
LOCUS       WP_457608838             188 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608838
VERSION     WP_457608838.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19816
     Region          7..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpdrplrada lrnrqrllda avqafsqdgp evtldrvare agvgigtlyr hfpsrealie
       61 aayrnelekl cdaapallaa qpadaalraw mdrfvdylat krgmadalrl viasganpya
      121 qsrdrllaal gallaagaaa gvvrvdvaaa dvlaslsgvs lvagepdqra qagrlldllm
      181 dglrhrpg
//
LOCUS       WP_457608842             974 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608842
VERSION     WP_457608842.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..974
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103211
     Region          <4..974
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mtvraastvl vgrrselaal gdalarsrtg epatvlvgge agvgktrlle efgtqvdaag
       61 arllvgqcle lgeaglpfap faaalrdvlr hdgpaafagy eaefarllpe larmpagvaa
      121 pagpaladtp rgylfdlvad lfrriaeerp lvlviedlhw adrstrdlig flvraaratr
      181 llvvctyrtd elhrghplrp flaeldrvrg vdrielgrld rdgtaavlad llgvdqiart
      241 vdevhertqg npffieelaa aggpvgcaai petlrdllla rvdrlpepaq rvlriaaagg
      301 trfahqllae vaglpeaele dalraavagq lvvadpdgdy efrhalvrea vhddllpgeh
      361 arlharyaaa ieaqphlvaa grapaeiahh wyaahdhpra ltaarvaaea aaeryayaeq
      421 srllervlel weqvpdaadr lgmdhlrvle dtltaavtag dlsraltltr aalaevdsda
      481 eplraarlld hrgrlfallg ksdgatelre ayrlaagarh gperlgvlad iashlmkvdp
      541 reaasvatea aagasevgtd lvllptrial lhridgtpel glaelrrvea raraaddswa
      601 lvsalvflsd vlyelgryde seqaaaagvs earrvgisrs igayllsnra ealialgrwd
      661 eadatcaeaa ridppgvsgl hwlqlraglh larahpgade vvgralaflg rpylwpnhrl
      721 plhelrveaa laagdkpeav raagaalada hladlpregw pvlnalarta altgdatlaa
      781 dvsavaaalp arypaehaha ahvtavltgl gsaapaeala awratvaawr aagqpyllgr
      841 allglaeaaa aagerdevaa avretaelaa rlgatplgeq aatlarrvgl rgtgrpgpdl
      901 ltsreqevlr lvaeghsnsr iaerlfispk tasvhvsrii akldvtnrve aaalahrlgl
      961 ldrpspapaq rrvr
//
LOCUS       WP_457608845             287 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase, partial [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608845
VERSION     WP_457608845.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>287
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          11..262
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mlssdvvlsg ryrlddrvat ggmgdvwrat dlvlgrpvav kvllpalvsd pdfiarfrse
       61 arimaslrhp gvvqvfdcge ddlpgggrad ylvmefvage plsrriesag qlevaetmsi
      121 vaqvaqalha ahgrgivhrd vkpsnllvqd dgtvvlvdfg varstnvtsi tstnavpgta
      181 lymapeqaag rpvsgatdvy algavayccl tgsppftgdn plqvavrhld deppelpaei
      241 pasvrelvsr alakdpadry psaaamadaa raartdspta tvalrga
//
LOCUS       WP_457608839             336 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608839
VERSION     WP_457608839.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 336)
  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 336)
  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 11430362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..336
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35767
     Region          3..330
                     /region_name="PdxI"
                     /note="Pyridoxal reductase PdxI or related oxidoreductase,
                     aldo/keto reductase family [Coenzyme transport and
                     metabolism, General function prediction only]; COG0667"
                     /db_xref="CDD:440431"
ORIGIN      
        1 mtttrrlgrs gievsaigmg cwaiggplwd gtqplgwgev dddesvrtvh raldlgatlf
       61 dtssnygagh servlgrala grrdraviat kfgyptdeet rqalgedasp eyarrslegs
      121 lrrlgtdhvd lyqlhlgglp vpraldlvgt ledlvaegki raygwstddp asarafagag
      181 phcaaiqhdq svlrdnaaml avcaefdlas lnrgplamgl ltakyqdapt arggddvrgv
      241 apewldwftg gvpraewaqr varvrealta dgrmlaqgal gwllarspht lpipgcrtva
      301 qaeenlgala ygplpqdafa everllaelr tapada
//
LOCUS       WP_457608851             434 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608851
VERSION     WP_457608851.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..434
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44019
     Region          81..350
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrarvlaaat avtllttgvp apataaapal tpaaapagva aaapaaapvp cprlpapkvs
       61 rpprptppat tpeqaavgge alagtglvtp pgspappavt attwlvadld tgavlgacga
      121 hvpgtpastq klllaatmls rldpkqvava tradldiepg ssavgllvgg rysvetlwlg
      181 lllqsgndaa nmlarlgags sqagvaemna qasrlgagqt havtpsgldg pgqftsaydl
      241 aliaracfad aafrryalte rtqipaqpal kkggfqiqne nqliyrypga lggktgftel
      301 arhsyvgaaq rggrrlvvtl lgaearpvrg wqqgaqlldw gfrqprgasv grlvepgerd
      361 aeaaeprpaa aaepsrtasp pwrgpagtal rrvgdgdwrm ivplagllal tvggvaavla
      421 arrgrsrrrg rrra
//
LOCUS       WP_457608854             399 aa            linear   BCT 27-JAN-2026
DEFINITION  RtcB family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608854
VERSION     WP_457608854.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..399
                     /product="RtcB family protein"
                     /EC_number="6.5.1.8"
                     /GO_function="GO:0008452 - RNA ligase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=42862
     Region          5..399
                     /region_name="RtcB"
                     /note="RNA-splicing ligase RtcB, repairs tRNA damage
                     [Translation, ribosomal structure and biogenesis];
                     COG1690"
                     /db_xref="CDD:441296"
ORIGIN      
        1 mgftplagtr apvrvwtdpy aieaqaarql rnigalpwvq gvavmpdvhf gkgatvgsvi
       61 amrqavspaa vgvdigcgms avrtsltaad lpddlgplrs aieaaipvgf akrddavdpr
      121 rvrgleqagw ddfwrrfgtl drkvaqletr aqrqlgtlgg gnhfievcle qggaddgrvw
      181 lmlhsgsrni gkelaerhma varglphntg lpdrdlavfl agtpemeayr rdlwwaqeya
      241 rrnravmlal lsqvvrdafp hvgydepisc hhnyvaeesy dgvdvlvtrk gairagkgdl
      301 giipgsmgtg syivrgkgnl daycsashga grrmsrgqak rtystadlaa qtagvecrkd
      361 agvvdeipga ykditevmaq qddlvevvah lkqvvcvkg
//
LOCUS       WP_457608855             258 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608855
VERSION     WP_457608855.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..258
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26643
     Region          5..206
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mnrqilvtgg tgtigrhvvp llraaghpvr vlsrrggrgg dgvthvtadl lggadlgpal
       61 rgvstvlhla ggakgddrat ahlaraahra gvahlvhisv tgadrlplaw irskldaera
      121 vadsgvpwtv lraaqvhdlv ltmltamtrl pvvpvpgglr lqpvdaaeva srlaeltlga
      181 paglvpdlag pdiygvgell tgyltatgkr rvrlpvripg ragrayrdga nlarpgaarg
      241 vrtwadflae rapsrpvi
//
LOCUS       WP_457608857             299 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608857
VERSION     WP_457608857.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..299
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31866
     Region          217..297
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtaaptlhfc adpgeflada eaylaadpvv gtvvasvtrr maarraegva lpedvwwlvv
       61 rdaagavvgv amrtapfppr ppfllpmpre aatalaeawh rrgervravn galpaaraca
      121 devarldggr vvvaqhtrlh lldrltppap vpgalraatt ddidlvtawf gaftadadeq
      181 agrprgasah etpdraellh rirdgrvwfw tdesgapvhl taanppsfgv arvgpvytpp
      241 gqrgrgwagn avaevsrrlt aegarvclft dqanpvsnrl yarlgfrpvv dmvnlvlvd
//
LOCUS       WP_457608859             158 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608859
VERSION     WP_457608859.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16952
     Region          8..114
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtdllaqrds wstancsiar alevvgnrtt llllreasfg trrfddfarr vgvsepvaaa
       61 rlkqlvadgl ldrrpyrepg qrtrdeyvlt akgsdlipvl valrqwgday aadeagpavr
      121 vthdecgapv harlrcdagh dvppgelavl pgpgllsa
//
LOCUS       WP_457608863             209 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608863
VERSION     WP_457608863.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..209
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22276
     Region          1..196
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mtrlivwrhg ntdwnaesrv qgqtdvplnd lgreqaraaa pvlaalrpda ivasdlrraa
       61 dtaaalaalt glpvrsdarl rerhfgqwqg ltlteaaerf pdeyarwrag dpdpgagiep
      121 lgdlgarlga gfqdaadlav ggtvvvtthg ggarqgvghl lgwdhtvlrs lgalanchwt
      181 elrhddvrgw hlraynvgli tqpaltdav
//
LOCUS       WP_457608864             258 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608864
VERSION     WP_457608864.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26438
     Region          18..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msplsyvvtg ggrgvgraiv erlaadggtv vvverdtnal dwlanhplad rlhavtgdag
       61 deavteraad raetraplag wvnnaavfrd adlhrapase vvdlialnlr pavagagtav
      121 rrflaagtgg aivnvsshqa rravpgalpy atakaalegl tralavdygp rgiranaval
      181 gsihterhaa ylagldpagv ehvdsemarl hplgrigrtd evaevvafll sdrasfvnga
      241 tvpvdggraa lgldpear
//
LOCUS       WP_457608865             803 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608865
VERSION     WP_457608865.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12047261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..803
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=81198
     Region          247..504
                     /region_name="Competence"
                     /note="Competence protein; pfam03772"
                     /db_xref="CDD:461044"
     Region          545..792
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC C-terminal domain,
                     metallo-beta-lactamase superfamily [Intracellular
                     trafficking, secretion, and vesicular transport]; COG2333"
                     /db_xref="CDD:441904"
ORIGIN      
        1 mtarrgprpa aldgdaagrd vpdlrlagla vaawlaalag lhlsvrssvw maavaaalal
       61 ltglhlggvl grpgvtasry gwiavavllg vlcgaaatga rvavrdaapi ralvadsalv
      121 taelvlrddp rpvrgapgre pmllvrvdlv rltgpggarv tgpvralvla tdpawrpllp
      181 gqrvtsrgrl aaprggdlta avlstadppt lrgdaswpqr aagvlraglq raceplpdap
      241 ggllpglvvg dtsrllpeve edfratgmth lnavsgsnva ivvgavllla rwaragprta
      301 avlcvlalvg fvilvrpsps vvraaamgai glaalaagrs rsalpalaaa vtglvlydpd
      361 lagdpgfals vcatggllll apgwrdalrr rgvpagfaea lavpaaaqla cgpviaglsa
      421 tvslvavpan llavpavapa tvlgvlaavl splwpggaef lawlaswpar wlvavaayga
      481 dlpagnlpwa ggvagallla tvsvalllaf rrrrarrlia vvvvavvlga vpirllasgw
      541 pprgwvvvac avgqgdavvl pvaagravvv dagpepsgvd aclrrlrvre vpllvvshfh
      601 vdhvggvagv frgrrvgavv gpswseppfg aarvreaarg agaplapvqa gwrwragavd
      661 lvavgppypl rgsrsdpnnn slvlaatvgg vrilltgdae teeqramlet tpaaairadv
      721 lkvahhgsay qapeflaavr pavalvsvgv dndyghpnag lldrltrgga rvlrtdtdgd
      781 vaavragggl avvkrgaesg rpr
//
LOCUS       WP_457608867             358 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608867
VERSION     WP_457608867.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   2  (residues 1 to 358)
  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..358
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..358
                     /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=36987
     Region          77..276
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 magslaeptd apvrrappvr qhgavhpisl ppvpygstav rpgwadlpag lrdalsarig
       61 gepsavrvtd ggftsgfaav ltgpagervf vkaaalhgqr hlvdwyahea ailarlpagl
      121 pvprprwalt eagwyalald aidghtpalp wapaeldaal atyaevaaal aeppaelaal
      181 rlprladlar ddilwwgeva agreplpepa agaplaelvt lesrlpgyaa aapglahgdl
      241 rvdnllldpg grawlcdwpw lchgpawfdl aglllsayas gldadaafag hpaaagapad
      301 aldvtlaala gyfltgaaag psnasphlra hqrwsgeqal gwlaerqgws warptpss
//
LOCUS       WP_457608869             458 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608869
VERSION     WP_457608869.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49143
     Region          1..342
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtdvsdrlar mvrqaqatgr ipavsaalhr adrplwtctv gdtgndtplg petvfrigsv
       61 tktftaalvm qcrdeglldl ddpigrhldl pahgdatvrr llshttglqr ephgdvwdsl
      121 rapaveemla dlarvervlp tgrrfhysnl glallgeava rlrggtwaev ladrvltplg
      181 ltatgpypte raatgflvda ysdeahpepp adfgavapaa qlwstasdma rwaafladpa
      241 avdpdgavla attveemrwp ltptdesvws agfglglili pqpervthvg hdgampgfla
      301 avygrrggqg tagamgaavl gssgagvevl dlphrllaaa aehdpaeiep wrpgppapdh
      361 lrgvlgrwwg egfeyvfswh dgtlrargad dpagkppavf aplpdrpdvf rtvsgreage
      421 llrltrderg vvvrmhwaty rftrtqetfd gydfragd
//
LOCUS       WP_457608872             266 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608872
VERSION     WP_457608872.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Swier,L.J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural insight in the toppling mechanism of an energy-coupling
            factor transporter
  JOURNAL   Nat Commun 7, 11072 (2016)
   PUBMED   27026363
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wang,T., Fu,G., Pan,X., Wu,J., Gong,X., Wang,J. and Shi,Y.
  TITLE     Structure of a bacterial energy-coupling factor transporter
  JOURNAL   Nature 497 (7448), 272-276 (2013)
   PUBMED   23584587
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..266
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27441
     Region          1..238
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(26..27,29..30,33..34,73,77..78,81..82,112,116,123,
                     126..127,132,148,152..153,155..157,159..160,163..164,
                     167..168,192..193,195..197,199..201,203..204,206..207,211,
                     214..215,221,223)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(151,155,158..159,161..162,206,209..210,212..217,
                     220..222,226,228)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(172..179,194,197..198,201)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 miglepvaap gaplarrnpv aklaaavvft lilvatldpv apaiaiavel avlplfgvry
       61 rvlarrgwpl lagavgilvt lvlfaadrsg pvllqagpil vtqgvlmtal glvlrmvava
      121 lpgivvfatt dptdladali qnaktparfa igalaafrmv plleqewrmi smarrargvd
      181 agrnpvaklr lfgstaftll vgairrgtrl avamdargfd agtprtvarp qrftsadtll
      241 vvgaallaga alatsialgt frplig
//
LOCUS       WP_457608874             657 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608874
VERSION     WP_457608874.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..657
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=71169
     Region          76..458
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtttqnsrpe spdgagplpa eagqvsekea rqvaeaares awdrpsfgke lflgrfrldl
       61 idpwprpdpa evaradeflg slrayltsev dgeaierdar ipdevfhgla glgtfgmkid
      121 rkygglglsn lhycralmlv gsvnpavsal lsahqsigvp qplkmfgtpe qkerflprla
      181 agevsafllt epdvgsdpar lattaepiad gtgyrlngvk lwatngtlat llvvmarvpa
      241 gegrrggita fvvegdsdgi tverrnsfvg lrglensltr fhdvfvpken viggegkglk
      301 ialttlntgr lslpamcvga gkwalnvare waadrvqwgr pvgeheavak klsfiaatty
      361 gmesmldlsc mladddrndi rieaalvkly asemawriad eliqirggrg yetadslaar
      421 gerpaaveql lrdlrinrif egsteimhll iareavdahl svagdiidpd aglgrkakag
      481 aragafyakw lptlavgkgq tpgayqefgp laghlrhver tsrklarstf yamsrwqgkm
      541 erkqaflgrv vdigaelfam savcvrayae rdahpenvel adlfcrqarl rvdelftglw
      601 sntdsvdvaa akrivagrya sveegvvtpp adlpwvarwe pgasteqdvr rrippag
//
LOCUS       WP_457608875             254 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter ATP-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608875
VERSION     WP_457608875.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..254
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25967
     Region          1..226
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mtspvieiah atvgydgrpv lrdvsltvta sevvavlgan gsgkstlvra alglvplgag
       61 svalfgtpqr rfrqwhrigy vpqrlgagsg vpatvrevva sgrlarrgvl rpagqadrea
      121 vaaaldavgl adragdpvst lsggqqqrtl iaralaggpe llvldeptag vdaasqeafa
      181 galrafrdgg gtvllvahel gplrplisra vvvhqggiah dgavpepagh hadpdhehvh
      241 phcdeeparl wtgi
//
LOCUS       WP_457608882             269 aa            linear   BCT 27-JAN-2026
DEFINITION  metal-dependent hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608882
VERSION     WP_457608882.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10515426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..269
                     /product="metal-dependent hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28624
     Region          1..>219
                     /region_name="YdjM"
                     /note="LexA-binding, inner membrane-associated putative
                     hydrolase; pfam04307"
                     /db_xref="CDD:427854"
ORIGIN      
        1 mmgpshalsg aavwltgswa maqfadyhqt plalavgtav caggalfpdl dlsgkvtrnq
       61 ggatvartfg vvslfvaevm ekislgvyya tklskdprrn nghrtlthti pftvlvgwgt
      121 talcahygkw avvgilffmi glalrglfde waeragwvvv tlvsaaaawf tfatlpgdrg
      181 ypmiglavgv gcfvhilgdm itragvpilw pipikrrmwt miglpnkial rtgskaetvv
      241 lrtamtilsv laavglvaps vlqrfdiqv
//
LOCUS       WP_457608891             329 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608891
VERSION     WP_457608891.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..329
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33015
     Region          4..287
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 msdtvvvgld vggtstrata lsldgtrlga gragggnpts hgadraaael laalraalag
       61 idphrvragv iglagagrll adphgrdafd rawaeaglrc pyavhgdalv ayasgtatpd
      121 gtvlvagtga iaaqvrdlrl drtadghgwl lgdagsgfwl greavrrllt dldraetpge
      181 lgrrvltelt gtpavdaqpr vtagavvqav trrppvelar laplvvssar dgepaavali
      241 aeaaallaes vsrirplgat dpvvlgggll tgdtplagav raeladrwpd aplhsagdga
      301 aaaawlaard lpevtdpaal htrlvpppa
//
LOCUS       WP_457608900             598 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608900
VERSION     WP_457608900.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..598
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=64221
     Region          7..129
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          253..593
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mfptvrevle lvpvrhgapr lvagnagldr svrwvhiaev pdiatllggg elvlttgigl
       61 pgddaglref igaladvgvs glavelgrry vsgvprvmaa aaerrglpli elrrgtpfvr
      121 iteavhaliv daqltelrat eeihqrftdl svegaepaev lrqaaelagc pmvlenlsrq
      181 vlaydpagen aqllldgwer hsrqirppgr taydpdsgwl vtivgargqd wgrlllrwpa
      241 testpptrlt ilieraastl algrlirrda eglerqihrt lltalidhtr pvdevalrak
      301 algvvldrrh lvgvvvrhra depagdagap edepaarrga rrdtdaegpe agparlrdla
      361 eavsqavrda kltaltspld dqavgallal pdpaaeekal safasalrrv rldaaparpp
      421 asrpsespdr pagravasgs arpvdappra aivvaagsgv sslrearrsl iearqvaeaa
      481 rrdprdlpcy rlphvglagl lhllrdeprl qtfverelgp llaydaqhpr eqllgtlray
      541 leqgrnksag aaaahlsrpa fyerlarigr ildadldsvd rclslhvall aldairtp
//
LOCUS       WP_457608902             269 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608902
VERSION     WP_457608902.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..269
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28950
     Region          6..251
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpvheitdpd ddriadyral tdvelrtrwe pphglfiaeg elvlrralra gyparsylvd
       61 akrvdqladl dtgdapvyaa tpdvlqratg fhvhrgvlas fhrkplrsad evlaaarrvv
      121 iledvnnhtn lgaifrgaaa lgvdavllsp tcadplyrrs vrvsmgevfa vpyakldrwp
      181 dgldevraag ftvlamtpap davpmqrltp aqreraalll gaegpgltaa aqaasdvrvv
      241 ipmrrgvdsl nvaaaaavaf welgrddal
//
LOCUS       WP_457608908             436 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608908
VERSION     WP_457608908.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..436
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46761
     Region          9..333
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpllpetarq vdllvaraqa egrgpslalg vvrdgrlahl avagetprpd gdlqyrvgsi
       61 tktmtavlvm qqrdagrlal ddpldahlpg tpvgavtvrq llghagglqr epdgdwwera
      121 egmdldtlla gltpdkiayp phfvyhysnl aygllgaale ritgipwadl lterlltplg
      181 mrrttyhpae pyahgyvvhp whetlreepr tdtgamapag qlwstvedlg rwaafladpd
      241 pavlspatlt emcapvvind ldswtgghgl gvelyrigdr vyvghggsmp gyvaglavhr
      301 ptrtavvnfa nayglrghhi galgrealtl vldaepaapa pwrpagppaa dvaaltgrww
      361 wmggeyefrv daagdlvggq vgrpllrftp egpdrwrgrs gsqdgeiltv irdasgtpta
      421 ldiatflltr spdelp
//
LOCUS       WP_457608915             248 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608915
VERSION     WP_457608915.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..248
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26167
     Region          1..246
                     /region_name="ElaC"
                     /note="Ribonuclease BN, tRNA processing enzyme
                     [Translation, ribosomal structure and biogenesis];
                     COG1234"
                     /db_xref="CDD:440847"
ORIGIN      
        1 mrttvlgglg ayptahqaca gflvehdgfr llidpgyatl qpllaltrae hvdavyvshg
       61 hpdhcadlqp lirarvlanr sgpplpvyap tgslagllai depgllepgy rltgftpget
      121 lrlgpyevrt falphwvpna garfsaaglv laytgdtgps palvelarda dlliaeatyp
      181 delpqrhegn lssavevgry ateagvrrll lthlwpgtep realtavrrg fagpvevaap
      241 gltltvgr
//
LOCUS       WP_457608884             237 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmannosamine-6-phosphate 2-epimerase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608884
VERSION     WP_457608884.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Arif,T., Currie,M.J., Dobson,R.C.J., Newson,H.L., Poonthiyil,V.,
            Fairbanks,A.J., North,R.A. and Rendle,P.M.
  TITLE     Synthesis of N-acetylmannosamine-6-phosphate derivatives to
            investigate the mechanism of N-acetylmannosamine-6-phosphate
            2-epimerase
  JOURNAL   Carbohydr Res 510, 108445 (2021)
   PUBMED   34607125
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Currie,M.J., Manjunath,L., Horne,C.R., Rendle,P.M., Subramanian,R.,
            Friemann,R., Fairbanks,A.J., Muscroft-Taylor,A.C., North,R.A. and
            Dobson,R.C.J.
  TITLE     N-acetylmannosamine-6-phosphate 2-epimerase uses a novel
            substrate-assisted mechanism to catalyze amino sugar epimerization
  JOURNAL   J Biol Chem 297 (4), 101113 (2021)
   PUBMED   34437902
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..237
                     /product="N-acetylmannosamine-6-phosphate 2-epimerase"
                     /EC_number="5.1.3.9"
                     /GO_function="GO:0047465 - N-acylglucosamine-6-phosphate
                     2-epimerase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006051 - N-acetylmannosamine metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0019262 - N-acetylneuraminate catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24298
     Region          <50..227
                     /region_name="NanE"
                     /note="Putative N-acetylmannosamine-6-phosphate epimerase
                     [Carbohydrate transport and metabolism]; COG3010"
                     /db_xref="CDD:442247"
ORIGIN      
        1 msvldelagg lvvscqplpd dpddpmrdpy vqarvaaavv rggavavrvn gpddvravra
       61 avdvpvigly khgtqgvfit ptaghaleaa ragshvvavd atdrprpdgr tfadtvravh
      121 eqtgtlvlad vatvaegvaa veagadavat tlsgytpagp pidgpdlglv arlaallpvp
      181 viaegryrtt eqisrafeag ahavvmgnav tsplwitrrl vpatpraasa pekrehr
//
LOCUS       WP_457608920             451 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608920
VERSION     WP_457608920.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..451
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=47910
     Region          3..449
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mgevispvdg arigivpgcs vedvdaavar aaaafqtwrh vapgdrgrll rrfaaavdah
       61 leelallevr naghtignar weagnvrdvl dyyagaperl tghqipvpgg ldvtfheplg
      121 vvgvivpwnf pmpiagwgfa palaagntvv lkpaeltplt alrlaelard aglpdgvftv
      181 lpgrgsvvge rfvthpavrk icftgstevg irimagcaaq vkrvtlelgg ksanivfada
      241 dlekaaatap yavfdnagqd ccarsrilvq rrvydrflel lepavravrv edpardtaem
      301 gplisaahrd rvagyvdgad vaftgscpdg pgfwyaptvl lagspadrhw reevfgpvvs
      361 vlpfddeada irlandteyg lsgsiwtrdv gravrvarav esgnlsvnsh ssvrywtpfg
      421 gmkrsglgre lgpdalhaft dvknvfigte e
//
LOCUS       WP_457608926             194 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608926
VERSION     WP_457608926.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..194
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21337
     Region          21..176
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtpppsvtfd qcrpgelasv vdaladlyal vyaeppyleg paqvarfrtg lpdeaarpgf
       61 rlvlaregee ligaaygwtm aagtwwsrak eepptevrdr dkfavlewiv hpryrshgig
      121 aelmrrllqg rpeswatlas dprslangiy rrngwrvagh selpwgssme llvrdlarva
      181 agersdgggp wlst
//
LOCUS       WP_457608927             403 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608927
VERSION     WP_457608927.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
REFERENCE   4  (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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..403
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44510
     Region          2..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"
ORIGIN      
        1 mdqfgdilrr hrvaagwslr kfadlirydf gylgqiergd rpvnpavvaa ydralstdgs
       61 irkaydsgra ddvdmprrsv lqamtslaal ptvdrmvgwe alrhgldaav dvdsdawaei
      121 vssygtayyr qphdqlmtql grdltvlqhq laasddrrrp qllraaatls vivalslvas
      181 ghallrrwwa saqraadksg dpdtrvltra wdivngcydg rrpmtvvais devlplagrp
      241 saatcgllag raqalslagr hdeavatvrh lseqieklpa avvgnveslw gwpehrlrht
      301 eswvythssd rraaeaaqar alelypasqi rlrtqvqlhq aaatvragdi tdgltaaadl
      361 ldrlpreqhn elvravtlqv taavpdrerh rplytelmdr vqr
//
LOCUS       WP_457608934             440 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608934
VERSION     WP_457608934.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..440
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44351
     Region          14..430
                     /region_name="MATE_DinF_like"
                     /note="DinF and similar proteins, a subfamily of the
                     multidrug and toxic compound extrusion (MATE)-like
                     proteins; cd13136"
                     /db_xref="CDD:240541"
ORIGIN      
        1 msttaapavt asprriaala lpalvvlaae plyvlvdtav vghlgrvpla alavggtvmt
       61 ltawvgtvva ygttgrsarr fgagdraaav aegvqaswla latgvlvava igigggalar
      121 tlvggpgeva daaagwlria algapgllla aagngwlrgi qdtrrpllfv lgpnllsavl
      181 cpllvypagl glvgsavana vaqtlsgvlf aaalvrerva lrprprvigq qlvlsrdllv
      241 rgvafqasfl satavaarfg aaavgahqia lqlwfftvlv ldalaiaaqs lvgaalgagd
      301 aagarflarr iallgglcgv afavliaaga glvpswfssd pqvreqamta wpwfvalqpi
      361 ggvvfaldgv ligagdvryl rnltivcafg gflpaiwlay afdlglggiw agltlfvvlr
      421 laglllrmrs gawavvgavr
//
LOCUS       WP_457608951             124 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608951
VERSION     WP_457608951.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..124
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13306
     Region          21..91
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mdhrdgtgqa kadnpvepay relgdtlsri rraagltqre vadragvgrp tlaniekgrq
       61 rvlyhqlldi adalgtdpre llpppaatsp aldrlddlqs padvidwvrr glarggghdr
      121 gdeg
//
LOCUS       WP_457608943             388 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608943
VERSION     WP_457608943.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41896
     Region          24..385
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtrrtfpvav gaaalltvta lgvpaasatt tdarrpaada vqqrldglva ehgfpgalas
       61 vrrdgrvrdy tagvgdlrtg aaiprdarvr igsntktfta vvvlqlvgeg rvdldatver
      121 ylpglvrang ndgrritvrq llqqtsglpd yddvvfgeaq dlvdrrsdyf dprrlldeal
      181 tqsrhfppge rweysntnfv lagliiervt qrpvgeeitr riieplrlrd tywpqtgeqd
      241 lpgrlprgyv avepgapwid vtrmdpslgw aagqlvstps dlrtffeall agrllkpaqq
      301 aaltrtvpap dfeptgvwey glgiarhelp cgghawghgg diqgfetrnl sttdgrsavv
      361 avtalptsle mmeavtstvd aalcgtgr
//
LOCUS       WP_457608967             195 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608967
VERSION     WP_457608967.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..195
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20504
     Region          1..187
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mttlwirhgt sldgitrpha harpdtplta rgaaqiaata halrdrgvrp aivltsphlr
       61 aatsaeilaa mlgarlatpn plyaewrapd cvlgkgpdey pseyqtwrtd rlrdpnsala
      121 ggesltalye rataasailg hagkgstali vshrmligav aaitagasrp qdvfqaarrf
      181 tlapagiwpa laelr
//
LOCUS       WP_457608965             238 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608965
VERSION     WP_457608965.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..238
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=26726
     Region          15..236
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 msvaealpdt mligdlhfav resprratvg itvdrdgsly lqapsgcppd alaawayskr
       61 mwvyrklaek dlllsarpak efvsgegfay lgrshrllla dtdevrmerg rlllprkaaa
      121 gpdpsgylvr wyrargrqwl pgrirpwtdr mglfptgldv rdlgyrwgsl sangrlnihw
      181 atlqlppsli dyvlvhelah vahpqhtaaf wamverampd yerrksdllg agarlwmg
//
LOCUS       WP_457608964            1086 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction endonuclease subunit R [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608964
VERSION     WP_457608964.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1086)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1086)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1086)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1086)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1086
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120802
     Region          10..1075
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mrfgpeyerv erplieqlvr lgwghteggr aasstttgrd sfrdillldr lraalrrinl
       61 nddsrewldd grinqaisql trpqatalle ineelterll rgatvdgvdg wdggrvrtvh
      121 fidwaslnpl arndflvvnq frvdppggra piwpdavlfv ngiplvvvea ksptapdpvg
      181 saveqlrrya nqresvepeg serlfhtnqf vvatcfetak agtftglveh yaewkttapm
      241 pegdveaslg vahlssqqrl vagmlhparl ldlvrhftlf mqpedrkvkv iaryqqyrav
      301 rttierlltg ptraqdgehd rrggiiwhtq gsgksltmvf lvramrshpa lvgfkvvvvt
      361 drkdlqkqla etaeltgetv rtatkvakak ellgipgkal ifvmvqkyrn pqakktddaa
      421 lknigeldks aevlvlvdea hrshsnalha alqkalpnaa rvgftgtpii mgakkkthti
      481 fgeyldrydi rqseadgatv pilyegrttr ggindaddid efidlyglth eqteelkkry
      541 atkrhvaeae qliaakaanm lrhyvevvlp ngfkaqvvst srlatvryrt aflaardali
      601 aeldaldpaw ktpdalervd rltakrsllv rawpyrdvva qldfvpvisg tqndkapiae
      661 wtsgyeqvvd dfkkkklpmp gvpadqtspv amlivnamll tgfdapreqv lyldkairea
      721 dllqaiarvn rttsgksvgy ivdyygvahh laqaleayad ddidgaltsl ndevprlaaa
      781 haavrqlfag isdfstvaaq dtcvealaee rlrarfeaal kafnrsieiv lpsdkalpyv
      841 adakafgtia llarrryrdh tlfdvrvyge kvralidahv qslgitqkip pisitsadya
      901 ekvsgltspr akasemehai rhhinermdt dpahyqrlse hleqiisqlr dqweqlalal
      961 anflpvvtsg rtedsngldp gieapfhdli aqeladygrp vtaeiagplr qatidvvhli
     1021 rddirlvgfw dnphkreqlr raiiarldds rledgsdlfk yamlrpladr llelakhnhh
     1081 rlassp
//
LOCUS       WP_457608968             248 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608968
VERSION     WP_457608968.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..248
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26173
     Region          1..247
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msrpiavitg agtgigaaia arlsaafdli lthryddtnl aavveaarrd gaqthtvtgd
       61 ltaadtqtal ratieqhatq lavlisnaga ypripwsqtn lnvlrdqlel nlvthaaiir
      121 aatpafisnn ygrivavssv mtqlgrvdla gyiaaksgle glvralarel gphnitvntv
      181 rpgsievpae hsvvpdheam vrrqldrqci krrgqpsdva aaiaflttpe aefitgqain
      241 vdggwhls
//
LOCUS       WP_457608970             358 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 9 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608970
VERSION     WP_457608970.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 358)
  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 358)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..358
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38565
     Region          <133..324
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtlveepvch rggrylvrre qaplgrllpy rrangerppr rarldavrqt gwrvdfgsrg
       61 lgdlllglam aqalqdathd qfgtlqyags ragliarctl pvtvtggdgh qlgtlgsdna
      121 lefdavpeap ptlldlidtd tvevhaalpm ryyldveqsl gvrlpasadp sprfrssvaa
      181 pkpfhvifva ttsrpdrkdy gidnfgalae hlsarhsgaw rfslvtppdh qppasvgqie
      241 vlhgptavec idlfaaaelv igndtglthl aaltiradgt qphvvglygr hgyakwitgs
      301 aghhavatpf shlmsvadac pvrdryddtl wsmgsdlrai pakviadfag qcagwwtr
//
LOCUS       WP_457608976             226 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608976
VERSION     WP_457608976.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..226
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24349
     Region          10..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtasipqlpl rdelfllghh ddtgqphlhr qalalgmaga vlidlflagr vtldsygdhs
       61 aadrwlrlns dqavgdliad talaaihhsr ttptvkaflr sfaddlyert raglvaagil
      121 rhtarrrlag lvradaylat dtkwavvara rlrylaagre qpdnhtaala glvavlglae
      181 hlyldddttt ltahlktiaa qhhrpireit aavdaaigdl atatyr
//
LOCUS       WP_457608977             468 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457608977
VERSION     WP_457608977.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..468
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49396
     Region          11..441
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mttsndlary gyrqelsrql rfrdllaygl vymvpiapma ifgsvyagsg gmvalayavg
       61 vvalvftafs yaqmvkafpm sgsvynyagr gisppvgfla gwvilldyvl vpgllylvas
      121 vamhatvpav pvwlwllgfv avntivnsvg irmtavvtrv mlvgelivla vflavagwal
      181 atgkgrfswd afynsdtftw svvagavsia vlsflgfdgi smlaeetrdg arqigramaa
      241 vlvlagvlfi aqtwlaamlv pnpgallaeg dvngtafyda aavagggwla tvcavataia
      301 wglpnsmvaq vatsrllyam ardrqlpafl akvsvrrsvp inatlltgvv slalglymat
      361 radgitllss linfgamvaf lvlhvsvvvh hlirrrsgnw fahllmpaig fvilayvvvn
      421 aniaaqrlgl awlalgmvvl aglyltgrrp vlsglaptqa agrdmerv
//
LOCUS       WP_457608978             489 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608978
VERSION     WP_457608978.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..489
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=51878
     Region          30..122
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 marttgtkaq rdhvrqtltd fgatptaiaa elqrrfglrp rdafrqahgw tqdavaerln
       61 akgngsatft garisdyerw pfggrrptla alnalaqvfg tepsslvdld dltampeadr
      121 aalsgrsaap mpapsvassa ppgavaeplr wdlgalqdet elviamaert asfgawaqas
      181 nvgpftlddv aastrriavd ylteppvvvy araglladrv frllqtgrqn pdqsrelytw
      241 agylctllaw magdlghpaa aesqartawm caetvrdstl rawvlstvsk thlwerrfed
      301 aanaavrgyg haaegsaavm lacqeadawa eigavepara alqraeearq qasrdpvggl
      361 lacgtvrqhn yagsvllrig eaanaiehae halaeaaadp svaygtlaqi riwaaaahlk
      421 agsldgavsv lspvlalppe qrldplvhrl rgvgrniagn pslrasiear nvqaaiiefc
      481 atgaarqlp
//
LOCUS       WP_457608983             520 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457608983
VERSION     WP_457608983.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..520
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=58565
     Region          28..420
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mvrrkarsgd rgrfdskdal laggsdvral ryqrasqdkk eqgksvhdqg vlnlaeitkr
       61 swtdagsftd nhrsasrrat kereqfelli eqiragkgdv lvvweisrke rdlavfvkir
      121 dmchevglnf wlvggvlydl rdkndrmmlg fqavqaewma dsirdnvlrg ivgaaeagrp
      181 hgkvtygyrr iydqrtrall rqepdteirt avaadgtvte ysraqvvrdn frkvsegtpl
      241 taieaelnrl gipasegglw rrgilrkqvm npayigkrvl rgeivgdgiw palveeetyw
      301 svvrmlgdps rtttrparav hllsylvrcg vcdgplssqk vnrhgwtgqv ysclhkrcaa
      361 vkaeyldeyv qrtvvawlsr pdvydiltaa satdedvaha raeaqrlrge ledwrklgee
      421 gevtaiayar aekgllaqia eheqraadag ipavlrgrig deavqawqel sddiavkrei
      481 irlvadikll ragfkgerrt fgrhrldwrw kfgpqdqqaa
//
LOCUS       WP_457608984             145 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608984
VERSION     WP_457608984.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..145
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16528
     Region          6..145
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mkaedeqafr efvtsqmasl rklaymtcgd whtaedavan alvklyprwr klerpdlyvk
       61 tmvyraaide trrpwrrers agdampdvtv rdtaavtder mrlraaleav parqrtavvl
      121 rhyldlsled taavldctvg tvknr
//
LOCUS       WP_457608985             272 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608985
VERSION     WP_457608985.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..272
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27789
     Region          22..259
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mlavvcllvl aglpagssda gatgpgtlrv lqmnlcnsgr agcytgravp raadviaaea
       61 pdvvtlneic rddvatlert lraaraggtv vsafqaagdr psggptrcdn gepygiglla
      121 rldgrdarss vhrgtypaqd ladpeervwl cvrgdglhac tthlantsgq valaqcgqll
      181 gavvpetrgg agnaptvlgg dlnlraggtp dvrscvpvgy rriddgarqq imasggvtic
      241 crravdmrgt tdhpalvatm igswpepppg py
//
LOCUS       WP_457608987             334 aa            linear   BCT 27-JAN-2026
DEFINITION  acetamidase/formamidase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608987
VERSION     WP_457608987.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wyborn,N.R., Mills,J., Williams,S.G. and Jones,C.W.
  TITLE     Molecular characterisation of formamidase from Methylophilus
            methylotrophus
  JOURNAL   Eur J Biochem 240 (2), 314-322 (1996)
   PUBMED   8841393
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mahenthiralingam,E., Draper,P., Davis,E.O. and Colston,M.J.
  TITLE     Cloning and sequencing of the gene which encodes the highly
            inducible acetamidase of Mycobacterium smegmatis
  JOURNAL   J Gen Microbiol 139 (3), 575-583 (1993)
   PUBMED   8473863
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..334
                     /product="acetamidase/formamidase family protein"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=35668
     Region          3..315
                     /region_name="FmdA"
                     /note="Acetamidase/formamidase [Energy production and
                     conversion]; COG2421"
                     /db_xref="CDD:441971"
ORIGIN      
        1 mshftyrpar delaytfggr lpvahlrsgd litvhtedcf gglvrgpadl psqvcqmpyl
       61 npvsgpffve daepgdtlav hlvaiepard wgvsatfpyf galtstshta tlqppleerv
      121 wvygidrqag vvryratasd hmvelpldpm igtigvapag mesrstivgd yyggnldtpe
      181 lragttlylg vnvhgamlal gdgharqghg eacgvgveia tvttlaievi kgaatarprl
      241 etdktimsvg carpledayr mahqdltawt vhlcglqvld ayqlisqagr apignvcdpn
      301 ytvlaaidka llpqpqaayr daharlrdia avqe
//
LOCUS       WP_457608988             281 aa            linear   BCT 27-JAN-2026
DEFINITION  carbon-nitrogen hydrolase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608988
VERSION     WP_457608988.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..281
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29063
     Region          11..268
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(47,126,130,133,158..159,161..162,183)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(47,126,158)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(127..130,132,139..141,159,161..165,168..169,
                     194..195,197..199,201..202,223..224,266..268)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mtalparplt vaavqaqpvp gdvagnaraa arlvgraega rvvvlpelfl payhpptlga
       61 dpegtdvaad aggrvsdarl dplrsaaada gaavvigaav rhpdrrrtis slvvdpagtv
      121 taaydkqqlw sgerelfdag rrgatlevdt wrlglgvcyd gcfpeharaa ardgahgylc
      181 psgylvgsah rrdlyyaara ldntmyvvfa navggadpwr fnggaavydp egrplargad
      241 tgedvlvatl dpdalaatra ahtmlrdrpl dagaaravlv a
//
LOCUS       WP_457608992             381 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457608992
VERSION     WP_457608992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39140
     Region          57..360
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mtstpteiap aapsplrrll pgapagrdar gstllrhlav avfagtlvvl vtnqlapyqn
       61 lqvarvcafl cvtaghtvlv glngqlslgh galmatgayt valtqqalde ravrgwwtlp
      121 asllvavavt algglvvgla aarlrgpyla gvtlavatlv pavttiftgv fngeqglrfp
      181 aqtppaalga yfqperwlaw ialaaalltm lllvnlvrsr fgrslravrd devaarlagi
      241 pvartqvlaf vvsaacaglg ggvyamltat vapgkfpldl slfllmaivi gglgslagav
      301 wgavllvalq dlpglltehl slsaglaqrl egnlalavfg lilivvmlaa pgglqggvra
      361 vgarlraalr rrratrrspd r
//
LOCUS       WP_457608995             596 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457608995
VERSION     WP_457608995.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 596)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 596)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 596)
  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 596)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..596
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63516
     Region          26..595
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mdripdgrrd grtvspaeka qardvslrri gglftahrgp latvvaiiva ssiiamatpf
       61 llrtvidral pgrdltllaw lvagmvtvaa vtavlgvaqt wistrvgqev mhrlradvfa
      121 hlqrqsigff vrtrtgevqs ritndiggmq avvtstatsi aanlttvvat tvamlalswr
      181 ltlvsavvlp palwltrrva rlrreitaqr qreladltvt ieeglsvsgv rlaktlgtgp
      241 alvdrftass arlvdlelrs elagrwrmaa msivfaaipa viylsaglpg tagtltigtl
      301 vaftalqgnl frplmgllnv gvtltaslal farifeyldl pvevaeparp vpldpatarg
      361 hlrvedvtfs ypgsdtaala gvsldvpagt slalvgetgs gkstlaalis rlhdpdagri
      421 tidgidlrdl rpadlaavvg vvsqetyllh gtvrdnlrya rpdatdadie aaaraarihd
      481 lvtalpdgyd tmvgsrghrf sggeqqrlai artllrdpri lvldeatsal dteteravqr
      541 aldelargrt vvtiahrlst vrdadriavl dhgrivesgt hdalldrrgr yaalvg
//
LOCUS       WP_457609001             388 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609001
VERSION     WP_457609001.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..388
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40584
     Region          8..271
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msaggpprva liganghgrw hrrtiaglha agrarlvalv dvrpleaepe apvppeaavl
       61 tdhrdmlaac rpdvvvvctp phthlpiald vlaagadlll ekppvldlae hltltgaada
      121 agravqvnfq algsaaltel tgalgrlgpv tgiatlaawq rpdayyarsp wagrrtvdgr
      181 paldgalanp lahalmqcla vaesvtgapv rparievery rvrpievddt tvlrltphag
      241 ppvlaaltla aeehvpgevl vtgergrall eyptdrlrlp gddaprpvpg rrgllanlld
      301 hradgtplia plartepfta vldalrdapv ptlldgdlvr eagdgpqrvr mvrgvgavlr
      361 aaartgalps eaavpwavkp hvvdlpmq
//
LOCUS       WP_457609002             494 aa            linear   BCT 27-JAN-2026
DEFINITION  mannitol dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609002
VERSION     WP_457609002.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..494
                     /product="mannitol dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=51335
     Region          7..492
                     /region_name="MtlD"
                     /note="Mannitol-1-phosphate/altronate dehydrogenases
                     [Carbohydrate transport and metabolism]; COG0246"
                     /db_xref="CDD:440016"
ORIGIN      
        1 maltsdrlgl atlrhlppes rpllrpgtvp agivhlglga fhrahqavht eaavgaaggd
       61 wgvigvaprs tdvvdalaaq dclfsvttla aggaatrvvg alagvrhaas dpdavaalla
      121 dpairvvtlt vtekayrldp vtaaltvdad ltadlttgrp prtvpgllvr gllaraaada
      181 gpialvscdn lpangrrlrg lveqclalar vpdataervl tavtcpgtmv drivpastde
      241 trdtarralg vtdlaavaae pwsqwviedd fpggrpawer sgailtgdag pwerlklral
      301 ngvhsatayl galagaetva ealtlphlda vlrrllaeei apsftpppga dvagygeqvl
      361 arfgnpairy rttqvamdgs qklpqrvlqt vadlraagrs arwsalvvaa wlrfllgyad
      421 dgrplplddp ladrlraala agahtpagvv davfalrevf padlaadeef radvtgwlta
      481 lerhgvratl adar
//
LOCUS       WP_457609004             447 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609004
VERSION     WP_457609004.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 447)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 447)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..447
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48042
     Region          57..359
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mhpatsptag apagrdhrtp ltrrrlvrgl aaaalavpla lgaagcgdds aggdggpvkl
       61 svfwwggear akltedalal ytkkhpevtf ektwqanqgy fdklatltag gnppdlfqid
      121 dnylaeyagr sttldlssyr dsgkldvskf pkslleygvv dgklagvaag entqglvynk
      181 tlltrnglpe pttgmsweeh iawaeqvakk tkvpgtqdps adykalwvwl rqqgkdlykg
      241 kelgftaedv tkwfelwkga rdrgatptpd vihegnssdi tkqlvvtgks atswvwvnqm
      301 pdlkkntkde lgvvaypgdp saqwarasmy wsvfkgskhk dvavdvinfl nndpeavall
      361 gtdrglpsnm dlrakvseta tdpamkqsiq vesdlaqkfg aspqvpikgh skvkselvka
      421 aenaqygrat paqaaeqfva acksaia
//
LOCUS       WP_457609008             331 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609008
VERSION     WP_457609008.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..331
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33423
     Region          8..297
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(39..40,43,95,108,110,139,172,257,260,296)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,248,257..259,262,284,288)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 msptggpevv cvgetmvvla pddggrleha arltvgvgga esnvaaglar lghraawvsr
       61 vgddpfgrrv vaevaaagvd vslvtvdrda ptglylkdpg pdrtrvhyhr agsaasrlgt
      121 adlarpglag arllhlsgit aalsgtcrdl lvsaldgral pgarvsfdvn hrpalwpadr
      181 agpvlrdlad radvvlvgld eaavlwsagd pagvrallpg pelvvvkdga vgatalprtg
      241 pavvvpalpv dvvepvgagd afaagflsgl lrgldlracl rlghltaapv lavpgdtapp
      301 pdaetiaral alpdeawped ararvrggsg r
//
LOCUS       WP_457609005             289 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609005
VERSION     WP_457609005.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 289)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..289
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32030
     Region          1..289
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtaltvarrr pgsgrnvlrl vvlvaivavv lyplfwmlgt svksqaeivn nvgllpeeft
       61 pgnyldgwtn fdisfgrffl nsmlvsgltv vgnalsclla ayalgrlrfr lrklwftvmi
      121 gtlllpghvl ivpqyilfrs lglvggdwpy lpllvpqfla teaffvflmv qfmrgiprel
      181 deaatidgas pygvfrhvil plsrpalvtt aifsfiwtwn dffrqlvfls slddytvpva
      241 ltlfidstsq ssvgpmfams vlsllpvflf flafqrmlve gintsglkg
//
LOCUS       WP_457609011             495 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609011
VERSION     WP_457609011.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..495
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51182
     Region          82..495
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 magrlvhadq vllhrlllvt grpraalsps trtadagfdt pgrvnpagsg vrrrvrrhrv
       61 vvvgagfsgl acalaldaag aqvrvleard rvggrtlsrp lpgggwldlg aqwigptqdr
      121 myalvaaygl ttfsspahga aalllggrpa tgeppglsal lgtldemaga ldpaapwraa
      181 eaalwdritf ggwldasaad pvtagyagrm laggllaasp devsllhmlf ylrsgggtgs
      241 llrmaggaqq driaggpaal aermaaalpp gslclrapvd gvaqdgdgvr vrsggetyhg
      301 davvvalapt lagrirydpp lpplrdgltq rmpmgvalkv halypepfwr adgrsgvsst
      361 dtgpltetvd nslpdapggv ltafsygtqa ralrrlpeda rrdalceala aifgpaaarp
      421 ddlveydwsa dewtrgcfcg vlppgawcay gpelrtpvgr vhwagtetat rwsgylegav
      481 tageraaaea laqlg
//
LOCUS       WP_457609016             851 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional acetate--CoA ligase family protein/GNAT family
            N-acetyltransferase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609016
VERSION     WP_457609016.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 851)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 851)
  AUTHORS   Sanchez,L.B., Morrison,H.G., Sogin,M.L. and Muller,M.
  TITLE     Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming)
            gene from the amitochondriate protist, Giardia lamblia
  JOURNAL   Gene 233 (1-2), 225-231 (1999)
   PUBMED   10375639
REFERENCE   4  (residues 1 to 851)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
REFERENCE   5  (residues 1 to 851)
  AUTHORS   Mai,X. and Adams,M.W.
  TITLE     Purification and characterization of two reversible and
            ADP-dependent acetyl coenzyme A synthetases from the
            hyperthermophilic archaeon Pyrococcus furiosus
  JOURNAL   J Bacteriol 178 (20), 5897-5903 (1996)
   PUBMED   8830684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18515002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..851
                     /product="bifunctional acetate--CoA ligase family
                     protein/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.2.1.13"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0046356 - acetyl-CoA catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87819
     Region          17..154
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          188..845
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mttveqpldv llsdgttvql rqirpedape ivamhgrfse rtrylryfsp ypriperdlk
       61 rfvnvdhrdr eafvvlager ivavgryerl gpaspeaeva fvvedayqgr gigsvllehl
      121 adaagrhgiv hfvaevlpan gtmlrvfadf gyqvqrqyad gvvhlsfpia pteatlevqr
      181 grehrtears iarllaprgi avygasttgq gvgaallghl rdggfagaiv pvhpsaatva
      241 glpaypsaad agqdidlavv avppdavtdv vhdaaragah glvvisagfa esgpagaaaq
      301 ralvraahla gmrvvgpncl gvantdpavr lnatlapvlp aagrvgvfsq sgafgvalla
      361 easrrglgls sfvsagnrad vsgndllqyw qddpatdvit lyletfgnpr kfarlarrig
      421 rrkpvvalas larppgvgea paldaaavsa lfaqsgvirv dtvselldvg vllahqplpa
      481 grrvavvgns saltglaata caaqgltvag gyprdvgpsa gaaayaaalg eavadervda
      541 vvavfapplp gqladpvadf aaalpearvt gkpvvatfla glvpagvpay psveeavral
      601 grvtayadwl grppgvlpel advdraagha alrpdgadaa allraygidv vesvpagsad
      661 evlaaadrlg rpvalkaaap glrhrldlga vrldladaaa lrrayaemaa vfgaevlvqp
      721 mvapgvacvv elvedpafgp vvgfglggva tellgdrawr avpltdrdaa elvdepraap
      781 llrghrgaap vdraalvdll vrvgrladeq prvrsltlnp vlarpdgisv lhatvrtgae
      841 sprpdtgprr l
//
LOCUS       WP_457609025             189 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609025
VERSION     WP_457609025.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..189
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20805
     Region          14..187
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 migqvavrrf paltvstpri evrhlvaada eamdevfadr qtqrwlplad asgqidgraw
       61 ctelarqrrd sgdgdhwavv rredqrvvgs lwarrtdwga rltelsyaia pharghglav
      121 eavdavaial ilehgfqrve lrvaagnvas rrvaekagfs yegllrnagf vrgarvdlel
      181 wsfvaadlr
//
LOCUS       WP_457609027             457 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609027
VERSION     WP_457609027.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47637
     Region          27..411
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(37..38,41..42,45,77,128..129,131..133,136,156,
                     159..160,163,239,242..243,246..248,251,278,282,335..336,
                     340,344,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 meatvsdarp areapatfrd vfgqsefrai faantlswvg dylaraavtv lvlretdsva
       61 lsaaafaasy lpwlvggpll salaerhhyr rvmvicdllr malmalvamp wmptwsifal
      121 iflatlanpp sqaarsalmp hiltgdrlvv glsaftsagq aaqvvgylig atvaalnpnt
      181 allvnavtfa vsaaivrfgv rerppamtev hrshllretv qgfrivferp vlraiavlvf
      241 samlfsivpe glaagwaadr tdgrmdagta qglimaavpv gyilggltis rlvgpdrrlt
      301 lmrplmiiap atlvpalfnp ppavvallaa gcgfavaglv pvanglfvqa lpdgfraraf
      361 gvmasgtqii qgaavlatga laerfsvpsv vgvwsaagvl imsvaalawp rpqviheava
      421 aaraesaagg gsahahapgp asgdrnrehg rrrhavt
//
LOCUS       WP_457609037             212 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609037
VERSION     WP_457609037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..212
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22158
     Region          2..165
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlfdmdgtlv dseklwdval qelaavyggv lsedarraiv gtgmadamri vhddlgqper
       61 dvqesadwis arildlfrtg lrwrpgalal lravrdagip talvtssgrs lvevaldtlg
      121 rdsfdavvcg devdsakphp epyltaarll gvpvercvai edsptgvasa laagaavlav
      181 paevplapad gvqqlesllg adlellaall nr
//
LOCUS       WP_457609034             254 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609034
VERSION     WP_457609034.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..254
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26332
     Region          27..228
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mpdrtelphv sngaddavrp gpsrrpveav lfdfhgtlaq veeplawvla aaaacgield
       61 riratsladr lltagraggp lparvpprla elwadrdlyp hahrgaytgl aetvdtgidg
      121 fadalyervl vpegwvpypd tapvlgalrs vgvkvavvsn igfdlrplfa awdldglvda
      181 yalsyevgrc kpdpgiflra cgmlgvdper tlmvgdtpad agavaagcgv lvlpcadagr
      241 pnglgavldl agaa
//
LOCUS       WP_457609039             108 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609039
VERSION     WP_457609039.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..108
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11217
     Region          1..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrtlhhsqal srfghalsdp lrarlllalr dgpgypaela ealgtsrqnl snhlaclrgc
       61 glvvavpegr rtryeladar lahalgdlvg vvlavdpavc paaadgcc
//
LOCUS       WP_457609047             320 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609047
VERSION     WP_457609047.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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   2  (residues 1 to 320)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..320
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34222
     Region          2..320
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 marhaqvsrq tvsnvlntph ivredtrrrv heaiaalgyr anqaarqmrt grsrliavri
       61 eptrdgings vldrflhglt etadaagyrv llytargdeq eiatyddllg aydldafvlt
      121 gtkhgdprta wlaerevpfv tfgrpwdtpe ahpwvdvdga agtaqatrhl laaghrriaf
      181 lgwpagsgvg ddrragwrtt maeaglegaa pdratedgit egeresrall aldvpptavv
      241 casdslalga wqaardtead lavvgfddtp vaaavglssv sqplgeaaar cvqlltglld
      301 gqqrdpqlll hpslvlrhsa
//
LOCUS       WP_457609048             415 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609048
VERSION     WP_457609048.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   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 415)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Domain dislocation: a change of core structure in periplasmic
            binding proteins in their evolutionary history
  JOURNAL   J Mol Biol 286 (1), 279-290 (1999)
   PUBMED   9931266
REFERENCE   6  (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   7  (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 11450659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..415
                     /product="sugar 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=43289
     Region          20..415
                     /region_name="MalE"
                     /note="Maltose-binding periplasmic protein MalE
                     [Carbohydrate transport and metabolism]; COG2182"
                     /db_xref="CDD:441785"
ORIGIN      
        1 mtprilaraa vagiaavall gsaacgsgfd dsaddakqss gpanlqilig ssgdaetkav
       61 kdaaaawags sgnsatvtpa qdltqqlgqa laggtppdvf yvdaarfady asvgalepyg
      121 dkvsnpddfy eslrtaftyd gklycapkdf stlalqintd lwtkagltda dvpttwdqlt
      181 avsqkikakg qvaialgdtr drigaflvqn ggwlmssdgk qptadtpenl qalqyvksll
      241 aagyakfpkq ldsgwsgeaf gkgkavmtie gnwikgalqn dfpnvkykvv plpagpkgqg
      301 tlsftqcwgi aakskykeqa ikfveamtag eqqigfakaf gvmpsrqsvr dqytgafpad
      361 kpfidgveya qgpvnapkmd svlrdleagl qglatgdpkt ilstfdknak aalgg
//
LOCUS       WP_457609049             372 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609049
VERSION     WP_457609049.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40735
     Region          16..334
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttdtlaspg tapagrprrr tggirsneni agwlfvapvi vilglflllp ilmalwvslt
       61 dwngqgspft gdvpfvgadn ysrlftedgl arrdfmtair nniyyvgivv pvqtalalgl
      121 alvvnnrllk gksffrsafy fpsvtssvai svvflflfan sgavnrllal vgidgpewfa
      181 dgrgvlhlvl gafgldsppa altsggpfgl swwewlsgps vamtsiiclv iwttsgtfml
      241 mylaalqnvp valdeagmld gasrwqrfry vtlplikptt flvvtlglig swqvfdqvyv
      301 msqgdpaktt ltpaylsyrt afrdfdygsg aaisfvlfli iilltlfqrr lmadrdeprr
      361 grwrrrrvpe gs
//
LOCUS       WP_457609054             270 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM hydrolase/SAM-dependent halogenase family protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609054
VERSION     WP_457609054.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kornfuehrer,T., Romanowski,S., de Crecy-Lagard,V., Hanson,A.D. and
            Eustaquio,A.S.
  TITLE     An Enzyme Containing the Conserved Domain of Unknown Function DUF62
            Acts as a Stereoselective (Rs,Sc)-S-Adenosylmethionine Hydrolase
  JOURNAL   Chembiochem 21 (24), 3495-3499 (2020)
   PUBMED   32776704
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Deng,H. and O'Hagan,D.
  TITLE     The fluorinase, the chlorinase and the duf-62 enzymes
  JOURNAL   Curr Opin Chem Biol 12 (5), 582-592 (2008)
   PUBMED   18675376
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Eustaquio,A.S., Pojer,F., Noel,J.P. and Moore,B.S.
  TITLE     Discovery and characterization of a marine bacterial SAM-dependent
            chlorinase
  JOURNAL   Nat Chem Biol 4 (1), 69-74 (2008)
   PUBMED   18059261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004885
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..270
                     /product="SAM hydrolase/SAM-dependent halogenase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27112
     Region          6..261
                     /region_name="COG1912"
                     /note="Stereoselective (R,S)-S-adenosylmethionine
                     hydrolase (adenosine-forming) [Coenzyme transport and
                     metabolism, Defense mechanisms]"
                     /db_xref="CDD:441516"
ORIGIN      
        1 mpvasisltt dyglsdgfva achgvlarla pavrvidvth lvppadvrrg aavlaqtvpy
       61 lpwgvhvavv dpgvgttrrg ialaapggll vgpdngllip aaealggvte aveltnpdwl
      121 gpvvsrtfhg rdvfapvaar lalgapptea gpavdpgtlv rlpepvvrae pggfsaevlt
      181 vdhfgnvqla apgtlleglp srvlvnghea vhgrtfgdae pgalvvyvds aaqvaiavnt
      241 graagtlhtt pgalvtitrl prdlavgapa
//
LOCUS       WP_457609062             406 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609062
VERSION     WP_457609062.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..406
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44498
     Region          1..405
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtdvgealtr vhrqewarvv atlarrigdl dvaeemtaea faaaverwsa dgvppnpgaw
       61 ltttayrrav drirresrrd dkhrealmla dvpeplgvid ddrlrliftc chpalamdar
      121 valtlrlvgg ltvpeiaray lvqeaamsrr itraktkika agipyrvpsr edlparvagv
      181 lavlylifne gylasdpare avradltaea irltrlvrtl lpddheaagl lalmlltear
      241 rparvsatge lvvlaeqdrs awdrdliaeg halvraciaa grppgryqil aainavhtda
      301 rdardtdwaq iaalydhlvr vdpspivrln ravavaeldg pqvalaevdg lplegyhayh
      361 atraellrrm grggeartay draielagns aetaylsrrr dqlgar
//
LOCUS       WP_457609097             294 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609097
VERSION     WP_457609097.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..294
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30251
     Region          19..279
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mqsrsqgrrl davpgpftpr tprvvaarrl qrrrdrdqag rflaegpqav realdrtgtv
       61 velfgtpaal dryadlaaaa aradvpvsev tddalaalae tvapqglvav crhldvpleq
      121 avaraprlva vlagirdpgn agtvlrtada agagavvfag eavdpyngkc vrasagslfh
      181 vdvvraadpl aavealraag ltifattgyg dsdlddlads grlaaptawl fgseahglpe
      241 eltgaadarv rvplhgraes lnlaaavavc lyssaralrv prgtretage sass
//
LOCUS       WP_457609100             320 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609100
VERSION     WP_457609100.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..320
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30742
     Region          9..154
                     /region_name="ydcZ"
                     /note="Uncharacterized membrane protein YdcZ, DUF606
                     family [Function unknown]; COG3238"
                     /db_xref="CDD:442470"
     Region          173..279
                     /region_name="ydcZ"
                     /note="Uncharacterized membrane protein YdcZ, DUF606
                     family [Function unknown]; COG3238"
                     /db_xref="CDD:442470"
ORIGIN      
        1 mrplplpaal avvvaggvas aaqgavnaem gertgapvlg avvnnlggcl lvlagivalp
       61 smraglaglr rsglpwwayl ggvggavivl vapvvvpvlg vavftiaqva ggslgglavd
      121 raglaatgrm pltvprvgga vlgvgavala qlgrpvgdla vglvllcvlg glavatqsal
      181 ngrvaatvgp aaglavnfav stvvigavaa ltgalasqpr wpgqwwlyvg gllgvgivls
      241 llvgvraagv lrtglalvag qlggallldl vlpggpgvrl pvlagalltl lavvvtslrr
      301 ggpdrvaaeg arepdgrlvg
//
LOCUS       WP_457609123             686 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609123
VERSION     WP_457609123.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..686
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=71401
     Region          2..662
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mlviwlviaa agftvgngvf armttsvgai agsesqqgaq algdaklapp vinavisggs
       61 vtdpafrtkv saaltelrav dgvlavtdpf gpqapvatdg aavlvnvela hqgdlladkv
      121 rtqltgidgt ttvvsggplt drefndqats dtrraeivsa pllllllllv fmsliaaglp
      181 llialvgvgg tfttllvmsf ftdvsiysiq vttmlaiglg vdyallmvsr freeralted
      241 aeealvrase ragrtivfsg ltiavslasl vvfadpflrs igvagaavvl idmlaaitll
      301 pallqllrnr ikpvrarker grsfaavarg vqkmpvltll vvlvgllvag lsatnlrldt
      361 snpkslpads atrqlteelr ehfpalagps aitivartsa ddpdlaefrq rvaavpgisv
      421 vnpgrsgggl avlqatpenp tsdpdtarav rdirdldapf tvqvtgdaar lvdyqqelrd
      481 rlpiaggivl latfvlllaf trsvliplka vltnllslfa algvvvwvfq eghlvgllgg
      541 erldgidltv pvvvaaiafg lstdyevfvl srirerrfag aapdqavreg lqrsggivta
      601 aalllavtfa gfmtggfapi kevglglvla vlidavivrm llvpatmail graawwaprf
      661 lggrppvpsa pdagdaqpel tataqg
//
LOCUS       WP_457609133             573 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609133
VERSION     WP_457609133.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..573
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60744
     Region          34..400
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 maaptlplaa avarhlderl gdpddadvvf nharvaaade setfpaeica hldrlglpah
       61 yvpaayggel rgfdilvqvl rvvarrdltt aighgktflg aasvwarspr deadlaqara
      121 lagtvlagvp vcwaltepgh gsdllggevs alrsdggyrv tgtkwlinna tragvvclla
      181 rtdpdggprg ftvlladkre lpahsyrclp gepthgirga disgitldda wvpetavvga
      241 rgagletvlr alqltrttca alslgaadha lalvrryltd rrlygrrlad vpylrrgvgr
      301 lhtmlflaea vtalvsraat aeteelgvla pvlkafvpal tdeliggcge qlgaravltg
      361 ipdygrfqkv erdhrivgif dgstpvnrna linqfpqlar gwpgdpvdva rlrsladlrv
      421 pvpeldpdrl slaagrgclp lrglaaavpa vraaggpaar aeallaatel lhtelagyrp
      481 rphdvepaay dlahryelcv agasavhlwl hnhehagadp lwvdglwlda altwvlhrlg
      541 vapdhpegyd rvyaslapdr rpsvldldga gea
//
LOCUS       WP_457609135             590 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acyl-AMP ligase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609135
VERSION     WP_457609135.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..590
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62952
     Region          13..564
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(169,172..177,179..180)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(196,216..218,292,295..298,323..327,332,374,440,451,
                     454)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mpdhetfvdl lqeraavhpe rpalifdvdp gsgdaevrtv swadlaarar qiavlladtv
       61 rpgdrvlvln epgtafaenf lgvqhagaip vpaplpdgyr rqrdrlagia hdaqvaavvt
      121 daaaldavrd waaecglsav pclafddvpl eratawrrpa vdgatiaflq ytsgstsdpk
      181 gvvvdhanll pnlrafneil gggegvrvgg wlpmyhdfgl igqllaplsr ggcsvgmsat
      241 tflkrpgtwl rlidrhdiei spapnfaydl ctrritdeqi agvdlsrwkr avngsepvqa
      301 atlaafgsrf aaaglrpdam cpgyglaeit lsvsgatigr ppvvltvdae elernivtpv
      361 gaghpepvre lvssgestpe fdirivdpat rlpqppdrig eiwlrgtsva rgywanpeat
      421 revfgnelad geggflrtgd lgllrdgqly vtgrikelli vngrnlyphd ievtvravde
      481 slsrgvgaaf tvevpheelv vvqecrarsl dpaaraavvt avrhvlsref gtgavsvvlv
      541 rpgtvprtts gkiqrglarm lfltgalgae heeltdgvra arrtgdpvra
//
LOCUS       WP_457609141             222 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609141
VERSION     WP_457609141.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 222)
  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 222)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..222
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24175
     Region          4..198
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mriviaddav lireglsall rqagmtvlaa vkdahellda vaghrpdavi vdirmpptyt
       61 teglavaeri rrdysgiavl vlsmhietey alaivnsgeg gvgyllkeri ldveqvvtal
      121 relasggavi dpalveelma rrrtggridr ltvreqevla lmaqgltnra iadrlrlssk
      181 tiesyvtsil erlqidsaeg vhrrvravlm ylrsntsagw ep
//
LOCUS       WP_457609145             253 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609145
VERSION     WP_457609145.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..253
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27495
     Region          17..251
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mttpdtdngl wvrrfhpapg garrlvclph aggsasfyfp vsralspave vlsiqypgrq
       61 drrhekcigd ihdlarevft vlrpwrdepl aifghsmgas lgfelarlie qdggsvahlf
      121 asgrrapsks rhetvhlldd eglladvrkl sgtnsavlgd pemlraalpa irndyraaer
      181 ytyrpgppls cpitvltgdd dpkttveear twsdhttaaf dlkvypgghf flaehqpail
      241 raistalsaa tav
//
LOCUS       WP_457609144            1855 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609144
VERSION     WP_457609144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1855)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1855)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1855)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1855)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1855
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1855
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=193314
     Region          3..31
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          33..1427
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1221..1669
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1422..1423,1425,1446..1449,1474..1477,1501..1503,
                     1524..1525,1547..1548,1562,1589..1590)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1525,1549,1562,1566)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1685..1767
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 mmdteeklre ylkrvtadlr rtrqrlrdve adaqqpiaiv gigcrfpggv rtaeelwdlv
       61 asggdaiasf ptdrgwdlda lydpersrpg tssvreggfv adaaefdprl fgvspreala
      121 mdpqqrlllq tsweavetag idptslkgar vgvfagmths gyahppetpp agvedylglg
      181 nagsiasgrv aysfgfegpa vtvdtacsss lvalhlavqa lrsgecdlal aggvtvmptp
      241 avfvdftrqg nlspvarcra fadaadgtal aegagvllvq rlsdarrdgr rvlavvrgsa
      301 vnqdgasngl tapngpsqqr virqalanar lgvadvdvve ahgtgttlgd pieaqallat
      361 ygqgrdvpll lgsvksnigh tqaaagvagi ikmvsamrhg vvpaslhvdv psshvdwssg
      421 avelvtasre wpgvgrprra gvssfgisgt nahviveqpe aeadlepvav pvgvpvpwvv
      481 sgrseralag qagrlasfvr srslspvdvs wslvtsraal ehravvwgsd vdelvaglsa
      541 vaeggsvvsg vvsagrravl ftgqgsqrag mgrelyetfp vfaasfdevc aeidrrlpra
      601 lrdvvfaepg tadgalvdrt vfaqaglfvv evalwellas wgvradylag hsigevtaay
      661 vsgmvslsda cvlvaargrl mqalpaggvm aavgaseeav aeliassgaa vdvaavngpt
      721 svvvsggade vasvvagcre rgwrvkelav shafhsrlme pmleefrsvv agldwqvprv
      781 pivsnvtgav adaaeitepg ywvrhvrqpv rfadavrtlh qqdvtqflev gpdavltama
      841 qdcveaagev rftatmragh seadtlrtal aeryvtgdhv dwtgylaald gsgperaaea
      901 rpraialpty afdqqrywln asagvetvpg lgvrpvdhal lgaavrvadd dvrvfgtels
      961 vlthpwladh vvwdsvvvpg aalvemvlha gaqvgcdtld eltlqaplal aedgtravqv
     1021 klgavdedgr rtvtihsraa adpdgewdrh aagvlapavp qpdrsdpapw ppsaatavav
     1081 dgiytelsrl gveygplfrg lravwrtgde vcaevavpdg tevagfglhp alldaalhvv
     1141 glldsdaeda sgvrlpfawt gvtlsavgat alrvrarrsg ggvaltltdp agapvarids
     1201 lvsrpvtagq vrggdsaadp lyalnwqsvr pgtpatvrvv llgdapsdls eiaryrlael
     1261 aeavgsgrid pelvllaayt ddedapvpaa trtrltavla avqgwladdr laerrlvvlt
     1321 rgavaagstc rtgdlpgaav wgllrsaqae hpdrfvlvdl dearqpesct vdlvaravat
     1381 gepqlavrde qvltprlapa vldpapaaal epdgtvlvtg atgalgglla rhlvsthkvr
     1441 hlllvsrrgt dapgaaella eltalgaqar lvaadvadrd rlaavladvp aehpltgvvh
     1501 aagvlddtvi saltpgrlsa vlsakadaaw hlheltrsrp lamfvlfssv agvlggpgqg
     1561 nyaaanafld glaghrhacg laatslswgl waadsgmtga lgaagrqrms rnglsplgtg
     1621 qalrlfdngl hggrphlvpa lldlaalrrq adagqlpapl rglvrarrrv vegggdggps
     1681 faqrlagtpe aergrlvedl vkaqvievlg yppatvvpsg qtftglgfds ltavelrnrl
     1741 taltgirlpa slifdcptpa aladfllvda appkpepgll aeldrleaaf aatapeeler
     1801 laaddetrta vavrlralvt rwsdttdrpd dvgqalddas ddelfdfidq kfgrs
//
LOCUS       WP_457609147             859 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609147
VERSION     WP_457609147.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>859
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          8..859
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 msvgfdgaqa adgavalelv gdlrrpavwp araasvhrvl pawpscvtpa ghvvvaglva
       61 vlarwtgqde vvlglapagg svarvdvsgd pgfgelaarv glawtapvag pdrpdpvave
      121 ctdgpvaetg pavvdvdmvv rvaadgsvlr vdyavegfsa qfvrglvdqv vvlvsagtaa
      181 pqvalsrlpl ldaaererll twgrgpvrei pgepihelvl swarrspeav agvagdevlt
      241 ygeldrrsgl laaylrsvgv ragdvvsval erglwslvat mgvlragaay tpmdvswpae
      301 rmrvlladhg arvvltvgav apripagdgv tvvalddgwp avpagavadl pavpvdapaf
      361 viytsgstgt pkgvvlsher lanflawmtg ecaigpgsrm lhsaapvfda afgeifaalt
      421 gggrvvvcpr ddlldarrlt dlvntqgvth tfgpatniap ldpaacpglr cvifggeavp
      481 prlaqrwlta gtrvvnaygp aeiavactwf dasagwggay vpigwpmpnr qvrvvdanld
      541 lmpagvpgei liagfgvadg ylnrpeltaq rfvtdpyggg layrsgdlgr wnsagaleil
      601 grmdhqvkvn girielgeie silaqhpeve tavvvrredr gmarlvayvt grdgrtpgtg
      661 dlrdhaaahl pgymvpaavv vldrfplggt gkidrsalpa pgaqrpdlgv pyvepatege
      721 rlvaevfasv lgiervgard sffhlggtsl qsaavavald eaadvvvpvs qihrtptphe
      781 larwlatapr rtdtgstagq trqrpgpvpl aqqvakclms plevvvpvtw wiegeldlra
      841 lmaalgdihh rhqalhary
//
LOCUS       WP_457609154             423 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609154
VERSION     WP_457609154.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..423
                     /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=45199
     Region          <185..373
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 msrtvtlvll daaggplgal ppfgvpepww qevhsivdtv rrryglevav lrlldadrpa
       61 ppgghvryla qvvdapavpl epagnalgvp lepvtvdlap hplrqpwaea ggparsvawa
      121 tgelrrlgrr vtavaqqrtw nlsaiwrldt tqgptwlkql ppfsrheptv ltfpgdqgvg
      181 vdvdlpgdtn slingpvvla adgegrmlla dvpgedryga gegeraavva ehhsvqlrac
      241 gvvdelvaag vpdlrgarla dwireglagh dvsaavgrlg hdlsaasall dgldrrlrqv
      301 gdcglpdtlv hgdlhpgnvr gddrrrtvid wadsfaghpa fdilrltedv dadaaarlvd
      361 awarrwrtdv pdsdprravd llrpvaplrl aavyamflaa iepgehpyhv hdvpaalara
      421 aaf
//
LOCUS       WP_457609153             286 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609153
VERSION     WP_457609153.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     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=31258
     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 mldrlnaald hleqrldqpl dvaelariag vsehhfgrlf salaglplse yvrrrrmtla
       61 gadvlagres lldvavrwgy gsneafaraf ravhgvgptq arqagavlrs qprmsfrlvv
      121 egntsmdyri vtkdafrlag ltarvplvhe gmnphivafv rgidpatvrr iealsdqepr
      181 givnvsaela gardegaeld ywyaavtgad vpddlrslpv eagdwavfss sgafpvavqh
      241 lwrvvftswf psnpyetrpg peisrvrvae dggtadaelw ipvrrv
//
LOCUS       WP_457609155             513 aa            linear   BCT 27-JAN-2026
DEFINITION  gluconokinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609155
VERSION     WP_457609155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..513
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - obsolete D-gluconate catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53638
     Region          6..485
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 mgdpavvvgv digttsskav afdttgrqla shsigyplee pnpgwaeqdp dliyqavlgv
       61 iravvdelrv pvaglsfsta mhsligldad gtpltpsitw adsrasaqae rlraapsgla
      121 lhrrtgtpvh pmaplpklvw faeqepklhe rvahwvgikd lvlrrladal vtdhsvasat
      181 glmdihrlaw dtealriagi teeqlpqlvp tthvlpgltp eaaratglpv dtplvvgagd
      241 gplanlglga vrpgvvacsi gtsgamrvmv erpgvdplgg vfcyaltedr wvvggainng
      301 givlqwanda lapelgehae eelldlaata pvgsggliml pyllseraph wsalprgayv
      361 glthghgrph lvraalegvc qqlalvlasv raagnevrev rasggfarsa lwrqiladal
      421 gmpvrfpagh egsgfgaall gmqalglies ievaadlvri eetvrpdpas aatyaallpl
      481 fselydalvp tfaslrrmap slppepppta ppr
//
LOCUS       WP_457609156             759 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609156
VERSION     WP_457609156.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 759)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..759
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=80292
     Region          85..757
                     /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 mslaaaapar hplvgrvgla aavvvvlgem awlaarlpga alvsdvgama vsswaavlcv
       61 gaarrqpatl rrfwqllsat mmlaalgrav wtgerlgglg lphtplvagl faagivtgtg
      121 allcsrtgpr sligrartll dgvivglali pigwvvvfhr itdaeladpm rtfgllypmf
      181 dlmqltilva vagpgrpmwr altvigagla irsgadavyv slvargdytp ghpvdvcwpl
      241 syllvglatr ypppsdgdge ddvvdsplpp wwrvalpylp vggaivavll srqpsgqtpq
      301 vvfigmmgll gvlalrqgla anenlrlvgr lrrlaysdql tglpnrltfv rrlrralrag
      361 gpvavvlldl dgfkqvndrf ghaagdrllt vtaermrdav gpdgmiarlg gdefavlvag
      421 erqvsperla vrllaalepl pgeedlgvhp sasigiaeyg pqhashtdll rdadiamyaa
      481 kaagkaayrt ctpelresav sraeliadlr ravdegqllm efqpivdldt gtvrsaealv
      541 rwrhprlgvl tparflplae etglivaidr wviheacraa atwrqhapdv tvavniaaah
      601 lcrpdliatv tgavgaaglp praltlelte saliegsesv ldrlsqlrdl giriaiddfg
      661 tgysslsylh ripatelkid rsfvsrldag darayatvem vnrlagafdl avvaegvetv
      721 aqhaavtaig crqgqgwryg rpaalpdllp alsgagaer
//
LOCUS       WP_457609157             165 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609157
VERSION     WP_457609157.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..165
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17768
     Region          5..82
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mtddpleird paqfkalahp frhrllfalg agpatlsrla arlgaakgtv ahhlavltea
       61 gmvrpahsrq vrggteryhe rtfrrlvgad tdasataall gayaeelaad pdplvhlrhv
      121 rltpaqaqrl rstldelvge aeeapsgqpr ygvlvslyrh ppavr
//
LOCUS       WP_457609158             317 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609158
VERSION     WP_457609158.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..317
                     /product="S41 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33447
     Region          9..299
                     /region_name="Peptidase_S41_IRBP"
                     /note="Interphotoreceptor retinoid-binding protein; serine
                     protease family S41; cd07563"
                     /db_xref="CDD:143479"
     Site            order(68,212,269)
                     /site_type="active"
                     /note="active site triad [active]"
                     /db_xref="CDD:143479"
ORIGIN      
        1 mdpdqitaiv eraaalvade yvlpdvadqi aghlrerlha gayaeagdaa tlgalvtadl
       61 qsanrdlhlr lkhhdqplsd etddptgehf arlaalgmgg vtrvqrlpgn vglleikpyv
      121 fppdlagdal taalrllagt dallldlrgt eggspdgval lcgwffaept hlhtmhersg
      181 atrqfwsaaw lpvpryapek pvhvltgpat fsggeelayd lqqfgratvv geptrggahp
      241 rvghrlhphl eltvpvarpv havsgtnweg cgvtpdlasp adgardvayr rsleallaad
      301 pdrptaaear talaalg
//
LOCUS       WP_457609160             461 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609160
VERSION     WP_457609160.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..461
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51781
     Region          27..450
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mhavrdhera vdtlrrsyaa vpagepvrla kqtsnlfrpr saprtpgldv sgltgvlavd
       61 paartadvqg mctyedlvda tlphglmplv vpqlrtitlg gavtglgies tsfrnglphe
      121 svremdvltg ageivttrpq gehadlhraf pnslgslgya trlrielqpv rryvslrnir
      181 ftrleelvda igevvakgaw ggepvdamdg vmfspgeayl vlgaftdead dgpsdytgqe
      241 iyyrslrrrt rdtltaydyl wrwdtdwfwc saafgvqhpv vrrlwprryr rsdiyhrivr
      301 lehrhqvaar vdrwrgrpar ervvqdvevp ldrtpeflrw faanvgmtpv wlcplrlrep
      361 sgpgsakawp lyplqpgety vnigfwgsvp iaagaadgdv nrqiermvse vgghkslysd
      421 ayydrgefdr lyggdtwrav kdrydpdhrl tglyekavtr a
//
LOCUS       WP_457609162             253 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609162
VERSION     WP_457609162.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  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 253)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..253
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26711
     Region          3..181
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(6,8,90)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(35,89..90)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            88..90
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mivlvpvyrp gdrlpplvgd lrdalpgadv lvvddgsgpa aaevldaara rgatvlrrrv
       61 nrgkgvvlrt gfryasthhp grdvvcvdad gqhgvpdvca vadrmrataa ptlgvrafdg
      121 evparsrfgn aatrvafrla tgrdvrdtqt glraypaall gwlttipgdr feyemtvllr
      181 lvraglpveq veiatryhgd nsgshfsala dsvriyrpla asalarlagr aevddvpaaa
      241 vttprpapas rtp
//
LOCUS       WP_457609164             449 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609164
VERSION     WP_457609164.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 449)
  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 449)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..449
                     /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=48403
     Region          116..420
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtrpglrarv taafavgall lsalmalfsy dltrrsllde rertavraay ydaavvrsgl
       61 dtgtpdvvav lrsldtgsar rpllhlpdgw yartadvgar svpvelqrmv adgkpavqri
      121 rldgqpallv gvplpgalgy yeltslreve etfqvvglal iavaimvaga gaalgwyatr
      181 hslrpltava daaeriaagd fatrldsttd pdltrlsssf nemvdklvhr ierdrrfaad
      241 vshelrsplq tlaaaasvln rrrehqdert ataaglvade vtrfqrlvdd liqlarteqp
      301 ahretvdvve lartvcrers lpeslvtvdg daprlwwvdr rrfaqtllnl lenaeryggg
      361 pvavrlagrd gvgvldvdda gpgvppgdre iifdrfvrgr aahdragtdg tglglalvaq
      421 haaahggtaa vldrepgarf rvelpgalr
//
LOCUS       WP_457609166             458 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609166
VERSION     WP_457609166.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..458
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48766
     Region          21..344
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msvpqyrkva avalaaglgl slaacstksd dssdaggkvt itvdcqpvga qkellknwnd
       61 dvaefqrqnp divvksvsvg eqcnnppdft arlaggtvtd vfygymtdlq qvldsgqamd
      121 igqyatkdti ptwdsvdpal kevftdggkl yavpvknysm gliynkalfq ragldvnnpp
      181 ktwpevraaa kkistlgdgi agyaeysagn tggwhftsll ysqggqvlsa dgkkadfnna
      241 mgkqvlqnlk dmrygdnsmg arqllqwgdl ltnagagkvg mfigapdatq aivsqfqgky
      301 qdwamgplpg qdgpakatlg ggegyffkkg lspeqvkagl kwlayqkltp gkgqfdyvra
      361 kpqnypvglp qpllftngsd aqkqelelrk ananvdttnf avfeanpvpi kgeprnaqai
      421 yavldaamsg vltnpnanid allktaedkv nqllaaqs
//
LOCUS       WP_457609167             295 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609167
VERSION     WP_457609167.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 295)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..295
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31996
     Region          17..295
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 maadsttrtl ishaqlrrgr grvlywvvlc vvvagftlvf lgplywmvtg alksgqeiaq
       61 tpptlfprdp qpgnyvdawt nldlakllfn tfyyaagavl fqlvfdtaaa yalsklrpvl
      121 grlilgmmla tlmipamvli vpqyvtvidl pivhvnllds pfaiwlplva nafnifllkq
      181 ffdsipedlm aaavmdgasp lrtlwsivlp msrpilgvva ifavtavwkd flwpklvmps
      241 petrtvsvgi yafaggtpmn vviaasviaa iptvvlflif qrnimsgltt gglkg
//
LOCUS       WP_457609170             478 aa            linear   BCT 27-JAN-2026
DEFINITION  cellulase family glycosylhydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609170
VERSION     WP_457609170.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..478
                     /product="cellulase family glycosylhydrolase"
                     /EC_number="3.2.1.4"
                     /GO_function="GO:0008810 - cellulase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030247 - polysaccharide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50721
     Region          40..139
                     /region_name="CBM_2"
                     /note="Cellulose binding domain; pfam00553"
                     /db_xref="CDD:425748"
     Region          184..435
                     /region_name="Cellulase"
                     /note="Cellulase (glycosyl hydrolase family 5); pfam00150"
                     /db_xref="CDD:395098"
ORIGIN      
        1 mfsiprpsrr hllaggavga lalaavavlp spnamaatgc avtyttsswp ggftasvavr
       61 nlgdpvsnwt lgftfpdggq rvvqgwsatw qqsgsavtar sldyngtlgt gasttigfng
      121 swtgsnpnpt sftlngtvct ggtstpppat tpppattppp ttpptgttpv aingqlqvcg
      181 vnlcnqygrp iqlrgmsthg lqwfancytd asldvlanew rsdllrvsmy vqeqgyetnp
      241 agftaqvntl vdkaeargmy alidfhtltp gdpmynldra ktffatvsar naakknviye
      301 itnepngvsw stirtyaeqv ipvirandpd aviivgtrgw sslgvsdgan sdeivnnpvr
      361 aqnimytfhf yaashrdnyr nevqraasrl plfvtefgtv tytgdgavdt assnawldll
      421 drlkisyanw tfsdapegsa alrpgtcasg sfsgtsvlte sgaymrdrir tadnfpts
//
LOCUS       WP_457609171             541 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609171
VERSION     WP_457609171.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 541)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..541
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59612
     Region          6..479
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(62,65,102,105,150,173,177,209,260,321..322)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(209,260,322)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          460..536
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 madnspwwrs aviyqvyprs fadgdgdgig dvagirsrld hlaalgvdai wfspwypspm
       61 adagydvsdy rdidpvfgtl aevetliaea halgirsivd vvpnhcsdah pwfqaalagg
      121 paaperdlfw fragrgpggd lpptdwtgef ggptwtrstd pdgtpgdwyl hlfapqqpdf
      181 nwdhprvrae fedilrfwfd rgvdgirids agllvkdgtl pevgpdrphp frdqdgvhdv
      241 yrawrriads ypggralvge vwlpdrqrfa nylrpdelht afnfdflgca wdatalresi
      301 dgtlaahapv gapatwvlsn hdvtrhvtry gradtrfsfa akregiptdl elgtrraraa
      361 allslalpga ayvyqgeelg lwevedipye lrqdpmwers grvdpgrdgc rvplpwqgdm
      421 ppfgfspdga taapwlpqpa dwkdrtvraq tgdphsmlel yrsaltlrra epalgdgtlt
      481 wlpapdgvla farepgltcl vnlgdaavgl paydrlllas gpldddrlpp dtavwlrtrs
      541 a
//
LOCUS       WP_457609173             199 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609173
VERSION     WP_457609173.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..199
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20659
     Region          51..>193
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mvdvaappar pvaappappa pavvprrtgr llglggralh rsaallalaa iwetvpragl
       61 vdrvflppls evlaawwell rtgqladhvg asltrsltgl alavvtavpl glligwyrpl
      121 adllspllev frntaalall pvfvlilglg etskialvvy acswpillnt iagvkgvdpl
      181 lirsarsmgl nhrpgsats
//
LOCUS       WP_457609174             272 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609174
VERSION     WP_457609174.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29354
     Region          1..261
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mstdkilfdr vrkvfpgrrg gggavtaldd ltlgvrpgef lvvvgpsgcg kstlldllgg
       61 laaptagqvl vdghpvtgpg ldrgivfqqy allpwrtaag nvafgleakg lpraeradlv
      121 ayhldlvglt gfadryphel sggmkqrvai arslaydpdv llmdepfaal daqtrdslqd
      181 elvriwqatg ktvvfithgi deavhlgqrv avmtsrpgri kqvidielgd rdaeedvrst
      241 dafrhhrhqi wtllrdevra aqsavreear vg
//
LOCUS       WP_457609175             520 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609175
VERSION     WP_457609175.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 520)
  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 520)
  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 12138572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..520
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=54437
     Region          <17..>211
                     /region_name="FxSxx_TPR"
                     /note="FxSxx-COOH system tetratricopeptide repeat protein;
                     NF040586"
                     /db_xref="CDD:468560"
     Region          129..204
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
ORIGIN      
        1 mssgfadltv qahhlvsegd ldgahrllad alsdadprpg naspelaeaa glqakvlval
       61 gephsargwa afayaaatrl ygrsdertvt aaatlaavlh rvgsdaraar lysdviielt
      121 ardgpesqqv laahadlatv eyargqceva rdrlqdawel hrevygdghp sgikmlaklg
      181 amerdcgrya dshehltlae elcrlhldfd dplaaqvaal araaadpdhv cpaptpapep
      241 pparttpvvp aarvppqaeg phdlppyspp aldepvetpl yhppgraaet ahvptprtap
      301 eadgfddypw ppddpaeqpw rpgadplppt vvgladdqpd gvrrvppppp eppsrylpvh
      361 vprppaaerr arpwlplvvl gvtvalllgt iaviagvsrv ddgrgtpppa ssapsatsaa
      421 papstpaaak pgtppgkltl tdrrdsivls wtypagaegp vvvaggragq pqgtfatlpa
      481 gsadyiaygl drttdycftv alvwstdsva rtgpvctkrr
//
LOCUS       WP_457609176             669 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-galactosidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609176
VERSION     WP_457609176.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..669
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73653
     Region          4..613
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          605..660
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mrnwhgegiw ygadynpeqw peqtwaedvd lmrragvnlv svgifswali eptpgrydfd
       61 wldraidllh dggisvdlat ataspppwla hrhpetlprr adgtvlwpgg rqaycpsspv
      121 frdhslalve avarryaghp avvlwhvsne lgchnvhcyc dvsaeafrgw lrerygdlds
      181 lnaawgtafw sqryhdwaei npprtaptfa nptqqldflr fssdeqraql raerellnrl
      241 vpqpvttnfm igtgikyldy hswasdvdvv andhyltaad pqpqvnlala adhtrgvagg
      301 apwllmehst savnwqprnv aktpgqmrrn slahvargad gvlffqwras ragaekfhsa
      361 lvphagpdtk vfrevcrlga dlralaevrg srvdadvail fdyeawwgae ldshpsvdvt
      421 ytdrlsalha alwragvtad vvhpsadlsr yrlvvvptly lvrdadadal rrfveaggta
      481 vvtyfsgivd ehdhirlggy pgafrdllgv rveeffplra getvrlddga radvwtewlh
      541 aegadvlaay tegplpgvpa ltrqavgaga awyvgtrldd datdrlvarl ldetgvrppv
      601 gappgvevvr rrsadrswlf vvnhttepar lavtgtellg gvrcdgelev pagevavvre
      661 epapvpata
//
LOCUS       WP_457609177             739 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609177
VERSION     WP_457609177.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..739
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80904
     Region          1..738
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mlydrldgmr eqaarrldee lrhtggtqqa rsqrdstvam yadqveqfsa vesglcfgrl
       61 dgddgavryi grigifdssg dydpllmdwr apaarpfyla taanpqgvrr rrhlrtrdrk
      121 vtglndevld iaaasptahe eltgeaslla alnagrtgrm rdivetiqae qdriiradlp
      181 gvmvvqggpg tgktavalhr aayllythrq qlstrgvllv gpnatflryi sqvlptlaet
      241 gvllrtqadl fpgvharrae pattaalkgr avladvlaaa vrdrqwvpde pvtielpqre
      301 vltldpetvr qardrvrrtg rphnlaralf dveivhalad qvaerigadp lggenllsea
      361 draeirrelr eepeiraald elwpvltpqr lladlyaspe riataapmlt dderaalhre
      421 pggwtpadvp lldevaellg ederaavarr eriramerey aegvleiwrg srsidvedea
      481 dggeilgvtd lidadrlser qeesdrltta qraaadrtwa fghvivdeaq elspmawrll
      541 mrrcpsrsmt ivgdvaqtga lagtpswgea lapyvadrwr leeltvsyrt paeimavaad
      601 vlaeidralr pprsvratgv ppwdrtvpad rlvtelieat areaaslgdg rlgvlvptgr
      661 vaelggavva alpeatvgeq pelanrivvl tteqakglef dsvlvvdpar ivsesprghs
      721 dlyvaltrat qrlgilrtp
//
LOCUS       WP_457609179             202 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609179
VERSION     WP_457609179.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..202
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20657
     Region          3..184
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtaaflltsl vvaispgtgv mhtlatavaa grraglaaaa gatlslvphv iaavtglaal
       61 lrvgtpafra vtwlgvayll wmawsalrdr gtltvggdrp prptsavfrd gvllnllnpk
      121 vtvffvallp qfvppgapaa tarmlacglv fmavtllvfa gyallagalr rrvlsrprlt
      181 allrhafagg flvlglglal ta
//
LOCUS       WP_457609181             226 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609181
VERSION     WP_457609181.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..226
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24389
     Region          20..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttartptga aptrgrragr stgddretai lataerllae rpfadisidd largagisrp
       61 tfyfyfpskd avlltlldrv teeadaaagg lferlaedpr ahwreliarf hatfgghrdv
      121 vlacaqvrgt naevrrlwae vlerwvravq aaieaerarg aapdglparg laialnsmne
      181 rvwyatfagd gpavaerdvv dvlldvwlta iyrtttppvt ppggsp
//
LOCUS       WP_457609182             209 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609182
VERSION     WP_457609182.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..209
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21810
     Region          23..188
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(64,66,68..69,128..129,147,188)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mtarvdhavt sgtfsldgqt fdvdnnvwvv gddaecvvld aphdvaaige vigdrrvvai
       61 iathahddhv rvapelarat gapvllhpad rvlwdmvhpd tapdgeltdg qtitvggttl
      121 rvlhtpghsp gacslyapdl gtvftgdtlf aggpgatgrs ysdfgtives irtrlltlpp
      181 etvvhtghgd dttigaeaph ldewiargh
//
LOCUS       WP_457609184             484 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609184
VERSION     WP_457609184.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..484
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50236
     Region          28..470
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,290,293..294,297..299,302,330,334,389..390,
                     394,398,414,417..418,421..422,425)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msegrsssav pdtgyddrrr wralsvglia afmtlldvsi vnvavpsidr alqatpsdlq
       61 wvlsgyaltf glvlvpagrf gdargrrtaf vvgvglftlt salaglarsp ewlvvarlvq
      121 gaaagvvnpq vsgmiqelfr gadrgrafgl lgatigista vgpllgglli qlggaehgwr
      181 wvffvnipvg ivamvlgwrl mparatnpag rgrldplgvl llgagvtvil lplvqreqwr
      241 gpgkwllipv gllllagfal wehryarraq plfdlrlftv rsytlgslig liyfagftai
      301 ffiftlylqm glgysalvag laitpfalgs alasalggrv vtrygrplva igllavvagl
      361 iatdlvlagg phdnvplrta lpllvaglgs glviapnqtl tlsevpvpma gsgagmlqtg
      421 qrigsaagia avgalffstl aqdrgdwgaa frhslllaag iivlalgaav advalghrrs
      481 agrs
//
LOCUS       WP_457609188             177 aa            linear   BCT 27-JAN-2026
DEFINITION  2'-5' RNA ligase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609188
VERSION     WP_457609188.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..177
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=18694
     Region          1..156
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mrtvellcsp eleaavraaw drlaaaglps larnthptnr phltlasvee fppgaeqrla
       61 dlcdaalplp vrlgrvavld gsaplvwlvr ptpqlvalhg avwdvlaeas gghswhqpgr
      121 wvphlslalr fgaadrrrar avagahppag afvaarsydg dtrtiseltt arprsgg
//
LOCUS       WP_457609189             247 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609189
VERSION     WP_457609189.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 247)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..247
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25504
     Region          1..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mttgadgrgl agfaalladp tragfclall dgrawtagel araagvaast asdhltrlva
       61 ggllveqrqg rhryvrladp gvaqlvedla arapapaapp rtlraasaga alayartcyd
      121 hlagrlgvll hdalldrgvl drtgglalte tgmgwldrlg vpveplrgtr rplvrdcldw
      181 terrphlaga vgaalcgrfl dlgwtargtg ravrvtpagr dalaealgld pvllaepatr
      241 dtgpara
//
LOCUS       WP_457609191             264 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609191
VERSION     WP_457609191.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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..264
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..264
                     /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=27255
     Region          8..238
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtdryrafre lhrpgdplll pnawdhasaa alaarghqai gttslgvaaa agrpdavrat
       61 raetlelayr lrrlpalltv dvedgfhddp aevaryvgel aalgvvgvnl edgrpdgrla
      121 pvehvaavia avraavprmv vnartdawwl gvpapldear rraaafrdag adclfvpgap
      181 ddlvgllate aglplnvlyr pggpdlaalg rlgvarvstg sllfraalga alhltdaiga
      241 grdaglpapp gyeevqalap psat
//
LOCUS       WP_457609193             536 aa            linear   BCT 27-JAN-2026
DEFINITION  asparagine synthetase B family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609193
VERSION     WP_457609193.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Nagler,D.K. and Menard,R.
  TITLE     Family C1 cysteine proteases: biological diversity or redundancy?
  JOURNAL   Biol Chem 384 (6), 837-843 (2003)
   PUBMED   12887050
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417543
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..536
                     /product="asparagine synthetase B family protein"
                     /EC_number="6.3.5.4"
                     /GO_function="GO:0004066 - asparagine synthase
                     (glutamine-hydrolyzing) activity [Evidence IEA]"
                     /GO_process="GO:0070981 - L-asparagine biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59865
     Region          1..460
                     /region_name="AsnB"
                     /note="Asparagine synthetase B (glutamine-hydrolyzing)
                     [Amino acid transport and metabolism]; COG0367"
                     /db_xref="CDD:440136"
ORIGIN      
        1 mcgialsigp eadpatfrrm laalaprgev tetrqengll agvrrlkivd rersvqpwms
       61 pderhllcfn gevfnhhelr aeltrlghrf rtagdtevvl aafrqwgena vrrlrgeyaf
      121 viverdtgra ylardplgvk plywsrlpgc lhlasevkal vghgapigev apghhgwvep
      181 grpvrlgphv dlltlgdglp viddpdeaal lvrvaltdam rtrldtdltv gvvlsgglds
      241 slallharel hpdcvavtig vpespdvaya rrlaadlgvp hevielrprd irladvreai
      301 riselteygd iinavvsvpi frrlrelgvr vvltgdgsde lfggypmyhr vgpersrrlf
      361 lhkirnlcrt elqrvdrasm ahgvearvpf ldlsvvelam rlpldlklrd gqekwivrra
      421 fadllpsyvr qrpknpmsys sglherarly kplfarlhrs fgydllepvr rdfdsvltrc
      481 gndldraiae giarpdytvl ehardlvgaa rwnaapmvrr lvnprrtrgd eaplpg
//
LOCUS       WP_457609196             148 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609196
VERSION     WP_457609196.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..148
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15559
     Region          59..142
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mqspsltgil vlvavlagat afgwwrrrhd grlravrkrp saadaphrat ltalgvrpge
       61 vtlvqfsapv capcraahrv ladvaarvdg vavrevgvde hldaareldv wrtptvlvvd
      121 vagrvvrraa gvpdrddlia altagaar
//
LOCUS       WP_457609200             432 aa            linear   BCT 27-JAN-2026
DEFINITION  FUSC family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609200
VERSION     WP_457609200.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..432
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45165
     Region          <89..236
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 madrradtvr spldraverg glalsrarae ggaagrnrlr qleitvvisa qaglaaalaa
       61 lladellgsg ahvfapaaai gtiataigqr arrtfellig vglgilvgdl lrallgsgsw
      121 qtglvvtlai atallvagrg galvgqaggt avliatlapv qpglelprif dalvgglvgl
      181 fvvalllpvn pirvldrave pvvarlteql davahaltrr dadaaqrale dlrgiepdig
      241 rlndalsgae evvtiaparw hrrarfhrya datqhlerlv lyarsiarrs atalqydepv
      301 ppalpdavar lgqavremkr acksgedler tremvrqgae lagrawsqgv rafgeamisd
      361 lrtaqsellr atgcrpedan gsvrraagag esearppara rmsrpapgrp ggrhrpkatg
      421 rqlaparagp ag
//
LOCUS       WP_457609206             309 aa            linear   BCT 27-JAN-2026
DEFINITION  sporulation protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609206
VERSION     WP_457609206.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sonoda,Y., Mizutani,K. and Mikami,B.
  TITLE     Structure of Spo0M, a sporulation-control protein from Bacillus
            subtilis
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 12), 1488-1497 (2015)
   PUBMED   26625291
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Han,W.D., Kawamoto,S., Hosoya,Y., Fujita,M., Sadaie,Y., Suzuki,K.,
            Ohashi,Y., Kawamura,F. and Ochi,K.
  TITLE     A novel sporulation-control gene (spo0M) of Bacillus subtilis with
            a sigmaH-regulated promoter
  JOURNAL   Gene 217 (1-2), 31-40 (1998)
   PUBMED   9795118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..309
                     /product="sporulation protein"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /calculated_mol_wt=33017
     Region          14..251
                     /region_name="Spo0M"
                     /note="Stage 0 sporulation-control protein Spo0M [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG4326"
                     /db_xref="CDD:443467"
ORIGIN      
        1 mrltgvsrds twtglsvstt lpnpstrpgl rlpgrvtlaa ggsdvpvrhi rlglvtqvep
       61 edpeaprrlv qfqtwtiagr fvvpagrrra vefavplpwe spvttyggvp llslrtglrt
      121 evsvdpevdq gamvpvlihp lpaqehvlaa ldtlgfairq aglregrlpg veqtlpfqqw
      181 ygfwaaplya gpmtelemim rtdsagmevl lwldrrlsla githqsisrf rvwhagadkr
      241 dwvatvdgwl rhaidrhaaa aahadwsati resahvsrpp drpvapgygl ggtaggagig
      301 ggggggdgt
//
LOCUS       WP_457609208             361 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609208
VERSION     WP_457609208.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  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   5  (residues 1 to 361)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   9  (residues 1 to 361)
  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 16062768
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..361
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37386
     Region          <58..103
                     /region_name="SH3_16"
                     /note="Bacterial dipeptidyl-peptidase Sh3 domain;
                     pfam18348"
                     /db_xref="CDD:436429"
     Region          142..361
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mapqpgrrav vrvpvatlwt apeavrpidc palagspdva awiagmdrdq lvgdcvltql
       61 llgepvrvte srpdgwvrvv algqpaaklg adgypgwlra ahladpadae pssthpahvd
      121 pagpalsgpa lsatasagpa pvgsgpagpg qtrsgsagtg sagtgsaadr pltvdvarta
      181 lraepgggaa ltgvvlgtrl tpagpavngr rpvrvpgrpd plwapeddlv plpaerpeae
      241 qvlavaerlr dlvyvwggms tdgidcsglv hlawrrygit lprdaddqaa atsrlpldae
      301 rpgdlyffar pgrrihhvgi vsaeprggrr rmlhacyltr rvieeelpad rtatlvgahr
      361 v
//
LOCUS       WP_457609209             221 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609209
VERSION     WP_457609209.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..221
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23017
     Region          6..137
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mttplydgia dwyeeyaset ssvymdrvrs vladllgdgp grcvdlccgt gahaaelrrl
       61 gwtpvgvdls ggqlrharar lpvaradata lplstgavpa vvcvlahtdm pdypaavaea
      121 arvlapggrl vhvgvhpcfv gafadrsepe rividggyas rertvrswna agvrarvgaw
      181 hlplagllda vaaaglrltr vvesgsgpvp dvlaleatkp h
//
LOCUS       WP_457609210             499 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609210
VERSION     WP_457609210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..499
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51814
     Region          32..178
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mpdllswlqe lpplliyvaa aaivaaetav ivgllmpgea tlllvgflay agtlrlapvl
       61 vamtaaavig dtlawragrr ygprlrasgv garigahrwr radsllerlg grgvlaarwi
      121 afartlaprl agsagmpyrr fapwnlagva swvgasvlag ylagesyerv skllgratga
      181 vlvlllclla vvlagrwlgr npdpvralaa raaalpplrw lrarygvlff lvamrvgpaw
      241 tllfnlalgl allfvaglav avlleavvaq sglyvldglv adwfaarrtp gvvdtalpav
      301 svlrgwvlia avavvaavva rrgrawradp lgvlgtvgaa vplvllvvva dltgpggpdr
      361 pgdlfptqna vvtasfgtla wllsrgarwp vgaavwtvas agvvtvtgar lylgfstasg
      421 tvtavllgva wttvfvvawa trdrladrde rsagadreeg sagaapdegp ddavagespp
      481 rprgrrsafr vppgpvdpc
//
LOCUS       WP_457609211             708 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609211
VERSION     WP_457609211.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..708
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72934
     Region          50..691
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mslftrvvrg rlaawltlaa alvvgvvafg lpkpdnpapv sdtglsvewq stqverlqeq
       61 lpskdaqtal vvvsradqap lsgadrsvld glggelnsla vggrvspaqv spdgtvalva
      121 vplsteggps avvdeveklr eavgdlpgel tvevtggpaf tadlgkvfqg adttlllvta
      181 avvavlllvt yrspflwlvp llvvgateqi tlrvveslvp afgiylpsgq vtgiasvlvf
      241 gaatnyalll iaryreelrr eedrfaamrs alrrtaepil asgstvvlgv ltlllseqet
      301 nralaiacat gvilamlsal fvlpaalllf grglfwpfvp rvgsaaregr iwgrlgelvv
      361 rrplpvaala vlllaglalg glgirtglse teqfsekpea vagaetlara fpagstqpva
      421 vlttpqaaqa vlaaangvdg vasarpgaag drvaqidvvl taepgsaasd ravvalrdav
      481 aavpdsappa vdgadapdga lvggsvaaty dsneantkdl klilplilll vgavlvlllr
      541 gllaplllvl tviasffasl gaawllfdhv ldfpaldsgv lllafvflva lgvdyniflv
      601 traredarrt gtrdgmlsal rvtggvitsa gillaavfav lgvlplitlt qigiivcigv
      661 lldtllvrtv lvpalafllg drfwwpgria rdadapatap aepvaard
//
LOCUS       WP_457609212             549 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609212
VERSION     WP_457609212.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..549
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59934
     Region          15..544
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mrlvtraatt alrlpaartg rvtvtrdipv rvrdgvtlrt dhyapglpaa pcvlirtpyg
       61 rggpvrllgr liaergfhvv iqscrgtfgs ggefaplvhe rddgldtldw lrrqrwwtga
      121 fgmfgasyqg fvqwalaaea gdelramvav vtasgtrdst yagesfaldt vltwaellqa
      181 qtvpwlarqw elkrgqprla ralahlplae adrvatgvtv pffqewlrhh tpgadywrtr
      241 vfgdritevr apvamvsgwq diflpaqldd yarlraagtr trlvvgpwth gspglllasl
      301 reglawldth lagrpgpdra pvrvhvggvg ggwrdlpdwp ppatparwhl rsagglapqp
      361 qehgapdriw ydpadptpsl ggpllvaqra gavdnrpvea rpdvltyase plrdpvevag
      421 pvaaeihlrs elsyldvfvr lcdvdrrgrs wnvcdglvrv epgrfprdps gvvtvpvtlw
      481 ptayrfapgh rlrvqvsgga hpryarnpgt geplgtavtl ragwreifhd rehpsalvlp
      541 lvpapstag
//
LOCUS       WP_457609221            2253 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase, partial [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609221
VERSION     WP_457609221.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 2253)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 2253)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 2253)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 2253)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..2253
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>2253
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
     Region          7..35
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          36..1450
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1228..1697
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1451..1452,1454,1475..1478,1503..1506,1530..1532,
                     1553..1554,1576..1577,1591,1618..1619)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1554,1578,1591,1595)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1713..1796
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1813..>2253
                     /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 mrsgpmptea efldylrrat adlrdarrrv reveakdrep mavigmacrf pggvsspael
       61 wdlvdrggdg vgdfptdrgw dlerlfnvdp dnpgtstsnq ggflydapqf dpgffgispr
      121 ealamdphqr llletsweaf ehagidpqal rgsrtgvfag vmyhdyasrv ldlpdgvegy
      181 igtgnsgsvv sgrvayifgl egpavtvdta cssslvavhl atqalrqrdc dfalaggvtv
      241 mstpgtfadf srqrglasdg rcksfaaaad gtgwsegvgv lllqrlsdar rdgrrilavv
      301 rgsavnqdga ssgltapngp sqervirqal anarlspadv dvveahgtgt tlgdpieaqa
      361 llatygqdrg dggplwlgsv ksnlghtqaa agaaglikmi eairhrtmpa tlhvdapsph
      421 idwsagqvsl ltearawsat drprraavss fgisgtnahv ileetpgdda pstdeapsav
      481 dapvalplap vflsartpea lagqagrwad hlarvdaprp vdvavssvsr aglehravvl
      541 agdaddllag lralaagept gavttgasap rgrvaflfsg qgaqragmgr glygafpvfa
      601 aaldevcghl dpllprplre vlfagagtpg aelldqtvft qaglfaveva lfrliesfgv
      661 apdlvaghsi geiaaahvag vlsladacal vaargrlmqa lpagggmlav aadeaavtas
      721 laglsgrldl aavngpaavv vagdvealde vqrvwsergv qtrrlrvsha fhsarmdpml
      781 aefaavaegl tfrpptipvv snltgrvada dqlcdpgywv rhvrgtvrfa davdclraee
      841 vdtylevgpn gvltamtqnc laeraedepa pllvpvsrhd rpepqallea laslhvhgra
      901 vgwaglldra ggrhvdlpty afahqrywle pagrwtdvsg aglgaaghpl lgaavsvage
      961 dmvvltgrls tsthawladh vvsgavivpg aalvelavra gdevgasrvr eltvaaplvl
     1021 pqvgavrvqv rvgaadgagv rsvtvhsqpe edadpewvrh aegvlepasa depgvgewpp
     1081 vggievdvag wypalaergl sygpvfrglr rvwtvgedvf aevalpdeva gdvagfgvhp
     1141 alldaalhpi gllsgsegsg garvpfafeg vqvwaagarv lrvrlmrags avrlvacdes
     1201 gaavvsvdal tlreltgvsa spdasarslf evawqtqeva pagdaagwal lgspaadlpa
     1261 vaelpvyadv eavavasgva prlllvpagg lrrarhvete pasvpgempa avdngpesvr
     1321 aatsqvlatv rswlvadala esrlvvvtrg avsvgdgdrv tdlaaaavwg llrsaqsehp
     1381 grivladvdg dvdagllavl ssvadepvaf ggqvavrsge vfvprlvrav apssadgavv
     1441 gdgavlvtgg tgalgalvae hlvsvhgvrs lvlvsrrgpg avgagelser lsalgaavrv
     1501 vacdvtdrdq vfglvgevsa ggrlagvvht agvlddgvve gltaerlaav lapkvsagwl
     1561 lheataglgl dlfvvfssva gvlgspgqsa yaagnafldg lavhrrqlgl pavslawgmw
     1621 dtpgmgasld eaerarstrg gitamgaetg lrlfdaalta grpalvpavi dlaalraaag
     1681 aglvppmlrn lvgttttrrq agqgttwatr iggltadear aqldvlvrgl vaqvlghgga
     1741 eavpadrafr elgfdsltav dlrnrvnaat glrlpstlvf dyptpqalas hvhaelagaa
     1801 grpaapgtrt ttradeplai vgmacrypgg vetpdqlwel laaggegige fptdrgwdle
     1861 slfdpdpghp gtsytrhggf lydagafdpa ffgispreal amdpqqrlll easwetfesa
     1921 gldpqrlrgs rtgvfagvmy hdyashlmel adevegyvgt gnsgsvlsgr vaytfglegp
     1981 avtvdtacss slvalhlaaq alrsgecdla laggvtvmat pgtfiefsrq rglsqdgrcr
     2041 sfaasadgtg wsegvgvllv qrladaqreg rrihavlrgt avnqdgasng ltapngpsqq
     2101 rvihqalana rltpadvdav eahgtgttlg dpieaqalla tygqerpvdr plllgsvksn
     2161 ightqaaagv agvikmvmam rhglvpptlh vdepsphvdw tagavalate ptpwpavdrp
     2221 rragvssfgi sgtnahviie qppaetvgar ptd
//
LOCUS       WP_457609223             275 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609223
VERSION     WP_457609223.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..275
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28931
     Region          11..224
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(66,68,70..71,155..156,174,213)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(66,68,70,155,174,213)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mtagfsevaa gvhvlreptl avnvvlvvgd gaallvdtls tagqarelae aaravtpypw
       61 tivnthhhfd hcfgnatlag pdtaiyaqaq aaaalrdrsg avrraayeem raghpalaee
      121 lahtelrapt hevheetvld vggrrvvlrh pghghtdadl vvhvpdadvl vagdlveqsg
      181 ppafeesypl kwpdaladll rlttpttvvv pghgepvgad fvreqhaqla rqawliragh
      241 tgsapperva aespfgarpg liaarrgyae ldgta
//
LOCUS       WP_457609227             453 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609227
VERSION     WP_457609227.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..453
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=48962
     Region          19..442
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 mppypgpwgp aagppggeep rqrlhplspa lhgakslvvv iaglswstls rvgfgwfavl
       61 vtvfvlgatv lsvvswwntg yhlvgrelrv yegllwrrtr aiplerlqav evvrpllaql
      121 tglaelrlev vgggkteapl aylsvaeata lrqrllavag rsapapvaaa epgapvapvp
      181 egrrlhavrn qdllvsqllt pqafllplgl vfvgaqflse gswsfiavas tltamagvvl
      241 qpirrvlddw sfrldrddgt lrvhngllet rmqtvplhrv qtvratwpll wrmkgwlrlr
      301 levagysage pddrnrpdrl lpvgdagtga mvvaevlpgv rldalpatpp psrarwlrpl
      361 srkvvgagld ervfvarsgl ltrrltlvpy ariqsvrvtr gpvqrllrla tvhadtagga
      421 gaaavdrdlt dawelaaelt ersraarrtd sgr
//
LOCUS       WP_457609232             800 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609232
VERSION     WP_457609232.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..800
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89781
     Region          10..788
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mdtavnlhsp ltedelrrld aywraanylt vgqiylldnp llreplrpeh vkprllghwg
       61 tspglnllyt hldrvivnrn lsaifvtgpg hggpalvant wlegtysely hhiprdetgm
      121 qrlfrqfsfp ggipshvape vpgsihegge lgyalshayg aafdnpdllv acvigdgeae
      181 tgplagswls nvflnpardg avlpilhlng ykianptvld ripgddlrdm mrgfgyqpyv
      241 vegddpatvh qllagtldrv ldeiaaiqrr arsgehverp rwpmiilrtp kgwtgpsrvd
      301 gkqvegtfra hqvpisevrd nqehlaeler wlrsyrpeel fdatggpvae vaglpptgdh
      361 rmsanpvang grllrnlelp dfrdyavdvp tpgepmagat gvlgpwvrdv iarnpetfrl
      421 fgpdevasnr lgaafevtdr afvgaevpgd dhlspdgrvm evlsehlcqg wlegylltgr
      481 hgiftsyeaf ihivdsmvnq hakwlkvtrn ipwrepvasl nyllsshvwr qdhngfshqd
      541 pgfidhvvnk kaevvrvylp pdgntllstm dhclrsrqyi nvvvagkqpa pnwltmdeai
      601 qhcrrglgiw dwassddgte pdvvlacagd vptletlaav dllrrhlpdl rvrvvnvvdl
      661 mrlqppsehp hglpdnefdt iftrdrpvif ayhgypwlih rltyrrtnhe nlhvrgykee
      721 gttttpfdmv mlndldrfhl vidvidrvpg lrsraahlrq dmvdarqacr dytrrygedd
      781 prvaewrwir endpavrsge
//
LOCUS       WP_457609235             555 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609235
VERSION     WP_457609235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 555)
  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 555)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   3  (residues 1 to 555)
  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   4  (residues 1 to 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12186828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..555
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60193
     Region          45..192
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
     Region          221..350
                     /region_name="GAF_2"
                     /note="GAF domain; cl21515"
                     /db_xref="CDD:473894"
     Region          343..555
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtplsrvrld ellqemldrv gevvtsrerl ralldavvgi gsdldlrstl qrivqsacel
       61 agarygalgv igpdrmlhdf ivhgispelh akigelphgr gvlglliddp kpvrmpditk
      121 hpnsygfpph hppmhsflgv pvrirdhvwg nlylaekqga aefteddeei vvalaaaagv
      181 aienarlyal ahrrerwlaa aaeitavllg evrrtdaltl varrarevae aelalvllyd
      241 edeaqftvev vdgadpvare lvgavlpaae tsfaasvtqg rhdqvedlaa aapwprpvva
      301 gpavvsplaa adtlhgvlvi gyrpdhgpaa dddlallasf agqaalamer argqeerell
      361 vvledreria rdlhdvviqr lfatglqlqs gamnarpeaa krinqavddl datirdirrt
      421 ifelrtpmsa alrteireai evaaeslgyr peleligpid savpddlrpe ltavlreals
      481 navrhaqagr vsvrvrvdsg rveitvtddg igcdpeaars glvnlrerae rlggefslrr
      541 aeprgtevrw svpld
//
LOCUS       WP_457609240             886 aa            linear   BCT 27-JAN-2026
DEFINITION  cation-translocating P-type ATPase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609240
VERSION     WP_457609240.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 886)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 886)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 886)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 886)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..886
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=90474
     Region          36..869
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mlglpgaggd dmeddvving gpatattpte ispapatglg saeaaarlra dgpntvaapr
       61 krglagrvfr qltdplvall laaavvttll rdypdtaviv lvvlintaig vvqevradra
      121 vaaldrlaap tarvvrdgrd lvlpaadlvr gdlvrleagd vvpadldltd avrlsldesa
      181 ltgesvpvar vageeasagt vvttgratgt vartgaasal grisalvaat rpaptplqrr
      241 lsslgrvlgl tavvlsglvf aigvldgrpv tqmavtavsl vvaavpeslp avvtlalalg
      301 arrmagsrai prrlhavetl gsvtviasdk tgtltegrma vqyavvpgrd ryavtgtgya
      361 pdgevhhrge pvsapdelra laragllcnd atvtpptder pewtaigdpl eaalvtfgar
      421 cgldpdttrd awprvaeapf dqdlrrmttv hrrcdgrylv vckgapenll aaplvdadaa
      481 elaeltdaah rlateglrvl avasavvdtl pdparptglr plglvavgdp lraaapgiaa
      541 gfeeagirlv litgdhpata aaiggrlglw rdgdplangd dgdpggahpe trvyartqpe
      601 qkldiiaglq nrghvvamtg dgvndapalr radigvamgg gtevarqasd lvlvdddltt
      661 vataigegrr iydnirrflr yalaggvaei avmllgplvg lpvpllpaqi lwinllthgv
      721 pgvalgaepa epgtlrrppr spqesvlgag lgrdvlvtgg liaaatlgag vwaaaadrpw
      781 qsvvfvvlgl aqlgvalavr airtpgsrer nlalpvavai savlqvagvl lpplrellgt
      841 splsvldlla caaigvlpgl vlrltrrfrg tngphagavg pagpaa
//
LOCUS       WP_457609277             406 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609277
VERSION     WP_457609277.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..406
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44230
     Region          2..406
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 mtdvlvsrad dfddiaalla lafhgdldpd vqalerpife pdrsllvrdg gtavahaaaf
       61 srrlavpgad vpaahvtmva vapthrrrgl lttlmhrqlr eirdagrepi avlwasegri
      121 yprfgygsaa prymlsvdtt glrlpapapt egrlrldrpd ahrdelarly ervragrpgw
      181 srrderwwsy vladlkahrg gaterrvllh egadgldgya lyrtkdssta vgpqaevqvg
      241 evvaatpeay talwrlllsv dltrrlsfgi aaldepllrl vdeprqlsph ladalwvrvv
      301 dvpaalaarr yatdvdvvie vtdellkent grwrlvggpa gaectpttap aglacdvral
      361 gelylgganp yalaaagrvk elipdtltal tpaftwyrap spmevf
//
LOCUS       WP_457609289             141 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609289
VERSION     WP_457609289.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..141
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15196
     Region          3..141
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mtpddeaflr raveladrag asgerpfasl lvgadgtvli edhntvvsdr dvtahpelkl
       61 arwaarqlap eaavattmyt scqpcpmctv ainasglgrv vyalsteqfe qvkpatpatr
      121 pvrydgpalf dearrpieeh y
//
LOCUS       WP_457609291             217 aa            linear   BCT 27-JAN-2026
DEFINITION  Type 1 glutamine amidotransferase-like domain-containing protein
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609291
VERSION     WP_457609291.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Hakansson,K., Wang,A.H. and Miller,C.G.
  TITLE     The structure of aspartyl dipeptidase reveals a unique fold with a
            Ser-His-Glu catalytic triad
  JOURNAL   Proc Natl Acad Sci U S A 97 (26), 14097-14102 (2000)
   PUBMED   11106384
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007242
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..217
                     /product="Type 1 glutamine amidotransferase-like
                     domain-containing protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016805 - dipeptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23173
     Region          3..216
                     /region_name="PepE"
                     /note="Peptidase E [Amino acid transport and metabolism];
                     COG3340"
                     /db_xref="CDD:442569"
ORIGIN      
        1 mkllltsagv qnpsindalv dllgkpiaes salciptaay pmggpasawr fitgqtplpm
       61 sglgwkslgv leltalpsig rehwipwvre advllvhggd atylchwmrq sgladllpsl
      121 rdtvwvglsa gsmvltprig tefvewqsap ddrtlgivdf sifphlglep dntmasaekw
      181 aaeiagpaya iddqtavkvt dgavevvseg qwrrfpa
//
LOCUS       WP_457609295             272 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609295
VERSION     WP_457609295.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 272)
  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 272)
  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..272
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..272
                     /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=27325
     Region          11..231
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mddqqtraqr fralhqpgdp lilvnawdal sarivaaaga ravattsaav awsrgapdgd
       61 vlardtavdv irrvadavhv pvtadiesgy gdspaevaet itavlaagav gvnvedsrhd
      121 gggplrpade qvarlaaira aadragiply vnarvdtylr raggvpetva raeaylaaga
      181 dgifvpgtve petvaalaaa ipaplnvlag pgappiaela rlgvarvsig pavaeaayav
      241 aqraaaevlg agtygalagg ldfdalnelm rs
//
LOCUS       WP_457609318             366 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609318
VERSION     WP_457609318.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..366
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40937
     Region          1..353
                     /region_name="LLM_CE1758_fam"
                     /note="putative luciferase-like monooxygenase,
                     FMN-dependent, CE1758 family; TIGR04036"
                     /db_xref="CDD:274934"
ORIGIN      
        1 mqfgvftvgd vtvdptngrp psererikam taialkaeev gldvfatgeh hnppfvpssp
       61 ttmlgwiaar terlllstst tlittndpvk iaedyamlqh ladgrvdlmm grgntgpvyp
      121 wfgqdirngi plaienydll hrlwredvvd wkgrfrtplq sftstprpld gvppfvwhgs
      181 irspeiaeqa ayygdgffan hifwpkehtq rmvglyrery ahyghgsldq aivglggqvf
      241 mrrnsqdavr efrpyfdnap vyghgpslee ftretpltvg spqqvidrtl gfreyvgdyq
      301 rqlflidhag lplktvleql dllgeevvpv lrkefdslrp ahvpeaptha sllaardaap
      361 aageqr
//
LOCUS       WP_457609336             280 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein, partial [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609336
VERSION     WP_457609336.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>280
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /EC_number="1.14.99.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          8..>225
                     /region_name="COG3397"
                     /note="Predicted carbohydrate-binding protein, contains
                     CBM5 and CBM33 domains [General function prediction only]"
                     /db_xref="CDD:442624"
ORIGIN      
        1 mrisrtarrl glgavavlla sftmvvvnqa gpasahgsvt nppsrnygcw erwgsdhlnp
       61 tmaqtdpmcw qawqanpntm wnwnglyren vggnhqaavp dgqlcsggrt qnglyaslda
      121 vgawtakpmp nnftltltdg akhgadymli yitkqgfdpt tqpltwnsle lvlrtgsypt
      181 tglyeaqvna gnrtgrhvvy tiwqashldq pyylcsdvif ggggnppptt papppppppp
      241 pppppppppp pppppppppp pppppppppp qpknkkppqt
//
LOCUS       WP_457609341             187 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609341
VERSION     WP_457609341.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..187
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20622
     Region          2..182
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 makliyvnnv sldgymeder gafawlpmdd evfvvytdll rsvgtflygr rlyeamavwe
       61 tdaalaaqsd lmadfasvwq aarkvvystt laavstadtr lerrfdpaev relkatadsd
      121 ltiggahlaa qaleaglvde cqlfvwpvav gggkpglptg mrvdlellde rrfrngvvrl
      181 ryrplgr
//
LOCUS       WP_457609339             348 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609339
VERSION     WP_457609339.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  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 348)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..348
                     /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=36313
     Region          116..345
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 misvvelllr ddrawapllv gvsvvvaacl lyrrtrplaa vtvafgtvla fdiariavvd
       61 atgllgiagl lvlpyallrw gagreaalgl gvilvwlpvt lvaeqtspae kvagygfflc
      121 saalgaavry rtrshdrdve qvrlhqrnel arelhdtvgh hvsaiavqaq agralaaadp
      181 eralatlvti eeeasrtlre mralvgvlrd gtdadlaprr gvadierlar pggevlgvrv
      241 qvsgdaeave pavgtalyli aaeavtnatr hargatgvtv dvtasrgqvh lrvhddgeat
      301 ttssphagyg lrgmaerasl lggtlragpa pdggwsvdas lprtalts
//
LOCUS       WP_457609344             111 aa            linear   BCT 27-JAN-2026
DEFINITION  RICIN domain-containing protein, partial [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609344
VERSION     WP_457609344.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>111
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <38..111
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(57..58,70,72,80..81)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mqrslpgrrl gvlstaaaaa lavpvaival vgpadaatpv gsgtytlang ssgkcvvvtg
       61 agtdngvrla qvacdaaasa qqfravsqng aygltnvnsg kcvdvpnyss t
//
LOCUS       WP_457609346             319 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase enzyme family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609346
VERSION     WP_457609346.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..319
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34849
     Region          41..264
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 midkpdider tlaaevaaaw pvdvvdlvfm pvgldgqawa yrvetsvggr yflkvrrgdf
       61 tpaavllpsf lraqglrqvv apldhggagr gygdyrllly pfhdggslwg rgltdrqwte
      121 ygdflgrlhr vtpsaevaav lpvetyrsga gerlrtlgvq aatsevlgaf werygaalhr
      181 laetvddlgs rvtpgqhvic hadihpgnli adgdgplhvv dwdapilapr erdlmfvysa
      241 dfgdhpidar raelfregyg alepdpvlls yyrserhldd vaaflgsild peastesras
      301 glywltriae avadpgyap
//
LOCUS       WP_457609287             343 aa            linear   BCT 27-JAN-2026
DEFINITION  questin oxidase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609287
VERSION     WP_457609287.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Fatima,S., Zahoor,A.F., Khan,S.G., Naqvi,S.A.R., Hussain,S.M.,
            Nazeer,U., Mansha,A., Ahmad,H., Chaudhry,A.R. and Irfan,A.
  TITLE     Baeyer-Villiger oxidation: a promising tool for the synthesis of
            natural products: a review
  JOURNAL   RSC Adv 14 (32), 23423-23458 (2024)
   PUBMED   39055269
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Qi,F., Zhang,W., Xue,Y., Geng,C., Huang,X., Sun,J. and Lu,X.
  TITLE     Bienzyme-Catalytic and Dioxygenation-Mediated Anthraquinone Ring
            Opening
  JOURNAL   J Am Chem Soc 143 (40), 16326-16331 (2021)
   PUBMED   34586791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 141406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..343
                     /product="questin oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36475
     Region          49..>126
                     /region_name="Questin_oxidase"
                     /note="Questin oxidase-like; pfam14027"
                     /db_xref="CDD:464069"
ORIGIN      
        1 mlnsvldeay ervrhtgper dgwlsnhvpm aaealvrhgh eravhrwida ysdrleerpr
       61 gigriapeew rdplgdpvrt gdwldlfdre vagepwrdvl arwwprllpg iaagathgvi
      121 rvghavrall daetaprvte lgqglaywaa rwqplappgt gpypgtdars aldavprvpd
      181 qrfgirsrla qladldrwpa aaaavpgdaa advparlaav vdaavlrhgt hgyaspvmlv
      241 haatapnavl rtlpalppal wqpslaaawa ataavtaaya pagaralrpa agpeldevma
      301 raldtgdaha ikfidtlsda yarsgdpall avaarsvaqi aad
//
LOCUS       WP_457609362            1119 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609362
VERSION     WP_457609362.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..1119
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=119454
     Region          <2..921
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 meprfgqhli grehpaallr aevtrlvdsh gglvlvtgep gigkttlvsa aadearrsga
       61 lvlgaacwds dtapdywpwv qvlrrlarsa ddprgvreaa aaglaallge rapgdpaepg
      121 dpaepgdaae pgdaaepgda graefdrhda vtaalvavaq hrpvavvldd lhwadpaslr
      181 llqfvtqhaw ferllligty rdaevesgdh plrqwllplt akattvtlag lgraevaalm
      241 artagrepga slvdevhrrt ggnpffveqt arlwhthglt dtvapgvrev vrrrldqlpa
      301 gvvealtvaa vlgrefdgrt laacvpapva qvdrllgraa aarlvlprdg grfvfvhdlv
      361 retlydglad derrarhaav vraadrsdal agalspahla rhawlagael dperagdlll
      421 aaardaggri avdesvrhyr raleltgepg rrvrvllela gllhhagppa everllaeaa
      481 alarelpdpg vltrvaliah rqhsatrrrl daaelvreay rrsiaepdpe rpvralvtdl
      541 itatetlarh grddealtfs lwarhdttwg lgtaqeravv taeirevarr sgdretelwa
      601 talrwvalle lgdpgyrqel tafvagarrd dvarqrvaai adtaiiaafq gdlaaaeagf
      661 aeaesyrepg hsdhafmthh mrwsilllyg rlaeaeavld rvgaghpqve llraitaaer
      721 gdaatvlrlt aaieaagtay prsvsplwlr lraqaaaadg dparcaavra dlaphrgqwa
      781 aalfgcdivg pvdlwlggvd aaegrwdeav dcytaardaa drlgarpwsv laqaalvgal
      841 agrhgpgdaa etrrlraetv aearslgmiq vverlgaadp apaaasavva pvaarlgagv
      901 palavaaspp grrgasglsr agvvhgsarp pdpgadvvrp efrpdgpvwr laydgvvvhl
      961 pdakglhdlr lllsrpgtdv pavelldpaa gpevvaarrl gadpvlddea karyrrhlrr
     1021 lddeidraaa rddarrlael daeraallnq lraaaglagr drrlgdqaer arkavtgrir
     1081 dtlrriderh palaahlres vttggacryr paepvpwrl
//
LOCUS       WP_457609352             224 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609352
VERSION     WP_457609352.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..224
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24924
     Region          5..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgasyhqfcp vakamellde rwtllvvrel vsgserfndl rrglprmspt llsrrlhqlv
       61 ragvverrvd gadvryvptt agrelrpvle algawgvrwi gelgdadldp klllwdmhrh
      121 vdhdavppgr tvvrfrfrdv pttqrdwwmv iaageadvcd idpghdvtvt vtadlrtlvq
      181 vwmgdlewaa alrggaveva gpealrraap gwftlspfaa vprp
//
LOCUS       WP_457609366             262 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609366
VERSION     WP_457609366.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10595285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..262
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28251
     Region          5..241
                     /region_name="Y_phosphatase3"
                     /note="Tyrosine phosphatase family; pfam13350"
                     /db_xref="CDD:463853"
ORIGIN      
        1 mtappdfatl cnfrdlggwr tgdgrtvarg rlyrsdslak lagedlerfa algvrtvidl
       61 rypweiadrg rapeslgvtw hnlsiehrpy vqadidpgvd pwryladrya evaedgvael
      121 rqaieviadg ehplvfhcas gkdrtgllaa lvlsvlgvdd dqiaadfalt ehatdrlvae
      181 wrdrnggatp gwpaygrapa eiirlvlael raahgsvhgy vtgrlgvgee tidalrarll
      241 tgdtnplptq gttgstptpa ar
//
LOCUS       WP_457609367             372 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609367
VERSION     WP_457609367.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..372
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39362
     Region          10..361
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdtrwdglra evratidelv ssgretgvqv aayldgvail teqagladpt tgrpmtagtp
       61 vhavstgkgl tatvvhvlae rgrldydrpl aavwpefarh gkdgitlrhv lthtaglpal
      121 padvtpedft dwtrmcella garplwapge rlayhawtwg wllgevirrv tgapvsrvla
      181 eevagplgvd relflgvpea dlprlarled aglsalmtwa ganlphfdav appgvrpdtv
      241 igsrpdvlra dvpsvgtmsa ravarmyaal lgpvdgvrli saermrevsa pavrapewvf
      301 gqestfglgy avdddgsfgt agsggslafa ypdlgltvaa vrnrlgagdg dpmehlrtlv
      361 rdrvteatgh rg
//
LOCUS       WP_457609369             367 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609369
VERSION     WP_457609369.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..367
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38275
     Region          144..366
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrcasrsrfl llldggiata slavcllall asdagpdttg atavavglav aqascllwir
       61 rhpgyalgva alagvgleal cpqlgwlglv aipmaytarl rppryslval glllaptpwk
      121 lvtggwrdll lavtaltlsw tlgelqrgqa qrrcawerqv laaererisr elhdvvahhv
      181 aviavqaaaa edvfdehpaq araalaaidt aarsaltelr amlhalavdd gsaqggpqpg
      241 laqldalada vravglpvtl hregdgealp ggvqlsayri vqesltnalr hghatradvd
      301 vhyrdgvlrl evvndgpapa rrpgtptgrg ivgmrerarl lggtldagpl paggfrvhar
      361 lpvgadr
//
LOCUS       WP_457609370             424 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609370
VERSION     WP_457609370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43756
     Region          24..409
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,75,130..131,133..135,138,158,
                     161..162,165,242,245..246,249..251,254,278,282,338..339,
                     343,347,363,366..367,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtapartsgp veappgrlfr hrdfrllwtg htvsavgsnm tavalplvav avldattfqv
       61 avltaaawlp wllaglpvga wvdrvrrrpv miaadlaaaa lfasvpvaal aglltvghll
      121 ivalgaglar vffetadqvy lptllrpeqv peanarlhat qtasylvgpg laglvaqlvg
      181 avtavaldaf sfllsalclr riradeprpr rpagstslrr evaaglrfvv rdpylrvltv
      241 fgaasniglt gyqavlvvfl vrsadlpagl vglliglasl ggvigatlaa rlsrrlgsar
      301 tllvagaltg ppalliplag pgartgwlvl ggvlvslgva vgnvvkgsfr qtytphrllg
      361 rvtvsmhlln ygtiplaall agalgavwgp ggairamtaw laltplilla gplrkrrdlp
      421 aapf
//
LOCUS       WP_457609372             357 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Micromonospora aurantiaca (nom.
            illeg.)].
ACCESSION   WP_457609372
VERSION     WP_457609372.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..357
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38079
     Region          40..297
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(45,48..50,53,64,66,98,117..120,219,221,223..224,226,
                     238..239,242,257..258,261)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(45,49,53,64,66,98,117..120,219,223..224,226,
                     238..239)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(48..50,219,221,224,239,242,257..258,261)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mtdpaadvaa pptgsaprgl dldrlaahla vhrpdlsgpl sarliaggks nltyllrtgd
       61 revvlrrppl ghvlatahdm arehrvisal aptgvpvpea lllcadesvi gapfylmakv
      121 dgevyrrreq tdaltaaqrr dlamammdtl atlhrvepae vgladfgrpe gylarqvrrw
      181 agqldrsrsr plpgtdelrd alaasvpega nagrivhgdy rldnllatvd pvavravldw
      241 ematlgdpla dlgllltywd vlgdsdhgag npvadgigpr agfptgaeli eryagrsdvd
      301 vgplhwhval gcfklavice gihyrhtlgq tlgegfdrig dmvaplvahg lhavres
//
LOCUS       WP_457609373             519 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609373
VERSION     WP_457609373.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..519
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56508
     Region          4..507
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mthfdrrtll raglvagagv aggallgapg apaapglrrs grpllthgvq sgdvtadsal
       61 vwtradrpgr mlvevsrrpd lrgarlvrgp vvdptgdltg kvrlrglpag erlhyrvrve
      121 sldrhglcse pltgsfatap grhqrrdvrf vwtgdivgqg wgistdfdgl aiframrerr
      181 pdfflcsgdt vyadgplaes vvlpdgrtwr nlvtpekskv aetlteyrgq faynlldehl
      241 rafaaevpqi nqwddhevvn nwypgeiltd erygekrvdv laararqafh ewlpvpsggp
      301 myrklsygpl ldvfvldmrt ykdpndgnty adrsrgllgr aqrewlirel rasratwkvi
      361 andlpigvvv pdgsaaqegv aqgdngapag relefaevlr ashragvtgl vfltadvhyt
      421 aahhydpara avrdfspfwe fvsgpahaga fgpnaldgtf gpkavfvhap prantspaeg
      481 fqhfgevtid gpsaaltvhl rdragaslwt ttlpapsrr
//
LOCUS       WP_457609374             146 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609374
VERSION     WP_457609374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..146
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16041
     Region          10..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrmdmaava peayqavlgl ekyvranvdh tvlelvklra smrngcafcv dmhsrealaa
       61 gedsrrlfav aawreapffd erertalalt davtrlgehg vpddvwdaaa kvwsekelad
      121 lvmaiatinv wnrvavtcrt qppaqv
//
LOCUS       WP_457609377             444 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609377
VERSION     WP_457609377.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..444
                     /product="bifunctional folylpolyglutamate
                     synthase/dihydrofolate synthase"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0004326 - tetrahydrofolylpolyglutamate
                     synthase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008841 - dihydrofolate synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006730 - one-carbon metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46852
     Region          5..444
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msdrtefaev eaalnargft rmhfelekie tlldllgspq raypsihltg tngktstarm
       61 idsllrafgl htgrytsphl etvrerisld geavseerfv styreiapla elvdqrfaep
      121 ltyfdmttal afatfadapv dvavvevglg gaedatnviq agvavitpig ldhtewlgdt
      181 iedialhkag iihpgatvia aaqeqeaarp ilercaevna tvaregaefg vlrravavgg
      241 qvltiqglgg vyeeifiplh gahqaqnaav alaaveaflg agarrqldid avregfaats
      301 spgrlervrs aptvlldgah nphgmaatva avqeefafsk lvgvlavlgd kdaasllell
      361 epvldsivva enssarampv delaalarei fgpervqvtr empdaieaav aeaeadvpge
      421 lagvgvlitg svvtvadarr llkr
//
LOCUS       WP_457609382             313 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609382
VERSION     WP_457609382.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..313
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33038
     Region          37..311
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mdtrtaerpd ttpapaappa gvvavvahrk ktfgggldel rsrlvaagvg rllwyevpks
       61 rkapkrvraa ldsgaelvlv wggdgmvqrc adalagsgvp mgilpagtan lfavnlgipv
      121 dlpeavrial hgrrreldlg ringehfavm agagfdgdli rdadrqlkgr fgriayvwtg
      181 lrhvrgecvr trirvdgads fddeascvlf gnvgtitggi pafddarpdd galevgvsta
      241 sgavdwartl grmaagrsee spfvritrgr kikvrfdapk tyeldggarg kaerlkvkvv
      301 pgaltvccpd pad
//
LOCUS       WP_457609390             498 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609390
VERSION     WP_457609390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..498
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50705
     Region          10..497
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgggmstalg trdfllpdlg eglseaeive wrvavgdvvt vdqtvvevet akavvdvpcp
       61 yagrvvalhg aagevrpvgq plitiasldd apdphatyre eeragsgnvl igygtghggt
      121 grrrrrprla lapepgtpva sdpvpgpaag apagtpapas plpagssrpv gldpagvsvp
      181 ngtaapadrt aepaqtgaqs aplvispivr rlakehgidl aslrgtgpgg virradldaa
      241 vaapaaatrl aavpdapaah aglapagdgd tvipltgirk viadklsrsr reipevtiwv
      301 dvdatgllet raainaatpd tpvsilalla riclsglrry pqlnahvdte gqrivqsagv
      361 hlgiaaqtdr glvvpvlrda qrlttrelaa alaettaavr agtlpparlt ggtftlnnyg
      421 vfgvdgstpi inhpeaallg vgrivdkpwv vdgqlavrkv tqisltfdhr vcdggvaggf
      481 lrhvadcveq pallvanv
//
LOCUS       WP_457609404             736 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-galactosidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_457609404
VERSION     WP_457609404.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..736
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=80160
     Region          21..275
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          285..622
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(328,359,403,469,473,513,532,535)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          639..720
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mtivhlrrar tslvldargp glprvvhwga dlgplpdedl pavvdatvpp vvpssfdtpt
       61 alsllpeasa gwsgrpglag hrdgrdwsta frltgldvhd epaappellg gdplhapgvn
      121 kgpflssgrv vvraadpgag lsltveitld aagvltlrhr lrndgdgrye vreltpvlpv
      181 pavatelldl tgrwcrerap qrhpwpmgaw vregrhgrtg hdatlllvag tsgfgfrhge
      241 vwavhtawsg dhvtaaerrp tgestlggge llapgeivlg pgeeyatpll yaahsadgld
      301 glsdalhthl rartshprtp rpvtlnvwea vyfdhdldrl rtladraaev gverfvlddg
      361 wfrgrrhdqa glgdwwvdge vwpdglqpli dhvrghgmqf glwvepemvn pdsdlfrahp
      421 dwvlqapgrl pppwrhqqvl dlahpdayay llerldavls ehdglaylkw dhnrdlteag
      481 hagrpgvhaq tlavyrllde lrarhpdvei escssggarv dleilrrtdr vwasdcndal
      541 erlsiqrwtg lllppeligt higpershtt hrvhdlsfra vtalfghhgi ewdisaiepg
      601 eraelaawva lhkrlrpllh tgrvvrvdhp dpavqahgvv ahdsshavya vsrlatsaaq
      661 vpgqvrlpgl dpqrryrvrp pagvpepall elsppgwlaw pgdgitvtgs vlgsvglqlp
      721 alhpeqalll evtvdg
//
LOCUS       WP_457609405             276 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Micromonospora aurantiaca
            (nom. illeg.)].
ACCESSION   WP_457609405
VERSION     WP_457609405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..276
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30182
     Region          1..274
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvlvplllvt glvwlpavat vllsgtnwdg igpiseiewv gaknyddvvn iyppfvpavq
       61 nnllwlaalf vvatpfgmfl avlldkelrg srfyqtalyl pvvlslalig fvwqliysrd
      121 qgllngvfgg dtdwygdpdv niwavlvaag wrhvgyimll ylaglkgvdp slreaaavdg
      181 ssetstffrv vfpvlrpini ivlvvtvies lrafdlvwvi nkgrngleli salvtqnvvg
      241 easrigfgsa latimlavsl vfitiylwtv mredkr
//
LOCUS       WP_457609408             865 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609408
VERSION     WP_457609408.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..>865
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <69..865
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 msvgivgaqa tdvagpgfei ldlmgdlrrp aawparaasa yrradlpvpa garspgpvll
       61 agllgvlary tgqaevavgl ssggvlrvdv adepgfgelt srvatalagp varsagtagp
      121 vvvglvdapv aevgpdvvdv divvtvagdg salrvdyaad gfsadwvrgl vdqtvsllsa
      181 gvrepgvplg alpllgater erllawgrgp arpvpgvplh elvlewarrt pdavagvaag
      241 evltyaelar rsgelaarlr smgvrpgdvv slaldrsmwt lvatlavlra gaaytpmdvs
      301 wpaermrmll adhgarvvlt vgevaprvpr pdgvrvvald adwptvtaae aadlpvvaps
      361 rpafviytsg stgtpkgvvl thehltnfvt wmreecavgp dsrmlhscsp vfdvalgeiy
      421 taltsgarvv vssrddllda rrlteliake qathafcppt nlaavdpadc psltcvtlag
      481 epipprmahr wtaagarlin aygpaeasva ctwydaskgw pgayvpigrp mpnrqirvvd
      541 anldlvpmgv pgeilitgag vadgylnrpe ltaqrfvtdp ygggtayrtg dlgrwnaaga
      601 leilgrmdhq vkvngiriel geieatleqh pdvgtavvtr redqgtarlv gyvtgrdgrv
      661 pvtadlraha aavlppymvp avimvldrfp tggtgkidrr alpepgsrrp dldvpytepa
      721 tdserlvagi fatvlgldrv galdgffhlg gtslqsaava valdeaadvv vpvsqihrtp
      781 tphelarwla taprrpgaep apsvtgrpgp skpvpltpsv akcvvlpfel vcpttwwieg
      841 eldlralmaa lgdihhrhqa lhary
//
LOCUS       WP_457609415             196 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Micromonospora
            aurantiaca (nom. illeg.)].
ACCESSION   WP_457609415
VERSION     WP_457609415.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         <1..196
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <1..182
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 feqyphefsg gmrqramiam alvndpdlli adepttaldv tvqaqildll adlqeefrsa
       61 ivlithdlgv vsqvaddvlv myagrgvehg svqrvmrapq hpytwgllss vpslhgdada
      121 dlvpipgnpp slinlpsgca fhprcrwagv ngdrsrteip elgpagaagh lvachlsagd
      181 reriyrdeva qvgvar
//
LOCUS       WP_457609429             571 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 39 protein [Limosilactobacillus
            fermentum].
ACCESSION   WP_457609429
VERSION     WP_457609429.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 571)
  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 571)
  AUTHORS   Ernst,J.F. and Prill,S.K.
  TITLE     O-glycosylation
  JOURNAL   Med Mycol 39 Suppl 1, 67-74 (2001)
   PUBMED   11800270
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 571)
  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 571)
  AUTHORS   Gentzsch,M. and Tanner,W.
  TITLE     The PMT gene family: protein O-glycosylation in Saccharomyces
            cerevisiae is vital
  JOURNAL   EMBO J 15 (21), 5752-5759 (1996)
   PUBMED   8918452
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10590977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..571
                     /product="glycosyltransferase family 39 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61869
     Region          22..180
                     /region_name="PMT_2"
                     /note="Dolichyl-phosphate-mannose-protein
                     mannosyltransferase; pfam13231"
                     /db_xref="CDD:433048"
ORIGIN      
        1 mskswhnfwy aifdpagfit vdkppvalwf mvicvkifgl hgwsivlssv lfgigsvyli
       61 ykmvkptfgp ltariaaffm titpivvads rtnnmdatlv fflllagwvl qravrkrrgw
      121 lvlvsfalvg vafnikmlqa ymvlpamyly ywvasrqnwk rvltqtvlat lalavvslsw
      181 plavdstsks mrpyigssst nsvlnlafgy ngtqrlfgqt tgtggtfsgm gtkasgktkt
      241 gaptggtkqg gmkkpaggap tgqakptsgm kkgttnggkp sgkslssmpk ttkgrptgmk
      301 ggagqggngi fnvgtagvtr lfqtalrrqi swflplalfg mvaaylaayd rkkkwwqtnr
      361 kqqdvlywag wlipvgaffs vanffhpyyt imlapplavl aalaitsglk katskrddkr
      421 arwlryllfm glgttaclqs yyvwayypwl slvililtav alvmmtlipa kerlfltlgv
      481 gflclapgfw altptisges aavpttglgt gtvntqliky lkqhngkstt ylfattdsnt
      541 aapyiiktgq avmtiggyng tdnaislkkf k
//
LOCUS       WP_457609432             218 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Limosilactobacillus reuteri].
ACCESSION   WP_457609432
VERSION     WP_457609432.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..218
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23996
     Region          1..217
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mhgfkgnlgy ddskilyvls hylnqqgist lrfdfdgtgh sdgefkdmtv fseildgmki
       61 idyahttmqa kkiylighsq ggvvalmlaa yysdiitklv llapaatlkd dalkgvcqgs
      121 qydlnhipet vdmhgftvgg dyfrtaqllp iyetaqhysg ptllihglad nvvspeaskk
      181 ynvimpnsel hlipgeghmf ngsrrqeilk lvanflkn
//
LOCUS       WP_457609457             140 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Mediterraneibacter gnavus].
ACCESSION   WP_457609457
VERSION     WP_457609457.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter gnavus
  ORGANISM  Mediterraneibacter gnavus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Mediterraneibacter gnavus"
                     /db_xref="taxon:33038"
     Protein         1..140
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=16580
     Region          <81..140
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mmkpsefqtt ienqfdyick vamederkdy lkalsrqckr etlfcdmddy tvnlfssedt
       61 ypshfhtfem dgftvriens llaealenld gkkrdvilry yflgfddtei skilevnrst
      121 iqrrrhaglq fikkfmeeea
//
LOCUS       WP_457609487             207 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Mediterraneibacter
            gnavus].
ACCESSION   WP_457609487
VERSION     WP_457609487.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter gnavus
  ORGANISM  Mediterraneibacter gnavus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Mediterraneibacter gnavus"
                     /db_xref="taxon:33038"
     Protein         1..207
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24510
     Region          5..68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mkishlgnni qtirkfrgmk qqeladkigi nmqslskier glnypayetl ekimevldvt
       61 pnellsgewk yvnqsekevc qflraeerln aelkhghydn ffdseeewle yeleklreyi
      121 tdyingksie asdlypikef iqhlkfqkll dryddlysmd mfgesieghk yktpyqvvkm
      181 inpnskedme llsklpwvtg kfddede
//
LOCUS       WP_457609498              56 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Mediterraneibacter
            gnavus].
ACCESSION   WP_457609498
VERSION     WP_457609498.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter gnavus
  ORGANISM  Mediterraneibacter gnavus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 56)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 56)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 56)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..56
                     /organism="Mediterraneibacter gnavus"
                     /db_xref="taxon:33038"
     Protein         1..56
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6387
     Region          <14..53
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mgqksvkssv fsllsrhyck nkisridlki larlceylkc dltdilklve eeeens
//
LOCUS       WP_457609546             120 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Lutibacter sp.].
ACCESSION   WP_457609546
VERSION     WP_457609546.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..120
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13345
     Region          19..>101
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 meiqkptveq ilskmkgsmn gelpnvvklv sekmpemlye qirsnmfamp engalenetr
       61 tliylgiaia tgsktcikam lnkakaqnis kdklvetykv aryaessrim gnaellfeei
//
LOCUS       WP_457609522             632 aa            linear   BCT 27-JAN-2026
DEFINITION  amidophosphoribosyltransferase [Lutibacter sp.].
ACCESSION   WP_457609522
VERSION     WP_457609522.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Smith,J.L.
  TITLE     Glutamine PRPP amidotransferase: snapshots of an enzyme in action
  JOURNAL   Curr Opin Struct Biol 8 (6), 686-694 (1998)
   PUBMED   9914248
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1005923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..632
                     /product="amidophosphoribosyltransferase"
                     /EC_number="2.4.2.14"
                     /GO_function="GO:0004044 - amidophosphoribosyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006164 - purine nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0009113 - purine nucleobase biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71769
     Region          3..610
                     /region_name="PurF"
                     /note="Glutamine phosphoribosylpyrophosphate
                     amidotransferase [Nucleotide transport and metabolism];
                     COG0034"
                     /db_xref="CDD:439804"
ORIGIN      
        1 msdaikhecg iamvrllkpl qyykdkygta fyglnkmyll mekqhnrgqd gaglasikfd
       61 vapgiryisr irsnddqpiq difaqingrl nklnedfpnk indvewqnnn apyignlflg
      121 hvrygtfgkn siesvhpflr qsnwmhksli vagnfnmtns pklfndliei gqhpkemtdt
      181 vtvmekighf iddevaslyk kikeeginkk easpliekri nikkilkksa knwdggyama
      241 gllghgdafv lrdpagirpa fyyiddeviv vaserpviqt vfnvaikdvk eidrghalii
      301 krngyvsldk ikeplpqksc sferiyfsrg sdadiyterk nlgkfvfpqv lekinedikn
      361 tvfsfipnta etsffgmrea aedflnlqka kvilkgqrsl svekvkeila erprieklai
      421 kdaklrtfia ddnsrddlva hiydvtygiv kptdnlviid dsivrgttlk qsiikildrl
      481 npkkivivss apqirypdcy gidmaklgdf iafraalall qetqqnnive qvykdckqqq
      541 lledfeitna vvkiydpftn eqisdkiakm lktsvinadi evvyqsvenl hkaipnhlgd
      601 wyftgdyptp ggnrvvndaf infyegsnkr ay
//
LOCUS       WP_457609847             116 aa            linear   BCT 27-JAN-2026
DEFINITION  toxin-antitoxin system YwqK family antitoxin [Lutibacter sp.].
ACCESSION   WP_457609847
VERSION     WP_457609847.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Brantl,S. and Muller,P.
  TITLE     ToxinAntitoxin Systems in Bacillus subtilis
  JOURNAL   Toxins (Basel) 11 (5) (2019)
   PUBMED   31075979
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 706116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..116
                     /product="toxin-antitoxin system YwqK family antitoxin"
                     /calculated_mol_wt=13557
     Region          <47..106
                     /region_name="YwqK"
                     /note="Antitoxin component YwqK of the YwqJK
                     toxin-antitoxin module [Defense mechanisms]; COG2849"
                     /db_xref="CDD:442097"
ORIGIN      
        1 mmkaiismvi llfsitafsq eqrveyekis nnlvkatyyf vdnsdiiqre gffnsnnqlq
       61 dmwvsyding nkkiiayydk nkkvgvwtyf skdkinfvty kenkligvee kllvvn
//
LOCUS       WP_457610018             254 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Lutibacter sp.].
ACCESSION   WP_457610018
VERSION     WP_457610018.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13745342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..254
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29536
     Region          <121..173
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     Region          <126..239
                     /region_name="arsM"
                     /note="arsenite methyltransferase; PRK11873"
                     /db_xref="CDD:237007"
ORIGIN      
        1 mkgffkfiln tiprpllikv sywvrplisf ylkgttyidp idgksfrafl pygygkqrln
       61 alspstfsle rhrllwlylk netnfftkqk kvlhiapeqc flkpfkalhn ldyitadlys
      121 piadvkadic dlpfkentfd vilcnhvleh ieddkkamse llrvlkpggm gifqvpqdln
      181 rektyedsti tsaeertkhf gqydhvriyg kdyfdklrti gftvneidys sklpnnliek
      241 yclvkgeilp vcfk
//
LOCUS       WP_457610066             238 aa            linear   BCT 27-JAN-2026
DEFINITION  3'-5' exonuclease [Lutibacter sp.].
ACCESSION   WP_457610066
VERSION     WP_457610066.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Rothwell,P.J. and Waksman,G.
  TITLE     Structure and mechanism of DNA polymerases
  JOURNAL   Adv Protein Chem 71, 401-440 (2005)
   PUBMED   16230118
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Shevelev,I.V. and Hubscher,U.
  TITLE     The 3' 5' exonucleases
  JOURNAL   Nat Rev Mol Cell Biol 3 (5), 364-376 (2002)
   PUBMED   11988770
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Zuo,Y. and Deutscher,M.P.
  TITLE     Exoribonuclease superfamilies: structural analysis and phylogenetic
            distribution
  JOURNAL   Nucleic Acids Res 29 (5), 1017-1026 (2001)
   PUBMED   11222749
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Taft-Benz,S.A. and Schaaper,R.M.
  TITLE     Mutational analysis of the 3'-->5' proofreading exonuclease of
            Escherichia coli DNA polymerase III
  JOURNAL   Nucleic Acids Res 26 (17), 4005-4011 (1998)
   PUBMED   9705512
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..238
                     /product="3'-5' exonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27740
     Region          10..223
                     /region_name="DNA_polB_like1_exo"
                     /note="Uncharacterized bacterial subgroup of the DEDDy
                     3'-5' exonuclease domain of family-B DNA polymerases;
                     cd05782"
                     /db_xref="CDD:99825"
     Site            order(14..17,117..118,121..123,171..172,209,213)
                     /site_type="active"
                     /db_xref="CDD:99825"
     Site            order(14,16,123,209,213)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99825"
     Site            order(15..17,117..118,121..122,171..172,209,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99825"
ORIGIN      
        1 mnlklnfeni lfldietvpe venftdltea kqelfalktq yqrkedfspe dfyekagiwa
       61 efgkivcisv gyftnfnkan rafritsffg devkiledfk kllnshfnka qhllcghngk
      121 efdfpyiarr miinqielpe klnlfgkkpw eiphldtmel wkfgdykhft slklltsilg
      181 ipspkddidg sevgavfyke knikrivkyc ekdtiavaql llrfnnepli eevniirv
//
LOCUS       WP_457610288             254 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Lutibacter sp.].
ACCESSION   WP_457610288
VERSION     WP_457610288.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 254)
  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 254)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19802864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..254
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28226
     Region          26..231
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(134..135,138..139,141,165,169..170,173..174,
                     176..177,203,206..207,210..211,214)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          134..158
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          138..248
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          163..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..227
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 matykktgsk akkkhasved ksttaevfnt ldetasrsek wviknqktif ivlglivvli
       61 lsylpyqkyi kapkekeaan elafpkvyfd eankssvavd sllnlglnga dgkygfidia
      121 seykgtkagn ianyyagisy lklknykqai dylekyssed ellapiakga igdafsdinq
      181 pedaldyylk aanlrdnnfs tplflfkagn tamdleqysk alelfnrikl dyptsdeakn
      241 idiyiskaty askk
//
LOCUS       WP_457610504             478 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Lutibacter sp.].
ACCESSION   WP_457610504
VERSION     WP_457610504.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 478)
  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 478)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 478)
  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 478)
  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 10157591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..478
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54392
     Region          65..284
                     /region_name="CESA_like"
                     /note="CESA_like is the cellulose synthase superfamily;
                     cd06423"
                     /db_xref="CDD:133045"
     Site            175..177
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133045"
     Region          <272..>339
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
ORIGIN      
        1 mntttlngii qvihylffgy aflaissyii lsiisafeti eyfkknsfin ykkilssnaa
       61 psisiiapay neslnivenv rsllsnhyvn ydviivndgs kdnsleklie aydlvnvdyl
      121 inqqistqpl rkgvfkstnp afeklivvdk enggkadaln mglnisnsky vacidvdcll
      181 ledalqkmvk pfleatekkv vatggviria nssiikdgkl mdvnlptkli ekaqileylr
      241 sfllgrmaws rlngllvisg afgmfdkkia ievggydtst vgedmeiivr vrryleekkv
      301 nykvayipdp lcwteapdny kifisqrnrw trgtievlrk hrkiafnpny rnlgllsypy
      361 wliferfapv ievigiiyfg ilialnevkw dyalaffila ylftillslg aifseeltyh
      421 qykkkktglk liiisllepf vlhpfilyaa vrgnldyffn kkkkwgemtr kglgnink
//
LOCUS       WP_457610830             479 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease [Lutibacter sp.].
ACCESSION   WP_457610830
VERSION     WP_457610830.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Ruiz,N., Gronenberg,L.S., Kahne,D. and Silhavy,T.J.
  TITLE     Identification of two inner-membrane proteins required for the
            transport of lipopolysaccharide to the outer membrane of
            Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 105 (14), 5537-5542 (2008)
   PUBMED   18375759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10509922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..479
                     /product="LptF/LptG family permease"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54533
     Region          6..451
                     /region_name="LptF_LptG"
                     /note="Lipopolysaccharide export system permease
                     LptF/LptG; pfam03739"
                     /db_xref="CDD:427477"
ORIGIN      
        1 mkildkyilk sflqpflatf fvvlfvlvmq slwlafdeia gkgidiffil kflgylaltl
       61 tpmalpigil lssimalgnl senyefaalk sagislkrim rpliifilfi svfnfiflnn
      121 iypwatlkqk nlylnikkkk palalvpgaf nteipgysik fdekygeekn llknvqiadl
      181 sgangkikvi takrgiiste egskymtltl kdgnyyedyi krtaprkeka kmpfsnatfd
      241 tyiinidiss fndednldke dikqhhsmls itqldsiskv nkitydkfis srakyfydmi
      301 egeklikypd slidskldpe ilnnfnlnnk tivlneslql lkriidqssn qktsfknkrk
      361 llnlydhefy yrisfslacl vlffigaplg siirkggfgl pmimaitifv iyffisklgg
      421 nlseesaist llgswlstii llpfgilltr ratkgmgvyn idavfekiqn iykkfikrn
//
LOCUS       WP_457610865             326 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Lutibacter sp.].
ACCESSION   WP_457610865
VERSION     WP_457610865.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         <1..326
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Site            order(45,48..49,52..53,55,79,82..83,86..87,89..90,113,
                     116..117,120..121,124)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          45..72
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          58..>166
                     /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          62..>321
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          77..107
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          112..140
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 ncilqigmkq aylhrlllii ilmvlsvska qevkvideeq hlkfqtfffe alkqkaikny
       61 gkaienlekc yeidslnigv efelsknelf lknyaeavff idkalekepk nsyllkhkvt
      121 iykaqrnfkd aieiqkkvve iqpnnidell llyfenknfk kaekliveie kkafssqrik
      181 rlkkylenrk lldkkvnvki tssfsdikil ketynqkkey ktlveilnre vekelfedly
      241 ndslqalelf ptqpylykin gfalnklgky neaidvltlg idfvidntvm eadfyeelsk
      301 sykglndtnk alkfmkkaks lrnkik
//
LOCUS       WP_457610968             290 aa            linear   BCT 27-JAN-2026
DEFINITION  phospholipase D-like domain-containing protein [Lutibacter sp.].
ACCESSION   WP_457610968
VERSION     WP_457610968.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 60949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..290
                     /product="phospholipase D-like domain-containing protein"
                     /calculated_mol_wt=33632
     Region          16..113
                     /region_name="PLDc_SF"
                     /note="Catalytic domain of phospholipase D superfamily
                     proteins; cl15239"
                     /db_xref="CDD:472788"
     Site            order(84,86,98,100,111)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197200"
     Site            84
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197200"
ORIGIN      
        1 mkiippyqit seilnlines ekyliivspy vnfknwdrik idiknalkrn vqinfytrfd
       61 nenfksweei ealgikpkli knlhaklyfn eksgivtsmn lltssnlnai efgsiyntes
      121 eltelrgfvk kylesnleke kpndedlyla kekfdivlsn flshhleryv scrwnngvln
      181 vnannqyfms idkvkklfsv sgiisgyend sfgifysknk gkfktsdifv qgekgcmasa
      241 vlltkksfts snfdflsvfe kkeildisln firelksfkd dcyknrkasf
//
LOCUS       WP_457610964             561 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Lutibacter sp.].
ACCESSION   WP_457610964
VERSION     WP_457610964.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 561)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 561)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..561
                     /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=60781
     Region          7..552
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,383,386..387)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mdiqtwtwgi vgftftlyig iaiwsrasst gefyvagkgv hpianglata adwmsaasfi
       61 smaglisfsg ydgsvylmgw tggyvllall lapylrkfgk ftvpdfigdr yysdvarvva
      121 vvcaliisft yvagqmrgvg lvfsrflevn intgviigmf ivlfyavlgg mkgitytqva
      181 qycvlifafm vpaifisiqm tgnpipqlgf gssadgvyll dkldglhrel gfheytsgnk
      241 skidmffitg almvgtaglp hvivrfftvk kvsdarksag wallfiaily ttapaiavfa
      301 rinmietvsn kkytelpnwf snwektglis fddknndgli qyvadtsvne ltidkdimvl
      361 anpeiaylpn wvialvaagg laaalstaag lllvisasis hdiikkivnp kisekgelva
      421 arlsaviavi iagwfginpp gfvaatvala fglaaasffp aivlgifykr mnregavtgm
      481 vvgmflmlyy mmrfkfdwfg ggtkddwwfg vspegfgtfa mlvnfvvslv iasftpkppk
      541 evqeivdnir iplganeaqi h
//
LOCUS       WP_457611215             115 aa            linear   BCT 27-JAN-2026
DEFINITION  translation initiation factor [Lutibacter sp.].
ACCESSION   WP_457611215
VERSION     WP_457611215.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000256
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..115
                     /product="translation initiation factor"
                     /calculated_mol_wt=12613
     Region          6..115
                     /region_name="SUI1"
                     /note="Translation initiation factor 1 (eIF-1/SUI1)
                     [Translation, ribosomal structure and biogenesis];
                     COG0023"
                     /db_xref="CDD:439794"
ORIGIN      
        1 mgkklnsldd lggfvfstnn nfefneeqne etrtpnkqfl eahfsnkgra gktvtvisgf
       61 igdkadlksl skllktkcgv ggsikdneii iqgnyrdkim iilkkegynv krvgg
//
LOCUS       WP_457615587             116 aa            linear   BCT 27-JAN-2026
DEFINITION  translation initiation factor [Lutibacter sp.].
ACCESSION   WP_457615587
VERSION     WP_457615587.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000256
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..116
                     /product="translation initiation factor"
                     /calculated_mol_wt=12832
     Region          7..116
                     /region_name="SUI1"
                     /note="Translation initiation factor 1 (eIF-1/SUI1)
                     [Translation, ribosomal structure and biogenesis];
                     COG0023"
                     /db_xref="CDD:439794"
ORIGIN      
        1 mskkklnsle dlggfvfstn tdfefnqnke ketlppsqqy lealfskkgr agktvtvirg
       61 fvgneidlka lakllktkcg vggsvkdfei iiqgnyrdki mdilkregyn vkrigg
//
LOCUS       WP_457615672             828 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Lutibacter sp.].
ACCESSION   WP_457615672
VERSION     WP_457615672.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 828)
  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 10154659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..828
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=93989
     Region          45..>171
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Region          111..323
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06238"
                     /db_xref="CDD:349457"
     Site            order(119,122,182,201..202,231..232,236,307)
                     /site_type="active"
                     /db_xref="CDD:349457"
     Region          609..>667
                     /region_name="A4_beta-galactosidase_middle_domain"
                     /note="A4 beta-galactosidase middle domain: a type 1
                     glutamine amidotransferase (GATase1)-like domain; cd03143"
                     /db_xref="CDD:153237"
ORIGIN      
        1 mkkvilsvcv llvgfssliq aqhikspsef lgyelgtrft rhhkvvdyfk yvssisknvk
       61 lekygetnef rplyvvyiss eenianieni rennlkqagi vqgtaalktg ivwlsynvhg
      121 neassteaam qtmytlittk sewlkntlvi idpcvnpdgr dryvnwynqt kstpydtnpd
      181 aiehhepwpg grpnhylfdl nrdwawatqv etqqrlmvyn kwlphvhvdf heqyinnpyy
      241 fapavepfhe iitdwqrsfq tqigknhaky fdkngwryft kesfdlfyps ygdtyptymg
      301 avgmtyeqag hgkaglgidl angavltlvd rvkhhtttgl stvevasknt tklitefgkf
      361 fnntnlkykn yivrgnhtki nqvvsllnkh qinsyrasqk tikafdyytg ttksvrinsg
      421 dlvistnqpk gkmvkvlfep eaklsdslty ditawsipfa yglhgfatty siekssttpq
      481 teivknniqk tayayvckwd evadaaflgk lleadfkvrf shkkfsvdgn qfergslvil
      541 rgenkhlqnf delitdisnq mnekltpast gfvdygadfg sdyvafiehk kvavisgegt
      601 sslsfgeiwh ffetqlqypl hiintayfnh tdldeynvli lpngfrasek qlkkitsfae
      661 kggnviaigs alnsfadkeg fnlkrkkddd esdeddtakk dmkklfipyn qleresvkss
      721 itgsifksti dnthplaygy tntyyslkls asaydvledg fnvgyfpegt tttsgfagve
      781 alekvqnsll fgieyqgkgk iiymvdnplf rsfwehgklf vanaiffn
//
LOCUS       WP_457615918             238 aa            linear   BCT 27-JAN-2026
DEFINITION  3'-5' exonuclease [Lutibacter sp.].
ACCESSION   WP_457615918
VERSION     WP_457615918.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Rothwell,P.J. and Waksman,G.
  TITLE     Structure and mechanism of DNA polymerases
  JOURNAL   Adv Protein Chem 71, 401-440 (2005)
   PUBMED   16230118
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Shevelev,I.V. and Hubscher,U.
  TITLE     The 3' 5' exonucleases
  JOURNAL   Nat Rev Mol Cell Biol 3 (5), 364-376 (2002)
   PUBMED   11988770
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Zuo,Y. and Deutscher,M.P.
  TITLE     Exoribonuclease superfamilies: structural analysis and phylogenetic
            distribution
  JOURNAL   Nucleic Acids Res 29 (5), 1017-1026 (2001)
   PUBMED   11222749
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Taft-Benz,S.A. and Schaaper,R.M.
  TITLE     Mutational analysis of the 3'-->5' proofreading exonuclease of
            Escherichia coli DNA polymerase III
  JOURNAL   Nucleic Acids Res 26 (17), 4005-4011 (1998)
   PUBMED   9705512
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..238
                     /product="3'-5' exonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27824
     Region          10..223
                     /region_name="DNA_polB_like1_exo"
                     /note="Uncharacterized bacterial subgroup of the DEDDy
                     3'-5' exonuclease domain of family-B DNA polymerases;
                     cd05782"
                     /db_xref="CDD:99825"
     Site            order(14..17,117..118,121..123,171..172,209,213)
                     /site_type="active"
                     /db_xref="CDD:99825"
     Site            order(14,16,123,209,213)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99825"
     Site            order(15..17,117..118,121..122,171..172,209,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99825"
ORIGIN      
        1 mntkidfeki lfldietvpe eadfsklsee kqdlfalkta yqrkeelspe afyeragiwa
       61 efgkiicisv gyftnfnske mvfrvksfyg eettllnefk nlletyynkp phvlcahngk
      121 efdfpyiarr miinkivlps klnlfgkkpw eiphldtmem wkfgdykhft slklltsilg
      181 ipspkgdidg smvakvyyee knikriveyc erdtiavaql llrffgydli neekiifv
//
LOCUS       WP_457616010             562 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Lutibacter sp.].
ACCESSION   WP_457616010
VERSION     WP_457616010.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 562)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 562)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..562
                     /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=60547
     Region          7..553
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,384,387..388)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mtlqlwtwal igitfalyig iaiwsranst kdfyvagggi splanglata adwmsaasfi
       61 smaglisfng ydgsvylmgw tggyvllall lapylrkfgk ftvpdfigdr yysniartva
      121 vvcalivsft yvagqmrgvg lvfsrflevd intgviigmi ivlfyavlgg mkgitytqva
      181 qycvlifafm vpalfisiqm tgnpipqlgf gstgtdgvyl ldkldglhka lgfheytsgs
      241 kstidvffit aalmvgtagl phvivrfftv kkvsdarksa gwallfiail yttapaiavf
      301 srtnlietvs nknydelpew fsnwektkli kftdknndgk vqyvanpein eltvdkdimv
      361 lanpeiaqlp nwvialvaag glaaalstaa glllvisssv shdlikkmin paisekgelv
      421 aarlsaivav viagyfginp pdfvaatval afglaaasff paiilgifhk kmnkegaiag
      481 mvigmltmlf ymlkfkfdwf gggtkndwwf gispegfgtv amllnftvsi ivanftpnpp
      541 esvqelveni ripsnatkpq ah
//
LOCUS       WP_457616094             254 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Lutibacter sp.].
ACCESSION   WP_457616094
VERSION     WP_457616094.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 254)
  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 254)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19802864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..254
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28118
     Region          40..194
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(134..135,138..139,141,165,169..170,173..174,
                     176..177,203,206..207,210..211,214)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          134..158
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          138..248
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          163..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..227
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 matykktgsk vkktqhntee kyttaevfnt ldetaskseq wviknqkqif ivlgvivagi
       61 laflayqkyv qapkekeaad elafpkayfe dainnsvavd slltlslnga dgkygfvdia
      121 teysgtkagn lanyyagiay lklknyeeai kflenfssed ellapiakga mgdafadinq
      181 lddaleyylk aadlrdnnfs tplflfkagn tamdlgkydk aldifnrikt dypnsneakn
      241 idiyinkatf askq
//
LOCUS       WP_457616122             482 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease [Lutibacter sp.].
ACCESSION   WP_457616122
VERSION     WP_457616122.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Ruiz,N., Gronenberg,L.S., Kahne,D. and Silhavy,T.J.
  TITLE     Identification of two inner-membrane proteins required for the
            transport of lipopolysaccharide to the outer membrane of
            Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 105 (14), 5537-5542 (2008)
   PUBMED   18375759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10509922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..482
                     /product="LptF/LptG family permease"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54566
     Region          6..451
                     /region_name="LptF_LptG"
                     /note="Lipopolysaccharide export system permease
                     LptF/LptG; pfam03739"
                     /db_xref="CDD:427477"
ORIGIN      
        1 mkifdkyilk sflkpflatf fvvlfvlvmq alwlafdqia gkgidlvfil kflgylalil
       61 tptalpigil lssimalgtl aenyefaaik sagvslkrvi kplvflaill savnfvflnn
      121 iypwatlkqk nlylnmkkkk palalvpgaf ntdipgysik fdekygpeen llknvqiadl
      181 skgkgkikvi takkgtiste egskymtlil edgyyyedhl kkmmtidera hmpasratfk
      241 kyiinidiss fnddeslnqe kikehhgmls isqldsiskk nkiaydafie srarnfylti
      301 gankiydypd slihkklkpe ilenfvpknq klvlsnaiqi lkrvmdrkkn qkkgfkdkrk
      361 llnlydyeys yrisfalacl vlffigaplg siirkggfgl pmvmaitifv iyffisqfgk
      421 nlaeesaiss llgswlstii llpfgimltv raakgmgifn inlffdkvln ffkklklikk
      481 np
//
LOCUS       WP_457616232             415 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Lutibacter sp.].
ACCESSION   WP_457616232
VERSION     WP_457616232.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..415
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47314
     Region          117..300
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          234..261
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          239..>411
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          267..295
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(268,271..272,275..276,278,302,305..306,309..310,
                     312..313,336,339..340,343..344)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          300..330
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkkqllflsa fiisltifgq kselktaeka lksnnfaaam aainqaegli anadqktkak
       61 fyylkgkaly qngaantdie ktakafnqll dfeketkkyk yskeigelin kliddtanka
      121 sesyklaakt kapedykvaa knfhqvylls prdtsyldna alvyylgkdy dtsiklyqql
      181 ldlgytgiak iykatekesg kdlifpdkks mdlqvklgla enprtemkes rreyifknla
      241 qsyaakdnpd kaleilaqgr kefpnsysll ideaniyykk gdkqrfkdnl elaislnpte
      301 ptlyfnvgvm nmdlgyeeea vknftkaiel dpeygnaynn lgsiilkkse avqeelnkna
      361 mdfakydkik eekllpiyre alpyfekays flkteqlknl vnslyenldm ekrie
//
LOCUS       WP_457616344             251 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Lutibacter sp.].
ACCESSION   WP_457616344
VERSION     WP_457616344.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18109313
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..251
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29221
     Region          109..224
                     /region_name="COG4627"
                     /note="Predicted SAM-depedendent methyltransferase
                     [General function prediction only]"
                     /db_xref="CDD:443666"
     Region          <118..170
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mfkfilntip rpllikasyw vrpfvalylk gskytdpidg rsfrkflpyg yqsqrknals
       61 pstfslerhr llwlylknkt sffsaklkvl hiapeqcflk ifkkqknldy itadlyspia
      121 dvkadicnlp fannsfdvvf cnhvlehied dkkamselyr vlkpggmgif qvpqdlnrek
      181 tyedftitdp kerakhfgqy dhvrvygrdy fnklraagft vkevdytqii dksllekfcl
      241 segeilpvct k
//
LOCUS       WP_457616657             599 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Lutibacter sp.].
ACCESSION   WP_457616657
VERSION     WP_457616657.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 599)
  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 599)
  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 599)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19997826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..599
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68408
     Region          13..343
                     /region_name="AAA_15"
                     /note="AAA ATPase domain; pfam13175"
                     /db_xref="CDD:433011"
     Region          <182..468
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mikkielkkf kkyknqiihl rskgitilag gnnsgkstll haiavwefsk lilelekgkk
       61 alladskeqg lgisadeflp iaiptlkhlw tnlktqkdge dndgynlkik cfwdigenek
      121 yleislslvn drlfikatss nlllddyipt aaylptfagi lekenkvsla errkyigkgl
      181 agsvlrnlll elyennqkvr ndlkngkski sskelknlre tdpfelllks irtyfktsir
      241 ikkfndlyht aikidsfkge ftdkgifkkf ptfnyrdlmv egsgflqwln vftlslnpdi
      301 diilldepda hlhpslqidl inelskiskn kqtliathss eiiryvnpyk ilninksspk
      361 ylkeekqkvg llagiganyl pkidnikrtk kvlfvegeid lkllkkvgel igepinneii
      421 pwitssghke rkhlflelkk eipelkglsv rdrddegint vqndlidkvh dvqdenlkim
      481 kwkrrnlesy lilpnviski tnvsieeint hitekfgivi aenykesnap davlhingkk
      541 nllgdensif kkygvtikei itnltkndic edlitmvkti nshfvpphqn ikhliqkql
//
LOCUS       WP_457616782             632 aa            linear   BCT 27-JAN-2026
DEFINITION  amidophosphoribosyltransferase [Lutibacter sp.].
ACCESSION   WP_457616782
VERSION     WP_457616782.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Smith,J.L.
  TITLE     Glutamine PRPP amidotransferase: snapshots of an enzyme in action
  JOURNAL   Curr Opin Struct Biol 8 (6), 686-694 (1998)
   PUBMED   9914248
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1005923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..632
                     /product="amidophosphoribosyltransferase"
                     /EC_number="2.4.2.14"
                     /GO_function="GO:0004044 - amidophosphoribosyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006164 - purine nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0009113 - purine nucleobase biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71740
     Region          3..610
                     /region_name="PurF"
                     /note="Glutamine phosphoribosylpyrophosphate
                     amidotransferase [Nucleotide transport and metabolism];
                     COG0034"
                     /db_xref="CDD:439804"
ORIGIN      
        1 msdaikhecg iamvrllkpl qyykdkygta fyglnkmyll mekqhnrgqd gaglasikfd
       61 vnpgiryisr irsnkahpiq difsqiderl ndfttrfpdk kddvqwqvnn lpyignlflg
      121 hvrygtfgkn siesvhpflr qsnwmhksli vagnfnmtns lrlfndlvel gqhpkemtdt
      181 vtvmekmghf iddevaelyq eiksegigkk easplieqri niqkilkksa knwdggyama
      241 gllghgdafv lrdpagirpa fyyvddevvv vaserpviqt vfnvaindvk elerghalii
      301 krngkiside ikeqlpkksc sferiyfsrg sdadiyterk nlgklvfpqi lkkinndikn
      361 tvfsyipnta etsfygmrea aedflnlqkt eailkgqrsl saeavtkila erprveklav
      421 kdaklrtfia ddssrddlva hvydvtygiv kpndnlvvid dsivrgttlk ksiikildrl
      481 npkkiiivss apqirypdcy gidmakmgdf iafraalall kevdryhive evyksckqqq
      541 dlediavkna vkeiynlftd eqisdkiaem lktddisaei evvfqsvenl hkacpnhlgd
      601 wyftgnyptp ggnrvvndaf infyegksgr ay
//
LOCUS       WP_457616876             115 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Lutibacter sp.].
ACCESSION   WP_457616876
VERSION     WP_457616876.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..115
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13146
     Region          4..114
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mpnnveefda yrkrmndkil atdnkvikri fnldtnayke ghlpvktkel lglvastvlr
       61 cddcikyhle tcfkegvskd evmetlsiat lvggtiviph lrrayefwee letkn
//
LOCUS       WP_457616933             406 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Lutibacter sp.].
ACCESSION   WP_457616933
VERSION     WP_457616933.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118302
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..406
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44509
     Region          17..394
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
     Region          215..399
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 miltifkkdl klffsnkknv vltflipill islfafafgg istsssenkq vtllytrfdt
       61 slisnkikaq ldtlstinlv qvtleegnka llkgknagfl ilneglkdsl llskklpivf
      121 kydasnpfea kmlqsivtgv vmntigsqly mhkiahymdt kfksmpadlk qriltdvskv
      181 slknkistvv savpvvkkss ntgnlgliqa vagtaimmll fsisgvgggl leekesgtls
      241 rllytpikpt ailygkmlat lfismlqlvt mfvfswiafg lpifkditsl illtiavafs
      301 vssfgvflvs vsktrqqlqn lstiiillms aiggsmiplf vmpnimqkia vislnywgiq
      361 gyydifwrnl siveilprig vlgliglvml lisiplfkrn ivaltn
//
LOCUS       WP_457617134             482 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Lutibacter sp.].
ACCESSION   WP_457617134
VERSION     WP_457617134.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 482)
  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 482)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 482)
  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 482)
  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 10157591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..482
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54938
     Region          68..284
                     /region_name="CESA_like"
                     /note="CESA_like is the cellulose synthase superfamily;
                     cd06423"
                     /db_xref="CDD:133045"
     Site            175..177
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133045"
     Region          <267..>401
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
ORIGIN      
        1 mdpktvhtli lifhylflvy tvavitsyvv lsiisaketv eykkknsfvn yseilsssis
       61 psisiiapay neslniienv rsllsshyvn ynviivndgs tdnsleklie aydlvkidyl
      121 ineqiitkpl regifkstnp afeklivvdk enggkadaln mglnisnney vacidvdcll
      181 ledalqkmik pfleatsvkv iatggviria nscvikdgkl idinlpnslm eiaqileylr
      241 sfllgrmaws rlngllvisg afglfdkria idvggydttt vgedmeiivr mrrfmedkke
      301 kykvayipdp lcwteapdny ktlisqrnrw trgtietlkk hrkigfnsky rslgllsypy
      361 wfffermapi velagiiyfa ilvaldyvrw dyalaffvaa ylftltftiv aifseeltyh
      421 qykkkgtgfk llvttilepf ilhpfilyaa ivgnidyyfn kekkwgkmtr kglvksknyq
      481 dn
//
LOCUS       WP_457617530             632 aa            linear   BCT 27-JAN-2026
DEFINITION  amidophosphoribosyltransferase [Lutibacter sp.].
ACCESSION   WP_457617530
VERSION     WP_457617530.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Smith,J.L.
  TITLE     Glutamine PRPP amidotransferase: snapshots of an enzyme in action
  JOURNAL   Curr Opin Struct Biol 8 (6), 686-694 (1998)
   PUBMED   9914248
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1005923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..632
                     /product="amidophosphoribosyltransferase"
                     /EC_number="2.4.2.14"
                     /GO_function="GO:0004044 - amidophosphoribosyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006164 - purine nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0009113 - purine nucleobase biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71817
     Region          1..610
                     /region_name="PurF"
                     /note="Glutamine phosphoribosylpyrophosphate
                     amidotransferase [Nucleotide transport and metabolism];
                     COG0034"
                     /db_xref="CDD:439804"
ORIGIN      
        1 mseaikhecg iamvrllkpl qyykdkygta fyglnkmyll mekqhnrgqd gaglasikfd
       61 vtpgtryisr irsnddqpiq difaqingrl nklnedfpnk indvewqnnn apyignlflg
      121 hvrygtfgkn siesvhpflr qsnwmhksli vagnfnmtns pklfndliei gqhpkemtdt
      181 vtvmekighf iddevaglyk kikeegvskk easpliekri nikkilkksa knwdggyama
      241 gllghgdafv lrdpagirpa fyyvddevvv vaserpviqt vfnvaikdvk eidrghalii
      301 rrnghismdr ikeplpqksc sferiyfsrg sdadiyterk nlgkyvfpkv lekinkdien
      361 tvfsfipnta etsffgmrea aedflnlqka kiilkgqrsl svekvkeila erprieklai
      421 kdaklrtfia ddnsrddlva hiydvtygiv kptdnlviid dsivrgttlk qsiikildrl
      481 npkkivivss apqirypdcy gidmaklgdf iafraalall qetqqndive fvykdckqqq
      541 tledfeitna vvkiydpftn eqisdkiaem lktsvinadi eivyqsvenl hkaipnhlgd
      601 wyftgdyptp ggnrvvndaf infyegsnkr ay
//
LOCUS       WP_457617588             561 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Lutibacter sp.].
ACCESSION   WP_457617588
VERSION     WP_457617588.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 561)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 561)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..561
                     /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=60778
     Region          7..552
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,383,386..387)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mdiqtwtwgi vgftftlyig iaiwsrasst gefyvagkgv hpianglata adwmsaasfi
       61 smaglisfsg ydgsvylmgw tggyvllall lapylrkfgk ftvpdfigdr yysdvarvva
      121 vvcaliisft yvagqmrgvg lvfsrflevn intgviigmf ivlfyavlgg mkgitytqva
      181 qycvlifafm vpaifisiqm tgnpipqlgf gssadgvyll dkldglhrel gfheytsgnk
      241 skidmffitg almvgtaglp hvivrfftvk kvsdarksag wallfiaily ttapaiavfa
      301 rinmietvsn kkytelpnwf snwektglis fddknndgli qyvadtsvne ltidkdimvl
      361 anpeiaylpn wvialvaagg laaalstaag lllvisasis hdiikkivnp kisekgelva
      421 arlsaviavi iagwfginpp gfvaatvala fglaaasffp aivlgifykr mnregtitgm
      481 vagmflmlyy mmrfkfnwfg ggteddwwfg vspegfgtfa mlvnfvvslv iasltpkppk
      541 evqdivdnir iplgtnkaqi h
//
LOCUS       WP_457617924             823 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Lutibacter sp.].
ACCESSION   WP_457617924
VERSION     WP_457617924.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 823)
  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 10154659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..823
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=93990
     Region          45..>171
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Region          111..322
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06238"
                     /db_xref="CDD:349457"
     Site            order(119,122,182,201..202,231..232,236,307)
                     /site_type="active"
                     /db_xref="CDD:349457"
     Region          610..>668
                     /region_name="A4_beta-galactosidase_middle_domain"
                     /note="A4 beta-galactosidase middle domain: a type 1
                     glutamine amidotransferase (GATase1)-like domain; cd03143"
                     /db_xref="CDD:153237"
ORIGIN      
        1 mkksiftiit vcffstasiy sqnlkspsef lgyelgshft rhskvidyfn yisntsknve
       61 lekygetnen rplyvsyiss eeninnleei rkdnlkrtgi lkgntnskig ivwlsynvhg
      121 neassteaam ltlytlitkk qdwlkntivi idpcinpdgr eryvnwynqt kstpyntnpd
      181 asehhepwpg grpnhylfdl nrdwawatqv etqqrlkiyn kwmpqihvdf heqginnpyy
      241 fapasepfhe iitdwqrnfq ieigknhaky fdengwryft kerfdlfyps ygdtyptymg
      301 aigmtyeqag ngrsglgitl enkevltlkd rilhhtttgl stvevatans skmitefkkf
      361 fdtsnlkyks yilrgdkeki nsvikllkkh eissyfsvpk tikaydyysk ktktikltkn
      421 dlivstnqpk gkmvkvlfel eaklsspity ditawsipfa yglhgfssev eivkntsssn
      481 tnsvtpiqin kntyayihkw deisdaeflg dllekkfnvr lsnkdfsing kkykkgtivi
      541 mkgenkhisd fdetitkian qlktpltstt tgfvtsgydf gssyfslikp kkiavlagng
      601 tsslsfgelw hffetqlnyp ltvintsyfk qidltkyqvl ilpngyrstk dalkkitaft
      661 ssggtviavg sslnnfannd dfllkknnse nkdsikpsen ltpygerqrt dikkritgsi
      721 fksnidnthp laygytnnyf slklssnsfk llkegenigy fpensksisg yagekavvfv
      781 snsllfgieh kgkgkiiymv dnplfrsfwe ngklffanav ffn
//
LOCUS       WP_457618127             480 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease [Lutibacter sp.].
ACCESSION   WP_457618127
VERSION     WP_457618127.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Ruiz,N., Gronenberg,L.S., Kahne,D. and Silhavy,T.J.
  TITLE     Identification of two inner-membrane proteins required for the
            transport of lipopolysaccharide to the outer membrane of
            Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 105 (14), 5537-5542 (2008)
   PUBMED   18375759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10509922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..480
                     /product="LptF/LptG family permease"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54684
     Region          7..452
                     /region_name="LptF_LptG"
                     /note="Lipopolysaccharide export system permease
                     LptF/LptG; pfam03739"
                     /db_xref="CDD:427477"
ORIGIN      
        1 mlkildkyil ksflqpflat ffvvlfvlvm qslwlafdei agkgidvffi lkflgylalt
       61 ltpmalpigi llssimalgn lsenyefaal ksagislkri mrpliifilf isvfnfifln
      121 niypwatlkq knlylnikkk kpalalvpga fnteipgysi kfdekygeek nllknvqiad
      181 lsgangkikv itakrgiist eegskymtlt lkdgnyyedy ikrsaprkek ekmpfsnatf
      241 dtyvinidis sfndednlnk edikqhhsml sitqldsisk vnkitydkfi ssranyfynm
      301 iegkklikyp dslidhklds eilnnfnlnn knivlneslq llkriidqss nqktsfknkr
      361 kllnlydhef yyrisfslac lvlffigapl gsiirkggfg lpmimaitif viyffisklg
      421 gnlseesais tllgswlsti illpfgillt rratkgmgvy nidavfdkiq niykkfikrn
//
LOCUS       WP_457618340             408 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Lutibacter sp.].
ACCESSION   WP_457618340
VERSION     WP_457618340.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118302
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..408
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45107
     Region          17..396
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
     Region          217..401
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mittifkkdl klffsnkknv vltflipill islfafafgg istksseykq vtllyadfds
       61 sstskkikeq ldtisavnlm qvtleegsna llkgkysgfl ilnkglkdsl llskklpity
      121 kydasnpfea kmlqsiitgv imstigsqly irkvenyint efktmpnnlk qriltdisqv
      181 sfknkastsa iieavpvike ssntgnlgli qavagtaimm llfsisgvgg glleekesgt
      241 lsrllytpik ttsilygkml atlfismlql ftmfvfawia fdlpifkdli slilltiava
      301 fsvssfgvfl vsvsktrqql qnlstiiill msaiggsmip lfvmpsimrk iavislnywg
      361 iqgyydifwr nlstfeilpr igvlnligiv mllisiplfk rnivsltn
//
LOCUS       WP_457618897             254 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Lutibacter sp.].
ACCESSION   WP_457618897
VERSION     WP_457618897.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter sp.
  ORGANISM  Lutibacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13745484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Lutibacter sp."
                     /db_xref="taxon:1925666"
     Protein         1..254
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29461
     Region          <119..173
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     Region          <125..224
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mkdffkfiln tiprpllikv sywvrplisf ylkgttytdp idgksfrafl pygygkqrsn
       61 alspstfsle rhrllwlylk nettfftsak kvlhiapeqc flkqfkalsn ldyitvdlns
      121 piadikadic dlpfkedtfd iilcnhvleh iendkkamse llrvlkpggm gifqvpqdln
      181 rektyedfti tspeerskhf gqydhvriyg kdyfdklrav gftvneidys ntlpnnliek
      241 yclvkgeilp vcfk
//
LOCUS       WP_457621000             330 aa            linear   BCT 27-JAN-2026
DEFINITION  cache domain-containing protein [Pantoea ananatis].
ACCESSION   WP_457621000
VERSION     WP_457621000.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Cheung,J., Bingman,C.A., Reyngold,M., Hendrickson,W.A. and
            Waldburger,C.D.
  TITLE     Crystal structure of a functional dimer of the PhoQ sensor domain
  JOURNAL   J Biol Chem 283 (20), 13762-13770 (2008)
   PUBMED   18348979
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10499564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..330
                     /product="cache domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36122
     Region          35..261
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
ORIGIN      
        1 mlkrkihlrl lltsltaggv iitcmlmiga lflfqkkyie esllsdniay aqkladttdr
       61 ylktaqqela wsaseintld dvvqlasese rlrlqsdffn tvvvvnrnav vtatspqslk
      121 lvgvrlkpva slqsidmekp yisppfvaet gnyvifisqp lftskgnylg yiggtiylkk
      181 qsmlsdilsr hffgkdsvvs ivsnegliiy sqdpgktgtk mflpvsiqkr ladtksgqkn
      241 ghklligyan lrstgwnvfm tgtsetvkai llnsvrntfw fiigilalts gvmallagri
      301 alpleklaam vreggsnata esvigthawy
//
LOCUS       WP_457620999             174 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Pantoea ananatis].
ACCESSION   WP_457620999
VERSION     WP_457620999.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..174
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18540
     Region          9..158
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(41,84)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(46,49..50,54,58,80,82..85)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(76,104)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 maaisdeamt dpltglynrr gftvtadevv dsaehciiai didhfkyind kfghdagdfa
       61 lvglaellak asrpmdlvsr fggeefiilm pntslldgaa taerirlevn kanfpgvgrm
      121 avsagvavfs gqevaheeal rhadealyfs kragrnqvsv sisgkiivpf stvg
//
LOCUS       WP_457621009              65 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Parabacteroides merdae].
ACCESSION   WP_457621009
VERSION     WP_457621009.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     Protein         1..>65
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          26..>63
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mpndmekdle lrvselekml flsknvlsfd easrflnlsk sylykltsgn liphykpqgk
       61 mlyfe
//
LOCUS       WP_457621072             363 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Persephonella sp.].
ACCESSION   WP_457621072
VERSION     WP_457621072.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 363)
  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 581140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..363
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42903
     Region          54..>155
                     /region_name="PHP"
                     /note="Polymerase and Histidinol Phosphatase domain;
                     cl23724"
                     /db_xref="CDD:451507"
ORIGIN      
        1 miylillaif lvfasflfyl efrpirkiki desnisslse sfpeeifryn vishihtqfs
       61 fdslgkpsdi rravevneid fvfvtdhdnd nykffedhri fagiekntpd grllllgnel
      121 pvishpnnfe fehyrwkgef kedhlyeiid ikdgivwskv ftgltlikni llypftrnil
      181 hkwnalipld rwvdlyfera kglkliggld lhikfvyqeh thgvlipsyq egfkwlvnkv
      241 fskseirnke dildalrrgl lyislkkkeg yfwgsngfni ylfwekmpvg ssincdfrel
      301 rtikilkcnn spvlvteenr fsytayrpgy yhfevyeydf kignlyfgvr pvavtnmfev
      361 vnv
//
LOCUS       WP_457621116             664 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Persephonella sp.].
ACCESSION   WP_457621116
VERSION     WP_457621116.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..664
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=74833
     Region          59..297
                     /region_name="NIT"
                     /note="Nitrate and nitrite sensing; pfam08376"
                     /db_xref="CDD:462453"
     Region          143..664
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mhlfsnlsik tkllilslvp ilvillfagy lfitnynkym eekaleqavk lsvkisavvh
       61 evqkergrta gflgskgref rselsaqrkl tdekvrdlkn yiksvdlshl peglkmeikv
      121 ilekvdtipl irkevddfsi tlkdaigqyt einqkllhai gsiakyssda kitrqlaayv
      181 nfllakermg ieravlsavf ardtfnehly qrflsllseq kafltgfkll asddflkfyk
      241 ktmvgkavke vermekiale kaseggfdld psywfdmitq kinlmkkved ymskkliddi
      301 taeedrvlrn lmietvfslv visailylgf iirksinrsi dtikndvnyi aetkdftrki
      361 hletkdemhe iadainnfid askkaieqak msaeenasia selsatavei gkraeeeski
      421 vmettekalg tqeplrnlvg kldetreeik kangilnras sqineliltv krsaeeemgi
      481 vkeletlkks tdktqevlkl iediadqtnl lalnaaieaa ragevgrgfa vvadevrsla
      541 eksreyvdsi tetiseline inlitekisf naenitrlte sssnverdvd evtsvmdqtv
      601 kmaddasisv rsivseieei ikdiekinei sganarsvee iatatehlyk lienlnkile
      661 efkt
//
LOCUS       WP_457621293             140 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Persephonella sp.].
ACCESSION   WP_457621293
VERSION     WP_457621293.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     gene            1..140
                     /gene="rimP"
     Protein         1..140
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=16052
     Region          1..139
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mllplleerg lklvdieyit egrpilriyi ynpegttied cewisrriga lldiedlipv
       61 sytlevsspg lerklknvee ydifkgrdik ivlkqpvnkr nvikgvlkgr kdnnvvveee
      121 gkeiniplee iaranlefkh
//
LOCUS       WP_457621337             266 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Persephonella sp.].
ACCESSION   WP_457621337
VERSION     WP_457621337.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..266
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28421
     Region          10..265
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 mfneeqffkd dklvigdref tsrlivgsgk ykdfeetaka teasgaeiit vavrrvnitd
       61 pdkpnlldyi dtskvmilpn tagcytaeea iltaklarea lghgfvklev igdqktlypd
      121 mvetlkaaev lvkegftvlp yttddpimak kfedigcaav mplaapigsg lglqnpynii
      181 fikeavnvpv ivdagigtas daaivmelgv dgvlmntaia qakdpikmav amkyavkagr
      241 laylagripk kmyasasspi egiigr
//
LOCUS       WP_457621610             325 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Persephonella sp.].
ACCESSION   WP_457621610
VERSION     WP_457621610.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14206253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..325
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=38174
     Region          30..322
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK00059"
                     /db_xref="CDD:234605"
     Region          169..311
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mlkvlifllg fvisavgyeg fgwkidpstk nkvvakvgdt eitemevqrm mkillpmnfy
       61 hrnitddklk eirekaiknl iyrellyyea kkkglkvtde eidklmeqli kqykskenle
      121 kllketgltl edfkkelekr llveklikey itvsltekdl keyyeknkek fkepasvkar
      181 yiyikidptd pegrkkarek akkayqeike gkdfgdvayr ysddlsrikg gdigyvhkgr
      241 fpkqieekiy nldigqvsei ietdtglhiv kiegkrpsrl vpfeeikdkl kkeltqsmqe
      301 kkfnelieda kkhlkveiye ekkds
//
LOCUS       WP_457621680             469 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Persephonella sp.].
ACCESSION   WP_457621680
VERSION     WP_457621680.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..469
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54264
     Region          1..116
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          247..>389
                     /region_name="polC"
                     /note="DNA polymerase III PolC; Validated; PRK00448"
                     /db_xref="CDD:234767"
ORIGIN      
        1 mkeitlilhg wsdcsdsfkd lkaflikngi gsvdtiyyad yesrednvtf ediidglydr
       61 fkekgfidkh gnktadlnvi vhstgglvir hfiaeyyrhr ldrcpvkkiv mlapanfgsp
      121 lahygksllg rvfkgrykfg dlfevgrkll nglelaspyq wklahldllv espyfnrnqi
      181 qtfifvgnkg ysglrklank kgtdgtvvvc ganlnpvkfi fdfskegkal diyvkdykfd
      241 tafavlrnyd hgsivedikp dkksqigklv lkalriksad eyvafkkdle kitensfknr
      301 eiyqqfivra vddhnkpikd ytieffvyry nnryikngef irkkiseeee lwskkiheli
      361 tdefhnnstd psfrrflvgi krlkgeieec ckslgsdivl smkiyvprvd egiyyetekl
      421 kniillktkd gkivnekpsi fypntttfie mkinrstkyv tvdikpkkh
//
LOCUS       WP_457621821             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Persephonella sp.].
ACCESSION   WP_457621821
VERSION     WP_457621821.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..358
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40324
     Region          1..309
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          173..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrafiaillk elvvfvrnwg lilvliysft idiyiagqgf evkprnvsvg yvdyssgvis
       61 kkilshlhpp efkepvrfns qeelsraifn reiivgivfe pdfekdfikg katvnillds
      121 taaaqayitl tyirnilvrf hrfdtpveik thklfnqnad trkfisfsef lsivtlvgvi
      181 lsavvfvrek engtwdimll tpvnpkliil aktfsqmiii magvivsvgl ilfgvfdvpi
      241 ngsfivfimf tftflfaitg iglfiasvak smlqvaqlsv vimmpmifls gawtpihsmh
      301 pfiqylsyis plryyiegcl siffrgidsp dllphfaalt vlstalyifg frkigklf
//
LOCUS       WP_457622004             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457622004
VERSION     WP_457622004.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51320
     Region          1..446
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 miridytnvm aetigerdgi lreellsfrh fviethariq kekerkfyft klpyqdtqdi
       61 kefakeiser fdyfvligig gsslgaqmlf eslksinhni ydkpkffimd nvdpdkfssi
      121 leiidiektc fnvvsksgst vetianfaii ldilkkrlgd swnehlvftt dpekgflkkf
      181 geensikilq vppkvggrfs vlspvgifpa avlgididql legakkmdlv csieehvehn
      241 payliaithy ianmrrgkti svmmpysekl ssfvdwyrql waeslgkdgl gqtpvkalgt
      301 vdqhsqiqly rdgirdkiit fiqverraed fkipdeiped ihylsghtlh eilnkellgt
      361 kaalikskvp nitismdkis pynigmliyl yematgfsgy lykinpfdqp aveegknfty
      421 almgregysq kleefeelyk ekykieiq
//
LOCUS       WP_457622036              95 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Persephonella sp.].
ACCESSION   WP_457622036
VERSION     WP_457622036.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..95
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10767
     Region          6..84
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mgklkvvvdr ticegigpca eetkyieldk rhkavviepd kpkeevmeka qhvkrqevil
       61 dltpeeeeei frsaeacpvk aifiydpetg eqlyp
//
LOCUS       WP_457622666             127 aa            linear   BCT 27-JAN-2026
DEFINITION  YbbR-like domain-containing protein [Persephonella sp.].
ACCESSION   WP_457622666
VERSION     WP_457622666.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1003777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..127
                     /product="YbbR-like domain-containing protein"
                     /calculated_mol_wt=14524
     Region          4..>121
                     /region_name="YbbR"
                     /note="Cyclic di-AMP synthase regulator CdaR, YbbR domain
                     [Signal transduction mechanisms]; COG4856"
                     /db_xref="CDD:443884"
ORIGIN      
        1 mekikgifln nlplkilsll vafllwlnit stqkarvefy sdveikpypk dliieqiqpe
       61 kvliiiegpk nalsnvnisq iqtyvdgfkl kegenllpve iskdliknfk iisiypdrvl
      121 vyakkrk
//
LOCUS       WP_457623025             933 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Persephonella sp.].
ACCESSION   WP_457623025
VERSION     WP_457623025.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 933)
  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 933)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..933
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=108252
     Region          <238..851
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          307..331
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          343..369
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(345..346,349..350,352,376,379..380,384..385,
                     387..388,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          374..400
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          405..433
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          438..471
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          669..928
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(675..676,679..680,682,706,710..711,714..715,
                     717..718,744,747..748,751..752,755)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          675..699
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          704..735
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          743..768
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(777..778,781..782,784,809,812..813,816..817,
                     819..820,845,848..849,852..853,856)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          777..801
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          806..837
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          844..867
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrilllllvl avtiknvhss vqikvpevvf pieiiaekre eipeikppdi lefkeelkie
       61 lftedikpvp pytvnppvvd mekpksvlgi peknallsgg iddfymgnli sakeklekli
      121 kkypetsnsg tanyvlgliy yklenkkkay ehfkngclhk yvfpqkdtsc lsatllsfqi
      181 gddsltdefl rrikyedins lflhgvnfav ksnteesyrl lkdidcteld infveychyi
      241 kgyvsfsqkd ydravesink vkspvykkhi lvlkgflnle ngkineaeky fndflegygt
      301 vekisnyvly glgvidiekg nlkkgferag sleprdkkla qnlyikladv yserndfena
      361 fallqkslqv sprykeilkk klgitaynrg kynyaylimk nidqpefyly tgytlmkmgk
      421 iplssdyfek avkysidnnl kekalkfltn iylrlnkdqk flsavkqlkd ldedysrnil
      481 gwfffkkkny hkayeaflde ymkavsafns gsldeayqiv kdkkdrksrf llayifmrkg
      541 eiekareilk elsqgndkia keagylyays yfsegnylla iesfknyaer fkgtelgnla
      601 tlrmadsyyn agqkekarri yqqfieehan tpeaidaayq ltvlemeesg sdvaeqierf
      661 ikkypqypfv sllklqladl yteegnyeka ekiylelids dikesenaly klgylkyvsg
      721 dtdnaikilk nylkiypnge fdvqakells kiyeergdld raiavmkklp atdenkfkla
      781 mllykagkyt eaksyfeeiy trfpkyrsdi afylgkiqfe ngyyqnairy leealnssdy
      841 nnvaesyyll giihsklede enalnslinv iylypeakeq vikarlkaae imkkqgrrse
      901 ascilkplss eeltdeqref lkdlmkdlpe cfe
//
LOCUS       WP_457623111             351 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Nocardioides
            secundeburneus].
ACCESSION   WP_457623111
VERSION     WP_457623111.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides secundeburneus
  ORGANISM  Nocardioides secundeburneus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Nocardioides secundeburneus"
                     /db_xref="taxon:3151851"
     Protein         1..351
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38336
     Region          9..288
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          284..340
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(310,312..314,316,327..328,332..333,336,340)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 migqaevlgl peasscrdta rwlqqqtrvt rrsatakvgl atslrsrewt rvamargelh
       61 aeqataiavk larlddervs thdqeraevc lvgeardhda ialgrlghei yahldpdsad
      121 eresaalerl eadaraatrl tmrddghgtt hgqftiptaq aemlrrhlha laapksvrae
      181 qgagsydwlr psaeklgraf vdwierisaa alpdvgglna tvvvigdyda lqgrvkaasl
      241 dtgarishtq flrlacgagv vpmwmnasde llamgrkrrf htakqrlaai veqrhcqhas
      301 gcdvpgylch lhhrepwasg ggtdlrtahl lcpfhhhath aeagrnhpmr t
//
LOCUS       WP_457623321             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457623321
VERSION     WP_457623321.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51392
     Region          1..446
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 miridytnvm aetigerdgi lreellsfrh fvlethaliq kekekkfyfa klpyqdvedl
       61 kilaeeirsk feyfvligig gsslgtemlf eslkdlnhni fdkpkffimd nvdpdkinsi
      121 leridiektc fnvisksgtt vetianfgii lkilkekvgd rwnehliftt dpekgflref
      181 grenniktld ipknvggrfs vltpvgifpa avmgidvdqi legakkmdli csveehvehn
      241 paylialthy ianmrrgksi svmmpysekl ssfvdwyrql waeslgkdgl gqtpvkalgt
      301 vdqhsqiqly rdglrdkivt fiqiekrdid fkipedipes ihylsghtlh eilnkellgt
      361 kaalikskvp nititldkit pynvgmliyl yematgfsgy lykinpfdqp aveegknfty
      421 almgregysq kleefeelyk ekykieiq
//
LOCUS       WP_457623457             651 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Persephonella sp.].
ACCESSION   WP_457623457
VERSION     WP_457623457.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 651)
  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 651)
  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 18562633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..651
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=77754
     Region          <42..106
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          42..70
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(43,46..47,50..51,53,79,82..83,86..87,89..90,122,
                     125..126,129..130,133)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          77..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          82..>306
                     /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          121..147
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(203..204,206,234,237..238,241..242,244..245,271,
                     274..275,278..279,282)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          206..307
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          232..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          267..293
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlkfkiital flaitfttys qqervnsenp vdiyksltke eataiyreav qmykrksyys
       61 alnlltklit hrnnifypda lfltakiyle lgrktgkkdl lqkalnyink ysymaknset
      121 wdfyytkgni yenlymyera ialyklafyr tvtkkqqfkt vaailrtaaw tkrmdlvtry
      181 ivlvnveels heerkefefi egllefqkgn yeeayhylsk vykeyepyli enpyyyyifa
      241 entyrikkye fskqlfrrii slikdeeiir rsllrlgdif nikgdkvtaf nyyysiveky
      301 pdsqeakvgk lkilsmsddk sikekiyllr kkdedfkdpl rfiykmlvsn rntyignfai
      361 gnfgrevfls ksdslfselv relsliyper mlyeqreyte klwkdellkl ssekvcelyk
      421 tnrnffkyif drnvltkivm dlkkcgktkd ridlakwilk kwnddkskll laevyfdngm
      481 fkdsldtlkt vkernckysk lfiknmlslk nyeklnqnyl kickndkegd vlrgilkfik
      541 gdlnsalkif ygvkddlymf ytdsfykkfi qdvveksiee nrykdvvnli spmserlndc
      601 nlfswmvism irtgsgnved yykklkgcet gwsliaknvf ldyqliqeag k
//
LOCUS       WP_457623487             291 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Persephonella sp.].
ACCESSION   WP_457623487
VERSION     WP_457623487.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 79029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..291
                     /product="polysaccharide deacetylase family protein"
                     /calculated_mol_wt=33333
     Region          105..278
                     /region_name="CE4_SF"
                     /note="Catalytic NodB homology domain of the carbohydrate
                     esterase 4 superfamily; cl15692"
                     /db_xref="CDD:472828"
ORIGIN      
        1 mvilivflli iglsygdile ykvvrytfiy ndkrfvslre fndgksvkil avnvdslktd
       61 vfnkgiiiek kfnisdskyk kllrksisde lqnggikngg tdkffltvdl cpsskkepfe
      121 lgiiekfikk ghkdigfavs grwiiknqky lnwikekise gklkviwinh sfnhfydskl
      181 pldknfllkk gtniefeile vekillkngi ipsvfirypg lvadyklrkk vaeryglial
      241 gsdswlakge lptegsiili hgnknepkgi kifekilerd lefmslldlk p
//
LOCUS       WP_457623590             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Persephonella sp.].
ACCESSION   WP_457623590
VERSION     WP_457623590.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..358
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40404
     Region          1..>288
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          173..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mklfttilfk eiltflrnwg lvailiysft idvyiagqgf evkprnvtvg yvdytdgyis
       61 nkilshlhkp efkepiryls pedlkedifn rkiivgiifd pdfeknfykg ytklnvllds
      121 tasaqayitl syleniilnf sdinppvelk ihklfnqnad trkfisfsef lsvvtllgii
      181 lsavvfvrek engtwdimll tpvdpkilil aktisqmiiv ligvimsvgl vlfgvfnvpi
      241 ngsffvfilf ttaylfavtg iglfiasvak smlqvaqlsv vvmmpmifls gawtpiesmh
      301 pviqyisyis plkyyiegsi giffrgvsfs dliihftalt clsislylfg frkigklf
//
LOCUS       WP_457624087             233 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Persephonella sp.].
ACCESSION   WP_457624087
VERSION     WP_457624087.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 233)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  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 13398337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..233
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26633
     Region          <68..233
                     /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"
     Region          167..232
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mdqdlkdaik kleeakqrqe kieriiills glliivifsi iginiysgke etisepeini
       61 vakeekekqe pqpapviqek kqqvvsqpee kkpeekkevq ksavatkqqk eenktpakke
      121 ekpkteqkkk eikavatpek pvsgsekkea kkpekkkpqp qvkttlpsgy yiqagafstr
      181 kkaekllkkl slpnayirke gelykvligs fknrkeayrf mkeknikgfi rki
//
LOCUS       WP_457624316             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457624316
VERSION     WP_457624316.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51063
     Region          1..442
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 mvridytnvm aevigerdgv lreellsfrh fvvevhsiiq keksrkfyfc rlpyqdvshi
       61 keyaqhirek fenfvvigig gsslgakmlf esltdfnynq knspkfylle nvdperfasv
      121 leqidvektc fnvvtksgst vetianfsii msmlkdrlgd rftenlvftt dpekgflrkf
      181 gqehnikifd vpplvggrfs vlsavgllpa avagididql lagakkmdlv csveehvehn
      241 paylialahy itnmrrgkti svmmpyaekl asfvdwyrql waeslgkdgl gqtpvkaigt
      301 vdqhsqiqly regirdkiit fiqvekfstd fripdelped isylsghsla eilnkellgt
      361 kaalikskvp nltivldeis pynigmliym yelatgfsgy lykinpfdqp aveegknfty
      421 almgrkgyee kleefkelyk ekyrievq
//
LOCUS       WP_457624337             323 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Persephonella sp.].
ACCESSION   WP_457624337
VERSION     WP_457624337.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14206253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..323
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=38454
     Region          32..323
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK00059"
                     /db_xref="CDD:234605"
     Region          172..313
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mvrllqilmv lflikgavay qgfswkidpe mkkkvvaevg dvkitemdvq rymkvllpmn
       61 yyhrtvtdek lkelrkkalk alidrellyy eakkkgikip ekeidrlmde lakryksrek
      121 leelvkqtgi tleefreelk krlmidkllk eyvqvnltek dlkeyyeknk ykfkepeslk
      181 vryiyikvdp tkpkgrqiar eraekaykei qegkdfgdva ykysddlsri kggelgyvhk
      241 grfekkieee iyklkpgevs giietelgfh ivkvedkrpe rivpfdkike klrkeltekl
      301 qqekyeklle dakkdvkvvi ynk
//
LOCUS       WP_457625272             110 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Persephonella sp.].
ACCESSION   WP_457625272
VERSION     WP_457625272.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1562428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..110
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=12474
     Region          18..93
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
ORIGIN      
        1 malkiypvse nfspekpvse kliatdnmvi vhfylkkgqk iplhasksdv fvtvlrgkgk
       61 ffygseeqye iletenslyy qpeephgfea eedmivqavi apnpqkkiel
//
LOCUS       WP_457625423             154 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Persephonella sp.].
ACCESSION   WP_457625423
VERSION     WP_457625423.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     gene            1..154
                     /gene="rimP"
     Protein         1..154
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17393
     Region          4..151
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mkeniiervk ellqplieer glklvdveyi tagkpvlriy vynpegtsie dcewisrrig
       61 alldiedlip vsyilevssp gldrklknre eyeifkgrei kiitrepveg knvfegvlkg
      121 lennsvvlet ggktvkiplk nisranleyk igge
//
LOCUS       WP_457625524             120 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Persephonella
            sp.].
ACCESSION   WP_457625524
VERSION     WP_457625524.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..120
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13188
     Region          5..120
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msnndetkid melyykrfla lfeevkkdyp tfvegfmkff qategpgaid kktkelisva
       61 lsvksqcpyc iafhvknaia egatraeive samvaalmgg gpcvaymkyv fdacdqfgak
//
LOCUS       WP_457625595             336 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Persephonella sp.].
ACCESSION   WP_457625595
VERSION     WP_457625595.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 18414217
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..336
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39219
     Region          9..34
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          37..>204
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(78,81..82,85..86,88,112,115..116,119..120,122..123,
                     144,147..148,151..152,155)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          78..105
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          80..331
                     /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          110..139
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          143..171
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          176..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          211..246
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maslevlqli ekaklafese nyemaqvyld eallqspdip evyfwrgkva ttdlndevie
       61 taigdftqav elkpdyweay fergkvylyf ekfeeaeedf kkvirlnpsf kdvysylaqi
      121 eiqrgndeka meylnnvttg gdfkyyynlg kiflnaknys aaienftkal ednkylvdgy
      181 ylrskayeav gkyrealedl kkaatltpee kkfftdmakv yfkkamkaad egdirksadl
      241 fieglkinyn lkirpeyeki leeaakdamk kgeyrqavly lefaervvdn rcvdeqlpfe
      301 ecykrkqein almkqaekgl plkeriikkl ndiyak
//
LOCUS       WP_457625597             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457625597
VERSION     WP_457625597.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51213
     Region          1..446
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 mikidytnam aetigerdgi lreellsfrh fvvethsliq kekerkfffc klpyqdttqi
       61 kefaqhirek fdyfvvigig gsslgakmlf esltdfnyni qekpkfflle nvdpekfdsi
      121 lgqidikktc fnvvtksgst vetianfsii lsmlkkelgd ryrehlvftt dpekgflrkl
      181 gqsegikmfd ippkvggrfs vlspvgllpa avlgididql lsgarkmdlv csieehvehn
      241 paylialihy itnmrrgksi svmmpyaekl asfvdwyrql waeslgkdgl gqtpvkaigt
      301 vdqhsqiqly rdgirdkiit fiqvdkmstd fkipdelped iayltghslh eilnkellgt
      361 kaalikskvp nitvildein pynigmlvym yelatgfsgy lykinpfdqp aveegknfty
      421 almgrkgyen kleefkelyr ekyrieiq
//
LOCUS       WP_457625613             266 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Persephonella sp.].
ACCESSION   WP_457625613
VERSION     WP_457625613.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..266
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28169
     Region          10..265
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 midaqqllkd dkliigdkef ssrlivgsgk ykdfeetaka teasgaemit vavrrvnitd
       61 pdkpnlldyi dtskvmilpn tagcytaeea vltaklarea lghgfvklev igdqktlypd
      121 mvetlkaaei lvkegftvlp yitddpvmak kfedigcaav mplaapigsg lglqnpynil
      181 fikeavsvpv ivdagigtas dasvvmelgv dgvlmntaia qakdpikmav amkhaviagr
      241 laylagripk kmyasasspl egvigr
//
LOCUS       WP_457625859             664 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Persephonella sp.].
ACCESSION   WP_457625859
VERSION     WP_457625859.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..664
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=74462
     Region          59..297
                     /region_name="NIT"
                     /note="Nitrate and nitrite sensing; pfam08376"
                     /db_xref="CDD:462453"
     Region          131..664
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkflnnmsik vkilllvlip llttlfyasi ilyqdydlyk kqayleknvi fstkisalvh
       61 elqkergata gfigsggtkf kkqlsrqrml tdqkraefes ylqkldiqdf peeikvklge
      121 irsqlsrlds irssvdslsi elkdaisyyt klngnllsvi gafakytdda timhemvpyv
      181 dflmakermg ieravlsavf aknaftpely rkyisllseq rafltsfkli apkkmldiyn
      241 rivrgravee vermekiaie nmetgnfnve ptywfktmte kinlmkkved emskmmvgdi
      301 qslkssafkn liavlimtvv vaalivvigy visrsitqnv elieselkdi adskdftktv
      361 evttkdelks iadsvnylie asreaieqak vsaqentsia aelsatavei ekrveeeaei
      421 vnktttkalt iqkplessvs kldrtkeeik randilgkvk eqmiqlistv kqsaaeeeki
      481 vgelerlkes tdrtknvlkl iedianqtnl lalnaaieaa rageagkgfa vvadevrnla
      541 eksreyveni tdtiaellne insiaekist naktvnllae esanvekdve svseamdktv
      601 etsedasesi kaiveeikvl iseiekinei ssantksvee iakatehlya mteklskile
      661 efkt
//
LOCUS       WP_457626082             206 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Persephonella sp.].
ACCESSION   WP_457626082
VERSION     WP_457626082.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 206)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  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 18658991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..206
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23499
     Region          <68..205
                     /region_name="FtsN"
                     /note="Cell division protein FtsN [Cell cycle control,
                     cell division, chromosome partitioning]; COG3087"
                     /db_xref="CDD:442321"
     Region          140..205
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mdqdlkdtik kleeakskqe kieriiills glliviifsi iginvysgke etisepeini
       61 vakqkeieks pplvekpaqe kekkeikavq peksaektek tkteqkivka vpeaekkikk
      121 kekaqpkaqp kkkvaknpfp sgyyiqagaf stkkkaekll kklnlqnaki rkegelykvl
      181 ignfknrkea yrfmkeknik gfvrki
//
LOCUS       WP_457626355             380 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Persephonella sp.].
ACCESSION   WP_457626355
VERSION     WP_457626355.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..380
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=43229
     Region          1..380
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 meikiyegsd leelierakk elgddikilh yetveekkfl ffkgkkkyrl fvepvdeeel
       61 aepvikfeel lekvedlidk kikmtlpkva remanpenip shiqkvrpst avfneftgda
      121 lhlveqlldk dvlpetakkl imegcgldid tnkwdlntvt qkealikgik khirftgafd
      181 kdnqglkifa figptgvgkt tnlfkiasql vidkkkkvav istdtfkvga sqqartyani
      241 lnipfysise skklkntved lknfdfilid tvgrshydyw rlgeikeils sleeninhvl
      301 tiscnykned alevvnkyqt ffpihslfft kidetlkpgl linlpvetkl pvsyvstgqr
      361 vpedlkvltp eviasyiigs
//
LOCUS       WP_457626551              95 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Persephonella sp.].
ACCESSION   WP_457626551
VERSION     WP_457626551.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..95
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10693
     Region          6..84
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mgklkvvvdr ticegigpca eetkyieldk rhkavvlepg kpkeevmeqa qhvkrqevil
       61 dltpeeeeel fraaeacpvk aifiydpetg eqlyp
//
LOCUS       WP_457627130              95 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Persephonella sp.].
ACCESSION   WP_457627130
VERSION     WP_457627130.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..95
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10669
     Region          6..84
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mgklkvvvdr ticegigpca aetkyieldk rhkavimepg kdknqvmeka qhvkrqevvl
       61 dltpeeeeei fraaeacpik aifiydpetg eqlyp
//
LOCUS       WP_457627522             128 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Oceanithermus sp.].
ACCESSION   WP_457627522
VERSION     WP_457627522.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 128)
  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 128)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   3  (residues 1 to 128)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1001321
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..128
                     /product="response regulator"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=14723
     Region          9..>128
                     /region_name="RpfG"
                     /note="Response regulator c-di-GMP phosphodiesterase, RpfG
                     family, contains REC and HD-GYP domains [Signal
                     transduction mechanisms]; COG3437"
                     /db_xref="CDD:442663"
ORIGIN      
        1 mesndalali vspnpplkty lelvfedfgl tphteptplk glhylkehtp riivldelhe
       61 kgldsagfvw rikrikrlkr vptiqivhgs nererltmei sgadhivelp ikdrrfrrmv
      121 eellsisr
//
LOCUS       WP_457627707             323 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Persephonella sp.].
ACCESSION   WP_457627707
VERSION     WP_457627707.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14206253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..323
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=38420
     Region          32..323
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK00059"
                     /db_xref="CDD:234605"
     Region          172..313
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mvrllqilmv lllikgavay qgfswkidpe mkkkvvaevg dvkitemdvq rymkvllpmn
       61 yyhrtvtdek lkelrkkalk alidrellyy eakkkgikip ekeidrlmde lakryksrek
      121 leelvkqtgi tleefreelk krlmidkllk eyvqvnltek dlkeyyeknk ykfkepeslk
      181 vryiyikvdp tkpkgrqiar eraekaykei qegkdfgdva ykysddlsri kggelgyvhk
      241 grfekkieee iyklkpgevs giietelgfh ivkvedkrpe rivpfdkike klrkeltekl
      301 qqekyeklle dakkdvkvvi ynk
//
LOCUS       WP_457627837             233 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Persephonella sp.].
ACCESSION   WP_457627837
VERSION     WP_457627837.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 233)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  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 13398337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..233
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26665
     Region          <68..233
                     /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"
     Region          167..232
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mdqdlkdaik kleeakqrqe kieriiills glliivifsi iginiysgke etisepeini
       61 vakeekekqe pqpapviqek kqqvvsqpee kkteekkevq ksavatkqqk eenktpakke
      121 ekpkteqkkk eikavatpek pvsgsekkea kkperkkpqp qvkttlpsgy yiqagafstr
      181 kkaekllkkl slpnayirke gelykvligs fknrkeayrf mkeknikgfi rki
//
LOCUS       WP_457628257             617 aa            linear   BCT 27-JAN-2026
DEFINITION  polyphosphate kinase [Oceanithermus sp.].
ACCESSION   WP_457628257
VERSION     WP_457628257.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..617
                     /product="polyphosphate kinase"
                     /EC_number="2.7.4.1"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006799 - polyphosphate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=70936
     Region          3..613
                     /region_name="PRK05443"
                     /note="polyphosphate kinase; Provisional"
                     /db_xref="CDD:235469"
ORIGIN      
        1 mrlsrerswf rfnrrvlata rrpdvpller lrylaifaan tdeffsariy rlfqearaar
       61 rlprgyrell gevqqasaea arlfaelrpe laragvrllr peelspteqr yfgaylaevv
      121 apetdlldaa aigdlssqal yfaagrrnlr yllrqptrrr flevpgrpga fvrlgelirw
      181 rsdlflprpm pmyelrltri aqleaerldw eelplalegr ldghpsrlev eqgfpwraai
      241 arslelrdee vfelpapldl ralfeladle rpdlrwpplr lrrrrgftaa pldylrerdl
      301 llyhplddyg qvvafvqaaa rdagvariaa tlyrvgehnp imealmeaae rgkrvevlle
      361 grarfdelvn lywrlqlegr gvrvldyprg kkvhakllla egprgrwlhl gtgnynpana
      421 rvytdlsylt tcpeltadaa nffaalaegr epeltrlwlg srareellar iraaararge
      481 vivkvnhltd vrllralera adegarvrli vrstltrnhp rfqalslvgr fleharvaaf
      541 ktgagwevwa ssadwmernf drrlelffpv qgerdrarvl hglrrqladd vnafvllpdg
      601 rdrprwggrr daqalgl
//
LOCUS       WP_457628609             154 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Persephonella sp.].
ACCESSION   WP_457628609
VERSION     WP_457628609.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     gene            1..154
                     /gene="rimP"
     Protein         1..154
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17338
     Region          4..150
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mkeqiiervr ellqplieer glklvdveyv tagkpvlriy vynpegtsid dcewisrrig
       61 alldiedlip vsyilevssp gldrklknke eyeifkgrdi kvvtkepleg knvfegvlkg
      121 leedevvldt egetvriple avaranlefk agge
//
LOCUS       WP_457629163             502 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Oceanithermus sp.].
ACCESSION   WP_457629163
VERSION     WP_457629163.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 502)
  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 502)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19960403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..502
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=55005
     Region          <33..491
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Site            order(52..53,55,79,82..83,86..87,89..90,113,116..117,
                     120..121,124)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          77..107
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(157..158,161..162,164,188,191..192,195..196,
                     198..199,222,225..226,229..230,233)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          186..216
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          221..249
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          272..491
                     /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          290..320
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          325..353
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          361..389
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          395..423
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(396,399..400,403..404,406,429,432..433,436..437,
                     439..440,463,466..467,470..471,474)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          427..457
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          462..490
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkstwftfll lglgfgavfg qappaqapdp aalearlksq pgdlptmval grayldagry
       61 ddaarvfedv laldyqnfqa hfglglalyr kgdlrgalfe fdqvtrlfpd rfegwynlav
      121 ayadsgrwde aaaafqraia lgeeqklapd vlrpaylgla taqrklgkpd qaaqtlmmaa
      181 ekmgedeeil yliaenlsla gkpkeaipyl ykvlnkdrgn vaavnlladi fvgqglvdra
      241 lreldrslea tqdpairanl llkkamllka idpekaakll eeasaldprl wqahydlgss
      301 wlragdpdra lrafqkaysv nptepkilvg laaayfqkqd ykqayryaql aadssegavk
      361 adalliagks ayrlgryaea ralllravdl apdradawlw lglaayalqd fdtavpaler
      421 avqldpspva klnlgaayla vkrfsdaeqi ltqvvledpe naeawynlgw alnalgrese
      481 aqrawkaald lgyeparsli kk
//
LOCUS       WP_457629272             172 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Oceanithermus sp.].
ACCESSION   WP_457629272
VERSION     WP_457629272.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..172
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19731
     Region          4..151
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          86..171
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mekvhfeplg erdveavfhl warahgvpae rmrqrleima rhfgypgfag lgawregrlv
       61 gfvygftgmp gqwwyervra lmppemarvw lerhfeftel avdpaqwgrg lggrlhdail
      121 khrgeprall tvnadneraq alyrgrgwth lledvrlvka gpllwvmgkr lg
//
LOCUS       WP_457629383             502 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Oceanithermus sp.].
ACCESSION   WP_457629383
VERSION     WP_457629383.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 502)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..502
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57192
     Region          6..500
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mkperaydel rrfqletayy eslgalaawd qrtyiprkgh ahrarqfaal aqllhrrrtd
       61 prigewldal egsplvadpe sptavnvrew rrdyeravrv peklavalae aksegesawe
      121 slraknnwta fkpylkrlld lqreyaevvg yetepydall edyepgerae rltrlfdelg
      181 aatrrlldgi lgssvrppte vlhrdfpvat qrevvhevta algynlesgr idptahpfel
      241 svgpgdvrit tryypdyfna affgsvheag hamyeqglpa ehwgspmgqa vsmgvhesqs
      301 rlwenmvgrs lgfwrrfypl vqarfaalag vpledfhlav navkpslirv eadevtynlh
      361 ilirfelela lfrgelgvdd lpgawnekyr aylgvtppdy kdgvmqdvhw gsglfgyfpt
      421 ytlgnvyaaq lfaraeaelg pqepaferge fapllewmrk kihahgrryp prrlveeatg
      481 epptaiylir yledrfaaly dl
//
LOCUS       WP_457629486             602 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Oceanithermus sp.].
ACCESSION   WP_457629486
VERSION     WP_457629486.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Baharin,A., Ting,T.Y. and Goh,H.H.
  TITLE     Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure,
            Molecular Properties, and Applications
  JOURNAL   Plants (Basel) 11 (10) (2022)
   PUBMED   35631755
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18487223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..602
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67702
     Region          29..188
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          <167..485
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
     Region          349..601
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msvkriplev lfgdpelsqv qvapdggrla fvapweevkn lwvqdrhtge rrrvtadrgr
       61 gvlwyrwlps gllvyaqdkd gdenwrlyav dpvggeprll tpgegvqaql lavhpdypde
      121 llvllndrdp alhdvwrvna rsgerrrvle npgfigflad erlevrlahk ssddgggely
      181 lregdawkpf mrwglddslg tmplrvrgdt lymlssigrd tsalvavdpk sgsqevlatd
      241 pdydldgssl lfhpraekpe aigvmrdrmg wivlddnlqp dfdrlgeleg dvyltsrdle
      301 krvwviyeql drksprywly dhqsgdleli geaipalaey tlapmqpvry rardgleiea
      361 yltlppgrep rglpaviaph ggpwhrdvwg yhpwaqwlan rgyavlqpnf rgstgygkvl
      421 lnagnkewgr amqddltdav rwlveqgiad pgrvaimggs yggyatlagl aftpelyaag
      481 vdivgpsnlf tlletippyw kpmialfytr mghperdael lraasplfsa dkirapllig
      541 qgandprvkr teslqiveal rekgkpveyv eypdeghgfm naenrldfyr raeaflekhl
      601 np
//
LOCUS       WP_457629801             114 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Oceanithermus
            sp.].
ACCESSION   WP_457629801
VERSION     WP_457629801.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..114
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12739
     Region          1..114
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msvrkkiwge haekiarrld aidpdlsryi qdfayeevma rpgldlktre llaitalial
       61 gnpdelkthl rgalangate relretiihs alylgfpral gamkmlaell edrd
//
LOCUS       WP_457629913             502 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Oceanithermus sp.].
ACCESSION   WP_457629913
VERSION     WP_457629913.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 502)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..502
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56864
     Region          3..500
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mnpenayael rqfqietayy hslgalagwd qrtyiprkgh ehrarqfaal aqllhrrrtd
       61 prigewldav sgadflsdpa apaavnvrew rrvyersrrv peelavalaq aqsegesawe
      121 qfrraddweg fwpylkrlvd ltreyaeavg yeseaydall edyepgeraa rlqevfallg
      181 retrslleav laspqqppag vlerdypvev qarvvrelvg rigydleagr idptthpfel
      241 svgpgdvrit tryypdylga alfgaiheag hamyeqglpa ehwgtpmgea agmgvhesqs
      301 rlwenavgrs lgfwrhfypl lqenfsslag vgleefhraa navrpslirv eadeltynlh
      361 iqirfelela lfrreldvad lpgawnekyr dylgveppdy ksgvmqdvhw aaglfgyfpt
      421 ytlgnvyaae lygaaraelg dfeeafarge fapllewlrg rihahgrryq prrlielatg
      481 rppgagtlva ylrerfgnly gl
//
LOCUS       WP_457630408             616 aa            linear   BCT 27-JAN-2026
DEFINITION  polyphosphate kinase [Oceanithermus sp.].
ACCESSION   WP_457630408
VERSION     WP_457630408.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..616
                     /product="polyphosphate kinase"
                     /EC_number="2.7.4.1"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006799 - polyphosphate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69706
     Region          3..616
                     /region_name="PRK05443"
                     /note="polyphosphate kinase; Provisional"
                     /db_xref="CDD:235469"
ORIGIN      
        1 mpvsrelswf rfnrrvlata rrpdvpller lrylaifaan sdeffsariy rlfqearark
       61 rvprayrell aevgdaaaea salyaelare laaagvrlle pagltpteqr yfgaylaeev
      121 aprtdlldaa aigdlssral yfaagrrnlr yllrqppgrr flevpgrpga fvrlgalirw
      181 rsdlflpqpm pmyelrltri arleaarldw eelpqalesr ldgrpsrlev ergfpwraai
      241 arslelrpee vfelpapldl rllfelaald ipglrwpprr prrrrgfaad playlrrrdl
      301 llyhpgddyd qvvafvaaaa rdpgverlra tlyrvgeqnp imdalleaad rgkqvevlle
      361 grarfdelvn lywrlwlegr gvrvldyppa rkvhaklfla eggglryahl gsgnynpeng
      421 rlytdvsllt trpepagdva rffaalrrga vprlrrlltg paarkaflse iaataavrgr
      481 iivkvnhltd arllaalgra aaagarveli vrstltglpp garavsivgr yleharvmaf
      541 cregelsvwa gsgdwmernf drrlevffpi peperrrlwr flnfqlsddv nafvlepsgg
      601 frpkwgghrn sqlkll
//
LOCUS       WP_457630506             111 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Oceanithermus
            sp.].
ACCESSION   WP_457630506
VERSION     WP_457630506.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..111
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12169
     Region          10..110
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msvrekiwge hagkiarlld evdpdlsryi qefayeevma rpgldlktre llaitalial
       61 gnpdelkthi rgalasgase reiretiihs alylgfpral gamkvlaeml g
//
LOCUS       WP_457630866             462 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Oceanithermus sp.].
ACCESSION   WP_457630866
VERSION     WP_457630866.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..462
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48109
     Region          3..400
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 merrhvlali gfstaigmlv glvaaaftwa lfsaqnlflg glvgylppgy sgengvlhtf
       61 rnphplalvl llplifaaas lfghnrglsk iiasfhqgrp gtlgeklrya lgslaelgag
      121 splgregpma vlgnwigdal grrflpeair ghlpfagmaa gfaaafhapv ggallavelf
      181 ypglvleigs lgpaliggla gfvvygafwg yqplldlkpl pphvyhlgfa llagallali
      241 gslwmlaarq vrrrtaklsf lprhallgla valfavflpq vtgdglvwve laaspllpvv
      301 filqlalarl vllsiavglg gygtligpal algglftial arafpaispd agsaallgmg
      361 allagvvrtp faalllvsem ggyaalpltl pavftayllt wahaypeqnl gdrrlagvpy
      421 aglrcgelpf eleaivrdge rlapradevv raddeliper gg
//
LOCUS       WP_457631676             201 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Oceanithermus sp.].
ACCESSION   WP_457631676
VERSION     WP_457631676.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13408398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..201
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22809
     Region          14..>192
                     /region_name="Eis"
                     /note="Predicted acetyltransferase [General function
                     prediction only]; COG4552"
                     /db_xref="CDD:443616"
     Region          73..157
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mekeavelci rcpaarlreh pfhpglnifr ppqrqhealv glveegrglv saafaagqtv
       61 ayaafqlpdp fecwsqdpsg kiwelgavev apewrgrgla rrlleetfat gffddkvvia
      121 qllswhydte rtglsafayr ellinlyrrv gfepwrtddp diaghienal marigprase
      181 etvkcfhrlr rrgrapwdip f
//
LOCUS       WP_457631743             639 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Oceanithermus sp.].
ACCESSION   WP_457631743
VERSION     WP_457631743.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 639)
  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 639)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18797862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..>639
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          225..375
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          306..>433
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          315..340
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(316..317,320..321,323,346,349..350,353..354,
                     356..357,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          344..374
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          393..421
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrriltaaia flglaaasgl vlpfggsggn avglalsqsl gagspfvael afpetpwpqg
       61 wslvmgdpdg pggariaaea tgadwvlvge vgedgwitay lrhdgrtlea rfadasllas
      121 waalqlglea gpvvvypeld eplaelmnta phfdpgpyla glsetaggil keqtllvngl
      181 yahgpasfaa tlpaavidyw ehrrepekmg dsgmgpvwka ffpimnndda eatrrarall
      241 dspraldvag allvlratgd sswhvaarrl trvapelvfg weelsfaafe qndaalaasa
      301 lrralelepd sslywtnlgw aeyllgrpyr aiyaslrgfe lennpvaayn lglfhallgd
      361 yadafeyyqs alrldesdev qmalkdiadt rdsqmlfwqg yllarsgrwq eareaysafl
      421 kahpshrlae narlelaslq nvsldlavng yrlgplettp pfgarenirp lltaeasayl
      481 psgravarvy kghsvvaqsv teltipplta eftrelepft vnepgiyrlv veyaggraet
      541 afdvgpasla rqllsldivp adldgnplva edvlagpsgt eelisatqkv iraaaaearq
      601 ikrfseplpn gpfkgrsvaa vmeeadagli refyedvle
//
LOCUS       WP_457632042            1528 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-directed RNA polymerase subunit beta' [Oceanithermus
            desulfurans].
ACCESSION   WP_457632042
VERSION     WP_457632042.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 1528)
  AUTHORS   Chen,T. and Romesberg,F.E.
  TITLE     Directed polymerase evolution
  JOURNAL   FEBS Lett 588 (2), 219-229 (2014)
   PUBMED   24211837
REFERENCE   2  (residues 1 to 1528)
  AUTHORS   Werner,F.
  TITLE     Structural evolution of multisubunit RNA polymerases
  JOURNAL   Trends Microbiol 16 (6), 247-250 (2008)
   PUBMED   18468900
REFERENCE   3  (residues 1 to 1528)
  AUTHORS   Morse,R., O'Hanlon,K. and Collins,M.D.
  TITLE     Phylogenetic, amino acid content and indel analyses of the beta
            subunit of DNA-dependent RNA polymerase of gram-positive and
            gram-negative bacteria
  JOURNAL   Int J Syst Evol Microbiol 52 (Pt 5), 1477-1484 (2002)
   PUBMED   12361249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478913
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1528
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..1528
                     /product="DNA-directed RNA polymerase subunit beta'"
                     /EC_number="2.7.7.6"
                     /GO_component="GO:0000428 - DNA-directed RNA polymerase
                     complex [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003899 - DNA-directed RNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /calculated_mol_wt=170011
     Region          1..>162
                     /region_name="PRK00566"
                     /note="DNA-directed RNA polymerase subunit beta';
                     Provisional"
                     /db_xref="CDD:234794"
     Region          449..1503
                     /region_name="PRK00566"
                     /note="DNA-directed RNA polymerase subunit beta';
                     Provisional"
                     /db_xref="CDD:234794"
ORIGIN      
        1 mkrelkkvri alaspekiha wsygevekpe tinyrtlkpe rdglfderif gpvkdyecac
       61 gkykrqrfeg kvcercgvev tksivrryrm ghielatpaa hiwyvkdvps kigtlldlta
      121 geleqvlyfa kyividpgga mlegvpikrg ellsdeqyre lkfgrqetya iplgtdalik
      181 dgdyvtkgqe lapgvvskmd gvalfrfprr isveylerer ahlvlpkeaw ieaeryeage
      241 piaeladpfv feseaagvae vlewdegalv rlrdpesdev vavylvpvgf alkvghgelv
      301 nagdpvaaae pgavrlprgv kvteleaeee gdrvflsmtv ewarvqdyrl ephmhvlvge
      361 gaevlkgdkl vgaidpeeev haeadgivhl hepasivvmk arlypfeddv evttgdriap
      421 gdvladggkv tseiygrvev dlvrqvvrvi esydidarmg aeavqvllse ldldqleael
      481 eeemlgpsrh krsrarkrle ivrafkasgn rpewmvleav pvlppdlrpm vqvdggrfat
      541 sdlndlyrrl inrnnrlkkl msqgapemii rnekrmlqea vdalidngrr gspvtnpgsd
      601 ralrsltdil sgkqgrfrqn llgkrvdysg rsvivvgpql klhqtglpkr malelfkpfl
      661 lrrmeekgia anikqarrml erhrdikdev wdaleevihg kvvllnrapt lhrlgiqafq
      721 pvlvegqsiq lhplvceafn adfdgdqmav hvplssyaqa earvqmlsah nllspasgep
      781 iakpsrdiil glyyitqlrr ekkgagrefa tpveaieayd kgeialnapi kiageettvg
      841 rykfvfasvd eaivavdqgl idlqdvvsir vngrlrvtsp gralfvrmvi eaikdgdpea
      901 evpeellnyg vaqeknslrd lvyrsflllg iektarlldv lkaegfhfst ssgitigidd
      961 viippekqqy lreadealdk iehaykqgll tdeerrrqii klwadvtekv tealfknfee
     1021 rypfnplyvm aqsgargnrt qirqlggmrg lmakpsgeim evpvranfre gltvleyfis
     1081 thgarkggad talrtadsgy ltrklvdvah eivvreedcg ttdfmevplf qtsatgersl
     1141 rregeieqtl ygrtvardfe aggrsfregq mlsredvdal vaaaragele tvpvyspltc
     1201 rteygvcrkc ygydlsmaqp vsigetvgvv aaesigepgt qltmrtfhtg gvatgsditl
     1261 glprvielfe arrpkvkaii aeidgeveve etddkllvrv vsgefkkeyk vdkgarltvr
     1321 sgdrvtagtp ltrgavdphq lleaqgpeav qrylvseiqr vyraqgvkvh dkhievivrq
     1381 mlkyvevtdp geskllegqv lerwevervn ealmeegkmp aswkpllmgv tksalntrsw
     1441 lsaasfqhtt hvlteaaiwg kkdeliglke nvilgklipa gtgtdfvrrt qvvdertler
     1501 lkearkaaee vvttqvlpga gaeagaeg
//
LOCUS       WP_457632281             603 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Oceanithermus desulfurans].
ACCESSION   WP_457632281
VERSION     WP_457632281.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Baharin,A., Ting,T.Y. and Goh,H.H.
  TITLE     Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure,
            Molecular Properties, and Applications
  JOURNAL   Plants (Basel) 11 (10) (2022)
   PUBMED   35631755
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18487223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..603
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67131
     Region          29..181
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          <211..486
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
     Region          350..602
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msvkkiplev lfgdpelgqv qvapdgrsva fiapwegvkn lwvmdlasge rrrvtsdrgr
       61 gvlghgwlps glqvyvqdkd gdenwrlyal dpaggeprll tpgegvqarp lathpdfpde
      121 ilvmlndrdp slhdvwrida rsgarervve npgfigftad eqlrvrvalk atddgggelf
      181 vregeawrsl mkwglddslg twplavrgdt lylsssvgrd taallahdls sgeervlaed
      241 prydlpdagg llfhpraerp eavavmrdrl gwivldpale pdferlaele gdvqivnrda
      301 enrlwvvled ldahsprywi ydrsarelrr lgdahpalae ytlaerrpvr yrardgleie
      361 ayltlppgre prglpavilp hggpwhrdvw gfdpwaqwla nrgfavlqpn frgstgygka
      421 llnagnkqwg rkmqddltdg vrwlveqgia dpkrvaimgg syggyatlag laftpelyaa
      481 gvdlvgpsnl ftlletvppy wkpmialfht rmghperdae llraasplfs aekiqaplli
      541 gqgandprvk raeslqivqa lkekgkpvey veypdeghgf vkaenrldff rkaeaflekh
      601 lnp
//
LOCUS       WP_457632439             502 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Oceanithermus desulfurans].
ACCESSION   WP_457632439
VERSION     WP_457632439.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 502)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..502
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57159
     Region          3..500
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mkpeqayeal rafqidtayy qslgalagwd qrtyiprkgh ahrarqfaal arllharrtd
       61 priaewldgv egsdlvadpe speaanvrew rrdyeravrv pddlavalaq aqsegesawe
      121 slreaddwag frpylkrvlq ltreyaeavg yetepydall edyepgeraa rlqamfaelg
      181 ratrdlleri rasavrppve vlhrnypvev qravayevtg llgydleggr idptahpfel
      241 svgpgdvrit tryypdylga affgsvheag hamyeqglpa ehwgtpmgqa vsmgvhesqs
      301 rmwenlvgrs lgfwrfyypk lqprfaalad vrledfhrav navkpslirv eadevtynlh
      361 ilirfelela lfrgelevdd lpeawnakyr dylgvvppnf kdgvmqdvhw sggmfgyfps
      421 ytlgnvyaaq lfeaarrdlg eleeafarge fapllewlrd rvhrhgrrfp prrlveratg
      481 tppgtdalvr ylndrfgaly el
//
LOCUS       WP_457632766             118 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Oceanithermus
            desulfurans].
ACCESSION   WP_457632766
VERSION     WP_457632766.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..118
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12976
     Region          13..116
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msvrkkiwgk naeriaeale ridpdlasyi qdfayeevma rpgldlktre llavtalial
       61 gnpdelkthl rgalangate revretiihs alylgfpral gamkvfsell artderga
//
LOCUS       WP_457633138             242 aa            linear   BCT 27-JAN-2026
DEFINITION  cyanophycinase [Oceanithermus desulfurans].
ACCESSION   WP_457633138
VERSION     WP_457633138.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Law,A.M., Lai,S.W., Tavares,J. and Kimber,M.S.
  TITLE     The structural basis of beta-peptide-specific cleavage by the
            serine protease cyanophycinase
  JOURNAL   J Mol Biol 392 (2), 393-404 (2009)
   PUBMED   19591842
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Obst,M., Sallam,A., Luftmann,H. and Steinbuchel,A.
  TITLE     Isolation and characterization of gram-positive
            cyanophycin-degrading bacteria-kinetic studies on cyanophycin
            depolymerase activity in aerobic bacteria
  JOURNAL   Biomacromolecules 5 (1), 153-161 (2004)
   PUBMED   14715021
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790602
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..242
                     /product="cyanophycinase"
                     /EC_number="3.4.15.6"
                     /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]"
                     /GO_process="GO:0043170 - macromolecule metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25250
     Region          4..238
                     /region_name="CphB"
                     /note="Cyanophycinase and related exopeptidases [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG4242"
                     /db_xref="CDD:443384"
ORIGIN      
        1 mrrsgwfall ghadplrget raveerllem aggvvlfvtp kamlplveaw reifhthgar
       61 htgvlalsrr eqamdariag qvadaplvll vdeqgerlle litgtrlvna laqvhlrggv
      121 vaaaleaspl lgsavplgrg etpavryglg llpglavqea fegagafhrl sevvigrpdl
      181 lgvglergaa vvvgpegrae vvagrvalld asgarsspaa vhglrvdvla aparfevplf
      241 pe
//
LOCUS       WP_457633426            1528 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-directed RNA polymerase subunit beta' [Oceanithermus
            desulfurans].
ACCESSION   WP_457633426
VERSION     WP_457633426.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 1528)
  AUTHORS   Chen,T. and Romesberg,F.E.
  TITLE     Directed polymerase evolution
  JOURNAL   FEBS Lett 588 (2), 219-229 (2014)
   PUBMED   24211837
REFERENCE   2  (residues 1 to 1528)
  AUTHORS   Werner,F.
  TITLE     Structural evolution of multisubunit RNA polymerases
  JOURNAL   Trends Microbiol 16 (6), 247-250 (2008)
   PUBMED   18468900
REFERENCE   3  (residues 1 to 1528)
  AUTHORS   Morse,R., O'Hanlon,K. and Collins,M.D.
  TITLE     Phylogenetic, amino acid content and indel analyses of the beta
            subunit of DNA-dependent RNA polymerase of gram-positive and
            gram-negative bacteria
  JOURNAL   Int J Syst Evol Microbiol 52 (Pt 5), 1477-1484 (2002)
   PUBMED   12361249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478913
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1528
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..1528
                     /product="DNA-directed RNA polymerase subunit beta'"
                     /EC_number="2.7.7.6"
                     /GO_component="GO:0000428 - DNA-directed RNA polymerase
                     complex [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003899 - DNA-directed RNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /calculated_mol_wt=170069
     Region          1..>162
                     /region_name="PRK00566"
                     /note="DNA-directed RNA polymerase subunit beta';
                     Provisional"
                     /db_xref="CDD:234794"
     Region          449..1503
                     /region_name="PRK00566"
                     /note="DNA-directed RNA polymerase subunit beta';
                     Provisional"
                     /db_xref="CDD:234794"
ORIGIN      
        1 mkrelkkvri alaspekiha wsygevekpe tinyrtlkpe rdglfderif gpvkdyecac
       61 gkykrqrfeg kvcercgvev tksivrryrm ghielatpaa hiwyvkdvps kigtlldlta
      121 geleqvlyfa kyividpgga mlegvpikrg ellsdeqyre lkfgrqetya iplgtdalik
      181 dgdyvtkgqe lapgvvskmd gvalfrfprr isveylerer ahlvlpkeaw ieaeryeage
      241 piaeladpfv feseaagvae vlewdegalv rlrdpesdev vavylvpvgf alkvghgelv
      301 nagdpvaaae pgavrlprgv kvteleaeee gdrvflsmtv ewarvqdyrl ephmhvlvge
      361 gaevlkgdkl vgaidpeeev haeadgivhl hepasivvmk arlypfeddv evttgdriap
      421 gdvladggkv tseiygrvev dlvrqvvrvi esydidarmg aeavqvllse ldldqleael
      481 eeemlgpsrh krsrarkrle ivrafkasgn rpewmvleav pvlppdlrpm vqvdggrfat
      541 sdlndlyrrl inrnnrlkkl msqgapemii rnekrmlqea vdalidngrr gspvtnpgsd
      601 ralrsltdil sgkqgrfrqn llgkrvdysg rsvivvgpql klhqtglpkr malelfkpfl
      661 lrrmeekgia anikqarrml erhrdikdev wdaleevihg kvvllnrapt lhrlgiqafq
      721 pvlvegqsiq lhplvceafn adfdgdqmav hvplssyaqa earvqmlsah nllspasgep
      781 iakpsrdiil glyyitqlrr ekkgagrefa tpveaieayd kgeialnapi kiageettvg
      841 rykfvfasvd eaivavdqgl idlqdvvsir vngrlrvtsp gralfvrmvi eaikdgdpea
      901 evpeellnyd vaqeknslrd lvyrsflllg iektarlldv lkaegfhfst ssgitigidd
      961 viippekqqy lreadealdk iehaykqgll tdeerrrqii klwadvtekv tealfknfee
     1021 rypfnplyvm aqsgargnrt qirqlggmrg lmakpsgeim evpvranfre gltvleyfis
     1081 thgarkggad talrtadsgy ltrklvdvah eivvreedcg ttdfmevplf qtsatgersl
     1141 rregeieqtl ygrtvardfe aggrsfregq mlsredvdal vaaaragele tvpvyspltc
     1201 rteygvcrkc ygydlsmaqp vsigetvgvv aaesigepgt qltmrtfhtg gvatgsditl
     1261 glprvielfe arrpkvkaii aeidgeveve etddkllvrv vsgefkkeyk vdkgarltvr
     1321 sgdrvtagtp ltrgavdphq lleaqgpeav qrylvseiqr vyraqgvkvh dkhievivrq
     1381 mlkyvevtdp geskllegqv lerwevervn ealmeegkmp aswkpllmgv tksalntrsw
     1441 lsaasfqhtt hvlteaaiwg kkdeliglke nvilgklipa gtgtdfvrrt qvvdertler
     1501 lkearkaaee vvttqvlpga gaeagaeg
//
LOCUS       WP_457633449             436 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Oceanithermus desulfurans].
ACCESSION   WP_457633449
VERSION     WP_457633449.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Sun,Y. and Cheng,K.
  TITLE     Structure, function and evolution of the HerA subfamily proteins
  JOURNAL   DNA Repair (Amst) 142, 103760 (2024)
   PUBMED   39236417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..>436
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          98..>434
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 mkkeaigvvl gsreatplef wigiqdglvr lddvvwvead hgglvvryyg mvdrvhkvle
       61 gtqfdsdtfl aaghliptnt ayvahvtvtr lepeeylppd pgspvylarg dslnaalyyd
      121 rmkqklpvgf mrngepafvn lafldgrqgg hvnisgisgv aaktsyalfl lhslytsgvl
      181 edaasaktli fnvkgqdlfy ldrpnrelap eereryaamg laaepfasva ffapprlaqg
      241 qghitasshr aegvrayhws lvdfcrdgll pflfsdrgam snlgflidhv tarlaalahg
      301 qkgpelyvdd wpdgptaeag vfdslgrvki dsfgrlvdyl efqllgaese geaasgnqrw
      361 tarqhtgtlq afvrrlraaa rnvghlirgd apssapdplg ssaqinvvdl hnlspqaqmf
      421 vvgsllrrvf gakesg
//
LOCUS       WP_457633762             118 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Oceanithermus
            desulfurans].
ACCESSION   WP_457633762
VERSION     WP_457633762.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..118
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12918
     Region          13..116
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msvrkkiwgk naeriaeale ridpdlasyi qdfayeevma rpgldlktre llavtalial
       61 gnpgelkthl rgalangate revretiihs alylgfpral gamkvfsell artderga
//
LOCUS       WP_457633777             568 aa            linear   BCT 27-JAN-2026
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Oceanithermus desulfurans].
ACCESSION   WP_457633777
VERSION     WP_457633777.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Jenkins,J., Mayans,O. and Pickersgill,R.
  TITLE     Structure and evolution of parallel beta-helix proteins
  JOURNAL   J Struct Biol 122 (1-2), 236-246 (1998)
   PUBMED   9724625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..568
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=61199
     Region          105..448
                     /region_name="NosD"
                     /note="Nitrous oxide reductase accessory protein NosD,
                     contains tandem CASH domains [Inorganic ion transport and
                     metabolism]; COG3420"
                     /db_xref="CDD:442646"
ORIGIN      
        1 mdhatarltl tlalllgllg acapgeappg ngepppetsf alpagipape fgieerledr
       61 ytrpdpwdre tpgwyyvhrq hpdasdersy gtpaapratv pdpvpagsvv vlagtydfap
      121 agydrivtrg taaapvflvg epgavvtrkw vleasytive gleftdrgkv vlvypshhva
      181 lrnnehhhla gkiggrgnsg aervhdvviy nnkihsqdgw dqnpdldldn hgikfdawvd
      241 rvwvlnnegy hnggnfiqig dayggdltrn ryfyvggnrl yanrqspigv kqasdvvise
      301 nelfdnrkvq nnaagqsgiv fqygpdrlwi lfnhihdsna gitggsnsgg tgegpyivgn
      361 lihglrvppd fsynpdtgwa paavmlaggn gryvidntiy dvdggihtps sspveihgnl
      421 vaevrlgyhl flettaavta srasenaffq pggpalfrlg satvhrgvva metvwdraag
      481 nleadprlad paagdyrpra dsplvdsgre hdvyrrfhdl ygldirrdqa gaarpqgagw
      541 drgalehraa slartyalre ltsgggap
//
LOCUS       WP_457633991             502 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Oceanithermus desulfurans].
ACCESSION   WP_457633991
VERSION     WP_457633991.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 502)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..502
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57174
     Region          3..500
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mkpeqayeal rafqidtayy qslgalagwd qrtyiprkgh ahrarqfaal arllharrtd
       61 priaewldav egsdlvadpe speaanvrew rrdyeravrv pddlavalaq aqsegesawe
      121 slreaddwag frpylkrvlq ltreyaeavg yetepydall edyepgeraa rlqamfaelg
      181 ratrdlleri rasavrppve vlhrnypvev qravayevtg llgydleggr idptahpfel
      241 svgpgdvrit tryypdylga affgsvheag hamyeqglpa ehwgtpmgqa vsmgvhesqs
      301 rmwenlvgrs lgfwrfyypk lqprfaalad vrledfhrav navkpslirv eadevtynlh
      361 ilirfelela lfrgelevdd lpeawnakyr dylgvvppnf kdgvmqdvhw sggmfgyfps
      421 ytlgnvyaaq lfeaarrdlg eleeafarge fapllewlrd rvhrhgrrfp prrlveratg
      481 tppgtdalvr ylndrfgaly el
//
LOCUS       WP_457634414             603 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Oceanithermus desulfurans].
ACCESSION   WP_457634414
VERSION     WP_457634414.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus desulfurans
  ORGANISM  Oceanithermus desulfurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Baharin,A., Ting,T.Y. and Goh,H.H.
  TITLE     Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure,
            Molecular Properties, and Applications
  JOURNAL   Plants (Basel) 11 (10) (2022)
   PUBMED   35631755
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18487223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Oceanithermus desulfurans"
                     /db_xref="taxon:227924"
     Protein         1..603
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67147
     Region          29..181
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          <211..486
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
     Region          350..602
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msvkkiplev lfgdpelgqv qvapdgrsva fiapwegvkn lwvmdlasge rrrvtsdrgr
       61 gvlghgwlps glqvyvqdkd gdenwrlyal dpaggeprll tpgegvqarp lathpdfpde
      121 ilvmlndrdp slhdvwrida rsgarervve npgfvgftad eklrvrvalk atddgggelf
      181 vregeawrsl mkwglddslg twplavrgdt lylsssvgrd taallahdls sgeervlaed
      241 prydlpdagg llfhpraerp eavavmrdrl gwivldpale pdferlaele gdvqivnrda
      301 enrlwvvled ldahsprywi ydrstrelrr lgdahpalae ytlaerrpvr yrardgleie
      361 ayltlppgre prglpavilp hggpwhrdvw gfdpwaqwla nrgfavlqpn frgstgygka
      421 llnagnkqwg rkmqddltdg vrwlveqgia dpkrvaimgg syggyatlag laftpelyaa
      481 gvdlvgpsnl ftlietvppy wkpmialfht rmghperdae llraasplfs aekiqaplli
      541 gqgandprvk raeslqivqa lkekgkpvey veypdeghgf vkaenrldff rkaeaflekh
      601 lnp
//
LOCUS       WP_457634781             380 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Persephonella sp.].
ACCESSION   WP_457634781
VERSION     WP_457634781.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..380
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=43188
     Region          1..378
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 meikiyegyd lekliqkakd elgedikilh yetveekkff ffkgkkkyrl fvepvdeqel
       61 tepvlkfeel lekvedlidk kirnslpkya qglatpenlp phiqtgsvss nifneftgda
      121 lylveqllek dvlpdvakki vtegcgldid tnkwdlntvt ikeavikgik khikftgsfe
      181 ngsdglqiya fvgptgvgkt tnlfkiasql vidkkkkvav istdtfkvga shqartyani
      241 lnipfysise skklkntveq lrkfdfilid tvgrshydyw rlgeikeils sleeeikhvl
      301 tvscnfkned avevvykyqt ffpihslfft kidetlkpgl llnlpvetnl pvsylstgqr
      361 vpedlkvlnp evmasyliss
//
LOCUS       WP_457635191             143 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Persephonella sp.].
ACCESSION   WP_457635191
VERSION     WP_457635191.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     gene            1..143
                     /gene="rimP"
     Protein         1..143
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=16026
     Region          1..139
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mlqplieerg lklvdveyit ggkpvlriyv ynpegtsied cewisrriga lldvedlipv
       61 syilevsspg ldrklknkee yeifkgrdvk ivtkepvegk nvfegvlkgl egdnviiqen
      121 geiikiplek isrtnlefkv gge
//
LOCUS       WP_457635285             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Persephonella sp.].
ACCESSION   WP_457635285
VERSION     WP_457635285.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..358
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40201
     Region          1..>288
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          164..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrafltvllk elimffrswg lvavvlysft vdvyiagkgf evkprnvsvg yvdytdgvvs
       61 kkilshlhpp efqepvrfns qeelskavyn reiivglifd pdfeknyfkg kaqlnlllda
      121 taaaqsyitl syiqnivlrf ndlnfpvdlk thklfnqnsd tpkflalaef lsiltlitvi
      181 lssvvfvkek esgtwdimll mpvdskviil aksisqiiiv mvgtiictgi vlfgvfdlpm
      241 ngsffafvll tlmytfsttg iglfiasvaq slvqvaqlsv iimmpiifls gswtpiysmh
      301 pilqqlslls plryyiegce slffrgtpvs dlwlyfaalf ilgsvlylfg frkigklf
//
LOCUS       WP_457635515             126 aa            linear   BCT 27-JAN-2026
DEFINITION  YbbR-like domain-containing protein [Persephonella sp.].
ACCESSION   WP_457635515
VERSION     WP_457635515.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1003777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..126
                     /product="YbbR-like domain-containing protein"
                     /calculated_mol_wt=14336
     Region          5..>121
                     /region_name="YbbR"
                     /note="Cyclic di-AMP synthase regulator CdaR, YbbR domain
                     [Signal transduction mechanisms]; COG4856"
                     /db_xref="CDD:443884"
ORIGIN      
        1 mkkvkdivln nlhlkilsll vafllwlnit stqktrfeff sevkilnvpk giliekvepe
       61 kvlvviegvr skldqvnisk ievyvdgrti kkgkntlkvf vkpsktenfd ivkvipdkih
      121 vyakpk
//
LOCUS       WP_457635546             120 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Persephonella
            sp.].
ACCESSION   WP_457635546
VERSION     WP_457635546.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..120
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13215
     Region          21..120
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 maqnddtkid melyykrfls lfeevkkdyp kfvesfmgff kategpgald kktkelisia
       61 lsvksqcpyc iafhvknava egakraeiie samvaalmgg gpcvaymkyv fdacdqfgak
//
LOCUS       WP_457635642             322 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Persephonella sp.].
ACCESSION   WP_457635642
VERSION     WP_457635642.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13466756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..322
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=38075
     Region          44..>276
                     /region_name="PRK10770"
                     /note="peptidyl-prolyl cis-trans isomerase SurA;
                     Provisional"
                     /db_xref="CDD:236758"
     Region          170..311
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mrkiiylllg lfitaeafqg fswnidpelk kkvvavvgke kitemdvqry mkvllpmnyy
       61 hrtltdeklk eirkkaieal inrellyyea qkkgikipek qvddlidqla kkykskekle
      121 kllketgvtl eqfrlelkkr laidkllsey vavnitekdl reyyeknkyk fkeppalkir
      181 yiyikvdpsk pkgrqiaker aekaykeike gkdfgdvayr ysddlsrikg gelgfvhrgr
      241 fdkpveeviy klkkgqvsgi ietelgfhiv kvedkrperl vpyekikdkl kkeleekyrk
      301 ekfnqlieda kkdlkvvvyd nk
//
LOCUS       WP_457635960              95 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Persephonella sp.].
ACCESSION   WP_457635960
VERSION     WP_457635960.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..95
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10781
     Region          6..84
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mgklkvvvdr ticegigpca eetkyieldk rhkavilepd kpkeevmeka qhvkrqevil
       61 dltpeeeeei frsaeacpvk aifiydpetg eqlyp
//
LOCUS       WP_457636234             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457636234
VERSION     WP_457636234.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51206
     Region          1..446
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 mlridytnam aeiigerdgi lreellsfrh fvvethsliq kekerkfyfc klpyqdvsei
       61 keyadhirek fdyfvvigig gsslgakmlf esltdinyni ekkpkfflle nvdpekfdsv
      121 lrqidiektc fnvvtksgst vetianfsii lsilknrlgd kytehlvftt dpekgflrkf
      181 gqsegikmfd vppkvggrfs vlspvgllpa avvgididql lsgakkmdlv csveehvehn
      241 payliallhy itnmrrgkti svmmpyaekl gsfvdwyrql waeslgkdgl gqtpvkaigt
      301 vdqhsqiqly rdgirdkiit fiqvekmetd yeipddlped isyltghslh eilnkellgt
      361 kaalikskvp nitltvdqin pynlgmmiyl yelatgfsgy lykinpfdqp aveegknfty
      421 almgrkgyed kleefkelyk ekykieiq
//
LOCUS       WP_457636749             502 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Oceanithermus sp.].
ACCESSION   WP_457636749
VERSION     WP_457636749.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 502)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..502
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57114
     Region          3..500
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mkpedayael rrfqietayy qslgalaswd qrtyiprkgh ehrarqfaal aqllhrrrts
       61 prigewldal egasflsdet apeavnvrew rrayersrrv peelavalaq aqsegesawe
      121 elrrlddwkg fkpylerlva ltreyaeavg yeteaydall edyepgeraa rlqemfavlg
      181 rdsqrlleav mgspfqppeg vlnrdyplda qvrvvreivg rigydleagr idptthpfel
      241 svgpgdvrit tryypdylga alfggiheag hamyeqglpa ehwgtpmgea agmgvhesqs
      301 rlwenavgrs lgfwehfypl lqgsfdslsg vslasfhrav navrpslirv eadeltynlh
      361 iqvrfelela lfrgqlevad lpeawnakyr eylgiepkny kdgvmqdvhw aaglfgyfpt
      421 ytlgnvyaae lyraasnalg dlegrfargq fapllnwlre nihahgrryl prrlieqvtg
      481 repsaktlta ylkekfgnly ri
//
LOCUS       WP_457637288             201 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Oceanithermus sp.].
ACCESSION   WP_457637288
VERSION     WP_457637288.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13408398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..201
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22807
     Region          14..>192
                     /region_name="Eis"
                     /note="Predicted acetyltransferase [General function
                     prediction only]; COG4552"
                     /db_xref="CDD:443616"
     Region          77..>153
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mksdavelci ncpadrlreh pfhpelnifr ppsrqheall klvesgqgmv saafaaqqtv
       61 aytafqlpdp fecwsndpgq kiwelgavev apawrgrgla rrlleetfat gffddkvvia
      121 qllswhydte rtglsafsyr ellvklyqkv gfelwrtddp diaghienal marigpkasa
      181 etvrcfhrlr rrgrapwdip f
//
LOCUS       WP_457638207             129 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Oceanithermus
            sp.].
ACCESSION   WP_457638207
VERSION     WP_457638207.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..129
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14039
     Region          13..108
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msvrekiwgs kaakiaemld avdpdlsryi qefayeevma rpgldlktre llaivalial
       61 gnpdelkthi rgalangase revretiihs alylgfpral gamkqlaelv gpvdrrvsge
      121 piqdergss
//
LOCUS       WP_457638279             462 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Oceanithermus sp.].
ACCESSION   WP_457638279
VERSION     WP_457638279.1
KEYWORDS    RefSeq.
SOURCE      Oceanithermus sp.
  ORGANISM  Oceanithermus sp.
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Oceanithermus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Oceanithermus sp."
                     /db_xref="taxon:2268145"
     Protein         1..462
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47894
     Region          3..400
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 merrhvlsli gsstvigfiv glvaaaftwa lfttqnlllg eligylppgy sgengvlhtf
       61 rnphplalvl llplifavas lfghnrglsk iiasfhqgkp gtlgeklrya lgslvelgag
      121 splgregpma vlgnwigdal grrflsdetr shlpfagmaa gfaaafhapv ggallaveif
      181 ypglvleigs lgpaliggla gfvvygafwg yepllnlkpl pphlyhvgfa llvgvlmaiv
      241 gtvwmlaarl vrlrtarmsy lprhallglv iaavavflpq vtgdglvwve mssapllsvs
      301 filqlavvrl lvlsvalglg gygaligpal algglfaial arafpaaspd aataalvgms
      361 allagvvrtp faalllvsei ggyatlpltl pavftsyllt tahafpeqnl gagelkgapy
      421 aglragelpf tpkeilrggq tlpaspdevi kaddvlipel sd
//
LOCUS       WP_457638556             444 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457638556
VERSION     WP_457638556.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..444
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=50172
     Region          1..442
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 mvridytnam aevigerdgi lreellsfrh fvvethsviq keknrkfyfc klpyqdtsqi
       61 keyaqhirds fqyfvvigig gsslgarmli dslsqkensp qifflenvdp egfhsviesi
      121 eiektcfnvv tksgstveti anfsiilsml keklgdrfke nlvfttdpek gflrkfgsen
      181 gikmfdvppp vggrfsvlsp vgllpaavag ididqilaga kkmdlvcsie ehvehnpayl
      241 valihyianm rrgktisvmm pyaeklasfv dwyrqlwaes lgkdglgqtp vkavgtidqh
      301 sqiqlyregi rdkiitfiqv enfstdfkip eglpeeisyl sghslkeilt kellgtkaal
      361 ikskvpnitv vldeispyni gmliylyela tgfsgylykv npfdqpavee gknftyalmg
      421 rdgyqdklee fkelykekyr ieis
//
LOCUS       WP_457638717             125 aa            linear   BCT 27-JAN-2026
DEFINITION  YbbR-like domain-containing protein [Persephonella sp.].
ACCESSION   WP_457638717
VERSION     WP_457638717.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1003777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..125
                     /product="YbbR-like domain-containing protein"
                     /calculated_mol_wt=14529
     Region          4..>121
                     /region_name="YbbR"
                     /note="Cyclic di-AMP synthase regulator CdaR, YbbR domain
                     [Signal transduction mechanisms]; COG4856"
                     /db_xref="CDD:443884"
ORIGIN      
        1 mkkikeilln nwhlkilsll vafllwlnit stqktrlefy advkvlnkpk nikiekiepe
       61 kvliviegvr sklnqvnisn ikvyvdgrrl kkgknqlkvf vkpsdgenfn vvqvkpdriy
      121 iyttr
//
LOCUS       WP_457638811             119 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Persephonella
            sp.].
ACCESSION   WP_457638811
VERSION     WP_457638811.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..119
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13232
     Region          4..119
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 medkdtridm elyykrflal feeikkdypt fvqsfmgffk ategpgalss ktkelisial
       61 svkaqcpyci afhvknaike gatrqeiies amvatlmggg pcvaymkyvf dacdefgar
//
LOCUS       WP_457639038             380 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Persephonella sp.].
ACCESSION   WP_457639038
VERSION     WP_457639038.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..380
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=43150
     Region          1..380
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 meikvyegyd leeliqkake elgddikilh yetveekkff ffkgrkkykl fvetvddeel
       61 tepvvkfeel lekveelidr kiktslpkia qniaspenlp phislengag tavfneftgd
      121 alhllnqlvg kdvlpevakk lvkegcgldi dtnkwdlntl tekealikgi kryikftgaf
      181 dkedgklkif afigptgvgk ttnlfkiasq lvidkkkkva vistdtfkvg ashqartyan
      241 ilnipfysis eskklrntve elknfdfili dtvgrshydy wrlgeikeil sgleeeinhv
      301 ltiscnyknd dafevvhkyq tfftihslff tkidetlkpg lllnlpvetr lsvsyistgq
      361 rvpedlkvlt pevtasyllg
//
LOCUS       WP_457639182             227 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Persephonella sp.].
ACCESSION   WP_457639182
VERSION     WP_457639182.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 227)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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 11459734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..227
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25950
     Region          91..226
                     /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"
     Region          161..226
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mdqdlkdaik kleeakskqe kieriiills gllmviifai iginiysgke etisepeini
       61 vakqeqeksk keekqtesak enkqnavpvv sekneakteq ketavkkeea vkqktaevkk
      121 qpeekktavh srqekqekka vktenkpakt ekktavlqkf psgyyiqaga fstkkkaekl
      181 leklslpnay irkegelykv ligkfknkke ayrfmkeknl rgfirkl
//
LOCUS       WP_457639934             265 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Persephonella sp.].
ACCESSION   WP_457639934
VERSION     WP_457639934.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..265
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28085
     Region          9..264
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 mtaeellknd klvigdrefs srlivgsgky kdfeetakat easgaemitv avrrvnitdp
       61 dkpnlldyid tskvmilpnt agcytaeeav ltaklareal ghgfvklevi gdqktlypdm
      121 vetlkaaeil vkegftvlpy itddpimakk fedigcaavm plaapigsgl glqnpynilf
      181 ikeavsvpvi vdagigtasd asivmelgvd gvlmntaiaq akdpikmava mkhaviagrl
      241 aylagripkk myasasspve giigr
//
LOCUS       WP_457640050             359 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Persephonella sp.].
ACCESSION   WP_457640050
VERSION     WP_457640050.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 359)
  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 581140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..359
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42061
     Region          50..209
                     /region_name="PHP"
                     /note="Polymerase and Histidinol Phosphatase domain;
                     cl23724"
                     /db_xref="CDD:451507"
     Site            order(50,52,83,101,206,208)
                     /site_type="active"
                     /db_xref="CDD:213985"
ORIGIN      
        1 mfyifllvlv sivlylefrp frklelsent ieplksefpe nikqynviah ihtqfsfdsl
       61 gkpsdikkam eensidfvfv tdhdndnyrf fedgkifagv ekntpegrll llgnslpvis
      121 hpnnfefehy rwkgefrpdh lyelidikda vvwnkalsii slvknvlvfp ltrnilhkwn
      181 cliplekwsr lyyararglk iiggldlhik lvyqehthgl lipsyragfk wlinrvysrk
      241 elktkqdvld slkngnlyis lkqyfgdfwg eadevvylpg erlpigtaln csfrhrktvk
      301 ilkrenqpvv vtekdsfsyr teesgmyhfe vyeydfrign iyfgfrpvav tnpfevvng
//
LOCUS       WP_457640135             152 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Persephonella sp.].
ACCESSION   WP_457640135
VERSION     WP_457640135.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     gene            1..152
                     /gene="rimP"
     Protein         1..152
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17113
     Region          4..150
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mkeqviekvk ellqplleer gvklvdveyi tagkpvlriy iynpegtsid dcewvsrrig
       61 alldiedlip vsyilevssp gldrklknke eyeifkgrqv kivtkepveg knvfegelkg
      121 lenesavvnt geeevkiple siaranlefk ge
//
LOCUS       WP_457640208              95 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Persephonella sp.].
ACCESSION   WP_457640208
VERSION     WP_457640208.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..95
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10707
     Region          6..84
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mgklkvvvdr ticegigpca eetkyieldk rhkavilepg kpkdevmeka qhvkrqevil
       61 dltpeeeeei fraaeacpik aifiydpetg eqlyp
//
LOCUS       WP_457640487             651 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Persephonella sp.].
ACCESSION   WP_457640487
VERSION     WP_457640487.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 651)
  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 651)
  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 18640031
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..651
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=77957
     Region          86..322
                     /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          208..318
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 msgfklilit fliiitpsfs qqdavseiqe kqesvfksls eeeatrlyre avkmykrksy
       61 ysalnlltkl ithrdniyys dalfltakiy lelgrktgkk gliqkalnyl nkysytakka
      121 ytwdfyytkg niyenlymye ralasyklaf yravtkrqqf ktvaailrta awtkkmdlvt
      181 ryivlvnvee lsheekkefe fikgllefqk gnyekayqyl skiykeyepy lienpyyyfi
      241 faentyrtgk yylakqifrr iislikdeei irrsllrlgd ifnikgdkit afnyyysiie
      301 kypdsreakv aklkilamsd dprikkkikl iededfkkpl rfvyrmlvsn rnnyignfaf
      361 gnfgnivlks kndrlfhelv keisliyper mlyehkeyin klwknelldl eyqkscelyi
      421 tnknffksvf drkvlikivk dlklcgkeks ridlaewilk rwnddrsrll laqvyfeegm
      481 ytkslstlkn iknkdcnyyk llaknkielq qadkkllktl drckkdteti ilksiisfql
      541 gnidrtlmyl dqvkneiykf yenrfynkyl iyiveksfsl nryreifnil kpvsekidec
      601 dlnsfllisa vriglksidk yaekiknckt lwtqvaeniy edyllmeeal k
//
LOCUS       WP_457640812             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457640812
VERSION     WP_457640812.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51588
     Region          1..446
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 miridytnvm aetigerdgi lreellsfrh fvvethsriq kekerkfyfa klpyqdteyi
       61 kivaqeirek fdyfvligig gsslgaqmlf eslkginhni fnrpkffimd nvdpdkfkai
      121 mdiieiektc fnvisksgst vetianfaii ldvlrselse rwnqhliftt dpekgflrkf
      181 gsennikmld ipshvggrfs vlspvglfpa avlgididql legakkmdli csieehiehn
      241 paylialthy ianmrrgkti svmmpysekf ssfvdwyrql waeslgkdgl gqtpvkalgt
      301 vdqhsqiqly rdglrdkiit fiqiekresd fkipeniped inylsghtlh eilnkellgt
      361 kaalikskvp nitisldris pynigmliyl yematgfsgy lykinpfdqp aveegknfty
      421 almgregykh kleefeelyk erykieiq
//
LOCUS       WP_457641072             258 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF58 domain-containing protein [Persephonella sp.].
ACCESSION   WP_457641072
VERSION     WP_457641072.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10486977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..258
                     /product="DUF58 domain-containing protein"
                     /calculated_mol_wt=29952
     Region          89..>186
                     /region_name="YeaD2"
                     /note="Uncharacterized conserved protein, DUF58 family,
                     contains vWF domain [Function unknown]; COG1721"
                     /db_xref="CDD:441327"
     Region          154..229
                     /region_name="DUF58"
                     /note="Protein of unknown function DUF58; pfam01882"
                     /db_xref="CDD:426489"
ORIGIN      
        1 mivsamlafm gisgfigrkn isklefdlkf peeiyakref piriiiknkk rflpsfilri
       61 hlfdkelfvp yignkeetel hlfisfeerg mihldeiyvc svfpfnffvr cnfvkinknl
      121 ivfpkpekca yymednirsk gkgeevsgvk gfegdilsir dytsgdplky ihwkasaktg
      181 klktkeltfl dtqpvvvdle siggsierkv scgtymilnl ykravpfglk tkekfyrpey
      241 sykqkirllk elavygkd
//
LOCUS       WP_457641350              95 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Persephonella sp.].
ACCESSION   WP_457641350
VERSION     WP_457641350.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..95
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10685
     Region          6..84
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mgklkvvvdr ticegigpca eetkyieldk rhkavilepg kskeevmeka qhvkrqevil
       61 dltpeeeeev frsaeacpvk aifiydpdtg eqlyp
//
LOCUS       WP_457641538             266 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Persephonella sp.].
ACCESSION   WP_457641538
VERSION     WP_457641538.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..266
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28462
     Region          10..265
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 mfneeqffkd dklvigdref tsrlivgsgk ykdfeetkla teasgaeiit vavrrvnitd
       61 pdkpnlldyi dtskimilpn tagcytaeea vltaklarea lghgfvklev igdqktlypd
      121 mvetlkaaei lvkegftvlp yitddpimak kfedigcaav mplaapigsg lglqnpynil
      181 fikeavsvpv ivdagigtas daaivmelgv dgvlmntaia qakdpikmav amkyavkagr
      241 laylagripk kmyasasspi egiigr
//
LOCUS       WP_457641584             151 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Persephonella sp.].
ACCESSION   WP_457641584
VERSION     WP_457641584.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     gene            1..151
                     /gene="rimP"
     Protein         1..151
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17296
     Region          3..150
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mkqevigkvk ellkplleer elklvdieyi tegkpvlriy iynpegtsie dcewisrrig
       61 alldiediip vsyilevssp glerklknke eyeifkgrdi kivlkepvdn qnvikgvlkg
      121 meddtvlveg egkefkiple nisranlefk q
//
LOCUS       WP_457641981             363 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Persephonella sp.].
ACCESSION   WP_457641981
VERSION     WP_457641981.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 363)
  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 581140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..363
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42951
     Region          54..>158
                     /region_name="PHP"
                     /note="Polymerase and Histidinol Phosphatase domain;
                     cl23724"
                     /db_xref="CDD:451507"
ORIGIN      
        1 mliyilfgvl llillfvfyf efrffkiltl neknlnklqe kfpenineyn vivhihtqfs
       61 fdslgkpsdi kkameensid fvfvtdhdnd nyrffedeki fagieknisd grllllgnrl
      121 pvishpnnfe fehyrwkgef kpdhlyeiid ikdgvvwnkt lsaltllkni iifpftrdil
      181 hkwnsliple kwvelyfdra rglklvggld lhikfvyqeh thgilipsyr sgfkwlinkv
      241 ysrkeikskd dildalkkgs lyisikqnfg yfwgsngdkv ylfwekmppg snlnchfkks
      301 ktvkilkhen npvlvteeds fsykakkvgy yhfeiyeydf kigslyfgfr pliitnlfev
      361 vdv
//
LOCUS       WP_457642371             473 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Persephonella sp.].
ACCESSION   WP_457642371
VERSION     WP_457642371.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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 473)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19981757
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..473
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54588
     Region          125..386
                     /region_name="AAA_21"
                     /note="AAA domain, putative AbiEii toxin, Type IV TA
                     system; pfam13304"
                     /db_xref="CDD:433102"
     Region          <259..470
                     /region_name="COG4938"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443965"
ORIGIN      
        1 mkiyiknlgn vkkanieikn ltvlvgknnt nktwtayliy alaaetmlts yfnnllkkrr
       61 dskikdnfrk lssllkkvsl aitegnents fkqealklee elsfniedfl kefikdytkf
      121 vkrqfpgfls vsdedlknls fsirfstnel keikyrfles idenmfnkhf snlltikelk
      181 niflkivktl igepfnipae rktltvfsip itlgeaktde lkdiifeqll krekinisit
      241 klirimtelk kldynypipi idfkdfilri intkekddtl nkeltgllee svlegkilvd
      301 stgklkyfin ddnsldvsvs ssmvkglsgl dlylkykasp gdlliidepe mnlhpeaqvk
      361 mieflailan kgikvlitth spyivdhlin lieaykskke nvedlfwepk fikkgkfkki
      421 kpkdifinkn nvsaylfndn gevidildkk tglinwqtfs sisekiasly yev
//
LOCUS       WP_457642529             127 aa            linear   BCT 27-JAN-2026
DEFINITION  YbbR-like domain-containing protein [Persephonella sp.].
ACCESSION   WP_457642529
VERSION     WP_457642529.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1003777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..127
                     /product="YbbR-like domain-containing protein"
                     /calculated_mol_wt=14449
     Region          4..>121
                     /region_name="YbbR"
                     /note="Cyclic di-AMP synthase regulator CdaR, YbbR domain
                     [Signal transduction mechanisms]; COG4856"
                     /db_xref="CDD:443884"
ORIGIN      
        1 mekiktvffn nlplkilsll vafllwlnit stqkarvefy sdvevkphpe dymiehiqpe
       61 kvliiiegsk sslsnvnisk iqtyvdgssi kegknvmpvl vsrelikdfk ivsiypekvl
      121 vyakkik
//
LOCUS       WP_457642760             444 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457642760
VERSION     WP_457642760.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..444
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=50256
     Region          1..442
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 mvridytnam aevigerdgi lreellsfrh fvvethsviq keknrkfyfc klpyqdtsqi
       61 keyaqyirds fqyfvvigig gsslgarmli dslsqkensp qifflenvdp egfhsviesi
      121 eiektcfnvv tksgstveti anfsiilsml keklgdrfke nlvfttdpek gflrkfgsen
      181 dikmfdvppp vggrfsvlsp vgllpaavag ididqilaga kkmdlvcsie ehvehnpayl
      241 valihyianm rrgktisvmm pyaeklasfv dwyrqlwaes lgkdglgqtp vkavgtidqh
      301 sqiqlyregi rdkiitfiqv enfstdfkip eglpeeisyl sghslkeilt kellgtkaal
      361 ikskvpnitv vldeispyni gmliylyela tgfsgylykv npfdqpavee gknftyalmg
      421 rdgyqdklee fkelykekyr ieis
//
LOCUS       WP_457642887             359 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Persephonella sp.].
ACCESSION   WP_457642887
VERSION     WP_457642887.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 359)
  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 581140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..359
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42089
     Region          50..209
                     /region_name="PHP"
                     /note="Polymerase and Histidinol Phosphatase domain;
                     cl23724"
                     /db_xref="CDD:451507"
     Site            order(50,52,83,101,206,208)
                     /site_type="active"
                     /db_xref="CDD:213985"
ORIGIN      
        1 mfyifllvlv sivlylefrp frklelsent ieplksefpe nikqynviah ihtqfsfdsl
       61 gkpsdikkam eensidfvfv tdhdndnyrf fedgkifagv ekntpegrll llgnslpvis
      121 hpnnfefehy rwkgefrpdh lyelidikda vvwnkalsii slvknllvfp ltrnilhkwn
      181 cliplekwsr lyyararglk iiggldlhik lvyqehthgl lipsyragfk wlinrvysrk
      241 elktkqdvld slkngnlyis lkqyfgdfwg eadeivylpg erlpigtaln csfrhrktvk
      301 ilkrenqpvv vtekdsfsyr teesgmyhfe vyeydfrign iyfgfrpvav tnpfevvng
//
LOCUS       WP_457643649             585 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Persephonella sp.].
ACCESSION   WP_457643649
VERSION     WP_457643649.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 79029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..585
                     /product="polysaccharide deacetylase family protein"
                     /calculated_mol_wt=67059
     Region          252..505
                     /region_name="CE4_SF"
                     /note="Catalytic NodB homology domain of the carbohydrate
                     esterase 4 superfamily; cl15692"
                     /db_xref="CDD:472828"
ORIGIN      
        1 mrllallfcl yigvasaggf sknvlvvyak klplikaies vlqeegvsyq tgsiyslldk
       61 dpedvldifp viiipdrvnq sipydlrfwf knyvmeggnv fiiydagvkd iygryrekpv
      121 fseltgvnyc tyfhkrekay tvdffriree vlekldippg ktingyisgy kygklrypva
      181 dtelidknvh iiaetgsgkv gaslkksgkg wvlfvnlplc hlkansddlp lrvfiryflf
      241 nlsniphlvn vpygrgglvi nwhidsyldw ksipmmireg yynkelvyss hitagdflek
      301 pgdglgfdac grgrkiarml npygitgshg gwahnwfaer lregkfsree ikryikinne
      361 clekiagyki reysapqgvh pqpvttevle elgmvayyyt gdsgsspnrt fyngkmvsrk
      421 vlafpitple dvaslyemse kgfprdkvgk wlkgmvdfvv errtirliys hpydiphype
      481 eiknfinyai kkvregklsv kpmvyfyeym erflntryrf ifgdgefkae issskslrgi
      541 pvavpkkfcq kpnmdvsfed enylyfvine diksfslkcs ygntg
//
LOCUS       WP_457643751             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457643751
VERSION     WP_457643751.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51091
     Region          1..442
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 mvridytnvm aevigerdgi lreellsfrh fvvevhsiiq keksrkfyfc rlpyqdvshi
       61 keyaqhirek fenfvvigig gsslgakmlf esltdfnynq knspkfylle nvdperfasv
      121 leqidvektc fnvvtksgst vetianfsii msmlkdrlgd rftenlvftt dpekgflrkf
      181 gqehnikifd vpplvggrfs vlsavgllpa avagididql lagakkmdlv csveehvehn
      241 paylialahy itnmrrgkti svmmpyaekl asfvdwyrql waeslgkdgl gqtpvkaigt
      301 vdqhsqiqly regirdkiit fiqvekfstd fripeelped isylsghsla eilnkellgt
      361 kaalikskvp nltivldeis pynigmliym yelatgfsgy lykinpfdqp aveegknfty
      421 almgrkgyee kleefkelyk ekyrievq
//
LOCUS       WP_457644241             664 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Persephonella sp.].
ACCESSION   WP_457644241
VERSION     WP_457644241.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..664
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=74861
     Region          59..297
                     /region_name="NIT"
                     /note="Nitrate and nitrite sensing; pfam08376"
                     /db_xref="CDD:462453"
     Region          159..664
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mhlfsnlsik tkllilslvp ilvillfagy lfitnynkym eekaleqavk lsvkisavvh
       61 evqkergrta gflgskgref rselsaqrkl tdekvrdlkn yiksvdlshl peglkmeikv
      121 ilekvdtipl irkevddfsi tlkdaigqyt einrkllhai gsiakyssda kitrqlaayv
      181 nfllakermg ieravlsavf ardtfnehly qrflsllseq kafltgfkll asddflkfyk
      241 ktmvgkavke vermekiale kaseggfdld psywfdmitq kinlmkkved ymskkliddi
      301 taeedrvlrn lmietvfslv visailylgf iirksinrsi dtikndvnyi aetkdftrki
      361 hletkdemhe iadainnfid askkaieqak msaeenasia selsatavei gkraeeeski
      421 vmettekalg tqeplrnlvg kldetreeik kangilnras sqineliltv krsaeeemgi
      481 vkeletlkks tdktqevlkl iediadqtnl lalnaaieaa ragevgrgfa vvadevrsla
      541 eksreyvdsi tetiseline inlitekisf naenitrlte sssnverdvd evtsvmdqtv
      601 kmaddasisv rsivseieei ikdiekinei sganarsvee iatatehlyk lienlnkile
      661 efkt
//
LOCUS       WP_457644279             374 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Persephonella sp.].
ACCESSION   WP_457644279
VERSION     WP_457644279.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..374
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=42637
     Region          1..374
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 meikiyegyn leeliqkake elgedikivh yetiterkwf ifgskkrykl fvempdleep
       61 vvqfddifek ieeiidkkiq qtlpkvtspa pviqnietgq qiipeqfnef sgealelinq
      121 llnrdvlpdv akklvkegcg ldidtnkwdl ntlttreali kgirkyikft gafdkekegl
      181 kiltfigptg vgkttnlfki ashfvinqkm kvavistdtf kvgatqqari yanilnipfy
      241 saseskklks tvselenydf ilvdtvgrsh ydywrlgeik eilgdlsenm hivltvscnf
      301 knedafevvn ryssffdids llftkidets kpglllnlpv etkipvsyis tgqrvpedik
      361 ilkpeniasy ilgd
//
LOCUS       WP_457644416             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Persephonella sp.].
ACCESSION   WP_457644416
VERSION     WP_457644416.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..358
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40310
     Region          1..309
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          173..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrafiaillk elvvfvrnwg lilvliysft idiyiagqgf evkprnvsvg yvdyssgvis
       61 kkilshlhpp efkepvrfns qeelsraifn reiivgivfe pdfekdfikg katvnillds
      121 taaaqayitl tyirnilvrf hrfdtpveik thklfnqnad trkfisfsef lsivtlvgvi
      181 lsavvfvrek engtwdimll tpvnpkliil aktfsqmiii magvivsvgl ilfgvfdvpi
      241 ngsfivfimf tftflfaitg iglfiasvak smlqvaqlsv vimmpmifls gawtpihsmh
      301 pfiqylsyis plryyiegcl siffrgidsp dllphfaalt vlstalyvfg frkigklf
//
LOCUS       WP_457644446             363 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Persephonella sp.].
ACCESSION   WP_457644446
VERSION     WP_457644446.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
REFERENCE   1  (residues 1 to 363)
  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 581140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..363
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42907
     Region          54..>155
                     /region_name="PHP"
                     /note="Polymerase and Histidinol Phosphatase domain;
                     cl23724"
                     /db_xref="CDD:451507"
ORIGIN      
        1 miylillamf lvfasfvfyl efrpirkiki desnisslse sfpeeifryn vishihtqfs
       61 fdslgkpsdi rravevneid fvfvtdhdnd nykffedhri fagiekntpd grllllgnel
      121 pvishpnnfe fehyrwkgef kedhlyeiid ikdgivwskv ftgltlikni llypftrnil
      181 hkwnalipld rwvdlyfera kglkliggld lhikfvyqeh thgvlipsyq egfkwlvnkv
      241 fskseirnke dildalrrgl lyislkkkeg yfwgsngfni ylfwekmpvg ssincdfrel
      301 rtikilkcnn spvlvteenr fsytayrpgy yhfevyeydf kignlyfgvr pvavtnmfev
      361 vnv
//
LOCUS       WP_457644597             448 aa            linear   BCT 27-JAN-2026
DEFINITION  glucose-6-phosphate isomerase [Persephonella sp.].
ACCESSION   WP_457644597
VERSION     WP_457644597.1
KEYWORDS    RefSeq.
SOURCE      Persephonella sp.
  ORGANISM  Persephonella sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Persephonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Persephonella sp."
                     /db_xref="taxon:2060922"
     Protein         1..448
                     /product="glucose-6-phosphate isomerase"
                     /calculated_mol_wt=51323
     Region          1..446
                     /region_name="PRK00973"
                     /note="glucose-6-phosphate isomerase; Provisional"
                     /db_xref="CDD:179193"
ORIGIN      
        1 miridytnvm aetigerdgi lreellsfrh fviethariq kekerkfyft klpyqdtqdi
       61 kefakeiser fdyfvligig gsslgaqmlf eslksinhni ydkpkffimd nvdpdkfssi
      121 leiidiektc fnvvsksgst vetianfaii ldilkkrlgd swnehlvftt dpekgflkkf
      181 geensikilq vppkvggrfs vlspvgifpa avlgididql legakkmdlv csieehvehn
      241 payliaithy ianmrrgkti svmmpysekl ssfvdwyrql waeslgkdgl gqtpvkalgt
      301 vdqhsqiqly rdgirdkiit fiqvekrnid fkisediped ihylsghslh eilnkellgt
      361 kaalikskvp nitismdris pynigmliyl yematgfsgy lykinpfdqp aveegknfty
      421 almgregysq kleefeelyk ekykieiq
//
LOCUS       WP_457644839             403 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Pseudomonas chlororaphis].
ACCESSION   WP_457644839
VERSION     WP_457644839.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            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="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42924
     Region          21..380
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,230,233..234,237..239,242,270,274,322..323,
                     327,331,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mvaqlnevyi ekgtpmfmrt vlalfsggfa tfallycvqp mmpllsrefs inaaqsslil
       61 svatgllaig llvtgpisdr igrkpvmvaa lfaaalctla salmpswhgv llmralvgls
      121 lsglaavamt ylseeihpqh iglamglyig gnaiggmsgr litgvlidfv swhtamlvig
      181 glaliaaavf wrilpesrnf rarslhprsl ldgftmhfrd aglpllflea fvlmgafvtl
      241 fnyigyrlla apyhmdqafv gllsvvylsg iyssakigal adrlgrrkml watislmlag
      301 laltmlsalp vviigmlift fgffgthsva sswigrralk akgqasslyl fsyyagssia
      361 gtaggvfwhm agwngiglfi sallvvallv alklaklppl atr
//
LOCUS       WP_457644856             363 aa            linear   BCT 27-JAN-2026
DEFINITION  fimbria/pilus outer membrane usher protein [Providencia stuartii].
ACCESSION   WP_457644856
VERSION     WP_457644856.1
KEYWORDS    RefSeq.
SOURCE      Providencia stuartii
  ORGANISM  Providencia stuartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Providencia stuartii"
                     /db_xref="taxon:588"
     Protein         1..363
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=40152
     Region          <10..363
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 meyttdfsas nndpyesgrk kqqfqasisq slkdigylsi ngyqqyywdr sgvdknltvg
       61 fnsnyrqiny gisysytkqe htnsknemls infsvpftlg qknnwvnyry ntsqngdsis
      121 svsvsgtrle dnnlqfditq nynhsrhens gsvsgnyivs sgeynggysy dpryqsanig
      181 atgalllhsg gitparaiyd savlvkandi ndlkvnnaqs lytnswgyav vpsatryern
      241 kisvdpstlt gnndvglstt tvvptrgaiv ladfkgkrga rvmlklthhd qlipfgaqvs
      301 vlvdkeevtt givandgevy lsgvpeqsri vvkwgshadq qcelplqldl sndkiqfier
      361 icq
//
LOCUS       WP_457644866             343 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Rhizobium ruizarguesonis].
ACCESSION   WP_457644866
VERSION     WP_457644866.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium ruizarguesonis
  ORGANISM  Rhizobium ruizarguesonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 343)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 15746491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rhizobium ruizarguesonis"
                     /db_xref="taxon:2081791"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38155
     Region          <74..214
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <163..343
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          251..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqisfrsent arapereayg fapthegsdf esmvraysag ygvfsakpls ndrafawaad
       61 lrtseaftvl hsvyqsswti rtldetpqhl afyiphtgsf rlsigkkvve sgpgrllman
      121 nheagdrfiq gphcsdalfl dwkvvrrmlv slmetpiles ldlepvvdla tqsgqligsv
      181 vqtivqgmrn dgpllsspla vaamsetlan lvirfgrhrl sghmekkkvs lvapwhvrra
      241 idymhaniae pltmtmvadd vgvslralqt gfkafrgtsp gsylrtirlq aardqlldpm
      301 nqrsvreica mwgfshagrf sivyrstfge sprdtrlrae rlr
//
LOCUS       WP_457644867            1695 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-2-macroglobulin family protein [Proteus terrae].
ACCESSION   WP_457644867
VERSION     WP_457644867.1
KEYWORDS    RefSeq.
SOURCE      Proteus terrae
  ORGANISM  Proteus terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
REFERENCE   1  (residues 1 to 1695)
  AUTHORS   Arimura,Y. and Funabiki,H.
  TITLE     Structural Mechanics of the Alpha-2-Macroglobulin Transformation
  JOURNAL   J Mol Biol 434 (5), 167413 (2022)
   PUBMED   34942166
REFERENCE   2  (residues 1 to 1695)
  AUTHORS   Wong,S.G. and Dessen,A.
  TITLE     Structure of a bacterial alpha2-macroglobulin reveals mimicry of
            eukaryotic innate immunity
  JOURNAL   Nat Commun 5, 4917 (2014)
   PUBMED   25221932
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1695)
  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   4  (residues 1 to 1695)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1695
                     /organism="Proteus terrae"
                     /db_xref="taxon:1574161"
     Protein         1..1695
                     /product="alpha-2-macroglobulin family protein"
                     /GO_function="GO:0004866 - endopeptidase inhibitor
                     activity [Evidence IEA]"
                     /GO_process="GO:0010951 - negative regulation of
                     endopeptidase activity [Evidence IEA]"
                     /calculated_mol_wt=188387
     Region          65..1695
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mnqnqfrqyt ekrgyrwssl avvlasalal tgcddkaden vsstdktqnt qvtepkdtaq
       61 stsgtatqts ekpavttktn netalkskev rdelamrfag kevtvldase lqrdgastmv
      121 vtfsvpldpd qkfddvihlv dtkkgklega welsdnlmel rfrhlppste lnltidekik
      181 ginertlttp fsqkltteei fpsvgftskg sllpleaaeg lpiialnvgq vdvnffrvkd
      241 dqlaqfltqw esrsninywe sdeflsqadl vytgrfelnt etntrenvll plksidalkk
      301 egayiavmqq agkysytvpa tvftfsdigl smhsyldtld iftqslkngs aldkveirll
      361 dekggliska qtdsqghatl eksdkarllm airdgqtsmi dlrkpaldls efdiggpqgy
      421 skqffafgpr dlyrpgetli vnallrdgdg npikeqpvkv dllktdgqvs rsfvwqpeng
      481 lyqlklvipa dentgtrtlr fdvgdgtprf yefqvedfmp ermaleitgk kgiilsghda
      541 yfdikgryly gapaadnrlq gqvflkasre avsklpgyef gavkdenfsr lldefelnld
      601 sdgeggvnvd seryeelksp iniilqasll eaggrpvtrr yqqavwpath lagirpvfpk
      661 kevydyrtdk yksgysvden smaefeivyt dqdgkklpan dlkvkfiyer hdyywrwsss
      721 ngwesgynek dlqmdeqtik iakdgtakva fpvewgsyri evvdpktelv sslrfwagys
      781 wmdntggtga vrpdqvklkl dkegylpgek vklnivaphp gkgyvlless ngplwwqeid
      841 vpekgldvev pinkewarhd lyltsvvvrp gdtskqatvk ravgilhlpl qdknrridis
      901 ldapekirpn qdlkirikan pvagqplpen invlvsavdt gvlniteykt pdpydaffgr
      961 krysidqydv ygqliegqgr lanlrfggdg geaaalsrgg kkpltdvqii aqqtapvkln
     1021 aqgegevslp ipefngevrl maqawtadkf gsqegkvvia aplvtqlslp rfmaggdnal
     1081 lsldltnltd daqsitlnyt asglvglgga esktvsltkg ertqiqipvk akhgfgqgef
     1141 slsiygikvp geeikpyhnt wnigvrpafp aetihyastl qdgdtwrlps eilsrfnnst
     1201 legellltsr pplqvaryir elfaypygcl eqtvsglyps lystekelkq lgiktqtdad
     1261 rkaaiekgia hlltmqkseg gfslwdqggr eeywltayat dflfrasqqg ysvpadslkr
     1321 andrllrylq dknlvnyeya vnqdaarfsa rayaalvlan qqkaplgelr rlylernqag
     1381 sglalvqlgi alklmgdssr aesliaegvt ttrkynyglg dygstirdqa liiallsenn
     1441 letqsrdasv ialsdnltsr ewfstqesns lylagrffin maeqpwevav nrqvptissd
     1501 rainetltsa qlqeglelnn rggvaiysrm nivgypkvap apysnvlnvh rsyydlkgnr
     1561 vhpnrlqsge mlvvklevsa drdvpdalvv dllpagleie nqnlasssas lsdsaadlqe
     1621 fiddmgqani khleyrddrf vaaisvdkyr pttllylara vtpgsyqvpp pqvesmyvpy
     1681 wraigstetk idvvp
//
LOCUS       WP_457644882              64 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Providencia stuartii].
ACCESSION   WP_457644882
VERSION     WP_457644882.1
KEYWORDS    RefSeq.
SOURCE      Providencia stuartii
  ORGANISM  Providencia stuartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Providencia stuartii"
                     /db_xref="taxon:588"
     Protein         1..64
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7300
     Region          14..>57
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 menknhqqen fkstyqslvn sarilfvekg yqavsideis gkalvtkgaf yhhfknkkqw
       61 gcpr
//
LOCUS       WP_457644883            1202 aa            linear   BCT 27-JAN-2026
DEFINITION  pilus assembly protein [Shewanella algae].
ACCESSION   WP_457644883
VERSION     WP_457644883.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algae
  ORGANISM  Shewanella algae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Nguyen,Y., Sugiman-Marangos,S., Harvey,H., Bell,S.D.,
            Charlton,C.L., Junop,M.S. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins prime type IVa pilus assembly
            and promote surface display of the PilY1 adhesin
  JOURNAL   J Biol Chem 290 (1), 601-611 (2015)
   PUBMED   25389296
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Takhar,H.K., Kemp,K., Kim,M., Howell,P.L. and Burrows,L.L.
  TITLE     The platform protein is essential for type IV pilus biogenesis
  JOURNAL   J Biol Chem 288 (14), 9721-9728 (2013)
   PUBMED   23413032
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Orans,J., Johnson,M.D., Coggan,K.A., Sperlazza,J.R., Heiniger,R.W.,
            Wolfgang,M.C. and Redinbo,M.R.
  TITLE     Crystal structure analysis reveals Pseudomonas PilY1 as an
            essential calcium-dependent regulator of bacterial surface motility
  JOURNAL   Proc Natl Acad Sci U S A 107 (3), 1065-1070 (2010)
   PUBMED   20080557
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):5260]
REFERENCE   4  (residues 1 to 1202)
  AUTHORS   Rahman,M., Kallstrom,H., Normark,S. and Jonsson,A.B.
  TITLE     PilC of pathogenic Neisseria is associated with the bacterial cell
            surface
  JOURNAL   Mol Microbiol 25 (1), 11-25 (1997)
   PUBMED   11902714
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465761
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Shewanella algae"
                     /db_xref="taxon:38313"
     Protein         1..1202
                     /product="pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /calculated_mol_wt=130908
     Region          322..1125
                     /region_name="PilY1"
                     /note="Type IV pilus assembly protein, tip-associated
                     adhesin PilY1 [Cell motility, Extracellular structures];
                     COG3419"
                     /db_xref="CDD:442645"
ORIGIN      
        1 mtnhgcigpc wrqisrrfla lllscigsfi lasplladdt elyvyesssr sgarpqmlii
       61 fdnsasmgny vydvdesysp gagggalepk kefiyftkga pdsdnmpvpg kqdktwrflr
      121 snngcqtswe ylnkygiytg fvreysfsgq ngtwkelpen nganvtlvdc fediqderyg
      181 naegipdglp ldsagnrnqv isytqvsngs teaqkkaakd aaertgfgtg rvvtlytedy
      241 lrwyhsdkkk vtktrlqlaq eaiqnvivtt pgvdlglaif nlnhdregvr dggriisgik
      301 qqsaaskial iesvkeiaya qntplcetly eayryfsgqg vyfgdddsdy tfykrdywgr
      361 vvtdrwgrpi vtrtyltent pqadpsiikn giydspfkkc qnqayviyit dgeptldsaa
      421 dglvqgmtgg kdayvsrngn sylsalsswm asndvnpnma gkqtvntfti gfsegaarae
      481 allrktaekg ggryfdaqna sklqsaiqlv vnqileknas ftspsvasnn fnkvqtfdsv
      541 yysmflpnkg prwrgnikkf rvtgtgdvvd kngnpaiadn gnintsacsf wssqaacnag
      601 gdgddvtkgg vaealynqkq rtfygnfask gglspltkaa assyaggeak laqhmgvdks
      661 qlqdlfdwvi gkdidddnqn nsrsdkrhdl lgdplhskpl aidfgssakn pdirilvgsn
      721 hgmlhmfqdk gdsvneswaf mpweflpnla tlranvpsgv hsvygfdgsp vayikrsgnk
      781 mekawvfmgl rrggrgyyam nvtnpdkpsl mwhisadsag mselgqswak pvvttipgqg
      841 dkpvlifgag yspakdtlev ggadsqgrgv fildaetgkl lhrfgpggdt pmpglrdsip
      901 nsvaildsng dgvtdriyat dtganvwrld magadtkqws afkfaslggs tentdrrffa
      961 apvvaqtmfg nlsenrvtvn gqsktvisaq qipydavvvg sglrpspsnt srsdmffvlq
     1021 drntlsqsfk gkavpqaltl adlydvtaka pvsekehiaf grkrgwyydf trngekslsd
     1081 asiikgrvff tsyvpgsqts tnqclvagqg ylygfdlhkg trsytktyle mgesvpdtpq
     1141 lvvppnirsd gtvadsymyl igignagedm ekvkpdpgcp sgdhkcvggg pstnkiyyyq
     1201 an
//
LOCUS       WP_457644922             521 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Pseudomonas savastanoi].
ACCESSION   WP_457644922
VERSION     WP_457644922.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..521
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=55137
     Region          1..520
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 milalgiisl rqvsslnase kfvetnvvps islvgsmdre fvsirgsnsr lrnpiepadr
       61 kaaaledvkk skqavqdlis klqplivtpk gkqifgelsq ayseyqvlqd qylvliaaan
      121 vdeavklssg amkqsadave rlmkslieln nakakkagee ataiyadtkl ivggfiaast
      181 laaivlalmy trsithpisq sltiaeriak ndlteviepq ghdevarlmm alkamqsglr
      241 ttlssisdss nqlastaeem havtedankg mqrqnnevem aatavtemsa aveevarnas
      301 aaseaatrsn ssavsgrarv dqtveaislm vgsvevatqe vqglavmatd iskvldvira
      361 iaeqtnllal naaieaarag eagrgfavva devralahrt qqstseieqm issiqkgtga
      421 avsamsntna qaqktldtah gagsalveit esidnitern vliataseeq aqvarevdrs
      481 lvsirdlsnq asdgssqtai atseltklav elnrlvsqfr m
//
LOCUS       WP_457644923             293 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Pseudomonas savastanoi].
ACCESSION   WP_457644923
VERSION     WP_457644923.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..293
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=30790
     Region          <1..292
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mralsvmqhg lrntlslisd ssnqlastse emhavtedan kgmlrqnnev emaatavtem
       61 saaveevarn asqaseaanr snsaalagra rvdetvqais lmvanvedas qevqglavma
      121 tdiskvldvi raiaeqtnll alnaaieaar ageagrgfav vadevralah rtqqstseie
      181 qmissiqkgt gsavsamtht ntqaqktldt aqgagsalve itesidnite rnvliatase
      241 eqaqvarevd rslvsirdls nqaaegssqt aiatseltkl avelnrlvkq fqm
//
LOCUS       WP_457644925             832 aa            linear   BCT 27-JAN-2026
DEFINITION  VirB4 family type IV secretion system protein [Pseudomonas
            savastanoi].
ACCESSION   WP_457644925
VERSION     WP_457644925.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 832)
  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 832)
  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..832
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..832
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93916
     Region          201..760
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mgypvdelmt tlsgnrlvsl iqlkgvspet rsdeelirlc etrnryflal gkkegknllv
       61 htyttktgie ldtqytmplp vlqdfvdayt epfrngtfyq vgyglalvlk yrelddgiqr
      121 mndllsltrt llaeydpaim gleenehgal fsqigryysl linghekdvl vsdtrlgdai
      181 idsvtnfeny dfvenrpnrg gqrfattfdl rdypsggtyp gmwdeaneqq feftlvqtfl
      241 fedrnkakdk fkkhkadlgs vendshqike lekaieditl gdkafgryha slivygktpd
      301 qaiengtkma svftvrdatf vrstmsnidt wytqfpgvte amypmmkste nlacsfslhs
      361 tptgkvkgnp igdgtgvmpv ltankalyvl nvhdsppgqn nlgemlpgha vftgqtgvgk
      421 ttaeailltf lsrfdplifs idyneslrhl lcalgaeyyt vqlgqftgvn pfqfhdspgl
      481 rqmlfdlvlc caggpdksnd adqkrikdsi eavmahtnvr nrsmslllrn ipeqgenclr
      541 trlskwcrla gegregqyaw vldspvnqfd aqtyrrlafd ctqllknnya ekhpevmeaf
      601 lntlfymkre mhearpgnll lnvvaeywap lsfkstadai qevlqsgrmr geilimdtqy
      661 peqalatkya paviqqvttp mwlpneralp enyakfgvtg klfeavrdmg plsremvvqq
      721 ghqtvklkme lggplkywlp llsatkknla vaervrqhlg ttdpkvwvda flvaeavrqw
      781 lntedpavwl pafdyadnlr qsmdtrdaqr wmpafqkawk alqehnevev ss
//
LOCUS       WP_457644939             237 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Pseudomonas asiatica].
ACCESSION   WP_457644939
VERSION     WP_457644939.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas asiatica
  ORGANISM  Pseudomonas asiatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12199791
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudomonas asiatica"
                     /db_xref="taxon:2219225"
     Protein         1..237
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24824
     Region          1..235
                     /region_name="MA"
                     /note="Methyl-accepting chemotaxis-like domains
                     (chemotaxis sensory transducer); smart00283"
                     /db_xref="CDD:214599"
     Site            order(10..11,14..15,18,21..22,24..25,28,31..32,35,38..39,
                     42..43,46,49..50,52..53,57,59..60,63,66..67,70..71,74,77,
                     80..81,84,88,91,98,102,105,108..109,112,115..116,119..120,
                     122..123,126..127,140..141,144,147..148,151,154..155,
                     157..158,161..162,165,168..169,172,175..176,178..179,
                     182..183,185..186,189,192..193,196)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206779"
     Site            80..113
                     /site_type="other"
                     /note="putative CheW interface [polypeptide binding]"
                     /db_xref="CDD:206779"
ORIGIN      
        1 mnqmsatvqe vaqnaeqasl aatnadqqaq igdqvvaeai grieqlagqm dnclaamqhl
       61 agesqrigsi ldviksvseq tnllalnaai eaarageagr gfavvadevr glaqrtstat
      121 eeigqlidsl hngtdevtrl ldnsknlteq svalsrkagh alsqitdtvs siqgmnqqia
      181 taseeqsvva eqinrsvlnv rdvsdqtsaa seqtaassge leqlgqqlrg mvgrfni
//
LOCUS       WP_457644842            1152 aa            linear   BCT 27-JAN-2026
DEFINITION  YadA family autotransporter adhesin [Pseudomonas chlororaphis].
ACCESSION   WP_457644842
VERSION     WP_457644842.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Lyskowski,A., Leo,J.C. and Goldman,A.
  TITLE     Structure and biology of trimeric autotransporter adhesins
  JOURNAL   Adv Exp Med Biol 715, 143-158 (2011)
   PUBMED   21557062
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Meng,G., Surana,N.K., St Geme,J.W. 3rd and Waksman,G.
  TITLE     Structure of the outer membrane translocator domain of the
            Haemophilus influenzae Hia trimeric autotransporter
  JOURNAL   EMBO J 25 (11), 2297-2304 (2006)
   PUBMED   16688217
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Hoiczyk,E., Roggenkamp,A., Reichenbecher,M., Lupas,A. and
            Heesemann,J.
  TITLE     Structure and sequence analysis of Yersinia YadA and Moraxella
            UspAs reveal a novel class of adhesins
  JOURNAL   EMBO J 19 (22), 5989-5999 (2000)
   PUBMED   11080146
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..1152
                     /product="YadA family autotransporter adhesin"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111641
     Region          6..594
                     /region_name="Hia"
                     /note="Autotransporter adhesin [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG5295"
                     /db_xref="CDD:444098"
     Region          372..1151
                     /region_name="Hia"
                     /note="Autotransporter adhesin [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG5295"
                     /db_xref="CDD:444098"
ORIGIN      
        1 mkyfhsnsvl adstasgqds vaigplasat iangvalgsn ssatgttlan aaygvggaat
       61 ggevnianga dgrritglaa gssatdavnv sqlnligqsa alalgggaql dpatgvwtap
      121 systnsigat gantgplvsn nvgaalsdln tsvtntaava vkyddastkt qvtfnpvgta
      181 vkltnvaagt lnatstdvvn gsqlfatnqt vdnlvnngag ikyfhsnsvl adstasgqds
      241 vamgpaavss gansvalgng atasfdnsva lgsgssatga tlanaaygvg gaatggevni
      301 angadgrrit glaagssatd avnvsqlnka gqdtatalgg gaaldattgv wtapnfstns
      361 isatgantgp lvsnnvgaal snlntsvtnt aavtvkydda atknqvtfnp agtavkltnv
      421 aagtlnasst davngsqlfa tnqtvdnlvn ngtgikyfhs nsvladsqat gldsvaigpq
      481 siaagahsfa vgsganvtad gglalghlsq aqvaggialg egsvadrvla pttgsiaags
      541 gaiiydtsda tllgsvsvgk agsyrqitnv adatddhdav tlrqltgamg slsstgtlyf
      601 hanstnpvds lasgaesiav gpgtvvngdn giglgnqakv gqaaaggiai grdtqvllas
      661 gialgsaaqa aaeqsvalga ganashamsv algssslttv gaetdysayr laapqtsvge
      721 igigtalgnr kltglaagsq dndavnvaql kvvgdqvdqn ttditnlggr vggletliga
      781 gggikylhvn stradsaatg tdamalgaqa qasgngsvam gtsatasadg svavgsgssd
      841 dgrgaetysg kysgannata gtvsvgnatt getrtvsnva dgkdakdavn vrqldgavae
      901 akqytddsia nlganagqqe gritaveddv snikkgtdgm fqvnnrsaaa kpkatgvdsi
      961 aggagavasg knsaavgtgs qasgensval gngakasarn atalgansva drdssvsvgs
     1021 tgnerqithl aagthgtdav nldqltqsva dittsanayt dqryrelknd lkqqdeilsa
     1081 giagamamas lpqsyspgss mtvaavssyr gqsslafgvs hmsgngrwvt klqgstdtqr
     1141 kvgvavgigy qw
//
LOCUS       WP_457646249             569 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Profundibacter sp.].
ACCESSION   WP_457646249
VERSION     WP_457646249.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..569
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59653
     Region          39..461
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mtrwvprvln eektlaarkl geaadslrag lrvlrqkgps qvqfwfiall igiasgyaal
       61 gfrkgitalq swlygaedlh mlhtfaetlq wywiltipia gglvvgliln rytddgvvrs
      121 vadviegaam negrveqkeg iasaiasmit lasggssgre gpvvhlasvi sswvsnriha
      181 ngitgrdllg cavaaavsvs fnapiagalf alevvlrhfa vhafapivia svagtvisri
      241 hlgdvteftv pvegslvfyv elpafmilgl vsglvavalm kavfwaddlg tyvqnrthmp
      301 rwlrpavaga mlgalaivfp hiigvgyett sraltgnlll yqamvfavvk viavaitmag
      361 rmgggifsps lmtgaltgla fglistsifp nvsgsetiya lagmgavaaa vlgapisttl
      421 ivfeltgdwq tgiavmvavs lstalasriv drsffltlle rkgvhlsagp qayllsmcgv
      481 asvmrakgte gapsddacwe ligqgvyidg natlkqampi fdstahsfip vvtlgseaes
      541 pelwgalfqv dalkaynkal aataaeehs
//
LOCUS       WP_457646446             311 aa            linear   BCT 27-JAN-2026
DEFINITION  methylenetetrahydrofolate reductase [Profundibacter sp.].
ACCESSION   WP_457646446
VERSION     WP_457646446.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1049
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..311
                     /product="methylenetetrahydrofolate reductase"
                     /EC_number="1.5.1.20"
                     /GO_function="GO:0004489 - methylenetetrahydrofolate
                     reductase [NAD(P)H] activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006555 - methionine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009396 - folic acid-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=33663
     Region          28..295
                     /region_name="MTHFR"
                     /note="Methylenetetrahydrofolate reductase (MTHFR).
                     5,10-Methylenetetrahydrofolate is reduced to
                     5-methyltetrahydrofolate by methylenetetrahydrofolate
                     reductase, a cytoplasmic, NAD(P)-dependent enzyme.
                     5-methyltetrahydrofolate is utilized by methionine
                     synthase...; cl00246"
                     /db_xref="CDD:444783"
     Site            order(57,83,114..116,127..128,148,150,154,156,163,169,
                     172..173,187,189,283)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:238299"
ORIGIN      
        1 mallqfkkkp eadplpvnpq leaflkgysi evmprtaakv edftallpkg trvyvahieg
       61 tpiedmvata arlsadgydv mphfpariia dratladwis ryrgdadvtq alllaggvsk
      121 plgefdnsmq lletglfdsa gftnlhfagh pegnrdidpd gsdknvmdtl rwkqdfsnrt
      181 daktalatqf ifeakpview adalkdagid mpihlgiagp aklqtlvkfa iacgvgpslk
      241 vlqkrakdmt klllpfeptd lltelaayka enpdsniaqv hffplggikt nanwaithgg
      301 ksavpanqtq d
//
LOCUS       WP_457646535             407 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Profundibacter sp.].
ACCESSION   WP_457646535
VERSION     WP_457646535.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13466756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..407
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=43815
     Region          19..>248
                     /region_name="PRK10770"
                     /note="peptidyl-prolyl cis-trans isomerase SurA;
                     Provisional"
                     /db_xref="CDD:236758"
     Region          162..283
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mmriltlclt ftglvltgma apvsaqnlys pavkvndqvv tnyevqqrar fmtllrapgn
       61 aqeqalkgli derlqtaaaa aagitptdee iqggmeefaa ranltaeqfv qalagggvaa
      121 etfrdfvktg lawrslvrak fgprvqvted eidraiaqts skgglrvlls eiilpantpq
      181 ataasqkrae kiaqttslsv fsanarrysa spsarqggrl qwmplsnlpa eirgqilals
      241 pgqvtapisi tngivlfqlr aieetdavap kdlsleyaqy fiaggrseaa lkeaarikar
      301 vdtcddlygi nkgkpeellq vdtlpvsqvp qdialelakl dpgevstrlt rnngqtlvfl
      361 mlcgrtpelg edisretira qlvnqrlqsy adgylselka dativyp
//
LOCUS       WP_457646898             492 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Profundibacter sp.].
ACCESSION   WP_457646898
VERSION     WP_457646898.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 492)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..492
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54256
     Region          1..490
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 maayddlmay erdtqalgqv sgrlgwdqet mmprgaagqr aeemaamssv lharrtdpkv
       61 gdwlaaidds tldvvgqanm rhirrgytrt mkiparlate qaklhsmaqg iwaqaraged
      121 faafaptlkq vlklkreeaa aladggdlyd allddyepna kaseleamfg alrprlvalr
      181 ervlgaqnqp aalsykfdea lqleltrkla vtfgydlnhg ridkavhpfs sgsghdvrit
      241 trtnpydpfn cfystihetg hgcyeqnidd aylltplgng vsmgvhesqs riyenqigrg
      301 qaftgwlfgq mrevfgdfgv adadafyatv nrvnsgyirt eadevhynlh vllrfdlera
      361 miagdldvdd lpdawnerfe ddfgvavdkp sngclqdvhw svglfgyfpt yslgnvyagc
      421 lnkamrdalp dldadlatgn tapatgwlre niqqygglyr pkdliekacg fapseaplld
      481 yleakfggiy gv
//
LOCUS       WP_457646904             388 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Profundibacter sp.].
ACCESSION   WP_457646904
VERSION     WP_457646904.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 388)
  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 388)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
REFERENCE   3  (residues 1 to 388)
  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 10560168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..388
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=41543
     Region          51..310
                     /region_name="PGA_cap"
                     /note="Bacterial capsule synthesis protein PGA_cap;
                     pfam09587"
                     /db_xref="CDD:430701"
     Site            order(57,59,95,150..151,247,279,281)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:277327"
     Site            order(57,59,95,150,247,279,281)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:277327"
ORIGIN      
        1 mkralgwgll altllagcvp eqqmqtggqc vpkpafqapp vnpcadserv rltivgdvll
       61 hwpiqqtgyk ygfrkmwaqa dpylawgdlt ignmegpvap gvnqsghkvg dpgpvygtgv
      121 ytgfpmfnyh pqilkelkas gfdlmttann hamdrgslga dltlremaka glgavgtirs
      181 gaarqfavrr gtslgtvsfi gcsfstngnp dpkrqvllcy gnrsellslv rreaadpsva
      241 avivlphwgq eysstpdtqq valardlaaa gataivgthp havqpfrlln tgrgqvvpvv
      301 ystgnfiamq tempsrvgam amlemckapd gkgltvnrlg wiaeqmyftk trywmeiapv
      361 gatgdkglpy rhlskiapgf saqpqacr
//
LOCUS       WP_457647263             495 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Profundibacter sp.].
ACCESSION   WP_457647263
VERSION     WP_457647263.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 495)
  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 495)
  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 495)
  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..495
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..495
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51115
     Region          258..494
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <373..>445
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 mtgfnytavf qsdawtylng itsfqlvpdg ggyrlyggsg syggiigfel sagavashig
       61 dwlvddrgns frlsdftmig tdllvaelgs shlerysfda ggslfnpapa sygggtpalt
      121 pqitslsvga ttfvvtggga ggpeglniye vqggtlvhrd tvtdhikvtv gdiadlinvt
      181 vdgttylvag staeggistf tidasgnahl vdaigakegl wlsgldslta teangtsyii
      241 vastlsssls vvrinpmgvl yvtdhitdtl gtrfdnidai dsftvngrgf ivaggsddgl
      301 tlleimpdgk llehdsienq ngwtlenita iqtavfngev qvfaagsrvs gimqftiptd
      361 alatpingds gnntlsgtal ddliyggagn dtlygnggdd ilfggsgldq lyggagadvf
      421 iidsgpdqdq irdfelgldr idlsrwgmvy dpsdliitsh aggaiiqfgd lsldimtddg
      481 stltaadlta dsfvf
//
LOCUS       WP_457647272             282 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Profundibacter sp.].
ACCESSION   WP_457647272
VERSION     WP_457647272.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19884976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..282
                     /product="peptidylprolyl isomerase"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=30662
     Region          1..>221
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK04405"
                     /db_xref="CDD:235295"
     Region          129..261
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mlkrnkfwls avlvaslalp alaeeptadt vvatvngeki tvghvlavks slpeqyqalp
       61 ddvlfpglve qliqqvalsq slkgevplri kltaenelna qragyvldqk lraamtdeai
      121 qaayderyan mepeteynas hilvetedea kaikkqlddg adfaelakek stgpsgpngg
      181 slgwfgkgmm vkpfedavvt mkageisdpv ktqfgwhivk lnetrmkdap pldevrdeie
      241 adiqqklveq imadatkgae itradeetvp asvlshpeli dn
//
LOCUS       WP_457647711             176 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase, partial [Profundibacter sp.].
ACCESSION   WP_457647711
VERSION     WP_457647711.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         <1..176
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
     Region          15..147
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
     Region          85..176
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 nrvvrevkqr iksaletpdm prtrpavaed ldaladiwfd gwfeahadhv pdqlkalrnr
       61 dslrirlenm lettdvvgpv gapvgfctvk gdeiyqfyvs paargtgtad aliqagekrl
      121 kdseievgql wvipqnarai afyqrngwdg dtvenvpldt tegpyllpcr ilqkal
//
LOCUS       WP_457648352             188 aa            linear   BCT 27-JAN-2026
DEFINITION  EF-hand domain-containing protein [Profundibacter sp.].
ACCESSION   WP_457648352
VERSION     WP_457648352.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000101
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..188
                     /product="EF-hand domain-containing protein"
                     /calculated_mol_wt=20334
     Region          68..183
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mrrktggday nlyefnnpnv kkdnkmkrip lliaaialgs vayaqpnvpg ahfienwdfn
       61 edgqvtkeea verrgdiftt fdenddgils asdyaafdea raadhasmrq gggmgmgqgk
      121 gmgqghgmgk gggqysrgeg mtlkfndvng dgqvtreefm artndwfamm dkngdgtita
      181 ddfgrgnn
//
LOCUS       WP_457648351             115 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Profundibacter
            sp.].
ACCESSION   WP_457648351
VERSION     WP_457648351.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..115
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12542
     Region          14..112
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mdwkensrdm raeiremnkl ipetaagfat lskavkdngt ldvktkefla laisisercd
       61 pcigfhveal iragatreel advlamniqm gggpalmyaa kaleawdqma kkqen
//
LOCUS       WP_457648646             569 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Profundibacter sp.].
ACCESSION   WP_457648646
VERSION     WP_457648646.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 569)
  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 569)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13537404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..569
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=62177
     Region          <34..523
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          360..560
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          362..390
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(363,366..367,370..371,373,401,404..405,408..409,
                     411..412,435,438..439,442..443,446)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          399..429
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          434..462
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          468..498
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          503..531
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpvkpntpfa alalgfaavf pgysamaeps agdylaarha symsdykags eyytkallsd
       61 ptnpvllena lvsfvglgdf sraipvarkm esdgivsqis rmvlvvalak aedydtllak
      121 ldkgetvgpl vdgliaawae iakgnkpaam agfdevaqgk gmrsfglyhk alalasigdf
      181 deaekifagd esgpvritvg gvlahveils qlgrndegle ilskvfgdep dprvaqlrda
      241 lkagdkvpfs lvhnanegma evffsvasal kgetddgytl iysrmaeqln pnhidaills
      301 agmlerlery dlatdtynrv prddpsffaa eqgraaamrk agkeeaalev lqqlakshgn
      361 lpsvhtalgd ayrqqkryee aakaydrave lsgkptpddw flyyargisr eridewdkae
      421 adfrmaleln pnqpqvlnyl gysllehnik ldealkmiqr avlaqpndgy itdslgwalf
      481 rlgkydeamk ymqraaeltp vdpivtdhlg dalwavgrkl earfqwrral sygpepkevt
      541 rirrklevgl davleeegad pipvaangd
//
LOCUS       WP_457648784             406 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Profundibacter sp.].
ACCESSION   WP_457648784
VERSION     WP_457648784.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13466756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..406
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=43575
     Region          63..>247
                     /region_name="PRK10770"
                     /note="peptidyl-prolyl cis-trans isomerase SurA;
                     Provisional"
                     /db_xref="CDD:236758"
     Region          161..296
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mriltlcltf tglvltglat pasaqnlfsp avkineqvit hyevqqrarf mtllrapgna
       61 qeqaleglid erlqtaaaaa agitpneeev qggmeefaar anltaeqfvk alagggvaae
      121 tfrdfvkagl awrslmrakf gprvqvtede idraiaqtsg kgglrvllse iilpantpqa
      181 taasqkqaek iaqttslsvf sanarrysas psaqqggrlq wmplsnlppe irgqilalsp
      241 gqvtapisit ngialfqlra ieetdaaapk dlslefaqyf isggqseaal keaarikarv
      301 dtcddlygin kgkpeellqv dtlpvsqvpq dialelakld pgevstrltr nngqtlvflm
      361 lcgrtpelge dvsretiraq lvnqrlqsya dgylselkad ativyp
//
LOCUS       WP_457649299             388 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Profundibacter sp.].
ACCESSION   WP_457649299
VERSION     WP_457649299.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 388)
  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 388)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
REFERENCE   3  (residues 1 to 388)
  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 10560168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..388
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=41539
     Region          51..310
                     /region_name="PGA_cap"
                     /note="Bacterial capsule synthesis protein PGA_cap;
                     pfam09587"
                     /db_xref="CDD:430701"
     Site            order(57,59,95,150..151,247,279,281)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:277327"
     Site            order(57,59,95,150,247,279,281)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:277327"
ORIGIN      
        1 mkpalgwgll altllagcvp eqqvqtggqc vpkpafqapp vnpcadserv rltivgdvll
       61 hwpiqqtgyk ygfrkmwaqa dpylawgdlt ignmegpvap gvdqsgrqvg gpgpvygtgv
      121 ytgfpifnyh pqilkelkas gfdlmttann hamdrgslga dltlremaka glvavgtirs
      181 gaprrfavrr gtalgtvsfi acsfstngnp dpkrqvllcy gnrsellslv rreatdpsva
      241 avivlphwgq eysstpdtqq valardltaa gataivgthp havqpfrlln tgrgqvvpvv
      301 ystgnfiamq tkmpsrvgam allemckapd gkgltvnrlg wiaeqmyftk tkywmeiapv
      361 gatgdkgvpy rhlskiasgf saqpqayr
//
LOCUS       WP_457649359              82 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB N-terminal domain-containing protein [Profundibacter sp.].
ACCESSION   WP_457649359
VERSION     WP_457649359.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 706361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..82
                     /product="ParB N-terminal domain-containing protein"
                     /calculated_mol_wt=9054
     Region          22..>79
                     /region_name="ParB_N_Srx"
                     /note="ParB N-terminal domain and sulfiredoxin
                     protein-related families; cl28891"
                     /db_xref="CDD:452888"
     Site            order(24,26,56,59..60)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:319246"
ORIGIN      
        1 mlvkesfpva qirvpvkrak tldaakvqei aesmleegqt tpirvrkskd gyvlieglhr
       61 lealkalgee mvegylvrav lh
//
LOCUS       WP_457649457             311 aa            linear   BCT 27-JAN-2026
DEFINITION  methylenetetrahydrofolate reductase [Profundibacter sp.].
ACCESSION   WP_457649457
VERSION     WP_457649457.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1049
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..311
                     /product="methylenetetrahydrofolate reductase"
                     /EC_number="1.5.1.20"
                     /GO_function="GO:0004489 - methylenetetrahydrofolate
                     reductase [NAD(P)H] activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006555 - methionine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009396 - folic acid-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=33540
     Region          28..295
                     /region_name="MTHFR"
                     /note="Methylenetetrahydrofolate reductase (MTHFR).
                     5,10-Methylenetetrahydrofolate is reduced to
                     5-methyltetrahydrofolate by methylenetetrahydrofolate
                     reductase, a cytoplasmic, NAD(P)-dependent enzyme.
                     5-methyltetrahydrofolate is utilized by methionine
                     synthase...; cl00246"
                     /db_xref="CDD:444783"
     Site            order(57,83,114..116,127..128,148,150,154,156,163,169,
                     172..173,187,189,283)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:238299"
ORIGIN      
        1 mallhfkkkp eagplpvnpq leaflkgysi evmprtaakv edftallpkg trvyiahieg
       61 tpiedmvata trlsadgfdv mphfpariia dratladwis ryrgeadvtq alllaggtak
      121 plgefdnsmq lletglfdsa gftnlhfagh pegnrdidpd gsdknvmeal rwkqdfsnrs
      181 daktalatqf vfeakpview adalkdagid mpihlgiagp aklqtlvkfa iacgvgpslk
      241 vlqkrakdmt klllpfeptd lltelaayka enpdsniaqv hffplggikt nanwaiahgg
      301 ksaapanqtq d
//
LOCUS       WP_457649560             492 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Profundibacter sp.].
ACCESSION   WP_457649560
VERSION     WP_457649560.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 492)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..492
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54332
     Region          1..490
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mtayddlmay erdtqalgqv sgrlgwdqet mmprgaagqr aqemaamssv lharrtdpkv
       61 gdwlaeidds tldavgqanm rhirrgyert mriperlate qaklhsmaqg iwaqaraded
      121 fagfaptlkq vlklkreeaa aladggdlyd allddyepga kaseleamfg alrprlvalr
      181 ervlgaqnqp atleakfdea lqleltrkla vtfgydmnhg ridkavhpfs sgsghdvrit
      241 trtnpydpfn cfystihevg hgcyeqsidd ahlltplgrg vsmgvhesqs riyenqigrg
      301 qaftgwlfgq mnevfgdfgv adadafyatv nrvnsgyirt eadevhynlh vllrfdlera
      361 miagnldvdd lpdawnerfe ddfgvavdkp sngclqdvhw svglfgyfpt yslgnvyagc
      421 lnkamrdals dldaelaagn tapatgwlre niqqygglyr pkdliekacg fapseaplld
      481 yleakfggiy gv
//
LOCUS       WP_457649926             300 aa            linear   BCT 27-JAN-2026
DEFINITION  SPOR domain-containing protein [Profundibacter sp.].
ACCESSION   WP_457649926
VERSION     WP_457649926.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 300)
  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) (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  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 18658991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..300
                     /product="SPOR domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31794
     Region          103..298
                     /region_name="FtsN"
                     /note="Cell division protein FtsN [Cell cycle control,
                     cell division, chromosome partitioning]; COG3087"
                     /db_xref="CDD:442321"
     Region          228..299
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrrtvggtwg kigrltilas vaitlagced gktfnlfkpk aqadgtatts qrpgkvvekd
       61 veapelfhkt esglwdgrps lggiwiahpd vkdplrviir neangksvvg alfrrerenp
      121 gpriqvssda asalkmlagq pvkldvvalr rekieetspe pepapevapt ketldapeti
      181 eekslgpias aaaaidaaeg kpvarpdaas aepaaapava psklakpyvq lgtfaskena
      241 dkavedmrkv glfavpkeqt angktiwrvl vgpagrraer tamlrkvksm gfkdayivsn
//
LOCUS       WP_457650145             561 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Profundibacter sp.].
ACCESSION   WP_457650145
VERSION     WP_457650145.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..561
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58699
     Region          31..453
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mneektlaar klgeaadslr tglrvlrqkg psqvqfwfia lligiasgya algfrkgita
       61 lqswlygaed lhmlhtfaet lqwywiltip iagglvvgli lnrytddgvv rsvadviega
      121 amnegrveqk egiasafasm itlasggssg regpvvhlas visswvsnri nangitgrdl
      181 lgcavaaavs vsfnapiaga lfalevvlrh favhafapiv iasvagtvis rihlgdvtef
      241 tvpvegslvf yvelpafmil glvsglvava lmkavfwadd lgtyvqnrtr mprwlrpava
      301 gamlgalaiv fphiigvgye ttsraltgnl llyqaivfav ikviavaitm agrmgggifs
      361 pslmtgaltg lafglistsi fpnvsgseti yalagmgava aavlgapist tlivfeltgd
      421 wqtgiavmva vslstalasr ivdrsffltl lerkgvhlsa gpqayllsmc gvasvmrakg
      481 tegapsddac weligqgvyi dgnatlkqam pifestahaf ipvvtlgsea espelwgalf
      541 qvdalkaynk alaataaeeh s
//
LOCUS       WP_457650177             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Profundibacter sp.].
ACCESSION   WP_457650177
VERSION     WP_457650177.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20368101
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..372
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39651
     Region          <2..368
                     /region_name="ABC2_perm_RbbA"
                     /note="ribosome-associated ATPase/putative transporter
                     RbbA; NF033858"
                     /db_xref="CDD:468210"
     Region          190..371
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrrliniywl sgkelksvlg dpvmvilimw sfvvavllea sgagdtvyna aiaildedns
       61 tltrhlagal gppwfqlpvm itpdqvtpem dagrimfvlg fppnfeadvi aglspvvqle
      121 vdatavsqaq lgtdyianil qaesrafltg tplgpeppit ldlrqafnpn anpvwfksvs
      181 sllnqlsllt ialtgaamlr eremgtiehl mvmpltpiei alskvtaniv vvlvaftlsl
      241 mfvvqgllkv pvvgsiplll fgtatylaaa aaigmlmgtl arsmaqfall vimviipiim
      301 lsggmgaies qpdlvrkltn ilpsrhflaf akavvfrgag idtvwpqlal maglgatffg
      361 aslalfrrsm sl
//
LOCUS       WP_457650300             138 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF4177 domain-containing protein [Profundibacter sp.].
ACCESSION   WP_457650300
VERSION     WP_457650300.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 83317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..138
                     /product="DUF4177 domain-containing protein"
                     /calculated_mol_wt=14672
     Region          4..76
                     /region_name="DUF4177"
                     /note="Domain of unknown function (DUF4177); pfam13783"
                     /db_xref="CDD:433476"
ORIGIN      
        1 mpnfeykvvp apkkglkgkg ikgaeekfan alatvmnelg aggweyqrsd tlpceersgl
       61 rgktttfhnv lvfrrrvaak aettapkpvt prpvkkaseq rapqldsaia resgtapavg
      121 pateatevkd prtvsdgq
//
LOCUS       WP_457650743             495 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Profundibacter sp.].
ACCESSION   WP_457650743
VERSION     WP_457650743.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter sp.
  ORGANISM  Profundibacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 495)
  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 495)
  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 495)
  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..495
                     /organism="Profundibacter sp."
                     /db_xref="taxon:3101071"
     Protein         1..495
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51351
     Region          243..493
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <373..>445
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 mtgfnyiavf qsdawaylng issfqlvpdg ggyrlyggsg syggiigftl tagaaashig
       61 dwlvddggns frlsdftmvg gdllvaelgs shlerynfst sgslinpapv sysgntpslt
      121 pqivsisvgt ttfvatggga ggpeglniye vqggtlihtd tvmddikvtv gdiadlvtvt
      181 vngtdylvvg strdsgistf tidasghthl vdaigqkegl wlsgldslaa teangtsyii
      241 vastlsgsls vvrinpmgvm fvtdhvtdtl gtrfdnvdai dsftvngrgf viaggsddgl
      301 tlleimpdgr llehdsienq ngwtlenita iqtavfdgev qvfaagsrms gimqftiptd
      361 alatpingds gnntlsgtal ddliyggagn dtlhgnggdd ilfggdrldq lyggagadvf
      421 iidsgpdqdq irdfelgldr idlsrwgmvy dpsdltitsh tggatvqfgd lsldirtddg
      481 siltaadlta dsfif
//
LOCUS       WP_457651053             350 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Propionibacterium freudenreichii].
ACCESSION   WP_457651053
VERSION     WP_457651053.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..350
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37703
     Region          21..>334
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrpmpdeetm spttkkasra rlkvfgvlwv iillnyidra tlsiaipfis qdlhitpeak
       61 gsimgtffwt ylifqipggw lldkfgprri iticaalwgl aqaaiglarg gmsmgilrlg
      121 lgafeapaap agsklnanwl paserargat fvdmagsfgt avggvlvtav iglfgswrwa
      181 fvatglltlv vavfyffyvr dvpedhsgvn eaelahirge vateevadst gplptvfdya
      241 rsmsfwglwl grlgwalvww giiswspsyl rdvmhfdlat lgwstfliyg mgvvgqlvag
      301 aladkgralt gnynlvmkvl lgisglgmla cmlsllgisn gyvgssrlrv
//
LOCUS       WP_457651063             267 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Propionibacterium
            freudenreichii].
ACCESSION   WP_457651063
VERSION     WP_457651063.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28140
     Region          13..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mrddnseiaa ytrdltkvyg sgdaevvald hvdvdfvkar ftavmgpsgs gkstlmhcva
       61 gldaptsgev vigdtniatl kdsrltelrr drigfvfqsf nliptltale nielpmaiag
      121 rkpdpewldh vidivglrsr lkhkpsqlsg gqqqrvacar alvgkpdiif adeptgnlds
      181 aasaeilgfl assvtdlgqt ivmvthdpta aayanralfl adgrivadmd dpdrdkvlar
      241 mvelsspvda sapgastqaa gpstvqg
//
LOCUS       WP_457651086             341 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Propionibacterium freudenreichii].
ACCESSION   WP_457651086
VERSION     WP_457651086.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium freudenreichii
  ORGANISM  Propionibacterium freudenreichii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Propionibacterium freudenreichii"
                     /db_xref="taxon:1744"
     Protein         1..341
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36616
     Region          12..>325
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mspttkkasr arlkvfgvlw viillnyidr atlsiaipfi sqdlhitpea kgsimgtffw
       61 tylifqipgg wlldkfgprr iiticaalwg laqaaiglar ggmsmgilrl glgafeapaa
      121 pagsklnanw lpaserarga tfvdmagsfg tavggvlvta viglfgswrw afvatglltl
      181 vvavfyffyv rdvpedhsgv neaelahirg evateevads tgplptvfdy arsmsfwglw
      241 lgrlgwalvw wgiiswspsy lrdvmhfdla tlgwstfliy gmgvvgqlva galadkgral
      301 tgnynlvmkv llgisglgml acmlsllgis ngyvgssrlr v
//
LOCUS       WP_457651102              31 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial [Serratia
            liquefaciens].
ACCESSION   WP_457651102
VERSION     WP_457651102.1
KEYWORDS    RefSeq.
SOURCE      Serratia liquefaciens
  ORGANISM  Serratia liquefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 31)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 31)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 31)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..31
                     /organism="Serratia liquefaciens"
                     /db_xref="taxon:614"
     Protein         1..>31
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          2..>31
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 mlrifctaae srnfkdaail lgispqvvtr a
//
LOCUS       WP_457651151             562 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Rhodocaloribacter sp.].
ACCESSION   WP_457651151
VERSION     WP_457651151.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13256266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..562
                     /product="peptidylprolyl isomerase"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=63093
     Region          2..268
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase PrsA; PRK03002"
                     /db_xref="CDD:101162"
     Region          131..263
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
     Region          406..541
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mrrfvsilfl tigtavlagc graqtsgtpl vtvagtdvst dafrtqytdy llrvglhdtp
       61 rlrdgflqrl ittalvvrea rdagiereea yrlheekarr kllleafadr vlfdtirvte
      121 aemaevfvri ntqvkarhly artragadtl aarlrrgetf ealaeevfad talarhggsl
      181 gyfsfdemdp afedaafslr vgersepvrt aygysiieve drftkpilte tefaekkdrl
      241 aayvlrrkra earsayvrrl aaeldatfhe paftrlvdra agrsvttdde traawlaepl
      301 vtfgpegarr twtvadfrar arftdearla eidtpeetad fvrglavrev mleraeaarl
      361 delpeykeal rramdewvwe raferitagt tvpedtlray yathraafti pervrvweil
      421 vgtkaeaeal rarlgaepfe alarahstrp gadatggdlg fvtpgqlgml agpvfdareg
      481 tvlgplevag ryvllkvgar qparqasfee arpeierqlr erferrrfra hadalrerye
      541 vvlhkkaaaa vanafeakkt sf
//
LOCUS       WP_457651271             230 aa            linear   BCT 27-JAN-2026
DEFINITION  energy transducer TonB [Rhodocaloribacter sp.].
ACCESSION   WP_457651271
VERSION     WP_457651271.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 2264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..230
                     /product="energy transducer TonB"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25759
     Region          137..230
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     cl10048"
                     /db_xref="CDD:471968"
ORIGIN      
        1 mrridstydr reryalhvma alvasllvvi aavrwwplpn hdappgmvfd vrgqeiiafe
       61 evvqtrqqmr rppppaplvp vvvpdevvle dydlelldny lpveepgddq efvegdvvgt
      121 qatmasaevg pkpvrivepe ytkaarkkki raevvievlv nergrveqar ileryllgkk
      181 qtdpkqsvst lgfgleeaal aaaegwmfrp arqngkpvrs ffvftlsfgi
//
LOCUS       WP_457651358             397 aa            linear   BCT 27-JAN-2026
DEFINITION  homogentisate 1,2-dioxygenase [Rhodocaloribacter sp.].
ACCESSION   WP_457651358
VERSION     WP_457651358.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..397
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=45682
     Region          1..384
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyfklgqv phkrhtqfrk pdgglyseev igaegfsgiq siayhlhppt vvdriedpip
       61 ygvaytdldf lrhrhikgfe iessgdwlaa rryvmgnedv rlalaeptde mdyfyrnava
      121 devvfvhege gvlespfgvl eftagdyvhv prtithrwkf kegvkrrlli iesfsevrfp
      181 krymnqfgql lehspfcerd vrppselmti daegefevri akhgylhrlf fryhpfdyvg
      241 wdgymypyaf sihdfepitg rihqpppvhq tfagrnfvic sfvprlydyh peaipapynh
      301 snidsdevly yaegnfmsrr giergsftlh pggiahgphp gtveasigkk gteelavmvd
      361 tfrplrltkl alehedpdym fswrpeafat plpsngh
//
LOCUS       WP_457651410             454 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Rhodocaloribacter sp.].
ACCESSION   WP_457651410
VERSION     WP_457651410.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 454)
  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   4  (residues 1 to 454)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19835644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..454
                     /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=51143
     Region          1..454
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          249..454
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrayrvsvnl klglivfagl iavaslvytn rlvkrlgere qsimqlwgka yeqlskaaqp
       61 qalnpylpel reldallrqw eqgagetalp perleayrka vlwaqgmpea selsfitdai
      121 lvpntfdipa ivvdadtkra vnwrnidgvp dsfeglsped slrvvetler rledmakafd
      181 pipieidygd qklnqllyfd esnlvkrlri fpyiqlifvs lfilvgyfgf syvrrneqss
      241 lwagmakeaa hqlgtpissl mgwlevlrmp dlppgqaeta lneiehdier lhrvanrfsd
      301 igslpklesm spavviarta dyirrrmpqr gvtldveapa elraplnael fewvienllk
      361 naldaietee grievkawge hgkviievkd tgkgidrrnw knvfrpgyst krrgwglgls
      421 lakrivedyh ggtltlaqsr lgrgstfrie lpaa
//
LOCUS       WP_457651552             469 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Rhodocaloribacter sp.].
ACCESSION   WP_457651552
VERSION     WP_457651552.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..469
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=51266
     Region          <52..>154
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          145..453
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 mnvktltgss isallaearq lfgddvllle svpaqgdrha ritvmvdrrl parqpraepq
       61 paregapppt yrqkvivrpe palvdvreav gagggatppa agygysaarp vpadaahgge
      121 gfsrdhapga gsprkrrtgr gslfpaetaa parrpveaas wkplgdlfst rierlekrle
      181 afenlfghaf igaaqpwmth plyglllkqg lrtrtltrlf nrlaemgiap gddpsrvqwa
      241 latelrsmld vtqpktcaga qlfigasgag ktalqlklar hprflgrrkt tilviepeke
      301 eavshhcpve lyrkfdlsvq tvrrpeemra aldrarrfsh ilidtpplpl qpqaahaall
      361 rlqymteava plqihlvlda trvldafdar ylermplrpd tlafthldea dglgrvaecv
      421 melglpvqfv sngmrvpddv gsfspsrlve ellnmsivsk srslawsml
//
LOCUS       WP_457651886             596 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Rhodocaloribacter sp.].
ACCESSION   WP_457651886
VERSION     WP_457651886.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 596)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 596)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..596
                     /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=65142
     Region          4..525
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(52,55,366,369..370)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mqgidwlivf tylfatlgig vylgrrasss ieeffvsgrs lpwwlagasm aattfsidtp
       61 lyiagvvgnr giagnwewwa famghvvliy vfarlwrrse ivtdaeviev ryggrpaavl
      121 rgakaflfav pinciaigyi mlaavkvvga lgiwqglgya peervlgldp klltvagism
      181 lvlayagfsg lwgvvttdff qfflalfgai lvaffavrsp eigslsvlve kaqavtgfdv
      241 lafipftier sgdwwrvgws afagisastf fgyvllqwwt frrsdgggef iqrlaaskde
      301 aeaekaawff nlmhyvvrtw pwvlvalaal viyptledre lgypklmldy lppgvlglvv
      361 asliaafmst vstqinwgas yltndlyrrf irpqatqrel irtgryasvl italgavaaf
      421 fardvatvfr lviaigtgpg vvlilrwfww rinawaelsa miagflvglf ttvvpvltia
      481 dfgvrlfvit vitsavwvsv myltqpetpe tlaafyrkvr pggpgwraqr aatgvppaqs
      541 lkhdvlrvla alpllfglmf giggalllrw dvagamalta aagglwlhrl rvagps
//
LOCUS       WP_457651893             156 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Rhodocaloribacter sp.].
ACCESSION   WP_457651893
VERSION     WP_457651893.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     gene            1..156
                     /gene="rimP"
     Protein         1..156
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=17429
     Region          12..156
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 mtesmkiaat peervrtlve evidasmfvv evivrgrkgs rvvevfldgd eplsiealar
       61 vsrevgflld veevidgkyr lnvsspgldr pltlprqykk hvgrtlrvrf rdgenertvk
      121 gklletaedg iviaagkeal ripftemvqa kvelpw
//
LOCUS       WP_457652193             493 aa            linear   BCT 27-JAN-2026
DEFINITION  LptF/LptG family permease [Rhodocaloribacter sp.].
ACCESSION   WP_457652193
VERSION     WP_457652193.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Ruiz,N., Gronenberg,L.S., Kahne,D. and Silhavy,T.J.
  TITLE     Identification of two inner-membrane proteins required for the
            transport of lipopolysaccharide to the outer membrane of
            Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 105 (14), 5537-5542 (2008)
   PUBMED   18375759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10509922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..493
                     /product="LptF/LptG family permease"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55701
     Region          7..456
                     /region_name="LptF_LptG"
                     /note="Lipopolysaccharide export system permease
                     LptF/LptG; pfam03739"
                     /db_xref="CDD:427477"
ORIGIN      
        1 mlthfhrmii rllpgpflgw lgtlmflllm qflirylpdl vgkglptgvi lelivynlay
       61 mlvlavpmsa listlmtfgr laetkayvvi kgagaslpql lwpvlliglg laggmwyfnn
      121 qilpeanfra rnlwwdirkk kpgfelqagv fyegvnnysi lvqsippdrp nvlediliyd
      181 ytegsrkrvd ikaregriep lgngeqidlv lfdgeihrrn kppssrdper yerlafarhr
      241 frldlsdfif ersdpsrtrr sdrtmrtdem irivdslrts varekqklfe asmrlltdtt
      301 taspgeatpa lptptvaagt erpfsdrpvl aglrrgqqve vydvavmkar nartqvdnar
      361 ravkwqqeqa nrylveihkk rsialaclif vligaplgls irrgglgtag alaiglflff
      421 wvtlvqgekl adrnlltpwv gmwaanlitl vagtwlvlyv tfdlratprl rtrlaewlrr
      481 rrlgtkaaap eps
//
LOCUS       WP_457652613             428 aa            linear   BCT 27-JAN-2026
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Rhodocaloribacter sp.].
ACCESSION   WP_457652613
VERSION     WP_457652613.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 153005
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..428
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:2001070 - starch binding [Evidence IEA]"
                     /calculated_mol_wt=46560
     Region          <328..>395
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mnkwinglap tlsaallaiw tlagcglldv enpnnlvedd lsnpaaadpm angaeasvtr
       61 alsyitapys vatdeltwvg srdawgqldd gvidfsgnef tdqafpfvge arwmtdefig
      121 rleafqeaga gstnalirvy lynaiiytti admfddftls drtepgppvg penmvtlydh
      181 algsvnkala lnpsgdleaa lmgmkariiy skavwqkvnp vntssplvna gaaeaaaaln
      241 vmdsdfvfkl iadggfqlen ymsgqindrl eftftdtwvk rneagnkvde vtypdmidgv
      301 vhpylkafie dfvaqrqyad lpivsaremh lilaesalaq gdmngftthi nhiraldglt
      361 pysgqvdaqd lliesravnl flqgrrladl yrfglqspew esgtpamtrp gtflpitkve
      421 ieanplvk
//
LOCUS       WP_457652632             597 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Rhodocaloribacter sp.].
ACCESSION   WP_457652632
VERSION     WP_457652632.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 597)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 597)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..597
                     /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=65627
     Region          6..519
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(54,57,356,359..360)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mqlggidwai mavffalslv iglavsgrsg knfnafflgg rdmpwwllgv smvattfstd
       61 tpnlvtdiir tngifgnwtw waflltgmlt vflyaklwrr sevltdvefy eirysgklaa
      121 flrgfravyl gilfniiima svtlaaikig gvmmgwsaie tvvvaatvtm iysalgglrg
      181 vvltdlvqfi iaiggsigaa iyilnmpevg gldglfshen vrsalsfwps feeltwqeml
      241 pvffiplavq wwaayypgae pggggyivqr mlsakdekha vgatllfngl hyalrpwpwi
      301 lvalsslivf pelsmmaerf pdlsaqvirn dlgypamltf lpsgllglvv tslaaaymst
      361 mstqvnwgss iivndlyhrf lnpeaterql vwvgraatva lmvvactlal flenalqvfn
      421 illqigagtg llfllrwfww rinaatelta mivsfllavy fqvagrmewp gggladwqrl
      481 lyivalttaa wmivayttap tdpevlkrfy rrirpggpgw gavqaalrre gvavateasd
      541 lpyglaaavc galgiysvlf atgfflyerp ltgllfvaia avsflgiyrl wprlrfe
//
LOCUS       WP_457652692             267 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF5683 domain-containing protein [Rhodocaloribacter sp.].
ACCESSION   WP_457652692
VERSION     WP_457652692.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1750719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..267
                     /product="DUF5683 domain-containing protein"
                     /calculated_mol_wt=29780
     Region          145..>201
                     /region_name="DUF5683"
                     /note="Family of unknown function (DUF5683); pfam18935"
                     /db_xref="CDD:465918"
ORIGIN      
        1 mrafrttalv lcmalaalpa hgqrtraavv eeirqayerl dyaeaeakah ealaantdft
       61 vdqlveihtl laliafsdnr eaearaqfms altlnpdlel dpllvspkil tffdeikrsr
      121 qratseqepg aairyvrved praaaamrsl llpgwgqqyk gektkgwilt glwglaaagt
      181 vaahlrrkqt rdaylaesnp dlvparydtf ntwhkarnnl alatallway syfdallfrp
      241 appgdrrlli tadpsptrpr lslrlrf
//
LOCUS       WP_457652890             881 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Rhodocaloribacter sp.].
ACCESSION   WP_457652890
VERSION     WP_457652890.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 881)
  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 10154659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..881
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=98348
     Region          63..>195
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Region          137..353
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06238"
                     /db_xref="CDD:349457"
     Site            order(147,150,214,233..234,263..264,268,339)
                     /site_type="active"
                     /db_xref="CDD:349457"
     Region          <669..>760
                     /region_name="A4_beta-galactosidase_middle_domain"
                     /note="A4 beta-galactosidase middle domain: a type 1
                     glutamine amidotransferase (GATase1)-like domain; cd03143"
                     /db_xref="CDD:153237"
ORIGIN      
        1 msrlprllfa sllalfglas garaqvdlap erfafspdlp ydpdvpapsd flgyelgtql
       61 tlyadvvayl raldaasdrv tmhaygrtye grplhylvit tpenharlde irrnnlrlad
      121 gealpedeae aliaaqpvip wlsynvhgne assteaamqv ayrlaaatdd dtrallsrav
      181 vlldpcinpd grdrfvywnr amqndrvste avdmehtepw pggrtnhywf dlnrdwvwlv
      241 hpesqgriaa yrrwmpqvhl dyheqgsnan yftmpgqtpr nlnlpdeydq wadafgrana
      301 rafdqnriny ftresfdffy pgygssypsn lgaigmlaeq gsargravet ndgyvltlrq
      361 gvfdhyttsi atirtavenr eallryyrrf ftqaanksnt aaylladdgg agyvydvvdv
      421 llkhgvrver aeapftvrda rdyrdgrpra rtfeagtfvi rtdqprhvfv ntilqrqmai
      481 edsvmydmat wsaplaynld aawtttapka rtqplaeapa ppsgltnpda qyafvidgrq
      541 rhtpralaml wdagyrvraa rkpfsdgers fargslvvll grnrerldra aedmariare
      601 arvrivgmds grmaegidla sndsrpvkkp kaamlvgrpf ssytagqiwy lfdrwtglgl
      661 trvrsdrfpt lkladydvli lpgagdpssv ldsaqvdrlr rwvrdggtlv ategsalflt
      721 kdrsgltnvk rvkeakddek ddekgggppp aaytpyaarr dslglrripg saflahvdat
      781 hplafglrgd qlyslrfste alepsetlqt vghytadpda vlvsgyasaa nrrrlagktf
      841 aavqpmgrgr vvflvdntqy rmfwvgparm mqnavmlmpg m
//
LOCUS       WP_457652960             132 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein
            [Rhodocaloribacter sp.].
ACCESSION   WP_457652960
VERSION     WP_457652960.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..132
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14063
     Region          24..114
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mgtqthepet pakhawqtgs gmlpglihdl drlraeamgd raldkkvkel ialgiavaer
       61 setsiayhvh nalaagvsre eiaetigvai fvgtepaaiq giqllealar devekyaegv
      121 frpaahpyms pd
//
LOCUS       WP_457652980             469 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Rhodocaloribacter sp.].
ACCESSION   WP_457652980
VERSION     WP_457652980.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (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   2  (residues 1 to 469)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 469)
  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 469)
  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 10157591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..469
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53251
     Region          64..278
                     /region_name="CESA_like"
                     /note="CESA_like is the cellulose synthase superfamily;
                     cd06423"
                     /db_xref="CDD:133045"
     Site            171..173
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133045"
     Region          <243..>393
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
ORIGIN      
        1 mhtvfwtfla afhavvftyf vvlnsyylvm sifafralrr yarrltsidv ddlvatagap
       61 pvtlivpayn eaetivaatr slltlrypey eilivndgsk dgtlevlrea ydlipaprfp
      121 lahlgtapvr gayhsrthpn lwvldkengk radainagin hcrtpllciv dadgllepda
      181 lirvvrpfle dehtvasggi irivngcrve dglvrevrlp rnpiarfqvl eylrsflagr
      241 vgwdalkimf lvsgafglfr rslvvevggl apdslgedle ltvrlhrhcr ergipyrihf
      301 vpdpvawtea petlkvlgrq rdrwqrglid tmirhvrmlf nprygriglv aypyffflem
      361 igpiveftgy lvfltvlalg iaslpfallf lfvavmlgsv lsiaavglee ltfrrytrlr
      421 dllrlfrlaf aenlgyrqil tyyrlrgtis yfrgldgwgd merkgfeer
//
LOCUS       WP_457653110             518 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Rhodocaloribacter sp.].
ACCESSION   WP_457653110
VERSION     WP_457653110.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1001326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..518
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=58729
     Region          35..373
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mrklsigiid vasrtgkqnl ygrvmranlt simpqviavw ceeaghdvsl tvhngpnpll
       61 dplpddldlv iigaftqsaq vayalsnyyr skgavtalgg pharcypeda aqyfdyvlgf
      121 tdkpildevl hdcaphrpmg vhlsadrqpa qlpsvrarwk yverlmekap liqvvamlgs
      181 lgcpytcsfc vdsivpyqpl dfdemkadlr fvrekmkrpi vgwhdpnfgv rfndyldaie
      241 eavppgsvef iaestlslls epnvkrlkkn gfkailpgie swfdmgyktk tgktlgrdkv
      301 ltvaeqvnmi lshlpylqan fvlgldtdeg dgpfeltklf ldrapgafpa ysmltafgrs
      361 aplnleyqrq drvlpfpfhf lnnngamnvr pknydwpdfy ermidlhrhs fsrraiarri
      421 ganrgwipkt mnviravtfe gwgkiryfte vrrmldedra fraffeqett eippffteqi
      481 rkdlgwlwdw lpegalehdp yaylktegvv tpdvvqaa
//
LOCUS       WP_457653160             909 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing sensor histidine kinase [Rhodocaloribacter
            sp.].
ACCESSION   WP_457653160
VERSION     WP_457653160.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   4  (residues 1 to 909)
  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   5  (residues 1 to 909)
  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 909)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 909)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   8  (residues 1 to 909)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18589043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..909
                     /product="PAS domain-containing 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=100635
     Region          103..348
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          386..894
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          653..893
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mslpewkiis aygaqilphl pdradvavae vdgdgvclri nplgaslwgw krgerlpgei
       61 vgmlgelpse aprllpvkpg gllllglrsg raagwilvgy pgeaaasqse ssfrtlvenm
      121 pvlalrmrad gavcyanaea rrmtgyapee mtgrafwfea vlpeeqgrlt eafeealseg
      181 rasvrtpfls rngalrmaei hlfrapegag pelesvvfdv teqmeveeal fqseslyrtf
      241 leqspigmlh ldaegmvtfe nhpfrqivge gvddawigln ifeipgldlg ihgpvrdile
      301 kgkafygvea tferrseaea rrlvvhgspi flpgrvvvgg vlmiedvtre rrreeelalr
      361 drygkaegdl rsaalahpde neflkaaari lgevtgadrl hllihnpvda lcvsrsvwvr
      421 atartdalhl rhddfpafrt ldasgrrhvh acegaaearp llaltgasea lwspfydadr
      481 lggfvlferv gegaeqpwgh aerglidhlv gvfetlwawv qvgnryrqtv aaiddglfhf
      541 tftedgerhy lfathqfeal vghtpealle rgpsalrwid dlvhpadhal vrahdealrs
      601 grehrvtyrv rrpdgatrwl rehatphrdd aghvtvsgiv advteqktae evllqakqea
      661 easnrlktaf iatmsheirt plgavsgfae llaaeleece aplppqihef veaiqdraqh
      721 lltlvndlfd lsnvemgalt vqraplnlht llrdaiekik palerkkltl tcdldpanpv
      781 vvgdpqrigq vlsnllsnav kftetggvsv rtrrrehevl vevsdtgigm aeayvqrlft
      841 pfsqeddwrs rrfegaglgl alvkrlldll ggrievesek drgttfrvyl paahrtttrt
      901 rpkrarpha
//
LOCUS       WP_457653234             594 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Rhodocaloribacter sp.].
ACCESSION   WP_457653234
VERSION     WP_457653234.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 594)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 594)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..594
                     /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=65370
     Region          7..521
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(54,57,344,347..348)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mqlvtadwiv iaaygvitla lglwftgrag qsieeyfvag rtlpwwlagt siaatwfasd
       61 aplaaaslvr qqgiygnwlw wyeaagimll vffyaklwrr aevitdaefi elryggrsas
      121 alrgftalyq gvlrncvimg wvmlamvkfs rvllgwgpvl tltvcvtmal vytvasglwg
      181 vvatdflqft vgiigsvila giilykvggp vemvrqigal sdapagaldl vpnpahispl
      241 effsylclil vlwtrsgneg ymaqrlfatk ddkqatltal wfafagtlmt wpwivaglgs
      301 liifpmssaa phlaadpela ypmmiaemmp aglrgllvaa flaafmstmd thlcwgasyl
      361 vtdvykrflr knetarhyvl asrvaviilv viaaltawqm esierawiyi ieltagmamv
      421 lllrwywwrv nawaeisamv gsvaiangfl aarllekigl lpdaavhavd tfygeeynfi
      481 ravfillfct fvwvvvalkt kpvsdekldr fyrkvrpggw wgpvaarcpe vkadmtasqk
      541 wmgwflgvlf iysallgvgy lilgkpfagv lliafstlsa lgtvriarta hlas
//
LOCUS       WP_457653690             194 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Rhodocaloribacter sp.].
ACCESSION   WP_457653690
VERSION     WP_457653690.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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
REFERENCE   3  (residues 1 to 194)
  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 10582454
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..194
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20588
     Region          1..167
                     /region_name="Metallophos_2"
                     /note="Calcineurin-like phosphoesterase superfamily
                     domain; pfam12850"
                     /db_xref="CDD:432832"
     Site            order(8,10,34,58..59,97,118)
                     /site_type="active"
                     /db_xref="CDD:277317"
     Site            order(8,10,34,58,97,118)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277317"
ORIGIN      
        1 mkiavlsdvh dhlwnlraal galdgvghli ccgdlcspfi mkrladdfpg eihvvfgnnd
       61 adtfritsia rgygervrlh gefadvtlgg rriavqhfda varplaasgr fdvvcfghnh
      121 taevtreplg grevlllnpg tlmgvrferg epvpvdatfa vydtdagtva rfavrgegge
      181 aaptaravvs lgsv
//
LOCUS       WP_457654010             294 aa            linear   BCT 27-JAN-2026
DEFINITION  cyanophycinase [Rhodocaloribacter sp.].
ACCESSION   WP_457654010
VERSION     WP_457654010.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Law,A.M., Lai,S.W., Tavares,J. and Kimber,M.S.
  TITLE     The structural basis of beta-peptide-specific cleavage by the
            serine protease cyanophycinase
  JOURNAL   J Mol Biol 392 (2), 393-404 (2009)
   PUBMED   19591842
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Obst,M., Sallam,A., Luftmann,H. and Steinbuchel,A.
  TITLE     Isolation and characterization of gram-positive
            cyanophycin-degrading bacteria-kinetic studies on cyanophycin
            depolymerase activity in aerobic bacteria
  JOURNAL   Biomacromolecules 5 (1), 153-161 (2004)
   PUBMED   14715021
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790602
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..294
                     /product="cyanophycinase"
                     /EC_number="3.4.15.6"
                     /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]"
                     /GO_process="GO:0043170 - macromolecule metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31697
     Region          24..276
                     /region_name="CphB"
                     /note="Cyanophycinase and related exopeptidases [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG4242"
                     /db_xref="CDD:443384"
ORIGIN      
        1 mmkrlsklfl avvpvfffvp gvgaqsvgpa hgalllaggg vhdpaiyerf lalaggpdap
       61 ivviptagga ddygpdwpgt rvferagath vtvlhtydpk vadtdafvap lraargvwft
      121 ggrqwrlada ylgtkvheel wkllerggvi ggssagatiq gsylargdtr tntvmmgdhe
      181 eglgflknta vdqhvlrrnr hfdlleiiea rpellglgld edtavvvrgd rfevigqhyv
      241 avydhartld sgapfyflap gdtfdlatrt ayrpgedgtp apfdrivdrp wsnh
//
LOCUS       WP_457654399             662 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Rhodocaloribacter sp.].
ACCESSION   WP_457654399
VERSION     WP_457654399.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Baharin,A., Ting,T.Y. and Goh,H.H.
  TITLE     Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure,
            Molecular Properties, and Applications
  JOURNAL   Plants (Basel) 11 (10) (2022)
   PUBMED   35631755
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15775175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..662
                     /product="S9 family peptidase"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74020
     Region          44..632
                     /region_name="lasso_peptidase"
                     /note="Atxe2 family lasso peptide isopeptidase; NF033523"
                     /db_xref="CDD:468059"
     Region          409..656
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrrlllgffl ltltltlpal gqdtprplei ddyfriknvs dpqvspdgqw vaylvtetnl
       61 ddderetslw mipaaggeal rmtaegysas rprwspdgry lsfmaskgek aktqvwafdr
      121 rggdarplts vkqgvsgyaw spdgarllls irdpkpddde phpwvidrlq fkrdyvgyld
      181 drhthlylat pgdstltqit sgpydesqpv wspdgkriaf vsnrtdnsdg ndntdiwiva
      241 adntdkgqtl lqvttnpgsd sspawspdgr fltyvtvtep dkiwyatnhl avvpatggaa
      301 rvlttkldrn vsaprfsddg rsilfvleds aerhlarigt dgrglsrpva ghlsvrafdr
      361 dggvtavlvs ephlpgevfv regdglrrlt tvnddlfagl rlaevrnihf pskdgteieg
      421 flflppgydp alryptllri hggpvsqydf rfnfeaqlfa angyvvvttn prgssgygqa
      481 fsyaiwadwg hkdfedvmag vdyaiaegia dperlgvggw syggiltnyv itktdrfeaa
      541 isgasevlyr snyghdhyqy ywekelglpw rnaeaweris pfndvenivt ptlimggekd
      601 wnvpilnseq lyqalkrlgr ttelvvypge hhgirkpsfq kdrferylaw ygryvkgvet
      661 er
//
LOCUS       WP_457654431             500 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxypeptidase M32 [Rhodocaloribacter sp.].
ACCESSION   WP_457654431
VERSION     WP_457654431.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 500)
  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 10789370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..500
                     /product="carboxypeptidase M32"
                     /EC_number="3.4.17.19"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56225
     Region          1..498
                     /region_name="YpwA"
                     /note="Zn-dependent carboxypeptidase, M32 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2317"
                     /db_xref="CDD:441891"
ORIGIN      
        1 mkenfeklka rlarvmdlna aaamlewdqe tymppgaagv ralqistlrk lahehltade
       61 igalldrlep avsgldpast eaalvrvtrr dyerarklpg rlvaalaeas ahareawkta
      121 retdtfetfa phlerlveln vekaetlgye ehlydpllde fepgmktadv eqifadlrae
      181 lvplvhaiae rpapdetvlh rpfdpqkqwd fgvavirnfg fdfehgrqdh sahpfttsfs
      241 vfdvrlttrv dehffnpaff gtlheaghgl yeqgidpald rtplasgtsl gmhesqsrlw
      301 enlvgrslpf wtyyyphlrk tfpesledva ldaffravnk vaptlirvea devtynlhim
      361 lrfelekaml egrlavadvp eawsdkmety lglrpdsdad galqdihwsl gafgyfptya
      421 lgnlmsaqlf dqakkdlagl eeqiaggnfe allgwlrthv hrhgrkktat eilvdttgeg
      481 lraeswltyv rekfgglygl
//
LOCUS       WP_457654534             107 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein
            [Rhodocaloribacter sp.].
ACCESSION   WP_457654534
VERSION     WP_457654534.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..107
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11224
     Region          10..102
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mnqppkrylk fieaheavga ayqalgeatt qagpldkkqv alvklgiavg mrhegavhah
       61 arkargagct peeirhavvl atttlgfpsm maayswvddv ldsgdge
//
LOCUS       WP_457654630             411 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Rhodocaloribacter sp.].
ACCESSION   WP_457654630
VERSION     WP_457654630.1
KEYWORDS    RefSeq.
SOURCE      Rhodocaloribacter sp.
  ORGANISM  Rhodocaloribacter sp.
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rhodothermaceae; Rhodocaloribacter.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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 708416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rhodocaloribacter sp."
                     /db_xref="taxon:2893092"
     Protein         1..411
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=44038
     Region          164..>378
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
ORIGIN      
        1 mrlfrppqll gifpapasyl llpavdgaps ldaartagrw pedvpeawrf fslalagdae
       61 aahaavtged avarynrfvl apdaaayerl kaeaeaedal lmravgylyr leaeppeppd
      121 dapdvlaafl watragrhle agdadaalah laraveaart vspalaarll attararrhv
      181 egpspalvpv yraavdalgd taferllget wldlgslyhe isggrrgall eaakcyqsaa
      241 qccpkeafpe lfalaqnnla laylaipltq agdrlrmava igalrealtv ytreahpeaw
      301 asatlnlana lqyaptgtpe ehlwqavdly eqvlevrape adplayarvl anqanalahl
      361 gafsravprl eeaarlfrah depdaaasve ailhdietrr anhgvarktt v
//
LOCUS       WP_457654824             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457654824
VERSION     WP_457654824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31559
     Region          30..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 meidrpglaa flrrrrellq pedvglprgq rrrtgglrre evavlchmst dyyarlerer
       61 gpqpseqmia siaqglhlsl derdhlfrls ghmppargtt gehispgllr ildrlddtpa
      121 eivtelgetl rltplgvaht gdttrytgla rsigyrwftd patrtlyvae dhaflsrmfa
      181 sglrelatlr gtgsraahca ellreesqef rrlwdqheig irpdqvkrfv hpevgvleln
      241 cqrlldpdqs hsllvytaap ggesherlrl lsvigtqtlr
//
LOCUS       WP_457654826             352 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457654826
VERSION     WP_457654826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..352
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34282
     Region          275..344
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mpcrcgagag sapltedeqr aartaeiaaa edfdplrirp yvtltdldar agggglaesg
       61 gsaatsgpgt seaatapvgt psapgaaett mplflgddgp gvgvgtgvdt gtgtvagasa
      121 sagpggrrrs agaepvfapd pvqprrrrpf galavgaava avvgtaafag glfggddsrd
      181 ealpeattsv pdtedepaas vapspsasta psrtpsasat psaspsasas ptknqeptpt
      241 atasasptas apatpdgggg assappaeap paelagpslr pgdrgpevae lqnrlmevwl
      301 ysgpsdanyn nrvenavaiy qsykaiqgdp agvygpntrr aleaetsgrg rr
//
LOCUS       WP_457654828             328 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces griseus].
ACCESSION   WP_457654828
VERSION     WP_457654828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 328)
  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..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /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=33008
     Region          17..328
                     /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 mghlahllsp rmsettavva gayggpevlt vidvavpepk pnqvritvra agvnpfdhks
       61 ysgafgvdpe rlpvrlgvea agvvtavgad aigpagpiav gdevitysap gayaaeivvp
      121 atsvvpkpva lsweqaggll aagvtavhtl eaiglgkget vlihgaaggv glvavqlava
      181 rgatvvatas rakhdllrel gaipvvygpg ladrvrevvp egvhaaadlv gteeavdvsv
      241 elvpdrlria tiaghergar agikllggvp gadpgteirq aarlqlaeaa tagrlrivia
      301 dsyplreaat ahreimaght tgkivlvp
//
LOCUS       WP_457654830             779 aa            linear   BCT 27-JAN-2026
DEFINITION  M9 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457654830
VERSION     WP_457654830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 779)
  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 10553015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..779
                     /product="M9 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /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=83911
     Region          125..306
                     /region_name="Peptidase_M9_N"
                     /note="Peptidase family M9 N-terminal; pfam08453"
                     /db_xref="CDD:430004"
     Region          365..649
                     /region_name="Peptidase_M9"
                     /note="Collagenase; pfam01752"
                     /db_xref="CDD:426409"
     Region          697..764
                     /region_name="PPC"
                     /note="Bacterial pre-peptidase C-terminal domain;
                     pfam04151"
                     /db_xref="CDD:427748"
ORIGIN      
        1 mggnnvrttl vrrgvgavlp lalagamsva llaqpaqaqp nspsaatasn asqpsspagt
       61 adpapqaqqs ptsdtghqlk drlkasqlpp lsadksalke ayghhdaprk qdavkkpsak
      121 aaaacdpadf tgrtgselvr qikgstidcv ntlfgltgnn aqlafreaqm vtvayalrdn
      181 aayypgdast gtpqlvlylr agyyvqwynp dvvgpygsal ttairsgldt ffasprshdv
      241 tdengetlse avilidsaqe narylhvvkr mladydsswn ayarmlaavn nvytvtfrgh
      301 qvpafvsave adpglidalh rfaadhlall ggdqayltsn agrelgrflq heslrgkarp
      361 latallqqts itgptaplwv giaemadyyd kancsdygvc dlqerlkrev lpvrhacsps
      421 irilaqqmts aeldasctsl ieqdayfhri akddgpvadd nntsieviay dssadyqtya
      481 gamygidtnn ggmylegdps vvgnqprfia yeaewlrpdf hiwnlnheyt hyldgrftmy
      541 gdfaegmstp tvwwvegfae yisyhyrgep ytaamteagk gtyalstlfg tnyshdttrv
      601 yrwgylavry mleqhpadmd tvlghyrage waaartyltg tvgtrydsdf rtwlagcaag
      661 dcgdgstapv sectdpdtrv lgencrrsdl sattgnyayh ylyipagtdr lkitvsggtg
      721 dadlyysgtg wattsahtsr dtgpgnthtl tvtnppagan yislhaastf ggatlttah
//
LOCUS       WP_457654831             372 aa            linear   BCT 27-JAN-2026
DEFINITION  Dyp-type peroxidase [Streptomyces griseus].
ACCESSION   WP_457654831
VERSION     WP_457654831.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Sugano,Y. and Yoshida,T.
  TITLE     DyP-Type Peroxidases: Recent Advances and Perspectives
  JOURNAL   Int J Mol Sci 22 (11) (2021)
   PUBMED   34074047
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Colpa,D.I., Fraaije,M.W. and van Bloois,E.
  TITLE     DyP-type peroxidases: a promising and versatile class of enzymes
  JOURNAL   J Ind Microbiol Biotechnol 41 (1), 1-7 (2014)
   PUBMED   24212472
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Sugano,Y.
  TITLE     DyP-type peroxidases comprise a novel heme peroxidase family
  JOURNAL   Cell Mol Life Sci 66 (8), 1387-1403 (2009)
   PUBMED   19099183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..372
                     /product="Dyp-type peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=40196
     Region          82..359
                     /region_name="EfeB"
                     /note="Periplasmic deferrochelatase/peroxidase EfeB
                     [Inorganic ion transport and metabolism]; COG2837"
                     /db_xref="CDD:442085"
ORIGIN      
        1 mgqqthwsev evvrrrnlma sglavalagg gaaayrlsvn ggagaaaapg dstgiplqlr
       61 gnlperylal ialdsggprg glrnlvnrvh asaepgasvg falgaaffgp raslprprql
      121 ramphfagdl lepsmshgdl lvhvvgnkaa aiqktverir ntdsahwtir whidgsrpdn
      181 rvedgrslar npfhftegfg npdteresld lalipsdqne pqwavggsyq vvriirfatd
      241 lwdkdsvgeq erivgrqrdg rwldgtpvde qpnfaadptg ritpldshvr laapdrrnpp
      301 pivrrsysyn kgngdkgiif scfqrdlaqg feavqnrleg eamakylltt gggyffvpph
      361 gdgwidalsy sg
//
LOCUS       WP_457654832             453 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces griseus].
ACCESSION   WP_457654832
VERSION     WP_457654832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 708416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..453
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=50088
     Region          145..>351
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
ORIGIN      
        1 mdeilerggl ealveatrvr edwfclagav rglcaagefg qawavvepfa atgwqpavrt
       61 gadvlwqwgr vdqalelarp agpqehafdt wrdyaemlvr agqlddaigv lgphlrdpra
      121 ldalvemtag lgcdervlel lapiaedfrr dpeqddlral wavlpaqarv leragrtdqa
      181 iqllgadvaa rrygvlntve fyaellarcs rieelgnlad thrhsavhpy vraleslgrt
      241 eeaeaylrgl iaaglpgwye smlmellirq grfddaikaa ehtfddlyds nllqgalill
      301 adqgqhdkai gltqgrspef laeneaywlr snrwwlmgea grareaiaei ealptdeved
      361 revtiawlla qdarveeait llrslpgkra atdlaellir qgrfmeaita ipdvatqree
      421 ergarakqhe saspdnghvy dapwaapnta ple
//
LOCUS       WP_457654833             379 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces griseus].
ACCESSION   WP_457654833
VERSION     WP_457654833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..379
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43106
     Region          40..362
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgvavrtidv pgaiqlvvpg nvraldpgpa mfgamlrgwe qqqqsrllar ktiddrlslv
       61 rrfalftaty pwewtpedve ayfshqlsld pplahstvrg qqgdlqmfca fitdgrygwa
      121 kaceeafgqf pvqvchgwnt adhvaefegr pgrraltyde lqalfdaadd rveqtrkrrr
      181 kgvlaawrda vmlkqvyayg trrretsmld lsdlrhnpra kdygrfgale vrfgkasrgs
      241 ppkrrtvltv peadwivsvl eewvdevrpg fspgghpalw vtercgrlgv rrldevftiv
      301 rehaalppel dlhclrhtyi thliefgype rfvqeqvgha yasttalytw vsdeyrnrll
      361 eeslrrrter aggkglgsr
//
LOCUS       WP_457654839             503 aa            linear   BCT 27-JAN-2026
DEFINITION  TniQ family protein [Streptomyces griseus].
ACCESSION   WP_457654839
VERSION     WP_457654839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..503
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=54294
     Region          57..204
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mslcpspipr ssartscgsr gtaaraslss rwpptpklrv rrprprsigh smttplprsl
       61 dpaqgellas yllrlahqvg ispldlahrc glttgtvlss aqhlvrladh haeqiatlcr
      121 ldlaevhalt lveqapsyap lhpvylgrhq shttmandgw vftafsrycp dcladtadqp
      181 ggsiwpgswr lphtflcprh qrlldwrcpq cqapafsngy rtdgrwrptq ltpaprsrlh
      241 parcrhrlgi gqvpacgyrl dqpsatgnap taamahtqqr lteaarsvag qdigslgrpt
      301 spqrflndvr avtliicstw paaaetlrdv ehldavaaha dtrnraater agppeggwla
      361 rsvdrppgdp lraaalmnlv vrildapdgq talarslsrl psngaayrrl qrltlhcspg
      421 mnaaiaestp lrhttvvgpt plfpqppthq glldpntipc plpdawarpl delkgpsapl
      481 rrdaairllq mthggsrata asa
//
LOCUS       WP_457654841             463 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457654841
VERSION     WP_457654841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  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 463)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 463)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 463)
  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 463)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..463
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=51087
     Region          132..461
                     /region_name="COG4586"
                     /note="ABC-type uncharacterized transport system, ATPase
                     component [General function prediction only]"
                     /db_xref="CDD:443643"
ORIGIN      
        1 mlpgsfsfkr rrctrenppp gsrgrrtrrn eddrsgqgns gtapsgpdpt hpdrgrptls
       61 hlrvhrerrt saltrptpvg lgdqklriep sgpagllspr lrlplgsrsr tglravpqrf
      121 seavssatvq pviiaddlsm efrkyhrksg lrgaltnlfs reyetlravd gvsfhipags
      181 ktayiganga gksttikllt gimtpssgrc lvngiepyrd rrtaaqamgv vfgqrsqlww
      241 dlsvadsfki lqriyeipap vfernmkiyr emldidalgg tpvrmlslgq rmraevaasl
      301 lhdpkvifwd eptigldivv kdavralvnr antelgttvl ltshdigdin sicdqvlvvd
      361 kgrvihqgti agllatadrr svlfshsgtq tlqetareva smlpkatptv tddlriridy
      421 padeltsrev lacllerfev tdcyapepdl qsviqeiylr rrv
//
LOCUS       WP_457654864             467 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleobase:cation symporter-2 family protein [Streptomyces
            griseus].
ACCESSION   WP_457654864
VERSION     WP_457654864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..467
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46962
     Region          41..452
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 maqpatgpae gpgitsptta adtavhpvde klpparlvpa alqhiaamya gvvtppliig
       61 qavgldtagm trliaaslli aglatilqti glgpfagnrl pfvnaassag iapmlavaet
      121 sapghqlpai ygavlvagvf clavgpffgr llrffpplvt gvvitligvt lmpvpvawaq
      181 ggdataddfg amkylalaaf tlvvillvqr fgrgflkqva llvgmfvgtl aaipfgladf
      241 salksaplaa lptpfafgap efqpaailsl civmlvlmte ssagmlalge icdrrtdgrt
      301 itrglrtdgi atllgpvfgg fptsafaqnv gvvsltrvrs ryvvaaagga llilgafpvl
      361 gavvslvpmp vlggagivlf gsiavsgirt lseaglddss niilvavalg agiiplaapt
      421 fyagfpawaq tvlgsgisag alvavvlnlf fhhlgthsrt avalkss
//
LOCUS       WP_457654868             414 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter, partial [Streptomyces griseus].
ACCESSION   WP_457654868
VERSION     WP_457654868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..414
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          35..392
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(39..40,43..44,47,83,130..131,133..135,138,161,
                     164..165,168,239,242..243,246..248,251,281,285,335..336,
                     340,344,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 ggggagwppp ppprgggaar gggprppppa alpalcatqi tswgivyyaf pvlnpqitta
       61 tgwptgatta afsaallvsa iagirvgrii drhgprtvmt tgsvlgvtsi liiasapnlp
      121 vftagwllag lamaatfyqp afaaltrwwa pdhvraltiv tlagglasta fapltatlas
      181 hlswrttyvv lalilaavti pahalalkap wpepftptgl hddvgvekvt rtrpfwmlat
      241 tltlsaftvs aavialvplm iergytstea awalglggag qtlgrtlyat larhtspttr
      301 titlvalgal ttaalaitpg pyamlvalsi aagtvrgnlt llqatattdr wgtthygrls
      361 gllaapttta aaiapfagta iaaplggypq lfialaaisa aacitalktt psra
//
LOCUS       WP_457654870             330 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457654870
VERSION     WP_457654870.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006587
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..330
                     /product="DsbA family oxidoreductase"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35381
     Region          35..259
                     /region_name="FrnE"
                     /note="Predicted dithiol-disulfide isomerase, DsbA/YjbH
                     family (virulence, stress resistance) [Posttranslational
                     modification, protein turnover, chaperones]; COG2761"
                     /db_xref="CDD:442047"
ORIGIN      
        1 mtdepertpa aaggatsrpp sarrtapged pppqlevvey tdplcpwawg sepvfrrlra
       61 sltgrvhwrr vyavlfdddd dpppdpvaet awyarhladi gthtlaprah tlsrvaassw
      121 psslaakaae lqgpevadgv lrrlresvfv lgepadtsal alrcvqgvpg ldadrlarda
      181 assgvrqqvr adraearrpv pevlsvraes phpgtaketp dgeiryalpt llfrtpaghr
      241 avpgwrpfea yagavdalap gllrtappld pagaleryrs ltdperlvla egvwpppgav
      301 rvdtgqgplw lypheaqlhp avtpdgsapr
//
LOCUS       WP_457654871             241 aa            linear   BCT 27-JAN-2026
DEFINITION  AlbA family DNA-binding domain-containing protein, partial
            [Streptomyces griseus].
ACCESSION   WP_457654871
VERSION     WP_457654871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Jo,U. and Pommier,Y.
  TITLE     Structural, molecular, and functional insights into Schlafen
            proteins
  JOURNAL   Exp Mol Med 54 (6), 730-738 (2022)
   PUBMED   35768579
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Chen,J. and Kuhn,L.A.
  TITLE     Deciphering the three-domain architecture in schlafens and the
            structures and roles of human schlafen12 and serpinB12 in
            transcriptional regulation
  JOURNAL   J Mol Graph Model 90, 59-76 (2019)
   PUBMED   31026779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>241
                     /product="AlbA family DNA-binding domain-containing
                     protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
     Region          34..141
                     /region_name="COG2865"
                     /note="Predicted transcriptional regulator, contains HTH
                     domain [Transcription]"
                     /db_xref="CDD:442112"
ORIGIN      
        1 marswtrlhe hlgaapgpld fdmvrraaad lleesddldw kehlpqpprd grwnelakdv
       61 aamantrggl lifgvrdktc dltgidpgqa spqqyhqwir nhvqpylpdi tfttltspdg
      121 ttsvlvcdip aspmaphhvy gtaqkdkdqq aavvpyrdkd qtgwmaehqi erayrdrftr
      181 teraeeeaer llgqtretvf tlqtepsawf laiarperpl prtaprltrq easavlhtar
      241 n
//
LOCUS       WP_457654876             493 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces griseus].
ACCESSION   WP_457654876
VERSION     WP_457654876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 11419012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..493
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=54301
     Region          18..>212
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          20..48
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          60..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(101,104..105,108..109,111,141,144..145,148..149,
                     151..152,181,184..185,188..189,192)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          139..169
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          179..398
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          180..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          220..246
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          260..288
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(261,264..265,268..269,271,301,304..305,308..309,
                     311..312,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          293..329
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          340..366
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 miralaldac tklkdtqnka svwnnlggal qelrrfddal haletardly hqtgntngea
       61 sawnnlggtl qelrrfddgl haletardlh rrtgntngea dawnnlglal ieqrrlddal
      121 haletahdly qqtsdtngea sawnnlgttl relrrfddal hahqtardlh qrtgntngea
      181 dawnnlggtl relrrfddav hahqtardlh qqtgdthgea gawnnlgnay rglrhfddal
      241 htnqtargly qqtgdthgqa sawnnlgtvl qdlrrfeeaf qahetardly rqngdthgqa
      301 sawnnlgtsl kelrrfeeal qayetardly rqtgdthgqa vawnnlgnaf qdlrrfedal
      361 hahetardfh eqtgdahgqa vawnnigtay rgldradeaa vageraaaml aatkdwfntg
      421 eawgelattl taagadsarv reaweqsada yaragareea dasrervgst epagvqplaa
      481 adrperdgps esg
//
LOCUS       WP_457654877             218 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457654877
VERSION     WP_457654877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..218
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23086
     Region          25..197
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(74,76,78..79,133..134,155,197)
                     /site_type="active"
                     /db_xref="CDD:293792"
     Site            order(74,76,78,133,155,197)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mtysgavkvg gpasvheltd lmiskvavgg mnnnayllrc ratgeqllid aaaepetlla
       61 ligddgiasv vtthrhgdhw qalaevvgat gartyagrhd aegipvptdv lvedgdtvtv
      121 grveltarhl tghtpgsial vyddphgaph lftgdclfpg gvgnthddpe afasllhdve
      181 tklfdrlpde twvypghghd tplgaerpql pewrargw
//
LOCUS       WP_457654881             816 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Streptomyces griseus].
ACCESSION   WP_457654881
VERSION     WP_457654881.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 816)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..816
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <1..806
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 vlraelsgsp tfgellrrvr rsalagfthd rvpferlide lgierrlgvs plfqtlltvh
       61 tqdeqpsaer dfaglrcada dgghaagkfe vmldlrregd dliavfgyrt dlyddawvtr
      121 farhfetllr galadpdapv selpllarse vdellalgtg aevpaadtea lpavlgraae
      181 tygdrtavrd asgeqsgelt yrglwtaaga lavrlreagv rrgdvvgvll prgtravtam
      241 laawragaay lpldpaypaa rlefmvadtg vrvvvadpde tgngagaevm gdglaervtv
      301 lapggpdgtg vpdahweagp ddpayvihts gstgtpkgvv vphralaara gwmrenygit
      361 addevlqfas lsfdthaeei ypaltagarl vvagsdstlp dhlrlaaagd grgptvldlp
      421 tpywhelvdd ldalprppgl rllilgadqv qqravaawra rfgdtvrvvn sygptettvi
      481 aataelgrad aihrppigsp vggttltvcd algrlmpyga pgellvggag vtygygggpg
      541 atarafvpdp ygppgarryr tgdlvrwrad grleflgrid dqvkvrgfrv epgevetall
      601 aldgvgravv tvrdealvgy vvperdrger peapagggrp egrspeasgs ggqrltagsl
      661 raalaavlpa hlvpnslvvl eslpltpngk vdrralpape qrpdlgpgyv aprtdaeglv
      721 aevwtevlgl drvgalddff dlgghsllat rvvariraaa glsvplralf ahrtveafav
      781 avedlllaei ealsdedaeq llaaesgper ngttta
//
LOCUS       WP_457654883             256 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457654883
VERSION     WP_457654883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 256)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..256
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28068
     Region          10..79
                     /region_name="HTH_MERR"
                     /note="helix_turn_helix, mercury resistance; smart00422"
                     /db_xref="CDD:197716"
     Site            order(11..13,27,44..46)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 matgtdeptl tvdelaarag vtvrtvrfys trgllpppvi gprrvgrygp dhlsrlalie
       61 elqqqgmtla aieryleqlp pdlsahdlai hralvaswap dktedfsrae lerrtgrals
      121 epdverlaam gvlvrpqeag gayrvdlgll rlgvelldvp vahetilaar tvllehtrsa
      181 aqemtrlfrd evwnpyrere gdpehvaamk slsadmqpiv vqalvtafqr slkeelraav
      241 taecrctrpt agpgeg
//
LOCUS       WP_457654885             457 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Streptomyces griseus].
ACCESSION   WP_457654885
VERSION     WP_457654885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>457
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <27..>453
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mkpsrplyer epelaaaaea vdalcgaqav ggllvfsgea gigktallae iqamaadrct
       61 vwsarggetv tsvpfhvvrq llqpaldqfp pdetralfgd wydttapalg laepsgpqpd
      121 pqgvrdgldf vvgrlasrls hrplllivdd ahwadgesla wlasftarlg elpvlvvqah
      181 rpqelaerda nyiadreaer gaggqgrvnr valraltpda tavlvraglg dhaddpfcre
      241 vwavtggnpy eavelvakvq drelppvees agelrelgas argsglvarl erlgtnanrf
      301 awaaavlgtd isqelaatla gmssaeaadc tarlrdariv sgfdplefvh pliatavyrs
      361 ippatrtamh graawaitra glgaaaasrh llevhpdddq elvaqlreaa gqhlavgape
      421 aarrcperal eepprpkdra vllyelgcat llssppt
//
LOCUS       WP_457654889             240 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta, partial [Streptomyces griseus].
ACCESSION   WP_457654889
VERSION     WP_457654889.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..240
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
     Region          <1..237
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 adgnrpydmh qvieelvddg dyleiherwa rniicamarl dgqvvgivan qpqalagvld
       61 ieasekaarf vqmcdafnip iitlldvpgf lpgvdqehgg iirhgaklly aycnatvpri
      121 slilrkaygg ayivmdsqsi gadltyawpt neiavmgaeg aanvifrrqi adaedpeamr
      181 trmvkeykae lmhpyyaaer glvddvidpa etreiliasl amlrtkhadl psrkhgnppq
//
LOCUS       WP_457654891             422 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457654891
VERSION     WP_457654891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 422)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 422)
  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 422)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..422
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44369
     Region          135..417
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkrsvlrrla dasklphtti rtrialvygg vflvlgtall atvnlasrag tetdaraias
       61 saavgppgyv tgppgyvvap pghlvngpvi srssvasptv yeitdhvsda agkqlmnwsf
      121 aallvmtaga vgvgwwiagr vlrpvhamta karrlsertl heriassgpd delkelgetl
      181 dallgrleka fdsqrrfian ashelrtpla tqraaiqvgl ddpspedlvr trqtlldtnr
      241 rserliegll vlarsergla tderesvrld hvvreetarh pavrgpiggp eerradggpa
      301 vkvtvagcsv rgnrlllaql vanllanavt ynvpggsvev slsgegallv rntgpvvsea
      361 diagffepfr rgegrdrmgp gsglglsivr siamahggtv tarpgpeggg lartltlavc
      421 vl
//
LOCUS       WP_457654892             126 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Streptomyces griseus].
ACCESSION   WP_457654892
VERSION     WP_457654892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>126
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          4..>125
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mslrivvcvk yvpdatgdrh faddltldre dvdgllseld eyaveqalqi adeaddaeit
       61 vvtvgpedak dalrkalsmg adkavhvedd dlhgsdvmgt slvlakavek tgydlvicgm
      121 astdgv
//
LOCUS       WP_457654903             357 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457654903
VERSION     WP_457654903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..357
                     /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=37575
     Region          113..352
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpvgiavvdg llvngfgpgp glwvalvaag alvlrrrcpe vpllvglpgm yvgqlafapl
       61 ialycladrr rsvavgavga aavalaqflp ypvtglrela ldretlimam dscvlavgal
      121 vlgrtarvrr erqrelaegr erehrllaek tlsterawla remhdvvahq vslislqaga
      181 lqvgepdaat vrstagvvre lsvktltelq hmvgvlraag vaapglapqp rltdlpalvr
      241 dcglrvtlda pdgtghwsqa aeraayrtvq ealtnvrkha pgaevdirvq pldgglrvdv
      301 rntaadgsta plglpggghg liglrerahl ldgtfdagpe pdggfriqav fpsrqtf
//
LOCUS       WP_457654904             425 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457654904
VERSION     WP_457654904.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..425
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45472
     Region          13..>74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mwhspkaral varhelgali rigreergwr qadlgtrigc sastvsrleq rghhadlrll
       61 rraasevglp tavlaeclgl arptatsvap vgprveedpm rrrtllaaag laapvqllag
      121 mdtalaampd ptgssipldv rlaearcafe sarndhllkv lpglladahd garrtrtdva
      181 hgrlssaysl asqvltkmgr yeqsrltadr asvyaelsgs pltvaaaare lsivlrhqnq
      241 ptaaqrlils avtqveatgl ttdaqasaya qmlcttsyta avagdrqeav tlireasraa
      301 rdlpadppag rlfsvtpasv dqyavsvhwa lgdagaalea gqslraaqfk taerrgrmht
      361 dlarawwqwg kpeqttaell savraspgev rdrpairrmv teihsrhprt tgirelvkaa
      421 glrst
//
LOCUS       WP_457654907             211 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457654907
VERSION     WP_457654907.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  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 211)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13014796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..211
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22367
     Region          61..138
                     /region_name="HATPase_RsbW-like"
                     /note="Histidine kinase-like ATPase domain of RsbW, an
                     anti sigma-B factor and serine-protein kinase involved in
                     regulating sigma-B during stress in Bacilli, and related
                     domains; cd16936"
                     /db_xref="CDD:340413"
     Site            order(62,65,88,90,92,94..95,110..113,125,127,131..132,134)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340413"
     Site            order(100,113)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340413"
ORIGIN      
        1 mcegsvmcre sqeachryvv pfeaapaqls vlrravrsql gcwgasavae eaelaatelg
       61 anvikhvgrd vaaslvlelr ndrvrlevhd rsralpasla evcaendecg rglhliaama
      121 cdwgsvrtat gkavwcelal kpaeceerag caaavlsayr qlsstseldp aaldetvtdv
      181 itdllhwlaa rggdpdgalg raqmhyeaea a
//
LOCUS       WP_457654910             449 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein, partial [Streptomyces griseus].
ACCESSION   WP_457654910
VERSION     WP_457654910.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>449
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          27..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maaqraytth plvlrrvtvr rveevtprmr rvvlggedla aftrdgidhp gfaapgfddh
       61 vklilaadgn iraalpaqlp hgiewtpaeh rvtrdytprr vdlrtgelhl dfvvhgegpa
      121 eawsasareg delwfvgpks slrlperldw illigdetal paigrflder pldatahvlv
      181 tvsddaarqe lalrdgdtvt wvhaepgdaa aleaavralp vpagegyawa aaesrallpv
      241 rrylqrerkl akdrvnitgy whreeatape aegaaetgaa gqgpagipsp lpwlvaraal
      301 qlgvvdavad apglsagtla arlgvpgpgi gvllpllaty gvvtggdegl rlgpageell
      361 edhereeyag heaelllala qfapalrsgt spwrlasgat lhetvtrdae rygelveece
      421 qlvfllnglt adslwadves clltgpgsa
//
LOCUS       WP_457654912            3125 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase/type I polyketide synthase
            [Streptomyces griseus].
ACCESSION   WP_457654912
VERSION     WP_457654912.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 3125)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 3125)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   3  (residues 1 to 3125)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 3125)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 3125)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 3125)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   7  (residues 1 to 3125)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
REFERENCE   8  (residues 1 to 3125)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 3125)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18690202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3125
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..3125
                     /product="non-ribosomal peptide synthetase/type I
                     polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="6.-.-.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=336620
     Region          10..1402
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1283..1684
                     /region_name="KR_2_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 2, complex (x); cd08955"
                     /db_xref="CDD:187658"
     Site            order(1450..1451,1453,1473..1476,1514..1517,1543..1545,
                     1566..1567,1589..1590,1604,1631..1632)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187658"
     Site            order(1567,1591,1604,1608)
                     /site_type="active"
                     /db_xref="CDD:187658"
     Region          1722..1805
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1817..3045
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 madannralr nkvaiigmgc rlpggasdhr tywrnlmagk dcitptppdr ydvrtlgsrf
       61 rdkpgrlvgg rggyidgfde fdpaffgisp readhmdpqq rkllevawea ledggqrpad
      121 laggnvavyv gaftldykil qfadlgftsl aahtatgtmm tmvsnrisyc fdfrgpslsi
      181 dtacssslva vhlacqalnn gesdlalagg tllhmapqyt vaetkggfls pegrsrtfda
      241 aadgyvraeg vglvalkrld davrdgdrih aviagsgvnq dghtngitvp nadaqvdlir
      301 rvcaeagitp gdlqymeahg tstpvgdpie analaralai grapgarayv gsvktnight
      361 esaagiagli ktvlsiqhrt vpphinlenl npaidpatlp yeiptrptaw pahegparag
      421 vnsfgfggtn ahvvleeapp pppktgaapp agrpwsilpl sarnpdalve laagirgela
      481 gdngpavald dlghtlahrr qhlperlsvv ystrasldea ldahgrgeph prvvhgrare
      541 sadrrlvwvf tgmgpqwwgm grqllaeepv frvaveacdr alrefadwsl ieemtadesv
      601 srmsetwlaq panfavqval aalwrshgvr pdavvghstg eiaafhaagv yslrdaariv
      661 vhrsrlqqtl agtgamlavs lsedeaerrv rpyrdrvsva avnsptaitl agdeaaltll
      721 aeelraeqqf akfltvevpy hsvgmerikd ellaelaple prparvplyl tgvegtargg
      781 eldaaywwkn vrdrvrfrsa vdriaadghq lfleigphpv lghairecle aggttgltlp
      841 sirrrenege rfaaslgslh tlgvtvdwdv lqptgrpvtl prhpfrrdrh wteprpvaqv
      901 rrghrdhpll grrtdrtept wqarldtedl pyladhriqd tvvfpaagyl emaaqavlrl
      961 tggttavlad idlrkalflp dgedrtvevs lslenaafti asptgddger avhasgivrt
     1021 gqrrrtappl dapairarsl rhlegpdcyt alaalgyhyg pafqaveevw igagevlari
     1081 rppeaigdda aghhlhpvll dacfqtlltp lipptpegpa pgtgirlpls vdevalepig
     1141 dqpfwahatl lpgdadttlg nialyaddgt plgrvhgfra advekaatav arttidswla
     1201 epawteappl paedtardhd wlvladnggv adafaalaaa rgercrlvrr gaaytasgdg
     1261 vtftvdpasd adlrrlladl draggpfrga vlhlwnldap aladcdraal rdhagagayg
     1321 lialarllla rggggrlhiv trgaqpalpg egpeplgapa wgigrvlrhq elinhpgkli
     1381 dldprrrpgp dgdraeaeal laevlsgdee eialrdggrr tsrlrpaehl trplplrlra
     1441 dgsylvtgaf galgrllcht lvrrgarriv lvgrtpvpar ekwagtdpat aegravallr
     1501 elealgaqpv latlditded altgwldahr qsgappvrgv fhlagqvrdt lvadldraaf
     1561 davhdpktvg ahllhrhlrd eplehfvlfa siasllttag qtnyaagnaf ldalahhrra
     1621 qglpalsldw gpwatgmiee lglvehylhs rgmsslspdt gmavlervig qdhaqlvvat
     1681 vvdwpaflaw yptppplvad laaaaappgd aasgngfldt fraadeetrr alvaerfaal
     1741 satvlrtgtd ridpatglge lgldsllame lrarihaelg valpvvalls gtpagelaaq
     1801 lhdglsalaa adtpdgaaga velhrderqy pltqnqkalw flkhlnpdgy ayniggavev
     1861 nvalepdlmf davrrliarh palrtnfllv dgqavqrvse daatdlalfd vqgedwdsih
     1921 ativqeyrkp ydlahdplvr frlfkrgpdr wiimkavhhi vsdaistftf ieellavyea
     1981 lrrnqepqlp pvearyldfl nqqnaflagp eaagmldhwr ahlpaevpll dlpvdkprpa
     2041 vqthngasef fvlddalsar vhalarahgv tpfmvllsay ylllhrysgq dhivvgspvt
     2101 grtrqdfasv ygyfvnplpl hadlsddptv aellqqvrrt vlggldnqey pfvllveelg
     2161 lqhdpsrsav fqamfillth kvateqygyr leyielpeee gqfditlsay edeaegrfhc
     2221 vfkyntdlfl petmrrmaah ytrlldrmth apgeqpasrl emlgdqerar ligqwsrpal
     2281 patgsreepf aavqtliart aaehpaavav ttpsphggah rltyaelerr aadsaarlrt
     2341 lgigegsvvv lcldkspeli vallavlkag aaylplrpdq padrlahlvt atgaalvlva
     2401 ddagpeqtga lavptltlga lartaphpdg psdeagpesp ayiittsgst grpkavrvsh
     2461 rnlasahaaw rqeyrletdv rvhlqmaeps fdvftgdlvr alcsggtlvl adrdllfdtt
     2521 rlyrtmrqer vdcaefvpav vrglmdhcar eglrldflkl lvvgsdawsv geyrrlaelc
     2581 gpgtrlvnsy glteatidsa sfegpvddle pgamvpigrp lpnsalhvld ahgepvppgv
     2641 pgelwiggdg valgyagdpe qtearfvtrt lsrsadgdar perlyrtgdi arwdahgrvh
     2701 llgrtdgqvk lrghrieige ieahlaqwpp laravvtvra dtggeaalca ycvpapgatl
     2761 dgralrrhla rslpsymips hfvelpalpl tangkvdtaa lpapraetgd rpyeepvtly
     2821 eisvarhwkt llgreqvgle ddffelggss ikliellhql rtefgvgvpv srlyqvttlh
     2881 gmaatvedvl hgtsadelps ltfnagqhpa lfcfppaggh glvyrglaah lpdhtligfn
     2941 ylpgddkvar yadlieaarp dgpyrllgys lggnlafeta kelerrgrsv ahvvildsrr
     3001 iltayepdas giavfeaela dhlrkhtgse avtretlaha aeylafcgrt pntgtvaatv
     3061 svitdeekaa lyaagehgtw hgsstgatav lrgsgvhadm ldakhlprna elvrsvltgd
     3121 pahgg
//
LOCUS       WP_457654914             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457654914
VERSION     WP_457654914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31491
     Region          30..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 meidrpglaa flrrrrellq pedvglprgq rrrtgglrre evavlchmst dyyarlerer
       61 gpqpseqmia siaqglhlsl derdhlfrls ghmppargtt gehispgllr ildrlddtpa
      121 eivtelgetl rltplgvalt gattrytgla rsigyrwftd patrtlyvae dhaflsrmfa
      181 sglrelatlr gtgsraahca ellreesqef rrlwdqheig irpdqvkrfv hpevgvleln
      241 cqrlldpdqs hsllvytaap ggesherlrl lsvigtqtlr
//
LOCUS       WP_457654915             276 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase, partial [Streptomyces griseus].
ACCESSION   WP_457654915
VERSION     WP_457654915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>276
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          28..223
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mnepipvire vdcgtarllp dvdrdrawll tvddapqsyv dlddpsylef eyvrrlahvv
       61 dgaaepgapl dvlhlgggal tlpryvavtr pgsrqdvvea drallrlvre hlplpdgsgv
      121 slhaadarqr leatapasvd lliadvfggs rvpahltsve yaraagralr edgvyaanla
      181 dsapfaflrs qlanfaavfp elaligepav lrgrrfgnvv llashapidv dplvrgcaad
      241 afparvthga altrflggar pvadadavas peppdg
//
LOCUS       WP_457654919             310 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease, partial [Streptomyces
            griseus].
ACCESSION   WP_457654919
VERSION     WP_457654919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..310
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          44..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 gdgsraarpp rrgrsvspkg hsgwtpwlyl lpalvllagl lvypiyqlgl isfleytqaq
       61 vsggepttfq gfgnyatlfn dsqfwqvlla tvlfaaacvv stlvvgcala vlltriralp
      121 rlalmmaalg awatpaitgs tvwvflfdpd fgpvnkvlgl gdfswtygry safalvllev
      181 lwcsfpfvmv tvyagiraip tevleaasld gasqwriwrt imapmlkpil ivvtiqsiiw
      241 dfkvftqiyv mtngggiagq nlvlnvyayq kafassqysl gsaigvvmlv illavtlvyl
      301 rlvrrqgeel
//
LOCUS       WP_457654922             540 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase, partial [Streptomyces griseus].
ACCESSION   WP_457654922
VERSION     WP_457654922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>540
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          81..440
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtsserserq drtprsrpar grgrgqgagt qaasngrgga prsrnqggsk paarrkpaaa
       61 qpaefalpet vtpalpsvea fadldmpaal lktlaaqgvt epfpiqgatl pnslagrdil
      121 grgrtgsgkt lafglallar tagrrsepra plamvlvptr elaqqvtdal tpyatavnlr
      181 matvvggmsi tkqsatlrrg aevlvatpgr lkdliergdc rldqvsitvl deadqmadmg
      241 fmpqvvallk qveadgqrml fsatldknid rlvkmfltdp vvhsvdpsag avttmehhvl
      301 hvldetdkka vatkiaardg rvimfvdtkr aadrfakrll asgvraaalh ggrsqpqrnr
      361 tldqfktgev talvatnvaa rgihvddldl vvnvdpptdh kdylhrggrt aragesgsvv
      421 tlvlpeekre mtrlmqdagi aprttrvtss daelgritga repsgvaivi evpqptppkq
      481 rarsggsags gsgggavrsg srgrgrrgag gaggagggag rsggagrsgg eargagrsga
//
LOCUS       WP_457654926             423 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457654926
VERSION     WP_457654926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..423
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
     Region          16..421
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 aqgrwaaaap adrarllrrf avvvdehiee laqlevreag htignarwea gnvrdlldys
       61 aggaerllgr qipvaggidf tvleplgvig viapwnfpmp iaawglapal aagnavllkp
      121 aettpltalr laelaleagl pdglfqvlpg egpvagsalv ehpgvakivf tgstrtgkhi
      181 mtrcaervkr ltlelggksp nlvfadadva aaaaaapmsf ldnagqdcca rtrilversv
      241 ydrflellvp avaavvvgdp adektqmgpl isalqlervr gfvdgdrgad gvrtllgtap
      301 egpgfwyppt vltgvspdap vaveevfgpv avvlpfedeq dalrlanate yglagsvwtr
      361 dvgralrvgq glragnlsvn shssvrystp fggykqsglg relgpdalaa ftetknvfis
      421 tea
//
LOCUS       WP_457654928             388 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Streptomyces griseus].
ACCESSION   WP_457654928
VERSION     WP_457654928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12206295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..>388
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          280..>383
                     /region_name="AAA"
                     /note="ATPases associated with a variety of cellular
                     activities; smart00382"
                     /db_xref="CDD:214640"
     Site            order(290..292,311,313..314,376..377)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410865"
ORIGIN      
        1 pydwtpvrdr vaqaaerasa alwrrrdglp pawaswcarm agaagwglav agrhgaavvg
       61 smggalrqwe rwplvaraal rlwalavvlv lavdapagtl walvgdaalp ailvgavvav
      121 vvavagpagl rwwaprritd aealvpglwq gvapvlgldt egdeerqpev akdwivfppa
      181 lrddlaeivi llpitwqatt aqtnmlehav atripgewvp kyqlfgdthw vafthkpkpv
      241 kraplptyvk wipsgdpyrt hygqthdgpa yvltsdktph igvsgetgag kstianialv
      301 sarlagwlvt iidpkqnslp eaqdrdgiry htdtydcvma iaeyftsmma aekynrrkyh
      361 gyegadrptp rlliidelps frdfvaaw
//
LOCUS       WP_457654938             181 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457654938
VERSION     WP_457654938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>181
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          25..73
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(27,31,56)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mpkrthkwke lpsslpfahr afvlrlrelr evsdrtqaei aqdvylaats lsnhlnggri
       61 peaehvekly kilrdeaata srempcslpl llelrvkalv khcdccpags seavaaapep
      121 qpmtavspap khlrrrprrp rirlstrhrg iprtpaqaev pgprrkggrp httpagcara
      181 e
//
LOCUS       WP_457654940             345 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457654940
VERSION     WP_457654940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  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   2  (residues 1 to 345)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..345
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36814
     Region          10..345
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 maaarvrsgg rptleevaar agvgrgtasr vingsprvsd atreaveaav aelgyvpnra
       61 aralagnrtd aialvvpepe trffaepyfs aivrgvgaal adtemqlllt lvgndrerrr
      121 laqyltahrv dgvllvavha ddplpelleq lgmpcvisga rhaaetlpsv dsdnfegara
      181 avdhlvargr rqvatitgrl evygaqrrld gyraalsaag lapderliap adfteeggar
      241 amrdllarrp dldavfvasd vmaagarqvl readrriped valvgfddsv varhmhpplt
      301 svrqpieemg rrmaqlllde iagrapgder psvvlptelv vrdss
//
LOCUS       WP_457654943             447 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein, partial [Streptomyces griseus].
ACCESSION   WP_457654943
VERSION     WP_457654943.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>447
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          27..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maaqraytth plvlrrvtvr rveevtprmr rvvlggedla aftrdgidhp gfaapgfddh
       61 vklilaadgn iraalpaqlp hgiewtpaeh rvtrdytprr vdlrtgelhl dfvvhgegpa
      121 eawsasareg delwfvgpks slrlperldw illigdetal paigrflder pldatahvlv
      181 tvsddaarqe lalrdgdtvt wvhaepgdaa aleaavralp vpagegyawa aaesrallpv
      241 rrylqrerkl akdrvnitgy whreeatape aegaaetgaa gqgpagipsp lpwlvaraal
      301 qlgvvdavad apglsagtla arlgvpgpgi gvllpllaty gvvtggdegl rlgpageell
      361 edhereeyag heaelllala qfapalrsgt spwrlasgat lhetvtrdae rygelveece
      421 qlvfllnglt adslwadves clltgpg
//
LOCUS       WP_457654948             407 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces griseus].
ACCESSION   WP_457654948
VERSION     WP_457654948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 407)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=41198
     Region          6..406
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mkrpaiavtg lgmitpvght tdttwdgvca gespartvpe lhgcavdfac tvsgidldda
       61 vggrtafrmg ryvkfavlaa reavadagld pehwdgtrva vvvgtssggs aglteqaval
      121 errgpeatsp sgilltipnm paaeiairmk atgpslapct acssgvtals vardmltlgh
      181 cdiaiagate sivfpvamtg farsgaaapr dgdparlcrp faadragivm gegaavmvle
      241 raedararga spraliagag attdahhpts phpsgdvara avdgalrdag wrpedvdhvn
      301 ahgtstplnd ateaaligra yphrppvtap kgvlghcmga agaieaglti ltlqhgmipp
      361 ianldapepg fdidcvtkap revpvrravs hsfgfggqna vialqas
//
LOCUS       WP_457654950             246 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457654950
VERSION     WP_457654950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..246
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27149
     Region          10..79
                     /region_name="HTH_MERR"
                     /note="helix_turn_helix, mercury resistance; smart00422"
                     /db_xref="CDD:197716"
     Site            order(11..13,27,44..46)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 matgtdeptl tvdelaarag vtvrtvrfys trgllpppvi gprrvgrygp dhlsrlalie
       61 elqqqgmtla aieryleqlp pdlsahdlai hralvaswap dktedfsrae lerrtgrals
      121 epdverlaam gvlvrpqeag gayrvdlgll rlgvelldvp vahetilaar tvllehtrsa
      181 aqemtrlfrd evwnpyrere gdpehvaamk slsadmqpiv vqalvtafqr slkeelraav
      241 nppfrg
//
LOCUS       WP_457654951             565 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457654951
VERSION     WP_457654951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 565)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 565)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 565)
  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 565)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>565
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          16..560
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mktpdttrpr pgaailrtal rrnvgamiag tvlmglyqaa etafpialgl ivehtmqdrs
       61 lgslgvsigs laviittvsl swrfgmrvlq kantteahrw rvqvaacglq pvardvdlks
      121 geiltiated adqtadiiev vpllisslva vvvaavalgl adlrlgllvi vgtvailsvl
      181 avmskrigas tqeqqarvar agakvadlii glrplhgfgg nhaafgayrk vstdakrqai
      241 tvarvngtya gtalalnavl aaavsltagw lafegrisig elvmavglaq fimeplkmfs
      301 empkyvmmar asaermalvl nappvtapgp erpepggdle vdgvrhgtlq gvtfsvrage
      361 fvaiaayqpr aaaelasvla mnvapqaygg avrvggrevg elsieavray llvnpydgei
      421 fagtlrtnid psgsgrsiae aveasmltdv valhregldh vvrdrganls ggqrqrlsla
      481 ralaadteml vlhdpttavd avteqliarn iaklrrgrtt lvmtsspall daadrvlvld
      541 ggaitaedth rnllasdeay clava
//
LOCUS       WP_457654959             450 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase, partial [Streptomyces griseus].
ACCESSION   WP_457654959
VERSION     WP_457654959.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..450
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          25..441
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 artssegrav artqtllkgs ngigtvrrtv lpgglrivte tlpsvrsatf giwanvgsrd
       61 etptlngath ylehllfkgt akrtaldisa aidavggemn aftakeytcy yarvldtdlp
      121 laidvvcdml tgsliapedv daergvilee iamteddpgd cvhdlfahtm lgdtplgrpv
      181 lgtvdtinal nrgqiarfyk khydpthlvv aaagnvdhat vvrqvrkafe kagalsrtda
      241 apmapregsr tlrtagkvel lnrkteqahv vlgmpglart ddrrwalgvl ntalgggmss
      301 rlfqevrekr glaysvysyt sgfadcglfg vyagcrpsqv hdvlkicrde ldrvaahgld
      361 ddevaraigq lsgstvlgle dtgalmnrig kselcwgeqm svddmlaria evtpddvrev
      421 agellthrps lsvigplkdk qadrldeavs
//
LOCUS       WP_457654962             423 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457654962
VERSION     WP_457654962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..423
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
     Region          16..421
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 algrwaaaap adrarllrrf avvvdehiee laqlevreag htignarwea gnvrdlldys
       61 aggaerllgr qipvaggidf tvleplgvig viapwnfpmp iaawglapal aagnavllkp
      121 aettpltalr laelaleagl pdglfqvlpg egpvagsalv ehpgvakivf tgstrtgkhi
      181 mtrcaervkr ltlelggksp nlvfadadva aaaaaapmsf ldnagqdcca rtrilversv
      241 ydrflellvp avaavvvgdp adektqmgpl isalqlervr gfvdgdrgad gvrtllgtap
      301 egpgfwyppt vltgvspdap vaveevfgpv avvlpfedeq dalrlanate yglagsvwtr
      361 dvgralrvgq glragnlsvn shssvrystp fggykqsglg relgpdalaa ftetknvfis
      421 tea
//
LOCUS       WP_457654947             514 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457654947
VERSION     WP_457654947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..514
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52586
     Region          28..470
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide)-like multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17504"
                     /db_xref="CDD:341047"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,152,
                     155..156,159,283,286..287,290..292,295,329,333,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341047"
ORIGIN      
        1 mrrtqrirha eelpeprkar sgpivpvlaf agitvavmqt llvpvikdlp vllstdpana
       61 twvttatlla gavstpimgr lgdlygkrrm llaslavmvi gslicastdd lvvmitgral
      121 qgfamgaipl gigimrdelp reklgsamal msssigvggg lalpaaalva qhadwhalfl
      181 gsaglgvlam altytlvpep plrapgtfdv vgalglslgl vllllpvtkg gdwgwtsapt
      241 lgllaasvat lllwgrfelr tpaplvdlrt tarrevlltn lasimvgvaf yavslvlpql
      301 lqlptatgyg lgqsmvvagl cvaplgvtmm fvaplyaris arrgpkttlm lgmliiavgy
      361 gaglgllsaa wqtvliavvl gagiglayss lpaliigavd psetgaangl ntlmrsigts
      421 vssavigmvl antsvtmgsa qvpsmegfri sfliatgavl iglvlaaflp aqrpsahpvl
      481 lassaedaqa aedaraaeda qsvvsaperr taap
//
LOCUS       WP_457654967             271 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457654967
VERSION     WP_457654967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..271
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28472
     Region          4..264
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mtfpyklvat dldgtllred dtvsertraa laaataagaa hiivtgravp wtrhilddlg
       61 yeglavcgqg aqvyhagerk lltsltldrq laglalskie aevgplhlaa srdglegevl
      121 vgpgyrvqeg plpylfvdda semwtaplnk vyiqhpeldd dalvfaarsa vgslvdvvma
      181 gagvveilpl glskatglsl aarrlgvkaa dtiafgdmpn dipmfgwahh gvamanahed
      241 lkavaheita sneddgiavv leellrtaav r
//
LOCUS       WP_457654968             153 aa            linear   BCT 27-JAN-2026
DEFINITION  copper chaperone PCu(A)C [Streptomyces griseus].
ACCESSION   WP_457654968
VERSION     WP_457654968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fisher,O.S., Sendzik,M.R., Ross,M.O., Lawton,T.J., Hoffman,B.M. and
            Rosenzweig,A.C.
  TITLE     PCuAC domains from methane-oxidizing bacteria use a histidine brace
            to bind copper
  JOURNAL   J Biol Chem 294 (44), 16351-16363 (2019)
   PUBMED   31527086
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Abriata,L.A., Banci,L., Bertini,I., Ciofi-Baffoni,S., Gkazonis,P.,
            Spyroulias,G.A., Vila,A.J. and Wang,S.
  TITLE     Mechanism of Cu(A) assembly
  JOURNAL   Nat Chem Biol 4 (10), 599-601 (2008)
   PUBMED   18758441
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Banci,L., Bertini,I., Ciofi-Baffoni,S., Katsari,E., Katsaros,N.,
            Kubicek,K. and Mangani,S.
  TITLE     A copper(I) protein possibly involved in the assembly of CuA center
            of bacterial cytochrome c oxidase
  JOURNAL   Proc Natl Acad Sci U S A 102 (11), 3994-3999 (2005)
   PUBMED   15753304
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..153
                     /product="copper chaperone PCu(A)C"
                     /GO_function="GO:0016531 - copper chaperone activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16212
     Region          3..145
                     /region_name="COG2847"
                     /note="Copper(I)-binding protein [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:442095"
ORIGIN      
        1 mnrrrtalag ilalttglal agcssdggsg ggpelkvtda fmpqpvsdma agflvvqnsg
       61 gtgdrltsvt splsddvtih etknqkmrev ssfevpange ldlerggnhi mfmklkqkpk
      121 qgekvsvelh fekadpitvd lpvketthnp kkq
//
LOCUS       WP_457654969             495 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457654969
VERSION     WP_457654969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..495
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51828
     Region          44..495
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mldigllvrv hvdalivaqn hmgvcdairr iapvgklaam saphlpkvag idpedpvsth
       61 tpapltevpg ppgafiqdrl agwvsdlttl helterlagt stlddalnel lragaalvga
      121 rrgllvlepa hgegpsatlg lglshaelgh ietvprpata lgrvldgapg tadgaaspdl
      181 lgeqdldprh revavrlgya asyalplsse aagrlgaavw lydepaepaq kqrhlaglya
      241 ryatehlarl ieleraradv aavaeellps rlprisgvql aarhrtgprg ggdwydalpl
      301 pdrtlglavg svggsgpsam aamgrlrasl rayavmeged pvavlsdlel llrltepart
      361 atalfaycep aarkvvlaga ghtpplvlge rrcefvettl saplgmlacw eapsvefspa
      421 pgetvllytd gllrrtgdpm drafarlhsa aasvpkagrh dpaavadhvl rtmlpdgldr
      481 tdsaedvvil aahfd
//
LOCUS       WP_457654971             568 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457654971
VERSION     WP_457654971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..568
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55344
     Region          284..566
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mstenegned havpavpsvp sappvpadtp epatggatpp aapapapaqd athgtapeta
       61 pgpadpvqdt arlpvhetga pettphapga pahaeaprhn pthqgapatp aygqaaqpsp
      121 ppqppqhspy gapselpaga aswpppppav psyaggntgh asdhasggig ngsghgpvwg
      181 apvppgtdpa ggkngksrag glvaavavaa lvaggiggal gywaadrndn gssgnsttis
      241 asdtprdlkr pagtvagvaa kalpsvvtid aqggdgeggt gtgfvydkeg hiltnnhvva
      301 saaesgelsa tfsdgkkyaa evvgraqgyd vavlklknpp agltplplgn sesvavgdst
      361 iaigapfgls ntvttgiisa knrpvasgdg qsnknsymsa lqtdasinpg nsggplldat
      421 gaviginsai qstggglgqs qagsiglgfa ipinqaknva eqliktgkpv ypvigatvtm
      481 eektggaais aegaggtpav tpdgpaakag lkagdvitkf ndtvidsgpt ligeiwtrkp
      541 gekvtltyer dgktataevt lgqregds
//
LOCUS       WP_457654973             467 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces griseus].
ACCESSION   WP_457654973
VERSION     WP_457654973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..467
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=51434
     Region          156..436
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mltfdvviws irqrkgrpkp welrwrvgae ghsksftlkp qadgrrsqlm aalragqqfd
       61 eetglpekel aalamptwfe hakayalmkw pgaaakhras iaeslavvtp vfttgpsaqp
      121 darvlraaly qwafravdgp kdqlvsrsda qeppgdvrka lewigqhsmr vdeaakpehv
      181 raaltalsrl lngkpaaent anrkrmvlsn afryaveera lltrhpflsv dwdapqtsde
      241 vdfrwvpgpr larallaava aqgdrgeqle afygavyyva trpgeaaalk esdfilppes
      301 epeawgevlv seshpevggg wtdsgkshde rglkhrarka vravpvppiy vrmvrahiar
      361 fgvapdgrlf ravrggrlts neysevwsea rkavlseqel rtalaevpys lrhaaislwi
      421 ksgmdpveaa craghslavl yrfyakllkg gsaaanrlve aglrael
//
LOCUS       WP_457654982             214 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457654982
VERSION     WP_457654982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..214
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22570
     Region          35..180
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(65,108)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(70,73..74,78,82,104,106..109)
                     /site_type="active"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mstlltalaa agplaagwsv htvwlrrslr sarrdpltgl rtrdgftrra nvllkdprav
       61 vvladvdhfk qindqyghaa gdallkvtad rlahyvgrdg vagrlggdef aalvidthgt
      121 igdllavlhg vlarpadgmn pavrttvslg wvraadhpge dlsgllrrad eamyaakqar
      181 agvrraglgr llatwsgrra grrgtalagp rdaa
//
LOCUS       WP_457654985             252 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457654985
VERSION     WP_457654985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..252
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28143
     Region          4..77
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtnerlrsal laqgmtvrdl aeaidvnakt verwitqgkv pyrkhqyata svlavdvttl
       61 wddgravdsa tdlskaeivt vyphrhmvpn glwrelyara rthldvlvys glwlsedplf
      121 hgllkakves naqvrimlgd pgcdavrqrg ideghrimdg kirnalvnyq plftshpdig
      181 frlhdatlyn slfrsddeml vnthvygmga ymapvlhlrr lpggglfdty arsieqtwgs
      241 arpvtdddmv ga
//
LOCUS       WP_457654986             190 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457654986
VERSION     WP_457654986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..190
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20976
     Region          25..127
                     /region_name="HD"
                     /note="HD domain; pfam01966"
                     /db_xref="CDD:460398"
ORIGIN      
        1 mtttgltkwa yllaeellae plprrwahcq gvaerarsla pilgddtell eatavlhdig
       61 yapdlaktgf hpldgarylr dvahaderiv clvahhscaw meaeargmrd eleaefpreh
      121 ldladalcyc dmnttpdgts tnpvdrvdei agrygpdsli gtfirraepe ilactarvvl
      181 rlaevkrqpm
//
LOCUS       WP_457654990             251 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457654990
VERSION     WP_457654990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27255
     Region          1..248
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mseqppylri adelrqriae hvwepgdrlp sraqigqecg vgenvvrraq ellisqgvle
       61 gragsgtyva eprqrvrvvr ssareqpsgs pfrqdmkalr lqsdwesrtd akvpapaeia
      121 trlgiaegel cvrttyefla ngkpvqlsts wepyavtggt lvvlpeggph agagvvnrma
      181 aigvtishav eqpeprhata eeasllgiqk aalvthirrt yysddgrpve tadivvpaah
      241 ceivyeipin r
//
LOCUS       WP_457654992             247 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457654992
VERSION     WP_457654992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..247
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26451
     Region          8..237
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtrsvprrhh diaddlrhqi ttgsikpger lpseaglaar yrvstvtlrr alavlqgegl
       61 vekihgkgny vrhprrkimy vggwgtldpw taaeptlrit irsttvpasv hlttllkvpt
      121 gsplaeytcl sleqgspqgl ariyipldla pagvldndsv creaatrfav lgpspatire
      181 tvsarsptpd easalrignn mavlaitria tdatgrvvea allafpgdrv davftahhvl
      241 nerptqg
//
LOCUS       WP_457654998             154 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces griseus].
ACCESSION   WP_457654998
VERSION     WP_457654998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 154)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..154
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16531
     Region          19..121
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mllymsqpqe atpaplhsvs vagvvvredg rllairradn gtwelpggil elnetpeagv
       61 arevweetgi hvevdqltgv yknttrgiva lvfrckpsgg tertssesta vswltpdevs
      121 ermaevyavr lldaldgngp hvrshdgkql itag
//
LOCUS       WP_457655002             375 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces griseus].
ACCESSION   WP_457655002
VERSION     WP_457655002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..375
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41116
     Region          70..362
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maakrksrra fgrirklpsg rfqarypgpd gvlraadqtf atttdadrwl arkriemeeg
       61 rwldpaegrt tvrdwsarwl tavspqlkhk tqasyrslin slivpalgdr elsslrpiti
      121 vewvgamktr glsasrirqa yrvlsqimra avdnemigqs pcrgvklprm pqtephiltp
      181 leasrivrsa tnphdllisl layaglrvge afalrradid vsgglvlvde nlaeangtlv
      241 fdspkshqkr vlrigpslaa rigrhletlp ggedallfvt pggkplrynq wrkayfdpav
      301 avagltdvtp hdlrashgtw vadrygvmta ahrlghsnas vttrhyarpv agrddqvata
      361 advwlsggdg tdhan
//
LOCUS       WP_457655013             388 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655013
VERSION     WP_457655013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40556
     Region          6..380
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mttsttlhel ldthiaagsm pgavalvarg ervevvsagt aglagsapmr rdsifriasi
       61 tkpvvaaaam tlvedgliap adpvaawlpe lasplvvrtp espvddvvsa vrpitlldll
      121 tfragygfps dfslpavapl faelrqgppe pqaglapdaw maelsrvpll hqpgdgwlyn
      181 tcsdilgvli arvadrplpa ylaerifepl gmkdtgfwve paaldrftss yrpgadggsd
      241 pvlddapdgq wssppafpsg agglvstvdd wyafgrmlla eglndagdrv lagesvrqmi
      301 tdhltpeqra asglftegqg wgfggavdve iaapwnvlgr ygwvggagtt ahivpatgtv
      361 avlltqmams gpttpqvmrd fwtyaagf
//
LOCUS       WP_457655014             296 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655014
VERSION     WP_457655014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31852
     Region          47..287
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mslrrrsarf prlllaasll sallappaaa asahrsspsg gsgaglplrv atynihagag
       61 ldgvfdldrq taelrsldad viglqevdrh wgarsewrdl agelarrlrm hvsfapiysl
      121 dpaepgapra eygvavlsrh rivsaenhei trlstqdpnp vpapapgfge vvvrvrglpv
      181 hvyvthldyr pdpavrvaqv adtrrimaed rgprillgdf naepaapela plwreltdad
      241 pgaptfpaqd pvkridfvav skggvgvrra wvpesvasdh ravvadllvr grardr
//
LOCUS       WP_457655018             335 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces griseus].
ACCESSION   WP_457655018
VERSION     WP_457655018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..335
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36266
     Region          19..292
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msdgaegigv drgghpgwda trswvekngl seaerieqvv plrggwtsem rrldlggpgg
       61 arslvlrsfv kpfyvrhaeg llnreadilr llgdtgvpaa tlvavdaaae hcdhpsllms
      121 llpgalrldd hgaddradll arqlvrihrl pvaahqrprt yqawasperv vlppatarpe
      181 lwrravdvir reapayegcf lhrdfhpgnv lfsgtgdgdr dgggdglris gvvdwvetsw
      241 gpadldvahc stalallhgv pagmrfadry vaaggtlagd psdhlywrll dalgfapdge
      301 kvavpwrevg rvdltadvla qrlegyvqal ferya
//
LOCUS       WP_457655020             220 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457655020
VERSION     WP_457655020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..220
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24569
     Region          2..212
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 miravvfdvg eclvdetrey gtwadwlgvp rhtfaaqfga viaqgkdyre tfqvfrpgfd
       61 lhaerqaraa agqpehfdes dlypdvrdsl kalradglwl giagnqttra ggilrglfaq
      121 dvdligtsdd wgaskpdpef fvrvaevvpa epeeilyvgd rvdndlrpav aagmrtalvh
      181 rgpwatiqwe teearrlptf rmesllelsp liaqfnerer
//
LOCUS       WP_457655025             447 aa            linear   BCT 27-JAN-2026
DEFINITION  COG1470 family protein [Streptomyces griseus].
ACCESSION   WP_457655025
VERSION     WP_457655025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11444751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..447
                     /product="COG1470 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45522
     Region          1..>187
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 msltasldas svtvapgeet tlplqilnsg rtveeyrfev vgacaawsav epavlslypg
       61 dsgtvslvlr pprdatvpag ettfgirvkp tgdqgdtvvp egrvtvlpft ettaelvprs
      121 sngsrsgrhq favdnrgntp vtvrlgaqpg terarvvfav selriepgha efaklrvrpa
      181 krmwrgtpvt hafqvfaapq vpegaepppp vlvdgsyqqe pilprwlpra lltaallllv
      241 lvglwyallr pavksaarea vtpeavrsaa aadkskapee ggqggagsgg gdssgagtgg
      301 gsagptpspg asapggtggg daasgaptsa qtrvqdavgg gpntgtalev paghtfqltd
      361 ivvqnpqgda gtvtvtaged trvlslglen frdsdyhfvt pilvpaggkv tmtidcrrvg
      421 kpvgapapar cstsmflggt mrpdsag
//
LOCUS       WP_457655034             763 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457655034
VERSION     WP_457655034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..763
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=79148
     Region          27..735
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mpssparpdr aaaprrrgal rrtgewcarn fvtvlvlwva alaglqvlqh ayggdysddf
       61 slpgtqsqeg ldvlkahapq aggysaqvvl hdadkpltsv sdqvatavsd lqklpdvlsa
      121 qnplpssgst pppppdpntg plstdqktay itvrfsvqps tldpsyldgv ddavrplrsa
      181 gveveyggpl gelarpepsd rtseaigfgv aivvlligfg sllaavlplv talicalcgl
      241 allgllaaaa tfatvsptla tmigigvgid yalflvtrhr qnlvdgqdpv taagnaaats
      301 ghavllsgct viialsglwv sgigfigklg laaavtvvta vlgaltlvpa ilgligrrid
      361 rvrvrkpvae tvpapegaep ggwhryaqrv errpwwflag gvvllavlsf pvlfiqlghi
      421 gdgadpksft drrafdlmst afgpgsngpl tlvidqskvp ssdrsaladq aqkaltnvpd
      481 aavitpltat sdgdvltata ysvaapqder ttsltnrltd dvlpqavsgy dagtyvtgtt
      541 aaqvdfldiv ssrlpliiav vvglaflvil avfrgllval kaavlnvlsi aasygvvvav
      601 fqwgwggpal gvsgkvpies yvpmmmfaiv fglsmdyeif llsriheawv rtgdarasva
      661 haleitarvi tcaalimvsv faafvisdni vvkmlglgla asvlidatvv rlllvpavmt
      721 llgraawwip gpldrilphl daeggaegga etraepagpv gkk
//
LOCUS       WP_457655035             408 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Streptomyces griseus].
ACCESSION   WP_457655035
VERSION     WP_457655035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..408
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42365
     Region          7..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mehpgtlvli malavlapll gyatgrwlpv pvvifeivlg vlvgpdvlgw ahhdqvidal
       61 sdfglsmlif lagyeikfae vrgdtlrrag gawvlsfaag lgvalllsga dlakslvigt
      121 altstalgav lpilrdsgrl egrfgsvvla fgsvgefgpi iamallfsgr spgaasavla
      181 vfavvtagav fwamrprppw farivavtlh ssgqfavrfv mlllagmlgl ahvfgldtll
      241 gafaaglltr lvlqgsvpes gdailervea igfgflvpff yvvtgidfdl aallddgrpl
      301 lllpvflllf llvrgvpayl laprdltgra praalglfas tclplvvait aigldekvig
      361 sgeaaalvaa amvsvlvfpl lafrllrree dgggrsvpgr aaesgeaw
//
LOCUS       WP_457655036             256 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan recognition protein family protein [Streptomyces
            griseus].
ACCESSION   WP_457655036
VERSION     WP_457655036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Dziarski,R. and Gupta,D.
  TITLE     The peptidoglycan recognition proteins (PGRPs)
  JOURNAL   Genome Biol 7 (8), 232 (2006)
   PUBMED   16930467
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Guan,R., Roychowdhury,A., Ember,B., Kumar,S., Boons,G.J. and
            Mariuzza,R.A.
  TITLE     Structural basis for peptidoglycan binding by peptidoglycan
            recognition proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17168-17173 (2004)
   PUBMED   15572450
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Steiner,H.
  TITLE     Peptidoglycan recognition proteins: on and off switches for innate
            immunity
  JOURNAL   Immunol Rev 198, 83-96 (2004)
   PUBMED   15199956
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Dziarski,R.
  TITLE     Peptidoglycan recognition proteins (PGRPs)
  JOURNAL   Mol Immunol 40 (12), 877-886 (2004)
   PUBMED   14698226
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11274790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..256
                     /product="peptidoglycan recognition protein family
                     protein"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0016019 - peptidoglycan immune receptor
                     activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045087 - innate immune response [Evidence
                     IEA]"
                     /calculated_mol_wt=27589
     Region          46..180
                     /region_name="PGRP"
                     /note="Animal peptidoglycan recognition proteins
                     homologous to Bacteriophage T3 lysozyme; smart00701"
                     /db_xref="CDD:128941"
     Site            order(77,112,212,218,220)
                     /site_type="active"
                     /note="amidase catalytic site [active]"
                     /db_xref="CDD:133475"
     Site            order(77,212,220)
                     /site_type="other"
                     /note="Zn binding residues [ion binding]"
                     /db_xref="CDD:133475"
     Site            order(78..79,108,112,126,137..138,143,212,215,218..220)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133475"
ORIGIN      
        1 mwsrrlvlgv lvlplallvf gdgrafhapg aelatgprpa rglpqpavvs rrdwgadesl
       61 vregphytap aravfvhhtg npndydcada peliravqrd hirqdgwddi gynflvdrcg
      121 tiyegraggv grsvlgahtk gfntdtvgia aignfgpgve vpkpmmdalv rlaawklrpg
      181 adplgsvdlv stndesrfdr gqvarlhvis ghrdsfetrc pgdalydllp elreraaklr
      241 atvpghaata rlrpsf
//
LOCUS       WP_457655038             131 aa            linear   BCT 27-JAN-2026
DEFINITION  TOBE domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655038
VERSION     WP_457655038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13764
     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 idgralaafs ievgqsagge
       61 detpytsarn afpgivtavk lgdvaaqvei qagphrlvsl ltreaveelg levgmqatar
      121 vkstsvhidr t
//
LOCUS       WP_457655039             290 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655039
VERSION     WP_457655039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28854
     Region          33..213
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mstdtrtgtg tvaradrgas aatatgavst adllrsevlk ltttrlwwil llavvacsag
       61 ftalivfggl naprsplsfg tagdavpayn lavalayvfp laigviavtq eyhartisat
      121 llaeprrarv ygakllvglg tafvygtvav vsgalvaaal lsghgkpayl tdgtvlgalg
      181 gsivvmtlwg aigvgvgalv rnqvaaivgi llvtqflept lrilasslgn aelgnllpgg
      241 agdlagggti mtaaaeadgg sqglgflvlt lyavaigavg avrftryeas
//
LOCUS       WP_457655040             717 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidase domain-containing ABC transporter [Streptomyces griseus].
ACCESSION   WP_457655040
VERSION     WP_457655040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 717)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 717)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..717
                     /product="peptidase domain-containing ABC transporter"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78464
     Region          10..711
                     /region_name="SunT"
                     /note="ABC-type bacteriocin/lantibiotic exporters, contain
                     an N-terminal double-glycine peptidase domain [Defense
                     mechanisms]; COG2274"
                     /db_xref="CDD:441875"
ORIGIN      
        1 mrrvrrvrev qqfaqaecgl cciamilsay gsrdsvaglr rehevgrdgl tikqiaailr
       61 grgfevrafr agaqrlgqlr lpliaywdds hvvvveeide hrvtvvdpgg grrtypaeef
      121 aehysglale avptpdhrpe rhrepsvwre flrsltgark plvqaflmsl vlysftifmp
      181 iatqyavndy agylekapia lvlvaftapm avffllsllr tvalasvirs lgeammgktf
      241 rrllelpyky fanrsqgelf yrlssitsvr dmissqlsvv lldlgsliai fsymfyrsft
      301 lgatafavfl tmlavavaty rpirritere isettksssl qmealssiet lkvsgmtgtf
      361 fqdwrqvyaa gmeqtrrriv lqgvatsgya vfqvfgpllv lavglwlvln gsldlgsava
      421 aqtltatslg mvmslsgaft qlitanaqva rvgdilhqpe dpgafgdrqv tvrgavrlrn
      481 vgfsypgsgv paladvsfdv rpgervaivg ssgsgkstlg kllmglypir sgdvlydgvs
      541 igeidadtfy rsaayvpqdi vlsnrsiadn irfgvpdatm eavvdaarqa hvhddiaamp
      601 lgyhtpvrem ggslsggqrq rvalaralar rprvlvldea tsaldtvtes riaaaldrle
      661 ctriiiahrl stivnadlvv vlehgrvvqt grhedlitep gpyrdlvrsq vdlntvr
//
LOCUS       WP_457655045             336 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655045
VERSION     WP_457655045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..336
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34225
     Region          90..322
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mqplpadptv tpsagrgarf rrsvllplta avllaagtgg wyafggggpv tgaggadgpg
       61 egvaplarsm qlpwpregqa svavegigsl gtrgeqkpvp iasvtkvmta yvilkgrpmr
      121 adapgatvva dqraadesys svettapvla grtysqrrll elmmvpsgnn varllarwda
      181 gdekafvakm nrtaaalgmr attytgvsgm eastrstaad qlrlaraamk dpafrqivat
      241 gsvtapgagv tfrntnkllg hdgviglktg sstpaggnlv watrqevagv srlvigvvlh
      301 qragttpaeg saaaheasra litairadlp daanra
//
LOCUS       WP_457655046            1068 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655046
VERSION     WP_457655046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1068)
  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 1068)
  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   3  (residues 1 to 1068)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1068)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1068
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=115601
     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"
     Region          189..1064
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mdfgvlgplt vrragvplel gtpkgqmlla vllsrpgrtv tddalveavw gaeqpksatk
       61 nvqtyvhrlr rrlgdpgrit regrgyrlra drgeldsarf edlanaaraa saagdhersr
      121 rlfdealglw rgpafgeiad vpalraeatr ldelrlgvle ervdvdlrlg rhgevlgelt
      181 altmehpfre rmwaqlmlal yrcgrradal laylqvrdvl veetglepgh rlrnlhravl
      241 dedpaldrvt agaearapgr tavttpgptp drmevaadel aprrtafaad dpaqrpvpdp
      301 apgrpalvse eqaradvara rmlppalgdf sgqerelaei eavlrtrhaa depaatvtvs
      361 gpggvgktal avqaahrlrs aypdgrlfaa lagsrtqpas atavlgrflr algvpatavp
      421 ddpeervdly rgllaerril vvlddaynea qlapllpasg tcgviatgrv rlgglggahr
      481 velremsead saallrgstg grlasasgae lselvrlcar lplalriags llvsrphwrp
      541 adlvsrlade qhrldalryr dlevrasfgl syeglrpgar rlfrllglle apdfplwaaa
      601 aavdtelrea qelldelvdv hlldvrlpda sgtpyggqar yafhdliray areradaeet
      661 aaardgsvvr vlgallaftd iadrdhmgqn mfqqdadrwe parveaglpt svppmellda
      721 eraslmagvr qaaelgrdel cwelavgghv lfeteryfdd wqecydtamg laraagnlrg
      781 rarllismag llytrrrygp aeesnteamg lferigdrrg ylealsnapf flvpngrlte
      841 aitagreaye rldaggqaaa alhaysqvgl ahlqagrper avavlteiva garkqgirtl
      901 iardtywlgq aqlalgrhqe aeesfaelte cargigasgp fytahawgcl hlargefaea
      961 rsrllegvev aralhdpmfe trvlvdllda rlyelhdgqd aqdghdapal aaaivqgeha
     1021 vavargidyp yllagvlekl arlraaagdp ggakdlddea aalrdtih
//
LOCUS       WP_457655051             307 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655051
VERSION     WP_457655051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..307
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31439
     Region          46..305
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 msdspgspds aardrdeaes asafahppva pdataaygdh pdqvvdfyap rdgrtaaplv
       61 vllhggawra pydrvhtspl adflarrgfa vanveyrrgg ddipqqrdga entrpsgadp
      121 vagrwpetfd dvaaaldamp vvaarelpga dvrrivvagh sagghlalwa aarhvlpegs
      181 pwrlpapppl rgvvalapia dfataaglgv cggavdqllg gnadfeerat hadpgvllpt
      241 giataivqgv ddivvpkava eayvdaaars getvgltllg gvghfplidp aadacavvae
      301 eitqlaw
//
LOCUS       WP_457655060             515 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces griseus].
ACCESSION   WP_457655060
VERSION     WP_457655060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..515
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55658
     Region          3..512
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 meqealtela viraealrgp serateaqha kgkltareri ellldsgsfk eveqlrrhra
       61 tgfgleakkp ytdgvitgwg tvegrtvfvy ahdfrifgga lgeahatkih kimdmaisag
      121 aplvslndga gariqegvsa lagyggifqr ntrasgvipq isvmlgpcag gaayspaltd
      181 fvfmvretsq mfitgpdvvk avtgeeitqn glggadvhae tsgvahfayd deetciaevr
      241 yligmlpsnn renpptaqsd dpadrrsdvl ldlvpadgnr pydmhkviee lvddgdylei
      301 herwarniic amarldgrvv givasqplal agvldinsse kaarfvqlcd afniplvtlv
      361 dvpgflpgvd qehggiirhg akllyaycna tvprislilr kayggayivm dsqsigadlt
      421 yawpaneiav mgaegaanvi frrqiadaed peamrtrmvk eykaelmhpy yaaerglvdd
      481 vidpaetrev liaslamlrr khadlpsrkh gnqpa
//
LOCUS       WP_457655063             407 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655063
VERSION     WP_457655063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=42689
     Region          8..>294
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mrqniqqhrv vvigagytga taagrlarrl rsedvsitlv naepdfverv rmhqlaagqd
       61 lrprpyremf agtgvrlrla kvtgvdvdrr tvsvtapdga gepedlaydt lvyalgsawn
      121 thavpgaaeh ahdiagrpga lrlrerlaal gpgepvvvvg ggltgveaat eiaetrpdld
      181 valiargalg dwlspkgarh lrkvftglki tahehttata veadrvttak gdipaavtiw
      241 ttgfsvhpia rattlktgdt gqimvdatmr svshpdvyai gdaalvagpg dkplrmscas
      301 gvptawqaad aiaarltdgk lptisaryfn qcislgrkeg liqyvtaddr avsaaltgrl
      361 aafykelvck gaawgvanpt lglptrrrrt tsepapastt vtaaeaa
//
LOCUS       WP_457655066             298 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655066
VERSION     WP_457655066.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..298
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30687
     Region          27..297
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mlavgavvwa avtalhasip ntgvnagslf qtllpwtglg vpfllvlaav lrsrlaavav
       61 lapavvwvtl fggaltdkrs gggdltvvsh nvdeantdpa gtarvlagag advlaleels
      121 dasapvysre lasayphhav lggvgiwsrh pladvkevpi mpwtramrat vrapdgppva
      181 vyavhlasvr vsaagfttgr rneaarelaa alraesahrv vvlgdlngty rdralapvts
      241 qlrsaqgeag aglgftwpaa fpmariddvl vrgltpraaw tlpatgsdhl pvaarltr
//
LOCUS       WP_457655067             361 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655067
VERSION     WP_457655067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..361
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36523
     Region          106..158
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          174..357
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(206,231,265,268..272,274,282..286,289,293..296,298,
                     307,312..317,332..334,339,343)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(206,294,296,298,312..317,332..334)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mkhrrisrkr atlagsavva lvaagftfqs anasddvpef avktlgvdaa gklattldrd
       61 lgaaaagsyy dstakalvvn vvdeagaeqv rqaggkariv enslaelksa rqtltdrati
      121 pgtswavdpv tnkvkvtads tvdgaawkkl savvdglggk aelnkaagef kpliaggdai
      181 wgsgsrcslg fnvvkdgepy fltaghctes vtswsdtqgg seiganegss fpendyglvk
      241 ytsdtehpse vnlydgstqa iaqagdatvg qqvtrsgstt qvhdgevtal datvnygngd
      301 ivngliqttv caepgdsgga lfagdtalgl tsggsgdcss ggttffqpvp ealaaygaei
      361 g
//
LOCUS       WP_457655070             442 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655070
VERSION     WP_457655070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43953
     Region          14..354
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtvrprtgpg rgwllrlvia fafaqgavsm arpavsyral algadeaavg viagvyallp
       61 lfvavplgrr tdhgrcapll plgvllisgg calsgvvssl pamaawsgvm glghlcfvig
      121 aqsivarqsa pdeqdrnfgh ftigaslgql igpiaagali sadsgalgrt salallvsag
      181 vcavaltslw riehrrapgs gpapghkvpv railgargvp agifismavl satdiltayl
      241 pvvgehrsia patvglllsl raaatiacrl vmtpllrllg rrallttscl lagllcagva
      301 lpvsvpvlav mlavlgfclg vgqplsmttv vraapaqars talalrltgn rlgqvaapaa
      361 agliagavgv aapfallgvl llgaaglglr geartkpara aadpapapvp pnpgpvppdp
      421 apvrpdpgpv ppavrdttes sg
//
LOCUS       WP_457655071             244 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457655071
VERSION     WP_457655071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 244)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..244
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25899
     Region          28..102
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdrslrqrpr phdaaaprla alaalladet rasfclalld grawtagela ryasvapsta
       61 sehlgrlvag gllaqerqgr hryvrlader aahlveelas haapdaperp rslraasiss
      121 alargrtcyd hlagrlgiri teamtvrgll rqdtgfalte aglewfaalg ipldrsarrp
      181 largcldwte rrphlagaal cahvlavgwc ervgsgravr atpagvgals dlldiapgsl
      241 ddha
//
LOCUS       WP_457655079             946 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457655079
VERSION     WP_457655079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 946)
  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 946)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..946
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105054
     Region          13..943
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtedlspaer yqasraraae matalgpfre myefgldpfq ieacqaleag kgvlvaaptg
       61 sgktivgefa vhlaleqgrk cfyttpikal snqkfadlvk rygadkvgll tgdnsvnsea
      121 pvvvmttevl rnmlyagsqs lsglgyvvmd evhylsdrfr gavweeviih lpesvtlvsl
      181 satvsnaeef gdwldtvrgd tevivsehrp vplwqhvmag rkmydlfeea tdhggrgagr
      241 revnpdlvrl arqesqntyt prdrrrgkmv readrererr qrsriwtpgr pevidrldne
      301 gllpaitfif sragceaavq qclyaglrln dedkrrlvre iveertasip gedlhvlgyy
      361 ewleglergi aahhagmlpt fkevveelfv kglvkavfat etlalginmp arsvvleklv
      421 kwngeqhadi tpgeytqltg ragrrgidve ghavvlwqrg mdptalagla gtrtyplrss
      481 frpsynmavn lvqqfgrhrs relletsfaq fqadksvvgi srqvqrneeg legykegmtc
      541 hlgdfeeyar lrrdlkdret elakqgaaqr raaaasslek lksgdiihvp tgkfaglalv
      601 ldpglpagra nghrgfdhhd gprplvltae rqvkrlasmd fpvpvealdr mrvpksfnar
      661 spqsrrdlas alrskaghiv pdrhrkgrap aaddreiarl rtelrahpch gcderedhar
      721 waeryhrlqr dtrqlekrie grtntiartf drivalltem dylrgnevte ngrrlarlyg
      781 eldllasecl regvweglnp aelaacvsal vyearqadda vapklpsgpa kaamgemvri
      841 wgrldaleed fkinqtegvg qrepdlgfaw avymwasgrt ldevlreaem pagdfvrwck
      901 qvidvlgqva aaaprdagag asgvarnark avdavlrgvv ayssvg
//
LOCUS       WP_457655083             455 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Streptomyces griseus].
ACCESSION   WP_457655083
VERSION     WP_457655083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..455
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50283
     Region          1..452
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msvavvlfts dlrlhdnpvl raalreadev vplfvrddav hrtgfdapnr lafladclad
       61 ldaglrhrgg rlvvrrgepa revrrvaees gaasvhiaag vsgyaagree rirealagtg
      121 relrihdavv talapgrvvp tggkdhfavf tpyfrrweae gvrgtltapr tvrvpdgvtg
      181 dplperdtvk nlspglargg eeagrklvts wlhgpmagye dghddlagda tsrlsphlhf
      241 gtvsaaelvh rarekggpgg eafvrqlawr dfhhqvlaar pdaswsdyrp rhdrwraded
      301 eidawksgrt gyplvdaamr qlahegwmhn rgrmlaasfl tktlyvdwrv garhfldllv
      361 dgdvannqln wqwvagtgtd trpnrvlnpv iqgkrfdprg dyvrrwvpel aelegaaihe
      421 pwrlegldra gvdypepvvd laeararfer argld
//
LOCUS       WP_457655089             106 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine kinase dimerization/phosphoacceptor domain-containing
            protein [Streptomyces griseus].
ACCESSION   WP_457655089
VERSION     WP_457655089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..106
                     /product="histidine kinase dimerization/phosphoacceptor
                     domain-containing protein"
                     /GO_function="GO:0046983 - protein dimerization activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=11060
     Region          1..60
                     /region_name="HisKA_3"
                     /note="Histidine kinase; pfam07730"
                     /db_xref="CDD:429624"
ORIGIN      
        1 marelhdivg hrlsgislma svvarqtasa pgearcgale irkqsnaild dlrrlvgllr
       61 gvghqdegvk sldtlsglie tarptgacvd fdprsgerrd asslgg
//
LOCUS       WP_457655090             484 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457655090
VERSION     WP_457655090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..484
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=49769
     Region          20..482
                     /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 mqerssvael vtslraelnr yspggklpss ralverfrvs pvtvsraiaq laaeglvttr
       61 pgsgafrahp rtelpapgdt swqevslsgd ggpevvprtv dasgvlvtla apppgviefn
      121 ggylhtslqp eralsaalar agrrpgawgr pptdglpelr swfareigpa vsaadvlita
      181 ggqsalatal ralappgapv lvesptypgm laaaratglr pvpvpmdadg vrpelladaf
      241 ratgarvfvt qplfqnptga tlaparrpev laiaraagaf vveddfarrl vhddagplpv
      301 plaaddpdgv vvhvcsltkv tspslrvgal aargpvlerl raiqvvdsff vprplqeaal
      361 elvgspswgr hlaavatelg hrrttmaaai aselpeltlp hlpagggslw lrlpgggaga
      421 gadepavvsa alrasvavap grpyfcaepp aghirlsfag vsgaaeiaeg vrrlrtafdg
      481 lpds
//
LOCUS       WP_457655092             476 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457655092
VERSION     WP_457655092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..476
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49813
     Region          1..472
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mttaivvgsg pnglaaavvl arsgarvtvl eaadeigggt rsgeavmpgl lhdhcsaihp
       61 maagsaflrs ldperhgliw rwpevdcvhp ldggeagvlh rsveetaagl grdgsrwrla
      121 fagpaarfdl laedvmgpll rlpghplala rfglpallpa savarlftte rgralfggva
      181 ahafrplhhp lsaaiglgii taghrhgwpv aaggsrsiaa alasalaehg gtietgvevr
      241 rvqdlppadi tmfdlaprav adivgdrlpa rvarayrrfr hgpgafkvdf aveggvpwtn
      301 pdarragtvh lggpyaetaa aerdvhagrm perpfvlvgq qyladprrsv gdihpvysya
      361 hvphgytgda tgavidrier fapgfrdrvv ghvarsttam hahnpnyvgg divtgakdpr
      421 qlvlgprstl spydtgvpgm yicsaatppg pgahgmcgan aaeaalrhlt rrprdr
//
LOCUS       WP_457655103             290 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655103
VERSION     WP_457655103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..290
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29364
     Region          21..140
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          102..214
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mtvtghdtga srgtsagtga dagavralrg ledgrpavrl raalavgttp dprfvdklve
       61 rsavepdffv rdmltwaltr hpvsvtlprl lgevhseras arsqalhtls kigdrrawpa
      121 itralltdad devarsawra avvlvpeeee falgallatq lgrggpetrl slsralialg
      181 damasalaaa andpdprvra halatdrllr dpdagftfal eeakrvvalg agsgegggsg
      241 gssgeageas gsgesgeasg sgesgeagea gesggfegar avrrsggegp
//
LOCUS       WP_457655104             235 aa            linear   BCT 27-JAN-2026
DEFINITION  bleomycin resistance protein [Streptomyces griseus].
ACCESSION   WP_457655104
VERSION     WP_457655104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..235
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=25490
     Region          6..127
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,40,47..49,51,66..71,76..77,80,125)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(31..32,40,51,53..54,68,107,114,116,120..122,124)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 mtettipllp crtslietav dfytalgfet tylqkspyay avvergavel qlygmkdydp
       61 asshsgcyvl tddvdglhta fraglkaayg rvptrglpri gplkdmsygv rqflmtdptg
      121 ntirigqais ddpshrpapk etfaralhma dlfadskqdl pgaakiidrv lgltdeqptp
      181 vqrlrllvlr gdiaqrmgev eraaglleea aavrldadqq tlggdalarl aelrs
//
LOCUS       WP_457655106             282 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655106
VERSION     WP_457655106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..282
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30150
     Region          12..278
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtndggggdl srlsinqetl kqwslpdlae gcvkagidkv glwrapvqey gvertarlla
       61 dagievtslc rggfftaldp aeraralddn raaideaagl stdtlvlvsg glppgsrdlh
      121 garervgeal aelapyaaar dvrlaieplh pmyaadrcvv stlaqaldla erfpaeqvgv
      181 vvdtyhlwwd dqapaqiara gaggrihsfq ladwitplpa gvllgrgqlg dgsvdfrafr
      241 rwvedagfdg pieveifnea lwardgaeal aevadryvrh ac
//
LOCUS       WP_457655108             383 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457655108
VERSION     WP_457655108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..383
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42708
     Region          4..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtrrtvriam ngvtgrmgyr qhlvrsilai reqggldlgn gevlwpepvl vgrrahalee
       61 lagrhgltew stdldavlad dtveiyfdaq vtsarveaik kaiaagkhvy tekptatdve
      121 galdlarlar dagikhgvvq dkiflpglrk lkrlidggff geilsvrgef gywvfegdwq
      181 eaqrpswnyr aedgggivvd mfphweyvlh elfgqvtsvt aqvqthvprr wdeqgkpyea
      241 taddaaygif qlaggavaqi nsswtvrvnr delvefqvdg thgsavaglr ncrvqhrsat
      301 pkpvwnpdlp vtesfrdqwq eipdnqefdn gfkaqwelfl rhvaldtpyt wdllagargv
      361 qlaelglkss aegrrfdipe ltl
//
LOCUS       WP_457655115             610 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces griseus].
ACCESSION   WP_457655115
VERSION     WP_457655115.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..610
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63796
     Region          52..555
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mphrtsrrtl ltataaataa aatgvlaapt aasahsadgf tdhrlrriia gmsleekvgq
       61 lfvmrvyghs atepdqadid anlkeigvrt aaelistyhv ggiiyftwah ntrdphqiad
      121 lsngiqraal aerhrvpllv stdqehgivc rvgepatllp gamalgaggs rsdtrraawi
      181 agaelaalgi nqnyapdadv nvnpanpvig vrsfgsdpda vadlvaaqvk gyqgagiast
      241 akhfpghgdt ntdshtglpv inhtraqwee ldappfraai raridsimta hivvpaldps
      301 edpatlsrpi ltgilreelg ydgvvvtdsl gmegvrtkyg ddrvpvlall agvdqllnpp
      361 nlsvawnavl eavrsgeise aridasilri lrlksglglf rdpfvshrgv ertvgsrahr
      421 aaadriaert ttlladpgtl lplsrrthrk llvvgadpas psgttgpptg tlahafgelg
      481 ftaralstgt apdrakiaea vaaaegkdav ivatynvtat ssqrtlvtal vatgvpvitv
      541 avrnpydvah ltgtgvaasl aayswtdvel raaarviagr adpegtlpvp vqraddptqv
      601 lypvghglty
//
LOCUS       WP_457655123             195 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655123
VERSION     WP_457655123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..195
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21565
     Region          27..194
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 miralstppa mssgclsrap qpvlpvgdgl llrpwerada aaflsvyqde etrrwhthrp
       61 stvaqveewf dgyrldwere rgchfavvre dgdvlgrval rgldfddgva naaywvlpaa
      121 rgagvatral aalsawaldd igfwrleldh strnaascrv atkagyrleg tkrnaavhdd
      181 grhdmhlhar vrgdr
//
LOCUS       WP_457655124             650 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces griseus].
ACCESSION   WP_457655124
VERSION     WP_457655124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..650
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67935
     Region          3..461
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          575..641
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(598,607..609,616)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            608
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mtmfdtvlva nrgeiavrvi rtlreqgvrs vavfsdadad arhvreadta vrigppaase
       61 sylnvaalle aarrtgaqav hpgygflaen aefaqacada glvfigppas aialmgdkir
      121 aketvaaygv pvvpgssgsg ltdaqleeaa reigtpvllk psaggggkgm rlvrdaavla
      181 deiaaarrea rasfgddtll verwidrprh ieiqvladah gnvihlgere cslqrrhqki
      241 ieeapsvlld aetraamgea avqaarscgy vgagtvefiv pgndpasyyf memntrlqve
      301 hpvtelvtgl dlvewqlrva sgerlpyaqe ditltgwaie arvcaedpsr gflpsggtvl
      361 alrepqgggv rtdsglsegv pvgslydpml skviaygpdr atalrklraa ladtvilgvp
      421 tnagflrrll ahpdvvsgdl dtglvereae glvpdgvpde vyaaaaavrl dalaprpdag
      481 gwtdpfsvps gwrtggvrap lvfplrvagr epvtqnppas atvtadrvtv eqdgavvhfh
      541 rsgdwlgrdg dawhvqdhdp veaslsgagr ggadtlaapm pgtvtvvkva agdeveagqs
      601 llvveamkme hviaaphagt vteldvtaga tvamdqilav vvpvadgeds
//
LOCUS       WP_457655127             491 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 18 protein [Streptomyces griseus].
ACCESSION   WP_457655127
VERSION     WP_457655127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Poria,V., Rana,A., Kumari,A., Grewal,J., Pranaw,K. and Singh,S.
  TITLE     Current Perspectives on Chitinolytic Enzymes and Their
            Agro-Industrial Applications
  JOURNAL   Biology (Basel) 10 (12) (2021)
   PUBMED   34943233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Chen,W., Jiang,X. and Yang,Q.
  TITLE     Glycoside hydrolase family 18 chitinases: The known and the unknown
  JOURNAL   Biotechnol Adv 43, 107553 (2020)
   PUBMED   32439576
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huang,Q.S., Xie,X.L., Liang,G., Gong,F., Wang,Y., Wei,X.Q.,
            Wang,Q., Ji,Z.L. and Chen,Q.X.
  TITLE     The GH18 family of chitinases: their domain architectures,
            functions and evolutions
  JOURNAL   Glycobiology 22 (1), 23-34 (2012)
   PUBMED   21750098
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Zaheer-ul-Haq, Dalal,P., Aronson,N.N. Jr. and Madura,J.D.
  TITLE     Family 18 chitolectins: comparison of MGP40 and HUMGP39
  JOURNAL   Biochem Biophys Res Commun 359 (2), 221-226 (2007)
   PUBMED   17543889
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Simpson,P.J., Xie,H., Bolam,D.N., Gilbert,H.J. and Williamson,M.P.
  TITLE     The structural basis for the ligand specificity of family 2
            carbohydrate-binding modules
  JOURNAL   J Biol Chem 275 (52), 41137-41142 (2000)
   PUBMED   10973978
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Aronson,N.N., Blanchard,C.J. and Madura,J.D.
  TITLE     Homology modeling of glycosyl hydrolase family 18 enzymes and
            proteins
  JOURNAL   J Chem Inf Comput Sci 37 (6), 999-1005 (1997)
   PUBMED   9392855
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10652546
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..491
                     /product="glycoside hydrolase family 18 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50088
     Region          49..141
                     /region_name="CBD_II"
                     /note="CBD_II domain; smart00637"
                     /db_xref="CDD:214754"
     Region          199..488
                     /region_name="GH18_PF-ChiA-like"
                     /note="PF-ChiA is an uncharacterized chitinase found in
                     the hyperthermophilic archaeon Pyrococcus furiosus with a
                     glycosyl hydrolase family 18 (GH18) catalytic domain as
                     well as a cellulose-binding domain. Members of this domain
                     family are found not only in...; cd06543"
                     /db_xref="CDD:119360"
     Site            order(202,229,268,304,306,308,374..375,419,453)
                     /site_type="active"
                     /db_xref="CDD:119360"
ORIGIN      
        1 masrthrrtt ttrtraigai vaaaviggtv faltgtaqaa aigaaytrts dwnggytgqy
       61 vvtnetdkpl tdwtlefdlp agtrigslwn gehtvqdnhv tvkpaswdke lapgrsvtvg
      121 fvtsatgtag dpagclinda acsvdggatp tpsgrptdtp ttaptptatp sataptsppt
      181 ptptatgrpg gggetgarfa pyvdtslypa ydlldtatkt gvkefhlafi tsgggcaplw
      241 ggvtglgddq vasqigalre kggdvrvsfg gaagaelaln cssadelaaa ygkvvdaygl
      301 tkvdfdiega alpdtaantr rsqaiaqlqk kypdldvaft lpvmpegltq pgvdlladak
      361 kngvrvdgvn imamdygpay sddmgayaiq aatatqaqik gvlglsdaaa wqtvavtpmi
      421 gvndvvteif tvedagqlvq fagqkgigrl amwsgtrdka cpggpkpsad atcssidqep
      481 laftkafaay q
//
LOCUS       WP_457655130             379 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655130
VERSION     WP_457655130.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..379
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39817
     Region          35..373
                     /region_name="oxido_grp_1"
                     /note="luciferase family oxidoreductase, group 1;
                     TIGR03558"
                     /db_xref="CDD:274646"
ORIGIN      
        1 mdeirgdetr ddarggasdg dgirgvaagt aavplsvldl vtvgqgrtat halrtsveia
       61 kltesrgfhr fwvaehhsmp gvassspavi lahiaahtgr irlgsggvml pnhaplviae
      121 qfgtleamap gridlglgra pgtdgataaa lrrsdrlneg addfpqqlme lirfldddfp
      181 dghpygriha vpgpvqatad ggvqsahrpp vwllgssgfs arlagtlglp fafahhfsaq
      241 ntipaldlyr esfrpsavld apyaligvsa laadderear rqvltgalsm vrlrtgrpgl
      301 ipspeeaeay afspmerefv dgwlsnvvhg tadevrggld dlakrtgade lmitanahgg
      361 darlrsydli adayglpaa
//
LOCUS       WP_457655139             262 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655139
VERSION     WP_457655139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..262
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29108
     Region          21..250
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mdypndqapg apirsgipeh gripkyyavk ariavlldel geggllpter elaqrhevsr
       61 etvrqalrel llegrlrrqg rgtvvagpkl eqplslasyt egvrrqgrrp grrliglerf
      121 pcpealaaev gvergepvwh lervlladde rvglestyvg varvpgldtr fdpdssfyay
      181 lrdrlgiafg daderietvl atpreallig tppalpmlli hrlsrdtdgr plervrtlfr
      241 gdrfsfsahl rgegrgwgeg rg
//
LOCUS       WP_457655141             506 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces griseus].
ACCESSION   WP_457655141
VERSION     WP_457655141.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 506)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 506)
  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 506)
  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 506)
  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..506
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..506
                     /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=52913
     Region          35..440
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnaavatsvf avfmvatval gllalrgrgg gggldewsvg grslgpvfiw vlmagegyts
       61 fsylgaagwg ynygapvlyv vaymscgyai gyvvgpmlws yarrhglvgi tdmvahrfgr
      121 pwlgavvavl atvfllpyiq lqitgmgvvl svisygavsl nwayfvafav ttgfvvvsgl
      181 rgsawvsvlk dvlviatlgf lalyvplhyf dgygsfldrl vteksdwltl pghggggtgg
      241 sggsglgevw fisttflnsl tvvifpttva gylgarnada lrrnamylpa ynvllfvpml
      301 lglaalfvvp glvgaesnla lfklvvdalp awavgvigva aalssivpma vfmlvigtmw
      361 grsvlsllpr lahadrqksa aqvvvvvags lallltytap ntlvrlslis yegmaqllpm
      421 vllalvwrrl tfrgafsgli vgvavvcvlv fsgndpvwgv naglvalaan lavalavtfa
      481 grpdadprpd aevladdrde yaadpv
//
LOCUS       WP_457655146             793 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655146
VERSION     WP_457655146.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..793
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=82065
     Region          80..724
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msdepqhwap repsdaaatp ggdrggppgt dahgaqgaks gkggkkrrpr rtgwrravpt
       61 wrmalgtvlg lglllvggiv agyqlvdipa anasataqsn vylyndgsvi ardgdvnrek
      121 vklsqvpmtv qhavlaaedr dfysddsavd vkamvragwn tvtgkgkqgg stitqqyvkn
      181 yylgqertvl rkakeaiiav klnrevtkdq ifegylntsy fgrnaygiqa aaqayygknv
      241 eelstaegay laallnapsa ydvvahpdnk paaqrrwnyv lngmvkedwl paaerattrf
      301 ptpgeakpst glsgqrgyiv qavedylnrh gildektlat ggyritttld kakqdafvka
      361 vdtnvtarts pdrkadrdvr vggasivpgs gavvalyggi dytqqyvsna trrdyqvgsv
      421 fkpfvltsav vndsttqdgr pitpntvydg snkrtvvgpq gatdyapane ddvdhgditv
      481 rtatdesvns vyaqmaqdvg pgkvrdtaia lgipadtpdl taspsialgp anasvldmae
      541 ayatladhgr hgpyvlvdki tkdgaevelp ertteqavsr eaadtttavl rsvveggtgt
      601 aaqavgrpav gktgtaeedr aawfagytpd latvvavmgq npdtgaqtsl ygalglprin
      661 gggapaetwa ayteaalrss paqefdletm pgsdeedepl ldedsdgste psaasdatap
      721 satapsgtap sspaassapt sgtdtggadg tgggnasggs ggtggtegtg gaggtgglte
      781 gargpdfpdg rpv
//
LOCUS       WP_457655148             250 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457655148
VERSION     WP_457655148.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..250
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26798
     Region          2..182
                     /region_name="RNaseZ_short-form-like_MBL-fold"
                     /note="uncharacterized bacterial subgroup of Ribonuclease
                     Z, short form; MBL-fold metallo-hydrolase domain; cd07716"
                     /db_xref="CDD:293802"
     Site            order(34,58..59,61,63..64,140..141,161,181)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293802"
ORIGIN      
        1 mkltvvgcsg sfpstgsacs sylveadgfr llldmgngal gelqrhvgly dldaiflshl
       61 hadhcidmca yfvvryyrhd garpvpipvy gpegteqrlt aahgdtpsdr amsevfdfht
      121 lksgsfeigp fsvrtekvch pvdtfgirve hggssivysg dtgtcdaled latdadlflc
      181 easfvdgked ipdlhlngre ageaaaragv rrlvlthipp wtdadrnvad aravypgpve
      241 lavpgavyei
//
LOCUS       WP_457655093             176 aa            linear   BCT 27-JAN-2026
DEFINITION  fluoride efflux transporter FluC [Streptomyces griseus].
ACCESSION   WP_457655093
VERSION     WP_457655093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..176
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18396
     Region          45..>139
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mhpdrpehht pptgrqaepv dpdtavdpwp pakasgpkrr qgeilaaiaa ggvigacary
       61 gatliwpaap tafpwtvfwi nvsgcaamgv lmvliterft vhplarpflg tgvlggyttf
      121 statldtqrl ldhgrhgtgl lyaaatltaa faavwaaaal trlvvlprtg aergrs
//
LOCUS       WP_457655149             346 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655149
VERSION     WP_457655149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..346
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34963
     Region          37..340
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mscrasaprr plgyvlvlgv laallaaavl aalalgsvri ppgqvldilt graeaspfrt
       61 ivldvrlprv llgivvgagl avigtvlqal vrnqladpfl lgvssgastg avlvivlgig
      121 atlattvtip aaafagalls lllvytlarg ggglttnrlv lagvavsyvl saltslilvt
      181 saradhlqev lywtlgglga arwdmlalpa itlvagtavl ltlarpldll lvgeegatvl
      241 gldtarfraa vfvlaslmtg vlvaysgaig fvglmvphma rmvvgaahra llpvvalgga
      301 vflvladlaa rtlaapqdip vgvltaltgg pfflwmlrrr peggpa
//
LOCUS       WP_457655151             555 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces griseus].
ACCESSION   WP_457655151
VERSION     WP_457655151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  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 555)
  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 18638503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..555
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58726
     Region          140..396
                     /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          230..256
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          265..528
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          265..293
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(266,269..270,273..274,276,300,303..304,307..308,
                     310..311,334,337,340..341,344)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          298..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          333..360
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          370..398
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(371,374..375,378..379,381,405,408..409,412..413,
                     415..416,439,442..443,446..447,450)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          403..433
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          438..466
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mamdvmpqqd pgsrrppeqs sqdpyampae gatavppppp tlrttlrraa vgavaagvll
       61 agalvavddg egdgpkepgp veraeaatta gspaslsdlt aligdrqkwv eshpedapsl
      121 atlgtayvew arrsadtayy araeqalkrs learpgergn geawvglaal anarhdflaa
      181 krwgetvrkq qpkswsvypv lidaytglgd qkaataatek fgelrkgvpa lartadlyrg
      241 qgwredalat areaadratq paekaealhr lgelawerge peeavaqfda alrtdaghhp
      301 alagraralv aldrtdeala ayqsaleqlp rpeyalelge lyeslgldgd artqytklre
      361 mvaearkaga deslvlarfe adhgepeaav ellraqwrgq hrsaavadal gwalhragks
      421 eegleyaera vdtgvrnasy ayhlgviqre ladygparrn leqavrtnpa fsplaaplar
      481 ealdalgepp pggpgdmqpp pppppapept pepkreqekk peapapaask tatapsesps
      541 ptaspspspa aaksp
//
LOCUS       WP_457655153             304 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655153
VERSION     WP_457655153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..304
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31864
     Region          13..301
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mvaggavvva gvlafhrgvp nwpgragsll esflpwvgvl vvvllvvalv rrsavalval
       61 llpvgvwvhl fgglllpyge sggrelvvvq hnvsdenrdp aataralsdv gadlvaleel
      121 vdpqlavyek alasdyphhv vrgtvglwsk yplsgarlvd ikppsieegw srgvravvrs
      181 pygdvaayva hlpsvrvgag glasqrrdes aallgraiad esvetvillg dlngavedrg
      241 lrpltsrlnv aergfalsfp aafpvaridq vmarsavvgh irtlpatgsd hlpvvarvvl
      301 pghr
//
LOCUS       WP_457655154             232 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655154
VERSION     WP_457655154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..232
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25588
     Region          60..161
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(79,82,127,157,160)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mrtttygdwi rdfeaarrer aergdpdwrt gveqhpairr svqrfqvged gdgaglitka
       61 eaagdaeyas avrmfvaeer nharllalll asggapliss hwsdrifval rralglrlel
      121 lvlmiaevva lryyralrdg agdaltreva gliladeerh vpfhrhrlrr alrplpppvr
      181 vlvtsgwraa laaaalvvav dhgpalrrlg vgrfrfarev vrssgpiaat mr
//
LOCUS       WP_457655157             520 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655157
VERSION     WP_457655157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..520
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56038
     Region          186..>287
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          415..504
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrtaalytsi gslvlsalaa apanaweapg saeargtaia aarataagid faacpeeeml
       61 pdslkcgtvk vpldyaepdg rqleltvsrt patgpaqerq gafvynpggp gassitfpla
      121 gelpewkeia gaydlvgyap rgvngssapl scqdpaaytk gptdapthpt qaykerrvar
      181 akayargcae hagatlrhyt slnnardldv lraalgenrl tfmgasygty fgalyatlfp
      241 shvrrmvfds vvdpdpeqiw yrsnmdqsla fetrwedfrr wvarhddvyh lgttpeavqk
      301 hydevraela vkpaggkvgp gqlhsaflga gyyddywamr atalseyvrg npeplvaqas
      361 pravaakdne naqavytave cndapwpeef evwdrdhtdl arvapfetwd naftnlpcaf
      421 wpaprqrple vgtrwgelpp vlilaaerda atpykgalel rrrlpgsslv tergagthgv
      481 ggagntcvdd hlrrylltge vpgrgadcaa hpepnpvsld
//
LOCUS       WP_457655163             153 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655163
VERSION     WP_457655163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..153
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16393
     Region          22..151
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 meastkaqpp vtvrvfnrqy cadprgarla rriglhklht wgipylsdas esaaliigel
       61 tanaathgrv pgrnfelrls ympgdpaapg llrievsdtr gerrppgpge itvpdggadg
      121 grglliveal adrwavfdrn pgktvraeld llh
//
LOCUS       WP_457655165             755 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional serine/threonine-protein kinase/ABC transporter
            substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457655165
VERSION     WP_457655165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 755)
  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 755)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 755)
  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 10196220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..755
                     /product="bifunctional serine/threonine-protein kinase/ABC
                     transporter substrate-binding protein"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=77285
     Region          16..271
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,75,91..94,98,100,137,139,
                     141..142,144,153..154,157,174..177)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,75,91..94,98,139,141..142,
                     144,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,98,100,137,139,141,157,174..177)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(37..38,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(153..161,170..177)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          374..724
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mddlrptdpa rigghrllgr lgaggmgvvy lgrtdagala aikvilpeha gdddfrarfr
       61 reaeaarrvd spwavpvtga dteaerpwla tefvpgptls dvvvrrgplp vrsvtvlgrl
      121 laralaavha aglvhrdvkp gnvlltasgp rlidfgiara adataltatg livgtpgflp
      181 peqasgsatg atgadgadgs agsagdvfsl gcllayaatg rppfgsgavd avlyrtvhga
      241 pdldgiddpg lrslldrcla kdpderpaaa dldtliaedv pagasadwlp edvariiadr
      301 aaallalpdi datvavteep gpprpapgrr rflflaagga lalgagafaa vrltgdgadg
      361 aggdgapggr rliigvhadl tgplsaagra qergvrlavd rfnslgdqpf rlavkvlddq
      421 gdaarsarva eefardpevi avigptgdaa agaalstyde avlpvltvsa llmafperan
      481 gsffqaspty aelsfpvvnh lllrpdverl gilidrsggq sayqagyavn lmtpqlttgt
      541 thprvvpagt tvfdpvvtdl lshrsdalfy ageaagaakv arilaeqsfa gprmaqhtvm
      601 gpdfleqaga aaegwefvap fidattpaaa tfaaahrkrf gaapaawsae aydvaglvar
      661 elatlagaas kaatagtksa tagdkspsag atpsgdgrpt rsalttaiaa aryegvsrsy
      721 afdeerqqlv gqdahlyrve dgrlryvgpa pkpks
//
LOCUS       WP_457655169             326 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655169
VERSION     WP_457655169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35744
     Region          163..306
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mppapsrlti rplsgpgeld lfrrlsyvld heladdlatg rrlpewmwia ldggrvvara
       61 awwtnapgge plaldffdld dalpaperie igvrllerat gavvpagarr peygrfvppd
      121 wredpvarea vgariaavea tgarmlverl rlewragtpv pgdsgrlvfr pvtgredlla
      181 lmtpvmegtl dahgqedlas gldaraaaek hydeelagys tpmawwriae lptgepvgfv
      241 lparnnyhpi iayigvlpar rghgyiddll aegtrvlaae gvdriraatd lgnvpmaksf
      301 drlgyvnfer afnmvwdaek seertg
//
LOCUS       WP_457655171             343 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655171
VERSION     WP_457655171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..343
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36920
     Region          58..331
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtsvtatkrs gpdgphdgrs grggrdgqgg rggrggkggr agrfrrpeqp erkafgdrag
       61 wflvlpalip ililsvgpll ygialaftda qsgrtrstqw igtlnfqdll hdtlfwdsfr
      121 iglvwavgvt vpqfllalgl alllnrnlrm rwlaralaii pwampevvvg imwrfvynpd
      181 agilnetird lglgdgrdwl tglatalpav ilvgiwagmp qttvallagl qntprelhea
      241 aaldgagawr rfrtvtwpai kpialaisal nliwnfnsfa lvyvltsggp ggrtrlpmlf
      301 ayeeafrygq fgyaaamgcv mvavisvlla vhlvgrlggg edr
//
LOCUS       WP_457655174             563 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655174
VERSION     WP_457655174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 563)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 563)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 563)
  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 563)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..563
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56749
     Region          11..558
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mgadtagrgv irravagqrr dvvvgsllga chqigealvp vliglivdra vvrpdggala
       61 iwlvvlavvy tllsfgfrfg arageraaeq aahqlrldvv rrvlaphgga eagrppgalv
      121 nvatedarrv gavnmaltlg iaavvgvvag avlllraslp lgllvlvgap llmalghfla
      181 rplehrseae qeqaahasgv aadlvagvrv lkglraeraa vdryratsqa sreanvraar
      241 aaalqtglml tltgafialv alvggrlvlg gsiglgalvs avglalflpg pisvlarvga
      301 elakgrasaa riadvlaapg ettggtaepa agapgelrln glghagldal dltvhpgehl
      361 givvtdpada atllhclarr cdpdrgsvel dgvpltelap aalrsallva ehdaqlfdgt
      421 lldnvtaaap agadphpamd aaavdevasa laggvggrig ergsslsggq rqrvalaral
      481 aadrgvlvvh dpttavdaat eariaagirr artgrttvlv tsspallaat drvvlvdggt
      541 itaeaphedl irdhpvyrta vlt
//
LOCUS       WP_457655175             623 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655175
VERSION     WP_457655175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 623)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 623)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 623)
  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 623)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..623
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64265
     Region          24..618
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttadiper aesdgdsael lpvatpartr aalralirpd rvlaltgigv lvaatavgll
       61 vqpllgrivd ivadgrpaad ltlpvvllva vaavqglttt igltrvarlg etvlarlrer
      121 fveralnlpa drleragagd ltarvtgdva rvaeavrsal pemarsvlai vltlgalall
      181 dvrfllaall avpvqlltar wyvrraltly adqriangaq qqqlletigg avtvrghrle
      241 arhtersagr srravdltmr svnlvlgfyg rlhiaeyigl aavliagfwl vrdgavsigt
      301 ataaalyfhs lfgpvnaalv llddaqsaaa glarlvgvtd laeepdpaag kadpdpcpvp
      361 hqrtapdaap daapgrkavt apataavtah avghaygpgr pvlhevsltl esgehvalvg
      421 tsgagkstla rivagvqqpt sgtvtapagt geaavvlvtq evhvftgtla edlrlarpda
      481 tdadlraala tvhaldwaea lpdglgtvvg egghrldpar aqqlalarlv ladpalavld
      541 eataeagsag arvlersaea alagrtalvv ahrltqavaa drvvvleagr vvesgpheel
      601 rdadgpyaal wrawsgsrta lhp
//
LOCUS       WP_457655179             406 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655179
VERSION     WP_457655179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 406)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..406
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42071
     Region          4..405
                     /region_name="PRK06205"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:235741"
ORIGIN      
        1 mpldvvicep lrtpigrfgg afaqqtpaal aarviaeivt rtgiapdrvd evilghaypt
       61 seapaigrva aldaglpttv tgtqidrrcg sglqavldaa mqiragfsev viaggvdvms
      121 aapyythdgr wgikgpglql hdalargrvt aggvnhpvpg gmietaenlr reygigradq
      181 dalalcsqqr aaravaegry daetvpvtvr trrgeatvta dehprpdtta eqlaalrpvm
      241 aksdpdatvt agnasgqnda aaaclvtsae taerlgltpl vrlvsfarag vpaatmgiap
      301 vaatrtaldr agltladldl ielneafaaq vlactrelgl gekdheqrin vngsgislgh
      361 pvgatgaril atltrelhrr qarygletmc igggqglaai feriad
//
LOCUS       WP_457655189             485 aa            linear   BCT 27-JAN-2026
DEFINITION  catalase [Streptomyces griseus].
ACCESSION   WP_457655189
VERSION     WP_457655189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..485
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53817
     Region          3..481
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 makrvlttes gapvadnqns atagvggpil lqdqhllekl arfnreripe rvvhargsga
       61 ygyfevtddv tgftradfls svgkrtetfl rfstvadslg gadavrdprg falkfytdeg
      121 nydlvgnntp vffikdpikf pdfihsqkrd pftgkqepdn vwdfwahape athqitwlmg
      181 drgipasyrh mngygshtyq wtnaegeaff vkyhfktnqg vrslsadqaa elvgkdansh
      241 qtdllqaier gvnpswtlyv qvmpaaeaad yrfnpfdltk vwphsdyplq rvgrlvldrn
      301 pdnvfaeveq aafspnnfvp gigpspdkml qgrlfayada hryrlgvnht qlpvnaprta
      361 vvdnygrdgv hatrngsrhd knyepnsyag paqtdaalaa praihgwtgt heapahtkdd
      421 dffqagelfr lmsedekgrl vaniagglsq vtrddviekn lahfhaadad ygkrveeavr
      481 alred
//
LOCUS       WP_457655190             482 aa            linear   BCT 27-JAN-2026
DEFINITION  cellulose binding domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655190
VERSION     WP_457655190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Henrissat,B. and Bairoch,A.
  TITLE     Updating the sequence-based classification of glycosyl hydrolases
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 695-696 (1996)
   PUBMED   8687420
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469668
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..482
                     /product="cellulose binding domain-containing protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51146
     Region          46..128
                     /region_name="CBM_3"
                     /note="Cellulose binding domain; pfam00942"
                     /db_xref="CDD:425958"
     Region          220..448
                     /region_name="Glyco_hydrolase_16"
                     /note="glycosyl hydrolase family 16; cd00413"
                     /db_xref="CDD:185683"
     Site            order(319,321,323,338,340,342,356,358,374,424,426)
                     /site_type="active"
                     /db_xref="CDD:185683"
     Site            order(338,340,342)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185683"
ORIGIN      
        1 mnpsrrnprg srlrtaaasa aavalaatgl aalpssasaa adgivvqyrt sasgasadqs
       61 epwlkvrnag stsvplssvk vryyfkadsa saayrfacsw avkgcgnitg tfgtlatpta
      121 tadryleigf tagagslapg adtgdmqlrf hqsswaslvq sddysfgpeq aaygdwskvt
      181 ahvsgatvwg eapggngptd ppdptdpptd ppgdaaalfd dfdysshtdp kinangwsvr
      241 snsggpgvpg atwapenvtf adqggntvmn letstagtga stkhteiltq smkfkngtya
      301 srvkfsdapr sgpdgdrvvq tfftindlka pmaddyaeyd feylpnggwg epanilytts
      361 wetyrpdpwe avnahsesrq syagwhdlvv tiddneityy vdgqhfgthg aaylperpms
      421 infnqwlidl egqpsttpra ydqqvdyvlh vkdqvltpaq vnamvgsyrd agtsfedtvp
      481 gs
//
LOCUS       WP_457655191             538 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces griseus].
ACCESSION   WP_457655191
VERSION     WP_457655191.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..538
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58541
     Region          3..517
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mpasrpspal sllprpsris slggrltldr ettvralrga epaadllrtl vgrttglpla
       61 papdgrvvla lddrlgglge egygltvapr alqlraahlt gllrgvqtir qllpaealsg
      121 gpastgpwel pcveitdvpd rpwrgamldv arrfqpigyl rryvdlmalh klnvlhlhlt
      181 ddqgwrmpvd ayprlisvgs rragsqqgpt gpdgayvdav pheghytkae lkglvryaae
      241 rgitvvpeie mpghvraala aypelgnhpe rqldvwtrwg vcdtilgvhe gvfdfcravl
      301 eevlevfpsp yvhiggeecp tteweespaa reraaelgla dpaalhgwfm grigailver
      361 griplgwved gaelppeftv mtwrdsshtr aavhrghqvi aahhratyld yaqsgdpsep
      421 vaqpgapvsl htvhayepap rdwpeaergr vlgtqaqvwt eyartpeeie ylsyprlcal
      481 adrswsgghg dwpgfverlr hhtarldalg vpyrpldars latagsaspp sgtarphs
//
LOCUS       WP_457655192             467 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleobase:cation symporter-2 family protein [Streptomyces
            griseus].
ACCESSION   WP_457655192
VERSION     WP_457655192.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..467
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46934
     Region          41..452
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 maqpatgpae gpgttsptta adtavhpvde klpparlvpa alqhiaamya gvvtppliig
       61 qavgldtagm trliaaslli aglatilqti glgpfagnrl pfvnaassag iapmlaiaet
      121 sapghqlpai ygavlvagvf clavgpffgr llrffpplvt gvvitligvt lmpvpvawaq
      181 ggdataddfg amkylalaaf tlvvillvqr fgrgflkqva llvgmfvgtl aaipfgladf
      241 salksaplaa lpapfafgap efqpaailsl civmlvlmte ssagmlalge icdrrtdgrt
      301 itrglrtdgi atllgpvfgg fptsafaqnv gvvsltrvrs ryvvaaagga llilgafpvl
      361 gavvslvpmp vlggagivlf gsiavsgirt lseaglddss niilvavalg agiiplaapt
      421 fyagfpawaq tvlgsgisag alvavvlnlf fhhlgthsrt avalkss
//
LOCUS       WP_457655193             226 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655193
VERSION     WP_457655193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23685
     Region          12..221
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtltltdvtl typdgegrlt aldrvsldvp agtltavvgp sgsgksslla aaatlvtpds
       61 gevvvagtpa gglsragraa lrrdrigivf qqpnllpslt aaeqlqamrh lsggpvraar
      121 rralelldav gladradrrp hqlsggqrqr iniaralvne pavllvdept saldhergaa
      181 vldllvtltr eratatvlvt hdrahldrmd rtvtmddgrl tvparg
//
LOCUS       WP_457655194             344 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655194
VERSION     WP_457655194.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  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 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   3  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..344
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34962
     Region          1..193
                     /region_name="CcmA"
                     /note="ABC-type transport system involved in cytochrome c
                     biogenesis, ATPase component [Posttranslational
                     modification, protein turnover, chaperones]; COG4133"
                     /db_xref="CDD:443308"
ORIGIN      
        1 mhlrgvghry glrgawvlrg vdltlparal vrvegangvg kstllrllag idapaegrit
       61 grpsrtayvp erfpaalplt atgylvhlgr ihglrtaeak rragewlnrf gaaehartpl
      121 aelskgtsqk vavaqallaa pdllvldeaw tgldtaarae ldravaerva agatvvfvdh
      181 dprrlagaad ltlrtadggv hrataatapc pdpgprvlie aagppgatlp aalpgdpvre
      241 rrsgtggfga gaavsvpggg pdtgggtady spgpgyhgpd hgagsavvrl tvpapysdal
      301 laalltarpp whirqvapaq apapvtppes pesseaaaev seat
//
LOCUS       WP_457655198             478 aa            linear   BCT 27-JAN-2026
DEFINITION  PrsW family intramembrane metalloprotease [Streptomyces griseus].
ACCESSION   WP_457655198
VERSION     WP_457655198.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Ho,T.D. and Ellermeier,C.D.
  TITLE     PrsW is required for colonization, resistance to antimicrobial
            peptides, and expression of extracytoplasmic function sigma factors
            in Clostridium difficile
  JOURNAL   Infect Immun 79 (8), 3229-3238 (2011)
   PUBMED   21628514
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..478
                     /product="PrsW family intramembrane metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51875
     Region          56..324
                     /region_name="PrsW"
                     /note="Membrane proteinase PrsW, cleaves anti-sigma factor
                     RsiW, M82 family [Signal transduction mechanisms];
                     COG2339"
                     /db_xref="CDD:441909"
ORIGIN      
        1 msdpsvryqq arpavpvlhe qrldevlgaa pergqwryrp rrvgmvwrsk vfragaviva
       61 lvlcglvila lvreqtgpeg flvglglavl pvpllmaafr wldrvepgpw rnlifsfawg
      121 acaaalvaii ansfatrwia tatadpagad tlgatviapv veesakaaav lliflfrrre
      181 fggvvdgivv agftatgfaf tenilylgna fgedqqlgss gfasvtagtf fvrivmspfa
      241 hplftvltgl gfgfaavsar rhrgrrialp vlglllamgl halwngssaf gpygfyavyg
      301 ivmvpafglv twlaiwsrqr elrtlaaelp ayaaagwltp aeptalssmr argmardlar
      361 hwqqdrtrgr aaaravaeye sfatslaglr rrarhgavgp nfgarerell hhlwqrrdia
      421 apalthaarl tshrppthhy rhrpppygng hgygygygap vpqqpysgpp hshrrppq
//
LOCUS       WP_457655212             180 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655212
VERSION     WP_457655212.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..180
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18790
     Region          2..72
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mkieeaigan larlreeagl sqaqlgnalg sylekpwsrq avsgaekgrr aftaaelial
       61 alslgvsldf llmpvspqel tdllpgkaei taaayeravv gaasdggpnd rdlaraqgal
      121 vaslrsqidt qqalqrevrq qalllghasi algvsqadda elaellnelr hvdetegggk
//
LOCUS       WP_457655215             553 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces griseus].
ACCESSION   WP_457655215
VERSION     WP_457655215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     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]"
                     /calculated_mol_wt=58515
     Region          275..452
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mvrvpfraaa arvrhrlsql vrpkprtrtg apagsrtrtg aaapgdltsp arrpylralg
       61 mlavvvlgaw lgllavgsir tpvgpmdtnm tlrpsltggs kinvsplgal eldshtaplr
      121 ldvdvdrldp ersqalvdrp erfshlqdev trdvaagtre lavrscvavv sgatalglvv
      181 yrrprralaa gglaltllaa sgvsayatwn pksvlepkfs gllssapslv gdarsivtef
      241 diyqqelarl vtnvtklyda tstlpvyqpd pgtirvlhvs dihlnpaawh iiaslveqye
      301 idvivdsgdt mdhgsaaeng fldpirdlga pyvwvrgnhd savtqaylek fenvhvlddg
      361 ravnvgglri agtgdvsftp drtapvggra aarlegarla salrdqeqag tpadiavahd
      421 pntaretdgt vplvlaghlh rrineqlklg trlkvegstg ggglravqne kpekvhasvl
      481 ymdrstrrlq awdeitlggl glttaevgrh lpeenlkpgs ptsptpspts spgsppassp
      541 sptrsparpt psp
//
LOCUS       WP_457655216             265 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Streptomyces griseus].
ACCESSION   WP_457655216
VERSION     WP_457655216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..265
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27903
     Region          91..248
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mptpkksapk tstaaskkpl vygaavvlaa gllgfasyka tapddtskdt tatgpaaevs
       61 adpnegvype laklarrdad dklatgrada pvvlieyadf kcgycgkfar dtepklieky
      121 vkdgtlriew rnfpifgees enaaraawaa gqqdrfwefh raayaegake kgfgkdrvka
      181 laaeagvkdl nrfmkdldge paraavakdq eqgygigats tpsflingrp iagaqpdetf
      241 traieaaaeq aktagaagqa gepak
//
LOCUS       WP_457655222             194 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655222
VERSION     WP_457655222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20446
     Region          7..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msegtgrast saararlldt atrifyaegi hsvgvdriia eaqvtratly rhftgkeelv
       61 layldqadrg iragieaara gelsaadavr aigrfitggi qspgfrgcaf lnaaaeypdp
      121 ahpihqavla hrqwfletvt ellaqvgdep aegagrhlvm lrdgamaagc lsdpkpiaet
      181 fllgvegilr arga
//
LOCUS       WP_457655237             225 aa            linear   BCT 27-JAN-2026
DEFINITION  FMN reductase [Streptomyces griseus].
ACCESSION   WP_457655237
VERSION     WP_457655237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10024315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..225
                     /product="FMN reductase"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23798
     Region          9..220
                     /region_name="LLM_duo_CE1759"
                     /note="LLM-partnered FMN reductase, CE1759 family;
                     TIGR04037"
                     /db_xref="CDD:274935"
ORIGIN      
        1 mfattplrvv avsaglsqps strllagrla aatrerlvae rdrndrddrd vevrvielrd
       61 lavdianhlv sgfpsaglre aidavteadg liavtpvfta sysglfksff dlidhtaltg
      121 kpvviaatgg tarhslvleh alrplfaylr avtvptsvya asedwgssgd eyteglpsri
      181 rraggelasa vlgrtvsgas rtpglddged aivpfeqqla dlrld
//
LOCUS       WP_457655238            1140 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655238
VERSION     WP_457655238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1140
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=120370
     Region          <2..1014
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mtpalfgrdh pvgvlrseia ratdshgglv lvtgeagigk stlvtdaahe arrrgalvvg
       61 gscwdsdttp gywpwvqvlr glrrsataae wtaaqeasdg rlavllgdpa kvvtggsdgp
      121 gpstlsapga aaggpdsgaa qggepgtatg tsppgdgspg hgspgggfpg ggapegpeaf
      181 glfdavttal vtvsqsrplv vvlddlhssd paslrllefa aqhawferll ligtyrdvev
      241 eapghplqql ilplvsraaa tltltglgrd evgalmtvtt grepapqlvd evhrrtggnp
      301 ffveqtarlw hsgapvstip pgvreavrqr lallpepvvs lltsaallgr efrrqvlavv
      361 hgapvphver llesavvarv vvprpsgqya fahdllretl yasldeagar dahaaavral
      421 dahggigdav gpgelarhah laggalerdr ridlllaaar dasgrlaeee aaghyrrala
      481 vasgedpdlr raaligldla gqlrhagega eaqrlldgav artrelddpe llarvaitly
      541 rdgsmggghd astrdlllga hrgltgkegq eslsddrlaq elaihimala rggsddeala
      601 fslwarhdsv wglgsaveri eltdemtvig rrtrhqdmel hatsmrwval lelgdpafid
      661 qfrtfvrlae qtelprfalg iavdtslias lqgrfaeaat alqdealdpe nndhaafgfm
      721 ghhlrwalhl lrghfaeaee vlgrlpasgy pypgllesvt aveqgdatpa lrliaeqtdr
      781 dgpyprafmp lwlrllaqta avtgdrrlia raedeltpyt gqwivslygc diggpvdlwl
      841 gllaaarddq daavaaltea aasadrlgar pwavrarlgl arallarsga agsgaegsgd
      901 agrarrllge vireageldl shleaeasal rtapptaprt vavpdasadp gtdasaapga
      961 aefrrngpvw qlrwdgvtvh vpdakglrdl hsllglpgad vpavrllape ggelvvaagq
     1021 lggdpvldee akrrykerla rldaeidraa arddtrqvet ydrerqalld elrtaaglgg
     1081 rarrlgdqte rarktvtari rdtlrkletl hpalaahlka svttgttcay rpehspdwrl
//
LOCUS       WP_457655244             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655244
VERSION     WP_457655244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21996
     Region          8..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matkqrgrpr sfdredalrk atltfweqgy eatsiadltr vmgiaapsly aafgdkrtlf
       61 aevvetyadl fggfgdrama eeptarrgfa rmlreaaaey taagrphgcm vlsaaencss
      121 devvaalrgr rernmtefrr riqadidagv lpadtdaaal arctaavhqg msqqardgas
      181 raeletlaev amrvwpeesg evg
//
LOCUS       WP_457655246             404 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457655246
VERSION     WP_457655246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..404
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=44247
     Region          1..383
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mnrrtdieaa vraaaphall atlrtklrsv ygalavelhl adyglrvlks ldrpegesep
       61 lslhnspegr afgsqepreq qvrhddavdh hlpvtvrger lgiltvrlpq alstpelvge
      121 lthmadllgh eilvaerdtd lyqrarrttr ltlaaemqwq llparactaa efaigaqlep
      181 ayaihgdnfd waadadeltv avtngmgegi qaslltnlav nalrnarrag igiadqaala
      241 dqalydqhrg ashvstlllr felatgrvgv vdagspqlwi qrgrtvrrve leaqlplgmf
      301 eesrytvqef qvepgdrlll fsdgvydavs plgeaygerm laraiqstrl lpaatvprav
      361 lgelaeyrgt etpddalvlc ldwfgrqedq kdlegregre greg
//
LOCUS       WP_457655247             128 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457655247
VERSION     WP_457655247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14453
     Region          29..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtkqfsgsp edadlrrads lareifsdva nkwalliiea lgegtlrfte lrsavegish
       61 kmltqnlrml eryglvercv hptvpprvey sltvpgqglr rtvhvmcdwt hehlthleas
      121 rrafdtpd
//
LOCUS       WP_457655248             483 aa            linear   BCT 27-JAN-2026
DEFINITION  lipase maturation factor family protein [Streptomyces griseus].
ACCESSION   WP_457655248
VERSION     WP_457655248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Doolittle,M.H. and Peterfy,M.
  TITLE     Mechanisms of lipase maturation
  JOURNAL   Clin Lipidol 5 (1), 71-85 (2010)
   PUBMED   20543905
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10535984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..483
                     /product="lipase maturation factor family protein"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=54604
     Region          121..463
                     /region_name="LMF1"
                     /note="Lipase maturation factor; pfam06762"
                     /db_xref="CDD:462004"
ORIGIN      
        1 mewftadgyw lsrlifqral avvylvafls aalqfralig ergmlpvpel lrrtpwraap
       61 gifrlhysdr ffaavawsgc avsvaliagl dgllplwggm llwalpwvly lsivqvgqvw
      121 ygfgweslll etgflavflg sggtaapvlg lwllrwllfr vefgaglikm rgdacwrelt
      181 cldfhhetqp mpgplswffh hlprpvhrie vaanhvtqll vpfllftpqp vasaaaglmv
      241 ltqlwlvlsg nfawlnwlti alalsaidwt plagpppaqv applwyevvv faatalvlvl
      301 syrparnlls rrqamnrsyd plhlvntyga fgsisrmrle vvvegspdpv aregaewrey
      361 gfrgkpgdpr rmprlfapyh lrldwmmwfa alspayarsw fgpfaerlld gdrdtlrllg
      421 hnpfpdgppr rvrarvyryr ftglrelrat gcwwhrtyvr eflrpvsrpl pperegggtg
      481 rgp
//
LOCUS       WP_457655249             396 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457655249
VERSION     WP_457655249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42910
     Region          <169..388
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mtgaaiavlv vlvalllgtg fwlgrrtarp lrpsdvgtpv ehatfetlht aslaapplra
       61 glteesarrs arrlrsllgt dalcltdrdr vlvwdgagqh hgkevmeylk vlldngrgta
      121 fdsgcgdldc plrwavavpl tvenrvlgal vayapresav laraagevar wvcvqlelae
      181 ldrsrtqlie aeikalraqi sphfifnsla aiasfvrtdp eearelllef adftrysfrr
      241 hgefttlade lhsidqylal vrarfgerla vtlqvapevl pvalpflclq plvenavkhg
      301 legavtrsri tisaldagse aevvieddgt gmdperlrqi lrgeggtstg igllnvderl
      361 rqvygddygl vietgvgagm kitlrlpkyr agvhgs
//
LOCUS       WP_457655253             323 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein, partial [Streptomyces griseus].
ACCESSION   WP_457655253
VERSION     WP_457655253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..323
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          47..>172
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
ORIGIN      
        1 ghrperssph hdrrrtteda tvtdqlvrgd rnpataetts hppvtgllva vdercdlgck
       61 fclradvgrs aldlptyara lsrckelgat svcltggept dhpdfrelvr vavqfgyacs
      121 vvtaaregrr ldalasvagl lshvtvsads lgaqrvgate rtitgsaavf dalghgrasl
      181 hvtvweleda dleamaaida afgvefelsp llltdhqlkk atpeavrsry agdlaalrdr
      241 fglsdrftda laaldrslag tldrtcssdr lylsprgalr rcpydrknev dvrlsrkava
      301 dgvralhtsp savgsrcall cge
//
LOCUS       WP_457655255             820 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Streptomyces griseus].
ACCESSION   WP_457655255
VERSION     WP_457655255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>820
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <8..820
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 magksrslia eifseqvaar adhpavlceg rrltyarldq esdliaarla ehgvgdgdiv
       61 gialrrselc avawlavakv ngvclwldpd ypadrlafmi edaapsvlvi apdadgttre
      121 lavglrtvtv epasgdagpl apdtarslpp rrtapaqsaa yviytsgttg rpkgtiltst
      181 glrsllatav qgfgagrdsr vlqftsmsfd vaflemsmal llggtlvvvp gerrvaetaf
      241 lellreqrit haalppafle llpeenplpd gltimtgadk vplalagrwa rrarvvacyg
      301 ltevtvnstl wdydaswdga vaplgtedpg tvahllddsl rpvpagqpge lylggdglar
      361 gylhrpglta erfvadpyga pgarmyrtgd ravrhgsgvl eflgrvdgql kirghriept
      421 dvesvllrht svaqavvtsh ddtaggaela ayvvpaegae idarelrrhv artlpsymvp
      481 sllvpvsgla tlpsgkldrr svlrkataql padageadee alrqllsavl gcdeeefddg
      541 fdfvglgghs ltamrlatec rrlfgrepam rdvfaargvr dlldrltssg pdrprpgqpg
      601 nepfllsyeq erlwlleals gggthyhvpw awqvhgdldp ealrgaledl aachdilrtr
      661 fpavhgtprq eilppqeysp dyavlpvdgq dltaaiteaa resfdletrp pwrvrvltap
      721 dtpptvlfcl hhmvvddwsv drlatqlaqa yaarldpgle pparpalqfa dfsawqrrvh
      781 dapaggpesg gvgfwrgflr gvpvesgvpl drvrpdvpvv
//
LOCUS       WP_457655272             405 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655272
VERSION     WP_457655272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40718
     Region          12..362
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 msgttdparr gkhlgrrrlg ylaaaavfai gmagttlptp lyglyreqlg fselmvtvvf
       61 avyalgviat lllagnvsde agrrpvllaa lgfsaasalc flfegglpal fagrllsgfa
      121 agllsgaatv tvmelappgr aaraglaata anmgglgcgp llsgllaeya pwplrlpfvv
      181 hlglialaaa ltcllpetvt trvrrfrlrp qglavppevr avfapsalaa fagfsllglf
      241 tavapafvae tldvhnlalt glvvfsvfla stagqalmgr vgerralpgg cfvlvaglll
      301 vgasllfasl pllvagalcg glgqglafrg avkaisaaap pehraatvsa ffviaylgis
      361 lpvvgvgalt lgiglrnagl tfsgcvlala lgvglhlarr ppapg
//
LOCUS       WP_457655273             346 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655273
VERSION     WP_457655273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35276
     Region          49..335
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtvmttepap vapipsssst rlvdrvfrmr elailvvlvv mlvltqlgns aflseqgikd
       61 lllnatilal vatgqslvvi trnvdlsvgs tlgisafaag tylqggghpv vavalavllg
      121 vgfgllngll vslgqvpalv vtlgtlyiir gidsiwvgsr qitaadlpgg fvdfgsggis
      181 avpwlamial allvstayyl khfgsgrely algsnpeaar lagipvrrri llaytfcgal
      241 aglagalyla rfgnvdsgtg tgyeltvvsa vvvggvvftg gsgtvygaal gallltsvns
      301 vlpalgvssv wvlaingfll ilaiavdriv alrvasalkk rnarhg
//
LOCUS       WP_457655277             715 aa            linear   BCT 27-JAN-2026
DEFINITION  iron ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655277
VERSION     WP_457655277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 715)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Koster,W.
  TITLE     Cytoplasmic membrane iron permease systems in the bacterial cell
            envelope
  JOURNAL   Front Biosci 10, 462-477 (2005)
   PUBMED   15574383
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11484808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..715
                     /product="iron ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=71331
     Region          34..713
                     /region_name="PRK10577"
                     /note="Fe(3+)-hydroxamate ABC transporter permease FhuB"
                     /db_xref="CDD:236720"
     Site            order(468..470,592..593,595..597,599..600,602..607,
                     609..611,652,659)
                     /site_type="active"
                     /note="ABC-ATPase subunit interface [active]"
                     /db_xref="CDD:119348"
     Site            order(469,471,476,530,532..533,536..537,540..541,544,
                     547..548,550,562..563,566,642,694,697..698,701,704..705,
                     708)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:119348"
     Site            order(550,576,634,638,682,691)
                     /site_type="active"
                     /note="putative PBP binding regions [active]"
                     /db_xref="CDD:119348"
ORIGIN      
        1 mstrtttapp apvktaagaa gpagavapvt agpparrgrm lllalaglla laalavthvs
       61 qgtaavdlht lwqlatgsss drtaheqtaa vvldsrlprl aagllvgcal gaagaalqsv
      121 srnmlaspdt lavnagayfa vvtvaafgis lpalpagata flggllaagv vlglsragag
      181 pirlvlagsa ltlalsgmsg tllllrsqqt tglfawgegs laqigmqsid rlapvallaf
      241 aglmlmgrrl dilalgddga avvgvsprlt rsiavvlavl laavsvavag pvgfvglcap
      301 avvrllstwi pglvrhrafl pasalagvlv vlgadvllra vfggqagaev ptgivttcfg
      361 alvlvvlayr srdmgsdsgs tafarlrgrr afvltlsvtv vallgavvaa tlfgdatlll
      421 gdvgnwltgr sgqlvtyild trvprvvaal lagaalavag avvqavsrnp laepgvlgvv
      481 sgagvgavtv ltfvplasfw lisgsalaga aaaaglvfgl aarrgleqnr lvligigvqa
      541 gagafvslli vltdpynqtk alawlggsty grtfpelipv lvalvvalpv lavmrreldl
      601 igldnetpal lgvrigatrl gllslavllt agavaavgvi gfvglvapha aralvgrrhv
      661 rvvplsallg allvvvsdtv grtviapaqi pvglltavvg apyfiwllwr srreg
//
LOCUS       WP_457655279             484 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457655279
VERSION     WP_457655279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..484
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50749
     Region          16..484
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 mpdaaknper sepssydvvv igagpvgenv adraraaglt tavveselvg gecsywacmp
       61 skallrpvva radarrvpgl rdavqgpldv aavlahrdee tshwkddgqv awlesvgadv
      121 yrgtgrltgp revsvtapdg tehrltarha vavctgtrav lpalpgieev rpwtsrdats
      181 akeapgrlvv vgggvvgvem atvwqalgse vtllirgkgl lpkmepfage liadalteag
      241 armrtgvsvt avrrpapdgp vtvelddgdr veadeilfat grsprtddlg letiglepgs
      301 wltvddscrv egtdwlyavg dvnhrallth qgkyqariag aaiaaraaka apdtapwgah
      361 aatadhaavp qavftdpeaa svgltlaeae ragrrvravd ydlasvagsg lyadgyrgra
      421 rmivdldrei llgvtfvgpg igellhsatv avagevpiar lwhavpaypt isevwlrlle
      481 tfrg
//
LOCUS       WP_457655280             254 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655280
VERSION     WP_457655280.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..254
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26946
     Region          119..248
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 meqnlaehac hlhrtlkgas vaqtgdllia dsgldddtfn ivatarftpd taparaaeta
       61 rtlaatgrpf swwvgptstp ddlaehlqaa gleaseteag mwkdlraplp dahvdrlair
      121 pattpeqlad yatvlaanwn ppaatvrqff adtadralae dcparylvgy vdgrpvcsae
      181 vflhagvagi yniatlatdr rrgyggaita atlhtardag yetavlqasa dgepvyrrlg
      241 ftvsghftey altp
//
LOCUS       WP_457655281            1049 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655281
VERSION     WP_457655281.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1049)
  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 1049)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Rosinski,J.A. 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 1049)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1049
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=113351
     Region          <24..939
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          986..1045
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mitvgeihpa ashayamlgg vetrsvspvf vgraeelasl tealgraasg dpqalligge
       61 agvgktrlve qfvtaaerrd avvavgscve igadglpfap fptalralrr alpeemaaav
      121 agqegelarl lpelgeahrd atdehstarl feltvrller isadravvlv ledlhwadts
      181 trhllaylfr tlstgrlmvv gtyraddihr rhplrpllae ldrlrtvtrv eldrfshdev
      241 ghqlagilaa tpeaalvdei fdrsdgnaff veelarslec cgdssgltes lrdlllvrve
      301 alpehaqria rlvaeggsfv ehellaavag lgedeldeal raavganllq papdsdgyrf
      361 rhslvreavs ddllpgertr vnrryaeale adpslvrdde ratrlasywy aahdapkalp
      421 avlraavear rryayseqlr lleramelwd dvpdavratl rpfdyaevyp asacdpentp
      481 lryldvmaea tvaayfggdr tralaiskka mrvlasesdp lreawflvqr srlaqsldkg
      541 dgweelataq ervrglppsa vqadvltnva swkalhrpgp ealadsdrav eyarlvgdey
      601 ielharltrg wltadaggve dglaemyavr draeqlhlmn llgrvsvnlp ssleamgrsl
      661 eavaaadhgi eichshglad sgawvyanqs qslfslghws qseaaaassa rlalgsrgkg
      721 laalrrtela vsrgdfaege ellaqvhklf ghrdpqhqhv idpvrhgmvl aalqgrlaea
      781 rtafeelaga gfppgtqrya lpllqtaami eadarglpaa epdrprllal irrclknlpm
      841 lvpvwvaygv fieaelarae gtdtpghwar aaeafgplcr pyqlaqihrr waeslliapg
      901 dratatallh rsleaarrlg arplaeavvq laararitld gsgtapgdds gihpavlaae
      961 pggegrepap geeqdpavva vasfgltpre qdvhrlvaag htnrriaeel fispktasvh
     1021 vsnilaklgv ssrgeaaala hrlrlypta
//
LOCUS       WP_457655282             277 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655282
VERSION     WP_457655282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..277
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30141
     Region          26..122
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(68,71,75..76,85,97,101,107,111,114..115)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          148..263
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 msneerrpgk ppaggpadgl tggrtaalvg vsvktlhhwd tiglvrpggr trsgyrvygd
       61 ddvarlhrvl vyreigipla aigrllddpe vdarehlrrq rgqlvdrisr lermvgavdr
      121 mllesrpgir ltpeeqveif gadwqpgwae eaeerwggtd qwaqyteraa gmsaedwkdv
      181 aaatealtad laeacrtgva agsdpanala erhraqisty fdctyamqvc igrtyvtdpg
      241 yaayydaiap glndwlcavi aanarahgvd pesaswe
//
LOCUS       WP_457655287             493 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457655287
VERSION     WP_457655287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..493
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51412
     Region          6..480
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 msdivagaap rvttvhgtvr gavergvavf rgipyaaapv gvrrfrapgp pepwtgvrea
       61 vaygptapkr pyappldrll pdpavagddw lnlnvwtpap gaaglpvlvw ihggslvhgs
      121 savpvydgaa fardgvvlvs vnyrlgvegf gvlpdapanr glldqlaale wvrdniaafg
      181 gdpdrvtvag esagavsvaa llaaprsagl lrravlqsgv paalppdaar gtteliakrl
      241 gvpataaala avdpeallta qtgvtsggnp ltgrnsfqlv vdgellpqdp vaalhagaaa
      301 gvdllmgtns eeyrlwfvpg glterigrlr lrlallkfgv pnatarvyra nrpdatpgel
      361 lgalatdlll rvplnrlada rtdapgstyv yefgwptpvq rlgachalel gfvfdtlahp
      421 dtqaltgpda pqdladamhr awvdfatdgd pgwpswdarr pvtvfgpgap elvlaprdde
      481 lrgwkpyrhp dtp
//
LOCUS       WP_457655288             291 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces griseus].
ACCESSION   WP_457655288
VERSION     WP_457655288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..291
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29493
     Region          94..265
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(99..102,152..157,190,193..194,215,222..223,246,248)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(101..102,152,156,193..195,215,246,248)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mdgrrapmgr rdalgagagv laaalavgca rsdraaggaa gaagpggpgg pggpggpggp
       61 ggpavseagp aaapaprrfp glpfriahgp rdlprvaltf dgrgdpglar talarceqag
      121 arvtvfavga wlaehpglar rildggheig nhtehhldla alderaayee idacarrlrr
      181 ltgsigawfr psptayaspl vqrlaqragy phvlgcdves ldhaatrvat vtrkvagelr
      241 ngsvvelslg rpvtvdalpl llaeigrrgl ravtatelmg rpatgvtrta r
//
LOCUS       WP_457655290             643 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655290
VERSION     WP_457655290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 643)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 643)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 643)
  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 643)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..643
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68687
     Region          11..582
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mpekpaertd rsavrsllrl wpyvrpvrvr lfsaafvaiv asslglvipl vlkwmvdgpv
       61 adrdpggvwl galyllllgi aeallfgfrr wlvarplagv easmradlfr hlqrlpvafh
      121 drwasgqlls rgttdlmllr mflafpltfl ivntttilvg fvllfaqdwt lglvllapav
      181 plmilcslfe tkysvvarra qdqvgdlttv veesvlgiri vkgfgrhrsq aqafralshr
      241 lrttelgkar llagiwalit aipelaigaa lvlgtiqvad gslsagtlva flstalalrw
      301 pvesigflla msqesatatd ryfevmdvpe epgavavreg apataagmvf egvefrypda
      361 epgsppvlag idlhirpget lalvggtgsg kttltalvpr lheatggrit ldgediatme
      421 rsrlrelvsv afeeptlfsa tvgenvtmga agadeaqvrr alsvaqadfv helphgldte
      481 vgeqglslsg gqrqrlalar avvgeprflv lddplsaldv htetlveaal rqvlerttav
      541 vvahrpstvm ladrvallsg griaavgthq ellrdnaeya wlmsgaetgg parphegagp
      601 tgtghenrrg tgheaghedr rgagdenhra avgqvpaeeg sar
//
LOCUS       WP_457655292             374 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655292
VERSION     WP_457655292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..374
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=39326
     Region          1..372
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtgtatvvga gigglataig lrragwsvtv lerrtelery gaafgihpta qsaldrlgvg
       61 dalrdhavpy rdahirtpdg tpiarlpler ierkagrpel lisrpyllda lragleafgd
      121 vplklgervt dvdalaagqd lvigadgirs avrtarfgdr sgprevgtva wigiadfpsa
      181 vhgetwgsgr ffgltpvepg rtnwyatape attaaelrgl fagwhdpipr ildatdpaaw
      241 iryemrhlyp alptfvsvda rhapsaagps aagssaagpd ssaapvalvg daahamtpnl
      301 gqgactaild adaltralaa appgpagvtg alraydrerr rsaqrtafas rtlhrfmste
      361 rtrlrdravr llpg
//
LOCUS       WP_457655293             681 aa            linear   BCT 27-JAN-2026
DEFINITION  M4 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457655293
VERSION     WP_457655293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     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=70386
     Region          82..659
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrstpsrrat atgaliaaaa liavavpsga atatsapasa plggitagtk adpgalpakl
       61 spaqraells eanatkaata kelglgstek lvvrdvvqdr dgtthtryer tldglpvlgg
      121 dlvvkesaag rtegvskask atsaqlkavg ltadvapaaa ekqalgaaka egskaeeaen
      181 aprkvvwlgs gapqlayetv vgglqhdgtp nelhvltdat tgeklyewqa vhngtgntqy
      241 ngqvtlgtap sytltdttrg nhktynlnrg ssgtgtlfsg pddiwgdgtp qnaetagada
      301 hygaaetwdy yknvhgrsgi rgdgvgaysr vhygnnyvna fwqdscfcmt ygdgsgnvkp
      361 ltsldvaahe mthgltsvta klvysgesgg lneatsdifa agvefysnts edpgdylvge
      421 kidingdgtp lrymdkpskd gaskdywysg ignvdvhyss gpanhwfyll segsgaktvn
      481 gvnydsptsd glpvtgigrd kalqiwfkal ttkftsttny aaartgtlav aselygatsp
      541 eyaavahawa ginvgarpgg gdpdpggkvf enttvvnipd agaavtssvt vsgvagnaps
      601 alkvgvdith twrgdlvvdl vapdgtnyrl knrssgdsad nvvetytvna ssevangvwk
      661 lkvqdlarqd tgrinsfklt f
//
LOCUS       WP_457655300             243 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655300
VERSION     WP_457655300.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  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 243)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..243
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25579
     Region          52..243
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 maavlltetr lflrepgslf wilafptvll vilgfvpafk eadenlggrr vidlyvpvsv
       61 llamimaglq amppvltayr ergilrrmst tpvrpsallt aqitlhgaaa lcsallvvav
      121 grvgygvalp gqllgyalal llavaavlsl gaticalsrt tkaatavgsv aylammftag
      181 vwvpvqampd tlrrvvqltp fgaasqaldq aasghwpswa ylgvvalwtv ilgiaagrlf
      241 rwq
//
LOCUS       WP_457655303             385 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces griseus].
ACCESSION   WP_457655303
VERSION     WP_457655303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..385
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43841
     Region          73..374
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mppqrkrnpn gagtitkrkd gryqaavyvl qtdgtrarkf aygktwaecd akrrdllakv
       61 dqgvpvptrs aklsewlpyw leniikprrk rttyakyeth irlylapmlg skrleslsva
      121 dvrrflarle qqttaatake shrvlrtalt aacreelvmr nvatlvepps avardlspws
      181 ldetlsflta arkdplyaaf vlaialgfrr geivglrwen vdldkreirv rtqrqrvrge
      241 ayeddpkgrr rkqtlplpal cvaplrwerl rqtamreaag dqweetgyvf ttrsgrpiep
      301 rnlyrsftrv adtaglrvir lhdarhgcat lltaagvapr vvmeilghsq iavtmniyah
      361 vvqdtqreav shldrmlkrq rpdrg
//
LOCUS       WP_457655306             264 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655306
VERSION     WP_457655306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 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   4  (residues 1 to 264)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..264
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28861
     Region          2..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mttkwrelad klaeqikage ygpgaqlphi relvdagegs kstvhaayka leaeglvtss
       61 rghgtvvrqr vplkrlgidr ydkakwrdgd evafiadrva sgrayrrneq tqtvslveap
      121 laaseahglp agaevyarar lvkegqqpth cltsyyrpeh vegtrlvdpt pgpagrgggf
      181 rvlydagyei dhmkeqifar tatadeskll qlppgepvve lhrttytadg tvvefaigvh
      241 aasrfaweyk fqvpdsatdk enpq
//
LOCUS       WP_457655307             258 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457655307
VERSION     WP_457655307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..258
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=28606
     Region          3..244
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(3,27..28,61,66,71..74,86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(10..11,13..16,18,31,33,69,85..88,91,93,129,131,
                     133..134,136,145..146,149,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(10..11,13..16,18,31,33,69,85..88,91,131,133..134,
                     136,145..146)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(14,91,93,129,131,133,149,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(145..153,164..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 makfkrvasl dkgaqgsvwk aeavgtgemv alkylslepg ssridranrk trfvrevesq
       61 rrlahpgimp vlacatnasp pwyamplang slqqildgsr qplpwamtvi nevmdaleha
      121 hnrgvihrdl kpnniltveg kwvisdfgyc rridsdsaii teknhlvgsm ayaapeqydd
      181 phaaseaadi falvkilihl lvwripfpyf hieetpgdwh dllnrgladd paqrpqsvas
      241 lrsevnslfa snfdkens
//
LOCUS       WP_457655309             541 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces griseus].
ACCESSION   WP_457655309
VERSION     WP_457655309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  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 541)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..541
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=58842
     Region          123..506
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(129,171,174,233..235,239..240,451,453)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(129,171,174,233..234,239..240,451,453)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 maglrlgpll ryvdwetgst atvwveasrp ctvevrcadg asgssptfav aghhyalvvv
       61 tgltpgstta yevligsrrv wppddarlpp stittppvat asttattaat asagagaepp
      121 gvrisfgscr waaapggghd pvgpdalvtl aarlaadpaa erpdvllllg dqvyadetsa
      181 atrrrlaarr dlreppgaei adyeeytyly deswrdpevr wllstvpscm ifddhdvidd
      241 wntsaawqrd mratpwwher ivsglmsywv hqhlgnlspa elaadpvyaa vraspdgtea
      301 lrrfaaetda dpartrwsyr rvfgrvrlvm vdtraarvla eeqramldae eagwlreavl
      361 ddptsydhll igsslpwllp plvhdaehwn aalcagvrgr rwarfgeklr rasdlehwaa
      421 fpesfdrfte llreagsgpd apatvcvlsg dvhhayiaep rwpdteprrp dtgpapatgp
      481 gpgstadsgv apasrvlqlt cspvhnsipr sirtgfrfgw sragrwigra larhgrtgrr
      541 r
//
LOCUS       WP_457655310             380 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457655310
VERSION     WP_457655310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..380
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36974
     Region          303..372
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mtghacpecg rrtagepgte hrvpcrcgag agaapltede qraartaeia aaedfdplri
       61 rpyvtltdld aragggglae sggsattsgp gtseaatapv gtpsapgaag apgaaettmp
      121 lflgddgpgv gvgtgvdtgt gtvagasapa gpggrrrsag aepvfapdpv qprrrrpfga
      181 lavgaavaav vgtaafaggl fggddsrdea lpeattsvpd tedepaasva pspsasaaps
      241 rtpsasatps aspsasaapt rsqqptptat asasptasap atpdngggas sappaeappa
      301 elagpslrpg drgpevaelq nrlmevwlys gpsdanyngr venavavyqs ykaiqgdpag
      361 vygpntrral eaetsgrgrr
//
LOCUS       WP_457655315             374 aa            linear   BCT 27-JAN-2026
DEFINITION  phytanoyl-CoA dioxygenase family protein [Streptomyces griseus].
ACCESSION   WP_457655315
VERSION     WP_457655315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..374
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42710
     Region          50..305
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mnlmttpapr rrprlhraas dipyfsadge aylaqtalre ldksrllrvl seedfahwqt
       61 ygyvivreav pasvarelld ftwdfqgldp erpeswyedr plrseldqql hiygfveayh
      121 hqllwnnrqs qrvydafvdv wdceelwvtl drlnlnppnr gnrdraliep tdrgfdielh
      181 wdidttlavp pqrvqgiial ndtrpetggf qccpelfrqf dawkvaqpgd rdplrpdidr
      241 delpvvrpdl rpgdlliwng llahgvarnl sengvravqy lsmmpaleeh erlrrsrves
      301 wrhlrtprwn rtlvgdpvlp eskryptael nalgsrllgl aswqdpveet edtpgdagaa
      361 saapsgepsc aasa
//
LOCUS       WP_457655323             737 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Streptomyces griseus].
ACCESSION   WP_457655323
VERSION     WP_457655323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..737
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77409
     Region          14..372
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
     Region          369..733
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(454,484,486,517,519,715..717,719,721)
                     /site_type="active"
                     /db_xref="CDD:173841"
ORIGIN      
        1 mgrgtaigtg igiteehral ahsvrgwlar aappgevrkl ldahgpaatg vrpahweala
       61 aqgltgihlp eaygggggdl ldlavvleea aygslpgpyl atalvgavlr ravgpgtgdl
      121 lralaagdrt aafaltpgtl tatpapgghr ldgtappvlt geaadllllp aadasggvlw
      181 flvdagtdgf tvrphrsvdp trptaevrad avpvpahrnl pldatlvrdl aavllaadac
      241 gtaarsldta vahaavreqf grpvgafqav khlcadllvr leqaraltwd aaraaderpe
      301 vrgltaalaa atapeaaytc akdaiqilgg igftwehdah lqlrravlar qllgpadlhr
      361 lravrlaeag arreltlelp peaarhraea rphlaaargl aprearrala gtgyaaphlp
      421 apyglgagpv qqlaiqqesh eqgirlsdls vatwvvpsli aygteeqrer ylpatlrgdl
      481 qwcqlfsepe agsdlaalrt ravrtdegwr itgqkvwtsa artadhgill artdpdapkh
      541 rgltyflvdm rkargidirp lkeitgdslf nevyfddvll padavvgevg ggwrvardtl
      601 gnervhmadq mtfdsgletl iarsagldep vrartgalaa eahalgcigl rttlqqvsgr
      661 epgagasvrk lvqtrhqqkv aeltlellgp dgavdepaag gralhgflms rcltiaggtt
      721 qiqlnvvaer ilglprd
//
LOCUS       WP_457655325             261 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Streptomyces griseus].
ACCESSION   WP_457655325
VERSION     WP_457655325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..261
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26122
     Region          10..>199
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mnwstgllgf aagllisvat apvgvsgavf llpvqisvlg vpspavtptn llynvvagpg
       61 allrhhragt lrgpltrllv lgtvpgvvvg avirvfavpg psvfrlliav lllplggwlc
      121 lrtlrrasrt aparepsara vtrlamavgv aggiygiggg sllgpilvgr gmqvakvapa
      181 alaatfvtsv vgagtyalls lsvtgdiapy wslglacglg glcggylgar lqprlpetal
      241 rlllgvlalg vgglyavqll r
//
LOCUS       WP_457655327             253 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655327
VERSION     WP_457655327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..253
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26892
     Region          1..101
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(49,52,56..57,66,86,90,96,100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrigeiaalv gvtsravrhy hhigllpepa rqangyrayt vrdavllari rrlteiglsl
       61 devrdvladd agrelaevlg eldadlarqe reiqerrqvl avlleaplsp dgpflspala
      121 allekapatg spaaakdreh ltlldaaggg agaevfaalr plaedpgvla lyerldelag
      181 agvddpriap laaelvaavp devlavipdg epspsgfgrv llddyppaqr evvrrvmval
      241 aervrlrvhr gtp
//
LOCUS       WP_457655329             208 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655329
VERSION     WP_457655329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21431
     Region          29..75
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          89..187
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mtsdgpaadg vepgmvrpgg rtarvreavl raagdalveh gfdgldladv arraevgktt
       61 vyrrwsapag lvadllsdma eqslpraetg slaedlrana rlvvrtltdp rqgalfaavi
      121 aaatcdprta dalhrfyavr igewsgcvee avgrgevpvg tdpgeviaav saplyyrlla
      181 sgapldeaaa draadaavaa aragvfvr
//
LOCUS       WP_457655331             555 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces griseus].
ACCESSION   WP_457655331
VERSION     WP_457655331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..555
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61107
     Region          53..554
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtaaqtimtp nqstranelr aaarflrpgv grrrfltatg aaaalafavn lpaagtasaa
       61 eldsrrited pftlgvasgd phpgsvliwt rlaprpyepg gglpgarvav rwevarderf
      121 rrverrgtvt ahpefahsvr aevrgldagr iyyyrfrtgg wtspvgrtrt apapgarnss
      181 ltlaavscqa yhdgyftahr hlaaedvdvv fhlgdylyey avtatggarn ytdrtlpahy
      241 nretqnledy rmryalyksd pdlraahaah pfvvtwddhe tennyaggip endvppeefl
      301 lrraaayray wenqplrtpq rptgpdmtly rrlrfgrlaq fdildtrqyr sdqaygdgwr
      361 tpgpesedpa rtmtgatqer wlidgwrasd atwnvvpqqv tfarrrdvpa dayklsmdsw
      421 dgypasrqri lagaeaagve nlmvltgdvh vsyafdlkkd vddpasrtvg teivttsvss
      481 gkngadrpan wenqtranph lkhyngrrgy avvtlgaeea radfrtvaav ttpgaplata
      541 asfvteagnp gltpv
//
LOCUS       WP_457655332             331 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457655332
VERSION     WP_457655332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35007
     Region          3..247
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgetvrwgvl atggiaatft advqklpdae vvavasrtea sarafaerhg igraygswae
       61 lvaddavdvv yvatphsahh aaaglalrag khvlcekaft lnsreavelv elarerglfl
      121 meamwtylnp vvrrltelvr dgaigeirtv qadfgfagdf apghrlrdpe lgggalldlg
      181 vypvsfahll lgepdriqad allspegvdl ntgmllgwes ganallscsi vghhptaatv
      241 igtagridip rdffhpdhvv lrragaepet itsgpgpqgl sgmqyeaaev mravragete
      301 splvptagsl avmrtldavr drigvrypad r
//
LOCUS       WP_457655333             360 aa            linear   BCT 27-JAN-2026
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457655333
VERSION     WP_457655333.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=36947
     Region          86..357
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrisqdfapr gpdtgraarr rpargraaaa ltaavafalv ltgcgggdgp apksasgkss
       61 adadrvepla appapklpvt vdsadgtkvt igstdrivpl tgslseivft lgfgkqvvar
      121 ditatfeqae klpvvtrahd vsaesvlslk ptivladttt gpseaidqir dagipllvve
      181 pakglddvgr ridtvaealg vpsagtelke rtekriadvq ksipdyadgk kprvaflylr
      241 gsasvyllgg aesgasslle aagavdagke sglnkdftai tsealakaap daillmtkgf
      301 esvggmdglv kipgiaetpa gmdrrvvtvd dgvllnygpr tdrvlteive qlyakggkgr
//
LOCUS       WP_457655346             499 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655346
VERSION     WP_457655346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..499
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51574
     Region          13..412
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,273,276..277,280..282,285,313,317,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mdhrhvlrsl sgllivlfva misstvvsva lpqiigsldg tqsqytwvvt atllastast
       61 piwgkladlf skklllqiai gifvvssvac gfaqsteqli afravqglgm galqvlvqvi
      121 iaamispker gryngylggv mavatvggpl lggfitdasw lgwrwcffia vpftllasvm
      181 lartlhlvev rrpdtkvdyl gasliaagvs llllwvtfvg ddfgwlswqs almvggsvvi
      241 ltaavlvear vgepvvplhv vrrrdpalai vaslavgmam fggavflgqy fqigrgyspt
      301 eaglltiplm agvlvsstva grlvsktgkv kpfivagvvv lalgflglsf idhrtslvlv
      361 sagmlgvgag vgmsmqnlvl vlqntvplse igaasgaitf frslggtmgv svlgavlahq
      421 vankiadglt klgidpaasg sggstlnvaa mppevqdvvr aaygeatghi flisagiavv
      481 gviaslfltp tklrdsvdl
//
LOCUS       WP_457655339            1162 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655339
VERSION     WP_457655339.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1162)
  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 1162)
  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   3  (residues 1 to 1162)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1162)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1162
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=123684
     Region          1..240
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          161..1108
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrycilgttr alrddgtava lggarlrall tvlalhpgrt vpagalvdev wdgdppadaa
       61 galqalvgrl rralgrsave svaggyrlaa ppdavdlhrf erlagegsra ladgdaasal
      121 avlgealalw ngpaladlpd rtatasrwea rrldarraaf gallalgrpe aalpelaalc
      181 dahpldeplq vlritalrda grpaealaay eevrtllddr lgtapgpalr alhadllhqe
      241 paepnpsgrt gpglpgpaap epagptgegr aldpaqapta qapappapts paqaspvsap
      301 pppaygnlra rltsfvgrdt diatlredlg rarlvtllgp ggagktrlsq eaaeaaaeaw
      361 pdgvwlaela pvddpdivpe avltalgare tvlrgagaee lratdrtgad plvrltehca
      421 prrmlllldn cehvvgaaaa ltdhlltrcp qltvlatsre plgvpgefvr pveplpdpma
      481 lrllaergaa arpgfrtdad eataaacaei crrldglpla ielaaarlrm ltprqiadrl
      541 ddrfrlltng srtvlprqqt lravvdwswd lldaaeravl rrlsvfaggc slaaaeevca
      601 lpvpadgvtv daldvapllg slvdkslvva apgddgemry rlletvgeya aerldeaaer
      661 daverrhlth yrelaritgp kvrgagqlaa iavfqreyen lrsalrhava vrdehealci
      721 vlsmawywml rdlrsdarqw gewagslgpd pfaapgvrap slleratdrp ppmddeqlae
      781 arrgvaliql sgvddaistw ttpegkarlr iiadtyrpgm pqtcrmpgtl wifailltgd
      841 mdrlhrllde tvratrvygy ewelgsalht ranllsnnpe lvadaradad esleiytrlg
      901 ddwgaaeals argeanerag eflaalddyr aaveyarkig aqsqvgllra ryagalield
      961 rlpeaeeilr dvtgnsrqsg heatpmarmh lvfvlglqgr vdeareeael vradfrsrdv
     1021 aifggfvfgv lawldnldgd hasaldnalt alagarepls mmvapqmpsa hltaiaqala
     1081 gfggadaakd aarllafqat llpkahvpsv mearnlvlad ravrarldde aaftaayaeg
     1141 ggltldeata laetyrrahp pa
//
LOCUS       WP_457655347             296 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457655347
VERSION     WP_457655347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          35..95
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          110..268
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msvvedgteh gndavdepgw evdpddesga avvaavgrqi ktwreaaglr aaelgsllgy
       61 gedliykveg gsriprpefm davdvavgag gklaamkpdl aevrypkkir dlakleakav
      121 elaaygshnl hgllqteeya rallgtrrpi ltpdelerav agrmarhsif drspapqlgf
      181 vqeeaslrrp iggraiwrrq lenllrigel pfvdiqvmpt srwdhagtgg riqvlkfadg
      241 savgraddef agrpishpkq lrilervfca dnsagrgits rahgsltpgs yrappe
//
LOCUS       WP_457655352             744 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457655352
VERSION     WP_457655352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..744
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77489
     Region          13..704
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 matflyklgr ltfrrrgfva liwvallava gigaatasta tsssfsipgt eaqrafdlle
       61 ernpggsadg atarvvfqap egekvtdagn kreisgivke lqsgsdqiaa vadpfqqqav
      121 srngstayis vsykvnsmel tdatrdaled agkeaqssgm kveiggdalq vmphtgtaei
      181 igvviaaivl vitfgsliaa glplvtalvg vgigvstita lasvmdlgst tsilammigl
      241 avgidyalfi vsryraelae grereeaagr avgtagsavv fagltvvial aglavvnipm
      301 ltkmglaaag tvaiavlial tlvpaalgfa gkrimgrkar kaaeaekspd akpnmgtrwa
      361 rfvlrkpvwv mlvgvlglgi iavpaaslem glpddgaqpk sttqrqaydm lsdgfgpgfn
      421 gplltvvdtk nssdgkaaad rvaeeiealg vsavippvfn kagdtatitv ipkdrpssha
      481 teevvhdird agkdikadtg aevlvtgata mnidfsqkmn dallpylalv vglaflllml
      541 vfrsilvplk aalgfllsvv aalgavvavf qwgwlgslfg veqtgpimsm mpifmvgvvf
      601 glamdyevfl vtrmreayvh gespgqaivt gfkhgarvvt aaavimmavf sgfigsseqm
      661 ikmigfslai avffdafvvr maivpavlal lgrkawwlpr wldralpnvd vegeklqkql
      721 tdehgsgqgs gdgggegere lvrv
//
LOCUS       WP_457655351             156 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655351
VERSION     WP_457655351.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..156
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16800
     Region          70..148
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 midhghtdkt grpvtlhavd adnwravads aprddqrdwv palaarylvl ssredtwhsl
       61 avlagdrvtg himwgrdeed gsywiggmli daahqgtgig gaavrtlaaw lsaredstav
      121 rlsyapenea aahlytalgf rptgveedge vvaelr
//
LOCUS       WP_457655353            1134 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655353
VERSION     WP_457655353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 1134)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 1134)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 1134)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 1134)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1134
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=122376
     Region          2..1116
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 msddvaylrf phlhqdllcf aaeddlwvap laraghrper awrvtvdrtr vshprfspdg
       61 asiayttwrt ldpeihlapv aggparrlty wgstdarvcg wspdpgeacq ilavsshnqp
      121 fsyfswaysv ptdgspggrl pwgpvsdiav adidgerrtl lltgtpphep aawkryrgga
      181 mgrlwlhger llpdidghla npmfvgrria flsdhegvgn lysclmdgtd lrrhtdhdaf
      241 yarnassdgh rviyqcagdl wlvedleapd atprklevrl ggprtgrrvh qvpaassvds
      301 lsvdetgras avtvrgslyw lthrdgpart iadtpgvrvr lpemlgsggq vayvtdadgp
      361 daveiaylpr asgdrpprrl atgqlgrvqe misdpdgerl aiasndgrll lldtaepeae
      421 aaepletaek ppsgstradl haatgaaapd saapvdehpg ltelirsvng pvrdlafspd
      481 gdwltwshpg vgrslrqikl arisgpgapv ivdvtngrfe denpvftedg rylaflswrg
      541 fdpvydvhtg dlsfplgcrp ylvplssatp spfalspdgr paaggldpvd vpeagstgeg
      601 stvmvefegl esrvtpfpvs askysalapv sggglvwlrw pisgalgetf anpadmsgrp
      661 tlehfniaka rkaelvdhld wfavsgdatr lvvmddgelr avpatepgds dstvyldlrr
      721 ilhevdpgae wrqaygeagr iirsyfwepd mcgidwdgvl dqyrplvqrv aspdefadll
      781 revlgelgts hayvsparrn egpphyqrai gllganlvcr dgawvlqril pgdssdskar
      841 splagtgire gavlthvdgr pvdpvtgpyp lltaaggttv eltfspaggg psrrvaimpl
      901 iderplryqd wvakrrdvvr elsggkcgyl hipdmggsgw aqfnrdlrle vsrpalivdv
      961 rgnagghise lvvekltrti lgwdltrnaq avsyasnapr gpvvaladea tssdgdmita
     1021 afrllklgpv vgqrtwggvv gmtgrhrlgd gtvitvpmna awfdtygwsv enhgvepdve
     1081 alrtpldwae gryavlddav rlaldllaah paatppsydt apdlrrpplp prna
//
LOCUS       WP_457655356             782 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces griseus].
ACCESSION   WP_457655356
VERSION     WP_457655356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 782)
  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   3  (residues 1 to 782)
  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   4  (residues 1 to 782)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..782
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=82841
     Region          9..244
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          241..653
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          662..773
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mapgsddpld vghsaglvvd asgtilrctp aaesllgrsa aelhgrrlqd llaapeswpt
       61 vleqrdgpvw qgravlapsl ggevefrvlp ltgegpdgra reflvlaaph vlvaqwrqgh
      121 aflrelflqd riglavfdne lrlvrtnthl lpypgvpdel ygarlgdflq eadarvidtr
      181 lrnvlttgip ligfdvtvht rvepgagrtm slsvfrlqga dghviggtgl fvdvtdqkls
      241 rfrldllhra ttvlstnlsa eesardladv lvpaladvav vdvaeavfty depapedhgd
      301 hvvrrtatag avpdgfatga vfevstggtl sdrmwsdrae egaepadtlg rphgmsawlr
      361 argsllgrir vgrgpdrppf taedldllae iasraalvvd narrytrern aavglqrsll
      421 pspttdtatv htasvylptd tatgasgdwf dviplssarv alvvgdvvgh glqatatmar
      481 lrtavrtlad ldldpdellt hlddlvsala idseddeaaf gsfgatclym tydpvtrqcl
      541 vasaghpppa lmdpggsaah idlspgpplg vgglpfepva feaadgsvla lctdglitrg
      601 hadpdagmta lrhalsaalv sgrsleeigp evvgelvprp laddvtllla eargvrardh
      661 aswtlaadpa vvsearahvl gqlslwgldd lafttelvas elvtnairya ggtiglrlir
      721 aaslicevsd vsntqprmrr arateeggrg lfliaqltdr wgsrytrsgk tiwteqalpp
      781 sp
//
LOCUS       WP_457655358             503 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces griseus].
ACCESSION   WP_457655358
VERSION     WP_457655358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..503
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52317
     Region          24..495
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mssahsatsp aarlrdlkpd wisdpkvwrt evlaglvval alvpeaisfs iiagvdpaig
       61 lfasftmavv isvvggrram isaatgaval viaplnrehg lgyliaavil agvfqvalga
      121 lgvaklmrfi prsvmvgfvn alailifmaq vpemtdapwp vyplivggla lmvlfpkitt
      181 vipaplvsiv iltaitvgat iavptvgdkg dlpsslpvpg lpdvpftldt lttiapyafa
      241 malvglmesl mtaklvddit dthsdktres vgqgianivt gffggmggca migqtminvk
      301 vsgartrlst flagaflmvl civfgpvvsd ipmaalvavm vmvsfatfdw hsiapgtlrr
      361 mpagelavml itvacvvtth nlavgvvvgs vtamvvfakr vahlaevtav tdpdrttvvy
      421 rvtgelffas sndlvgqfdy andpdrvvid lssahiwdas svaaldaiea kyaqrgktve
      481 itglndpsah lhdrlsgela agh
//
LOCUS       WP_457655359             914 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces griseus].
ACCESSION   WP_457655359
VERSION     WP_457655359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 914)
  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 914)
  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 914)
  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..914
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..914
                     /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=100750
     Region          43..914
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mpanttassg psdakkpgrk kgrrarlivl vlvlalvagv gygaywsvst vrasypqttg
       61 smtldglsgd vevkrdsygi pqiyadsdad lfraqgfvqa qdrfwemdvr rhmtsgrlse
      121 mfgsgqvetd sflrtlgwrq vaqkeydevl destkknlqs yaegvnaylk gkegrdisve
      181 yaalgftndy kpgewtpvds vawlkamawd lrgnmqdeid rslltsrldk dqiedlypgy
      241 pykknrpive qgaispvtgk fdpeatpsdn vgsatpegat eglntqlsal sdtldeipal
      301 lgpngngigs nswvvdgkht tsgkalland phlapmlpsl wyqmglhcre lsktcqydta
      361 gytfsgmpgv iighnqdiaw gltnlgadvt dlflekvsgd gylydggtkp fktreetikv
      421 aggrdrtitv retnngplvs drskeldkvg qkapvsnaap dradgyaval kwtalepgks
      481 mdavfalnra kdfatfrkaa eyfevpsqnl iyadtegnig yqapgkipvr segydgtlpa
      541 pgwdpkyawk gyipfdelpy eynpdrgyiv tanqavidek kyphlltkdw gygarsqrin
      601 dllaqkikgg ekvstddmqk mqmdnfseia allvpelkki nisdpsvrea qkllegwdyt
      661 qepdsaaaay fngvwrnilk lafgnklpke mrvkgdclnv ppaknsgpvd qqkklvrecg
      721 qrdgdtaqpd ggdrwfqvvr dimddpdnew wkapargred alesrddlfa ramedarwel
      781 taklgknist wswgrlhrlt lknqtlgteg pgllqralnr gpwnlgggea avnatgwnaa
      841 sgyevvwvps mrmvvnvgdw dksrwinlsg asghafnahy tdqtekwvdg elldwsfgte
      901 avdastvdtl tlkp
//
LOCUS       WP_457655362             775 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces griseus].
ACCESSION   WP_457655362
VERSION     WP_457655362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     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=85222
     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 cgmylrvdqg gkvfgveprn hdinrmrlcp kginayqqvn hpdrltaplm rrsrdeefre
      121 vswdealdft vseirriqqt hgndafgllg gaslfsekty lvgkfarval ktrhvdyngr
      181 lcmvsaagan klafgidrag npfsdilltd clliagsnvg ecfpvmtqyv wgardrgasl
      241 ivvdpretai artadihval kpgtdsafft svlhvvieer ltdesyldgh atgwdevkak
      301 aaeyppsraa aicgipaeqi vqvartfara pkamawharg iehhsqgven clsvinlcta
      361 tghigrpgag ygtitgqgng qggrehgqks dllpggrsim neehrrqice iwgieeselp
      421 pagtsmmemv wqmqrreirg ligicnnpfv slpnyrvvke gydatefhaq fdfflsetaa
      481 nahvvfpvtt waedegvman aearvvkhnk aqdpppgvrt dtwaicelar rlgagdkfdf
      541 pdsrsvfdel rvasagtvnd yygityerle etggiawpcp ttdhpgtprl fedgktyhpd
      601 gkihlqvvew hppmdpydde hpmslttgrt vahflsgnqt rrlgalveqt prpwaeihps
      661 hgfrngepvr vvtrrgsevf palvteairp dtvfvpyhwp vptaanalti daldprskip
      721 eykvcacrie haeridevpa ppvapghvay petqvsrtdp lpptapqgrg tsers
//
LOCUS       WP_457655363             360 aa            linear   BCT 27-JAN-2026
DEFINITION  P1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655363
VERSION     WP_457655363.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Bompard-Gilles,C., Villeret,V., Davies,G.J., Fanuel,L., Joris,B.,
            Frere,J.M. and Van Beeumen,J.
  TITLE     A new variant of the Ntn hydrolase fold revealed by the crystal
            structure of L-aminopeptidase D-ala-esterase/amidase from
            Ochrobactrum anthropi
  JOURNAL   Structure 8 (2), 153-162 (2000)
   PUBMED   10673442
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..360
                     /product="P1 family peptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35435
     Region          10..350
                     /region_name="DmpA"
                     /note="L-aminopeptidase/D-esterase [Amino acid transport
                     and metabolism]; COG3191"
                     /db_xref="CDD:442424"
ORIGIN      
        1 mtredrtpar pplldaltdv agirvghaev agagalsgtt vvlapeggav aavdvrgggp
       61 gtretdaldp rnlvqrvdav vltggsaygl daasgvmawl eergrgvrvg agptqvvpvv
      121 paaalfdlgr ggdwrarpda stgraaveaa aatgsgepva eggvgagtga vagqlkggig
      181 tastrlasgv tvaalvavna agsvvdprtg vlfgeygage ppahppaevh aaaerrlare
      241 rmaaeeaggg vppfnttiav vatdadltra qaqklagtah dglaravrpv hlltdgdtvf
      301 tlatgrvpva pgdpvavnei laagadvlar avvkavraar stegtggrll sytelyggra
//
LOCUS       WP_457655365             582 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457655365
VERSION     WP_457655365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..582
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=61535
     Region          64..577
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mphtvpspdp gaadaaelar raarieaalt apgapfavvi gergtpeyad gprtlwefve
       61 ttwaygdapf liagertysy geffaaasal avrlrerygl rsgdraviam rnhpewqiaf
      121 waaqlaglva vplnawwtee efgralddce pgvllvdger lgrvagwarr tgayvvlfhg
      181 agrtaeglrl dryeefpapd plaappdvep rpeddatily tsgttgrpkg avatqlaqag
      241 aalnpryhaa asalargvip gqgpapvslm tfpffhvaaf tgfyaamaag galvlmhkwd
      301 adealrlirt hrvthfsgvp atglqlleaa eragdgdalg glglfstgga apppalvarl
      361 tarygtrvep rngygltets ggvlahfgde yraepggagr ptpvtetria gpsgdelpdg
      421 eagelwlrgq slfrgywrdp aateeafadg gwfrtgdlav rsegrisvvd rikdvvirgg
      481 envscveveg vlhdhpdvad aavlgiphpv lgeevaavvr pragavvtae dlrehvggrl
      541 aafkvparvl fteqplprna tgkllkhrlr vlleaaapvt ga
//
LOCUS       WP_457655372             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655372
VERSION     WP_457655372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20702
     Region          6..196
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 maaplpdrrd liadtaiatv aaaglrglth ravdtaaglp agstsyyfrt rsalisacyl
       61 rlatltvtdv drweerhgvp dpdsaaeala allhhwlteg rdrqlarfel sleatrrpel
      121 ragletagra araraaalla slgapdpeqa adllvawtdg llydriagap aasrpapdpa
      181 eltlvvrrml tallap
//
LOCUS       WP_457655370             288 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655370
VERSION     WP_457655370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=31886
     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 mlerlneamd hiedhldetv daaelariam tseyhfrrmf salagiplse yvrrrrmtla
       61 gaevlsgert lldvavrygy ssgeafaraf ravhgvgpge arrtgaalhs qplmsfrliv
      121 egsssmryrv vekdrfrlvg rgtriplvye gmnpaivefv ksigketlgr weehatgepd
      181 gvvaavsnhs aedaegteld yfhgvvsete vpgasealdi epglwavfes sgefplavqy
      241 lwrdvytqwf psnpyrsrpg pslsrtrvse dgthadaevw ipveragd
//
LOCUS       WP_457655373             281 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655373
VERSION     WP_457655373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30137
     Region          17..262
                     /region_name="F420_Rv2161c"
                     /note="probable F420-dependent oxidoreductase, Rv2161c
                     family; TIGR03619"
                     /db_xref="CDD:274680"
ORIGIN      
        1 mristtiflt detvtpvrla releqrgfgg lylpehthip vsrrtpypmg gelpreygrt
       61 ldpfvalgqa aavterltlg tgitlvaqhd pidlakqaat ldhlsggrft lgigygwnve
      121 eaadhgvewa trrdlgrdrm almralwade ptgyagafgs vqpseahpkp aqrprgpvng
      181 prtligggag pklfahiaey adgwlpiggg glteslpklr aayeeagrdp kdlqvvpyav
      241 lpspgklghy aelgieevvl qlppaaepev lrtldayaay l
//
LOCUS       WP_457655376             296 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655376
VERSION     WP_457655376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  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
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32086
     Region          8..292
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 masyatgfge egsawiaelp slatdmldhw qlrrdgavrs gqaslvlpvl rhdgtravlr
       61 lqmpreetaa aliglrtwng dgtvrlldhd pasgsmller ldaartlasv ddddmamgil
      121 aglharlval rapqglrglg dvaaemleqa pqavaqltdp adrhllrgwa savaeladdp
      181 gdrllhwdlh ydnvlaaqre pwlaidpepl agdpgfdlwp aldsrwddvv vaqgeplrvv
      241 rrrfdlltea lgldraraag wtlgrllqna lwdiedgetr lapsavvmae algshr
//
LOCUS       WP_457655381             302 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655381
VERSION     WP_457655381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..302
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32414
     Region          26..273
                     /region_name="F420_Rv2161c"
                     /note="probable F420-dependent oxidoreductase, Rv2161c
                     family; TIGR03619"
                     /db_xref="CDD:274680"
ORIGIN      
        1 mqlpvqsqsv iyaepweaaa tpadlvriar aadrggfayi agcdhvaipr rlaegmstvw
       61 ydpvatlsfl agvtervllm shvavvglrh plitakqyat ldhlsggrli lgvgaghvre
      121 efeavgadfd grgrvldesi dalraalgpe eypeftgerf sfgglgqlpr paqervplwv
      181 ggsspaavrr aavrgdgwlp qgdprdrlpa qiarlhalre eagvgapivv gaiteplyvg
      241 epawsvgrrt lkgkpevlae slreyaaigv hqiqvrfrsr svdeltdqmt afgadvaphl
      301 dr
//
LOCUS       WP_457655382             661 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655382
VERSION     WP_457655382.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 661)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..661
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67907
     Region          56..334
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          375..651
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mataqatgar avpagarrgp vaalrdrpaa akllllalva avvvpvvhgr wgggvwpdal
       61 tadlsaplgd vtdwivsnrd shplflyffg hisnavvlsv rgvylvllal gwagvtvfaa
      121 avawrvaglr laltaavsfl vcgllgmwvp tmqtlalmvv avlasvvlgl llglaaglsd
      181 rvfrilrpvl dtmqvlpafa yllpvvlvfg igvpgavlat vvyaappmar ltalglrgad
      241 sgvmeavasl gatgrqrlls arlplarkel llglnqtimm alsmaviasv igagglgdrv
      301 yqalssvdvg aalaagipiv llavvldrtt eaagrrigae ptgpaflrgw rgwtlaavvt
      361 aavavvgrat dgrvwpedvt vaiagpvnta kdwmvdhlyt gvpvvggtad lashftsgvl
      421 nplrsgltgl pwwsvlliva alawtigtwr taatavlama aigvlgvwep smdtlsqvla
      481 avavtlvigf gvavgaarse rlerllrpvl dvfqtmpqfv ylipvvalfg vgrapaaaaa
      541 vvyalpavir ittqglrgvd paamecarsl gatpgqqlrq vqiplarpsl llavnqavvl
      601 vlavviiggl vgsgalgyev vlglaqgdla tglvagaaiv clglmldrvt qpttrrqrqe
      661 s
//
LOCUS       WP_457655383             397 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457655383
VERSION     WP_457655383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   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 397)
  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 397)
  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..397
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..397
                     /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=42020
     Region          25..359
                     /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 mtgtqtieat epagnaaatg pdrnavfsvr nlwkvfgpka dripgsehaa lppaelreat
       61 gctaavrdvs fdvrkgevfv vmglsgsgks tlvrcltrli eptsgtlsid gedvlamdra
      121 rlrelrrhra amvfqhfgll phrtvldnva ygleiqglgk aerrakaael vakvglagle
      181 drrpsqlsgg qqqrvglara lavdpsvllf depfsaldpl irremqdevv rlhreegrtm
      241 vfithdlsea lrlgtrialm rdggivqlgt peeivgspan dyvrefvrdv preqvltvat
      301 amrpalages ergpavrpda tvseaieavs rsgdpaarvm dggrlvgvvd haclldvvag
      361 tsgpgeattt atapgastvt dapdapdapd gsrevtl
//
LOCUS       WP_457655389             417 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457655389
VERSION     WP_457655389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 417)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..417
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45496
     Region          29..416
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(63,70,99..100,107,111,118,248..249,252,256..257,260,
                     293,298..299,302..303,305,328,357..359,362..363,365..367,
                     371)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(70,92,95,98,100..101,187..188,197,247..248,251..252,
                     256,299,302..304,406)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mncphaeaaq adrnagviti dpmvqdldge tarlrdagvl aridllgvpa wtvtrhaear
       61 qllvdprlvk didawglwqs gvvtrawpli gmidagrsmf tvdgsehrrl rtktsqaltp
      121 rrleairpdi ekfteellda ldaaqgedgv vdlkavfaqp lpmkvvgmlm gvdesqhaml
      181 trqykaffsm ltpqderlal laeldvfytd lvrektarpt ddltsalila eeggdpltee
      241 evvgnlkamv aaghettigl vlnavralls hpdqlravla geigwdavve etlrwdtptt
      301 hllmrfated lavgdevirk gegvvisyra igrdteqhgp dadafditrp trnrhmtfgh
      361 gphicpgaal srveagialp alfgrfpglr lavpdeqitk lpvmtqndma afpvllg
//
LOCUS       WP_457655393             334 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655393
VERSION     WP_457655393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..334
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37543
     Region          4..317
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mprpftlftg qwadlpleev crhardfgyd glelacwgdh fevdraladp gyldsrhqll
       61 dkyglkcfai snhlvgqavc dhpiderhqg ivpariwgdg epegvrqraa aeiadtaraa
      121 aafgvdtvig ftgssiwhlv amfppvpphm iergyedfae rwnpildvfd aegvrfahev
      181 hpseiaydyw ttkraleavd hrpafglnfd pshfvwqdld pvgflydfrd riyhvdckea
      241 rkrldgrngr lgshlpwgdp rrgwdfvsag hgdvpwedvf rmlrsigyeg pvsvewedag
      301 mdrlhgapea laslkrfdfd ppsasfdaaf ggge
//
LOCUS       WP_457655394             599 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces griseus].
ACCESSION   WP_457655394
VERSION     WP_457655394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..599
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64826
     Region          10..598
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 maaapqvggl advvfdyaed dphrvalgrk daggqwrdvt sgefrdsvla lakgliahgv
       61 rfgdrvalms rtryewtlfd falwtvgaqs vpiyptssae qvlwmlhdae vvavmvehed
      121 hsmtvgsvid rlphlkrlwq ldagavdelv aagagiddev vqrhrravtp dsvatviyts
      181 gttgrpkgcv ithasfmfes dtmvtrwepv fhskpgdeaa tllflplahv fgrmveiaav
      241 rgrvklghqp elsanalmpd lmtfrptfil avpyifekvf ngarrraeae gragpfdkav
      301 diavkyaeal eqkafgdgpg psaglrmqhq ffdkvvykkv rdamggrvrh amsggsgmdr
      361 rlglffagag vtvfegyglt estaaatanp pertrygtvg qpipgtsvhi addgevwvhg
      421 pnvfsgylgn paatrsvlqd gwlatgdlga ldedgyltit grkkeilvts ggksvspagl
      481 eervrahplv aqcivvgndr pyiaalvtvd qesvehwltm qgrtplgpad lvrdpdleme
      541 vqravvaant avsqaesirt frilahpfte elglltpslk lkrkaietay avevdalyh
//
LOCUS       WP_457655395             823 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655395
VERSION     WP_457655395.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..823
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84706
     Region          75..460
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(76..77,80,111,161..162,164..166,169,189,192..193,
                     196,285,324..325,328..330,333,361,365,418..419,423,427,
                     443,446..447,450..451,454)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          413..>807
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mvggitlvkd epdgtgpdgp tsdgtaatve lpaapppppp ptgpapgpsa aeisprqvrm
       61 vflglmltll laaldqmiva talpkivgel hglekmswav tayllastiv lplygklgdl
      121 fgrkgvfqfa ivvfiigsal agwsrtmdel iafralqgig ggglmigvqa iiadivpare
      181 rgrymgliga vfglasvagp llggfftdha swrwcfyinv pfglvtlavi avvlklprpa
      241 vrprldvlga vllavastcl vlvtswggte yawgsrtila lsagavltta lfvlaehraa
      301 epiiplrlfr dsvfnvtglv gavvgialfg aasylptylq mvdgvsates gllmlpmmmg
      361 ivggsvvsgq litrtgryri ypilgsavsv vgmgllslle adtsplvysf yqavlgigig
      421 lvmsvlvlav qnsvrpsdlg tatsannyfr qiggsvgaai fgtlfagrls dalgvrlptg
      481 aelpdpesit pqivhamepa lrdayiqayv dampriflyl vpvlvlglvl afflkekplv
      541 shhspeaaae ptttqipaar adsgrpatgy lsgvpvhgsv qhpdgttvsr aaltlidvqg
      601 qqvgrgasge dgryalsvpg agsyvliaaa gghqpqavsv tvgerpveld vvlggagrla
      661 gsvltpdgap vpdaavtltd vrgevvastr tgreggyvig eliageytla asapafrpaa
      721 lpvsvqaare trqdielagg avlrgvvrat ggrpvedarv tlldaagnvv dtlttgadgs
      781 frfvdlssge ytviaagypp vatvlqvagg grterdlqlg hed
//
LOCUS       WP_457655396             130 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457655396
VERSION     WP_457655396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13843
     Region          7..125
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 maskftelai dcadpaalac fwcavlgyev qdadeddgvv migspevpeg ksrpgpvppa
       61 ltfarvpegk tvknrlhidv nptdreqgee verllalgar radvgqgdah wvvltdpegn
      121 efcvlgtrcp
//
LOCUS       WP_457655398             528 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655398
VERSION     WP_457655398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..528
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56727
     Region          117..336
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          392..484
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mtkragilva vgatvagllt aapgpaaatp astppapklk wtdcptesyp tlqcakvrap
       61 ldhrrpsgrq itlalsrvph takkfqgpll vnpggpggsg lsmagfvass lpkkvaaqyd
      121 vigfdprgvg kstpalnclp ghfdpvrpds vptsyraeri nrdraesfar acgekhgdvl
      181 pymdtvsaak dldvirralg srqinyfgys ygtylgavya klypervrrl vldsvvdpdd
      241 vwyegnlgqd yafddrhkaf aswvaqhdaa yglgtdpaav eaawyrmrad varepaggtv
      301 gaseledtfl pggyyngywp ylaeafaayv knrdaealve vyenfgavda sgdngysvyt
      361 avqcrdagwp ehwstwrnds rrihkkapfm twnntwynap canwpvaplq pvpvnnrqlp
      421 palilqatdd aatpyggavs mhrklkgssl vveegggnhg itlsgndcld ehltayltdg
      481 tvprgrgead avcaalpdpk plpaekaaaq svdnskgsrl hgllgfrr
//
LOCUS       WP_457655401             401 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457655401
VERSION     WP_457655401.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44056
     Region          10..398
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtrlaqtagl ndiqreilst vrdfvdkeii pvatqlehrd eypteivegl kelglfglmi
       61 peeygglges lltyalcvee iargwmsvsg iinthfivay mlkqhgtqeq kdtflprmal
      121 gevrgafsms epalgsdvsa isskgvkdge eyvlngqkmw ltnggtsslv avlcrsdegh
      181 pegtaphksm ttflvekepg fgevrpglti pgkidkmgyk gvdttelimd dlripanrvl
      241 ggttgrgfyq mmdgvevgrv nvaargcgva qrafelgvsy aqqrhtfgkp iaqhqaiqfk
      301 laematkvea ahammvnaar kkdsgerndl eagmakylas eyckevveda frihggygfs
      361 keyeierlyr eapmlligeg taeiqkmiig rrlleeyrsq g
//
LOCUS       WP_457655406             396 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces griseus].
ACCESSION   WP_457655406
VERSION     WP_457655406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  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 396)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 396)
  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   5  (residues 1 to 396)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41667
     Region          16..313
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msllrdttte prpdiqleal tlavsadlpv llwgepgigk taaltqlaas ldlplttvia
       61 svhepsdfsg lpivgddpae qgvpmappdw avrlvragkg llfldelsta ppavqaallr
      121 lvlerrigal qlppgvriva aanprssaad gwelspplan rfvhlqwthd hevvvrglag
      181 twpratlpll dpeklpeavd farravcgll sarptlvhrl pttetrrggp wpsprswdmt
      241 lsliafataa gsskevlsll vrgtvgdgpg lellasldrm dlpdpedlla gpagavlper
      301 gdlrqaaldg vvaavrtrpd rarwdaawal lvraletgap dlvvvpattl aalrqedwdv
      361 paaieqlagv vslsgradra aarvaakaks patvgr
//
LOCUS       WP_457655409             843 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655409
VERSION     WP_457655409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 843)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 843)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 843)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..843
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87278
     Region          2..843
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mfrtalrnvl ahkarllmtv lavmlgvafv sgtlvftdtl gnafrnqsak sydnvavsve
       61 tyagddeknp gideatleki rgldgvasat grvsgfagva dpdgkligng wsntganfap
      121 gkdgkdtqyv ftdgsgpakd gavaldkdta ekgkyrvgdp vrvatngpvk eytlagiftt
      181 edgavnaggs lvlfdtataq qlylkpgvfk datvtaagdv sdqklldeit pllpedataq
      241 tgkalaeqqa kdiesglngl ntmllafagi alfvgiflia ntftmlvaqr trelalmrai
      301 gatrrqvkrs vlleaafvga lasvigfalg lglatglrsa mgvmggkipa gplvvsptav
      361 isafavgili tvlaawlpar raakiapvaa mssvhatasv kslvvrnsig gviallgsag
      421 ivggaasggt sgrqlvaaga ffaligviil ipllsrpvia lvrpllkkvf gvsgklasqn
      481 avrnprrtga tasalaiglt lvtgisvlgv tlgqaidkmt tdnikadymv tmasgdtlde
      541 saltalskad gvsalspqqa awfevdgehh sasgvtpgdv ekvfslttes gslaslkdgq
      601 vavgsktaks ngwktgdtlp vkfddekkge ltigatyeen eflspfvipk qladqhsast
      661 rpeireiwik tdggasqane qsivdalgdn pamsvmdrqd irdmfggfin talnimygll
      721 amalliavlg vvntlamsvf erqqeigmlr aigldrgrvk rmirleavvi svfgavigvg
      781 lgvflgwaig rtlsgdipgy alvvpwdrlg iflllaglvg vlaslwpars aaklnmltai
      841 kte
//
LOCUS       WP_457655412             130 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655412
VERSION     WP_457655412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..130
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14277
     Region          8..126
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 msssqlrrfp rrrtsvgasr dfvvhvlrew qltdliddie lcaselatna llhgvppgre
       61 favrldltdd lvrlavrdsg dgrpeiqypd esscsgrglf ligelaadfg idhhvvgktv
      121 waafkrppap
//
LOCUS       WP_457655422             204 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655422
VERSION     WP_457655422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..204
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=22460
     Region          35..201
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 masvsselpg ertpladaae tglkivvvgg fgvgkttlvr svseirplnt eevmtqagvg
       61 vdetdgvdak ttttvafdfg rislnerivl ylfgapgqer fwflwdrlfs gtlgavvlvd
      121 trrmddswya idrlehhgtp fvvavnrfdd dhvhsldeir kalalpehip midcdarvrr
      181 ssknvlitlv dhlrtmaivr ettp
//
LOCUS       WP_457655432             798 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655432
VERSION     WP_457655432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..798
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86859
     Region          121..>354
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mgrrprpgsf wrraaavlgv lmvgagavvi lrsrptgdvd pfgalvgvvg avigvaglll
       61 pfwehrqsrr egavralvra veghedqqyr nilgpgsafl pvrfrftaap dgspdaagse
      121 ewrtvvdryl glpgpvrrla vtggpgtgks llareltral aarhdeaagd gvpvllslss
      181 wdgppdredp rsegfhlafr rwavqqaaqt ygqpsaqvee altdkavlvl dgldeldpag
      241 aearpraaal lrylavnrdc frhvvvtcrs dvyerfegpa plagagrael lpvppdmald
      301 ylksrsewsh sglterwdgv ldemrvspgg plaralstpw rltmtanafh vrgeggagwl
      361 rdpselvtrw grdvlweryr aesedfaaeh glpgrlwslf speerlrsae dspaadamss
      421 eaeeyllslf vpsvvaehpr dpdrypaerv sawltllsth rdvdrfagpr ylsliadlra
      481 dltphqlwpl ggrrlvrtlh gslytlfall vaglavvalr dplevalcfp vvvaagfsah
      541 lawsdradid pasrirmsgr agglldlymr tvgmpmlgvc sggmfgfivs anltraplpd
      601 vpttvwvata agallgipll qnrsaetytt vrgslpgqrh kiflicaals grlplrlgrf
      661 ldwaheggll rvdghayrfr hdefeqylwr shwrpeilpp claaadaalr tgeaaadrpa
      721 ragrrmleql dtldrnrvdl yatcmmsigi agarartalr awadhlatga vapeaeavlr
      781 dragqavrrf heaaarag
//
LOCUS       WP_457655434             401 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655434
VERSION     WP_457655434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40369
     Region          10..371
                     /region_name="MFS_FsR"
                     /note="Fosmidomycin resistance protein of the Major
                     Facilitator Superfamily of transporters; cd17478"
                     /db_xref="CDD:341031"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,133,
                     136..137,140,210,213..214,217..219,222,250,254,302..303,
                     307,311,326,329..330,333..334,337)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341031"
ORIGIN      
        1 mrrntpivll svghacvdvy qgcvaalvpf fiaeraysla vasgivlaas llssvaqpvf
       61 gvladrwamp wllpvstllg gagialsgls gsypltlafv alsgigvaay hpesarlari
      121 aaggshramg wfsmggtvgf alaplmvava maagglrwtp llvlpalaga alclpvvrvl
      181 qqrqtadgsg ttpaagsddv asfvklslav vfrsiafial stfialyarq rlgggtavgt
      241 aaltvlylgs tvgsvlggsl aarwdrvvva rwaylisvva vagvvwvpgp afylfvalts
      301 aglyvpfslq vtlgqdylps rvgtasgitl gltvsiggla gpavgslada tslrtalapl
      361 almpllswlf frslpepgvp raelaegaaa pssgggavka g
//
LOCUS       WP_457655435             286 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655435
VERSION     WP_457655435.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 286)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30491
     Region          50..141
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          204..281
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvrpgssval siicqmmpni rhaaagqaaa rpaavggata vrhspvaptr trrlapggsi
       61 dahrhddhqi vyagrgvltv ttdagswvap gtraiwvpag vvhahrayge ldlhlvglpv
      121 tenplgldap tvlavspllr elliaytrae ddgesperar lravlldqlr asdaqqplhl
      181 ptptapplrd lcailradpg dgrtlaelgr qvgagdrtls rlfrsdlgmt fpqwrtqlrl
      241 hhalillter tpvtavahqc gwssasafie vfrrtfghtp gshpae
//
LOCUS       WP_457655436             518 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces griseus].
ACCESSION   WP_457655436
VERSION     WP_457655436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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 11434433
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..518
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=55282
     Region          <422..502
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          422..450
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          454..480
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 maedreapdg tvvgvgnsvs gggfhapvvq tgtfsggvht yygppahssl ppvpewpqlg
       61 taepialgvr rtrrlpgesp lppyverdcd ralgsrvrea vrsgglvvvt gaplsgktrt
      121 awaalfsnls gttrifapsp gadlrglpal lrergeqvcv lwlddleghl gehglttavl
      181 aelvrlrvpv latmddgayd arrfgtadra rvlsgaepve lqrewsesel grlaasdqep
      241 rlraaaarhg vhtvpeylav gpelleewrr arrpdahprg hllvraaidl grcgvsrisa
      301 rallnaqely peeaaaaeae sfedalawaa dirhgvtgll slvpgvrpaa wsvfgslvad
      361 vegrpdappv ptgmwrfafv vapdkgerwa vrwraheelv pladtdpeip allghinavm
      421 gdvetamhwf rraadaghae saadigqllm grdaeairyl eqaaeagvvr aqyqlgmlla
      481 graqswltra aeaghttagr alpalrtvtd tppdtvea
//
LOCUS       WP_457655438             201 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457655438
VERSION     WP_457655438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  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 201)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..201
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21926
     Region          14..198
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtaesttahs srwpvppqdg ytvddlftlp dlpphtelid gslvfvspqr tfhstvidll
       61 vaglrstapp evkirremtv vldrrngpep dvsvvrsead tkgmeqtsya aadvllavev
      121 vspdseardr eakphkyata giphfwlvem tgtdqhpvvr vyeldpvtkv yaltgihhdr
      181 lktgvpfpvd idisaealaa l
//
LOCUS       WP_457655441             363 aa            linear   BCT 27-JAN-2026
DEFINITION  glutamate--cysteine ligase 2 [Streptomyces griseus].
ACCESSION   WP_457655441
VERSION     WP_457655441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Lu,S.C.
  TITLE     Glutathione synthesis
  JOURNAL   Biochim Biophys Acta 1830 (5), 3143-3153 (2013)
   PUBMED   22995213
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Franklin,C.C., Backos,D.S., Mohar,I., White,C.C., Forman,H.J. and
            Kavanagh,T.J.
  TITLE     Structure, function, and post-translational regulation of the
            catalytic and modifier subunits of glutamate cysteine ligase
  JOURNAL   Mol Aspects Med 30 (1-2), 86-98 (2009)
   PUBMED   18812186
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..363
                     /product="glutamate--cysteine ligase 2"
                     /EC_number="6.3.2.2"
                     /GO_function="GO:0004357 - glutamate-cysteine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016879 - ligase activity, forming
                     carbon-nitrogen bonds [Evidence IEA]"
                     /GO_process="GO:0006750 - glutathione biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0042398 - modified amino acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0052699 - ergothioneine biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39230
     Region          3..362
                     /region_name="PRK13517"
                     /note="glutamate--cysteine ligase"
                     /db_xref="CDD:237408"
ORIGIN      
        1 martvgveee lllvdavsge aralssavla laeknaagas afepelhrqq lefathpcad
       61 mgeladavhr wraeavrhaa dagtsvvama tsplpvspti gtgeryrwma ehygltaqeq
      121 ltcgchvhvs vasdeegvav ldrmrrwlpv llalsanspf wqgrdsgyss yrsqvwgrwp
      181 sagpvdvhgs aeayhdrvrs lvgtgalrde gmiyfdarls hryptvevri advcldpadt
      241 vllatlvrgl vdtaarewra gepppdidts llrvatwrag rsglegrlvh prtqrpepap
      301 dvlralldhv rdaledngdr esaesalaav hrrgngarvq rdilartgsl rdtvaacvri
      361 tag
//
LOCUS       WP_457655442             342 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655442
VERSION     WP_457655442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Nocek,B., Tikhonov,A., Babnigg,G., Gu,M., Zhou,M., Makarova,K.S.,
            Vondenhoff,G., Van Aerschot,A., Kwon,K., Anderson,W.F.,
            Severinov,K. and Joachimiak,A.
  TITLE     Structural and functional characterization of microcin C resistance
            peptidase MccF from Bacillus anthracis
  JOURNAL   J Mol Biol 420 (4-5), 366-383 (2012)
   PUBMED   22516613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Korza,H.J. and Bochtler,M.
  TITLE     Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with
            a Ser-His-Glu triad and a nucleophilic elbow
  JOURNAL   J Biol Chem 280 (49), 40802-40812 (2005)
   PUBMED   16162494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..342
                     /product="S66 family peptidase"
                     /EC_number="3.4.-.-"
                     /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=36420
     Region          13..328
                     /region_name="Peptidase_S66_mccF_like"
                     /note="Microcin C7 self-immunity protein determines
                     resistance to exogenous microcin C7; cd07062"
                     /db_xref="CDD:132883"
     Site            order(91..92,220..221,223..224,254..255,257..258,261..262,
                     296..297)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:132883"
     Site            order(114,247,313)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:132883"
ORIGIN      
        1 mpvrypsplr pgdrigitap ssgvpeelre rlavavreve argyavvtgr cmdgsghasa
       61 saadraaelt amltdpgira vvppwggeta idllplldwd rlreaeptwv vgysdlstvm
      121 tpltlltgaa tvhgnnlmdt pyrvpeglvs wldivaappg hrftqipper hratgrddya
      181 kqpdvrdfal dtpgrwtrld gggdvdvegr liggcvemla niagtpyldt safarahape
      241 gllvyvepgg hdafticrnl hgmrlagffd aadavlvgrt sapdmasltq hqavldalgp
      301 lqvpivadve cghvqpflpl vngararvvh tatrseltqt ld
//
LOCUS       WP_457655443             297 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457655443
VERSION     WP_457655443.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..297
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32224
     Region          1..248
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtihravvar vrplsatmtr vtfhgeglag fgstgvgdey vriflphgpd rtdvslprtt
       61 eqggwetpeg qpvapmrtyt iravrpeege vdidfvlheg gvasgwaaea rpgdvvgvnd
      121 ptglynppad ltwqvlvadq tglpaaarll entpdhvrtr vvleapdrsa vlplrelsds
      181 kvtwtyggng hgpsrladlv taavppgtdl aggyvwvage tnalrtvrry lrrelglpae
      241 rfkvvgywip nsdtwserye alpdavrsel ealwdnpagd sedltiryea rlsdlgl
//
LOCUS       WP_457655447             197 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655447
VERSION     WP_457655447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21064
     Region          7..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtartprkda vrnraavlaa adelfarses patitmadia aaagvgkatl frgfgdrtgl
       61 irelfatrle pirtavedgp pplgpgtaph rripalldav lclkldnrhl alaledtgda
      121 gpyraehyer whqdlremld ridgladsaf aahallaatr adlvehlvaq qgmtheeira
      181 hlarytaqvi gagapda
//
LOCUS       WP_457655448             312 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457655448
VERSION     WP_457655448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31422
     Region          16..303
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(46,256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(196,226,254,257..258,261)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtestvpgaa pdpgavlvlg ealvdlvpad ggsgvltaqp ggapanvavg larlggrpsf
       61 vgglgddafg grieawltga gvdlslsars alptalavad lgdhgntyhf hlqdtatfrl
      121 pdrapeaarf gavyvgglaa vvepaagvva ataratsrag llvvdpnvre drtldpvrsl
      181 drlrelcsla qvvkasdedl vrlwpdaape escrrlagqg rlvvmtrgar gatayvhdap
      241 avsvpalpvr vvntigagda fmagmltwlg aeagwdpals agrtkamley avgtaasvca
      301 ragteptapl gv
//
LOCUS       WP_457655453             286 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces griseus].
ACCESSION   WP_457655453
VERSION     WP_457655453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31298
     Region          1..265
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mhtavitpaa grhqhltlqh rglaagsrap dqyvvvamdd pelravvggr epvatvvdcp
       61 vtngnlplar arnlgaarav eygadllvfl dvdcvpgehl leryrqaald sehrrsllcg
      121 tvsylpppap ygyrlnelgg laephpgrpa papgelrrsg dhrlfwslsf avtaetwhav
      181 ggfceeyegy ggedtdygqr arvadvpltw vggapafhqy hpvseppvah lhdilrnaet
      241 fhrrwgwwpm tdwlkafaer glahrdpatg rwslgpepeh phdnag
//
LOCUS       WP_457655455             548 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457655455
VERSION     WP_457655455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..548
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57093
     Region          1..503
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mvdavvigsg pnglvaanll adagwsvevl eaqdepggav rsdrgvhpey vndlfssfyp
       61 laaaspvlar lelhrqglrw shapqvlahp lldgrcavld rdrsataagl drfapgdgdg
      121 wlglcdiwdr vgdgivsalf spfppvragt vlaarlraag glrlarslvl pvrrlgeeef
      181 ageggrllla gnalhadlap eaagsggfgw lmsmlgqfhg fpapvggaga ltaalvgrlr
      241 srggnvrcgq rvtevvvrgg ravgvrtesg eavparravl advsapslyg slvaaehlpg
      301 rllddmrrfq wdfatfkvdw alngpvpwss aaaasagtvh laegvdeltr casqiargla
      361 pdrpfllmgq mttadptrsp ldtqsawayt hvphtvkada gpdgltgrwg ageqqrmadr
      421 mearveryap gfrsrirarr ilapaflqaa danlhngain ggtaamhqql vfrpvpgtgr
      481 petpvkglyl asasahpggg vhgapganaa raairstrat taalsavqrl pahrgrtggt
      541 trvrgega
//
LOCUS       WP_457655459             144 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle structural protein GvpA [Streptomyces griseus].
ACCESSION   WP_457655459
VERSION     WP_457655459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10013202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..144
                     /product="gas vesicle structural protein GvpA"
                     /calculated_mol_wt=15591
     Region          1..137
                     /region_name="PRK09368"
                     /note="gas vesicle structural protein GvpA"
                     /db_xref="CDD:236485"
ORIGIN      
        1 mtlvqqsnat sggngsgnly dvlelildrg lvidafvrvs lvgieilkid vrvvvasvdt
       61 ylrfaeacnr ldlesgrkap sqltdlvgdm tenvakgksk galtgaveaf seslqgkree
      121 peeeprkrpa rkstssrqtq rree
//
LOCUS       WP_457655461             371 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457655461
VERSION     WP_457655461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..371
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40868
     Region          26..357
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mpqatatvad padesspgrp agahgaapgs dfapllravr dqdllerrtd ryvlgitanl
       61 valgalitgf vllgdtwwsl cltlpwavlw trtafvahda ghaqisgdrr tsrliglvha
      121 nlllgmneaw wndkhvrhha npnhidkdpd vgvgalvwtq kqaaqregfa rwltrnqarl
      181 ffpmlllegi alkiygfqfl rrqplrerav sallltahig lyaalllstl spgkaivfvl
      241 vlhalfglhl gmafapnhkg mempdpdger wghlqrqvlt srnvrgavlt dwflgglnyq
      301 iehhlfpsmp rpnlrlaqpl vkahcsaigm pytetglies yrqalshmhe vgeplrqggq
      361 tgnvperegv h
//
LOCUS       WP_457655468             399 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457655468
VERSION     WP_457655468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10145376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..399
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41492
     Region          39..385
                     /region_name="M20_ACY1L2-like"
                     /note="M20 Peptidase aminoacylase 1-like protein 2-like,
                     amidohydrolase subfamily; cd05672"
                     /db_xref="CDD:349921"
ORIGIN      
        1 mtvpaaprpe traeevadtv adkrmralrt avretvggha palldlsrrl haepetafee
       61 hkaaalcsel laahgfevta pahgldtafr atigsgpvtv aiaceydalp glghacghnl
      121 iaaagigaal glaphadelg ltvrvigtpa eergagkall ldagafdgvd aammvhpcpf
      181 emadfrsfal gtldvtytgr aahpslnphe grnaadaltv aqvalgllrq qlppqwrvhg
      241 ittaagtapn aipdrstaty eiralaaedl relrqrvedc fragalatgc evtlerpepd
      301 yldfrgdpel irlwtanare lgraepverp pfactdmgnv shvvpsihpv ldisggacgp
      361 heaafadaav spaaeqalld gavgmawtaa dfaaarasa
//
LOCUS       WP_457655470             262 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655470
VERSION     WP_457655470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27784
     Region          3..254
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 meirveqlta gyaghiavdq vdltvpsgqv vaivgpngcg kstllrsmar lhqprsgavf
       61 vgdadiwqlr qrdaahrial lpqapqapea vtvaglvryg rhphqglfrq wsredeeavt
      121 raleatgtaa lagrridqls ggqrqrcwla malaqetpvv lldeptsald ighavevldl
      181 vrevaaegrt ivmvvhdlaa aaryadtlva mrdgriiatg ppretvdaal vqelygieae
      241 iltatsdgap vvvptvrtpa aa
//
LOCUS       WP_457655476             394 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655476
VERSION     WP_457655476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..394
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42582
     Region          158..384
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 msmpmgyvas tavltwctff avvaprrprp lasmsfwfgl ginevpfmgl yllvgstvla
       61 gaegdlrspg akvtaavaav aaaglavsaw rgvrtdrvvg aalrqglgad wrervrvplr
      121 rhrpwarill lpalmwrrdv eripdirygp agrrnlldvy rhrgaprggp vlvyfhgghf
      181 tggaknrear pllyrlasqg wvcvsanyrl rpetsfpghq idakkviawa rehaadhggd
      241 psklfvagss agsnlaglca ftqndprfqp gfesadtsvt aaiclygyyg hyfgdrpdee
      301 pspnqpqgyl rsgappvlvv hgakdalatv eaarnfvgrl rrisddtvvy aelpgaqhsf
      361 dvfhsprfea vvdgveafaa rvladpgrss adtp
//
LOCUS       WP_457655477             383 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655477
VERSION     WP_457655477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..383
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40626
     Region          20..372
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtttphhpia viggglgglt larvlhvhgv hatvfdleas paartqggml diheetgqaa
       61 lrearlyeef tarvhpggqa mrvldrhgvv rreepddgsg grpeidrgdl rdlllsslpd
      121 gavrwnakav scrpldgggh evvladgsvf ttdllvgadg awsrvrplvs patpaytgvs
      181 fveldlndad vrhpgaagli gggmffalge ekgflghret dgslhiyval radeswlgtv
      241 dftdtdaaka ilakhfdgwa palrdlidaa dgrlvprhih alpaghrwpr tpgvtllgda
      301 ahlmspfage ganlalidga dlgrclathp gdteaaltay eeimfpraed taresaegld
      361 vifdprapqp lvdmfarfdg eqh
//
LOCUS       WP_457655481             324 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces griseus].
ACCESSION   WP_457655481
VERSION     WP_457655481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..324
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35250
     Region          1..322
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mlfdmdlerl reyrpepqep adfdafwakt laeadrhdvd arfvpyetgl atvdvldvtf
       61 rgwegqpvka wlmlpkqrsg plpavvqyig ynggrgipya wltwsafgya hlvmdnrgqg
      121 gggkntadtp digpeghgss spgfltrgie dphrhyyrrl itdavravda araheavdag
      181 rvavlggsqg gglalavagl rddvsaavad vpflchyrra sqitdsgpya eiarwlsghr
      241 frieeametl syfdgvnfaa rasapawfsv glmdrvcpss tvfaayhrya gpaeievfpy
      301 ngheggaeyd lprklgalrg vfga
//
LOCUS       WP_457655482             309 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655482
VERSION     WP_457655482.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 309)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..309
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34119
     Region          18..309
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 matvdtrkpv apstakprep sgrrpvspgr ialyitlsvi sllmvvpfvw mvitslkspv
       61 diasqdagll psswqfgnyv dafraapfat yarnsfiiai shtvlnvlva smagyalari
      121 rfrgsevify lfiaalmipt ytkvlpefli vrfmplaggn dilgqggsgw ldtwwaliip
      181 gtvtpfavfl frqfyldlpv eleeaarldg lgefriyari mtpqvkpalt tvalltfess
      241 wnnflwpllv trtdslrviq vglsvfkten gtqwhylmag ttlatlpmvl lfligqryfv
      301 qgfataglk
//
LOCUS       WP_457655483             280 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655483
VERSION     WP_457655483.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30566
     Region          2..274
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mlmvapallh aslwiglpvl aavvlaftky dvltapqfvg ldnfrdmlnd avfrksivnt
       61 vvytfftvpf gmllglllal alhtglkarg ifrtavflpq vtatvaialv wlwiynpgng
      121 lfnallsfig idgpawlsst awampsvilv giwqgigmkm liylaalqsl prelyeaasv
      181 dgaskvrqff sitlpllkpa tffvlitsmi gafqsfdqiy iltdggpans ttmmtyeiyk
      241 safrefrvgy acaqslvlfv llmgftlvnr rimggtrghs
//
LOCUS       WP_457655489             336 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655489
VERSION     WP_457655489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..336
                     /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=36171
     Region          19..320
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpktsarlla llsllqarrd wpgsllaerl qvsprtvrrd vdrlrelgyp iaafkgpdgg
       61 yrldagaqlp pllfdddqav alavalrtaa atgagigeaa aralttvrqv mparlrhrvd
      121 alqvtavert ggqtqpqadp rvlltlsaav harevlrfdh spayvpaead aapavrrvep
      181 hrlvtwggrw ylvawdldra dwrtfradri tprtptgprf tprevpggdv aafvaarfqg
      241 sdtpgewpcr geailaapas evaghlrhgv veehgpdrcr vilgawswpg laaelgrfdv
      301 dievvgpdal rdafahlarr yadaagagag aepdrp
//
LOCUS       WP_457655492             669 aa            linear   BCT 27-JAN-2026
DEFINITION  PTS fructose transporter subunit IIABC [Streptomyces griseus].
ACCESSION   WP_457655492
VERSION     WP_457655492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 13938247
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..669
                     /product="PTS fructose transporter subunit IIABC"
                     /EC_number="2.7.1.202"
                     /GO_function="GO:0005351 - carbohydrate:proton symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0022877 -
                     protein-N(PI)-phosphohistidine-fructose phosphotransferase
                     system transporter activity [Evidence IEA]"
                     /GO_function="GO:0090563 - protein-phosphocysteine-sugar
                     phosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=67737
     Region          1..147
                     /region_name="PtsN"
                     /note="Phosphotransferase system
                     mannitol/fructose-specific IIA domain (Ntr-type)
                     [Carbohydrate transport and metabolism, Signal
                     transduction mechanisms]; COG1762"
                     /db_xref="CDD:441368"
     Region          173..652
                     /region_name="FrwC"
                     /note="Phosphotransferase system, fructose-specific IIC
                     component [Carbohydrate transport and metabolism];
                     COG1299"
                     /db_xref="CDD:440910"
ORIGIN      
        1 mselitaelv dldlsaatkd aaarslaerm vaadrvtdld gfladvaare aqmptgldgg
       61 igiphcrseh vsaptlafgr saagidfgaa dgpadlifli aapagadddh ltilsalarr
      121 lmdpeftaal ragtdpgava alirgeepte npdpdpepee ddataaaaap frivavtscp
      181 tgiahtymaa eslaaagrae gvevtvetqg sagfkkldpa ivaaadaviw ahdvevrekg
      241 rfrgkplvdv gvkaginrpa eliaearrka ergeiaavse dggstdsgdg dgggsgadha
      301 hfgvrlrtyl msgvsymvpf vaaggllial sfaiggyeia saksvadhfv wgeadswaal
      361 lnqigsaafa flvpvlagyi aygmadrpal vpgfvggaia ltvnagflgg lvagllagav
      421 vmaiqrvpvh atlrgimpvl vipliasavv gflmfivvgk piaslqnalt dwlnglsgsn
      481 avilgvvlgl mmcfdmggpl nkvayafavg gladptdgsl kvmaavmaag mvpplamala
      541 ttvrkklftk terengraaw vlgasfiteg aipfaaadpl rvipsvmagg avtgalsmaf
      601 gatlraphgg vfvvpligqp flyllaiaag tlvatalvvl lkgarrtasd pageaeatgs
      661 ddsrvtvaa
//
LOCUS       WP_457655497             586 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457655497
VERSION     WP_457655497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Scheurwater,E., Reid,C.W. and Clarke,A.J.
  TITLE     Lytic transglycosylases: bacterial space-making autolysins
  JOURNAL   Int J Biochem Cell Biol 40 (4), 586-591 (2008)
   PUBMED   17468031
REFERENCE   2  (residues 1 to 586)
  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 586)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   4  (residues 1 to 586)
  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   5  (residues 1 to 586)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     'Holy' proteins. II: The soluble lytic transglycosylase
  JOURNAL   Curr Opin Struct Biol 4 (6), 810-813 (1994)
   PUBMED   7712284
REFERENCE   8  (residues 1 to 586)
  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
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     A conserved domain in putative bacterial and bacteriophage
            transglycosylases
  JOURNAL   Trends Biochem Sci 19 (3), 106-107 (1994)
   PUBMED   8203016
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14419880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..586
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=59482
     Region          121..255
                     /region_name="Slt35-like"
                     /note="Slt35-like lytic transglycosylase; cd13399"
                     /db_xref="CDD:381602"
     Site            order(131..133,135,139,174,187..189,192,221,241..244,248)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381602"
     Region          361..426
                     /region_name="Big_1"
                     /note="Bacterial Ig-like domain (group 1); pfam02369"
                     /db_xref="CDD:460541"
ORIGIN      
        1 maahirrrlr kgatttavaa aavaalaasq apaatladgs agngdpkaag edtasadndg
       61 aatgnspyyt dlpplvtpdk pgsssnlpat gsaeagipas ilaaykqaeq tvattdpncr
      121 lpwqllaaig kvesgqargg rvdangttts pilgpalngq gfalikdtdg gaydgdavhd
      181 ravgpmqfip stwaswgqda ngdgrkdpnn iydaalaagr ylcandrdla iaadldkavl
      241 synrsteylr tvrswfsyyq rgtheipdgt gtlpttpstp spnpgpstgp satpspkpsp
      301 gkpggkpspg pskpgggsts ptpkpptptp tptppaetfg slenagtgpl ratagqefde
      361 rvsvrarnal gaplakvpvt ftvtgntgtl ftggkktvkv ttgadgtata palqagekag
      421 eftvtavagv grprtltyaa avtarqadai artdekella apgekfghav tvkatykdav
      481 aagvavtatm vkdplglidn dkgpyfkdad gkpvrtlttl ttdadgvlrl peifaddteg
      541 tftlrltteg gasvvieltv rapeetapee tdpeepvpgk tetpea
//
LOCUS       WP_457655498             288 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457655498
VERSION     WP_457655498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..288
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31422
     Region          90..192
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 msqeihgtys serperpglp apeepaepea trraadgaes srasrgwwdr nadeyqsdhg
       61 gflgddrfvw gpegldeaea allgpaaalk gldvleigag aaqcsrwlag qgarpvaldl
      121 shrqlqhalr igeglplvea dagrlpfrdg sfdlacsayg avpfvadpvq vfrevhrvlr
      181 pggrwvfsvt hpirwafpde pspeglsvta syfdrvpyve qdengdavyv ehhrtlgdrv
      241 rdvvaggfrl vdlvepewpa wndqewggws plrgnlipgt aifvcera
//
LOCUS       WP_457655500             459 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Streptomyces griseus].
ACCESSION   WP_457655500
VERSION     WP_457655500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 10008453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..459
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49142
     Region          <3..454
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          44..235
                     /region_name="COG4279"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]"
                     /db_xref="CDD:443420"
ORIGIN      
        1 msprmsprpa prpttgpaar rsaprarigp ddlrrtfeav partsaegep fadswwgraw
       61 vdaleslsmd earlargray addgqvaait vtpgrvvayv hgsrarpyra elrlrtfadp
      121 gwealldava erpghlsall akemphslar taqeagvrll paaddldpsc tcpdhgrpck
      181 hvaalcfqta llldsdpfvl llmrgrgere lleelgrrna ehsarerpaa pavpsvgaee
      241 afagrflppl paplpvpphp gqppsypdlp gardplgldh laadaaarah allttgrdpl
      301 agftawqdav rlaasrptag ltattralyr elayatgrtt tdlaravaaw rqgaagglav
      361 letpwdppag pfdrarpala aagyprftpw rnhlthpags lqlrfgqdmr wygyesdpga
      421 ddwwpraapd pdpvsalgal lagdsvpdta gdddphyvr
//
LOCUS       WP_457655504             504 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655504
VERSION     WP_457655504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..504
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=53735
     Region          10..492
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 mstvappadw hrldprtvlv talvvagvva gaaipvtlgl trwfslpvav lqvfagavlv
       61 igaaagadrv rwhrtryrig eervdlhtgl llvkrrslar grirtvdlta nlllrllglv
      121 tvrigtgeqg sestleldpv traegerlrr llleraatap pgvhregela vldprwirya
      181 pvsfvapmlg gaaagavmqv sdwvgaqgqv iewvgdrfre tpllwviivl vlaalvagvv
      241 galglwiemw wnyrlerepg gtlrvrrglf tsrsisveea rlrgvdlvep lgvrllgaar
      301 ldaittglak dqearnadhn tllpaaprtr adavaadvlr eadtptgaal tphpraargr
      361 rlrwslaavl gpvlvltllg alltpvllwi algcavvavp vavvlalday ralghtlsgr
      421 ylvtrsgtvr rstaalerag vigwtvkqsv fqrragllti tattaaggga ytaydtdaae
      481 glafaaeavp gllepflerp pkdv
//
LOCUS       WP_457655505             592 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces griseus].
ACCESSION   WP_457655505
VERSION     WP_457655505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..592
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58742
     Region          3..554
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 maraprrdll agltvaival plalgfgvas glgaeaglat avvagalaav fggsnlqvsg
       61 ptgamtvvlv pivaeygpgg vltvglmagg llivlallra grsmryvpap vvegftfgia
      121 cvialqqvpn algvaapegd kvlvvawrav eefvggpnwt alaitvgvag lmlagarlrp
      181 gvpfsvvavv aatlavqlfd ldgvtpigal paglpapslg fldvsavgsl vapavavaal
      241 aalesllsat vadgmttgqk hdpdrelfgq gianlaaplf ggvpataaia rtavnvrtga
      301 gsrlaaltha avlavivfaa aplvsripla alagvllata vrmvevgalr amaratrsda
      361 vvlvltavat lvldlvlavv iglavaglla lravaaearv drvhpyddgv pelpgaqtyg
      421 gevpelpgae pykggdadgg gelagtagqv vayrvegplf fagahrslle lgeisgvrvv
      481 ilrmcrvttv datgalalkd tvhrlngrgi vvlasgirpd qrralesvga lellrregre
      541 yataseafga arqrlavaga argdgavaaa gvgparggrd vpvaapaeea ar
//
LOCUS       WP_457655509             433 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655509
VERSION     WP_457655509.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43858
     Region          13..378
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,114..115,117..119,122,142,
                     145..146,149,223,226..227,230..232,235,252,256,309..310,
                     314,318,333,336..337,340..341,344)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrtyrelfrt peftpffaav svqtaastat glalgtlvyt rtgspllsal amfgpslaqv
       61 ggaltllsaa drlppraalt alallsaaaa cvqaapglpl waafavllvv gtaaapgggv
      121 rygllneivp regfllgrsv lnmtggatqi cgyavggllv tvfsargtll igaalyvvaa
      181 tvtrfgltar ppraagrpsv retrrtnall wsstprryvf lalwvpnglv vgceslyvay
      241 apghagllfa agalgmlagd tlvgrfvaar wrarlgaplr lllaapyllf alrpglplal
      301 avvvlasvgf aaslllqerl laltpqelsg qalglsssgm lamqgvgaav aggiaqltsp
      361 atgmaavagl svavtlalap glrdrneadr grllgadgsp rasrtpstps tpspprtsst
      421 sstsstsste ett
//
LOCUS       WP_457655510             458 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-amylase [Streptomyces griseus].
ACCESSION   WP_457655510
VERSION     WP_457655510.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 458)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..458
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47378
     Region          35..372
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(79..80,83..84,119,122,171..174,204,206..207,
                     209..210,232,234,239,293..294,299)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(121,176)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(206,232,294)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          378..458
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mssraaratl agllaaggla vlapwssqat ppgektvtat lfewkydava aactdtlgpa
       61 gygyvevspa tehiqgdqww tsyqpvsyki agrlgdrdsf aamveschta gvkvvadavi
      121 nhmaagsgtg tggtsytkyd ypgtfqdqdf hgcrkdiany gdrddvqnce lvgladldtg
      181 sdavrttiag ylsdlrslgv dgfridaakh msaddvaaik gkmddpgfwv tevihgggea
      241 vqpeeytaig dvdefryggh lksafqgggl sglksiadgk lpggsartfv dnwdterngs
      301 tltykdgaah tlanvfmlas pygspnvfsg ytwsdkdagp pnggaadcgs dawtcvhaqq
      361 svtgmvgfhn atagaeltdw wddgssalaf aragkgfval nngdaeltrt ftttlpagty
      421 cnvvaaapda cdgnevtvad dgtatatvpa hgavalht
//
LOCUS       WP_457655513             820 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter family substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457655513
VERSION     WP_457655513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Lewis,K.M., Greene,C.L., Sattler,S.A., Youn,B., Xun,L. and Kang,C.
  TITLE     The Structural Basis of the Binding of Various
            Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA
            from Chelativorans sp. BNC1
  JOURNAL   Int J Mol Sci 21 (11) (2020)
   PUBMED   32486296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Marland,Z., Beddoe,T., Zaker-Tabrizi,L., Lucet,I.S.,
            Brammananth,R., Whisstock,J.C., Wilce,M.C., Coppel,R.L.,
            Crellin,P.K. and Rossjohn,J.
  TITLE     Hijacking of a substrate-binding protein scaffold for use in
            mycobacterial cell wall biosynthesis
  JOURNAL   J Mol Biol 359 (4), 983-997 (2006)
   PUBMED   16698034
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..820
                     /product="ABC transporter family substrate-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86724
     Region          61..791
                     /region_name="PBP2_Lpqw"
                     /note="The substrate-binding domain of mycobacterial
                     lipoprotein Lpqw contains type 2 periplasmic binding fold;
                     cd08501"
                     /db_xref="CDD:173866"
ORIGIN      
        1 mshvgvprgt vrkrrslall ttgvltipvl agcssggeet srgvpqdiap aaretvadgs
       61 tvnwavdalp atfnafqada dsattritga llptlfpmdk sgqpklnpdy lesakviere
      121 pkqvvlykln qqavwsdgre igapdfvaqw ralsgkdsaf wtarnsgyer iekiergadd
      181 lqvrvtfskp yadwrslfsp lypkeitgsp dtfndgartt lkntagpfvl rsvstskgtv
      241 tlarnprwwg dkakldtlvf ravaakdrtq aladgtvdva didaatadri tlarrdrgnn
      301 gqqpahgpgs eitpaaalrs walahgsdee aaeiaqaare knrkavvaya teqkalrdfa
      361 vrkslepayt qlalngesgp laddrvrrav araldrqela qtvlgplglp akplgshlal
      421 agqpgykdgs galgdqntke aqalladagw trggaaqlpk dtkagseaek kgdkdakedk
      481 dkdtkegaea ekgtaedakk dedkdaktek gekeskeeka deeaedekgd kkagraseds
      541 aasrdeglyi vgednkpraq apahasasga sglhviapar aaaaqsaall rqagvvgedg
      601 tvaaqdkqpg gaagayapvg taapapaaak gqlgkdgktl tlrfvlpsgp gsqslrsvgd
      661 kiatmlekig igteitkvpd esyfkdhias geydlalysw pataypatdg rpiyakpepa
      721 tdgsllveqn ytrvgtdhid qlfdqaaael dekaarelmk qadariwaaa gsiplfqrpq
      781 lvavdkklan vgafgfaapr yqdigfknrq aagspadrkk
//
LOCUS       WP_457655517             191 aa            linear   BCT 27-JAN-2026
DEFINITION  SMI1/KNR4 family protein [Streptomyces griseus].
ACCESSION   WP_457655517
VERSION     WP_457655517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Brantl,S. and Muller,P.
  TITLE     ToxinAntitoxin Systems in Bacillus subtilis
  JOURNAL   Toxins (Basel) 11 (5) (2019)
   PUBMED   31075979
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Hong,Z., Mann,P., Brown,N.H., Tran,L.E., Shaw,K.J., Hare,R.S. and
            DiDomenico,B.
  TITLE     Cloning and characterization of KNR4, a yeast gene involved in
            (1,3)-beta-glucan synthesis
  JOURNAL   Mol Cell Biol 14 (2), 1017-1025 (1994)
   PUBMED   8289782
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 4183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..191
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=20706
     Region          8..>64
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); cl01747"
                     /db_xref="CDD:445532"
ORIGIN      
        1 mphpavvrlr ellppprsgg davdweqier ttglafpady refvelyggg eideylsvst
       61 ppvpgspygd lldrgepals drdreelcaf lsggalqpll pfvdsassdv afwlrdgapd
      121 dwraavfrrq tphgtsrwtv fdggvaalcv aaltgevhpf serlsasggh efvswrgved
      181 rqppapgrhg w
//
LOCUS       WP_457655521             498 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457655521
VERSION     WP_457655521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..498
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52457
     Region          10..484
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mhfaslpslr adarpdgpcl sdetvgtltn qafaarveaa srvlaahggt rgtvvavrlp
       61 ngtdlvvalf aawrlgaavt pvnpalarge vgyqvadsgs hvlvthddla legvttlspe
      121 dlttpdaavd agpaepdldd lallvytsgt tgrpkgvelt hanldamtgt mvealslder
      181 dhsllilplf hvngivvsvl splraggqat iagrfnpqtf lttletarpt yfsavpaiyt
      241 llanlpaqie pdtsslrfva cgaapmpaal igrieerfgv vliegyglse gtcasmsnpl
      301 ngvrkpgtvg valpgqtvav mapdgtlmpp gergeiviqg ptvmrgylnr lqetaqalkd
      361 gwlhtgdvgv ldedgylriv drikdmiirg geniypqeie qalhahpavl eaavigrphp
      421 vmgeepiafv alkngtslde delvaflthr iakfklptsv ifvdevpknp vgkfdkprlr
      481 ttlaltstsa mgrdeetp
//
LOCUS       WP_457655522             480 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces griseus].
ACCESSION   WP_457655522
VERSION     WP_457655522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..480
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48780
     Region          33..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 masvsesgsg sgsgsgsggg pgggsgssae egklrrtlgf rdlvvygllf iapmapvgvf
       61 gtldaksdga valvyvvatv vmaftafsya qmvrvapfag svftyarkgl gegpgfiagw
      121 mamldyllip avaylfsgia mnalvpevsr wvwtaiavlv ttllnlwgvr aaarvgfavl
      181 ameivvllvf vvsavvvlvr dgaqrgwltp ltgdtgfsma avlgavsiav lsylgfdaia
      241 sfaeevtggs qkvaravlfc lvlagvlfva qsylaallep vssaelaadp aaqgsafyda
      301 vdasvgtwlh dlvavskaig aafaalagqa aagrlvfama rerrlphlla kvdpksgvpr
      361 vailgaavvt lvaavwaarr ddgldhlvsv vdigaltafv llhasvvgwf vvrrmagppv
      421 wwrhvlvpvv gagvliaviv eatasaqvvg lcwlavglvv lavqgtgrrg gapgpggpgr
//
LOCUS       WP_457655530            3125 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase/type I polyketide synthase
            [Streptomyces griseus].
ACCESSION   WP_457655530
VERSION     WP_457655530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 3125)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 3125)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   3  (residues 1 to 3125)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 3125)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 3125)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 3125)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   7  (residues 1 to 3125)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
REFERENCE   8  (residues 1 to 3125)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 3125)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18690202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3125
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..3125
                     /product="non-ribosomal peptide synthetase/type I
                     polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="6.-.-.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=336985
     Region          10..1402
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1283..1684
                     /region_name="KR_2_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 2, complex (x); cd08955"
                     /db_xref="CDD:187658"
     Site            order(1450..1451,1453,1473..1476,1514..1517,1543..1545,
                     1566..1567,1589..1590,1604,1631..1632)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187658"
     Site            order(1567,1591,1604,1608)
                     /site_type="active"
                     /db_xref="CDD:187658"
     Region          1722..1805
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1817..3045
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 madannralr nkvaiigmgc rlpggasdhr tywrnlmagk dcitptppdr ydvrtlgsrf
       61 rdkpgrlvgg rggyidgfde fdpaffgisp readhmdpqq rkllevawea ledggqrpad
      121 laggnvavyv gaftldykil qfadlgftsl aahtatgtmm tmvsnrisyc fdfrgpslsi
      181 dtacssslva vhlacqalnn gesdlalagg tllhmapqyt vaetkggfls pegrsrtfda
      241 aadgyvraeg vglvalkrld davrdgdrih aviagsgvnq dghtngitvp nadaqvdlir
      301 rvcaeagitp gdlqymeahg tstpvgdpie analaralai grapgarayv gsvktnight
      361 esaagiagli ktvlsiqhrt vpphinlenl npaidpatlp yeiptrptaw pahegparag
      421 vnsfgfggtn ahvvleeapp pppktgaapp agrpwsilpl sarnpdalve laagirgela
      481 gdngpavald dlghtlahrr qhlperlsvv ystrasldea laahgrgeph prvvhgrare
      541 sadrrlvwvf tgmgpqwwgm grqllaeepv freaveacdr alrefadwsl ieeltadesv
      601 srmsetwlaq panfavqval aalwrshgvr pdavvghstg eiaafhaagv yslrdaariv
      661 vhrsrlqqtl agtgamlavs lsedeaerrv rpyrdrvsva avnsptaitl agdeaaltll
      721 aeelraeqqf akfltvevpy hsvgmerikd ellaelaple prparvplyl tgvagtarge
      781 eldaaywwkn vrdrvrfrsa vdriaadghq lfleigphpv lghairecle aggttgltlp
      841 sirrrenese rfaaslgslh tlgvtvdwdv lqptgrpvtl prhpfrrdrh wteprpvaqv
      901 rlghrdhpll grrtdrtept wqarldtedl pyladhriqd tvvfpaagyl emaaqavlrl
      961 tggttavlad idlrkalflp dgedrtvevs lslenaafti asptgddger avhasgivrt
     1021 gqrrrtappl dapairarsl rhlegpdcyt alaalgyhyg pafqaveevw igagevlari
     1081 rppeaigdda aghhlhpvll dacfqtlltp lipptpegpa pgtgirlpls vdevalepig
     1141 dqpfwahatl lpgdadttlg nialyaddgt plgrvhgfra advekaatav arttidswla
     1201 epawteappl paedtardhd wlvladnggv adafaalaaa rgercrlvrr gaaytasgdg
     1261 vtftvdpasd adlrrlladl draggpfrga vlhlwnldap aladcdraal rdhtgagayg
     1321 lialarllla rggggrlhiv trgaqpalpg egpeplgapa wgigrvlrhq elidhpgkli
     1381 dldprrrpgp dgdraeaeal laevlsddee eialrdggrr tsrlrpaehl trplpprlra
     1441 dgsylvtgaf galgrllcrt lvrrgarriv lvgrtpvpar ekwagtdpat aegravallr
     1501 elealgaqpv latlditded altgwldahr qsgappvrgv fhlagqvrdt lvadldraaf
     1561 davhdpktvg ahllhrhlrd eplehfvlfa siasllttag qtnyaagnaf ldalahhrra
     1621 qglpalsldw gpwatgmiee lglvehylhs rgmsslspdt gmavlervig qdhaqlvvat
     1681 vvdwpvflaw yptppplvad laaaaappgd aasgngfldt fraadeetrr alvaerfaal
     1741 satvlrtgtd ridpttglge lgldsllame lrarihaelg valpvvalls gtpagelaaq
     1801 lhdglsalaa adtpdgaaga velhrderqy pltqnqkalw flkhlnpdgy ayniggavev
     1861 nvalepdlmf eavrrliarh palrtnfllv dgqavqrvse daatdlglfd vqgedwdsih
     1921 ativqeyrkp ydlahdplvr frlfkrgpdr wiimkavhhi vsdaistftf ieellavyea
     1981 lrrnqepqlp pvearyldfl nqqnaflagp eaagmldhwr ahlpaevpll dlpvdkprpa
     2041 vqthngasef fvlddalsar vhalarahgv tpfmvllsay ylllhrysgq dhivvgspvt
     2101 grtrqdfasv ygyfvnplpl hadlsddptv aellqqvrrt vlggldnqey pfvllveelg
     2161 lqhdpsrsav fqamfillth kvateqygyr leyielpeee gqfditlsay edeaegrfhc
     2221 vfkyntdlfl petmrrmaah ytrlldrmth apgeqpasrl emlgdqerer lveewsrpal
     2281 ptagsreepf aavqtliarv aaehpaavav ttpsphggah rltyaelerr aadsaarlrt
     2341 lgigqgsvvv lcldkspeli vallavlkag aaylplrpdq padrlahlvt atgaalvlva
     2401 ddagpeqtga lavptltlga lartaphpdg psdeagpesp ayiittsgst grpkavrvsh
     2461 rnlasahaaw rqeyrletdv rvhlqmaeps fdvftgdlvr alcsggtlvl adrdllfdtt
     2521 rlyrtmrqer vdcaefvpav vrglmdhcar eglrldflkl lvvgsdawsv geyrrlaelc
     2581 gpgtrlvnsy glteatidsa sfegpvddle sgamvpigrp lpnstlhvld ahgepvppgv
     2641 pgelwiggdg valgyagdpe qtearfvtrt lsrsadgdar perlyrtgdi arwdahgrvh
     2701 llgrtdgqvk lrghrieige ieahlaqwpp laravvtvra dtggeaalca ycvpvpgatl
     2761 dgralrrhla rslpsymips hfvelpalpl tangkvdtaa lpapraetgd rpyeepvtly
     2821 eisvarhwkt llgreqigle ddffelggss ikliellhql rtefgvgvpv srlyqvttlh
     2881 gmaatvedvl hgtsadelps ltfnagqhpa lfcfppaggh glvyrglaah lpdhtligfn
     2941 ylpgddkvar yadlieaarp dgpyrllgys lggnlafeta kelerrgrrv ahvvildsrr
     3001 iltayepdas giavfeaela dhlrkhtgse avtretlaha aeylafcgrt pntgtvaatv
     3061 svitdeekaa lyaagehgtw hgsstgatav lrgsgvhadm ldakhlprna elvrsvltgd
     3121 pahgg
//
LOCUS       WP_457655531             322 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655531
VERSION     WP_457655531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..322
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33703
     Region          83..290
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msydprldpe maaalaaapl pptvlpgltr eglaalraar aaavspppae gvrvtdhrlp
       61 gpgavrlrvh rpraaptgpl pclvwmhggg mvlgtpemdd arlsayvlea gcavvsvdyr
      121 lapehpypap vedcyralrw tadqadalgv dperlavggi saggglaaat allardrggp
      181 plafqlllcp mlddrnttas sreftdpvtw prannlygwa allgpladgd evppyaapar
      241 atdlsglppa yvdvgelevf rdecaqyalr liaagvstef hlwpgafhgf dgvlphltlp
      301 rraaaeqiav lrralgnpaq ga
//
LOCUS       WP_457655533             537 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655533
VERSION     WP_457655533.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12122902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..537
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=58817
     Region          27..512
                     /region_name="FAD_oxidored"
                     /note="FAD dependent oxidoreductase; pfam12831"
                     /db_xref="CDD:432816"
ORIGIN      
        1 mtsepdiliv gaglggvaaa laacragrtv vlteetdwig gqltsqavpp dehpwveefg
       61 ttasyrtlrd airdyyrqwy pmrsealalr nlnpgagrvs klcheprval avmeamiapy
      121 rssglltllt ehrpvaaeag eddtvrsvtl adlrggnrlt isaryvidat etgellelag
      181 vehvigaear seydephape eaqplnqqgi tvcfalshhe gedhtierpa dydfwrtyrp
      241 dfwpgpllgf lapdprslea vprtfvpnpe ldpldvsadq sadagdkelf gfrrilarkl
      301 hrpgafdsdi tlvnwplndy wlkpligdge etsaaalaea rqlslsvlyw lqteapradg
      361 gtgfpglrlr pdvtgtadgl akapyvresr rikavttvte hdvsidivgp yggtryrdsv
      421 gvgnyridlh pstggnnyid igsvpfeipl galvprrvrn llpagknigt thitngcyrl
      481 hpvewnigev agalaahcva esvephqvqa edkrfevfar llerdgvqrh wpdvrgy
//
LOCUS       WP_457655534             329 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655534
VERSION     WP_457655534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35655
     Region          31..327
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpateateat rstaaprgsa vrtsrpappg tgrrqrtfeq anrrlkwaml apavlfvglm
       61 ivfplvftln lsltdafgav nadsahvglr nfadalgdtr rfwpaarrtl vftvgavvle
      121 tvlglalaml mrrpftgmrw vrtvlivpll atpvaigilw llildptngi anhlleavgv
      181 prqeflgsvg qslptlmlid vwqwtpmmtl lllaglttlp eepeeaalvd ganawqrfry
      241 vvlpmlgptl atalvlravd alktfdilya tkgagggsdf evetlnvyay gltfdyqeyg
      301 laaavlvlft lfiigvvvll rrrggrknv
//
LOCUS       WP_457655537             303 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphate ABC transporter substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457655537
VERSION     WP_457655537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 303)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 303)
  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   6  (residues 1 to 303)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Takemaru,K., Mizuno,M. and Kobayashi,Y.
  TITLE     A Bacillus subtilis gene cluster similar to the Escherichia coli
            phosphate-specific transport (pst) operon: evidence for a tandemly
            arranged pstB gene
  JOURNAL   Microbiology (Reading) 142 (Pt 8), 2017-2020 (1996)
   PUBMED   8760913
REFERENCE   9  (residues 1 to 303)
  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 10194586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="phosphate ABC transporter substrate-binding
                     protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31424
     Region          45..294
                     /region_name="PBP2_phosphate_like_1"
                     /note="Substrate binding domain of putative ABC-type
                     phosphate transporter, a member of the type 2 periplasmic
                     binding fold superfamily; cd13653"
                     /db_xref="CDD:270371"
     Site            order(53..55,81..82,100,178)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270371"
ORIGIN      
        1 mstesrsraa rltgrrvrqg asvasaslll saaltgcags akagsdaiqa sgsttvapva
       61 sdaaealkak glnitvatqg gsaggisqlg tgqinialss kplsekdqka ypdtdfvttq
      121 igadavgvii tkevadggvk dltkaqvagl fegkiinwke vggpdlqvfv ydkepgrgtr
      181 evldkfiygk geapappksa nyaivggnle trnklkstrg siaplstgfi eghpelvavp
      241 ledvaptlen vasgkypmtr plymitngrp kdgvkqyidy ilspegqkll pqhgyltreq
      301 mgl
//
LOCUS       WP_457655539             177 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655539
VERSION     WP_457655539.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..177
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18381
     Region          6..163
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mddvrevivi gsgpagytaa lytaraqlrp llfgssifvg gsltttteve nfpgfptgid
       61 gpdlmdnmra qaerfgaemi dddivsvdlt gdikevtdse iaeikaengm lagvvlrdts
      121 trtnlpgvfa agdvvdhtyr qaitaagsgc qaahdaeryl aaladkrkaa asvtvaa
//
LOCUS       WP_457655547             192 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655547
VERSION     WP_457655547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..192
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20634
     Region          39..189
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtitvrpasa fedvrtlvgp kspganvcwc lsyrvpskln nelrgperga yvaglcraep
       61 ppgvlaydgd epvgwaavap rsdtsfarsr kiphvdevpv wslwcvrvrp ghrkkgisha
      121 liagavefar ahgapaieay pidsggaevd ltmayagirk nferagftha adttsvlagh
      181 prvlmrldlr dr
//
LOCUS       WP_457655551            1001 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457655551
VERSION     WP_457655551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1001)
  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 1001)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437895
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1001
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=109831
     Region          129..946
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 msvttvalra plvlvpgfrl deqlrgkaet saglppdvsq ivhdlnrlka gvavtvnpag
       61 gnykpsllvh trmyrirlea tnrgtgylvk hidplrladh arlarsclvv rppawhmvfe
      121 lkavptgsda qwqvleqawq rlgqtqpdrs dapssddaqa rfldsvdrli dateeittre
      181 erqaapflyq sftatggkrg ktaqsvyefq lvgsepppsg afvriqgdtd trgkvgrasd
      241 ryvtvrfdqp vswdrlptrg alelipssvi fnkqrqavas lrahdsknpg llpavvehhv
      301 rpipatdaqp hqpldpeqlr afraalttqd llvvlgppgt gktrtiteia htaattsavd
      361 sgrvlvtsht nravdnvlar lpqdlvvirv gdeskvhadv kpllleeqse glseeirham
      421 aqrtqaykea adveprtael aarvqqvdsh aeeartadlr lhaaaraaaa paherltalg
      481 seeqmlrtll edrteradrl rakahsarqr sdalftgrlh rfrarrreae latesaeiek
      541 lnaslhdvlr qteaagveae raaredtavi aaramrqtag dhlaksvqsa yeeadravha
      601 lravvptaal parlsdpada atalrelhrq ltdwipvlar rqeltgqwla aiaqdpgqlv
      661 pelvryahvv gatcigaasr pelsgvefdl giideagqig iadtlvpltr vrrgvlvgdd
      721 rqlppfrdad vdewaqgigd pelvrlmsqs alerlraglp sshvvqlarq rrmpaeiadf
      781 isaafyrgql ltekehrhrd plftspmafv dtaalpdrvr hesgrgrkeg rgqkgpfnpc
      841 earllarlaa fyhrrgaewt vivpylaqrl evvrqltpli gdsqlanasv gsvdsyqgge
      901 cdivlygftr snpegrigfl kelrranvaf traksqlvmt gdlstlmrgd dpgfrmligd
      961 lhqhlldrgd lrghrevmaa ldetvpdlgd atgparegfr p
//
LOCUS       WP_457655559             473 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457655559
VERSION     WP_457655559.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..473
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=50096
     Region          28..311
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,65,67,102,126..129,132,134,169,171,
                     173..174,176,186..187,190,205..208)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,65,67,102,126..129,132,171,
                     173..174,176,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(38,132,134,169,171,173,190,205..208)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(61..62,94,99,104..107,127)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(186..194,200..201,203..208)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msapqglrdl adgdgaellp pgyrvgdwvv trpigsggws tvyaarpaeg rtggaavprg
       61 htdvalkimp taglaprqar rivesarrev elgrgaghpr ligvlesfvl aapdrpaleg
      121 aivlvmerav gslrelidag vpeadrgrli agiceglahl hrsgwvhadl kpenvllgrd
      181 rsvrlsdfgl ateltgthgh vpplgtldyf pperwraplg elgvrvrpsa dvwalgivih
      241 evfasgaspf pgatpmarga avqeygqgra plrmdqavpp fwrelaadcl apthearaph
      301 saerllaria ahragagava grrgsraraa vlatalcgia gatlcadavr aassassgra
      361 gttppgtiqv ynaerdcrar adrdprcslg laidpvrpyt aenvvptrvw hgdvlvadcr
      421 vldgetiide edrrsthwfr vrlppgsepp tgwlpavrak qrpalpecfs drp
//
LOCUS       WP_457655560             818 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces griseus].
ACCESSION   WP_457655560
VERSION     WP_457655560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 818)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..818
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87329
     Region          34..808
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mavvaavavm stlaatgsta tgaaaaeagp drptirytey giphiiasdw eglgtgygya
       61 aaednictla dtylmvdarr srylgpdgra spgqnqntts nlnsdlyfqr lkddrvverl
      121 ldqpapdgpe pevreairgy vqgynrylae tgvdgisdpa crgadwvrpi temdvyrhah
      181 aeiimgsada lldgqvnaap pgasaaaqpk aasgepapra sspeetaaki rdamaasreq
      241 gmgsnalavg sqgvsggtam llanphfpwq gknrmwqsql tipgkvnvsg asllgfpavn
      301 ighnenvaws htvatvapfg lfdvqvdpln pttylvdgaw ermtsqrvev dvlkpdgsla
      361 kagrtlwstr ygpvttsmqg iplpwvvsah avrdvnlhnl ralnswfrld qaedvhdvvn
      421 ilettqgvpf fntvaadrtg nalyadiqat pnitdqhaes cltatgrllf dqslrlpnvp
      481 pisildgkrs acdwpddpna aapglldphq qprlirgdfv gnandspwla npaqplsfpr
      541 vmgdtaaprs lrtqelilta qkriagtdgl pgkgftpetm gqllfadnsr aadlaldatv
      601 tmcqnvpfgh ilvdgnlvdv reacpvlaaw kshdyttdsr gswlfanywa fllngqgvek
      661 lpwrvpfdpk dpvhtpnsld sgssavrdaf gravlalrka niplnaplsd iqkvtrggeq
      721 ipihgslgql gvlnvitpgq vdgapdivfg ssfiqqvrft atgppqalsv maysqsadpn
      781 sphhadqtkl fsaggwvter fteeqiaasp qlrttvln
//
LOCUS       WP_457655561             750 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457655561
VERSION     WP_457655561.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11602166
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..750
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=76821
     Region          13..265
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,36..37,66,71,76..79,91)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,40,42,74,90..93,97,99,136,138,
                     140..141,143,152..153,156,173..176)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,40,42,74,90..93,97,138,140..141,
                     143,152..153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,97,99,136,138,140,156,173..176)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(152..160,169..176)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          462..705
                     /region_name="PQQ_2"
                     /note="PQQ-like domain; pfam13360"
                     /db_xref="CDD:433144"
ORIGIN      
        1 mslrggdpae iggypledrl gsggmgtvfl artssgrpva iklihqqfag ddefrirfrq
       61 evaaarrvsg aftaavvdaa peadqpwmat tyiegptlaq riteqgplng pelrslaigl
      121 aealrdihrv gvvhrdlkps nvvlsaegpr vidfgisrav dqqtltmtgr vigtppfmsp
      181 eqlqaprgvg prsdvfslgt llvyaatghg pfdadspyit ayqvvheeps lgavptalra
      241 vvepcldkep egrpsvdell vllrdlptdl ggagpggpva grtrdmvtqh hlatgadpap
      301 aapagsgtgs tgtaiggrlr rrwrpvlaaa vavaaigggv aalttggfga sgggadpggg
      361 dtgrstaasp agalpkgfap wrrtvpggre dipdelrcva rddalfcggg gvvatridar
      421 dgsrvwvaks pgvpvqgmhl vgatddtvlg yrfaaqddpq gprsevvald adsgrelwsv
      481 psgaqstavt grsmdavvtg savvtvdasn srfeardahs geitwttpfp gstqcapvpa
      541 gprllamcat daevdavqvs rptlatldla sgalgepvav dgpvvpvgaa dgrlvllskr
      601 yegasragyd gvarfdpaar kvtysrfgqv yagtagmadg tvyvsgqtgr vtaldsatgk
      661 rkwsrqtgve gasgpatggd avyfssatgr vvalsrddga plwstdpqad gltgeqdasp
      721 rvtvagravf vaaaentlfa fdaqkpprsd
//
LOCUS       WP_457655564             326 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655564
VERSION     WP_457655564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35718
     Region          25..319
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msltatakag ppgpagtgpg pddgraaalr rtwrkaspya yiapfftlfl afglfpllyt
       61 afvslyrvel qtsgemewrg ianytalftd eyfwtslrnt ftigvlstvp qlamalglah
      121 llnyklrgrt lirtaillpy atsvaaatlv faqlfgkdfg linyviglvg fdpvdwqtgt
      181 vasqiavssi vvwrwtgyna liylagmqsi phelyeaaem dgasrwrqfl hvtlpglrpt
      241 ivftviisti gatqlfgepl lfegsisggi shqyqtlgly myeqgwgffh lgraaaiawv
      301 mfvlivvlvg vnallvrrra rkeagr
//
LOCUS       WP_457655565             503 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457655565
VERSION     WP_457655565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  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 503)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..503
                     /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=53396
     Region          163..502
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrsrpraprs lrtrlvliat vlatcavllc qtagltvlrs wltdqiddrl tgfrppgriy
       61 ediaddgrlh vprngdilps dyrvyiygsd grlmadslgr kddrgprlpg rtsrltlrds
      121 apatvpaatg dgswrviads gpdrirtvva lpldtvdgat tkllwfsasl gvvvaagval
      181 lgnaavrlgl rplsrveata qritdgaldl rvpdtdpate vgrlgqalnt mldrlrtalh
      241 rtaaserqmr rfmadaghel rtpltavqgf aellhddprm saerraeaha liaanadrms
      301 rlvddlflla klghapgphp epvdllslaa dsitttavrr pgrtitlepl rtgstdtsgq
      361 eldvvetvgd adqlaqvvtn llanacthtp aparihvrvg tmrtslaagg vdrpgrtsat
      421 palppgipaa vievadtgpg lgpedahhvf drfyraapad adepgsglgl aiasaiaeah
      481 rgrieldtrp gagctfrlll pah
//
LOCUS       WP_457655572             696 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457655572
VERSION     WP_457655572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..696
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69759
     Region          29..284
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(29,52..53,82,87,92..95,107)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,56,58,90,106..109,113,115,152,154,
                     156..157,159,168..169,172,192..195)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,56,58,90,106..109,113,154,156..157,
                     159,168..169)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(40,113,115,152,154,156,172,192..195)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(168..176,188..195)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgkgkdsgry tamegirpla agdpvrigpy pllgrlgagg mgrvylarsa ggrtvavkvv
       61 heehiangef rarfrreiea arrvggryta pvldagpdae qpwvatgyvp gpsleqavre
      121 hgplpadsvn alaegllral rgihaagivh rdlkpsnvll tvdgprvidf giaralqvsv
      181 eslltstgmv igspgfmape qilgeetgpg advfslgcvl myaatgqlpf gagvsnqhav
      241 mfrivqsppd ltavsdaplr aliercltkg paerpgveal lesltpeqss daargawlpp
      301 vllarlaqqs allldaevpe epgvpeeade pegaepaavs npvsgpvadp vpvpvpvpdp
      361 dpdpvsapas gsdpdpvsap rdlgtvdlrp epgrkpgpep vagpspestg aaaavpvaap
      421 vaagprrnrr rvwavaavvv avlaaggtta flnrdpggga darggesaap padgatasps
      481 gkgddeddkg seeekakdka edsaeekeke kgngddggqg gdagggqgag sgdgsasggg
      541 ssgtgesgss ggggaqggag ssasggsgga akppaadpdp apdgrvpqhf vgtwsiaspy
      601 dvlqphtvvi rrvspgqsav tliadvqgsg hceytaklgs vadggnrinv gtavvnkars
      661 gsmcrdtdps fftvagsgil hdvgpahgsg yrynra
//
LOCUS       WP_457655574             509 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655574
VERSION     WP_457655574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..509
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53521
     Region          100..>285
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          407..502
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mttrrllrtf aigigtagll isgcsgsgss pnasatgtaa peglssyyaq klswrdcgve
       61 gfecttmkap kdydkpddgd idlavsrkka tgpgkrigsl lvnpggpggs aigylqgyaa
      121 lgypaqvrar ydmvaidprg varsepvecl tgpemdaytq vdqtpdddae vqklsaafek
      181 faagcekrsg eilpyvstvd tardmdvlra llgdeklhyv gasygtflga tyadlfpera
      241 grlvldgamd pslkaidmnr dqtagfegaf qsfaadcvkq pdcplgttst adaatalkql
      301 fadldakpip tgddrelges lattgviaam ydeaawpqlr ealagaqrsd gsgllslads
      361 yyerepdgky anlmfanaav ncldlppafd gpdavekavp dfekaspvfg rgfawaslnc
      421 aywptkatgt phrteakgaa pivvvgttrd patpytwses laeqlssgtl ltydgdghta
      481 ygrgsdcidt aintyllegt ppirgkkcs
//
LOCUS       WP_457655580             755 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655580
VERSION     WP_457655580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..755
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=80403
     Region          1..684
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mpkkrsgggl tttqqaakfl gvaalsgavl agialpaaga lglaakgtve gfdeipsnlk
       61 tpplsqrtti qdrdggtiat vysrdrtvvp lkdispymqd aiiaiedsrf yehgavdlkg
      121 ilramnrnvq aggaaqgast ltqqyvknvf veeagddpek vaqatqqtlg rkvrelkyai
      181 qveeelgkkk ilenylnitf fgqqaygiea asqryfskha kdlkleeaal lagivqspsr
      241 ydpvndteea tkrrntvlar maavktisqa eadkametpi klkvsrpkng citavsgsgf
      301 fcdyvrktil tdpafgktde draklwnlgg ltirttldpr aqkaaneaat akvnkddkfa
      361 asvvqvrpgn geilsmgqsr pygldqkqne tvlnlavsnk mggstygfqv gstfkpftaa
      421 aalekgispa tsfssdwkmt lqerdfrncs gspagyapwe lqnelesekg swdmtsalgk
      481 sintyfamle qkaglcetve makkvgyerg dgkkigeyps itlggevstp lsmagayaaf
      541 anrgtyctpi aiasikdpqg kkipvpktsc sramsektad tinqmlkgvv edgtgtqagl
      601 sdrdnagktg ttndrkdawf vgytpnlsta vwvgddigek ssmfnvtigg qyydkvcggc
      661 lpgpiwriam tgaldaaetp gfnpvsvprg kekkdkdkdk ekgdrdrdrg dedredgkpg
      721 dndgnrfpgv elpdgviggg gggggrgqgg gqngp
//
LOCUS       WP_457655579             276 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457655579
VERSION     WP_457655579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14427476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..276
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28849
     Region          27..208
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(87,89,91..92,142..143,161,204)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
     Region          239..276
                     /region_name="BLACT_WH"
                     /note="Beta-lactamase associated winged helix domain;
                     pfam17778"
                     /db_xref="CDD:407650"
ORIGIN      
        1 msdaaalpgq prgtvvsgpa tartvnvlap npsamtldgt ntwivaepgs dlaviidpgp
       61 lddvhlravi eaversgrrv gltllthghp dhaegagrfa eltrtkvral dvalrlgdeg
      121 lgagdvittg glelrvvptp ghtadslsfh lpadravltg dtilgrgttv vahpdgrlgd
      181 yldslrrlrs ltvddgvhtv lpghgpvled aqgavefyla hrahrlaqve taveaghrtp
      241 sevvakvyad vdrslwpaae lsvraqleyl sghgli
//
LOCUS       WP_457655608             699 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457655608
VERSION     WP_457655608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..699
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73645
     Region          435..656
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtrrperisf rfsarsrfaa clvatadgal apgwwdldgt hppyagdppr yregapaett
       61 atqvlptedg gllrlrgaag sgrhllllsr papaaatata tgtslagprv pypaelelrg
      121 pspaefelkd pppagpepka pappeelive arglrlvpgg ppgtlalave tthdgrtrvr
      181 rvratplrls dpvilpgrvt allpldgtgr ryatdlegpd gyrpvsldlr dgtwhalpsp
      241 angrihrlll sapasglllt asdpgdgrlr iahaalgdrt rlsfpdrlns lngavlplaa
      301 dpagervalr vtrgararlf lydvgadrpr paalppgafh pvagwstggl rvvyatpdrp
      361 adlvtvpdta ahpdptstaa hpdptsydap ssslgapsnt pdadgtshaa tewfatpsgr
      421 feavvlgdrr taptvvvalh ggpedhwtlg hdpvlarlsd agaavvapnq rgstgygrah
      481 aeaihgawgv pdladirslv rtlteqrppd aeppvllgts yggflallav cadpyawarc
      541 aviapflsar glrersspav ralidrhglg eppdddlgpr dverlahrir vplltlhgsd
      601 dpvvpvdetr rlrqalarag gpqraphdcl dipgaghhpl qerggagltd rlvsfltara
      661 pdrrralapp eltvadaavr hrrspavfgh ithdertpp
//
LOCUS       WP_457655592             324 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces griseus].
ACCESSION   WP_457655592
VERSION     WP_457655592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..324
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33223
     Region          7..308
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mgvnvsvvai dagnsktdva ligedgavla targggfqpp vvgveaaidv laaalerava
       61 elpappvlsg hvsaclanad lpveeaelat alesrgwgss vevrndtfai lragvdeprg
      121 vavvcgagin cvgmtpdgrt arfpaigris gdwgggsgla eealwfaara edgrgepsel
      181 srtlpahfgl dsmyglieal hrggiplerr heltpvlfat aadgdpvaga lverlaeevv
      241 amasvalnrl glleeevpvl lggsvlaarh pqlndriael laarapkaev rvvseppvlg
      301 aallgldrtd agpearrrlr ahya
//
LOCUS       WP_457655586             301 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655586
VERSION     WP_457655586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 301)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..301
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32773
     Region          12..120
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(12..14,28,45..47)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(59,62,66..67,76,102,106,112,116,119..120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mhvsfvpprr vrigdaaafv gitprairhy heigllpepe rgsddrrryg yedmirllwi
       61 rrtaeagial ddirdafadp astgadsddg iagilerlee alvaqeaelr rqrtavrrmr
      121 tegsrtglls dfvtdrlkgl pegslrradl dsllvterif gplgaavqas rfialathpd
      181 lreesdrvda aeealddtva vddprvaqva aerhafeetl htviedsgla eeddalfdaw
      241 dalhpataee gepeagrssg ggqgsmsafe aigkmpydfs parlrcmela aelaaheppp
      301 s
//
LOCUS       WP_457655591             421 aa            linear   BCT 27-JAN-2026
DEFINITION  6-phospho-beta-glucosidase [Streptomyces griseus].
ACCESSION   WP_457655591
VERSION     WP_457655591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Varrot,A., Yip,V.L., Li,Y., Rajan,S.S., Yang,X., Anderson,W.F.,
            Thompson,J., Withers,S.G. and Davies,G.J.
  TITLE     NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases:
            structural insight into specificity for phospho-beta-D-glucosides
  JOURNAL   J Mol Biol 346 (2), 423-435 (2005)
   PUBMED   15670594
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..421
                     /product="6-phospho-beta-glucosidase"
                     /EC_number="3.2.1.86"
                     /GO_function="GO:0008706 - 6-phospho-beta-glucosidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45176
     Region          1..418
                     /region_name="GH4_P_beta_glucosidase"
                     /note="Glycoside Hydrolases Family 4;
                     Phospho-beta-glucosidase; cd05296"
                     /db_xref="CDD:133432"
     Site            order(9..10,12,36..37,41,81..83,106,126,142,144,272,294,
                     299)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(90,106,144,165,194,244,264,294..295,299)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(164,194)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(183,186,202,208,314,326,345..346,348,350..353)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(230,232,235..237,249,251..252,358..359,366,370,377,
                     385,388..389,399..400,402,404)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mklavvgggs tytpelidgf arlrdtlpie elvlvdpaad rlelvgglar rifakqdhag
       61 kitattdlda gvadadavll qlrvggqaar nqdetwplec gcvgqettga gglakalrtv
      121 pvvldiaerv rrtnpdawii dftnpvgivt rallqaghka vglcnvaigf qrkfarllev
      181 epgqvhldhv glnhltwelg vrlggpdgen vlprllaehg dtiaddlrmd rrivdrlgvv
      241 psyylryfya hdevvrelgt kpsraaevaa mekellamyg dptldekpel lakrggafys
      301 eaavdlaasl lgnggspvqv vntynkgtlp flpddaviev qarvghdgat plavpaldpl
      361 yaglianvta yedlaleaal rggrdrvfka llahpligqf dyaegltdrl iahnrehlaw
      421 a
//
LOCUS       WP_457655604             318 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655604
VERSION     WP_457655604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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   4  (residues 1 to 318)
  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 318)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10126257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..318
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=33900
     Region          2..209
                     /region_name="ABC_BcrA_bacitracin_resist"
                     /note="ATP-binding cassette domain of the
                     bacitracin-resistance transporter; cd03268"
                     /db_xref="CDD:213235"
     Site            34..41
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213235"
     Site            order(37..38,40..42,80,153..154,186)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:213235"
     Site            77..80
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213235"
     Site            129..138
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213235"
     Site            149..154
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213235"
     Site            157..160
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213235"
     Site            182..188
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213235"
ORIGIN      
        1 mieateltkr yggrtavdrl sftvrpgrvt gflgpngagk sttmrlilgl dsasagrvtv
       61 ggkayadlpv plravgslld akgvhggrsa yhhlaglaas ngiprrrvee vldlvglpaa
      121 tarrrtkgfs lgmaqrlgia aaligdpevl ildepvngld tegirwirgl mrslaaegrt
      181 vflsshlmse meltadhivv igqgrliadt tmrdfietns rahtlvrspe perlrallet
      241 agarvrldat ggwrvegpdp aaigdlardh gvavheltpa hssleevyta lsqssveyrt
      301 edrtedraaa pgrketvr
//
LOCUS       WP_457655596             460 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655596
VERSION     WP_457655596.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..460
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47690
     Region          361..459
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mptcpnghqs gsedwcevcg hrmatggapa gavppppppp ppapgygypq qgsegggptm
       61 qaelcpqcrt preamapfce ecrwnfltnt atsytplapq hgtpggpppg lnlppgfqaq
      121 spggqggpga qggppgapqp rdpfdyqgsr psqmnrpaes lapeqngphg nggqggqggs
      181 ggqggpppsf qqqgppppps fqqqghqppa qqqaapstrs pfepqqaspf appqqqsapp
      241 appqpsghtg geddwmlppp sqaqppqppq hfqqppsphq gqgqqgpgqd pgqgydqgrp
      301 qhgqdqgydq gqqhggvpgq grppqpaswt aviapdrayf lammqrsgpe atglnlpays
      361 peqrlpltgs qitigrrrhs tgespdvdls vppedpgvsh qhavlvqqpd ggwavvdqns
      421 tngttlngae dpiqpyvpvp lqdgdqvhvg awttitvrrd
//
LOCUS       WP_457655612             214 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655612
VERSION     WP_457655612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23747
     Region          17..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maeswtvqrt gpgdvartqa reqlleaare lygvngyrqt aehdvceaag vpaevlrqey
       61 gsregllial hnrvtttglr aaesallaed ieecsiaerv rrlfdayvea vtsdprearv
      121 tfvevlgvsa vvdehcklwr alwtefltge aeravergea edrdhrvdvm vmvgtvhelm
      181 ahharrcrra rpgevsgelt qlalsmlgpq rsqe
//
LOCUS       WP_457655614             174 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655614
VERSION     WP_457655614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..174
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18200
     Region          9..>138
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mptttgplpf ttprldalpl dpayaeemaa vladpalyaf tgggppdpat lrsryerqsa
       61 gspdpaelww nwvlrvradg rlagyvqatv rgpraeiawv vgtswqgrgy aseaakglaa
      121 hltsaggvrt lvahvhpdha aseavasaag laptgewedg errwtgnppv pgsr
//
LOCUS       WP_457655618             294 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655618
VERSION     WP_457655618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30624
     Region          12..292
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mnegpstgrp velrhlrafl avadelnitr aaarlrltqp avsrtlaale rhlgvrlvdr
       61 sthhlaltpd gvafrdkaaa avaafdeala pgrlrtwplr lghawsafgp yttpllrtwq
      121 erhpgtplel lriddrtagl trgevdaall rgpvdapglv tevlftevrv aavtadgpla
      181 graslaladl adgpvvlntv sgtttvglwp pharpaatlt vgntddwlta iaagrgsgis
      241 tastatlhph agvayvpldd apgvpvllar rdapghpalp qlaalaseii argp
//
LOCUS       WP_457655616             531 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457655616
VERSION     WP_457655616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 531)
  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 531)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..531
                     /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=54660
     Region          170..369
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrpshrptal allisaaatg tltlwgvaaa pdtvrtplaw gagaaavlls vcvavtvhtl
       61 gtartlralr aadaqrftse tsrlvsssav eaqrftaeta rikgaasaet arvaaearae
      121 neriatdaaa eqarlqvtvd rltaratrae tersaavaac anaagrmqal atsmladlre
      181 mehrhsdesv lgdllhldhr taqagrlads iavltgarsg rrwakpivme silrgamgri
      241 gsyqrvrlhs tsdvaiagha aegvmhalae lldnaanfsp ptaevhvyve evpagivitv
      301 edsglvmsev qlrraeravs aenqdltnls gtrlglavvg rlarkhgltv sfrpsarggt
      361 galmmlpqel isratapaaa aaptataaip aqtgpdqaqd ragttapata tastpaepep
      421 shasaagtdt sdaaptarsl aeddastppt pvaesesest gavpafgesg lpkrrrgrtl
      481 aaaeartgna tpggadtpra rttdpkvqaa rfstfskavr ansphpegnt r
//
LOCUS       WP_457655624             246 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655624
VERSION     WP_457655624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25475
     Region          15..234
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mstnaaadpa hrprtvvals gvtkeypgpv aalrgvdlav eegellgivg psgsgkstll
       61 hiigtldrpt agsvhiaghd vaalsdrrls alraqhvgfv fqafhlvpgv sardnvaegl
      121 lysglsrsar rrraaealdr vgladrldhk phqlsggqkq rvaiaravvg epallladep
      181 tgaldsasga avmellrdln qegatiavit hdteiarelp revrirdgrv vadvihgtaa
      241 atgagr
//
LOCUS       WP_457655625             354 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Streptomyces
            griseus].
ACCESSION   WP_457655625
VERSION     WP_457655625.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..354
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36822
     Region          49..349
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkrgravtaa vavavlaata gslaltrlgp deetggaknt glppatapve rgdlrdsaqa
       61 dgtlgydker kvnagaagtv twtprtgstv ernerlyeid grpvrlmygs gpmyrtlkag
      121 dkgrdveqle rnladlgytg ftpddeytel taaaverwqk shgakqtgkv gpaditfapg
      181 kvriksigag lgeqaqpgap vlettgseri vtfrldvaes rlaktgtkvt vdlpdgttaa
      241 gkvssvgrta kqgddpqdds pkvtltvsfd epdevdgfdq apvtvnltge tredvltvpv
      301 nallalpggg fglqvvrggt vrevkvelgm faegrvevsg gglregvkvg vpki
//
LOCUS       WP_457655632             523 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457655632
VERSION     WP_457655632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..523
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56475
     Region          20..521
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtavndvtat ahalgssrtf welierraal tpdrpvllqe drsltfgelr draervaagl
       61 ygmgvragsv vawqlptrle tallsfalsr lgavqspvip fyrdrevrfa lresgaaffa
      121 vpgvwrgfdh tamaeriaag lpdpprvfea ydvlpdgdpa vlppppepac geevrwiywt
      181 sgttsdpkgv lhtdrsliag gsclahalql saddvgsmaf pyahvagpdy tvmlllygfp
      241 avlfeqfalp dalaeyrlhg vtvaggstaf yamflaeqrk apdrplipsl rllagggapk
      301 ppevyhavvr emgvqlthgy gmtevpmitm gapddtaehl altegrppqg meiritdehg
      361 kplpygvege vrlrgeavcr gyldpaasaa afdaegflit gdlgrvresg hltltgrlkd
      421 iiirkgenis akeiedllht hpavadaavi glpdperger vcavveqppg appltlaels
      481 ahlreaglsv hkvperlell dalprnetlr kvlkyrlrer fgg
//
LOCUS       WP_457655634             431 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457655634
VERSION     WP_457655634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  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 431)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..431
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=45109
     Region          <200..414
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mttlssgfar arrwlrdhpl afdaalalga lvamiggsfa dpgtghgptf gtrtpeplsv
       61 llmvlaalal vlrrrrpmav laatgflsat eyvlmdppap vvmsavialy tvasrtdrpt
      121 twrvglltmg gltgaamvfg stpwysqenf gvfawtglag aagdavrsrr afvdairera
      181 eraertreee arrrvaeerl riardlhdvv ahhialvnvq agvaahvmdk rpdqakeala
      241 hvrdasrsal nelrvtvgll rqqgdpeapt epapglavlg elvttfrnag lpvevarayr
      301 dplpaavdla ayrviqealt nvrkhagaga kaevsvvrvg ataeitvldn grgsagrppg
      361 sgaagtaadd gldsgghglv gmrervtalg galtagpryg ggfrvhailp veartgeper
      421 pgtaggtgir r
//
LOCUS       WP_457655633             341 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457655633
VERSION     WP_457655633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 341)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..341
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36855
     Region          <269..331
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhfttediar vrvatgpdpl weivnsfhvl ltgakplvfg dwrrrvlhrp ppairplgpl
       61 lpprgffpdf ltpdlrgdld lphavdtvlg ttrtvlrgdl rrlaaarprs rplpaetral
      121 adgrpqdlrr lgeallgyhr qalapfgpri rerldadltv raravlsggt eallqslrpv
      181 lrwrppvlea dypvdqdlrl dgrglllqps ffcvrtpitl aceeltpviv ypvehslgwa
      241 adrdtscgae gaegpdgrgg glgalmgctr aavledvvng rttgdlarrl gispaavsqh
      301 tavlrgsgll lsvrrgrhvl htvtpkglal ldhphgtpva g
//
LOCUS       WP_457655638             260 aa            linear   BCT 27-JAN-2026
DEFINITION  adenosylcobinamide-GDP ribazoletransferase [Streptomyces griseus].
ACCESSION   WP_457655638
VERSION     WP_457655638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Cameron,B., Blanche,F., Rouyez,M.C., Bisch,D., Famechon,A.,
            Couder,M., Cauchois,L., Thibaut,D., Debussche,L. and Crouzet,J.
  TITLE     Genetic analysis, nucleotide sequence, and products of two
            Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide:
            dimethylbenzimidazole phosphoribosyltransferase and cobalamin
            (5'-phosphate) synthase
  JOURNAL   J Bacteriol 173 (19), 6066-6073 (1991)
   PUBMED   1917841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001250
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..260
                     /product="adenosylcobinamide-GDP ribazoletransferase"
                     /EC_number="2.7.8.26"
                     /GO_function="GO:0008818 - cobalamin 5'-phosphate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0051073 - adenosylcobinamide-GDP
                     ribazoletransferase activity [Evidence IEA]"
                     /GO_process="GO:0009236 - cobalamin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25633
     Region          7..258
                     /region_name="CobS"
                     /note="Cobalamin synthase CobS (adenosylcobinamide-GDP
                     ribazoletransferase) [Coenzyme transport and metabolism];
                     COG0368"
                     /db_xref="CDD:440137"
ORIGIN      
        1 mtslnshglr fafgtltvlp vrvtrwdrat aragmlcapl agfvvgllaa algslsllag
       61 pgpllaavas vavpaaltrg lhldgladta dglgsgkpae dalrimkqsd igpfgvitll
      121 lvllaqvavl felygqgwah galgavvaav aarlaltlas rqgvpaarpe glgatvaatv
      181 pagrallavv vtvalcaaag allgpyaalr halavlgala aaelllrhcv rrfggvtgdv
      241 fggveetaat aalvvltlgt
//
LOCUS       WP_457655640             327 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655640
VERSION     WP_457655640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /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=35627
     Region          1..327
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mraarlikmv lllqarpamt aaelaaelev sertvtrdaq alsdagvpvy aergraggyr
       61 lvggyrtrlt glardeaeal flsglpaalr emgledaasa arlkvsaall pslrdasssa
      121 arrfhldaps wyhepetpdl lpaiadavwd drllraryrr gggrdhagte varelapygl
      181 vlkagvwylc aragedfrvy ridrftaadp aderferdes fdlpgfwaer aagfarsllr
      241 tevtvrvser ggrmlayagd raaaaaalae asepgsdgwr tltlpvesld vaygqllalg
      301 pelevvapee lrarfteaae rlrelyr
//
LOCUS       WP_457655644             422 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457655644
VERSION     WP_457655644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 422)
  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 422)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..422
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45438
     Region          18..202
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          201..420
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mkvfsgrlrp smvaagrglf lsvaglagsi tlfvlavlsi sfillgigvf ttpvvleavr
       61 khanqrrlwa vtwsdvripv pyrpfpkdlr tgvtgqvert slmlkdpatw rdlqwllvdm
      121 tagtvvafla aglmiypveg lvlaaglwhv frddpywygf vpvdsqltgl aalalgivlf
      181 hvgmwasrpl lrlhfvlart llaptqdqel eqrvqrltet rheavdtaas elrrierdlh
      241 dgaqarlvam gmnlgtieal iekdpaqakk mlamaressa ealtelrdlv rgihppvlae
      301 rglgdavkal alrlpvasev tvelpgraea pvesaayfav sealtntvkh aaatriyvdl
      361 hhaegmlris vtddgrggav vgsgsglsgi errlgtfdgv lavsspvggp tmvtmeipce
      421 ls
//
LOCUS       WP_457655646             250 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457655646
VERSION     WP_457655646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..250
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27402
     Region          10..136
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtkpvqarsf daiaaaydah rpsypptlfd aieelagvel agarvadvga gtglgtarly
       61 ergarvtave pgdgmaeqfr rslpdvplvr gdgnnlplrt gsmdlityaq awhwtdpars
      121 ipearrvlrp ggalalwwnd gdpsvewlve qenrmrvffg veipaapnhr arfraalpdg
      181 ldfrtrqvaw srrvpvdahi anmathsdfl igdpvevrdf fdrerallaa lfpdgeveea
      241 ylvslavahp
//
LOCUS       WP_457655651             135 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Staphylococcus capitis].
ACCESSION   WP_457655651
VERSION     WP_457655651.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus capitis
  ORGANISM  Staphylococcus capitis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Staphylococcus capitis"
                     /db_xref="taxon:29388"
     Protein         1..135
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15528
     Region          17..114
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(64..66,76..77)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mtefmeevli ddnmvfdidn lkgflndtss fgfiakennk iigfaycytl lrpdgktmfy
       61 lhsigmlpny qdkgygskll sfikeyskei gcsemflitd kgnprachvy eklggkndyk
      121 deivyvydye kvink
//
LOCUS       WP_457655652             592 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding SpoIIE family protein phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457655652
VERSION     WP_457655652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 592)
  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 592)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18599219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..592
                     /product="ATP-binding SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=61483
     Region          31..446
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          472..584
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 maggggpphp aplgrlagvf aaasrerars reaalaavrd avggsldvaa tcraladalv
       61 pgfadlavie vvdeilrgaa ppvgplppdt plcraasgrc aavrdgaeng sgaggrrara
      121 gavrrlpart phalavadlr prlvpigpdt pwldadpdga gaaaqagahs livvpltlrg
      181 avlglvslyr caaaepfded dvtlattaat raalavdnar ryerehvias tvqrrllpqa
      241 erqqaaveta hvllpgrdsg rwfdaialsg artalvvggv ageglqsaia mgqlrtviqa
      301 lagldlepee vlarlkdtad rlageraalp pddslhgepl sagcvygvyd pftrtctlar
      361 aghpapliig pdgrpvdldv pegpglfsad salfapatvt leegsllafc taellsgdra
      421 aeritrtlar pgrslrqlgd divyalpddt rsagaallla rtgtvsehrv atwdlaqdra
      481 tpatarvlvr drlqgwglde dtvdateliv selvtnavry gtpplrlrll ldstltcevh
      541 dgstaaphlr hartvdeggr glfivsrlas hwgarhgpdg kvlwteqelp ga
//
LOCUS       WP_457655657             329 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457655657
VERSION     WP_457655657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34230
     Region          1..307
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mstptprttd afgpaspvls vapvtlpapd ravdlqirvs vpltaltalt gegrlpvill
       61 shgqgfsnnl sslngyaplv sfwaahgfav iqpthlsstt lklpadtpga pmhwrsraed
      121 isrlidrlde ieaavpglag rldrdriava ghsmgghtag lllgarltdp dggtevdlad
      181 srigagvlla gpgrggdalv pamaemlpfl ttadfsrmtt ptlvvngekd gsthltvrgp
      241 awhtdpytls pgpktlltlf daehglggis gydvaettde sparvaalar lswaylrsrl
      301 yaddaawqaa realasgpda fgrveskeg
//
LOCUS       WP_457655659             357 aa            linear   BCT 27-JAN-2026
DEFINITION  2-oxoacid:ferredoxin oxidoreductase subunit beta [Streptomyces
            griseus].
ACCESSION   WP_457655659
VERSION     WP_457655659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Chen,P.Y., Li,B., Drennan,C.L. and Elliott,S.J.
  TITLE     A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes
            C-C bonds from CO2
  JOURNAL   Joule 3 (2), 595-611 (2019)
   PUBMED   31080943
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Yan,Z., Fushinobu,S. and Wakagi,T.
  TITLE     Four Cys residues in heterodimeric 2-oxoacid:ferredoxin
            oxidoreductase are required for CoA-dependent oxidative
            decarboxylation but not for a non-oxidative decarboxylation
  JOURNAL   Biochim Biophys Acta 1844 (4), 736-743 (2014)
   PUBMED   24491525
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Fukuda,E. and Wakagi,T.
  TITLE     Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from
            Sulfolobus sp. strain 7
  JOURNAL   Biochim Biophys Acta 1597 (1), 74-80 (2002)
   PUBMED   12009405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..357
                     /product="2-oxoacid:ferredoxin oxidoreductase subunit
                     beta"
                     /EC_number="1.2.7.-"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38530
     Region          18..355
                     /region_name="PRK11867"
                     /note="2-oxoglutarate ferredoxin oxidoreductase subunit
                     beta; Reviewed"
                     /db_xref="CDD:237006"
ORIGIN      
        1 mpdtdelrhn ellqlvpkae akqsmkdfks dqevrwcpgc gdyavlaavq gfmpelglak
       61 enitfvsgig cssrfpyymn tygmhsihgr apsiatglat srrdlsvwvv tgdgdalsig
      121 gnhlihalrr nvnlkillfn nriygltkgq ysptselgki tkstpmgsld apfnpvslai
      181 gaeatfvart vdsdrkhlts vlraaaehsg talveiyqnc nifndgafev lkdkeqaaea
      241 virlehgqpi lfgsqepkgv vrdpatgdlr vvvvteenrs qilvhdahaa spttafalsr
      301 ladadtlhht pigvlrsver pvydtlmsdq ldaaveregk gdlasllagn dtwtvvg
//
LOCUS       WP_457655661             321 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 1/NuoH family protein [Streptomyces griseus].
ACCESSION   WP_457655661
VERSION     WP_457655661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   3  (residues 1 to 321)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="complex I subunit 1/NuoH family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=34196
     Region          3..321
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mndvldvalr laivfvvflv apllvgqteh kvmahmqgrl gpmyaggfhg waqlvadgvk
       61 faqkedvvpa aadrrvfqla pavallpyll vlvvipvgpe gavgqavdag iffvlavmgi
      121 gvlgslmagw asankfsllg glrtaaqlls yelpmllaaa svamaagtvs ltgildafaw
      181 wwlpwqivga lvffvaglae lqrppfdmpa adseiifgay teytglrfal fllaeyagiv
      241 ilcalttvlf lggwhgpfga dglgwlwtll ktallafvvi wlrvsyprlr edqlqklawt
      301 tlvplalaqi altgivkvai n
//
LOCUS       WP_457655663             528 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Streptomyces griseus].
ACCESSION   WP_457655663
VERSION     WP_457655663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..528
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=54574
     Region          27..524
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mtadlattpg slvaytaaad apslvqsidw laiapptlta laalvvlvad lflpahrkrl
       61 lgygtltala aalalllplr agdratfcvt tgtracsyta dhftlviqal vlggaflivl
      121 lslddtrklp ageywfllla saagaallpa srdlatlvva levaslpafa lvgikrgdrr
      181 sseaalkffl ssvvatavml lgvsfvyatt gtlhlteiav rlddvspvld tlaktgvalt
      241 lvgfafktaa apfhfwvpdt yvgaplpiaa ylsvvgkavg fsglilvtvi afpsyadvwg
      301 palavlaalt mtvgnvaalr qradrarsav rllawssvaq agyllvpiaa aayssdqqig
      361 stvayalmya vvnlgafava alvarthpgn rlsdyrglya trplaalalg ffllclaglp
      421 pgiiglfakv tvfsaavdag lgwlavvmav nvvialyyyl qwtailfrtp dgatetaeea
      481 tgaaasapsr rfrapapltt aivltavagi llsgvpqtvl rfasvnlf
//
LOCUS       WP_457655667             282 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655667
VERSION     WP_457655667.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..282
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=29840
     Region          3..282
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 marklaviga glmgsgiaqv saqagwdvvl rdvtdaaltr grdgikasyd kfvskgklda
       61 adaeaalari ttttdldaaa dadvvveavf eklevkheif rtldkvvgeh tvlasntsai
      121 pitkiaavte rpervvgvhf fspvpmmqlc elvrgyktsd etlatarefa esvgktcivv
      181 nrdvagfvtt rlisalvvea aklyesgvas aedidiackl gfghamgpla tadltgvdil
      241 lhatgniyte sqdekfaape lmrrmvdagd igrksgqgfy ty
//
LOCUS       WP_457655669             399 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457655669
VERSION     WP_457655669.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 399)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..399
                     /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=41728
     Region          133..395
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mltslrpdrd avalavsgll gglllwllgl htqgghssla pwvtlvplsa maaaellrrt
       61 aprtaltiga lalvadqftw gnlatilmft dvvyaavlyg tpaaarrlpv atllvtvast
      121 igflawfrkp ealliglvig lvtfipaltg vsvrshrtaa daarlaaaqt arlaemdrtq
      181 aviaerarma relhdmvanh lsavaihsta alsiddpkts rnalkviren sveglaemrr
      241 ligllregge drapaaaptl aaldtlieqt nvngasgglv ctledtrdpa sgalptpvel
      301 aayrivqesl tnalkhaapg pvvvrlgrtg elltvevtsv fgsrpgptap gsgaglvgmr
      361 ervallggti taraepdgge tkiwrvrael pvtertire
//
LOCUS       WP_457655671             464 aa            linear   BCT 27-JAN-2026
DEFINITION  MraY family glycosyltransferase [Streptomyces griseus].
ACCESSION   WP_457655671
VERSION     WP_457655671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..464
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49018
     Region          42..322
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            101..102
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            227..230
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(298,312..315)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mgqpvrdyll tlcvtaavty lltgpvrkfa iavgampair ardvhreptp rlggiamfgg
       61 lcaglivadh lfnlngvfel sneprallsg aaliwligvl ddkfeidali klggqmiaaa
      121 vmviqgltil wlpipgvgtv altqwqgtll tvalvvitin avnfvdgldg laagmvcias
      181 aafflyayrl wygygieaaa patlfaailm gmclgflphn mhparifmgd sgsmliglvl
      241 sagaisitgq vdpdlmklfe gsereathal lpvfiplvlp ltiiaipaad lvlaivrrtw
      301 ngqspfaadr ghlhhrllei ghshsravli myfwsaliaf gavgysvhsa sswivfviia
      361 ssavglalll mprftpraph wanrfvppry rhraaeqapa pspsngekpa pvtsgaqqga
      421 adaqmgeeaa erapvavgvs gvngataiga rsrlpdrrsi dssr
//
LOCUS       WP_457655675             588 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457655675
VERSION     WP_457655675.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..588
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=62218
     Region          14..276
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,76,81,86..89,103)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,84,102..105,109,111,147,149,
                     151..152,154,164..165,168,185..188)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,84,102..105,109,149,151..152,
                     154,164..165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,109,111,147,149,151,168,185..188)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(164..172,181..188)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mseeaparrv idgrftlver lgsggmgmvw rardealhrd valkevrppd paledydpeg
       61 artlrarvlr earalarvdh pnvvtvhhiv dpgeegypwi vmelvagssl herlaagpme
      121 paeaaelgrg ilsalraaha vgiqhrdvkp anvllrtdgr pvltdfgiaa irestsltat
      181 galigspdyi aperirgteg dpssdlwslg mmlyvavegr hplrrattla tlaavldeei
      241 ppparagalt pvltalltrn iparpdaeal drmlaeaart ggspaptpte pvrerpasvh
      301 ttptqtasvs ppaapedrvp tgyghghgyq qvvtgpfatp gapggpgapg speerqrrvl
      361 rrvrmisaas svvsavviag vilwmvdpfs kgsdsddrpr dsasapqasa papaadgaga
      421 sdpsdpsdsp dekdvpepen lltpdgaraa ikalkplmgg tkvtdftlyg ehasaeaplk
      481 snaalydrfs yrdgraendd mggtlmsgsa tidlnsvdwd vlpallktae ktlnvdepes
      541 ryvivdpasp fhedrpvlrv yvsdshggaf ltaeldgrvi eknprpkg
//
LOCUS       WP_457655681             166 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655681
VERSION     WP_457655681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  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 166)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 166)
  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 10548922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..166
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17954
     Region          103..157
                     /region_name="SH3_3"
                     /note="Bacterial SH3 domain; pfam08239"
                     /db_xref="CDD:462405"
ORIGIN      
        1 msplsrpsrl rrlglcvatg tlaaltaaap aamaadpqpv gqraeatapd ptsdelsasa
       61 lqreheaqqk earqearqqg qakpqapkrt ykgrviakpy lllrdkptrs srivgsvkyg
      121 svvhifcktk gdnvdgnnrw ylltdgtwaw gsaryienig sapkwc
//
LOCUS       WP_457655682             485 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            griseus].
ACCESSION   WP_457655682
VERSION     WP_457655682.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..485
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50863
     Region          <74..484
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 miryirraaa lcllllvall vnaarvqlfe adelddnpan rrnsiarydq prgnilvgdr
       61 pvtgnketre qlsfertylh gplyapvtgy asqtygttli enaedavlsg tdsllaplpf
      121 wneltrgrqp ggdvvttika smqeaaydgl rgrrgavaal dpstgailal vstpsydper
      181 lsgtgaavtd awtrlnaaks lpmlnrairq typpgstfki vtaaaaldsr avtdadaatd
      241 tpspyvlpgt sttlpnessg cenasladai rvscntvmah lgvqvgldgm vdaaerfgfn
      301 daglripsgv arsnfdtdms edqlaqssig qfnttatplq mamvasavan ggdlrrphlv
      361 drvttnngdt vrqegsrpye ramnpstavq lqrmmvdvve sgtganaaid gvkvggktgt
      421 aqhgvdnsgl pyawfiswaq apdsgrpava vavvvedasa dradisgggs aapiaravme
      481 aalee
//
LOCUS       WP_457655693             333 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655693
VERSION     WP_457655693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34289
     Region          26..249
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtttgeaaad avgvadgtdg agapvirtrg ltkryrggql avdgldlavp agsvfgflgp
       61 ngsgktttir mlmglidpts gtaevlgrpm ptaartvlpe vgaliegpal ygflngrdnl
      121 lrydradpta dprtrrarvd dalarvglaa asgkkakays lgmkqrlgla aallrprrll
      181 vldeptngld pqgmreiral vrelaaegtt vflsshllde ieqvcthaav margrlivqg
      241 pvadlaagar grlavttpdp gdaarilreh gltglsadgd rltadappaa vdladlnaal
      301 vtggmrvrff gvergsleda fvaltgegfd vag
//
LOCUS       WP_457655702             258 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655702
VERSION     WP_457655702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..258
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26906
     Region          3..234
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 malriereaa agvalvtldr paklnaidle tagelislwr glrfdeavra vvltgagtra
       61 fctgidrnve vpqppspyav ddpllrigpk andlwkpvia avegmacgga fyllgeaefv
      121 vasreatffd phttygmvsa yeamamaqrm pygevarmal mgtaervsae rayavglvse
      181 vtepggavaa alraaaviag cpteavqgtv ravwaakeaa rtqamaqapa lialgnlppe
      241 rqaelfgarg gggeprvr
//
LOCUS       WP_457655703             408 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457655703
VERSION     WP_457655703.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..408
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41916
     Region          1..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdaactaeqh eirrtlrell araagpgtip aavgaaegyd pvlwrrlard lglpglalae
       61 eyggagctat elalaceetg rallpsplla taalaaplia algtpdqraa llpriaggal
      121 taalavpggs latalgltgd nrdgawaggg raggiqaray gsddsrgegg wrlygeaerv
      181 ldghsaglll vaahtggypr srtllflvph dagglvrtrl taldetrpla rvelrdtpat
      241 llgaddtadt aealaavgrt aaailaaeav gtaasalert veyvktreqf gravgsfqav
      301 khrladlyvr veaarsaayh aarepeagpl alaqaleaar ittgeavqlh ggigftwehe
      361 ahrhlkraag dellfgpvhr lrdhaaqrag lfepgrmpla aapgagvr
//
LOCUS       WP_457655700             275 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655700
VERSION     WP_457655700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..275
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29392
     Region          2..110
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,82,86,92,96,99..100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          121..268
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mftigdfary grvsprmlrh ydaigllhpd rtdpatgyrr ygaaqlarln riialkdlgf
       61 tlqqvgavld eqvgpeelrg mlrlrraela eavaaastrl arvearlrsi esegrmpadd
      121 vviktvpavr vaeltgtaas yqpedigpvi gplyerlfpl legaglrptg pgiaryedap
      181 ggggaitvha gvtvsapaga vgetgvrvve lppfeaativ hrgamddvlp tahtlarwld
      241 angyrptgyt revnlecpad rsawvtelqe pvaka
//
LOCUS       WP_457655704             230 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxine/pyridoxamine 5'-phosphate oxidase [Streptomyces
            griseus].
ACCESSION   WP_457655704
VERSION     WP_457655704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liang,J., Han,Q., Tan,Y., Ding,H. and Li,J.
  TITLE     Current Advances on Structure-Function Relationships of Pyridoxal
            5'-Phosphate-Dependent Enzymes
  JOURNAL   Front Mol Biosci 6, 4 (2019)
   PUBMED   30891451
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Safo,M.K., Musayev,F.N. and Schirch,V.
  TITLE     Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a
            tetragonal crystal form: insights into the mechanistic pathway of
            the enzyme
  JOURNAL   Acta Crystallogr D Biol Crystallogr 61 (Pt 5), 599-604 (2005)
   PUBMED   15858270
REFERENCE   3  (residues 1 to 230)
  AUTHORS   di Salvo,M.L., Ko,T.P., Musayev,F.N., Raboni,S., Schirch,V. and
            Safo,M.K.
  TITLE     Active site structure and stereospecificity of Escherichia coli
            pyridoxine-5'-phosphate oxidase
  JOURNAL   J Mol Biol 315 (3), 385-397 (2002)
   PUBMED   11786019
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..230
                     /product="pyridoxine/pyridoxamine 5'-phosphate oxidase"
                     /EC_number="1.4.3.5"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_component="GO:0032991 - protein-containing complex
                     [Evidence IEA]"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:1902444 - riboflavin binding [Evidence
                     IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0036001 - 'de novo' pyridoxal 5'-phosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0042823 - pyridoxal phosphate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24999
     Region          27..230
                     /region_name="PdxH"
                     /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase
                     [Coenzyme transport and metabolism]; COG0259"
                     /db_xref="CDD:440029"
ORIGIN      
        1 mtdntaapaq ppspgfrdll haqrvwdvel pafdpadapp dpvrlfhtwf aeavaagqpe
       61 phamslatad aeglpdvrtl llhgadergf hfashatsak ghqlaarpha algfywpaqg
      121 rqvrvrgpvl rctpaeshad lharstgala aaltgaqsev vgsvaelhra adaawerara
      181 epdteaptwt ryvvepaeae ffqgdarrrh irlryrrtgg gdwtrellwp
//
LOCUS       WP_457655706            1213 aa            linear   BCT 27-JAN-2026
DEFINITION  CHAT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655706
VERSION     WP_457655706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1213)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1213
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1213
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=127876
     Region          512..1204
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 mrrsgevtgw aflaevdgvr haglavgqag lgpftgagpg gslatlacvr glptltslda
       61 lplvgpmdar wcvhrdaegv vsvfgpgglq laydlalelp pgwlesvtga gslvlvvshv
      121 lpssddmaav ltyetqqgmv cagrvrfgpp gdetagpppf ahvldpvsdl lelvlhvrdr
      181 vlsldvarrr arglertrrs lgeghwltag allgllvaqa arnrgpsadl rylywrlvae
      241 vaeecgvdaa wreaalrtve naapvlaerc erpvfedade lagrlierle gapggtsgva
      301 pdsasgsspd laaallaaar lrlavrgped lggdayagae gsvraaqlaa dlyrsplyrp
      361 wsggawplrf darlraetre llvratesdd revgpgsalr prilaalaqv taeeghggee
      421 erageeqsgg geqgggeeey ggvdratara afdalfavra pgppdltvfl lravddvpds
      481 fvdviranvf gsdvpaflaa hggavaartv dqainlarer adrpllraal dwadrspllp
      541 gpahrrqlie arlhalpddp tdcpgpgplp dpdsfpagwt paqrsaallh laahardrrq
      601 palgaallrq arpedgagvr llaadlhrla veqgepvagp vpfpwghsty aalsyaslnq
      661 qdlaracllp vlhdlprlrg edlrnavyai ivdlpnfdts gapalgevlr dlvhaavwql
      721 tveiesmpva lmlglhqagk gpeagawrri dgaitrpahi enyvgklral espsavggat
      781 anlldaldgd hrpggegaea gdgreefarn lrrrissfid delrsrsaaf vddehvwart
      841 gellddrtvl ltwflptavn gaavllavtr egsaitvqlg egegeseggg ydddggggpe
      901 gaavsadrhp vadlveavrt everdplfge vtpegrrllt ghelplpdgd qlaawrtrgk
      961 drlllwphga lhylpvalcs aggrtiaddw tvvtvaglea llpatgpvrp rrtavlasgs
     1021 ggvpyglpae paleehartv aaavgahalt gpaatraall aelatadvvh lavhgtmdqd
     1081 apwlhclylt pdedddgrlf ahdfleldls gvrlvtlaac esalgrfdra dnvrgvpaal
     1141 itagvqavvg clwavrpepa tyffqhlhgr agladapeqa fraaqtatra rypayrdwga
     1201 ftyllgrseg ata
//
LOCUS       WP_457655707             742 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate--CoA ligase family protein [Streptomyces griseus].
ACCESSION   WP_457655707
VERSION     WP_457655707.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     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=78252
     Region          50..738
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt tgfrarvvac geephaavvs lptasapggl dvsgrplhlt vpdldrffrp
       61 rsvavvgasd aegrpntgit rqlvdwagrv garlhpvhpt rrtvfgrdcf asvaaipdpv
      121 dlavllvadp lpvieelgea kvpfavafas gfaetgeaga aaqarlaaav ersglrllgp
      181 ntnlnaferf redldgpaia litqsghqgr plhalqelgi rlshwaptgn eadletadfl
      241 ayfaqlpevg aiacyveglk dgrsfllaad raaragvpvv avkvgrteag artaashtgk
      301 ltgadqvvda amrqfgvvrv dgldelqdta allararppk adgvalysis ggtgahfadl
      361 ataagltlpt lspakqdelh twipeyltva npidngghpv gdwrgrkiid ailadpsvgv
      421 licpitgpfp pmsdrlaqdl adaaeatdkl vcvvwgspvg tedayrttll gssrlatfrt
      481 arncvtavka yldhhrftdr yrspfedapr tpspsfrkaq nllrpgqqls ehaakqllra
      541 ygirvpreql vtsaaaavra agpvgypvvm kasgprlahk telglvkvgl tsasqvrday
      601 reltdiarye svdldgilvc qmidrgvemm vgvthdalfg ptvtvglggv lvevlhdtav
      661 rvppfgeqqa rdmlgelrgr allegvrggp pvdvdalvev vlrvqrmale lgddlteldi
      721 nplvvlgrgq gavaldalav cr
//
LOCUS       WP_457655708             294 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655708
VERSION     WP_457655708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..294
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=30086
     Region          36..287
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mpvsgeagag pdehartglp dagpeaagpg pgaatvlhsl dggvswitln rpeamnavtw
       61 dqreriiall adasadpgvr avvltatgrg fcagadlrga paparervpg dvartirlga
      121 qrliaavldc ekpviaavng taagigahla facdlvlaad tatfievfvr rglvpdggga
      181 yllprlvgpq rakelmffgd altaadaerl glvnrtvpgg elealaeewa grlaagptra
      241 laltkqlvna sldgdrattf aaeaaaqein mttrdanegv asfverrspe yrgc
//
LOCUS       WP_457655710             459 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655710
VERSION     WP_457655710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46503
     Region          69..447
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(79..80,83..84,87,119,174..175,177..179,182,200,
                     203..204,207,284,287..288,291..293,296,318,322,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mekptgrasi pdaardtrts pvpnpdrrpn pspapldggg pggpsgtgpg agpsfgsapg
       61 raglwnrnfr yffvartval fgdgmipval tagllgagrp assvgfalaa wmgplavfvl
      121 fggvladrft prrmmiiada lrligasvla vtfatgnppl wavyvlcsva gvgaalfqpg
      181 vastvprvst dvqranavlr vaealmtmag pafagalvgl asagavyaan aatfavsgac
      241 lflmrlapap hddavrgtfa aelvdgwref rarswlwgvi avwtvygfav lgpmlpltav
      301 lvteahgsga ygmlmavnga gsvvggllal rlrpshplaa gavalplvav sllvlalglp
      361 vpvlaagqll aggaaafwlv mwsttvqtrv ppealnrlha ydvagsllmv aagralagpv
      421 aeavgapell vaaavinmgv vavllvarpi rrlkrighi
//
LOCUS       WP_457655714             374 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655714
VERSION     WP_457655714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 374)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..374
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39983
     Region          92..230
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mtvpettaai epeagaealr phaedafade lkaleaaddr prparwrlsp wavatylqgg
       61 alpdgtvitp kyvgprrlve vavttlatdr allllgvpgt aktwvsehla aavsgdstll
      121 vqgtagtpee avrygwnyae llahgpsrea lvpsplmram segmtarvee ltripadvqd
      181 slitilsekt lpvpelgqev qavrgfnlia tandrdrgvn elssalrrrf ntvvlplpat
      241 pdaevdivsr rvdqigrsld lpaapeglae irrvvtvfre lrdgvttdgr tklkspsgtl
      301 staeaisvvt sglalaahfg dgvlrpgdva agilgavvrd paadrvvwqe yletvvrerd
      361 gwkdfyracr evsa
//
LOCUS       WP_457655715             468 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Streptomyces griseus].
ACCESSION   WP_457655715
VERSION     WP_457655715.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  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 468)
  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..468
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..468
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48277
     Region          69..>94
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mllshggeps ptggpvarws veqvlalapd dasrtagtrl gtagpwsgtg rdgagavwgl
       61 ckgsgstpyr tvvdttgpac scscpsrkfp ckhalgllll lasddtafrp gepadwaaaw
      121 iegrrgraae qagaatggga srgpadaaar kraerraerv tggaeeleqr ladllrggla
      181 atdrsgyalw detaarmvda qapglaarvr elgaitgsgp gwpvrlleec gllhlldtaw
      241 lgrerlpdpl aatvrtrvgl pmsaegvpvr drwlvlaqyd tpdgrivtrr iwlygresgr
      301 talllsfgaa grspvqslpv gatidaeltp ypgggqlrae lgeqfgttap agpppgiaaa
      361 aapavygtal redpwldacp vtlrdvipvp sedgwqvada hadsalpiap aalsrpglwk
      421 lvalsgggpv tvfgeighrg fdpfaawdpg ergevggrtt ggpvvqlv
//
LOCUS       WP_457655720             709 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457655720
VERSION     WP_457655720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..709
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72955
     Region          22..278
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,46..47,80,85,90..93,105)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,88,104..107,111,113,150,152,
                     154..155,157,167..168,171,188..191)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,88,104..107,111,152,154..155,
                     157,167..168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(33,111,113,150,152,154,171,188..191)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(167..175,184..191)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mseaeqsrep qrdkngrlla gryrlgevlg rggmgtvwra ddetlgrtva vkelrfpsai
       61 dedekrrlit rtlreakaia rirnnsavtv ydvvdeddrp wivmeliegk slaeairedg
      121 tltpkraaev glaildvlrs ahregilhrd vkpsnvlise dgrvvltdfg iaqvegdpsv
      181 tstgmlvgap syisperarg hkpgppadlw slggllyasv egcppydkgs aiatltavmt
      241 epldppknag plteviygll ardpeqrldd agarallndv inapdvpapa padstqimai
      301 ppvpaadplv krtpkqpkap kppkqstgsg esgegardrl rgalrsvrna ktpavatgaa
      361 agaaaasass paaatgspva ppkppsppgt stpgapsgaa akgavaapaa pvgapkstat
      421 asasvpgqrp pappastras itdvvprrtl aiiaavvala ilgtilaltl gdgdgngdgn
      481 ggkddtaasa gassggaddk gdtgggsagg kgdgqkegqg kedgrasedp sgegsddpkg
      541 ddpegdegdd paagdslpag ykevtdtrfh ftmampgdfk rtgiagtnsg giynaaqgsf
      601 prvqvdfnss pkddaaaawr gavgsakvls dgykhgsikk veyngyptva dwtfernhng
      661 vrvrvlnrgf kvdakrgysi misckidewd gdacrtlrdt afatftptd
//
LOCUS       WP_457655722             442 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457655722
VERSION     WP_457655722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 442)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 442)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..442
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47062
     Region          25..339
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msrswsrpvh alvgaatala vvtacggadd srargtaddp vpvsfwawtk gsqevvdafn
       61 athdtirvef eeipsgglgg ypkianavka giapdllsie ypqlsafvsq gslqdispyl
      121 tedvkkkflp qtiemttlgg knwavpfdaa pqifyyrkdf ftehsieppa twddfrsaae
      181 qvkkasprtr iatffpddpt ffqamawqag aqwfragtda wridttdpas ertaaywqgl
      241 iddrlvstas sfspewtgsl kqgttvgylg aswsagvlag ivpeqkgqwa avrlpsqead
      301 rpasgmiggs tfavskgstr taaavefalw msthedaika rigastssal paspamvpia
      361 rkafdtsfyg gqdlyglfee agrsigpdwv wgpspgatna algdelgevv gggstlprai
      421 rraheatvad lrkrglkvae gs
//
LOCUS       WP_457655723             331 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655723
VERSION     WP_457655723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35695
     Region          25..327
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstqdterrp gvpgprttpp rdtartgrrs talstgartr laagtllapf falftvamiv
       61 pvgyalwlsl fterqsglgf dgprtvfdgl gnyatalgdq afrdgfwvll gycafyiplm
      121 gggaivlall ldtalararr ffqlalflph aipgliaali wiylytpqls pvvaameagg
      181 fgfdffsseg tlpsivnial wqwlgynvvi fyaalqavdr slleaatvdg agnwriafsv
      241 klplirsslv mvllftiigs lqlfteplil srgsgsavts twtpnmyays aaferndygl
      301 aaaasvlial vaavlsfvvt rfanrrkear r
//
LOCUS       WP_457655733             403 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457655733
VERSION     WP_457655733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..403
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43544
     Region          2..403
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mfreerglll aslvrrfgdl dlaeevtsea ieaalrhwpa egvparpgaw llttarrrav
       61 drlrrdqaya arlavlrada eraeavapap dvagvgelpd drlqlfftct hpalaaedra
      121 altlrclagl ttpevarafl vptatmaqri vrakkkirea ripfrvpgpd elperlpgvl
      181 qvvysvfteg yaassgprlq rlglaeeair larilhrllp aeresaglla llllvharrd
      241 artgpegepv lledqdrgrw drpmieegra lvvraltggp agpygvqaai aalhdeaadv
      301 agtdwpqiva lydvlltltp spvvalnrav avamrdgpea glalldalae eprlrayapy
      361 avargdllsr lgrdgeaaea yrealeragt gperaalrrk lge
//
LOCUS       WP_457655741             326 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces griseus].
ACCESSION   WP_457655741
VERSION     WP_457655741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36125
     Region          1..214
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvklsvivpf fnvqtyapdt lrslranare dvefllvddc stdgtlpllr raaeeipgav
       61 llrhevnggl atarntglda argeyiafld gddwlapghy arllarteal gcdfvrtdhv
      121 rvngssrtvr rvphgphgvv sdprsailpa hrttsvdyaf awaglyhrrl ldrgllhftn
      181 glrtaedrpw iwrlhreaes favlgllghf yrrgvatslt qigdvrqldf lrafdqviad
      241 tatdreaemf lpkavrtyca viahhlgdld kfepavarel ksrgaaalgr lpqrlldeal
      301 dsmdvtratr vrrlrrrpaa kgasaa
//
LOCUS       WP_457655737             391 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Streptomyces griseus].
ACCESSION   WP_457655737
VERSION     WP_457655737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 391)
  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 391)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - obsolete lipid glycosylation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=40109
     Region          23..391
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mntasrpasa frlivtgggt gghtypalta irtlqarlaa sgrtldvlwi gtaeglearv
       61 tsaegipftt vatgkvrrha nplkmvspan vrdmarvplg vaqarsavsa frpdvvlatg
      121 gyvavpagla armcrvplvl heqtvrlgla nrklagsatr iavssestlp llpesvrsaa
      181 vvtgnpvrpe vlpghpdkav talglhsfdr rlptvyvtgg aqgsqqindv vggelpwlle
      241 ranvvhqcgp ahqealsara aglpaplaar yhltpfvgpe lpdvlaladl visrsgagtl
      301 aeltalgkpa vfiplataag neqahnarhl eesgaavall gevtgghlre avgpllddpe
      361 rrgamaaaag ahgrpdaaer lvdvilsaas r
//
LOCUS       WP_457655742            1112 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655742
VERSION     WP_457655742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1112
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=115570
     Region          120..593
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava aavavalaag mtqtavaqpd pkgasgarak drevrhltlv tgdrvtvdaq
       61 gkpvafrpak grenipvqrm snkghtlvip adahrlivsg kldrrlfdvt elsrpenlra
      121 rkdglklivg yrgkqaaaak aqvrdaggte vgrsltslna esvttptada pdiwkaltdr
      181 gtdgervtta agidrvwldg vrrasldksv aqigvpaawk agftgkgvki avldtgtdtt
      241 hpdlkgqvla eknfsdakdt kdrvghgthv asiaagtgak sggkfkgvap dakllagkvl
      301 ddegygddsg ilagmewava qgadivnlsl ggmdtpevdp leaavdklsa ekgvlfaiaa
      361 gnegdgagtv gspgsadaal tvgavddkdq ladfssrgpr igdgaikpdv tapgvdttaa
      421 ippgsliare vgekpagyat isgtsmatph vagaaallkq qhsdwtyael kgaltastkp
      481 gaynpfqqgs griavdraia qtviaetvsv sfgvqqwpha ddkpatekvt yrnlgtsdvt
      541 ldlkatgtnp kgkpapagff tlgadrvtvp aggtaevtlt adtrlggtvd gtysaylvat
      601 gggqtvrtaa averevesyd vsikhlgrdg rpaayadstl frfgvesgnp flspqvvdgt
      661 akirvpkgty vanstvykdp ddvtkgadwi aqpkvavtkn tsltfdarka kpvkvtlpda
      721 kakgelfspd yvveaandav sfgwvmdspa girtlhvgpk itdgslaqhw sgtwskgast
      781 eydiavggtv kqlatgfdrk ftsaqlakvk iamgsaapkk kgsitafpfl ptqgggwats
      841 idqklpgtrt lyvstadkvt wtfdfdqqgp ldadgwptye anyqvgkeaa ykagktysks
      901 vntgvfgplv dkdygvareg neitgslpll adgqgnaggm vftsaktvly rngkklgqnt
      961 dpvtgfesfk vpagaadykl tttvkhsakv nplstrvdaa wtfrskktaf tmlpvstvrf
     1021 tpavgadgrv kagktvsvpv kvhgaaagkn lkslktyvsy nggktwkkvt vkkgkitvkn
     1081 pakgkaisfs akvtdkkgnt ssvkiysayl gk
//
LOCUS       WP_457655743             436 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655743
VERSION     WP_457655743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44161
     Region          48..418
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(57..58,61..62,65,97,147..148,150..152,155,175,
                     178..179,182,256,259..260,263..265,268,296,300,348..349,
                     353,357,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mppastgast iavdasaprs pvtttaapda atherlepgr pgyrrmsfal faagvaafal
       61 lystqallpa vsasfdatag qaswtvsaat galalfvlpl salserfgrr qmmtasltva
      121 vlvgllvpfa psmgalialr avqgaalagl pasamaylae evrpkaliaa iglfvagnsi
      181 ggmsgriltg wvaqawgwra alaavgllal acavvfhlli pkaknfrpgs lnpkalaktv
      241 aghladpllv rlyaigalfm tvfgavytvi gyrlveepfs lpqgvigsif lvylvgtvss
      301 aaagrlvarl grrgalylav stttagllls ladqlaavll glvlitagff aghavasssv
      361 srtattgraq asalyqsayy lgssaggtlg avafhtggwt atvalgllav lgvvsitlyg
      421 trvaraerra lvpatr
//
LOCUS       WP_457655744              69 aa            linear   BCT 27-JAN-2026
DEFINITION  PspC domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655744
VERSION     WP_457655744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Joly,N., Engl,C., Jovanovic,G., Huvet,M., Toni,T., Sheng,X.,
            Stumpf,M.P. and Buck,M.
  TITLE     Managing membrane stress: the phage shock protein (Psp) response,
            from molecular mechanisms to physiology
  JOURNAL   FEMS Microbiol Rev 34 (5), 797-827 (2010)
   PUBMED   20636484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..69
                     /product="PspC domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=7108
     Region          5..>47
                     /region_name="PspC"
                     /note="Phage shock protein PspC (stress-responsive
                     transcriptional regulator) [Transcription, Signal
                     transduction mechanisms]; COG1983"
                     /db_xref="CDD:441586"
ORIGIN      
        1 maaalvrpse grmiggvcag larrfgisag tmrvifvvsc llpgpqflly lalwallpse
       61 ksassataw
//
LOCUS       WP_457655746             546 aa            linear   BCT 27-JAN-2026
DEFINITION  phospho-sugar mutase [Streptomyces griseus].
ACCESSION   WP_457655746
VERSION     WP_457655746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Shackelford,G.S., Regni,C.A. and Beamer,L.J.
  TITLE     Evolutionary trace analysis of the alpha-D-phosphohexomutase
            superfamily
  JOURNAL   Protein Sci 13 (8), 2130-2138 (2004)
   PUBMED   15238632
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..546
                     /product="phospho-sugar mutase"
                     /EC_number="5.4.2.-"
                     /GO_function="GO:0016868 - intramolecular
                     phosphotransferase activity [Evidence IEA]"
                     /calculated_mol_wt=56838
     Region          44..520
                     /region_name="PGM2"
                     /note="This CD includes PGM2 (phosphoglucomutase 2) and
                     PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2
                     is thought to be a phosphopentomutase that catalyzes the
                     conversion of the nucleoside breakdown products,
                     ribose-1-phosphate and...; cd05799"
                     /db_xref="CDD:100092"
     Site            order(48,50,53,147..149,157,294,296,298..299,343,364..366,
                     380,382,384,498,500..502,507)
                     /site_type="active"
                     /db_xref="CDD:100092"
     Site            order(50,147,299,343,364,366,380,382,384,498,500..502,507)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100092"
     Site            order(147,294,296,298)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100092"
ORIGIN      
        1 mqhdliaqar twlaedpdpe traelaalve agdtqelaar fagtlqfgta glrgelaagp
       61 mrmnrsvvir aaaglaaylk argeegglvv igydaryksa dfardtaavm tgaglraavl
      121 prplptpvla yairhlgava gvevtashnp prdngykvyl gdgsqivppa dgeiaaaiaa
      181 vgpladvvrp edgwqtlgee vleaylartd avlaagsprt artvytamhg vgtsvltaaf
      241 aragfpepvl vaeqaepdpa fptvafpnpe epgamdlafa tarraapdli iandpdadrc
      301 avavpdtaae ggwrmlrgde vgallaahlv ergasgvfae sivsssllgr iaekaglgye
      361 etltgfkwia rvdglrygye ealgycvdpe cvrdkdgita allvaelasv lkeqgrtlld
      421 llddlalahg lhatdqlsvr vedlsviada marlreqppt alaglavtsa edlsqgtdrl
      481 pptdglryhl egarvivrps gtepklkcyl evvvpvadaa glpaararga ellagikrdl
      541 aaaagi
//
LOCUS       WP_457655747             478 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Streptomyces griseus].
ACCESSION   WP_457655747
VERSION     WP_457655747.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 478)
  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 478)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..478
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49720
     Region          229..476
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mvfalvglvv lallgavhry lwrrfvgdtt apgsplrrag tvaafvlpll svgamtsgrv
       61 gapfwlqqvl awpgflwlac llyltlallv gevvrpvllr vlagrdrkaa taesgapsat
      121 psgassaprs gtlvevpeet rprteelvps rsagtsdaav rtatepqaep eteattgaea
      181 epstgpdtep apnpaeappa papnpsrrlf vsrvvggaaa aaglatvgyg tygvlrgpsv
      241 rritvplakl praahgfria vvsdihigpi lgrahtrriv dtinrtspdl vavvgdlvdg
      301 svadlgsaae plaalrarhg sffvtgnhey fsgaeqwvdh vrelglhple narveiegfd
      361 lagvndvage tegqgpdfvk algdrdrgra avllahqpvv ihdavehgvd lqlsghthgg
      421 qlwpgnllae lanptvagle rygdtqlfvs rgagawgppv rvgapsditv velasrqa
//
LOCUS       WP_457655750             279 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces griseus].
ACCESSION   WP_457655750
VERSION     WP_457655750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10118426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..279
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31596
     Region          9..259
                     /region_name="Beta4Glucosyltransferase"
                     /note="UDP-glucose LOS-beta-1,4 glucosyltransferase is
                     required for biosynthesis of lipooligosaccharide; cd02511"
                     /db_xref="CDD:133005"
     Site            order(90,92)
                     /site_type="active"
                     /note="putative metal binding site [active]"
                     /db_xref="CDD:133005"
ORIGIN      
        1 mtastpklpi avaiptkneg lniaeavksv lghfeavvvv dshstddtvk iaeecgaevv
       61 tytwdgghpr kkqwclenvr tdldwillld gderlspgll aelreafrdp aapkpaaydi
      121 plgywfsgkr lrhgytirkr sltdrtrchy pevgdldapg igeveghyqp vaasvgtlth
      181 piehqdldpv tawferhnry sdweawleqh pqvkeqvrqv ksrqgqlfhk apfkpavsfa
      241 ymylykrgfl dgragfdfal amsfyrwqia lksrekpvr
//
LOCUS       WP_457655753             401 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457655753
VERSION     WP_457655753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42049
     Region          4..367
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtafslepeq tawceelrtl avrelrplae kgepgqvnrp llaalgelgl lermfgsgal
       61 dlcllresla rgcteaetal alqglgatpi vqagtpahre rwlpevragr avaafalsep
      121 gagsdaaals laaehtpagw altgqkcwis napeadfavv farttpgags rgitaflvps
      181 drpgltgsal dmlsphpigt lefdgvpvta ddvlgepdrg fpvamntlnl frpsvgafav
      241 gmaraaldat lehtahrtaf ggplsdlqav shqvaematr teaarllvya aaaaydages
      301 gvprraamak lyatetaqyv vdaavqlhga ralrrghlle hlyrevrapr iyegasevqr
      361 tiiakelyan aaqlpdphqp paatpeppaq qpasptqepp a
//
LOCUS       WP_457655755             276 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655755
VERSION     WP_457655755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..276
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29077
     Region          193..268
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtwtftddvd vflasagpsl aarpvehtva ltvterlrrs gphhygaddp vlgwwrgadg
       61 avagtlvrtp phgalltavp aeavgplvaa lgpgpdlddv tadrdtaaql aallpdhrtv
      121 qeqrlyrlgt lrppcpapeg raraatradr allvvwvrgf adatgqakss aewlvdegte
      181 rgsftlwesg gapvalagrs rmlagtvrvt svytppefrg rgyaaavtae asraalaega
      241 aevllftdla nptsngvyqr igyepvadrv qlrrnt
//
LOCUS       WP_457655759             295 aa            linear   BCT 27-JAN-2026
DEFINITION  SIS domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655759
VERSION     WP_457655759.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..295
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31240
     Region          5..293
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 msyaetetas qpacwrraaa ladgpeaaal pvageriavv gcgtsfymaq ayaglregsg
       61 qgesdafaas efpfgrgydr vvaltrsgtt tevlalldrl hgtcrtvavt aapetpvraa
      121 addlvvldfa dersvvqtrf attaltllra hlglhsdsvv adaetalaep lpeellrstq
      181 fsflgrgwtv glaheaalkm keaslswtes ypameyrhgp isistagtat wmfgeapegl
      241 adqvratgar wvddaldpla dlvrvqrlal araaaqgldp dlprhlsrsv vldwa
//
LOCUS       WP_457655764             505 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Streptomyces griseus].
ACCESSION   WP_457655764
VERSION     WP_457655764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A., Buglak,A.A. and Kritsky,M.S.
  TITLE     UV Radiation in DNA Damage and Repair Involving DNA-Photolyases and
            Cryptochromes
  JOURNAL   Biomedicines 9 (11) (2021)
   PUBMED   34829793
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Muller,M. and Carell,T.
  TITLE     Structural biology of DNA photolyases and cryptochromes
  JOURNAL   Curr Opin Struct Biol 19 (3), 277-285 (2009)
   PUBMED   19487120
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Deisenhofer,J.
  TITLE     DNA photolyases and cryptochromes
  JOURNAL   Mutat Res 460 (3-4), 143-149 (2000)
   PUBMED   10946225
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..505
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57353
     Region          4..503
                     /region_name="COG3046"
                     /note="Uncharacterized conserved protein related to
                     deoxyribodipyrimidine photolyase [General function
                     prediction only]"
                     /db_xref="CDD:442280"
ORIGIN      
        1 malrthwlfg dqlgphfldp rhggpdehap llmiearsal rrrrfhraka hlvlsamrhr
       61 avelgdrvry vhartyaegl aeagfggrrd rlsvchptsr aaldfvtard gidvlpargf
      121 llaqeefgaw akehgddrlr megfyrwvrr ehdllmdgda paggtwnldh dnreppprgv
      181 qtldvpapyg phedeiddev rrdldrwerd gevafvgrdg prrfpvtrre alaalrrfva
      241 hrladfgrye damlaadpvm shsllsvpln lglldpaecv draeeawrag eaplnsvegf
      301 vrqiagwrey vwqlywhfge eyrhrnalrh raqlpdwfld ldadavtanc lstvlaqvrd
      361 tgwthhiprl mvlgsralqd gwdpaavtdw fhrcfvdgyd wvmlpnvvgm sqyadggrmt
      421 tkpytsggay inkmsdlcgp cayrptdrtg ehacpytagy waflhrhres lssnhrmara
      481 vkgldrlkdl delldatsar gdrap
//
LOCUS       WP_457655766             338 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces griseus].
ACCESSION   WP_457655766
VERSION     WP_457655766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..338
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37151
     Region          45..>310
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mphsaesgpe hdsvatpenw wvfrgpadlp ppppwrgiag sqgtqaaqey llsaedvavv
       61 ntalhlrrpl lvtgrpgtgk sslayavaed lglgdvlrwp vnsrstleda lcrydavgrl
      121 revslererr strgasgklr yrargrhsdi gdflrlgplg talaarrgpr vllideldka
      181 didlpndllv vleearfeip elarlpegqq nvevlvtgsr ervpvnrgtv tcenfpivvm
      241 tsngerdfpp aflrrcvrld lqdpgeeklr divrlhlgdd alavaedlvq dflqraasqt
      301 latdqllaav hlritgadls reqlintvmr rldeafpa
//
LOCUS       WP_457655772             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655772
VERSION     WP_457655772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31382
     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          93..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mptrravtgr sreprarfae elrllrtarg hslrqlgdrl gwdwslfgkm ekgetvggpe
       61 vvqaldthyg tpglllalwe lavsdktqfk eryrrymale aeavsmwhfa vsvlpgllqt
      121 payarellas gglhgaeltq qvdarmgrrn llegegapqf rtilseatlr talqdvgewr
      181 kqlehllema erpnltlqvl pqeaglhgls stdvwflrlp dartvayteh gyggdlieen
      241 vavervqray datrdlarsp aesrnfvlrv leelpcdpst
//
LOCUS       WP_457655779             447 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457655779
VERSION     WP_457655779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..447
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47314
     Region          4..441
                     /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 mkdfrsvadl vaaeiaagrl ragerlppqr efarryaian stavrvyqel arrgltvgqv
       61 grgtfvtdap gapapapals epadsrvdle lnhpvvpeqa gllaaglekl vrsdhlesal
      121 rpvgpdgtaa ardaaaevla rgggrpdper ilfagngrqa isaavaaltr pgarlgveef
      181 typvlkaiaa rlgvtlvpla mdedglvpea veeahradpl havyvqpvlh nplsvtmpgr
      241 rldrladvll tagihaieda vwaflrddlp plasrapent vlvdslskrl spglslgfav
      301 apaasagrva galrsggwtp mrfpleamvr wqadgtvdtl vrakqrevra rqeiadrhlg
      361 dfrtrsdpas cyrwwelpgp wradtfvaaa arhgiavtpa aaftagrprg phairlglas
      421 ptrevlsral atladlarsa pdelagd
//
LOCUS       WP_457655780             753 aa            linear   BCT 27-JAN-2026
DEFINITION  M9 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457655780
VERSION     WP_457655780.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 753)
  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 10553015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..753
                     /product="M9 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /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=81328
     Region          99..280
                     /region_name="Peptidase_M9_N"
                     /note="Peptidase family M9 N-terminal; pfam08453"
                     /db_xref="CDD:430004"
     Region          339..623
                     /region_name="Peptidase_M9"
                     /note="Collagenase; pfam01752"
                     /db_xref="CDD:426409"
     Region          671..738
                     /region_name="PPC"
                     /note="Bacterial pre-peptidase C-terminal domain;
                     pfam04151"
                     /db_xref="CDD:427748"
ORIGIN      
        1 msvallaqpa qaqpnspsaa tasnasqpsr pagtadpapq aqqsptpdtg hqlkdrlkas
       61 qlpplsadks alkeayghhd appkrdavkk psakaaaacd padftgrtgs elvrqikgst
      121 idcvntlfgl tgnnaqlafr eaqmvtvaya lrdnaayypg dastgtpqlv lylragyyvq
      181 wynpdvvgpy gsalttairs gldtffaspr shdvtdenge tlseavilid saqenarylh
      241 vvkrmladyd sswnayarml aavnnvytvt frghqvpafv saveadpgli dalyrfaadh
      301 lallggdqay ltsnagrelg rflqheslrg karppatali qqtsitgpta plwvgiaema
      361 dyydkancsd ygvcdlqerl krevlpvrht csssirilaq qmtsaelaas ctslieqday
      421 fhriakddgp vaddnntsie viaydssady qtyagamygi dtnnggmyle gdpsvvgnqp
      481 rfiayeaewl rpdfhiwnln heythyldgr ftmygdfaeg mstptvwwve gfaeyisyhy
      541 rgepytaamt eagkgtyals tlfgtdyshd ttrvyrwgyl avrymleqhp admdtvlghy
      601 ragewaaart hltgtvgtry dsdfrtwlag caagdcgdgs tapvsectdp dtrvlgencr
      661 rsdlsattgn yayhylyipa gtaqlkitvs ggtgdadlyy sgtgwattsa ytsrdtgpgn
      721 thtltvtnpp aganyislha astfggatlt tah
//
LOCUS       WP_457655782             326 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655782
VERSION     WP_457655782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /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=35415
     Region          19..308
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mittsarllr lvsllssrpt wsnaelarkl dvtertvrrd vdklrelgyg vesvpgpggg
       61 yrfgagnrmp plnldddevf avavalreaa hgaalgadpa alsallklrq ilptrmarrl
      121 sgldatveht prcetprasa dvllllasvc raserttlty rdmhgtttvr cvdphrlvyt
      181 gahwyfvard vgrsawrtfr adrvvevvst gevvevpdap daaqlvsdti trtgypffar
      241 vrlplsydda rrlvapivat hepdgpnatv isiggsdpdq lagyllslrt plevlspdsv
      301 reallarldv lyrgngagrq eadeqk
//
LOCUS       WP_457655783             337 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457655783
VERSION     WP_457655783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  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 337)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..337
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36792
     Region          11..321
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(14..16,46,51,77,140..141,181..182,205,234..240,276,
                     293..296,301,304..305)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(46,51,77,140)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 msltrllpgs lgfgtapmgn mfraipeeea qatlqaaweq giryydtapf ygaglaeirl
       61 gellaqqprd syvlstkvgr vildeeedps arelgekggl fehgrlnrmv ddytadatkr
      121 siedslkrln tdrldivwvh diaqdfhgdr wlaqfetart gafrvldelr dqgvikawgl
      181 gvnrvepvel tlaldeprpd gfllagrytl ldhrqalqrl lpaaqeqgvd mvvggpyssg
      241 vlaggthfey qeapahivet vrrireltdr hgvsikaaal qfalahpaaa aaipgatrps
      301 riaedlgalr eeipaafwhd lraaglldha aplpagv
//
LOCUS       WP_457655784             306 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces griseus].
ACCESSION   WP_457655784
VERSION     WP_457655784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..306
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=31926
     Region          62..290
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtepapeqcq qppppidsta qlltritdrl gaqlslvsrn gtrrpmhrtr qpdhpaphpd
       61 gapapslvav ahgsrdpeal rtvlalldrv relrpgldvr lghielnrpl lpdtlgglrg
      121 adavlvplll grghhvkrdl pataaaapav rtriaaplgp hpllvealyg rlveagwdaa
      181 drggrgaavv laaagsrdpd sardtrrtar llaerlgvpv vpayasattp tvpaalrala
      241 argrhrafva syftapgrfa sacaeaaphr aaaplgahpa marlvlhryd qaraaaapav
      301 sllasa
//
LOCUS       WP_457655785             256 aa            linear   BCT 27-JAN-2026
DEFINITION  SanA/YdcF family protein [Streptomyces griseus].
ACCESSION   WP_457655785
VERSION     WP_457655785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Chao,K.L., Lim,K., Lehmann,C., Doseeva,V., Howard,A.J.,
            Schwarz,F.P. and Herzberg,O.
  TITLE     The Escherichia coli YdcF binds S-adenosyl-L-methionine and adopts
            an alpha/beta-fold characteristic of nucleotide-utilizing enzymes
  JOURNAL   Proteins 72 (1), 506-509 (2008)
   PUBMED   18393394
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Rida,S., Caillet,J. and Alix,J.H.
  TITLE     Amplification of a novel gene, sanA, abolishes a
            vancomycin-sensitive defect in Escherichia coli
  JOURNAL   J Bacteriol 178 (1), 94-102 (1996)
   PUBMED   8550448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..256
                     /product="SanA/YdcF family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=27882
     Region          50..248
                     /region_name="SanA"
                     /note="Uncharacterized periplasmic protein SanA, affects
                     membrane permeability for vancomycin [Cell
                     wall/membrane/envelope biogenesis]; COG2949"
                     /db_xref="CDD:442192"
ORIGIN      
        1 mtgetgetgg rrkvlgrsgr plgrrlkevr wparpvlrlp rtrrgrrrlv qglmaacvla
       61 llpatwmrle agdrvgttae aparevavvf gaglwkgrpt pylahrldaa aelyrtgkvk
      121 vvlvtgdnsr veydepdamr tyltgrgvpd erivsdyagf dswdscvrak kifgvdravl
      181 vsqgfhihra vtlcrsagid aygvgvdepr dsvwyyggvr elaasgkaal davfrpdprf
      241 lgpeepgvte aladtp
//
LOCUS       WP_457655789             230 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457655789
VERSION     WP_457655789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..230
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23262
     Region          4..196
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msapaavlfd mdgtlvgtev lwwetadeva aglghrltga dapevvgrav adtaahliav
       61 tgraaealdg vaseltasff rkvdagaplr pgaaalltal ersrvpfalv sasprsvvda
      121 vvagslaaap faftlsaddt vrtkphpdpy raaatrfgvp asacvaveds pdgtasahaa
      181 gcavlvvpsl lpvepargrt farsleevdl gvlsdclrrp dpeipgpkpa
//
LOCUS       WP_457655790             387 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655790
VERSION     WP_457655790.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..387
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40185
     Region          29..361
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msalpapsta arrpdparaa saadgraatg arvefrslrr afgptvaldg ldltaepgel
       61 lallgpsgcg kttalrvlag feqpdsgevl vdgeditrvp anrrdagmvf qsyslfphln
      121 ardnvafglr vrkvsaaerh ataaelldlv glpdhggrfp hqmsggqqqr valaralalr
      181 prvllldepl saldakvrls lreeirrlql slgittifvt hdqeealsma drvavlnagr
      241 leqcappael yerpatafva efvgtmnrlp grltgtgsve vagatlpvdg gapagggpvd
      301 vlirpegira dadpegtatv vsasflgsvt rvlldlpggv alkadlpsrd aadllpgvra
      361 rvtpvprpvl vvpatpvtdg rtgkasa
//
LOCUS       WP_457655791             251 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655791
VERSION     WP_457655791.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27465
     Region          1..232
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mgrsryeeia eslrqairsg vhppgsrlps esdlaarwea srgtvrqava llasegligs
       61 rqgarrvvlr qerrqsfeql nsfaqwaram gcevssrilt rttrpatdee aarldtepga
      121 eilyvlrlrh ldgepvmver tvyadsvapv vralpedcvs imdniaerad ivahhgehli
      181 davaagseda rllrirragp llrqrhltyt aagraiewtd dryragsvvf nvmnsaaaap
      241 lerragpsvg g
//
LOCUS       WP_457655793             497 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655793
VERSION     WP_457655793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..497
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50964
     Region          43..492
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,168,
                     171..172,175,271,274..275,319..321,324,352,356,411..412,
                     416,420,436,439..440,443..444,447)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msessvhtsl tperatpatg eptgpvrhdh ptpvlgalgl ftvllgaalp lidffivnva
       61 lptidrdlda gpamlelvva gyglayavll vlggrlgdmv grrrlfligm aafgitslac
      121 glapdawtlv garvaqgaaa almlpqvlat iqaatrgprr aramslygat aglsmvagqi
      181 lggvlvatap mssvfgesag wrsvflvnvp vavvglilaa ravpetrsdr papvdvpgtl
      241 llalslitll apltegraag wplwtwvsla lfpfsayafy rverradrlg rvplvppsll
      301 rleslrrgla lvvpfsigfg gfmfviaval qqglrlgpaa aglslapmal affgaslagp
      361 rlirrygtrv vtaggliqav givvlaltah vawqglglwg llpgvaiagl gqglqlpvlf
      421 rivlsdvppe kagvgggvmt ttqqaalalg vatlgtlfla lapglgmrda lvvtllvqla
      481 avaltvglsl rlprtva
//
LOCUS       WP_457655795             197 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655795
VERSION     WP_457655795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21534
     Region          9..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mteqtgrrer kkaatrqkia dtalrlfler gyeavgirdv aaqadvavtt lfshfaskea
       61 lvfeqdpgfe qgllravadr apdeplipal rrevhalvrh ctapeaapvw nmiesspalr
      121 eyeesmrlrh aeslgaalaa dlgvpetsia crtiarfvid ayalareaad peaavdevfr
      181 mieaawgvar ldrpita
//
LOCUS       WP_457655798             314 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655798
VERSION     WP_457655798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 314)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..314
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34194
     Region          7..108
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(8..10,24,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,90,94,100,104,107..108)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mngdtlysig elarrtgltv ktirfysdrg ivaptdrspa gyrlytvdav arldlvrtlr
       61 elgldlptir kvvdrelslp avaaahaeal avqirvlsmr ravltavaer gstpeetelm
      121 nrlaqlsqde rrrligdfld avfggldaap aapafagvmr smtpelpdnp daeqvrvwve
      181 laemsqdpdf ramvrrmied laaeqarsgt avprrdiaaa vrdeagpala dgldpasaqa
      241 dpvvaaftah yaqligrpdd vdlrrllaar lenvddprre ryfqllavvn gwpapaslap
      301 vldwsvealr vrta
//
LOCUS       WP_457655800             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655800
VERSION     WP_457655800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31552
     Region          30..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 meidrpglaa flrrrrellq pedvglprgq rrrtgglrre evavlchmst dyyarlerer
       61 gpqpseqmia siaqglhlsl derdhlfrls ghmppargtt gehispgllr ildrlddtpa
      121 eivtelgetl rqtplgvalt gdttrytgla rsigyrwftd patrtlyaae dhaflsrmfa
      181 sglrelatlr gtgsraahca ellreesqef rrlwdqheig irpdqvkrfv hpevgvleln
      241 cqrlldpdqs hsllvytaap gsesherlrl lsvigtqtlr
//
LOCUS       WP_457655802             188 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655802
VERSION     WP_457655802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20053
     Region          18..159
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mnapvvlqva atsaspalvl rpwrmadvaa lvevsrdpal rrwaasavdd dadgarwvqa
       61 qqrgwaagdr fgfavleaqt aagraqlmgn vvlkdvahgk paaevgywta aharglgvap
      121 ralealtswa feafgaarle rlellhqvdn lascrvaqks rydfdsvlpa tppsfpldgh
      181 lhirrlsa
//
LOCUS       WP_457655803             556 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarate hydratase [Streptomyces griseus].
ACCESSION   WP_457655803
VERSION     WP_457655803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   van Vugt-Lussenburg,B.M., van der Weel,L., Hagen,W.R. and
            Hagedoorn,P.L.
  TITLE     Biochemical similarities and differences between the catalytic
            [4Fe-4S] cluster containing fumarases FumA and FumB from
            Escherichia coli
  JOURNAL   PLoS One 8 (2), e55549 (2013)
   PUBMED   23405168
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Flint,D.H.
  TITLE     Escherichia coli fumarase A catalyzes the isomerization of enol and
            keto oxalacetic acid
  JOURNAL   Biochemistry 32 (3), 799-805 (1993)
   PUBMED   8422384
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11487765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..556
                     /product="fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /calculated_mol_wt=60059
     Region          1..538
                     /region_name="PRK15389"
                     /note="fumarate hydratase; Provisional"
                     /db_xref="CDD:237955"
ORIGIN      
        1 maefaysdll plgedttpyr lvtaegvstf eadgrtflkv dpealrtlaa eamhdishyl
       61 rpahlaqlrr ivddpeassn dkfvaldllk naniaaagvl pmcqdtgtai vmgkrgqnvl
      121 teggdeeals hgiydaytkl nlrysqmapl tmwdekntgs nlpaqielya tdggaykflf
      181 makgggsank sflyqetkav lneasmmkfl eekirslgta acppyhlaiv vggtsaefal
      241 ktakyasahy ldelpaegsp tghgfrdkel eekvfeltqk igigaqfggk yfchdvrvvr
      301 lprhgaslpv aiavscsadr qatakitaeg vfleqlekdp arflpdttde hldeaggdvv
      361 einlnrpmde vlaeltkypv ktrlsltgpl vvardiahak ikerldagee mpqylkdhpv
      421 yyagpaktpe gyasgsfgpt tagrmdsyve qfqaaggskv mlakgnrskq vtdacgahgg
      481 fylgsiggpa arlaqdcikk vevveyeelg meavwrieve dfpafivvdd kgndfftepa
      541 paptftsipv rgpgla
//
LOCUS       WP_457655808             388 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces griseus].
ACCESSION   WP_457655808
VERSION     WP_457655808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..388
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39522
     Region          16..346
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(47..48,51,103,119,121,150,182,306,309,345)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(238,243,297,306..308,311,333,337)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 msgpaagtas aatttdvvcl gesmvtflps qpgrladvps fgrgiggaes nvacalaaag
       61 hraawvgrvg adgfgehlve tiagygvdts avrrdpdrpt giyfrtatdr gtdthevayy
      121 ragsaasams panvpyeelf agrilhlsgi taalsadcla llreltaarp grplvsfdvn
      181 hrphlwrggd adasvllela rrsdlvfvge deaeeawgiv gaeairaalp epsvvvvkrg
      241 sagatvfasg lrpgprssia ggaenapgar stegggaeca vggaesgpdt vthvpalrvd
      301 vvaavgagda faagflsatl rglpvrdrar hghlmaaavl tvpgdltepp ardhadrlaa
      361 ldddawgrlr lgpgwtaadr apeevrtp
//
LOCUS       WP_457655807             361 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457655807
VERSION     WP_457655807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..361
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=37889
     Region          179..358
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mshtirrtad parqeefagr mvevlndacl gylcslghrt rlfdvmaglp pstseeiada
       61 aglneryvre wlggvtvggi vgydpadgty rlppehaasl craagpdnla sflqdlalig
      121 lvedevvtaf rdgggvpyss ypkfqelqae etarvydaal vdviiplapg lpellgsggg
      181 ldvldvgtgq ghavnllara fpasrftgvd mseggiaaar aeaarlglrn ahfdladaaa
      241 vtgpydlita fdvihdlarp aatlvavaga lrddgvflmg diaassrlee nldlplgptl
      301 yafsvfycmt tslseggagl gtvwgrqtal rmlkeagfge vavrevegdi lnvyyvarkg
      361 s
//
LOCUS       WP_457655810             284 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457655810
VERSION     WP_457655810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..284
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30725
     Region          1..265
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 msrampvsyv rvtgveritp rtarvgftge alprlledrp dqqmklclpr egrsvregll
       61 perdaddpyg mrwyeaflai peaerpwmrg ftvrsydrqr nvmavdfvlh gadgpasrwg
      121 aaarpgdvlg mvgpsslyar plpaarrmll agdesalpai atvlealpag tgavvyaeva
      181 daaeerelps aaggaevrwv hrdrggalvd avrdagadld gvdaawvage asavrairrh
      241 lvedrrlpka avefsgywrr altqddapte edlawaaera adas
//
LOCUS       WP_457655811             293 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655811
VERSION     WP_457655811.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..293
                     /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=30102
     Region          63..231
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mnkplvgafl aalllgagaa pvvaaepagn asevsaeaas qaseatpaak avtfagtval
       61 sncsgsvvrs pdaeptdpal vlsnghcles gfpgpgevvv dqpssrtftl lnasgsgvgt
      121 lkaskiaygt mtdtdlslye ltstyqqiee sygiqalele tahptagtai tvasgywkrt
      181 yscdidgfvh qlkegrwtwk dsvrytpecq tiggtsgspv iddatgkvva vnntgnesgq
      241 ectdnnpcev dengevtvre ginyaqqtyt mvpcigvgsk idldaegcal pkp
//
LOCUS       WP_457655813             805 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Streptomyces griseus].
ACCESSION   WP_457655813
VERSION     WP_457655813.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..805
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83802
     Region          13..406
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          376..552
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          673..744
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 msgrarlalc ayaatllaag sliplvegig wlvqaamllg vqsgvgalar rvplartlti
       61 alqtlvtlvl ltlvfardha lfgllpgpga vmrlgellva ggedvgtyst papltdgikl
      121 mviggvvlig lvvdalavtf rsaapaglpl lalysvaagl sdggaswlwf llaasgylll
      181 llaegrdrls qwgrvfggaa rnagglsdgl agvgggtspv rtgrrigvla lgialvapla
      241 lpaldsgllg gsgpgngkgs gggtisavnp lvslqnnlnq pdnrevmtyr sniedpqsly
      301 lrilaldefn gsewrsstrr ltdvperlpq ptglsgdvav tevrtnisas rsyqqtylpl
      361 pypasevrvg grwryepegr tlvgddgqtt rgaqyevgsl vveptadqla aagtppeelv
      421 reytrvpgsl pgvvadtaee vtegaanaye qavklqdwfa sdggftydtt vtsgtgssai
      481 arflrdkegf cvhfsfsmaa martlgipar vavgftpgtm kangatsvgl rdahawpely
      541 fegvgwtrfe ptpsrgsaps ytrpevptds asdvaepsad tsdapsaaps addscppqlr
      601 qeggcgpsqd agaalptdrg tpagtvllvi laavlavvlp lspllwrtrt rnrrlgsggr
      661 tpadaaartl aawreitdta wdhgigpdes ltprkaaari vrlgrldtga aeavhriags
      721 veqvlyapep rpaaglaeda pavraglras agrgarlrat llprssvrvv wavaerrtal
      781 aerwanrpga grwtarlrrl srqhg
//
LOCUS       WP_457655816             504 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457655816
VERSION     WP_457655816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..504
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52490
     Region          24..496
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag tgamaaaarl avagnrvtvy ersasyggsv grfehegfvf dtgpgllhlp
       61 avqrdlfvkt gkesleqcvt ltqvdpasrh lfadgtavsl pnasragvaa aldgalgaga
      121 garwsafmdr ardtwdrsrr plleeplrad hqvlgrdpyp avrqrrllrg arqagtvaei
      181 gaweladdrl aalldgyals hgldprsapa saallpymeq tfgswyvrgg mrelaravye
      241 rcvarrvefv fgaevvrvve kdgraagvel aggevaeadr vvlgarprpd lvpgqqavga
      301 gdvpvragsg agaagrftvl lslrgaread avhrtvvhsa qgaaeqeavf gcrvaghptv
      361 tvlrpddpat rpdaeheavt ltatvapqgp vdwrdaavrq rfadvlvera aaavpglrer
      421 ilhteirtpa eteaetgaeg gavpppalag aggaylhpgn ptrlpglyra ggwshpgggl
      481 ahagmsgtlv aglvvegddf rgsr
//
LOCUS       WP_457655819             264 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Streptomyces griseus].
ACCESSION   WP_457655819
VERSION     WP_457655819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..264
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27505
     Region          1..255
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msddvfslgp aafgsrlimg tggapslevl ersliasgte lttvamrrld ptvqgsvlsv
       61 lerlsiqvlp ntagcftage avltarlare algtdwvkle viadertllp dtvelldaae
      121 tlvddgfvvl pytnddpvla rkledvgcaa implgspigs glgirnphnf eliveragvp
      181 vildagagta sdaaqamelg caavmlasav traqepelma gamrhavegg rlayragrip
      241 rrrfaeassp vdgraafdpe rpaf
//
LOCUS       WP_457655820             395 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsA family ATPase [Streptomyces griseus].
ACCESSION   WP_457655820
VERSION     WP_457655820.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Castillo,R. and Saier,M.H.
  TITLE     Functional Promiscuity of Homologues of the Bacterial ArsA ATPases
  JOURNAL   Int J Microbiol 2010, 187373 (2010)
   PUBMED   20981284
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 395)
  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 395)
  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 395)
  AUTHORS   Zhou,T., Radaev,S., Rosen,B.P. and Gatti,D.L.
  TITLE     Structure of the ArsA ATPase: the catalytic subunit of a heavy
            metal resistance pump
  JOURNAL   EMBO J 19 (17), 4838-4845 (2000)
   PUBMED   10970874
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Rosen,B.P., Bhattacharjee,H. and Shi,W.
  TITLE     Mechanisms of metalloregulation of an anion-translocating ATPase
  JOURNAL   J Bioenerg Biomembr 27 (1), 85-91 (1995)
   PUBMED   7629056
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Rosen,B.P.
  TITLE     The plasmid-encoded arsenical resistance pump: an
            anion-translocating ATPase
  JOURNAL   Res Microbiol 141 (3), 336-341 (1990)
   PUBMED   1704144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14288110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..395
                     /product="ArsA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42284
     Region          1..293
                     /region_name="ArsA"
                     /note="Anion-transporting ATPase, ArsA/GET3 family
                     [Inorganic ion transport and metabolism]; COG0003"
                     /db_xref="CDD:439774"
     Region          327..384
                     /region_name="ArsA_HSP20"
                     /note="HSP20-like domain found in ArsA; pfam17886"
                     /db_xref="CDD:436117"
ORIGIN      
        1 mrtvlvtglg gagrstvaaa talaaaargd rtllisaevi pglpagtepa rvadrldhar
       61 idsgehfrae ltelqkrasg vldllgagrl egeeltelpg saqlallhtl rraaegdwsg
      121 ydtlvvdlpp ltealallal pqqlrrylrr llpaerqaar alrpvlaqla gvpmpaqwly
      181 eaaarkdeel aavqaliedg sttlrlvaep gpaaedalrt artglalhgl sadllvasrv
      241 lprhssdpwf aalaaqqekc ldhwhqdvap dvpvheaahl grdpqgpddl avlelpapdd
      301 rtpgraedpw wteeetgaee tptvltwclp lpgaakedlr lvrrgdelll tvgpfhriir
      361 iasalrrctv sgaaladgvl rvrftpdpal wprts
//
LOCUS       WP_457655821             380 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces griseus].
ACCESSION   WP_457655821
VERSION     WP_457655821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..380
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40852
     Region          3..380
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mdktlivtnd fpprpggiqa flhnmalrld pdrvvvyast wkrgeegaaa taafdaeqpf
       61 tvvrdrttml lptprvtrra tallrehdct svwfgaaapl glmapalrra garrlvatth
      121 gheagwaqlp asrqllrrig egtdtitylg eytrsriaaa ltpdaagrmv qlppgvdekt
      181 fhpgsggdrv rarlglsdrp vvvcvsrlvp rkgqdtlila mpailaqipd avllivgggp
      241 yaedlkrlaa etgvqdsvrf tgvvpwaelp ahygagdvfa mpcrtrrrgl dveglgivyl
      301 easatglpvv agdsggapda vldgetgwvv rggsaeesad rivtllgdpe lrqrmgergr
      361 awveekwrwd llaeklktll
//
LOCUS       WP_457655823             391 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655823
VERSION     WP_457655823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40432
     Region          1..388
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 magvqsaval reagfagpvt ligaephqpy drpplskavl lgkaehsafd vdfealditl
       61 rlgldvtalr aadhvldtae gpvhydslil atgaepitlp gaegvpgvhl lrtlddaarl
      121 rpvldrqhdv vvvgagwiga efataaraag cavtvveaaa rplagtlpae vaapmadwya
      181 dsgaelltga rvdrveegav vltdgrtlpa gavvvgigar patgwlagsg velgphgsvt
      241 adsalrtslp dvyavgdcas fpsarygtrl lvhhwdnalq gprtaaaail aarsgepvpv
      301 ydpvpyfwse qfgrfvqyag hhacadtllw rgdgsdaaws vcwlregalv avlavgrprd
      361 laqgrrlies gavldpekva dpavplksav l
//
LOCUS       WP_457655824             595 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655824
VERSION     WP_457655824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 595)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 595)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 595)
  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 595)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..595
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60567
     Region          3..564
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtsprrlvwd atartrgwfv lasatavlgs agtlafpwam araldavvar rsvtgpvlvc
       61 aallalvvtt galqtlangg ygsgtvaalr rslarralda gvpgtadfpa gdlagrlsag
      121 caqagsagvt lvtastavlt slggvvalwl ldwriglcfs lgvpplalia rmfmnrgsgl
      181 flryqetqgr isalllealg gartigasgt aaaetrrvld plpelsrtgh rvwalqrdtg
      241 wqvgllipav evlvlcaggl allhgdisag elaavvgyta lamaaldqld alfalgmsaa
      301 garrvaevvd qpvpapgtra rpaggsgtvt lsgvtvrsga rtvldavdlv vpagtalavv
      361 grsgagkstl aaligrlrep daglvaidgv plrelspqal raavgyafer pallgttvag
      421 miafarpdas heevtaaaaa araddfiarl pggydtplte aplsggevqr lglaralvhd
      481 pavvvlddal ssldtatear vgsalasaws grtrvliahr vstaaradlv awledgrvra
      541 lgphadlwql ddyralfaas tgpeagpdrd tgsgaeawtg rdtpphtnph aqepv
//
LOCUS       WP_457655825             602 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655825
VERSION     WP_457655825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 602)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 602)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 602)
  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 602)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..602
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62755
     Region          1..599
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mseaaprpid rhlfagflrr hrkaavavag wslleavpal asgllvaaal drgflaerpa
       61 egffwigllg aamvfralmt rtltpwlgri veplrddlvt avaagavqra aagardtaga
      121 gvarltvqve tvrslvsall rsarqlgvsl lmafvglaal sapvaaltlp pvlltlllcv
      181 prlrvlarrq rrqlraeerl tgvagetfdg irdvvacgar drvadelsar itdhrdavra
      241 vartasantl lvslgshlpl lvlllsaprl ldsgalsege llgatsylvs gvapalrslv
      301 avlgswgvql atllrqlsrs trearpgppg gqgpalpprt rrtprtpqtp rtpltpltps
      361 spdlslvnvv yaygpgaapv idglsldipa gshltvvgps gagkstlttl laglagpdsg
      421 rltlggvpvt evdrawlhra vtlipqeayv ftgtvrdnlr ylrpqardtd ilasatavga
      481 rtlvdrlggl dapvgldgpp lssgerqlva larahlspas ivlldeacch ldpaaeerae
      541 rafadrgttl vvvahrissa lraprvlvld gertavgtpa qlldssplya dlvghwvsag
      601 ap
//
LOCUS       WP_457655828             312 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457655828
VERSION     WP_457655828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..312
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33705
     Region          41..188
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mppdtdahaq ehaqaqahty aharrddqpe etrrvllsrt fdedaelydr arpgyppely
       61 ddlvdlagar pgrrvleigc gtgqatvpla algcritave agprmaavar rnlaeaeiga
      121 edgagaegga gvgvgsaevv taefenwplp aepfdvvlaa tafhwidpav rvsraadalr
      181 pggalavvrg qhvwggteef fvevqrcyer fdpatqpgtr ppeaddvdns dhaeevarsg
      241 rfgetvfrry awdltyttae yldvlrtysg hralpdaarn gllacvagli dgryggrvtk
      301 rylielavsq rn
//
LOCUS       WP_457655831             364 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655831
VERSION     WP_457655831.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..364
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37531
     Region          24..359
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msvtrtpekt vrpvrvrpag yavvkagprg rfllhrrasv aaaallvlla avcvaylcvg
       61 esfvapgevv kvilgqpssa elvvgtlrlp rmvvgllvga afgvagaliq tvarnplasp
      121 diigisqgas altvgamtfg itsytvlpyl sviggvaaaa lvyvfawrgg lhatrfvlig
      181 igfavalrsv ttlfltkgdy lvaqqaqiwm tgslngrgws eaapigwtll illpaiawaa
      241 raqrtvtmdd dtatalgvrl grvrlglval gvvlasvatg tagpvdfval lapqiarrmt
      301 rtaqipllss allgavivvv gdllarrlfs ptelpvgvlt aavgapyliw liirghrgrs
      361 ggta
//
LOCUS       WP_457655832             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457655832
VERSION     WP_457655832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  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 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   3  (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   4  (residues 1 to 327)
  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 327)
  AUTHORS   Clarke,T.E., Tari,L.W. and Vogel,H.J.
  TITLE     Structural biology of bacterial iron uptake systems
  JOURNAL   Curr Top Med Chem 1 (1), 7-30 (2001)
   PUBMED   11895294
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34711
     Region          9..327
                     /region_name="FecB"
                     /note="ABC-type Fe3+-citrate transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4594"
                     /db_xref="CDD:443650"
ORIGIN      
        1 msqrsflpra laavslttva sltlaacggs ddsgsgsdsa ssggstrtve tpmgdvqvke
       61 apervvvldt aeldsaltlg vkpvgathad vtsgflnylp kdqlsgikdv gqmmtpnlea
      121 iaalkpdlil tskirhgdky delskiaptv mtentgypwk enfqlhaeal gkrteakmvt
      181 ddyanhvadv tkalggkdka aatevnmvrf vegadiriyg rknyiatila dvglgrpait
      241 dqakdgfsyd vspekidlad advvfhstyg dpkksketet tgsglwknmd avkngkvfav
      301 ddqlwiqgig ytaadkilge lhqsltk
//
LOCUS       WP_457655838             245 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655838
VERSION     WP_457655838.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..245
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25122
     Region          3..244
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnlkdkvavv tggtrglglr iteafvaega qvvaaargad gaaeslahlg dravfeqadv
       61 rdpasvrsll svaadrfggv divvanagls rpgpvsalsf edwsdvvdtn vnglfhcvke
      121 avphleksgg griitlssal gsrptrgass ycstkaavem ftrvvalela plgitvncls
      181 pgfidegmgt llkkneavws qyapkvslgr mgqgqevada avylasaaas yvnghvlevn
      241 gglaw
//
LOCUS       WP_457655841             300 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457655841
VERSION     WP_457655841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..300
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31944
     Region          12..216
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(71,73,75..76,149..150,168,205)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(71,73,75,149,168,205)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 maephlreva ddvyayvqpd ggwclnnagl itsggrpali dtaateartv alraavaavt
       61 pepprfvint hphgdhvfgn rffadeaviv sheatraemd laglhltslw pevcwgdvsv
      121 elpsltyrga ltlhlgdttv elmhlgtaht rndtvvwlpr qrvlftgdvv msgatpfclt
      181 gsiagslevi eqlralepet vvsghgpvgg pelleqsagy lryvqrlaag giaagltple
      241 aarasgpgpy aelldserlv pnlhrayaea rgaepghwld ieelfaemvt yhgrlpacaa
//
LOCUS       WP_457655845            1049 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655845
VERSION     WP_457655845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1049
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=115303
     Region          250..1031
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          842..858
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          864..886
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          887..909
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          933..977
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          978..1000
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 msgtevavlr lattvigaaa kalltpkpga rlvpspvrpl prpakpdrla evlagrmacs
       61 fadlpeherl aavasvqdtf aaagepdagr lfaldldpdr lsaelsapaa glseravdly
      121 edllgdccah lveqltahps faaraaveqv ratgrtrelv edvrarvgpr pdaadldfer
      181 ryaefmatan srmglfgltl grsasewple tayislsvsg yeaagppglg gpvrtsvsgy
      241 egshahgpde pvrttariee algertrlll rgpagsgktt lvqwlalnaa rrtfgtelad
      301 wnrcvpfvlr lraftardal papadflraa gvplhgsapd gwadrlmleg ralvlvdgvd
      361 evpdrlrrrt erwlkdlita ypraryvvtt rpsavpeswl sgsgfephtl lamrrddiha
      421 fighwhraar secrsdeera eletyesalr ravgtrrdla rlatnplmca llcalnrdrr
      481 mqlprarkel ydaaldmllv rrdnerevsg vegvdltree qttllqrlay wlirndlvqa
      541 aqdeavslia dwlrsmsqvr gtpeqvfthl lnrsgllrep vpgavdfvhr tfqdylgaka
      601 avevrdfgvl vrhahedrwd dvvqmavgha rpderaallt sfleradaep ghehrlilla
      661 aaslghapel dpsvreavea rterllppds qesidqlaev gdlalellss mldglserea
      721 asvvrtaaav ggetayelvr qfrddersli tyevsmawer fdperyarev lagpgwedty
      781 vyvksdrhls alkhvprahs vnlsgdrhdl spvtsrtdvr rvfvwhnarl igvrqlaamp
      841 glrelglsnc prirtiepla rtglewlslv qlhpeldpap ladlpalryl alghpflmes
      901 vgelpacpqv trldllaesr yldlegledw tglrdltlyg gtqfrqlvrt palhglrdlg
      961 liripaldln ltapltglrv ltlaecalts glaplaelps lttlrlsgka ecydlaplaa
     1021 sehltvhlah dtpvtgaell pperivrlp
//
LOCUS       WP_457655858             281 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatase PAP2 family protein [Streptomyces griseus].
ACCESSION   WP_457655858
VERSION     WP_457655858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=29533
     Region          95..271
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(173,180,191..193,243,249,253)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mretprpret aadsgpglpq rrpgrafaht gasgsgtphr sdgrpphtpr garrtdlagh
       61 pgttppvpgw paplvsgyvs gflgliavlf alitwqvvve gpllrlderv gpkllgqgpg
      121 altqvlsdlg gtavalpvlt vviayalwrr alrlavyaal tmaavpalvi plkvatarqg
      181 plteavnyyp sghtataava ygasalvlla lprpswlrra swprawmmpv aaillttatg
      241 iglvlhgyhw pldvlaswcl gplvlaplww vscrssrrss g
//
LOCUS       WP_457655856             343 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655856
VERSION     WP_457655856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36313
     Region          1..339
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlslqaatvr fgkraaldav dlevadhriv cvlgpsgsgk stllravagl qpmdggrvll
       61 agqdqagvpv hrrglglmfq dhqlfphrdv ganvafglrm hgvgraetda rvrellelvg
      121 lpgaerrava alsggeqqrv alaralaprp kllmldeplg qldrslrerl vvelrtlfqe
      181 lgttvlavth dqgeafalad rvvvmrdgri aqegspldvw qrpasafvar flgfdnvtaa
      241 tvtgqaaata wgkvpvpegs pqgevdllvr pagvrigape dglrcavgvr tfrgnhvtvr
      301 llpenapvle aecalrdtpd egavvgvrfd aaetvvladp dhs
//
LOCUS       WP_457655851             144 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Streptomyces
            griseus].
ACCESSION   WP_457655851
VERSION     WP_457655851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Daines,D.A., Wu,M.H. and Yuan,S.Y.
  TITLE     VapC-1 of nontypeable Haemophilus influenzae is a ribonuclease
  JOURNAL   J Bacteriol 189 (14), 5041-5048 (2007)
   PUBMED   17496075
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..144
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=15732
     Region          2..140
                     /region_name="PIN_MT3492-like"
                     /note="VapC-like PIN domain of the hypothetical protein
                     MT3492 of Mycobacterium tuberculosis CDC1551 and other
                     uncharacterized, annotated PilT protein domain proteins;
                     cd09874"
                     /db_xref="CDD:350222"
ORIGIN      
        1 miyldscalv klivreketd alvafleers qqrhvtseia vtevmrvirr arcgpqgqpl
       61 ldeatfirll tvaekrldat dqvtldsavl kaagaleefn iksldaihla samvlgpslt
      121 sfvtydeklr ghaenrglqa lsps
//
LOCUS       WP_457655861             436 aa            linear   BCT 27-JAN-2026
DEFINITION  M50 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457655861
VERSION     WP_457655861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 436)
  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 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..436
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46991
     Region          7..431
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 msltsvlltv lgiavfvvgl lfsiawhelg hlstakmfgi rvpqymvgfg ptiwskkkgd
       61 teygikaipa ggyirmigmf ppgpdgrlea rstspwrgmi edarsaafee lepgdekrlf
      121 ytrkpwkrvi vmfagpfmnl ilavaifmgv amtfgfqtqt tevggvqqcv iaqsekrqtc
      181 kagddpspak aaglqegdki vafagakvdd watlsdrire tigpativve rdgkevtlna
      241 vlrenvvaek dskgevipek fvkagylgfa aqteivplgf gdsvvrmgdm iengvdsiia
      301 lpskipalwd aafsdgerad dspvgvvgaa riggevmnld ipaqnqvamm lfllagfnls
      361 lflfnmlpll pldgghiaga lweslrrnla kvfrrpdpgp fdvarlmpva yvvaglficf
      421 tllvlvadiv npvkit
//
LOCUS       WP_457655863             541 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655863
VERSION     WP_457655863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 541)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..541
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57230
     Region          2..533
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mavpvaffav ffaypvtaiv grglkaggdw qfgrigdvls rpdildvlwf ttwqalasta
       61 ltllialpga yvfarfdfpg kqvlravvtv pfvlptvvvg taflallgrg glldelwgvr
      121 ldttvwaill ahvffnyavv vrtvgglwsq ldprqeeaar vlgagrfaaf rrvtlpalap
      181 avaaaalmvf lftftsfgvv qilggpayst leveiyrqta qlldlptaav ltlvqfaavg
      241 gilavhaatv rrreralklv dpaqtsrrpr gagqwallgg vlltalllil lplgvlvers
      301 fdgaggaggy gfgyyralqs agaggsstfl vppleavgns lryalvatlv alvvgglaaa
      361 altrragrlv rgfdallmlp lgvsavtvgf gflitldkpp ldlrtswilv plaqalvgvp
      421 fvvrtmlpvl ravderlrea aavlgasplr awrevdlplv rravlvaagf afavslgefg
      481 atvfiarpdn ptlpvavarl lgrsgelnyg qamalstilm lvcavsllll erirtdrsge
      541 f
//
LOCUS       WP_457655864             361 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655864
VERSION     WP_457655864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36051
     Region          49..358
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msadsrtavq aadpppaatr parggapltv llrsggllll lasvavavti gparisvpdv
       61 wsavaahlgf gagdlspird giiwnlrmpr tllaavcgag lavcgtvmqs llrnpladpf
      121 vlgvssgast gavvvvvlgv gggtvslsag afagaicsfg lvlllshtlg gstdrvvlsg
      181 vaamqlfsal tsfvvmtsad aeqtrgvlfw llgslsgvgw sevalcsavl avclvvclah
      241 artldafafg qdaaaalgvn vartrivllc ttalltaalv saagaigfvg lvlphaaral
      301 tgsghrrllp vtalagavfl vwvdtlartv ldpqevpvgv vtaligvpaf vlvlyrtrst
      361 s
//
LOCUS       WP_457655868             396 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457655868
VERSION     WP_457655868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10531344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39798
     Region          46..106
                     /region_name="Inhibitor_I9"
                     /note="Peptidase inhibitor I9; pfam05922"
                     /db_xref="CDD:428674"
     Region          124..376
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(127,130..131)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(155,188,250..251,278,338,341)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(155,188,341)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(292,294,317)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mrlparwata alllvaplia vpttasadtg pegvlveqst ravpgqyivt lepelspetv
       61 lrefglsplf tygsvlhgfa atltaaelea vrtvpgvlav eenaevavea pragslfrap
      121 aagwgadrid qralplddtf tttatgkgvk ayvvdtgida ahsefggrvv ngfdaigdgr
      181 ggmdcnghgt hvagtvggat sgvaqdvslv nvrvlncegr gtwagilagf dwvakdaarg
      241 tapavlnasl ggarssavda avesvadagv lpvvaagndd rdacdvspaa adgvvtvgas
      301 drqdretsfs nwgsclelya pgadivsarl gggtvalngt smasphvagv aalykqenps
      361 aspaavarwl tdtatpdvls glgqgspdrl lytggl
//
LOCUS       WP_457655871             138 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces griseus].
ACCESSION   WP_457655871
VERSION     WP_457655871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15065
     Region          1..130
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtfsvdvtvr gyeldtqghl nqavylqyae harwellraa glpqekllad gigpvqlevt
       61 vkyrrelrgg ervrvtcrfd ygsgktftle qqvikedgtv aaeitgvagv ldlterrlvp
      121 dpqgrlaala gnpdlltg
//
LOCUS       WP_457655873             360 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein [Streptomyces griseus].
ACCESSION   WP_457655873
VERSION     WP_457655873.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..360
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38816
     Region          20..348
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
     Site            order(71,82,107,181,183,250,290,316)
                     /site_type="active"
                     /db_xref="CDD:185696"
     Site            order(181,316)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185696"
ORIGIN      
        1 mptvhrkpfg rahgqsetel wtldsgtgvr aeiltyggvl hsltvpdtag epgpvvrslp
       61 alddytdknp yfgavvgrya nriahgrftl dgtthhipan drghalhggp dgfhtkiwqa
      121 aghrtdsaav lrltlhspdg dmgfpgaldv satytldttg tlavdytavt drptvvnltn
      181 haylnlgddd ilghtlqvda daylpidads ipegppapvt gtpfdltaph rigerldhsd
      241 aqleraggfd hcwvlrpaap galrraarlt apgdrrtlel wttepglqvy tanqldgaft
      301 dgtgrrhqrh gsvcletqhl pdspnrpghp stvlrpgetl rsrtewrfph lrarngapar
//
LOCUS       WP_457655875             556 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457655875
VERSION     WP_457655875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..556
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59683
     Region          115..>271
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          426..519
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrrrrlaplv avsltaalap alaaspataa paaapsagtp savsppaaks aldryakqkp
       61 dwkrcevdsp aayqcatvkv pldyrkpggk ridlaisrir taepgkrrgi llsnpggpgg
      121 eglwmpmmmk eelpasvlks ydlvgfdprg vgrsspvscn ltpeqenwlr pykaetyakd
      181 vawartvadk crkkmgdrlp hittrntard ldlvrailge kkisyfgysy gtylgavyaq
      241 lfpsradrfv ldsavdpqra wrgmiqwwae gaepafdrwt ewaaarskty glgdtpkkvd
      301 rtfwnlvaqa dedpievdgq pttgdeirdg mralaftpky aseavvelkk aaagkpasak
      361 rpapiteggg agapewagka alaaetpadn gtagfwavvc gdnsaawsrd petyrrdaie
      421 dkgryplygd fassikpcaf wgksaepvtv vknkvgslvv qnewdsqtpl psgqalhaql
      481 kgskmvtvlg geghgvypsg nactdgavnr ylatgklpak dvtcrataes nararqnqkp
      541 dvlpgspvpe rapnrf
//
LOCUS       WP_457655880             213 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655880
VERSION     WP_457655880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10451994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23225
     Region          15..58
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          85..193
                     /region_name="TetR_C_6"
                     /note="BetI-type transcriptional repressor, C-terminal;
                     pfam13977"
                     /db_xref="CDD:433619"
ORIGIN      
        1 marvrlnvae rreellraav eqievrgvss vriadvasvl gvsnalvlyh fstkeklvaa
       61 afayaaeadl ahlrkllarr ttavrrlraa vrwyaptgqa kgwrlwiegw aaslrdpalr
      121 evagdldqrw kaelaqviee gaaagefrce dprsaawrlt alldgmavqt tsysgplsra
      181 tmlrwtdqal arelgidlae ltgspvadts tdg
//
LOCUS       WP_457655884             300 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase family protein [Streptomyces griseus].
ACCESSION   WP_457655884
VERSION     WP_457655884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..300
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31495
     Region          1..298
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mdtmrdrfis tasrlldeep rlavvladis adgfgparra hpdrvvnvgi reqllvgaga
       61 gmaltgmrpi vhtfasflve rpfeqvkldf ghqgvggilv saggsydwpa ggfthmapgd
      121 valldtldgw tvqvpghpde aeallresva gddrvyvrls lqanrearav ggaggftvvr
      181 qgrrgtvvav gpmldnvlaa tegldvtvly attvrpfdaa gvrraagaaa tadvvivepy
      241 lagtsaaatg ealmdlphrv lglgvgrael rrygrieehl aahgldpqgl raritgflrp
//
LOCUS       WP_457655886             167 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655886
VERSION     WP_457655886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..167
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18448
     Region          11..149
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 matyetmpfh leterlilrp waesdaadfs allaergngt ppverirksi aellaatett
       61 giallpierr eegdfigycg liigrttlee peiayelfrh ahgrgyatea agavleaava
      121 tgrkrlwstf gtwnapslrv lekhgferdh vstedngevv wltrslp
//
LOCUS       WP_457655892             353 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Streptomyces griseus].
ACCESSION   WP_457655892
VERSION     WP_457655892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..353
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=37443
     Region          18..330
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mpavmaaata allhrgtvvp ahplaltadr elderrqral tryyldagag gvavgvhttq
       61 favrdhgllr pvlelaaees aaaaaerpfl riagvagpvr qavaeattar elgydavlvs
      121 paglpdatld dlldrsaavg evlpvigfyl qeavggrelp raywraladq eatvavkaap
      181 fdryrtlelv qgiadsdrga evalytgndd tivadlltpy hvttptgpav rrfvggllgh
      241 wavwtrsavr lladvhaada gderarqral arlagdtdan aavydvrgrf agviagvhev
      301 lrrqglltgi wcldptegls pgqareiarv htaypwlaee dafiagalpr wla
//
LOCUS       WP_457655896             171 aa            linear   BCT 27-JAN-2026
DEFINITION  Jag family protein [Streptomyces griseus].
ACCESSION   WP_457655896
VERSION     WP_457655896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Winther,A.R., Kjos,M., Stamsas,G.A., Havarstein,L.S. and Straume,D.
  TITLE     Prevention of EloR/KhpA heterodimerization by introduction of
            site-specific amino acid substitutions renders the essential
            elongasome protein PBP2b redundant in Streptococcus pneumoniae
  JOURNAL   Sci Rep 9 (1), 3681 (2019)
   PUBMED   30842445
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Zheng,J.J., Perez,A.J., Tsui,H.T., Massidda,O. and Winkler,M.E.
  TITLE     Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins
            suppresses the requirement for PBP2b by overproduction of FtsA in
            Streptococcus pneumoniae D39
  JOURNAL   Mol Microbiol 106 (5), 793-814 (2017)
   PUBMED   28941257
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Errington,J., Appleby,L., Daniel,R.A., Goodfellow,H.,
            Partridge,S.R. and Yudkin,M.D.
  TITLE     Structure and function of the spoIIIJ gene of Bacillus subtilis: a
            vegetatively expressed gene that is essential for sigma G activity
            at an intermediate stage of sporulation
  JOURNAL   J Gen Microbiol 138 (12), 2609-2618 (1992)
   PUBMED   1487728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..171
                     /product="Jag family protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=18239
     Region          29..171
                     /region_name="Jag"
                     /note="Predicted RNA-binding protein Jag
                     (SpoIIIJ-associated), conains KH and R3H domains [General
                     function prediction only]; COG1847"
                     /db_xref="CDD:441452"
ORIGIN      
        1 mtegttrtaa aeagsdtltr leqegeiaad yleglldiad ldgdidmdve adraavsiis
       61 esardlqklv grdgevleal qeltrlavhr etgdrsrlml diggfrakkr avlaelgaka
      121 anevkstgep vkldpmtpfe rkvvhdaiaa aglrsesege epqrfvvvlp a
//
LOCUS       WP_457655898             448 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine protein kinase [Streptomyces griseus].
ACCESSION   WP_457655898
VERSION     WP_457655898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..448
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47218
     Region          1..419
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mgevfagrye lidpigrggv gavwrawdhr rrryvaakvl qqsdahtllr fvreqalrie
       61 hphvlapasw aadddkvlft mdlvsggsla hvigdygplp prfvcllldq llsglstvha
      121 egvvhrdikp anilmeatgt grphlrlsdf gismrkgepr ltetnyvvgt pgyfapeqmm
      181 gaepdfpadl favglvalyl lqgqkpdsqa lvehfvehgt pgapngipep lwqvlagllq
      241 pdpharfrta tgarkaltaa vemlpeagpd depvevfdqi gplpagfgpd gpvtapqqpa
      301 gpvpgpaaga apqpsatppv smsetgsfhl apppaagpsq qqpyvqsgfr qpppaapftt
      361 dapppyavga phssqaptsg vpdpaatray taqqqhppvp sppvqhaaph apvrvrqtrp
      421 gpppkvavpv lvvalicfav giwaltqi
//
LOCUS       WP_457655904             263 aa            linear   BCT 27-JAN-2026
DEFINITION  TraR/DksA family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655904
VERSION     WP_457655904.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..263
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26974
     Region          144..262
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvakktaedt aaehdgthep pagqgaapak rtakkaaark taarktaakk tvakkaaakk
       61 taagekpaak ktaakksaar ktsekaataa teaapaaeqt gaptvvakks asrpaaggqa
      121 tapvpparaa apdelavrpg edpwtpeevt eartlltsei lrlrseleas gaalaglmrd
      181 sgdgagddea dtgtknitre helslaanaq emleqteral arleagtygl ceicgqpigk
      241 armqafprat lcvedkqkqe rrg
//
LOCUS       WP_457655905             384 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Streptomyces griseus].
ACCESSION   WP_457655905
VERSION     WP_457655905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..384
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41887
     Region          80..331
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mesvlrpliv iggsvvitll igwladlllr radsrhhetp lwgllrrcrp plqvvvital
       61 lrgsyrqtri dwvwdhragi gqvltlvlig asawlvvria atvveasyar yatatrdpar
      121 vrrvrtqvtl iqrvviavvt vvaiaamllt fppmravgts mlasagllgi vagvaaqstl
      181 gnlfaglqia fgdmvrigdt vvvdgewgti deitltflav rtwderritm pvsyftsqpf
      241 enwsrggvqm tgtvffhldh sapvaamrek lrdllgdiaa wdgrdwslav tdttpstiqv
      301 ravvtakdan diwtvrcavr eqligwlrdh hpyalpriat apavlppgeq waeptgaktd
      361 rpgrngtspp vdrgdsrapr tgrg
//
LOCUS       WP_457655906             556 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces griseus].
ACCESSION   WP_457655906
VERSION     WP_457655906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..556
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59729
     Region          30..524
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtsrhlpsps rrtvvraaaa saaavpvlat asvtsaapar aagapaflhg vasgdplpdg
       61 vllwtrvtpe pgaepgsglg adtpvrweva edreftrisa tgttiasaas dhtvkadvrg
      121 lrpataywfr ftagddtada vvspvgrtrt apatdaavsg irfgvvscan weagwfsayr
      181 hlaarpdlda vvhlgdylye ygtgeygtrg ttlrahrpah eildladyrt rhgnyktdad
      241 lralhaahpv iaiwddhefa ndawsggaen htpvaegawe qrvaaakqay fewmpvrast
      301 egtvyrrlrf grlaelhlld lrsfrseqas vgsgavddpe rtvtgraqld wlkaglagsd
      361 aawklvgtsv mispvafgal pahlleplag llglpkegla vnvdqwdgyt ddrreliahl
      421 rdrgvadtvf ltgdihmawa ndvpvkaaty plsasaatef vvtsvtsdnl ddilrvapgt
      481 vsvvaatavr aanrhvkwvd mdahgygvld vtaeraqmdy ytlsdktdre attawtrsyr
      541 trrgtqrver adrpvr
//
LOCUS       WP_457655912             426 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457655912
VERSION     WP_457655912.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..426
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45792
     Region          146..424
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpqvvrprig altgppptap lphrfrslad reavevlhra arvlvaslpa ltdrlvealy
       61 aqepgyraai esdraevwqe vhhslrhnvg sliqprefre sahrtsrwig eiraeqgvpl
      121 davlhafrmg gamvwqdlvd etarrdpddv rllvhvaadv wnfvdehcgi vadayrqaer
      181 rltwrrenrq rlmvaalldg tariadlada avmlglpeqg ryavlavatv prgpgsaarp
      241 altlpaapea vvlwhpgqda efailplaga pgelselaaa ldvppgarag igsaveglaa
      301 lgdarrlaet alracpasgg tvlldehlpd alvvsspala galadrvlgp ldrldpadrd
      361 vivetltawl dadgsaqrag arlychrntv lnrlrrfeql tgrcltrprd avevslalag
      421 rrllgg
//
LOCUS       WP_457655913             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655913
VERSION     WP_457655913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41669
     Region          20..407
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(29..30,33..34,37,68,123..124,126..128,131,151,
                     154..155,158,243,246..247,250..252,255,279,283,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msapvtevpv rpahrdpnvl rwlgaytasm igdsvyfmal awaaartgsa sgtglvlaag
       61 slprallmlg ggvladrlgp rrvvigsdaa rallvlslaa vlvltaptvg vlvavallfg
      121 avdalflpav galpprisgp gqlariqglr alaargssii gaplggvava tggpalafaa
      181 agvlfalslp lllrlrirpl peptetsgea paaekasnaw hdlvdglryi rrhpllgplm
      241 lvialselgf vgplnlglil lseqrgwgaa gmgwivagfa ggaagsalvl avrgrvprag
      301 tvmclmalvg atgiatlaqv psvalaaaia afvgltagla galcgalvqt aadpaylgrv
      361 tsvstfftya iaplsypvtg aavalwgtgp vfavsaavca aggvmglavt tlrraelpr
//
LOCUS       WP_457655918             423 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457655918
VERSION     WP_457655918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 423)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..423
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44629
     Region          29..422
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mlsrrrrhar rgaadraavp ersrfavrdl lseavagvvq rparsvltsl gtvlgvgafi
       61 svlgltgsaa sqidarfnrl tatevtvedt ggndadrvpl afpddadsam grvngveaag
      121 vhwrvrlapg esvrstpaeg angsvsrtsv vaaspgvlsa arphfvqgrg ydrfhesrnq
      181 tvavigsata srlgittlrt qpavfigdta ftvigvfddv erkpdlllsi ivprttaeki
      241 wgpprderak mlistrlgaa tqvadqaava lrpdhpeyfr aipppapkal rddvgsdlgq
      301 lflllsivcl fvgavgiant tliavmertg eiglrrslga rarhitwqfl tesaalglfg
      361 gmagtslgtl vvvgvclhne wtpvinlttl asapaigllt gllaglypsw rasriqpvea
      421 lrr
//
LOCUS       WP_457655920             327 aa            linear   BCT 27-JAN-2026
DEFINITION  COG1470 family protein [Streptomyces griseus].
ACCESSION   WP_457655920
VERSION     WP_457655920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11444751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="COG1470 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33874
     Region          28..>240
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mspptprlrr allvltaala allcalastp aaaddgpadw tarpaggsgd rdarpyvyle
       61 gtpgtvlqdr lavtnsgrap ltvrlrgdgr agawirfaad tvtvpartra evplaltvpp
      121 davpggasge vvavdggees rvpvrvrigg ptlaaltved vgisgetlry alvnrgnall
      181 rprlavrvdg vfgtlldrpe rplplelapg rrveltepwp dapaldavtv rlrvtapgga
      241 rdeaeasaty lpvlpavggg llvlgvlall gsgayrrrrr tgrgapeppd teteaetkae
      301 teagtetete tetetdtrpl akagaek
//
LOCUS       WP_457655928             295 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655928
VERSION     WP_457655928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..295
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31311
     Region          1..289
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 matvvdlisy pvkgcagtsv dsthltpagl ahdrsfmvvs vdgvyrtqrr dprlalvrpt
       61 asadgsrltl asvepdsghg avhldvttsa prrevdlfga tyqgidqged aaawlteflg
      121 tpsrlvrvpp ehdrktdglt pgtsgyadss avhllsrssl allntrmaer dapplamdrf
      181 rpnlvvdshp egahgedgeh gedwaaepha edrirrmtig aaelgytkla vrcavtlvdq
      241 eagarggpep lrtlagyrrf saggvvfgak favvrpgkls vgdevaveew gepes
//
LOCUS       WP_457655929             278 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457655929
VERSION     WP_457655929.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..278
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29061
     Region          <63..149
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrrsprtcll allaliggll tvtataspaa aapnfkapya cgqqwtyshh saevrqaldf
       61 vrtdgggtag apvlasaagt ayrysqpsga gnyiavehgg gwktyyfhla afsvangaqv
      121 aqgqqigttg stgnssgahi hyeqlyngvg qtivingqsl asypgsyysk yltsdngcgg
      181 ggggkywvdt fanatgyaaa ntadaqgvln agtnyvyckv wgarvgtasq fnhwwlrtdl
      241 dvvyagkngr nayvsayyls rwgndeardn ngtvipdc
//
LOCUS       WP_457655930             644 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces griseus].
ACCESSION   WP_457655930
VERSION     WP_457655930.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..644
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69497
     Region          41..644
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mstppsavpa sasasagsrp vlieptkkrg pdgrvqevsv pkfapiverg slaeipfdna
       61 reapddlvls rkdaegawqd vsaaefaaev vavakglmae glragdrvai marttyewtl
      121 ldfaswaagl vtvpiyptss afqarwilqn sgavacavet keqgrlisqe rkqlgdlahl
      181 wqfdtgaigh lkslgkdipd aavaarratl epdtpatliy tsgttgrpkg cvlthgnffa
      241 evdnaiellh pvfksvskdp astllflpls hvfgrmvaig cmrarvrlgh apsiqtedll
      301 adlagfrptf llaipyvlek vyntgratae kmgrassfdr aariaqrygq aveaaehgtg
      361 pgpglglraa ralydplvyr riraalggkv ryvicggspl grrlaafyeg agigifegyg
      421 ltettaahtv tpplkprlgt vgwplpgtsv riaedgevll kggqvfrgyw dgeraevtpa
      481 lladdwfptg dlgaldedgy ltitgrkkdi iitsggknvt papledwlra hplvsqcmvv
      541 gdnrsfital itlepdglqh wrqmtkkqdv pmrdlihded lrtslqkavd eanrlvsrae
      601 sirkftvlpv dfteekghlt pslklkrdai ardfsgeieg lyrk
//
LOCUS       WP_457655933            1081 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces griseus].
ACCESSION   WP_457655933
VERSION     WP_457655933.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1081)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1081
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=113049
     Region          19..1081
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mtntttspsp svsvpsspel algpaqhgmw vteqvlrpgs ahhlavtarf avppdpaald
       61 agcarllarh pvlasrldpe gpalapatgl apelrrltca adeldallae esarpfdlaa
      121 gplvrfalvt agdagpvlha vahhlvfdgm skdvllaeil gaettaglpp dgpaeptaee
      181 aaaagefwtg rwsdpavpvl pglpssvrds tapapgsavp ftldgplhar itdtarslgv
      241 trfelllalw htllfrygdr apvtalelst rrpgspdhig lyvnelplfs rpapdrqfad
      301 fardvraelr alyahrtvpl gravrggltp rtaltplsvs yrrrtgwear eapdvavdwi
      361 gfthavrnla hlqlvegpdg vdgslqyrtd afapgapari vghfrtllda vltapdtrla
      421 dlpllagdel dralytgngt paarpadatv wamfaeraaa dpsavavvap dgaelsygel
      481 haaaeafadr laaegigpgd lvgiqvarsa geltavlgtl aagaayvpld pgypadrlaf
      541 vradarlaal vvegpapdgl pdglpvlspg hgesrehvas sehgaspehg aspqrraspe
      601 rrgdsapprg rsaapgaedp ayvlytsgst grpkgvevph salanligal adrlaagprd
      661 rwlgltslsf distvelllp lttgarvvlv peerqrdgaa llklieahdv thvqatpsgw
      721 rlmlasglhr pglvglagge alpeplaael arsvgrlinv ygptettvws tlaeltpgdp
      781 vtigrplaat rayvldahgr pvpdgvpgel hlggaglahg yrgrpgltaq rfvpdpwgpp
      841 gsrmyrtgdl vrrlpdgrle fagrvdtqik lrghrielge iearlvdhpa vsqavvvldr
      901 addaketgea reagetegtg qdrlvayvvg agqqapaadd lrahlartlp aamtpatwvp
      961 lpalpltpng kvdrarlpqa prtrpeaaag tgavaaggek agtaavvrdi wqevlrlddi
     1021 gpdedlfdlg ghsltitaia arirkrlgve vpldvffdtp tlaevsavvs elqqqeessd
     1081 e
//
LOCUS       WP_457655934             500 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457655934
VERSION     WP_457655934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..500
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52569
     Region          8..500
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtaaprslpa llghraaadp grtalicgpr tltfgtwher aealaaglrs rglgpgarvv
       61 lrygggdwia yavaycgvlr agcvavplsd rqapataahv ltdsgatavl hpagadlpsg
      121 plppgvwsat teeieaaeaa ppgpdpladp dpaalaqily tsgttgrpkg vtathgnlay
      181 gctlderrrp lrhsrhflha fpvgtnagqt mlvnaldsaa tavaapqftp grfarlieey
      241 gvgsvflvpa maiellgsea arryatdsvr lvgstaaalp gpvalglara fpraqvvnyy
      301 tsteaapaqi tllfdpdrpd spgrpaslrd lritapdgtp lppgepgevr lrtpaapray
      361 lgedaarsev fqghwvrmgd lgrldedgyl hlldrerdvi ksgaykvstl qveealhahp
      421 avadaaafgv phpvlgsvva avvvprgelt vpqlrtflld rlaahelpar llfrpflprn
      481 eggkilkrel rlllddealr
//
LOCUS       WP_457655942             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457655942
VERSION     WP_457655942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44017
     Region          24..405
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(33..34,37..38,41,73,126..127,129..131,134,154,
                     157..158,161,239,242..243,246..248,251,273,277,331..332,
                     336,340,356,359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mttdsrapap dvrdrpagpw qrwrilllan acsllgnyvq nlalplwvla vtgsytatgi
       61 tfavgtlpvv lcaplagriv drfnrlrvli icellcallv vvlvmgvrae slavvyvvsa
      121 llkavgsaai pavqallker isaeearpvi akfevifgaa mslgpiigaa lstgigieaa
      181 lwvnfssfvv sgliamtlrp saavgdraek sgddrpksrl eplrwsvidp rlrrvavaea
      241 syflflgaet vialavfket vgvaaaavyq tlaglgwvvg sylfvrrfnr qpfliwagaa
      301 vstvatvalv lsghawswaa vvvvgllgga gnvmiagaat vvyqaltpnd fmgrifafrr
      361 gtlnllmtvs yvsiplvgdv tghpahvllv agavnlaatt wlllrhlgas mdgtgddtp
//
LOCUS       WP_457655948             329 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457655948
VERSION     WP_457655948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34964
     Region          42..>215
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 msakrrvfls atgaavalaa taavavagpa grpdeatkpg rpaaaselrv mtlnlwhgga
       61 kvddglakqv avikkhrpdv vglqetsghs akelaeelgw dhwqsdadlg iisrfpfsse
      121 vetsraaagv rirideatgq evelwtahlg ydpygpydac fdempveeif lreaqsgrtp
      181 qaeaiakdla pkiaaadetp vllvgdfntp shldwteatk dshcgygqvd wpvtkifega
      241 glkdsfrean pdpaavpgtt wspvypkhdg stgvdepqdr idfidyaggk ltvkesvsfv
      301 egdpkpvpdq agnawptdha avlttftvg
//
LOCUS       WP_457655954             522 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Streptomyces griseus].
ACCESSION   WP_457655954
VERSION     WP_457655954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..522
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=54706
     Region          28..319
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mtgasdsvrv vvvwvpdfpv lacgtrdgap vavahrgavv acsasaraag vrrrmrlraa
       61 qarcpglrvv erdlaaevrm feqvvhrvea evvprlevir pgliaaparg aarywggeaq
      121 lsvrladtvt alglparvgi adstfaaala arrgdgvivp adgnaaflap ypvgvlgvpg
      181 ladllkqlgi rtvgdfarlp agrvaerlgt egigahrvar ggqarpvsvr taaqdhtvrr
      241 lfevpeqqtd avvfvavala delherlaaa gvvcarveav vgtadgrtlt rifrhegrls
      301 sravaervrg vlaawsekgl ldaggtepgi rslalrpegi spdtgsqgaf dgerdtpvev
      361 eraaarvqav lghravtrii evggrgpgdr irlvpvgdvp ddgagatgae gaaggpwpgr
      421 lpaphpaavy pvrrparltg tdgapvgvag rlelsaepaf lavdgrrrag vngwagpwpv
      481 leqwwtrdsg rriarmqvtt ddghawlllv drgrwwaeah yg
//
LOCUS       WP_457655956             254 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655956
VERSION     WP_457655956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..254
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25771
     Region          1..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgdlsgrtal vtgasrgigq aiavrlaaeg atvfvhfgtd ergaaatlda mehaggtgfa
       61 vraelgvdgd vetlfagvea gldgrpldiv vnnaaaapag plgittraef dhlfavnvra
      121 pyfiieralp llregariis issvatrman ssqtsfamtk gaietmtktl avqlgprgis
      181 vnavapgatr ttangavfdv pglteqisvm talsrlgtpd dvadvvafla sdaarwvtgq
      241 ildasgglfl gpri
//
LOCUS       WP_457655959             730 aa            linear   BCT 27-JAN-2026
DEFINITION  Hint domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457655959
VERSION     WP_457655959.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Burglin,T.R.
  TITLE     The Hedgehog protein family
  JOURNAL   Genome Biol 9 (11), 241 (2008)
   PUBMED   19040769
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Perler,F.B.
  TITLE     Protein splicing of inteins and hedgehog autoproteolysis:
            structure, function, and evolution
  JOURNAL   Cell 92 (1), 1-4 (1998)
   PUBMED   9489693
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10051399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..730
                     /product="Hint domain-containing protein"
                     /GO_process="GO:0016539 - intein-mediated protein splicing
                     [Evidence IEA]"
                     /GO_process="GO:0016540 - protein autoprocessing [Evidence
                     IEA]"
                     /calculated_mol_wt=77009
     Region          470..611
                     /region_name="Hint"
                     /note="Hedgehog/Intein domain, found in Hedgehog proteins
                     as well as proteins which contain inteins and undergo
                     protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In
                     protein splicing an intervening polypeptide sequence - the
                     intein - is excised from a protein; cd00081"
                     /db_xref="CDD:238035"
     Site            order(470,543,610..611)
                     /site_type="active"
                     /note="protein-splicing catalytic site [active]"
                     /db_xref="CDD:238035"
     Site            order(470,540,543)
                     /site_type="other"
                     /note="thioester formation/cholesterol transfer"
                     /db_xref="CDD:238035"
ORIGIN      
        1 msqqnsasgd deprtgpvst tgpvhawwqg lsswqrialp agiltlviav iaaaalnsgg
       61 asegsratap dlqpfreavd glaeapglry kdtstlgite nditvtadgs qfgttssgrs
      121 drgrdvlrig gkkftrwqvd paprktvaad ekappsewiv glddgselmd ealartvapp
      181 qlaavldkal adlekspppa ngsktpgtpg qrpltvngtp algidtsagr llvteekphr
      241 vlrleaydlr dgladmkdql engetpsapr tvttgplaag gaegmdltpv ladaadkmfd
      301 tlveyadqle datdrgitft ldgagemdcs adgctatqnf tgevtsiark ervtkgkvta
      361 vmgatftidg kpagectspq rtfpvrgnnv sgtlkcsnpa agplyasvaa rvqaqaqada
      421 drcgckvrlt yplrastlid aralakveaq klaaqakser dradcvkphs fpsgtqvlla
      481 dgttraiedi rvgdrvatsd prsasaatrp vtntfatdgd kdftritvtt drgpttvtat
      541 dnhpfwltdd qrwknagdlr vgdelrttdg tgvavtevrd qqgrhrthdl tvdelhtyyv
      601 lagrtpvlvh nnngcpphvt gkgddplvpe lvkdinaryp ghvraqgvdi vgangkaltd
      661 fdivtrnavv qvktgsgkga lkqalrtqsl tdypvivylp qgrgsviksl eqagimvtrd
      721 knvlldalap
//
LOCUS       WP_457655963             578 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces griseus].
ACCESSION   WP_457655963
VERSION     WP_457655963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..578
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62095
     Region          12..569
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mhpqrdraql amkdvskayg drsvldqvtl tvrpgektav igengsgkst llrllagveq
       61 pdtgeitvrf pgstgylaqt ldldpsdtvq davdaalael rdlehrirea eaglsgrkpg
      121 dpeptdaelt aygdlltaye drdgyraear teaalhglgl ahltrdrala tlsggeqsrl
      181 alacvlaaap elllldeptn hldaravgwl edhlrahrgt vvaithdraf lervtsvile
      241 vdrdlrtvtr ygdgwdgyrt akaaarrrwa qeheeyvadl arteelveaa garlaatggd
      301 pkqgfgkhrr sheaklsgqv rsartrldal rrspvppppr pltftgrptv ttatagaeha
      361 gtteaagtae aadaigmpdr trplveldgv svgdrlrlps lrvapgarll vtgengagkt
      421 tllrvlagdl apdtgtvtrh arigylpqel parptrrtll atfaagrpgf pdeyadella
      481 lglfrpedlg vpvaslsvgq qrrlalarlv trpadllvld eptnhialsl veeleqaldq
      541 yrgavvvvsh drsfrsrftg dvlelragrr vgtvpapa
//
LOCUS       WP_457655965             407 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457655965
VERSION     WP_457655965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=42887
     Region          14..383
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 maqkraskqt rkqrgvrhrs gaapgpdagt asvsrsrign wtlfgglvll tvlvvfldir
       61 tgndlrvvpl lvvvpalasv ycslrqtiwv avwittvvvg fragadgtfw dflfgigfav
      121 lacalgvaac aarirhatem arlrsaavtl qrqilrplpv vtghvlahgl yepieedrfv
      181 ggdiyevves pygtrviigd vqgkglaaig agfaaiaafr eaaireptlt gvvealedav
      241 vrhnvfsaqt geaerfvtal vlgfdgsgrv eavncghlpp rllhdgrasa vtlhrtyvpl
      301 glaglsresr atesfafppg atllvvtdgv teardtagaf ypldervcaw agrgpselld
      361 alrvdledfs ggvrrddiaa lalshapvgg ggrsettged alrvvav
//
LOCUS       WP_457655966             253 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457655966
VERSION     WP_457655966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10552919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..253
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27056
     Region          146..233
                     /region_name="FR47"
                     /note="FR47-like protein; pfam08445"
                     /db_xref="CDD:117022"
     Site            order(174..176,186..187)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mpqnpampra htpprlhpld nparssltgp hahfaesrgr ilrypvdvtp wiglpddpda
       61 qdwadlaala gpggsvalaa fqaqppdewe itfraegvql vdasveaapd peavplgprd
      121 vpemlelvar trpgpflprt velgtylgir rggalvamag erlhppgwte isgvctdesv
      181 rgqglasrlv lavahgirer getpflhasa sntgavrlye slgfrlrrrt efiaalvpat
      241 lpsaegdrrp slr
//
LOCUS       WP_457655968             244 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655968
VERSION     WP_457655968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..244
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25527
     Region          20..243
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtestsgqsg talaedpart vmvtvedlhr sygsgaaavh alrgvsfeip rgelvalkgr
       61 sgsgkttlln lvggldtpdg gritvdgtdl sglgekglle lrrdrvgfif qsfglipilt
      121 aaenvgvplr lrkadpderd ervalllslv gladhaeqrp gelsggqqqr vaiaralanr
      181 palliadept gqldaetgla vmellravvr senvtalvat hdpqllglad rvlelsdghi
      241 veqa
//
LOCUS       WP_457655971             362 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Streptomyces griseus].
ACCESSION   WP_457655971
VERSION     WP_457655971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..362
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /EC_number="1.14.99.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37865
     Region          1..315
                     /region_name="COG3397"
                     /note="Predicted carbohydrate-binding protein, contains
                     CBM5 and CBM33 domains [General function prediction only]"
                     /db_xref="CDD:442624"
ORIGIN      
        1 marrkklfaf maavlatllg gigltlmgqs saqahgvtmt pgsrtylcml daktatgald
       61 ptnpacraal desganalyn wfavldsnag grgagyvpdg klcsagdrsp ydfagynapr
      121 sdwpqthlts gstiqikhsn waahpgsfrv ylskpgysps telgwddlel ietvsdppqs
      181 ggpgtddghy ywdldlpsgr sgdavmfiqw vrsdsqenff scsdivfdgg ngevtgirgs
      241 ggtpnptptp tptptptdph tgcmalysvt sswsggfqgs vevmnhgtaa regwavqwkp
      301 gpgtevssvw ngaltrepdg tltvrnvdhn rtiapegsat fgftatstgn nfpvgsigcv
      361 ap
//
LOCUS       WP_457655974             396 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457655974
VERSION     WP_457655974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 396)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=42948
     Region          18..395
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,86..87,94,98,105,229..230,233,237..238,241,
                     274,279..280,283..284,286,309,336..338,341..342,344..346,
                     350)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,80,82,85,87..88,170..171,179,228..229,232..233,
                     237,280,283..285,385)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtaprqdplr dprffadpyp tydrlrercp vqrvptgsgg hqgylitgha earaaftdpr
       61 lskdtarffa drpsdrdlhp aisrtmlasd ppahtrhrrv atplfttgrv rdlrpfitrv
      121 vdglmakwrp gtevdlvael avplpvtvic ellgvpesdr aalagwshel fdatdtarvd
      181 aashrigdyl thlvdtarat pgdgplhall rdcdeggldr dgavslaall lvaghetttq
      241 fignavlall rhpeafdrlr rdpdlipgal dellrydspv svatfrysaq elsvggvdvp
      301 agfpvliatg aanrdpavfp dpyrldldrd atghlsfghg ihrclgapla raeaeialra
      361 lvtrfpdtgl avdaealawr rtrltrglta lplvlg
//
LOCUS       WP_457655976             386 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655976
VERSION     WP_457655976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..386
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39428
     Region          23..363
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkvvvvgagi vgaacafhav aagldvtvld rgpvgagtts rgegnillsd kepgpelela
       61 rlsrelwgev aaelgpesve fetkgglvva stpealtalh afaarqaesg vrtepverpg
      121 dlephiapgl pggvhypqda qvqpvlaaag llraavrrga rthtgeavaa vtgtggritg
      181 vrtadgsvla adavvnaagt wggevgrrlg apveilprrg fvlvteplpr mirrkvysad
      241 yvanvassda gletscvveg tragtiliga srervgfdta mnpavvtala aracrlfpfl
      301 rgvhlirayr gfrpycpdhl pvvgpdprvp gvvhacgheg agiglapatg alvtaqllgk
      361 pwrgadpaah tgllpdrflt tggapk
//
LOCUS       WP_457655977             527 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655977
VERSION     WP_457655977.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Blumer,C. and Haas,D.
  TITLE     Mechanism, regulation, and ecological role of bacterial cyanide
            biosynthesis
  JOURNAL   Arch Microbiol 173 (3), 170-177 (2000)
   PUBMED   10763748
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Castric,P.A.
  TITLE     Glycine metabolism by Pseudomonas aeruginosa: hydrogen cyanide
            biosynthesis
  JOURNAL   J Bacteriol 130 (2), 826-831 (1977)
   PUBMED   233722
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14289850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..527
                     /product="FAD/NAD(P)-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53512
     Region          33..386
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     Region          428..480
                     /region_name="GlpA-like_Fer2_BFD-like"
                     /note="bacterioferritin-associated ferredoxin (BFD)-like
                     [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate
                     dehydrogenase subunit A, hydrogen cyanide synthase subunit
                     B, and similar proteins; cd19946"
                     /db_xref="CDD:381079"
ORIGIN      
        1 msesgdllvt gephdlvvvg agpagmaaaa taldgglrvv lvdagaalgg qfwrhpppla
       61 qeavptadlh hglgvyrelc arlaahertg rlalllnhpv wttareddgf tvhavdrsra
      121 peertvvlra pallvatgay drqlpfpgwd lpgvltaggl qallkgggav agrrvvlggt
      181 gpfllpvaaa lavrgaevva vceaaapsaw lrhpaallrn pakwaeaary agtlarhrip
      241 vrtrtaiiga eaeagagaga gagvgvggqa gvggaaegrv afvrtaslda dgnplpgter
      301 riaadtvgvg wgfvpqvdll lplgcdlada gdgtmaaavd dgqrttvpgl ytagetcgvg
      361 gaalavsegr vaavsiltdl sapglpntrr laaerrtvtr hrafaramar ahplppawpa
      421 wltddtpvcr ceevtagavr saraddaaad hrqvkqltra gmgwcqgrmc gpavhclvar
      481 dqpyapaerl iatpvtlgal adadasppgp ppdpapdldp apasdpt
//
LOCUS       WP_457655979             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655979
VERSION     WP_457655979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38091
     Region          17..344
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpsttepdrl lepdrpllrv hdlrvafdtp agtvqavdgv sftveagrtl glvgesgsgk
       61 svtslavmgl hrrarvsgsv tlagqellgl tdrrfgrlrg rrmamvfqdp lsalhpaytv
      121 geqiaeahrh hfgsgrrvar rravemlgev gipeparrag eyahqfsggm rqramiamal
      181 acepellvad epttaldvtv qaqileliar lqqerglgvl mithdlgvva rvahevlvmy
      241 ggcgaeqapv ddlfrspahp ytrglldslp rlddpddapl raipgsppsp aapragcpfa
      301 prcpraaaat aperarcage sprprdvpgg grlvachlpl pptphsgpag gvpvpaeear
//
LOCUS       WP_457655980             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457655980
VERSION     WP_457655980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36499
     Region          20..342
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mkptyinspl srarsvegdg aaapllsvrg lvkafpgrrv lgraaapvra vdgvdlelaa
       61 getlglvges gcgksttgrm lvrlleptag tvefegrdit hlsprelrpv rrrlqiifqd
      121 phaslnprqt variiaepll vqgatasaar draaelldlv glgsehldrh pyrfsggqaq
      181 rigiaralat gprlivadep vsaldvsvqa qvvnlmerlg eelglsflfi ahdlsvvkrv
      241 cdrvavmylg riveigdkhe lydspahpyt rallsavplp dpaaerrrer illlgdppsp
      301 aappsgcgfh prcpkaqavc rterpllqvv gsgartaacl fp
//
LOCUS       WP_457655982             372 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            griseus].
ACCESSION   WP_457655982
VERSION     WP_457655982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..372
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39369
     Region          8..367
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtsineqpip aarpvigede ieaavrvlrs grvvqgpeva afeegfsrlv ddrhcvavns
       61 gtsalhllll algigpgdev ivpsfsfaas anavrlvgad vvfadiepgs fgldpaavea
      121 aitprtaaim pvhlyghpaa mdkimpiaek hklavvedac qahaaalngt pvgafgaggt
      181 fsfyptknmh sleggmvtta daelartlrl lrnqgmeqry aneivganmr mtdvsaavgr
      241 vqlgkvegwt eqrranaayl dahitapavt tppvaegarh vyhqytvris gdrdaamakl
      301 teagignavy yptpihrlrp ywepdqkagr twdlpetera aaevvslpvh pslteddlar
      361 iaaavnalge nl
//
LOCUS       WP_457655983             537 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces griseus].
ACCESSION   WP_457655983
VERSION     WP_457655983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..537
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58615
     Region          3..176
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mttpdvtvvv avyntmpylt ecldslvgqs igherlqvva vddgstddsg keldrfaqly
       61 pdvftvvhqp nsggpaapsn raldlatgry vyfigsddhl geealermvg hadahesdvv
      121 vgkmvgtngr yvhqklytgn rdvtlddsel pftlantklf rrelvekhkl rfpedmpvgs
      181 dqpftieacv rarkisvlsd ytcyyavkrg dasnityran hlarlrcvqr imehtaalip
      241 agprrdavfk rhfdweltkl lqkdfpaldl dtrrqvcegv gglvdayftd glrdgtgvkr
      301 rvrfglarsg avqeltraia eetehgappf llegdrafaa ypgfrdpavg lddryyevlg
      361 etvagrlstg trlesagweq hgtdltcvvn lrvgitgdts tavvalaqga mpqsadkpga
      421 rklpadaprp qrsgtltagp aedggtllta riplapartk rgvrlyvdva gstyeipvrt
      481 egqpmplarr wgtadphrvs anintkgrlv ittaplrepk sgvgarlrrt lsrskrk
//
LOCUS       WP_457655988             247 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces griseus].
ACCESSION   WP_457655988
VERSION     WP_457655988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..247
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27037
     Region          12..>141
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtsselwtre tadrydaeea ensspaalgp tldflaelag dgralefaig tgrvgvplrq
       61 rgvpvtgiel sepmaavlrr kadedtlpvv igdmattvvs geftlvylvy ntignlltqd
      121 eqvacfenaa rhlapggrfv ieltvpplrf lppgqaavpf dvserhlgfd tfdlveqtlv
      181 shhftrdgdd gryrrgtcrq ryawpaeldl mariaglele srvedwdgtp fgpdsakhis
      241 vwrkpva
//
LOCUS       WP_457655991             261 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457655991
VERSION     WP_457655991.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  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 261)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1008156
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..261
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28923
     Region          42..141
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mrqrpigtat rgttnpnrlr rmdrwiadah gpalrragtp vavdlgygaa pwtavelldr
       61 lrtaeprtvv agieidperv aaakpyereg ltfvhggfev plevrpllir aanvlrqyde
      121 eqvaevwarl csrlapdgil vegtcdeigr rhvwvalgpe gprtvtfatr lgslerpsdl
      181 aerlpkalih rnvpgepvha flrdfdrawa aaspyaslga rqrwiaavra vaadwpvtdg
      241 vrrwrqgeit vpwnalrpns r
//
LOCUS       WP_457655993             334 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457655993
VERSION     WP_457655993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..334
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35413
     Region          1..331
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,127,131,153..158,177..178,180,194,
                     213..214,235..236,278..280)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mkaflieryg dkagvragev pnpevgaddv lvkihaasvn pldlklrdga fkaflpyrlp
       61 lvlgndlagt vvrvgpavtr favgdeiyar pdkdrigtfa eliavhqddv aikpatltme
      121 eaaslplval tawqalvera qvqpgqkvli hagagglgti avqlakalga hvaatastak
      181 adlvkelgad vvvdyrkqdf etvldgydvv ldslggenla kslrvlkpgg kaigvagppd
      241 aafarelgln pilrivmsal sfttrrrakr rgvtysflfm kagggtlref arlvdagkir
      301 pvvdrvfpfd qtpkameyve kgrakagkvv iamt
//
LOCUS       WP_457656000             364 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457656000
VERSION     WP_457656000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..364
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35642
     Region          144..>361
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtenlrpsgt hstdqdptay pyassygpaq dgtaysgtaq dgtayagaag gypppppyap
       61 tnrrrakrpv allaavaiaa gvigggtatl igqlngqnsa atgsggavng ttvsqsskgt
      121 vagvaeavsp aiveigatss agkstgsgvv itedgeivtn nhvisgaqqi qvtlstgrty
      181 tadvvgtdpd kdlaliklqg asglktatlg dssqvkvgde vvaigspegl tgtvtsgivs
      241 aldrdvtvak ddsggsgqdq gqgrqgggqq wpfefggqqf ngdtgeettt ykalqtdasl
      301 npgnsggali nmdgeiigin samyapsssa sgsgssagsv glgfaipvnt lkadldtlra
      361 gngs
//
LOCUS       WP_457656006             605 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            griseus].
ACCESSION   WP_457656006
VERSION     WP_457656006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  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 605)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..605
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62912
     Region          52..585
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msatpqknra trrvlaaaag latvgalvaa mpagahdrgh ghghghghkp rtvdvqllsf
       61 ndlhgnlepp agsagnvset qpdgtvkaip aggveylats lrtarkgnpy svtaaggdmv
      121 gaspllsglf hdeptiealn kldldvtavg nhefdegate larlqnggch pvegcyekgk
      181 kfkgadfpyl aanvtkektg kpllkpytvw kkngvkigfi gvtlegtpdi vtangvkglk
      241 fhdevetink yakeldrkgv ksivaliheg gapastsyny dcdspgagdg isgpivdiak
      301 gitpkvdalv tghthqayvc tvpdpsgkpr mvtsassfgk lytdttltyd rrtndivrts
      361 vksanhvvtr dqpkaadmtr lidrwnklaa piankpqgwi sadingrgst apekplgnvi
      421 adaqleglap adkggaevaf mnpggiradl vhkasgsegd gvvtygeaft vqpftnmmnv
      481 vdltgaqlvt alqqqvsggn easpkilqvs kgltytldlt ksgadrvvad tiklngeaid
      541 partyrvamn eflagggdgf aalgegtnkl vgasdldlfn aylaahstaa aplappatdr
      601 itviq
//
LOCUS       WP_457656013             467 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457656013
VERSION     WP_457656013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..467
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50069
     Region          51..458
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(165,167..168,299..303,318,321..322,325,340,344,396)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mnrprparrr tatvllalal lgggcsggve gtpgavglrd pyfpglgngg ydvthyglel
       61 dvdpaagrlr gtatitarat qdlsafhldl lgldvesatv egrraavnra gkeltlrpap
      121 gaesrlrkgr tftavvrysg spltvtdpdg skegwlptad gavalgeptg smawfpgnhh
      181 psdkaaydig itvpeglaai sngelvsrrt angrtayrwr taepmasyla tvavgrfate
      241 qsvtpdgvrl ftavdpesaa asedvlarmp avlkwaagkf gpypfssaga ivertgdssy
      301 aletqnrpvy pgppdtallv helahqwfgn svtpktwrdm wlnegfatya ewlwaadhed
      361 vpveesfrea yeddanwafp padpptaael selpvygrga mavhrirlav dddaaffalv
      421 rgwtkkyrhg naatddftay veeetgqnlg rlwdawlygg srppleg
//
LOCUS       WP_457656014             308 aa            linear   BCT 27-JAN-2026
DEFINITION  1-phosphofructokinase family hexose kinase [Streptomyces griseus].
ACCESSION   WP_457656014
VERSION     WP_457656014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..308
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31382
     Region          2..300
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltvtlnta ldvtytvdal vphgshrvge vierpggkgl nvarvlgalg hdtvvtgfag
       61 gatgtvlrdl laplpprdal vevagntrrt laitdrstgd ttqlnepgpq vspaewaafl
      121 qtyedllaga davalcgslp pgihvgayae lvriaraaav pvlldtsgep lrrgiaarpd
      181 lvkpnaeela rltgsreplr aagdarrrga havvaslgpe gvlaltpdgv wraappapvr
      241 gnptgagdsa vagllsalae gldwprrlar avalstatvl apaagefdaa ayaellprvt
      301 vephvpap
//
LOCUS       WP_457656017             282 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase, partial [Streptomyces griseus].
ACCESSION   WP_457656017
VERSION     WP_457656017.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  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 282)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>282
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          28..223
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mnepipvire vdcgtarllp dvdrdrawll tvddapqsyv dlddpsylef eyvrrlahvv
       61 dgaaepgvpl dvlhlgggal tlpryvavtr pgsqqdvvea drallrlvre hlplpdesgv
      121 alhaadarqr leatapasvd lliadvfggs rvpahltsve yaraagralr edgvyaanla
      181 dsapfaflrs qlanfaavfp elaligepav lrgrrfgnvv llashapidv dplvrgcaad
      241 afparvthga altrflggar pvadadavas peppdgafsv gs
//
LOCUS       WP_457656020             246 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457656020
VERSION     WP_457656020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  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 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..246
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26770
     Region          38..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mhwyeddalw sdfaptmfpp araesaaalv assplldfpp gtrvldlccg pglfvvplag
       61 rgyevtgvdl spsmlesara aceaagaavr leradmltyr epgafdvvln vftsfgyfde
      121 aednlqvlrn ayeslapdgq llidvmgkev lagwigrpka vdlpdgayvv qrdtvldswr
      181 rlrtdwtlvr gtsartasit swlysaaelh alfesagftd vecfggfdas gydqrsdrli
      241 vrgrrt
//
LOCUS       WP_457656022             202 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656022
VERSION     WP_457656022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 202)
  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 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   5  (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 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..202
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21467
     Region          62..135
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrshghgyeh gpghygpghh grgegdgrra afgpfgppfg ggpfgggrgr ggggrgrarr
       61 gdvrasilal lkdrpmhgye miqeigersg gawrpspgsv yptlqllede glivsasegg
      121 kklftltesg rseaetgpea pweeagrgvd weavneirqa gfglmeafgq vwktgsadqr
      181 qkaltvinda rkklylilad eh
//
LOCUS       WP_457656023             434 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656023
VERSION     WP_457656023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44483
     Region          24..419
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,75,130..131,133..135,138,158,
                     161..162,165,252,255..256,259..261,264,288,292,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mqspasspsp spsptpslwr dadfrrlwvg qtasqlgeht tlvvlplfav ltldagagrl
       61 gvlravgqap vlllsllaga wvdrwrartv mvltdagrav algaaavagl lgllglpalf
      121 vvafavgals vlfdvayqas lvrmvrrdql vrgnsalegs rsaaqiggpa lggalvslls
      181 apfaaasgal ffavsflslr rirrpesvpp vcgerpedrp cpepaprirh riheglrfva
      241 gnpwlravcl asaafqfsla atmtvyllfl pralhlpgat vglalaatgp gallgsvlaa
      301 rlpgrfghga vlvsaavlgn gallcvpalh gsstatvlal lavnvvfgaf sqlvnvtvms
      361 vrqavtpdgm qgraaatitf vgmgltplgs llggflaqew glragllmaa agmmlspavm
      421 aasplvrlgr rltp
//
LOCUS       WP_457656024             273 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces griseus].
ACCESSION   WP_457656024
VERSION     WP_457656024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..273
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28328
     Region          1..269
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mririvdaft drpfsgnpag vlllesgafp aaerlqeiaa evnlsetafa hplppggtad
       61 walrwftpaa evdmcghatl atahvlhttg latgpvrfaa rcgiltatah pdgsltldfp
      121 tsplaeepvp ygladalgad pvsvhatgeh igdllvelrd eatvralapd faalvahsrr
      181 gviataeaed pargydyvsr gffpgvgide dpvtgsahta lapfwsarlg rddltglqas
      241 arsglvrtal rgertlltgs avtvidgelv tal
//
LOCUS       WP_457656025             264 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces
            griseus].
ACCESSION   WP_457656025
VERSION     WP_457656025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..264
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=28016
     Region          154..245
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 meagrvadsf pqeavsrril rsevvlvlal slgasalssl isfvgsltkp gglqdqaakl
       61 ngsyapdrpw ldlswqmfgi atalvpvalv ahlliregtg lraigfdrar pwfdlgrgtl
      121 vaagigsagl afylaahatg fsltvvpesl pevwwkypvl ilsaiqnsvv eevivvgyll
      181 rrlgqlgwtp maalvassvl rgsyhlyqgi ggfignvvmg vvfvllyrrw grvgplvvah
      241 alldigafvg yallagrvgw lptl
//
LOCUS       WP_457656027             507 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces griseus].
ACCESSION   WP_457656027
VERSION     WP_457656027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 507)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..507
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51501
     Region          71..486
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msagtppapg aqgvpaglla ggadgpgrlr dlttivldal edaprarggp lpaggpgava
       61 lstralcspv lpaegvgpea aladvvrava egaadpadpa cvahlhcppl avavaaelag
      121 aalnpsmdsw dqapaagvie elttaalarl vhpaapapda litsggtesn lvalllarer
      181 ampgplrvvt ganahhsvhr aawmlglpap tvvacrdgvi dpdaldrvlt glagapllvv
      241 atagttdegr idplpeiari aerhtarlhv daayggpllf serlaplltg leradsvtfd
      301 lhklgwqpva agvlavadag mltplslrad ylnadddtea glpdllgrsi rttrrpdavk
      361 mavtfralgr rglgelvehc vrtahefgea vdarpalrrr pggigistvl frpavadtlp
      421 edagdavvaa vrrillaegr avlgravaed gdgrrrlwlk atllhpnaat adllplldlv
      481 taaadravse apaaegtqap gaerlsp
//
LOCUS       WP_457656033             401 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Streptomyces griseus].
ACCESSION   WP_457656033
VERSION     WP_457656033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /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=41495
     Region          64..245
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          250..367
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 msparphirr tapagrrarl altgpaalla aaltacsggs sgsagsggdd kapatnvsvn
       61 ltgkaatpgg pvkvtlahgk lqavsvtagk ggalagkisa dgrtwtserv aapgtaytve
      121 akdtgggsdr aafttaaaek vnklslapgk nttvgiaqpl svvfdhpvkd kaavekalkv
      181 stsngtegsw gwlqdysgkd rvdwrpeeyw kpgtkvtlda rlngvntgad ggwfvrdyat
      241 tftigaaqvv evdldrhrla lrrdgkqvld lpmsagtpgg ekaswrgtav lmskegtinm
      301 rsetvglgda ydkmvdysmr ltwsgmyaha apwnarhfgq anrssgcvgm sdadaaalyg
      361 qvrvgdpfem tgaeakgtva egngygawnv swadwraksa l
//
LOCUS       WP_457656038             362 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656038
VERSION     WP_457656038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 362)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 362)
  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 362)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..362
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39365
     Region          32..358
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 marrrglsvr lrltlsyagf lmvagvlllt avwvylleyv pddwnqrmlh qnpnrqllay
       61 tfapaaatvl aillvfgllg gwflagrmla pltriteatr aatdgslshr irlpgrkdef
      121 reladafdtm larleahvae qkrfaanash elrtplavsk tllevaradp drdtgeiidr
      181 lhavnsraid lteallllsr adrrsfprer vdlsllaeea aetllplaev rgvtvethgd
      241 iaptigsptl llqlttnllh naivhnlpdr gtvrvttsvh petvditven tgarltpeva
      301 stltepfqrg aerlrthhtg vglglaiaet itrahdgtlt laprsggglr vtvelpatap
      361 hg
//
LOCUS       WP_457656040             352 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656040
VERSION     WP_457656040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..352
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36989
     Region          64..352
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mtqvdtpstp stadvveetp gadtadpaea sgtwrrgrll aasalllglv lllharipnr
       61 ignlgslvet flpwfgllvp vllagavlrr sapavialll plvawlnlfg gmltdkaheg
      121 gdltvashnv gaenadpigt aralagsgad vlaleelaah aretyekela keyphhtvqg
      181 tvglwsrfpl sdsrpvdvkm digplgdakp aevkmvynrg lrttvatdrg plavyvahlg
      241 svrvnpragl stgqrdagaq slgqalaaer nervvllgdl ngtlddrayd gitarlesaq
      301 eaagdgfgfs wpatfpvvri dqilvrgvep ksswvlpatg sdhlpvaari sw
//
LOCUS       WP_457656042             369 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656042
VERSION     WP_457656042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..369
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37361
     Region          48..362
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 matsldhlss kpsrpapvgt gsapprrvpl pllltglgla lplslvcgag lgssglswad
       61 vlrylwaglt ggaigpdevp aytivwelrl pravlaavvg aglsaigvav qamvrnalad
      121 pfvlgissga avganavlif galgalgiwa lstaaflsal lamllvyava rtergltplr
      181 lvltgtamyy gfsavttfmv faaergeaar sammwllgsl sganwaavpi aagavlagla
      241 hlgwsarrln alamgdetaa algvdagrlr kelflvsaav tgavvavsga igfvglmvph
      301 avrmlvgadh rrllaaapla gavlliwvdi lsrvvlapae lpvgvltavi gvpcflllmr
      361 rraysfggi
//
LOCUS       WP_457656044             430 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces griseus].
ACCESSION   WP_457656044
VERSION     WP_457656044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 430)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..430
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46932
     Region          52..430
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(98,119,121..122,205..206,214..215,218,221..222,225,
                     261,264..265,268..270,273,316,317..320,344,420)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(120..121,128,132,139,184,187,265..266,269..270,
                     273..274,277,315..316,318..319,321,344,371..373,376..377,
                     379..381,384..385)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtesttepar qdpaptcpvt rpgagpvtat patatppsat pfpqdrdcpy hppagyaplr
       61 edrplsrvtl ydgrpvwavt ghalarrlla dprlstdrth pafpvpaerf anarqrrval
      121 lgvddpehna qrrmlipsfs vkriaalrps iqetvdrrld amerkgppae lvadfalpvp
      181 smvicallgv pyadheffee csrrllrgpa aadvdsarae leeylgalid rkrtepgdgl
      241 ldelihrdgp ngpvdrqdlv sfavillvag hettanmisl gtftllghpg qlaalraget
      301 ttsvvveell rflsiadglq rlaaedieva gttirkgegv mfstslinrd tevfadpetl
      361 dwdrsarhhl afgfgvhqcl gqnlarteld ialrtlferl pdlrlavpah eiehkpgdtv
      421 qgllelpvew
//
LOCUS       WP_457656047             287 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457656047
VERSION     WP_457656047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18601933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..287
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30302
     Region          40..151
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     Region          48..270
                     /region_name="PRK08317"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:181382"
ORIGIN      
        1 mtapppegap gdgrygeayf rpdrageaer idfgalaydd ltmarllalg agpgwhcldi
       61 gagtgtvshr llgeagvgsv lavdrdvrfl narpapglev lqadvtapgf apgrfdliha
      121 rfvlmhlper drligelael lvpggvlvls davdltsdrp pttpystamr amwqglrtti
      181 gtdvsrvpsy pqllrgagle pvaaeihvpp llpgspisrf wadtwqrgre amlatglvdd
      241 tavdealhyl estacaalsa gmltawghrp tvtttpsspr rtdsspg
//
LOCUS       WP_457656048             544 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656048
VERSION     WP_457656048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..544
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=57898
     Region          20..72
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 msensveall eearltaaip ppaerqrlre aaglsraqva savgvgrstv anwetgvsdp
       61 qpparlsylr llkglveiyp aapasapata pdpapgptse ptptptptpt papaavadpe
      121 ptvpvpaftg hdtlrgpdgl avegepgpcv rcgvtttfrs tdghplhaga fcvpaapsne
      181 taptpavtpa atvpapatas ptpapvptrp qrrarsaara qaettsligr avqeeaersg
      241 gdeeaalkal vkraipdvmh lfnetratar ydytaypalp dilkkpskkd pdqiwearpr
      301 fhhpgyslka pgdirvtald vnaaylsalk cwlpigkldh stgadgvepk rsgvhlitpa
      361 pwthphlpdp igdrdepgal wvtnatlrll qrlsgpkhgl teapvihesw tsgatenfld
      421 alrktlgaar eaaiaeddfl tleyvkamys kfistmgesi hnremvrpdw mhiihsqaya
      481 nlwgkaykah qagldvvamt gtdelhvtgd wrqvfpegrg vaqmkikyge grasgeytig
      541 tvtr
//
LOCUS       WP_457656052             147 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457656052
VERSION     WP_457656052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>147
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          2..>147
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mtsrlllvrh getewhaenr yagvtdvalt prgtaqaagl gswaarngvd aiacsplsra
       61 rrtaepaaaa lglavdvqeg lrevdfgwge grtvqemaee dpeavrrfre dadsgafpgs
      121 epvaraaara tralrdhapp hqgdrvl
//
LOCUS       WP_457656054             373 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457656054
VERSION     WP_457656054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..373
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39746
     Region          34..369
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltstavla vvavlavalf aatvrfwprl arpgaaavsg riglllatql tlfaavglaa
       61 nnaflfygsw adlfgrqqel gvvsdhagng pgprhmtrid sqhpdvpggr vpavggridk
      121 vvvsgrasgi espayvylpp eyfqaayagr kfpavvvltg ypgtaenllk glrypqtahe
      181 rvkagkaqpm ilvmlrptva pprdtecvdv pkgpqtetff akdlpeaiag syrvgkkarn
      241 wgiignstgg ycalkiglhh pdryaasagl sayykaaedp ttgdlfhgrg elrdradlmw
      301 tlenrppsgg sflvttsreg ednlgdtmtf iekvkapakv ssivldsggh nfttwrreip
      361 palewlsarl gen
//
LOCUS       WP_457656055             389 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein [Streptomyces griseus].
ACCESSION   WP_457656055
VERSION     WP_457656055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..389
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41597
     Region          55..344
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 matmdeqeqr rrrltawrgs rrvlarvgad gtlgerlaal aagaasvhdp edwtdvyggg
       61 vvadlerrva gllgmeeaaf fptgtmaqqv alrcwagrtg natvalhpls hpelheggal
      121 gvvsglrtvh psseprlpsa devrefpepf gtlmlelplr dagfvlpswe eltavveaar
      181 erdavvhfdg arlwecgphf grelseiaal adsvyvsfyk sldglsgavl agpstlveea
      241 rvwrhryggq vfqqypaals allglerelp rlpsyvahak vvagalaegf aasgvpwfrv
      301 rpepphthqf qvwlpygtev ldeasvrqae etgvtlfrrw fagapgsglp pgvsvtevtv
      361 ggaglewsae dvrgavagfl gylgqgalp
//
LOCUS       WP_457656061             436 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656061
VERSION     WP_457656061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..436
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46418
     Region          16..146
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          63..88
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          124..146
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mdglvrdlgc pdrcvaaaev lasggevaae aivrgltdel spvqwldavp vlqhigdaaf
       61 dclvqgllda staeakdrag laftrlgagf ldqyvtamsh tsafvrcqav vgirlcdgag
      121 vstvpallsl lgdpdpevar qaqdtlvirg keieaslvpl lqqirragpg rqraralavl
      181 aaldgetvlp aqdvaalerl irvklpddrl aasgacwnhw iavpsgdqag iisilgltdp
      241 rpvtfalgnd ivdsdghdte pgnhgrftrv fvtpeldgwt fvlgawcdpc naersedilr
      301 lctllssryg radayyygaq gdgsawlvte hgkvlrryse tgegedhllt lgdpltfeqt
      361 rreelglqpv wdaaleseah adewqwaafe lapqiaqdlg tsplridset tsrgvgvial
      421 tpygvahgvp agtyci
//
LOCUS       WP_457656074              87 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656074
VERSION     WP_457656074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..87
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9637
     Region          13..72
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mtifppdpnl talrlelarl rgergwsyde larrtglarr tlieieqgrt igsltswhai
       61 ahaldvpvdh lfarlceghe ppaepts
//
LOCUS       WP_457656076             189 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457656076
VERSION     WP_457656076.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..189
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21073
     Region          28..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 medaaelrvs dpldrfspvd lqgrdlaedl hhaefpglvr flllhgasws eaqdaaqdaf
       61 tqmcrpgtsi rypkawlrtv awrswlrqqv reepceevpd rptahwdspa havelgveer
      121 rviemllslp skqraalawt ldgfttqesa aamgispeaa rqnlsrarat lktrlglegs
      181 gykaaeedr
//
LOCUS       WP_457656078            1151 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase III subunit alpha [Streptomyces griseus].
ACCESSION   WP_457656078
VERSION     WP_457656078.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Kelman,Z. and O'Donnell,M.
  TITLE     DNA polymerase III holoenzyme: structure and function of a
            chromosomal replicating machine
  JOURNAL   Annu Rev Biochem 64, 171-200 (1995)
   PUBMED   7574479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1151
                     /product="DNA polymerase III subunit alpha"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=123733
     Region          7..1074
                     /region_name="DnaE"
                     /note="DNA polymerase III, alpha subunit [Replication,
                     recombination and repair]; COG0587"
                     /db_xref="CDD:440352"
ORIGIN      
        1 mrgsvphlhv ssgfsaryga shphdlvara sergigalal tdrdmvtgtv rfakaataag
       61 vkplfgvdlg iaphapsaak vrrrtpvrgg ahvaeaafra tflardaagw arlcrmvsav
      121 haeafaadap paaswevlgr yageglmvll gpvseplral aggrpdiaeq llapwreavg
      181 gglrleivcw glsgtgpgsv rlaahtlala drlgitavlt navryadrsq hrvadvldaa
      241 rllrpvdrrr ldcgerwvkd gatmseiaer vaaaagsdra ravrliadta avaeacevdp
      301 vrdlglgvph fpepsvvgae agpggamrll rqrcesgmaa rgldrdrrsm dqldyelgvi
      361 grlhyepyfl avaqvvadvr dmgirvaarg sgagsmvnhs lfvatanple hhllferfls
      421 errsslpdid idvesarrle vydrimdrfg rervavtgmp etyrarhalr dtglalgiap
      481 aavdriaksf phiracdirs alselpelrd laaeagrygp lwelaeslda lprgiamhpc
      541 gvilsntsll drlpiqptpg geypmlqadk edvedlgllk ldvlgvrmqs amahavteir
      601 rttgraidld npdhvplddr fafaliqasd tvgmfqlesp gqqdlvgrlq prgpqdviad
      661 islfrpgpvq ggmpalyiaa rhgaapayph pdlepvlrdt ygvtiwheqi igilavmtgc
      721 dralgevarr alsdkerlpk veawfrrqag argyspavld evwdvvasfg aygfcrahav
      781 afavpalqsa wlkahhpaal yagllehdpg mwparvivad arrhdvpvlp vdinaskaqy
      841 avertgsgwg vrislstvhg isedevariv egrpytslqd fyarahpklp tverlisiga
      901 ldqlkgeasr rdlmlqatel hrqartrpga gqlpltttpq aagssglrem tarerldael
      961 gvlkidvsrh lmedhhrllr eigatdakhl ramhpgqrvl vagvrastqt ppiasgkrii
     1021 fvtledgsgl vdlaffedsh ercahtvfhh glllvrgtve argprrtvvg emawdldela
     1081 aarathgpqa vldllgqaps ptpaqpapap grtipdgtag arlhpwsdlq pagtrsadlt
     1141 rfghkspgsa g
//
LOCUS       WP_457656085             247 aa            linear   BCT 27-JAN-2026
DEFINITION  ComF family protein [Streptomyces griseus].
ACCESSION   WP_457656085
VERSION     WP_457656085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..247
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=25422
     Region          1..213
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mrnvwhelsg lllpvvcagc grprtelcpa cavalhggpa rrvrpsprpp glpavyaaap
       61 yenavravll ahkergalgl agalgralag svragtgrpg gagplllvpv psarsstaar
      121 ghdpvrriaa aaardlrrrg lparalpllr qrravadqsg lgarqrranl agaleltaeg
      181 grlvrhglfr hgrvilvddl lttgstlaea aravgearga grqpsvhgrc raavvaasps
      241 afeinrn
//
LOCUS       WP_457656079             339 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Streptomyces griseus].
ACCESSION   WP_457656079
VERSION     WP_457656079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..339
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=36457
     Region          <25..289
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mtakpapprr srailrihfh paerneelyg qllavvdgis srveplpgdw sayadltgal
       61 tywgrdaegl vavlrlrlla lhgvqcsaga gptrsiaama adatppgaat vvrddpyevs
      121 aflrtrpasa lpgigpktar tlarygitti gdiadtqlpt lqrilgttaa rqahdrahgi
      181 derpvvpgaa prtvstshrf erdeldpdrh hravlglvqe lgrklrtsae iaqaltltvt
      241 yadrtqttrt rtlteptaht palattalel ltglglqrar vralavraer lrpaehtvrq
      301 laldghddkl hrletaldka anrygpgitg tastfswtt
//
LOCUS       WP_457656077             535 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine protein kinase, partial [Streptomyces griseus].
ACCESSION   WP_457656077
VERSION     WP_457656077.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>535
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          36..508
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 malphvrila mmvssrkrgc rvselswgvp paegdpvrvg pytvlrvlge ggmgrvflar
       61 glgmrlfavk tirphlahda dfrkrfvlea qaaqrvngvf tapvvgvsge deqvpwlata
      121 fvpapaleev varcgvlper glwwlaagva ealvaihgqg lvhrdlkpgn vlvaedgprv
      181 idfgiakalh gstastsvgh vvgtagfmap ehlrgaatpa sdvfalgall vhaatggppf
      241 sgtdifavmt atffdapamd gvpggvaelv rdcldkdper rprpeqvler fqryagteat
      301 ghavrrwlpt avcdlvetra rpslvfgdaa eqtamipppp ptrlvtqaqt ptptqarepa
      361 aggtasgteg sdgddrstlv alrdratslg esgepgeard lfallirrcs evlgadhpdt
      421 laarvhharw tgdagdpaqa rdlwatlvtd rvrvlgadhp dtlrarhsha nwtgktgdaa
      481 qardlfaalv tdrarvlgpd hphtlaarvh harwtgdagd paqardlwat lvtdr
//
LOCUS       WP_457656087             206 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656087
VERSION     WP_457656087.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21648
     Region          30..76
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          88..197
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mlramtterg trrrapagaa vlredvtdai raavfeelaa vgfarmsieg iarragvgkt
       61 avyrrwkskl alvldlvaav aaqgmpapat gslygdvrav lelaayalrh pvasqaipdl
      121 lveaarnpei seaikaalld qqqgvaavvv reavargelp egsdpdrald livgplywrl
      181 vvvrgelpkg ylddlaasav aalkha
//
LOCUS       WP_457656086             263 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656086
VERSION     WP_457656086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..263
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27891
     Region          16..263
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 madtenvsgd rrvptvavdd vhitytvnga rtgrgsatsa lsrlttrrat pgarkvhavk
       61 gvsfaaytge aigligsngs gkstllkava gllpptrgrv htqgqpsllg vnaalmgdlt
      121 gernvvlggl amgmtreqir erydaivdfs ginekgdfit lpmrtyssgm garlrfsiaa
      181 akshdvllid ealstgdakf qrrskdrike lraeagtvfl vshsnksitd tcdralwlea
      241 gtlrmdgpak dvvaayeaft nrk
//
LOCUS       WP_457656089            1241 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces griseus].
ACCESSION   WP_457656089
VERSION     WP_457656089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1241
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1241
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=132696
     Region          3..220
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          859..1236
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mkspllsvvv pvhnveayla dclrsvaeqt laaievvmvd dgstdgsari aaefaardsr
       61 frlvrqqnag lsaarntgvr httptvpyla fadsddivvh dayermtasl estgsdlvtg
      121 nvwrltgqgr qqawqyrwlt gprsrthitr dprlladrva wnkvfrrsfw dahgfafpeg
      181 rlyedtpvmi pahylagavd vlaehvyywr vregsitrrr tdvtgvrdri aaceqvsafl
      241 ggrdaeqrra ydasclrddf gyfldglpmg geayraafle gagafvdrag pkaleglpve
      301 lrikwqlvre rrlaellevl aferangagt faveglpgrr raaypgvhga sarlagpdip
      361 avarlsearw gadgklrlrg yaylrnlpaa sgrqrltvgm vraergrqvr pvpvrsvpap
      421 eatvnsgqel hdydhagfem tldpdrlpat agggwlvglv lagpgtvrrv avrapdagad
      481 qplthdlgdg rravldfrag rlrltvsrlr alaeghrtve aagsalditg rhiggsrpta
      541 lvltrdggee rsyaveyaeg gargengegg egredgargg sfrvrvplae laaappaphr
      601 apreveaang pesgdrwrvr llladdsrvp lpaapdlppp ayadpagdlv ldlaglpyad
      661 evectpeggv rirgayagta tappsayggr lvlrhetlqe tvpvagaavd asgaeaerpa
      721 gaeaeaasgp rtdaatraga gnhtasgtea gagagnhtas gtgadaavaa adgsaprpla
      781 atapgrfsal vvpplpegrw elrldgrpvr vlgsvaarlp raggvegalr lerrhgdrls
      841 vvagpespav gigrsaygrr llraahhgdr rttlplrdtv lyaggdspra vhaelvrrgt
      901 eaehlwvtgt tpgrithvpp garavpvhsp awyealarsr rivtdeqlpg wferrpgqtv
      961 vqtwhgtplg rfgggladtl yadhqylatl pqrsaqwsvl vspsrfatpw lrrslvyege
     1021 vleagspand vlfppvrdka aeevrrglgi pedhrvvlya ptyrdhlahp paasadrtap
     1081 gpyrwdpald pyalaralgp ghtvlvrrhp rvtgdvpagp gvldvsghpg aaglllvadv
     1141 lvtdyaglmf dfaltsrpml fhtydlehyr dtvrgfcldf etrapgpllv ttdevaqalr
     1201 dtgslaarha dayesfrrdy cdlddggaaa rvadrlladg p
//
LOCUS       WP_457656091             743 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces griseus].
ACCESSION   WP_457656091
VERSION     WP_457656091.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..743
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=82716
     Region          1..213
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          355..710
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mprftvivpa frvqaylhac ldsvlsqsfk dyeiivvddc spdacgpiad eyarrdprvt
       61 alhlprnigl gparnagmar aggdylvfld gddtllpdal rtiadridat gepdvlmydy
      121 artywtgrsv rnvlaahlde ggparfrltd rpellqllmv vwnkayrrtf veaegfafpp
      181 gyyedtpwty pvlmaadsia vldavcvsyr qrrrgnilst tsekhfdvfd qydrvfafid
      241 srpelalwrp vmfrrmldhf salfasrdrl pphsrtaffr ratascrryh tpgapvprra
      301 llrhglmhlg arrtyralsv aqrlggrlrr aaeavrravr gaalrahyri qlllplrprd
      361 avftvrggrg yggspaaiea kvrelvpgar tywicravda htvptgsrhl apgtfahgta
      421 larstylvnd ssfdrglvkr rgqvlvqthe gtplrsvgtd lldrpaaarg tdfeqllrsv
      481 dtwdfslsan phstlvrera ypsayttley gsprndvyqr tgpaevarlr etlgipagst
      541 allyapthrd yrrvqrpald lerlvrilgp qfvilarapr ppgpggvrra phpriidvsa
      601 hrsvetlala sdalitdyas lmfdyvnldr pvvlhlddie ayeaargtyf ditafppgiv
      661 arsqdelfdi fatdhwrgsr saqlraafrd rfcpyddgya aervvrrvfl getdglplpv
      721 ppaarrtpaa lpaqdgagat vgg
//
LOCUS       WP_457656094             519 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457656094
VERSION     WP_457656094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..519
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56185
     Region          46..456
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(154,156..157,290..294,314,317..318,321,336,340,395)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mhrrfivpsa laatlllaip aaaapgtvga pgigdpyypa sgnggydvsh ydlrlkyqpv
       61 tdllegtati latttqelsr fnldfgldvs evrvngrkar fatsgdhele vtpadplakg
      121 kdvsvvvrya gkpselking wtawartpdg gvaaqepesa vwwypsndhp ldkatydvsv
      181 svpdgtqais ngvlqsqssk lgwtrfnwrs dkpqatyltt laigrfditt drtadglpvl
      241 nayskdlgan agaarasier ttevaewlte vfgpypfnal ggyvpnvtsg faletqtrpf
      301 ysprqfanga nvsvvvhela hqwygdsvsv dgwkdiwine gfarysqwlw sekegegtaq
      361 eladyayaqh paddpfwqvk pgdpgpdnqf diavydrgal alqalrnevg ddtffellkg
      421 wpaehaygna nvgdfvryae rvsgkplaal fdtwlyrpar paapaaadag laeaalsars
      481 aarverpasw kkiaatntvh dhgdhtasah rsegghehr
//
LOCUS       WP_457656095             158 aa            linear   BCT 27-JAN-2026
DEFINITION  macro domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656095
VERSION     WP_457656095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Rack,J.G., Perina,D. and Ahel,I.
  TITLE     Macrodomains: Structure, Function, Evolution, and Catalytic
            Activities
  JOURNAL   Annu Rev Biochem 85, 431-454 (2016)
   PUBMED   26844395
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Li,X., Wu,Z. and Han,W.
  TITLE     The macrodomain family: Rethinking an ancient domain from
            evolutionary perspectives
  JOURNAL   Chin Sci Bull 58 (9), 953-960 (2013)
   PUBMED   32214744
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Han,W., Li,X. and Fu,X.
  TITLE     The macro domain protein family: structure, functions, and their
            potential therapeutic implications
  JOURNAL   Mutat Res 727 (3), 86-103 (2011)
   PUBMED   21421074
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Karras,G.I., Kustatscher,G., Buhecha,H.R., Allen,M.D., Pugieux,C.,
            Sait,F., Bycroft,M. and Ladurner,A.G.
  TITLE     The macro domain is an ADP-ribose binding module
  JOURNAL   EMBO J 24 (11), 1911-1920 (2005)
   PUBMED   15902274
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..158
                     /product="macro domain-containing protein"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /GO_function="GO:0072570 - ADP-D-ribose binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16978
     Region          3..146
                     /region_name="Macro_Poa1p-like"
                     /note="macrodomain, Poa1p-like family; cd02901"
                     /db_xref="CDD:394873"
     Site            order(9..12,24..27,31..37,39,84..85,123..130)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394873"
ORIGIN      
        1 mseityvrgd atapqgkgvk livhvcndlg gwgkgfvlal srrwpepeaa yrrwhreraa
       61 ndfalgaaqf vrvgpylwva nmigqrgmrt gskgvpvrye aidaalgava vragelgasv
      121 hmprigcgla ggtwsrvepl ierrlisagl pvtvydhd
//
LOCUS       WP_457656096             267 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656096
VERSION     WP_457656096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 267)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..267
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28885
     Region          10..79
                     /region_name="HTH_MERR"
                     /note="helix_turn_helix, mercury resistance; smart00422"
                     /db_xref="CDD:197716"
     Site            order(11..13,27,44..46)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 matgtdeptl tvdelaarag vtvrtvrfys trgllpppvi gprrvghygp dhlsrlalie
       61 elqqqgmtla aieryleqlp pdlsahdlai hralvaswap dktedfsrae lerrtgrals
      121 epdverlaam gvlvrpqeag gayrvdlgll rlgvelldvp iahetilaar tvllehtrsa
      181 aqemtrlfrd evwnpyrere gdpehvaamk slsadmqpiv vqalvtafqr slkeelraav
      241 tppragtrgp gggggrglgv cgapkpp
//
LOCUS       WP_457656098             396 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457656098
VERSION     WP_457656098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42165
     Region          7..395
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mnrqndttrp ldvvlfgatg fvgtltaeyl aahapaglrw alagrsrtkl aalrerltai
       61 apgcaelpll dadaddaeal aelaastrvm attvgpyiry geklvaacae agtdyadltg
      121 eaefidrtyl ehdararetg arivhacgfd svphdlgayf tvkqlpedvp lavdgfvrtn
      181 avfsggtfas altamgrgpq mlaaarerrl heprlvgrrv rtpagsphfn gsvgtwalpl
      241 ptvdptivgr saramerygp dfryrhfasv ktlpmtlgap vaigalvaaa qvegvrewlm
      301 gryepgqgpd eerrerswft irfvgegggr rvftevsggd pgygetakil aesavslald
      361 elpetsgqvt tavamgdall drltaaglrf rvaavr
//
LOCUS       WP_457656100             739 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457656100
VERSION     WP_457656100.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 739)
  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 739)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..739
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79322
     Region          64..698
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mkqsgaaggt lvrgaaggpv ptggaarell araerllesa ravpadraaa gdavrtvldp
       61 lldalvdqel ahipvgrlkd vtegrlrlga leqagfgtvg qvhgtgryel rqlpgvgaht
      121 adqalaaagq iahavrdtvs vridvdapdd tstalvialh rlveagaear ravdaarrlg
      181 erlgpavata apagsrlrml fsgrekrarv realdavrsa vaeaverelp vlfaqasadl
      241 lrspaspaea wvdfelrsae yysllaelsg sgpdrdaaeg flpagiadrv ralrlddtrl
      301 rvslrgyqaf garfaltqkr viigdemglg ktvqaiaala hlaahgeshf lvvcpasvli
      361 nwtreirars tlravpvhga erteafadwr egggvavttf dalhllpega aaevrpgmlv
      421 vdeahfvknp earrsravag waervervlf ltgtpmenrv eefrslvrql rpelapsvss
      481 thgaagsraf rravapaylr rnqadvlael palvqvdewe efgaedraay reavasgrfm
      541 rmrraayaap gtsaklerlr elvdeardng lkvvvfsyfr evlatvgdal gpdafgplsg
      601 svpparrqel vdafsavdgh avllsqiqag gtglnmqaas vvvlcepqik ptlehqavar
      661 ahrmgqvrtv qvhrllatds vdqrlvella rkdrlfdaya rrsdlaettp davdvsdael
      721 arriveeeqr rlvddsrrp
//
LOCUS       WP_457656104             481 aa            linear   BCT 27-JAN-2026
DEFINITION  SLC13 family permease [Streptomyces griseus].
ACCESSION   WP_457656104
VERSION     WP_457656104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..481
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49109
     Region          90..466
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mplplrqtvg lcavlglcal lavpgaapgl saegrlslav fvlataawia apvddayial
       61 gaglaltvtg vissetlfat lgdetvwlli cafvlaaavt rtglagraav flvggartvr
      121 qlthlttagl vvtafavpat sgraalalpv flalaaalre rtrlvvmlal lfptvillsa
      181 vatligagah litvgvlweq tgeqlsfvqw lvvglplavv sshlaaelvl ltttrradrr
      241 gpvtitaaqi qehsetaveg pftpaesrcl lllatvvllw cseplhgvsp avvaligalv
      301 atspalgtvr fkdglrtvpw plllfmaatm amgvalsdsg aadwlvgwip lgastppwlf
      361 ltgmvvvsta ahlalqsrsa rssvlvplvv aaavgagvnp vtaalastaa agfchtlpss
      421 akpvalfadv pgtptytprd llrlsaflap ltaalvlafa lvvwpllgvp vlldpnerpq
      481 p
//
LOCUS       WP_457656105             394 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457656105
VERSION     WP_457656105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ornston,M.K. and Ornston,L.N.
  TITLE     Two forms of D-glycerate kinase in Escherichia coli
  JOURNAL   J Bacteriol 97 (3), 1227-1233 (1969)
   PUBMED   4887503
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Doughty,C.C., Hayashi,J.A. and Guenther,H.L.
  TITLE     Purification and properties of D-glycerate 3-kinase from
            Escherichia coli
  JOURNAL   J Biol Chem 241 (3), 568-572 (1966)
   PUBMED   5325263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..394
                     /product="glycerate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0031388 - organic acid phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39522
     Region          7..383
                     /region_name="Gly_kinase"
                     /note="Glycerate kinase family; pfam02595"
                     /db_xref="CDD:460609"
ORIGIN      
        1 mthriaiaps gfkeslsaar vaeaiavgvr rvvpdadldl iplvdggegt aealalaggg
       61 rlvpctatgp vgdpvashfa llggpgplta vvemaavagl alvppdlrhp gatttygvge
      121 liraaldaga rrilvgcgds gtsdggagal qalgarlidr hgrelrrggg alhelehida
      181 sgldprlaea dllvacnpyn vlcgkrgvar vfgpqkgatp aevellsagl erlaavltrd
      241 lapafataal dlrtapgtga sgglgaglaa vgarllpryd vlldgldlda rlaradfvit
      301 aegaldhqtv rgkipaevar raraagvpvl vlagtigpga qdvravgvda ysailpapmt
      361 lveaigrsde fladateram rimalgtrla plaa
//
LOCUS       WP_457656106             274 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656106
VERSION     WP_457656106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30494
     Region          18..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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 maniqtldpd asplayygae lrrhreaqgl tqpqlgsaif ctgslvgqve ttkkvptrdf
       61 servdaalgt dgvfsrlvgl vlrsqlptwf qpyadmeaka ayistyqaql vygllqtedy
      121 aravlatgmp ddlegllaar merqrilera kpplawaild eavlyrpigg hevmraqlqr
      181 lldyashrwm riqvlpfeag ehaslagsfn qlrfdddpei vytedvisgh mtanpetvre
      241 aslryahlqa talsveesva risrvmeery garp
//
LOCUS       WP_457656112             877 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656112
VERSION     WP_457656112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..877
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=94186
     Region          <14..848
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mgndvkstap afpgretilh eirqalgraa sggggclvve gaagtgksel lrlagmhgea
       61 sgfglvagta vpldtgapfs tlrrvlrenl sardyvlltd rrtfdplapv driveflrrs
      121 trdrpllval ddahlvddlt adalrnlida svtlpvlwil argtsrtpgh aqetidwlir
      181 egaahhrles lspeavaeis aeligarpdd dvlalvarvn gnpfllnell vtslsdgrmc
      241 vqdgvavlld aepapafrqa vvhhlrglsh eclrildava vlgqrfsihe aagllgrnpv
      301 ellpligeli aasvledegp tlafrhplvr etlydrlsep trtalhreaa atlwregrsa
      361 ptflehlmlg rrgegdglvp aavraearfa pepeqfvpta aplvpeagqf lpeagpfvpe
      421 tgqflpeagp fvpeagrlvl sgaaggtaap happpapyae lmhrttlrys aaqvqglhaq
      481 mvaharaalr iardhgdrts rahhrlwlav altasdefdq ageilaercd psdhvalpwv
      541 rpmwhyhraq lklaagqlee adedaveavr icerlaapal avgplalrir vavhrhelte
      601 anrhvvhasr lsaaasgear eelswvtall hsaeenrqsa hdtlspvysg vpkrpllltr
      661 ephagaclvr tamsagdcer atavagaarl vatrnptvas avaaaahaeg vlrndvdrlr
      721 aavsayrsgp rplslaaate dlalaeneag grstaiglld ealaryqnhg argdalrvrk
      781 tlrslavrrr trgrdrdldp vegprarwdq ltpselrvvr lvaqgltnre vaeklflsph
      841 tvdshlrhsf tklgvtsrve ltrqvlthee vppagpa
//
LOCUS       WP_457656120             570 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Streptomyces griseus].
ACCESSION   WP_457656120
VERSION     WP_457656120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..570
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=56855
     Region          156..558
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mtgpdgprra sgsdggdfrp agggsdlare eeeraveqal alvggttlrp grgrdipgtp
       61 gtpgtprasg asggdlssgp tgdgpdqsas tdsastdsap vgsspggngp saggpsggar
      121 ataqasgsdq rhrpgrssse asapnaepat pkapplswdr aravatragr agppatirlp
      181 ldralghvla eplgaltdlp sfdtsamdgw avagpgpway eagagllagr gpdtplpdgt
      241 avriatgarv ppdttavirs ehahpdeakg llharrsvvt gqdirprgqe crsgeqlvpa
      301 gtvvtpavlg laaaagydal pavprprvdi lvlgdellaa glphdglird algpmlgpwl
      361 ralgaevagp vrlgddagal rdalassdad livttggtas gpvdhvhpvl dalgaellvd
      421 gvavrpghpm llarlpapgq mkgqaegpyl vglpgnplaa vsglltlaep llagvagrpa
      481 qdayralvha evhghphdtr lvpvvhragr aggrdhvapl ryngpamlrg iaaadglavv
      541 ppggvrsgte veildlpwap atpwtegcft
//
LOCUS       WP_457656121             207 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656121
VERSION     WP_457656121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..207
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23032
     Region          1..83
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          90..172
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 msirhgllal lergprygsr lrtefesrtg stwplnvgqv yttlsrlerd gmivqdgtdd
       61 aghdlyaitd dgraelrtwf etpvdrtspp rdelaiklam avgapgvdir dviqsqrhht
      121 lqamqdytrl kaqaladipa nrdevawllv veqlifqaea earwldhces rlvrlaeaaa
      181 vepteepgpa atrgparsla srirsrr
//
LOCUS       WP_457656124             483 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656124
VERSION     WP_457656124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..483
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49473
     Region          12..482
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mttmtetsar frefkmpdvg eglteaeilk wfvqpgdtvt dgqvvcevet akaavelpip
       61 fdgvvhelrf pegttvdvgq viiaidvapg sgdapapaaa apaqepaaep eaeaepkgrt
      121 pvlvgygvae sstkrrprkg asaapeaaav aaavqaelng haapaapaap aaavpaqggr
      181 plakppvrkl akdlgidlat vvptgkdgii tredvhaaaa paaapaaapa papaavapav
      241 aeapavvsds aretripvkg vrkaiaqamv gsaftaphvt efitvdvtrt mklvaelked
      301 kdmagvrvnp llviakallv aikrnpevna awdeanqeiv qkhyvnlgia aatprglivp
      361 nikdahdrtl pqlaaalgel vttardgkts paamaggtvt itnvgvfgvd tgtpilnsge
      421 sailavgaik lqpwvhkgkv kprqvttlal sfdhrlvdge lgskvladva aileqpkrli
      481 twa
//
LOCUS       WP_457656125             401 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457656125
VERSION     WP_457656125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42058
     Region          1..399
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdftfteeqq aaveaaravf sdvapdraps paltpgavae didrrlwhel artdllgltl
       61 spdhggagld pialclvlre sakvlarvpl lescavamai erfgdrtlaa ellpragrge
      121 liltvgangr sghdpaelav sarpygvrdg eedgqtgseg gaetdgpagg sgwvldgvqs
      181 avpwaqvadr iavpahtagg rpvlalvprt regvtladqv stsgerlaev rldgvrvtar
      241 elidapgcwe wlrsllttgt calalglger vlamtaeytg rreqfgfpva tfqavavqaa
      301 dryidlrame atlwqaawri stdaggplpa agdvavakiw asdgvrrvvq taqhlhggfg
      361 adtdyplhrf hawakqiels lgpaaaheea lgdllaahpl g
//
LOCUS       WP_457656134             159 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Streptomyces griseus].
ACCESSION   WP_457656134
VERSION     WP_457656134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..159
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16852
     Region          1..151
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mathdseltg yaheairlsg ehvaqggipf sgvvvaggri lgtgfnrvre dndptahaev
       61 valreatakh girsvagatl iasgepcalc ylaaryagig hivhaadrrt aarygfdyts
      121 tytlfaedpa dwtikvtalq lpeaeqpfqd fltlsraar
//
LOCUS       WP_457656131             184 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457656131
VERSION     WP_457656131.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  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 184)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..184
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20355
     Region          6..179
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 msteefeela rrapelvrle fiqgqvrvkp vpdgnhgaiv mwllrqcmrr rpelslfpdq
       61 glaietyrkg rarpdgvlap dehfagagew aapngvlmtv evtsrdadtn rrdrvavekp
      121 dgyaavgipv yllvdreacs vtvftepekg tyrsattrpf gavvelpepv gfaldteklk
      181 eyad
//
LOCUS       WP_457656135             391 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces griseus].
ACCESSION   WP_457656135
VERSION     WP_457656135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="trypsin-like serine 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=40654
     Region          148..>335
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrsirpllaa tglvaaltlt atacgpdeda asaakpsasd gvadkgpggg lagdlgdale
       61 khgvdpekwk dggwknwdkd swlrkaedfv npvieglwep drmasadepa ktmaagdlsa
      121 gqdvsdpepa pvraepektp yhrhaapvgk vffdspkgsm vcsgtvvkdp knpgrsnlvw
      181 taghcvhaga gggwyrnivf vpsyndqgkn aaqlrtaqpq eiapygtywa dwaassgewi
      241 sgggptggag apydyailhv kaekgtksle etvgnalpvs fdapevqqis gmgawgypag
      301 ppydgllmhq cvdrpgrlsi apgtptmyri gctmtggssg ggwfvagpdg ksmlvsntsi
      361 gpvtsgwlag pqlgedarrt ftmmsdkfag r
//
LOCUS       WP_457656136             481 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457656136
VERSION     WP_457656136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..481
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52353
     Region          46..462
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(153,155..156,286..290,315,318..319,322,337,341,401)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mphltrrlra allatasatl vaatlpapep lgigdrlfpe lgnpgydvla ydialtyhgs
       61 ntepldavts ikarttapld rinldfargt vrgvevngqs vdfgsknedl vlqaphrlpa
      121 gvplnitvrh tsdpsgsged ggwvrtadgl amanqadaah rvfpsndhps dkayftfrit
      181 apekltavag glpvgktrhg atttwtyrte hpmatelaqv sigssavthr tgphglpvrd
      241 vvpaadrkkl epwlkktpah ltwmeeqvgr ypfetygvlv adspigfale tqtlslfgks
      301 fftepgypqw yvesvmihel ahqwfgdsvs paswsdlwln eghaswyear yaeengggtl
      361 errmrqayel sdgwradggp pahpdgpapg qklslfrpvm ydgsalvlya lrqeigeaaf
      421 drlertwvrv hrdstattad ftrlasgiag rdltaffdgw lygkktppmp ghpdwssakp
      481 a
//
LOCUS       WP_457656137             721 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Streptomyces griseus].
ACCESSION   WP_457656137
VERSION     WP_457656137.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 721)
  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
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..721
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=77448
     Region          34..716
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msaeaadpga plrrrsrpri dlrrlgrval rgpvsrdrlp daighvaeah rahhpdadlt
       61 ilhrayvlae sshrgqmrks gepyithpla vtlilaelga etttltasll hdtvedtevt
      121 ldqvreqfgd evcylvdgvt klekvdygaa aepetfrkml vatgndvrvm sikladrlhn
      181 mrtlgvmrpe kqariakvtr dvliplaerl gvqalktele dlvfailhpe eyehtralia
      241 aaagpdapld tiadnvrhtl rdagisaevl irprhfvsvh rvrrkrgelr gtdfgrllvl
      301 vgedadcyav lgelhtcftp visefkdfia apkfnlyqsl htavvgpega vaevlirthr
      361 mhkvaeagvv algnpyaqdh aaaqhaepsd eradptrpgw lsrlldwqes atdpdtfwtt
      421 lrddlaqdre itvfrtdggt lglpagascv daayaqygdr ahtsigarvn grlatlstvl
      481 sdgdtvqlll aqdtasgpsp dwldhvrtpa ariaitgwlt dhpdeakpap smmtsadaga
      541 pgpaglaper daqvtapart rsgpratgvv vegaggpvrl agcctpvppd eltgfvvrgg
      601 avtvhrrecp avaamqeigr dpvgarwada egresdagcr vtlvaesfgr prlladltea
      661 iataeaaivs atveppseqr vrhtytlqlp daaglpalmr amrevagvyd vsraqhpapa
      721 g
//
LOCUS       WP_457656140             230 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces griseus].
ACCESSION   WP_457656140
VERSION     WP_457656140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  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 230)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..230
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25072
     Region          1..217
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrlllveddd hvtaalsavl arhgfqvvha rngeealral lpagkepfgv illdlglpdq
       61 dgyevcgkir krtatpvimv taradvrsri hglnlgaddy vtkpydtgel larihavarr
      121 ttsgedtapt pvaslrlgpv aielptrrvs vdgeevqltr kefdllalla qrpgvvfrre
      181 qiisevwrts wegtgrtlev hvaslrsklr lpalietvrg vgyrlvapsa
//
LOCUS       WP_457656143             311 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656143
VERSION     WP_457656143.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32856
     Region          41..271
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(44,47..49,52,60,62,92,111..114,205,207,209..210,212,
                     222..223,226,241..242,245)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(44,48,52,60,62,92,111..114,205,209..210,212,
                     222..223)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(47..49,205,207,210,223,226,241..242,245)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 mtdaeteien gteaeagaei taelvrdllr eqhpdlagla vrevaggwgn qqwrigdela
       61 vrmprterap dlqrkerrwl pvlaprlplp vpnpvrtgep salfpkpwtv mtwvpgepld
      121 hasisrgdha aealagflra lhveapagap issdrgahps gctdgfdgff eavapgdiad
      181 airavwadav aapawegppv wvhgdlhpan vvvsdgtlsg vidfgdlfag dpawdlaaaw
      241 vilpagtasr ffdayahade gtirrargla vlkglvlmlv grngdrglpg gkpawgpagr
      301 aaldraleta r
//
LOCUS       WP_457656149             602 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding SpoIIE family protein phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457656149
VERSION     WP_457656149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  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 602)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18599219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..602
                     /product="ATP-binding SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=63531
     Region          31..459
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          471..583
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mehrpggpgt plravlarlp vprtlrravg aatamsgtrr lewlnaagdh igttldldrt
       61 aqeladyavp kladaaavdl lesilrggeg ersgsaeapl tramavahid elgnlepdpv
      121 gelttshpsk vahqclitrr palvrriaph qyeyiaptsh aalvlrragv hsylalplvs
      181 rgvllglvdf lrsgdrppfs hadvalacel aakaavfvdn arlygreraa vvtlqrallp
      241 raapstpglq vvsgyrpavd pggvggdwfd vvalpsgrsa lvvgdvmghg laaaatmgrl
      301 rsvartllgl dispervlar ldlaardlee dqvatclcav ydhagrtyrl asaghppplt
      361 idaagraafl dvppgaplga gvipydevta evpeggrivm ytdgliknrh edvdvllerl
      421 raavdgppaa ladsceaiwt gtdscgggrf ddavvlmaes lsqpdaevvv wslpsdgsaa
      481 gaarrlvraq lerwsltelm dvtelvvsel vgnalrhggg psglrllrhd rlcvevsdig
      541 pdlpriqhap lsaeggrglq linmlcrrwg scrtpdgkvv waeqdlpstt anphhappqp
      601 gr
//
LOCUS       WP_457656150             382 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656150
VERSION     WP_457656150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..382
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40060
     Region          92..382
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtgdyqelvd eisalldapa tlenrdfglv afgahdsddd tamdpvrtrs iltrrstpav
       61 rawfegfgit ratgpvripa apeagvfrdr iclpvrhrgv vlgyvwllda dpgptdeqla
      121 aamevaarig allsdevrag adlsrefgav ltagpgrqhd tavaalgeal grdaeglhtv
      181 vcvtpwaddt psvrgvasaa alatvtapga agprslaalv rlrspdrldp alsaadrlrt
      241 gagpaatggi aaprrgleel tvswreataa araaraetrf gpvarwsaig pyrlltalpg
      301 tgndpgdpav aslltplhre lahtaevfld cagqagrtaa algihrqtly yrlsriqqit
      361 gldlndgedr lllhmavkra rl
//
LOCUS       WP_457656151             347 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Streptomyces griseus].
ACCESSION   WP_457656151
VERSION     WP_457656151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
REFERENCE   2  (residues 1 to 347)
  AUTHORS   McGraw,W.T., Potempa,J., Farley,D. and Travis,J.
  TITLE     Purification, characterization, and sequence analysis of a
            potential virulence factor from Porphyromonas gingivalis,
            peptidylarginine deiminase
  JOURNAL   Infect Immun 67 (7), 3248-3256 (1999)
   PUBMED   10377098
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..347
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0004668 - protein-arginine deiminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37747
     Region          11..342
                     /region_name="AguA"
                     /note="Agmatine/peptidylarginine deiminase [Amino acid
                     transport and metabolism]; COG2957"
                     /db_xref="CDD:442197"
ORIGIN      
        1 mpptpapfrm ppewaphert wmawpgpnpt fasdaelaea rrawaavara vrrfepvtmv
       61 vgpgqeegaa allgpevelv vrplddawmr digptfvtdg rtlaavdwtf ngwgaqgwar
      121 weqdrhiars vaeltgvpah ssplvnegga ihvdgegtvl ltetvqlgee rnpgwskeqv
      181 eveiharlgt ekaiwlprgl tgdygtygtl ghvdivaafa rpgtvlahvq pdpahpdhev
      241 trellavlra atdargrale vvevpaptvl rdedgewvdy syinhylcnd gvvlcafddp
      301 rdeeaaaifr glfpdrtvtl vdartifagg ggihcitqqq pkvranp
//
LOCUS       WP_457656153            1033 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces griseus].
ACCESSION   WP_457656153
VERSION     WP_457656153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 1033)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 1033)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12044314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1033
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=108490
     Region          49..230
                     /region_name="CBM_11"
                     /note="Carbohydrate binding domain (family 11); pfam03425"
                     /db_xref="CDD:427290"
     Region          <269..>302
                     /region_name="Calx-beta"
                     /note="Calx-beta domain; cl02522"
                     /db_xref="CDD:413355"
     Region          372..775
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          744..946
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
ORIGIN      
        1 mtrtphlrpr kgrarpataa faaaavlatl lagsatgpaa aadepapvlv drfegevplg
       61 nnppadaift wggdaddhpq lklaeradap egekvlegsy disayggfsh efavdtppqn
      121 wtahqgirfw wygqntaplp pgsgkkinfe ikdggangga selwttsftd dwegwhlvei
      181 pfadfvyrad yqpvggidqv lglnemwgya ltlpgggpge faldavelyg kadpaltasv
      241 vtdtavrpvk ngataeltls vattgsvpte epvtvayate ggtaeagkdy tpvtgshtfp
      301 agtasgtthk vtvrtakask paeaktiple ltvtgakapr enpqvvidah glpyqnaklp
      361 vqqrvadllg rlspaekagq mtqaernalr tpgdiaaydl gsllsgggsv ptpntaaawa
      421 kmvdsyqlra qatrfqipli ygvdavhghn nvvgatimph nigigagrdp ksaertgavt
      481 akevratgvp wdfapcvcvt rderwgrsye afgedpalve ametviqgmq gspsgkdlhr
      541 ndkvlgsakh fvgdggteyg sattgsyttd qgitkvtree leavhlspfa esvkrgvgtv
      601 mpsyssldil gddrgpvkmh anaemingvl kdrmgfegfv isdwqaidqi pgdypsdvrt
      661 sinagldmim vptayqdftk tlkdevaagr iseariddav ariltqkfrl glfekpyadt
      721 thldkvgsae hravareaaa ksqvllkndg avlplkpdqk vyvagsnadd ignqaggwti
      781 swqgssgktt tgttilegmk kaarspgsvt ysrdasaatd gydvgvvvvg etpyaegigd
      841 vgnghdlelt aadkaavdkv caamkcavli vsgrpqligd rlgdmdalva swlpgsegdg
      901 vadvlygrra ftgqlpvtwp kseaqlpinv gdtaydpqfp ygwglttlkk ppaggeltla
      961 alavaaqvae kaklgktpag kaivdqarll vqqkidgkfg qavakpfaea dhlllkgdlt
     1021 gavaklrtay raa
//
LOCUS       WP_457656154             314 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656154
VERSION     WP_457656154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..314
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31711
     Region          1..311
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,131,135,156..161,180..181,183,197,
                     240..241,256..258)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mravgvcefg gpealrvldl pepqagpgev rvrvhaaavs ptdvmlrtgg havrmpgrrp
       61 pfvpgmdaag vidqigpgag grlavgqrvv alvlftgphr gayaeqvvvp aasvvpapeg
      121 mgfpeastlp mnamtarlal dvldlppggt vavsgaagav ggyavelara dgltviadaa
      181 grdvetvrgf gadhvverga giadrirtlv pegvagavdg saqtaelvpa irdggtlvel
      241 rgwpgpagrg irvcpvmvpe rigdtagldr lcrqaeagvl tprvaqvlpa aeaarahrll
      301 eagglrgrvv ldfs
//
LOCUS       WP_457656155             328 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656155
VERSION     WP_457656155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34084
     Region          24..289
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkqqrydvvi vgggaaglsg altlararrs vlvidagepr napashvhny lgrestppge
       61 llaigrgeaa gygaeivegr vasaerlsgd gdgdgdgerg frvvtedgrs vearrllvtt
      121 glvdelppvp glaerwgrev lhcpychgre vadrpigvla tgplavhqal mwrqwsedvt
      181 lflhtgpeps eeeyeqlaar gvavvdgeva glevaddrft gvrlasgrvv arealvvqar
      241 ftarsavles lglkavaqem ggvvigsyvp adptgatevp gvwaagnvtr lteqvigaaa
      301 aglmaggain gdliaedtrd avaarrrg
//
LOCUS       WP_457656157             205 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656157
VERSION     WP_457656157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..205
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21771
     Region          11..194
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          113..198
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtcmsisntp raatlddaaa isgtlarafq gdpmmewffp ggasrepdlv ryfttiftrq
       61 ygrhgvcert asaaafwvap egqektvpda etvaeleeil gdraplfrda vaaaaeqgpk
      121 ephwylavvg adpaargqgh gaallrsgla kadaaglpvy lesskpdnlp fyehfgftvl
      181 geaqlpgggp alwvmrrepr pvdaa
//
LOCUS       WP_457656163             386 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces griseus].
ACCESSION   WP_457656163
VERSION     WP_457656163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 386)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..386
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41261
     Region          2..360
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mkigivcpys wdvpggvqfh irdlaehlir lghevsvlap addetplpry vvsagravpv
       61 pyngsvarln fgflsaarvr rwlhdgtfdv ihiheptsps lgllacwaaq gpivatfhts
      121 nprsramiaa ypilqpalek isariavsey arrtlvehlg gdavvipngv dvgffaeaep
      181 kaewqgqtlg figrideprk glpilmkalp ailaarpgar llvagrgdee eavaslpkel
      241 rerveflgmv sdedkarllr svdvyvapnt ggesfgiilv ealsagapvl asdldafaqv
      301 ldqgaagdlf anedadalaa aairllgdpe rrkglrerge ahvrrfdwat vgadilavye
      361 tvtdgaasva adersglrar fglard
//
LOCUS       WP_457656164             273 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656164
VERSION     WP_457656164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  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 273)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..273
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29160
     Region          67..271
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtardttglp gawrlgllrg glelkqffrl rdqvvfslaf pvvlqmllas ifggdladge
       61 vpvsqiyvaa mlgagimats fqslgisiai erderllrrl istpmppaay flgkvwlvlv
      121 tgaleaavll avgvglydld lpgdvstwlt fgwifllgta acallgiais slpgsgrsag
      181 svvilpflvl qfisgvyipa selpdwmlni galfplkwmc qgfrgvflpe saavleqagg
      241 wefgrialvl gawcigglll clltfrwksr rdg
//
LOCUS       WP_457656170             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656170
VERSION     WP_457656170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33783
     Region          66..310
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mseallvqea gaapavapas garlflrrlr aqraacaaal vvlllvlval aaplltalag
       61 qdpnayhpdl vdsaaggvpi gsfggisaeh wlgvepqtgr dlfarvvyga rvslgvalva
      121 tvlqialglv iglaaalgsr wvdqllgrit dvnvalpvmv ialallaivp esfprpvlia
      181 lviggigwsg tsklvraqal tlksldfvsa arlsgrgkws iarrellpsl aapvityaal
      241 afptniivea alsflgvgik pptpswgqml teadtwyqaa pmyllipagl lfitvlaltv
      301 lgegirtald praasrlrvg ttkkgeaa
//
LOCUS       WP_457656171             548 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656171
VERSION     WP_457656171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 548)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..548
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58609
     Region          3..531
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtpheplvev tgltvdfgsv ravdglsftl eaggalgvvg esgsgksasa yallglhrgt
       61 garvgglvrv agtdvnaadd rdlralrgak aamvfqdpls sldpyypvgd qiaevyrvhr
      121 pvsrkaarar avevldrvgi pdaarrsrlr phefsggmrq raliamalac epllliadep
      181 ttaldvtvqa qildllhdlr hetgmglllv thdvgvaaes vdevlvmrhg kevergpvar
      241 vlgaprepyt kellaavprv etrrvvpvpa praeetsvpl leavglrref grgsgrvaav
      301 dgvsltvhag rtlgivgesg sgkttlgrml vrlldptagr lryggteigs lpekelrsfr
      361 rdlqmvfqdp vaslnprrsv gesvadplra agesdqgrir drvgallerv gldpahfery
      421 phefsggqrq rigiaralaa epklivcdep vsaldvttqa qviellselq relgiglvfi
      481 aydlavvrqv sdevavmrrg viveqggade vygqprdpyt rqllaavpal dpglaearrt
      541 arkelara
//
LOCUS       WP_457656174            1115 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Streptomyces griseus].
ACCESSION   WP_457656174
VERSION     WP_457656174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1115)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1115
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=120311
     Region          37..847
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          850..1110
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 msssstrhsp hresrprttg ayrlvrtppg svdpplldag qravvdhpgg pllvlagpgt
       61 gktttlvesv aarvnrgadp arilvltfsr kaavelrdrm aarlgaargp qattfhsycy
      121 alvrahqdad lfadplrlls gpeqdvtvre llagqldlek eglahvrwpd elrsclttrg
      181 fadevravla rsrelglgpd alaafaartg rpdwsaaaqf laeyldildv qgvldyaelv
      241 hravllaerp evaaelagry davyvdeyqd tdpaqvrllh alagnrgrge dpsggrtlia
      301 fgdpdqsiyt frgadvngil dfpdtfrrad ggpapvgvlt tsrrsgagll aatrlltrrm
      361 pltrlpgdtv rahrdlhavr dggrvetyty pttsteleni adllrrahle dgvpwqemav
      421 lvraggrslp avrraltsag vplevdgddl plrhepavap lltalrtvat aalhhrpvet
      481 eaedqpeagp tswldtetal tlltsplgam daadlrrlgr alrdeeraag irvpapsddl
      541 laralaeper lvthdpayah gaqrlgallr karellhggg taeealwilw ngtpwpgrla
      601 raalrggagg rnadrdldav calfdtaara eertggrgal nfleevdaqd iaadtlsrrt
      661 arpdavrlmt ahrskglqwr lvvvagvqeg vwpdlrrrgs lleadrigrd glaepltpga
      721 llaeerrlfy vaatrardrl ivtavkapad dgdqpsrflt evgveprdvt grprrplava
      781 alvaelratt vdpaasaalr eaaahrlarl aaltddegqp lvpaahpyrw wgleeptrsa
      841 vplrdrdqpv tlsgsaldql antcalqwfl grevkadapa taaqgfgnvv hvladevass
      901 rtpadldvlm erldsvwngl afdapwkseq ekdqaraale rflhwhvldr ggrtptaseh
      961 dfdvtleage yavrirgsmd rveqdaegra yvvdfktgks aptkdevaah pqlavyqlav
     1021 regavdevfd grrpepggae lvqlrqpapk keggdafpkv qaqeplagew vsdllataag
     1081 kvlderftpt tgnhcahcaf rascsaqpeg rqvve
//
LOCUS       WP_457656177             481 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457656177
VERSION     WP_457656177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..481
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49809
     Region          218..457
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mndptaglpl sapealtvlg alvlvaarwl perlrgpaal aagallagsv tvlvmtglrw
       61 qlvpvvvaaa vvgafllapv varrsgrtpw rarwwlagpg svvcaaliaa gpvsvwafpv
      121 pnfpapsgdf pvgtealews arpagagpda eprtlvvqlw ypagrsgpda rrarylgrte
      181 aeartvssal adyagvpgfl ldslpraqsh avpgapvadg ggrfpvvvfs pglggvrtqn
      241 tawaeelash gyvvaavdhp ydsaavvlsd grtlrtrvsa tgdrakdraa aegwtrtrtg
      301 dlravlsrle rldrgegegp lagridtgrv aaaghslgga aalraarqdr rfdavvdldg
      361 fphgpvgdrf eqpvlaltqe igprtdpdyl prltrvlels dtagyrltvp gaahltftda
      421 plylppapgv igspgrtegp ritagatrsf ldatlrgtav dlpaalsayg evtvhrpega
      481 g
//
LOCUS       WP_457656179             147 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase, partial [Streptomyces griseus].
ACCESSION   WP_457656179
VERSION     WP_457656179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 147)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>147
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          4..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpdfirei rataghqlll lpgvtaivld degrvllgrr adtgkwsvig gisepgeepa
       61 ataerevlee tgvhcvaerv vltqalepvq yangdrcqyl ditfrcratg gearvnddes
      121 levgwfpldg lpplgefalf rikqalt
//
LOCUS       WP_457656183             172 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656183
VERSION     WP_457656183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..172
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18091
     Region          10..129
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 misepsrhct velqalpsri gqvrriisaq lrywhldpli dqaalgvtel ltnvhrhaqp
       61 dksctvdiel lldrltvsvh dhdprlptvn eadsfatsgr glaliaavse swgvrpigsa
      121 gkavwftlpa asgastlppl avygsmtdgp fgavtitpdd iasaparsav vg
//
LOCUS       WP_457656184             251 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces griseus].
ACCESSION   WP_457656184
VERSION     WP_457656184.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27245
     Region          28..201
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mqiaehiasl sgegrllaaa aeragpgasv ptcpgwqirh llrhtgmvhr waaafvtegh
       61 tayqpdggep dldgaelltw freghdhlvg sleeapadld cwtflpapsp lafwsrrqlh
      121 ettvhrvdae salggpltpv paeravdgid elltgfharp rskvrsrkpr tlrvravdte
      181 atwtvrised ppeavrtaap dapedgvdce lsgtaeglyl tlwnrlplaa lslrgdrsva
      241 rlwtdnsavt w
//
LOCUS       WP_457656185             432 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656185
VERSION     WP_457656185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  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 432)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..432
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=45259
     Region          <218..416
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdeqrpphrg ggppcglpgr sgrpggrggp ppwlsgarsr taaglpwlst avllvfvmvg
       61 tgfaehgqdr rpldlvarll lfvavgvlll rhrrpvlavv ttcavtlgyl aagypygpvf
      121 vavavgcfsa ivaghrkaaw wslgglwagh vlvahwlyrw lppdgdpaap waqegfitaw
      181 vvavvaaael lrvrreqwaa araeraaaer rradeerlrm arelhdvlah sisvinvqag
      241 vglalldsdp eqartaltti kgaskealde vrqvlanlrt pgdaptapap gldrlpelvd
      301 qaaaaglavt vesegdpaav ppgaglaafr ivqealtnvv rhsgsrtalv hiahgsgrvr
      361 lriddagpat gddaggsgng lvgmreraaa lggtveagpr pdggfrvrae lpftapdhdr
      421 rqdppepaee tp
//
LOCUS       WP_457656187             206 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein,
            partial [Streptomyces griseus].
ACCESSION   WP_457656187
VERSION     WP_457656187.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..206
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          <1..205
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 atdleageqg vvatqaafaa syttksrvsr gvpvitvkpn sapvepaaaa gavealsvsf
       61 gatatgtkvt srtarestgr pelteaaivv sggrgvngae nfpviealad slgaavgasr
      121 aavdagwyph tsqvgqtgks vspqlyiasg isgaiqhrag mqtsktivai nkdaeapife
      181 lvdygvvgdl favvpqltee intrkg
//
LOCUS       WP_457656195             332 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces griseus].
ACCESSION   WP_457656195
VERSION     WP_457656195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35702
     Region          1..324
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mpsvdltlae chayrpelpl pdgfdafwsg tldgkapsga tdrqprfeev dsglvqvrcy
       61 dvsvpgydgr pvrgwlrmpa gstgplgciv eflgygrgrg laheqlmwac agyahlvmdt
      121 rgqgwssatg dtpdtdpgsa gavpgfltrg vespgthyyr rvftdavrcv qamrehpevd
      181 parivvtgvs qgggialava glvpglagvm pdvpflcnip raariaatpp yteiatylrl
      241 hrdrveevfr tlsyfdaahh atratapalf svamaddvcp pstcftaynq yagpkdvrvy
      301 efngheggte hhraeqlawv rdlfaglpad rv
//
LOCUS       WP_457656198             469 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces griseus].
ACCESSION   WP_457656198
VERSION     WP_457656198.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..469
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50191
     Region          7..450
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 maaedlverr sidvvpdger hgtafsqftl wlganlqita vvtgalavvs ggdvvwsvvg
       61 lllgnvlgga vmalhsaqgp klglpqmiqs raqfgvkgav vplllvilmy vgffasgsvl
      121 agqatarlmh tddstgivvf avvtavmaav gyrvihllgr vasvvcalaf vylgirlldr
      181 vdlsallada hfdlpmflla vslsaswqla fgpyvadysr ylprttsgrs tfwwtlsgsa
      241 vgsqwsmtfg vlvaatagea fltnqvgyvv glggtglias flyfvialgk ltinvlntyg
      301 gfmsmvtsis gfrglrtlsp rgravyigli mvagtalall gkdsfltsfk dfllflltff
      361 tpwsainlvd yylisreryd ipalfdpgar ygawrwdalt vygigilaql pflvthfytg
      421 pladplggad vswivglvvp aalywllarr dtrhipektl ytlaspyen
//
LOCUS       WP_457656199             176 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656199
VERSION     WP_457656199.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  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 176)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..176
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17884
     Region          24..154
                     /region_name="DUF4439"
                     /note="Domain of unknown function (DUF4439); pfam14530"
                     /db_xref="CDD:434020"
ORIGIN      
        1 msirserrsd dadesdadsp eltavqaala aehaavygyg alggrlegkr gaearaaydg
       61 hrarrdalar tardlggrpv asdaayalpf avadapsaer laavledria gayadlvrat
      121 egdrrgdaag alreaavrsa rwrggnvafp glaeraagad paatgpveaa gadstr
//
LOCUS       WP_457656208             234 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656208
VERSION     WP_457656208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..234
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24499
     Region          22..143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          90..233
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 madretrqtt vwsrpargar gpapersrae ittaalalad aegltavsmr alaqrlgagp
       61 aslyryvgsr delldlmada vaaeldlsad psgdwlddlv glarqskaah vrhpwladln
      121 drrgevlgph aidyldhalr ilapapgtpg qkleaigllg glatlfarre alavdtetpp
      181 araahlaava aegrhphlla altaagappt agpddrdalf vrllrrvlpa mltg
//
LOCUS       WP_457656215             148 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656215
VERSION     WP_457656215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..148
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16190
     Region          7..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtdyspdatd wrildvlqrd gratfaelar avamsasavt ervrrleelg visgyaavvd
       61 aerlglpila lvrlrypngn ykpfhdllet tpeiieahhv tgddcfvlkv tarsmrhlee
      121 ttgrigalgs vttsvvyssp lprraigr
//
LOCUS       WP_457656224             158 aa            linear   BCT 27-JAN-2026
DEFINITION  RrF2 family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656224
VERSION     WP_457656224.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..158
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16184
     Region          1..137
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 msggvewalh ccvvltatee papaarlael hdvspsylak qlqalsragl vqsvqgkagg
       61 yvltrspali tvldvveavd gpgpafvcte irqrgpmatp peactapcav nramgraeaa
      121 wrealrsvtv adlaadvtsd ygtgalgsis twlnpaea
//
LOCUS       WP_457656225             220 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656225
VERSION     WP_457656225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24078
     Region          21..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnqsvgrpa rsqarprtpr spearqrqqd ilaiamdafa argynnasla eiadrvgltq
       61 agvlhyfrsk allltsvlel rdqrdiehlg pdrpqglefl rhlvstalln aeregivrly
      121 avlsaesvtd dhpaqdyfrd ryhglrafvs dalreacelp adraeltdna anaiiavmdg
      181 lqvqwllspe svdmaastdl vvtsllakld perfgphaag
//
LOCUS       WP_457656222             288 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656222
VERSION     WP_457656222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31794
     Region          12..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(17,21,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(20,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(27..28,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mlhgpvvrrr klgeelrslr hasgltsrda arllgwhqsk vsrietgasg vtpadvsrll
       61 dvyavrdtql rsllevlags aggggsgwwh ayrglippqy rdfislesqa stvrtletsv
      121 vpgllqtagy aravtrasld glpdgrldsl vevrltrqrv lraspplrft avldeavlhr
      181 evggpevmrd qlhhliqvsq lphvqlqllp fsvggyiglt spfvifsfpn isdldvvvld
      241 hltsslyler redleayssa frtlqahals persqdlite irrsfrrs
//
LOCUS       WP_457656227             566 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656227
VERSION     WP_457656227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..566
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57515
     Region          41..519
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,166,
                     169..170,173,298,301..302,305..307,310,338,342,395..396,
                     400,404,420,423..424,427..428,448)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mstnqpgpvs vdpddaprls gadegegvld arrrrtillt vclalmavia svsglnvaqp
       61 dlavafgasq stilwiiniy tlglaalllp lgaigdrlgr kpvlvaglvv fgvasaaagl
      121 apsaevmlga rllsgvgaam impitlavit ttfpenergr aigvwtgvag gggvlgmfls
      181 aalvdvanwr wlfvlplvlg aaalvmtlrf vpdsreafrh gfdaggalts avavvglifv
      241 lqegpergws spvtliglvv gvlaavgfvv qelrrgdaal ldvrlfrera laggsvtllv
      301 vfgvqagifv vlfpflqavl gwsgllstsa lmpmavlmmm asglaphlta rvgaratmat
      361 gillagagla lmagivsvdg gylsvlpgml amglgmglam tpsteaitga lprerqgvas
      421 alndvtrefg talgvallga llsagyrgai dsrlagvpdg padsaregva naveaangag
      481 pyaqeliraa rqsfvdgwqn amwagvavma alflyvlfrg plrparaaeg phlaesthla
      541 esartaegts rpvgpdaser adatas
//
LOCUS       WP_457656218             404 aa            linear   BCT 27-JAN-2026
DEFINITION  trans-sulfuration enzyme family protein [Streptomyces griseus].
ACCESSION   WP_457656218
VERSION     WP_457656218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..404
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42438
     Region          18..384
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mdnevsmtpp aptpsralat eavhagrddl aflgvhappi dlsttypsyd sraeamridd
       61 fattgarpdg ppvyarldnp ttgrfetala rlegaesava fasgmaalta vllarasqgl
      121 rhvvavrply gcsdhllgag llgtevtwtd pagiadairp dtglvmietp anptlaeidi
      181 ravahacgsv pllvdntfat pvlqrpvehg arivlhsatk ylgghgdvmg gvvacdeefa
      241 atlrqvrfat ggvlhplagy lllrglstlp vrvraastsa aelvrrltad priarvhypr
      301 iggamvsfev ygdphrvisg vrlitpavsl gsvdsliqhp asishrivde gdrrasgvgd
      361 rllrmsvgle dvedlwadlc qalsdgpvpp arkaeqplrs sagr
//
LOCUS       WP_457656228             381 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457656228
VERSION     WP_457656228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..381
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41179
     Region          3..375
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mneallrslt psvlgilvrr gadfaaaeda vqdalveavr vwpdeqprdp kgwlvtvawr
       61 rfldatraea arrrredrvd eepvpgpapa tddtlqlyfl cahpsltpss avaltlravg
      121 glttrqiara ylvpeatmaq risrakrtvs gvrfdqpgdv atvlrvlylv fnegysgdvd
      181 laaeairltr qlaaaidhpe vagllalmll hharrasrta pdgslvplak qdrgrwdtam
      241 iaegveilqa alvrdrlgef qaqaavaalh adartaeetd wvqivewyde lagltdspvv
      301 rlnravavge adgpraglae laalsdslpr htavaaylhe rdgdletaar lyaeaahkap
      361 tlaerahltr qaarlntgrp g
//
LOCUS       WP_457656229             402 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457656229
VERSION     WP_457656229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..402
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43832
     Region          27..401
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrvllvgagg vgtaiariaa rrsffdhmiv tdydlsraea avaalgeera rftalrvdas
       61 dreavtallt eqrcdilvna tdprfvmplf eaalaagvdy ldmamslssp hperpyeecg
      121 vklgdgqfer aaaweeagrl alvgvgvepg lsdvfaryaa delfdtveei gvrdganltv
      181 dgydfapsfs iwttieecln ppvvwekdrg wfttapfsep evfdfpegig pvecvnvehe
      241 evlliprwve srrvtfkygl gdefidtlkt lhklgldrtd kvsvpggdvs prdvvaaclp
      301 dpallgdrmh gktcagtwvk gtkdgaprev ylyhvvdnqw smreygsqav vwqtainpvi
      361 alelvangvw sgvgvlgaea ldprpfldll vaygspwglr eq
//
LOCUS       WP_457656230             394 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656230
VERSION     WP_457656230.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..394
                     /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=42058
     Region          133..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mntdgaprlg wwqqtwrlaa aavlsvpiwl yigvllhnqg vgpdpwfrig dplvalaclt
       61 vlpwrrrfpl avamtvtias tasalatgaa llalgsistr rrpveigavv layvtatqfv
      121 ggfypvqnpp gtfwfqlalp altagiavav gmaigarrve vrslrdraes aereqaaraa
      181 qarvlernri aremhdvlah rislvamqag vldhrgdlra eenrllvrgi aegshqalee
      241 lrdvlgvlra dpghpeppqp sleripdlva darasgldvt ltttvtgtpa dvvgrtcyrv
      301 vqegltnaak hapgarvhia vegrsgdglg vsvrnspatd rpaqrppasg fgllglterv
      361 dlaggtlhhc ptpdhgyvlt vrlpwpapth ekrt
//
LOCUS       WP_457656231             602 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces griseus].
ACCESSION   WP_457656231
VERSION     WP_457656231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..602
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=66463
     Region          62..544
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtnphlpaph epaalreryr yererrvrpd gaaqyrdada efgyyaadpy ikeprrrgpc
       61 hdtvdvavig ggfggiltga hlrqqgverv rfvekggdfg gtwywnrypg vhcdveshvy
      121 lpmldetgyv pewkyapgde irrhavriad tfglytdtlf stgvtsltwe etsgtwivat
      181 drgdafraty vvnatgtltd pklpgipgie kftghtfhts rwdyaytggt pqggmtrlad
      241 krvgivgtga tgiqvipmla qdaahlyvfq rtpstvdvra nrrttaqdvg aghdgwargr
      301 renylrivsg entdhdlvad rwttsaglle kllpsfrrhg draafeaaye aadaakmnel
      361 rtrveqsvtd petaeklkpw yryackrptf sdlyypafnr dnvtlvdtad thgiehiteh
      421 gvtvgaatye ldclifatgf nvgtsaistg klpvhgrggt qllhawarrg prtlhgftsn
      481 gfpnlihlga lqnassvnft hildeqarha aaliaaaeda aalieptpea edawtavlaa
      541 dapdhewfha ectpgyynre grgrpngpfa yphsavafha llarwraesi qeilrdrtgh
      601 ps
//
LOCUS       WP_457656232             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656232
VERSION     WP_457656232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20460
     Region          20..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtehtepggr rpandgpkaa grnraalvaa arevfaehgl eaplsaiarr agvgqgvlyr
       61 hfpdrtaavs avleenvrqi eqaaeaesat fpavlgvltw hlaesaafig llhtdragsr
      121 sgirvhalnl sgrvehalrk hlppghrlgv adglalsvam vsaaatgptr eerehralaa
      181 wrllgvevgp vqafgg
//
LOCUS       WP_457656235             710 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656235
VERSION     WP_457656235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..710
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=74658
     Region          <269..594
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          492..632
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          510..532
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(528,531..532,560..561,564,567..568,571,590..591,594,
                     597..598,601,623..624,627,630..631,658,661,664..665)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          543..571
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          576..602
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          606..631
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          638..666
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mvsvlfgivp rmmineidgv dwesmghayg pasdvpgwlr gmssadpevr deafsdfyna
       61 ahhqgdvypc taaslpflfk madspatpdr gsviglllsi gresldmdpe gvyftpdgte
      121 srahvdaltv iggrakafvr wvadpdqevr rpaieglglf lddsaravev lrsllpgdgl
      181 verllvvrtv atvalrdpav hgaaaswlea lasdtaqape vrlaalvhrv rctpgelgda
      241 vvpaavglir eiapeetggy ddascrtgae pgvaagsaps sgvppqiaaa fedlerhgrv
      301 hapttsllea fhtvlddrvl ertalltgql rsadpgvryd airmarelig qwrgdhsglv
      361 lliagcldtg dpytsaaaae algalvpvse parealagyv eaaraehgpg vwaarerlvr
      421 rahqeavral aclgdlralp cvlaaldegt dawravqvag hlggaagdlt prlskllaev
      481 dfsdasqsms analvsalre lgdpgsapvl asavsaavre eqwhttasal kalasfgpea
      541 afalevvrpl adaqdvtvra aataalwelq gdaagvvprl velldthadd eaaavlgrig
      601 saappalprl rkmltagyew trvyaaaalw disgdaeapa vvetllaawa endstsnhvl
      661 aclsrmgpaa rpalprvree ltllrrsgrf rdiphdedll aacrsvtsrl
//
LOCUS       WP_457656236             425 aa            linear   BCT 27-JAN-2026
DEFINITION  AlbA family DNA-binding domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457656236
VERSION     WP_457656236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Jo,U. and Pommier,Y.
  TITLE     Structural, molecular, and functional insights into Schlafen
            proteins
  JOURNAL   Exp Mol Med 54 (6), 730-738 (2022)
   PUBMED   35768579
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Chen,J. and Kuhn,L.A.
  TITLE     Deciphering the three-domain architecture in schlafens and the
            structures and roles of human schlafen12 and serpinB12 in
            transcriptional regulation
  JOURNAL   J Mol Graph Model 90, 59-76 (2019)
   PUBMED   31026779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..425
                     /product="AlbA family DNA-binding domain-containing
                     protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46893
     Region          34..141
                     /region_name="COG2865"
                     /note="Predicted transcriptional regulator, contains HTH
                     domain [Transcription]"
                     /db_xref="CDD:442112"
ORIGIN      
        1 marswtrlhe hlgaapgpld fdmvrraaad lleesddldw kehlpqpprd grwnelakdv
       61 aamantrggl lifgvqdktc hltgidpdqa npqqyhqwir nhvqpylpdi tfttltspdg
      121 ttnvlacdip aspmaphhvy gtaqkdkdqq aavvpyrdkd qtgwmaehqi erayrdrftr
      181 teraeeever llgqtresaf thqtepaawf laiarperpl prtaprltrh easavldtar
      241 trtqtshrsa agplaglqiv ssnprpglrr wvvqtltrql grdihaelhh dgttvlaadl
      301 swdarrgral qeapegsllf sqdytmacce nftalargla hrtgadsalh itatiasstg
      361 tapltpvvse hggafpeidy darqptriqp vttslspsgg apardeaahe iftdlmnqfg
      421 ldpqt
//
LOCUS       WP_457656243             341 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656243
VERSION     WP_457656243.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 341)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..341
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36807
     Region          15..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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"
ORIGIN      
        1 mtslpsakdp fadlaellva lrraarlsqr dlaaratisr gtvqnaesgr tapsalllda
       61 ylkacgadsr tadrarrlrt rgrsdqrgrl rglcapapdl ihdrhdlaaa lataferaga
      121 pplgdrhlig dreplprtta wrivnrqglp anvtqlktfl tacgispavq rlytdayrrv
      181 taarparpap lrarrndirt ivearserhe ltgtaaaiar qlpaealeei lftaitreaq
      241 rngsglpdgw vasspyqdtg vdismrtaag ervymqvkny rrpeppllap gpgappsrpg
      301 sspsgwwsgt rraapapdqp earrardydr daaavlaapa r
//
LOCUS       WP_457656269             262 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces griseus].
ACCESSION   WP_457656269
VERSION     WP_457656269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..262
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28857
     Region          17..252
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mgnvlesrwi qrlqpistad vrliafphag gaasyffpla halrqaehps aldimavqyp
       61 grqdrrrepc iddlqalada acrellpfad rplllfghsm gallayevtr rleqehgivp
      121 ltlfasgrra psiscpesvh rlpdsdvvke iglldgtdsa llsdpellqm vlpairgdyk
      181 avetyafrpg prlqcpihti lgdadprvsv edaeawaeqt sgsfelsvvk gghfylkdqq
      241 dflvakimdr ltkisegrtr hg
//
LOCUS       WP_457656271             329 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457656271
VERSION     WP_457656271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34604
     Region          1..251
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 meplrigvlg cagiarrrml pafracpgte lvavasrdrl rsretaaeak ceavhgyael
       61 lartdidavy lplpaalher waraaleagk hvlgekpltt dpaatarlaa laaasglalr
      121 envmfvhhpq haavahlvad gaigdvrsfr aeftvprlpd ddirydpalg ggalfdtgvy
      181 pvraalhflg dglelvgavl thgvphrsvd tagvallrda agtgvqltfg ldhgyrsrye
      241 ilgsagaltv draftppaga rplvrwergt gteqldlpah dqvlasvaef aeavrtgapp
      301 dpalfrqadl lariradarv vtgpagpar
//
LOCUS       WP_457656273             776 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces griseus].
ACCESSION   WP_457656273
VERSION     WP_457656273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..776
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79502
     Region          22..774
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msahsattas tatgseagtt avelaiggmt cascaariek klnrmdgvea tvnyatekak
       61 vtyqgaevsv ddliatveat gytarppapp appassggsg tetagaagta gpaaesaedd
      121 glttlrqrlv tavllsvpvi amamvpalqf dywqwlsltl aapvvtyaaw pfhraawtna
      181 khgaatmdtl isvgtsaafl wslwalffgt agmvgmthpf eltiarsdga gniyleaaag
      241 vtafilagry fearskrkag aalkalmelg akevtvlhdg vettiptaal qvgdrflvrp
      301 gekiatdgtv vegssavdas mltgesvpve vsagdtvtga tlnaggrlvv eatrvgadtq
      361 larmarlved aqngkasaqr ladrisavfv pivialalat lgfwlgndag ltaaftaava
      421 vliiacpcal glatptalmv gtgrgaqlgi likgpevlet trradtivld ktgtvttgrm
      481 tlqtthttdt tteaevlrla galenasehp iaqavataat dttgplptpe dfqnvpglgv
      541 qgvveghavl vgreqllaew eirlpaplae akkaaeaagr taitvawdge aravlevada
      601 vkdtsaeavr rlrdlgltpi lltgdnrava esvaaevgid evyaevmpqd kvdvvkrlqa
      661 egrsvamvgd gvndaaalaq adlglamgtg tdaaieagdl tlvrgdlnaa adairlsrrt
      721 lstirtnlfw afaynvaalp laaagllnpm iagaamafss vfvvgnslrl rtfkga
//
LOCUS       WP_457656276             386 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656276
VERSION     WP_457656276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..386
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41601
     Region          6..322
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtpprtpqip vvvlagflgs gkttllnhll rnragtrigv ivndfgaiei damtvsgqvg
       61 stvslgngcl ccavdaseld tfletltrps arldviviea sglaepqelv rmllasdnph
      121 irygglvevv daaefdstre rhpeldrhla vadlvvlnkt drvgeaerer lratvaelsg
      181 paavisavhg ridpellfdp alrpdheema gqlsfedllr qeecdeheec dghghgdhlh
      241 asyesvdfta dvpldprrfm afldsrpegl yrikgfadfg agdrdntyal havgrflrfv
      301 prpwargeqr ltqlvmigag idaeallagl aacradepap datasdastt evsadadsda
      361 vergmwgvlr yvqeqapepq eaaaea
//
LOCUS       WP_457656277             982 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional acetate--CoA ligase family protein/GNAT family
            N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656277
VERSION     WP_457656277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Sanchez,L.B., Morrison,H.G., Sogin,M.L. and Muller,M.
  TITLE     Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming)
            gene from the amitochondriate protist, Giardia lamblia
  JOURNAL   Gene 233 (1-2), 225-231 (1999)
   PUBMED   10375639
REFERENCE   4  (residues 1 to 982)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
REFERENCE   5  (residues 1 to 982)
  AUTHORS   Mai,X. and Adams,M.W.
  TITLE     Purification and characterization of two reversible and
            ADP-dependent acetyl coenzyme A synthetases from the
            hyperthermophilic archaeon Pyrococcus furiosus
  JOURNAL   J Bacteriol 178 (20), 5897-5903 (1996)
   PUBMED   8830684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18515002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..982
                     /product="bifunctional acetate--CoA ligase family
                     protein/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.2.1.13"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0046356 - acetyl-CoA catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=103135
     Region          30..178
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          206..973
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 meptpeqsph haypdhwead vvlrdggtar irpittddae rlvsfyeqvs deskyyrffa
       61 pyprlsdrdv hrfthhdyvd rvglavtigg efigtvrydr iddtgrpasa padeaevafl
      121 vqdahqgrgv asallehiaa varergirrf aaevlpannk mikvfrdggy tqrrsfedgs
      181 vhltldlept ekslavqrgr eqraearsvq rllapgsvav igagrnhggv grtvlrnlla
      241 agftgrayav nrafdeglat ldgvpahrsl geideqvdla viavpahrvp eavadcgehg
      301 vqglvvlsag yaergadgre lqrelvrqar sygmriigpn afgiintaes vrlnaslape
      361 spargriglf tqsgaigial lsglhrrgag lssfisagnr advsgndflq ysfedpdtdv
      421 allyleslgn prkftrlarr taavkpvvvv kgarhsgstp pghavpvsri pdatvsalmr
      481 qagvirvdtv temvdaglll agqplpagpr vailgnsesl glltydacla eglrprppid
      541 lttaaspqdf rdalaealad gtcdavivta ipwvgengea etgdgqvlae altkavaggs
      601 akpvavvhve igglaealaa asstaaprpr tvtsaartra attatttqtt ttgtpaaqat
      661 ttgtgtpaap eattapatpd aatapeaapr pgripaypaa eravralaea vkyaqwrrqa
      721 aipgkvpefl ddtideagaa alieaqlsta pdprgrplth dearellgry gvdvrptlpa
      781 pdpeaavaaa arlgypvalk ttaphlrhra dlggvrldla deealrrayg dltdllgkpa
      841 ellpvvqama prgvdtvvra sidaaagavl sfglagapse llgdtahrlv patdrdaael
      901 irsiraapvl fgwrgsapvd taaleelllr lsrlvddhpe vvsvalepvv vapqgltvlg
      961 asvrlapppa rndlgprrlp ny
//
LOCUS       WP_457656279             534 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces griseus].
ACCESSION   WP_457656279
VERSION     WP_457656279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 534)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..534
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59379
     Region          12..474
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(67,70,107,110,155,173,177,209,259,320..321)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(209,259,321)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          455..532
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 maavppsrtd twwrdaviyq iyprsfadgd gdgtgdlagv rahlpylaal gvdavwftpw
       61 ylsplvdggy dvadyrtidp afgtldeaek liaeaagfgi kvivdivpnh lsdqhvwfts
      121 alaagpgspe relfhfrpgr gengelppnn wpsqfsgdtw trvpdgewyl hlfapeqpdl
      181 nwshptvrre hedvlrfwfe rgvagvrids aalltkhpdl pdftegvdph pyidqdeihd
      241 vyrswrtiad ayggvfvgev wlpdserfar ylrpdelhta fnfnflscpw dperlrrtid
      301 gtlaehapvr apatwvlcnh dvtrtvtryg rtdtafdfat kefgtpadle lgtrraraaa
      361 lltlalpgsv ylyqgeelgl peadipldri qdpmhfrsgg tdpgrdgcrv plpwaaaepy
      421 ggfgsttepw lpqpadwpty avdrqdadpa smlslyraal rlrretsgfg dgpmtwlpse
      481 dgvlafartd glvcvvnlld rsvelpvhee pllasgplda dgrlpsdtav wlrr
//
LOCUS       WP_457656283             286 aa            linear   BCT 27-JAN-2026
DEFINITION  endo alpha-1,4 polygalactosaminidase [Streptomyces griseus].
ACCESSION   WP_457656283
VERSION     WP_457656283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="endo alpha-1,4 polygalactosaminidase"
                     /EC_number="3.2.1.109"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=30613
     Region          13..286
                     /region_name="COG3868"
                     /note="Predicted glycosyl hydrolase, GH114 family
                     [Carbohydrate transport and metabolism]"
                     /db_xref="CDD:443077"
ORIGIN      
        1 mpqhavppfl rrrstlaala cgvavatgag lllshtfatg stdeaapeiv ppranvtfdy
       61 qiggaytppa gvgavsrdrg dapaeglynv cyvnafqtqp daldqwqkdd pdlllrdgdg
      121 elvsdeawde vlldtstagk rarlaeivge widgcaasgf qavepdnlds fersddlltr
      181 ehnaafakll adrahsvgla igqknttdll drreaigfdf avaeecgryd ecadyasaye
      241 dkvfvveytd gdfakacssv gakvsvvrrd ldvrpagrpg yvfrtc
//
LOCUS       WP_457656284             445 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656284
VERSION     WP_457656284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..445
                     /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=47981
     Region          212..424
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 makpvrrrsp arrrlrrlql rltaaytlit vvglaalswl virtddrarq daeydemrrr
       61 asvaaslvyy eddrirldgl ddddatsgtp qilvlegrpg gdpvtvfrgr teqfavpaga
      121 lravartamd eeepvraear drtgepvhll avpfyhdatd evagaavavg dpeygaaehr
      181 slvlslvvgt galtalaalt ghvlsgrsvr pawqaleqqe rlladaahel rtpvavmrgs
      241 vevaaaspdg paahlprirr aadrmadvve nlltrgrlda dvdvvraepl rldqlveevc
      301 aelpengrrp elrltesvte adaalvrvav rnlldnavrh grapgapadr adllvtvrgp
      361 evwvadrgpg vdpdrlpelm erfsspgggt glglslvgri aeahrgtlav rerpgggaef
      421 vlrlapagsr qgrrrgtrrt ltirs
//
LOCUS       WP_457656290             376 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656290
VERSION     WP_457656290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..376
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39802
     Region          22..358
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtgpahaggd ggdgrhgpvd palqrglqal vdtpggppga iavlraggrs evyragtsql
       61 gtgrpprttd hmriastaka fsgsvalqlt ergalglddt igrrlprlpa awhrvtlrql
      121 lnhtsglpdy tedptfvael tadprrhfds rrlldyvagd plrfrpgsay rysnsdniav
      181 almaeaatgr ryeklladlv yrplglrdts lpqgyrlpep flhgyavdpp napedvstvl
      241 sasgvwasgg ivstpqdlga fvrgyagglg lgpavrrqql sfvagssepa gpgrnragla
      301 lfsyttrcgt vyghtgnfpg ytqlaagtkd gkrsltvslt sqvnsttnpr llatlrelqe
      361 dfvcrlldrr kpggaq
//
LOCUS       WP_457656288             309 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656288
VERSION     WP_457656288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..309
                     /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=34300
     Region          42..>94
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          119..285
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mddqpeaaap epldrraels eflrtrrakl qpqdvglpef grarrvpglr reelaqlagv
       61 svayytrleq gngrnvsaev ldaiaralrl tdaehahlnh larparhkkk rrpakvqrvr
      121 tglvylldnm egipayvaga rsdilawnpm atavfgdwaa lppaernwar lvflspayrd
      181 lflnwdskas dmvsylrlya gchpddpqls alvgelslks eefrrlwath nvkekghgik
      241 lirhplvgdl tlsyetlnlp ddedqqlvty haepgsesaq alrllaswga dagradvisg
      301 agrgpdder
//
LOCUS       WP_457656285             224 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces griseus].
ACCESSION   WP_457656285
VERSION     WP_457656285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..224
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24319
     Region          1..209
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrvllveddd dlreviasgl rdggfavdca adwpeadvll hvtaydcvvl drmvpsgdtl
       61 vplevrrrag wsvpvlclta ldslperlrg lesgaddyla kpfampelvl rvrglsrraa
      121 arlpsflsca dvvmdvarye vrrggvllsl spkeyavlrq llvhrdavvt rtdllehcwd
      181 emadpvsnvv davvaglrrk lgspglvhtv rgqgfllsae pgps
//
LOCUS       WP_457656298             391 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanine--D-alanine ligase family protein [Streptomyces griseus].
ACCESSION   WP_457656298
VERSION     WP_457656298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11479728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="D-alanine--D-alanine ligase family protein"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008716 - D-alanine-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42381
     Region          21..385
                     /region_name="ddl"
                     /note="D-alanine--D-alanine ligase; PRK01966"
                     /db_xref="CDD:234993"
ORIGIN      
        1 mssenlpqsp errespeqqr rkprvavvfg grssehgisv vtagavmkai drttydvlpi
       61 gittdgrwal tadepermai adrkvpdvdg laesaegsvt lsvdpgsrev lysepgsvpk
      121 algevdvvfp vlhgpygedg tlqgllelsg vpyvgagvla savgqdkeym krvfrsfglp
      181 vgpyevvrpr ewesdpaaar krivdfageh gwplfikpar ggssmgitkv dglesldeai
      241 eearrhdpkf lvesllrgre iecgvlefed gprasvpaei ppvtahdfyd feakyidsaa
      301 glvpapltde qtaevqrlav aafdavsceg lvradfflte dgtfvinein tlpgftpism
      361 yprmwqesgv dypelvdrli qaalnrstgl r
//
LOCUS       WP_457656295             548 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces griseus].
ACCESSION   WP_457656295
VERSION     WP_457656295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..548
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56691
     Region          9..546
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 msqstapqsa pehrtvllrg gdvhspadpf atamvvergh vawvgsegaa dafasgvdev
       61 idlegalvtp aftdahvhtt atglaltgld lsgartlaea lglvrafanr haagdvllgh
      121 gwdaarwper rhpsraeldk aaggralylp ridvhsavvt talldlvpgv tamagyhpda
      181 pltgdahhav raaahgalst aqrtaaqcaa ldhaaslgig svhecggpei sdeedftgll
      241 alaaerpgpr vlglwaeeia nekdarrire lgaigaagdl fvdgslgsht aclhepyade
      301 phtgtahlda ariaahvtac teaglqagfh aigdaavtav vdgiraaaat lgldriraar
      361 hrvehaemlt petiaafael gltasvqpaf daawggpegm yaerlgaera aglnpyaall
      421 rtgvplafgs dspvtpldpw gtvraaahhr tpehrisvra gfaahtrggw ravgrddagi
      481 lvpgapadya vwrtaellvq apddrvarws tdprsgtpgl pdltpgadlp vclrtvvlgq
      541 tvyvrpne
//
LOCUS       WP_457656303             560 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces griseus].
ACCESSION   WP_457656303
VERSION     WP_457656303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..560
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57663
     Region          18..555
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 msagqgrgsr pvagwlvgyr rgmlrgdvlg altawalivp esvayaqiag vppqnafyaa
       61 pvallvyalf grsnflviga tsaaavlsaa avseisgdpq davglsaala vvvgavllva
      121 giarlgfitn flaepalvgf lfgmaltivv rqgaklvgvp ggdgnfferl wtilskapdw
      181 slatlavgas alalllller fvprlpaali vlalalalsa vldlkdhgvd ivggiasavp
      241 vprlpgvpae dwialsagal gvalvvfaea fsiagrfare hgqevdadre maavglsnia
      301 vglvrgfvvs gsasrsaaai gaggrtpmvs liaaglillt gafltplftd lpepvlgaiv
      361 ivavrgfmrv gelrryaald rrslwvalta lvgvllfdll pglllavals lvlfisaagr
      421 rdvavlgrlp gtrlyadvaq hpdaattagv lavrpdgslf fgnvnrvrla vrdqvartdp
      481 ppravvldln ssyrlgipvl dtldelreel agkdialhla hvraraeqdl trhaladrvg
      541 pyglhrtvdd avsaatggpv
//
LOCUS       WP_457656307            1488 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Streptomyces griseus].
ACCESSION   WP_457656307
VERSION     WP_457656307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1488)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1488)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1488)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1488)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1488
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1488
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=155467
     Region          5..33
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          35..1407
                     /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 mtlrtstdtv tealrasllk neqlrqener laagatepva ivgiscrfpg ggrgpealwa
       61 qvregvdtls alprdrgwnv pepngyvggf lgdaadfdpa ffgispreal amdpqqrlll
      121 etawetiera gvdprslret rtgvyiggtp heyvsvlaas eeaegyqitg asgsvlsgri
      181 ayvlglegpt vtidtacsss lvaihlavqa irngecslal aggvavmstp gtfgefsrqg
      241 gmaddgrcka faaaadgtgw gegvgvllle rlseaqrrgr rilalirgsa vnsdgasngl
      301 tapngpaqqr vvrqalasag lasndvdave ahgtgtmlgd pieaqalidt ygqgrrtplw
      361 lgsvksnigh tqaasgvagv ikmvmamrhg vlpktlhvda ptphvdwaeg avqlltesrp
      421 wpridrprra gvssfgisgt nahvileeap eeaesepdas vslpavpvvl sgrcepalrd
      481 qaervrdlvl adpelnpvdl aysmiasrsa werraavvas drdqlltgle avargearag
      541 vvegrtgsss laflfagqgs qragmgaelc saypafsral devaahldpr lghplkavlc
      601 apegtpeaal ldrtaytqaa lfafevalyq lfeswgvtpd vlighsigel saahaagvls
      661 lpdacalvta rgalmqalpa ggamvvirap eaevlpllgd hvslaavngp davvisgred
      721 avlavadrfp rttrlpvsha fhsplmepml eefgavarsv sfhppeipiv snltgrladp
      781 nelctpeywv rhvretvrfg dgihaleaag vgtvlelgpd grlagtvaen crsddpiaav
      841 asvrfdrpeg sgliealarl hvhgvpvdwa avfagsdart velptypfqg qrfwlaapat
      901 papaadtlfr ldweevrvpg gsgdvptvht vshgekdepi haagaalelv qgllaaepqd
      961 gpmpilltrg avgvhatdlv dvfgaaawgl lcaaqaehpd rfvlldgdgt dpdpdvlaaa
     1021 aasgesrlav rkghlfaprv vraeggtgap rsfdprgtvl vtggtsglga lvarhlvarh
     1081 evrhlllvsr rgdtadgvge lraelaeaga avtvvagdvs dretlrrlla avpsqhpltg
     1141 vihcagvvdd gvvealtpnr mrrvlapkad aalhldeltr dtdlaafvlf ssaaailgga
     1201 gqgnyaaana cldalaqrrh aegkpavsla wglwaeetgm tgrlsqters riarsgvlgl
     1261 ttteglslfd talacsdavl lpvkfapgll qtsadllprl lrplasvpag tgeraedfse
     1321 rlaglsgler eravlalvrn haaavlghas ddqveaergf lelglnslga vdlrnslgtv
     1381 tglslpatlm fdhptpsala qhlldrlige stsstaapvl rqldeiadrl seldpqvela
     1441 atvtarlral ladwsdrqvt gssddapdfe aatagemfef inkdlgls
//
LOCUS       WP_457656309            1070 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Streptomyces griseus].
ACCESSION   WP_457656309
VERSION     WP_457656309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Keatinge-Clay,A.T. and Stroud,R.M.
  TITLE     The structure of a ketoreductase determines the organization of the
            beta-carbon processing enzymes of modular polyketide synthases
  JOURNAL   Structure 14 (4), 737-748 (2006)
   PUBMED   16564177
REFERENCE   7  (residues 1 to 1070)
  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
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Keating,T.A. and Walsh,C.T.
  TITLE     Initiation, elongation, and termination strategies in polyketide
            and polypeptide antibiotic biosynthesis
  JOURNAL   Curr Opin Chem Biol 3 (5), 598-606 (1999)
   PUBMED   10508662
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10286311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1070
                     /product="type I polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="4.2.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016218 - polyketide synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=112989
     Region          <15..123
                     /region_name="Acyl_transf_1"
                     /note="Acyl transferase domain; cl08282"
                     /db_xref="CDD:471802"
     Region          190..352
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          470..917
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(670..671,673,694..697,722..725,749..751,772..773,
                     795..796,810,837..838)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(773,797,810,814)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          933..1018
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 mceaervrvr rvsvdyashs sqvealesel lgllegvear dsvvpfystv tgglvggael
       61 ggdywyrnlr ervcfrsavd avleqrfgvf vevsphpvlv pglvegfdea gvdavalgtl
      121 rrgeggwdrv vasvaeawvh gvevdwsslv pagprvdlpt ypfqrqrywl dsapmvatdv
      181 agaglnspdh pfltagvela dsdglvltgr lslksqpwla dhtvmgttll pgsafaelal
      241 yaadqvacfq ieelalqapl alpetgavdl qvnvsgpdgs grrsltiysk aadsvgsswt
      301 qhadgmlsqe eppapgelvv wppagadpvs ldglytrmte agvefgpafq glrqvwrrgd
      361 evyaevhlad qepgfgihpa lldsalhavg vgqffpgtaa grrpfawtgv slfatgastl
      421 rvrlalaged sisvqladht gapvaavesl vlratsseel rpvahqdaty hvdwttvalp
      481 qmptdppqki avigpvppda glpsysspaa laeamessga rlpekvlvtq dvdrllgare
      541 vretterlls lirtwltder faesqlvvtt tgavvtggmd pvidlnaapl wgllrsaqae
      601 npgrfvlldv dehvdswral paalvtgepq lalragvmrv prlarlqpta pkephawadp
      661 agnvlvtggt gglgalvarh lvlhhgvsrl llvsrqgpna sgatelrdel aeagaevtiv
      721 acdvadrdal grllhelpdd rpltavvhca gvfddglvss ltseqvdrvy rpkidavlnl
      781 hdltagldmt afvlfssvag tfggggqgny aaanafldaf ahyrraaglp atslvwglwe
      841 ertgmagrvg eahltrasgr gvmpmsaaeg larldagldt dqavvlpvql dlaalrakaa
      901 sgtvpallrg lvraparrvv gsgeqavgls qrlqglteae rrqelhglvk gqvaavlgyp
      961 dssavdpekp frelgfdslt avelrnrlsa vtglrlpvtv vfdyprldal vrlvherlfp
     1021 garpepsapa aglqpvadrs dqiktmdada liqlalgdgg dtaatdlgrg
//
LOCUS       WP_457656315             787 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 31 protein [Streptomyces griseus].
ACCESSION   WP_457656315
VERSION     WP_457656315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 787)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 787)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 787)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 787)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11605349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..787
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85111
     Region          160..285
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            196
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          268..712
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
ORIGIN      
        1 mdgrdlvrrv rlvgsvrglr tvrsawrrrs adaaalparg perarvpgal tgaepgpggg
       61 vvrfarselr irvsvggavf wawdgaeplp syavpgeapa pdpravlepd kdggwqvvse
      121 rltvvvsrtg avelrtpggl llrrelpprw wepvgggpvr wvqrsevpad arffglggra
      181 ggprlrdgvy glwntdpggr fgpeddplyl tmpvqvvvsd agthlafhdn swagrvvlre
      241 geegagsghd rpgtcevrme ggplrcwvva gtparvlqgw taltgapalp pswalgpqha
      301 rwgfggerev rrvvagyrer glplsvlhld idhfdghrvf tvdrerfpgl palakelred
      361 gvrlvsivdp avkaepgdav fdagrsvger gayvrdargr vvvgevwpga svypdftdpl
      421 vrdwwgslye erlaqgfsgv whdmnepvsf aafgdpslpr sarhalegag gdhreahnvy
      481 alamaragye gllrfrpeer pflfsrsgwa gmqryggtws gdvstgwpgl raslslvvgl
      541 glcgvpysgp dvggfdgfps pelyvrwfql gaylplfrth satgagrrep wefgpealea
      601 araalverer lrpyfvtlsh varltgapyv rplwwgapgd ralrecedaf llgdallvtp
      661 vlepgarrra vrlprgrwyd tvtgrayegp gqvlvdapls rvpvlaraga vvpvrgadgg
      721 pelevwapap grtggglvvr dpgdgwaeae veryvtrweg drvvverdga eggvdcpvrv
      781 rgvaees
//
LOCUS       WP_457656322             293 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656322
VERSION     WP_457656322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10142960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..293
                     /product="SDR family oxidoreductase"
                     /EC_number="1.6.5.2"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=30739
     Region          7..275
                     /region_name="TMR_SDR_a"
                     /note="triphenylmethane reductase (TMR)-like proteins,
                     NMRa-like, atypical (a) SDRs; cd05269"
                     /db_xref="CDD:187578"
     Site            order(10,12..15,35..36,39,52..55,73..76,140..142,170)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187578"
ORIGIN      
        1 migpltavtg asgavggrva rrlartgvpv rllgrdparl pdvpgadhap aapygdgeam
       61 rraldgahtl flvsahesps rvrehttaie aavavgveri vyvsfqgaap datftfardh
      121 wateahirta evrhtflrdn wylaglpamt gtdgvlrgpg gdgrvaavah ediadaaaav
      181 lldegtdhdg rvydltgpea ftlaeaaeel srvtgrpvvy vpetreeaya sragygaedw
      241 evagwvtsye aiaegelaav sdavptltgh patsfaeflv enpdsyrhll pgs
//
LOCUS       WP_457656324             390 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces griseus].
ACCESSION   WP_457656324
VERSION     WP_457656324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..390
                     /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=40406
     Region          17..360
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msglvariea atppgrdrav dalralailg vvgghwlvta lvadsgtvrg asplahlpel
       61 tpvswvfqtl avfflvggav aagswasark rgvsygawvg grlarlfrpv aavlvvwala
      121 aavmlvagvg estaralakl vwsplwfllv faaltaltpl varlhplwpl vvvlhvdlvr
      181 lglggprelg winvvagwlv pyclgalvar gglrgragrw gllsggasaa aglvlwagyp
      241 asmvgvpggr vsnldppsla avafglaqcg aallllgplr rvlrrpaawa vvavvnlsam
      301 tvflwhqtam iivtasvlll adgplpglht vpddvgwvva rllwlpvfal allgcwaafr
      361 gyeqggrrgg ggslvvresa perkgrarra
//
LOCUS       WP_457656329             347 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457656329
VERSION     WP_457656329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..347
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36715
     Region          6..335
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mgsgqpvavf gayghtgrfv taelaacgyv pvpsgrnaha leelalgqgw ksrvasvddp
       61 asldralagt vavincagpf asttgpviea alraeipyld vaaeleanld tfghyrerdr
      121 edgavivpam affgglgdll vtaamgdwtg adeahiayal sswhptagtr lsgavsrerr
      181 gdhrlryrgg rwerrtdaap alewtfpelv grrpvigeft madvvtvpqh laipdvttym
      241 saeaardfvs pdtqaptaad gsgrsdqtfl vdavvrsgdt erratasgqd iyavtaplva
      301 ealdrvltgr trslgvvpag eifdardflr alephitldl hpgrada
//
LOCUS       WP_457656330             442 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656330
VERSION     WP_457656330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  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 442)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..442
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=46832
     Region          183..426
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgavtssrav rlraavrrap ralyeevwaa padrvprmge pdapvwrpsl lvlliiaaac
       61 favprtnelv teasngvsgw avlaalaqsv vlvagmirpv gawwaatals vttvlvtepv
      121 mspdrlfpws vmgmvfqgga lfllalrvpl rratgalalt llagmaltlh qtqrhnldld
      181 rsapvfvval vlgaalrslr larkdlvvqa eltaeerarr tlleernria relhdvvahh
      241 msvisiqaqv aphlvehpte elrenlngir enalealael rrvlgvlrse dapaqsarha
      301 pqpdldgida llatvrsagl avtvsttgap rplspgvels ayrivqeals nvmrhapgas
      361 aevvighraa gltvrvvnsp perpatpsag vrhgllgmre raamlggela tgptpdggwe
      421 vtailpagtg ttepdttted tp
//
LOCUS       WP_457656335             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Streptomyces griseus].
ACCESSION   WP_457656335
VERSION     WP_457656335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33339
     Region          11..315
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mssrqskfpl pndgliaald iggtkiagal vdqdgvlihr arrttpares advllgavyd
       61 vlgslaaspl wervgavgig sagpidlahg tvspvnipaw rnfplaesva rhpdvghrqv
      121 tlagdavamt taehrhgaar ghrnalclvv stgvgaglvl ngsvhhwltg naghlghisi
      181 dfdgeacpcg argcleaias gtaitrhala lgwqapltad tagvaasaqa geaaavdafd
      241 ratralaagi aataalieid iavvgggvaq agevffeplt rhlrhyaamp flkelrivpa
      301 elgpdaglvg aavlasagds avpvmlghgs r
//
LOCUS       WP_457656343             516 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces griseus].
ACCESSION   WP_457656343
VERSION     WP_457656343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..516
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54477
     Region          128..516
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mghveipetd lsgpvglrga prprtaasrn rtaaleqlwr aptaqrdpar paparrrrap
       61 gtalaaltdl lglagpawll lragdqprpv aaaavaglmw aglrgargry adppgaepgg
      121 algavgdwlv ligllavlht aagspvdpat avvavapgll vaaavaglrr wplsgrrdhr
      181 vrrvllvgda agvdraaell nsrtdhdfsl vavvpvgaar leldgvqmpg rlascpaddd
      241 vstvlggvya haadlvlvap gpqltgdrlr rlgwglhdgg valsvlsels gvaaervrpv
      301 taagltllhi applrggpqa vfknvldrtg alfglltlap lllavalsvr lssrgpvfhr
      361 qvrqgqhnrp ftmwkfrtmv adaeelkaql aaanegdgpl fkmrgdprvt pvgrllrrts
      421 idelpqlfnv llghmslvgp rpplpeeasr yderehrrla vkpgltglwq vsgrsdlswq
      481 etvsldlwyv dnwsvaadlg llartvravt dgrgay
//
LOCUS       WP_457656336             437 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457656336
VERSION     WP_457656336.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..437
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46804
     Region          1..347
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrragvvlga ailvavtacs gqedaasgei aappsdpakv sggitvltnr tdqiadgslk
       61 kyaaefnkiy pgvkvkfegl tdyegetkir mntenygdvl lipnslsveq ypnffaplgs
      121 siklsaafdy tdhatvggkv yglanigvan gfvynkavwe kagikdwpat peefvadlat
      181 ikaktdavpy ytnykdgwpl tnwtnaigsp scdsgsydsl aktkepwssg sdlyeidkll
      241 ytvvekklse pdptttnwed skaqigsgki asmwlgswai sqmragaeaa gknpddiafm
      301 pfpakrdgay csvlrpdyqy avnahsenke aarawldwyi tksgqaaseg sissvkgapl
      361 pdtlkafsdn dvtmipqrqe nivdvnkidk aseigitaqg yrqklvdvar gaadgdmgsy
      421 fgelngkwae aqqalgg
//
LOCUS       WP_457656342             327 aa            linear   BCT 27-JAN-2026
DEFINITION  GDP-L-fucose synthase family protein [Streptomyces griseus].
ACCESSION   WP_457656342
VERSION     WP_457656342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35886
     Region          22..320
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(27,29..32,52,55..58,78..80,82,102,121..123,152,156,
                     179..180,182)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(99,123,152,156)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(123,152,181,200,217,225)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mttelpvppq estrsllrpg srifvaghrg lvgsavarrl addghevltr grdlldlrda
       61 artetylkev rpdvvvlaaa kvggimanst ypvqflednl riqlsviaga haagterllf
      121 lgssciyprl apqpiredal ltgeleptne ayalakiagi vqtrsyrrqy gasyisampt
      181 nlygpgdnfd letshvlpal irrfrearrd gapevtlwgs gsprreflhv ddlaaacvrl
      241 leaydgdepv nigcgedlti relaetvrdv tdyqgriewd tskpdgtprk lldvtrlssl
      301 gfkpqiplrd giartyawwl gqlpsgq
//
LOCUS       WP_457656348             487 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces griseus].
ACCESSION   WP_457656348
VERSION     WP_457656348.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Singh,R., Goyal,V.D., Kumar,A., Sabharwal,N.S. and Makde,R.D.
  TITLE     Crystal structures and biochemical analyses of intermediate
            cleavage peptidase: role of dynamics in enzymatic function
  JOURNAL   FEBS Lett 593 (4), 443-454 (2019)
   PUBMED   30582634
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Wilk,P., Uehlein,M., Piwowarczyk,R., Dobbek,H., Mueller,U. and
            Weiss,M.S.
  TITLE     Structural basis for prolidase deficiency disease mechanisms
  JOURNAL   FEBS J 285 (18), 3422-3441 (2018)
   PUBMED   30066404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..487
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53414
     Region          51..192
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          223..469
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(286,303,315,399,430,454)
                     /site_type="active"
                     /db_xref="CDD:238520"
ORIGIN      
        1 msdarqgqav adepdenrar knglygevss elaenmrqgw adterhdlap vaqaaytahr
       61 raalsarfpg ellvvpagnp kvrandtnyp frpssdyvhl tgdqsqdsvl vlepgpggeh
      121 raiayllprs drengefwrd yhgelwdgrr nsltenerll glpcrdvrtl terlatasgp
      181 vrllrgydag vdaalhdrvt aerdaefrat lselrlikda feiadlreac ratvrgfedv
      241 vralgtdtpt pervvegtfw mrariegndv gyasvcaagp hattlhwgrn dgearpgell
      301 lidagvesrn lytadvtrtl pvdgrftpvq rrvydavyaa qsagvaavrp gakyrdfhha
      361 aqrvlaehla swglfggrsv deayglglhr rwtlagtghm lgldvhdcak artelyvdgt
      421 laagmvltve pglyfqpddl tvpeelrgig vrieddflvt edgsenlsag lpraadevea
      481 wmarlrg
//
LOCUS       WP_457656346             527 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces griseus].
ACCESSION   WP_457656346
VERSION     WP_457656346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..527
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56486
     Region          26..509
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgakgpegr aapdsshddd algelgykpe lrrtlgnfht faagisyisi ltgtfqlfyf
       61 gvsfggpayw wswpmvfcgq lmvalcfcel aarypvagsv ynwakkmggp hvgwlggwmm
      121 mtatmvtlsa valayqitlp qiddwfqfvg dgsgkndqaa navllgtvli lfstlvnafg
      181 vklmarinsa gvfieliaav aliiflaahi trgpstalte tyglgsgqsl gyfgafltas
      241 lasayvmygf dtasslgees hnpgrnapra ilraliasfl igafillfal lsvpdlhaee
      301 lstgglqyvv latlgdtvge iflwavvvai tvcvlavqaa girlmfamar dnnlpagskl
      361 arvsprfktp vvpavligvv gvvilvvnin qpqifsvits iaiimiyvay llvtvpmllr
      421 rlrggwepre gafslgrwgl pvtvlavlwg tamslnlawp raevynatgp qhwylrwgaf
      481 lfigvvalgg fayywfvqrh rtgvlaehrf eaqddptapt tpppsag
//
LOCUS       WP_457656347             486 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces griseus].
ACCESSION   WP_457656347
VERSION     WP_457656347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659804
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..486
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51910
     Region          58..193
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          222..469
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cl00279"
                     /db_xref="CDD:469704"
     Site            order(287,304,316,399,430,454)
                     /site_type="active"
                     /db_xref="CDD:238517"
ORIGIN      
        1 mtgghaveqr dgsrgarshd rqapavvaev frqgwadtgr rlppvsgaas aakrraavse
       61 rfpgerivvp agglrtrsnd fdyafrphsa fihltaeqgt savpdsvllf epagsghevt
      121 lftrprsprd agpsgsefys dpqhgefwvg rrrtlretad algveaaard gleralgggv
      181 ptrvvrgtda fvdalvppsa padaellsfl selrlvkdaw eieqlraavg htvagfrdgv
      241 gelpratrla rgerwvegtf nrrarlegyg lgfetiaaag ahacvlhwmh ndgpvregel
      301 llldagvead sfytgdvtrt lpvggrftdv qrrvydlvfa aqsagiaalr pgapygafhd
      361 aatrviaegl dawglrpggg aiphepdlyr rytvcgtghm lgldchdcaa arsgtypggv
      421 leeghvltve pglyfqpddl tlpeelrgig vrieddfvit aegalclssd lprgadgiea
      481 wmdasr
//
LOCUS       WP_457656349              81 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656349
VERSION     WP_457656349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10450557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..81
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9131
     Region          18..64
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
ORIGIN      
        1 mapdrprtkp aeerradlmd aaervfaerg idaarideit eragvaigtf ylhlssqrdl
       61 mlavqarfvd rlverqheav r
//
LOCUS       WP_457656357             780 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457656357
VERSION     WP_457656357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..780
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=80938
     Region          19..725
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 msevnrsapp svggwtrfvt arprlallaa lvitalavfa gsgvadrmgs ggwqapdaes
       61 tyatealare fpasqpnlll lvdsgsatvd dpavaaeaar lverleaeqg isgigsywgt
      121 qapalrsedg heaiiaarig gdektagetl driapdfage rgpvtvsigg pvavqhemqt
      181 iiqedllrae lialpvtlvl lvmvfgsava amlplgvgiv ailgtnavlr glteftdvsv
      241 famnlttalg lglaidyalf ivrrfreela ggadprtavg ttlrtagrtv lfsaltvavs
      301 lsamlvfpqy flrsfayagi avvllaaaaa lillpaalvl lghrinsldl rrllrrrkrd
      361 tstegdfagt gtganagaga spgrgwakla alvmrrapvf avvttvglll lglpflgvkf
      421 gtaddrqlpa gaqsrvvqeh irdgfpgspg gglevlaegq gspaeyadlk srieqlpgvl
      481 rvdgpvtads vayysvlpeg eavgeetqql vrdlravpsa ssldtsvtgt aavlvdskda
      541 iadrlpwala iivvvtlllv flltgsvlip lqavvlnals ltamfgavvw vfqdghlsgl
      601 laftstgdie ttlpvlmfcv afglsmdygv flisrikeey drtgdhehsv tfglrhtggl
      661 itaaavilav vmvaigtsrv tntkmlglgi alavlmdamv vrsllvpavm klmgrstwwa
      721 paplrafhrr fglsegdaap vgpaapetpg drggpggagp taeveeisga gaeiaeparr
//
LOCUS       WP_457656359             802 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces griseus].
ACCESSION   WP_457656359
VERSION     WP_457656359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..802
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82169
     Region          15..801
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mastaaadhp aadaseaelm iggmtcasca arvekklnrm dgvtatvnya tekarvtfge
       61 glelgdlvat vektgytarp vtrperkapa aaapaaeaap apnaeakaka kagteagaea
      121 etkpepepea eaeaeaapdg vaepdastes dslrqrlvvs avlavpvvll amipalqfds
      181 wqwlsltlaa pvvvwgglpf hraawtnakh gaatmdtlvs lgtlaafgws lwalflgdag
      241 mpgmrhgfdl tvsradatst iylevaagvi tfillgryle arakrksgaa lralmhlgak
      301 dvavlragre vrvpagelvv gdrfvvrpge kiatdgtvve gssavdasml tgesvpvevs
      361 agdtvtgatl naggrlvvea trvgadtqla rmarlvedaq ngkasaqrla drisavfvpi
      421 vialalatlg fwlgndaglt aaftaavavl iiacpcalgl atptalmvgt grgaqlgili
      481 kgpevlettr radtivldkt gtvttgrmtl qtthttdttt eaevlrlaga lehasehpia
      541 qaiataatda tgplptpddf anipglgvrg tveghavlvg rprlladaai plpaelseal
      601 aeagrhgrta vvvawdgear gvfgvadavk dssaeavael ralglrpvll tgdnravaea
      661 varevgidev haevlpedkv nvvkslqaeg rvvamvgdgv ndaaalatad lglamgtgtd
      721 aaieasdltl vrgdlkvtad airlsrrtla tirgnlfwaf gynvaalpla asgllnpmia
      781 gaamafssvf vvtnslrlra ft
//
LOCUS       WP_457656361             400 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656361
VERSION     WP_457656361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41614
     Region          <158..359
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgeltgpavm vlgalpslva agtlgwavac rrsvarrrfg rlarptavca vlslttsfal
       61 pqagsgwklv eaalllllva vvtrwsplre latalpaaal avtlwplplv tgesflesig
      121 igafwllpvv gavavgaypr rqelrrrrav aearsaqrlq lsrdlhdfva hdisgivvqa
      181 qaarfvaatd pshavlaler iekaglsala amdrtvrmlh gpeaaatepl pdlsrlpflv
      241 ddftaagate ayldlpptvt ealsreagsa ayrivvealt nirrhapgas ratvvftpta
      301 ttveievtnd rgageasarr gsrgglgipa ltehaqalgg tlsagphgdg gwrltavlpa
      361 dvpavlpadl pgvrpvalpk dlpvelpedq pgalpkektp
//
LOCUS       WP_457656362             477 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 76 protein [Streptomyces griseus].
ACCESSION   WP_457656362
VERSION     WP_457656362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Thompson,A.J., Speciale,G., Iglesias-Fernandez,J., Hakki,Z.,
            Belz,T., Cartmell,A., Spears,R.J., Chandler,E., Temple,M.J.,
            Stepper,J., Gilbert,H.J., Rovira,C., Williams,S.J. and Davies,G.J.
  TITLE     Evidence for a boat conformation at the transition state of GH76
            alpha-1,6-mannanases--key enzymes in bacterial and fungal
            mannoprotein metabolism
  JOURNAL   Angew Chem Int Ed Engl 54 (18), 5378-5382 (2015)
   PUBMED   25772148
  REMARK    Erratum:[Angew Chem Int Ed Engl. 2016 Feb 5;55(6):1949. doi:
            10.1002/anie.201511540. PMID: 26836331]
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008866
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..477
                     /product="glycoside hydrolase family 76 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50659
     Region          144..474
                     /region_name="COG4833"
                     /note="Predicted alpha-1,6-mannanase, GH76 family
                     [Carbohydrate transport and metabolism]"
                     /db_xref="CDD:443861"
ORIGIN      
        1 mlgalpavan pasaavpapg aaaevcnkhc dardpasata drvpvhasvh grsialhlsd
       61 ndvmgwasid egaagdetwl drsfdggrtw asgsklgata vpsgrtgwrs qmynvddwnt
      121 ggigalracg kagdrseiac tgwarvnwna gsrstaaata lmmnydrnsg kfagwwtsat
      181 altslidnir ishmpsytya isntyeklig aeggdftnsy lddtgwwgla wvaaydltge
      241 rryldtarkd adhmaaywtg tcgggvqwat dkpyknaitn elyiqlsaal hnriagdtty
      301 lrraedgwnw fkgsgminsg ntindglsen sdgtcsnngd ttwtynqgvi laalaelsra
      361 tgdasllgsa rtladastts sylnpggtlh epyepdsdct tdgdsfkgay arglgilnka
      421 lpdrpysayl drqadtahek nrnsldqyga hwagpltrtg ngcqhsaldl mnaaqds
//
LOCUS       WP_457656364             288 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656364
VERSION     WP_457656364.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30184
     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 vgghkqaida lpegltlvtg
       61 aelscrvdgv gmhllaylfd padtelerar elvrddrvpr aqemvrklra ldvpiaweqv
      121 ariagdgsvg rphvaaalve lgvvrtvsda ftpewlgngg rayaekhefd pfeavrlvka
      181 aggvtvfahp aaakrgavvp estiaalaea gldgvevdhm dhdepararl rgfardlgll
      241 ttgssdyhgs rktvelgact tdpeiygeit rratgafpvp gaggagrr
//
LOCUS       WP_457656365             194 aa            linear   BCT 27-JAN-2026
DEFINITION  suppressor of fused domain protein [Streptomyces griseus].
ACCESSION   WP_457656365
VERSION     WP_457656365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Das,D., Finn,R.D., Abdubek,P., Astakhova,T., Axelrod,H.L.,
            Bakolitsa,C., Cai,X., Carlton,D., Chen,C., Chiu,H.J., Chiu,M.,
            Clayton,T., Deller,M.C., Duan,L., Ellrott,K., Farr,C.L.,
            Feuerhelm,J., Grant,J.C., Grzechnik,A., Han,G.W., Jaroszewski,L.,
            Jin,K.K., Klock,H.E., Knuth,M.W., Kozbial,P., Krishna,S.S.,
            Kumar,A., Lam,W.W., Marciano,D., Miller,M.D., Morse,A.T.,
            Nigoghossian,E., Nopakun,A., Okach,L., Puckett,C., Reyes,R.,
            Tien,H.J., Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T.,
            Xu,Q., Yeh,A., Zhou,J., Hodgson,K.O., Wooley,J., Elsliger,M.A.,
            Deacon,A.M., Godzik,A., Lesley,S.A. and Wilson,I.A.
  TITLE     The crystal structure of a bacterial Sufu-like protein defines a
            novel group of bacterial proteins that are similar to the
            N-terminal domain of human Sufu
  JOURNAL   Protein Sci 19 (11), 2131-2140 (2010)
   PUBMED   20836087
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Merchant,M., Vajdos,F.F., Ultsch,M., Maun,H.R., Wendt,U.,
            Cannon,J., Desmarais,W., Lazarus,R.A., de Vos,A.M. and de
            Sauvage,F.J.
  TITLE     Suppressor of fused regulates Gli activity through a dual binding
            mechanism
  JOURNAL   Mol Cell Biol 24 (19), 8627-8641 (2004)
   PUBMED   15367681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="suppressor of fused domain protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /calculated_mol_wt=20663
     Region          29..189
                     /region_name="SUFU"
                     /note="Suppressor of fused protein (SUFU); pfam05076"
                     /db_xref="CDD:461543"
ORIGIN      
        1 maeilalvea rlisalgepd aradvtflgt drievlrfld gdivryatlg msgqpmadpt
       61 spladpvkgp raelilsvrg gladtdqvlr plavlaaspq veglivaaga sldlgeplwa
      121 gapftsvlva esgglvedle ldepmdpvrf lpllpmtrne aawkrvrgaq elqerwlthg
      181 tdlrdplrts vpld
//
LOCUS       WP_457656366             611 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457656366
VERSION     WP_457656366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..611
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=61209
     Region          319..610
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mddgkptgpq akwwsrpsaa gpaaedrtpa aedrepvaed rgpavedres aarsqipapv
       61 pvpaqpsdgs grpdehgrev pgprpsgqpl hepdeystpp yggpgpwapa ppvqrptpah
      121 gtvvppgagg pppqyapgpq apapaaappp qpapadafap pqgatpaggf tppparpada
      181 faapqpapnd afapppphph pgpaapaqqq htqwlqydpw gapgqpltrp gppegmepgg
      241 rkkrrggafm gvllltlvag gigggvgayi erngglttve lpqatrdsgd rapesvagia
      301 asalpsvvtl hvsgtaesgt gtgfvldgqg hiltnnhvva pagssgditv tfssgetasa
      361 elvgkdsgyd lavvrvrgvs glkplplgns dnvqvgdpvv aigapfdlsn tvtsgiisak
      421 qrpitaggek gdgsdisyvd alqtdapinp gnsggplvdt qahviginsa iraadsgrgp
      481 eaggqsgsig lgfaipinqg krvaeelist gkathpvigv tldmkytgdg akvgtkgadg
      541 tpavakdgpa dkagiksgdv itqvegqrvh sgeelivkir ahrpgddldl kltrggkert
      601 vtlklgsasg s
//
LOCUS       WP_457656370             958 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457656370
VERSION     WP_457656370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 958)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 958)
  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 958)
  AUTHORS   ter Beek,J., 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 958)
  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   6  (residues 1 to 958)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (residues 1 to 958)
  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   8  (residues 1 to 958)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   9  (residues 1 to 958)
  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   10 (residues 1 to 958)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   11 (residues 1 to 958)
  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 10156764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..958
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=104302
     Region          545..>772
                     /region_name="PBP1_ABC_transporter_LIVBP-like"
                     /note="periplasmic binding domain of ATP-binding cassette
                     transporter-like systems that belong to the type 1
                     periplasmic binding fold protein superfamily; cd06268"
                     /db_xref="CDD:380492"
     Site            651..652
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380492"
ORIGIN      
        1 marevwrdsa dneaasavfh lmqqlidryr vnrpvmplvv aqaadaaagp eidarvervv
       61 hqvhranelr rvpvrlldge gatpyeaald mvrtlsekpw etrentqykt fsfprsrllg
      121 aieqatatvv eqshgntsev reerileqls rlrwrsgrpr rgsrweslre svrpetfvga
      181 lfiallsvll geidwlltal vaavallgla vvglasraap pllwlrrasr wfattsslaa
      241 sstgypsdgw swfspsgswr viraraaava ervadagagd eharqfhlel rvqalledlr
      301 hnyrphsldw rrgkrtvppv vflpratqdn ggillinain nvrsrrsevd pllllaslpa
      361 seimrhtppl pperpgpgap sgssgarary erwvddlslg qspvaaatla wvlllplste
      421 klthehahaq lvthrvrrtw awwvmsrasi avvvvgsllg aflwaghwrd tychgpltdr
      481 ntdaiwageg ddrecvgvat apevlfargn dlelngagkg itferieqgi raenadiapg
      541 dayvtvvyag pltatgkdre atrkgleelt gvylqqravn ktvgrsvklr vltanggedm
      601 lrqltavrki ievarrdpsv vgvvglgrnt yesddatrll rdaglplvnt tnssgdlprr
      661 fpnyfglaat deeqtyalgl varqvakeld rphaivlsrg dhngdldryt aeqraagkem
      721 lrtsgfslgr dvsydlagga slnaplttic qaervpdaly fagrvedvpt lmaglsgttg
      781 csdrrmtvft gddltkgtfd dstsiaanvt lyhsslapld rgknlgfygd ayrtlralhp
      841 egevaalvsg rpayedelfa sgqtvisysa taalydaaar gdqrrsaaet watlhtvdln
      901 nmptgtisfs rakssvsdnv hglnivkvvr pgpsaertlv cgkpagvapp ltakdckp
//
LOCUS       WP_457656371             311 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease, partial [Streptomyces
            griseus].
ACCESSION   WP_457656371
VERSION     WP_457656371.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..311
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          45..308
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 agdgsravrp prrgrsvspr ghsgwtpwly llpalvllag llvypiyqlg lisfleytqa
       61 qvsggepttf qgfgnyatlf ndsqfwqvll atvlfaaacv vstlfvgcal avlltriral
      121 prlalmmaal gawatpaitg stvwvflfdp dfgpvnkvlg lgdfswtygr ysafalvlle
      181 vlwcsfpfvm vtvyagirai ptevleaasl dgasqwriwr timapmlkpi livvtiqsii
      241 wdfkvftqiy vmtngggiag qnlvlnvyay qkafassqys lgsaigvvml villavtlvy
      301 lrlvrrqgee l
//
LOCUS       WP_457656372             577 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces griseus].
ACCESSION   WP_457656372
VERSION     WP_457656372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..577
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62568
     Region          12..556
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mtpedrtatd tadpaalgli paprtltaap cgpyaldrgt plsaapgteg vahwlrtmlg
       61 aatglplpea ggtgaatdtg aaadtgagdg sgsagqgivl aldaalapea yrlavetdav
      121 rltggsaagv frgaqtlrql lgpdafrrap lapgrswqvp pvriedeprf gwrglmldvs
      181 rhflpkddvl ryldllaahk lnvfhfhltd dqgwrieikr hprltevgsw rartkyghra
      241 selwdetphg gfytqddire ivayaaerhi rvvpeidipg hsqaaisayp elgntdvidt
      301 ttlsvwdtwg vnpnvlaptd ttlrffegvl eevlelfpae tspfvhmggd ecpkdqwkes
      361 plaqariael gvkdedglqs wfirhfdawl targrrligw deilegglae gaavsswrgy
      421 aggiaaaeag hdvvmcpeqq vyldhrqdgg pdepmpigyv rtlenvyrfe pvppglseea
      481 arhilgtqan vwtevmqnra rvdyqvfprl aafaevawsa lpapadrdfa afdarmtahy
      541 arldalgvdy rppagpyprq qrpgilgrpl egeppvv
//
LOCUS       WP_457656374             786 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces griseus].
ACCESSION   WP_457656374
VERSION     WP_457656374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..786
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81916
     Region          40..778
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msgdaataan atstglprid alsggsgggp dqgqeqprmg lgaslpaada rartegtfpy
       61 aadlwaegll waavlrsphp harivsidts aaeempgvra vvthedvpgd snygrhvvdr
      121 pvfasdlvrh hgepiaavaa dhpdtarlaa aaiavryevl epvtdpekaf aaeplhpdgn
      181 lirhiplryg daeatgevvv eglyrigrqd papigaeagl avprpdggve iytastdpht
      241 drdliaacfg lepdrvkvvv tgvpgatgdr edpgfqiplg llalrtgcpv klaasreesf
      301 lghthrhptl lryrhhadte grlvkveaqi lldagayada sseslaaava facgpyvvph
      361 afiegwavrt nnppsghvrg egamqvcaay egqmdklaak lgidpaelrl rntlstgdil
      421 ptgqtvtcpa pvaellqavr dyplpalpkd apeddwllpg gpegagepga vrrgvgyglg
      481 mvhmlgaegt devstatvrv hdgvatvica avetgqgftt larqivqetl gveevhvaav
      541 dtdqppagpa thgrhtwvsg gaveraakmv rtqllqplah kfgmstellq iadgkitsyd
      601 gvlsttvtea ldgkelwata qcrphptepl desgqgdafv glafcavrav vdvdielgsv
      661 rvvemavaqd vgrvlnpaql airieagitq gigaaltenl rtarglirhp dltgyalpts
      721 ldapdirivk lveerdvvap fgakpasavp vvtapaavas avrsatgrpv nrlpirpqaa
      781 vatpkp
//
LOCUS       WP_457656378             454 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656378
VERSION     WP_457656378.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46141
     Region          11..393
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(17..18,21..22,25,57,112..113,115..117,120,142,
                     145..146,149,231,234..235,239..241,244,267,271,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mghrtplaat laansistag tsltligvpw fvlettgsag ragvvafcat lpivvaalig
       61 gpvidrigrr rvavvsdavc alaiaaipll hfagvldfwm lcalmalngf ahtpgntary
      121 vlipdlaeha gttlaraasl fdavsrgarm vgaalagvli afvgaesvll ldaatfglsa
      181 llvaagvrgi raaeprkaet pvsvraygte lregyahlfs nrlllsvvvm vmfmngldqg
      241 wyavllpvha eaelggatdi glltavfgag gltgallyga vghrfprrav ftacvilcga
      301 prylvaavtg ttlplavtml lggivggvln pilttviyer vpdrlrsrvs galtagcefa
      361 mplgglaagl lvegagatga lvamggiyfl atlsplvfps wrtlddqvve eagpvpgtpe
      421 aeeakesget gkpgdpsvpp rvsssapsrp tpgp
//
LOCUS       WP_457656379             445 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656379
VERSION     WP_457656379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  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 445)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..445
                     /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=48032
     Region          174..443
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtdrpqppsp ltgtgtgtdg ttapltriir dtldrlrafd rhrprawdta vtafwvvaav
       61 ldytsggwrt vahddvtape flvllmslgf slpllwrrth pvavlllmap vsvvniwtga
      121 vvqaallqli pvfqivlrss lrtvgsaall fvvpvlaggv ripaawgqev vsyvwglvfv
      181 vllgiavrtr reytealver ahrleherdq qarlaaaaer triaremhdi ighnlsvitg
      241 ladggayaar knperagqal eaigttsrqa laelrrllgv lrddhpdadr tpqptldela
      301 plidrvrrag lpvhlelngd plqasltpgr qltvyrviqe altntlkhat gptsatvtlt
      361 rsrthldthi tdtgtgaelg tsagttagtt tgtiavteea plpaqgimgm reraalydgt
      421 leagplpdhg gwqirlrlpl edthq
//
LOCUS       WP_457656386             546 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656386
VERSION     WP_457656386.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  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 546)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..546
                     /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=58806
     Region          151..374
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mvrvespptd reipvvrvvl lpvvlllgat aagsalvapa aripvavcga ittlvvavlt
       61 aalhrrrram rvqraeyeqr iaylehriqs hdaetvrltk dvmpaairrl rvgnspeevm
      121 rdivdadvan rhlpkalreq iyqvlevidn eearrdsaqr afvsvarrvq aivhrqasel
      181 remenhygrn pevfddllri dhgtaligrl adsiavlgga rpsrqwpkpv plfsvlrgam
      241 srileyqrvd lhsiakvaiv gtsvepliha caelldnatr ysppqtrvhv tavevqtgia
      301 ieiedggvsl seeararaen mlaqaqagin mndlgesprl gmavvgrlsr myqlqvslrq
      361 sayggvravl ivprdmittg papgiahgig atsrptssld msqlqhvvpp pgkrkpkpaa
      421 tgpvpsvaap vstgapaats rpavppaame ddvpvvtewt englpqrrsr graplgshnl
      481 pqqpppppap angfqpgpde gtdggrgeek ppglwleaft kavngvpqer khgedsddaw
      541 dkgdlk
//
LOCUS       WP_457656392             277 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457656392
VERSION     WP_457656392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..277
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=29126
     Region          <10..269
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mnrrrshrsa saedllntlq dltararrev efhqarvela qalqrdmlpa tlptlpglqa
       61 aaryaparhg ldiggdwydg fpladgalgf aigdvqghdv eaaafmgqvr iamraiagta
      121 sdpgevlgrt ndlllsvdsg lfatctfmrl dpttwelhsa raghvacvwa ttegrsgite
      181 dpggmplgie pgecypvtrr tldsdgaivl ltdgvvegps lliedglerv rqlvaahsga
      241 saaqladevl gaaevtghed daavlvlrha asgrgpq
//
LOCUS       WP_457656393             821 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces griseus].
ACCESSION   WP_457656393
VERSION     WP_457656393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 821)
  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   3  (residues 1 to 821)
  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   4  (residues 1 to 821)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..821
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=87438
     Region          37..261
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          251..693
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          704..817
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 masadegspa epgplpsgdg rgpastaada aaviagdgtv igwtrgaeal lgypaaevvg
       61 rsaarlltgp pdprrtaava arcragsgws glvplrnrdg rsldidvrat asfpiagqeg
      121 flvsgreltp hwtmsgsvld dfltrspvgm avldpelryl wlndtlerfg gvpreqrlgr
      181 rpgevlpgal aapierlmrq vlstgeavtd yeylgwswad phrrrayass ffpladaqdr
      241 rigigyvvld vtdrwnarrl lalvneagaa igstldvhrt aqeladfavp rfadfvfvdl
      301 letpfggdrp gaaapaeger pamrraglss vregcpeavv rvgeavdfvp pphdahflld
      361 gapvllpvld pdshgwtveq paraarlref glhslisvpm rardtvlglt tfmrsqnpvp
      421 fdeddvapar elvaraavcv dnarrytreh taalvlqrsl lphtlrggta ldvawsylpa
      481 dakdgvggdw fdviplsgar vglvigdvvg hgigaaatmg rlrtavqtla dmdlppdell
      541 arlddlvlrl seeepatgpv erggttvvga tclyavydpa sgcctmarag hpppvivtpd
      601 gavsfpdlps gpplglgglp fesqeielpe gsllglytdg liegtdkdme sgmgrlgrav
      661 srgglpledl cpavvkellp vpqpddiall larthilspe hlvswevpvd paavgetrak
      721 vsrqleawgl telsmtteli vselvtnair yasgpvrlrl lfqsaltcev sdasntsprl
      781 rharttdegg rglflvaqla hrwgtrytpr gkiiwaeqpl p
//
LOCUS       WP_457656397             142 aa            linear   BCT 27-JAN-2026
DEFINITION  NfeD family protein [Streptomyces griseus].
ACCESSION   WP_457656397
VERSION     WP_457656397.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..142
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14352
     Region          1..141
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mdidawvwwl igavglgipl vltampefgm favgavaasa vaalgggiva qvlvfvvvsv
       61 aliavvrpia arhraghtgq asgidalkgr qavvlervsa dggriklage vwsarsldad
      121 qvfepgsqvd vvdidgatav vm
//
LOCUS       WP_457656403             444 aa            linear   BCT 27-JAN-2026
DEFINITION  pseudouridine synthase [Streptomyces griseus].
ACCESSION   WP_457656403
VERSION     WP_457656403.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..444
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=47006
     Region          206..431
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrssgrnsgs gsggsgrsgg qggrpgqggg rgqggrdggg sfrqgqgggp ggrsggqggg
       61 grggsqggrp gapggrpgap ggrpggqggr pgsqdgrksf qggrdeqeqr prrprpeerr
      121 ydvgndapga rggedgprkg rgsaarggak ggpkpaqggn rggfrrggap srpreldaki
      181 eqrnrdryan kpdiklpkth pgaeqegerl qkvlaragmg srraceelie qsrvevngei
      241 vveqgmrvdv hkdeikvdgl tvaaqsylff alnkpagvvs smedpdgrqc lgdyvtnret
      301 rlfhvgrldt etegiimltn hgelahrlth pkygvkktyl aavqgplprd lgkrlkdgiq
      361 ledgyaradh frvventgkn ylvevtlheg rkhivrrmla eagfpverlv rtsfgpiplg
      421 dqksgwlrrl tntevgmlmr evgl
//
LOCUS       WP_457656407             252 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656407
VERSION     WP_457656407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27510
     Region          17..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgdqagpept vsvlqdlrll eaagahpdga saqqlaheag lsdltarrll helardgyld
       61 eldggafalh erelrsqpdv dalalqrirp llsslrdnls aaayltlyde geirvleivd
      121 sprapkvdvw vsfqeaghat algksvlrel deearanyls rhsligltpr tithreellr
      181 eldsapagpl sldrgeyarg ttcvavpvys gdqvgsigvs frsdrmyrtt evrtrlleaa
      241 lrvtrrltlp ec
//
LOCUS       WP_457656408             559 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457656408
VERSION     WP_457656408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..559
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58173
     Region          108..>306
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          460..554
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mnypvrrpal vtalalacav altsctagpa agpgraatap asadpasrpd lkpfygqrlr
       61 wtdcetegyv carltvprdy ddpgngrtfv lpvaraaagk perrigslvf npggpgaagv
      121 asleegmdes fgraardrfd ivafdprgvg asvpaltcta addeedgaee peaeenatgp
      181 aasegvvplh prtdeertaa dagaraaakd ceqhsggllr hvgtqdaard ldvlraalge
      241 reltylgwsy gtslgtayae lfprrvramv ldgaidpsld wsqrvlsqsa gfrrsvddya
      301 dhcaevagds cpadspdair alierlytra greplpvsed ssyaeyggmd atavldavsm
      361 amytpedqwe plsralaaad agdatglgal deeepaeegp aeekpapeds gvggpgdedv
      421 tpvdnegaal tavncldvph prdldaywdv lpraekaagv ygtagvtael tcrgwpsggr
      481 tphrvdadgv ppvlvvgttg dpstpyaeae slaeqfpggm lltyegmght aygrgdacvt
      541 ekvdaylvgl kpvrpgatc
//
LOCUS       WP_457656409             434 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457656409
VERSION     WP_457656409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  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..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /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=44640
     Region          54..426
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mcventppps grltrrgvla gaaalagtsa vlaqtapaas aaqassrgas grggdlvveg
       61 gtlldpltge vtedavvvit rgvvraagar nrlgtrvpsg vpvlrahgqw ilpglvdahi
      121 hlntaaeard avlkgatsar sgstnfyqdi avrelarqap eqaprlraag ifvtpdlgdt
      181 iladpdlapl arlrdgvrsp ealrrvvevn largadtvkt rvneraglpe qdplvqvydh
      241 eqlseivaaa rrggkgvlch sysekgchda vtagirsleh gafvgertlr dmrrrgtyft
      301 ptltaiagla espdpvlaer grtylpvlkr avlaahelgv plaagtdssg gtvdpigrev
      361 elmhaaglsa ldairtattg aakllgldat agrlargfag dvlvvdgnpl adlgalsrpa
      421 rvvragfpvp vpaa
//
LOCUS       WP_457656412             390 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces griseus].
ACCESSION   WP_457656412
VERSION     WP_457656412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..390
                     /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=43133
     Region          27..373
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtaptvpavp agpsvappaa akkpgrdryl dllrtialvr vviyhifgwa wltvlfpsmg
       61 vmfalagslm arslsrpalg virgrvrrll ppmwvfslvv vpmmfalswq pvkseglwwf
      121 vklawyvfpv gappfpwssg draglledtw avqaagplwy iraylwfvla splllrafrk
      181 lpwatllapl gltavigtgl vtipgetgna lsdfavfgsc wvlgfahhdg lfkdvprylt
      241 islasivmgf glwwasghlt adgwdlndip laqaawslgf cvillqyaps wqelpgrlar
      301 fdrlvtlann ravtiylwhn llilatvpli dllwkipyvd ahlgstveag ytllmtlliw
      361 pllalmivav gwvedvaarr rprlwpdgrr
//
LOCUS       WP_457656413             217 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656413
VERSION     WP_457656413.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23367
     Region          20..167
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 meyegelrmd rtgrydgsdv igsgglrlrr wreedlpall rayedpamhr wlatqvsgpd
       61 gaadwleaqr tgwasgtrfa favteggqed eplgnavlkr pdpvsdlaev gywttasarg
      121 rgvapralaa ltdwafttfa eqgltqlell hqvdneascr vaekcgypla rvipalppdy
      181 pldghvhare apaaalsrpa drrgeaagtd ggrasgr
//
LOCUS       WP_457656425             389 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces griseus].
ACCESSION   WP_457656425
VERSION     WP_457656425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..389
                     /product="trypsin-like serine 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=40911
     Region          145..>333
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mpssalaata vaavlaltat acgpeednag gtpsasaeqs sdgkvtipdd lknrlkehgi
       61 dpdkwrdgew knwdkdkwlr eakdfvnpii dglwdpdrmr eadkppenpv dndisgddgv
      121 tdptpapvqa agvatpyhdn apesgkllfd gpqgsmvcsa tvvkdpanpg ksnmvwtagh
      181 cvhagkkggw yrniafvpay nndglsldql etapkekiap ygvwwgqwaq tseqwieqga
      241 avggqgapyd favlhvtpek gsggksleet vgsalpvefn apavpqitdm tatgypaapp
      301 ydgqkllqck dkpgrlsvfq dqptmyrigc tmtggssggg wvaagqdgkp alvsntsigp
      361 vtagwlagpr lgkeaegiyr avsekyagq
//
LOCUS       WP_457656426             263 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656426
VERSION     WP_457656426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..263
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27946
     Region          100..245
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mppadasaet daapvdhgsa paagpgsaer sgsgagerda vedtldlklt eellaliaee
       61 rntgadrard rvpqellgdp gawppaatta gefallpvrp erdlpvlsrw mndpavaafw
      121 elagpesvta dhlgpqlegd grsipclgvl dgtpmsywei yradldplar hyparphdtg
      181 ihlliggvnn rgrgvgttli ravadlvldn lprcgrvvae pdlrntpsvs aflsagfrfs
      241 aevdlpdkra almirdrtyr dql
//
LOCUS       WP_457656427             643 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces griseus].
ACCESSION   WP_457656427
VERSION     WP_457656427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..643
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=71243
     Region          22..637
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mptypasrds aespqlfspp eldrqiwdra aarllakmlg efayekiiep vpgpgtdglh
       61 rltlddggvl afaarrgvyg swrvdpdsie itarppaaap tdapsngtpa ttgsvdapsn
      121 gsatatgprp frdpltflar arellgldgt tlghlirelt rtlsadarld htalaadrla
      181 aldyaelegh qtghpwlvas kgrlgfsaad aarftpetrs plrlpwiavs triaqyrgvg
      241 rlttpgrlya geldrdvqda faeelrsrgh dprdylylpv hpwqwdewiv plfapaiadg
      301 divalhtdgd arlpqqsirt fanvdrperh tvklplsiln tlvwrglpte rtlaapavta
      361 wvqglcegdp flrdtcrvvl lgevasvave hplydhlpea pyqykellga iwreplpprl
      421 apgerartla sllhtdpagr aftaelaers glspetwlkr lfaallppll hflyrygtvf
      481 sphgenaivv fdendvpvrl aikdfvddvn isahplpehd ampeevravl lteepsfltq
      541 fihsglfvgv frylsplcee qlgvsedtfw slvraeivrh hgrfpelker felfdmltpe
      601 ierlclnrnr lhvdgyrdra srphaaihgt vpnplhpsar ire
//
LOCUS       WP_457656428             656 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase [Streptomyces griseus].
ACCESSION   WP_457656428
VERSION     WP_457656428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..656
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=70102
     Region          18..635
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtkpslpell haavtavggt erpgqvtmae avaeavddqs hllvqagtgt gkslgylvpa
       61 lahgervvva tatlalqrql verdlprtve slhpllrrrp qfamlkgrsn ylclhrlheg
      121 vpqdeeeglf dqfeaaapss klgqdllrlr dwsdetetgd rddltpgvsd rawaqisvss
      181 reclgatkca ygaecfaeaa rerakladvv vtnhallaid aiegapvlps hevlivdeah
      241 elvsrvtgva tgeltpaqvn ravrraaklv nekaadalqt aaegfervme lalpgrleev
      301 pedlgyalma lrdaartvis aigatrdksv edenavrkqa lasvesihgv aeritqgsey
      361 dvvwyeqddr fgasvrvapl svsgllrekl faersvvlts atlklggdfn gvgaslglap
      421 egtagedvpq wkgldvgspf dypkqgilyv arhlntpgre gsrtdmldel aelveaaggr
      481 tlglfssmrg akaaaeelrg rldkpillqg eetlgelikn faadpetclf gtlslwqgvd
      541 vpgpscqlvv mdripfprpd dplmsarqka veeaggngfm avaathaall maqgagrlvr
      601 atgdkgvvav ldprlanary gsylraslpd fwyttdrnqa rrslaaidak akadda
//
LOCUS       WP_457656432             311 aa            linear   BCT 27-JAN-2026
DEFINITION  1-aminocyclopropane-1-carboxylate deaminase/D-cysteine
            desulfhydrase [Streptomyces griseus].
ACCESSION   WP_457656432
VERSION     WP_457656432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Thibodeaux,C.J. and Liu,H.W.
  TITLE     Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase:
            characterization of an unusual pyridoxal 5'-phosphate-dependent
            reaction
  JOURNAL   Biochemistry 50 (11), 1950-1962 (2011)
   PUBMED   21244019
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Nagasawa,T., Ishii,T., Kumagai,H. and Yamada,H.
  TITLE     D-Cysteine desulfhydrase of Escherichia coli. Purification and
            characterization
  JOURNAL   Eur J Biochem 153 (3), 541-551 (1985)
   PUBMED   3908101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32323
     Region          17..299
                     /region_name="Acd"
                     /note="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase, PLP-dependent ACC
                     family [Amino acid transport and metabolism]; COG2515"
                     /db_xref="CDD:442005"
ORIGIN      
        1 mnsppdrpsr ldallrprvp splpavqher farhgvtlll krddlihpdl pgnkwrklvl
       61 nleaaagrpv ltfggaysnh lrataaagrl lgfptigvvr gdelahrpln pslarcaadg
      121 mrlhfvdrtt yrakaspevl agllsrygdv evipeggsna laaqgctalg relageadva
      181 avacgtggtl aglaaglapg qralgvpvvg ggflagever lqreafggpa gswtlderfa
      241 fggyarstpe laafaadfed rhglpvervy vakllfaltv laeegafapg srvaavitga
      301 paplqessvs r
//
LOCUS       WP_457656434             509 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces griseus].
ACCESSION   WP_457656434
VERSION     WP_457656434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..509
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52542
     Region          18..>372
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mttlvsttdt vtrdalavlq pgftgttapd wllrrvgegl asvglfgrni tspeqltalt
       61 grlrserddv lvaideeggd vtrlevthgs sfpgnfalgs vddvhltrav aqelgrrlae
      121 cgvnlnwaps advnsnpgnp vigvrsfgad trlaarhtaa yieglqaagv aactkhfpgh
      181 gdtavdshla lpridvdldt lharelvpfr aaiaagsksv msahillpal dpdrpatlsp
      241 qiltgllrqe lgydglivtd avemdaiagt ygiergsvla laagadaicv gggladeetv
      301 lrlrdalvaa vrsgelteer ladaaarvra laswtqrarg dvpepgaavq egtapgtgvs
      361 sdiglvaarr avrvtgsgdr lteaayvasf savaniavgd etpwgiaael drilpgtgtd
      421 tyteeteava dailaaager rivavvrdeh rhawmgaald allaarpdtv vvemglpqsd
      481 prgalyiath gaarvcgtaa aealtsska
//
LOCUS       WP_457656442             432 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656442
VERSION     WP_457656442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44875
     Region          18..413
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(29..30,33..34,37,72,119..120,122..124,127,151,
                     154..155,158,244,247..248,251..253,256,287,291,343..344,
                     348,352,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mapstslrsv rparvhrawl maavagaaiv tagafttvpg llvtplheey awergqiala
       61 asvnmvlfgl tapfaaalmd rigarrvvvg alllvaagal ltgvmtrpwq lvaywgvlig
      121 lgsgcltmtf aagvtarwfd rrrglvtgal gsashlgqll flpllawsvd rfgwrppvvt
      181 lalvalavaa avflllrdhp adagvkpyga pefvprpapa pgaamrtlkv laraartgpf
      241 wllagmfalc gastngimws nwapaahdhg mrataaasll slvgvfsalg avlggwltdr
      301 fdprrlltvc favraltlla lplvfassvt apmllfvavy glvdvatvpp vielarrvyg
      361 adgpvvfgwt naahqlgaga saflgatard vfgtydvvwa alaagclvaa llapavrvra
      421 hrpalrepgg lp
//
LOCUS       WP_457656444             332 aa            linear   BCT 27-JAN-2026
DEFINITION  sporulation protein [Streptomyces griseus].
ACCESSION   WP_457656444
VERSION     WP_457656444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Sonoda,Y., Mizutani,K. and Mikami,B.
  TITLE     Structure of Spo0M, a sporulation-control protein from Bacillus
            subtilis
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 12), 1488-1497 (2015)
   PUBMED   26625291
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Han,W.D., Kawamoto,S., Hosoya,Y., Fujita,M., Sadaie,Y., Suzuki,K.,
            Ohashi,Y., Kawamura,F. and Ochi,K.
  TITLE     A novel sporulation-control gene (spo0M) of Bacillus subtilis with
            a sigmaH-regulated promoter
  JOURNAL   Gene 217 (1-2), 31-40 (1998)
   PUBMED   9795118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="sporulation protein"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /calculated_mol_wt=34487
     Region          1..255
                     /region_name="Spo0M"
                     /note="Stage 0 sporulation-control protein Spo0M [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG4326"
                     /db_xref="CDD:443467"
ORIGIN      
        1 mvfkkllgal gvggpsvdtv lepgpalpgg llsgevrlrg ggtevsvdri slflvarver
       61 edqeeehegt vvlerftvgg gfrlaeeaeh tvpfsltlpw etpitelhgq plgpvlgirt
      121 eleiagardr gdldplavgp lpaqeailea fgqlgyafks adlelghirg tgqqlpcyqe
      181 ieilppagha havneievtf laapgglevv ieadkraglf seghdtvhrf tashhavpqt
      241 ewnarvdawl keviaghagh gapspygtps sygehhgdqh rsgpgagavv agvaagvavg
      301 vvggmvaaev vdeigdvfed eegdedaggd eg
//
LOCUS       WP_457656447              66 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces griseus].
ACCESSION   WP_457656447
VERSION     WP_457656447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..66
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6906
     Region          1..57
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mrisvnrdlc igsgncarma peifdqddng lvtllvtdpg aayarvrqas ticpvgavnl
       61 sqresv
//
LOCUS       WP_457656448             401 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces griseus].
ACCESSION   WP_457656448
VERSION     WP_457656448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 401)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44259
     Region          22..401
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(68,88,90..91,174..175,183..184,187,190..191,194,230,
                     233..234,237..239,242,285,287..290,314,391)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(89..90,97,101,108,153,156,234..235,238..239,
                     242..243,246,284..285,288..289,291,314,342..344,347..348,
                     350..352,355..356)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 magevengtl efpirrgcpf kppveydvfr eseaptqvrl yngkpawvit rfadaravlg
       61 derfssditn pgypifaeal epmrrtptlv tmdapdhtrl rrlviseftm rrmntlrpqi
      121 qevadrlidr mlqleqpvnl aeaysfplag gvigsllgls ldtiegfmsd arkatvvrdl
      181 qefvriqrgl refilagiee rertpiddvl snivakykat gaesydelvt lilvitgagy
      241 gptasmistg vmallehpdq leilranpsl fpdaveetlr fvsvsdlssm rvatedveig
      301 gqliragdgv vvpngganhd psafsdpaal dvrrqearqh lafghgihqc lggnltriel
      361 eiayrtlftr iptlrlavpa seidspekaq lpeihhlpva w
//
LOCUS       WP_457656449             281 aa            linear   BCT 27-JAN-2026
DEFINITION  arylamine N-acetyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656449
VERSION     WP_457656449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30915
     Region          15..271
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mvttahnase wgiekvdvpa yldrigytgp tgptletltg lqrahmlsmp fenldilfgd
       61 gisldlesiq dkmvnrgrgg ychehnllfa avlerigftl trllcrirlg stdvqsrshs
      121 vlivelgerr ylsdagygcl gplepieiad gtvslqdgwe yrikregavt vlqmlnngsw
      181 idslgfdttl fhpvdfqman ylsstyprsp mvtgffaqrv vsteagpvrk alfganiqdf
      241 ttegiadqra lstkaemvsa lrdvigirla deeikkieai d
//
LOCUS       WP_457656454             409 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656454
VERSION     WP_457656454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40611
     Region          19..385
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(29..30,33..34,37,69,119..120,122..124,127,146,
                     149..150,153,221,224..225,228..230,233,261,265,314..315,
                     319,323,338,341..342,345..346,349)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtndptvtvc sapqvkrari avaavftvhg avtgsfatrv pwiqdhagvs agqlglalaf
       61 paigasiamp lagrishrfg artalrgllt lwtlalilpa lapslvtlca alfvygatag
      121 msdvamnalg vevenrldks imsglhgmws vgaligsaag tvaahtgtda rlhhlvaava
      181 ltvlgliacr gvldlqsape eeppprftlp pksalvigai gfcavfaega sldwsavylr
      241 dvldssdgla aasttafalt mavariagdr ivdrfgavrt vrtggllata ggllvvfspd
      301 paaamcgfgl lglgvavvvp lafaaagrsg pnpsqaiagv atitytsgli apsaigslae
      361 atslvvsfgv vtalafglvl gagvlrsadr kvtgsavggg tttksatgs
//
LOCUS       WP_457656456             564 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces griseus].
ACCESSION   WP_457656456
VERSION     WP_457656456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..564
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62675
     Region          48..540
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtstvpnavq htdaaappit mfgpdfpyay ddflahpagl gqipatehgq evavigggls
       61 giiaayelmk mglkpvvyea dqiggrlrtv gfdgcdgdlt aemgamrfpp sstalqhyid
      121 lvgletrpfp nplspatpst vvdlkgeshy aetiddlpqv yrdvaeawna cleegadfsd
      181 mnralrerdv prireiwaql verldnqtfy gflceseafk sfrhreifgq vgfgtggwdt
      241 dfpnsileil rvvyteaddh hrgivggsqq lplrlwdrep qkivhwplgt slsslhggep
      301 rgavtrltrt agnritvtda tgdirtfraa vftgqswlll skidcddalf pidhwtamer
      361 thymessklf vpvdrpfwld kdeltgrdtm smtltdrmtr gtylldegpd rpaviclsyt
      421 wcddslkwlp lspkermdvm lkslgeiypn vdirshiign pvtvswenep yfmgafkanl
      481 pghyryqrrl fthfmqdklp adkrglflag ddiswtagwa egavqtalna vwgvmhqfgg
      541 atdatnpgpg dvfdeiapve lped
//
LOCUS       WP_457656457             101 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656457
VERSION     WP_457656457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..101
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11514
     Region          4..90
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mgtrvadnpd esryeifdgd eragfveyhr frdeiaflht eidphfggrg lggtlarsvl
       61 dearkqeltv lpfcpfirgw lrkhpeytdl vpeaqharfg l
//
LOCUS       WP_457656459             258 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            griseus].
ACCESSION   WP_457656459
VERSION     WP_457656459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..258
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27635
     Region          6..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mtkrsaeerr rliadhvveq gtvtgaalar ltgvslmtvh rdlddlarqg vlrrfrggas
       61 alpstvfess ldyrlgvnta eknavaraaa elvepgmsvm lddsttvlvm agllvdlapl
      121 tvvtnarrvl dvftdregir lialggeysr thdsflgmpc veavealsvd lvavstsald
      181 artayhqeqd vvlvkramlt saatkvmlmd htklartalh rvgpvadldh lvvddgadae
      241 llgklrertq vtvaavaw
//
LOCUS       WP_457656461             149 aa            linear   BCT 27-JAN-2026
DEFINITION  Rieske (2Fe-2S) protein [Streptomyces griseus].
ACCESSION   WP_457656461
VERSION     WP_457656461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Schneider,D. and Schmidt,C.L.
  TITLE     Multiple Rieske proteins in prokaryotes: where and why?
  JOURNAL   Biochim Biophys Acta 1710 (1), 1-12 (2005)
   PUBMED   16271700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..149
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=14246
     Region          56..144
                     /region_name="Rieske"
                     /note="Rieske domain; a [2Fe-2S] cluster binding domain
                     commonly found in Rieske non-heme iron oxygenase (RO)
                     systems such as naphthalene and biphenyl dioxygenases, as
                     well as in plant/cyanobacterial chloroplast b6f and
                     mitochondrial cytochrome bc(1) complexes; cd03467"
                     /db_xref="CDD:239550"
     Site            order(94,96..97,111,113..114,116,118)
                     /site_type="other"
                     /note="iron-sulfur cluster [ion binding]"
                     /db_xref="CDD:239550"
     Site            order(94,96..97,111,114,116)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239550"
ORIGIN      
        1 mnarrrtvla agaagaaala tgcgssdegg ggdtsgtpta sdgasdgasp gasdgvelaa
       61 tgdipvgggt vfkerkvavt qpeegefkaf savcthascl vstvsdgtin cpchgsrfsi
      121 tdaaveagpa prplpaeris vsggtirlg
//
LOCUS       WP_457656462             218 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656462
VERSION     WP_457656462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..218
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22834
     Region          28..212
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msdatgaptl rgaavgrsig iglmyglfkp rvlgawrvpa agpvilavnh shnidgpmlm
       61 gtaprpvhfl ikkeafvgpl dpflhgigqi evdrttvdrt aishalgvle dggvlgifpe
      121 gtrgegdfas lraglayfav rggapivpva vlgsterrgr lirglpplrs rvdvvfgdaf
      181 dasagdgrrt rkaldeatlr iqarltahle gakrltgr
//
LOCUS       WP_457656468             206 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces griseus].
ACCESSION   WP_457656468
VERSION     WP_457656468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..206
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22488
     Region          4..196
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mrelilirhg etewsrsgqh tswtdlpltd ggerqaralv plladrhigl tlvspmirar
       61 rtaelaglae prvtpelrew dyggyegvtt reirrtrpfw nlwtdgvdpg sdehpgespa
      121 qigqradqvl agvrsaaeev addedialva hshflrvlta rylgltpaeg rlfqlatgav
      181 srlgtehgrp vvvalnvalp eslqga
//
LOCUS       WP_457656470             313 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces griseus].
ACCESSION   WP_457656470
VERSION     WP_457656470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..313
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=31364
     Region          38..291
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mstptgpasg lpvrmprprq sgrhrrpepv vapegaaalv lavpgtpssa trslaeevis
       61 iarselpgln arigyldgdd aeyptlatvl aqtaaervar feqavaagre vaepsgppav
      121 vvpllagpds alirrirqav mdsgtqaelt dvlgphplla ealhvrlsea glaradrarl
      181 ftvataadgi vlatvggeea vqaagitgml laarlavpvm aaaldvegsv asiaeqlqgs
      241 gsaqlalapy lvgpevdpgl ldaaakeagc ataeplgayp aigklvlsly atalgitpat
      301 pqgtqgaqga qah
//
LOCUS       WP_457656471             386 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces griseus].
ACCESSION   WP_457656471
VERSION     WP_457656471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..386
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37988
     Region          20..341
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mthppaspta agpaagpgay vigvdsggsg lrvalgrvgl pgplattvca epvrtgpggi
       61 daghlldqll paarellera aessadgtpa gedeapvgev aalaigaagm atlgerlrae
      121 lpgaladalg vrrlalaada vtayagavgq rpgavvaggt gmialgtdlm ewhradgwgh
      181 llgdsgggaw igragldaam rahdgrrggs palldrlrav fgpadelpgl lyprsdrpav
      241 lasfapevaa cagadpvaag ilraaaghia eaaaavcpta arpaaaepdd ggdelgegge
      301 valtgglfrm gepllaplre elahllpgar vtsaegdplt galriarala agdlclprhp
      361 tmlfvpleha tgqrggtaar deprsg
//
LOCUS       WP_457656472             417 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite oxidase [Streptomyces griseus].
ACCESSION   WP_457656472
VERSION     WP_457656472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Hsiao,J.C., McGrath,A.P., Kielmann,L., Kalimuthu,P., Darain,F.,
            Bernhardt,P.V., Harmer,J., Lee,M., Meyers,K., Maher,M.J. and
            Kappler,U.
  TITLE     The central active site arginine in sulfite oxidizing enzymes
            alters kinetic properties by controlling electron transfer and
            redox interactions
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (1), 19-27 (2018)
   PUBMED   28986298
REFERENCE   2  (residues 1 to 417)
  AUTHORS   McGrath,A.P., Laming,E.L., Casas Garcia,G.P., Kvansakul,M.,
            Guss,J.M., Trewhella,J., Calmes,B., Bernhardt,P.V., Hanson,G.R.,
            Kappler,U. and Maher,M.J.
  TITLE     Structural basis of interprotein electron transfer in bacterial
            sulfite oxidation
  JOURNAL   Elife 4, e09066 (2015)
   PUBMED   26687009
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Barber,M.J. and Neame,P.J.
  TITLE     A conserved cysteine in molybdenum oxotransferases
  JOURNAL   J Biol Chem 265 (34), 20912-20915 (1990)
   PUBMED   2249998
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Campbell,W.H. and Kinghorn,K.R.
  TITLE     Functional domains of assimilatory nitrate reductases and nitrite
            reductases
  JOURNAL   Trends Biochem Sci 15 (8), 315-319 (1990)
   PUBMED   2204158
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Neame,P.J. and Barber,M.J.
  TITLE     Conserved domains in molybdenum hydroxylases. The amino acid
            sequence of chicken hepatic sulfite oxidase
  JOURNAL   J Biol Chem 264 (35), 20894-20901 (1989)
   PUBMED   2687265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..417
                     /product="sulfite oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45111
     Region          96..416
                     /region_name="SO_family_Moco_dimer"
                     /note="Subgroup of sulfite oxidase (SO) family
                     molybdopterin binding domains that contains conserved
                     dimerization domain. This molybdopterin cofactor (Moco)
                     binding domain is found in a variety of oxidoreductases,
                     main members of this family are nitrate...; cd02110"
                     /db_xref="CDD:239028"
     Site            order(97..98,100,102,148,216,247,252,260,263,265..266)
                     /site_type="active"
                     /note="Moco binding site [active]"
                     /db_xref="CDD:239028"
     Site            148
                     /site_type="other"
                     /note="metal coordination site [ion binding]"
                     /db_xref="CDD:239028"
     Site            order(305,335,339,341,350,352,384,389..391,395,411)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239028"
ORIGIN      
        1 mspvpteday drirmrqwsr grarsagier rdllklvaaa saavplasva aparaadglp
       61 gvvkplppel ftlrgtnaet nfgalrdtgl ltpadrffvr nhtatpridr agwkltvwgd
      121 glrgdpvdft fadllalppv trtafvecag ngrsyftsqq gqpvsgtawt lgaigtarwr
      181 gvrladvlrr agigrhavdv lprgldaevv tdgvnlgrvr rplpvakald dvllayemng
      241 eplppdhghp vrlivpswvg ianikwvgdi evsaeplltp wntglyrlfg pgyppegsap
      301 ltrqtlksaf elapgasfra hrralltgrs wsggapvrav evstdggthw rtarlrdepr
      361 agswvrwtad wvprergpav llarasdrsg rrqpvttahn tqgylfdavv rhpvtvv
//
LOCUS       WP_457656476             249 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457656476
VERSION     WP_457656476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>249
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Site            order(1..2,13,16,20..21)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          <2..45
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          72..249
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meeaaerigg dkpkisrqen grqgvsklei eallalygvs derlrtaltt laregrrkgw
       61 waqysdilpa gfqerlsmes daariltfqp mlvpgllqtv eyatevirsv dkgvteeerd
      121 syievrkarq eiftrdnppq yvclldeavl rrevggpavm aaqldkilev nnpprltiqv
      181 vpfsqgwhag adgafniysy pdpmdldvvn ldyldgalyl eedqpvgryq lafdelraaa
      241 lasrqsmel
//
LOCUS       WP_457656477             138 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656477
VERSION     WP_457656477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..138
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15140
     Region          15..>103
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mapaieldpp dyrqelvarp etlaimrriv sahldlwdlr elsdaatlca helltnvmrh
       61 tgsplctitl rrrpdgvrvt vsdsdtappe rrepdwsees grgalliaal aaqcgtvmrq
      121 dgkdvwadir aatpayar
//
LOCUS       WP_457656483             344 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656483
VERSION     WP_457656483.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..344
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34837
     Region          6..343
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msgafvlrag plslratrrs vlvcgllsva lvalavwaft lgsyqlslgd lsavlsgtar
       61 nsvrtvvlew raprivaavl fgaalamgga ifqsltrnpl gspdvigftt gsytgvvltl
      121 lagassysal avgaltgglv tafavyllaf rrgvrgfrli ivgiavgall ssvntwfsvk
      181 advdtalraa vwgagslsai gwpavlmssg liavvalvap vaqrrmrwle lgddtaamlg
      241 vrvertklll vvlgvaataa vtaaagpivf valaapqiar rltgrgtsvd lagsalvgal
      301 lllgadiaaq haipgvvlpt gavtvcvgga yllvllvres rrgf
//
LOCUS       WP_457656485             451 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein, partial [Streptomyces griseus].
ACCESSION   WP_457656485
VERSION     WP_457656485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>451
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          27..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maaqraytth plvlrrvtvr rveevtprmr rvvlggedla aftrdgidhp gfaapgfddh
       61 vklilaadgn iraalpaqlp hgiewtpaeh rvtrdytprr vdlrtgelhl dfvvhgegpa
      121 eawsasareg delwfvgpks slrlperldw ifligdetal paigrflder pldatahvlv
      181 tvsddaarqe lalrdgdtvt wvhaepgdaa aleaavralp vpagegyawa aaesrallpv
      241 rrylqrerkl akdrvnitgy whreeatape aegaaetgaa aqspagipsp lpwlvaraal
      301 qlgvvdavad apglsagtla arlgvpgpgi dvllpllaty gvvtggdegl rlgpageell
      361 edhereeyag heaelllala rfapalrsgt spwrlasgat lhetvtrdae rygelveece
      421 qlvfllnglt adslwadves clltgpgsas v
//
LOCUS       WP_457656488             211 aa            linear   BCT 27-JAN-2026
DEFINITION  DJ-1/PfpI family protein [Streptomyces griseus].
ACCESSION   WP_457656488
VERSION     WP_457656488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10123420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..211
                     /product="DJ-1/PfpI family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=22318
     Region          3..181
                     /region_name="GATase1_PfpI_2"
                     /note="Type 1 glutamine amidotransferase (GATase1)-like
                     domain found in a subgroup of proteins similar to PfpI
                     from Pyrococcus furiosus; cd03139"
                     /db_xref="CDD:153233"
     Site            100
                     /site_type="active"
                     /note="conserved cys residue [active]"
                     /db_xref="CDD:153233"
ORIGIN      
        1 mqiaillfdr ftaldavgpy eilsrapgae tlfvaertgp vrndsgslal vaektlaevp
       61 spdlvivpgg pgqsdqmane allgwlrtvd vtttwttsvc tgslllaaag llrgrratsh
      121 wlalelleef gveptgervv ldgkyvtaag vssgidmglt llgriagddv arsvqlltey
      181 dpqppydsgs phkapaalve ewrsrsrhsa r
//
LOCUS       WP_457656489             816 aa            linear   BCT 27-JAN-2026
DEFINITION  Tex family protein [Streptomyces griseus].
ACCESSION   WP_457656489
VERSION     WP_457656489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Fuchs,T.M., Deppisch,H., Scarlato,V. and Gross,R.
  TITLE     A new gene locus of Bordetella pertussis defines a novel family of
            prokaryotic transcriptional accessory proteins
  JOURNAL   J Bacteriol 178 (15), 4445-4452 (1996)
   PUBMED   8755871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..816
                     /product="Tex family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /calculated_mol_wt=86829
     Region          1..727
                     /region_name="Tex"
                     /note="Transcriptional accessory protein Tex/SPT6
                     [Transcription]; COG2183"
                     /db_xref="CDD:441786"
ORIGIN      
        1 mttsiegria eelgvrerqv raavelldgg stvpfiaryr keatesldda qlrtleerlr
       61 ylreleerrt ailesvteqg kldaaleasi raaetkarle diylpfkpkr rtkaqiarea
      121 glepladgll gdpsvdplva aaafvdgdkg vadaaaaldg arsilterfs edadltgelr
      181 ermwtrgrla akvregqeea gakfadyfdf aepftalpsh rvlamlrgek envldlvlep
      241 eepeaagqpg pssyenmiar rfeiadrgrp gdkwlgdtvr wawrtriqvh lgidlrlrlr
      301 taaedeavrv fasnlrdlll aapagtratl gldpgfrtgv kvavvdatgk vvatdvihph
      361 vpankwdqal aklahlakeh avdlvaigng tasretdkla gelidkhpel kltkvmvsea
      421 gasvysasaf asqelpdmdv slrgavsiar rlqdplaelv kidpksigvg qyqhdlsevk
      481 lsrsldavve dcvngvgvdv ntasapllsr vsgissglae nivahrdtng pfrsrkalkd
      541 varlgpkaye qcagflrirg gddpldgssv hpeaypvvrr mgksaggeva slignadalr
      601 alraadfvdd mfglptvtdi lkelekpgrd prpafrtatf kegveklgdl epgmvlegvv
      661 tnvaafgafv dvgvhqdglv hvsalsktfv kdprdvvkpg divkvkvmdv dvprkrislt
      721 lrlddepgag ggsgggqqgr gerggrppkq rqgqgqgqps gggqgrqggg grdrrggggg
      781 srqggqgapa pansamadal rragladpkp gggggr
//
LOCUS       WP_457656491             328 aa            linear   BCT 27-JAN-2026
DEFINITION  pirin family protein [Streptomyces griseus].
ACCESSION   WP_457656491
VERSION     WP_457656491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35658
     Region          33..291
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msnvehepvs rhgtrgpeaa epalrrveil tprdvplggp rsmsvrrtlp qrarsfvgaw
       61 cfvdhygpdd valrggmdlp phphtglqtv twlfdgeveh rdslgshafv rpgeinlmtg
      121 grgichsevs tarttvlhgv qlwvalpdeh reaerdfqry vpspirkdga eikvflgsll
      181 davspvrtft pllgaelile agaslalsvd aafehgllvd egdieldgta lspaqlgflp
      241 pgngsltvrn tssararvil lggppfeeei vmwwnfigrs hddivrarkd weeaserfga
      301 vegyagerlp apelpnatla prrnppts
//
LOCUS       WP_457656498             235 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein,
            partial [Streptomyces griseus].
ACCESSION   WP_457656498
VERSION     WP_457656498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>235
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
     Region          8..226
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msrpvigist yqdparwgvw emsavllpaa yprlvraagg ravllppdda adaardtvaa
       61 ldglviagga dveparygav adprtgppar erdawelali raaveqrvpl lgicrgmqll
      121 nvalggtlhq hlddhtggpg vfgshpvtpv pgtayadavp etavvpayhh qavdrlgagl
      181 vasahapdgt vealelpghg slvlgvqwhp emgedtrvma alvraaggaa glpda
//
LOCUS       WP_457656506             421 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457656506
VERSION     WP_457656506.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..421
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
     Region          10..419
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 gggaaaapad rarllrrfav vvdehieela qlevreaght ignarweagn vrdlldysag
       61 gaerllgrqi pvaggidftv leplgvigvi apwnfpmpia awglapalaa gnavllkpae
      121 ttpltalrla elaleaglpd glfqvlpgeg pvagsalveh pgvakivftg strtgkhimt
      181 rcaervkrlt lelggkspnl vfadadvaaa aaaapmsfld nagqdccart rilversvyd
      241 rflellvpav aavvvgdpad ektqmgplis alqlervrgf vdgdrgadgv rtllgtapeg
      301 pgfwypptvl tgvspdapva veevfgpvav vlpfedeqda lrlanateyg lagsvwtrdv
      361 gralrvgqgl ragnlsvnsh ssvrystpfg gykqsglgre lgpdalaaft etknvfiste
      421 a
//
LOCUS       WP_457656514             456 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457656514
VERSION     WP_457656514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 456)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..456
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48171
     Region          56..429
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(93,100,114..115,122,126,133,261..262,265,269..270,
                     273,306,311..312,315..316,318,341,368..370,373..374,
                     376..378,382)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(100,108,110,113,115..116,198..199,210,260..261,
                     264..265,269,312,315..317,419)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 madapnaapa agppaptagp paptagppap patpeipagm pdenslvygd avladphavy
       61 armrsecplh qdviqgggkv lvptryddvr allaesrllr sfavedpgaf qghlgnsdpp
      121 rhtrlrrlta kaltpkrver lrpaverlad glldalagrp qadlvaeyth plaalagael
      181 fgigeadaee fhgcwdamaa fpestsfpef qaatdrlgrl farlfadrre qpsddllsal
      241 vharsgedrl tdgeleqtav flviasdktv pamlasamla lldhadqldl lrsrpellrg
      301 aveeclryea pvaltnplra gepmsvgdre laagdlvqla liaanrdper fadpdrldit
      361 rpvgghvsfg hgihmclgaq larmtgeval grlidrfpal rlahddpaqd avwsrehvmr
      421 rlsalhvglg eaapagsaaa pvasatsahp tgadpt
//
LOCUS       WP_457656519             260 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces griseus].
ACCESSION   WP_457656519
VERSION     WP_457656519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..260
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28233
     Region          20..247
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 maegsdvwfr rfrrvarprl rlvclphagg sastfrswpq wlpedvevla vnlpgrqdrl
       61 gedcvsdmdr ladgvaeall plsgepfalf ghsmgasvaf evahrleqry gtvatalivs
      121 gqqpparyrv neahlggdpg llaevrrlgg egaafldspe mrellmpair gdfalmgayr
      181 pdpslriaap vdawvgdadv dvtveetraw aevttgpfay rvfsgdhfyl naqsaeftga
      241 lverlarpea kvgsaphqvr
//
LOCUS       WP_457656521             372 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta fold hydrolase [Streptomyces griseus].
ACCESSION   WP_457656521
VERSION     WP_457656521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..372
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=39683
     Region          <1..>86
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          114..350
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mssatgtatg avapalpdtl paprvrpeav attappetpt asapvrqttt atapvrpkpa
       61 taapvrqepp atapvrsart rtavvprgfa tgtgppvelh rhpvaggpvt grmlllhglg
      121 nsatvwdafl ahrpagqelw tadlpwrgag dggwhrapda trwlaealdg vpggagtvva
      181 hsfsalqtla lldrelgagr dpferygieg lvlvspfyrr taeefdwdsm trypaeferi
      241 meegirvhsg grldpeiqls marrvcdrig pygwlrfvds ylrtpwlrpg rirvpaavvc
      301 galdiavdpa egrdltadlp dayirvltdc ghflmterpa efssvvgdfv mslssrarsq
      361 rpgdrapgep ap
//
LOCUS       WP_457656524             244 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656524
VERSION     WP_457656524.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  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 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..244
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=25429
     Region          10..187
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtalqasaat dvavhwwqla gnstdsadla vlgpnererl driqhpaqaa qfvgsragvr
       61 rilaellgva pgavalgrlp cpgcgaadhg ppavlhprsp frislshasg rcllavaqvp
      121 vgidieaerp lnlselarva ltatehrqll glpagaarer aflrcwtrke aalkalgtgi
      181 atnlsrieth pdrrgpvtvt agppgtardw svhdvtvpgp wvataavpyg vsarvtvsqh
      241 pgvh
//
LOCUS       WP_457656531             307 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457656531
VERSION     WP_457656531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..307
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31443
     Region          46..305
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 msdspgspds aardrdeaes asafahppva pdataaygdh pdqvvdfyap rdgrtaaplv
       61 vllhggawra pydrvhtspl adflarrgfa vanveyrrgg ddipqqrdga entrmsgadp
      121 vagrwpetfd dvaaaldamp alaarelpga dvrrivvagh sagghlalwa aarhvlpegs
      181 pwrlpapppl rgvvalapia dfataaglgv cggavdqllg gkadfeeraa hadpgvllpt
      241 giataivqgv ddivvpkava eayvdaaars getvgltllg gvghfplidp aadacavvae
      301 eitqlaw
//
LOCUS       WP_457656537             372 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457656537
VERSION     WP_457656537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..372
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42604
     Region          11..357
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtaidptahl taeqieelgr eldairdevi adrgekdaay irrvisaqrk lelasrgvll
       61 fsifppawli gtaglsvaki mdnmeighnv lhgqwdwmrd pkihsttwew dhvspsdqwk
      121 hshnelhhty tnvigkdndl gygimrvded qkwhpfhlgq plwnflnacf feygiaaydl
      181 elgknlskrr rknpefrara ravgrkirkq vlkdyvihpl lsgpsflttl aatftanlvr
      241 nvwthsvimc ghfpegvqvf errsiegetr gqwylrqmmg sanisgskam hfmtgnlshq
      301 iehhlfpdlp snryaevavk vralfekyel eyvtgplpkq vfsawhkvfr lalpnrqpka
      361 gtldreqdli aa
//
LOCUS       WP_457656538             351 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin reductase [Streptomyces griseus].
ACCESSION   WP_457656538
VERSION     WP_457656538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10865445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..351
                     /product="ferredoxin reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37702
     Region          22..257
                     /region_name="FNR_iron_sulfur_binding_2"
                     /note="Iron-sulfur binding ferredoxin reductase (FNR)
                     proteins combine the FAD and NAD(P) binding regions of FNR
                     with an iron-sulfur binding cluster domain.
                     Ferredoxin-NADP+ (oxido)reductase is an FAD-containing
                     enzyme that catalyzes the reversible electron...; cd06216"
                     /db_xref="CDD:99812"
     Site            order(72,86..89,104..106,108,112..114,153,156,255,257)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99812"
     Site            order(86,88..89)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99812"
     Site            order(111,114,117,124,132,134)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99812"
     Site            order(148,152..155,157)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99812"
     Site            order(153..154,175..177,231..232)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99812"
     Region          270..350
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mtstalrgra wkllemvttp llpsdyldlv splrtgadlr grieavrpet sdaatvvirp
       61 grgwrghtag qyvrigvdvd gvrlwraysi tsptnrqdgr ititvkaipd gkvsnhlvrr
      121 akpgtliqld qatgdfvlpq akpakvlylt agsgitpvmg mlrdtglddv vmvhcapqpq
      181 dvifrkelhg lvadkklrla evhtdtdgkl diarlqelvp dwaeretwac gpaglldaae
      241 ehwteqgvre rlhterfrpg iivageggei tfsatgktid adgatplldi geeagvlmps
      301 gcrmgicfgc vtplkagavr dlrtgeitea epgvliqtcv saaagpcdie r
//
LOCUS       WP_457656539             379 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656539
VERSION     WP_457656539.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..379
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40601
     Region          125..374
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msyairrase ltldettvta lraalkttad evvqaiidev ppyaralsgr mgatirravr
       61 talghyldla sgsatggdag daayelgrge vrdgrsmdal lsayrvgarv awrclaagav
      121 paglpaaeva kfaeltfayi delsaasaag hadelaargr aherhlehla rdllagaspd
      181 allasgqrar wqppvsltav llpaaqarpa yrtldpstlv lddlpddtgv llvpdadrsr
      241 llrqltdraa vvgparpwth asasyaralr arslssdird tedhlpdlvl sadadafadl
      301 raralaplrt lpaatarrle etlrawllhq grrdevaaal fvhpqtvryr msqlrelfpd
      361 lasphrvlel tlavglrar
//
LOCUS       WP_457656543             281 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656543
VERSION     WP_457656543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29292
     Region          1..209
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mivvtgatgn vgrtlvplla eageevvavs rqphpaglla garharadvg daasmapvle
       61 gadaffvllg gelngrgerp kalldaavaa gvkrvvllss qvgatrpeel sharlrefea
      121 avrtagpdft vlrpggfasn afawaesvrt rrtvfapfgd valpvidpad iaavaaaals
      181 edghagrtye ltgpeaispr rqaaviseal geevafvels reeahehlar fmpeeviggt
      241 ldilglplla eqavgsdves vlrrparpfg ewvarnlpaf r
//
LOCUS       WP_457656548             333 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656548
VERSION     WP_457656548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..333
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33944
     Region          87..319
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mpaaptvtps agrgarfrrs allpltaavl laagtggwya fggggpvtga ggaegpgegv
       61 aplarsmqlp wpregqasva vegigslgtr geqkpvpias vtkvmtayvi lkdrpmrada
      121 pgatvvadqr aadesyssve ttapvlagrk ysqrrllelm mvpsgnnvar llarwdagde
      181 kafvakmnrt aaalgmratt ytgvsgmeas trstaadqlr laraamkdpa frqivatgsv
      241 tapgagvtfr ntnkllghdg viglktgsst paggnlvwat rqevagvsrl vigvvlhqra
      301 gttpaegsta aheasralit airadlpdaa nra
//
LOCUS       WP_457656552             344 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457656552
VERSION     WP_457656552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  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   2  (residues 1 to 344)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..344
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34632
     Region          3..344
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtsrtvtlld varaagvsks tvsdalqgsg rvaeatrdrv ravaeelgyr pnsaarrlrr
       61 astgavglhl patatrldyy mnlafgaver aqedgldmvl lapsgasggr iasrvdgllv
      121 idpeagdsav pglldagvpv vtgerylgpa aapsgavvcd naasltalld hvaergarrp
      181 avlapsgssa watalratar swglahgvev alrtvpfaat paeaeettra lltadpavda
      241 vicapdgsap gvlraaaalg revgdsekag gsgksgsgll vaacvdgpat rnaeppvtav
      301 dlrpaaygra caellcdila draapdtvrr hawsldtras tgpa
//
LOCUS       WP_457656555             721 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidase domain-containing ABC transporter [Streptomyces griseus].
ACCESSION   WP_457656555
VERSION     WP_457656555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 721)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 721)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..721
                     /product="peptidase domain-containing ABC transporter"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79023
     Region          15..715
                     /region_name="SunT"
                     /note="ABC-type bacteriocin/lantibiotic exporters, contain
                     an N-terminal double-glycine peptidase domain [Defense
                     mechanisms]; COG2274"
                     /db_xref="CDD:441875"
ORIGIN      
        1 mawrmrrvrr vrevqqfaqa ecglcciami lsaygsrdsv aglrrehevg rdgltikqia
       61 ailrgrgfev rafragaqrl gqlrlpliay wddshvvvve eidehrvtvv dpgggrrtyp
      121 aeefaehysg laleavptpd hrperhreps vwreflrslt garkplvqaf lmslvlysft
      181 ifmpiatqya vndyagylek apialvlvaf tapmavffll sllrtvalas virslgeamm
      241 gktfrrllel pykyfanrsq gelfyrlssi tsvrdmissq lsvvlldlgs liaifsymfy
      301 rsftlgataf avfltmlava vatyrpirri tereisettk ssslqmeals sietlkvsgm
      361 tgtffqdwrq vyaagmeqtr rrivlqgvat sgyavfqvfg pllvlavglw lvlngsldlg
      421 savaaqtlta tslgmvmsls gaftqlitan aqvarvgdil hqpedpgafg drqvtvrgav
      481 rlrnvgfsyp gsgvpaladv sfdvrpgerv aivgssgsgk stlgkllmgl ypirsgdvly
      541 dgvsigeida dtfyrsaayv pqdivlsnrs iadnirfgvp datmeavvda arqahvhddi
      601 aamplgyhtp vremggslsg gqrqrialar alarrprvlv ldeatsaldt vtesriaaal
      661 drlectriii ahrlstivna dlvvvlehgr vvqtgrhedl itepgpyrdl vrsqvdlntv
      721 r
//
LOCUS       WP_457656556             249 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656556
VERSION     WP_457656556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26222
     Region          14..242
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 maqhaqdaqr qqvisvrdlr kefkgttavd gvsfdvrpgr vtgflgpnga gktttlrmil
       61 glirptggna llwgspyael aaptrrigvg ldggafvgrr tgrghlrcya paagcgperv
      121 gqlladvgls gaadrpvagy stgmkqrlsl asallgdpel lvldepangl dpegmlwlre
      181 flrdfaasgr tvllsshllg eleqtvddvl lmhhgrllss gpldgllepg erlesaflrl
      241 tragngvra
//
LOCUS       WP_457656557             357 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656557
VERSION     WP_457656557.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..357
                     /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=37581
     Region          113..352
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpvgiavvdg llvngfgpgp glwvalvaag alvlrrrcpe vpllvglpgm yvgqlafapl
       61 ialycladrr rsvvvgavga aavalaqflp ypvtglrela pdretlimam dscvlavgal
      121 vlgrtarvrr erqrelaegr erehrllaer tlsterawla remhdvvahq vsliglqaga
      181 lqvgepdaat vrstagvvre lsvktltelq hmvgvlraag vaapglapqp rltdlpalvr
      241 dcglrvtlda pdgpghwsqa aeraayrtvq ealtnvrkha pgaevdirvq pldgglrvdv
      301 rntaadgsta plglpggghg liglrerahl ldgtfdagpe pdggfriqav fpsrqtf
//
LOCUS       WP_457656563             408 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Streptomyces griseus].
ACCESSION   WP_457656563
VERSION     WP_457656563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..408
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42280
     Region          7..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mehpgtlvli malavlapll gyatgrwlpv pvvifeivlg vlvgpdvlgw ahhdqvidal
       61 sdlglsmlif lagyeikfae vrgdtlrrag gawvlsfaag lgvalllsga dlakslvigt
      121 altstalgav lpilrdsgsl egrfgsvvla fgsvgefgpi iamallfsgr spgaasavla
      181 vfavvtagav fwamrprppw farivavtlh ssgqfavrfv mlllagmlgl ahafgldtll
      241 gafasglltr lvlqgsvpes gdailervea igfgflvpff yvvtgidfdl aallddgrpl
      301 lllpvflllf llvrgvpayl laprdltgra praalglfas tclplvvait aigldekvig
      361 sgeaaalvaa amvsvlvfpl lafrllrree dgsgrsvpgr aaesgeaw
//
LOCUS       WP_457656564             506 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457656564
VERSION     WP_457656564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..506
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53451
     Region          95..368
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          412..500
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mttwtrkall ltvsaaaaag tltavgapva hsrpagpaat plawgpcapi pgttvpagqq
       61 catlrvpldh rapggrtvdv avtrlrtdrp earrgtllvl aggpggsgvq rlaqkgealr
      121 aategaydlv gldprgvggs tragcgipea drhlvtlray paadgsiten vararrtaea
      181 cardggpvvr sfstrnqard idrlraalge rklsvwghsy gsyaaavyaq ehpdrvdrlv
      241 ldsvgdpdpa rvaygwmtnv gpavalrfpd faawaadpar eaeglrlarr aedvrplfla
      301 lareldrepr esetpgvplt gnrlrqalhg slnsdtafap larlirsaqd prgrpvlppe
      361 lagalpdeda sltmavicnd vrwpgpdsgy arrvaadrae ypltagmpan iapcafwkyd
      421 eeprptrita egpsnvlmiq slrdpatpla garkmraalg erarmvtver gghgmylgng
      481 nacgdravsd flvtgkrptr dahcpd
//
LOCUS       WP_457656565             362 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces griseus].
ACCESSION   WP_457656565
VERSION     WP_457656565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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..362
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     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=40642
     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 mpspltsrrl prptaaaspg tgvpdadgrd hffdnakyla ivlvaighaw eplppgrlve
       61 aaytfiytfh mpvfiliagy fsrnfelrpe rvwklvtsll vpylvfevly tlfhralrdp
      121 dfslsllepy wllwflpalf lwrlstplwq tvrfpvlvsl aiaavatvsp aadgtlpvqr
      181 ilqflpfyvl glrlgphhfa mvrrtwvrvv svpvfvagml laywlvprts tswffrknsa
      241 qeldtaqwtg paatlllfla avvlgacfla wvprgrswmt algtctlygy llhgfviral
      301 ryegfydqpf fdttmgtvav tvgaavmvtl lctppvrrll kplleprmew arqkpppaap
      361 ap
//
LOCUS       WP_457656569             232 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457656569
VERSION     WP_457656569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  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
REFERENCE   2  (residues 1 to 232)
  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 10144160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..232
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25079
     Region          8..76
                     /region_name="NT_KNTase_like"
                     /note="Nucleotidyltransferase (NT) domain of
                     Staphylococcus aureus kanamycin nucleotidyltransferase,
                     and similar proteins; cd05403"
                     /db_xref="CDD:143393"
     Site            order(25..27,30,37..38,40,62,64)
                     /site_type="active"
                     /db_xref="CDD:143393"
     Site            order(25..27,30,37..38,40)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143393"
     Site            order(38,40,64)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143393"
     Site            order(62,64)
                     /site_type="other"
                     /note="antibiotic binding site [chemical binding]"
                     /db_xref="CDD:143393"
ORIGIN      
        1 mddpvltara lvrdrfpaar aaflagsvlt drrtptsdld ivvlvddpla agrenltyrg
       61 wpvelfvqte srwhafadqe takrssplla mcaegmllad tdglgaalqd eartrwaagp
      121 pplseqerny rryiltdlld dlrgctdpae rvylvshllq raselvllvg ghwlgagkwl
      181 srrlaaaape ahralsgsaa qamtgdtkaf aeavagvldr sggtlwdgya ir
//
LOCUS       WP_457656573             528 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail sheath family protein [Streptomyces griseus].
ACCESSION   WP_457656573
VERSION     WP_457656573.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Bock,D., Medeiros,J.M., Tsao,H.F., Penz,T., Weiss,G.L.,
            Aistleitner,K., Horn,M. and Pilhofer,M.
  TITLE     In situ architecture, function, and evolution of a contractile
            injection system
  JOURNAL   Science 357 (6352), 713-717 (2017)
   PUBMED   28818949
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Ge,P., Scholl,D., Leiman,P.G., Yu,X., Miller,J.F. and Zhou,Z.H.
  TITLE     Atomic structures of a bactericidal contractile nanotube in its
            pre- and postcontraction states
  JOURNAL   Nat Struct Mol Biol 22 (5), 377-382 (2015)
   PUBMED   25822993
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..528
                     /product="phage tail sheath family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=55939
     Region          241..522
                     /region_name="COG3497"
                     /note="Phage tail sheath protein FI [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442720"
ORIGIN      
        1 mpsylspgvy veevesgsrp iegvgtsvaa fvgfaqkgpf deptlitnws qfvaafgdfv
       61 dgaylasavy gffangggvc yvvrigdgtv aadgqegqdd qdgegapgks reagelpvga
      121 evrvgpyavr prpgvsgeis vevapvegdd ppadvfrflv krdgqvvety psvttkrskd
      181 nvatrvnaks elievresgg gaapappepq tvtlapaapa aggsgamape vyvgdadrrt
      241 glggleavde vtmiavpdlm sayerglldl esviavqqgl iahcelmgdr vaildpppgl
      301 tpqqvrgwrt gqanfdskya tlyypwisva dpasgratlv ppsghiagiw arnddtrgvh
      361 kapanevvrg avalatqltk gehdllnpig lncirsfpgr girvwgartl asdpawryln
      421 vrrlfnylee silagtqwvv fepnddalwa rvrrtvsafl vnewrkgslf gltpeeafyv
      481 kcdretnppe sidagqvice igvapvkpae fvvfrlsqlt ggsggvde
//
LOCUS       WP_457656575             757 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656575
VERSION     WP_457656575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..757
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79446
     Region          343..741
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mtardavgpd lrhllaraaa verrirhave lrrstdpdpd ddfrglyltd esiarlldde
       61 gargfpevdg alagdavegt paegarglsa lggtsaegag glpaladasa egarglppla
      121 gtsaegaldg lpaesedsrl asfarefglt aldteillia lvpdlddrfe afygylnddv
      181 srrrpsigla lglcgvalsd paararlaag aplragglll aedlnrpfls ralrvpdrva
      241 ahllgddtpd prlgellapw qavpgvgdpa plagvlaegg alaylsedqg gagtalaasa
      301 lraagrrvlg ldlarlaedp spaeavralv rearltgagl vcapldavar erpgllrllt
      361 atpvptvlvg rapwdaswsa applllhapr vepsargalw reayeqaagf aaghtsglta
      421 gastpslppa iapdhllapf lltpeqitga arsaaqaarl aggeltadhv rrgaraqnaa
      481 gldrlarrie ptvtwddlvl ppdthtqlre ltararhrdr vlgewgmrpg ggrgrgvsal
      541 fagdsgtgkt msaeviaadl gldlytvdla tvidkyvget eknlerifte aagvngvllf
      601 deadaifgkr sdvkdahdry anvesayllq rmesfdglai latnlranld daftrrldlv
      661 idfpvpdpeq rlllwdrclg ptlprgtdld lpfcaenfel pggnirsiav tsaylaaeag
      721 gavtmetvih aiqreyqklg rltlasefgp ylewvqg
//
LOCUS       WP_457656579             518 aa            linear   BCT 27-JAN-2026
DEFINITION  M28 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457656579
VERSION     WP_457656579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Rawlings,N.D., Morton,F.R. and Barrett,A.J.
  TITLE     MEROPS: the peptidase database
  JOURNAL   Nucleic Acids Res 34 (Database issue), D270-D272 (2006)
   PUBMED   16381862
REFERENCE   2  (residues 1 to 518)
  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   3  (residues 1 to 518)
  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 11559072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..518
                     /product="M28 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54014
     Region          58..486
                     /region_name="M28_SGAP_like"
                     /note="M28 Zn-peptidase Streptomyces griseus
                     aminopeptidase and similar proteins; cd03876"
                     /db_xref="CDD:349873"
     Region          124..245
                     /region_name="PA"
                     /note="Protease-associated (PA) domain. The PA domain is
                     an insert domain in a diverse fraction of proteases. The
                     significance of the PA domain to many of the proteins in
                     which it is inserted is undetermined. It may be a
                     protein-protein interaction domain. At...; cl28883"
                     /db_xref="CDD:333703"
     Site            206..208
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:238300"
     Site            order(277,289..290,323..324,352..353,404,407..408,424,
                     451..452)
                     /site_type="active"
                     /db_xref="CDD:349873"
ORIGIN      
        1 mhatrrraia vvaatalatp lllaasphpg rpaphdpgke aaklsrelvr nasareahrh
       61 lrqfqaiads aeghraagsl ghdasaayvy rqlqragytv syesfrfiyt etlaeklsvv
      121 tptprdvtik amtytpstke ggltaelvav pvdettgcea sdyasanftg kialikrggc
      181 sfaekqaaaa eagaagavvy nnvegvlsgt lgevaagkip tggltqeege klvadlagge
      241 vtvsfeiref qedrptrnvi aetpggsaar tvmlgahlds vtegpgindn gsgsagllev
      301 alqlaksksk pankvrfaww saeengligs ekyvealsek qreqiqlyln fdmiaspngv
      361 qfvfdgdnsd evgegpgpeg saqlerdine fldgkgkphe gtdftgrsdy gpfieagips
      421 ggtdtgaegi ktaaqaevyg geagiaydpc yhaacddldn idmghfdtni dvianavgty
      481 ahdlrsltrp vdpdtgtgtp gsggsggglr eghgrvar
//
LOCUS       WP_457656584             212 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457656584
VERSION     WP_457656584.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..212
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22806
     Region          1..209
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mktfvfdige tlvrddrywg swadwlgtpr htlsalvgav taqgldnsea lklvkpgidi
       61 paeyaareaa grgeyldesd lyedvrpala glrrlgmrvv vagnqtvrag ellrgldlpa
      121 dlvvtseewg cakpsaeffa kvleasgapa rdtvyvgdhp andtfpaaas glrtahirrg
      181 pwghlwvgdd rvhatadwvi qslseitdia gk
//
LOCUS       WP_457656586             337 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces griseus].
ACCESSION   WP_457656586
VERSION     WP_457656586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..337
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36544
     Region          14..305
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msegaesigv drgdrpgwda trswvekngl seaerieqvv plrggwtsem rrldlggpgg
       61 arslvlrsfv kpfyvrhaeg llnreadilr llgdtdvpaa alvavdaaae hcdhpsllms
      121 llpgalrldd hgaddradll arqlvrihrl pvaahqrprt yqawasperv vlppatarpe
      181 lwrravdvir reppayegcf lhrdfhpgnv lfsgngtggg drdgdgdglr vsgvvdwvet
      241 swgpadldva hcstalallh gvpagmrfad ryvdaggtla gdsgdhlywr lldalgfapg
      301 gekvavpwre vgrvdltadv laqrlegyvq alferya
//
LOCUS       WP_457656591             296 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656591
VERSION     WP_457656591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31766
     Region          47..287
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mslrrrsarf prlllaasll gallappaaa asahrsspsg gsgaglplrv atynihagag
       61 ldgvfdldrq taelrsldad viglqevdrh wgarsewrdl agelarrlrm hvsfapiysl
      121 dpaepgapra eygvavlsrh rivsaenhei trlstqdpnp vpapapgfge vavrvrglpv
      181 hvyvthldyr pdpavrvaqv adtrrimaed rgpqillgdf naepaapela plwreltdad
      241 pgaptfpaqd pvkridfvav skggvgvrra wvpesvasdh ravvadllvr grardr
//
LOCUS       WP_457656588             862 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656588
VERSION     WP_457656588.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..862
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87426
     Region          45..443
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(52..53,56..57,60,92,142..143,145..147,150,170,
                     173..174,177,305,308..309,312..314,317,345,349,402..403,
                     407,411,427,430..431,434..435,438)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          432..>845
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 matttptgvr gghakhgghg ggnasgapdg tpmthrqime altglllgmf vailsstvvs
       61 nalpeiisdl gggqsaytwv vtasllamta ttplwgklsd lfskkllvqi aliiyvlgsv
      121 vaglstssgm liacrvvqgi gvgglsalaq ivmaamiapr ergrysgylg avfavatvgg
      181 pllggvitdt swmgwrwcfy vgvpfaiial ivlqktlklp vvkregvkvd wsgaffisaa
      241 vslllvwvtf agdkydwlsw qtyvmvagsa llglifvfie srakepiipl rlfrnrtitl
      301 asiaslfvgi amfagtvffs qyfqlargks ptmsgvmtip miaglflsst vsgqvitktg
      361 rwkawlvsgg flvtaglgll gtirydtpyw hvavfmfvmg lgigmmmqnl vlatqnqvap
      421 edlgsassvv tffrslggai gvsalgavlg nrvtqyvkdg laalgpegak lghggtgggg
      481 ipdldklpep frvvmeaayg hgvgdvflya apcaliafiv tifikevalk ssagndtpvd
      541 tpadapaave taeapvpaav gaaglvsega agvtsvdtad aeadalaagg gagtgagvay
      601 envhdtvqgt pvrgvvrgae gapvaraavt lislggrqlg rsvarsdggy tldapgsgsy
      661 vliasadgyq pqastvvvge eplafdills gtsglagtvr aegsgtpvdg amvivtdvrg
      721 dvlatgtsgp tgefafgeli pgsvtvavna agfrplalpv eiggqgvtrv eaalrsgalv
      781 qgvvragsar spltdarvtl idaagnvvat attgedgaya ftdldtgeyt viatgyppva
      841 gsltvsgtgv dghdielahp ge
//
LOCUS       WP_457656592             388 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656592
VERSION     WP_457656592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40630
     Region          6..380
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mttsttlhel ldthiaagsm pgavalvarg ervevvtagt aglagsapmr rdsifriasi
       61 tkpvvaaaam tlvedgliap adpvaawlpe lasplvvrtp espvddvvsa vrpitlldll
      121 tfragygfps dfslpavapl faelrqgppe pqaglapdaw maelsrvpll hqpgdgwlyn
      181 tcsdilgvli arvadrplpa ylaerifepl gmkdtgfwve paaldrftss yrpgadggsd
      241 pvlddapdgq wssppafpsg agglvstvdd wyafgrmlla eglndagdrv lagesvrqmi
      301 tdhltpeqra asglftegqs wgfggavdve iaapwnvlgr ygwvggtgtt ahivpatgtv
      361 avlltqmams gpttpqvmrd fwtyaagf
//
LOCUS       WP_457656595             558 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457656595
VERSION     WP_457656595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 558)
  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 558)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..558
                     /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=57626
     Region          <189..542
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkvsrrpwtl rtrlvvsavs liavvaavig svtaiafhsy mygklddqlh svaeraerpp
       61 gptpvpealr etgplgfvgg ggqplgtfga lvgddgsvga skvvedsglr aqesakplte
      121 eqrraleeaa petgegttsv dlpglggyrv eaatttdght vlvgipsaev sgalttlivv
      181 evcvtaagll aasiagtvlv gvalrplrrv aatatrvsel plhsgevapl ervpeaeadp
      241 rtevgqvgaa lnrmlghvgs alaarqeset rvrqfvadas helrtplasi rgyaeltrra
      301 tggreapepd pvtrhalgri eseadrmtgl vedllllarl dagrplsygt tdllplvvda
      361 vsdaqvadrp dagpgggart aagpgagpgp dalvadrpga gpdarhrwrl elpdepvtvr
      421 adpdrirqvl vnllanarth tppgttvtvs vrppvrggep vtlavrddgp gipaellphv
      481 ferfargdas rtrgtdggga tgstglglai vqavvsahgg rvrvesapgr tvfvielpae
      541 epairtdsqa rdrlttpv
//
LOCUS       WP_457656596             293 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457656596
VERSION     WP_457656596.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..293
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32459
     Region          18..289
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mdtgsddvvr fwerlglpgi idvhthfmpe qvlrkvwayf dsagpltgle wpityryeed
       61 arlavlrsfg vlrftamlyp hkpgmarwln dwtagfaart pdclhtatlf peegvetyvk
      121 eaveggarvf kshlqvgayd andpllepaw gllaeagvpv vmhcgsgpap grftgpepig
      181 rllarhprlr livahmgmpe yaeflalaea ypevrldttm aftdfsegfs pfpaaergrl
      241 adlgdrillg tdfpnipypy vhqlevlerl glgeewlrav chgnaaalfp art
//
LOCUS       WP_457656598             254 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457656598
VERSION     WP_457656598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..254
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=27780
     Region          3..252
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mitlevrrre lltpgsacvt lggpgvrdlv agggdqavrl ffpregqsgl rmptasneaw
       61 mvqvmlmpka vrpwvrnltv rrlrpaeqei diefalhgds amsswvhrvr pgdqagifdl
      121 gtmyrlpeha rgrllvades alpavlsile ddqdppptev fvevataadi rsvapragvr
      181 ihwlsrddes lrpgtlalea vraaelpagp lyawvagesr latgvrrhlv ddravpkqni
      241 afygywrlgr sapg
//
LOCUS       WP_457656605             177 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces griseus].
ACCESSION   WP_457656605
VERSION     WP_457656605.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 177)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..177
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20342
     Region          36..158
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mqwkihgerp iyennwvnlw ltdvetpdgn rwehhvvklr hlavaavlne rrevlmmwrh
       61 rfitdtwawe lpmglveege spaeaaarev leetgwrpgp vrtliyaepa ngitdsqhhv
      121 fradgatyeg ppteknesdr iewipladvr gmidrreivs sgslvgllyv lmdeair
//
LOCUS       WP_457656603             190 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457656603
VERSION     WP_457656603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Rosinski,J.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 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..190
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21322
     Region          16..97
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mteerrteav erhtvespev lkalshplrl rilrhlgtag patsttlaaa lgentgtlsy
       61 hlrmlersgl iediperstg rerwwrgvrg ldirrppqge lteaeramsa eldrmrmeed
      121 velarqftag qaesegwmrg srslthltka elsafhddyl tllaryargp edapadarpv
      181 llrwfglpad
//
LOCUS       WP_457656608             293 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Streptomyces griseus].
ACCESSION   WP_457656608
VERSION     WP_457656608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..293
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32095
     Region          82..225
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
ORIGIN      
        1 mahaliaspf ldghlllkpg aragarisad hfeglrqaat nigslpawav qtasdvwgld
       61 lggqtahgtv lvrepspygy crasweinlg cnfgckhcyl gerpfsglgw hdkvrlldim
      121 reagvlwlqi tggeptmdph fqdayryawq agmmltistn gsllwrpdll klfqdcppyr
      181 lvvsmygase esfdtltqrr gawkafrrgm daareaglpl rinvvvtedn aseademaal
      241 adewnvenha ytnmtptiyg ggepllaqsa ahlrqrkpfa gcnagpepcp prr
//
LOCUS       WP_457656609             288 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656609
VERSION     WP_457656609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..288
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31317
     Region          162..265
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(227..229,239..240)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mffrwdwlrp vltapivptl gpvhpdalsv dlfedilraa dtgdflpydk drrwggekde
       61 kvlgedvvhq pertliptlt rrgrgtvkvf ayglrdsvve daaelaakla aahdvvsarv
      121 vrplrpetah prgtriqlkd ftagtcpdpg gpvrpvtawp tavqktfapf aeamatdgla
      181 flhhqmqadr cgpvlaavvd drivgaigpm evradaigrp qlmpqyfavl psvrgqglgr
      241 ilwraamhwg qthgaayqll qtevdgpsdq lcqseglatl gfshttra
//
LOCUS       WP_457656617             576 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457656617
VERSION     WP_457656617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..576
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56079
     Region          292..574
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mstenegned havpavpsvp sappvpadtp epatggatpp aapapapapa aaqdathgta
       61 petapepadp vqdtarlpvh etgapettph apgapahaea prhnpthqga patpaygqaa
      121 qpspppqppq hspygapsel pagaaswppp ppavpsyagg ntghasdhas ghasggigng
      181 sghgpvwgap vppgtdpagg kngksraggl vaavavaalv aggiggalgy waadrndngs
      241 sgnsttisas dtprdlkrpa gtvagvaaka lpsvvtidaq ggdgeggtgt gfvydkeghi
      301 ltnnhvvasa aesgelsatf sdgkkyaaev vgraqgydva vlklknppag ltplplgnse
      361 svavgdstia igapfglsnt vttgiisakn rpvasgdgqs nknsymsalq tdasinpgns
      421 ggplldatga viginsaiqs tggglgqsqa gsiglgfaip inqaknvaeq liktgkpvyp
      481 vigatvtmee ktggaaisae gaggtpavtp dgpaakaglk agdvitkfnd tvidsgptli
      541 geiwtrkpge kvtltyerdg ktataevtlg qregds
//
LOCUS       WP_457656620             248 aa            linear   BCT 27-JAN-2026
DEFINITION  YcnI family copper-binding membrane protein [Streptomyces griseus].
ACCESSION   WP_457656620
VERSION     WP_457656620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   de Oliveira Silva,Y.R., Zheng,D., Peters,S.C. and Fisher,O.S.
  TITLE     Stabilization of a Cu-binding site by a highly conserved tryptophan
            residue
  JOURNAL   J Inorg Biochem 253, 112501 (2024)
   PUBMED   38342077
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Chillappagari,S., Miethke,M., Trip,H., Kuipers,O.P. and
            Marahiel,M.A.
  TITLE     Copper acquisition is mediated by YcnJ and regulated by YcnK and
            CsoR in Bacillus subtilis
  JOURNAL   J Bacteriol 191 (7), 2362-2370 (2009)
   PUBMED   19168619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..248
                     /product="YcnI family copper-binding membrane protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25500
     Region          2..182
                     /region_name="YcnI"
                     /note="Uncharacterized conserved protein YcnI, contains
                     cohesin/reeler-like domain [Function unknown]; COG4549"
                     /db_xref="CDD:443613"
ORIGIN      
        1 mklsrialag gvaastvlli agpaaahvsv qpvgeaakgg yatlnfkvpn erdqastvkl
       61 evnfptdhpl ssvtpqavpg wkitidkskl dkplevhgkk iteavskvtw taddseiapg
      121 yfqqfpvsvg alpedadqlv fkaiqtydnk evvrwieept aggeepdspa pvlkltaaad
      181 dhhggaadda keaddhkaad tgasakesst aasssssdtt artlgiigiv igvagvafgv
      241 lagrrrsa
//
LOCUS       WP_457656625             427 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457656625
VERSION     WP_457656625.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..427
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47599
     Region          13..282
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,40..41,73,78,83..86,98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20,25,27..29,31,44,46,81,97..100,104,106,143,145,
                     147..148,150,161..162,165,185..188)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20,25,27..29,31,44,46,81,97..100,104,145,147..148,
                     150,161..162)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,104,106,143,145,147,165,185..188)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(161..169,181..188)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mleirrgmll ngryrleapl sppagramge vwktqdvrme rtvavkfpql yalrpaeaee
       61 rlkrfqveaa atarirrdev veiydrgeqd gypflvmeyi dgttledfmh envmidlgaa
      121 tsvvvgvayv laaahslgiv hrdvkpsnim itrqdgkvkv ldfgiarleg gendtrltrt
      181 gaqlgtvrym apeqfrsera tsvtdvyalg cifyemlagr pvfvgpgafe yqkqhlevkp
      241 iplsswrpdl pdevlelvdm mlskdpsdrp gtadevnirl rehlpksgsd apddlvhydp
      301 tlpfrnpcap aepvrgprgv ralpetppfr hrgevkdlcv qarklmlgdp aqaiammgar
      361 lpdarqfyga rdthvldlav qlagaleehg rriaayeayr svyedtmgla alerysaaah
      421 egmrrce
//
LOCUS       WP_457656632             300 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656632
VERSION     WP_457656632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..300
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32726
     Region          26..294
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mslrlstvil pvhrwheggr drwqraeelg fhtaytydhl swrsfrdgpw fgalptltaa
       61 ataterlrlg tlvtspnfrh pvtlakelis lddisggrit lgigaggngf datalgqeaw
      121 tpreradrfa efvplldrll tegavtergt hyaaeearni pgcvqrprlp favaatgprg
      181 lrlaarhgqa wvttgdpkly engtpeesra alraqnekft aacaeigrda aepdrvlltg
      241 ftpdrtaple svdafvdfag rhaelgftei vvhapipdsd fdvdpkvfer iateapaqlv
//
LOCUS       WP_457656633             285 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457656633
VERSION     WP_457656633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..285
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29500
     Region          14..277
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mtsvtdaplp avtrliatdl dgtllrddkt lsartvaala aaeesgievf fvtgrparwm
       61 dvvrdhvqsh gtaicangav vtdlrtdgdl lsvrplerga alhvvrtlre aapgtsfave
      121 mttginyepa yppfhldpga tvavaekllh edapglgapv ikllahhtel apdaflglar
      181 taagdraaft rsspsallev sglgvskatt laaccaergi apaevvafgd mpndiemlrw
      241 agasfamgna hpdavaaasg rtatneedgv alvierilag rrdtp
//
LOCUS       WP_457656638             160 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457656638
VERSION     WP_457656638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..160
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17659
     Region          <52..155
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mggvenvgvp edgtartper lrrrpsrlls qltvrsdrli sdglvrgdar kwhyavlasl
       61 eeygpgsqae lskrsgihrs dmvgvlnela erglvervpd pedrrrnvit vsalgrrrls
      121 lldealdgle gellaplsps erdqlvrllt rlldhhtgaf
//
LOCUS       WP_457656643             423 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457656643
VERSION     WP_457656643.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..423
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45616
     Region          15..423
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mrpdrtsddd stddiedllr rhapqvlgal vrryghfdpa edsvqealia aagqwpedgi
       61 pdnprgwlir vasrrltdrl rsdearrrre etaaaltpad afvapppgeg psgpgrapse
      121 ddtltllflc chpalspaaq ialtlravgg lttaeiarah lvpeatmaqr israkrtvrg
      181 trfrqpdaqd rdqrlaaalq vlylifnegy tatagpdlhr tdlareairl travrrllph
      241 egrvtgllal mvlteartpa rtgpdgelip ldeqdrgrwd rdaiaegtal aqealaqgpa
      301 gdyqlqaaia alhdeaerae dtdwpqilal ydllvrrtpd paaalgrava vamvhgprag
      361 ltavdalaga veppyrldav rghllerage paaaraayla aadatlsepe arylrmragr
      421 lap
//
LOCUS       WP_457656644             407 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656644
VERSION     WP_457656644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=42674
     Region          8..>294
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mrqniqqhrv vvigagytga taagrlarrl rsedvsitlv naepdfverv rmhqlaagqd
       61 lrprpyremf agtgvrlrla kvtgvdvdrr tvsvtapdga gepedlaydt lvyalgsawn
      121 thavpgaaeh ahdiagrpga lrlrerlaal gpgepvvvvg ggltgveaat eiaetrpdld
      181 vsliargalg dwlspkgarh lrkvftglki tahehttata veadrvttae gdipaavtiw
      241 ttgfsvhpia rattlqtgdt gqivvdatmr svshpdvyai gdaalvagpg dkplrmscas
      301 gvptawqaad aiaarltdgk lptisaryfn qcislgrkeg liqyvtaddr avsaaltgrl
      361 aafykelvck gaawgvanpt lglptrrrrt tsepapastt vtaaeaa
//
LOCUS       WP_457656646             244 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457656646
VERSION     WP_457656646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..244
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26122
     Region          1..237
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mptktvqipt adglsdafaa rpdqgdrhpa vlmyadafgi rpvvremare laghgyyvlv
       61 pnffyrngpt pvvglpehig eedrpaligr lmplieahtt ervlrdaday lgfladqpev
      121 aagpvavtgy ciggllatrt aaarpgqvaa laafhapvaa dgpdslrrlt aevhfghaat
      181 dvtpealgel nrsldaarid ytseiypdtv hgftmsdtda fdpaglrrhw drllplltra
      241 lthg
//
LOCUS       WP_457656648             552 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces griseus].
ACCESSION   WP_457656648
VERSION     WP_457656648.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  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 552)
  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 18638503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..552
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58310
     Region          138..394
                     /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          228..254
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          263..517
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          263..291
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(264,267..268,271..272,274,298,301..302,305..306,
                     308..309,332,335,338..339,342)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          296..326
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          331..358
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          368..396
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(369,372..373,376..377,379,403,406..407,410..411,
                     413..414,437,440..441,444..445,448)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          401..431
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          436..464
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdvmpqqdpg srrppeqssq dpcampaega tavppppptl rttlrraavg avaagvllag
       61 alvavddgeg dgpkepgpve raeaattags paslsdltal igdrqkwves hpedapslat
      121 lgtayvewar rsadtayyar aeqalkrsle aqpgergnge awvglaalan arhdflaakr
      181 wgetvrkqqp kswsvypvli daytglgdqk aataatekfg elrkgvpala rtadlyrgqg
      241 wredalatar eaadratqpa ekaealhrlg elawergepe eavaqfdaal rtdaghhpal
      301 agraralval drtdealaay qsaleqlprp eyalelgely eslgldgdar tqytklremv
      361 aeakkagade slvlarfead hgepeaavel lraqwrgqhr saavadalgw alhragksee
      421 gleyaeravd tgvrnasyay hlgviqrela dygparrnle qavrtnpafs plaaplarea
      481 ldalgepppg gpgdmqpppp ppapeptpep kreqekkpea papaasktaa apsespspta
      541 spspsptaak sp
//
LOCUS       WP_457656649             455 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656649
VERSION     WP_457656649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..455
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47488
     Region          1..455
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msdllerlra glppealitd pdvtasyahd masfceagtp avvvlprave qvqhvmrtat
       61 alrvpvvpqg artglsgaan asdgcivlsl vkmdrileis pvdriavvep gvvnavlsra
      121 vnehglyypp dpsswetcti ggnigtasgg lccvkygvta eyvlglevvl adgrllttgr
      181 rtakgvagyd ltrlfvgseg slgivvkavl alkpqppqql vlaaefpsaa aacdavcrim
      241 erghtpslle lmdrttvrav namasmglpe ttealllcaf dtpdpladla avgelctaag
      301 atevvpadnp aeselllqar rmsltaletv ksatmiddvc vprsqlgaml agtaaiaeqy
      361 dltigvcaha gdgnthpvvc fdhhdpdesr raresfdaim alglelggti tgehgvgvlk
      421 kewlarelge tgvelqrsvk aafdplglln pgklf
//
LOCUS       WP_457656655             177 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Streptomyces
            griseus].
ACCESSION   WP_457656655
VERSION     WP_457656655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..177
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=19194
     Region          71..173
                     /region_name="MazF"
                     /note="mRNA-degrading endonuclease MazF, toxin component
                     of the MazEF toxin-antitoxin module [Defense mechanisms];
                     COG2337"
                     /db_xref="CDD:441908"
ORIGIN      
        1 mdtfwwvala avvllalvaa vvdgrgrsdr gprsrrprqp vgstrppsrp srpsrpsgpd
       61 argggreegr tpragevwwa dvpyedgpgs kdrpclvisv rgrgrgrtal vakitskhhe
      121 erpgvialpa gtvgdrqgrq sfletdelre vrlagfrrrv gavdpslwer vrklgag
//
LOCUS       WP_457656654             265 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656654
VERSION     WP_457656654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28200
     Region          4..252
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mttlrtegls ygtgegrhlv davdltaadg etvglvgpng sgkttllrcv ygtlrpthgr
       61 vlldgddlat lpvkaraqri atvpqdghag feltvgqvva mgraphkrfw eadtaadttl
      121 vtealdrvgi aaleprtfas lsggerqral varalvqqps lvvldeptnh ldiryqleil
      181 slvrdlgttn llalhdlnla ayycdriyvl qdgrvvasgt pekvltaell sevygvtaev
      241 sthpktgapt vvylpegraa rqkst
//
LOCUS       WP_457656656             211 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Streptomyces
            griseus].
ACCESSION   WP_457656656
VERSION     WP_457656656.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10649802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..211
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23545
     Region          141..196
                     /region_name="HNHc"
                     /note="HNH nucleases; smart00507"
                     /db_xref="CDD:214702"
     Site            order(172,174..176,178,187..188,192..193,196)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mgparytrel leeaarmttn atdavrwcgr tptpgsrryl rqkmaeagis tshfadtrvr
       61 hteerlrelv arstsvaevv rrlgispvgg nqahigrrit alridtshft aappggrrsk
      121 gssgdlltlr tpsdgrvpge rlrrelvrmg venkcaecgn ngewlgqplr levdhvngdw
      181 wdnrpenlrl lcpnchaatd tyrgrkrrrt a
//
LOCUS       WP_457656657             799 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656657
VERSION     WP_457656657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..799
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=82513
     Region          80..724
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msdepqhwap repsdaaatp ggdrggppgt dahgaqgaks gkggkkrrpr rtgwrravpt
       61 wrmvlgtvlg lglllvggiv agyqlvdipa anasataqsn vylyndgsvi ardgdvnrek
      121 vklsqvpmav qhavlaaedr dfysddsavd vkamvragwn tvtgkgkqgg stitqqyvkn
      181 yylgqertvl rkakeaiiav klnrevtkdq ifegylntsy fgrnaygiqa aaqayygknv
      241 eelstaegay laallnapsa ydvvahpdnk paaqrrwnyv lngmvkedwl paaerattrf
      301 ptpgeakpst glsgqrgyiv qavedylnrh gildektlat ggyritttld kakqdafvka
      361 vdtnvtarts tdrkadrdvr vggasivpgs gavvalyggi dytkqyvsna trrdyqvgsv
      421 fkpfvltsav vndsttqdgr pitpntvydg snkrtvvgpq gatdyapane ddvdhgditv
      481 rtatdesvns vyaqmaqdvg pgkvrdtaia lgipadtpdl taspsialgp anasvldmae
      541 ayatladhgr hgpyvlvdki tkdgaevelp ertteqavsr eaadtttavl rsvveggtgt
      601 aaqavgrpaa gktgtaeedr aawfagytpd latvvavmgq npdtgaqtsl ygalglprin
      661 gggapaetwa ayteaalrss paqefdletm pgsdeedepl ldedsdgste psaasdatap
      721 satapsgtap sspaassapt sgtdtggadg tggtggttgg nasggsggtg gtegtggagg
      781 tggltegarg pdfpdgrpv
//
LOCUS       WP_457656658             266 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656658
VERSION     WP_457656658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28655
     Region          1..266
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mrlyavvagg afrryatyrt ataagvftnt vfgfimayty ialwdarpql ggydtsqalt
       61 yvwlgqallm tcammgggfe delmerirtg diavdlyrpa dlqrwwlagd lgraafhllg
      121 rgiapmvlga fafdlalpgs pwtwpaflls vflgvvvsfa vrylvalsaf wlmdgagalq
      181 ivslaglffs gmllplnlfp gllgevaral pwssllqvpa dvflgkhtgw glveayafqg
      241 gwavvlllag rllqtaatrr vvvqgg
//
LOCUS       WP_457656659             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656659
VERSION     WP_457656659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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 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   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 328)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=36348
     Region          7..327
                     /region_name="COG4586"
                     /note="ABC-type uncharacterized transport system, ATPase
                     component [General function prediction only]"
                     /db_xref="CDD:443643"
ORIGIN      
        1 madggfitld gvekvfqvrr kaglvrrerh evravdgisf rvargemvgy igpngagkst
       61 tikmltgilt psggrlrvag idpsrertrl ahrigvvfgq rttlwwdlpl rdsyrlmhrm
      121 yripdrryre nldrcvelld lgelldvpvr qlslgqrmrg diaaallhdp evlyldepti
      181 gldviskakv rqflkelnae rgttvlltth dltdieqlcn rvmvidhgrl mydgsvaglh
      241 eagesermlv vdlerelppi vlapeaaggt palravkveg prqwlafpaa vsaaplvari
      301 aaeyplvdls vrepdieavi armyesap
//
LOCUS       WP_457656660             415 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457656660
VERSION     WP_457656660.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..415
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=42959
     Region          207..400
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(214,250,289,383,386)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(214,383,386)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(214,250,289)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mprrqgyall ialvagtavl aaavafgttl lsgprstplp paetqaaarn pvdpaasggt
       61 wvatwtaapv rgepgteggl pghtirnvvh tsiggnvari tlsnlfgtap lvidqatvnt
      121 rpvtfkgaaa vtvaaggrvi sdpvvvpvap dsdlqvsfrt pqaggpvtyh pnshqtsyli
      181 dergtwttth wryltavdvr serargavva lgdsltagsg sttdanarwp dvladrlggr
      241 ygvanagiag nrvvgvgrgt ggqagtdrld rdalsvagar tlvvalgind vqqspqeadp
      301 rrivdslral adrahargls vvgatltpfe gfatwtpqre avrqavneqi ragtvfdayv
      361 dfdaavrdpa apgriltsyd sgdhlhlndd gyralgdhvd pklldragap rsdal
//
LOCUS       WP_457656664             233 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces griseus].
ACCESSION   WP_457656664
VERSION     WP_457656664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..233
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25892
     Region          1..191
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mrtlyvvthp eathhvegvv ggwhdsqltp egvraaaava ralrdripdg tevelyssdl
       61 rrtrrtadav aelfgvrpvl drrlreksyg eaegrpqewl drrfvpppav germdhdegv
      121 rgaetkmvwa rrvyaamdei lsspcehqiv vthggsltcv vaswirmpie aagyaafrap
      181 agsittlred dffhnrqvag lgdtrhldqe raspepegka lpprlpdssr fqr
//
LOCUS       WP_457656666             331 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656666
VERSION     WP_457656666.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34414
     Region          28..328
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mveqadpgva svarpvapga gggrrgrvls glavvvaggl afhrvvpnsp grvgsllesf
       61 lpwvgvfvvv llvvalvrrs avalvalllp vgvwvhlfgg lllpygesgg relvvvqhnv
      121 sdenrdpaat aralsdvgad lvaleelvdp qlavyeeala sdyphhvvrg tvglwskypl
      181 sgarlvdikp psieegwsrg vravvrspyg dvaayvahlp svrvgaggla sqrrdesaal
      241 lgraiadesv etvillgdln gavedrglsp ltsrlnvaer gfalsfpaaf pvaridqvma
      301 rsavvghirt lpatgsdhlp vvarvvlpgh r
//
LOCUS       WP_457656667             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656667
VERSION     WP_457656667.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31487
     Region          12..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(18,22,47)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(21,46)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(28..29,40,43,47..48)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          101..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpvrttttrr rqlgammrkl raskgmtlee agrlvgvska tvsryetqeg pvkwpivdal
       61 crqydateae rctvvalakd akqqgwwgpf sdsipadmnl lltledeavr edhfscmyvp
      121 gllqtrgyst aiqqanemrl apeeverlvd irmkrqeila rehpphlwai ldesvirrvv
      181 gsptimreql gqllranesp gitlqvlpfa kgahaaalgs fvilggaeps ldvvyvdlhv
      241 gsvfmeknhe ldryrlafey lraqaldmaa sssliervck ei
//
LOCUS       WP_457656668             193 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656668
VERSION     WP_457656668.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  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 193)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13014796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..193
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=20356
     Region          43..120
                     /region_name="HATPase_RsbW-like"
                     /note="Histidine kinase-like ATPase domain of RsbW, an
                     anti sigma-B factor and serine-protein kinase involved in
                     regulating sigma-B during stress in Bacilli, and related
                     domains; cd16936"
                     /db_xref="CDD:340413"
     Site            order(44,47,70,72,74,76..77,92..95,107,109,113..114,116)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340413"
     Site            order(82,95)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340413"
ORIGIN      
        1 mvpfeavpaq lsvlrravrs qlgcwgasav aeeaelaate lganvikhvg rdvaaslvle
       61 lrndrvrlev hdrsralpas laevcaende cgrglhliaa macdwgsvrt atgkavwcel
      121 alkpaeceer agcaaavlsa yrqlsstsel dpaaldetvt dvitdllhwl aarggdpdgt
      181 lgraqmhyea eaa
//
LOCUS       WP_457656670             611 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457656670
VERSION     WP_457656670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 611)
  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 611)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..611
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66582
     Region          8..573
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mtvqgepslr iafdvtrtra vlraqegrqs dlaqlaarfp gggprgplsa eieleaflvg
       61 igelgtwpsp edvewddela qlvggvldda daaqrqldgd ddeshqtith aeiagllgae
      121 waapltdfqq rdiarllslr hganfsvpga gktrvglavf aamrergeal rllvvspksa
      181 yeswefensv cfkeplrfgv mgnspdatae imvinyerlg rslaalaswl ratpsmvild
      241 eahrmklgtr giygsacmal gplsrrrlil tgtpapngar dlenllsfvw pghgrrvvtg
      301 avaggdlaya sqvlrplftr ttkselglpp fdpkiryvdm pslhqeiyda lvgrytarae
      361 aarddfdalg kamlrllmaa tspallaegt sryepltyqv ppldvphgds lytlmrdlps
      421 yelspkyqea lsivaanaeq grktlvwttf vrslstmerm fagyqpavvh ggtpdraeei
      481 rrfredpdcs vllsnpatlg egislhhvch davyvdrdfm agrflqsldr ihrlglapgt
      541 etnvtvlasr gtvdevvalr leqklefmgr ilddpsvqql adlqeeapva ggmdmadvra
      601 llrhvdavaa r
//
LOCUS       WP_457656672             217 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces griseus].
ACCESSION   WP_457656672
VERSION     WP_457656672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23926
     Region          78..144
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 malwlrdevg vgntfskaal raaitgaeqv drrmrdlrpa gwviktnldk pslqpdqlfl
       61 evigapvwek ehraaglrqi saktrrfvle rdlhrcrrcg vgaaeaypge pgsaarltlg
      121 hvnphaagss agaedlltec arcnelvknl tgvqmdagqv wtrikalpla qkrellawmd
      181 adarpsrpvd rawgmyrqlp avlrdemkdd lrgltes
//
LOCUS       WP_457656677             506 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces griseus].
ACCESSION   WP_457656677
VERSION     WP_457656677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 506)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 506)
  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 506)
  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 506)
  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..506
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..506
                     /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=52827
     Region          35..454
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnaavatsvf avfmvatval gllalrgrgg gggldewsvg grslgpvfiw vlmagegyts
       61 fsylgaagwg ynygapvlyv vaymscgyai gyvvgpmlws yarrhglvgi tdmvahrfgr
      121 pwlgavvavl atvfllpyiq lqitgmgvvl svisygavsl nwayfvafav ttgfvvvsgl
      181 rgsawvsvlk dvlviatlgf lalyvplhyf dgygsfldrl vteksdwltl pghggggagg
      241 sggsglgevw fisttflnsl tvvifpttva gylgarnada lrrnamylpa ynvllfvpml
      301 lglaalfvvp glagaesnla lfklvvdalp awavgvigva aalssivpma vfmlvigtmw
      361 grsvlsllpr lahadrqksa aqvvvvvags lallltytap ntlvrlslis yegmaqllpm
      421 vllalvwrrl tfrgafsgli vgvavvcalv fsgndpvwgv naglvalaan lavalavtfa
      481 grpdadprpd aevladdrde yaadpv
//
LOCUS       WP_457656678             286 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656678
VERSION     WP_457656678.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30433
     Region          69..281
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkllrvgtag terpalldrd gtlrdlsgiv pdidggllad asalarvraa aeapgvlpal
       61 datglrigpp lgrigkivci glnyhdhaae tgaeipaepi lffkapdtvv gpddtvlvpr
      121 gsrktdweve lavvigrtar ylesaeegla hvagyatahd vserefqier ggtwdkgknc
      181 etfnplgpwl vtadevpdpq alplrlwvng elkqngttae qifpvgevvr ylshfmtlyp
      241 gdvintgtpa gvamgqpepk pylragdvve levaglgrqr qelkda
//
LOCUS       WP_457656685             643 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces griseus].
ACCESSION   WP_457656685
VERSION     WP_457656685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 643)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..643
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=68923
     Region          59..640
                     /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 msgtsegpsa pagtasggps apvterhaaa vdptparpag adpspagpcr adagdgptaa
       61 elrdyraafn aatlpmgvvd grghvvrane alggllgapa avlagrqacd lldlasddrt
      121 whayrevllg rrsrfrctrr lkhpdgrslw aeitvvpmtg asaaesarvl ltvadvsdrl
      181 elqerlrhlq mhdpvtrlpn rtlfferlas aletppyqdd slpprqhgri glcyldldgf
      241 kaindtlghr tgdrllaava arltdcaend asrtpggsrl varlggdefa ilvedstgte
      301 eltdlarsvl talqqpfdla gqrlsvsasi gvvertaagt sptglmqaad ttlywakadg
      361 karwtvfdpe rnahrmtrqs lsstlrpave rgeftleyqp lvgmadgvlr gvealvrwnh
      421 pqfgvlppnr fvqiaeedgs ivqlgrwvlr tacrqarrwq ldhpdepplf isvnvavrqv
      481 wdsdlvadva eilaetelap gllqleltes avmgsggrpl ralqalsdmg vriaiddfgt
      541 gysnlaylsr lpvsvlkldg afvkgfryed gthpspadet iveamvqlah rlgltvtaec
      601 vetagqaerl rrigcdtgqg wlysravape qiagligsrp leg
//
LOCUS       WP_457656688             491 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 18 protein [Streptomyces griseus].
ACCESSION   WP_457656688
VERSION     WP_457656688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Poria,V., Rana,A., Kumari,A., Grewal,J., Pranaw,K. and Singh,S.
  TITLE     Current Perspectives on Chitinolytic Enzymes and Their
            Agro-Industrial Applications
  JOURNAL   Biology (Basel) 10 (12) (2021)
   PUBMED   34943233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Chen,W., Jiang,X. and Yang,Q.
  TITLE     Glycoside hydrolase family 18 chitinases: The known and the unknown
  JOURNAL   Biotechnol Adv 43, 107553 (2020)
   PUBMED   32439576
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huang,Q.S., Xie,X.L., Liang,G., Gong,F., Wang,Y., Wei,X.Q.,
            Wang,Q., Ji,Z.L. and Chen,Q.X.
  TITLE     The GH18 family of chitinases: their domain architectures,
            functions and evolutions
  JOURNAL   Glycobiology 22 (1), 23-34 (2012)
   PUBMED   21750098
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Zaheer-ul-Haq, Dalal,P., Aronson,N.N. Jr. and Madura,J.D.
  TITLE     Family 18 chitolectins: comparison of MGP40 and HUMGP39
  JOURNAL   Biochem Biophys Res Commun 359 (2), 221-226 (2007)
   PUBMED   17543889
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Simpson,P.J., Xie,H., Bolam,D.N., Gilbert,H.J. and Williamson,M.P.
  TITLE     The structural basis for the ligand specificity of family 2
            carbohydrate-binding modules
  JOURNAL   J Biol Chem 275 (52), 41137-41142 (2000)
   PUBMED   10973978
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Aronson,N.N., Blanchard,C.J. and Madura,J.D.
  TITLE     Homology modeling of glycosyl hydrolase family 18 enzymes and
            proteins
  JOURNAL   J Chem Inf Comput Sci 37 (6), 999-1005 (1997)
   PUBMED   9392855
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10652546
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..491
                     /product="glycoside hydrolase family 18 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50117
     Region          49..141
                     /region_name="CBD_II"
                     /note="CBD_II domain; smart00637"
                     /db_xref="CDD:214754"
     Region          199..488
                     /region_name="GH18_PF-ChiA-like"
                     /note="PF-ChiA is an uncharacterized chitinase found in
                     the hyperthermophilic archaeon Pyrococcus furiosus with a
                     glycosyl hydrolase family 18 (GH18) catalytic domain as
                     well as a cellulose-binding domain. Members of this domain
                     family are found not only in...; cd06543"
                     /db_xref="CDD:119360"
     Site            order(202,229,268,304,306,308,374..375,419,453)
                     /site_type="active"
                     /db_xref="CDD:119360"
ORIGIN      
        1 masrthrrtt ttrtraigai vaaaviggtv faltgtaqaa aigaaytrts dwnggytgqy
       61 vvtnetdkpl tdwtlefdlp agtrigslwn gehtvqdnhv tvkpaswdke lapgrsvtvg
      121 fvtsatgtag dpagclinda acsvdggatp tpsgrptdtp ttaptptatp sataptsppt
      181 ptptatgrpg gggetgarfa pyvdtslypa ydlldtatkt gvkefhlafi tsgggcaplw
      241 ggvtglgddq vasqigalre nggdvrvsfg gaagaelaln cssadelaaa ygkvvdaygl
      301 tkvdfdiega alpdtaantr rsqaiaqlqk kypdldvaft lpvmpegltq pgvdlladak
      361 kngvrvdgvn imamdygpay sddmgeyaiq aatatqaqik gvlglsdaaa wqtvavtpmi
      421 gvndvvteif tvedagqlve fagqkgigrl amwsgtrdka cpggpkpaad atcssidqep
      481 laftkafaay q
//
LOCUS       WP_457656690             592 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces griseus].
ACCESSION   WP_457656690
VERSION     WP_457656690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..592
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66118
     Region          12..590
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mttaltdsva hlsperwata nrllvrkala efsherllap tpigdgrftv rsddasteyr
       61 ftarlfaldh wqveaesitr hrhgselpld tlefftemrh tlgiseeilp vyleevsstl
      121 agtaykltke patsrqlvaa gfqaietgmt eghpcfvann grlgfgvdey rayapeaaae
      181 irlvwlaarr dratftagag ldydtlitde lseatrerfd galrglgldp qdyfllpvhp
      241 wqwwnklavt fagelaerhl vvlgegedgy laqqsirtff nadhpekhyv ktalsvlnmg
      301 fmrglsaaym eatpaindwl aglverddll rgarfsiire raaigyhhrs yeaatvkgsp
      361 yrkmlaalwr espvpglrpg ervatmasll htdheggsva galitesgld pqawlrhyld
      421 aylvpvlhsf yaydlvymph genvilvved gvvartifkd iaeeiavmdp davlpprver
      481 iraevpedmk llsvftdvfd cffrflgagl ategvldedt fwrtvaacvr dyqesvpyla
      541 dkfkqydlfe aefalsclnr lqlrdnqqmv dlndpagalq lvgrlknpia gf
//
LOCUS       WP_457656689             196 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Streptomyces griseus].
ACCESSION   WP_457656689
VERSION     WP_457656689.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..196
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /EC_number="1.14.99.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20683
     Region          1..>196
                     /region_name="COG3397"
                     /note="Predicted carbohydrate-binding protein, contains
                     CBM5 and CBM33 domains [General function prediction only]"
                     /db_xref="CDD:442624"
ORIGIN      
        1 mrrkitslll glgiagvsll atfgsaqghg ytdspvsrqq lcgdgtvrgc gqiqweppsv
       61 egpkgfpaag prdglicagg nqrfaelddp rggawpasrv sagashtfrw ritarhattd
      121 fryyvtkdgy dpakpltrad lepqpfltvp fggrqpgstv thagalpqks gkhlilgvwt
      181 iadtgnafya csdvtf
//
LOCUS       WP_457656691             304 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457656691
VERSION     WP_457656691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..304
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32508
     Region          3..274
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtsttattpe vapfrlfdla vlrtrrlgps ilritlggag iegfsgggrd qslsvllprp
       61 gqdeavvpag gsgtwhekwr alpegeravm rtytvraqrl radgstevdl dfvlhgdggp
      121 asrwartaap gdrlkvlgpa vadntavrfr ppadtdwvli radesalpaa aaalewlpag
      181 lparvwldip ctedrqalnt aakariswlv rsegaarcve avraaelpqg tpyawiagea
      241 sgvraldhhl irergfgrer vtcaeywrrg lsedqsreaa ataraagsga verpegkreg
      301 rveg
//
LOCUS       WP_457656692             219 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656692
VERSION     WP_457656692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..219
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23770
     Region          18..181
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mdhreittpg hwplyglrlr tprlelrlpg lelldelasv aadgvhdpdr mpfsvawtdg
       61 speavgravf qhllgtvagw svddwtlsla vlhegkvvgr qdlmargfgv rrqaetgswl
      121 glpyqgrglg temraaalhl afaglgarya asaamtdnpr slgvsrrlgy addgletdvv
      181 rgapvtlrrl rldrarweah rsvdvtvegl dacraefgv
//
LOCUS       WP_457656693             476 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656693
VERSION     WP_457656693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..476
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48812
     Region          12..410
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,138,
                     141..142,145,268,271..272,275..277,280,308,312,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtgrawgvll vlcgaifleg idvamlnval pairedldls tgtlqwvmsa yvlgyggfml
       61 lggraadlfg rrrmfvlwlv vfllfsglgg lategwmlit arfvtgvaaa fmtpaglsii
      121 ttgfpegpqr nkallvyagt aaggfsiglv vggllsavdw rwvffapvil sfgillaala
      181 lipapprpdr tgkgvdlaga vtvtagilll vlgveratha sagwtvgtig aalllflafv
      241 lierassspl vrlgifrsga lvranvsgll faagffgfqf iavlylqelr gwsslhtsfa
      301 livigvdavl splltpklva rfgnarvifg gllvaslsya lflpiaadwt yaamfpglll
      361 lgvsfslvyg pltitatdgi aeeeqgvagg llytsfqfga alglsavaav niaatdgssp
      421 salldgyraa lvvplvaalv aaavsafglr trrattpgsg tsadaggveq pagvga
//
LOCUS       WP_457656694             148 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457656694
VERSION     WP_457656694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..148
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16780
     Region          29..129
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 meegtsksps hcadtgagpd ydisqwdvre gcevrqildr vadkwsllai ahlerrtlrf
       61 selrrliegi sqrmltvtlr qlerdglvrr tvypvvpprv eyeltelgat lhatirslvd
      121 wteshqpeia karadydrrq eaeaapvs
//
LOCUS       WP_457656700             322 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Streptomyces
            griseus].
ACCESSION   WP_457656700
VERSION     WP_457656700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..322
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34029
     Region          15..309
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msdakadeta dggestftvi vaaaanlgia vakavaglis gssamlseaa hsvadtvtev
       61 mlltalrrse kpadedhplg ygperyiwam lasiatfvgg avfsiydgvh tlvageelgd
      121 plvsyivlgv afllegyslr tgvkqvrrea srlrvpdtyy lrhtpdtavk avvmedsaal
      181 tglllaaggl lggqlsgsgv wdgiasclig vllvyvawvl granaqllig rplpramrvg
      241 vreellsvph ivdvlelttl iqgpaeilia akidfrdmat aaevewacee aeaqlrerfp
      301 svrrvyldpt pgraqrlrrg gp
//
LOCUS       WP_457656703             236 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces griseus].
ACCESSION   WP_457656703
VERSION     WP_457656703.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..236
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24962
     Region          19..219
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mqqknenene nenendlliv edltllmmdd ksgaiagegt lyytlggavl velglgghia
       61 adendqglng vkvhavgsrt psdpllraaq akvgervrgv qtllieigtg vvkretvldr
      121 lvergmlrqe tkktlglfrt tsttvadtgy kkalvekvra vlidgaepdd rtaaltglls
      181 asgtlptlhr sipwsgkvyk rakeleqssw gaeavnaavm rtvaaisagt vvaats
//
LOCUS       WP_457656705             310 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457656705
VERSION     WP_457656705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  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 310)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..310
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32715
     Region          78..182
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mahdahttap ahrhdhghth gnghghgnah ghgnshahgs datpnglpei ldldaalfap
       61 hltaltgria clagddvrhi vdlgsgtgtg tfalleqfpt arvtavdssp amlerltsaa
      121 rdrglgdrvr tleadagagl pgvvdadlvw asaslhhldd paaalagira alrpggllav
      181 aevdgmpkfl aedgpwgele arcrealdgl haermphrga dwgallaaag lpveqeraer
      241 welraplpeg agryaylvfe rirgtlegrv daedlaaldr lvdggpedvr hrddlvvrst
      301 retwmarrpa
//
LOCUS       WP_457656710             400 aa            linear   BCT 27-JAN-2026
DEFINITION  MinD/ParA family ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656710
VERSION     WP_457656710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Lutkenhaus,J.
  TITLE     The ParA/MinD family puts things in their place
  JOURNAL   Trends Microbiol 20 (9), 411-418 (2012)
   PUBMED   22672910
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Szardenings,F., Guymer,D. and Gerdes,K.
  TITLE     ParA ATPases can move and position DNA and subcellular structures
  JOURNAL   Curr Opin Microbiol 14 (6), 712-718 (2011)
   PUBMED   21963112
REFERENCE   3  (residues 1 to 400)
  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   4  (residues 1 to 400)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Surtees,J.A. and Funnell,B.E.
  TITLE     Plasmid and chromosome traffic control: how ParA and ParB drive
            partition
  JOURNAL   Curr Top Dev Biol 56, 145-180 (2003)
   PUBMED   14584729
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418836
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /product="MinD/ParA family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42189
     Region          172..399
                     /region_name="FlhG"
                     /note="MinD-like ATPase FlhG/YlxH, activator of the
                     FlhF-type GTPase [Cell cycle control, cell division,
                     chromosome partitioning, Cell motility]; COG0455"
                     /db_xref="CDD:440223"
ORIGIN      
        1 mpnadnwqgd vlrdlrgtpp qsatgrgpah ghapaqnhgs vqgpapaqeq gpaqaqhqpq
       61 rqpqertate ssgaqppsrs apataparar rparspdsrp vvdsaltgta rrprqgepaa
      121 arisrairri vsssaareva eitrtaealq qpvttgrqia vtsirggagk ttvaallgta
      181 yahyrhdpvl lveadpalgs lplrlgaetl rwttadlael vepqmslldv tgylvqlpdn
      241 awllpgsqgr igamldtaay ervmvalrry fgvtvvdcet lpaevarval saaqarvlaa
      301 patldgitst yavlqwmqgl prhliagtvv altsttprpg idveaaaekl rstgaavqvl
      361 phdrhlaagg elrtellarp trlaatrlaa evfqlsqkrr
//
LOCUS       WP_457656701             795 aa            linear   BCT 27-JAN-2026
DEFINITION  excinuclease ABC subunit UvrA [Streptomyces griseus].
ACCESSION   WP_457656701
VERSION     WP_457656701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Pakotiprapha,D., Samuels,M., Shen,K., Hu,J.H. and Jeruzalmi,D.
  TITLE     Structure and mechanism of the UvrA-UvrB DNA damage sensor
  JOURNAL   Nat Struct Mol Biol 19 (3), 291-298 (2012)
   PUBMED   22307053
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Truglio,J.J., Croteau,D.L., Van Houten,B. and Kisker,C.
  TITLE     Prokaryotic nucleotide excision repair: the UvrABC system
  JOURNAL   Chem Rev 106 (2), 233-252 (2006)
   PUBMED   16464004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..795
                     /product="excinuclease ABC subunit UvrA"
                     /GO_component="GO:0009380 - excinuclease repair complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009381 - excinuclease ABC activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006289 - nucleotide-excision repair
                     [Evidence IEA]"
                     /calculated_mol_wt=84858
     Region          17..792
                     /region_name="UvrA"
                     /note="Excinuclease UvrABC ATPase subunit [Replication,
                     recombination and repair]; COG0178"
                     /db_xref="CDD:439948"
ORIGIN      
        1 maprtktqqp paphaadshd lirvhgaren nlkdvsielp krrltvftgv sgsgksslvf
       61 atiaaesqrl inetypafvq gfmptqarpd vdvldgltta iivdqqrmgs dprstvgtat
      121 danamlrilf srlgtphigp pgafafnvps vtasgaitve rgnkkavkat fsrtggmcqr
      181 cegrgrvsdi dltqlyddsk siaegaftip gwksdswwtv riyaesgfld pnkpiakftk
      241 remqdflhke ptkvkvegst ltfeglipki qksflskdre amqphirdfv dravtfatcp
      301 ecegtrlteg arsskikkis iadacsmeir dlaewvrgld epsvapllea lqqtldsfve
      361 iglgylaldr psgtlsggea qrvkmirhlg ssltdvtyvf deptiglhph dirrmndlll
      421 rlrdkgntvl vvehkpeaia iadhvvdlgp gagtaggtvc fegtldglra sdtvtgrhld
      481 draalkgevr kstaaleirg atshnlqnvd vdiplgvltv itgvagsgks slvhgsipag
      541 envisvdqsp ikgsrrsnpa tytgllepir kafakangvk palfsanseg acptcngagv
      601 iftdlgmmas vsspcedceg krfqpsvldy hlggrdisev lamsvteaee ffgsgeaalp
      661 aahkildrlv dvglgylslg qplttlsgge rqrlklathm gdkggvyvld epttglhlad
      721 veqllglldr lvdsgksviv iehhqavmah adwiidlgpg aghdggkivf egtpadlvaa
      781 rstltgehla eyvge
//
LOCUS       WP_457656718             610 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces griseus].
ACCESSION   WP_457656718
VERSION     WP_457656718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..610
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63752
     Region          52..555
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mphrtsrrtl ltataaataa avtgvlaapt aasahsadgf tdhrlrriia gmsleekvgq
       61 lfvmrvyghs atepdqadid anlkeigvrt aaelistyhv ggiiyftwah ntrdphqiag
      121 lsngiqraal aerhrvpllv stdqehgivc rvgepatllp gamalgaggs rsdtrraawi
      181 agaelaalgi nqnyapdadv nvnpanpvig vrsfgsdpda vadlvaaqvk gyqgagiast
      241 akhfpghgdt ntdshtglpv inhtraqwee ldappfraai raridsimta hivvpaldps
      301 edpatlsrpi ltgilreelg ydgvvvtdsl gmegvrtkyg ddrvpvlall agvdqllnpp
      361 nlsvawnavl eavrsgeise aridasilri lrlksglglf rdpfvshrgv ertvgsrahr
      421 aaadriaert ttlladpgtl lplsrrthrk llvvgadpas psgttgpptg tlahafgelg
      481 ftaralstgt apdrakiaea vaaaegkdav vvatynvtat ssqrtlvtal vatgvpvitv
      541 avrnpydvah ltgtgvaasl aayswtdvel raaarviagr adpegtlpvp vqraddptqv
      601 lypvghglty
//
LOCUS       WP_457656722             384 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Streptomyces griseus].
ACCESSION   WP_457656722
VERSION     WP_457656722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..384
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39982
     Region          17..174
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
ORIGIN      
        1 melaelvarr pfpaagllig ltrrcplrca hcstgsdlft rqepdggqle rfvgsfteen
       61 rpdvvmltgg eplllpalae rlstlarrag srtallsgmf farsgsarag grfgglsggr
      121 rgaaippail rairsvdhfs asldvhhere vpradvfral hriraegvav slhltgtgaa
      181 dpylagltra veeefggqvp clvnevrpfg raaawarpar sgpdpaaasp csmaawpvva
      241 fdgrvlaccn qdtvdrrpvp ahldlghiga ddwatvrrra lespvlrmlr tvgpthlaar
      301 ygsgppagsy cdgcralggd eaamagahav aggaagalld ltaavrgsre gaqgvvrrhg
      361 caayaplvvt ggpalpesea eevr
//
LOCUS       WP_457656729             281 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656729
VERSION     WP_457656729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30167
     Region          11..277
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtnddggdls rlsinqetlk qwslpelaeg cvkagidkvg lwrapvqeyg vertarllad
       61 agievtslcr ggfftaldpa traralddnr aaideaagls tdtlvlvsgg lppgsrdlhg
      121 arervgeala elapyaaard vrlaieplhp myaadrcvvs tlaqaldlae rfpaeqvgvv
      181 vdtyhlwwdd qtpaqiarag aggrihsfql adwitplpag vllgrgqlgd gsvdfrafrr
      241 wvedagfdgp ieveifneal wardgaeala evadryvrha c
//
LOCUS       WP_457656723             423 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656723
VERSION     WP_457656723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43099
     Region          11..392
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(21..22,25..26,29,61,116..117,119..121,124,144,
                     147..148,151,226,229..230,233..235,238,262,266,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 matplrsnrd frllwmsglf avlgsqmgal alpllilret gsavqagavg tvsvcavlit
       61 mlpggvmadr verrrlmrlc dvgslaavta ltlavwngha pmalvllvat agavlnsvya
      121 paafglmrav vppdqmgtat arlqartstv rlvgplvgga lfgvhqalpf vaqfvgllis
      181 tvcvalvrtr seartkagsv fsrreltagl aflwqlpylr tvllvfglgm nfafgaltft
      241 alavfseggr sglgggfvit cvsagalvga llaprlapdr hvrtlivitc wscvltaaal
      301 awvsspllag llcalcmgls tvasigflst llivtpedrl grvqsaasfl ssvvqpfgpl
      361 aggalltalg ssaafgvtgc vlavsaavvt lapsvragav pvpgrpaeep rpahdtagrp
      421 gal
//
LOCUS       WP_457656732             235 aa            linear   BCT 27-JAN-2026
DEFINITION  bleomycin resistance protein [Streptomyces griseus].
ACCESSION   WP_457656732
VERSION     WP_457656732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..235
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=25520
     Region          6..127
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,40,47..49,51,66..71,76..77,80,125)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(31..32,40,51,53..54,68,107,114,116,120..122,124)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 mtettipllp crtslietav dfytalgfet tylqkspyay avvergavel qlygmkdydp
       61 asshsgcyvl tddvdglhta fraglkaayg rvptrglpri gplkdmsygv rqflmtdptg
      121 ntirigqais ddpshrpapk etfaralhma dlfadskqdl pgaakiidrv lgltdeqptp
      181 vqrlrllvlr gdiaqrmgem eraaalleea aavrldadqq tlagdalarl aelrg
//
LOCUS       WP_457656735             434 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Streptomyces griseus].
ACCESSION   WP_457656735
VERSION     WP_457656735.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  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 434)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=46558
     Region          9..399
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mapndrpllt sieicagagg qaiglhqagf khlalveidt yavktlkqni eslpswswer
       61 qycdvisddv nnfrpipsek hpksslskpv kflggdlrrg dldllaggvp cppfshagkq
      121 lgkdderdlf prmlelvdel hpravmienv rgikdakfvd yrtyiearla ggrakrpetg
      181 leedfvgmgy eicewevlea sdfgvpqlrp ravlvairkd vigdikfvwp tpeggvrsvf
      241 aaletsmrer yhpyiaagga tggiarksld rwlkkasdaa agkrdggiap tlvggskkhg
      301 gadlgpsrak aawdtlgvdg mgvandhelg ekkksqgrdl fgpkgpmltv dqaatiqgfp
      361 eeweftggkt aqyrqvgnaf pppvaaavgq aiadvlraad erdgrtgalr qnalpgqivp
      421 aladgaddrq sagv
//
LOCUS       WP_457656740             355 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457656740
VERSION     WP_457656740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..355
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35483
     Region          <116..152
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          180..351
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(201,226,260,263..267,269,277..281,284,288..291,293,
                     301,306..311,326..328,333,337)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(201,289,291,293,306..311,326..328)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mrrnsrarlg vslllvagal glgaapstaa dtpaaapsai papsayalda kverslgdat
       61 agtyldaktg klvvtvttdr aeeqaratga tvrrvarsaa qldaamaale aeakitgtsw
      121 gidprtnrva veadssvsar dlarleavae rldgavdiqr vpgefrrevl gggaiygggs
      181 rcsaafnvtk ggaryfvtag hctnisanws assggsvigv regtsfptnd ygivrytdgs
      241 spagtvdlyn gstrditsaa navvgqaiqk sgsttkvtsg tvtavnvtvn ygdgpvynmv
      301 rttacsaggd sggahfagsv algihsgssg csgtagsaih qpvtealsay gvtvy
//
LOCUS       WP_457656741             347 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Streptomyces griseus].
ACCESSION   WP_457656741
VERSION     WP_457656741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
REFERENCE   2  (residues 1 to 347)
  AUTHORS   McGraw,W.T., Potempa,J., Farley,D. and Travis,J.
  TITLE     Purification, characterization, and sequence analysis of a
            potential virulence factor from Porphyromonas gingivalis,
            peptidylarginine deiminase
  JOURNAL   Infect Immun 67 (7), 3248-3256 (1999)
   PUBMED   10377098
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..347
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0004668 - protein-arginine deiminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37618
     Region          11..342
                     /region_name="AguA"
                     /note="Agmatine/peptidylarginine deiminase [Amino acid
                     transport and metabolism]; COG2957"
                     /db_xref="CDD:442197"
ORIGIN      
        1 mpptpapfrm ppewaphert wmawpgpnpt fasdaelaea rrawagvara vrrfepvtmv
       61 vgpgqeegaa allgpevelv vrplddawmr digptfvtdg rtlaavdwtf ngwgaqgwar
      121 weqdrhiara vagltgvpvh ssplvnegga ihvdgegtvl ltetvqlgee rnpgwskeqv
      181 eaeiharlgt ekaiwlprgl tgdygtygtl ghvdivaafa rpgtvlahvq pdpahpdhev
      241 trellavlra atdargrale vvevpaptvl rdedgewvdh syinhylcnd gvvlcafddp
      301 rdeeaaaifr glfpdrtvtl vdartifagg ggihcitqqq pkvranp
//
LOCUS       WP_457656742             376 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656742
VERSION     WP_457656742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..376
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40988
     Region          17..343
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttseqpeta pagtdvvlea rgvtkhfplr rtardlfare rrsvhavddv slrlrrgtvt
       61 alvgesgsgk stvarllaql hpltsgeirl ggepvvagrg rsfrryvrrv qlifqdpfas
      121 lnpvhtvryh ltralkihgr agngdaelae nlaallnrvq ltppqqfldk fphelsggqr
      181 qrvaiaralg adpqvllade pvsmldvsir lgvlnllrdl kerlhlaily ithdiasary
      241 fadttlvmya griveggdse tvtqhpahpy tqlliasapd pdriadgaeq eetgtgepps
      301 litppagcrf hprcpramer crtelpprfd lpdgqwaacw lyegtdrrta tdpdtratag
      361 adpraaagas aeevsr
//
LOCUS       WP_457656738             382 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656738
VERSION     WP_457656738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..382
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40076
     Region          92..382
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtgdyqelvd eisalldapa tlenrdfglv afgahdsddd tamdpvrtrs iltrrstpav
       61 rawfegfgit ratgpvripa apeagvfrdr vclpvrhrgv vlgyvwllda dpgptdeqla
      121 aamevaarig allsdevrag adlsrefgav ltagpgrqhd tavaalgeal grdaeglhtv
      181 vcvtpwaddt psvrgvasaa alatvtapga agprslaalv rlrspdrldp alsaadrlrt
      241 gagpaatggi aaprrgleel tvswreataa araaraetrf gpvarwsaig pyrlltalpg
      301 tgndpgdpav aslltplhre lahtaevfld cagqasrtaa algihrqtly yrlsriqqit
      361 gldlndgedr lllhmavkra rl
//
LOCUS       WP_457656743             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656743
VERSION     WP_457656743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35602
     Region          6..327
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msaepvltis glnvdygtda savhalrdid ltlhrgevlg lagesgsgks tlayavtrll
       61 sppgvitgge vhyhrpggdr vdilslapeq lrafrwqels ivfqgamnsl npvhtvhsql
      121 tdvlaahrpe lkkrqrtera eellelvgis adrlaayphq lsggmrqrvm iamalalepe
      181 ivimdeptta ldvvmqrqil rrlvqlreel nfsvvfithd islliefsdr iaimyggriv
      241 eqagaaeiyr dprhpysdgl lhsfpalhgp rreltgipgs pphlsamptg cafhprcgka
      301 fapcaaevpp lapptgepgr evachlhv
//
LOCUS       WP_457656746             314 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656746
VERSION     WP_457656746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..314
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31570
     Region          1..311
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,131,135,156..161,180..181,183,197,
                     240..241,256..258)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mravgvcefg gpealrvldl pepqagpgev rvrvhaaavs ptdvmlrtgg havrmpgrrp
       61 pfvpgmdaag vidqigpgag grlavgqrvv alvlftgphg gayaeqvvvp aasvvpapeg
      121 mgfpeastlp mnamtarlal dvldlppggt vavsgaagav ggyavelara dgltviadaa
      181 grdvetvrgf gadhvverga giadrirtlv pegvagvvdg saqtaelvpa isdggtlvel
      241 rgwpgpagrg irvcpvmvpe rigdtagldr lcrqaeagvl tprvaqvlpa aeaarahrll
      301 eagglrgrvv ldfs
//
LOCUS       WP_457656748             322 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656748
VERSION     WP_457656748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..322
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33511
     Region          24..283
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkqqrydvvi vgggaaglsg altlararrs vlvidagepr napashvhny lgrestppge
       61 llaigrgeaa gygaeivegr vasaerlpgd gnhgfrvvte dgrsvearrl lvttglvdel
      121 ppvpglaerw grevlhcpyc hghevadrpv gvlatgplav hqalmwrqws edvtlflhtg
      181 pepseeeyeq laargvavvd gevaglevad drftgvrlas grvvarealv vqarftarsa
      241 vleslglkav aqemggvvig syvpadptga tevpgvwaag nvtrlteqvi gaaaaglmag
      301 gaingdliae dtrdavaarr rg
//
LOCUS       WP_457656747             328 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656747
VERSION     WP_457656747.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 328)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     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 328)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35963
     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 mqtgkqssir rvtswqlvga qlrhlrklag mtqaalaeql gvgedtiasi eqgrralqld
       61 laiqldelle tkgvlrvave riprkeryqa lvkdfvqyeq davslisyes qlvpgllqte
      121 ayarfifgcn yppleedeie krvadrlgrq kilerkprpi lhfileesil haqmgdpevm
      181 reqllhlrrc mdlpfvtiqi mprntprhag lagplvllet pdhdglvyvd gqlrgelyde
      241 padvsalmqr ygmlrsqalt vaestrllda lldallgetc paqhtpplap ppstgsspat
      301 atvtaatask spttgvspat atvtaepa
//
LOCUS       WP_457656749             205 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656749
VERSION     WP_457656749.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..205
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21746
     Region          11..194
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          113..198
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtcmsisntp raatlddaaa isgtlarafq ddpmmewffp ggasrepdlv ryfttiftrq
       61 ygrhgvcert asaaafwvap egqektvpda etvaeleeil gdraplfrda vaaaaeqgpk
      121 ephwylavvg adpaargqgh gaallrsgla kadaaglpvh lesskpdnlp fyehfgftvl
      181 geaalpgggp alwvmrrepr pvdaa
//
LOCUS       WP_457656750             134 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457656750
VERSION     WP_457656750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..134
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14837
     Region          8..132
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mpadatahvr iarpsrdlaa aehfwvaglg ldvryrhead gtpgrhsllm vgwpgaawhl
       61 elvhdpadpv eprptpedll vvylgeevpd tlverleqhg gtrvpahnpy wdtwgvtlrd
      121 pdgyllvlst rtws
//
LOCUS       WP_457656753             527 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces griseus].
ACCESSION   WP_457656753
VERSION     WP_457656753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..527
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57083
     Region          15..524
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvvdetqge ptdargrvae llalreqarr gpserateaq hakgkltare riellldags
       61 freveqlrrh ratgfgleak kpytdgvitg wgtvegrtvf vyahdfrifg galgeahatk
      121 ihkimdmais agaplvslnd gagariqegv salagyggif qrntrasgvi pqisvmlgpc
      181 aggaayspal tdfvfmvret sqmfitgpdv vkavtgeeit qnglggadvh aetsgvahfa
      241 yddeetciae vryligmlps nnrenpptar sddpadrrsd vlldlvpadg nrpydmhqvi
      301 eelvddgdyl eiherwarni icamarldgq vvgivanqpq alagvldiea sekaarfvqm
      361 cdafnipiit lldvpgflpg vdqehggiir hgakllyayc natvprisli lrkayggayi
      421 vmdsqsigad ltyawptnei avmgaegaan vifrrqiada edpeamrtrm vkeykaelmh
      481 pyyaaerglv ddvidpaetr evliaslaml rtkhadlpsr khgnppq
//
LOCUS       WP_457656761             450 aa            linear   BCT 27-JAN-2026
DEFINITION  ammonium transporter [Streptomyces griseus].
ACCESSION   WP_457656761
VERSION     WP_457656761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, 57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..450
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46345
     Region          10..420
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mppgittlaa dapelsaant gfmlicsalv mlmtpglaff yggmvrvkst lnmlmmsfis
       61 lgivtilwvl ygfslafgsd vgsvigwssd yvglsnigvt elwdgytipv yvfavfqlmf
      121 avltpalisg aladrvkfta wavfivlwgs vvyfpvahwv wgtggwlfem gvidfaggta
      181 vhinagaaal gvilvigkrv gfkkdpmrph slplvmlgaa llwfgwfgfn agswlgnddg
      241 vgavmflntq vataaavlgw lvyeklrhgs fttlgaasga vaglvaitpa ggsvsplgai
      301 avgaiagvlc amavglkykf gyddsldvvg vhlvggiigs ilvgffatgg vqsdakglfy
      361 gggleqlgkq avgvvavlay slvvsalial lldktigmrv seddeisgid qvehaetayd
      421 fsgtgggsvs rttapapdtt aapkakkvda
//
LOCUS       WP_457656760             318 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656760
VERSION     WP_457656760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..318
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34956
     Region          34..317
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 maftvvrfnl vdpsaepval saryraalem avyadehgvd tvqteehhgv answlpspft
       61 fagavfgatr riavtvsaii gplhdplrla ediavldlls agrlvtvagi gyrpeeyera
      121 gvewgrrgrl qdelletlla awtgepfpyr grtvrvtprp ytrphplllv ggssraaarr
      181 aarlglplfp sahlpeleay yheqravhgt egfcmmpaae tpllhvsedp drtwaeygeh
      241 flheartyas wqskdirsav rsaattvael reegvyrivt pdgladleae slvlhplcgg
      301 mpveegwrsl rlfceavt
//
LOCUS       WP_457656763             265 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Streptomyces
            griseus].
ACCESSION   WP_457656763
VERSION     WP_457656763.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 265)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..265
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27081
     Region          <93..213
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrhqpaphrs pthrtllpla lltlplsllv lcgllpagpp apgpavapag avaalpgada
       61 dvdedadada dadadaepdt apdadadasa ddggrswpla grpavlrgwe ppagpygpgh
      121 rgvdlgarpg arvlaaaggr vsfagrvagr gvlavevags gspplrttye pvralveega
      181 rvragqpvgv leegpfhcae gclhwglrrg dayldplsll ppallrtgps rllpvfgvpe
      241 peavrvsrsg rrlhragpsr rrcpr
//
LOCUS       WP_457656764             343 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656764
VERSION     WP_457656764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36243
     Region          1..339
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlslqaatvr fgkraaldav dlevadhriv cvlgpsgsgk stllravagl qpmdggrvll
       61 agrdqagvpv hrrglglmfq dhqlfphrdv ganvafglrm hgvgraetda rvrellelvg
      121 lpgaerrava alsggeqqrv alaralaprp kllmldeplg qldrslrerl vvelrtlfqe
      181 lgttvlavth dqgeafalad rvvvmrdgri aqegspldvw qrpasafvar flgfdnvtaa
      241 tvtgqaaata wgkvpvpegs pqgevdllvr pagvrigape dglrcavgvr tfrgnhvtvr
      301 llpenapvle aecalrdtpd egavvgvrfd aaetvvladp gps
//
LOCUS       WP_457656767             651 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457656767
VERSION     WP_457656767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..651
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=71075
     Region          67..447
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaphntpqv prapkvtere arrvaeaare qdwrkpsfak elflgrfrld lihphplppp
       61 ddirrgeefl arlrafcear idsariecea ripdevisgl kelgalgmki etrygglglt
      121 qvyynkalal vgsaspaiga llsahqsigv pqplkifgtq eqkdvylprl attdisafll
      181 tepdvgsdpa rlatsavpdg pdyvldgvkl wttngvvadl lvvmarvpas eghpggitaf
      241 vveadapgvt vehrnafmgl rgiengvtrf hrvrvpgacr igpegaglki alttlntgrl
      301 slpamcvgvg kwslkiarew savreqwgrp varheavatk lsfiaattfa leavvdlssq
      361 madedrndir ieaalaklyg semgwliade lvqirggrgf etaaslaarg eravpaeqml
      421 rdmrinrife gsteimhlli areavdahlk vagdiidpdk plsakakaga naagfyarwl
      481 pqlvtgagql prtygefhpa ghrdlsghlr yvercsrkla rstfyamsrw qgrmetkqgf
      541 lgrivdigae lfamsaacvr aehlrgtgeh greayqlada fcrqsrlrve elfarlwsnt
      601 ddldrrvvdg vlsgtytwle egvvdpsgeg pwiadatpgp svqenqhrpv r
//
LOCUS       WP_457656770             176 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656770
VERSION     WP_457656770.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  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 176)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..176
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17897
     Region          24..154
                     /region_name="DUF4439"
                     /note="Domain of unknown function (DUF4439); pfam14530"
                     /db_xref="CDD:434020"
     Site            order(32,61,64,106,135,138)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 msirserrsd dadesdadsp eltavqgala aehaavygyg alggrldgkr gaearaaydg
       61 hrarrdalar tardlggrpv asdaayalpf avadapsaer laavledria gayadlvrat
      121 egdrrkdaag alreaavrsa rwrggnvafp glaeraagad paatgpveaa gadgtr
//
LOCUS       WP_457656771              92 aa            linear   BCT 27-JAN-2026
DEFINITION  YlxR family protein [Streptomyces griseus].
ACCESSION   WP_457656771
VERSION     WP_457656771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Osipiuk,J., Gornicki,P., Maj,L., Dementieva,I., Laskowski,R. and
            Joachimiak,A.
  TITLE     Streptococcus pneumonia YlxR at 1.35 A shows a putative new fold
  JOURNAL   Acta Crystallogr D Biol Crystallogr 57 (Pt 11), 1747-1751 (2001)
   PUBMED   11679764
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..92
                     /product="YlxR family protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=9882
     Region          7..91
                     /region_name="YlxR"
                     /note="Nucleoid-associated protein YlxR, Predicted
                     RNA-binding, DUF448 family [General function prediction
                     only]; COG2740"
                     /db_xref="CDD:442042"
     Site            order(13,29,51)
                     /site_type="other"
                     /note="putative RNA binding cleft [nucleotide binding]"
                     /db_xref="CDD:238173"
ORIGIN      
        1 msgrtqarac pertcvgcre ratksellri vvdegacapd prgtlpgrga yvhpvsvcld
       61 lavrrrafpr afkakgpfdt aaltrfvera tp
//
LOCUS       WP_457656774             370 aa            linear   BCT 27-JAN-2026
DEFINITION  XdhC family protein [Streptomyces griseus].
ACCESSION   WP_457656774
VERSION     WP_457656774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..370
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38604
     Region          2..359
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mrdilpdlra rcadgvpfal atvvavhgsa prdpgavmav daagtvlgsv sggcvegdly
       61 evarevlags gprlvsygis ddeafgvglt cggtievlvr ayasegerte laalldliaa
      121 drpvaettvl sgaaetgarl vvrpadagpt tgtlgnegld aavtddargl laqgltgiqr
      181 ygahgqrrmq evavfvrtya ppprmlvfga idhaaatari gsflgyrvtv cdarpafatr
      241 erfptadevv rawphtylks tevdartvic vlthdpkfdv pllvaalstp aayigvmgsr
      301 rthhdrlarl raagvdeahl erlaspvgld lgartpeeta vsiaaeiiqh rwggtgrplg
      361 altgaihrdr
//
LOCUS       WP_457656776             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656776
VERSION     WP_457656776.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37561
     Region          29..348
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtaatttttp npdpsgppgt tkptgdppll evrnltvtyg sgadavpavr gvdlrveagq
       61 klgiagesgc gkstlalall rllpttatls geilldgedv ltmkwgrlra vrwagasivf
      121 qgamhslnav hrvgdqiaep illhsgatpa aarkragell eqvglpaara qayphelsgg
      181 qrqrvmiama lacdprliva depttaldvm iqaqilrlie qlvadqdvgl imishdlavl
      241 adtcdrlsvm yagrvveegp arqvyadarh pygralsaaf prigdlssrh aprglpgdpp
      301 dpaalpggct fhprcpvald pcatedqvlr aaggerraac vlvdadraqh gdedarstr
//
LOCUS       WP_457656784             568 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding SpoIIE family protein phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457656784
VERSION     WP_457656784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  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 568)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18599219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..568
                     /product="ATP-binding SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=60127
     Region          21..425
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          437..549
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 msgtrrlewl naagdhigtt ldldrtaqel adyavpklad aaavdllesi lrggegersg
       61 saeapltram avahidelgn lepdpvgelt tshpskvahq clitrrpalv rriaphqyey
      121 iaptshaalv lrragvhsyl alplvsrgvl lglvdflrsg drppfshadv alacelaaka
      181 avfvdnarly greraavvkl qrallpraap stpglqvvsg yrpavdpggv ggdwfdvval
      241 psgrsalvvg dvmghglaaa atmgrlrsva rtllgldisp ervlarldla ardleedqva
      301 tclcavydha ertyrlasag hpppltidaa graafldvpp gaplgagvip ydevtakvpe
      361 ggrivmytdg liknrhedvd vllerlraav dgppaalads ceaiwtgtds cgggrfddav
      421 vlmaeslsqp daevvvwslp sdgsaagvar rlvraqlerw sltelmdvte lvvselvgna
      481 lrygggpsgl rllrhdrlcv evsdigpdlp qiqhaplsae ggrglqlinm lcrrwgscrt
      541 pdgkvvwaeq dlpsttanph happqpgr
//
LOCUS       WP_457656788             189 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656788
VERSION     WP_457656788.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19993
     Region          2..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maehrtmqrg alldaarsll seggtealtf palaertgla rssvyeyfrs raavveelca
       61 vdfpvwaaev enamdradtp eakieayvrr qldlvgdrrh ravvaisase ldagarekir
      121 aahggliami vealgdlgne qprlsamllq gsvdaavrri elgvaeepgv iadtvvamvl
      181 rgvtgglsg
//
LOCUS       WP_457656794             596 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c biogenesis protein ResB [Streptomyces griseus].
ACCESSION   WP_457656794
VERSION     WP_457656794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Dreyfuss,B.W., Hamel,P.P., Nakamoto,S.S. and Merchant,S.
  TITLE     Functional analysis of a divergent system II protein, Ccs1,
            involved in c-type cytochrome biogenesis
  JOURNAL   J Biol Chem 278 (4), 2604-2613 (2003)
   PUBMED   12427747
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Le Brun,N.E., Bengtsson,J. and Hederstedt,L.
  TITLE     Genes required for cytochrome c synthesis in Bacillus subtilis
  JOURNAL   Mol Microbiol 36 (3), 638-650 (2000)
   PUBMED   10844653
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Inoue,K., Dreyfuss,B.W., Kindle,K.L., Stern,D.B., Merchant,S. and
            Sodeinde,O.A.
  TITLE     Ccs1, a nuclear gene required for the post-translational assembly
            of chloroplast c-type cytochromes
  JOURNAL   J Biol Chem 272 (50), 31747-31754 (1997)
   PUBMED   9395519
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     gene            1..596
                     /gene="resB"
     Protein         1..596
                     /product="cytochrome c biogenesis protein ResB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=63711
     Region          45..557
                     /region_name="ResB"
                     /note="Cytochrome c biogenesis protein ResB [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG1333"
                     /db_xref="CDD:440944"
ORIGIN      
        1 mskanstgtr qradeqaqgs ahgaagdrls tapreerpdt gaavpamgvi gwvrwfwrql
       61 tsmrvalill fllslgaipg slipqtsvdd mkvqafkdqh ttltpiyekl qlfdvyssvw
      121 fsaiyillfv sligcivprt gqfvgqlrsr ppgapkrltr lpayttwrte aepdavreaa
      181 lavlrkrrfr thgvgdavaa ekgylreagn lvfhialivm llafasgqlf kseggklvve
      241 gdgfsntltq yddfksgsly dsdslapfsf vlddfagtye ksgpqrgtpr tfearvtyte
      301 gadgaerkgv ikvneplvvd gtkvyliahg yapvvtvrdg sgkvvsktav pllpiddnit
      361 ssgaikvmdg ykdkkgvktq lgfkaffvpt faghgkgqmf sqfpglefpv lalsayqgsl
      421 gvdsglaqnv yqldtskmke fkdkdgellk kmlmpgekld lpdgagsitf dgveewasfq
      481 vsqqpgtgwa ligavaaiag lagslfiqrr rvwvravrga dgvtvvemag lgrsesaklp
      541 eelgdlaaal vttapvepek paasstsmda dgpdatneag srpvhpaeap aegaek
//
LOCUS       WP_457656798             525 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457656798
VERSION     WP_457656798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..525
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54889
     Region          33..525
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mttasrpags ssrppagrpa sraaataaap rslpallghr aaadpgrtal icgprtltfg
       61 twheraeala aglrsrglgp garvvlrygg gdwiayavay cgvlragcva vplsdrqapa
      121 taahvladsg atavlhpaga dlpsgllppg vwsatteeie aaeaappgpd pladpdpaal
      181 aqilytsgtt grpkgvtath gnlaygctld errrplrhsr hflhafpvgt nagqtmlvna
      241 ldsaatavaa pqftpgrfar lieeygvgsv flvpamaiel lgseaarrya tdsvrlvgst
      301 aaalpgpval glarafpraq vvnyytstea apaqitllfd pdrpdspgrp aslrdlrita
      361 pdgtplppge pgevrlrtpa apraylgeda arsevfqghw vrmgdlgrld edgylhlldr
      421 erdviksgay kvstlqveea lhahpavada aafgvphpvl gsvvaavvvp rgeltvpqlr
      481 tflldrlaah elparllfrp flprneggki lkrelrllld dealr
//
LOCUS       WP_457656799            1056 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces griseus].
ACCESSION   WP_457656799
VERSION     WP_457656799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1056)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1056
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=110441
     Region          4..1056
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mtntttspsp svsvasspel algpaqhgmw vteqvlrpgs ahhlavtarf avppdpaald
       61 agcarllarh pvlasrldpe gpalapatgh apelrrlmca adelgallae esarpfdlaa
      121 gplvrfalvt agdagpvlha vahhlvfdgm skdvllaeil gaettaglpp depaeptaee
      181 asaagefwtg rwsdpaapvl pglpssvrdt tapapgsavp ftldgplhar itdtarslgv
      241 trfelllalw htllfrygdr apvtalelst rrpgspdhig lyvnelplfs rpapdrqfad
      301 fardvraelr alyahrtvpl gravrggltp rtaltplsvs yrrrtgwear eapdvavdwt
      361 gfthavrnla hlqlvdgpdg vdgslqyrtd afapgapari vghfrtllda vltapdtcla
      421 dlpllagdel dralyagngt paarpadatv wamfaeraaa dpsavavvap dgaelsygel
      481 hvaaeafadr laaagigpgd lvgvqvarsa geltavlgtl aagaayvpld pgypadrlaf
      541 vradarlaal vvegpvpdgl pdglpvlspe reasrerrgd sapprgrsaa paaedpayvl
      601 ytsgstgrpk gvevphdala nligaladrl aagprdrwlg ltslsfdist velllplttg
      661 arvvlvpeer qrdgaallkl ieahdvthvq atpsswrlml aaglhrpglv glaggealpe
      721 plaaelarsv grlinvygpt ettvwstlae ltpgdpvtig rplaatrayv ldahgrpvpd
      781 gvpgelhlgg tglahgyrgr pgltaqrfvp dpwgppgsrm yrtgdlvrrl ldgrlefagr
      841 vdtqiklrgh rielgeiear lvdhpavsqa vvvldradda getgeagete gtgqdrlvay
      901 vvgagqqapa addlrahlar tlpaamipat wvplpalplt pngkvdrarl pqaprtrpea
      961 aatagtgava aggetagtaa vvrdiwqevl rlddigpded lfdlgghslt itaiaarirk
     1021 rlgvevpldv ffdtptlaev savvselqqq eessde
//
LOCUS       WP_457656806             278 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457656806
VERSION     WP_457656806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..278
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29041
     Region          <63..149
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrrsprtcll allaliggll tvtataspaa aapnfkapya cgqqwtyshh saevrqaldf
       61 vrtdgggtag apvlasaagt ayrysqpsga gnyiavehgg gwktyyfhla afsvangaqv
      121 aqgqqigttg stgnssgahi hyeqlyngvg qtivingqsl apypgsyysk yltgdngcgg
      181 ggggkywvdt fanatgyaaa ntadaqgvln agtnyvyckv wgarvgtasq fnhwwlrtdl
      241 dvvyagkngr nayvsayyls rwgndeardn ngtvipdc
//
LOCUS       WP_457656811             140 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656811
VERSION     WP_457656811.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..140
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15327
     Region          17..132
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 maltlpaeld ppdyrqelva rpetlaimrr ivsahldlwd lrelsdaatl cahelltnvm
       61 rhtgsplcti tlrrrpdgvr vtvsdsdtap perrepdwse esgrgvllia alaaqcgtvm
      121 rqdgkdvwad iraatpayat
//
LOCUS       WP_457656807             295 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656807
VERSION     WP_457656807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..295
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31327
     Region          1..289
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 matvvdlity pvkgcagtsv dsthltpagl ghdrsfmvvs vdgvyrtqrr dprlalvrpt
       61 asadgsrltl asvepdnghg vlhldvttsa prrevdlfga tyqgidqged aaawlteflg
      121 tpsrlvrvpp eherktdglt pgtsgyadss avhllsrssl allntrmaer dapplavdrf
      181 rpnlvvdshp egahgedgeq gedwaaepha edrirrmtig aaelgytkla vrcavtlvdq
      241 eagarggpep lrtlagyrrf saggvvfgak favvrpgkls vgdevaveew geaes
//
LOCUS       WP_457656812             284 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656812
VERSION     WP_457656812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31634
     Region          13..74
                     /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          100..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maqsdmptmr srrlggelrq lrlnaglkvq daaealecgq pkisqiengk rgirpldltt
       61 llnlygvede rqraslkrla keihkvdwws gqgpflhdvl kdylmleads qairtfepmv
      121 ipgllqteay mrhlyevasp adqveslvet rmkrkelldd rlgfrlravi dapalhrigg
      181 gpdlvagqlv hlleagsssn vsiqvlplds alpmeqyapf tvfglqadpp vevvwlehit
      241 ggtlleqrpd vqayikawde ltaaalspta srqyirdlie etrp
//
LOCUS       WP_457656815             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656815
VERSION     WP_457656815.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30982
     Region          11..>68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          108..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mplsphsnaq qarqalanrl aelrreaglt grelarlcgw hpskssrien artaptaddi
       61 sawcgacgar drtgdliasl raaegmwiew rrmersglrq aqanrlplye rtqrfhayss
      121 wlvpgllqtr sytmavlrav qrrrglvddv aeavnarmdr qrvlhegdrr faflveesvl
      181 wagvggaqvm teqlatliam gslpnvsvgi vpaapdrerw pvegfwiyda aqvnvelvsg
      241 yltvtapsev asyaatfsel tecavygtaa rrlittamda lg
//
LOCUS       WP_457656816             279 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457656816
VERSION     WP_457656816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  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 279)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..279
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30098
     Region          14..265
                     /region_name="AKR_AKR13B1"
                     /note="AKR13B family of aldo-keto reductase (AKR);
                     cd19088"
                     /db_xref="CDD:381314"
     Site            order(20..22,51,56,81,124..125,154..155,174,201..207,227,
                     244..249,252,255..256)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381314"
     Site            order(51,56,81,124)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381314"
ORIGIN      
        1 mpsttfrigg dltvgrlgfg amhlpterpe drpsavavar ravelgitli dtahmygnga
       61 neevlaealh pypkdllitt kvgvlrspet gewalngrpe slrtevdhal rrlrvdrlel
      121 lqlhridpet pladqlgalr dlrdegkvar iglsevtape laaareivdi asvqnrynlt
      181 drehepvlea ceaagvaflp wrtvawgkag draevaaiaa eldatptqvc lawlldhspv
      241 mlpipgtssi ahleenvaaa dlvltpelra rldgiagde
//
LOCUS       WP_457656814             248 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces griseus].
ACCESSION   WP_457656814
VERSION     WP_457656814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..248
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=26397
     Region          2..226
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mdevevvvah seratlrvgd vflkvdadqa ridveveams lapvptpevl wrrppvlaia
       61 avpgttlgrl ggpatgspaa waaagaairk lhdaplpplp gragrsigel aaeldaecal
      121 lvangllpae lvtrnrevae aalrpwtpaf thgdlqiahv flegdqvtgi idwseagrgd
      181 alydlatftl gheehlddvl ggygddvdlq virawwavrs llavrwlteh gfdpflpgce
      241 vevlrslv
//
LOCUS       WP_457656817             129 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457656817
VERSION     WP_457656817.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..129
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13753
     Region          17..128
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mntsttenad nitglgvilg stdsdaliaw yraaleplga rwaehllivg pgaiigfder
       61 ddvadkaaep grqminitvr dvraaekhln slgvtwvrpv eevgggwyfs tivdpvgnyl
      121 qilqgpeap
//
LOCUS       WP_457656818             269 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656818
VERSION     WP_457656818.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..269
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29058
     Region          6..229
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mpaprtvllt gaagglgtlm rgllpaygyd lrlfdlvpve nepqaitadl ndrkalreav
       61 rgvdaiihla gislestfdk ilnaniegty hlyeaareeg vrrivaassn havghtprpl
      121 agdrlipsda phrpdtfygl skcfgedlaq lywdkhgvet vsvrigscfp eptsvrmlsl
      181 wmspadgarl fhaaltaedv ghtvvhgssa ntrlwwdlts aralgytpqd dsepyaakli
      241 aeqgepdpad paqtrlgghf vtdppiwph
//
LOCUS       WP_457656822             579 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656822
VERSION     WP_457656822.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..579
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=62355
     Region          1..573
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mldhlirrat vvdgtggpar iadvgirdgr iavvaepgtv teeavtheda dglvlapgfv
       61 dphthydaql fwdpyatpsm nhgvttvagg ncgftlaplh pdrpedadyt rrmmsrvegm
      121 alkaleegvd wtwstfreyl daldgriavn agfmvghcal rrhvmgpdav ggqptpaqmd
      181 amlalfhdam dagawglstt qsgthsdgdg epvasrhalp dellalsrav gehegtqlea
      241 ivagcldqfs deeidlfvdm taaagrplnw nvltidaavp ervprqlips eraraaggri
      301 valtmpiltp mnmslgtfca lnlipgwgei lalpvperie rlrdpatrae mlcradskea
      361 gvfrrlanfg ryvigdtysa aneglsgrvv ddiaaergqd afdclveica adglrtvlwp
      421 mptdndpdsw alrqrtwehe dvmlggsdag ahldrmcgap yttrflgdcl rgrklvpltt
      481 avrmltddpa rlfglrergr ieegfhadlv lfdperidag patlvhdlpg dsprldskai
      541 givsvrvngv etlrddkvtg avpgtvlrsg rdtrtvsta
//
LOCUS       WP_457656821             446 aa            linear   BCT 27-JAN-2026
DEFINITION  pectate lyase family protein [Streptomyces griseus].
ACCESSION   WP_457656821
VERSION     WP_457656821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Wu,P., Yang,S., Zhan,Z. and Zhang,G.
  TITLE     Origins and features of pectate lyases and their applications in
            industry
  JOURNAL   Appl Microbiol Biotechnol 104 (17), 7247-7260 (2020)
   PUBMED   32666183
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Hugouvieux-Cotte-Pattat,N., Condemine,G. and Shevchik,V.E.
  TITLE     Bacterial pectate lyases, structural and functional diversity
  JOURNAL   Environ Microbiol Rep 6 (5), 427-440 (2014)
   PUBMED   25646533
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Marin-Rodriguez,M.C., Orchard,J. and Seymour,G.B.
  TITLE     Pectate lyases, cell wall degradation and fruit softening
  JOURNAL   J Exp Bot 53 (377), 2115-2119 (2002)
   PUBMED   12324535
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Yoder,M.D., Keen,N.T. and Jurnak,F.
  TITLE     New domain motif: the structure of pectate lyase C, a secreted
            plant virulence factor
  JOURNAL   Science 260 (5113), 1503-1507 (1993)
   PUBMED   8502994
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Linhardt,R.J., Galliher,P.M. and Cooney,C.L.
  TITLE     Polysaccharide lyases
  JOURNAL   Appl Biochem Biotechnol 12 (2), 135-176 (1986)
   PUBMED   3521491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..446
                     /product="pectate lyase family protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0016837 - carbon-oxygen lyase activity,
                     acting on polysaccharides [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47814
     Region          18..442
                     /region_name="PelB"
                     /note="Pectate lyase [Carbohydrate transport and
                     metabolism]; COG3866"
                     /db_xref="CDD:443075"
ORIGIN      
        1 mparmrhtra vavtlgcasl alalsvpaqa aprpgphgtg ieravlpagd gwaaaegstt
       61 ggadaapehv ytvtdraelv aafeeagdap kivrvagtih gnsdadgtpi gcdqyetdgy
      121 tlekylaayd peawgrdrvp egpledarva saklqqaavn irvpsnttli gvganpeiig
      181 aslqvrdvsn vivrnisfed tydcfpqwdp tdgsegawns eydnlvvygs rnvwvdhntf
      241 sdgdrpdseq pryfgqlyqq hdglfdivrg adlvtvswnv lkdhdktmli gnsdgagatd
      301 rgklrvtlhh nlfkdvkera prvrfgqvds ynnhfvatrg saygysygig aesrlvaehn
      361 aftlagdvdr atvlkkwsea pltaennyvn grrtdliavh nagvpgeqlt egagwtpelr
      421 ttvhhpwavp vlvglkagag rvsglr
//
LOCUS       WP_457656824             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656824
VERSION     WP_457656824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20689
     Region          6..196
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 maaplpdrrd liadtaiatv aaaglrglth ravdtaaglp agstsyyfrt rsalisacyl
       61 rlatltvtdv drweerhgip dpdsaaeala allhhwlteg rnrqlarfel sleatrrpel
      121 ragletagra araraaalla slgapdpeqa adllvawtdg llydriagap aasrpapdaa
      181 eltlvvrrml tallap
//
LOCUS       WP_457656827             221 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457656827
VERSION     WP_457656827.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  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 221)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..221
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22974
     Region          7..195
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          55..143
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 meaphldair qsydavaady arsvkdpael dplsravlaa faelvasagl gptadvgcgp
       61 gkvtayltrl gvdafgvdls pgmvglaraa hpelrfdvgs msaleaddge lggvlafyst
      121 hhlppealpg tfaefhrtla pgghlllvtr vgdtghqrrt ygygggeaap fdsyrlpadr
      181 iaelleragf vvtgrtlqep eaganrpvag flarrpesgq a
//
LOCUS       WP_457656828             280 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656828
VERSION     WP_457656828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30786
     Region          5..100
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(6..8,22,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(52,55,59..60,70,83,87,93,97,100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrdlysisev aeafgltvat lrfyeerglv rhserrgrvr yyrradlarl ayaqlwhedg
       61 lltlaetsai vdsdrlgdrl aliagqrdal rerigrlera vgvlthmldc rtdralecpm
      121 tgayirgrvd aaldgtpept gfwpegfaga agdrapapap arpahparpa rsvgdeqlls
      181 ltrglvsdaa kvrertceti sdrvrsfdrr evrtlaslla saavleqdad cleselnalg
      241 elavtglfea ediaalrrlp rasvrpadae hldyltaeyf
//
LOCUS       WP_457656836             284 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656836
VERSION     WP_457656836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..284
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=30125
     Region          23..254
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(28,31..33,36,44,46,76,95..98,189,191,193..194,196,
                     206..207,210,225..226,229)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(28,32,36,44,46,76,95..98,189,193..194,196,206..207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(31..33,189,191,194,207,210,225..226,229)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 miiepslvrg liaaqfpqwa dlpveaveas gtanaiyrlg adksvrlprt egsaadvate
       61 hrwlprlapr lpcpvplpla qgvpceafpr pwsvhtwleg tnpgpgdass ssellaadla
      121 efvlalrria ptdappayra eplasrdrat realaaldgv vdrenttaaw tdslaappft
      181 arpvwahgdl qpgnvlvadg rltavidfgc tgladpavdl iaawylltag areafrtava
      241 addatwtrgr gwalsialme lahyresnpv mariaahvie eavs
//
LOCUS       WP_457656843             491 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656843
VERSION     WP_457656843.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 10612637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..491
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=54099
     Region          32..163
                     /region_name="HATPase_c_3"
                     /note="Histidine kinase-, DNA gyrase B-, and HSP90-like
                     ATPase; pfam13589"
                     /db_xref="CDD:433332"
     Site            order(35,39,42,63,65,67,69,98..101,114,116)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340391"
     Site            order(76,101)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340391"
ORIGIN      
        1 mkagvlaqer ldpyaedlve slrafgydlp taladlvdns iaaeaknvrv aycsdpgeaw
       61 vaivddgrgm seselhaamr farnpnhhra kgdlgrfglg lktaslsqar tltvlsrdav
      121 gqlatrtwdi dhiarqrewl vltepddetl riadqvgftg rgtaiiwrnt dklgdgrals
      181 rrisesgrel sllfhrflak grlnlsigrq aidpmdpylr rhpatqdrgv eeleyeghwi
      241 rvnpvvlphp srltrqeaas asgpggmlar qgfyvyrger lvvagswlgl ggmhnsaptr
      301 larisleipp gadlawavdv rksslrppac leqrlvelae dararsekvf thrgtpsrnr
      361 gklaqvepvw qqvrrlgqse ycinrghplv adalagangn alegvlrlve atlpreliaq
      421 eltshpeear lqpdptdtee vlamlralls giprdptqrt ilaealvkae pfcrhpglvr
      481 eiiesdspke t
//
LOCUS       WP_457656845             329 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457656845
VERSION     WP_457656845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 329)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35839
     Region          251..314
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrihftpad ltrvrlatrp dplwetvfsl hrlqtsqgrw ayadwyratq dtlastplgk
       61 avrrllvpvv praayfpdfl tpyeaaegld eglaavldtp ssrvaaevrr lqettggppw
      121 agslvesrar eelgkalray hdaviapfqd dvftriaaer aacarvtvdt gvdgllrgla
      181 pgirwrppvl eidyvvdrdl hldgrglrli psyfcwrkpv vladstlrav lvyplcdtwa
      241 paperpsevs lgallgktra aalrtlahga tttelaqrlg vspatathht tvlrnaglit
      301 trrsrntvlh tltpvgaall rtgtsrsaa
//
LOCUS       WP_457656848             582 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457656848
VERSION     WP_457656848.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..582
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=61482
     Region          64..577
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mphtvpspdp gaddaaelar raarieaalt apgapfavvi gergtpeyad gprtlrefve
       61 ttwaygdapf liagertysy geffaaasal avrlrerygl rpgdraviam rnhpewqiaf
      121 waaqlaglva vplnawwtee efgralddce pgvllvdger lgrvagwarr tgayvvlfhg
      181 agrtaeglrl dryeefpapd plaappdvep rpeddatily tsgttgrpkg avatqlaqag
      241 aalnpryhaa asalargvip gqgpapvslm tfpffhvaaf tgfyaamaag galvlmhkwd
      301 adealrlirt hrvthfsgvp atglqlleaa eragdgdalg glglfstgga apppalvarl
      361 tarygtrvep rngygltets ggvlahfgde yraepggagr ptpvtetria gpsgdelpdg
      421 eagelwlrgq alfrgywrdp aateeafadg gwfrtgdlav rsegrisvvd rikdvvirgg
      481 envscveveg vlhdhpdvad aavlgiphpv lgeevaavvr pragavvtae dlrehvggrl
      541 aafkvparvl lteeplprna tgkllkhrlr alleaaapvt ga
//
LOCUS       WP_457656850             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656850
VERSION     WP_457656850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23578
     Region          19..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mktventapa aqcrtvrpra dalrnreriv aaarelfvef gpdvalddva rragvgnatl
       61 yrnfpdraal thevvlavts rttrkaeeav aaesdpfaal srfvhaaade rigalcpmls
      121 gvfdkdhpel laerrrleea veglvarams agrlrtdiav gdvlvalsql trplpgiacq
      181 gidrfthrhl qlfldglesp arselpgsaa tledlrrp
//
LOCUS       WP_457656852             341 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656852
VERSION     WP_457656852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..341
                     /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=36957
     Region          16..328
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msdtparllk llsllqtpre wpggelaerl dvsprtirrd vdrlrdlgyp veasrgsvgg
       61 yrlvagaamp plllddeeav aiavglraga ghaiegvdea svralakleq vlpsrlrhrv
      121 salqnatvpl trgdgstidp rtlttlasaa tgrerlrfay rsgdgtrtkr qvepyrlvst
      181 gqrwylvayd ldredwrtfr vdrvgepyat garfaprplp vegagsdags gdaarflars
      241 mrrmkpelcl dvwfggpaef vaarlpahlg apepdgeggc rlrtsctdsl ewvalrlalv
      301 dcefsvtepp elvayleglg arltraarpg drrnpsgpeq g
//
LOCUS       WP_457656853             516 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656853
VERSION     WP_457656853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..516
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53899
     Region          51..504
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(58..59,62..63,66,98,148..149,151..153,156,176,
                     179..180,183,314,317..318,321..323,326,354,358,414..415,
                     419,423,439,442..443,446..447,450)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpssappppt ashlapptes appvppvpvk tpvapgsapa drrrwfalai vmtaafmdlv
       61 dvtivniaip siqretgasv saiqwitagy alafaaglit ggrlgdiygr krlfligigg
      121 ftlasalcgf agspeilvaa rilqgataal mvpqvlsivh atfpahergk vfglfgaivg
      181 lgavsgpllg alltewdlfg lgwrpiflin lpvgiaglll gakfiteska pkavrldllg
      241 valitlamlm liypltrghe lgwpvwghls mvgslfvfga lalnqrqktl angspliems
      301 lfrvksfaag iavqltfgvg lgifflvwtm ymqmglgwsv lragttgipf svavsvaagi
      361 svqklvprfg rkvlqagall miaglliylw esehygmgit swqmavplvv mgtgmgliva
      421 pltdavlsev pkehagsasg lintvqqmgt alglglvsvv ffgaigdrla peavgpafvd
      481 afqqslwwva gvlsviflvm falparprvh vegdpn
//
LOCUS       WP_457656854             360 aa            linear   BCT 27-JAN-2026
DEFINITION  P1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457656854
VERSION     WP_457656854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Bompard-Gilles,C., Villeret,V., Davies,G.J., Fanuel,L., Joris,B.,
            Frere,J.M. and Van Beeumen,J.
  TITLE     A new variant of the Ntn hydrolase fold revealed by the crystal
            structure of L-aminopeptidase D-ala-esterase/amidase from
            Ochrobactrum anthropi
  JOURNAL   Structure 8 (2), 153-162 (2000)
   PUBMED   10673442
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..360
                     /product="P1 family peptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35457
     Region          14..350
                     /region_name="DmpA"
                     /note="L-aminopeptidase/D-esterase [Amino acid transport
                     and metabolism]; COG3191"
                     /db_xref="CDD:442424"
ORIGIN      
        1 mtredrtpah pplldaltdv agirvghaev agagalsgtt vvlapeggav aavdvrgggp
       61 gtretdaldp rnlvqrvdav vltggsaygl daasgvmawl eeqgrgvrvg agptqvvpvv
      121 paaalfdlgr ggdwrarpda stgraaveaa aatgsgepva eggvgagtga vtgqlkggig
      181 tastrlasgv tvaalvavna agsvvdprtg vlfgeygage pparppaevh aaaerrlare
      241 rlaaeeaggv vppfnttiav vatdadltra qaqklagtah dglaravrpv hlltdgdtvf
      301 tlatgrvpva pgdpvavnei laagadvlar avvkavraar stegpggrll sytelyggra
//
LOCUS       WP_457656855             267 aa            linear   BCT 27-JAN-2026
DEFINITION  QcrA and Rieske domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656855
VERSION     WP_457656855.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Veit,S., Takeda,K., Tsunoyama,Y., Baymann,F., Nevo,R., Reich,Z.,
            Rogner,M., Miki,K. and Rexroth,S.
  TITLE     Structural and functional characterisation of the cyanobacterial
            PetC3 Rieske protein family
  JOURNAL   Biochim Biophys Acta 1857 (12), 1879-1891 (2016)
   PUBMED   27663073
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Levin,E.J., Elsen,N.L., Seder,K.D., McCoy,J.G., Fox,B.G. and
            Phillips,G.N. Jr.
  TITLE     X-ray structure of a soluble Rieske-type ferredoxin from Mus
            musculus
  JOURNAL   Acta Crystallogr D Biol Crystallogr 64 (Pt 9), 933-940 (2008)
   PUBMED   18703841
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Cosper,N.J., Eby,D.M., Kounosu,A., Kurosawa,N., Neidle,E.L.,
            Kurtz,D.M. Jr., Iwasaki,T. and Scott,R.A.
  TITLE     Redox-dependent structural changes in archaeal and bacterial
            Rieske-type [2Fe-2S] clusters
  JOURNAL   Protein Sci 11 (12), 2969-2973 (2002)
   PUBMED   12441394
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..267
                     /product="QcrA and Rieske domain-containing protein"
                     /EC_number="7.1.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=27194
     Region          64..174
                     /region_name="QcrA/PetC"
                     /note="Rieske Fe-S protein [Energy production and
                     conversion]; COG0723"
                     /db_xref="CDD:440487"
ORIGIN      
        1 msvtdqqpag ehpaggdpre alqdriaads lttrrdylri vttvsgglav ggigvaagil
       61 hrhgdgeegk apgpkriagg llpgesiafr ypgeedrava vrlddgtlvg ysavcthlac
      121 avlwrkdrgs egelycpche gvfdarsgev tagppprglp kvvvieqddg svwavgttrs
      181 gesveeglcr qlggerpdla trigcpdigg gaesppraag prarnrstde rpapraggag
      241 dagsrvsgpg rgaaatsata etpgrra
//
LOCUS       WP_457656856             121 aa            linear   BCT 27-JAN-2026
DEFINITION  FmdB family zinc ribbon protein [Streptomyces griseus].
ACCESSION   WP_457656856
VERSION     WP_457656856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..121
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11691
     Region          1..>59
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mptyqyqcte cgegleavqk ftddaltvcp scdgrlkkvf savgivfkgs gfyrndsrgs
       61 sssstpastt skssdsasss ssgsdtkasa sasssssgss ssgsssssas apasssgtsa
      121 a
//
LOCUS       WP_457656858             914 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces griseus].
ACCESSION   WP_457656858
VERSION     WP_457656858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 914)
  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 914)
  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 914)
  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..914
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..914
                     /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=100720
     Region          43..914
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mpanttassg psdakkpgrk kgrrarlivl vlvlalvagv gygaywsvst vrasypqttg
       61 smtldglsgd vevkrdsygi pqiyadsdad lfraqgfvqa qdrfwemdvr rhmtsgrlse
      121 mfgsgqvetd sflrtlgwrq vaqkeydevl destkknlqs yaegvnaylk gkegrdisve
      181 yaalgftndy kpgewtpvds vawlkamawd lrgnmqdeid rslltsrldk dqiedlypgy
      241 pykknrpive qgaispvtgk fdpeatpsdn vgsatpegat eglntqlsal sdtldeipal
      301 lgpngngigs nswvvdgkht tsgkalland phlapmlpsl wyqmglhcre lsktcqydta
      361 gytfsgmpgv iighnqdiaw gltnlgadvt dlflekvsgd gylydggtkp fktreetikv
      421 aggrdrtitv retnngplvs drskeldkvg qkapvsnaap dradgyaval kwtalepgks
      481 mdavfalnra kdfatfrkaa eyfevpsqnl iyadtegnig yqapgkipvr segydgtlpa
      541 pgwdpkyawk gyipfdelpy eynpdrgyiv tanqavidek kyphlltkdw gygarsqrin
      601 dllaqkikgg ekvstddmqk mqmdnfseia allvpelkki nisdpsvrea qkllegwdyt
      661 qepdsaaaay fngvwrnilk lafgnklpke mrvkgdclnv ppaknsgpvd qqkklvrecg
      721 qrdgdtaqpd ggdrwfqvvr dimddpdnew wkapargred alesrddlfa ramedarwel
      781 taklgknist wswgrlhrlt lknqtlgteg pgllqralnr gpwnlgggea avnatgwnaa
      841 ggyevvwvps mrmvvnvgdw dksrwinlsg asghafnahy tdqtekwvdg elldwsfgte
      901 avdastvdtl tlkp
//
LOCUS       WP_457656862             329 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656862
VERSION     WP_457656862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35060
     Region          5..221
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mktaiavagl hksfgrthal dgldlsvdvg evhgflgpng agksttirvl lgllrgdsgs
       61 aqllgkdpwk dsvelhrrla yvpgdvelwp gltggeaidl lsklrggldr qrrdelverf
      121 dldptkkgra yskgnrqkva ivaalasdae lllldeptag ldplmevvfq dvilqakaag
      181 rtvllsshil aqveklcdrv siirrgrtvq sgtlsemrhl trttveaqtq hpatgldilp
      241 gvhgvqvkgr rvsfavdgah ldaairrlge fgirslishp ptleelmlrh ygdelavngg
      301 qghtegsagp gdthsgtitp vrggdeadr
//
LOCUS       WP_457656860             198 aa            linear   BCT 27-JAN-2026
DEFINITION  MogA/MoaB family molybdenum cofactor biosynthesis protein
            [Streptomyces griseus].
ACCESSION   WP_457656860
VERSION     WP_457656860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Kanaujia,S.P., Jeyakanthan,J., Shinkai,A., Kuramitsu,S.,
            Yokoyama,S. and Sekar,K.
  TITLE     Crystal structures, dynamics and functional implications of
            molybdenum-cofactor biosynthesis protein MogA from two thermophilic
            organisms
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 1), 2-16
            (2011)
   PUBMED   21206014
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Bevers,L.E., Hagedoorn,P.L., Santamaria-Araujo,J.A., Magalon,A.,
            Hagen,W.R. and Schwarz,G.
  TITLE     Function of MoaB proteins in the biosynthesis of the molybdenum and
            tungsten cofactors
  JOURNAL   Biochemistry 47 (3), 949-956 (2008)
   PUBMED   18154309
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Schwarz,G.
  TITLE     Molybdenum cofactor biosynthesis and deficiency
  JOURNAL   Cell Mol Life Sci 62 (23), 2792-2810 (2005)
   PUBMED   16261263
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..198
                     /product="MogA/MoaB family molybdenum cofactor
                     biosynthesis protein"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19259
     Region          29..193
                     /region_name="MoaB"
                     /note="Molybdopterin biosynthesis enzyme MoaB/MogA
                     [Coenzyme transport and metabolism]; COG0521"
                     /db_xref="CDD:440287"
ORIGIN      
        1 mtppepaasg heghapasgs gpgpepgasg vaphapyral vvtasnrasa gvyadkggpl
       61 iaealtglgf tvegpqvvpd gdpveaalra gvaagydviv ttggtgispt datpeatrrv
      121 ldheipgipe airaeglakv ptaalsrgla gvaartlivn lpgstggvkd glavlgrllv
      181 havdqlrggd hprpgsps
//
LOCUS       WP_457656863             180 aa            linear   BCT 27-JAN-2026
DEFINITION  GbsR/MarR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656863
VERSION     WP_457656863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8) (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..180
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19911
     Region          32..171
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 msegrrgdgr adggrgevvg ggaadaeaaa srfierfaaq lveagmarmp arvfaallss
       61 ergdltsael gerlkispaa vsgavrylaq vdmvsrerep gsrreryrvq gdqwysalte
      121 rdamlrswqa tlkegvshfg letpqgrrin dtleffrfle nelgslmerw ethraqhrgr
//
LOCUS       WP_457656866             425 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces griseus].
ACCESSION   WP_457656866
VERSION     WP_457656866.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..425
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42832
     Region          13..417
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msrrpipdgv pdelrrrlgv pdavviglgs migagifval apaaqaagsg lliglavagv
       61 vaycnatssa rlaarypasg gtyvygrerl gdfwgylagw gfvvgktasc aamalavgsy
      121 vwpgqahava vaavvaltav nyagvqksaw ltraivavvl avlaavvvas ftsgetdaal
      181 lgvgpdadlr gvlqaagllf fafagyaria tlgeevrdpa rtipraipia lgitlgvyal
      241 vavcvlmvlg pqqladatap lsdaaraaga drlvpvvrtg aavaalgsll alilgvsrta
      301 lamardrhlp hvlaavhprh rvphraelav gavvavlaat tdvrgaigfs sfgvlayyav
      361 anasawtltp aegrphrlvp vigltgclal afslpvssvl tgaavlalga aaygirrfaa
      421 grrkp
//
LOCUS       WP_457656886             233 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656886
VERSION     WP_457656886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..233
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25213
     Region          6..204
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mddvrevivi gsgpagytaa lytaraqlrp llfgssifvg gsltttteve nfpgfptgid
       61 gpdlmdnmrd raerfgaemi dddivsvdlt gdikevtdse iaeikaengm lagvvlrdtf
      121 tgrtrdldat glfiaighdp rtelftgqvd ldhegyikve apstrtnlpg vfaagdvvdh
      181 tyrqaitaag sgcqaaldae rylarpcrqa qgrrerhrhg lrpqrsprcr hsp
//
LOCUS       WP_457656878             533 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457656878
VERSION     WP_457656878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..533
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55532
     Region          22..485
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mdvfatkaga vrgrraardr givvvrglpy aappfgdlrf raprpaeswd gvrdcpafgp
       61 vapqsaelpg apvwspgded iltlniwtpa dgpgdlpvlv wihggayvfg ssaqpdfdgt
      121 alagrglvvv tlnsrigfeg fghvpaaedr dgpilaegrg gpapdadgss apfpdnrgll
      181 dqiaalewvr dnisafggsp drvtlagqss gatsvacltv agrarglfrr avlhsavnaf
      241 amveqaartt aevaeaagvp atragllaap pealvaaadr vcaryaqdpg sgqrhydpai
      301 ygpvadgvll tadplealaa gaggtvellv chtteeywll davgssakvt teeqlasfaa
      361 dfglpaalvq ghrellpdap vldvylslcs gllfaeystr laeahalagg raflarfdrr
      421 rdhtgrrvra whcadvpfaf gnlheesvhf lvggppgaad qelsrhmtra wadfaahgdp
      481 gwdaldgpag sgaavrvwrt aeerqggrqe hgrgaagglr dlwrtaglpl lap
//
LOCUS       WP_457656868             270 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656868
VERSION     WP_457656868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..270
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28229
     Region          1..225
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnrspagavv tgagrglgrl iaailvergh rvlvtdided aahataaelg pdvlwaavdv
       61 rdetrtaaar dlimarsgrl dvwvnnagvl atgpaweqpp evrrlmlevn glgtvaaiea
      121 mrgtgghivn vvslagltav pgeavyaask haaigfslst ladlrlagik eidisclcpd
      181 giwtpmlhdk lddpasalsf sgtllepeea aaavrkvldr prpvtaiprr rglqvrlada
      241 fpslglravp lavargrrvq rkmragaapk
//
LOCUS       WP_457656887             419 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457656887
VERSION     WP_457656887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10605546
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..419
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44818
     Region          213..354
                     /region_name="Acetyltransf_6"
                     /note="Acetyltransferase (GNAT) domain; pfam13480"
                     /db_xref="CDD:433244"
ORIGIN      
        1 mggsprvvis tgqalpdmdw tgelagltds wpylgptwlr atekvlpdiq pwhtlahrar
       61 gelallpgyi lttppvvdhe prtylgwqap sgeevccgae tdaarsaevd algiepffpt
      121 lllgsplgyr tevaynfwtp tlmgaivdkl vpaafeagic civapwipnr rgndalvdal
      181 naagasstfw gyedfmslda pnweghlaal plkkrqrikg dvrraeaagv tiervdgtdi
      241 rpyiariael tclnreknga geepehivgi lsalidegad vraylgykdg alvatcvtir
      301 knhrlfpkwa gfdyaaiger sgiyfalvld apvrdayaeg lrtvefgaga hqakalrgct
      361 prevttsmll sdpalrpqak awldafgnsr raafgaaspa paqpanlpll ggsgdsccg
//
LOCUS       WP_457656892             324 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457656892
VERSION     WP_457656892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35572
     Region          87..295
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtdlpppitp ylepaakelc eatdphpriy evppekgrdl llglqsdlsv prpevdeewv
       61 dvdagewstv rtriirpqgt tgplpvvffi hgagwvfgdd rthdrlfrel tvgagaagvf
      121 pvydrapeat yptqveqnya vgrwvlehga ehgldtsria vtgesvggcm savfalmnke
      181 rggidlkaqv llypvadadf dtpsylqfae gyyltrdgmk wfwdaytsdp aqrtevhasp
      241 lrasldqlrg lpttlvitde advlrdeges yanrlreagv dvtsvrvagm vhdfllldsl
      301 rdtraanvar tlavdalkka lhdg
//
LOCUS       WP_457656888             303 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphate ABC transporter substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457656888
VERSION     WP_457656888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 303)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 303)
  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   6  (residues 1 to 303)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Takemaru,K., Mizuno,M. and Kobayashi,Y.
  TITLE     A Bacillus subtilis gene cluster similar to the Escherichia coli
            phosphate-specific transport (pst) operon: evidence for a tandemly
            arranged pstB gene
  JOURNAL   Microbiology (Reading) 142 (Pt 8), 2017-2020 (1996)
   PUBMED   8760913
REFERENCE   9  (residues 1 to 303)
  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 10194586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="phosphate ABC transporter substrate-binding
                     protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31354
     Region          45..294
                     /region_name="PBP2_phosphate_like_1"
                     /note="Substrate binding domain of putative ABC-type
                     phosphate transporter, a member of the type 2 periplasmic
                     binding fold superfamily; cd13653"
                     /db_xref="CDD:270371"
     Site            order(53..55,81..82,100,178)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270371"
ORIGIN      
        1 mstesrsraa rltgrrvrqg asvasaslll saaltgcags akagsdaiqa sgsttvapva
       61 sdaaealqak glnitvatqg gsaggisqlg tgqinialss kplsekdqka ypdtdfvttq
      121 igadavgvii tkevadggvk gltkaqvagl fegkitnwke vggpdlqvfv ydkepgrgtr
      181 evldkfiygk geapappksa nyaivggnle trnklkstrg siaplstgfi eghpelvavp
      241 ledvaptlen vasgkypmtr plymitngrp kdgvkqyidy ilspegqkll pqhgyltreq
      301 mgl
//
LOCUS       WP_457656894             366 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457656894
VERSION     WP_457656894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  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   2  (residues 1 to 366)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..366
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38339
     Region          20..363
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 meeprkrsrp grapapagrt srprqaevar lagvsqatvs lvlgarkqga tiseetrrkv
       61 ldavralgyv pdpaasrlaa arnnllgvfs ftstfptdvq hsyypflvgv eqeaavrgyd
      121 lvlftgsstg gagaagpnal nrvrladgcl flgrhapade llrlvadgfp vvhlgrrdel
      181 eglawvgady vsaaqevvah laalghrriv lvreddeapa stdrehgflk gleeaglpgg
      241 paavfrsadp erdltaerlr gwldegvtaf vaeetdtsda wralhgaahf vgihcphdas
      301 lallgspppd ladgpvptgf dvprpqlgaa avrmlaalva geeateplva ctfrpgstag
      361 papvhl
//
LOCUS       WP_457656893             439 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457656893
VERSION     WP_457656893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 439)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 439)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..439
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47019
     Region          45..426
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(156,158,278,280,315..317,360)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mstssqllsr rafgrlaagv aagagagals acsggggmps agtplrimai nhvwsqavkr
       61 rtaefeerig rrvsmtllta dqlassynvk lnasgtdvdv mmvralqeql lfghngwlad
      121 lsdrvaddar fawddfqdap reasvtagkv lsvpvvterp alyyrkdlve dlggpprtle
      181 almegarelt rrkdgfygyv grgqrsgavs qwssflyshg gdfvvdgtsg igsaeavaay
      241 eyygrllags gppgatnmsl eqampifaqg kaaffvdada iyssfldpkv srvretvgfa
      301 pfpagpagar phnipswslg intfsrlrdd awefirwaag pemsaalqse gipgarssvw
      361 sdpktlaafp pelaesmrln aergvgydrp rvlqvgrard ivgrplvagi lgesvrpvvr
      421 dadaefadfl vrdnrhkes
//
LOCUS       WP_457656897             569 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457656897
VERSION     WP_457656897.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..569
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63305
     Region          16..538
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msgerssarr pretmiiiga glgglstgcy armngyrthi lemheipggc ctawerggft
       61 ldacvswllg sgpgnemhqi wlelgalqgk eirhfdvfni vrgtdgravh fysdpdrlea
      121 hlialspada rlvrkfcaql rsfrkalavy pflkpvglmg rrerwrmlas flpyfnavrt
      181 titvlmtdfs kkfkdpllqe afnfilyekh pafpvlpfhf qlashanlsa gvpeggslgl
      241 aesiearyrr lggeisyntk vetviveddr avgvrlsdgk elradivvsa cdgytttmkf
      301 legrylgedy rklytetihe pgmvfpgyft lflglsrpfp egdpcttyll deataaeltg
      361 irhpsinvqf rsrhypelsp dgttvvyaty fcdiapwral degpeqvtrt rggtelhtlp
      421 vrhgrgyyaa krrarealvg fleqrhpglr daivvrdvss pltqvrytgn ydgtvlgwqp
      481 fvesgetlee likkhgpglp glrdfyqsgv wattgglira aaagrhvmqf vcrddgrpft
      541 asldltappp thrvipvpvr paapterkp
//
LOCUS       WP_457656898            3125 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase/type I polyketide synthase
            [Streptomyces griseus].
ACCESSION   WP_457656898
VERSION     WP_457656898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 3125)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 3125)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   3  (residues 1 to 3125)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 3125)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 3125)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 3125)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   7  (residues 1 to 3125)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
REFERENCE   8  (residues 1 to 3125)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 3125)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18690202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3125
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..3125
                     /product="non-ribosomal peptide synthetase/type I
                     polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="6.-.-.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=336997
     Region          10..1402
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1283..1684
                     /region_name="KR_2_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 2, complex (x); cd08955"
                     /db_xref="CDD:187658"
     Site            order(1450..1451,1453,1473..1476,1514..1517,1543..1545,
                     1566..1567,1589..1590,1604,1631..1632)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187658"
     Site            order(1567,1591,1604,1608)
                     /site_type="active"
                     /db_xref="CDD:187658"
     Region          1722..1805
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1817..3045
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 madannralr nkvaiigmgc rlpggasdhr tywrnlmagk dcitptppdr ydvrtlgsrf
       61 rdkpgrlvgg rggyidgfde fdpaffgisp readhmdpqq rkllevawea ledggqrpad
      121 laggnvavyv gaftldykil qfadlgftsl aahtatgtmm tmvsnrisyc fdfrgpslsi
      181 dtacssslva vhlacqalnn gesdlalagg tllhmapqyt vaetkggfls pegrsrtfda
      241 aadgyvraeg vglvalkrld davrdgdrih aviagsgvnq dghtngitvp nadaqvdlir
      301 rvcaeagitp gdlqymeahg tstpvgdpie analaralai grapgarayv gsvktnight
      361 esaagiagli ktvlsiqhrt vpphinlenl npaidpatlp yeiptrptaw pahegparag
      421 vnsfgfggtn ahvvleeapp pppktcaapp agrpwsilpl sarnpdalve laagirgela
      481 gdngpavald dlghtlahrr qhlperlsvv ystrasldea laahgrgeph prvvhgrare
      541 sadrrlvwvf tgmgpqwwgm grqllaeepv freaveacdr alrefadwsl ieeltadesv
      601 srmsetwlaq panfavqval aalwrshgvr pdavvghstg eiaafhaagv yslrdaariv
      661 vhrsrlqqtl agtgamlavs lsedeaerrv rpyrdrvsva avnsptaitl agdeaaltll
      721 aeelraeqqf akfltvevpy hsvgmerikd ellaelaple prparvplyl tgvegtarge
      781 eldaaywwkn vrdrvrfrsa vdriaadghq lfleigphpv lghairecle aggttgltlp
      841 sirrrenese rfaaslgslh tlgvtvdwdv lqptgrpvtl prhpfrrdrh wteprpvaqv
      901 rlghrdhpll grrtdrtept wqarldtedl pyladhriqd tvvfpaagyl emaaqavlrl
      961 tggttavlad idlrkalflp dgedrtvevs lslenaafti asptgddger avhasgivrt
     1021 gqrrrtappl dapairarsl rhlegpdcyt alaalgyhyg pafqaveevw igagevlari
     1081 rppeaigdda aghhlhpvll dacfqtlltp lipptpegpa pgtgirlpls vdevalepig
     1141 dqpfwahatl lpgdadttlg nialyaddgt plgrvhgfra advekaatav arttidswla
     1201 epawteappl paedtardhd wlvladnggv adafaalaaa rgercrlvrr gaaytasgdg
     1261 vtftvdpasd adlrrlladl draggpfrga vlhlwnldap aladcdraal rdhtgagayg
     1321 lialarllla rggggrlhiv trgaqpalpg egpeplgapa wgigrvlrhq elidhpgkli
     1381 dldprrrpgp dgdraeaeal laevlsddee eialrdggrr tsrlrpaehl trplpprlra
     1441 dgsylvtgaf galgrllcrt lvrrgarriv lvgrtpvpar ekwagtdpat aegravallr
     1501 elealgaqpv latlditded altgwldahr qsgappvrgv fhlagqvrdt lvadldraaf
     1561 davhdpktvg ahllhrhlrd eplehfvlfa siasllttag qtnyaagnaf ldalahhrra
     1621 qglpalsldw gpwatgmiee lglvehylhs rgmsslspdt gmavlervig qdhaqlvvat
     1681 vvdwpvflaw yptppplvad laaaaappgd aasgngfldt fraadeetrr alvaerfaal
     1741 satvlrtgtd ridpttglge lgldsllame lrarihaelg valpvvalls gtpagelaaq
     1801 lhdglsalaa adtpdgaaga velhrderqy pltqnqkalw flkhlnpdgy ayniggavev
     1861 nvalepdlmf eavrrliarh palrtnfllv dgqavqrvse daatdlglfd vqgedwdsih
     1921 ativqeyrkp ydlahdplvr frlfkrgpdr wiimkavhhi vsdaistftf ieellavyea
     1981 lrrnqepqlp pvearyldfl nqqnaflagp eaagmldhwr ahlpaevpll dlpvdkprpa
     2041 vqthngasef fvlddalsar vhalarahgv tpfmvllsay ylllhrysgq dhivvgspvt
     2101 grtrqdfasv ygyfvnplpl hadlsddptv aellqqvrrt vlggldnqey pfvllveelg
     2161 lqhdpsrsav fqamfillth kvateqygyr leyielpeee gqfditlsay edeaegrfhc
     2221 vfkyntdlfl petmrrmaah ytrlldrmth apgeqpasrl emlgdqerer lvgewsrpal
     2281 ptagsreepf aavqtliarv aaehpaavav ttpsphggah rltyaelerr aadsaarlrt
     2341 lgigqgsvvv lcldkspeli vallavlkag aaylplrpdq padrlahlvt atgaalvlva
     2401 ddagpeqtga lavptltlga lartaphpdg psdeagpesp ayiittsgst grpkavrvsh
     2461 rnlasahaaw rqeyrletdv rvhlqmaeps fdvftgdlvr alcsggtlvl adrdllfdtt
     2521 rlyrtmrqer vdcaefvpav vrglmdhcar eglrldflkl lvvgsdawsv geyrrlaelc
     2581 gpgtrlvnsy glteatidsa sfegpvddle pgamvpigrp lpnstlhvld ahgepvppgv
     2641 pgelwiggdg valgyagdpe qtearfvtrt lsrsadgdar perlyrtgdi arwdahgrvh
     2701 llgrtdgqvk lrghrieige ieahlaqwpp laravvtvra dtggeaalca ycvpvpgatl
     2761 dgralrrhla rslpsymips hfvelpalpl tangkvdaaa lpapraetgd rpyeepvtly
     2821 eisvarhwkt llgreqigle ddffelggss ikliellhql rtefgvgvpv srlyqvttlh
     2881 gmaatvedvl hgtsadelps ltfnagqhpa lfcfppaggh glvyrglaah lpdhtligfn
     2941 ylpgddkvar yadlieaarp dgpyrllgys lggnlafeta kelerrgrrv ahvvildsrr
     3001 iltayepdas giavfeaela dhlrkhtgse avtretlaha aeylafcgrt pntgtvaatv
     3061 svitdeekaa lyaagehgtw hgsstgatav lrgsgvhadm ldakhlprna elvrsvltgd
     3121 pahgg
//
LOCUS       WP_457656902             193 aa            linear   BCT 27-JAN-2026
DEFINITION  fasciclin domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656902
VERSION     WP_457656902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..193
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19651
     Region          41..190
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mtinrlqrta aaaaalafpa slaffapqaq avapaepygp acssvpaega gslegmakdp
       61 vataasdnpe lstlvsavek aglvdtlnna kditvfaptn dafdkipkad leallndkae
      121 ltkvltyhvv gekittqqle dgsfktlegs dlttkgsgta ftvndsskiv cgdvptanat
      181 vnlvdtvlmp pss
//
LOCUS       WP_457656903             695 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457656903
VERSION     WP_457656903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..695
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=71890
     Region          13..692
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mstparsirw lipvvlliaw lgiggglgpf agklgevatn dqaaflpqna estqvieaqk
       61 afqqnetlpa ivvwtsaekd apvsdeqrea atvalaslag sdgvvgapsp alpaedglal
      121 qgivqlspgl gdelptvler ideagasvpg ttvqlagpaa sqadlsdafa gidglllgva
      181 litvlvilll vyrsvllpfv iilgavfala lscaivyvla dhdivrvdgq vqgilsilvi
      241 gaatdyalll tarfreelav hgdrfvamri alresfgpit asaatvaagl lalllsdltn
      301 nralgpvgai givcsvlsal tflpaalvll grkaywpakp kpaddqvsgg hgiwhkvaal
      361 vdraprkvwa itlaaliaca afaptltskg vpldeifvnd apsvaaqetl sehfpggsgn
      421 paviiaaadr lpevteaaer tdgvasvapv sasgrpggep lvvdgkvrid atledaadsd
      481 gakeavaelr tavhavpgsd alvggytaqq ydtqrtaedd rmlivpvvlv iilvilvfll
      541 rsllmpvllv atvalnflat lgisslvfth vfgfsgtdss vplygfvflv algvdynifl
      601 msrvreeslr hgtregilrg ltttggvits agvvlaatfa algviplafl lqiafivafg
      661 vlldtlvvrs llvpalvrdi gpkawwpgal sretr
//
LOCUS       WP_457656913             353 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Streptomyces griseus].
ACCESSION   WP_457656913
VERSION     WP_457656913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..353
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=37362
     Region          18..330
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 maaamsaata allhrgtvvp ahplaltadr elderrqral tryyldagag gvavgvhttq
       61 favrdhgllr pvlelaaees aaaaaerpfl riagvagpvr qavaeattar elgydavlvs
      121 paglpdatld dllgrsaavg evlpvigfyl qeavggrelp raywraladq estvavkaap
      181 fdryrtlelv qgiadsdrga evalytgndd tivadlltpy hvttptgpav rrfvggllgh
      241 wavwtrsavr lladvhaada gderarqral arlagdtdan aavydvrgrf agviagvhev
      301 lrrqglltgi wcldptegls pgqareiarv htaypwlaee dafiagalpr wla
//
LOCUS       WP_457656915             388 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656915
VERSION     WP_457656915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450768
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..388
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=41214
     Region          12..>80
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
     Region          96..371
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mksaekkdsf lrgpkylhva erlrseitsg swapgsqlpv ereladrlev svntlrravg
       61 elvdegivqr rqgagtfvap lsgtapeetd ghrarrlvgv lvpsttyyyp rvvegiqrvl
      121 rdagvgivla sskydphleh devramldsg vqgmllvpnl hlvddpqqhv dalrrltvph
      181 vlverepptp apddptayvv tdhaggvcla vrhlrslghv righlgrlrt gtadavargf
      241 daaaallgvd vvegavared vwaaegiary vrrcaeagvt avfchgdrda aalvvaarrh
      301 glsvpgdlav vayddevaev gdipltavsp pkeevgslaa qlllrrmesg paavshrari
      361 lprlvvrasc ggtapdrram sgpapvgg
//
LOCUS       WP_457656916             340 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457656916
VERSION     WP_457656916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..340
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35547
     Region          32..271
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mppapptgrf rigvlgaggv gaahvhaaag apdyeiaavc dtdhaaaral aeaaalpvyt
       61 dhramfaeag ldavviaaph alhtpmtlea araglhvlve kpmattaedc almsracdaa
      121 gtllavahvi hfdpvvrear aliasgrygr pllithrrsa hyepgsrppw ffdravaggg
      181 ivlnvgthgl driqlfsdst vrrvsgvvrg rpglevetda lalveldngi dasialtsrg
      241 mpyvdetevv ldeatlrvsa teglfvlrdg ratqllraep shqhqafraq ldgfveaarg
      301 gpgryvdaay grgvvaaala vyasaelgqr vdvadrpvpr
//
LOCUS       WP_457656914             344 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656914
VERSION     WP_457656914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..344
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36144
     Region          33..324
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkellggvpe leeelgrpgp alvheaadwp gdvvvlgagg ktgagiasma rraldeagrs
       61 gakvhavsrw tdargragle ergvrtvrsd lsdpaaldal pdaevvihlv gakfgtasap
      121 eqawmtntvl pafvarryrg artvalstgn vygttapvtg gshesdeprp vgdyavtcrg
      181 reqvfthaar dgatpvalir lnyavepryg vladlartll aglpvdlgag avnvvwqrya
      241 nevvlrgvrh aaapepfvln ltgpetagvr alaarlgeal gvvpvftgee aatslladat
      301 lchtlfgypd rtlgqlvelq arwiagggel wdkptkferr dgrf
//
LOCUS       WP_457656917             258 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656917
VERSION     WP_457656917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..258
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26862
     Region          5..255
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnprafstlg cpgagldevv rlartngcsg velrcaegem vhpeltstea gllaaalgra
       61 glavpvlasy vqvaadgpdv verlarhisl aaglgagqvr vfgggadrpa grheravrhl
      121 aqaapiaeaa gvgialethd vfltgaevar vlkdvgspav gavwdavnpw ragesperta
      181 dvlgpwirhv qlkdvasptd lrpvlpgrgv lplgevlaql dtlgyegwis lewerawypd
      241 atpldealpa fhrvldgd
//
LOCUS       WP_457656918             308 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656918
VERSION     WP_457656918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 308)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..308
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32843
     Region          62..308
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mstpvrttps apvapagsap strrspggpr rtgrygpvaa nlvvgvsaly allpllwllm
       61 astvdaealf asdfldlshf alfdnigtll aqddgaylrw ygnsllyavg gaavgalvst
      121 aagyvfdkfa fagkrplsal ilisvmvpat vlalpmylla sdlglantvw svlipvlfnp
      181 fgvylarmfs asyvpdevle aarvdgagel rsffsvglrm lapgyvtifl fqltaiwnnf
      241 flplvmlsde slyplslgly swnasapinp dyyplmvigs llallplvva flllqrywrs
      301 gltagsvk
//
LOCUS       WP_457656919             318 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotriesterase family protein [Streptomyces griseus].
ACCESSION   WP_457656919
VERSION     WP_457656919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chen-Goodspeed,M., Sogorb,M.A., Wu,F., Hong,S.B. and Raushel,F.M.
  TITLE     Structural determinants of the substrate and stereochemical
            specificity of phosphotriesterase
  JOURNAL   Biochemistry 40 (5), 1325-1331 (2001)
   PUBMED   11170459
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shim,H. and Raushel,F.M.
  TITLE     Self-assembly of the binuclear metal center of phosphotriesterase
  JOURNAL   Biochemistry 39 (25), 7357-7364 (2000)
   PUBMED   10858282
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Kim,G.J. and Kim,H.S.
  TITLE     Identification of the structural similarity in the functionally
            related amidohydrolases acting on the cyclic amide ring
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 295-302 (1998)
   PUBMED   9537960
REFERENCE   4  (residues 1 to 318)
  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
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Tuovinen,K., Kaliste-Korhonen,E., Raushel,F.M. and Hanninen,O.
  TITLE     Phosphotriesterase--a promising candidate for use in detoxification
            of organophosphates
  JOURNAL   Fundam Appl Toxicol 23 (4), 578-584 (1994)
   PUBMED   7867909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004443
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..318
                     /product="phosphotriesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33735
     Region          7..312
                     /region_name="Php"
                     /note="Predicted metal-dependent hydrolase,
                     phosphotriesterase family [General function prediction
                     only]; COG1735"
                     /db_xref="CDD:441341"
ORIGIN      
        1 mnhppprtlr tvtgslapea vhgpvlpheh lvldldragd gaavldperh aatvsgelee
       61 lrrrfglalv veltcrgmgr dvtalarlsr etgvpvvaat gwyyepfhtp eidtadveql
      121 tavlvreied gvgatgirpg vlgeigshgd vptpsetkvl raagraalat glplathaql
      181 grggtaqlel ltgeglpaer icvghqdlld dpgvhrelaa rgayvafdtv gkesyqsdrt
      241 rlrlltalie aghadralls cdisrhgylr aeggqgyghl fegflpglra agadddlvdl
      301 ltrrnplrfl tganveen
//
LOCUS       WP_457656920             896 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656920
VERSION     WP_457656920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..896
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=98363
     Region          337..>836
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 miadlvaapa rqqeplktla hveyqlrvlg llcaaaaegp telttpgsld rwatyisqqq
       61 gsldcdtcqt salvvadsin teialgmplr rmrnqvfhgg pdpqnvdlda lhqvvednat
      121 rivrihehgh aanlepffll vrgepaalqd yssatatywp rrgpatdisd qatldalqkl
      181 glqggdrmfe sfaadiekdl rgfakpgsvq mlvdppepia arwelrtseg svlrvdhfel
      241 dvdhariwrs dagprpykaf laeickwdll kerlleglde qlelekkisd elfpdlkrhi
      301 pnvpaqvhia ngpfgegrdv titeacaris qqagiynact nlitltgeag sgkthsllqf
      361 areslssged lsplavyiss sgasansldt lldarmaptr ildkrsvlal craglvilvi
      421 dgfdellgfr tydnpltglk pildelrgkg tvvlsarssy searllrslt ardalawppy
      481 itplellpwr peqlraltsq lpievdgtgt pqeirqlltt pffclafvdw mrtgsgefmq
      541 fvvdtylqre rrkmpgqggn dlfssevlad ifsevselia rnvvpeisge dfelaaslal
      601 grdlnkeekr rlvalcglsa ewaddelafk fthlaiaeqf larqiarlpl dqavsllfsv
      661 pisplcaqli lsmwrsqgrg qptelvielq hkvsaayasd ahlpgaslsl galwakvhgv
      721 gegprtgrci svenlelsgs gqvtlvdarv qnltvqpgve lllvsghver ldlsrsgasa
      781 llgdsykhvr ellmhnelav grpsikralg ladeqsadds dnhfkanitr argpiivkrd
      841 yapdensqlh wvsdygldtw qafvrrmqke gkisvekvna sgrpkvrlrp tesfda
//
LOCUS       WP_457656921             167 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces griseus].
ACCESSION   WP_457656921
VERSION     WP_457656921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..167
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18263
     Region          5..65
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msdyeralpa wvravvlaag ggwctycgsn giraeavdhv vplhlggahs itnlvpscrs
       61 cnsskrdrtv lgwrrsihrr ifhngvwpne vadyteegal anvrriqddv aklarehqad
      121 avekllrrva ligmnlqhlt agqradvlea mrvlcdefas drvspga
//
LOCUS       WP_457656925             884 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656925
VERSION     WP_457656925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..884
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=94471
     Region          <27..861
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            order(609..610,612,643,646..647,650..651,653..654,684,
                     687..688,691..692,695)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          641..671
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          683..708
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkpsrplyer epelaaaaea vdalcgaqav ggllvfsgea gigktallae iqamaadrct
       61 vwsarggetv tsvpfhvvrq llqpaldqfp pdetralfgd wydttapalg laepsgpqpd
      121 pqgvrdgldf vvgrlasrls hrplllivdd ahwadgesla wlasftarlg elpvlvvqah
      181 rpqelaerda nyiahreaer gaggqgtvnr valraltpda tavlvraglg dhaddpfcre
      241 vwavtggnpy eavelvakvq drelppvees agelrelgas argsglvarl erlgtnanrf
      301 awaaavlgtd isqelaatla gmssaeaadc tarlrdariv sgfdplefvh pliatavyrs
      361 ippatrtamh graawaitra glgaaaasrh llevhpdddq elvaqlreaa gqhlavgape
      421 aarrcleral eepprpkdra allyelgcat llssppttvq hlraaldmpg lddglrvdat
      481 frlaaalahn nqlkdaalsl aaeaartapg pglmrlqaah fmwegmqaae ddgparsrrl
      541 trnadhlkgr dnaeralltl rafdamlrge naqlivdlce ralvdgspar glgwtdsewg
      601 felptmvgit ytfvdqldra eslfgeavra feisgwsgah lafahtllgm vhrrrgrlae
      661 aegflreglr ladrvgsglp vhwdaaclli dtllargrtd earkiadryd fgppypsamv
      721 lpdgpcvrgr lllaegrked aiaeleaaga aleprerfng iwapwagdla ralaeddpar
      781 aahlaarnrv haerfgtpta lgealrcval fappersaql laeavghlek sssayehala
      841 rvdygiaigs hrelaraqkq amtcgaegla araqqarasi rsse
//
LOCUS       WP_457656929             225 aa            linear   BCT 27-JAN-2026
DEFINITION  LutC/YkgG family protein [Streptomyces griseus].
ACCESSION   WP_457656929
VERSION     WP_457656929.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..225
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23583
     Region          18..221
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsapdnars tvgdtvgsar dtvlgrirda lalaptpavv vprayrtgra lpdderlalf
       61 tdrlldykar vhpctadrta evvgevlreh svrrigvpag ldarwlagyd gearqddadv
      121 tpaqldalda vvtasaagca etgtifldgs pgqgrralsl vpdlhvcvvd lstvevgvpe
      181 avarlvperp ttlisgpsat sdielerveg vhgprtlvvv irtda
//
LOCUS       WP_457656927             264 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Streptomyces griseus].
ACCESSION   WP_457656927
VERSION     WP_457656927.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..264
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27372
     Region          6..263
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mdtislwqla vlaaastlvg fsktavsgan tislavfaav lparestgvl lpiliagdll
       61 avrvyrrhah wptllrlfpa vavgvvagtl fmlwaddaav rtsigaillf mtgvtlwrrr
      121 iaeqeageqg tnkeagagad sggeggtgrt aargygvlgg fttmvanagg pvmslyllsa
      181 gfrklgflgt sawfflivnv skvpfsvglg lidansllln aclllfvlpg aylgrvcvdr
      241 inqkvfdriv igatvagglq llli
//
LOCUS       WP_457656930             243 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656930
VERSION     WP_457656930.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..243
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26001
     Region          6..236
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mpvewqpvqq srthelvlrs ieervvagel ragdrlpper elapvlgvsr salrealrvl
       61 etigvlvaqp grgpdagari vrnpddalgr llrlhfalgs yslqdvlear vvlerssfea
      121 aachapdedl daaeelvagm aepgigvsgf ndldtrfhvl iarssgnalt stltsavres
      181 vrplilrale aaedwpatar alnaeheall alvregkgad aadlverhir glhgtlvdep
      241 tap
//
LOCUS       WP_457656936             132 aa            linear   BCT 27-JAN-2026
DEFINITION  MmcQ/YjbR family DNA-binding protein [Streptomyces griseus].
ACCESSION   WP_457656936
VERSION     WP_457656936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..132
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14302
     Region          8..120
                     /region_name="COG3801"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443014"
ORIGIN      
        1 mtaeptitaa dvrssalslp dtteklawgq ptfrvagkif aslgddettm gvkcpredra
       61 eliatepekf fireghddhy awmrvrlsal edadelatil adswrqvapr rlaaahpela
      121 vqgedgpgeg rg
//
LOCUS       WP_457656938             242 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457656938
VERSION     WP_457656938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..242
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26336
     Region          1..240
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mhlytmrtpl aenfagtleq laeigyatvg vsgrhgnspa airqmldrtr lkavlehvgy
       61 divtgsglpq aledvhtlgg qwivvpslpg slhspdgyre varqfnrvgl aaresglkll
      121 yhnhgsdhqv vdgvslydil laetdpelvg feldlywaad ggssdpgelf vrhrgrfpal
      181 hvkdmapngd fadvgsgvld fpamfdtarq ggvkqwlveh dapadpfasa rasyrylsrl
      241 ry
//
LOCUS       WP_457656940             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656940
VERSION     WP_457656940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29517
     Region          24..276
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtmpkqqttp rapsaagagp aagvrltdva vrfrskkrdv talsevsldv apgefvaivg
       61 psgcgkstll klvaglltas sgdvllgger vtgprhdigy vfqraallew rsalrnillq
      121 aeirhmepaq aggradelir mtgltgfeda yphelsggmq qrvalcrall heppvllmde
      181 pfgaldaltr eqmntelnri wrttgttvll vthsiseavy ladrvvvmsp rpgtvteiie
      241 vglpaerdys etlgrpefra aaahirdllg avsahd
//
LOCUS       WP_457656951             272 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656951
VERSION     WP_457656951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29275
     Region          13..260
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 mdgntgnghr rvvaaldgvs mrrhatgqvi ldgidwtvra gehwallgpn gagktsvlrl
       61 vgatafpttg tvdvlghrlg rvdvrelrar ighvstsqrv pgdltghttv ltghsgtvqp
      121 lwkaygddvr erahallael rikeladrpy gvcsggqrar iliaralmad palllldepf
      181 naldlpsred lidtmrhlal nrpelstvtv thhveelspa ighalllreg rvladgaved
      241 vlteermtac fgrpievtrh agrwlarsgg fa
//
LOCUS       WP_457656956             321 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656956
VERSION     WP_457656956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32792
     Region          4..316
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mitaisigav tvpvtdvwni vahhltgqga tddpaadqiv wsfrtprvll aalagaglav
       61 agavlqtlva npladptvlg fsygasfgav lvitlggigi ggvgvagaaf lgalatgaav
      121 falgrrrgrl aptrlvlagv avgyvllsat sfvqlwatpt elrtvmfwml gsvagaqwdq
      181 lpvvatvvlt ctallglfgr qlnavlagde satalgvdvd rlravllvit alltgsviav
      241 aggigfvglm iphlvrltag adhrrllplt allgavylvl vdllsrtlir pnelplgilt
      301 allgapffvw llrrnkgldt v
//
LOCUS       WP_457656955             267 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656955
VERSION     WP_457656955.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28374
     Region          3..245
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mkltvdrvhv elegtpvlqg vdlevlpgav vglvgpngsg kstllrtvyr slrptrgivr
       61 vgeddvwrla prtaarrtaa vlqdpvgstg glsaaeivel grtphhglig regpddrrav
      121 adaidrcgvr pfaareyatl sggerqrvll aralaqeprl lvldeltnhl dirarfelld
      181 lirstgvstl avlhdldlaa rlcdrvivld egravaaghv ldaltprima dvfgvaaaae
      241 rhadgvvrit yaadpldtgr atgtadr
//
LOCUS       WP_457656941             194 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457656941
VERSION     WP_457656941.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21117
     Region          <41..>179
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mtsfatgrml ltptdrhgta raqrlrkldl gerpdasydn fdafadkvae vtatpfsmvn
       61 fidenrqffa glhtpagnrg gqdlgsvaag ssrssrymar dhgycphvlv rrkalvlddv
      121 cdyprfagnp vvddigirsy lgaplidrtg ialgtvcavd tvprpwgrag ldtikslahe
      181 lvrqiddreg hhpl
//
LOCUS       WP_457656946             405 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457656946
VERSION     WP_457656946.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..405
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43980
     Region          96..344
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mtgadyllpl rtklrsmrte sfgadpagar merirrsphf vdgafqnpvg arirpsgstv
       61 dfakiyfqke qrarrmptgt vpvhattltd laappasglr ltwmghssvl aeidgrrilf
      121 dpvwgercsp fpfagpkrlh ptplplaalg pvdvvvishd hydhldlpti ralagtdtvf
      181 avplgvgahl erwgvpaarm heldwnetat vagisltatp arhfcgrglr ngqhtlwasw
      241 avtgpehriy hsgdtgyfpg frdigaehgp fdatmiqiga yseywpdihm tpaegmrahl
      301 dlqggsphgv llpihwgtfn laphawaepg ewtkdageda gqpvafprpg epfepagslp
      361 vepwwrplsa plarpwrrta eqqgpgpgpg peaaargdld lager
//
LOCUS       WP_457656952             226 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457656952
VERSION     WP_457656952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..226
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23953
     Region          4..201
                     /region_name="Abhydrolase_6"
                     /note="Alpha/beta hydrolase family; pfam12697"
                     /db_xref="CDD:463673"
ORIGIN      
        1 mpavvlvhgl yhrpehfdav aerlrtggae vvvpelhrgs lpadtvavqa vvdslteppl
       61 llghsyggsv itgvrgaghl vhlaafvpdt gesaatlgga sprlqdaiva epdgstslrp
      121 draadvlyhd csapladrav allrpqapgc grgvpthhsw kdtpstyvvc grdrvidpal
      181 qrrmaarcte vrewrtghsp fvgqpgllad llrgllrelr epvlqq
//
LOCUS       WP_457656962             353 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-ACP synthase III [Streptomyces griseus].
ACCESSION   WP_457656962
VERSION     WP_457656962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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   3  (residues 1 to 353)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..353
                     /product="beta-ketoacyl-ACP synthase III"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0033818 -
                     beta-ketoacyl-acyl-carrier-protein synthase III activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36514
     Region          11..336
                     /region_name="PRK09352"
                     /note="beta-ketoacyl-ACP synthase 3"
                     /db_xref="CDD:236475"
ORIGIN      
        1 msvtsvgrtd raavlcgvgg wlprrqvgnd elaarldtdd swirtrtgir srhlaapdea
       61 tsdlavaagr raltnsgtrh adavvvattt pdrtcpatap avaarlglsg aaafdvgavc
      121 tgfvyalaag ggliasgaad rvlvigadvy srivdpadrq navvfgdgag avvlraghad
      181 epgalgpfdl gsdgdhedli tvaaggsrvr adpdrtsrae rhfamrgkev yrhalhrmtd
      241 saravldrsg lavdgvdrfv phqanlrilr tvatdlglpa drcathveta gntgaasipl
      301 aladdhahrv lrpgdrvllt afgggltwgs clltwpdlpp taepahreee pap
//
LOCUS       WP_457656963             467 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457656963
VERSION     WP_457656963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..467
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46624
     Region          22..445
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(29..30,33..34,37,69,119..120,122..124,127,148,
                     151..152,155,280,283..284,287..289,292,320,324,377..378,
                     382,386,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msataaepta grrrlglpvv vlalaqlvis ldhsivhval peigaglgfl dhdlqwvvsa
       61 yvvttggfll lggraadllg rrrmfvlata iyaasslvgg lapspgvlla vraaqgiggs
      121 llfpatlsli tttyaegpvr nralalwgaa gagglcfgsl lggvlvhayg wpsvflvnvp
      181 ialalavsgr llfpadpprd rtrrfdaaga ltatagltli vfllvhapaa gwtsaaalla
      241 aagglvllal favverrtpd plvpvrlfrh rglvlatvva alfsatfssl pyfltlyfqs
      301 vrgydafvtg lcfvlpavvv aagtqagppa varfgmrrll vgglaggsvg alalvpavaa
      361 dgsylsllpg ivlvslgqgs awtalwiaaa sgvapgdqgi asgiasaslq aggavglall
      421 vaaasgvgrq saaaelldgi rtalsvmaga lalgalavla trratsp
//
LOCUS       WP_457656964             172 aa            linear   BCT 27-JAN-2026
DEFINITION  copper chaperone PCu(A)C [Streptomyces griseus].
ACCESSION   WP_457656964
VERSION     WP_457656964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Fisher,O.S., Sendzik,M.R., Ross,M.O., Lawton,T.J., Hoffman,B.M. and
            Rosenzweig,A.C.
  TITLE     PCuAC domains from methane-oxidizing bacteria use a histidine brace
            to bind copper
  JOURNAL   J Biol Chem 294 (44), 16351-16363 (2019)
   PUBMED   31527086
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Abriata,L.A., Banci,L., Bertini,I., Ciofi-Baffoni,S., Gkazonis,P.,
            Spyroulias,G.A., Vila,A.J. and Wang,S.
  TITLE     Mechanism of Cu(A) assembly
  JOURNAL   Nat Chem Biol 4 (10), 599-601 (2008)
   PUBMED   18758441
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10515835
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..172
                     /product="copper chaperone PCu(A)C"
                     /GO_function="GO:0016531 - copper chaperone activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17829
     Region          53..159
                     /region_name="PCuAC"
                     /note="Copper chaperone PCu(A)C; pfam04314"
                     /db_xref="CDD:461259"
ORIGIN      
        1 mrnpsaagll rrareatgtg avvtlasvaa igglsawtta gyagspakid vrearvllpv
       61 ipgqntnayf rivnsggapd hlrsvtfsas sateltvhrm natngayrer sgsveipaeg
      121 evemsphgpa vtlrsdaswr pgdrvtftld fqrsgavtve advrpvtqgs tp
//
LOCUS       WP_457656965             762 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces griseus].
ACCESSION   WP_457656965
VERSION     WP_457656965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..762
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78919
     Region          12..747
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 maaeatptvv vtdiavagmt caacvrrver klgklegvaa evnlatgrar vshpsevtpe
       61 eltsavdaag ytahvvapep ehparagkep deeearrere rllvttllsv pvlvlsmvpa
      121 lqfdnwqwlc fvltapvata sawpfhrral sglrhstatm dtlvslgvla sfgwsayalf
      181 lggagmpdmr mpfslvpsas dgmahvylea avgvplfvll grflesrarr gtgaalrsla
      241 rlaakevtvr rggadallpi erlrigdtfv vrpgervatd gevtegssaa dlslvtgese
      301 pvevgpgspv tggavnmggl llvratavga dtqlaritrl vteaqagkar aqrladtvag
      361 vfvpvvlala attlgfwlga dadpqaaita avavlvvacp calglatpta lmaatgrgar
      421 lgvlvsgpqa leglqhidtv vldktgtlts ghmsvgrltv apdgpdadav mrlagaveqg
      481 sehplgrait acarraagdd dlpavtgfra tagigvrgtv egrevevltp dgvelpaalr
      541 vareraddva rtavlvride vpaavvevad lvrpgsyrav drlrrlgvrp vlatgdrapv
      601 aravaedlgi aevharctpe dkaelvrrlr aegrrvavvg dgvndaaala gadlgiamgt
      661 gtdaaigaad vtlvrsdiea ladavrlarh tlgtirtnlv wafgynavtm plamvgllnp
      721 mvaafamsls svlvvanslr lrtwqpapar kprpraaews ta
//
LOCUS       WP_457656968             296 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656968
VERSION     WP_457656968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31150
     Region          38..290
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mtishapppp aahlapekas aptrtppele avvpasvrrs wlraaprwvr ravgpslllv
       61 lwqvfsatgv lhpdvlaspg tiaragadlv adgtlpaamg vslqrvvvgl llggvvgtal
      121 alasglsrlg edlvdatvqm lrtvpwvgli plfiiwlgig eapkvalial gvafhlylnv
      181 yagirgvdaq lieageslgl grwglvrhvv lpgalpgamt glryslataw lalvfgesin
      241 adagigflmn qareffrtdv ivvclvvyaf lgltadvivr ilerlllqwr ptftgq
//
LOCUS       WP_457656969             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656969
VERSION     WP_457656969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..336
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35371
     Region          25..259
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 matdlhrpvk dildpgpgat asgdapeaav rvegltrafd graviddldl tlrageftal
       61 lgrsgcgkst llrvlagldr eisgtvlvpr rravafqapr lmpwkrvwrn vllglpgkpe
      121 ravaeralae vglaeragaw pktlsggeaq raslaralvr epdlllldep fgaldaltri
      181 kaqqlvaelw qrrgcavllv thdvdealll adralvmreg riaydtpval drprgvgspg
      241 faelrsrlla elgvegqgap eaedgpegeg fpegqdgpag erlahgesri pghrepdtsa
      301 adgppsdvaa pprpngpvvt knpaaspahp rhgdvs
//
LOCUS       WP_457656974             605 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656974
VERSION     WP_457656974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 605)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 605)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 605)
  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 605)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..605
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65451
     Region          26..595
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mkpdeptwtp ppdartdadr ppaevrrilr lfrpyrgrla vvgllvgass lvgvaspfll
       61 reildtaipq grtglltlla lgmiltavmt svfgvlqtli sttvgqrvmh dlrtavytql
      121 qrmplafftr trtgevqsri andiggmqat vtstatslvs nltaviatvv amlaldwrlt
      181 vvsllllpvf vaisrrvgre rkrittqrqk qmaamaatvt eslsvsgill grtmgrsdsl
      241 tqgfaeeser lvdlevrsnm agrwrmstig ivmaampavi ywaagitlqs gatavslgtl
      301 vafvtlqqgl frpavsllst gvqmqtslal fqrifeyldl tvditepekp vrlekirgei
      361 afenvdfsyd ekngptltgi dvtvpagnsl avvgstgsgk stlsylvprl ydvtggrvtl
      421 dgvdvrdldf dtlaravgvv sqetylfhas vadnlrfakp datdeeieaa araaqihdhi
      481 atlpdgydtl vgerghrfsg gekqrlaiar tilrdppvli ldeatsaldt rteqavqeai
      541 dalsagrttl tiahrlstvr dadqivvled graaergthe elldrdgrya alirrdshqv
      601 pvpss
//
LOCUS       WP_457656979             445 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Streptomyces griseus].
ACCESSION   WP_457656979
VERSION     WP_457656979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..445
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44121
     Region          39..408
                     /region_name="Voltage_gated_ClC"
                     /note="CLC voltage-gated chloride channel. The ClC
                     chloride channels catalyse the selective flow of Cl- ions
                     across cell membranes, thereby regulating electrical
                     excitation in skeletal muscle and the flow of salt and
                     water across epithelial barriers. This...; cd00400"
                     /db_xref="CDD:238233"
     Site            order(103..107,134..138,353..357)
                     /site_type="active"
                     /note="Cl- selectivity filter [active]"
                     /db_xref="CDD:238233"
     Site            order(104,106,136..137,353..355)
                     /site_type="other"
                     /note="Cl- binding residues [ion binding]"
                     /db_xref="CDD:238233"
     Site            136
                     /site_type="active"
                     /note="pore gating glutamate residue [active]"
                     /db_xref="CDD:238233"
ORIGIN      
        1 mpatppgppv aapedpyapv rtrryaglll maallgvpvs aiafgflalv selqsltyte
       61 lpralgfeat pswwpvpllg iagllvgltv rrlpgggghr paeglvstga paavdlpgia
      121 laallslgag avlgpeapli alggglavwa agrvkrdlap earalvgasg sfaavsallg
      181 spllgafllm evaglagpml gvvlvpglls agigaliftg lgswtglgty sltlgevpsa
      241 aapgvagfgw alvlgvaaaf agagirrlsl alqerverrt vvatavlglv vgglalvyae
      301 isgkdasevl ysgehelghl lsgsaaysvg alvllivcks laycaslscf rggpvfpamf
      361 vgavggials hlpgldltag famgvgamcv amlrlpmtsv llatlllgke gltvmplviv
      421 avvaayvvtl rltpapvdra gpeav
//
LOCUS       WP_457656980             162 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione peroxidase [Streptomyces griseus].
ACCESSION   WP_457656980
VERSION     WP_457656980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Arthur,J.R.
  TITLE     The glutathione peroxidases
  JOURNAL   Cell Mol Life Sci 57 (13-14), 1825-1835 (2000)
   PUBMED   11215509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..162
                     /product="glutathione peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004602 - glutathione peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17330
     Region          1..160
                     /region_name="BtuE"
                     /note="Thioredoxin/glutathione peroxidase BtuE, reduces
                     lipid peroxides [Defense mechanisms, Lipid transport and
                     metabolism]; COG0386"
                     /db_xref="CDD:440155"
ORIGIN      
        1 mtlhdiplrt ltgepttlga ysgrtvllvn vaskcgltpq yeglerlqqt ygdrgltvlg
       61 vpcnqfagqe pgsaeeiqif csttygvtfp llekidvnga drhplyaelt qladadgeag
      121 dvqwnfekfv ispagepvar irprsepest evvaaieaql pg
//
LOCUS       WP_457656981             765 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457656981
VERSION     WP_457656981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12122902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..765
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=84232
     Region          9..415
                     /region_name="FAD_oxidored"
                     /note="FAD dependent oxidoreductase; pfam12831"
                     /db_xref="CDD:432816"
ORIGIN      
        1 mreeeghydi aviggglagt caaiaaarlg rrvalvnnrp vlggnassei rvwvcgatah
       61 gvhrwaretg imgelytenq yrnpegnpyy wdqvvldavr aepnidlfln tdvreveasg
      121 pddrrevhsc tgwmmgserr itfrarqfld ctgdgllghl agaryrtgre grpefdepwa
      181 ppeaddallg stilfhtkdl grpvkfvppa hakdlsdtpi lrnrvlrtgd ngcdywwiew
      241 ggeldtvhdn erirdelqsv imgiwdhikn sgrfpdaadl tlewvgslpg kreyrrflgd
      301 hvltqqdilq qrrfedrvaf ggwsvdlhpv qgmyadepga rqryadgifh iplrslysan
      361 vtnlhfagrn isathiafga trvmatcatl geaagtaaal cvaegltprr laterpdlvh
      421 rtllrqdasv igladedpdn laltarvsas ssltrlaaep taaapgtpyp ltrdlalllp
      481 vdpvldtvdl lvhgapdgts reltvelwgt graenavpad hllttavavp pggphwvtvr
      541 ldhrpetsgn aillvracad taltllpert dgvlalrrka egdaavdhdi peedgqpvle
      601 wqarglrrqt fafraapdta afgparavgg yqrpyggphm wssgpvgeae wlrldwdaeq
      661 dvtevrlvfd ddvdeylnnl hrhrtpyevm pelvrdyrlq acdaagdwht lltvtenrrr
      721 hrvhpvrtad ggpvrtaalr lvvdathgar hahvvafkay gdrtd
//
LOCUS       WP_457656982             308 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656982
VERSION     WP_457656982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 308)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..308
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33366
     Region          33..307
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 msttsttptp ppvtdrprpp aarpgpaprr rvrkdllrsr vaawsavvvi gafgllpvyw
       61 llatalstpd atfqfppkli ptdltlgnft alaendqlis ymvnslivat itavlsvvva
      121 tymgysfskf ryrgrkslmh mvlasqmfpq alllvtlyav fssfgmlnty talvlsfttf
      181 tmplcvwmlk gifdtvpdal leaasidgas rwrtlhsiva plaapgmiaa glfafvrgwn
      241 dfifaltlad kekqtlppgl vstyigefqt awpqlmaasl vvsvpvivaf mflqrylvgg
      301 mtagsvks
//
LOCUS       WP_457656983             242 aa            linear   BCT 27-JAN-2026
DEFINITION  type 1 glutamine amidotransferase [Streptomyces griseus].
ACCESSION   WP_457656983
VERSION     WP_457656983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Noldeke,E.R., Muckenfuss,L.M., Niemann,V., Muller,A., Stork,E.,
            Zocher,G., Schneider,T. and Stehle,T.
  TITLE     Structural basis of cell wall peptidoglycan amidation by the
            GatD/MurT complex of Staphylococcus aureus
  JOURNAL   Sci Rep 8 (1), 12953 (2018)
   PUBMED   30154570
  REMARK    Erratum:[Sci Rep. 2018 Dec 21;8(1):18073. doi:
            10.1038/s41598-018-37082-9. PMID: 30573753]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Morlot,C., Straume,D., Peters,K., Hegnar,O.A., Simon,N.,
            Villard,A.M., Contreras-Martel,C., Leisico,F., Breukink,E.,
            Gravier-Pelletier,C., Le Corre,L., Vollmer,W., Pietrancosta,N.,
            Havarstein,L.S. and Zapun,A.
  TITLE     Structure of the essential peptidoglycan amidotransferase MurT/GatD
            complex from Streptococcus pneumoniae
  JOURNAL   Nat Commun 9 (1), 3180 (2018)
   PUBMED   30093673
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..242
                     /product="type 1 glutamine amidotransferase"
                     /GO_function="GO:0004359 - glutaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26013
     Region          6..236
                     /region_name="COG3442"
                     /note="Glutamine amidotransferase related to the GATase
                     domain of CobQ [General function prediction only]"
                     /db_xref="CDD:442666"
ORIGIN      
        1 msnnglrlvw vypdllstyg dqgnalvver rarqrgldvq rvdvrsdqpv ptsgdiylig
       61 ggedrpqrla aerlrrdggl sraasngaii fsvcagyqil ghefvndlge reqglglldv
      121 vstrgegarc vgdvladidp qlalpqltgf enhqgvthlg ptarpfarvq lgrgngtgdg
      181 tegayndtvf gtymhgpvma rnpqiadlll klaldvnalp ptddrwyeal raeritsatq
      241 pa
//
LOCUS       WP_457656989             206 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656989
VERSION     WP_457656989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22188
     Region          6..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marvsqehld arrrqilgga arcfarngfh gtsmqdvlke aglsagavyr yfpgkediia
       61 aiteetfavi rgafeeaart appptpdall gkvlggvlag qvhglerrif aalvvqlwse
      121 tlrderlaal ldegyatmrv awaklvdayr sagtlesdvp adhvartmia taqgfivqea
      181 lfgdvrpevl englrglmsm npqkis
//
LOCUS       WP_457656990             329 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457656990
VERSION     WP_457656990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 1000903
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32857
     Region          <168..307
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
ORIGIN      
        1 mptapnrrav avvlliplmv tlalwafawp aariaprdlp vgvagaapaa qqleqrfqqr
       61 dgafevhrfd degaaraaie drvvygavva tpqgphllta saaspvvsql lreavttsvp
      121 egtrvqvtdv vaappgdprg salgasvlpl alagmaagav vtlmglrgvr aaltlvgsaa
      181 lvglaatava hswlgvvtgd wwteagvlal tvlaigsava glaalfgprg igigallmvl
      241 lgnsfsgvts apqllpepvg aigqwlppgv ggsllrsvaf fdgsaaggav ltlslwslfg
      301 laavllarrt pkpaaptptg parepaltg
//
LOCUS       WP_457656991             143 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656991
VERSION     WP_457656991.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..143
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15728
     Region          8..133
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 madhqeatvt lpsdpvsvss arryvartla ewglpddtef adtirlivse lttnavqhtf
       61 gqsptftvdl rlerdeelyi gvtdshprwp qrlpaavrqd ngrgmviirt lakerggrlq
      121 vtptaeggkt vwialpwvvp vqg
//
LOCUS       WP_457656995             289 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457656995
VERSION     WP_457656995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..289
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=31606
     Region          9..191
                     /region_name="SGNH_hydrolase_like_1"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01832"
                     /db_xref="CDD:238870"
     Site            order(16,172,175)
                     /site_type="active"
                     /db_xref="CDD:238870"
     Site            order(16,172,175)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238870"
     Site            order(16,57,86)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238870"
ORIGIN      
        1 melnasytsl vavgdsfteg msdllsdgsy rgwadvlasr lasrspgfry anlavrgkli
       61 gqivdeqvea avalradvvt lvgglndtlr pkcdmglvkg rleeaverla psckrlvlmr
      121 sparngpvle rfrprmeelf tliddlaarh gatvvdlysa pslsdprmwd vdrlhltaeg
      181 hrrvaeavwq tlglpaeqdw wtpvpatapp rwasrrtedi rfarrhlapw igrrltgrss
      241 gdgrsgahfd aatgrafwit ptnaetpgpv tewlraaspd atlstpead
//
LOCUS       WP_457656998             310 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457656998
VERSION     WP_457656998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33441
     Region          4..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtsidvhelt keygttravd rlsfrvrpgr vtgflgpnga gksttmrlvl gldrptrgsa
       61 tiggrpyaql peplrtvgal ldaqaahgsr tarshlsala vsngipmsrv asvleetglg
      121 dvstrriksf slgmrqrlgi aaallgdpqv vmldepsngl dpegiiwire lmkrlaregr
      181 tvlvsshlmn etasfadhlv vlgrgrllad mpmkefldsr srprvrlrtt epdrlrsalt
      241 srgltgirae ddrwtidgvt aeeigaiaad egipllelgd eratleqayl dltagdtpfa
      301 astirdrtea
//
LOCUS       WP_457656999             385 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457656999
VERSION     WP_457656999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     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=40046
     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 lhalrgagap tltdltritg lsrptvegvv eglfeaglvv
       61 eavpdesear rqgrparrfr fraeaghllg veigphrvsa lisgldgriv gagsravset
      121 acaddrldqv raviadvlrr tgvarsslra vgvgspgive adgtvrlgta lpdwtglalg
      181 erlrrsfrcp vlvendanaa avaehwkgaa tesddvvfvl aglspgagsl iggrlhrgfg
      241 gaageigalh llgrevtpeh llsttdtpld pldepavaav fakaregdag aqaaverflq
      301 rlvhdvaalv laldpelvvv ggwaagldgv leplrrelar yclrpprvtl sllgeaavat
      361 galrlaldhv eeqlfavega vtarr
//
LOCUS       WP_457657002             404 aa            linear   BCT 27-JAN-2026
DEFINITION  trans-sulfuration enzyme family protein [Streptomyces griseus].
ACCESSION   WP_457657002
VERSION     WP_457657002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..404
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42408
     Region          18..384
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mdnevsmtpp aptpsralat eavhagrddl aslgvhappi dlsttypsyd sraeamridd
       61 fattgarpdg ppvyarldnp ttgrfemala rlegaesava fasgmaalta vllarasqgl
      121 rhvvavrply gcsdhllgag llgtevtwtd pagiadairp dtglvmietp anptlaeidi
      181 ravahacgsv pllvdntfat pvlqrpvehg arivlhsatk ylgghgdvmg gvvacdeefa
      241 atlrqvrfat ggvlhplagy lllrglstlp vrvraastsa aelvrrltad priarvhypr
      301 iggamvsfev ygdphrvisg vrlitpavsl gsvdsliqhp asishrivde gdrrasgvgd
      361 rllrmsvgle dvedlwadlc qalsdgpvpp arkaeqplrs sagr
//
LOCUS       WP_457657004             148 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657004
VERSION     WP_457657004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..148
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16262
     Region          7..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtdyspdatd wrildvlqrd gratfaelar avamspsavt ervrrleelg visgyaavvd
       61 aewlglpila lvrlrypngn ykpfhdllet tpeiieahhv tgddcfvlkv tarsmrhlee
      121 ttgrigslgs vttsvvyssp lprraigr
//
LOCUS       WP_457657006             389 aa            linear   BCT 27-JAN-2026
DEFINITION  exonuclease SbcCD subunit D [Streptomyces griseus].
ACCESSION   WP_457657006
VERSION     WP_457657006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=42119
     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 leaqaayldh lvatvrerev dvvlvagdvy dravppltav
       61 elfdralhrl aeagvptvmi sgnhdsarrl gvgaglldra gihlrtdpeg catpvvlada
      121 hgdvafyglp ylepalvkdv lraakaghea vlaaamdrvr adlatrpagt rsvvlahafv
      181 aggepsdser ditvggvaav pagvfdgvdy aalghlhgsq rvtdrvrysg splaysfsea
      241 dhrktmwlid ldadgdiaae eridcpverp larlrgrlgt lledpaldrh ehawveatlt
      301 dpvrpaepma rlarrfphtl slvfdperpp ddpgasyaqr lkgrddhqia edfvahvrgg
      361 sgpsdlertv lraafddvrv detvrevsr
//
LOCUS       WP_457657007             176 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma carbonic anhydrase family protein [Streptomyces griseus].
ACCESSION   WP_457657007
VERSION     WP_457657007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..176
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17717
     Region          11..173
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 maeqalitgm ggkepdidvd afvaptsvvi gevtlapgss vwyqavlrad cgpitlgpds
       61 niqdncsvht dpgfpltvga rvsvghnavl hgcvieddvl vgmgatvlng ahigagslva
      121 aqalvpqgmr vppgslvagv pakvkrplta eelegirfsa agyvelakah reahgg
//
LOCUS       WP_457657011             407 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657011
VERSION     WP_457657011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43012
     Region          58..312
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          329..404
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mtiaalesls fglgrmaeaa araghrlcll tgdravyrhe lavlppdald vvdvdtwdqd
       61 avrralaavp dlaglinttd twslpaaela aglglpgpdp eavrllrdkr rvretlhahg
      121 lsrstavavp pgpegagevl ravglpavlk dsagtssrhv wivhdeealh ralaeagqqs
      181 ltgalfaeaf lagplysaet lswdgstrll gvlsrqtsrt avvreeaaaf pvalpeeera
      241 gieewvgrvl aaaghergfa hvefiltaeg pelveinrri ggalvgevlc rtlrtnvyta
      301 mtdealgrrp vlldapldtg gpaygfvlvy aerpgvlkgw hgldelgafp gavewfpvre
      361 pgesvvhigd qrgctgmvla eaptaelaqh rawsaavrvr pvvaaap
//
LOCUS       WP_457657020             381 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657020
VERSION     WP_457657020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  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 381)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..381
                     /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=39952
     Region          151..381
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpaptprepg pvvaapppgv eslflasarr lagpargvav lvisvfglla vptgslplgy
       61 glfalilags avdfwsgltg rapvlspafa avrvlavcat qewtggppnl walnllttta
      121 itlqwewspa vsvpvtagll avdlavvgge glgtllprll fecllarlgf vllrrsgqrl
      181 delrarrsal arteavslar rrqereylal lhdtaastfl mvaaredarp arvaeyarrd
      241 lavltgtagg atahdspvnl taslrtalgr srlrldvrae pdapvpasva lafvravrea
      301 lvnverhagv gtaalslyrq ggrltvlvcd egvgfdpaev ppsrrgirss vverlaavgg
      361 eatvrsrpge gtrvrmvwpr a
//
LOCUS       WP_457657022             314 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457657022
VERSION     WP_457657022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..314
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31981
     Region          44..105
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          111..172
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mptetgappt gpatvrrmvv alaavcaala vslglaqgas aaptwpalgn gttganvtta
       61 qyllrghgyd isvdsdfgpg tenavlafqe skgyaadgvi gaetwpglvv tvregesgda
      121 vsaaqtalnk hgyglgvdgr fgpatasavk dfqskqglda dgvigpqtwq hlvgtgggdd
      181 dggcsvpsdp dpevlkavyq kavelgvddr vllagfeagv vesnmnnlpc gdrdslgvfq
      241 qrpsqgwgtp eqimdvayas nsfftraida aaahpdytag qvaqsvqvsa ypdrydavea
      301 tardlieqak glvg
//
LOCUS       WP_457657028             347 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457657028
VERSION     WP_457657028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..347
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35976
     Region          54..332
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mdaslsidvh ahyfgadmaq lpegaegprl vvdtpaagrl mrgaspfrev rselwdvdrr
       61 ldemdragvt hqvispvpva mehaatapdg aryardvnds vaaacarsgg rllglgclps
      121 pgsraaaael ercralglyg veigtsvagl dldapslrsf wreceatdsc vfvhpvaggs
      181 gavrrrggiy dlgigmttdt alaaaalvfg gvlaahprlr ialahgggtf aaafprleva
      241 aalatgpdap ghadlvrlly vdslvfddgl ypllarrfgp rrlllgsdap ffpdqmrrsv
      301 lavrsavtdg llpagdgpgv laenalsflg latapgrpsp epesftp
//
LOCUS       WP_457657029             272 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657029
VERSION     WP_457657029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..272
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29228
     Region          23..255
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mkisdaspvk elkqahdspa silskafell asfgpdrrvl tltqmsrisg lpkstvhrli
       61 grlvplgfle qhgagfklgi rlrtlaasmp veslresalp hlaalqswsr shvhlaalrg
      121 gqvvfverfv psgsrllsgq pgdhlpahat algkallafa pspvvdevlg gqlealtprt
      181 vtdpealsge lrrvrderva yareecrrgv tciatpvvik gravgavsis vssdnrfgrq
      241 hvdairvaad riskdnqqtl smghedwfpg qd
//
LOCUS       WP_457657032             454 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657032
VERSION     WP_457657032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47260
     Region          17..405
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30..31,34..35,38,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msqqtaesap pdartlrrvv gagflgttve yydffiygta aalvfpevff ptlgdsasva
       61 asfatfavaf varpvgglvf gqigdrvgrk ttlvatllim gvstvligll psgdsigvla
      121 pallialrfc qglavggews saalfvgeya ppekrglyal sptlgtsagi llatlaflgt
      181 gwsmssasfl awgwripfll ssvlvivgmw vrlriadtpv flaaaakaee ssrrkaplae
      241 llrhqwretl laagsvmmwi sffyigsvym tnygtgtlgf srntmlsvnm aaiaaniigs
      301 vagawlsdrl grrtvmigas lfavpwafal flladtgnlf llalgisval ffvgtasgtt
      361 taflpeifrt syrstatgvs ynlgslvaga ippivaapll aahgslalga mlallaavsa
      421 lcafrlqetr grslheheep vapaspraga saag
//
LOCUS       WP_457657033             443 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            griseus].
ACCESSION   WP_457657033
VERSION     WP_457657033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..443
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50078
     Region          15..411
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 msadhiiddr ekslfqvnre vftsqevfer errrifdtsw lfvgheteip ekndfrtrdv
       61 ggrsvifnrd rrgdvrvlln tclhrgasic rhksgnakif tcfyhgwayr nsgelvnvpa
      121 dedyavspse vygalhspri dsyrgfwfin fdreaedlrs wlgtsaylfd lvcdqspdgv
      181 eviagthnyt lqanwkllve nsidgyhaks vhhtyfemml elgqtppmlg adatngvppa
      241 glgtefgngh stlmypgngl planehvqrs ladlrgkave rfgesyasav fnlarnsvff
      301 psfvlidlnf gmiirtitpl gpartevasw qlvprgidqe slqyridnal tfwgpaglat
      361 pddvealeqa qrgfsalrev twsdiskgmg kkrpaandel qmrawwrqwh kvmnevvlps
      421 eveefvpfeq qdrprsvdal pka
//
LOCUS       WP_457657034             182 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Streptomyces
            griseus].
ACCESSION   WP_457657034
VERSION     WP_457657034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..182
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=20658
     Region          28..173
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mteitggavp prtrttpdsp grgrtvsrha ieeflyaeaa llddwrleew velftldcvy
       61 evpatdapda dpglswslih drrtmleqri irlkkpeaha efphsqtsri ignvivterf
      121 ddavqvranf ivsrmkagkf dqyvgryhye lvpdgtsfli rrkkavlahd rldpqgkisf
      181 vl
//
LOCUS       WP_457657035             117 aa            linear   BCT 27-JAN-2026
DEFINITION  non-heme iron oxygenase ferredoxin subunit [Streptomyces griseus].
ACCESSION   WP_457657035
VERSION     WP_457657035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Ashikawa,Y., Fujimoto,Z., Noguchi,H., Habe,H., Omori,T., Yamane,H.
            and Nojiri,H.
  TITLE     Electron transfer complex formation between oxygenase and
            ferredoxin components in Rieske nonheme iron oxygenase system
  JOURNAL   Structure 14 (12), 1779-1789 (2006)
   PUBMED   17161368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..117
                     /product="non-heme iron oxygenase ferredoxin subunit"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=12693
     Region          7..107
                     /region_name="Rieske_RO_ferredoxin"
                     /note="Rieske non-heme iron oxygenase (RO) family, Rieske
                     ferredoxin component; composed of the Rieske ferredoxin
                     component of some three-component RO systems including
                     biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase
                     (CARDO). The RO family comprise a...; cd03528"
                     /db_xref="CDD:239604"
     Site            order(50,52,70,73)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239604"
ORIGIN      
        1 msitrnfvca vddledgesm tvepealagi eepvavyrvd geffatsdtc thekwslgee
       61 gdlegheilc tlhnarfdvr sgeplcfpav lrlksyatsv eggkvyitag erggher
//
LOCUS       WP_457657037             406 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657037
VERSION     WP_457657037.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..406
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42128
     Region          8..404
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 msahavarsv tvlggglagl tvarelragg ydgavrivdp egvpydrppl skaylegsvt
       61 veklhlvpet wyteygvdli aaqavrldtg tgtvrladgr dmatdavvla tggtprrlpv
      121 pggdlpgvht lrtradadrl rdvlrpgtri aivgagliga evastavgrg aevtlidtvd
      181 pplaaavgpe marllhamhp aagirvvtga laaitprqgt hvlrvggeev hadvvlsavg
      241 iragtelarg aglatdngvl vdarqrtgnp svyaagdcar rvlphgvpga rtehweaalh
      301 qgqsvaaavl grpapapqvp wfwserhgsr lecvgamnae grtvvrqqdg qppvffrlgp
      361 dstllgcaal dsprlvraar riirsrrvta aealadptad lrgltr
//
LOCUS       WP_457657038             281 aa            linear   BCT 27-JAN-2026
DEFINITION  2-keto-4-pentenoate hydratase [Streptomyces griseus].
ACCESSION   WP_457657038
VERSION     WP_457657038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10008165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="2-keto-4-pentenoate hydratase"
                     /EC_number="4.2.1.80"
                     /GO_function="GO:0008684 - 2-oxopent-4-enoate hydratase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030145 - manganese ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28272
     Region          35..274
                     /region_name="MhpD"
                     /note="2-keto-4-pentenoate hydratase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3971"
                     /db_xref="CDD:443171"
ORIGIN      
        1 mperpapsgp saesapspav vaaadalaea aaratvcppv rtllpaddlt tayavqqlgv
       61 rraltrgrrl tgrkigltsp avqrqlgvdq pdfgalfadm avpegtavpa glllqpkvea
      121 evalvidrdl sqsdctvadv maatgfclaa leivdsrigg wdisivdtva dnassglyvl
      181 gsrpvplngl dlravtmtlt rngepasagt gadclgspln aaawlastla aagdplragd
      241 vvltgalgpm vpaapgdvfe aqisalgsvr aefamttega r
//
LOCUS       WP_457657042             340 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457657042
VERSION     WP_457657042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 340)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10053807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..340
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36760
     Region          257..329
                     /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(257,260,263..264,267..268,271,300,320..321,323..325,
                     327..329)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(260..262,275..276,285..288,290..291,294..295,
                     297..298,304..306,311..313)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(275,277,320)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mlrihftped ltrvkvapgp dllweisnsv qtlqrtdgar vfgdwrrwvr prlpesrrll
       61 spllppygys pdfltptsge rttlraavdt llgtprprlr aeltrlagst plpgwaaala
      121 egdtdalarl gdalhayqaq allphwrqvr adleadralr mrhlmdggte alltglgpgv
      181 rwqppvleva ypveqdlrld grglvlqasf fcwptpttla dgelppvlvh pihhtadwag
      241 gpgatgpate rgplgrllgq tradllratr tgcstveaar llqvthpavs qhmnvlraag
      301 ltttvrtagr afhvataegr allaaedrra grgpggeprp
//
LOCUS       WP_457657043             237 aa            linear   BCT 27-JAN-2026
DEFINITION  C39 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657043
VERSION     WP_457657043.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Kanonenberg,K., Schwarz,C.K. and Schmitt,L.
  TITLE     Type I secretion systems - a story of appendices
  JOURNAL   Res Microbiol 164 (6), 596-604 (2013)
   PUBMED   23541474
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Lecher,J., Stoldt,M., Schwarz,C.K., Smits,S.H., Schmitt,L. and
            Willbold,D.
  TITLE     1H, 15N and 13C resonance assignment of the N-terminal C39
            peptidase-like domain of the ABC transporter Haemolysin B (HlyB)
  JOURNAL   Biomol NMR Assign 5 (2), 199-201 (2011)
   PUBMED   21347827
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Schwarz,C.K., Tschapek,B., Jumpertz,T., Jenewein,S., Lecher,J.,
            Willbold,D., Panjikar,S., Holland,I.B., Smits,S.H. and Schmitt,L.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            an oligomeric species of a refolded C39 peptidase-like domain of
            the Escherichia coli ABC transporter haemolysin B
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 5), 630-633
            (2011)
   PUBMED   21543878
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10609171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..237
                     /product="C39 family peptidase"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25217
     Region          73..210
                     /region_name="Peptidase_C39_2"
                     /note="Peptidase_C39 like family; pfam13529"
                     /db_xref="CDD:379241"
ORIGIN      
        1 mrarlvtgtv atlflgalll pgtaqaspap avpvvdvrth hstagtalvs gydepgarlr
       61 vaagrtsdar wleidyqvqe tgywcgpaat rialsartaa psqgelaaql gtteagtdhi
      121 gqvtgvlnar lgggwyetke mpddpptqaq rdllwhdivf didrnyplva nivappgnqp
      181 pgyppdqtiy hyftvfgyda vdrtvliadp asfggnqiyw isfdqlaslv ppkgysa
//
LOCUS       WP_457657045             156 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657045
VERSION     WP_457657045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..156
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17803
     Region          6..151
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mtdtqrrgrr immtpeerda ylgeqrtcrv atlgsngaph igalwfvwdg gslwlysitr
       61 srrwsqlrkd triavvvddg egyeelrgve ltgraefige aprtgehcpe lveperlfpv
      121 kyfgvtemph dgrhawlrlt petitswdfr klaglt
//
LOCUS       WP_457657046             385 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces griseus].
ACCESSION   WP_457657046
VERSION     WP_457657046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..385
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39411
     Region          37..314
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 msapceprat apasalpppv psapparrpa ldwrirfaal sliwgfsfll ikvgtegyap
       61 fqvtfgrlla gtavlvaama mrrerlprsa rtwghltvaa fllnalpfsl fsyaeltips
      121 tlagicnats plwgmalsvv alsedrptrr rvaglglgfl gvltvlgawq gfsgldlpgt
      181 gmallasfcy pvgwiyvrrt lagtgsstla ltgsqlflgt aqlavvtplf tsaptsfpll
      241 ptlsvlalga lgtglavllq yglvqevgpt taqmvtyfip viataagval lgerlswntp
      301 vgalivlvga altqsrarpa ttaaakepag hpaaappeaa atavpdeptg hpaaaapgae
      361 ypatttvpre pagppgadap rlsrs
//
LOCUS       WP_457657048             343 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657048
VERSION     WP_457657048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..343
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36331
     Region          2..301
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlgatgqigr aavralaadg wevtaasrgg grgegwdagv ravaldrdee galakalgdg
       61 cdvlvdmvaf dgaharqltg lagrigsavv issgavyede rgrsfdtqae pdgfprypvp
      121 lpesqatvap gdatygtrkv qlerelpaag ealpvtllra gavhgpycrt prelyfvkrl
      181 ldgrrrrvla yggesrfhpv hvsnaaelir laarkpgsrv lnaadpeapt vaeiasaida
      241 vlgretetvl idgpapegqv getpwsgahp vvydmtaage qlgyrpvtgy aealpetvew
      301 lagelagrdw reafpkmlkn ygeglfdyaa edawlaaydr grr
//
LOCUS       WP_457657051             367 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457657051
VERSION     WP_457657051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 367)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..367
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38251
     Region          8..367
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtddlraaga ptledvaraa gvsratvsrv ingvrnvdpv iqeavrhavs vtgytpnraa
       61 rslvtrrada valvvsgagv epaaaeedsd agasgrdgtg dagsftaqvf adpffgrvvt
      121 gvvnylrprg mhpvlmfaet srareevvay lrqgsadgal vvsthaedpl paliadagla
      181 avlyarparp vpvsyvdlah qdgarlaaeh llgrgcrria tisgpldvpa gqarltgfrd
      241 tmarhghpyv ptaegqftqe sgeaamerll aehpdldgvf aandlmalga chvlrehgrs
      301 vpgdvavvgf ddssaalacr pplttvrqpv egmaaemtrl lldrlarpdg pvtsvifepe
      361 lvvrgsa
//
LOCUS       WP_457657053             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657053
VERSION     WP_457657053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21986
     Region          8..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matkqrgrpr sfdredalrk atltfweqgy eatsiadltr vmgiaapsly aafgdkrtlf
       61 aevvetyadl fggfgdrama eeptarrgfa rmlreaaaey taagrphgcm vlsaaencss
      121 devvaalrgr rernmtefrr riqadidagv lpadteaaal arctaaviqg msqqardgas
      181 raeletlaev amrvwpeesg evg
//
LOCUS       WP_457657057             483 aa            linear   BCT 27-JAN-2026
DEFINITION  lipase maturation factor family protein [Streptomyces griseus].
ACCESSION   WP_457657057
VERSION     WP_457657057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Doolittle,M.H. and Peterfy,M.
  TITLE     Mechanisms of lipase maturation
  JOURNAL   Clin Lipidol 5 (1), 71-85 (2010)
   PUBMED   20543905
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10535984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..483
                     /product="lipase maturation factor family protein"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=54618
     Region          121..463
                     /region_name="LMF1"
                     /note="Lipase maturation factor; pfam06762"
                     /db_xref="CDD:462004"
ORIGIN      
        1 mewftadgyw lsrlifqral avvylvafls aalqfralig ergmlpvpel lrrtpwraap
       61 gifrlhysdr ffaavawsgc avsvaliagl dgllplwggm llwalpwvly lsivqvgqvw
      121 ygfgweslll etgflavflg sgdtaapvlv lwllrwllfr vefgaglikm rgdacwrelt
      181 cldfhhetqp mpgplswffh hlprpvhrie vaanhvtqll vpfllftpqp vasaaaglmv
      241 ltqlwlvlsg nfawlnwlti alalsaidwt plagpppaqv applwyevvv saatalvlvl
      301 syrparnlls rrqamnrsyd plhlvntyga fgsisrmrle vvvegsadpv aregaewrey
      361 gfrgkpgdpr rmprlfapyh lrldwmmwfa alspayarsw fgpfaerlld gdrdtlrllg
      421 hnpfpdgppr rvrarvyryr ftglrelrat gcwwhrtyvr eflrpvsrpl pperegggtg
      481 rgp
//
LOCUS       WP_457657059             289 aa            linear   BCT 27-JAN-2026
DEFINITION  YndJ family protein [Streptomyces griseus].
ACCESSION   WP_457657059
VERSION     WP_457657059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10624444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..289
                     /product="YndJ family protein"
                     /calculated_mol_wt=30371
     Region          7..255
                     /region_name="YndJ"
                     /note="YndJ-like protein; pfam14158"
                     /db_xref="CDD:404946"
ORIGIN      
        1 msalvnaivm lgmlvivptg lrlsgrqele rirrlwplfa vpgalalwlp rsttatalac
       61 cyalgtvlla lhaprravra rdldpagial ltalvtpava atalvaersg helfgfdlgi
      121 laltvphfhy agfaaaliag lvcrvsdgpa grfaalsvpv gtllvlagyf igdwaelvga
      181 vvltagmwtv glltwrmgra dgrdrttrll lltsaavlva tmllalswal geatglphpt
      241 lswmaathgl gnalgfalcs llawrrirte rtertdrtag ltrtggrta
//
LOCUS       WP_457657063             153 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces griseus].
ACCESSION   WP_457657063
VERSION     WP_457657063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..153
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15995
     Region          17..152
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mteqqphqfe rgtdgpkviv agldgsdssm raaayaagla rrqsamlalv yvqpvltaga
       61 algapvgdtt gevaedlaae iraaterfsd awdmrwefht frgdpynglv taadelkada
      121 vvvgasesag hrfigsvavr lvkagrwpvt vvp
//
LOCUS       WP_457657068             281 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657068
VERSION     WP_457657068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30097
     Region          58..159
                     /region_name="Acetyltransf_5"
                     /note="Acetyltransferase (GNAT) domain; pfam13444"
                     /db_xref="CDD:463880"
ORIGIN      
        1 mtvlpvaplp asapaasvpa patiparsta pgpaaapepp yrvslatcqe diraaqrlrh
       61 lvfagelgar ldgpepglds dafdaycdhl lvretatgev vatyrllppd raraagrlya
      121 esefdltrlt pirddlvevg rscvhpahrd gavialvwag larymertgh twiagccslp
      181 ladggaqaar swntvraghl apqeywvtph rlwdssahgp eagsradlpp llrgylrlga
      241 qicgapaydp dfnvadlyvl lslrrtdpry lrhflslapl a
//
LOCUS       WP_457657069             299 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657069
VERSION     WP_457657069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..299
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31321
     Region          49..>201
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mstwlpvapc tpdgcarhag avraplpaal llltgctlvl lgvvcvplvr llgatrrerl
       61 vrrwaravpr afgvrvtvrr hapepaagge lvvanhiswl dipliasvlp grmlakreir
      121 hwpllgplaa lggtlfidrd rlralpaavr tvtaalrsgs rvvvfpegst wcgrgggafr
      181 pavfqaaida gatvrpvria yraipptata adargqaaga vafvgddpla aslwrvvraa
      241 gltarvdvla pvpvpgedgr ralarraraa vlgpedplrp rqtavasdra nrpaasvhh
//
LOCUS       WP_457657072             820 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Streptomyces griseus].
ACCESSION   WP_457657072
VERSION     WP_457657072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>820
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          <8..820
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 magksrslia eifseqvaar adhpavlceg rrltyarldq esdliaarla ehgvgdgdiv
       61 gialrrselc avawlavakv ngvclwldpd ypadrlafmi edaapsvlvm apdadgttre
      121 lavglrtvtv epasgdagpl apdtarslpp rrtapaqsaa yviytsgttg rpkgtiltst
      181 glrsllatav qgfgagrdsr vlqftsmsfd vaflemsmal llggtlvvvp gerrvaetaf
      241 lellreqrit haalppafle llpeesplpd gltimtgadk vplalagrwa rrarvvacyg
      301 ltevtvnstl wdydaswdga vaplgtedpg tvahllddsl rpvpagqpge lylggdglar
      361 gylhrpglta erfvadpyga pgarmyrtgd ravrhgsgvl eflgrvdgql kirghriept
      421 dvesvllrhp svaqavvtsh ddtaggaela ayvvpaegae idarelrrhv artlpsymvp
      481 sllvpvsgla tlpsgkldrr svlrkataql padageadev alrqllsavl gcdeeefddg
      541 fdfvglgghs ltamrlatec rrlferepam rdvfaargvr dlldrltssg pdrprpgqlg
      601 nepfllsyeq erlwlleals gggthyhvpw awqvhgdldp ealrgaledl aachdilrtr
      661 fpavhgtprq eilppqeysp dyavlpvdgq dltaaiteaa resfdletrp pwrvrvltap
      721 dtpptvlfcl hhmvvddwsv drlatqlaqa yaarldpgle pparpalqfa dfsawqrrvh
      781 dapaggpesg gvgfwrgflr gvpvesgvpl drvrpdvpvv
//
LOCUS       WP_457657073             591 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657073
VERSION     WP_457657073.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 591)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 591)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 591)
  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 591)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..591
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60887
     Region          24..583
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 msvaeelpta gmkktwqvvr ecgrgqagaa wtavvclals sasvlvvpll vgrivdmvtg
       61 sgdgrpfgpa avgalavtav gavlaavgtg rtalvcenvl grvreralgv vlglplptve
      121 rvgrgsvlsr tvgdvgvasd vargalpafl salltllvtg fgllaldwrl avagalplpv
      181 wavatriylr rsgpqyaher taearlsqfl ltgisgartl ralrleethr srieersqaw
      241 staalrtcvt rirfslhlng aellgllavl ltasalvrtg slslgaasaa vlllmrvfep
      301 vgtllyllde vqsagaalar lagivgspag gtedaarsgr ampsdgeltv cglefdygdg
      361 rpavrdvsfr vqpgervaiv gpsgagkstv vgivtgmhtp crgsvtlggv pvqrldprat
      421 glvtqeshvf agsvrdnlsi arpdadeaaq taalaqvgav gwvlelpegl dtvvgrsgrt
      481 lssvqrqqla larlvladpp lavldeptae syggdraavn aavdaalkgr tgivvahrls
      541 daraadrvlv ldegrvvafg thdallrdgg lyaelwstwq asrspagrgg p
//
LOCUS       WP_457657084             249 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657084
VERSION     WP_457657084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26219
     Region          2..243
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(8,10..13,33,51..53,75..78,98,125..127,140,144,173,
                     176..178)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(99,127,140,144)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(127..129,134,140,171..172,179,196,199,242)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mktvlitgas sgygretalh fhaqgwnvia tmrtprtgil pesdrlrvvq ldvtdpesit
       61 aafeaagpvd vlvnnagips isvfegmple rvrevfetnt fgvmattqav lpqfrergsg
      121 vvinvtssvv lghmplsavy kaskmavegf taslalelap fgvqartvqp gaclttgfaa
      181 natngaslde lvpapyaawa keamggftgq dlftkesdva etvwravhdt tgrlrfpagp
      241 davrlaeak
//
LOCUS       WP_457657086             331 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457657086
VERSION     WP_457657086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35326
     Region          84..291
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mnparpsldp elrellagmp lmsglsrevl gqlrrlpstp vepllahrqv vrrettvrae
       61 dgaavplsvf spastdratg rpcvywmhgg gmvmgdrfsq idiplewlda fgavvvsvdy
      121 rlapeatgtt lvddcyrglm wiaehagelg idparivvag asaggglaag vsllardlgt
      181 paiagqmlic pmldhrntsv ssrqysggpg vwtremnefg wravlgdltg devspyispa
      241 saedlaglpt tyidtgsaev frdedtdyag riwaaggqae lhvwaggfhg fdalypqadl
      301 satarrtrtd wlarllnrss saqpartdlv p
//
LOCUS       WP_457657088             291 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657088
VERSION     WP_457657088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001217 - DNA-binding transcription
                     repressor activity [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30978
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..286
                     /region_name="PBP2_LTTR_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08436"
                     /db_xref="CDD:176127"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176127"
ORIGIN      
        1 melqqmryvv avaetnnftr aaqrclvvqs alshqiarle kelgarlfer tsrrvrltpa
       61 gaaflpaarq cldaaeraaa evaaavgevr grltvglipt vaavdipavl kdfhqrhpka
      121 rvnlsvgasd elveqvrqge ievaflgvpv tarprgvmar elarerliav vspahplaga
      181 ysvdlrrlsc evfvdlpakt agraqsdlaf aaagltreva fevtnadyla rlvgaglgva
      241 llppsyvasl agvttievtd aparveyvvw grdsrtpaat aflellgvee e
//
LOCUS       WP_457657093             525 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces griseus].
ACCESSION   WP_457657093
VERSION     WP_457657093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..525
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55870
     Region          6..519
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlctrltnar iltmdphrpv ahdlgiwrgr vvgvdeavts lparevvdlg gatvlpgfid
       61 shvhlawagl kagtpsvapc eriedilavv daaarrpaps gawvdvagyd qralgrhlta
      121 aeldrvshgr kvflmhdsgh acvvntavld llpdgtphed gflaesamtt arrlrlpysq
      181 deladaiela aracldegit acaeagiggg llghspvelg ayqllrdrgr lplriqlmas
      241 gdtlrpraah addgftrald lglrtgfgdd wlsvgalkiy tdggmmarta altspyegta
      301 dnigrfqddp driaglivdg hlagwqlavh aigdraadla ldaleraqkl rprpdarhri
      361 ehaglirpdq lprfaelgvs avvqpnflrs fgddyatvmg egragwmyrg rgfldhgval
      421 vgssdrpvtd gsplraiqfm vertsasgrp igpdeavtvd ealraytvag ahagrwedaa
      481 galsagmrad lvvlgddphr vdpsrigdie ivrtyvdgrd graaa
//
LOCUS       WP_457657095             418 aa            linear   BCT 27-JAN-2026
DEFINITION  MraY family glycosyltransferase [Streptomyces griseus].
ACCESSION   WP_457657095
VERSION     WP_457657095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..418
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40595
     Region          50..273
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            96..97
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            200..203
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(252,266..269)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mnvlgiiasg vaalfitval aksarraalr phvpdepggr apragalrgi ggaaavlgvg
       61 tatggalwlg aadgsagsva gllagagava alglvhdlkp lgaalrlavq ttaavlvvcl
      121 aglspaagvl avlwivlvtn afalldhadg llttigvvta agllacalid gsaalallpa
      181 alaaglagfl lhnwhparlr lgasgaqftg falaasgali qaaapsgraa waalptlatv
      241 aladtalvli srrraarspl rdtddhiahr lrrvrvtvpg avillalwaa vpvvtgtlvh
      301 aellhpafll vppagsaaav fallripaya ppratstrat psrtavrrtt ahatgpaipp
      361 astgpaapgg gaapasgtaa papgkttata rtaeghptvp sppaptgrsa aqvaaerg
//
LOCUS       WP_457657097             244 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657097
VERSION     WP_457657097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  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..244
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..244
                     /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=25958
     Region          21..234
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mielllpadv scaatraesv pdgtlfpeee aliaksvakr rndfatarac arramaglgl
       61 ppvavlhghr grplwpegiv gslthcdgyr aaalaraknv lslgidaeph aplpsgvrel
      121 vtlpaereri gppvaevpde ddtgeihwdr vlfsakesvf ktwypvtgle ldfteadltf
      181 hrtdgpggdd garggvaaeg sfaarllltd palpttlhgl wriedgivat avlvrpdwrd
      241 sdav
//
LOCUS       WP_457657098             198 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces griseus].
ACCESSION   WP_457657098
VERSION     WP_457657098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..198
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20419
     Region          <49..186
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mtvrvmlisp amnaalrear fdgdapldrs greraraaag avpdaglalt gpsercrett
       61 aalglaartr tepalagwdl arwagrrlde vaaaepaqva awlgdataap hggeslhelv
      121 grtgrwldsl ggpdapgtsf lavaeaavvr aavvhglrlp teafwrldva pltltglsgr
      181 sgrwnvglgr pltappad
//
LOCUS       WP_457657102             321 aa            linear   BCT 27-JAN-2026
DEFINITION  pirin family protein [Streptomyces griseus].
ACCESSION   WP_457657102
VERSION     WP_457657102.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34648
     Region          31..287
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msnldrqatp svcggrgfvv aepvrellap rrvqlgeste vrrllpnlgr rmvgawafvd
       61 hygpddiade pgmqvpphph mglqtvswlh dgevlhrdsl gslqtvrpre lglmtsgrai
      121 shseespkdh arllhgaqlw valpdahrsv ephfqhhtdl pvvtapglaa tvilgeldgt
      181 aspgttytpi vgadvtltag aearlpldpd feyavlsmsg eaevdgvpvl pgsmlylgcg
      241 rtelplraas daglmllgge pfeeelvmfw nfiarsgeei vqarkdweeg srfgevqgyd
      301 garlpapelp ttplkprgrv r
//
LOCUS       WP_457657103             209 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657103
VERSION     WP_457657103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..209
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22610
     Region          3..190
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          54..142
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 manhqdetra aydgvvelya slfanrletq pfsramigtf aelvratgnl rtadvgcgpg
       61 hltamlhelg ldafgldlap gmvdharqah palrfqearm eslpiedaal ggvlahysmi
      121 htppgelpel laeqarvlap dglllvsffg tdeqepvrfd hkvapayswp adrlaellad
      181 tglvpfarll hdpasergfl dahllarrs
//
LOCUS       WP_457657107             157 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457657107
VERSION     WP_457657107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..157
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17310
     Region          5..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mewlevsten cpvqralevv gekwtllilr davngvrrfd sfhrhiglse avlsdrlrkl
       61 taagvlkava yrepgrrsrn eyhltrkgwd lwpvlltlgq wgethavgpe spgpvldvth
      121 tdcgapvrvt vqcsaehapl tskdvtvrlg sgarrls
//
LOCUS       WP_457657106             125 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457657106
VERSION     WP_457657106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Rosinski,J.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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..125
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13470
     Region          6..82
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdpfialadp vrrdllralv sgparvadla arypisrpav skhlrvltea glvtaedrgr
       61 erhyalarpg lapvrallde lagrrppipe safdaldlev rrtvhdrrag tdavpgtgrp
      121 qeesa
//
LOCUS       WP_457657110             361 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces griseus].
ACCESSION   WP_457657110
VERSION     WP_457657110.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..361
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38434
     Region          7..339
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(26,28,59,101,229,292,313,315..317)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(26,28,59,101,103,110,177,180,182,229,236,292,313,
                     315..316)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(28,103,177,180,182,316)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            182
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mttssslwqp fklgrvelph rlamapltrs ranadgtpgp laatyygqra slgliitegt
       61 qpsadgqgyp ntpgihtpeq iagwrevtda vhagggalfi qlmhvgrmsh pdntphhrrp
      121 vapsaisadq diftatgpkk tavprelsiq diqttiadfr haaasaiaag adgveihgan
      181 gyllhqflsp nanhrtdayg gsvenrsrlv vevaravaee igadrvgirl spsmplggid
      241 egdaedvraq yrhlagelap lnlaylhvhh vgddellrsl revwptallv vrygrtreqi
      301 addidaglad iaplgrfala npdiverlrt daplneidpa tlygggeagy tdyptlagth
      361 a
//
LOCUS       WP_457657111             200 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657111
VERSION     WP_457657111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21533
     Region          12..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpgasqsvgr rernkqlkld ritaaahelf aergidevtt qqiadkadig tgtlflyakt
       61 kgellllvqn slyaealerg radaenipdt ldavmaivrp vvecnrtqvd ngrvylremv
      121 fgdpaephhh ealtitgqte qavagvlcrd aqvsdadaat varvvsavmf lamaagvnva
      181 asvdeilrdi reqiavlltr
//
LOCUS       WP_457657113             341 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657113
VERSION     WP_457657113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..341
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35466
     Region          1..330
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(38..40,43,125,129,151..156,175..176,178,192,
                     213..214,235..236,278..280)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mkafvlekyg splrevempv pvpaphevlv rmvasginha dervrsgefk aifpfrlpkv
       61 mggelagevv eagsavrdia vgdqvygyvd laatgtlsef vavdasamtp aprsvslvea
      121 aglpvvalta wqaliemgkv kkgqtvlihg gtggvgsvai qlakhlgctv attvstania
      181 aarelgadia idyrhddlaq slagtpvdlv ldtqggatlq aslavlrrgg tvigitgppd
      241 pafarrvgvn pvvrlairal sartrrrart lgvtyrflfi tpdsaalrqv aglvddgvlr
      301 pvidrvlpfd qtpraldeal aggtrgkvlv ttdpkavtth g
//
LOCUS       WP_457657119             538 aa            linear   BCT 27-JAN-2026
DEFINITION  adenosine deaminase family protein [Streptomyces griseus].
ACCESSION   WP_457657119
VERSION     WP_457657119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Cristalli,G., Costanzi,S., Lambertucci,C., Lupidi,G., Vittori,S.,
            Volpini,R. and Camaioni,E.
  TITLE     Adenosine deaminase: functional implications and different classes
            of inhibitors
  JOURNAL   Med Res Rev 21 (2), 105-128 (2001)
   PUBMED   11223861
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004592
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..538
                     /product="adenosine deaminase family protein"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58614
     Region          83..476
                     /region_name="Add"
                     /note="Adenosine deaminase [Nucleotide transport and
                     metabolism]; COG1816"
                     /db_xref="CDD:441421"
ORIGIN      
        1 missirtahr pksllptglg llalvtllpa vpaaaapard sspraeaqap grlttpaerr
       61 tdarldalrd nparlkaffa alpkggdlhn hlsgavttey lihlagengl cidatdtavr
      121 ppcgpgtrpa adartdaafr qrivrawsmq dfpadqsghd hffdtfgkfg eatrdrgkml
      181 anvantvveq nqfyletlvt pasdsakkla esvgydadla afhrklvagg kldavvaeav
      241 readaadtqf retahcdtdr pdpgcrlpvr wisqvsrgss nervftqmav gmrlaerdpr
      301 fvavnlvqpe dgesalrnyr lqmrmlqylr tqypdarltl hageltpglv kpedltfhir
      361 eavlvagaer ighgvdlvhe ddwrrlartm arrdvavevp fssnkqilgv agddhpfnay
      421 rrygvpvvla tddpgvsrid isheyqyara tyglsytelk dlarasltya fldgdslwat
      481 gaqrsgyrpv rvcagsrpgi appapacary ladnakaate wrqeaafagf errqggar
//
LOCUS       WP_457657122             488 aa            linear   BCT 27-JAN-2026
DEFINITION  rhamnulokinase [Streptomyces griseus].
ACCESSION   WP_457657122
VERSION     WP_457657122.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..488
                     /product="rhamnulokinase"
                     /EC_number="2.7.1.5"
                     /GO_function="GO:0004370 - glycerol kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008993 - rhamnulokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0019301 - rhamnose catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51701
     Region          7..458
                     /region_name="ASKHA_NBD_FGGY_RhaB-like"
                     /note="nucleotide-binding domain (NBD) of rhamnulokinase
                     (RhaB) and similar proteins; cd07771"
                     /db_xref="CDD:466791"
ORIGIN      
        1 msaptrtlaa adlgassgrv mvgrvgpdtl dltevhrfpn rpvhlpeglr wdilglyrgv
       61 ldglraagpv dslgidswav dhglldarga lignpvhyrd rrtegvpeev watvppeely
      121 ratgiqyapf ntlyqlvaar htpqleatvr lllipdllty wltgeqgtel tnasttqlid
      181 prtgdwhhgl adrlgidlgl faplrrpgdp agatlplvqe ltglpgpvpv ttvgshdtas
      241 avaavpaarg erfaylctgt wslaglelga pvtteasrea nftnelgidg tvrflrnimg
      301 mwllqecmrt wgredvtsll aeaarapalr svvdaaapef lapgdmperi aaacratgqp
      361 vpatpgattr cildslalah rraihqaqrl adravdvvhi vgggarnall cqltadacgl
      421 pvvagpaeaa algnvlvqar ahglpgdlaa greliartqp ltryepsgdp avweaaarrt
      481 egtrrlha
//
LOCUS       WP_457657124             715 aa            linear   BCT 27-JAN-2026
DEFINITION  iron ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657124
VERSION     WP_457657124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 715)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Koster,W.
  TITLE     Cytoplasmic membrane iron permease systems in the bacterial cell
            envelope
  JOURNAL   Front Biosci 10, 462-477 (2005)
   PUBMED   15574383
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11484808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..715
                     /product="iron ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=71390
     Region          34..713
                     /region_name="PRK10577"
                     /note="Fe(3+)-hydroxamate ABC transporter permease FhuB"
                     /db_xref="CDD:236720"
     Site            order(468..470,592..593,595..597,599..600,602..607,
                     609..611,652,659)
                     /site_type="active"
                     /note="ABC-ATPase subunit interface [active]"
                     /db_xref="CDD:119348"
     Site            order(469,471,476,530,532..533,536..537,540..541,544,
                     547..548,550,562..563,566,642,694,697..698,701,704..705,
                     708)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:119348"
     Site            order(550,576,634,638,682,691)
                     /site_type="active"
                     /note="putative PBP binding regions [active]"
                     /db_xref="CDD:119348"
ORIGIN      
        1 mstrtttapp apvetvagaa gpagavapvt dgpparrgrm lllalaglla laalavthvs
       61 qgtaavdlht lwqlatgsss drtaheqtaa vvldsrlprl aagllvgcal gaagaalqsv
      121 srnmlaspdt lavnagayfa vvtvaafgis lpalpagata flggllaagv vlglsragag
      181 pirlvlagsa ltlalsgmsg tllllrsqqt tglfawgegs laqigmqsid rlapvallaf
      241 aglmlmgrrl dilalgddga avvgvsprlt rsvavvlavl laavsvavag pvgfvglcap
      301 avvrllstwi pglvrhrafi pasalagvlv vlgadvllra vfggqagaev ptgivttcfg
      361 alvlvvlayr srdmgsdsgs tafarlrgrr afvltlsvtv vallgavvaa tlfgdatlll
      421 gdvgnwltgr sgqlvtyild trvprvvaal lagaalavag avvqavsrnp laepgvlgvv
      481 sgagvgavtv ltfvplasfw lisgsalaga aaaaglvfgl aarrgleqnr lvligigvqa
      541 gagafvslli vltdpynqtk alawlggsty grtfpelipv lvalvvalpv lavmrreldl
      601 igldnetpal lgvrigatrl gllslavllt agavaavgvi gfvglvapha aralvgrrhv
      661 rvvplsallg allvvvsdtv grtviapaqi pvglltavvg apyfiwllwr srreg
//
LOCUS       WP_457657127             396 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Streptomyces griseus].
ACCESSION   WP_457657127
VERSION     WP_457657127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Benjdia,A., Guillot,A., Lefranc,B., Vaudry,H., Leprince,J. and
            Berteau,O.
  TITLE     Thioether bond formation by SPASM domain radical SAM enzymes:
            Calpha H-atom abstraction in subtilosin A biosynthesis
  JOURNAL   Chem Commun (Camb) 52 (37), 6249-6252 (2016)
   PUBMED   27087315
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Grell,T.A., Goldman,P.J. and Drennan,C.L.
  TITLE     SPASM and twitch domains in S-adenosylmethionine (SAM) radical
            enzymes
  JOURNAL   J Biol Chem 290 (7), 3964-3971 (2015)
   PUBMED   25477505
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428255
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43549
     Region          63..365
                     /region_name="AslB"
                     /note="Sulfatase maturation enzyme AslB, radical SAM
                     superfamily [Posttranslational modification, protein
                     turnover, chaperones]; COG0641"
                     /db_xref="CDD:440406"
ORIGIN      
        1 myldaaetra vregddgria dtlseygftp gngdavdlpg dvvnhlahlg isgqpshiag
       61 yrivvtdkcn mkcsycfvdt ntgapdltee dlrlgldllf evnrgrpevt yqwfggepti
      121 rpdlmmagdh yarelaekfd vgsiqptvvt ngakinddli ahfkefrygv gvsidgpppt
      181 nanerlllsg kpaderihrn iqrmleagih vganvtptqw nvhelpeivd yilslgikfl
      241 yvntpipahg twiahgpela rnlyqarmra lsrggmlfsh ldriyqalds rrprvyehlq
      301 gcggvnaall pggrislldl nwrdprfift ldqiredhsl lgraakdlhp fdgcktcpal
      361 aicggpsqne rllrrtqipt dlfwgsttvg aappva
//
LOCUS       WP_457657129             254 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657129
VERSION     WP_457657129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..254
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26904
     Region          119..248
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 meqnlaehac hlhrtlkgas vtqtgdllia dsgldddtfn ivatarftpd taparaaeta
       61 rtlaatgrpf swwvgpastp ddlaehlqaa gleaseteag mwkdlrdplp dahvdrlair
      121 pattpeqlad yaavlaanwn ppaatvrqff adtadwalae gcparylvgy adgrpvcsae
      181 vflhagvagi yniatlatdr rrgyggaita atlhtardag yetavlqasa dgepvyrrlg
      241 ftvsghftey altp
//
LOCUS       WP_457657134             408 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptomyces
            griseus].
ACCESSION   WP_457657134
VERSION     WP_457657134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..408
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43343
     Region          9..407
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(108..110,134,184,215,244,246..247,255)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(111,144,208,253..255,284,287)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            247
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 msaatspser rvsarigais esatlavdak akalkaagrp vigfgagepd fptpdyivda
       61 aveacrnpky hrytpagglp elkaaiaekt lrdsgyevda sqilvtnggk qaiyeafaai
      121 ldpgdevivp apywttypes irlaggvpve vvanettgyr vsveqleaar tektkvvlfv
      181 spsnptgavy seadaeaigr wavehglwvl tdeiyehlvy gdatftslpa ivpelrdkci
      241 vvngvaktya mtgwrvgwii gpkdvvkaat nlqshatsnv snvaqvaala avsgpldava
      301 emrtafdrrr klivrmlnei dgvfcpepeg afyayptvkd llgkeirgkr patsvelaal
      361 ildeaevavv pgeafgtpgy lrlsyalgdd dliegvsriq kllgeaka
//
LOCUS       WP_457657140             241 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657140
VERSION     WP_457657140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  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 241)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..241
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24308
     Region          34..241
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrisrlmpav aaaaacvlsl fapsataapa pplqdapppt tqiigggyaq napwaarlfs
       61 ngretcsati iaptwiltak hcvtggglsf rigsldqhsg gvvangvqty thssdlalvr
      121 ldrsvqatys rlgspgsvsv gqsvqvwgwg atsqcgsean cqsrylkvan vtvtggcgda
      181 yggsaicarr gngitaggds ggpmtangiq vgvastsdrq tttaytnvta yrswiqsvag
      241 v
//
LOCUS       WP_457657143             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657143
VERSION     WP_457657143.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31485
     Region          28..>70
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(29,33,58)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          97..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mideteedre fgleddsgav iaavgrqikl wreeaglraa elgsiigyse nlvfkveggk
       61 ripkpefldk tdaavgangk vsamkkdvee aryprkvrdl akleaeaiel gtyagvvihg
      121 llqteeyara lyaqrrpaya eddierlvaa rmarqvvfdr rpaplltfvq eeatlrrrtg
      181 grmvlrrqle hllelsrlrh veiqvmpmea eehaglggsh rilklkdgkt vghnevqlis
      241 glitdprqvq ilemrynlir sqaltprlsr efiekllget
//
LOCUS       WP_457657145             439 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457657145
VERSION     WP_457657145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..439
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46672
     Region          29..439
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 madedapagd glpadeglpa agedapagqa gvaveavfre erglllaslv rrfgdldlae
       61 evtseaieaa lrhwpaegvp arpgawlltt arrravdrlr rdqayaarla vlradaerae
      121 avapapdaag agelpddrlq lfftcthpal aaedraaitl rclaglttpe varaflvpta
      181 tmaqrivrak kkirearipf rvpgpdelpe rlpgvlqvvy svftegyaas sgprlqrlgl
      241 aeeairlari lhrllpaere sagllallll vharrdartg pegepvlled qdrgrwdrpm
      301 ieegralvvr altggpagpy gvqaaiaalh deaadvagtd wpqivalydv lltltpspvv
      361 alnravavam rdgpeaglal ldalageprl rayapyavar gdllsrlgrd geaaeayrea
      421 leragtgper aalrrklge
//
LOCUS       WP_457657151             707 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457657151
VERSION     WP_457657151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..707
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72693
     Region          22..278
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,46..47,80,85,90..93,105)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,88,104..107,111,113,150,152,
                     154..155,157,167..168,171,188..191)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,88,104..107,111,152,154..155,
                     157,167..168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(33,111,113,150,152,154,171,188..191)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(167..175,184..191)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mseaeqsrep qrdkngrlla gryrlgevlg rggmgtvwra ddetlgrtva vkelrfpsai
       61 dedekrrlit rtlreakaia rirnnsavtv ydvvdeddrp wivmeliegk slaeairedg
      121 tltpkraaev glaildvlrs ahregilhrd vkpsnvlise dgrvvltdfg iaqvegdpsv
      181 tstgmlvgap syisperarg hkpgppadlw slggllyasv egcppydkgs aiatltavmt
      241 epldppknag plteviygll ardpeqrldd agarallndv inapdvpapa padstqimai
      301 ppapaadplv krtpkqpkap kppkqstgsg esgegardrl rgalrsvrna ktpavatgaa
      361 agaaaasass paaaatgspv appkppsppg tstpgapsga apkgavaapa spvgapksta
      421 tasasvpgqr ppappastra sitdvvprrt laiiaavval ailgtilalt lgdgdgnggk
      481 ddtaasagas aggadgdkgd tgggsaggkg dgqkegqgke dgrasedpsg egsedpkgda
      541 pegdegddpa agdslpagye nvtdtrfhft mampgdfkrt giagtnsggi ynaaqgsfpr
      601 vqvdfnsspk ddaaaawrga vgsakvlsdg ykhgsikkve yngyptvadw tfernhngvr
      661 vrvlnrgfkv dakrgysimi sckidewdgd acrtlrdtaf atftptd
//
LOCUS       WP_457657154             548 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457657154
VERSION     WP_457657154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..548
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=58813
     Region          57..314
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(57,81..82,115,120,125..128,140)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(64..65,67..70,72,85,87,123,139..142,146,148,184,186,
                     188..189,191,201..202,205,222..225)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(64..65,67..70,72,85,87,123,139..142,146,186,
                     188..189,191,201..202)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(68,146,148,184,186,188,205,222..225)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(201..209,218..225)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtdhggrane ptsyglqpph apggsgaqhp appayvpspt apvsapdraa nrlvggryrl
       61 larlghggmg tvwrahdqvv drevavkepr vpehlgereh stvhqrmrre araaaridhp
      121 svvtvhdvvi edgkpwivme lvrgpslgdr lqegtldpre aariglavld altaahaigi
      181 lhrdvkpdnv mlgtgdrvvl tdfgiaqveg eqqltetgaf vgspeyiape rvlgqrpgpe
      241 sdlwslgvvl yaavegmspy rrshtpatlq avlsaepqvp argtgafgtl vmqllrkdpa
      301 arppaaevrr tlqqlaapap apvtspygav aagggggskw vppvlhrnrv aqfalgggal
      361 avvvalvlvl lnpfagdgpp enwqirpene vlsadvavpe eykrvqdddg elvwyadpsg
      421 vfeidfwhra pksddttddn pgadpaarka yyekggantt qmedasvtyk dathqgrkav
      481 emsteytpya ssadepvryr frellipgek esdpywhvrv rmpakgqaak dgdaiftevt
      541 eglkihas
//
LOCUS       WP_457657157             251 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657157
VERSION     WP_457657157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26560
     Region          <23..143
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msaeevravi sapgndrltw ntplseehaa rliaacapap garivdlgsg wgellmrlve
       61 aapgstgegv etdpeavarg rklaeergla drvrfhetpa aewsdggydl avsigsshaw
      121 pgttrealta laatvrpggr vlfgeavwqr eptpaalegi gagpgdfgsl lelirlaesa
      181 glralqvtva derewdlfes egpigrgqrw alanpdhplh aevtaeidar rtgyyggyrs
      241 yltlaylvlg t
//
LOCUS       WP_457657159             449 aa            linear   BCT 27-JAN-2026
DEFINITION  PspC domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657159
VERSION     WP_457657159.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Joly,N., Engl,C., Jovanovic,G., Huvet,M., Toni,T., Sheng,X.,
            Stumpf,M.P. and Buck,M.
  TITLE     Managing membrane stress: the phage shock protein (Psp) response,
            from molecular mechanisms to physiology
  JOURNAL   FEMS Microbiol Rev 34 (5), 797-827 (2010)
   PUBMED   20636484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..449
                     /product="PspC domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45932
     Region          18..80
                     /region_name="PspC"
                     /note="Phage shock protein PspC (stress-responsive
                     transcriptional regulator) [Transcription, Signal
                     transduction mechanisms]; COG1983"
                     /db_xref="CDD:441586"
ORIGIN      
        1 mtapsnaapg vappeapkpt lrrtprqkvv agvcgglgry cdvdpvifri vlgvlsatgg
       61 iglifygfaw lllpadgdde nearkllsgr vdgaslvall laligcglfl smlhnrgmla
      121 faalltlavv gfsvwtqsrr taapedpaap pgapasppgp ahtgglgtpp pevkapptpg
      181 gpswwrdpiv kdgttgpvgs gylwgppdtd adaaradvka grptpdapfr tprpssaprg
      241 prsigglvfl talvagglgt glswehqplg talqiglvaa lavfglglli asvlgrtgfg
      301 tvlmamvtag llagaaavpk didtswtrqk wrpatvaavq phyelrtgda rldlsglkvp
      361 kgetvrtgld vaagraavvv panvtvkvra eaglgeirle dgqrvqvrin sdestqrtlp
      421 pptgtkpagt ielelevgig qvevtraas
//
LOCUS       WP_457657160             255 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657160
VERSION     WP_457657160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..255
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26872
     Region          171..252
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtmanavqdy artltlrspd hyrvgpftvr hhpgwelkya nyaipdreae ptadevaalv
       61 dafreherlp rleflpawap avepallaag ftvenrapll acghgdlrtp tpvdglriav
      121 psteaeftda arvqhqgfgg dgepeqsmtd wlraaaggdg vaalavldgt pagaggcsva
      181 vdglselagl avaapfrrrg vgaalsawlt dralgqgcrt vwlepggpdv eriyasigyr
      241 rigekvnisl eqgga
//
LOCUS       WP_457657162             568 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457657162
VERSION     WP_457657162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..568
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59278
     Region          403..562
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mndqhphagh vgyddrstgs fdtdplfgsl pgghdtgyda ghpaagygdt tygvgydtay
       61 atgqpnhsgq ydasawntga qqpfaydgya aqehpqqqap qqepqqwdts gawqqvtdqd
      121 ltgqwttaay saetpyaaea yetgtydtga ydtgtypagt aygtggvyga dayetgaypv
      181 gaygtaavaa dtgtyattga ygtgtydgga ydtgaydata wnsgatpgdt ayepeqtsyp
      241 lyeqqheqha adatapeasa epdgttgdpa adpsstaafa alapdaaqdv apdreqdagd
      301 dlpaphtanr tavrtpaprs rarrrtpakr salltvavps acvmsvagia aasvsgmpgg
      361 eekqdettts lavadpstvk pvaannqlds qlaqlsegsd dfrerasrtq eridlrerqa
      421 aekkkreeea arrealrpkf vlpvkqhgls ayygqagvnw msvhsgidfp vsygtpvmaa
      481 tdgtvrtqln saygvmaivt aadgtetwyc hlsstkirsg pvkagdviay sgnsgnstgp
      541 hlhfevrpgg gaaidplvwl rskgvnpt
//
LOCUS       WP_457657164             468 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Streptomyces griseus].
ACCESSION   WP_457657164
VERSION     WP_457657164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  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 468)
  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..468
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..468
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48303
     Region          69..>94
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mllshggeps ptggpvarws veqvlalapd dasrkagtrl gtagpwsgtg rdgagavwgl
       61 ckgsgstpyr tvvdttgpac scscpsrkfp ckhalgllll lasddtafrp gepadwavaw
      121 iegrrgraae qagaatggga srgpadaaar kraerraerv tggaeeleqr ladllrggla
      181 atdrsgyalw detaarmvda qapglaarvr elgaitgsgp gwpvrlleec gllhlldtaw
      241 lgrerlpdpl aatvrtrvgl pmsaegvpvr drwlvlaqyd tpdgrivtrr iwlygresgr
      301 talllsfgaa grspaqslpv gatidaeltp ypgggqlrae lgkqfgttap agpppgiaaa
      361 aapavygtal redpwldacp vtlrdvipvp sedgwqvada hadsalpiap aalsrpglwk
      421 lvalsgggpv tvfgeighrg fdpfaawdpg ergevggrtt ggpvvqlv
//
LOCUS       WP_457657177             371 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457657177
VERSION     WP_457657177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..371
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40710
     Region          26..357
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mpqatatvad padesspgrp agahgaapgs dfapllravr dqdllerrtd ryvlgitanl
       61 valgalitgf vllgdtwwsl cltlpwavlw trtafvahda ghaqisgdrr tsrliglvha
      121 nlllgmneaw wndkhvrhha npnhidkdpd vgvgalvwtq kqaaqregfa swltrnqarl
      181 ffpmlllegi alkiygfqfl rrqplrerav sallltahig lyaalllstl spgkaivfal
      241 vlhalfglhl gmafapnhkg mempdpdger wghlqrqvlt srnvrgavlt dwflgglnyq
      301 iehhlfpsmp rpnlrlaqpl vkahcsaigm pytetglies yrqalshmhe vgeplrqggp
      361 agnvperegv h
//
LOCUS       WP_457657178             199 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657178
VERSION     WP_457657178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..199
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=20699
     Region          12..180
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 maddhahvld fftpraagwd srfpddgpay aaaagmlglr pgdavldagc gtgralpalr
       61 avvgpqgtvl gadltpamlk eaaqagrgds gtllradvar lplrdgalda vfgaglishl
      121 prpeadmael arvvrpggvl alfhpigraa laarhgrtit dddlraeprl rellagagwr
      181 lesytdeddr flalavrqa
//
LOCUS       WP_457657179             193 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657179
VERSION     WP_457657179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..193
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=20898
     Region          8..190
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 migedialtl kivvaggsga gkttlvgsvs eirplhseet lsesgrdrdd tdgverkatt
       61 tvamdfgrit vhegltlylf gtpgqnrfwf lwdelcegal aaivladtrr ledcfaavdy
      121 ferrripfvv avnrfpgapd hterdvaral dldpgtpvvp cdardrasgk evlirtveya
      181 grvhtarlla svg
//
LOCUS       WP_457657182             237 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces griseus].
ACCESSION   WP_457657182
VERSION     WP_457657182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..237
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24549
     Region          1..196
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mrmllirhgq tpsnlghfld tahpgpgltd lglrqaaalp galagediaa lyastltrtq
       61 ltaaplaaer glevlirdgi relsagdlem radedaarqy lttvfawpag dtarrmpgge
      121 ngtealarfd avvaeaarav ehgtvalvsh gaairvwtaa rarnvtvefa aqhsldntgv
      181 vvvegspdsg wtatswagrv vpgvtasgwa dggpagqtlp vaelrpeqgp tddrpiv
//
LOCUS       WP_457657189             125 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457657189
VERSION     WP_457657189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..125
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13796
     Region          8..123
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 miadlecvvl dcrdprelag fyasllggev drpdrrwgcd adwstlhtpg glvlafqrva
       61 dhqpprwpgq dppqqfhldf gvtdqerahe qvlangasll dagdeargwr vyadpaghpf
      121 clvrh
//
LOCUS       WP_457657192             336 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457657192
VERSION     WP_457657192.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  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 336)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..336
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36313
     Region          9..321
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(14..16,46,51,77,140..141,181..182,205,234..240,276,
                     293..296,301,304..305)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(46,51,77,140)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 msithllpgr lgfgtaplgn mfraipddea aatvraawdq giryfdtapf ygaglseirl
       61 gdvlaqhprd ayvlstkvgr vildeaedpa ardlgekggl fehgrpnkmi ndysadatlr
      121 siedslerlr tdrldivwvh dvaqdfygde wlaayesart gafrvltrlr eegvikawgl
      181 gvnkveplel tldldeprpd afllagrytl ldhdralqrl lpaaaehdvd lvvggpyssg
      241 ilaggahfey qkapadivak verlkaladr hgigikaaal qfalahpata aaipgatrps
      301 riaedlaald etipaafwta lreeklisad apvpta
//
LOCUS       WP_457657194             332 aa            linear   BCT 27-JAN-2026
DEFINITION  sporulation protein [Streptomyces griseus].
ACCESSION   WP_457657194
VERSION     WP_457657194.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Sonoda,Y., Mizutani,K. and Mikami,B.
  TITLE     Structure of Spo0M, a sporulation-control protein from Bacillus
            subtilis
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 12), 1488-1497 (2015)
   PUBMED   26625291
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Han,W.D., Kawamoto,S., Hosoya,Y., Fujita,M., Sadaie,Y., Suzuki,K.,
            Ohashi,Y., Kawamura,F. and Ochi,K.
  TITLE     A novel sporulation-control gene (spo0M) of Bacillus subtilis with
            a sigmaH-regulated promoter
  JOURNAL   Gene 217 (1-2), 31-40 (1998)
   PUBMED   9795118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="sporulation protein"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /calculated_mol_wt=34397
     Region          1..255
                     /region_name="Spo0M"
                     /note="Stage 0 sporulation-control protein Spo0M [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG4326"
                     /db_xref="CDD:443467"
ORIGIN      
        1 mvfkkllgal gvggpsvdtv lepgpalpgg llsgevrlrg ggtevsvdri slllvarver
       61 edqeeehegt vvlerftvgg gfrlaeeaeh tvpfsltlpw etpitelhgq plgpvlgirt
      121 eleiagardk gdldplavgp lpaqeailea fgqlgyafks adlelghirg tgqqlpcyqe
      181 ieilppagha havneievtf laapgglevv ieadkraglf seghdtvhrf tashhavpqt
      241 ewnarvdawl keviaghagh gapspygtps sygehhgdqh rsgpgagavv agvaagvavg
      301 vvggmvaaev vdeigdafed eegdedaggd eg
//
LOCUS       WP_457657196             176 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657196
VERSION     WP_457657196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..176
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18521
     Region          8..53
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mgnderelys vgevaellgl hvrtvrnyvr egrlkavrig kqyriskedf aaltgrpvdd
       61 taghpadgta pvptpapapg hvevssivqi dalgpdaahr lstfvtastq sardtadplr
      121 vqtvydkert rmkivilgga aatadllhmi dgllgpdndl lastdtstgg qgvdra
//
LOCUS       WP_457657200             352 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657200
VERSION     WP_457657200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..352
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36797
     Region          64..352
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mtqvdtpstp stadvvdetp gadtagpaea sgtwrrgrll aasalllglv lllharipnr
       61 ignlgslvet flpwfgllvp vllagavlrr sapavialll plvawlnlfg glltdkaheg
      121 gdltvashnv gaenadpigt aralagsgad vlaleelaah aretyekela keyphhtvqg
      181 tvglwsrfpl sgsrpvdvkm digplgdakp aevkmvynrg lrttvatdrg plavyvahlg
      241 svrvnpragl stgqrdagaq slgqalaaer nervvllgdl ngtlddrayd gitarlesaq
      301 eaagagfgfs wpatfpvvri dqilvrgvep ksswvlpatg sdhlpvaari sw
//
LOCUS       WP_457657201             286 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657201
VERSION     WP_457657201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31504
     Region          5..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          102..268
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 merdqladfl rrrreairpt evgiadgprr rtsglrreev amlagmsvdy vvrleqgrss
       61 qpspqlltal aralrltdde rdhlfhlagh qpppadsvag laraglvrml dllgdtpamv
      121 vsdlgevlaq nrmslllagd htafsgdrry lvyrwftdpa araagapeeh ehqarqlvad
      181 lraaagrrsg dpvvaglidr lraaseefrr iwaehevgvr radrktllhp rvgrlvmdce
      241 tlvtpdhgql llvltpadag trerldllrv lgieefpaga tsaper
//
LOCUS       WP_457657203             369 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657203
VERSION     WP_457657203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..369
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37347
     Region          48..362
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 matsldhlss kpsrpapvgt gsapprrvpl pllltglgla lplslvcgag lgssglswae
       61 vlrylwaglt ggaigpdevp aytivwelrl pravlaavvg aglsaigvav qamvrnalad
      121 pfvlgissga avganavlif galgalgiwa lstaaflsal lamllvyava rtergltplr
      181 lvltgtamyy gfsavttfmv faaergeaar sammwllgsl sganwaavpi aagavlagla
      241 hlgwsarrln alamgdetaa algvdagrlr kelflvsaav tgavvavsga igfvglmvph
      301 avrmlvgadh rrllaaapla gavlliwvdi lsrvvlapae lpvgvltaai gvpcflllmr
      361 rraysfggi
//
LOCUS       WP_457657204             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657204
VERSION     WP_457657204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27204
     Region          2..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mriyidaltv eiagarlvdq vtlgaadgql vglvgpngsg kstllrcvyr alrpsagvvr
       61 iggqdlhals vgegarrlaa lpqdavaefd ftvaeivamg rlphqgpvar ttdedrrfca
      121 daldgvgagh laergfltls ggerqrvlia ralaqqprvl vldeptnhld iahqlevlal
      181 vrgsgltvlt alhdlnlaal hcdlvhvidg grivasgapd avlttellad vfgvrahrva
      241 hpetgalqll fdlpparpts
//
LOCUS       WP_457657207             430 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces griseus].
ACCESSION   WP_457657207
VERSION     WP_457657207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 430)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..430
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47003
     Region          52..430
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(98,119,121..122,205..206,214..215,218,221..222,225,
                     261,264..265,268..270,273,316,317..320,344,420)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(120..121,128,132,139,184,187,265..266,269..270,
                     273..274,277,315..316,318..319,321,344,371..373,376..377,
                     379..381,384..385)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtesttepar qdpaptcpvt rpgagpvtat patatpptat pfpqdrdcpy hppagyaplr
       61 edrplsrvtl ydgrpvwavt ghalarrlla dprlstdrth pafpvpaerf anarqrrval
      121 lgvddpehna qrrmlipsfs vkriaalrps iqetvdrrld amerkgppae lvadfalpvp
      181 smvicallgv pyadheffee csrrllrgpg aadvdsarae leeylgalid rkrtepgdgl
      241 ldelihrdgp ngpvdrqdlv sfavilliag hettanmisl gtftllghpv qlaalrdget
      301 ttsvvveell rflsiadglq rlaaedieva gttirkgegv mfstslinrd tevfadpetl
      361 dwdrsarhhl afgfgvhqcl gqnlaraeld ialrtlferl pdlrlavpah eiehkpgdtv
      421 qgllelpvew
//
LOCUS       WP_457657210             287 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657210
VERSION     WP_457657210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..287
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30344
     Region          40..151
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtapppegtp gdgrygeayf rpdrageaer idfgalaydd ltmarllalg agpgwhcldi
       61 gagtgtvshr llgeagvgsv lavdrdvrfl narpapglev lqadvtapgf apgrfdliha
      121 rfvlmhlper drligelael lvpggvlvls davdltsdrp pttpystamr amwqglrtti
      181 gtdvsrvpsy phllrgagle pvaaefhvpp llpgspisrf wadtwqrgre amlatglvdd
      241 aavdeavhyl estacaalsa gmltawghrp nvtttpsspr rtdsspg
//
LOCUS       WP_457657215            1113 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657215
VERSION     WP_457657215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1113
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=114033
     Region          127..592
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrkrslkaca vaaaavavtm gmtgpasgkt dgpgtagtaa peglaaagtt vhtvtlitgd
       61 rilvdargrv ggierakgre dipffteihd grthvvprda rqliadgvld rrlfditala
      121 gpesrrahra glkvivgyrg daagsaragv rsadgttvrr tlsaldadav tasaatdgtg
      181 glwdaltrqr rdgsaattsg iariwldgvr tasldrstgr igapaawars fdgtgvkiav
      241 vdtgidathp dlagrvaaer nfsaspdard rdghgthvas taagtgakda rfkgvapgar
      301 linakvlddq gvgddsgiia gvdwavsqga dvismslggl dspgidplea qvnkvsaekg
      361 vlftiaagnn gpeqgtiasp gsaeaaltvg avddddliad fssvgprtgd kavkpditap
      421 gvsitaaaaa gvegqdppgy hslsgtsmat phvagaaail kqknpawtga qlkaaltgsa
      481 eggshsvfqq gagrlavdra ldrtvvaepv svslgtqpwp haddspvtgk vtyrnhgsad
      541 vtldlslaap tgadgqpapa gfftlgaprv tvpaggtaav dltadtrlgg tvdgsysatv
      601 vasgggqsvr taaaverepe sydvtftatg rdgapntgwq adlkghggsa sglrffpdls
      661 sgsatvrlpr gtynlsadll vdpaapgkga dlinnpqfsv tgpttvelda rttrpvsfav
      721 pdatatptra gmmyalntpe tgitlwsdft sfdnvrtahq gppvtgessl yqqwsahwer
      781 gdteynalag slvpklatgy gktyttrnma lvkvgigssv pgvdgivkay gelahggvdp
      841 lfsvhkvpgt rkvylstdde avwniaagvl gekdpagnrr ieavhtfdgt rrfepgttht
      901 enfqagvmgp klnagdgivr dgddihgslt lvsdgaghpg ftryagastt ihrdgvlyak
      961 edaaiderff tlppesakyk vattisrnpa vhragtrida swtftsarte apvtlpvstv
     1021 rflprlalds tvpaggaqtf pvvvqgaaae agpkslrvlv syedgkwlpa kvtagkvtvr
     1081 apekgkaisl kavvldrkdn estvtvhnaf fgr
//
LOCUS       WP_457657217             429 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657217
VERSION     WP_457657217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..429
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43895
     Region          48..425
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtepagsegd vvtepaaaas pelsrvgpre pttwsdgard rwravssrlr ggdlgllpvl
       61 aglvviwvvm qilnpiflss anltnlales vpvgiialgv vcvllvgqid lsvgsvsgls
      121 aavlavlfvd rglpswlava aalalaglig wfyaqvhnri gvpsfvitlg gllgflgvql
      181 wilgpkgsin lpfdsglvtf aqlqflppwl aytlvvagaa vlyatgaara gerrraglaa
      241 asrgllvgrs lallaglgaa vwylnrdrgv gwmfvfflal vlalhyvlsr tsfgksmyav
      301 ggnseaarra gvnvkavvtt afvlcttlac vggvlsasrl aaanqssggg dvnlnaiaaa
      361 viggtslfgg rgtafaallg vlviqsissg ltllnldsay rfmvtggvll lavsldavar
      421 rsrvshgra
//
LOCUS       WP_457657221             498 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Streptomyces griseus].
ACCESSION   WP_457657221
VERSION     WP_457657221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..498
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51690
     Region          15..449
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 mssdssgtgp hapavigidv atasvrvlcv dgqgqvlaea rtdlpppvrt spgtitgtrt
       61 gtseqdarsw wpavrsalrr ttaalprggr evlavavsat sgtivptgsd gepigpalmy
      121 ddrraaelna eaqrtgsarw nalglsvgpt aalgravwcr rtygsalhqv lhtpdligre
      181 ltghpvatdw shalksgyda rgsewahevf daldfplall pavrapgtga gvvgpeaaea
      241 tglpegcsvr lgmtdgcagq iatgavepgr fvgvlgttyv lkgvsadlvr dptgafyshr
      301 hpdgwwlpgg asntggecla rtaparlpal daaaaargpa sytryplcre gerfpfvsga
      361 ahgfargrpr detdahraal egvafverla ldrierlgvp vlgplyaagg gsrsavwtai
      421 ratvlnrpvr vveraetafg aallaatgtl hedltasaaa mvrtgalvep vpaerpaled
      481 aharfveelr ergwlpdd
//
LOCUS       WP_457657222             332 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657222
VERSION     WP_457657222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  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 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   Rosinski,J.A. 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 332)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18524816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /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=35888
     Region          1..250
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          <237..332
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mleiaglspd eesvygllva sgrasasdla eragltaaht aevlraltak glasptdgtp
       61 hlymaaapda allprirhsa daldiarrea arlmdsyret mrrrdagqll evitgaealr
      121 hclrqlqkga qdemlwfcka qyvampsgsn rdefdalarg vryrvlyeka ffddedavsn
      181 vmagvqagev aravpqlplr laivdravav fplvsggphg speepttalv rdsnllaali
      241 alferyweda vpldiddtgg padggphapd vlpptdrrll sllvagvsdk tiasqmqlsr
      301 rtvqrriqsl mersdaatrm qlawhaarhg wl
//
LOCUS       WP_457657226             301 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657226
VERSION     WP_457657226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..301
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30343
     Region          1..299
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,123,127,148..153,172..173,175,188,
                     211..212,233..234,247..249)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mraaryhdyg padvlviddv pephagprei rirvaaagvn pidwklrsge vrehfpvefp
       61 aipgrdaagv vdevgegvsg vtvgdevfgl ggifgaaaey avltawsavp eawtleqaag
      121 aglavatagr aldalgdlsg rtlliegaag gvggaavama aargatvigt sspakhaylr
      181 tlgvvptayg dgladrvrel apggvdaald laasgsladl valvghtdrv vtvadavrsa
      241 elgvrhvyae ndaavlaega alggrgaytp yvqatypldr iadahreaeg ghvqgklivt
      301 l
//
LOCUS       WP_457657227             193 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657227
VERSION     WP_457657227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20772
     Region          7..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdgrqtrna ertrravlda avqvildkga avtlaqvaaa agvsksglih hfgsrdqlvv
       61 alvedtherf retvrgyldl senypgkmlr ayvralcags aeaatardft sapmwgglyt
      121 ipavapvmee naawwdeqla ldglsperil ivrraaegia maavygerde ssistardll
      181 lelasegtfr tpl
//
LOCUS       WP_457657230             328 aa            linear   BCT 27-JAN-2026
DEFINITION  pirin family protein [Streptomyces griseus].
ACCESSION   WP_457657230
VERSION     WP_457657230.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35766
     Region          33..291
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msnverepvs rhgtrgpeaa epalrrveil tprdvplggp rsmsvrrtlp qrarsfvgaw
       61 cfvdhygpdd valrggmdlp phphtglqtv twlfdgeveh rdslgshafv rpgeinlmtg
      121 grgichsevs ttrttvlhgv qlwvalpdeh reaerdfqry vpspirkdga eikvflgsll
      181 davspvrtft pllgaelile agasltlsvd atfehgllvd egdieldgta lspaqlgflp
      241 pgngsltvrn tssararvil lggppfeeei vmwwnfigrs hddivrarkd weqaserfga
      301 vegyagerlp apelpnatla prrnppts
//
LOCUS       WP_457657238             356 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657238
VERSION     WP_457657238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..356
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38533
     Region          7..341
                     /region_name="LLM_2I7G"
                     /note="probable oxidoreductase, LLM family; TIGR03858"
                     /db_xref="CDD:274817"
ORIGIN      
        1 mdaspiefgi dsfgdlprnd rgaivshaea iraavaeavl adevgidvva lgehhlpefa
       61 isspetvlag iatvtkrirl asgvtvlssd dpvrvfqrfa tvdalsggra evilgrgsft
      121 esfplfgydl kdyevlfeek idlfhrllde kpvtwegttr palraadvyp ktesgrlntw
      181 vgvggtpqsv irtarygfrl mlaiiggapd rfapyvdlyr raseefgtta rpvglhspgf
      241 iastdeeake lfypgcketr drigalrgwp plrreefnae vdqgslyvgs vetvatkiah
      301 avrvldagrf dliysaagtv sasarlrave lygtqviprv rellteqpaa tagakr
//
LOCUS       WP_457657234             187 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457657234
VERSION     WP_457657234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..187
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20228
     Region          37..170
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msdlvspqhg gqhrlpssae sgdaatprat geqredwqsl vilahlveae lerktqcdag
       61 iahshfkila llagadrhtm gltrlgralr fhqsrlshal rsleaagllr redtpdkgra
      121 yqavltrrgl dlvervlplq dvfardvvls gltateiaql rtlaekiian ldvgrsgqvl
      181 qrgpass
//
LOCUS       WP_457657231             434 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457657231
VERSION     WP_457657231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46514
     Region          7..429
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mentllnpyp vsedslylni wrsrkpasak lpvivyipgg gfatgsgalp lydgeslasr
       61 getiavtiny rlgvlgflsh palaeesaag asgnygvldq iaalrwvrqn iaafggdpdr
      121 vtiagqsagg esvcvlgatp rakglvdgii ggggacmgtr gntergdqyd tgpvaedagr
      181 rlseklggat veemrrmpve rvvdaakslk shwrpsidgl vldrtpaeiy aagdqldvpt
      241 lvgsnadeas lallsppdad vagyrkkvrq ehgpdadlfl rlypgdteaq vldsllqakt
      301 dkimtramrr wgtlqtrtgk advyayyfah vppeaglrkf gayhgaevmy aydnlgkdgd
      361 aaygprdhtl rdqmsefwin fartgdpngp glpawptlre eaekvmrfdg gssvaprprp
      421 davdfwmryd gpla
//
LOCUS       WP_457657249             308 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Streptomyces griseus].
ACCESSION   WP_457657249
VERSION     WP_457657249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..308
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32617
     Region          72..308
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mslpaafhei akrvnnwgrw geadelgtln litdavvrea vgavrtgrri plalplrqdg
       61 vqsglipgri nplhtmvqin qelfgpgtva tsddavtmgl qaathwdalp hvshsgkiyn
      121 grpadtvtah ggarfssiaa vehlvsrgvl ldvarargvd rlpgdhavtp edlaaaeefg
      181 gvtvragdiv lvrtgqvqla lagdrnaygy pspglsvrtp ewfhardvaa vandtltfei
      241 fppeiedlwl pvhalhlvem gllqgqnwnl ealstacaee grytflltaa pepfagatgs
      301 pvapvavl
//
LOCUS       WP_457657250             523 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457657250
VERSION     WP_457657250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..523
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56494
     Region          20..521
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtavndvtat ahalgssrtf welierraal tpdrpvllqe drsltfgelr draervaagl
       61 ygmgvragsv vawqlptrle tallsfaltr lgavqspvip fyrdrevrfa lresgaaffa
      121 vpgvwrgfdh tamaeriaag lpdpprvfea ydalpdgdpa vlppppepac geevrwiywt
      181 sgttsdpkgv lhtdrsliag gsclghalkl daddvgsmaf pyahvagpdy tvmlllygfp
      241 avmfeqfalp dalaeyrlhg vtvaggstaf yamflaeqrk apdrplipsl rllagggapk
      301 ppevyhavvr emgvqlthgy gmtevpmitm gapddtaehl altegrppeg meiritdehg
      361 kplpygvege vrlrgeavcr gyldpaasaa afdaegflit gdlgrvresg hltltgrlkd
      421 iiirkgenis akeiedllht hpavadaavi glpdperger vcavveqppg appltlaels
      481 ahlreaglsv hkvperlell dalprnetlr kvlkyrlrer fgg
//
LOCUS       WP_457657253             354 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Streptomyces
            griseus].
ACCESSION   WP_457657253
VERSION     WP_457657253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..354
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36834
     Region          49..349
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mkrgravtaa iavavlaata gslaltrlgp deetggaknt glppatapve rgdlrdsaqa
       61 dgtlgydker kvnagaagtv twtprtgstv ernerlyeid grpvrllygs gpmyrtlkag
      121 dkgrdveqle rnladlgytg ftpddeytel taaaverwqk shgakqtgkv gpaditfapg
      181 kvriksigag lgeqaqpgap vlettgseri vtfrldvaes rlaktgtkvt vdlpdgttaa
      241 gkvssvgrta kqgddpqdds pkvtltvsfd epdevdgfdq spvtvnltge tredvltvpv
      301 nallalpggg fglqvvrggt vrevkvelgm faegrvevsg gglregvkvg vpki
//
LOCUS       WP_457657254             246 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657254
VERSION     WP_457657254.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25445
     Region          15..234
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mstnaaadpa hrprtvvals gvtkeypgpv aalrgvdlav eegellgivg psgsgkstll
       61 hiigtldrpt agsvhiaghd vaalsdrrls alraqhvgfv fqafhlvpgv sardnvaegl
      121 lysglsrsar rrraaealdr vgladrldhk phqlsggqkq rvaiaravvg epallladep
      181 tgaldsasga avmellrdln qegatiavit hdteiarelp revrirdgrv vadvihgaaa
      241 atgagr
//
LOCUS       WP_457657246             341 aa            linear   BCT 27-JAN-2026
DEFINITION  MASE1 domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657246
VERSION     WP_457657246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Pfiffer,V., Sarenko,O., Possling,A. and Hengge,R.
  TITLE     Genetic dissection of Escherichia coli's master diguanylate cyclase
            DgcE: Role of the N-terminal MASE1 domain and direct signal input
            from a GTPase partner system
  JOURNAL   PLoS Genet 15 (4), e1008059 (2019)
   PUBMED   31022167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Lacey,M., Agasing,A., Lowry,R. and Green,J.
  TITLE     Identification of the YfgF MASE1 domain as a modulator of bacterial
            responses to aspartate
  JOURNAL   Open Biol 3 (6), 130046 (2013)
   PUBMED   23740576
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Nikolskaya,A.N., Mulkidjanian,A.Y., Beech,I.B. and Galperin,M.Y.
  TITLE     MASE1 and MASE2: two novel integral membrane sensory domains
  JOURNAL   J Mol Microbiol Biotechnol 5 (1), 11-16 (2003)
   PUBMED   12673057
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..341
                     /product="MASE1 domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=36284
     Region          1..>312
                     /region_name="MASE1"
                     /note="Integral membrane sensor domain MASE1 [Signal
                     transduction mechanisms]; COG3447"
                     /db_xref="CDD:442670"
ORIGIN      
        1 mirskearrr avyvaqvlgv agayylsgrl glmrqvvvdg avvtplwppt gialaallcl
       61 garvwpgial gtlvtvseig daftvsrlai mfgntiapla syallrkvgf rselvrlrdg
      121 vclvflgafa gmlisatlgs ftlllndkvp pgrfwlvwss wwagdamgvl vvtpvllvlr
      181 rarrprpgdr wleasvlavv vvlssliatr sslgmiylvf pviiwaalrf qlpgsapcal
      241 vvsvlailag tdalgpfagh slmeimanls llngcvalta lllgaivaeh rnirreteha
      301 veelealveq laplsgpasa rygdrprrhg pldggphpdq p
//
LOCUS       WP_457657257             226 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657257
VERSION     WP_457657257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..226
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23232
     Region          40..155
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mssdstgtgt gtgatdsagf weshyaavda qwgtkpnvvl aevvtalape pggagraldl
       61 gcghggdalw laslgwdvta vdvsatalgr vaagadaagl adrvhpsrhd laasfpdgdf
      121 dlvtasyfht pveipreqvl rraaravapg gllvlvehas lapwswrdgh edvrfpapdd
      181 vlaslrlgdg wrterchapr rtatgpgget atvtdnvivv rrggta
//
LOCUS       WP_457657260             418 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657260
VERSION     WP_457657260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..418
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44824
     Region          60..387
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrsparrpf aamllaasvl tpmamapapa vhaatldqhd qsgqggqggr herhgddrcp
       61 pggldpalta eldrtiedvr eqagipgavv glwmlgkgsy ihasgvgntv tgepmsagtr
      121 irigsetktf tvtallqlvd dkrvklddpi sryvsgvrng dritlrqlag mrsglfpyta
      181 dagfvhdlls dpyrsftprg vlaygmqhkn tfkpgaefqy snsnlvllgl viekvtgqpl
      241 drvihervlr parlrstlfp tgaefpepha hgytdqtlsg etedatdwnp swawaagami
      301 sdlhdlrrwa kvvatgells petqaqrltt lptgfpglsy glgifetggw ighngslpgy
      361 etvtvylpaq katmvimint dslsggqeps tllaravtqi atpdhvydgs asqgrntp
//
LOCUS       WP_457657262             665 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces griseus].
ACCESSION   WP_457657262
VERSION     WP_457657262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..665
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69634
     Region          6..450
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          580..647
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(604,613..615,622)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            614
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrsdvihtll vanrgeiacr ifrtcrdlgi ttvavysdad adalhvread lavrlpgaap
       61 adtylrgglv vaaalaagad avhpgygfls enaafaaavq daglvwvgpp vkaielmask
      121 trakelmaga gvpllapvdp atageddlpl llkaasgggg rgmrivreld altgellaaa
      181 aeaasafgdg evfaepyler grhvevqvma dahdtvwalg trdcslqrrh qkvieeapap
      241 gldetlrtrl heaavaaara vdyrgagtve flvsadgrpy flemntrlqv ehpvteavfg
      301 ldlvalqlrv aegeplpsaa ppqpsghave arlyaedpar dwqpqtgalh alevpdapgl
      361 rldtgytggd tigvhydpml akviahaptr aeavrllara lerarihgpv tnrellvrsl
      421 rhpdfaaarl dtgfydrhla altapgagdp ataalaaala savrnttapg gpaptrfgaw
      481 rnvpsgpqrk pyrsepdgte hevayrtprs gvpephetpg trvltttpdr vtlevegvtr
      541 hfaisthgdr ihvdtadash tftalprftd pathtapgsl lapmpgtvvr laeglaagaa
      601 vtagqpliwl eamkmehril apaagtltal haapghqvev gallavvqed paatpvplsv
      661 peeta
//
LOCUS       WP_457657264             294 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657264
VERSION     WP_457657264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30665
     Region          12..292
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mnegpstgrp velrhlrafl avadelnitr aaarlrltqp avsrtlaale rhlgvrlvdr
       61 sthhlaltpd gvafrdkaaa avaafdeala pgrlrtwplr lghawsafgp yttpllrtwq
      121 erhpgtplel lriddrtagl trgevdaall rgpvdapglv tevlftearv aavtadgpla
      181 graslaladl adgpvvlntv sgtttvglwp pharpaatlt vgntddwlta iaagrgsgis
      241 tastatlhph agvayvpldd apgvpvllar rdapghpalp qlaalareii argp
//
LOCUS       WP_457657268             532 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657268
VERSION     WP_457657268.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  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 532)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..532
                     /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=54743
     Region          170..369
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrpshrptal allisaaatg tltlwgvsaa pdtvriplaw gagaaavlls vcvavtvhtl
       61 gtartlralr vadaqrftse tsrlvsssav eaqrftaeta rikgaasaet arvaaearae
      121 neriaadaaa eqarlqvtvd rltaratrae tersaavaac anaagrmqal atsmladlre
      181 mehrhsdesv lgdllhldhr taqagrlads iavltgarsg rrwakpivme silrgamgri
      241 gsyqrvrlhs tsdvaiagha aegvmhalae lldnaanfsp ptaevhvyve evpagivitv
      301 edsglvmsev qlrraeravs aenqdltnls gtrlglavvg rlarkhgltv sfrpsarggt
      361 galmmlpqel isratapaaa aptaaptata aipaqtgpdq aqdragttap atatastpae
      421 pepshasaag tdtsdaapta rslaeddast pptpaaeses tgavpafges glpkrrrgrt
      481 laaaeartgn atpggadtpr arttdpkvqa arfstfskav ransqhpegn tr
//
LOCUS       WP_457657269             204 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457657269
VERSION     WP_457657269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 204)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..204
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21749
     Region          30..185
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(35,51,93,121..122,134)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 msaaavehpc dgepefslld sanelsdqlp grrveiiggv itvapspdgp hadalttlal
       61 lfgaaglhgq esrilqgagl wlpsgpydya ipdlslvdad yrdhqaenat ydpsvfrlvl
      121 evtsgnyqnd lrnkvtayal akipvyvild rkhsrvhvlt eplaggydnh qvyapgqtvt
      181 lpdsigaevs ldveelvrag spkr
//
LOCUS       WP_457657271             240 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657271
VERSION     WP_457657271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..240
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25769
     Region          14..202
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          59..150
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mtisgpatgf qratrdsyda lapayvefar gelaakpler allgtfaela vasggglpva
       61 dvgcgtgrvt eylhglgrgl dvfgidlspr mlavarqehp glrfeegsml aldlpdaslg
      121 gllawystih vpdeelprvf aefhrvltpg ahvqlgfqvg deplrmteal gaeislvfhr
      181 rqperiaell rdaglevvsr vwreretdgp fperapqgfv larrpivsgg cedgdisttd
//
LOCUS       WP_457657273             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657273
VERSION     WP_457657273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31472
     Region          13..66
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(17,21,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(20,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(27..28,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mstdfqsari algarlrelr seaglngkgv aealgwqrsk vsrletgkqt ptardltews
       61 qavgrpevat elrgrlvgle sqyrswrrql agghrarqel avtettatkl irgvevsrip
      121 glfqtadyar htfqanaefr riprdieaav rarmrrqeal yeagklfrfv vweaalyvlt
      181 cprevmaaql drlagllgld tveigvvplg aqlrrapghg fwiydrrrvi vetlntemwl
      241 ddeenvvlye rawdlmaeaa vqgpqarhli grarasleld
//
LOCUS       WP_457657276             182 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657276
VERSION     WP_457657276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..182
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18853
     Region          17..>146
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mvgvgsgtvp ttitplpftt arldalplep ayaeemaavl adpalyvftg ggppgpaalr
       61 sryerqcags pdpgelwwnw vlrvrsdgrl agyvqatvrg praeiawvvg tpwqgrgyas
      121 eaakglaahl tsaggvrtlv ahvhpdhaas eavasaagla ptgewedger rwtgnppvpg
      181 ar
//
LOCUS       WP_457657277             268 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657277
VERSION     WP_457657277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28601
     Region          64..265
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttlerslpy wavsdcwnlt rrtlthyqrh psaivwqlgf pilsvllygy vfgsamkvpg
       61 ggdyrvflmp gmfamtmamg fmntavavvt dvskgvvdrf rsmpmapsaf asgrgaadlv
      121 vaaaeltila vtallvgwra dggamaalga fglllllrfs liwvgvwlgm lvptpeaagg
      181 lyavafpltm isstfvapsl mpgwlgtvaa wnpisstata trelfgnpva gggtwveeha
      241 vlmavvwpla itlvflplav rrfqrlsr
//
LOCUS       WP_457657282             406 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657282
VERSION     WP_457657282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 406)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..406
                     /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=41746
     Region          140..405
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mviatalyrg shlvaggvvv aqhqrdrlfp wlalsaaias taliwfmaar hrrlvpwvvg
       61 ldvlvigcll pfgayawgga rtqesvawvm llggsasama avafgarlla vavallvath
      121 lagylmvaad aavtgahlna lvfsavvswv ltwylcrqge qvdsanrral aaeaqrarfa
      181 ervahhnalh dtvlatltai arggvdants mmrercarea aylrrlveqa ddrepasevr
      241 aaleesvraa ealglrvtar yheppavpge ialamaratt ealnnvrcha gtghafltav
      301 gdsgrlivtv vdrgrgfdtg sagpegaggp ggpddaggaa gpgasggaag pgvsggpegp
      361 vgpvrqatgg igldrsvyar mrgvggrafv dsspgegvrv elrwpg
//
LOCUS       WP_457657285             690 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457657285
VERSION     WP_457657285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..690
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72815
     Region          426..647
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mnrrpervsf rfsarsrfaa clvatadgal apgwwdldgt hppyagdprr yregapaett
       61 atqvlptedg gllrlrgaag sgrhllllsr papaaatata tgtslagprv pypaelelrg
      121 pspaefelkd pppagpepka pappeelive arglrlvpgg ppgtlalave tthdgrtrvr
      181 rvratplrls dpvilpgrvt allpldgtgr ryatdlegpd gyrpvsldlr dgtwhalpsp
      241 angrihrlll sapasglllt asdpgdgrlr iahaalgdrt rlsfpdrlns ldgavlplaa
      301 dpagervalr vtrgararlf lydvgadrpr paalppgafh pvagwstggl rvvyatpdrp
      361 adlvtvpdta ahpdpasyda pssslgapsn spgtegtsha atewfatpsg rfeavvlgdr
      421 rtaptvvval hggpedhwtl ghdpvlarls dagaavvapn qrgstgygra haeaihgawg
      481 vpdladirsl vrtlteqrpp dseppvllgt syggflalla vcadpyawar caviapflsa
      541 rglrersspa vralidrhgl geppdddlgp rdverlahri rvpllalhgc ddpvvpvdet
      601 rrlrrslara ggpqraphdc lgipgaghhp lqerggaglt drlvsfltar apdrrrtlap
      661 peltvvdaav rhrrspavfg hithdertpp
//
LOCUS       WP_457657287             595 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657287
VERSION     WP_457657287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 595)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 595)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 595)
  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 595)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..595
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60595
     Region          3..564
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtsprrlvwd atartrgwfv lasatavlgs agtlafpwam araldavvar rsvtgpvlvc
       61 aallalvvtt galqtlangg ygsgtvaalr rslarralda gvpgtadfpa gdlagrlsag
      121 caqagsagvt lvtastavlt slggvvalwl ldwriglcfs lgvpplalia rmfmnrgsgl
      181 flryqetqgr isalllealg gartigasgt aaaetrrvla plpelsrtgh rvwalqrdtg
      241 wqvgllipav evlvlcaggl allrgdisag elaavvgyta lamaaldqld alfalgmsaa
      301 garrvaevvd qpvpapgtra rpaggsgtvt lsgvtvrsga rtvldavdli vpagtalavv
      361 grsgagkstl aaligrlrep daglvaidgv plrelspgal raavgyafer pallgttvag
      421 miafarpdas heevtaaaas araddfiarl phgydtplte aplsggevqr lglaralvhd
      481 pavvvlddal ssldtatear vgsalasaws grtrlliahr vstaaradlv awledgrvra
      541 lgphadlwql ddyralfaas tgpeagpdrd tgsgaeawtg rdtpphtnph aqepv
//
LOCUS       WP_457657288             599 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657288
VERSION     WP_457657288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 599)
  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 599)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..599
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62226
     Region          1..596
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mseaaprpid rhlfagflrr hrgaavavag wslleavpal asgllvaaal drgflaerpa
       61 egffwigllg aamvfralmt rtltpwlgri veplrddlvt avaagavqra aagardtaga
      121 gvarltvqve tvrslvsall rsarqlgvsl lmafvglaal sapvaaltlp pvlltlllcv
      181 prlrvlarrq rrqlraeerl tgvagetfdg irdvvacgar drvadelsar itdhrdavra
      241 vartasantl lvslgshlpl lvlllsaprl ldsgalsmge llgatsylvs gvapalrslv
      301 avlgswgvql atvlsqlsrs trearpgppg gsgsalpprt rqtprtprtp rtpltpsspd
      361 lslvnvvyay gpgaapvidg lsldipagsh ltvvgpsgag kstlttllag lagpdsgrlt
      421 lggvpvtevd rawlhravtl ipqeayvftg tvrdnlrylr pqardtdila satavgartl
      481 vdrlggldap vgldgpplss gerqlvalar ahlspasivl ldeacchldp aaeeraeraf
      541 aargttlvvv ahrissalra prvlvldger tavgtpaqll dssplyadlv ghwvsagtp
//
LOCUS       WP_457657292             312 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657292
VERSION     WP_457657292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..312
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34032
     Region          37..188
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mppdtdahaq eqahtyahar rddqpeetrr vrlsrtfded aelydrarpg yppelyddlv
       61 dlagarpgrr vleigcgtgq atvplaalgc ritaveagpr maavarrnla eaeaeaevga
      121 ededededgv gvgggsaevv taefenwplp aepfdvvlaa tafhwidpav rvsraadalr
      181 pggalavvrg qhvrggteef fvevqrcyer fdpatqpgtr ppeaddvdns dhaeevarsg
      241 rfgetvfrry awdltyttae yldvlrtysg hralpdaarn gllacvagli dgrydgrvtk
      301 rylielavsq rn
//
LOCUS       WP_457657298             194 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457657298
VERSION     WP_457657298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21436
     Region          29..187
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(37,52,90,116..117,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mtdvdsdria madaddcrtl dmmyewlepa pegfkveivs gnvylapqrd thwrntlaii
       61 rqlsarygen rllsdvridf pgplngfapd vaafaqgasr tedgrwryqd vefvaevisk
      121 ataandygvk kavyatagvp vylivdpytg twhlhtlpke deyrsvlsld fgtpvdltst
      181 vvglslatda fprd
//
LOCUS       WP_457657301             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457657301
VERSION     WP_457657301.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  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 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   3  (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   4  (residues 1 to 327)
  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 327)
  AUTHORS   Clarke,T.E., Tari,L.W. and Vogel,H.J.
  TITLE     Structural biology of bacterial iron uptake systems
  JOURNAL   Curr Top Med Chem 1 (1), 7-30 (2001)
   PUBMED   11895294
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34653
     Region          1..327
                     /region_name="FecB"
                     /note="ABC-type Fe3+-citrate transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4594"
                     /db_xref="CDD:443650"
ORIGIN      
        1 mtqrsflpra laavslttva altlaacggs ddsgsgsdsa ssggstrtve tpmgdvqvke
       61 apervvvldt aeldsaltlg vkpvgathad vtsgflnylp kdqlsgikdv gqmmtpnlea
      121 iaalkpdlil tskirhgdky delskiaptv mtentgypwk enfqlhaeal gkqteakmvt
      181 ddyanhvadv tkalggkdka aatevnmvrf vegadiriyg kknyiatila dvglgrpait
      241 dqakdgfsyd vspekidlad advvfhstyg dpkksketet tgsglwknmd avkngkvfav
      301 ddqlwiqgig ytaadkilge lhqsltk
//
LOCUS       WP_457657305             300 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces
            griseus].
ACCESSION   WP_457657305
VERSION     WP_457657305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..300
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=31968
     Region          167..251
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mrapagsryd eqgrngqggr fgwlgelavv valvvvgvlv vsiagfvvae lldagpesad
       61 selffedpva dlvvqllgia igipivllav rmlgrrpagt vssvvgrirw gwllrcaava
      121 fplmivqigl liawtwndep lgetgtgfpg wpvfllslav vlalvpfqaa aeeyvfrgwl
      181 vqvigravrt pwpaiviasl lfalahgfge lsgfllllys alwwgwlvir tggleavivm
      241 hvannllafg laagfgelas tetaadapwq amvvelvfap lycltmaria drrgvervsp
//
LOCUS       WP_457657310             286 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457657310
VERSION     WP_457657310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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
REFERENCE   2  (residues 1 to 286)
  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 10144160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31473
     Region          20..>85
                     /region_name="NT_KNTase_like"
                     /note="Nucleotidyltransferase (NT) domain of
                     Staphylococcus aureus kanamycin nucleotidyltransferase,
                     and similar proteins; cd05403"
                     /db_xref="CDD:143393"
     Site            order(43..45,48,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:143393"
     Site            order(43..45,48,55..56,58)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143393"
ORIGIN      
        1 mpharprpar tplpadalpl drriellrtt aeadprvegv llygswtlge adahsdlday
       61 vyvreedvda fdgrefverl aplklaytnm ygilavvfdd lmrgefhvep tgpgiaeiat
      121 wrdqvhlprp eaavlldrtg hltaaarela afdppepvtt aqqltdelan wtlmlahvqa
      181 rgeharahnl lhaviaplql klcrllrgst thwltpsral eadlpvadve ryatttgplt
      241 pdtlrtaaan swrwsrelaa eaaerwgirl plglheeiag alspmg
//
LOCUS       WP_457657311             261 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657311
VERSION     WP_457657311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..261
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27987
     Region          11..256
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtvhgpetee adgrplheri aadlrdgims gslapgdslp staqlkerfg aanatvqkal
       61 qllkgehlvv gragasvtvr ehrqrtirpa aymapspsge pyrwlteaan sgararstll
      121 dvaeveppad vadalglqsg gtailrhqll siddepaelv asyypldiae gtaiterrri
      181 pggtptllas fgypprlsvd rvsarvatqe qcrllrlpgd lpvlrtlrvv fsdddrpiea
      241 tvmvkaghly evqyefgpen g
//
LOCUS       WP_457657312             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657312
VERSION     WP_457657312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  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 179)
  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 179)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..179
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=18872
     Region          <27..178
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mgedevisas thylaptegg gdvwnteaas agrrgtqkiv sagevaaper vagllgvepg
       61 gqvvgrrrim yldgepcelt dtyypveiar gtglaataki rggavrllae lghvgvraqe
      121 dvaarmpseg eraalslead epvleltrlt ldaegrpiqa dvmvmpprgq rlryeirig
//
LOCUS       WP_457657313             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657313
VERSION     WP_457657313.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..336
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34644
     Region          26..238
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtstapraph dppagpsagp avaladvhkt ygatravdgv sltvargeff gllgpngagk
       61 ttlveimegq rradsgtvtv lgespwprnt allprlgvqt qsssffvrlt arehlvtmaa
      121 lyrcdaaaam ralasvglte qgntrvddls ggqrqrlaia salvhdpeli fldeptaald
      181 pqarrslwqv lrdlkgqgrt ivytthhlde aealcdrvai mvagkvaald spgrliaass
      241 pttrllvpad rltpeqarai pdvdrvteeg gsivletlaa grvlaavdei aglqgvqtrt
      301 asledvylel tgaeagagag agagtstgtg tgapqp
//
LOCUS       WP_457657319             861 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657319
VERSION     WP_457657319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 861)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..861
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89543
     Region          1..860
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mtiwktslrn flahkgrmal savavllsva fvcgtlvftd tmnttfdklf tisspdvtvs
       61 pksaaddgeq pdngkpaslp asaiqqvqka dgveraegsa fsmavtvvdr dnknmgsdtg
      121 aptiasnwte ndlrsmeits ghaprgptev mvdadtakkh klaigdelrt iaatgdlrak
      181 isgiasftvt npgaavvyld tataqkhllg apdvfnqilv tagsgvsdaq lkknvaaalg
      241 dttayklqtq qeaadankne mgafldvmky amlgfagial lvgiflivnt fsmlvaqrtr
      301 eiglmraigs srkqvnrsvl veavllgivg svlgvaagvg lavglmklmg avgmelstrd
      361 ltvawttpai gltlgvivtv laayiparra gkvspmaalr dagtpadgrs grvragiglv
      421 ltaaggaalw tttqadkate gsmflalgvl ltligfivig pllagvvvrg lsvvvlrlfg
      481 pvgrlaerna lrnprrtgat gaalmiglal vaclsvvgss mvasateeld ksvgadfivq
      541 dsgagrpivp qaaealkavp glehltsytf vkakittpdg tteddgitaa dptyqqdvrr
      601 talsgdlska ygenamsvge dyaekhgvev gdtltvafta ggtaklkvaa itsddtnidr
      661 gamytnltta asyvpadkmp qnvamfgkae egkekeayaa lksavaeypv ykvqnqadfk
      721 edlknqigql lnivygllal aiivavlgvv ntlalsvver treiglmrai glsrrqlrrm
      781 irlesvvial fgallglglg mgwgtaaqkl laleglevle ipwptiltvf acsalvglfa
      841 alvpafragr mnvlnaiatd g
//
LOCUS       WP_457657321             180 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657321
VERSION     WP_457657321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..180
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19516
     Region          41..167
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mitmtgkrat eakkagrkdk datpprprgf gltpngygcl srqfpstprg arlarrtvvr
       61 qlgewgfgpm sdascsvalv vaelaanavc hgrlrgrnfh vwvdyelpaa rfrievsdal
      121 lgrtpeapal ppddqesgrg lflveclatr wgweprnpig ktvwaevaad ppadavreqv
//
LOCUS       WP_457657323             420 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces griseus].
ACCESSION   WP_457657323
VERSION     WP_457657323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Manikandan,P. and Nagini,S.
  TITLE     Cytochrome P450 Structure, Function and Clinical Significance: A
            Review
  JOURNAL   Curr Drug Targets 19 (1), 38-54 (2018)
   PUBMED   28124606
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Guengerich,F.P., Waterman,M.R. and Egli,M.
  TITLE     Recent Structural Insights into Cytochrome P450 Function
  JOURNAL   Trends Pharmacol Sci 37 (8), 625-640 (2016)
   PUBMED   27267697
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Pochapsky,T.C., Kazanis,S. and Dang,M.
  TITLE     Conformational plasticity and structure/function relationships in
            cytochromes P450
  JOURNAL   Antioxid Redox Signal 13 (8), 1273-1296 (2010)
   PUBMED   20446763
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   5  (residues 1 to 420)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Degtyarenko,K.N. and Archakov,A.I.
  TITLE     Molecular evolution of P450 superfamily and P450-containing
            monooxygenase systems
  JOURNAL   FEBS Lett 332 (1-2), 1-8 (1993)
   PUBMED   8405421
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Nelson,D.R., Kamataki,T., Waxman,D.J., Guengerich,F.P.,
            Estabrook,R.W., Feyereisen,R., Gonzalez,F.J., Coon,M.J.,
            Gunsalus,I.C., Gotoh,O. et al.
  TITLE     The P450 superfamily: update on new sequences, gene mapping,
            accession numbers, early trivial names of enzymes, and nomenclature
  JOURNAL   DNA Cell Biol 12 (1), 1-51 (1993)
   PUBMED   7678494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15334917
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..420
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45695
     Region          46..415
                     /region_name="CYP_unk"
                     /note="unknown subfamily of actinobacterial cytochrome
                     P450s; cd20623"
                     /db_xref="CDD:410716"
     Site            order(115,119,126,170,250..251,254..255,258..259,262,295,
                     305,307,330,354..356,360..364,369..370)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410716"
     Site            order(193..194,250,253..254,258,303..306)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410716"
ORIGIN      
        1 mstsspsfdt gagtgcpvap gavrlagasy qqtptelyrs lrrehgavap vlldgdvpaw
       61 lvlgyaelsy vtshdelfar dsrrwnqwds ippdwpllpy vgyqpsvlft egdehrrrag
      121 vitealegid qfelardcrr iadqliaefa gsgraelmss yihalpmrav vqmcgmpvsg
      181 adtqqlvddl risldadegd dpvaaygrvg erlrqlvkdk radpgpdvts rmvthpagla
      241 deeivqdlis viaaaqqpta nwicnalrll ltderfavnv sggrlsvgea lnevlwldtp
      301 tqnfigrwav rdtqlggrhi ragdclvlgi aaantdpeiw pesyvgaens ahlsfssgeh
      361 rcpypaplla dvmartavet lleqlpdlml avesaelswr psiwmrglsa lpvqfspmaq
//
LOCUS       WP_457657332             588 aa            linear   BCT 27-JAN-2026
DEFINITION  dolichyl-phosphate-mannose--protein mannosyltransferase
            [Streptomyces griseus].
ACCESSION   WP_457657332
VERSION     WP_457657332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11449133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..588
                     /product="dolichyl-phosphate-mannose--protein
                     mannosyltransferase"
                     /EC_number="2.4.1.109"
                     /GO_function="GO:0004169 -
                     dolichyl-phosphate-mannose-protein mannosyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=66568
     Region          73..588
                     /region_name="PMT1"
                     /note="Dolichyl-phosphate-mannose--protein O-mannosyl
                     transferase [Posttranslational modification, protein
                     turnover, chaperones]; COG1928"
                     /db_xref="CDD:441531"
ORIGIN      
        1 mtstasetqr gqdagdplge qptswqrrlr rfghvprpet slrdrldppy trpgrqmwsv
       61 laipphvadl lvrwsgwggp llvtlvagll rfwkldqpha vifdetyyak dawalvnqgy
      121 egswpkdvdk qilndpssvp iptdpgyvvh ppvgkwiigf geqligftpf gwrfmvavlg
      181 tlsvlllcri grrlfrstfl gclaglllav dglhfvmsrt alldlivmff vlaafgclvv
      241 drdharrrls dalpmddegv lrpdariaet lrlgrrpwrl aagvmlglaf atkwnglyvl
      301 aafglmtvlw dvgarrtaga vhpyqavlrr dlvpaffstv pvaivtylvs wtgwivtdkg
      361 yyrnwaateg knsswnwlpd wlrslwhyen qvydfhvglt sghtyesnpw swlvlgrpvs
      421 yfyeeqtgck esstgkcaae vlaigtpllw wlacfalayv vwrwffrrdw ragaiacgvv
      481 agwlpwffyq ertiflfyav vfvpflclav tmmlgaivgp atntgtrael gltthdptge
      541 rrrtvgaiav gvlvlliiwn fiyfwplytg tqipedlwrd rmwldtwv
//
LOCUS       WP_457657335             215 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-70 family RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457657335
VERSION     WP_457657335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Davis,M.C., Kesthely,C.A., Franklin,E.A. and MacLellan,S.R.
  TITLE     The essential activities of the bacterial sigma factor
  JOURNAL   Can J Microbiol 63 (2), 89-99 (2017)
   PUBMED   28117604
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Campbell,E.A., Westblade,L.F. and Darst,S.A.
  TITLE     Regulation of bacterial RNA polymerase sigma factor activity: a
            structural perspective
  JOURNAL   Curr Opin Microbiol 11 (2), 121-127 (2008)
   PUBMED   18375176
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Mooney,R.A., Darst,S.A. and Landick,R.
  TITLE     Sigma and RNA polymerase: an on-again, off-again relationship?
  JOURNAL   Mol Cell 20 (3), 335-345 (2005)
   PUBMED   16285916
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Wosten,M.M.
  TITLE     Eubacterial sigma-factors
  JOURNAL   FEMS Microbiol Rev 22 (3), 127-150 (1998)
   PUBMED   9818380
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Helmann,J.D. and Chamberlin,M.J.
  TITLE     Structure and function of bacterial sigma factors
  JOURNAL   Annu Rev Biochem 57, 839-872 (1988)
   PUBMED   3052291
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11495650
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..215
                     /product="sigma-70 family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23928
     Region          64..193
                     /region_name="sigma70-ECF"
                     /note="RNA polymerase sigma factor, sigma-70 family;
                     TIGR02937"
                     /db_xref="CDD:274357"
ORIGIN      
        1 mhnapdirgp adphhlsstp qgsvpragel pepkprrrlt arqvdeltrl kpflenmtrq
       61 armeylmddl vqnaalqlir awtnpdfvld rqdggrafar kvmrnviada arandrnlss
      121 pmgdipdeva vepdegehvr ddrlrsigtf lrdnlpekly pvghlaiieg ltqgeiartl
      181 gidrhtvgrr lkkvgealep hkatvhdevl gdvts
//
LOCUS       WP_457657337             798 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657337
VERSION     WP_457657337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..798
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86563
     Region          121..>354
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mgrrprpgsf wrraaavlgv lmvgagavvi lrsrptgdvd pfgalvgvvg avigvaglll
       61 pfwehrqsrr egavralvra veghedqqyr nilgpgsafl pvrfrftaap dgspdaagse
      121 ewrtvvdryl glpgpvrrla vtggpgtgks llareltral aarhdeaagd gvpvllslss
      181 wdgppdredp rsegfhlafr rwavqqaaqt ygqpsaqvee altdkavlvl dgldeldpag
      241 aearpraaal lrylavnrdc frhvvvtcrs dvyerfegpa plagagrael lpvppdmald
      301 ylksrsewsh sglterwdgv ldemrvspgg plaralstpw rltmtanafh vrgeggagwl
      361 rdpselvtrw grdvlweryr aesedfaaeh glpgrlwslf speerlrsae dspaadamss
      421 eaeehllslf vpsvvaehph dpgrypaerv sawltllsth rgvdrfagpr hlsliadlra
      481 dltphqlwpl ggrrlvrtlh gslytlfall vaglavvalr dpleialcfp vvvaagfsah
      541 lawsdradid pasrirmsgr agglldlymr tvgmpmlgvc sggmfgfivs anltraplpd
      601 vpttvwvata agallgipll qnrsaetytt vrgslpgqrh kiflicaals grlplrlgrf
      661 ldwaheggll rvdghayrfr hdafeqylwr shwrpeilpp claaadaalr tgeaaadrpa
      721 ragrrmleql dtldrnrvdl yatcmtsigm agarartalr awadhlatga vdpeaeaalr
      781 dragqavrsf heaaarag
//
LOCUS       WP_457657340             290 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457657340
VERSION     WP_457657340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..290
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31472
     Region          44..166
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mqrtqrrltl llaaalsavl tmlavapaga agkpsrsnsa strvifvhgh spfgkhdctk
       61 tfkdarkhfs nkkwkgnllt fgyytnnkkc sanvtgsret pikdvakkfa nyvsknytkk
      121 gikvdvvahs mgglvvraal hythqrakgf paklyiedvv tlgtphagit ksratlcgka
      181 rqctdmkpgs sflkalgskm psttkngnms tdwttvssyn dgtvsessgi agtadhevqy
      241 kaginhgqli tkttgsyngr ikystkwtkf hkrvspveqa rlavywhatt
//
LOCUS       WP_457657341             401 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657341
VERSION     WP_457657341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40371
     Region          10..371
                     /region_name="MFS_FsR"
                     /note="Fosmidomycin resistance protein of the Major
                     Facilitator Superfamily of transporters; cd17478"
                     /db_xref="CDD:341031"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,133,
                     136..137,140,210,213..214,217..219,222,250,254,302..303,
                     307,311,326,329..330,333..334,337)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341031"
ORIGIN      
        1 mrrntpivll svghacvdvy qgcvaalvpf fiaeraysla vasgivlaas llssvaqpvf
       61 gvltdrwamp wllpvstllg gagialsgls gsypltlafv alsgigvaay hpesarvari
      121 aaggshramg wfsmggtvgf alaplmvava maagglrwtp llvlpalaga alclpvvrvl
      181 qrrqtadgsg ttpaagsddv asfvklslav vfrsiafigl stfialyarq rlgggtavgt
      241 aaltvlylgs tvgsvlggsl aarwdrvvva rwaylisava vagvvwvpgp afylfvalts
      301 aglyvpfslq vtlgqdylps rvgtasgitl gltvsiggla gpavgslada tslrtalapl
      361 almpllswlf frslpepgvp raelaegaaa pssgggavka g
//
LOCUS       WP_457657351             367 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657351
VERSION     WP_457657351.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     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 367)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..367
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..367
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39646
     Region          53..119
                     /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 mssrtdtdet raaearvtdt cltgprptea hvtaartgea itasalhaaa tgadtfpgvl
       61 realnrrgls lervserlrv rgitisqatl sswqrgrsqp erarslrave vleeilelpa
      121 galrsllgpr rprgrttppd aegaalqilg edsvvekalg arfrhfnqet sslmvhdivr
      181 vgetgtlsgi sttnvlrasr agadraifvl sfddeaaepv dirvtcgrlv eatylkglks
      241 lvleihfgre lakldttvvs yavdvspsdt pathyerwsr tnlheylqqv ffhpaalptd
      301 chryvrekvg apprgrrrip lsdahnvhvl tsrckpgvhg vewdygrgtg gteaagtgtd
      361 gtgdrpg
//
LOCUS       WP_457657344             148 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657344
VERSION     WP_457657344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..148
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16312
     Region          <56..136
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mttttsaqpg edtyevdtdp dridldrvhh wlstdafwal grsrdlvers lrgslnfgvy
       61 dgggtqvaya rvvtdhatfa wlcdvyvdpa hrgrglgvrl atavrdhlap yelkrillat
      121 ldahelyakv gfvpvsdpkm lmilsptt
//
LOCUS       WP_457657357             296 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657357
VERSION     WP_457657357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  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
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31967
     Region          8..292
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 masyatgfge egsawiaelp slatdmldhw qlrrdgavrs gqaslvlpvl rhdgtravlr
       61 lqmpreetaa aliglrtwng dgtvrlldhd pasgsmller ldgartlasv gdddkamgil
      121 aglharlval papqglrglg dvaaemleqa pqavaqltdp adrrllrgwa savaeladdp
      181 gdrllhwdlh ydnvlaaqre pwlaidpepl agdpgfdlwp aldsrwddvv vapgeplrvv
      241 rrrfdlltea lgldraraag wtlgrllqna lwdiedgetr lapsavvmae algnhr
//
LOCUS       WP_457657355             200 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457657355
VERSION     WP_457657355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..200
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21937
     Region          14..197
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtaepttahs srwpvppqdg ytvddlftlp dlpphtelid gslvfvspqr dfhstmidll
       61 mtglrstapp evkarremtv vldrrnapep disvvrteav tgldvtryqa advllavevv
      121 spdseardhe akphkyatag iphfwlvemt gtdqrpvvrv yeldpvtkay altgihhdrl
      181 ktgvpfpvdi disaealaal
//
LOCUS       WP_457657349             164 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657349
VERSION     WP_457657349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..164
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18274
     Region          1..138
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mlihprpfdh pdavklndqv qleyavrygd egdvtpldps mfvpphglyl laydeqerpv
       61 atggwrtqnr nadgyedgda eikrmfvipe grgrglarrm laaleedara agrtrmvlet
      121 gdqqpeaval ytscgytvce vkfghyreyd ssicmakplr qpga
//
LOCUS       WP_457657342             286 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657342
VERSION     WP_457657342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 286)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30445
     Region          50..141
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          204..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvrpgssval siicqmmpni rhaaagqaaa rpaavggata vrhspvaptr trrlapggsi
       61 dahrhddhqi vyagrgvltv ttdagswvap gtraiwvpag vvhahrayge ldlhlvglpv
      121 tenplgldap tvlavspllr elliaytrae ddgesperar lravlldqlr asdaqqplhl
      181 ptptapplrd lcailradpg dgrtlaelgr qvgagdrtls rlfrsdlgmt fpqwrtqlrl
      241 hhalillter tpvtavahqc gwssasafie vfrrtfghtp gsypag
//
LOCUS       WP_457657358             141 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces griseus].
ACCESSION   WP_457657358
VERSION     WP_457657358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..141
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15448
     Region          23..140
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtrepaagpr fdlpepdaft rpywdaaaeg rllirrcagc grahhypref cpycwseevg
       61 werasgnatl ytwsvvhrnd lppfggrvpy vaavvdlaeg prmmteivec ahgalrvgmr
      121 ltvafrgage dggeavavfr p
//
LOCUS       WP_457657359            1209 aa            linear   BCT 27-JAN-2026
DEFINITION  CHAT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657359
VERSION     WP_457657359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1209
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=127536
     Region          504..1200
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 mrrsgevtgw aflaevdgvr haglavgqag lgpftgagpg gslatlacvr glptltslda
       61 lplvgpmdar wcvhrdaegv vsvfgpgglq laydlalelp pgwlesvtga gslvlvvshv
      121 lpssddmaav ltyetqhgmv cagrvrfgpp gdetagpppf ahvldpvsdl lelvlhvrdr
      181 vlsldvarrr arglertrrs lgeghwltag allellvaqa arnrgpsadl rylywrlvae
      241 vaeecgvdaa wreaalrtve naapvlaerc erpvfedade lagrlierle gapggtsgva
      301 pdsasgsspd laaallaaar lrlavrgped lggdayagae gsvraaqlaa dlyrsplyrp
      361 wsggawplrf darlraeire llvraaesdd revgpgsalr prilaalaqv taeeghggee
      421 erageeqsgg geqggggeey ggvdratara afdalfavra pgppdltvfl lravddvpds
      481 fvdviranvf gsdvpaflaa hggavaartv dqainlarer adrpllraal dwadrspllp
      541 gpahrrqlie arlhalpddp tdcpgpgplp dpdsfpagwt paqrsaallh laahardrrq
      601 palgaallrq arpedgagvr llaadlhrla veqgepvagp vpfpwghsty aalsyaslnq
      661 qdlaqacllp vlhdlprlrg edlrnavyai ivdlpnfdts gapalgevlr dlvhaavwql
      721 tveiesmpva lmlglhqagk gpeagawrri dgaitrpahi enyvgklral espsavggat
      781 anlldaldgd hrsggegaea gdgrdefvrn lrrrissfid delrgrsaaf vddehvwart
      841 gellgdrtvl ltwflptavn gaavllavtr egsaitvqlg egesegggyd dgggpegaav
      901 sadrhpvadl veavraever dplfgevtpe grrlltghel plpdgdqlaa wrtrgkdrll
      961 lwphgalhyl pvalcsaggr tiaddwtvvt vagleallpa tgpvrprrta vlasgsggvh
     1021 yglpaepale ehartvaaav gahaltgpaa traallaelt tadvvhlavh gtmdqdapwl
     1081 hclyltpded ddgrlfahdf leldlsgvrl vtlaacesal grfdradnvr gvpaalitag
     1141 vqavvgclwa vrpepatyff qhlhrragla dapeqafraa qtatrarypa yrdwgaftyl
     1201 lgrsegata
//
LOCUS       WP_457657361             230 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxine/pyridoxamine 5'-phosphate oxidase [Streptomyces
            griseus].
ACCESSION   WP_457657361
VERSION     WP_457657361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liang,J., Han,Q., Tan,Y., Ding,H. and Li,J.
  TITLE     Current Advances on Structure-Function Relationships of Pyridoxal
            5'-Phosphate-Dependent Enzymes
  JOURNAL   Front Mol Biosci 6, 4 (2019)
   PUBMED   30891451
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Safo,M.K., Musayev,F.N. and Schirch,V.
  TITLE     Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a
            tetragonal crystal form: insights into the mechanistic pathway of
            the enzyme
  JOURNAL   Acta Crystallogr D Biol Crystallogr 61 (Pt 5), 599-604 (2005)
   PUBMED   15858270
REFERENCE   3  (residues 1 to 230)
  AUTHORS   di Salvo,M.L., Ko,T.P., Musayev,F.N., Raboni,S., Schirch,V. and
            Safo,M.K.
  TITLE     Active site structure and stereospecificity of Escherichia coli
            pyridoxine-5'-phosphate oxidase
  JOURNAL   J Mol Biol 315 (3), 385-397 (2002)
   PUBMED   11786019
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..230
                     /product="pyridoxine/pyridoxamine 5'-phosphate oxidase"
                     /EC_number="1.4.3.5"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_component="GO:0032991 - protein-containing complex
                     [Evidence IEA]"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:1902444 - riboflavin binding [Evidence
                     IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0036001 - 'de novo' pyridoxal 5'-phosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0042823 - pyridoxal phosphate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25015
     Region          27..230
                     /region_name="PdxH"
                     /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase
                     [Coenzyme transport and metabolism]; COG0259"
                     /db_xref="CDD:440029"
ORIGIN      
        1 mndntaapaq ppspgfrdll haqrvwdvel pafdpadapp dpvrlfhtwf aeavaagqpe
       61 phamslatad aeglpdvrtl llhgadergf hfashatsak ghqlaartha algfywpaqg
      121 rqvrvrgpvl rctpaeshad lharstgala aaltgaqsev vgsvaelhra adaawerara
      181 epnteaptwt ryvvepaeae ffqgdarrrh irlryrrtgg gdwtrellwp
//
LOCUS       WP_457657362             408 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457657362
VERSION     WP_457657362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..408
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42032
     Region          1..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdaaftaeqh eirrtlrell araagpgaip aavgaaegyd pvlwrrlard lglpglalae
       61 eyggagctat elalaceetg rallpsplla taalaaplia algtpdqraa llpriaegal
      121 taalavpggs latalgltgd nrdgawaggg raggiqaray gsddsrgegg wrlygeaerv
      181 ldghsaglll vaahtggypr srtllflvph dagglvrtrl taldetrpla rvelrdtpat
      241 llgaddtadt tealaavgrt aaailaaeav gtaasalert veyvktreqf gravgsfqav
      301 khrladlyvr veaarsaayh aarepeagpl alaqaleaar ittgeavqlh ggigftwehe
      361 ahrhlkraag dellfgpvhr lrdhaaqrag lfepgrmpla aapgagvr
//
LOCUS       WP_457657366             258 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657366
VERSION     WP_457657366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..258
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26911
     Region          3..234
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 malriereaa agvalvtldr paklnaidle tsgeltslwr glrfdeavra vvltgagtra
       61 fctgidrdve vpqppspyav ddpllrigpk andlwkpvia avegmacgga fyllgeaefv
      121 vasreatffd phttygmvsa yeamamaqrm pygevarmal mgtaervsae rayavglvse
      181 vtepggavaa alraaaviag cpteavqgtv ravwaakeaa rtqamaqapa lialgnlppe
      241 rqaelfgarg gggeprvr
//
LOCUS       WP_457657372             349 aa            linear   BCT 27-JAN-2026
DEFINITION  taurine ABC transporter substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457657372
VERSION     WP_457657372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 349)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
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   ter Beek,J., 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 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   6  (residues 1 to 349)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (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
REFERENCE   8  (residues 1 to 349)
  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 10008604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..349
                     /product="taurine ABC transporter substrate-binding
                     protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0015411 - ABC-type taurine transporter
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0030977 - taurine binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015734 - taurine transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36236
     Region          11..349
                     /region_name="TauA"
                     /note="ABC-type taurine transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4521"
                     /db_xref="CDD:443595"
ORIGIN      
        1 mprsrgllri tslaaalgsl lvmtacgqgg ggdggdggkt iriayqafps gdlivkekgw
       61 lekalpgydv kwtkfdsgas intafvagsv dlaaigsspv arglsaplni pyevtwvldv
      121 agdnealvar dgskissvkd legkkvatpf sstshyslla aldkagvdas kvqlldlepq
      181 dilaawtrgd idatyvwlpt leelkktgkv ivssrelaag gkptldpgva strflkahpd
      241 vlpawrkaqa qaldlihddp daasaavgkq lgispaeags qlkqgiflkp aeqadakwlg
      301 ttgkvgglad nlrsaaqflv dqkqidaapd iedlrkavhv eglsdavsp
//
LOCUS       WP_457657376             226 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces griseus].
ACCESSION   WP_457657376
VERSION     WP_457657376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..226
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=24812
     Region          10..202
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mthdapeltl peelillala pdrgkptcra rdlaygtaga vlaelelqgr ireergrvqv
       61 vnpldpadpi laamlrtldp pakgrrrpgi rarrwvgdyd ryvqekylds lversvvsre
      121 trrflgvfpy hrhfpgvpdl srgvldrfaa aeaagypdhr drvlaslvsa iglageltrl
      181 grtgrtvmkt mrrsewtava vrynvkqhes gngwsghsgg gggdgd
//
LOCUS       WP_457657377             664 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457657377
VERSION     WP_457657377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..664
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74642
     Region          1..519
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mnittefpye ttredvripl pdgtrlyari wrpvtdepvp alleylpyrl sdwtaprdwq
       61 rhpwyaghgy vsvrvdvrgh gnseglpgde ydaqeledgv avihwlaqqe wcsgrvgmfg
      121 iswggfnslq iaalapeplk aivtvcsadd rydndvhymg gsvlavdmha waatmlafvc
      181 rppdpaqagd dwkemwlkrl eavdpfihtw lahqsrdayw khgsvcedyg aikanvlavg
      241 gwhdpyrdtv lrlaehldpg qvrgiigpws hqypdrglpp gpaigflqet lrwwdqhlkg
      301 ketgvmrepl lrswisgshp patvyetlpg rwvgdaswps envnpvayal qggerivasp
      361 qqtgldagrf fpfgneadlp pdqrdedaks vsfefpvtda pieilgrprv klrlrmdvpr
      421 gqaiarlcdv apdgsstlvt rgvlnlaarh grdrtddwtp getedvvfdl ngightfppg
      481 hririaisss ywpwiwpqag sagftldadg sfvelpvrrh tedpaitfge peqseplgvv
      541 ypvtleeprp erlvvrdvak gewrlevdpr yggtrvypdg leftedalet ytvqqddpls
      601 artrsdwrir lhrpetawdv eietrseiaa ddqdfitsde vickdggevv fhrtwekrip
      661 rtag
//
LOCUS       WP_457657379             283 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457657379
VERSION     WP_457657379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..283
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28841
     Region          6..266
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mltppayalv atdldgtllr pddtvsarsr aalaraaaag arhlivtgrp vpgirallad
       61 laytglvvcg qgtqlyeags grllrsapld reaadtalgk ieaevgavfa avdqdgvdgv
      121 tlieagyrmp nptlpaqrva sraalwarpv ikvlvrhpdl gddeltaaar aavgelatvt
      181 magpgtvela prgvdkgtgl aaaaelleig aertiafgdm pndlpmfags gyrvamgnah
      241 pelraaadev tlsnaedgva vvlerlfgtq dapdsgaarr agp
//
LOCUS       WP_457657381             277 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657381
VERSION     WP_457657381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30671
     Region          14..75
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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          102..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtfqpeqlag sradlgallr dlrkraglsq vrlaqrctms rtklsnvetg ragptlvdve
       61 lilraleatp aetaevmsla rltrtdwqnk rtsrrrglek rqaelagles eatvlryflp
      121 amvtgllptp eyasaglsgs pgdksvtlar klerqavlyd ttksftfllt eqavrwpllh
      181 ragmavqvdr lislshlpnv rigllptdsa tcrgpmntft vydhrlttve tftgrivfqd
      241 ardiaehlgv fgtyehlalf gdaarnllth wathfrs
//
LOCUS       WP_457657384             391 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657384
VERSION     WP_457657384.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 391)
  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 391)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=41804
     Region          30..>148
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          145..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtmspsvpdp grlpparfai drwtwreiah llanlplavv gfvytvlvia vgvglsvtvi
       61 glpllvaglq garllgrler rrargmlgvr veepsplarg hrdqgffarl waglkdpvgw
      121 rallygfirl pwgvltfavt lvslfvlwpv lpfiargltt vdramvrgll spsdelerri
      181 aelesdrgvv vdtaaadlrr ierdlhdgaq arlvalamgl glakekltdd peaaarmvde
      241 ahgeikvalq elrdlargih pavltdrgld aalsaiasrc tvpvkvtvgl rnrpaeaieg
      301 iayftvsell qnvskhsgar sasvdvwrsa drlmlqvtdd ggggartdgg gtglaglaer
      361 ldavdgvlvl dspeggpttv taelpwrdra a
//
LOCUS       WP_457657385             235 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit B [Streptomyces griseus].
ACCESSION   WP_457657385
VERSION     WP_457657385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Friedrich,T. and Weiss,H.
  TITLE     Modular evolution of the respiratory NADH:ubiquinone oxidoreductase
            and the origin of its modules
  JOURNAL   J Theor Biol 187 (4), 529-540 (1997)
   PUBMED   9299297
REFERENCE   4  (residues 1 to 235)
  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 10001254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..235
                     /product="NADH-quinone oxidoreductase subunit B"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /calculated_mol_wt=24834
     Region          49..189
                     /region_name="NuoB"
                     /note="NADH:ubiquinone oxidoreductase 20 kD subunit (chain
                     B) or related Fe-S oxidoreductase [Energy production and
                     conversion]; COG0377"
                     /db_xref="CDD:440146"
ORIGIN      
        1 mgltsrptpa pesqqpapps pppsdpvllp epkrlgvlsr lapepmkvvl nwgrryslwv
       61 fnfglaccai efiaasmarh dfirlgvipf apgprqadlm ivsgtvtdkm apavkrlyeq
      121 mpepkyvisf gacsncggpy wdsysvtkgv dqiipvdvyv pgcpprpeal lqgilklqek
      181 iareslaery asgatggggp stealrsglv aaptpapapa papapssrpd gegrr
//
LOCUS       WP_457657388             179 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces griseus].
ACCESSION   WP_457657388
VERSION     WP_457657388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..179
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18326
     Region          3..178
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtttvyarve splgelllvg eetavadgpd aagaggvrlr slsmpgqkgg vvvqdgwkha
       61 peafaevarq leayfagrst rfdvpvaega gtefqrrvwa vlesipygst vsygqvaaqv
      121 gasgagvrav gtaigrnpll vlrpchrvig adgalrgyag glerkklllg legvealag
//
LOCUS       WP_457657387             228 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Streptomyces
            griseus].
ACCESSION   WP_457657387
VERSION     WP_457657387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 228)
  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   5  (residues 1 to 228)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..228
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=23421
     Region          30..190
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 mtlhtappll tataaatgdh pgflspsgve iafllvglat lgaavitvtt kqlvhaalwl
       61 vvalgglave yllltaefia wvqvliyvgs ivvlllfglm ltrapigrsp dadsgnrwva
      121 lgvaaaaaat lvwvvadafr ttwidldgpa qgstevtgaf lfrnwvlpfe alsvlllaal
      181 vgaivlsrkr dtdtdtgtdt gtgtdttprp gpsgtpgtta rpgkgekr
//
LOCUS       WP_457657389             470 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces griseus].
ACCESSION   WP_457657389
VERSION     WP_457657389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..470
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=52154
     Region          153..449
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpltydvriy sietrrdrpk phrvrwlvgp qkhsksytvk aqadgrrsel mtalrrgdqf
       61 dvetglpaae lriqgsrvtw yehtrayvdr rwdrlpaksr rndadslati tpalmksvag
      121 rpspgalrta lygwaynrsr weqeppaeva svlrwvekns lpiaaledpa tlrlaldals
      181 tlrdgspaag starrkracl sdvlglaver rhfsipvnpl stvkwtapks veevdpasva
      241 nprqirells avrhqgerga hleaffgcly yalmrpaeat glteaqcylp regwgditlr
      301 ggivhaghaw tdddrahqar hlkaraerds rvvpippvfv amlrshierf gtapdgrlfr
      361 tsrggviqdt gygevlaaar aealtphefe splarraydw raagvsllvf lgvdpmevar
      421 raghsvavll rvyakvlara qeranqkiea glrewdgeap spgghlgdtr
//
LOCUS       WP_457657406             262 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657406
VERSION     WP_457657406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..262
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28748
     Region          3..252
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mapkwrelad rlaeqiksge lppgrrlphi rdlvdagegs kstvhaayka leaeglvtss
       61 rghgtvvrsr aplkrlgiar ydkakwrdgd evafvadria sgrahkrgeq tqnvsrvpap
      121 pfvatahglp egsevymrar liregdrpth tltsyyrpeh vegtqlvdpt pgpagkgggy
      181 rvlydagyei dhmreqlfar aaasdesell qlmpgewvve lhrttftadg tvvefaigih
      241 aasrfaweyd fkvpdsaege aq
//
LOCUS       WP_457657408             151 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces griseus].
ACCESSION   WP_457657408
VERSION     WP_457657408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..151
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16112
     Region          19..145
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 msdsgslllp vvdedgapfw eyaargelrv qacaapacge lrfpprpccp hcgsfdsewr
       61 ltsgrgrlws yviphppllp gyaeqapyna vlveladapr irlagnvvas pdaplnsvdp
      121 arlrigapvr avfcpagpgg dvtlvrwlle r
//
LOCUS       WP_457657409             206 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657409
VERSION     WP_457657409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..206
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22148
     Region          2..203
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 melagtirhd gdggvlddlg tlegaarwir rqtgllstla pagepigaee pvrapefvvd
       61 eelrdavigv rravralfar vvspappsra dahrlmpage alallnaaaa repvapqlrw
      121 paegpptagl lsaeadprvr lvaalardav dflsgperer lrachaprcv ryfvrshgrq
      181 ewckpscgnr arvarhyert raadps
//
LOCUS       WP_457657410             251 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Streptomyces griseus].
ACCESSION   WP_457657410
VERSION     WP_457657410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 251)
  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..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25533
     Region          <98..249
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msavvallat glaaspavaa paasaaegka tvgadwakqs itftaapgqv ndlhvvpmdq
       61 gdgvrrigfr davplrpgdh ctyltpgdet yvvcelptds arpdridvfl gdgddeiats
      121 dpgvatvsgg pgddmlhaht ahtvrgdegd dmvmgrvvld ggdgddhlma vdgdqwlwgg
      181 rgddmieayd gddvvyagpg ddhvmggdgd dllfggsgdd mlygedgndl ivggsgkdtv
      241 eggpgrnitl p
//
LOCUS       WP_457657412             483 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657412
VERSION     WP_457657412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..483
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49433
     Region          12..482
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mttmtetsar frefkmpdvg eglteaeilk wfvqpgdtvt dgqvvcevet akaavelpip
       61 fdgvvhelrf pegttvdvgq viiaidvapg sgdapapaaa apaqapaaep eaeaepkgrt
      121 pvlvgygvae sstkrrprkg asatpeaaav aaavqaelng haapaapaap aaavpaqggr
      181 plakppvrkl akdlgidlat vvptgkdgii tredvhaaaa psaapaaapa papaavapav
      241 aeapavvsds aretripvkg vrkaiaqamv gsaftaphvt efitvdvtrt mklvaelked
      301 kdmagvrvnp llviakallv aikrnpevna awdeanqeiv qkhyvnlgia aatprglivp
      361 nikdahdktl pqlaaalgel vttardgkts paamaggtvt itnvgvfgvd tgtpilnsge
      421 sailavgaik lqpwvhkgkv kprqvttlal sfdhrlvdge lgskvladva aileqpkrli
      481 twa
//
LOCUS       WP_457657414             207 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657414
VERSION     WP_457657414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..207
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22988
     Region          1..83
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          90..172
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 msirhgllal lergprygsr lrtefesrtg stwplnvgqv yttlsrlerd gmivqdgtdd
       61 aghdlyaitd dgraelrtwf etpvdrtspp rdelaiklam avgapgvdir dviqsqrhht
      121 lqamqdytrl kaqaladipa nrdevawllv veqlifqaea earwldhces rlvrlaeaaa
      181 vepteepgpa atrgparsva grirsrr
//
LOCUS       WP_457657417             584 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Streptomyces griseus].
ACCESSION   WP_457657417
VERSION     WP_457657417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..584
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=58189
     Region          170..572
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mtgpdgprra sgsdggdfrp agggsdlare eeeraveqal alvggttlrp grgrdipgtp
       61 gtpgtprasg asggdlssgp sgspgndrrg ssgptgngpd qsastdsast dsapvggspg
      121 gngpsaggps ggarataqas gsdqrhrpgr ssseapapna epatpkappl swdraravat
      181 ragrtgppat irlpldralg hvlaeplgal tdlpsfdtsa mdgwavagpg pwayeagagl
      241 lagrgpdtpl pdgnavriat garvppdtta virsehahpd eakgllharr svvtgqdirp
      301 rgqecrsgeq lvpagtvvtp avlglaaaag ydalpavprp rvdilvlgde llaaglphdg
      361 lirdalgpml gpwlralgae vagpvrlgdd agalrdalas sdadlivttg gtasgpvdhv
      421 hpvldalgae llvdgvavrp ghpmllarlp apgqmkgqae gpylvglpgn plaavsgllt
      481 laepllagva grpaqdayra lvhaevhghp hdtrlvpvvh ragraggrdh vaplryngpa
      541 mlrgiaaadg lavvppggvr sgteveildl pwapatpwte gcft
//
LOCUS       WP_457657416             378 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces griseus].
ACCESSION   WP_457657416
VERSION     WP_457657416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..378
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40561
     Region          63..357
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mgpgdavdgr vfhvklpghd amarradelv vptrvmlprr valgparqva krllmallvl
       61 aatvlivwld rsgyndnadg kvdlldavyy atvtlsttgy gditpysdga rlinvvlvtp
      121 lrvmfliilv gttlevlter tredfrlkrw rsnlrdhtvv vgfgtkgrsa iltlcatgls
      181 kdqivivdpa skvieaanae gftgvlgdat rsdvllrael qkarqviiat qrddtavlva
      241 ltarqlnrga kivaavreee napllrqsga davitsasaa grllglsvls psagtvmedl
      301 iqqgsgldlv erpvikaevg knvretedlv vsvlrghrll gyddpqaspl qltdrvitiv
      361 rkspstssvp htsmpprp
//
LOCUS       WP_457657418             462 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457657418
VERSION     WP_457657418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..462
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47683
     Region          6..459
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 maqvlefklp dlgeglteae ivrwlvevgd vvaidqpvve vetakamvev pcpyggvvta
       61 rfgeegtelp vgaplltvav gaaegssgss pspssasssl ssspssgsgt essggsgnvl
      121 vgygtgapaa rrrrirpdrl dravaevlva eapvhegpvp vvsplvrrla rqhdidlrrl
      181 agsgpdglil radvdrairt veetaaatar vqapvaavva apngvaaasd aeriplrgvr
      241 gavadklsrs rteipdatcw vdadatelma vraamnaatg psagpkvsvl allarictaa
      301 larfpelnat vdtaareivr lpgvhlgfaa qterglvvpv vrdahtrnae sigaeiarlt
      361 elartgklsp aqltggtftl nnygvfgvdg stpiinhpea amlgvgrimp kpwvhqgela
      421 vrqvvqlslt fdhrvcdggt aggflryvad cveqpavllr tl
//
LOCUS       WP_457657421             321 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657421
VERSION     WP_457657421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10154716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=35429
     Region          <187..225
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(201..203,212,218..219,222..223)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 msdeaagvpt trndedrqdn drqdsdrtda pgpapeaqda pgapgdsgaa daaagepvga
       61 edaaprpear laravqaaeq aliefeiave tfrvevenfs rlhhqklgpm ytrldeldal
      121 iaearaartg dpederkare aravvmpmpg vdelfhdwmd tdglspeaaa mlteqpvrpp
      181 krvrpseear rlyrelarka hpdlaqdepe rqrrdefiar vnaaygrgdi ellkelvaew
      241 eagpaqpltp lseseelyar lewlsrrkel ltvlakelee gaigsmlrma pddpdqlled
      301 iaeqllgevs rreaelaelv q
//
LOCUS       WP_457657427             233 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces griseus].
ACCESSION   WP_457657427
VERSION     WP_457657427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..233
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=24827
     Region          2..233
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mttrliclpy agagagvyrr wktlstpdlt avpiqlpgre eefglpfypt feaavhgtad
       61 rvrtavgsgp fvvfghsfga alahgvtrel varggprprr livsgtvspr hrsplpisat
      121 ddaqavadlc aatgqslsgd laplldpelr tlllpalrad vallapdpar epeplpvplt
      181 airgtddalt ptgpwldwaa ytsqpfrtvd rpgghmylad dwdaawrtvr dli
//
LOCUS       WP_457657429            1050 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657429
VERSION     WP_457657429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1050)
  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 1050)
  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   3  (residues 1 to 1050)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1050)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1050
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=113456
     Region          13..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          189..1036
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mgerartgtl tkptfqilga lkgwqgeqpl rlggrlrert ltmllleanr vipvhrlvda
       61 gwddappssa ahqvrkaiae lrqnipygpe tivtdgpgyr acvtpeqvdl gryltllgqa
      121 rearargesa ttadrlhqal elwrgpvlag eggpvingas aaleeqhlga teqlfelrld
      181 agkdaeiiga lrtlvqrhpl retlrrqlml alyrtgqqae aleeygrart llaeefgidp
      241 saelsglyer ilrqspdlap trrpaavppa sapkepakta gaaggqgapg tpghtahtgy
      301 trsagtagpa aveadepntl pyglqdfsgr ateldwirda aertrgqsah ivaidgmggs
      361 gktalaaraa wqlaewypdg qlfidlrgft pgqeplspsa aheallamag vsgtelpata
      421 agraalwqsv trrrrlvvvl dnaadseqvr slipssphcl tlitsrprlv dldavewlsl
      481 dvlpeqdgie litrivgadr vdrepdavie lvrlcgrlpl airiaagrlr nrtnwtvrrl
      541 verlnddarr laelssggrs vagvlrlsyd smppeqrtgl rllslhpgrv igtedaaall
      601 gtgtedaeql mealtdahll qenrpgwytl hdlvrsfagg lsdestaped aaatrrlldh
      661 yvhtaerana tlfpervpyg dflppgrslh pgfgsrddal awldlhrddl laavevahah
      721 glprhaatlp relgfhsdir nyprlactay rravdasrql edvallrlnl tnlamhlwpl
      781 grfresvacl eearvlarel rderaeaacl gglgqnynsl gdfpaalrht eeaarmearl
      841 glvrglgssl nilssvrlrt grfieaaeaa eesikifest gethnsalgl thlalartal
      901 gdpaeaahll ttaqdlceqv hspantafvl acsadvmtll dradtaltli draralvqqa
      961 dvavrqaavm naagrvhral gepaealrhh rqardlsagi gfrfeealal dgmakahaqs
     1021 repteaadcr rradalfasm gvpegsrtlf
//
LOCUS       WP_457657430             446 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine protein kinase [Streptomyces griseus].
ACCESSION   WP_457657430
VERSION     WP_457657430.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..446
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47132
     Region          1..417
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mgevfagrye lidpigrggv gavwrawdhr rrryvaakvl qqsdahtllr fvreqalrie
       61 hphvlapasw aadddkvlft mdlvsggsla hvigdygplp prfvcllldq llsglstvha
      121 egvvhrdikp anilmeatgt grphlrlsdf gismrkgepr ltetnyvvgt pgyfapeqmm
      181 gaepdfpadl favglvalyl lqgqkpdsqa lvehfvehgt pgapngipep lwqvlagllq
      241 pdpharfrta tgarkaltaa vemlpeagpd depvevfdqi gplpagfgpd gpvtapqqpa
      301 vpgpaagaap qpsatppvsm setgsfhlap ppaadpsqqq pyvqpgfrqp ppaapfttda
      361 pppyavgaph ssqaptsgvp dpaatrayta qqqhppvpsp pvqhaaphap vrvrqtrpgp
      421 ppkvavpvlv valicfavgi waltqi
//
LOCUS       WP_457657437             256 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657437
VERSION     WP_457657437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..256
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26411
     Region          14..245
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrrgtrygal lgpllaggar pdlvaraarg lglpergrya vvvlgapvpd aavvegpdad
       61 garwwwggae gapgeaegre earevavvll gpagparava rlrelgagpg gvspvvgsla
      121 evgaarrlag talltcepgs reivrlderl paallvsrpe lstrllaevf gplltlvpae
      181 rsllvetlea wlacggsvgr aatrlgchrn tvfnrlrrle rltarslsrp relvdlvlal
      241 dvlrltsapp gpgggg
//
LOCUS       WP_457657438             296 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Streptomyces
            griseus].
ACCESSION   WP_457657438
VERSION     WP_457657438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30449
     Region          1..296
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mttfvelllg glsigsvyal ialgfvvifk atevvnfaha slllaggyvt avlhddigfw
       61 pallvgiaga atvgaaiefl vmrryrgsdh svlaivtigv dilliteltr rmgtdvlalg
      121 dpwgnevvhi gsitlaqtri aaflaaglli tvfllafryt swgvsmraaa enpqtaalmg
      181 iklgrvslaa wavagalaav aalfltvfpt pgleratsla alkafpaail ggldsttgal
      241 agglivgvte slatgyqsdl sflgrgigdl apylvmvavl lirraglfgt kelarv
//
LOCUS       WP_457657441             263 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657441
VERSION     WP_457657441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..263
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28134
     Region          127..259
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mrtdevrdly drtmreharp dgpgvrvera gpvvrqvggp ddwngvvwsd pqlaaagada
       61 airaqiehwa algheefewk lhshdrpadl gerlraagfv peppetllva ptelltgpvv
      121 lpegvtlrpv tdaagaelma raherafgtd gtrllhqvvk rleeapddfv avvalaggep
      181 vssarmelyp gtgfaglwgg gtvaewrgrg ayralvayra riaaergygf lqvdasamsa
      241 pilarlgfta lgtttpyvyr aag
//
LOCUS       WP_457657443             528 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457657443
VERSION     WP_457657443.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..528
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56771
     Region          117..336
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          392..484
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mtkragilva vgatvagllt aapgpaaatp astppapklk wtdcptesyp tlqcakvrap
       61 ldhrrpsgrq imlalsrvph takkfqgpll vnpggpggsg lsmagfvass lpkkvaaqyd
      121 vigfdprgvg kstpalnclp ghfdpvrpds vptsyraeri nrdraesfar acgekhgdvl
      181 pymdtvstak dldvirralg srqinyfgys ygtylgavya klypervrrl vldsvvdpdd
      241 vwyegnlgqd yafddrhkaf aawvakhdaa yglgtdpaav eaawyrmrad varepaggtv
      301 gaseledtfl pggyyngywp ylaeafaayv knrdaealve vyenfgavda sgdngysvyt
      361 avqcrdagwp ehwstwrnds rrihkkapfm twnntwynap canwpvaplq pvpvnnrqlp
      421 palilqatdd aatpyggavs mhrklkgssl vveegggnhg itlsgndcld ehltayltdg
      481 tvprgrgead avcaalpdpk plpaekaaaq svdnskgsrl hgllgfrr
//
LOCUS       WP_457657392             221 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657392
VERSION     WP_457657392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Dan,J. and Chen,T.
  TITLE     Genetic Studies on Mammalian DNA Methyltransferases
  JOURNAL   Adv Exp Med Biol 945, 123-150 (2016)
   PUBMED   27826837
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Bujnicki,J.M.
  TITLE     Sequence permutations in the molecular evolution of DNA
            methyltransferases
  JOURNAL   BMC Evol Biol 2, 3 (2002)
   PUBMED   11914127
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Robertson,K.D. and Jones,P.A.
  TITLE     DNA methylation: past, present and future directions
  JOURNAL   Carcinogenesis 21 (3), 461-467 (2000)
   PUBMED   10688866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1903316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..221
                     /product="DNA cytosine methyltransferase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24565
     Region          12..>83
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mnarvlqlrr pnglrvldlc cgagglsmgy ylagydvtgv dlhpmpnypf tfhqadaldy
       61 ltaitatgei erydlvhasw pcqnkarvta wrgsrddhpd litpgrelqa acgrpwlien
      121 vpeaswdgtl rpdyllcgsq fglnvrrhrv fetswggggd llspcwhhkg llafehkger
      181 ayadamgctw mtnvearqav ppaytqwigh qflthertaa a
//
LOCUS       WP_457657444             130 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457657444
VERSION     WP_457657444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13866
     Region          7..125
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 magkftelai dcadpaalar fwcavlgyev qdadeddgvv migspevpeg ksrpgpvppa
       61 ltfarvpegk tvknrlhidv nptdreqgee verllalgar radvgqgdah wvvltdpegn
      121 efcvlgtrcp
//
LOCUS       WP_457657448             671 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657448
VERSION     WP_457657448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Ozhelvaci,F. and Steczkiewicz,K.
  TITLE     alpha/beta Hydrolases: Toward Unraveling Entangled Classification
  JOURNAL   Proteins 93 (4), 855-870 (2025)
   PUBMED   39623291
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Baharin,A., Ting,T.Y. and Goh,H.H.
  TITLE     Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure,
            Molecular Properties, and Applications
  JOURNAL   Plants (Basel) 11 (10) (2022)
   PUBMED   35631755
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Garcia-Horsman,J.A.
  TITLE     The role of prolyl oligopeptidase, understanding the puzzle
  JOURNAL   Ann Transl Med 8 (16), 983 (2020)
   PUBMED   32953783
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Kaushik,S. and Sowdhamini,R.
  TITLE     Distribution, classification, domain architectures and evolution of
            prolyl oligopeptidases in prokaryotic lineages
  JOURNAL   BMC Genomics 15 (1), 985 (2014)
   PUBMED   25407321
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Szeltner,Z. and Polgar,L.
  TITLE     Structure, function and biological relevance of prolyl
            oligopeptidase
  JOURNAL   Curr Protein Pept Sci 9 (1), 96-107 (2008)
   PUBMED   18336325
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Venalainen,J.I., Juvonen,R.O. and Mannisto,P.T.
  TITLE     Evolutionary relationships of the prolyl oligopeptidase family
            enzymes
  JOURNAL   Eur J Biochem 271 (13), 2705-2715 (2004)
   PUBMED   15206935
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..671
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=72580
     Region          451..660
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
ORIGIN      
        1 mntvpaapyg swpspidaal aashdgrpdh lgtvgdevww teprpaeggr ralmrrradg
       61 ttapvlpapw narsrvieyg gqpwagtvra dgellvvfvh ftdqrlyays pdgpdepwpl
      121 tpvsdvgggl rwvdpqvrpe qgaagevwcv leeftgpapt dvrrvvaavp ldgsaaddra
      181 airelsddrh rfvtgpkvsh dgrraawiaw dhprmpwdgt vvmladitda gaftgvrplv
      241 gdldesvcqv ewdrdgsllf vsdladwwel qrirpdavag gvvpssrllp prgeefggpl
      301 wkiglrwfhp ldngliavlh gkggkrlgil dpetgelada pgpwtswsdt lavhgsrvvg
      361 vaasprsape vveldtttgr trtigaphhd avdpayypep eeraftgpdg reihahiypp
      421 hspdrtgpeg gkppyvvrah ggptghaplv ldleiayfts rgigvaevny ggstgygrgy
      481 rerlrdqwgv vdvadcaava salveegaad pdrlairggs aggwttaasl tstdlyacgt
      541 ilypildleg watdethdfe sryleslvgp faevperyre rspmnrtdrl ntpflllqgl
      601 ddvicppvqs erflaavagr gvahayiafp geshgfrrae tliraleael slyaqtfgid
      661 rpdveplelt t
//
LOCUS       WP_457657449             327 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 peptidase family protein [Streptomyces griseus].
ACCESSION   WP_457657449
VERSION     WP_457657449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  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..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /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=33886
     Region          21..325
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtgadrdraa eghspatpla rpprlhpgsr vavvapsgpv padrleegla vlrgwglepv
       61 vgahvrdthp eldylagada draadlqqaw cdpsvdavlc arggygahrm vdlvdwaair
      121 aagpkafvgy sditvlheaf alragfstlh gpmvatetfl kdaptrehlr atlfepetvr
      181 tlglesagal vpgrargily ggcvsllaad tgtpggraha rggllviedt geepyrldgi
      241 ltrllrsgal agvagvacgs wqecgpyeri ravladrlgp lgipvveelg fghgptalti
      301 plgvsavlda padggrctlt veepalr
//
LOCUS       WP_457657454             319 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-ACP synthase III [Streptomyces griseus].
ACCESSION   WP_457657454
VERSION     WP_457657454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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   3  (residues 1 to 319)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..319
                     /product="beta-ketoacyl-ACP synthase III"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0033818 -
                     beta-ketoacyl-acyl-carrier-protein synthase III activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32499
     Region          1..319
                     /region_name="PRK09352"
                     /note="beta-ketoacyl-ACP synthase 3"
                     /db_xref="CDD:236475"
ORIGIN      
        1 mtgsrvvalg hyqpakvltn ddlaalvdts dewitsrvgi ktrhvggpde pvdemaahaa
       61 akalaaaglq asdidlvlva tstaidrsps msarvaarlg mgapavmdin vvcsgfthal
      121 atadhtirag aatralviga dkmadiadwt drstcvllgd gagaavvtad paapdtpdgp
      181 gigpvlwgsv pemgnavrie gtpprfaqeg qsvyrwattq lppiarqvce kagiapedlg
      241 avvlhqanlr iiepvarkig avnaviardv vdsgntsaas ipmalsklve rgevasgapv
      301 llfgfggnls yagqvircp
//
LOCUS       WP_457657457             532 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657457
VERSION     WP_457657457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 532)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..532
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=57314
     Region          12..507
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mtpleeqpat apdellrieg lrktfpgvva ldnvdfdlrr gevhvllgen gagkstlikm
       61 lsgayrpdrg rilaegrevr iegaqdaerl giatiyqefn lvpdltvaen iflgrqprrf
      121 glvdhrrmrq daeqllrrvg vdvrpdakvr elgiarlqmv eiakalslea rvlimdepta
      181 vltseevdkl faivrqlred gvgivfithh leeiaalgdr vtvlrdgrsi dqvpastped
      241 elvqlmvgrs ieqqyprerp dagdallsvr gltrngvfhd isfdvhagev vglaglvgag
      301 rtevaravfg adpydtgtvd vrgerlarhd vpaamgagig lvpedrkgqg lvldasvqen
      361 lglvtlrsat rsglvdlkgq rtaaariakq lgvrmsglgq hvrtlsggnq qkvvigkwll
      421 adtrvlilde ptrgidvgak veiyqlinel tasghavlmi ssdlpevlgm sdrvlvmaqg
      481 riagelpade atqdavmala vgtqgpadpp tdapaltehp apkkeeegpr gh
//
LOCUS       WP_457657460             217 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657460
VERSION     WP_457657460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22985
     Region          15..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msmhtddvga vglreskkre trrlisdhat rlfieqgfer ttiaeiadaa rvakktvtny
       61 farkedmald hqdafaasla dtvgdrapge salmalrraf lasvaaqdpv agfagaafsr
      121 miadsptltv clrglhdrre ealaevlrsa tgaaagditp htvaallggv hrvlfgriqe
      181 ltlagrtnpe iaevvaeeae rsfdllgpsl gdyavag
//
LOCUS       WP_457657458             651 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease/substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457657458
VERSION     WP_457657458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 651)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 651)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 651)
  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   6  (residues 1 to 651)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (residues 1 to 651)
  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   8  (residues 1 to 651)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   9  (residues 1 to 651)
  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   10 (residues 1 to 651)
  AUTHORS   Park,Y. and Park,C.
  TITLE     Topology of RbsC, a membrane component of the ribose transporter,
            belonging to the AraH superfamily
  JOURNAL   J Bacteriol 181 (3), 1039-1042 (1999)
   PUBMED   9922273
REFERENCE   11 (residues 1 to 651)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   12 (residues 1 to 651)
  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 10003059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..651
                     /product="ABC transporter permease/substrate-binding
                     protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65072
     Region          8..323
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
     Region          376..633
                     /region_name="PBP1_ribose_binding"
                     /note="periplasmic sugar-binding domain of the
                     thermophilic Thermoanaerobacter tengcongensis ribose
                     binding protein (ttRBP) and its mesophilic homologs;
                     cd06323"
                     /db_xref="CDD:380546"
     Site            order(386,388..389,437,462..463,510,514,538,564,589,609)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380546"
ORIGIN      
        1 matetlksdt gtggtsvirr vlldngalsa lvvlvvamsl lsgdflttqn llnvgvqaav
       61 tailafgvtf vivsagidls vgsvaalsat vlawsatsag vpvvlavvla ivtgiacgfv
      121 ngalisygkl ppfiatlaml siarglslvi sqgspiafpe svsrlgdtlg gwlpvpvlvm
      181 iamglitali lgrtfigrsm yaiggneeaa rlsglrvkrq kiviyalsgl faavagivla
      241 srlvsaqpqa aqgyeldaia avviggasla ggvgkasgtl igalilavlr nglnllsvsa
      301 fwqqvvigvv ialavlldtl rrkagsgaas sagaapgapg sgrrnalklg gaalcvavvv
      361 gavsffnsgs sggttkvgms lstlnnpffv qmkegaqaea ekagidltvt daqndasqqa
      421 nqlqnftssg vssiivnpvd sdavgpgvrg ankadipvia adrgvnkadt atlvasdnva
      481 ggklaadala dklggkgsiv ilqgtagtsa srergagfae glkaypdikv vakqpadfdr
      541 tkgldvmtnl iqshpgvtgv faendemalg avkalgdkag ksvsvvgfdg tpdglkavea
      601 gtlyasvaqq paelgriavq navkaakdek vestvkvpvk vvtrenvadf s
//
LOCUS       WP_457657463             269 aa            linear   BCT 27-JAN-2026
DEFINITION  N-formylglutamate amidohydrolase [Streptomyces griseus].
ACCESSION   WP_457657463
VERSION     WP_457657463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10523391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..269
                     /product="N-formylglutamate amidohydrolase"
                     /EC_number="3.5.1.68"
                     /GO_function="GO:0050129 - N-formylglutamate deformylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006548 - L-histidine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28597
     Region          17..241
                     /region_name="FGase"
                     /note="N-formylglutamate amidohydrolase; pfam05013"
                     /db_xref="CDD:461519"
ORIGIN      
        1 msdphqpfal ipgaadspvl lhvphgsrhl pqqvragitl ndaalereld hitdahtael
       61 aaaaaraaps tpwrfvnnls rlvvdperfp dereemlaag mgavytrtth replrppetd
      121 pgpllesyfh pyaeamtaav earlaatgra viidvhsypt aplpyelhgm gprppvclgt
      181 dpfhtppgll aaaekafggr vghdgighdt pfagtyvplr hygtdrrvsa lmieirrdty
      241 msepggpagp gldalagalv elvglvgpm
//
LOCUS       WP_457657473             313 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657473
VERSION     WP_457657473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..313
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33171
     Region          7..233
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 menepvvqvr glvkrygtkt avngldlmva tgavtavlgp ngagktttie tcegyrrpda
       61 gtvqvlgldp vadaerlrpr igvmlqsggv ysgarademl rhmarlhahp ldvdalierl
      121 glgdcgrtty rrlsggqqqr lslamavvgr pelvfldept agldpqarrs twdlvrelra
      181 dgvsvvltth fmdeaealad dvaiidagrv iaqgspeqlc rggaentlrf tgrtgldlgs
      241 lvkalpdgsg aaeplpgtyr itgaidpqll atvtswcaqh gvmpegisve rhtledvfle
      301 ltgkelagke pha
//
LOCUS       WP_457657476             504 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657476
VERSION     WP_457657476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..504
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=53677
     Region          10..492
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 mstvappadw hrldprtvlv talvvagvva gaaipvtlgl trwfslpvav lqvfagavlv
       61 igaaagadrv rwhrtryrig eervdlhtgl llvkrrslar grirtvdlta nlllrllglv
      121 tvrigtgeqg sestleldpv trtegerlrr llleraatap pgvhregela vldpgwirya
      181 pvsfvapmlg gaaagavmqv sdwvgaqgqv iewvgdrfre tpllwviivl vlaalvagvv
      241 galglwiemw wnyrlerepg gtlrvrrglf tsrsisveea rlrgvdlvep lgvrllgaar
      301 ldaittglak dhearnadhn tllpaaprtr adavaadvlr eadtptgaal tphpraargr
      361 rlrwslaavl gpvlvltllg alltpvllwi algcavvaap vavvlalday ralghtlsgr
      421 ylvtrsgtvr rstaalerag vigwtvkqsv fqrragllti tattaaggga ytaydtdaae
      481 gltfaaeavp gllepflerp pkdv
//
LOCUS       WP_457657481             218 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457657481
VERSION     WP_457657481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..218
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23106
     Region          25..197
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(74,76,78..79,133..134,155,197)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mtysgavkvg gpasvheltd lmiskvavgg mnnnayllrc ratgeqllid aaaepetlla
       61 ligddgiasv vtthrhgdhw qalaevvgat gartyagrhd aegilvptdv lvedgdtvtv
      121 grveltarhl tghtpgsial vyddphgaph lftgdclfpg gvgnthddpe afasllhdve
      181 tklfdrlpde twvypghghd ttlgaerpql pewrargw
//
LOCUS       WP_457657477             403 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Streptomyces griseus].
ACCESSION   WP_457657477
VERSION     WP_457657477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..403
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41809
     Region          3..403
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mktidellae gvagkrvfvr adlnvpldgt titddgrira vlptvaklae agarvvvash
       61 lgrpkgapdp afslapaaar lgellgadva fatdtvgesa ratvagladg qvavienlrf
      121 nagetskdda ergafadqla eladvyvgdg fgavhrkhas vfdlparlph yagyliatev
      181 gvlkklttdv krpyavvlgg akvsdklgvi dhlleradri ligggmaytf lkaqghevgs
      241 sllqedqipa vreylrraee kgvefvlpvd vvvapafpdl ktkapaehtt vaadampagq
      301 mgldngpetn klyvsklada atvfwngpmg vfehpdfadg travaqalvd spafsvvggg
      361 dsaaavrilg fdenafghis tgggasleyl egktlpglaa led
//
LOCUS       WP_457657482             660 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces griseus].
ACCESSION   WP_457657482
VERSION     WP_457657482.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..660
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=68871
     Region          13..165
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cd06974"
                     /db_xref="CDD:132992"
     Site            order(27,29,68)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mtaelvrgqn htlpqtrlei rvsagtpvva gatlgdergt vrgvewiahp gspqlsgiev
       61 srqaaadhrl avdlealpdg vhrvtvllal pvgvggptrf gavpapfvav tgldgaeiat
      121 ftltgldaes avsalelyrr qdawkvravg qgyagglaem ladqgvaeaa glagsiqeav
      181 trslarsvap ppprtpggdr vrrttgaadh rpptpppape ppepltdpaa tgpaqtarph
      241 papgpaaags agagpinyah pgrqhaappt ppptappaqp gqpaqpvagd atgwsmderl
      301 ynqiwgmfed laravaayrs avdfaesrmd qeldralsdp rnriggagdr aretarakrd
      361 eltsrareal drdlaqlaae savvepalpa ayagwgnpvw hahripmeip malrigdlhl
      421 pertdlripl lvrlplergi wvdsgraase aaalidtdrl rrlametava hvarllavyp
      481 pgefavhvid pagsaagpla plvdagvlag ppaagpggva svlahltrrv dlvqmavrag
      541 aadslppdld tgeqllvvnd fphgfddrav tqlryladeg psvgvhllmv adreeasayg
      601 pvldplwrsl lritpvadsh ladpwvghaw tyepsaippg srvleqvlaa vaaarraagr
//
LOCUS       WP_457657484             303 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457657484
VERSION     WP_457657484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=30329
     Region          31..277
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mnaaaagggl lvvgdvvtdv varygsalah gtdtaarirt vpggaganva cwaarsgcpd
       61 vrllaragae sadwhrrale ragvraflav ddelptatvi alvdaaaert fltdggavlr
      121 laaedfapsm ldgvgrlhls gyllfaatsr taallalrta vergvpvsvd pasagflgel
      181 gpkrflefae gaelllpnad earlltglpg peaaaaelsr wfprvvvtlg argavvaarg
      241 evtgralapp vrepvdstga gdaftggfla allagaddlt aaaagcraga eavatvggrp
      301 pvr
//
LOCUS       WP_457657486             459 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Streptomyces griseus].
ACCESSION   WP_457657486
VERSION     WP_457657486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 10008453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..459
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49274
     Region          <3..454
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          44..235
                     /region_name="COG4279"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]"
                     /db_xref="CDD:443420"
ORIGIN      
        1 mnprmsprpa prpttgpaar rsaprarigp ddlrrtfeav partsaegep fadswwgraw
       61 vdaleslsmd earlargray addgqvaait vtpgrvvayv hgsrarpyra elrlrtfadp
      121 gwealldava erpghlsall akemphsltr taqeagvrll paaddldpsc tcpdhgrpck
      181 hvaalcfqta llldsdpfvl llmrgrgere lleelgrrna ehsarerpaa pavpsvgaee
      241 afagrflppl paplpvpphp gqppsypdlp gardplgldh latdaaarah allttgrdpl
      301 agftawqdav rlaasrptag ltattralyr elayatgrtt tdlaravaaw rqgdagglav
      361 letpwdppag pfdrarpala aagyprftpw rnhlthpags lqlrfgqdmr wygyesdpga
      421 ddwwpraapd pdpvsalgal lagdsvpdta gdddphyvr
//
LOCUS       WP_457657492             238 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657492
VERSION     WP_457657492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25403
     Region          2..236
                     /region_name="LivF"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivF [Amino acid transport and
                     metabolism]; COG0410"
                     /db_xref="CDD:440179"
ORIGIN      
        1 mtallevedl rvaygkieav kgisftveag qvvtligtng agktttlrtl sgllkplsgr
       61 ilfegkpltn ipahkivslg iahspegrhi fprltiaenl llgaylrndk agiekdvqra
      121 yelfpilger rkqaagtlsg geqqmlamgr almsqpkllm ldepsmglsp immqkimeti
      181 velkaagtti llveqnaqaa lsladqghvm evgkivlsgp gsdllhdesv rkaylged
//
LOCUS       WP_457657494             608 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            griseus].
ACCESSION   WP_457657494
VERSION     WP_457657494.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..608
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65212
     Region          51..583
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mplnrrtflg rsaaagagva maggavvgsa gaaeaagqgh ghghgrppkr ysftvmgttd
       61 lhgnvfnwdy ftdkeyddsa hndvglakis tlvdqvrrek grrntllida gdtiqgtqls
      121 yyyakvdpit arrgpvhpma ramnaigyda aalgnhefny gipvlrkfee qcdfpllgan
      181 aldaktlrpa fapyvikrmh tpcgrdvrva vlgltnpgia iwdkanvggk mvfpgleeqa
      241 akwvpklrsm gadvvivsah sgssgtsswg dqlpyvenaa alvaeqvpgi dailvghahv
      301 eiaehfvtnk etgkqvvlse pakwgqrltl fdfdlvwekg rwtvekagsr vlnsntvped
      361 rkvtsllrre hrkvveyvnq vigtsvvams tadapwkdep iidlinvvqt etvkaalagg
      421 eyaalpvlsq ascfsrtagi pagdvtikda aglypfentl earlitgaql kdyleysary
      481 yvqtpaggpv dtakltnadg ipdynydavs gvtydvdiak pagsrivgls fegeaidpaa
      541 rfvlavnnyr asgggnfphv pgaqqlwads deirntiigw vrekgsvdpa afasvgwrlt
      601 regtpvfp
//
LOCUS       WP_457657495             150 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657495
VERSION     WP_457657495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..150
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15894
     Region          14..141
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mitppdtlpy rhvltlptlg savriareta eqvlaewgva aqepcrdpal livselvtns
       61 vrhaaelspn vtvvfaggpd tfafgvhdrh pyrpalfasa gmapgrglat vmelthglgg
      121 savvrgdvde ggksiwvtlp lrwngrshdr
//
LOCUS       WP_457657496             123 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457657496
VERSION     WP_457657496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..123
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13163
     Region          10..84
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(14..15,19..21,34..36,45..48,50..51,54..55,57..58,
                     64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mstplyrlka effktlghpv rirvlellse rehavsemlt evgveaahls qqlavlrrag
       61 lvtarregsa vhysladpgv aellrvarti ltgvlsgqae lladlrsgnd gpddgrpgra
      121 gtr
//
LOCUS       WP_457657498             619 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 35 protein [Streptomyces griseus].
ACCESSION   WP_457657498
VERSION     WP_457657498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..619
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66410
     Region          14..325
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtdftvgddg frfdgkpvrl lsgalhyfrv heeqwehrla mlaamglncv etyvpwnlhe
       61 pregevrdvg algrfldave raglwaivrp gpyicaewen gglpvwvtgr fgqrvrtrda
      121 eyravverwf rrllpqvvrr qtgrggpvil vqaeneygsy gsdaaylewl agllrqcgvt
      181 vplftsdgpe dhmltggsvp gllatanfgs garegfevlr rhqpkgplmc mefwcgwfdh
      241 wgaepvvrnp gqaagalrei lecgasvnvy mahggtnfgg waganrggpl qdgvfqptvt
      301 sydydapvde ygratekfrl frevlegyae gplpalppep vglagpvrve ldgwaglgdv
      361 levlgdpeta esgvpptfee lgvdrglvry rvavpgprqa yplgvsglrd ravvyvdgvr
      421 agvlteesgp lpepvagpae velwveslgr vnygprlgep kgvtggvlhe rqylhgvrar
      481 alrldafdaa eavaavpfgp veaaagagea grtglfrgtf tvgdaagvtg gsgvtgvpgv
      541 dhaglelpgw trgfvwvngf clgrywsagp qrtlyvpgpv lrdgvnevwv leleeagepr
      601 velgpgapvr tgapgvvqp
//
LOCUS       WP_457657503             471 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657503
VERSION     WP_457657503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..471
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47614
     Region          36..439
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,162,
                     165..166,169,293,296..297,300..302,305,333,337,389..390,
                     394,398,414,417..418,421..422,425)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 maiespstsa gpaasppvas vpprlsgrar lvlfvlcaaq fmvaldfsvl nvalpvlgkd
       61 lglsttglqw aitafalpsg gflllfgria dlygrrrlfl aglavfggss llatlawdpa
      121 sflagralqg lgaavivptg mslltttfpe gplrdralgi sgtllslgft vgmvaggvlt
      181 etlgwrstmg llalasavvl vpapkvlees rttdrprldv pgavsvtggl laliyalsta
      241 aergfggadv lvtlalgvtl laafvvvesr saaplvslpm lrrrtvafgn lgglltfsmm
      301 stvvfvltly lqevldlspf atglvfgvqg vlsvvagmya pkvigrigar rtlalsllgq
      361 glfigallgl gtesgvwlat aavslasmch lgaiiayglt vtsgipneqq glatglvttt
      421 qqvgltvgip llgvlattqd tlfdgvrtvv avagavllaa gaavaaglrr g
//
LOCUS       WP_457657505             400 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457657505
VERSION     WP_457657505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41195
     Region          23..352
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mstetpgidp llalraprdp scdvfltgtv fldivftgld sapvrgtesw argmgsspgg
       61 vanmatalar lglrtslaaa fgddhygeyc wdaleqgegi dlsmshtvpg whspvtvsma
      121 yegertmvsh gheapaptaa paaagapept gaaaqppaga agpahvappv sepaapgpaf
      181 prcppraraa iaslapgrae pwvataardg alifadvgwd etgrwdldal pdlahceafl
      241 pnaeeamryt rtdcpraaah alaervplav vtlgaegaya vdgrtgaaaa vpaieveald
      301 ptgagdvfva gfvtgtladw pladrlafag ltaalsvqef ggslsapgwa evaawwqrir
      361 tcagqdpaal eryaflddll pttarawplr ravptigfrq
//
LOCUS       WP_457657507             289 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457657507
VERSION     WP_457657507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..289
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=30015
     Region          36..282
                     /region_name="SEST_like"
                     /note="A family of secreted SGNH-hydrolases similar to
                     Streptomyces scabies esterase (SEST), a causal agent of
                     the potato scab disease, which hydrolyzes a specific ester
                     bond in suberin, a plant lipid. The tertiary fold of this
                     enzyme is substantially different...; cd01823"
                     /db_xref="CDD:238861"
     Site            order(42,85,120,263,266)
                     /site_type="active"
                     /db_xref="CDD:238861"
     Site            order(42,263,266)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238861"
     Site            order(42,85,120)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238861"
ORIGIN      
        1 mkkpqrtlla aalltvsala vtpspafaag qdrpqyvalg dsyaaaplvr padpanprcv
       61 rslgnypnva advlgaeltd vtcsgatard ftrsahagtp pqydalsadt dlvsitigan
      121 daelfrlpnt cvnllpeplg tsceatntgs gtdryaaave awaptfdavl tavrarapha
      181 rvvvvgygty frpggcfpaq pywgrdadyi qaridqlgtv lreaavrhga lytdtagisa
      241 ghdacapqgd ryiqsalslr dgfplhptaa gsrafgeava atltddger
//
LOCUS       WP_457657508             477 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457657508
VERSION     WP_457657508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..477
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49952
     Region          2..472
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtlvdtrsgt vrgsaedgvt vfrgipyaaa pvgplrfrap vpapewqgvr datafgptap
       61 knpyaaplda llpdpdipgd aclnlnvwtp apdegqravm vwihggslrn gssavpvydg
      121 rafardgvvl vslnyrlgie gfgvfpdapa nlglrdqlaa lawvrdnira fggdpgnvtv
      181 fgesagatsi aalltsphat glfhravlqs gaptalppar asrttgamag hlgvdataaa
      241 faridparll aaqrtatsgg npltgnrgfh pvidgdvlpt apadafaaga tdgidlllgs
      301 nthehrlwfv psgladrigr galwaatlrn raplrapgiy raarpdappg eilgamatdr
      361 mlrapvnrla dartgrpgrt yvyefawpsp vgrlgachal elgfvfdtlh tedsrllagd
      421 aaprdlavam htawtafath gdpgweawng trpvrtfgad gprtvhaprn eelrmwg
//
LOCUS       WP_457657518             595 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces griseus].
ACCESSION   WP_457657518
VERSION     WP_457657518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 595)
  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 10228011
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..595
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=63377
     Region          <324..505
                     /region_name="LytR_cpsA_psr"
                     /note="LytR_cpsA_psr family; cl00581"
                     /db_xref="CDD:469829"
     Region          506..592
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mndrqnpydp yyqepqiigy daygqpvyqq qgqqgqqqyd pqgqgydtya aqqgqgqghq
       61 tqdagygyda ygnpqqqhqs ydpytgqhpg qapqpqhgqg dqgygygsyt dygygtgqqp
      121 aavdtgehwt ipqqgaaptp eqapqqapap qpaqpqqspr saeaeadpav pgqrkpapdy
      181 rteqfsfiee pdedsedvid wlkftesrse rreearrkgr nrmvalivva vlvvvggvgy
      241 lwsadmipgl sgsdekkava agaqqrdmiv vhlhdtkkgg tstallvdnt ttkqgttvll
      301 pnslavagdd gttttlgksv eddgrtgtre sidtllgtri tgtwrldtpy lenlvelvgn
      361 ievdtdtevp gakkgesalv nkgegqtlsg pmavayatyr apgepeakql trfgevmrat
      421 lrkvsedpka atvtietllq vldpslpekd lgaslaklas rakvgdykta llpvqddgtl
      481 teadtrgvvk dilggtvkap eagaplrvav rnatgdqkaa eaarvqlvng gyafvdsgka
      541 eaeassvvly rsaedkakav evaktlglaa gdvkkgepaa nadvsavlgq dykvr
//
LOCUS       WP_457657517             105 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457657517
VERSION     WP_457657517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..105
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11662
     Region          <11..41
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mfrvggsyfy rvhqerpvrh eyvltdfgrs lrpilvamaa wrneqlapse ramvlvdtdt
       61 grevepvtvd pvtglsvsdp rfafrsgpaa geqmraryad pgrpa
//
LOCUS       WP_457657526             279 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657526
VERSION     WP_457657526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 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   4  (residues 1 to 279)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..279
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29753
     Region          6..237
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mdtdvpgtvl krertrdavl eliesrspgd aipseralct llgvsrptvr aavdelvaag
       61 llvrehgrgm fvapakitqe lvagdraltv pqasgawssr llefttlqag arvgrklrms
      121 paaeivyvar lrlvdgapma iehlhirael vpglsaqele sgdlyehlrv thgvhvheav
      181 qaieptvvtr aeaglldvpe lspallferl tsdttgrpve yvhslyrgdr yrivsrlalg
      241 paagiapdre ghhpgippgd fahgdaiass trgdiqtga
//
LOCUS       WP_457657525             508 aa            linear   BCT 27-JAN-2026
DEFINITION  CYTH and CHAD domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657525
VERSION     WP_457657525.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Lorenzo-Orts,L., Hohmann,U., Zhu,J. and Hothorn,M.
  TITLE     Molecular characterization of CHAD domains as inorganic
            polyphosphate-binding modules
  JOURNAL   Life Sci Alliance 2 (3) (2019)
   PUBMED   31133615
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tumlirsch,T. and Jendrossek,D.
  TITLE     Proteins with CHADs (Conserved Histidine alpha-Helical Domains) Are
            Attached to Polyphosphate Granules In Vivo and Constitute a Novel
            Family of Polyphosphate-Associated Proteins (Phosins)
  JOURNAL   Appl Environ Microbiol 83 (7) (2017)
   PUBMED   28130300
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Martinez,J., Truffault,V. and Hothorn,M.
  TITLE     Structural Determinants for Substrate Binding and Catalysis in
            Triphosphate Tunnel Metalloenzymes
  JOURNAL   J Biol Chem 290 (38), 23348-23360 (2015)
   PUBMED   26221030
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Bettendorff,L. and Wins,P.
  TITLE     Thiamine triphosphatase and the CYTH superfamily of proteins
  JOURNAL   FEBS J 280 (24), 6443-6455 (2013)
   PUBMED   24021036
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Kohn,G., Delvaux,D., Lakaye,B., Servais,A.C., Scholer,G.,
            Fillet,M., Elias,B., Derochette,J.M., Crommen,J., Wins,P. and
            Bettendorff,L.
  TITLE     High inorganic triphosphatase activities in bacteria and mammalian
            cells: identification of the enzymes involved
  JOURNAL   PLoS One 7 (9), e43879 (2012)
   PUBMED   22984449
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The catalytic domains of thiamine triphosphatase and CyaB-like
            adenylyl cyclase define a novel superfamily of domains that bind
            organic phosphates
  JOURNAL   BMC Genomics 3 (1), 33 (2002)
   PUBMED   12456267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18995808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..508
                     /product="CYTH and CHAD domain-containing protein"
                     /EC_number="3.6.1.25"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050355 - inorganic triphosphate
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=56012
     Region          7..181
                     /region_name="CYTH-like_Pase"
                     /note="CYTH-like (also known as triphosphate tunnel
                     metalloenzyme (TTM)-like) Phosphatases; cd07374"
                     /db_xref="CDD:143620"
     Site            order(7,9,11,44,58,60,62,73,83,117,119,138,158,160)
                     /site_type="other"
                     /note="putative active site"
                     /db_xref="CDD:143620"
     Site            order(7,9,136,158,160)
                     /site_type="other"
                     /note="putative metal binding residues [ion binding]"
                     /db_xref="CDD:143620"
     Site            order(7,9,11)
                     /site_type="active"
                     /note="signature motif [active]"
                     /db_xref="CDD:143620"
     Site            order(9,11,44,58,62,73,83,119,158)
                     /site_type="other"
                     /note="putative triphosphate binding site [ion binding]"
                     /db_xref="CDD:143620"
     Region          213..500
                     /region_name="CHAD"
                     /note="CHAD domain, binds inorganic polyphosphates
                     [Function unknown]; COG5607"
                     /db_xref="CDD:444338"
ORIGIN      
        1 madtkreier kyeatddtrl pdltraagvd rsvhrgltel davyhdtadl rlaadaltlr
       61 rrtggadegw hlkfpvatgi rdelheplad tlprplaall rsrvrhaela pvvrlrsard
      121 vhhltaadgt llaevsvdrv raerlagegs gttaawteie veladdgdpa vldavekrlr
      181 kagirpagss sklaralaet tpvrdgkkqg ktaphtagdh vlayvrkqir tivdldpavr
      241 rdlpdsvhkm rvatrrlrsa fkthrrildr avtdplgael kwlaaelgld rdqevlderl
      301 garvealpat ltlgpvrgrl rawsaarrtg srrriidvld gkryldllea ldalsadppl
      361 rpaarrapgk alpravlkdy erlarrmeha lehppgperd iamhearkaa kraryagesa
      421 rpalgkpakr fakrvkavqt vlgdhqdsvv arealrtlai qshaagetaf twgllyaree
      481 aaaearerel pevwaraldp vlradlkh
//
LOCUS       WP_457657528             327 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657528
VERSION     WP_457657528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36411
     Region          34..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpvvgqrtap rtprrrpapr paarkapppr araqglwpya liapavggml yllvyplvra
       61 vlisfqdfrl rqliagdaef vglrnyrtll tdprfwevvr rtflfmavnv vlimviailv
      121 almverlgri grtvvlcslv lawampvvaa ttvfqwlfhs efgivnwslt slgldsfdry
      181 pwfangtaaf ailvtlivwq svpfaaitly salttvspel yesarldgag aarifrsvtf
      241 pmlrpifllv lsleviwtfk afvqiwvmtr ggpgdattil pvyavqtals sqrydlgsaa
      301 smvtvvlmsg vlvlyfrqml rqedetr
//
LOCUS       WP_457657529             482 aa            linear   BCT 27-JAN-2026
DEFINITION  cellulose binding domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657529
VERSION     WP_457657529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Henrissat,B. and Bairoch,A.
  TITLE     Updating the sequence-based classification of glycosyl hydrolases
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 695-696 (1996)
   PUBMED   8687420
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469668
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..482
                     /product="cellulose binding domain-containing protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51222
     Region          46..128
                     /region_name="CBM_3"
                     /note="Cellulose binding domain; pfam00942"
                     /db_xref="CDD:425958"
     Region          220..448
                     /region_name="Glyco_hydrolase_16"
                     /note="glycosyl hydrolase family 16; cd00413"
                     /db_xref="CDD:185683"
     Site            order(319,321,323,338,340,342,356,358,374,424,426)
                     /site_type="active"
                     /db_xref="CDD:185683"
     Site            order(338,340,342)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185683"
ORIGIN      
        1 mnpsrrnprg srlrtaaasa aavalaatgl aalpssasaa adgivvqyrt sasgtsadqs
       61 epwlkvrnag stsvslssvk vryyfkadsa saayrfacsw avkgcgnitg tfgtlatpta
      121 tadryleigf tagagslapg adtgdmqlrf hqsswaslvq sddysfgpeq aaygdwskvt
      181 ahvsgaivwg eapggngptd ppdptdpptd ppgdaaalfd dfdysshtdp kinangwsvr
      241 snsggpgvpg atwapenvtf adqsgntvmn letstagtga stkhteiltq smkfkngtya
      301 srvkfsdapr sgpdgdrivq tfftindlka pmaddyaeyd feylpnggwg epanilytts
      361 wetyrpdpwe avnahsesrq syagwhdlvv tiddneityy vdgqhfgthg aaylperpms
      421 infnqwlidl egqpsttpra ydqqvdyvlh vkdqvltpaq vnamvgsyrd agtsfedtvp
      481 gs
//
LOCUS       WP_457657535             364 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 5 protein [Streptomyces griseus].
ACCESSION   WP_457657535
VERSION     WP_457657535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Aspeborg,H., Coutinho,P.M., Wang,Y., Brumer,H. 3rd and Henrissat,B.
  TITLE     Evolution, substrate specificity and subfamily classification of
            glycoside hydrolase family 5 (GH5)
  JOURNAL   BMC Evol Biol 12, 186 (2012)
   PUBMED   22992189
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Badieyan,S., Bevan,D.R. and Zhang,C.
  TITLE     Study and design of stability in GH5 cellulases
  JOURNAL   Biotechnol Bioeng 109 (1), 31-44 (2012)
   PUBMED   21809329
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10445019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..364
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39104
     Region          77..328
                     /region_name="Cellulase"
                     /note="Cellulase (glycosyl hydrolase family 5); pfam00150"
                     /db_xref="CDD:395098"
ORIGIN      
        1 mhqrtnpptg saprtgrrgl arkallaasa lgvvtalmap vragaapapa sptgaaptaa
       61 tplaangqls vcglqlcnas geavalngms thgtqwyaqc vtdgsldala qdwrsdvlrv
      121 styvqeggye tdpagftara qkfvdaahar gmyavidwhm lspgdpnvnl draktfftam
      181 akkyknhpgv lyeianepsg vswsgiksya eqiipvirae dpeavvlvgt rawssfgvse
      241 gssesevvnn pvnasnimyt fhfyaashre eyldtldras drlpvfvtef gtqdyagega
      301 ndftmsqryl dlmkrkkisw tnwnysddhr sgavfktgtc sgsnwagtgv lkeagvwird
      361 rirq
//
LOCUS       WP_457657538             421 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces griseus].
ACCESSION   WP_457657538
VERSION     WP_457657538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 421)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..421
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=42386
     Region          20..421
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 msaatarpyr raplapfaaa vtgvglvtsa gtgvdaawrg vteglapaaa prpeladlpc
       61 dffysvtdcd pgavlgvaaq rlmdrfaqfa viaareavad agldpavwds grvgvvigsa
      121 hgglpfydeq aaalagrgpr rvspklaplc vvngaassvs ldlgvhgpsq avstacssgt
      181 vaigtahqml rsgacdivia ggaestctrl liasacslka vstrredpaa acrpfdthrd
      241 gfvvgegagl vvlehpehar argatvrarv sgygassdah savapdpegl gieralrtal
      301 adaglapadv ghvnahgtst vsndlieatm lrrvlgehpl vtstkamtgh tlgaaggiet
      361 altvlalqhq lvpptvnlda pdpripvevv akearaasfd cavktslgfg ghnaalvltk
      421 a
//
LOCUS       WP_457657540             243 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase family protein [Streptomyces griseus].
ACCESSION   WP_457657540
VERSION     WP_457657540.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..243
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26615
     Region          18..238
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtketvqadp splggpalfd tmstmramrr lkpdavpeet iqqliqaavw gpsggnmqcy
       61 eyvvvtdrav marlaplwkr cvdaylattg kyapegmdea aygrmvaaie yqrdhfadtp
      121 vlivpcyrfp eprldeegla asaralgpag tehmmttqtr fqalaegscv ypgvqnllla
      181 arglglaani tiwhlmleqe wkkelgipdd matfaavpvg rpagnfgpvr rrpvadvvhr
      241 drw
//
LOCUS       WP_457657545            1255 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657545
VERSION     WP_457657545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1255)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1255)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1255
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1255
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=129832
     Region          128..589
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          798..903
                     /region_name="PA"
                     /note="Protease-associated (PA) domain. The PA domain is
                     an insert domain in a diverse fraction of proteases. The
                     significance of the PA domain to many of the proteins in
                     which it is inserted is undetermined. It may be a
                     protein-protein interaction domain. At...; cl28883"
                     /db_xref="CDD:333703"
     Site            871..873
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:238300"
ORIGIN      
        1 mrpisrtalg aataavlavt viapsvaapp derdanrpit gsaaaaerpk pvtltlvtgd
       61 tvlvtmdpsg astatalpre dgtvplvqtr qsgpdlyvyp esavsalaag tvdeelfnvt
      121 glirqgydds rtdsvpliat ytgdtarrtl vtprgaerga aldiigglal kadkkkaaaf
      181 wadltaprsr sasglkklwl drkvqasldk stkqvgadla waagydgtgt kvavldtgad
      241 aehpdlqgri tasenftdsg gtgdfqghgt hvastvggsg aasdgknkgv apgtdllvgk
      301 vlndtgsgaa swiiagmewa vdqkadvvsm slgsaeptdc tdpmslaate lgknkdtlfv
      361 vaagnlgpsl ntvsspgcap gvltvgavdr ddstanfssr gpaivshtlk peiaapgvai
      421 saaaaggrgs qayrsmsgts matphvagaa avvkqrhpew taqqikaalv ssahsavpgd
      481 vretgggrld vdrairtpvl gapavqggtf nwpqdtsdrt tvavpytnts gkpvklslkv
      541 agvtgndgst vgskvaslgr tsvtvpagat vevplaldpd arltaaqygd vtgrvlatap
      601 ggvrvstpfs lyvepetvtl rvklvdrtgk padgvssldl igtdtasger rfnegatdqt
      661 yrvrpgayfv ssfiaspdtt datgqlvgsv gylarpqlnv tkdttlvlda rkahrlkvrt
      721 edraaetrga tlafgrswdd twlhsgsisg tgivkdylvd vqgkardgdf efasfwraya
      781 pqiqkfalvg gaalhprpat tgsvnldgag raevvdagag saaeleaaga rgrialvkvg
      841 ddssavltqa raaqdagata llvhrpsagd wqpslgygaa plpvlglrad eaavlkkalg
      901 kgkaevswta tavspfvynl sfpeqgrits drtykvrdrk lgsvvsthaa mgvaadyvdt
      961 llvsrpygat fgasslalvs apgkrteyyt agdtvwqkml sssfpwgelm tgeartyrag
     1021 raeteewyrg llvpgaprda kgeetlager qgdrigvapa fltdsehigq qgsfgdignv
     1081 qlkregelvg ssgypfgvfd vpaeaaayel tmtttkigsp aavwkrstqt ettwtfrser
     1141 kpdvvsqglp llfprydvpe dgmktvpakn gqkigldatg hagytpgelt gakvsfsydg
     1201 getwhaatta rqggrwtatv dhadasgksv alrteltdan gntvvqtvdd ayavr
//
LOCUS       WP_457657552             308 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657552
VERSION     WP_457657552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..308
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32731
     Region          81..302
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mastditsdr krpdgaagpv dtkpddlagl eagldaldav qirrtpvrev llrkvlppvv
       61 avtlvlvvwe llvraqvtev yklpppsavw dsaremwlkg tllevvwtsv srgllgflla
      121 vaigtplgll varvklvraa igpilsglqs lpsvawvapa viwlglndqm mfavillgav
      181 psianglvsg vdqvpplilr agrtlgatgi rgtwhivlpa alpgylaglk qgwafswrsl
      241 maaeiiassp elglglgqll engrsnfdmp gvflsillil fvgiaidlli fsplerwvlr
      301 srgllvkn
//
LOCUS       WP_457657548             406 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657548
VERSION     WP_457657548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 406)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..406
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42068
     Region          4..405
                     /region_name="PRK06205"
                     /note="acetyl-CoA C-acetyltransferase"
                     /db_xref="CDD:235741"
ORIGIN      
        1 mpldvvicep lrtpigrfgg afaqqtpaal aarviaeivt rtgvdpdrvd evilghaypt
       61 seapaigrva aldaglpttv tgtqidrrcg sglqavldaa mqiragfsev viaggvdvms
      121 aapyythdgr wgikgpglql hdalargrvt aggvnhpvpg gmietaenlr reygigradq
      181 dalalrsqqr aaravaegry daetvpvtvr trrgettvta dehprpdtta eqlaalrpvm
      241 aksdpdatvt agnasgqnda aaaclvtsae taerlgltpl vrlvsfarag vpaatmgiap
      301 vaatrtalgr agltladldl ielneafaaq vlactrelgl gekdheqrvn vngsgislgh
      361 pvgatgaril atlarelhrr qarygletmc igggqglaav feriad
//
LOCUS       WP_457657563             176 aa            linear   BCT 27-JAN-2026
DEFINITION  fluoride efflux transporter FluC [Streptomyces griseus].
ACCESSION   WP_457657563
VERSION     WP_457657563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..176
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18440
     Region          45..>139
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mhpdrpehht pptgrqaepv dpdtavdpwp pakasgpkrr qgeilaaiaa ggvigacary
       61 gatliwpaap tafpwtvfwi nvsgcaamgv lmvliterft vhpltrpflg tgvlggyttf
      121 statldtqrl ldhgrhatgl lyaaatltaa faavwaaaal trlvvlprtg aergrs
//
LOCUS       WP_457657554             635 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657554
VERSION     WP_457657554.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 635)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 635)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 635)
  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 635)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..635
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65448
     Region          24..614
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttadmper aesdgdsael lpvatpartr aalralirpd rglaltgigv lvaatavgll
       61 vqpllgrivd ivadgrpaad ltlpvvllva vaavqglttt igltrvarlg etvlarlrer
      121 fveralnlpa drleragagd ltarvtgdva rvaeavrsal pemarsvlai vltlgalall
      181 dvrfllaall avpvqlltar wyvrraltly adqriangaq qqqlletigg avtvrghrle
      241 arhtersagr srravdltmr svnlvlgfyg rlhiaeyigl aavliagfwl vrdgavsigt
      301 ataaalyfhs lfgpvnaalv llddaqsaaa glarlvgvtd laegpgpaag kadpdpcpvp
      361 hqrtapdaap gpkadtvpat aavtahavgh aygpgrpvlh evsltlepge hvalvgtsga
      421 gkstlariva gvqqptsgtv tapagtgaaa vvlvtqevhv ftgtlaedlr larpdatdad
      481 lraalatvha ldwaealpdg lgtvvgeggh rldparaqql alarlvladp alavldeata
      541 eagsagarvl ersaeaalag rtalvvahrl tqavaadrvv vleagrvves gpheelrdad
      601 gpyaalwraw sgsrtyqphd gppdaglrcp pmpsr
//
LOCUS       WP_457657555             563 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657555
VERSION     WP_457657555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 563)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 563)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 563)
  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 563)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..563
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56737
     Region          11..558
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mgadtagrgv irravagqrr dvvvgsllga chqigealvp vliglivdra vvrpdggala
       61 iwlvvlavvy tllsfgfrfg arageraaeq aahqlrldvv rrvlaphgga eagrppgalv
      121 nvatedarrv gavnmaltlg iaavagvvag avlllraslp lgllvlvgap llmalghfla
      181 rplehrseae qeqaahasgv aadlvagvrv lkglraeraa vdryratsqa sreanvraar
      241 aaalqtglml tltgafialv alvggrlvlg gsiglgalvs avglalflpg pisvlarvga
      301 elakgrasaa riadvlaapg ettggtaepa agapgelrln glghagldal dltvhpgehl
      361 givvtdpada atllhclarr cdpdrgsvel dgvpltelap aalrsallva ehdaqlfdgt
      421 lldnvtaaap agadphpamd aaavdevasa ltggvggrig ergsslsggq rqrvalaral
      481 aadrgvlvvh dpttavdaat eariaagirr artgrttvlv tsspallaat drvvlvdggt
      541 itaeaphedl vrdhpvyrta vlt
//
LOCUS       WP_457657564             476 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457657564
VERSION     WP_457657564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..476
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49767
     Region          1..472
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mttaivvgsg pnglaaavvl arsgarvtvl eaadeigggt rsgeavmpgl lhdhcsaihp
       61 maagsaflrs ldperhgliw rrpevdcvhp ldggeagvlh raveetaagl grdgsrwrla
      121 fagpaarfdl laedvmgpll rlpghplala rfglpallpa savarlftte rgralfggva
      181 ahafrplhhp lsaaiglgii taghrhgwpv aaggsrsiaa alasaiaehg gtietgvevr
      241 rvqdlppadi tmfdlaprav adivgdrlpa rvarayrrfr hgpgafkvdf aveggvpwtn
      301 pdarragtvh lggpyaetaa aerdvhagrm perpfvlvgq qyladprrsv gdihpvysya
      361 hvphgytgda tgavidrier fapgfrdrvv ghvarsttam hahnpnyvgg divtgakdpr
      421 qlvlgprstl spydtgvpgm yicsaatppg pgahgmcgan aaeaalrhlt rrprdr
//
LOCUS       WP_457657565             202 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces griseus].
ACCESSION   WP_457657565
VERSION     WP_457657565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..202
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=21748
     Region          4..186
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mttakdlfii amdpepehtv gqgdlslala gaelldliga gtitvdgdli vprgssapdd
       61 rllgeatagl trqppyerie dwlwrrgrdl saayqdaler dgeltqkrsg llpfgpkqve
      121 lvdtparrra larreegdpv laslasavgl dgvgsdddei rlddetvtav vatvheavme
      181 leavrqrrti entafanvwr gp
//
LOCUS       WP_457657567             274 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family substrate-binding domain-containing protein
            [Streptomyces griseus].
ACCESSION   WP_457657567
VERSION     WP_457657567.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..274
                     /product="LysR family substrate-binding domain-containing
                     protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28912
     Region          9..193
                     /region_name="PBP2_LTTR_aromatics_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators involved in the
                     catabolism of aromatic compounds and that of other related
                     regulators, contains type 2 periplasmic binding fold;
                     cd08414"
                     /db_xref="CDD:176106"
     Site            order(14,21,22,24..25,28,36,38,40,84,110..111,129..130,
                     135..136,138..139,158)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176106"
     Site            order(15,61,107..108)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176106"
ORIGIN      
        1 mtgsdipssf rlayvpgvtp tkwvrvwher lpdtslelvq ataaeapdll agrdadaglv
       61 rlpvdrnvls aiplytettv vvipkdhvvt aaeevalael adeivlhpld dvldwetlpg
      121 rpaverpatt adaielvaag igvllvpqsl arlhhrkdlt yrpvpdapes rvalswpqae
      181 etpdlveefi givrgrtvns trgraaapak akdkakdkak dkakdkakar skragggsgs
      241 gsggarnkpa agrkpqsggr agsqsgkrgk prgr
//
LOCUS       WP_457657569             358 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces griseus].
ACCESSION   WP_457657569
VERSION     WP_457657569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..358
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36049
     Region          67..325
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mraqdsattp ssiavaepat tprtasattp naastartai rstardatgs asasrptapg
       61 psagrggtvl aglgvvafsl tfpgtawgle sfgpwslval rsvlaaliag amllagrvpp
      121 perrhwagla vvgggvvvgf pllttlalqt sttshaavvv gllplttaal galrtgerps
      181 rtfwvaalag aavviaftvq qsggalasgd lylfgallvc aagyteggrl arempgwqvv
      241 gwalvlclpl avagslvalp lepvhlnshg viglvwvaag stflglyvwy rgmaaigvar
      301 asqlqlaqpl ltlvwsflll geeisaaapv aavavlvcia atqragrrag resrtvrs
//
LOCUS       WP_457657573             281 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657573
VERSION     WP_457657573.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29183
     Region          8..276
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mgtpelispr sprvaaarrl arrnfrgker rfiaegpqav reaaahrggd gqptlielfa
       61 tpeaadryad iveaahaaga rvhlagddvl advsqtvtpq gligvcrfld tpfqeilaae
      121 ptlvavlanv rdpgnagtvl rcadaagada viltdasvdl ynpksvrasv gslyhlpvav
      181 gvpveqavqg lrdagvrila adgagaddld deldagtmgt ptawvfgnea wglpeetral
      241 adavvrvpih gkaeslnlat aaavclyasa raqrprrvpd a
//
LOCUS       WP_457657575             315 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces griseus].
ACCESSION   WP_457657575
VERSION     WP_457657575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..315
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32072
     Region          1..283
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mnvllpvafv lcwssgfiga klgagsasal tilmwrflpl tvvlaavavt varaswrglg
       61 vrdvarqsvi galsqsgyll tvyyaiqlgv stgttalidg vqplvagala gpllrqyvtt
      121 rqwlglclgv sgvavvtlad asaaagvaww ayalpfvgml alvaatfles rsatrvapsv
      181 sltvhcaast viftalavgt gtalppaela fwgavgwlvv lstfggygly wlilrrsgvt
      241 avntlmflma pvtavwgalm fgepfgprta lglalglvav avvhrgaaap rgdgpagepe
      301 pgardraeal pgagr
//
LOCUS       WP_457657578             311 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657578
VERSION     WP_457657578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32652
     Region          20..78
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          112..306
                     /region_name="PBP2_CysL_like"
                     /note="C-terminal substrate binding domain of LysR-type
                     transcriptional regulator CysL, which activates the
                     transcription of the cysJI operon encoding sulfite
                     reductase, contains the type 2 periplasmic binding fold;
                     cd08420"
                     /db_xref="CDD:176112"
     Site            order(124..125,127..128,131,135,137..143,236..241,
                     247..248,250..251)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176112"
ORIGIN      
        1 mtgddaqtph iplshrvpdl gamelliava rhgslgraak dvgitqpaas srvrsmerql
       61 gvalldrspr gsrltdagal vtdwarrvve aaeafdagtq alrdrrdsrl rvaasmtiae
      121 yllpgwlial raerpdtavs llvgnsaava rrlvtgeadl gfveglsipe gldgtviahd
      181 rlvvvvapsh pwarrrtpll pgelaatpli mrehgsgtrq vldaalavhg glaqpllels
      241 sttaakgaae sgagpcvlse lalgeelssr rlvkvpvagv rlrrqlravw pgghrptgpa
      301 rdllsltgrd a
//
LOCUS       WP_457657580             360 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457657580
VERSION     WP_457657580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=38593
     Region          1..332
                     /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 mrklengsdr dalradgtta avidasftve pgqifvvmgl sgsgkstllr mlngllepta
       61 grvlfdgqdl talsprdlrh vrstkismvf qhfalfphrs vlenaaygle vqgvsreere
      121 vraaealrlt glegwekswp delsggmqqr vglaralatd adlllmdesf saldplirrd
      181 mqdqllelqk rlkktivfit hdlneamrlg driavmrdge ivqlgtaedi lvtpandyva
      241 sftqdvdrsr vltasaimae phtvmgskae dgkemrtpqd vlaaapatvs eatpiidlft
      301 pcsqstnpva vtdakgklvg vvpgsrllav lgepmtpaea prdtepaaaa gadvkkvagv
//
LOCUS       WP_457657581             283 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457657581
VERSION     WP_457657581.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..283
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30910
     Region          4..259
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maerparqgp kaqgaqvvrt eqitphmvrv vlggegladf tlsgftdhyi klcfapegad
       61 yghpfdmaai reeyprelwp ttrtytvrsw dpvaremavd fvvhgdegla gpwaqrarag
      121 eqvtflgpgg gygpdasadw hllvgdesal pavaaaleqm ptgavvhafv evpdaseeqk
      181 ivtpdgvavt wlhrgdrpvg elltaavkgl dfpggrvqaf vhgeagfvke irrylrvere
      241 iplsqlsisg ywrlgqndda wravkrewne qvereqesgt taa
//
LOCUS       WP_457657584             455 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Streptomyces griseus].
ACCESSION   WP_457657584
VERSION     WP_457657584.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..455
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50215
     Region          1..452
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msvavvlfts dlrlhdnpvl raalreadev vplfvrddav hrtgfdapnr lafladclad
       61 ldaglrhrgg rlvvrrgepa rvvkrvaees gaasvhiaag vsgyaagree rirealagtg
      121 relrmhdavv talapgrvvp tggkdhfavf tpyfrrweae gvrgtltapr tvrvpdgvtg
      181 dplperdtvk nlspglargg eeagrklvts wlhgpmagye dghddlagda tsrlsphlhf
      241 gtvsaaelvh rarekggpgg eafvrqlawr dfhhqvlaar pdaswsdyrp rhdrwraded
      301 eidawksgrt gyplvdaamr qlahegwmhn rgrmlaasfl tktlyvdwrv garhfldllv
      361 dgdvannqln wqwvagtgtd trpnrvlnpv iqgkrfdprg dyvrrwvpel aelegaaihe
      421 pwklegldra gvdypepvvd laeararfer argld
//
LOCUS       WP_457657589             318 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657589
VERSION     WP_457657589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..318
                     /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=34664
     Region          7..315
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 matnaidqtr rmlslvtylr erpgahvqdv arafgitedd lisdldvlpm cgtsfrggdl
       61 ldidtdgdri wwhnpddvae plrlaadeat allvaarava tlpglresdr dalvratakl
      121 etaagesgaa ssrlsvtfea eggvfadvdr aiserrrlwl ryyspardel terevdpirl
      181 favghtymeg wcrlsearrt frldrvaeir lldapaappe lelrdlsagl vqpaaedpev
      241 vievgtggrw vaeyyphdsa eelpdgglri tlrtpdpasl rrlalrlggd grivtppela
      301 dsaraaarea lgayedav
//
LOCUS       WP_457657590             123 aa            linear   BCT 27-JAN-2026
DEFINITION  FKBP-type peptidyl-prolyl cis-trans isomerase [Streptomyces
            griseus].
ACCESSION   WP_457657590
VERSION     WP_457657590.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11425492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..123
                     /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]"
                     /calculated_mol_wt=12740
     Region          19..123
                     /region_name="FkpA"
                     /note="FKBP-type peptidyl-prolyl cis-trans isomerase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0545"
                     /db_xref="CDD:440311"
ORIGIN      
        1 msiekpevdf pggeppadle ikdiwegdga vaqagqnvsv hyvgvsfstg eefdsswnrg
       61 tplqfrlggg qviagwdqgv qgmkvggrrq ltipahlayg dsgaggkiap getlifvcdl
      121 vav
//
LOCUS       WP_457657593             280 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657593
VERSION     WP_457657593.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..280
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28476
     Region          19..138
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          100..212
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mtvtghhtgr gtsagtgtda gavralrkle dgrpavrlra alavgttpdp rfvdklvers
       61 avepdffvrd mltwaltrhp vsvtlprllg evrseqasar sqalhtlski gdrrawpait
      121 ralltdadde varsawrasv vlvpeeeeva lgallatqlg rggpetrlsl sralialgda
      181 masalaaaan dpdprvraha latdrllrdp dagftfalee arrvvalgag sgegggsgag
      241 sggssgeage asgsgeagka geaggsegar avrrsggegp
//
LOCUS       WP_457657596             193 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657596
VERSION     WP_457657596.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20565
     Region          16..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtpaarrala aaellfyerg ihavgvdlia aeagvtkktl ydrfgskeqi vveyladrde
       61 rwraflaerl davpapratp aarilavfda srawmadhgs kgcsmvnaha eisdpshpah
      121 avitgqkrwm leiftglard vggigpdaad rlgrtlmllh egalvahglk vfpdpvahar
      181 dearallaga tgs
//
LOCUS       WP_457657599             750 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457657599
VERSION     WP_457657599.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11602166
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..750
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=76790
     Region          13..265
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,36..37,66,71,76..79,91)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,40,42,74,90..93,97,99,136,138,
                     140..141,143,152..153,156,173..176)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,40,42,74,90..93,97,138,140..141,
                     143,152..153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,97,99,136,138,140,156,173..176)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(152..160,169..176)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          462..705
                     /region_name="PQQ_2"
                     /note="PQQ-like domain; pfam13360"
                     /db_xref="CDD:433144"
ORIGIN      
        1 mslrggdpae iggypledrl gsggmgtvfl artssgrpva iklihqqfag ddefrirfrq
       61 evaaarrvsg aftaavvdaa peadqpwmat tyiegptlaq riteqgplng pelrslaigl
      121 aealrdihrv gvvhrdlkps nvvlsaegpr vidfgisrav dqqtltmtgr vigtppfmsp
      181 eqlqaprgvg prsdvfslgt llvyaatghg pfdadspyit ayqvvheeps lgavptalra
      241 vvepcldkep egrpsvdell vllrdlptdl ggagpggpva grtrdmvtqh hlvtgadpap
      301 aapagsgtgs tgtaiggrlr rrwrpvlaaa vavaaigggv aalttggfga sgggadpggg
      361 dtgrstaasp agalpkgfap wrrtvpggre dipdelrcva rddalfcggg gvvatridar
      421 dgsrvwvaks pgvpvqgmhl vgatddtvlg yrfaaqdnpq gprsevvald adsgrelwsv
      481 psgaqstavt grsmdavvtg savvtvdasn srfeardahs geitwttpfp gstqcapvpa
      541 gprllamcat daevdavqvs rptlatldla sgalgepvav dgpvvpvgaa dgrlvllskr
      601 yegasragyd gvarvdpaar kvtysrfgqv yagtagmadg tvyvsgqtgr vtaldsatgk
      661 rkwsrqtgve gasgpatggd avyfssatgr vvalsrddga plwstdpqad gltgeqdass
      721 rvtvagravf vaaaentlfa fdaqkpprsd
//
LOCUS       WP_457657600             818 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces griseus].
ACCESSION   WP_457657600
VERSION     WP_457657600.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 818)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..818
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87319
     Region          34..808
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mavvaavavm stlaatgsta tgaaaaeagp drptirytey giphiiasdw eglgtgygya
       61 aaednictla dtylmvdarr srylgpdgra spgqnqntts nlnsdlyfqr lkddrvverl
      121 ldqpapdgpe pevreairgy vqgynrylae tgvdgisdpa crgadwvrpi temdvyrhah
      181 aeiimgsada lldgqvnaap pgasaaaqpk aasgepapra sspeetaaki rdamaasreq
      241 gmgsnalavg sqgvsggtam llanphfpwq gknrmwqsql tipgkvnvsg asllgfpavn
      301 ighnenvaws htvatvapfg lfdvqvdpln pttylvdgaw ermtsqrvev dvlkpdgsla
      361 kagrtlwstr ygpvttsmqg iplpwvvsah avrdvnlhnl ralnswfrld qaedvhdvvn
      421 ilettqgvpf fntvaadrtg nalyadiqat pnitdqhaes cltatgrllf dqslrlpnvp
      481 pisildgkrs acgwpddpna aapglldphq qprlirsdfv gnandspwla npaqplsfpr
      541 vmgdtaaprs lrtqelilta qkriagtdgl pgkgftpetm gqllfadnsr aadlaldatv
      601 tmcqnvpfgh ilvdgnlvdv reacpvlaaw kshdyttdsr gswlfanywa fllngqgvek
      661 lpwrvpfdsr dpvhtpnsld sgssavrdaf gravlalrka niplnaplsd iqkvtrggeq
      721 ipihgslgql gvlnvitpgq vdgapdivfg ssfiqqvrft atgppqalsv maysqsadpn
      781 sphhadqtkl fsaggwvter fteeqiaasp qlrttvln
//
LOCUS       WP_457657601             473 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457657601
VERSION     WP_457657601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..473
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=50018
     Region          28..309
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,65,67,102,126..129,132,134,169,171,
                     173..174,176,186..187,190,205..208)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,65,67,102,126..129,132,171,
                     173..174,176,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(38,132,134,169,171,173,190,205..208)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(61..62,94,99,104..107,127)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(186..194,200..201,203..208)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msapqgsrdl adgdgaellp pgyrvgdwvv trpigsggws tvyaarpaeg rtggaavprg
       61 htdvalkimp taglaprqar rivesarrev elgrgaghpr ligvlesfvl aapdrpaleg
      121 aivlvmerav gslrelidag vpeadrgrli agiceglahl hrsgwvhadl kpenvllgrd
      181 rsvrlsdfgl ateltgthgh vpplgtldyf pperwraplg elgvrvrpsa dvwalgivih
      241 evfasgaspf pgatpmarga avqeygqgra plrmdqavpp fwrelaadcl apthearaph
      301 saerllaria ahragagaga grrgsraraa vlatalcgia gatlcadavr aassassgra
      361 gttppgtiqv ynaerdcrar adrdprcslg laidpvrpyt aenvvptrvw hgdvlvadcr
      421 vldgetiide edrrsthwfr vrlppgsepp tgwlpavrak qrpalpecfs drs
//
LOCUS       WP_457657602             328 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces griseus].
ACCESSION   WP_457657602
VERSION     WP_457657602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10007665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37694
     Region          1..293
                     /region_name="COG3662"
                     /note="Uncharacterized conserved protein, DUF2236 family
                     [Function unknown]"
                     /db_xref="CDD:442879"
ORIGIN      
        1 mtasdqrprp pgpatpeplg pdsltwrwfg dwrglllapw agsmqnmhpe lgagvaehsr
       61 ffeerwerlf rslypiggvv ydgplaarta revrgyhasi sgvdehgrpy halnpgtfyw
      121 ahatffmltv qvaerfgggl tdaqrhtlfd ehvrwyalyg lsmkpvprtw edfqrywdhm
      181 cadvlednrp trdvlnmrri akppllrllp splwalarip lvrltlwitv glyppavrer
      241 lglrwtphde rllralglvv hhtwqhvper hryhprarag wdrergravp gpvetparnl
      301 ppverrglpq hyapktdrpg epdlpgrs
//
LOCUS       WP_457657603             653 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457657603
VERSION     WP_457657603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10499999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..653
                     /product="acyl-CoA dehydrogenase family protein"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=71020
     Region          32..143
                     /region_name="Acyl-CoA_dh_N"
                     /note="Acyl-CoA dehydrogenase, N-terminal domain;
                     pfam02771"
                     /db_xref="CDD:460686"
     Region          99..649
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(118,148,150,188,190,433..435,437,439)
                     /site_type="active"
                     /db_xref="CDD:173838"
ORIGIN      
        1 mttdktatas ggyvqpeldv raltevldge yaevrdlvra nlvthasvld eadelgvdaf
       61 rervrelvva maatgqtgmg fpkryggggd vgasiaafet lafgdlsvlv kvgvqfglfg
      121 gailhlgter hhdahlpdlv tgklmgcfam tetghgsnvq algtvaryda atrefvitte
      181 gdrarkdyig naarhgelav vfaqlevggt segvhafvvp irvdgqvapg vdieddgrkm
      241 glngvdngri rfdgvrvpre allnrfadvt pegvytspid npdrrfftml gtlvqgrvsv
      301 ggagvnaakv alaiatkyal rrrqfaagsr deeqllldyg lhqrrllpli artyalhfaq
      361 dvvrtqlhdv fsgieddpqe rrrlesraag tkalgtwhat rviqecreac ggagylavnr
      421 faalkadsdi fttfegdnhv llqlvakgll tdyasefedl dqlgmvryvt nlavetviek
      481 tsahkllerv rdllpggdew dqeaglldse yqlamvryre ehllagvarr lkrgidqkrd
      541 pgvvfsqvqd hviavarahg erlvleafve kvrtlpeggn kvalgllcdl falstieadr
      601 awfmehgrlt vqrskaitre vndlcrkvrp lagglvdawg ipsellrapd lvg
//
LOCUS       WP_457657608             302 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657608
VERSION     WP_457657608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10015415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..302
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32786
     Region          20..280
                     /region_name="mthyl_TIGR00027"
                     /note="methyltransferase, TIGR00027 family"
                     /db_xref="CDD:272862"
ORIGIN      
        1 mvdtahrntg vegvaggvgl tallvaaara iethrpdsla rdayaehfvr aapastgwpv
       61 hprevpdgdt nplwgrfary fglrtrvldd fllrsahagn arqvvllgag ldsrafrldw
      121 ppgcvvfevd reevlafkhq vlgglsavsk aarvpvpmdl rddwagalpg agfdpaapsi
      181 wlvegllfyl ppaaetylid tvdglsvags alafevklek dllayrdspl ytatrqqigi
      241 dllelfdrep rpdsagrltd rgwstsvrtp fdftrllgrg plpepndala gnrwvfasrt
      301 rr
//
LOCUS       WP_457657609             224 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657609
VERSION     WP_457657609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..224
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24229
     Region          14..128
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          15..39
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          42..72
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          75..99
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mvpidangtp hhtrlagals aedpsvrlka amaigsapdp alletlverc gvepdlfvrd
       61 tlswalmrya pevtlprirr eldsasaqar sqamhtlski gdkaawdwit rdmlhdvdde
      121 tartawrvav slvpeaeerw ltaelvkelg rgnrslrmsl sralvdlgdv vepalkkaaa
      181 vpdpavaeha aateqllrsr radleaaaer akrvaapaeg aler
//
LOCUS       WP_457657610             144 aa            linear   BCT 27-JAN-2026
DEFINITION  ester cyclase [Streptomyces griseus].
ACCESSION   WP_457657610
VERSION     WP_457657610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..144
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15582
     Region          13..142
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mhaneqlvrv claaiseada egwlasytdd avsrdvplds vwrgraelea gvrswlaaip
       61 etrmavrsvf addrsgvcew tmsgtlegvl dglpeqlaal akgkhftmpg atvyrfsadg
      121 riqeeslywd lagvlgqfgl lprl
//
LOCUS       WP_457657621            1001 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457657621
VERSION     WP_457657621.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1001)
  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 1001)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437895
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1001
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=109813
     Region          129..946
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 msvttvalra plvlvpgfrl deqlrgkaet saglppdvsq ivhdlnrlka gvavtvnpag
       61 gkykpsllvh trtyrirlea tnrgtgylvk hidplrladh arlarsclvv rppawhmvfe
      121 lkavptgsda qwqvleqawq rlgqtqpdrs dapsgddaqa rfldsvdrli dateeittre
      181 erqaapflyq sftatggkrg ktaqsvyefq lvgsepppsg afvriqgdtd trgkvgrasd
      241 ryvtvrfdqp vswdrlptrg alelipssvi fnkqrqavas lrahdsknpg llpavvehhv
      301 rpipatdaqp hqpldpeqlr afraalttqd llvvlgppgt gktrtiteia htaattsave
      361 sgrvlvtsht nravdnvlar lpqdlvvirv gdeskvhadv kpllleeqse glseeirham
      421 aqrtqaykea adveprtael aarvqqvdsh aeeartadlr lhaaaraaaa paherltalg
      481 seeqmlrtll edrteradrl rakahsarqr sdalftgrlh rfrarrreae latesaeiek
      541 lnaslhdvlr qteaagveae raaredtavi aaramrqtag dhlaksvqsa yeeadravha
      601 lravvptaal parlsdpada atalrelhrq ltdwipvlar rqeltgqwla aiaqdpgqlv
      661 pelvryahvv gatcigaasr pelsgvefdl giideagqig iadtlvpltr vrrgvlvgdd
      721 rqlppfrdad vdewaqgigd pelvrlmsqs alerlraglp sshvvqlarq rrmpaeiadf
      781 isaafyrgql ltekehrhrd plftspmafv dtaalpdrvr hesgrgrkeg rgqkgpfnpc
      841 earllarlaa fyhrrgaewt vivpylaqrl evvrqltpli gdsqlanasv gsvdsyqgge
      901 cdivlygftr snpegrigfl kelrranvaf traksqlvmt gdlstlmrad dpgfrmligd
      961 lhqhlldrgd lrghrevmaa ldetvpdlgd atgparegfr p
//
LOCUS       WP_457657628             274 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces griseus].
ACCESSION   WP_457657628
VERSION     WP_457657628.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..274
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=30228
     Region          2..268
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtirrl addhterfag tpvrvsspqg kfsdsaalld ghtltatdah gkhlflgfgd
       61 tgwvhihlgl fgklgfgaap pppptdtvrl rlvnaahhad lrgpttcali tepekraihe
      121 rlgpdplrgd edgerawrri srsrttiaal lmdqkviagv gnvyraevlf rhgidpyrtg
      181 rdltralwdt iwadlaelmr egvrnnridt vrpehlpeam grpprkddhg gevyvyrran
      241 lpchicgtei rtadlvarnl fwcprcqppg psgg
//
LOCUS       WP_457657629             477 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces griseus].
ACCESSION   WP_457657629
VERSION     WP_457657629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..477
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50719
     Region          16..472
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtsqttlakp gqdpgepdrp dtsgglqagl knrhlsmiai ggvigaglfv gssagiaaag
       61 paillsyamv glmvvlvmrm lgemaaarps sgsfsayadq algrwagfsi gwlywffwvv
      121 vlaveataga kileswipgv pqwawalivm vvltatnlvs vgsygefefw fagikvvaig
      181 afvvvgflav fgllpgsdnp gsglahltdt ggffpegpga iltgvlmvvf sfmgseivtl
      241 aagessdpqr avskatnsvi wriavfylgs ifvvltllpw ndpsilekgs yvaaldsigi
      301 pqagnvmdfi vltavlscln sglytasrma fslgergdap ksfakvnrrg vpraailssv
      361 vfgfvavffn yqwpdtvfqf llnssgaval fvwlvicftq lrmrgiilre tpgklvvrmw
      421 lfpyltwati amisfvlvym ltddaareqv vlsllvaalv vgislvrerr srkavak
//
LOCUS       WP_457657632             220 aa            linear   BCT 27-JAN-2026
DEFINITION  CatB-related O-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657632
VERSION     WP_457657632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..220
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23821
     Region          38..194
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(43,45,76,90..91,96,98,100,128,130,133,152,168,176)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(45,47,89..90,92,101..102,130,133,150..151,156,164,
                     166..167,169,173)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(45,47,89,101..102)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100040"
     Site            order(90,92,120,130,133,138,150..151,156,164,166..167,169,
                     173)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 mssapspapv padptvlhpm pgqprvvqlk plvtsplvev gdysyyddpe hatefetrnv
       61 lyhygperlv igrfcalgtg vrflmngsnh rmdgpstfpf ptlggswadh fdlltglpdr
      121 gdtvigndvw igyeavimpg vrighgaivs srsvvvsdvp dygivggnpa rlirtryeea
      181 diarllavaw wdwpaehltr hirtvmsgtv aeleaaapka
//
LOCUS       WP_457657635             301 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657635
VERSION     WP_457657635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 301)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..301
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32753
     Region          12..120
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(12..14,28,45..47)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(59,62,66..67,76,102,106,112,116,119..120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mhpsfvpprr vrigdaaafv gitprairhy heigllpepe rgsddrrryg yedmirllwi
       61 rrtaeagial ddirdafadp asagadsddg iagilerlee alvaqeaelr rqrtavrrmr
      121 tegsrtglls dfvtdrlkgl pegslrradl dsllvterif gplgaavqas rfialathpd
      181 lreesdrvda aeealddtva vddprvaqva aerhafeetl hiviedsgla eeddalfdaw
      241 dalhpataee gepeagrssg ggqgsmsafe aigkmpydfs parlrcmela aelaaheppp
      301 s
//
LOCUS       WP_457657638             302 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657638
VERSION     WP_457657638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   3  (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   4  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32042
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..294
                     /region_name="PBP2_LTTR_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08423"
                     /db_xref="CDD:176115"
     Site            order(110..111,113..114,117,122,124..130,225..230,
                     236..237,239..240)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176115"
ORIGIN      
        1 mtewdvkklr ilrtlrdrgt vtataeallm tpsavsqqlt nlakqlgvdl leaqgrrvrl
       61 tdaahlvlrh aeavfaqler aeaeltgylr geagevrvaa fstavpalvv pavrllraed
      121 rpgpdvrvre aeaaqayell tagevdlals laahaptard prfslfplla dpldvalpad
      181 hpladapglr ladlaaerwi fggsgpwsei ttaaceaagf vpeqahsaag wtailalvea
      241 gmgvalvprm aarerregvv mrvleadrpr rhvvaavrhg aesgpavarv laaltetars
      301 fg
//
LOCUS       WP_457657641             407 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657641
VERSION     WP_457657641.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=42571
     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 magttpgppg tpgtprvlra mndraaldll lehgplsrtr igkltglskp tasqllarle
       61 aaglvvatgt segrpgpnaq lytvnaraah vagldvnaqr iiaavadvtg rtvgrfelat
      121 pgrradrvvr qvadaldgav kdagltradv hrlvigtpga fdpgtgrlry ashlpgwhsp
      181 tlldelaafl pmpveyendv nlvavaeqrl gaarghedfv llwneeglga alvingrlhr
      241 gftggagevg flpvpgtplv rqvvransgg fqelagaqav prlakalgid tpqqpyakva
      301 aelltraada yeqdealtel lrqyaqrlat glasvtavld pglivlsgea vaaggeilrs
      361 liqselaela asrprlvvgk idrepvlrga leraladtrd evfdtsr
//
LOCUS       WP_457657645             459 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657645
VERSION     WP_457657645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..459
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47636
     Region          360..458
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mptcpnghqs gsedwcevcg hrmatggapa gavppppppp papgygypqq gsegggptmq
       61 aelcpqcrtp reamapfcee crwnfltnta tsytplapqh gtpggpppgl nlppgfqaqs
      121 pggqggpgaq ggppgapqpr dpfdyqgsrp sqmnrpaepl apeqngphgn ggqggqggng
      181 gqggpppsfq qqgpppppsf qqqghqppaq qqaapstrsp fepqqaspfa ppqqqsappa
      241 ppqpsghtgg eddwmlppps qaqppqppqh fqqppsphqg qgqqgpgqdl gqgydqgrpq
      301 hgqdqgydqg qqhggvpgqg rspqpaswta viapdrayfl ammqrsgpea tglnlpaysp
      361 eqrlpltgsq itigrrrhst gespdvdlsv ppedpgvshq havlvqqpdg gwavvdqnst
      421 ngttlngaed piqpyvpvpl qdgdqvhvga wttitvrrd
//
LOCUS       WP_457657649             349 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657649
VERSION     WP_457657649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..349
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37819
     Region          37..264
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtsstetadt araagttlae leqraaarrd rpsyghdali acdrvvrift tdgvevqalq
       61 gldllvtege lmalvgasgs gkstlmnila gldvptagsa kvagcdllsm gpkerlryrr
      121 dvvgfvwqqt arnllpylsa iqnitlpmql rgggskrera araesllaml diadcrdrrp
      181 rqlsggqqqr vaiavalann psvlladept geldsatgeq vfaafrrane elgtsivivt
      241 hdqavanevr rtvairdgrt ssevlrrtev daatgqesqv areyamldra grlqlpadyt
      301 qtlgmehrvl leleqdhigv wpdthgapek pegasdrqeq qeqqeqqeq
//
LOCUS       WP_457657651             391 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657651
VERSION     WP_457657651.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /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=40970
     Region          <195..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtfdclaara ralppivadl lvvavvgaft tadaavnepg yrqadaltwt llavslaalv
       61 crrrwpvpvv cvtgaacagw alhghigell nlpvivalyt vavlgdrrrt lwtgviaatv
      121 sgavalkvgr dvvnpqglpv lemvwplvpl llgevvrtrr ellaeyaara araeedrere
      181 aarrvrqerv rvareihdil ahtvsamtvq agvaldalda apevsrramt qvrasgkeav
      241 relratlsvl reaestapap rldqldelva gveaggvrvs lrrdtgdaav pavveatayr
      301 ivqealtnvv khsaarhaav svtraagrlt vevvdegppv pppaappadr gfgligmrer
      361 aaavgggvty gpvpgggfrv havlpaegat p
//
LOCUS       WP_457657653             203 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657653
VERSION     WP_457657653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..203
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21201
     Region          115..174
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtvkdgamta evrtevrtvr ageldryadg irevyarafa appwnedpat adayaerlar
       61 dalrpgfaaa vataggtvtg famawitpev fpadrsygqv aealgpgrtr awlcgalevn
      121 elavapeahg agigaallht vteaapdgrc wlltsvraea alrlyertgw rrigaavpga
      181 aalvvllgpr hpqraeadgw aag
//
LOCUS       WP_457657655             141 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657655
VERSION     WP_457657655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..141
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15024
     Region          9..121
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(71..73,83..84)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mdirpastva ellaaghlfd apprevwatr flaadghvml iayvdgvpag fvsgiemlhp
       61 dkgtemclye lgvdepfrrr giggaltral vdlarergcy dvwvgvepdn eaalatyrsa
      121 gagddgrfam lvwefgggas r
//
LOCUS       WP_457657661             135 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457657661
VERSION     WP_457657661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..135
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14607
     Region          21..116
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mngnvesead vegdkavals daftadcpar tvlnhvssrw gvlilaalqe gpmrfyvlrn
       61 riggisekml sqnlrvfvrd gliareveat vppqvtyslt pvgrelaatl gglvewityr
      121 igdivaarer hdeas
//
LOCUS       WP_457657663             348 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Streptomyces griseus].
ACCESSION   WP_457657663
VERSION     WP_457657663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..348
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /EC_number="1.14.99.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35182
     Region          1..>220
                     /region_name="COG3397"
                     /note="Predicted carbohydrate-binding protein, contains
                     CBM5 and CBM33 domains [General function prediction only]"
                     /db_xref="CDD:442624"
ORIGIN      
        1 mtarrkaagi lalgfaplal tgltatpava hgsltdpvsr vsacfaegpe spksaacqaa
       61 vaaggtqaly dwngvniana agkhrdlipd gklcsaandk fkgldlprad wpatalsagk
      121 htfrfratap hrgsfelymt kpgydatkpl awsdleakpf aevtdpalvd gsyvfdgtip
      181 ersgrqlvyt iwqrsdspea fyacsdvtfg gesagsgsae keegkgeqga ggdggaeapa
      241 papsapseea itegaekssv ehnghgddda ntgakvnaaa paapekkaeg napevntask
      301 devlaetggs gsstylaigg agvlaagaav lfasqrrraa astgrhgr
//
LOCUS       WP_457657664             327 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Streptomyces griseus].
ACCESSION   WP_457657664
VERSION     WP_457657664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34012
     Region          38..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrlrtllall gaallvvvgp pllstgdgsd tgtqipglrf mvpntpgggy ditartmakn
       61 aedaglthni evfnlpgagg tvgltrlvge hgngklalsm glgvvgavht nkspstladt
      121 tpiarlteep divvvaknsp yrtiadllaa wkkdpahvpv gggsspggpd hlapmlmaqa
      181 agiaprtvny vpfdgggell asilgnkvgf gvsglgeyrd qieagelrll avtgpkrvpg
      241 ldaptlreag ldteftnwrg ivappglsda erdkltglir elhaskqwke smkkngwdda
      301 flagdpfgdf ldeqdrrvat vlkelgl
//
LOCUS       WP_457657671             483 aa            linear   BCT 27-JAN-2026
DEFINITION  CitMHS family transporter [Streptomyces griseus].
ACCESSION   WP_457657671
VERSION     WP_457657671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Korithoski,B., Krastel,K. and Cvitkovitch,D.G.
  TITLE     Transport and metabolism of citrate by Streptococcus mutans
  JOURNAL   J Bacteriol 187 (13), 4451-4456 (2005)
   PUBMED   15968054
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Krom,B.P., Warner,J.B., Konings,W.N. and Lolkema,J.S.
  TITLE     Complementary metal ion specificity of the metal-citrate
            transporters CitM and CitH of Bacillus subtilis
  JOURNAL   J Bacteriol 182 (22), 6374-6381 (2000)
   PUBMED   11053381
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Boorsma,A., van der Rest,M.E., Lolkema,J.S. and Konings,W.N.
  TITLE     Secondary transporters for citrate and the Mg(2+)-citrate complex
            in Bacillus subtilis are homologous proteins
  JOURNAL   J Bacteriol 178 (21), 6216-6222 (1996)
   PUBMED   8892821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..483
                     /product="CitMHS family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0046942 - carboxylic acid transport
                     [Evidence IEA]"
                     /GO_process="GO:1905039 - carboxylic acid transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=49914
     Region          1..483
                     /region_name="CitM"
                     /note="Mg2+/citrate symporter [Energy production and
                     conversion]; COG2851"
                     /db_xref="CDD:442099"
ORIGIN      
        1 mltilgfami atflvlimtk kmspiaalvl ipalfcvavg qgaqlgdyvi egvgnlapta
       61 amlmfaivyf gvmidvglfd pivrgilrfc kadpmrivvg tavlaaivsl dgdgsttfmi
      121 tvsamyplyk rlkmslvvmt gvaatangvm ntlpwggpta raatalklda seifvpmipa
      181 lamgllavfv layvlgrrer krlgmltlde alarepepet vsagvggaga aggedrlrkg
      241 aaasaggtgt dtgagtgaga daadgdgdee fqgldpnrst lrpklywfna gltaallaam
      301 imelmpipvl fllgaalalt vnfphmpdqr ariaahadnv lnvsgmvfaa avftgvltgt
      361 gmvehmadwv vgavpdamgp hmaivtgvls lpltyfmsnd gfyfgvlpvl aeagaahgvs
      421 pleiarasla gqalhmsspl vpavyvlvgm akvefgdhtr ftvkwavlts lvvlaagilf
      481 gim
//
LOCUS       WP_457657672             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657672
VERSION     WP_457657672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42562
     Region          14..354
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtvrprtgpg rgwllrlvia fafaqgavsm arpavsyral algadeaavg viagvyallp
       61 lfvavplgrr tdhgrcapll plgvllisgg calsgvvssl pamaawsgvm glghlcfvig
      121 aqsivarqsa pdeqdrnfgh ftigaslgql igpiaagali sadsgalgrt salallvsag
      181 vcavaltslw riehrrapgs gpapghkvpv railgargvp agifismavl satdiltayl
      241 pvvgehrsia patvglllsl raaatiacrl vmtpllrllg rrallttscl lagllcagva
      301 lpvsvpvlav mlavlgfclg vgqplsmttv vraapaqars talalrltgn rlgqvaapaa
      361 agliagavgv aapfallgvl llgaaglglr geartkpara aadpapapvp pdpgpvppav
      421 rdttessg
//
LOCUS       WP_457657676             426 aa            linear   BCT 27-JAN-2026
DEFINITION  exo-beta-N-acetylmuramidase NamZ family protein [Streptomyces
            griseus].
ACCESSION   WP_457657676
VERSION     WP_457657676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Muller,M., Calvert,M., Hottmann,I., Kluj,R.M., Teufel,T.,
            Balbuchta,K., Engelbrecht,A., Selim,K.A., Xu,Q., Borisova,M.,
            Titz,A. and Mayer,C.
  TITLE     The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the
            founding member of a family of exo-lytic peptidoglycan
            hexosaminidases
  JOURNAL   J Biol Chem 296, 100519 (2021)
   PUBMED   33684445
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..426
                     /product="exo-beta-N-acetylmuramidase NamZ family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0033922 - peptidoglycan
                     beta-N-acetylmuramidase activity [Evidence IEA]"
                     /calculated_mol_wt=45457
     Region          45..424
                     /region_name="YbbC"
                     /note="Uncharacterized conserved protein YbbC, DUF1343
                     family [Function unknown]; COG3876"
                     /db_xref="CDD:443084"
ORIGIN      
        1 mslsrrglla aggavgalaa taagtgpaaa spgsgpgsgp grgrvrtgfd rlaadgyrll
       61 rgqkvgivtn ptgvtadvrh ivdvmhpdar vnltavfgpe hgfrgtaqag gsegryddpa
      121 tglpvydtyl ksgqdladvf tasgvdtvvf diqdagarfy tyiwtlydcm eaaalagkrl
      181 vvldrpnpvt graalgpvld pafatfvgrr eiaqahgmtv aelalffnae flhenpvrld
      241 vvtmsgwrrs dffddtglpw vppspnmptp etalvysgtc lfegtnlseg rgttrpfell
      301 gaegidrswa aaanalelpg vafreayfap vfskfegktv ggvqvhvqdr evfdpvrtgi
      361 allvtakqtw sgfawrpdnw idkltgntrv rtmidagadt devvgawqrd lsafrakrrr
      421 ylrygg
//
LOCUS       WP_457657677             581 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            griseus].
ACCESSION   WP_457657677
VERSION     WP_457657677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..581
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=61291
     Region          55..578
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msdqnpgtvn sgpaasgpvd saattsaags iyaaqpwlal lsdaqrapvt ppatvlhawr
       61 aavdrapdrp alayfdgrls yretdalsds vagylaargl rrgdrvaiml qnsphfvlal
      121 lgawkagatv vplnpmyksg evghvlkdaq vtalicadra weaylrdtaa aapdltialt
      181 aceldlqsvn dprvlgferl papgpdnlad dllaaaragh papadrelta adtalisyts
      241 gtsgtpkgam nahgnimvna erqrtghpia egsayfalap lfhitgmvce lsacvanagt
      301 lvlayrfeag vvleafaahr paytvgpsta fmalaahpdv tpdhfssfrv issggaplpp
      361 alvekfragf gpylrngygl tectapcasv ppeheapvdp vsgtlsvgvp gpdtvvrild
      421 eegrevpfge qgeiavrgpq vvsgywnlpe ataaafpdge lrtgdigfmd aagwlyvvdr
      481 kkdminasgf kvwprevedv lythpavrea avvgvpdayr gesvrayvsl rpgatvepge
      541 lgayceerla aykyprevei ltelpktasg kilrrelrsh r
//
LOCUS       WP_457657680             523 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces griseus].
ACCESSION   WP_457657680
VERSION     WP_457657680.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..523
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53974
     Region          27..427
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstgssysse tgttrgtadt ggintykgee ralranrlgt pglllsvvaa saplmvvagv
       61 mptvfgvmgi vgqpllyiil glvlmlfsvg yaemsrhvhn agafyayiar glgptagaga
      121 slvalvaysa mqvgiygilg fevsgifaty ldielawwip alvsaavvgv lgwlkidlna
      181 kvlgvllvie calvvifdia avskpgpegl slhafnpetl tgaglgtalc fciaafvgfe
      241 qapvyaeets rpqivvsrvm flavgyaalf laisswaltv aagpgfiadt slkegpgmlf
      301 glteerlgst ftdilhilfv tgmfaallsf hnvvaryafa mgregllpar fgrtnrasga
      361 pgtgsllqsa vsvviiaafa ftddnpvgdp tapvlrlftw mgnvgalgvi llmaaasfav
      421 iaffvkrgag raqaprlvas alaglallai avftvrdfdv lvgsgpgsal nwllpgviil
      481 alagglvyga vlrsvkpevh ariglgneaf qlekaaeses arr
//
LOCUS       WP_457657684             327 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457657684
VERSION     WP_457657684.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   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 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34805
     Region          1..316
                     /region_name="PdxI"
                     /note="Pyridoxal reductase PdxI or related oxidoreductase,
                     aldo/keto reductase family [Coenzyme transport and
                     metabolism, General function prediction only]; COG0667"
                     /db_xref="CDD:440431"
ORIGIN      
        1 meqrhlgrtg lrvsriglgt ltwgrdtdeh daadqlkafw daggtlvdta dvygggeaey
       61 llgrlvgslv predlviatk agnvpdpyrr vngsrghlla aldaslerlg tdhvdlwqvh
      121 afdpatplee tlqavdlavs sgrvryagvs nfsgwqlaka atwqlavpgv rtrlastqme
      181 ysllqrgier evlpaaldlg igllpssplg rgvltgkyrq gtpsdsrgas erlapfvepy
      241 lddaaaritd avataadgla tsplhvalaw vrdrpgvaap ilgarnagql aealsveals
      301 lpyeicqald dvsapvhryp dhdwstl
//
LOCUS       WP_457657690             459 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657690
VERSION     WP_457657690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  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 459)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..459
                     /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=48982
     Region          192..457
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtdrpqppsp ltgtgpgvgt gagtgagtga gtgagtdgtt apltriirdt ldrlrafdrh
       61 rprawdtavt afwvvaavld ytsggwrtva hddvtapefl vllmslgfsl pllwrrthpv
      121 avlllmapvs vvniwtgavv qaallqlipv fqivlrsslr tvgsaallfv vpvlaggvri
      181 paawgqevvs yvwglvfvvl lgiavrtrre ytealverah rleherdqqa rlaaaaertr
      241 iaremhdiig hnlsvitgla dggayaarkn peragqalea igttsrqala elrrllgvlr
      301 ddhpdadrap qptldelapl idrvrraglp vhlelngdpl qasltpgrql tvyrviqeal
      361 tntlkhatgp tsatvtltrs rthldthitd tgtgaelgts agtttgtial teeaplpaqg
      421 imgmreraal ydgtleagpl pnhggwqirl rlpledthq
//
LOCUS       WP_457657699             303 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657699
VERSION     WP_457657699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31767
     Region          6..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtgvaieahg lgrtygrrgd ghralhdcsf rlpagrvcal vgpngagkst llklaagldr
       61 psagsltvlg stvpgdirdr iafvsqdkpl ypqltvadtl wagaelnpgr wdratadria
      121 gplehgarvr alsggqrtrl alalalgkrp elmlldepma dldplarhel mgvlmaetae
      181 hgttivmssh iltelegacd ylllvdggri rlggeaediv sahalltgra rdlsphtvve
      241 srttgrqlta lvrkegpvdt aawsvtepsl eelllahlrt pdapplltps asaagtraev
      301 asa
//
LOCUS       WP_457657701             603 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            griseus].
ACCESSION   WP_457657701
VERSION     WP_457657701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 603)
  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 603)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..603
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62775
     Region          50..583
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msatpqknra trrvlaaaag latvgalvaa mpagahdrgh ghghghkprt vdvqllsfnd
       61 lhgnleppag sagnvsetqp dgtvkaipag gveylatslr tarkgnpysv taaggdmvga
      121 spllsglfhd eptiealnkl dldvtavgnh efdegatela rlqnggchpv egcykkgkkf
      181 kgadfpylaa nvtkektgkp llkpytvwkk ngvkigfigv tlegtpdivt angvkglkfh
      241 devetinkya keldrkgvks ivalihegga pastsynydc dspgagdgis gpivdiakgi
      301 tpkvdalvtg hthqayvctv pdpsgkprmv tsassfgkly tdttltydrr tkdivrtsvk
      361 sanhvvtrdq pkaadmtrli drwnklaapi ankpqgwisa dingrgstap ekplgnviad
      421 aqleglapad kggaevafmn pggiradlvh kasgsegdgv vtygeaftvq pftnmmnvvd
      481 ltgaqlvtal qqqvsggnea spkilqvskg ltytldltks gadrvvadti klngeaidpa
      541 rtyrvamnef lagggdgfaa lgegtnklvg asdldlfnay laahstaaap ldppatdrit
      601 viq
//
LOCUS       WP_457657704             213 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457657704
VERSION     WP_457657704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..213
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21966
     Region          2..158
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mrisavlfdv dgvlldsaga hrrvwdawsa argldpekvw eltfgrrped tvrdvaahld
       61 pvaerqaldr lleqemgsiq pvegapdllg slsgspwaiv tsgnrdfvaa rfaatglalp
      121 avqvygsdvq hakpapdcfa laasrlgvap aeclvvedap agvraavaag cvavglttth
      181 tgdalaqara rlcvdsladv rsllagygfg ags
//
LOCUS       WP_457657713             369 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457657713
VERSION     WP_457657713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..369
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36132
     Region          149..>366
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtenlrpsgt hstdqdptay pyassygtaq dgtaysgpay sgpaqdgaay agaaggyppp
       61 ppyapttrrr akrpvallaa vaiaagvigg gtatligqln gqnsaatgsg gavngttvsq
      121 sskgtvagva eavspaivei gatssagkst gsgvvitedg eivtnnhvis gaqqiqvtls
      181 tgrtytadvv gtdpdkdlal iklqgasglk tatlgdssqv kvgdevvaig spegltgtvt
      241 sgivsaldrd vtvakddsgs sgqdqgqgrq gggqqwpfef ggqqfngdtg eetttykalq
      301 tdaslnpgns ggalinmdge iiginsamya psssvsgsgs sagsvglgfa ipvntlkadl
      361 dtlragngs
//
LOCUS       WP_457657714             321 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457657714
VERSION     WP_457657714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33527
     Region          25..319
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mssvsegrfl sssvplltpp prcatlltdd gvrveavyap ctagsaaard gvaatagahp
       61 attpaivvah gftgsadrpa vrraarvfaq raavitfsfr ghgrsggrst vgdrevldla
      121 aavawarelg htrivtvgfs mggsvvlrhg alytadsppg spdgsigdsp dadspvrvpe
      181 regrtrrtga hsdvlvsvsa parwyyrgta pmrrlhwvvt rpagrlvgry gfrtriatee
      241 wnpvplspva avpliapapl llvhgdrdpy fpldhprmla eaagpggael wlergmghae
      301 naaddallar iadwataalp a
//
LOCUS       WP_457657720             418 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657720
VERSION     WP_457657720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..418
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44902
     Region          1..418
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 msldvrpvtr seiadwmkav gtgflipaae kpgeelvadr fgdtdlsrmq gvfdagrcva
       61 tfrsfaqqlt vvggatvtad aitgvtvtpt hrrrgllsrm matdlaaake rgeavaslia
      121 aespiygryg fgpaawaaew evsvpragld prrsgqpagg grvemvdgae irktgpevha
      181 alaarqpgvv grgerwwrtr tgvapraahe twtepfyvvh raadgtvdgl lvygvddkwg
      241 dskqplntas vrdliaanpa aeralwhylc svdwittvrs gyrgpddllp lllpdpraar
      301 ivtatdwlwl rmldvprale artygteasl vlevrdeagl aggrflldas psgarctptt
      361 rsadlalgvg elstlylgde smrrlvdlgr aeelragaat tadavfragr rpwcpdvf
//
LOCUS       WP_457657726             245 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457657726
VERSION     WP_457657726.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..245
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26217
     Region          7..120
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          134..242
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 matrlvqinm kahddsalgr fwaealgwgv dsegpgvtnl epvgfaypgp tavcidliar
       61 pepktvknrv hldlattsaa hrtelverlk glgatladvg qgdvpwtvma dpegnefcvl
      121 eprpvyrdtg piaavvvdsa dprgmarfwg eamdwtphea tddlatlrsa kgvgpylefv
      181 rtpdtksgwn rvhldvapys gddlaaeaar lralgatdpa fdasaiswti ladpegnefc
      241 llspr
//
LOCUS       WP_457657727             449 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457657727
VERSION     WP_457657727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..449
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47815
     Region          20..417
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpvpvpqqrs vpaaetshgd ltllvieddp agttitvpel saaagtrvri rtarnlteaa
       61 rlltddvdci lldlalpvtg sdsgsgdgpv sgradelaal thvlriaplh avlaltsedd
      121 telaaeavrv gaqdylfrge ldarvlsrai ryaverkrad iaqhqltesr lraqenarle
      181 rgllptplld gsglsfaary rpgrsrallg gdfydvvrtp dgtvhamigd vcghgpdeaa
      241 lgvelriawr altlaglcgd ellstlqqvl eherqseeif atlctvdiap dgrraglcla
      301 ghpapllarh grparllpye dggpalgllp rarwprrqve lggawslmmy tdgliegrvg
      361 tggserlgqd gmvemvngrl eqglageell eaavaevrel nggeltddva vlllgrdper
      421 irrwggsapr shpassvtgr plgvqrppl
//
LOCUS       WP_457657732             247 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657732
VERSION     WP_457657732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..247
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27186
     Region          12..>141
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtsselwtre tadrydaeea ensspaalep tldflaelag dgralefaig tgrvgvplrq
       61 rgvpvtgiel sepmaavlrr kadedtlpvv igdmattvvp geftlvylvy ntignlltqd
      121 eqvacfenaa rhlapggrfv ieltvpplrf lppgqaavpf dvserhlgfd tfdlveqtlv
      181 shhftrdgdd gryrrgtcrq ryawpaeldl mariaglele rrvedwdgap fgpdsakhis
      241 vwrkpvv
//
LOCUS       WP_457657733             331 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657733
VERSION     WP_457657733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11624708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34583
     Region          45..173
                     /region_name="Lyz-like"
                     /note="lysozyme-like domains; cl00222"
                     /db_xref="CDD:469668"
     Region          112..316
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mfggigvgmv mcflallvvg tysaaaglag pggggavala kgavparfqp lvqkwgnlcp
       61 ainpallaaq lyqesgwnpr aqshaaaqgi aqfipgtwat hgidgngdgk rdvwdpadai
      121 psaasydcel agyvkkvpgd atsnmlaayn agayavikyg gvppyketqn yvkiirslek
      181 sfarpvgrva psqqaagaiy faqkklgtpy lwggngtpeq qgrfdcsglt qaayrtvgie
      241 lprvandqyn agphpsrdel lpgdlvffsd dltnsrairh vglyvgggym inapftgavi
      301 rfdkidtpdy fgatrvtkdg aaalprdlpt g
//
LOCUS       WP_457657735             149 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657735
VERSION     WP_457657735.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..149
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16254
     Region          10..132
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mgahaarryf dakrasvrlv rqfvvttlts wgitgepted irlcaselas nalihgtrpg
       61 hgflvrlsaf erlvslevhd srdiaaeryp qvrpavgthv sgrglrivds laddwgverr
      121 epfgkivwsh fravpecrpa gvagrvagt
//
LOCUS       WP_457657737             292 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657737
VERSION     WP_457657737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..292
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31645
     Region          15..292
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 mttatdtpsr havrkvrlrg ersplasvvl hltlivasvi avfpvlwvll tslkpakyat
       61 ttdffrettf vnytnlirdt eflnwfansv iisalstvig vfvaattgya vsrfrfpgkr
      121 glmwtllvtq mfpvavlivp iynimsslgl lnqpaglvit yltisvpfca wmmkgffdti
      181 preidesgev dgltpfgtff rlilplakpg lavtafysfi tawgevayas aflvgdenlt
      241 lagglqkfvn qygaqwgpmt aasvliaipa alvflfaqkh lvtgmsagav kg
//
LOCUS       WP_457657739             250 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657739
VERSION     WP_457657739.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..250
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27290
     Region          10..136
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtkpvqarsf daiaaaydah rpsyppalfd aieelagvel agarvadvga gtglgtarlh
       61 ergarvtave pgdgmaeqfr rslpdvplvr gdgnnlplrt gsmdlityaq awhwtdpars
      121 ipearrvlrp ggalalwwnd gdpsvewlve qenrmrvffg aeipaapnhr arfravlpdg
      181 ldfrtrqvaw srrvpvdahi anmathsdfl igdpvgvrdf fdrerallas lfpdgeveea
      241 ylvslavahp
//
LOCUS       WP_457657743             705 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457657743
VERSION     WP_457657743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..705
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73972
     Region          13..686
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mrrnlaarig vwsthhrkta vlgwllfvvl atgiggatgm vemtnaenga gesaraeqil
       61 ldagldkpag elvmvsapaa gewkpaadal adavrttget rniappvask dgkdalitfe
      121 mkgeaatssd riqpvldava avgedhadie ihqfgeasag kwlgdllaed fkkaeftavp
      181 lalgillvaf gavvaallpv glaltacmaa fgllsiashq lhlfqttysv mflmgfavgv
      241 dyclfylrre rderaagrda etalriaaat sgravlvsgl tvmvamggmf lsglllfkgf
      301 alatiivvfi amlgsvtvlp allswlgdri dagripllnr rakhgqagsg rivgrvlgpv
      361 larprafava avvlllalaa palgmktesl glekqfgsds qlsiahtrit esfpggpapa
      421 lvvvtapdit apevaqaldg fedvtvhrgk nvaeieiplp ggttdltelr ektlpaafdg
      481 tgaktqvtge iagsvdfndq lrrgivpvfa fitavtfllm lfcfrsyvia vtsivlnlls
      541 vaasygvmta vfqhgwgasl igsegvgaie awmplfvlvv lfglsmdyhv fvvsrirear
      601 gggldnraai etgirrtaga vtgaaaimva vfavfgtlsm qdmqqmgvgl avavlldatv
      661 vrmvllpsvm lllgernwrt prglsrlpsl ehdepaepvr dtvrv
//
LOCUS       WP_457657751             164 aa            linear   BCT 27-JAN-2026
DEFINITION  EF-hand domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657751
VERSION     WP_457657751.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Persechini,A., Moncrief,N.D. and Kretsinger,R.H.
  TITLE     The EF-hand family of calcium-modulated proteins
  JOURNAL   Trends Neurosci 12 (11), 462-467 (1989)
   PUBMED   2479149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11473824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..164
                     /product="EF-hand domain-containing protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18495
     Region          5..164
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mvtqterdrf hmmfkkvdad gdgvieqvdl dqmvqgalar ttthlgspew rrvtdlgnkl
       61 whmlqkdadt dgdsrvtare fvaayrrpdf rdqvavpfel allemagsdn dgrislgdwl
      121 twqeakglsq mesleefqqv dadgdgfltr eecaqhvkqs yaaq
//
LOCUS       WP_457657766             293 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457657766
VERSION     WP_457657766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..293
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30079
     Region          50..258
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mlwrrkllvp laalalalsa stgagtavaa pdtpvaaaap tasaaadfga pgpyatavev
       61 gaittlyypr diadsdrrhp vivwgngtgg vplvyrelll hwagqgfiva aantpqsnlg
      121 ismragidll tgrnadpgsv ffdrvdlehi gasghsqgga aaivvgadpr idailpiqpg
      181 planinavhv palllagqkd sivlpalvra fyhaadhipa lygelrgadh ftvvgdpgpf
      241 aapttawfra hlmgdqeara qffgpgcgic adtatwsdvr rnslslslpa ttp
//
LOCUS       WP_457657760             361 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457657760
VERSION     WP_457657760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..361
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36162
     Region          81..360
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mdaspsrsra rrlliplsaa vcalaltggc sgtapapape apasgtaqga vkrapddlqd
       61 ayqavindvl psvvqidasd slgsgvvydd rghivtnahv vgdekkfkvs vatgeavlna
      121 tlvssypeqd laviklddvp dglkpakfgn aekvevgqiv lamgsplgls ssvtqgivsa
      181 lgrtvsesra gggtgatian mvqtsaainp gnsggalvnl dsqvigiptl aatdpqmgds
      241 aapgigfaip vsmvktvadq iikdgkvtds graalnitgr tvvddnyrpa gvalvsvdrg
      301 gaadraglep gdtitkigdt avttitslse alagdrpgqk vtvtytrdgd srtaevtlge
      361 i
//
LOCUS       WP_457657764            1051 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Streptomyces griseus].
ACCESSION   WP_457657764
VERSION     WP_457657764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1051
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=108734
     Region          3..998
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mswlsrfsla qraliglisi valvfgaiai pqlkqqllpt ielpmvsvla pyqgaspdvv
       61 ekqvveplen slkavdgveg itstasegna limatfdfgd egtkqlvadi qqavnraraq
      121 lpdgvdpqvi agstddiptv vlavtsdkdq qvladqldat vvpalqdieg vgqvtvdgvr
      181 dlqvsvvpdd rklaaaglna gtlsqalqag gatlpagsfs esgksrtiqv ggaftslkqi
      241 edlqvvakdp aagpgeagkp vrvgdvaevr qepstavsit rtngkpslav matmdkdgsa
      301 vaisdavedk lpdlrkdlga gaeltvvsdq gpavsksisg lttegalgla favvvilvfl
      361 asirstlvta vsiplsivla livlwtrdls lnmltlgalt iaigrvvdds ivvlenikrh
      421 lgygeerhaa iitavkevag avtsatlttv avflpiglvg gmvgqlfgsf sltitaalla
      481 sllvsltvvp vlsywflrap kgtpedaaea rrlaeekeaa srlqriyvpv lrfatrrrit
      541 slviavavll stfamvpllk tnffdageqe vlsvkqelap gtsleaadea arkvekvlqe
      601 dkgvkdyqvt vgssgfmaaf gggtganqas yqvtlkdaad yedaqdride algkldgigd
      661 ttiaagdgfg sqdlsvvvka adadvlkkaa eavrtevatv kdvtdvqsdl aqsvprisvt
      721 andkaaaagf dsatlggiva gavrgtpagt atlddterdi virsskpaat maelkalplg
      781 pvelgdiadv kvvpgpvsmt ridgqrsati takpvsdntg avstelaeki daldlpegat
      841 atiggvtedq neafgqlgla mlaaiaivfm llvatfrslv qplillvsvp faatgalall
      901 litgtplgip amigmlmlig ivvtnaivli dlinqyraqg lgimeavieg grhrfrpilm
      961 talatifall pmalgvtgeg gfisqplgiv vigglisstl ltlllvptly amvelrkerr
     1021 akkkaakraa kagaadqqep eeareaepaq a
//
LOCUS       WP_457657767             496 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457657767
VERSION     WP_457657767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..496
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52414
     Region          1..495
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mdiiattrhg kvrgrvdrgi asyrgipyaa apfgvhrfra paavepwegv rdalefgpta
       61 pqrpyrppld rlipevdvpg declnlnvwa peraagplpv lvwihggslr ngsaamplyd
      121 geafardgvv lvsvnyrlgv egfgvfpdap dnrglldqia alawvrdnia gfggdparvt
      181 vcgesagais vaalltspra aglfhravlq sgaphtvprd rgartvrama kalrvpatae
      241 afaavdrarl ldtqhevagg adpisggpgf hvvadddvvp adppppsvdl llgcnreeyr
      301 lwfvpsgald rvngltlrla llkfripgrv arlyragrpg akpgvilgei atdlllrgpl
      361 nrladsrlpg paisgagtgg spaaasppgg pavsgsrpar tffyefawrs pvlelgacha
      421 leigfvfdnl rygealtgpd apqpladamh rawvgfaatg dpgwaawdgr rpvrvfdhpg
      481 tstvlaprqe elrawl
//
LOCUS       WP_457657770            1049 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657770
VERSION     WP_457657770.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1049)
  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 1049)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Rosinski,J.A. 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 1049)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1049
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=113354
     Region          <24..980
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          986..1045
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mitvgekhpa ashayamlgg vetrsvspvf vgraeelasl tealgraasg dpqalligge
       61 agvgktrlve qfvtaaerrd avvavgscve igadglpfap fptalralrr alpeemaaav
      121 agqegelarl lpelgeahrd atdehstarl feltvrller isadravvlv ledlhwadts
      181 trhllaylfr tlstgrlmvv gtyraddihr rhplrpllae ldrlrtvtrv eldrfshdev
      241 ghqlagilae tpeaalvdei fdrsdgnaff veelarslec cgdssgltes lrdlllvrve
      301 alpehaqria rlvaeggsfv ehellaavag lgedeldeal raavganllq papdsdgyrf
      361 rhslvreavs ddllpgertr vnrryaeale adpslvrdde ratrlasywy aahdapkalp
      421 avlraavear rryayseqlr lleramelwd dvpdavratl rpfdyaevyp asacdpentp
      481 lryldvmaea tvaayfggdr tralaiskka mrvlasesdp lreawflvqr srlaqsldkg
      541 dgweelataq ervrglppsa vqadvltnva swkalhrpgp ealadsdrav eyarlvgdey
      601 ielharltrg wltadaggve dglaemyavr draeqlhlmn llgrvsvnlp ssleamgrsl
      661 eavaaadhgi eichshglad sgawvyanqs qslfslghws qseaaaassa rlalgsrgkg
      721 laalrrtela vsrgdfaege ellaqvhklf ghrdpqhqhv idpvrhgmvl aalqgrlaea
      781 rtafeelaga gfppgtqrya lpllqtaami eadarglpaa epdrprllal irrclknlpm
      841 lvpvwvaygv fieaelarae gtdtpchwar aaeafgplcr pyqlaqihrr waeslliapg
      901 gratatallh rsleaarrlg arplaeavvq laararitld gsgaapgdds gihpavlaae
      961 pggegrepap geeqdpavaa vasfgltpre qdvhrlvaag htnrriaeel fispktasvh
     1021 vsnilaklgv ssrgeaaala hrlrlypta
//
LOCUS       WP_457657785             513 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail sheath family protein [Streptomyces griseus].
ACCESSION   WP_457657785
VERSION     WP_457657785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Bock,D., Medeiros,J.M., Tsao,H.F., Penz,T., Weiss,G.L.,
            Aistleitner,K., Horn,M. and Pilhofer,M.
  TITLE     In situ architecture, function, and evolution of a contractile
            injection system
  JOURNAL   Science 357 (6352), 713-717 (2017)
   PUBMED   28818949
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Ge,P., Scholl,D., Leiman,P.G., Yu,X., Miller,J.F. and Zhou,Z.H.
  TITLE     Atomic structures of a bactericidal contractile nanotube in its
            pre- and postcontraction states
  JOURNAL   Nat Struct Mol Biol 22 (5), 377-382 (2015)
   PUBMED   25822993
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..513
                     /product="phage tail sheath family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=55248
     Region          226..503
                     /region_name="COG3497"
                     /note="Phage tail sheath protein FI [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442720"
ORIGIN      
        1 mpsyltpgvy veevqsgarp iegvgtavaa fvgfaeagpf hqptlvtnwd qyvqtfgtft
       61 adtylthavy gffangggaa yivriggpaq gsegtaqgav apapaavalg gflveakpst
      121 gdglsveiad aegenppedr frllvrqggk tvetydvstr knvkgylvtq trdskfvqvt
      181 eqpgtaqsrp ekqtvalaaa gapgtgsgva ridaseyvgd asartgfagl eaideitmva
      241 vpdlmsafqr gdidaegvkt vqlavishce qmgdrvavld tppgmnaqrv rtwrnedagy
      301 dsryatlyyp wvkvfdpasg rnslvppsgh vagvwarsdg ergvhkapan evirgavdle
      361 irlskgeqdl lnpigvncvr afpgrgiriw gartlssdpa wrylnvrrlf nyleesillg
      421 tqwvvfepnd drlwssirrn vtaflteewr rgalfgrtae eafyvrcdrs nnpqesidlg
      481 qvvceigvap vkpaefvifr lsqfsdstsl vde
//
LOCUS       WP_457657789             493 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces griseus].
ACCESSION   WP_457657789
VERSION     WP_457657789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..493
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51484
     Region          6..480
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 msdivagaap rvttvhgtvr gavergvavf rgvpyaaapv gvrrfrapgp pepwtgvrea
       61 vtygptapkr pyappldrll pdpavpgddw lnlnvwtpap gaaglpvlvw ihggslvhgs
      121 savpvydgaa fardgvvlvs vnyrlgvegf gvlpdapanr glldqlaale wvrdniaafg
      181 gdpdrvtvag esagavsvaa llaaprsagl lrravlqsgv ptalppdaar gtteliakrl
      241 gvpataaala avdpeallta qtgvtsggnp ltgrnsfqlv vdgellpqdp vaalhagaaa
      301 gvdllmgtns eeyrlwfvpg glterigrlr lrlallkfgv pnatarvyra nrpdatpgel
      361 lgalatdlll rvplnrlada rtdapgstyv yefgwptpvq rlgachalel gfvfdtlahp
      421 dtqaltgpda pqdladamhr awvdfatdgd pgwpswdarr pvtvfgpgap elvlaprdde
      481 lrgwkpyrhp dtp
//
LOCUS       WP_457657711             213 aa            linear   BCT 27-JAN-2026
DEFINITION  fascin domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657711
VERSION     WP_457657711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Jansen,S., Collins,A., Yang,C., Rebowski,G., Svitkina,T. and
            Dominguez,R.
  TITLE     Mechanism of actin filament bundling by fascin
  JOURNAL   J Biol Chem 286 (34), 30087-30096 (2011)
   PUBMED   21685497
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kureishy,N., Sapountzi,V., Prag,S., Anilkumar,N. and Adams,J.C.
  TITLE     Fascins, and their roles in cell structure and function
  JOURNAL   Bioessays 24 (4), 350-361 (2002)
   PUBMED   11948621
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Yamashiro,S., Yamakita,Y., Ono,S. and Matsumura,F.
  TITLE     Fascin, an actin-bundling protein, induces membrane protrusions and
            increases cell motility of epithelial cells
  JOURNAL   Mol Biol Cell 9 (5), 993-1006 (1998)
   PUBMED   9571235
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Edwards,R.A. and Bryan,J.
  TITLE     Fascins, a family of actin bundling proteins
  JOURNAL   Cell Motil Cytoskeleton 32 (1), 1-9 (1995)
   PUBMED   8674129
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Bryan,J., Edwards,R., Matsudaira,P., Otto,J. and Wulfkuhle,J.
  TITLE     Fascin, an echinoid actin-bundling protein, is a homolog of the
            Drosophila singed gene product
  JOURNAL   Proc Natl Acad Sci U S A 90 (19), 9115-9119 (1993)
   PUBMED   8415664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10083566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..213
                     /product="fascin domain-containing protein"
                     /GO_function="GO:0030674 - protein-macromolecule adaptor
                     activity [Evidence IEA]"
                     /GO_function="GO:0051015 - actin filament binding
                     [Evidence IEA]"
                     /GO_process="GO:0007015 - actin filament organization
                     [Evidence IEA]"
                     /calculated_mol_wt=22451
     Region          69..208
                     /region_name="beta-trefoil_FSCN-like"
                     /note="fascin-like domain, beta-trefoil fold, found in the
                     fascin-like family; cd00257"
                     /db_xref="CDD:467441"
ORIGIN      
        1 mtstllslaa altasalaap aagaaprtdr papasgvpag weragaddla hlagaigsga
       61 radettnlal ksvrngkfaa aeindaapnt gvlrarspyp tgawegfafe wdeatqtfal
      121 kslannlyva veknftgnak nalrarstta ggwerfelyq neelnlyalr stlndlfvam
      181 ensytgplqy tlrarsaevt gsweqfdlys idg
//
LOCUS       WP_457657793             347 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457657793
VERSION     WP_457657793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  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   2  (residues 1 to 347)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..347
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36976
     Region          8..347
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mpeqspgsrp tleavaarag vsratasrvv nggdgvrkpl vdkvlkavee lgyipnhaar
       61 tlvtrrtgav avviaepetr ffsdpffsqq irgiskelta hdtqlvlllv egpgdfdria
      121 rylsgghvdg alafslhtdd pvpaitrrag ipavyggrps wtadpgdqav pyvdadnrgg
      181 arlavrylkd lgrrhiahig gpldqtsamd rldgyrdvll dvdptlvaag aftvesgara
      241 maelldrrpd ldavfvandl masgalrvlr ergiavpeqv alvgfddmds vasetdpplt
      301 tigqeieeqg rlmarlllra ldrdrtgsgd vpesvitpvt lvrrasa
//
LOCUS       WP_457657797             613 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457657797
VERSION     WP_457657797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..613
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=64791
     Region          13..266
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,75,80,85..88,102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,83,101..104,108,110,146,148,
                     150..151,153,163..164,167,184..187)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,83,101..104,108,148,150..151,
                     153,163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,108,110,146,148,150,167,184..187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(163..171,180..187)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtagsegsli derfellerl ggggmglvwr ardivlhrdv alkevrppdp ellrlrpdaa
       61 emlrkrvlre avslarishp nvvtihhivs saevahpwlv melisggslq drlergpctp
      121 aetarlgrgv laglraahga gilhrdvkpg nvlmrtdgtp lltdfgiaav reatsltntg
      181 eligspdyma perlrgrddd pssdlwslam mlyvaveghh pmhrsstlat laaileedvp
      241 pprragtlgp vlrsvlikdv asrpdaesfd rllaqaagar vatvldgiaa splpaepmer
      301 adeapvpytp tepdvpahaa sgpltrdvtg saasgqarde pqppaapept aapeprpspd
      361 gatdgatdga tegakgsgae tsrtpvrgtg sagplrrrlv lpaallgalv igllareyap
      421 dfgggdkpsa gapstpsaar tptsspsasl ssspspsptl keetdlltps garrvlkkmk
      481 evtggtkvlp tfdlrpdras gntlldeemv pgkkvfdnfs ykdgrgslqg aegilkghql
      541 ldldqvdwdt lprllriart elgvlkpdpd gsyvifdwye gqaamliyvn geyqtggili
      601 asfdgriirr vkd
//
LOCUS       WP_457657801             194 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657801
VERSION     WP_457657801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=21121
     Region          8..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          92..191
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 msvqerkere ragrerliva tarelaeqqg wdavttrrla erieysqpvl yshfrgkrei
       61 igavalegaa emagalraat satatdepra rvvalarayl dfaadnpavy damfqldggl
      121 afaeedtpep lkdafaafle tlgevagdgv hpalftelfw aclhglatlt ragrlppeds
      181 errvqllvdr lavv
//
LOCUS       WP_457657807             166 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457657807
VERSION     WP_457657807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..166
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18784
     Region          1..155
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mtveefeefy aravarltgq lyvmtgdlqe aqdvvqeafv kawvrrgrle rdgqpeawir
       61 tvawrlavsr wrfrrrsada wgrgsgapeh veppdpghvv lvdalrelpa qqrrtltlhy
      121 lcdltveqia aetglststi kthlvrgraa lahrlhdpri eeapdv
//
LOCUS       WP_457657809             665 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657809
VERSION     WP_457657809.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 665)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 665)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 665)
  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 665)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..665
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68708
     Region          89..663
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 msavsgttga earagaeaag sgpedagtpa agpagepvgp gqtageaaep eqptgeaagp
       61 erptgeaaap eapaggspad ttgnpaqgks gpsplrllla rvrphrgvli ragllsltgs
      121 aaglamplma kyavdafaad rspvaplval talvlagaci saygrylmar tgegvvlrar
      181 dqlvgrimrl kvpavdrltp gdlqsrvtsd ttllrtvlss glvesfnsvl mllgtvafma
      241 ymdvtllgvt lvvivgigav tallmpriqr aqlraqesvg amgaaldrvl qafrtvkasg
      301 aeeretaava eaarhahdrg vsvakwssvs dvtmmmsiql aflavlgvgg arvasgslei
      361 ssliafllyl fylmgpiggl vegwtglqsg laavrridev eslpgetstg sgamepeggp
      421 lgvafqdvtf gygderapah kgvtfdvpag glvalvgpsg agkstvfsll erfydhdggt
      481 itvggrdird wplaelrasl ayveqdapvl agtlrenllf aapnaegqal edavtrtrld
      541 alvdrlpdgl dtavghrgvt lsggerqria iarallrrpr lllldevtsq ldavneqalr
      601 dvilemaert tvlviahrls tvrhadrivv leegrvrtag theeliagdd lyrelattql
      661 aaeva
//
LOCUS       WP_457657811             696 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457657811
VERSION     WP_457657811.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..696
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69949
     Region          29..284
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(29,52..53,82,87,92..95,107)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,56,58,90,106..109,113,115,152,154,
                     156..157,159,168..169,172,192..195)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,56,58,90,106..109,113,154,156..157,
                     159,168..169)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(40,113,115,152,154,156,172,192..195)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(168..176,188..195)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgkgkdsgry tamegirpla agdpvrigpy pllgrlgagg mgrvylarsa ggrtvavkvv
       61 heehiangef rarfrreiea arrvggryta pvldagpdae qpwvatgyvp gpsleqavre
      121 hgplpadsvn alaegllral rgihaagivh rdlkpsnvll tvdgprvidf giaralqvsv
      181 eslltstgmv igspgfmape qilgeetgpg advfslgcvl myaatgqlpf gagvsnqhav
      241 mfrivqsppd ltavsdaplr aliercltkd paerpgveal lesltpeqss daargawlpp
      301 vllarlaqqs allldaevpe epgvpeeade pegaepaavs npvfgpvadp vpvpvpdpdp
      361 dpdpvsapas gsdpdpvaap rdlgtvdlrp epgrkpgpep vagpspettg aaaavpvaap
      421 vaagprrsrr rvwavaavvv avlaaggtta flnrdpggga darggesaap padgatasps
      481 gkgddeddkg seeekakdka rdsaeekeke kgngddggqg gdagggqgag sgdgsasggg
      541 ssgtgesgss ggggaqdgag ssasggsgga akppaadpdp apdgrvpqhf vgtwsiaspy
      601 dvlqphtvvi rrvspgqsav tliadvqgsg hceytaklgs vadggnrinv gtavvnkars
      661 gsmcrdtdps fftvagsgil hdvgpahgsg yrynra
//
LOCUS       WP_457657812             565 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457657812
VERSION     WP_457657812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 565)
  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 565)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..565
                     /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=59599
     Region          120..407
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlwsparivg eavlavtlag latgvgawmd tlgartvlla gvmallapar halpatvlil
       61 saplagggnv masvllvcaa wsagrritep wrvtaafgaa cvlhavpgly hgitsgaapv
      121 lpvtlgwnvv tfltlavvpa lvgryrnqrr rlldalwqnn qqlqreqamv arearllern
      181 riahdmhdsl ghqlalisvh agalqvdpel tgnqreavri lrgasvtama elraavgvlh
      241 deaeyreqqn eqqneqqyqg rrrqsvggga svpyaprtta aidglvassr gagttvsldr
      301 sgvrrplapa adheayrivq egltnahkha pgapirlalr yepdslvvev tngpvlggap
      361 evppeisggq glkglrervg raggmvhtgp tedggfriag mlpygatsvv pardvrgqrr
      421 pgavvdggtv ingadpqref ttimstrkni aigcavtavv lvagviglgv wgigvlteev
      481 kkaeispsvy eeakvgdaea dirarlpegd swltsdladq gpkpaegatc rhfgsedder
      541 vdaltvfrfc fqdgklvske tyeak
//
LOCUS       WP_457657814             509 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457657814
VERSION     WP_457657814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..509
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53506
     Region          100..>285
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          407..502
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mttrrllrtf aigigtagll isgcsgsgss pnasatgtaa peglssyyaq klswrdcgve
       61 gfecttmkap kdydkpddgd idlavsrkka tgpgkrigsl lvnpggpggs aigylqgyaa
      121 lgypaqvrar ydmaaidprg varsepvecl tgpemdaytq vdqtpdddae vqklsaafek
      181 faagcekrsg eilpyvstvd tardmdvlra llgdeklhyv gasygtflga tyadlfpera
      241 grlvldgamd pslkaidmnr dqtagfegaf qsfaadcvkq pdcplgttst adaatalkql
      301 ftdldakpip tgddrelges lattgviaam ydeaawpqlr ealagaqrsd gsgllslads
      361 yyerepdgky anlmfanaav ncldlppafd gpdavekalp dfekaspvfg rgfawaslnc
      421 aywptkatgt phrteakgaa pivvvgttrd patpytwses laeqlssgtl ltydgdghta
      481 ygrgsdcidt aintyllegt ppthgkkcs
//
LOCUS       WP_457657819             307 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Streptomyces griseus].
ACCESSION   WP_457657819
VERSION     WP_457657819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..307
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31385
     Region          79..302
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mtagtsayaa havalcagsa vwlamvrdpg vrrarvlfvd arpesrrtwg wgrwpglrka
       61 lgrvtesarg rrewwcvpaa vllavvggsv lplvagavav pvirrwlrrr aaareaekaa
      121 atvaalcgav vgelragrep gqallfalre gpsedspsaa tsggrlgqae aavlaaarfg
      181 gdvpaalrqa aagpglagls gmaacwrvav dggaglatgl erleaalred rrrreelraq
      241 lagawstvvv lallpvaglg lgaalgadpl rvllhtpggl vclaagafle taglfwacri
      301 vrggeaa
//
LOCUS       WP_457657821             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657821
VERSION     WP_457657821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  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   2  (residues 1 to 331)
  AUTHORS   Lindahl,P.A.
  TITLE     The Ni-containing carbon monoxide dehydrogenase family: light at
            the end of the tunnel?
  JOURNAL   Biochemistry 41 (7), 2097-2105 (2002)
   PUBMED   11841199
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Ragsdale,S.W.
  TITLE     Nickel containing CO dehydrogenases and hydrogenases
  JOURNAL   Subcell Biochem 35, 487-518 (2000)
   PUBMED   11192731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35796
     Region          1..271
                     /region_name="CooC"
                     /note="CO dehydrogenase nickel-insertion accessory protein
                     CooC1 [Posttranslational modification, protein turnover,
                     chaperones]; COG3640"
                     /db_xref="CDD:442857"
ORIGIN      
        1 mkiafvgkgg sgkttlsslf irhlaaneah viavdadinq hlgaalglde aeaaalpamg
       61 ahlplikdyl rgsnpriasa etmikttppg egsrllrvhe dnpifeacar tvrlddggvr
      121 lmatgpftes dlgvacyhsk vgavelclnh lvdgpddyvv vdmtagsdsf asgmftrfdm
      181 tflvaeptrk gvsvyrqyke yardfgvalr vvgnkvqgpd dleflraevg ddlligvghs
      241 dwvrsmekgr psrfellead nrmalqalqd aaedsyglrd werytrqmvh fhlknaeswg
      301 nektgadlaa qvdpafvlde ryagagvtap a
//
LOCUS       WP_457657823             258 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces griseus].
ACCESSION   WP_457657823
VERSION     WP_457657823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..258
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27174
     Region          77..236
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mthahthgst hththagndp aegpshsggd ggrvpdpava vttdglpdwl dpvaraarsv
       61 qpqqlsrflp pesgagrqsa vlvlfgeger gpelllmera gtlrshagqp sfpggaldpe
      121 dgdqattgpl raalreaeee tgldpkgvql fgvlprlyip vssfvvtpvl gwwrapspvg
      181 vvdpgetarv ftvpvadltd panratavhp sghagpaflv esalvwgfta gvidrivhya
      241 gwerpwdrar qvpldwra
//
LOCUS       WP_457657825             315 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Streptomyces griseus].
ACCESSION   WP_457657825
VERSION     WP_457657825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..315
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          6..312
                     /region_name="MDR1"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08267"
                     /db_xref="CDD:176228"
     Site            order(40..42,45,126,130,151..154,156..157,175..176,179,
                     194,211..212,232..233,260..262)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176228"
ORIGIN      
        1 mraalydsyg ppevlyegrv pvpvrkpgev lvrvhaasvn ggelhgragr vrfvtgrrfp
       61 qrtgldfage vaevdpdatg lrvgdrvwgi lgrtfgsaae yvsvrprqia yapgnvtlte
      121 aaslpaggtt sltalrdkag lragerllvr gasggvgsva vqlgkalgah vtglagakna
      181 dfvrelgade vldhratala dldrydvimd tvgtehpvlr rrlapggrlv siafdidhpv
      241 rsigyllgsa vygrqrvrff sgnpkhdlft eltayvergd lrpvvetvhp ladiatahra
      301 leaggvrgkh viqvv
//
LOCUS       WP_457657826             134 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657826
VERSION     WP_457657826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..134
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14368
     Region          7..119
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mksvvvfrid rrsgvatylq ivrqveqalr mgaleegdrl ptaaqvaatt kvnpnttlka
       61 yrelermgla evrqgagtfi trtlaqpqsg pdsplraala dwlaqarteg ltgqdvtalf
      121 haafesaypg eapd
//
LOCUS       WP_457657827             408 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Streptomyces griseus].
ACCESSION   WP_457657827
VERSION     WP_457657827.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 408)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..408
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43171
     Region          6..399
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mprtirdvvf vdgvrtpfgk agpkgiyhet raddlvvkai rellrrnpdl dpkkidevai
       61 aattqigdqg ltlgrtagil aglpqsvpgy sidrmcagal tavtstagsi afgaydvvva
      121 ggvehmgrhp mgegvdpnpr fvseklvdes alfmgmtaen lhdryptitk eradayavrs
      181 qekaakayan gkiqqdlvpv svrrtnaeag etgwglvtad epmrpgttme slaglktpfr
      241 ahgrvtagna aglndgatas llaaedvane lglpvkmrlv syafagvepe vmgygpipat
      301 ekalaqagls iediglfein eafavqvlaf lehygigddd arvnqyggai ayghplassg
      361 vrlmtqlarq feeqpevryg lttmcvgfgm gatvvwenph fnadggnk
//
LOCUS       WP_457657828             232 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657828
VERSION     WP_457657828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..232
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25405
     Region          60..161
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(79,82,127,157,160)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mgtttygdwi rdfeaarrer aergdpdwrt gveqhpavrr svqrfqvged gdgaglitka
       61 eaagdaeyas avrmfvaeer nharllalll asggaplias hwsdrifval rralglrlel
      121 lvlmiaevva lryyralrdg agdaltreva gliladeerh vpfhchrlrr alrplpppvr
      181 vlvtsgwraa laaaalvvav dhgpalrrlg vgrfrfarev vrssgpiaat mr
//
LOCUS       WP_457657833             229 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces griseus].
ACCESSION   WP_457657833
VERSION     WP_457657833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..229
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24817
     Region          <3..214
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 markstprkr rtesrgsvvv iglgrfgral alelvdedte vlgidenaev vqalsgslth
       61 avradstked alrqlgvhef dravvaigtd leasiltasl lvsfgidnvw akaiseahgr
      121 iltqlgvhhv vypehdmgqr vahlvrgrml dyiefeddfa mvktspptdi iglplansav
      181 rtrygvtvva ikrpgegfty ataetvvead dtiivagrtr aterfselq
//
LOCUS       WP_457657834             447 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Streptomyces griseus].
ACCESSION   WP_457657834
VERSION     WP_457657834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..447
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47099
     Region          30..435
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mvtpqwprlr hpaqvvvagf aaavvagagl lmlpvaktgp ggagvlealf tstsavcvtg
       61 lvvvdtpgyw tgfgqavilg liqvggfgim tfasllvllv srrfglkarm taaaetktlg
      121 lgdvrsvvtg vvkvslllea vialalalrf ataydeswpr alwlgvfhav safnnagfal
      181 ysdnlmgfvt dpwiclpial aviagglgfp vlfelrrrfr kprdwslhtk ivlwatgvfl
      241 iggsafital ewsnpatlgp ldvpgkllag ffqgvmprta gfnsldtsqm npaswlgtdv
      301 lmfiggasag taggikvttf avlffviyae irgegavnif hrrlhgdlqr qaltvvllsv
      361 aavavttmaf mvfsdhsldq slfevtsafa tvglstgita dlpvglqlll ialmfigrlg
      421 pitvasalal rtrvrlydlp eerpiig
//
LOCUS       WP_457657841             484 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457657841
VERSION     WP_457657841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..484
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51328
     Region          58..474
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnstrtndrt srasrnrsrt ggpssprpvg rgrrpvvvqg efappktltp alpaveafae
       61 ldmpalllaa ltvqgvsvpf piqgatlpnt lagrdvlgrg rtgsgktlaf glallartag
      121 qraeprqpla lvlvptrela qqvtdaltpy arsvrlrlat vvggmpisrq agalrggvev
      181 vvatpgrlkd liergdcvld qvaitvldea dqmadmgfmp qvtalldqvr pegqrmlfsa
      241 tldrnvdllv rryltdpvvh svdpsagavt tmehhvlhvh ggdkhratte iaaregrvim
      301 fldtkhavdk ltdhllhsgv raaalhggks qpqrtrtlaq fktghvtvlv atnvaargih
      361 vdhldlvvnv dpptdhkdyl hrggrtarag etgsvvtlvt pgqrrdmtrl mtaagivplt
      421 tqvrsgeeal sritgsqaps gipvtitapv aerrrrsaap rgrrgsasat rraagrqssf
      481 gaaa
//
LOCUS       WP_457657847             307 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657847
VERSION     WP_457657847.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   3  (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   4  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32143
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..294
                     /region_name="PBP2_LTTR_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08423"
                     /db_xref="CDD:176115"
     Site            order(108..109,111..112,115,119,121..127,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176115"
ORIGIN      
        1 midarrlril ravadhrtvt aaaaalyltp savsqqlaal eqetghrlve rgargarlta
       61 ageillshtn lvlaqlerae aeladysagv agtvtvaafa tgiglvlapa ltelartapg
      121 irvkvqdaeg dasvpmvldr qvdvavavey rgapaeddrr ltrvplysep fdvvlpvnhr
      181 ladqaqvaia dlakdlwigq ypgnpchdvv vlaceyagfa prlehasddf havvalagad
      241 agvalvprsa lrgmeltgvv vrpvegsapt rrvfaavrqg aeghplirpv laameavavr
      301 eaglara
//
LOCUS       WP_457657855             326 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657855
VERSION     WP_457657855.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35758
     Region          163..306
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mppapsrlti rplsgpgeld lfrrlsyvld heladdlatg rrlpewmwva ldggrvvara
       61 awwtnapgge plaldffdld dalpaperie igvrllerat eavvpagarr peygrfvppd
      121 wredpvarev vgariaavea tgarmlverl rlewragtpv pgdsgrlvfr pvtgredlla
      181 lmtpvmegtl dahgqedlas gldaraaaek hydeelagys tpmawwriae lptgepvgfv
      241 iparnnyhpi iayigvlpar rghgyiddll aegtrvlaae gvdriraatd lgnvpmaksf
      301 drlgyvnfer afnmvwdaek segrtg
//
LOCUS       WP_457657857             326 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657857
VERSION     WP_457657857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34476
     Region          1..288
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mslrqmeyfv avveessftr aaerlhvtqp alshqikale ravggeller lprgvlltpm
       61 graflphaer svrsaaqarr aaraaagaqg gelhiatvhs vavgvlpdvf ahwrrahpgv
      121 clvlheyasa daledqverg iadlalgpvp erwsgplvpv geeeivlvvp fddplagrss
      181 valheladra wvrcamepvv dgrpfldgic gaagfeprta vrtehtstai rmaaagvgvs
      241 tapghtvrga lgedcavlsv dppwlralav fsrvpltgaa aaftellatl pvtgirpphp
      301 taasleraya dcgahpavvp wenarr
//
LOCUS       WP_457657860             288 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase enzyme family protein [Streptomyces griseus].
ACCESSION   WP_457657860
VERSION     WP_457657860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..288
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31326
     Region          5..272
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mnemrarevl taagfpgtae llalgenavf aagdlvvkvg rdatghpelr eraerevala
       61 dwlaasgvpa vraaerrprl veghpvtlwh rlpdpvrtae prdlaplltl vhalpaptef
      121 tlprrellgg verwlslagd aidpadadyl rerrdgfaaa aadlvphlpp gpihgdalpr
      181 nvhvgpdgpv lvdletfsad lrehdlvvla lsrdrygldp aaydaftsay gwdvrewegc
      241 avlrgareta scawvsqhap anpkalaefr rrvaslregd pevrwypf
//
LOCUS       WP_457657861             321 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657861
VERSION     WP_457657861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  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 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   3  (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   4  (residues 1 to 321)
  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 321)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32265
     Region          2..177
                     /region_name="CcmA"
                     /note="ABC-type transport system involved in cytochrome c
                     biogenesis, ATPase component [Posttranslational
                     modification, protein turnover, chaperones]; COG4133"
                     /db_xref="CDD:443308"
ORIGIN      
        1 mlrgvdlalp aralvrvega ngvgkstllr llagidapae gritgrpart ayvperfpaa
       61 lpltatgylv hlgrihglrt aeakrragew ltrfgaadha rtplaelskg tgqkvavaqa
      121 llaapdllvl deawtgldta araeldrava ervaagatvv fvdhdprrla gaadltlrta
      181 dggvhraaaa tapgpdpgpr vlieaagppg atlpaalpgd pvrerrsgtg gfgagaavsv
      241 pgggpgtggg tgyhgpdhga dsavvrltvp apysdallaa lltarppwhi rqvapaqapa
      301 pvtppespes seaaaevsea s
//
LOCUS       WP_457657867             424 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657867
VERSION     WP_457657867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42898
     Region          13..378
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,114..115,117..119,122,142,
                     145..146,149,223,226..227,230..232,235,252,256,309..310,
                     314,318,333,336..337,340..341,344)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrtyrelfrt peftpffaav svqtaastat glalgtlvya rtgspllsal amfgpslaqv
       61 agaltllsaa drlppraalt alaslsaaaa cvqaapglpl waafavllvv gtaaapgggv
      121 rygllneivp rggfllgrsv lnmtggatqi cgyavggllv tvfsargtll igaalyvvaa
      181 tvtrfgltar ppraagrpsv retrrtnall wsstprryvf lalwvpnglv vgceslyvay
      241 apghagllfa agalgmlagd tlvgrfvaar wrarlgaplr lllaapyllf alrpglplal
      301 avvvlasvgf aaslllqerl laltpqelsg qalglsssgm lamqgvgaav aggiaqltsp
      361 atgmaavagl svavtlalap glrdrneadr grllgadgsp rasrtpsppr tsstsstsst
      421 eett
//
LOCUS       WP_457657868             194 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar O-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657868
VERSION     WP_457657868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="sugar O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20222
     Region          18..186
                     /region_name="LbH_MAT_GAT"
                     /note="Maltose O-acetyltransferase (MAT) and Galactoside
                     O-acetyltransferase (GAT): MAT and GAT catalyze the
                     CoA-dependent acetylation of the 6-hydroxyl group of their
                     respective sugar substrates. MAT acetylates maltose and
                     glucose exclusively at the C6...; cd03357"
                     /db_xref="CDD:100047"
     Site            order(21,30,75,87,89,95,97,107,109,115,117,119,121,
                     128..129,131,143,145..146,151,163..164,167,169..170,
                     179..182,184)
                     /site_type="active"
                     /db_xref="CDD:100047"
     Site            order(21,30,75,87,89,95,97,107,117,119,128..129,131)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100047"
     Site            order(31,34,38,45,71,73..74,90..91,105,107,111,113,115,
                     119,121..123,125..126,132,134,141,143,146..148,151,159,
                     161,164..165,169,181)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100047"
     Site            order(115,117,119,121,143,145..146,151,163..164,169..170,
                     179..180,182)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100047"
ORIGIN      
        1 msdetrpsqk eamlsgelyi addpelaaea lhaavlsery natsaadpea rravlaellg
       61 evgegvevrp plrvdygyqt tigprtfinf gavlldvari tigadvqmgp nvqlltpthp
      121 vapeprrakw eaaqpitigd nvwlgggviv cpgvsigent vvgagavvtk dlpanvvavg
      181 nparvirkig eaea
//
LOCUS       WP_457657871             352 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657871
VERSION     WP_457657871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..352
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38064
     Region          23..348
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttidktahv papresvsgd gplldvrdlh vefhtrdgva kavngvnytv sagetlavlg
       61 esgsgksvta qtimgildmp pgkitqgeil frgqdmlkms neerrkirgr kiamifqdal
      121 sslnpvlsvg yqlgemfrvh qglskkaaka ksielmdqvk ipaaaarisd fphqfsggmr
      181 qrimiamala lepdliiade pttaldvtvq aqvmdllael qreynmglil ithdlgvvad
      241 vadkiavmya grivetapvd elysrpahpy tkglldsipr ldqkgqelya ikglppnltr
      301 ipagcafspr cpkaqdicrt dipplapvte qdglelvgrg sachfwketi hg
//
LOCUS       WP_457657873             337 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces griseus].
ACCESSION   WP_457657873
VERSION     WP_457657873.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..337
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35344
     Region          14..333
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 massvafshd fpfdpaygyd apdalldipa ppapdgfdaf wreryarara vaprpvlgpv
       61 eeerdgvrih gvrytsvggv rlggwlalpa egpvrygfvv ghgyggrqep grdlpaplpg
      121 aaailpcvrg mgergrvdgi pdlaaehvlh gigsrdtyvi gdcaadlwca asaltelvpe
      181 laragrpggp rlgylgesfg gglgalalpw ddrfgaaqlt vptfgnhplr lilrcagsge
      241 avrahhrahp evtdvlgyfd aataatrltl ptlvaaalfd psvpppgqfa vhnalagere
      301 lqvltaghfa yrgmtaeaae ldanrtrffg krlgavg
//
LOCUS       WP_457657872             821 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter family substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457657872
VERSION     WP_457657872.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Lewis,K.M., Greene,C.L., Sattler,S.A., Youn,B., Xun,L. and Kang,C.
  TITLE     The Structural Basis of the Binding of Various
            Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA
            from Chelativorans sp. BNC1
  JOURNAL   Int J Mol Sci 21 (11) (2020)
   PUBMED   32486296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Marland,Z., Beddoe,T., Zaker-Tabrizi,L., Lucet,I.S.,
            Brammananth,R., Whisstock,J.C., Wilce,M.C., Coppel,R.L.,
            Crellin,P.K. and Rossjohn,J.
  TITLE     Hijacking of a substrate-binding protein scaffold for use in
            mycobacterial cell wall biosynthesis
  JOURNAL   J Mol Biol 359 (4), 983-997 (2006)
   PUBMED   16698034
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..821
                     /product="ABC transporter family substrate-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86712
     Region          61..792
                     /region_name="PBP2_Lpqw"
                     /note="The substrate-binding domain of mycobacterial
                     lipoprotein Lpqw contains type 2 periplasmic binding fold;
                     cd08501"
                     /db_xref="CDD:173866"
ORIGIN      
        1 mshvgvprgt vrkrrslall ttgvltipvl agcssggeet srgvpqdiap aaretvadgs
       61 tvnwavdalp atfnafqada dsattritga llpslfpmdk sgqpklnpdy lesakviere
      121 pkqvvlykln qqavwsdgre igapdfvaqw ralsgkdsaf wtarnsgyer iekiergadd
      181 lqvrvtfskp yadwrslfsp lypkeitgsp dafndgartt lkntagpfvl rsvstskgtv
      241 tlarnprwwg dkakldtlvf ravaakdrtq aladgtvdva didaatadri tlarrdrgnn
      301 gqqpahgpgs eitpaaalrs walahgsdee aaeiaqaare knrkavvaya teqkalrdfa
      361 vrkslepayt qlalngesgp laddrvrrav araldrqela qtvlgplglp akplgshlal
      421 agqpgykdgs galgdqntke aqalladagw trggaaqlpk dtkagseaek kgdkdakedk
      481 dtkdgaeaek gtaedakkde dkdaktekte ksekeskeek adeeaedekg dkkagrased
      541 saasrdegly ivgednkpga qapahasasg asglhviapa rtaaaqsaal lrqagvvged
      601 gtvaaqdkqp ggaagayapv gtaapapaaa kgqlgkdgkt ltlrfvlpsg pgsqslrsvg
      661 dkiaamleki gigteitkvp desyfkdhia sgeydlalys wpataypatd grpiyakpep
      721 atdgsllveq nytrvgtdhi dqlfdqaaae ldekaarelm kqadariwaa agsiplfqrp
      781 qlvavdkkla nvgafgfaap ryqdigfknr qaagspadrk k
//
LOCUS       WP_457657888             371 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine synthase [Streptomyces griseus].
ACCESSION   WP_457657888
VERSION     WP_457657888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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..371
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..371
                     /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=38332
     Region          51..366
                     /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..177,208,326..328,329..330,362)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(95,121,222..226,360)
                     /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 mttyhcpvdg trsettaltw ccpvcrgpwd ldftpvrgva pnalsvrads lwryeeflpl
       61 aaptislgeg rtplvaltdt vsakldylmp tlsfkdrgav llvelarrlg pdrvvadstg
      121 nagtsvaayc araglactvy vpegtsakkt eqirahgahl vtvpggreat alaaraaade
      181 pgvfyashvf npyflhgtkt yvyelweelg grlpdalavp vgngtlllga alaiaelhal
      241 glietrprli avqaeavspl aaafhagldd lppaapaapp sptlaegiai prpprarqil
      301 aavrasggtf ltvpedhira aqqdlasrgf yvettgvacw aavrdggggt aggsvvvplc
      361 gaglktgmaa g
//
LOCUS       WP_457657887             134 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces griseus].
ACCESSION   WP_457657887
VERSION     WP_457657887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 134)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..134
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14544
     Region          6..127
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mmavlidtva wvrieggril carprgkdvf yipggkrega etdlqtllre ieeeltvgli
       61 retvvhagty eapvdgrpda avvrmscyyg dyrgtlaass eieevawfsf adralvppvd
      121 qllfddlkaa gala
//
LOCUS       WP_457657891             363 aa            linear   BCT 27-JAN-2026
DEFINITION  SPFH domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657891
VERSION     WP_457657891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..363
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=39315
     Region          23..280
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mdpvvipilv aalvvvflva atvrivpqar rynierfgry rrtlqpglnf vlpvadrvnt
       61 kldvreqvys sdpkpvited nlvvnidtvl yyqitdpraa ayevadylqa idqltvttlr
      121 nvigsmdleg tltsreeina rlravlddat gkwgirvnrv eikaidppnt ikeamekqmr
      181 aerdkraail haegerqaki ltaegtkqkd ileaqgtqqa milradgesk avelvfqavh
      241 rnnadakvla ykyletlphl aqsdnntfwv ipgelteair tvttafgdqs aaagppaagq
      301 qdsaadiads dkdnvgvpei epnstlalda vaaadeaakq aaaavsdaka eaeaagetrl
      361 pgr
//
LOCUS       WP_457657893             492 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces griseus].
ACCESSION   WP_457657893
VERSION     WP_457657893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..492
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49599
     Region          41..475
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 masvsesgsg sgsgsgsgsg sgsgsgggpg ggpgggsgss aeegklrrtl gfrdlvvygl
       61 lfiapmapvg vfgtldaksd gavalvyvva tvvmaftafs yaqmvrvapf agsvftyark
      121 glgegpgfia gwmamldyll ipavaylfsg iamnalvpev srwvwtaiav lvttllnlwg
      181 vraaarvgfa vlameivvll vfvvsavvvl vrdgaqrgwl tpltgdtgfs maavlgavsi
      241 avlsylgfda iasfaeevtg gsqkvaravl fclvlagvlf vaqsylaall epvssaelaa
      301 dpaaqgsafy davdasvgtw lhdlvavska igaafaalag qaaagrlvfa marerrlphl
      361 lakvdpksgv prvailgaav vtlvaavwaa rrddgldhlv svvdigalta fvllhasvvg
      421 wfvvrrmagp pvwwrhvlvp vvgagvliav iveatasaqv vglcwlavgl vvlavqgtgr
      481 rggaagpggp gr
//
LOCUS       WP_457657901             451 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657901
VERSION     WP_457657901.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..451
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47920
     Region          15..421
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,75,133..134,136..138,141,161,
                     164..165,168,251,254..255,258..260,263,291,295,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpepastpaa raslrkvvta salgttveyy dftlyattaa lvfdkvffpd asplvgtlaa
       61 fatyfvgyla rplggiifgh ygdrigrknv littmlmmgi gtfaigllps ydsigiaapi
      121 llvlirliqg lgmggeyggg vlmaleyspp rrqgfftslv higtpagvli pvglvtilds
      181 tlpagsydsw awrlpflvsi llvgvgvwmr lhvtespefv kmredrgvqs lpvrevitrr
      241 trtvvlsvla kiaesglfni yyvvaityvt aeldlpkgpv llavliacav ecctlpffga
      301 lsdrigrrkv yvagaafqav lalpffllie tgqfwaytlg mtlglgvgha amygaqgalf
      361 snlypvnvry tglsvtqqig atlggglspl igtallsvgg ghwswlivyc vgvavlsgla
      421 asrlrqgemd aapdtvtaer rpespertqv s
//
LOCUS       WP_457657905             297 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657905
VERSION     WP_457657905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32027
     Region          1..295
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mqlfqveyfv avaetlsftk garranvvqs aasaavhrle relgcelfer kgrtvrltta
       61 gtallphaya llnevraard avdatrgvir gkvtfgtlvh pgpidllkvl aqlrhehdgv
      121 vvklrqtirg tassldevrd gtldlalvss aqpsvpgvhl thlyaepfvl ihserhplaa
      181 rpaveltdtv teafidfpqg wgnrgaidal faehgldrrv rtevvafdma lelvrsdlgi
      241 afvprstvtd atgirvravg dadvrwpvql arstarslsa agrvvsqavl shvhdgp
//
LOCUS       WP_457657906             942 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657906
VERSION     WP_457657906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..942
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99330
     Region          <22..916
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 msgepvdeyt attaagrsgt avirqaeldr llaavtaprt adgvtrpkdt lltlagepga
       61 gkttlveavv arfaanggrv lradsstset dlafsglhql lwpvrgrida lpprqrgalh
      121 aafgaaerse apdpmligta altvlsdlat krplllavdd aqwtdrasld tlsfvarrla
      181 depvtllvvt rdsaprglaa reptltlgpl drgaaerlld rqprvpiglt rarildqaeg
      241 nplalvelar avgdsddatr gtdgplpvtd rleriyadrl aalptetrra vvrlatadtq
      301 dpshtvlswl pdigdpvwap aeeaglvrrg ggrlrcghpl srlaiyhaap aeerraahle
      361 laglfgdqdp drhawhlaaa tsglsavvsa elegsadrar hrsgyaaaah mleraadlhp
      421 drrestrlla aatstavltg rldsverlaa rtragtddpt aaalaalqvg rlmalttshs
      481 aafgqlmrpa aalvgtdpga asealaaasv vrfyssdadq lheierllpl vqphpghrlg
      541 erktllaawt gvvahpdaad aslalrlpal vaaareepet ltllavaawl ldetelaaqt
      601 fdaalaswts qgplpdglgg vaafayleqg rwaraqtaca elaavassvg ldhaaacaaa
      661 teallralrg dvvgartqar yalslvdpre srsvlalahr algaaataeg dhetayqhyr
      721 vlfdgrgnpa hyhlaypalp elavaaarsg hheeatgivd gversladag alaprrtalv
      781 rlshaalapt geaehhftaa lgtpalarrp feraqallay gewlrrrrri adarpplaea
      841 eavfqrlaaq pwvaraqsel raagaqsgtt epdafadltp qqqqivrlaa lgltnrevae
      901 klylsprtvs shlyrafpkl gitvrsqlrh vvdamaadgg tg
//
LOCUS       WP_457657907             331 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457657907
VERSION     WP_457657907.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34391
     Region          10..308
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(44,257,260)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(197,228,255,258..259,262)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 martgspgsi tvlgesvadi fiepdrsgpd glslralpgg gpantavala rlgtptrflg
       61 rfsndafgsl frarlaasgv dltggvtape hstlavadld aagqasytfy adgaadwqwt
      121 vpeldtawvd npvclhtgsl alirqpggsr iedhlaqvre httvsidpnv rplfmppsay
      181 rdrmplwcpv adilrlseed cavlapgasl eeacdtwhda girlvvitmg grgalaslgg
      241 srvtvpappv dvvdtvgagd sftagllhrl atlgrlggrl ddlpledvad acsfaarvaa
      301 ltcsvpganp pwaddpalrf htarhqplpe g
//
LOCUS       WP_457657908             497 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 32 protein [Streptomyces griseus].
ACCESSION   WP_457657908
VERSION     WP_457657908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..497
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54418
     Region          6..470
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mptspadphl paihlrpprn windpnglvf hdghyhvffq ynphgpqhsn vhwghfrspd
       61 linweplpva ltptpggyda dgcysgnavs vdgsivafys ahrndrwwqp ittaasrddg
      121 rtwakrpell iadppagttm yrdpyvwqqd erwrmlvgaa lddgraaall yesddleqwt
      181 ylgpfhtsdt asgtgpvgwe cpqyatfgdr silivsdwtp qsgpshttvh tgrehngrft
      241 paaspvpldh gpdiyapall kvpgtnrwll wgwawearde gwaheagwag vltlprevsl
      301 ttdgtvvqrp arellalrsa rvlhrtgsvv rtepaelgqv srtfdltasl vpdptgtsgl
      361 rlvtsadgse yldihldpta gqlvvdrsha srdarartga ytvpcptasr pgtlvelrvv
      421 vdgsiaevyl adgqvltlrf ypvgdgpwrl earttgtgrs eyaveawnla leevrgetll
      481 tdrgrapelc agaiptt
//
LOCUS       WP_457657909             433 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457657909
VERSION     WP_457657909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 433)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 433)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..433
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46573
     Region          39..421
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(148,150,280,282,312..314,351)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mlfrtrrlaa asvavtaata lvagctsgga stsgasgdtl tlwthnagns veldvvkkii
       61 kdfngsqdty kvklqafpqs dynnsvvaaa sakklpclld vdgpnvanwa wggyldpidv
      121 tgsevpvlsq lestvgrydd klyafgfydv slaffarksv leehgirvat mdkpwtkaef
      181 dsalaklkks gkfeyplemg tggtgewwsy gyspqlqsfg gdlidrgdyk sasgtldsea
      241 avdwatwfqs lvakdymakk sgadpnkdfl agksaiqwdg swnaaknaek lgddlaiipp
      301 vdfgegpkig gaswqwamss tcsnkagaqe wlkfsrqtky fteyakatst ipateaaakq
      361 iadyqpggkf dvlvefarky atvrpatpay pyistefeka akdilagadp qkalgqaakd
      421 idsnlktnny ysn
//
LOCUS       WP_457657913             577 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657913
VERSION     WP_457657913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 577)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 577)
  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 577)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..577
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62062
     Region          2..574
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mlikllrshl gpykkpivll vclqllqtca tlylpslnad iidngvvtgd tgyilefggl
       61 miavsvlqvl cnvgavyyga rtasalgrdv raavfdrvqs fsarelgrfg apslitrttn
      121 dvqqvqmvvl laftlmvsap imcvggivma lgldvplsav llavvpvlgv svglivrkmg
      181 plfrtmqerl dgvnrvlreq itgnrviraf vrdgyeekrf rganteltdv svatgrlmal
      241 mfptvmtvvn lssvavvwfg ahridsggmq igaltaflay lmqivmavmm atfmfmmvpr
      301 aevcaeriee vlgtessvvp pvapvtelrr hghlevrgae frypgaeepv lravdlvarp
      361 gettavigst gsgkstllgl vprlfdvtdg avlvdgedvr tldpvllskt vslvpqkpyl
      421 fsgtvatnlr ygnpdasdee lwhalevaqa kefvealehg ldapiaqggt nvsggqrqrl
      481 aiartlvqrp eiylfddsfs aldyatdaal raalgretag atvvivaqrv stirdadril
      541 vldegrlvgs gthhelmegn etyreivlsq lteaeaa
//
LOCUS       WP_457657914             306 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces griseus].
ACCESSION   WP_457657914
VERSION     WP_457657914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..306
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=31909
     Region          62..290
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtepapeqsq qppppidsta qlltritdrl gaqlslvsrn gtrrpmhrtr qpdhpaphpg
       61 gapapslvav ahgsrdpeal rtvlalldrv relrpgldvr lghielnrpl lpdtldglrg
      121 adavlvplll grghhvkrdl pataaaapav rtriaaplgp hpllvealyg rlveagwdaa
      181 drggrgaavv laaagsrdpd sardtrrtar llaerlgvpv vpayasattp tvpaalrala
      241 argrhrafva syftapgrfa sacaqaaphr aaaplgahpa marlvlhryd qaraaaapav
      301 sllasa
//
LOCUS       WP_457657919             387 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657919
VERSION     WP_457657919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..387
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40432
     Region          29..361
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msalpapsta arrldparaa saadgraatg arvefrslrr afgptvaldg ldltaepgel
       61 lallgpsgcg kttalrvlag feqpdsgevl vdgeditrvp anrrdagmvf qsyslfphln
      121 ardnvafglr vrkvsaaerh ataaelldlv glpdhggrfp hqmsggqqqr valaralalr
      181 prvllldepl saldakvrls lreeirrlql slgittifvt hdqeealsma drvavlnagr
      241 leqcappael yerpatafva efvgtmnrlp grltgtgsve vagatlpvdg eapagggpvd
      301 vlirpegira dadpegtatv vsasflgsvt rvlldlrggv alkadlpsrd aadllpgvra
      361 rvtpvprpvl vvpatpvtde rtgkasv
//
LOCUS       WP_457657920             303 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657920
VERSION     WP_457657920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31777
     Region          25..283
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 maaltplstd pvstdsvaap vrtarrrpry wrgavltvag lyfltplvss fvftvqvpnq
       61 gltfaaysgi lsadgftesl flslslaaat ialalllvvp alvavrlgpp rlravveivc
      121 mlplvvppia lvtgiatvlr wgpdhfsrtp lyqtflavqn esfpvvlvla ytvlalpfvh
      181 rsldaglrav dvptlveaar ncgagrlyvi lrvilpnlrs slagasfltl alvlgeytva
      241 sllgfrpfav wivsvsgaea rmsvavslls llitwalllv lsragtgssa avpaaptpvp
      301 gke
//
LOCUS       WP_457657925             297 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657925
VERSION     WP_457657925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..297
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30321
     Region          1..294
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,121,125,146..151,170..171,173,186,
                     207..208,229..230)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mkkvtfaafg gpdvlrlvda eephagpgri rvsvraagvn pvdwrlregq vlgahpislp
       61 sgvgidaagv vdevgegveg veigdhvfge gadtyaefav lsawarmpeg ltfeeaagyp
      121 svvetalrvl revgarpget llvsgasggv gsavlqiard rgipvigtag aanqdylrgl
      181 galattygeg wvervrrlgp vgaaldlags gvipelvelt gdpakvisia dleaprfgvr
      241 fsgvagsvpd alaeaatlis hgrlhipvek syalgdaaaa hadsraghar grrvmvi
//
LOCUS       WP_457657926             177 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457657926
VERSION     WP_457657926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19338
     Region          19..158
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mpeepttstt ttldgvltrl vptteddldl lagwfaspdf vtywggvpls rdevaekyvg
       61 rrrprvqsyl vlaegvpvgy aqfwhadape dgtesgtegg idlvlqpasq grglgpdatr
      121 allahvggel gwrrvtvdpv renvravraw ekagfrqvps etgepllefr fpegrrh
//
LOCUS       WP_457657928             311 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657928
VERSION     WP_457657928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 311)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34017
     Region          7..108
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(8..10,24,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,90,94,100,104,107..108)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mngdtlysig elarrtgltv ktirfysdrg ivaptdrspa gyrrytvdav arldlvrtlr
       61 elgldlptir kvvdrdlslp avaaahaeal avqirvlsmr ravltavaer gstpeetelm
      121 hrlaqlsrde rrrlvgefld avfdgldaap afagvmrsmt pelpdnpdae qvrawvelae
      181 msqdpdfral vrrmiedlaa eqarsgtavp rrdiaaavrd eagpalaagl dpasaqadpv
      241 vaaftahyaq ligrpddddl rrllaarlen vndprreryf qllavvngwp apaslapvld
      301 wsvqalrvrt a
//
LOCUS       WP_457657936             231 aa            linear   BCT 27-JAN-2026
DEFINITION  SanA/YdcF family protein [Streptomyces griseus].
ACCESSION   WP_457657936
VERSION     WP_457657936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Chao,K.L., Lim,K., Lehmann,C., Doseeva,V., Howard,A.J.,
            Schwarz,F.P. and Herzberg,O.
  TITLE     The Escherichia coli YdcF binds S-adenosyl-L-methionine and adopts
            an alpha/beta-fold characteristic of nucleotide-utilizing enzymes
  JOURNAL   Proteins 72 (1), 506-509 (2008)
   PUBMED   18393394
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Rida,S., Caillet,J. and Alix,J.H.
  TITLE     Amplification of a novel gene, sanA, abolishes a
            vancomycin-sensitive defect in Escherichia coli
  JOURNAL   J Bacteriol 178 (1), 94-102 (1996)
   PUBMED   8550448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..231
                     /product="SanA/YdcF family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=25281
     Region          25..223
                     /region_name="SanA"
                     /note="Uncharacterized periplasmic protein SanA, affects
                     membrane permeability for vancomycin [Cell
                     wall/membrane/envelope biogenesis]; COG2949"
                     /db_xref="CDD:442192"
ORIGIN      
        1 mkevrwparp vlrlprtrrg rrrlvqglma acvlallpat wmrleagdrv gttseapare
       61 vamvfgaglw kgrptpylah rldaaaelyr tgkvkvvlvt gdnsrveyde pdamrtyltg
      121 rgvpderivs dyagfdswds cvrakkifgv dravlvsqgf hihravtlcr sagidaygvg
      181 vdeprdsvwy yggvrelaas gkaaldavfr pdprflgpee pgvtealadt p
//
LOCUS       WP_457657939             417 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite oxidase [Streptomyces griseus].
ACCESSION   WP_457657939
VERSION     WP_457657939.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Hsiao,J.C., McGrath,A.P., Kielmann,L., Kalimuthu,P., Darain,F.,
            Bernhardt,P.V., Harmer,J., Lee,M., Meyers,K., Maher,M.J. and
            Kappler,U.
  TITLE     The central active site arginine in sulfite oxidizing enzymes
            alters kinetic properties by controlling electron transfer and
            redox interactions
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (1), 19-27 (2018)
   PUBMED   28986298
REFERENCE   2  (residues 1 to 417)
  AUTHORS   McGrath,A.P., Laming,E.L., Casas Garcia,G.P., Kvansakul,M.,
            Guss,J.M., Trewhella,J., Calmes,B., Bernhardt,P.V., Hanson,G.R.,
            Kappler,U. and Maher,M.J.
  TITLE     Structural basis of interprotein electron transfer in bacterial
            sulfite oxidation
  JOURNAL   Elife 4, e09066 (2015)
   PUBMED   26687009
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Barber,M.J. and Neame,P.J.
  TITLE     A conserved cysteine in molybdenum oxotransferases
  JOURNAL   J Biol Chem 265 (34), 20912-20915 (1990)
   PUBMED   2249998
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Campbell,W.H. and Kinghorn,K.R.
  TITLE     Functional domains of assimilatory nitrate reductases and nitrite
            reductases
  JOURNAL   Trends Biochem Sci 15 (8), 315-319 (1990)
   PUBMED   2204158
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Neame,P.J. and Barber,M.J.
  TITLE     Conserved domains in molybdenum hydroxylases. The amino acid
            sequence of chicken hepatic sulfite oxidase
  JOURNAL   J Biol Chem 264 (35), 20894-20901 (1989)
   PUBMED   2687265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..417
                     /product="sulfite oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44994
     Region          96..414
                     /region_name="SO_family_Moco_dimer"
                     /note="Subgroup of sulfite oxidase (SO) family
                     molybdopterin binding domains that contains conserved
                     dimerization domain. This molybdopterin cofactor (Moco)
                     binding domain is found in a variety of oxidoreductases,
                     main members of this family are nitrate...; cd02110"
                     /db_xref="CDD:239028"
     Site            order(97..98,100,102,148,216,247,252,260,263,265..266)
                     /site_type="active"
                     /note="Moco binding site [active]"
                     /db_xref="CDD:239028"
     Site            148
                     /site_type="other"
                     /note="metal coordination site [ion binding]"
                     /db_xref="CDD:239028"
     Site            order(305,335,339,341,350,352,384,389..391,409)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239028"
ORIGIN      
        1 mspvpteday drirmrqwsr grarsagier rdllklvaaa saavplasva aparaadglp
       61 gvvkplppel ftlrgtnaet nfdalrdtgl ltpadrffvr nhtatpridr agwkltvwgd
      121 glrggpvdft fadllalppv trtafvecag ngrsyftsqq gqpvsgtawt lgaigtarwr
      181 gvrladvlrr agigrhavdv lprgldaevv tdgvnlgrvr rplpvakald dvllayemng
      241 eplppdhghp vrlivpswvg ianikwvgdi evsaeplltp wntglyrlfg pgyppegsap
      301 ltrqtlksaf elapgasfra hrralltgrs wsggapvrav evstdggthw rtarlrdepr
      361 agswvrwaad wvprergpav llaragdrsg rrqpvatahn tqgylfdavv rhavtvv
//
LOCUS       WP_457657940             261 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657940
VERSION     WP_457657940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27481
     Region          9..257
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msllgngglr aervgreagg rlildgvdia pppgstvgli gpngsgkstl lrilagllap
       61 atgvvtldgn plaglgrrtv arriavvdqh avtqvdlsvl dvvrlgriph srawsapdrt
      121 dedavaealr rtgltdrggq swhtlsgger qrvqiarala qqprelllde ptnhldiqhq
      181 ldllalvael pvtsvvalhd lnlaamfcdr itvmkagrvv aggtpaevit geliedvygv
      241 ravvtpegpd grpsvrflpr r
//
LOCUS       WP_457657942             407 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces griseus].
ACCESSION   WP_457657942
VERSION     WP_457657942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 407)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=41208
     Region          6..406
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mkrpaiavtg lgmitpvght tdatwdgvca gespartvpe lhgcavdfac tvsgidldea
       61 vggrtafrmg ryvkfavlaa reavadagld pehwdgtrva vvvgtssggs aglteqaval
      121 errgpeatsp sgilltipnm paaeiairmk atgpslapct acssgvtals vardmltlgh
      181 cdiaiagate sivfpvamtg farsgaaapr dgdparlcrp faadragivm gegaavmvle
      241 raedararga spraliagtg attdahhpts phpsgdvara avdgalrdag wrpedvdhvn
      301 ahgtstplnd ateaaligra yphrppvtap kgvlghcmga agaieaglti ltlqhgmipp
      361 ianldapepg fdidcvtkap revpvrravs hsfgfggqna vvalqap
//
LOCUS       WP_457657944             310 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457657944
VERSION     WP_457657944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..310
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31674
     Region          8..295
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(35,240,243)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,211,238,241..242,245)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mldhsellvv gecvadivrl pdeadrvhpg gspanvaygl arlghravll tqlgpdengr
       61 lvrdhlvsgg vdvrtdgsta rtpsaavtld gagqasyafd vswtlapvav epapvhvhtg
      121 sigavvepgs atvldlvraa ratatvsydp nvrpglmgdr taavrrveec vglsdvvkas
      181 dedlewlypg edpeqvaagw lgrgpavvlv trggdgalav lpggrvtvea pavevadtvg
      241 agdafmsgtl halaaqgllg pdarerlrav drdtvadvlr havasaavtv sraganppgp
      301 delrealahn
//
LOCUS       WP_457657946             504 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 32 protein [Streptomyces griseus].
ACCESSION   WP_457657946
VERSION     WP_457657946.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..504
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55091
     Region          26..493
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mthdltlpra rhqdapqgla eravldphrp rfhftapggw lndpnglahr dglyhlfyqy
       61 nplaaahhri hwghatsrdl vtwtdepval vpgadgpdrd gcwsgvlvdd agtptlvysg
      121 rhgdrelpcv atgspdlrtw rkdpanpvia apppgdltaf rdhcvwrega lwrhlvgsgi
      181 rgeggtafly esedlrswry vgplltgdas tgtaadpdwt gtmwecvdlf rvdgadilaf
      241 sawdegtthh plywtgryeg dtftpdrlhr ldyggryfya pqstrddrgr rimfgwlqeg
      301 rdedamarag wcgvmslprv vtltadgsla qapapelarl rrksvhagpf tvadgtyagl
      361 davrgdqldi eatlrlapgt aarvtvrasg dgtertvvev araqdgtgtl rlhreassld
      421 ptvdtepryg elplndsgev dlrilvdhsa levfaggral tariyptlpd algvgveavg
      481 eiaverfdaw qmaaifdgpr plwp
//
LOCUS       WP_457657948             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657948
VERSION     WP_457657948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34451
     Region          9..313
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtpsfdgpvl dvtnlrvayg gdgrsvlgad dvsfsigrge vfglagesgc gkstvanaim
       61 rllkppaait gsvtfkgrdv lamdprelra frwreiamvf qsamnslnpv ltvgeqigdi
      121 fttheklkkr hararsgell elvgidparl ksyphqlsgg mrqrvviama valkpsllim
      181 depttaldvv vqqeimaqig dlqrelgfsv lfithdmslm ielshrmgvm yggrlvelas
      241 akalfvdplh pytralmgaf ppltgprvhl tglsdaprta encgfhavcp vdrsdcshhi
      301 pdlrevadgr fvattaggpr
//
LOCUS       WP_457657949             332 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657949
VERSION     WP_457657949.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34013
     Region          21..296
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 msvldtrtas gertagaapt prrgragllr allanrkalf gaavlavfvl lavlapvlap
       61 gdpskinsag asepsaahpl gttakgqdvl altlwgarss llvgfsvgla atalavlvgm
      121 aaayfgritd dllslitnvf llvpgvpllv ilaafmppgt ttvilvlvit gwagsarvlr
      181 aqaksirgkd fvaasvvsge rplrimfrei lpnmasvvmt tllgcvifgi gaqagleflg
      241 lgdasvvswg tnlywagndg almtgawwvf vpsglcialv afalamanya vdeitnprlr
      301 trrpkgravt gsragahapa vteapapark es
//
LOCUS       WP_457657950             558 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457657950
VERSION     WP_457657950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 558)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 558)
  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 558)
  AUTHORS   ter Beek,J., 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 558)
  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   6  (residues 1 to 558)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 558)
  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 10170725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..558
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60563
     Region          44..536
                     /region_name="PBP2_TmCBP_oligosaccharides_like"
                     /note="The substrate binding domain of a cellulose-binding
                     protein from Thermotoga maritima contains the type 2
                     periplasmic binding fold; cd08509"
                     /db_xref="CDD:173874"
     Site            order(48,255,437,518)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:173874"
ORIGIN      
        1 msssirvrra rraallaaat alllsgcsga gasgaadtsg kqlltipred fatftrnfnp
       61 fapgqvvapl tsqavyeaml vynpadgktt pwlatsweta pdgktvtftl rpgvkwsdgk
      121 pltaedvayt falqkkllgg yeylesarae gagkvvftln kpyspgvfel gkqvivpkhv
      181 wekvkdpakd tnpnpvgtgp ytqvaafqsq syelrknpey wqpdkqaveg irvlgfsgnd
      241 sanlafvnge adwtqsfipd idksfvaknp ehnkywyprt gslvewtmnt trapfddaav
      301 rkalsqavdr ksvtkvgmng ytepadctgl sggydtwrdk slakactwtk hdavaagkal
      361 daagykkged gkrtlknakp fafdisvgsa ssdwlsvani ikqnlaeigv tatvkspdwa
      421 avvssyetgd ydtgivwsdn gatpyqfyrn tlstesvkpv gtralnnyhr fgtkkadvll
      481 dafaassdea aqreqidalq rlfdeqapvv plfpgpewgs ytdtrftgwp teddpyatlt
      541 nrgdttvlvl tslkpvkr
//
LOCUS       WP_457657951             460 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457657951
VERSION     WP_457657951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 999995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..460
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45152
     Region          20..>241
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
ORIGIN      
        1 mtgrpasaat ghvldgvtar rrfvtvsflf wlpigmslap avllftergm glaaiagffa
       61 ahsltaatme lptggfsdvv grravlatag llnlsaltll glgtdawvfi lgmalmgsar
      121 alssgpaeaw yvdtvhaaag peadvrtgla rgssavsaal algtllggal pwllglgpdp
      181 gawltdvtsg lvlplsapal lgaavegvfv lhvlralpep prpkatlrgv lggvpaaiad
      241 glrlgardtl irrvllaasa agaalatlel ltpgraaalt gaaesgavlf aglacagfvc
      301 salgsqlapg aarmagsser avlvglgaga tglvllgita atssttdala tttaaagygl
      361 vylglgiagp nendllhrrv dssgratals vqslalqlcg agaglvagvl plgplpwlla
      421 atavlaaall warrtapakp lpgavphtat eapaaasnqp
//
LOCUS       WP_457657954             315 aa            linear   BCT 27-JAN-2026
DEFINITION  YihY/virulence factor BrkB family protein [Streptomyces griseus].
ACCESSION   WP_457657954
VERSION     WP_457657954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..315
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33459
     Region          14..288
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mptqtasaae saaptagraa psgrwptalr rtpvslwndd vtdwaaalty yailallpal
       61 lvtvsvigla npdatsalia ditafapaes gealrrplea ateqrtavwv lvatgsvsav
      121 wsacsylavf rramhamhqv rdtrpalrka hiivvsaigl lvllmtsala lvltgplarw
      181 lgrriglphg getlwavlkw pvllclvacl ilvlfrtgpr pargirrglp ggvlaaflwl
      241 assagfalya trigsysrly gslaglvvfl iwvwfanlsl lagaqfnvel erreaepeee
      301 pgtaadkpvk aaers
//
LOCUS       WP_457657956             396 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457657956
VERSION     WP_457657956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10531344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39872
     Region          46..106
                     /region_name="Inhibitor_I9"
                     /note="Peptidase inhibitor I9; pfam05922"
                     /db_xref="CDD:428674"
     Region          124..376
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(127,130..131)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(155,188,250..251,278,338,341)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(155,188,341)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(292,294,317)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mrlparwata alllvaplia vpttasadtg pegvlveqst ravpgqyivt lepelspetv
       61 lrefgltplf tygsvlhgfa atltatelea vrtvpgvlav eenaevavet pragglfrap
      121 aagwgtdrid qralplddtf tttatgkgvk ayvvdtgida ahsefggrvv ngfdaigdgr
      181 ggmdcnghgt hvagtvggat sgvaqdvslv nvrvlncegr gtwagilagf dwvakdaarg
      241 tapavlnasl ggarssavda avesvadagv lpvvaagndd rdacdvspaa adgvvtvgas
      301 drqdretsfs nwgsclelya pgadivsarl gggtvalngt smasphvagv aalykqenps
      361 aspaavarwl tdtatpdvls glgqgspdrl lytggl
//
LOCUS       WP_457657958             346 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657958
VERSION     WP_457657958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..346
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34685
     Region          39..342
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mttldtrtpp davtrrpagv rllwvllsvl alaavmvasv afgsrdvpws dvvaalggad
       61 dtlgraaatk rvprtvlavv igaalglagg vmqgvtrnpl adpgilgvnm gaslavvtav
      121 affgltsptg yiwvaivgaa lsalfvytvg tlgrggatpl klalagaats aafaslvsav
      181 ilprndiags fklwqiggvg gasferigqv apflavgfvv cllsaralns lalgdelaag
      241 lgervavara vaalgavllc gaatavagpi gfvglvvpht crllvgvdhr wllplsavlg
      301 avlltaadvi grivarpsei dvgivtalvg apffiyivrr qkvral
//
LOCUS       WP_457657957             279 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657957
VERSION     WP_457657957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..279
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29896
     Region          6..259
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtthhrltae gltlgygert vvdsldlavp pgritvivga nacgkstllr smsrlltpra
       61 grvvldgkev hrlpakelar tlgllpqspv apegitvsdl vgrgrhphqg ifsrwnekdd
      121 aavaaaleat hteplaerav delsggqrqr vwiamalaqq tdlllldept tfldashqie
      181 vldlltdlnr srgttivmvl hdlnlaarya dhlialaggg lhasgtpaev lteetvravf
      241 dldsriiedp vsgrplmlpi grhhvldrae alpvgestt
//
LOCUS       WP_457657959             397 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657959
VERSION     WP_457657959.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..397
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41422
     Region          7..384
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnppgsvlvv gagaaglstv ealrrkgftg ritvlgdedt apydrpplsk qvlagdwtae
       61 rarlrareal daleadfllg eaarsldaaa rtvrtsagre ltadavvlat glrpralaca
      121 pgvrvlrtla eatalrgdll gasrvvvvgn gvlgseiaat vrrmgpavtl vgpqpapmad
      181 qigsgvalhl aalhrrhgve lrdstlvdgt vaetgpsrgv rlasgeivea dlvvaavgsl
      241 patdwlagsg lriadgvvcd srcraaegvy avgdvarwhh aalgvslrle nrtnageqal
      301 avaadilgad rpftpvpyyw sdqydvkiqv yglptpdada evvegspdeg rfvvrytrgd
      361 apvgvlgwnm pkqtrlhrqt llerytrtaa ptaptps
//
LOCUS       WP_457657960             410 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces griseus].
ACCESSION   WP_457657960
VERSION     WP_457657960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 410)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..410
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44400
     Region          28..410
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(74,96,98..99,182..183,192..193,196,199..200,203,238,
                     241..242,245..247,250,295,297..300,324,400)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(97..98,105,109,116,161,164,242..243,246..247,
                     250..251,254,294..295,298..299,301,324,351..353,356..357,
                     359..361,364..365)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtidspaavp sgvpdfpepr sarcpfdpsp elraladhgp ltrvrswggt tpwavtghae
       61 qkallsdprl saefsrpgfp spvdprhaha ggtdlsfvgm ddpeharlrr mvsgaftvkr
      121 vealrpvvqr madehidrml sgprpadlvt alalpipslv isemlgvpya dhaffqansk
      181 tlvsavatae erglahrilv dylhrlvgek ldspgddlls tlaerirage ltragaaamg
      241 vllllgghet tanmislgtl illdhpdqla rvrdtddpav vtaaveellr ylsivhlgrr
      301 rtaledieig grtiragdgv illgelanrd pavfpdpdrl ditrnarlhq afgagthhcv
      361 gqplarmelq viyptlfrri ptlraaeavd rlpfkydavv yglhalpvtw
//
LOCUS       WP_457657968             391 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657968
VERSION     WP_457657968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42030
     Region          42..324
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mifrrswltv avlalavssl psaaasaaph psgtgwsvqr dadalrdtgv tgvavrvetp
       61 rgttearsgv gdlvtrrpvp rdgylrlgst tktfvatvvl qlvgekrisl drsveellpg
      121 vvsgagndgr titvrdllrh tsglsdyihd vfpdpgarty faqrwtayep eelvalamrh
      181 epafpagtgw eysntnyvla gmiiqkvtgr tweqqvheri lrpldlrhtd tpgtdpflpy
      241 phtadyqqfa edgpmvdtti pyrpfdsgad gsmtgtardl nrfysalagg rllrpaelaa
      301 mrtmvpvpqd gghpagtrdg lglfftplsc gggylghggs gfgyvvraat ttdsrrtvtv
      361 sahsragdar saarqedalr tlvdralcrt p
//
LOCUS       WP_457657963             546 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657963
VERSION     WP_457657963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 546)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..546
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=58659
     Region          23..518
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 maptqatpqh petagagaaa vadpvlears vskrfpgvva ldgvsfalra gevhalvgen
       61 gagkstlikv ltgvyrsdeg evrvagepvr farpfeaqqa gistiyqevn lvplmsvarn
      121 iflgrepknr fglidfarmn rettelldgf gvrvdpkrpl htlgigtqqm valaravsvk
      181 aqvvimdept ssleprevet lfrvienlrg qgiavlyvsh rmdelyricd rvtvlrdgrh
      241 ihtgelaple rmqlvsmmlg rdmaevrreg ltnfdaaghe vartpvltat gldrrhqlhd
      301 isvelyagev lglggllgsg rsetakaltg alpldggeir vdgkrigrpt paaairagis
      361 mlpedrkaeg ivpglsvren ivlaamprls rggivsrakq drivdifmkr lrikasspeq
      421 kvgelsggnq qkvllarwlc lepkvlllde ptrgidvgak aevqslidel areglavlli
      481 ssdieelieg adrivvlrgg avagelagde vdesrllevl adhtpdtvnr tpesggkvpa
      541 gqedpr
//
LOCUS       WP_457657969             367 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457657969
VERSION     WP_457657969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..367
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=38757
     Region          <2..360
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mvqprraqwi pvgvivlavv ldlatppdvt sapllmaapv aaapllrlrg iiaigvlama
       61 vhavlawvdg tfgwkrgvan qltlmavtvl avlinraleg qhartrrarh iaavaqsavl
      121 prppsrlgel riaaryvpae neatiggdly vvqdtphgvr vmvgdvrgkg lgavsavcad
      181 lgafryaade aedlpglvss lerallregr rrggqeedeg fttaliaefa agldtvrvvn
      241 rghpppvlld aggratvlep seeapplgms algswsspvd tfpfppgatl vcytdgvtea
      301 rdesgvfyda avrlpllirh raltgdpatp aqilhllied vghhtggriq ddqallalhr
      361 prtrsra
//
LOCUS       WP_457657973             442 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent RNA methyltransferase [Streptomyces griseus].
ACCESSION   WP_457657973
VERSION     WP_457657973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  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 442)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..442
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=47988
     Region          12..436
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mqneptsslv geeyevevgp vahgghciar taenqvlfvr htlpgekiia kvtdgdtdsr
       61 flradavrii epskdrveap cpyagpgmcg gcdwqhakpg aqrrlkgevi aeqlqrlagl
      121 tpeeagwdgt vmpadgdklp agevpawrtr vqyaidaegr aglrkhrshd vqpidhclia
      181 apgvselgve krewpqiaav eaitatgshd rqviltpkpg grlplveldk pvsvlrvdek
      241 dggvhrvhgr afvreraddr tyrvgsggfw qvhpqaantl vravmqgllp rkndtaldly
      301 cgvglfagai gqrigekgav lgiesgkrav edarhnlkdl drvriehgkv dqvlprtgit
      361 ecdlivldpp ragagkqvvk hlsalgarki ayvacdpaal ardlayfreg gyrvrtlraf
      421 dlfpmthhve cvailepadr dr
//
LOCUS       WP_457657976             133 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457657976
VERSION     WP_457657976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14874
     Region          27..129
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtgprqpdhs sttagrsrpe agyehidddv crsfqrsvei vgkkwnaavl laamrgarrf
       61 vdyraripgi snhllsqrlr eleghrller lvvpttpvqi tyrptergag lmrvlhplie
      121 wsakneampp tps
//
LOCUS       WP_457657978             100 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657978
VERSION     WP_457657978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 100)
  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 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..100
                     /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=10963
     Region          39..90
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 meafdrlgag plrqraqreq dltgepgrrg ssdtramnrl taqeqrvaql aaeqltnrei
       61 gvqlrishrt vghhlgnvfa klgintrtel shlhagcels
//
LOCUS       WP_457657981             375 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457657981
VERSION     WP_457657981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..375
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39792
     Region          7..370
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtnsthtrig vglvgasadr gwggiahvpa lraldafqir avsttrmesa natarrlgad
       61 lafdthealv vrpevdlvvv avkvpdhqqi vsdalaagkm vycewplarn lseaealegf
      121 arerrlrtvv glqgglhppv lflrdlvaqg vigkplstsi rahladdmwv grfdppveym
      181 ahaengatll simlghglep larvlgtfes lsavvanqrg dgvrlsngas lpkdapdeiv
      241 vagvleggiv tslhysagrs agpamvweiq gtegsvrves asgyihftdf titlcrgsep
      301 vqvlevppay aapdlqldap aagvarlyaq faadlrdkta dapdfavald rhrvleaitr
      361 aaetghrqhl srpte
//
LOCUS       WP_457657982             301 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457657982
VERSION     WP_457657982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..301
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30092
     Region          1..299
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,121,125,146..151,170..171,173,186,
                     209..210,231..232,251..253)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mkavvitsfg epsvlrvaea prpvpgpgqv lvrvhaagvn paeiqaraga fhlrapaiig
       61 fefagvveav gpgidegavg drvagwpdsa tqgsyaeytv ssnfamipdg vsfeaaaatv
      121 igadnaaral gllnirpget lvvtgasgal ggaavqlarq rgvtvigvag tdnadfvrsl
      181 gatpvahgpg lvdriraaap ggvdaaldta gkgllpalvd llggpdrivt ladrdaalhg
      241 vvfspggsgn rdrgpvqeal nliaadawta rigrsfplde vadahrlvat ghthgkvill
      301 p
//
LOCUS       WP_457657984             200 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457657984
VERSION     WP_457657984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..200
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21066
     Region          50..181
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mastaddtng rhrrrprngp tseatarade gsgsgastgp vaetrwlngd elaawlansa
       61 imislpaald armqreaqlt ffeymvlsvl seqpdrtmqm salaartaas lsrlshvvgr
      121 lekrellarq ripgsgrrtt atlteagyev vaaaapghva avreyliddl gpqelaalrr
      181 igaavdaaik rgqsdassaa
//
LOCUS       WP_457657983             323 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457657983
VERSION     WP_457657983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 323)
  AUTHORS   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 323)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..323
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34595
     Region          5..302
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(19,201..204,207,257,275..279,282,285..286)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(51,56,81,122)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mqstslgrld vpriglgvmg msayytgagr dgaesirtir ravdlgvthl dtaevygpyv
       61 neellgraik grrdevvlat kfglvshtgr pgpdstpasi htavdgslrr lgtdridlyy
      121 qhrvdpntpi eetvgalrnl veagkvlhig lseaaaatvr rahavhpvaa vqseyslwtr
      181 dpeaevlptl relgiglvpy aplghgfltg dirtldglda adwrrsnprf tgdnltrnlr
      241 ivdqvrevad evgatpaqva lawllaqgdg iapipgtkri drlkensaad girltpgqia
      301 rlnnltpasg erhaepdmaa vdq
//
LOCUS       WP_457657990             396 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457657990
VERSION     WP_457657990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 396)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..396
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=42919
     Region          18..395
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,86..87,94,98,105,229..230,233,237..238,241,
                     274,279..280,283..284,286,309,336..338,341..342,344..346,
                     350)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,80,82,85,87..88,170..171,179,228..229,232..233,
                     237,280,283..285,385)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtaprqdplr dprffadpyp tydrlrercp vqrvptgsgg hqgylitgha earaaftdpr
       61 lskdtarffa drpsdrdlhp aisrtmlasd ppahtrhrrv atplfttgrv rdlrpfitrv
      121 vdglmaqwrp gtevdlvael avplpvtvic ellgvpesdr aalagwshel fdatdtarvd
      181 aashrigdyl thlvdtarat pgdgplhall rdcdeggldr dgavslaall lvaghetttq
      241 fignavlall rhpeafdrlr rdpdlipgal dellrydspv svatfrysae elsvggvdvp
      301 agfpvliatg aanrdpavfp dpyrldldrd aaghlsfghg ihrclgapla raeaeialra
      361 lvtrfpdtgl avdaealawr rtrltrglta lplvlg
//
LOCUS       WP_457657992             151 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457657992
VERSION     WP_457657992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..151
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16346
     Region          <47..96
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 meddrsptfa qlldhlfrev hppsrgpyty aevaegirka atsegrgvta saiqqlrtga
       61 krnptrhtik aladffgvpa gyfvdsaaae rtkaeiglla amrdqdvrkv alranglsvd
      121 slkmlstvie qarklegltt ddsphdlnld d
//
LOCUS       WP_457657994             333 aa            linear   BCT 27-JAN-2026
DEFINITION  proline racemase family protein [Streptomyces griseus].
ACCESSION   WP_457657994
VERSION     WP_457657994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Visser,W.F., Verhoeven-Duif,N.M. and de Koning,T.J.
  TITLE     Identification of a human trans-3-hydroxy-L-proline dehydratase,
            the first characterized member of a novel family of proline
            racemase-like enzymes
  JOURNAL   J Biol Chem 287 (26), 21654-21662 (2012)
   PUBMED   22528483
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Fisher,L.M., Albery,W.J. and Knowles,J.R.
  TITLE     Energetics of proline racemase: racemization of unlabeled proline
            in the unsaturated, saturated, and oversaturated regimes
  JOURNAL   Biochemistry 25 (9), 2529-2537 (1986)
   PUBMED   3755058
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..333
                     /product="proline racemase family protein"
                     /GO_function="GO:0016855 - racemase and epimerase
                     activity, acting on amino acids and derivatives [Evidence
                     IEA]"
                     /calculated_mol_wt=35407
     Region          1..333
                     /region_name="PrdF"
                     /note="Proline racemase/hydroxyproline epimerase [Amino
                     acid transport and metabolism]; COG3938"
                     /db_xref="CDD:443139"
ORIGIN      
        1 mrskvcyhav dshtegmptr vitggvgvlp gatmaerrqr fmaerdglrt llmceprgha
       61 smsgailqpp trpdadfgvl fievsgclpm cghgtigvat vlvetgmvea vepetlirld
      121 tpaglvtarv avrdgraesv tlenvasysh aldqvvevag fgavrydmay ggnfyavvrt
      181 ddlgipfdrs ekgrlldagl avmaaineqn pvahpenpai dvchhvylea pgstaehsrh
      241 amaihpgwfd rspcgtgtsa rmaqlhargl lkagqdfvne sfigsrftgr ilgegtvgdr
      301 pavlpsvtgr awitgtaqyl ldptdpyptg ftv
//
LOCUS       WP_457657996             236 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457657996
VERSION     WP_457657996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25919
     Region          6..226
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mselksrkli svqehlrdqv analraalia gelqpgviys aptlaaeygv satpvreaml
       61 dlareglvea vrnkgfrvte lserdldeyt eiralieipt igrvtrtasr eqlealrpva
      121 eeivtaaqgg dliayletdr rfhlellala gnarlvetva dlrkrsrlyg ltdlseegsl
      181 vssarehtal ldimiagdae aaeehmrghl ahvrtlwaar kreaeraapt rrlgar
//
LOCUS       WP_457657997             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457657997
VERSION     WP_457657997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34513
     Region          34..325
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtpvtqqtag pptgpgagpp vnpaadgpgs talpaapwra tlrrlwgdrg srtaliaaal
       61 lilvaltapl lsrlggwtpt afdadaidpy lgglprgtlg gisaehwlgv epvtgrdlfa
      121 rvvhgaqvsl liafaataiv vvtgtaagia agyfggrvdt vlsrlmdltm sfpslifmia
      181 mmsvaqdvnr vllmtvvigv fgwpgiarvv raealslrhr eyveaaracg sgpwriltrq
      241 vlpnisgpvi ayttllipgm isteaalsfl gvgvrpptps wgqmiaeava yyetdplyfi
      301 vpsvflfvav laftvlgdal rdildpqggr p
//
LOCUS       WP_457657998             363 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457657998
VERSION     WP_457657998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..363
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38496
     Region          17..337
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpsttepdrl lepdrpllrv hdlrvafdtp agtvqavdgv sftveagrtl glvgesgsgk
       61 svtslavmgl hrrarvsgsv tlagqellgl tdrrfgrlrg rrmamvfqdp lsalhpaytv
      121 geqiaeahrh hfgsgrrvar rravemlgev gipeparrag eyahqfsggm rqramiamal
      181 acepellvad epttaldvtv qaqileliar lqqerglgvl mithdlgvva rvahevlvmy
      241 ggrgaeqapv ddlfrspahp ytrglldslp rlddpddapl raipgsppsp aapragcpfa
      301 prcpraaaat aperarcage sphprdvpdg grlvachlpl pptpatphsg paggvpvpde
      361 ear
//
LOCUS       WP_457657999             779 aa            linear   BCT 27-JAN-2026
DEFINITION  M9 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457657999
VERSION     WP_457657999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 779)
  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 10553015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..779
                     /product="M9 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /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=83874
     Region          125..306
                     /region_name="Peptidase_M9_N"
                     /note="Peptidase family M9 N-terminal; pfam08453"
                     /db_xref="CDD:430004"
     Region          365..649
                     /region_name="Peptidase_M9"
                     /note="Collagenase; pfam01752"
                     /db_xref="CDD:426409"
     Region          697..764
                     /region_name="PPC"
                     /note="Bacterial pre-peptidase C-terminal domain;
                     pfam04151"
                     /db_xref="CDD:427748"
ORIGIN      
        1 mggnnvrttl vrrgvgavlp lalagamsva llaqpaqaqp nspsaatasn asqpsrpagt
       61 adpapqaqqs ptpdtghqlk drlkasqlpp lsadksalke ayghhdappk qdavkkpsak
      121 aaaacdpadf tgrtgselvr qikgstidcv ntlfgltgnn aqlafreaqm vtvayalrdn
      181 aayypgdast gtpqlvlylr agyyvqwynp dvvgpygsal ttairsgldt ffasprshdv
      241 tdengetlse avilidsaqe narylhvvkr mladydsswn ayarmlaavn nvytvtfrgh
      301 qvpafvsave adpglidalh rfaadhlall ggdqayltsn agrelsrflq heslrgkarp
      361 patallqqts itgptaplwv giaemadyyd kancsdygvc dlqerlkrev lpvrhtcsps
      421 irilaqqmts aelaasctsl ieqdayfhri akddgpvadd nntsieviay dssadyqtya
      481 gamygidtnn ggmylegdps vvgnqprfia yeaewlrpdf hiwnlnheyt hyldgrftmy
      541 gdfaegmstp tvwwvegfae yisyhyrgep ytaamteagk gtyalstlfg tdyshdttrv
      601 yrwgylavry mleqhpadmd tvlghyrage waaarthltg tvgtrydsdf rtwlagcaag
      661 dcgdgstapv sectdpdtrv lgencrrsdl sattgnyayh ylyipagtaq lkitvsggtg
      721 dadlyysgtg watttaytsr dtgpgnthtl tvtnppagan yislhaastf ggatlttah
//
LOCUS       WP_457658002             239 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658002
VERSION     WP_457658002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..239
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26735
     Region          38..151
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mkdpsfrrsa alfraflreq gdpataytll ardaadqver hgplrdkvvv digggdgyft
       61 refrrrgahs ylfepdpaei gpgqradtvv adgyllplad gaadvcfssn vlehvadpht
      121 flsemarvtr pggliyvsyt nwlspwgghe wapwhylgae rarsryerrt ggpakhrlge
      181 nlfkigvget lnhvrsrsdv avvsarsryw pvlpqlvpri pvlrefatwn lllilrrcs
//
LOCUS       WP_457658005             241 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658005
VERSION     WP_457658005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..241
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25381
     Region          29..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtgtaspppg lrnfyenpav pvasgdgrsr rqarlladal dapgqvildi gcgdgtaaat
       61 aapflaghrl igvdwsqdal rrarprmgav vrgelehggl pladgcadav lfseilehlv
      121 dpdqaldelr rvlrpgghlm lstpnlaawy nralllagvq pvfsevslrg ihgrpgsevv
      181 ghlrlytara lrsfltasgf tdvtvkgapf hgvprplrll draacavpga asillaharr
      241 r
//
LOCUS       WP_457658006             434 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457658006
VERSION     WP_457658006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  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..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /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=44566
     Region          47..426
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mcventppps grltrrgvla gaaalagtsa vlaqaapaas aaqaasrgas grggdlvveg
       61 gtlldpltge vtedavvvit rgvvraagar nrlgtrvpsg vpvlrahgqw ilpglvdahi
      121 hlntaaeard avlkgatsar sgstnfyqdi avrelarqap eqaprlraag ifvtpdlgdt
      181 iladpdlapl arlrngvrsp ealrrvvevs largadtvkt rvneraglpe qdplvqvydh
      241 eqlseivaaa rrggkgvlch sysekgchda vtagirsleh gafvgertlr dmrrrgtyft
      301 ptltaiagla espdpvlaer grtylpvlkr avlaahelgv plaagtdssg gtvdpigrev
      361 elmhaaglsa ldairtattg aakllgldat agrlargfag dvlvvdgnpl adlgalsrpa
      421 rvvragfpvp vpaa
//
LOCUS       WP_457658010             842 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Streptomyces
            griseus].
ACCESSION   WP_457658010
VERSION     WP_457658010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..842
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90802
     Region          43..819
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 msmafgsplg psdpfsdlln rffgmspass ppamqrvpig rlltesshel lgratskaae
       61 dgtadldteh llwaatqvep srgllsragv dpdalaaqld evlpresaep saepgltpaa
      121 krtltaayar sqaagvsyig pehilgalid dadsgagrfl gsddldvgkl rgaadraagq
      181 dgasggakqp attldefgrd lteeakagkl dpvvgraeei eqtieilsrr sknnpvlige
      241 pgvgktaive glaqsivage vpdtlkdkrv vsldlsgmva gaqyrgqfee rlkkviedvq
      301 naegeiilfi delhtvvgag atgegsmdag nmlkpalarg elhvvgatti deyrkhiekd
      361 aalerrfqpv lipeptveet vlileglrda yeahhqvrfa dgaltaaael sdryisdrfl
      421 pdkaidlmdq agarvrlrsa nrstevvsre drlaklrrek deavageefe kasglkqqia
      481 evegelagie erregvvsvt asdiadivsr rtgipvsqlt agekekllkl eeemharivg
      541 qdeavtavse avrrnragmg dpnrpvgsfl flgptgvgkt elaktlaell fgqddrmirf
      601 dmsefqekht varlvgappg yvgydeagql tekvrrnpys vvlfdeveka hpdvfntllq
      661 ilddgrltdg qgrtvdfrhc vvimtsniga hrilahegda aelkdelmed lrgrflpefl
      721 nriddiivfh slteddlsei vdhlldrskh rvhaqgmtle vteaakkllv ahgyqpefga
      781 rplrrtiqte ldnrvaslll ggeadpgdti vadviddslh ctirkddgdg gtpaadtpeg
      841 ke
//
LOCUS       WP_457658013             493 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Streptomyces griseus].
ACCESSION   WP_457658013
VERSION     WP_457658013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Phillips,R.S.
  TITLE     Chemistry and diversity of pyridoxal-5'-phosphate dependent enzymes
  JOURNAL   Biochim Biophys Acta 1854 (9), 1167-1174 (2015)
   PUBMED   25615531
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449461
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..493
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53125
     Region          3..489
                     /region_name="LdcC"
                     /note="Arginine/lysine/ornithine decarboxylase [Amino acid
                     transport and metabolism]; COG1982"
                     /db_xref="CDD:441585"
ORIGIN      
        1 mtmnhdeapv ldalaayheh delgfsppgh kqargasaav rsvlgdaaff gdvlatggld
       61 drrgrsavlr raeelmadav haehtffstc gsslsvkaam lsvaapgqkl lvgrdahksv
      121 iaglilcgve pvwlepqwda erhlahppsp atvekafaeh pdargalvts ptpygtaadl
      181 ramadichrr arplivdeaw gahlpfhpdl pswamdagad vcvtsihkmg sgleqgsvfh
      241 lqgdlvdhdt lasradllgt tspsvllyag idgwrrqmal dghallsral dltatvrsri
      301 eeiegmhvnd rddfcgpgaa aefdplpvii dirglgttgy raadwlrehh ridmhlvdhr
      361 risaqfthad dagtaerllt alrdlsrnah tlrpapevhv ptprelrpdq allprdayfa
      421 etedvpaaka vgrvaaqmlt pyppgipavl pgeritepll rylrsgvaag mnvpdpadpk
      481 letirvcaer edh
//
LOCUS       WP_457658015             222 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457658015
VERSION     WP_457658015.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23172
     Region          4..213
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 magaaifdvd gtltdtnhlh vvawweafrq aghavpmpdi hravglssgd lierllgadr
       61 drdqdpaisa ahkvlhatyf drlrafrgag dllralagrg wrvvlatsas gpelaalrra
      121 vdadeaicat assddveqgk psaepvelac rladvdagqa vfvgdtvwdm eaagragvrt
      181 vavlsggipr adleragaga vyrdvadlld rlddspfgpa sa
//
LOCUS       WP_457658017             178 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457658017
VERSION     WP_457658017.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..178
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19745
     Region          5..170
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mgksalivid mintydhpdv ellipsvgaa iphltrlier artrkvpviy andnfgewrs
       61 hhgeiiqtal agtnaelvep llpdddalfv vkarhsifye tplsyllsel hvdhvvlcgq
      121 vteqcvlysa ldahirhlrv tvprdavahi hsdladaalr mmqrnmgaav rdvdevdf
//
LOCUS       WP_457658018              75 aa            linear   BCT 27-JAN-2026
DEFINITION  CDGSH iron-sulfur domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658018
VERSION     WP_457658018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Sengupta,S., Nechushtai,R., Jennings,P.A., Onuchic,J.N.,
            Padilla,P.A., Azad,R.K. and Mittler,R.
  TITLE     Phylogenetic analysis of the CDGSH iron-sulfur binding domain
            reveals its ancient origin
  JOURNAL   Sci Rep 8 (1), 4840 (2018)
   PUBMED   29556009
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..75
                     /product="CDGSH iron-sulfur domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=8192
     Region          5..43
                     /region_name="zf-CDGSH"
                     /note="Iron-binding zinc finger CDGSH type; pfam09360"
                     /db_xref="CDD:462769"
ORIGIN      
        1 mlvegpvevv tadgttvrsd rfvvaicich rsraypwcdt shrrrkaagp gpsgrpqpqd
       61 garrqprdge eeprp
//
LOCUS       WP_457658023             317 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces griseus].
ACCESSION   WP_457658023
VERSION     WP_457658023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5) (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..317
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=32684
     Region          1..135
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          181..314
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mnrhvtvgld dsteshaaaa waareaasrg valrvvhvee wpitpeiplt ltealverye
       61 tllreaaera rrdhpgldvt temvhgraga eltraadeae vmalgsrglg gfvgflvgsv
      121 slavvaastr pvvlvraerp gaeagatesg aaaggagaag aaerasagae daaavgsppd
      181 vvlgldiahp seplldfafg taarrnlplr vvhswsppas ygyaaildpe igtglgrraa
      241 egltellrpw rsrfpevrvv ekvavgpaar elvhasrgae llvvgrcgrr palphlghva
      301 havihhssap vavvpla
//
LOCUS       WP_457658024             467 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658024
VERSION     WP_457658024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..467
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47081
     Region          19..419
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,65,115..116,118..120,123,143,
                     146..147,150,274,277..278,281..283,286,314,318,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpaqksrrlp slsgvlvlvm astglvvvdl tivaiglpli sadvgdgasa esvvvtymva
       61 mgaltqvvgs lsdrwgrrtl flagiavftl aslgatvapd lllldiarvv qgagaaaimv
      121 ngipllsdry sgeernlaig awgsfataag llapvlggvl aetfgwravf avnlplgaaa
      181 wllavrvlpr tpgtggagrt dwlgslllml glgtatllml rpgdtpwsrq dtavlltacl
      241 alvafllvql rvpaptlelr mfgrpafsga mlavllsrvl tiggsvylvl yfsdglglsp
      301 tragllmtpi flaqivmgmv gsrligdrap gpvigagyal kgigfaalal litpdtpwwa
      361 lllpllawga gggiagapvm avavrvtape rvgmvagtvs tlaslgagvg taalgavfal
      421 hgghgaeavt egaravlgvs aalaavavlt tltlidprrv prpdpgg
//
LOCUS       WP_457658025             509 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic amino acid ammonia-lyase [Streptomyces griseus].
ACCESSION   WP_457658025
VERSION     WP_457658025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  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 509)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..509
                     /product="aromatic amino acid ammonia-lyase"
                     /EC_number="4.3.1.-"
                     /GO_function="GO:0016841 - ammonia-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009072 - aromatic amino acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53174
     Region          22..450
                     /region_name="PAL-HAL"
                     /note="Phenylalanine ammonia-lyase (PAL) and histidine
                     ammonia-lyase (HAL); cd00332"
                     /db_xref="CDD:176460"
     Site            order(66..68,70,72,89,92,188..192,196,278,281,311,323)
                     /site_type="active"
                     /note="active sites [active]"
                     /db_xref="CDD:176460"
     Site            order(71..72,91,94..101,122,150..151,163,166,240..241,
                     244..245,247,250,275,277..279,281..282,285..286,292..293,
                     296,299..300,303..304,307..308,313..315,320,322..328,
                     330..331,334,338,345,348,352,356,359,362,374..375,
                     377..378,380..383,385,387..392,394..397,408..414,417,
                     423..424,427,430..431)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:176460"
ORIGIN      
        1 msshisdrva edasaivvld grrlmvadvv rmaessarpv pategmkrve dswnaareia
       61 swgrvygrst gvganrnesv pteaaadhgl rllrshagai geelparqvr amlavranql
      121 laggaglrpt vvtalceale tgaypkvnaf gsvgtgdiaa laqmglalag ehpwqgtgta
      181 pepqpldnnd alalissnal tlgqsalalq elraligatq vvaalslmai dgsyeayalp
      241 vhearrhags yavaermrll lgapdrptpp lgriqdpygf rclpqihgpa hdaadaleev
      301 laveinaaae nplisaddma ayhhggfyla qlalsldhfr lavtqvarls tsrlstlnep
      361 gftrlrpfla dgepassgvm ileyaagaal gdlraysapa slghavlsrg veeqasfasl
      421 aarqtlrace afrlvvgcel vaavralrqr elrldpelpv grafelaasv ldaeaadrpl
      481 tddvaaaagl ldrfaelwaa pgpagepgp
//
LOCUS       WP_457658028             314 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Streptomyces griseus].
ACCESSION   WP_457658028
VERSION     WP_457658028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..314
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=30345
     Region          4..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 mtgrtagavv igldlggtki aaalfapdge vlarhtratp aregaaavld alaaaaaavd
       61 peglaalvgi aaagvvdprs gmvtsatdsi rgwagtalga gladrtglpv acdndvrata
      121 gpeldalpds rgsllyaavg tgvggalavd grmlhgaagi aghlghlpst eaaglactcg
      181 atghlevias gpgiaahyer ltgtrpdrle tvaaraaegd raavraittg aaaagrvlgg
      241 lanalgpdrv vvgggvphig plyrdalaaa faaelmpplr gllpepplhg adaavlgaaa
      301 ltttlplhhp gahr
//
LOCUS       WP_457658030             332 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces griseus].
ACCESSION   WP_457658030
VERSION     WP_457658030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35622
     Region          1..324
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mpsvdltlae crayrpelpl pdgfdafwsg tldgkapsga tdrqprfdev dsglvqvrcy
       61 dvsvpgydgr pvrgwlrmpa gstgplgciv eflgygrgrg laheqlmwac agyahlvmdt
      121 rgqgwssatg dtpdadpgsa gavpgfltrg vespathyyr rvftdavrcv qamgehpevd
      181 parivvtgvs qgggialava glvpglagvm pdvpflcnip raariaatpp yteiatylrl
      241 hrdrveevfr tlsyfdaahh atratapalf svamaddvcp pstcftaynr yagpkdvrvy
      301 efngheggte hhraeqlawv rdlftglpad ra
//
LOCUS       WP_457658031             243 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658031
VERSION     WP_457658031.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..243
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26128
     Region          11..228
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 msgarpgrtl lrqevvegik ryilderlrp gdplptepal cealgasrss vreavkilaa
       61 ldivevrhgh gtyvgrlsls alvesltfrg llspdddfqv madlvdvrel fergmadrii
      121 ssldaeeldr ldglvatmre tgagdghgfv aadrafhall vaplgndlig qlsmafwdvy
      181 tivaphlqgf thadeaetva ahqnivdaar agdvaaflks lgehyapvrr riaeararge
      241 geg
//
LOCUS       WP_457658032             531 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces griseus].
ACCESSION   WP_457658032
VERSION     WP_457658032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..531
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57420
     Region          66..531
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mpelrpagve rrtflrytsa lgaaaaitag lsacggpsst adgaaakgdg ngtieaglsy
       61 plstgfdpmi tsgatpyaan mhifeglvdl dpatlvarpa latempkkin attyratlrd
      121 gatfhdgspv taedvvfsfe rildeknasl maqfvpfidt vtavdaktve fklkyafalf
      181 psriavariv pkkiveadvk gfdakpvgsg pykfveatre dkiafekfda yngphpakak
      241 kmiwrlmsdq sarvsamesg rvqaiedvpy idvqrlsatt ktesvqsfgl lflmfntadk
      301 rfadkrvrqa lhyaldteki iktamvgnat aatgyvptth pdyhqaatay thdvakakkl
      361 ladagvgklk ftvlttdtgw vkdiapllke swaaagidat lniaqsaaqy akvdggdfev
      421 mvapgdpsvf gndvdllmrw fyygfwpekr ygwsrtaeyk kvkqlldkaa qaadestrkr
      481 lwgeitdlva deaalypilh rklptawsek alpgfkplpt tglsfvgvgr a
//
LOCUS       WP_457658034             656 aa            linear   BCT 27-JAN-2026
DEFINITION  dipeptide/oligopeptide/nickel ABC transporter permease/ATP-binding
            protein [Streptomyces griseus].
ACCESSION   WP_457658034
VERSION     WP_457658034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 656)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Monnet,V.
  TITLE     Bacterial oligopeptide-binding proteins
  JOURNAL   Cell Mol Life Sci 60 (10), 2100-2114 (2003)
   PUBMED   14618258
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..656
                     /product="dipeptide/oligopeptide/nickel ABC transporter
                     permease/ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68844
     Region          11..278
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
     Region          335..646
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mfatgrlakk lsrpgiafra lpvtsrvalg vlvvvilgav laplltqdpl ttgtpvqapg
       61 aehwfgtdra grdvfarvvh gsryslvigl gatavalvag avlgslaats rklgdesvmr
      121 tldvvmsfpp ialaavlvav fgtsvpviif tiafvytpsl arvvranvla qygedyvaae
      181 kvigarrgyi vlrhvavncm apvmvfatvm vaeaiifeas lsfigagvqd pdpswgsvla
      241 ygrqillagg wwatffpgla llitvlalni lsegltdasa apksarapva pattapdpve
      301 aaatvdidaa laklarhida teptitpvra dadellvvrd lairfpdryg dipvvdrlnf
      361 tvhegetlgl vgesgcgksi tslavmglla rnaevsgeil yrgrdllklp pkerralmgp
      421 eiamvyqdal sslnpsvlvg tqlkqltsrg gtktpaelle lvglspertl rsyphelsgg
      481 qrqrvliama lsrsprllia depttaldvt vqaqvvelli klrdelgfam vlvshdlalv
      541 gdlahrvavm yagrlaevgd trsvltgpah hysrgllgsv vsleagadrl hqirgvvpap
      601 qgfgdgcrfa grcgaatglc rttapaltpr dpeddhgfac hhpagattek legsil
//
LOCUS       WP_457658035             352 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658035
VERSION     WP_457658035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..352
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35565
     Region          44..348
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 maqalaktaa ppptapsrsa rrrtrrlvgl gvalgallva vllsvaigsa llppdvvwqa
       61 ltapdgsash atvsgarvdr tllgivvgms lgvagalmqa ltrnpladpg vlgvnagagf
      121 avtlgvavfg vtrieqylpf alvgavvgaa fvylaasggr ggptpvrltl vgvaftavlv
      181 gisqtlalid tetfdrmrfw gagtitdrpt gtagdilpfv ltgllaaalc arplnaialg
      241 ddagravglr vgavrcgvvv avallcgaat aaagplmfvg lmvphavrwi tgpdwrwilv
      301 hsavlapviv liadvlgrli vipselqvgv mmpligapvl imlvrgsrvr el
//
LOCUS       WP_457658036             443 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein, partial [Streptomyces griseus].
ACCESSION   WP_457658036
VERSION     WP_457658036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>443
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          23..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maaqraytth plvlrrvtvr rvekvtprmr rvvlggedla aftrdgidhp gfaapgfddh
       61 vklilaadgn iraalpaqlp hgiewtpaeh rvtrdytprr vdlrtgelhl dfvvhgegpa
      121 eawsasareg delwfvgpks slrlperldw ifligdetal paigrflder pldatahvlv
      181 tvsddaarqe lalrdgdtvt wvhaepgdaa aleaavralp vpagegyawa aaesrallpv
      241 rrylqrerkl akdrvnitgy whreeatape aegaaetgaa aqspagipsp lpwlvaraal
      301 qlgvvdavad apglsagtla arlgvpgpgi dvllpllaty gvvtggdegl rlgpageell
      361 edhereeyag heaelllala rfapalrsgt spwrlasgat lhetvtrdae rygelveece
      421 qlvfllnglt adslwadves clr
//
LOCUS       WP_457658039             275 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658039
VERSION     WP_457658039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..275
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=27465
     Region          24..265
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msdntvapvp ptpptpltll glgamgaala rtwlaaghpl tvwnrspgrs aelaaagarv
       61 aataaeavaa splvvtclld dasvraalad adltgrdlvd lttstpaesr travwanerg
      121 arfldggima vppmigvpea ggyvfysgdr evfdahqevl svpvatryvg adpgfaalhd
      181 vallsamtam fagarhaaal vagsgvdeke fgalvagwlt amapstaaya ggplpddpts
      241 aavaeagdaa llrtareqgv dtallvasag smngi
//
LOCUS       WP_457658040             284 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457658040
VERSION     WP_457658040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..284
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30728
     Region          1..265
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 msqampvsyv rvtgveritp rtarvgftge alprlledrp dqqmklclpr egrsvregll
       61 perdaddpyg mrwyeaflai peaerpwmrg ftvrsydrer nvmavdfvlh gadgpasrwg
      121 aaarpgdvlg mvgpsslyar plpasrrmll agdesalpai atvlealpag tgavvyaeva
      181 daaeerelps aaggaevrwv hrdrggalvd avreagadld gvdaawvage asavralrrh
      241 lvedrrlpka avefsgywrr altqddapte edlawaaera adas
//
LOCUS       WP_457658041             541 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658041
VERSION     WP_457658041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..541
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57760
     Region          1..528
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdlvlrdalv vdgtgepgyr advaldggri aeihpegspg prptatrtvd adglalapgf
       61 idmhahsdla llrdpdhsak aaqgvtlevl gqdglsyapv ddrtlaevrr sitgwngdgs
      121 didfdwrtvg gyldrldrnf ggqgiavnaa ylipqgtvrm yavgwddrpa tdaelarmke
      181 lvdqgmrega vgmssgltyt pgmyaddael telcrvvarh ggyycphhrs ygagaleaye
      241 emvqltrnag calhlahatm nfgvnkgkap dllalldgal aagadisldt ypytpgcttl
      301 vamlpswase ggpesiltrl aepssaerir hhlevlgsdg chgvpiewdt ieisgvsaph
      361 laeyvgrtva esaaargeep wvtarrllte drlgttilqh vgheenvqqi mrhpvhtggs
      421 dgilqgdkph praygtfpqy lgryarelgi lsleecvahl tsrpaarlrl adrglvregy
      481 radlvlfdpe tvaagstfee prtlpvgiph vlidgrfvie dgrrtsalag ravrgagaaa
      541 v
//
LOCUS       WP_457658043             416 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces griseus].
ACCESSION   WP_457658043
VERSION     WP_457658043.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..416
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41889
     Region          16..374
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(47..48,51,103,119,121,150,182,334,337,373)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(238,243,325,334..336,339,361,365)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 msgpaagtas aatttdvvcl gesmvtflps qpgrladvps fgrgiggaes nvacalaaag
       61 hraawvgrvg adgfgehlve tiagygvdts avrrdpvrpt giyfrtatdr gtdthevayy
      121 ragsaasams panvpyeelf agrilhlsgi taalsadcle llreltaarp grplvsfdvn
      181 hrphlwrggd adasvllela rrsdlvfvge deaeeawgiv gaeairaalp epsvvvvkrg
      241 sagatvfasg lrpgprssia ggaecapgar steaggaena pgagpteggg aecapgagpt
      301 egggaecavg gaesgpdtvt hvpalrvdvv aavgagdafa agflsatlrg lpvrdrarhg
      361 hlmaaavltv pgdlteppar dhadrlaald ddawgrlrlg pgwtaadrap eevrtp
//
LOCUS       WP_457658044             491 aa            linear   BCT 27-JAN-2026
DEFINITION  GntP family permease [Streptomyces griseus].
ACCESSION   WP_457658044
VERSION     WP_457658044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Peekhaus,N., Tong,S., Reizer,J., Saier,M.H. Jr., Murray,E. and
            Conway,T.
  TITLE     Characterization of a novel transporter family that includes
            multiple Escherichia coli gluconate transporters and their
            homologues
  JOURNAL   FEMS Microbiol Lett 147 (2), 233-238 (1997)
   PUBMED   9119199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..491
                     /product="GntP family permease"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50223
     Region          29..491
                     /region_name="GntT"
                     /note="H+/gluconate symporter GntT or related permease,
                     GntP/DsdX family [Carbohydrate transport and metabolism];
                     COG2610"
                     /db_xref="CDD:442022"
ORIGIN      
        1 mllaatpspa etpphtggll llidgtagll tvaalgiall lfliikvrlq pfvallavsi
       61 avglgaglsv telfgtvqks aavsviesgm ggilghvaii iglgtmlgai levsggaevl
      121 sarllnafge kraplamgmt glvfgipvff dvgifvlapi vyaaakrsgk sillyampll
      181 aglsmthafl pphpgpvaaa glfnvslgwv ilmgivvgip sviaawgyaa wigkrifvdv
      241 pqdmveaaee akaavaaeqr aagvtphekp vplgtvlaii gtplililaa tfssialdps
      301 tlrsvieffg npfvaltial flayyllgir rgwsrksles vstsslkpvg nillvvgagg
      361 ifgavlkgsg iadaladtfn dvglpvilla wlisvvlrva qgsatvaivt tagivvplve
      421 gqdlsqahla liimaisags ifashvndgg fwmvskyfgi serdtlkswt vletvlsvag
      481 fvvaallslv i
//
LOCUS       WP_457658045             361 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658045
VERSION     WP_457658045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..361
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=37861
     Region          179..358
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mshtirrtad parqeefagr mvevlndacl gylcslghrt rlfdvmaglp pstseeiada
       61 aglneryvre wlggvtvggi vgydpadgty rlppehaasl craagpdnla sflqdlalig
      121 lvedevvtaf rdgggvpyss ypkfqeiqae etarvydaal vdviiplapg lpellgsggg
      181 ldvldvgtgq ghavnllara fpasrftgvd mseggiaaar aeaarlglrn ahfdladaaa
      241 vtgpydlita fdvihdlarp aatlaavaga lrddgvflmg diaassrlee nldlplgptl
      301 yafsvfycmt tslseggagl gtvwgrqtal rmlkeagfge vavrevegdi lnvyyvarkg
      361 s
//
LOCUS       WP_457658052             298 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658052
VERSION     WP_457658052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..298
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31831
     Region          98..185
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mpepsapaps grtsgpsnss sssssadsad sadsadssgs fvstasrdrf ealvaeadav
       61 svdgwdfswl dgrateerps wgyaramaer lgrahaaldl qtgggevlaa apklppvtva
      121 teawppnvar atallhplga vvvadadepp lpfgdaafdl vvsrhpvttw weeiarvltp
      181 ggtyfsqqvg pasvfelvey flgpqppevr rgrhpedava aataagldvv dlrsetlrte
      241 frdigavvyf lrkviwmvpg ftveqyrpql aalhrrieae gpfrartarf liearkpr
//
LOCUS       WP_457658056             797 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658056
VERSION     WP_457658056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 797)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18109208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..797
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84490
     Region          572..790
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          682..790
                     /region_name="FtsX"
                     /note="FtsX-like permease family; pfam02687"
                     /db_xref="CDD:460652"
ORIGIN      
        1 mtlldsrtap paapespkpp srgaatlrdl glgirfaaag gregwirtll tavgvglgva
       61 llllassvph lldernareq arsevkasaa dsaksdtsvl rldtdteyrd rsiggrllra
      121 dgsapvrppg varfpgpdem vvspalkell eapgnkllre rlpyditgti gdaglrspge
      181 lfyyagndtl tpaagagrvs gygahreadp lppllvvltv mvcvvllvpv aifiatavrf
      241 ggdrrdrrla alrlvgadir ttrrvaagea lfgavlglli glvfflvgre fvgsvevwdv
      301 saypadvvpd pllallitva vpltavlvtl vamrsvviep lgvvrrgksr grrlwwrllm
      361 pvaglallgf tgrideyaye pvkpfpiaag avlvlvglal llpwlveacv rrlrggpvpw
      421 qlavrrlqls sgaasravsg vtvavagaia lqmlfaamna dfnratgqdp traqfagyse
      481 hvtgeaatsa ieqfrategv evvigsvqay askpgvytdd dippttsltv gtcdtlrela
      541 ritscedgdt fvvhppgdkd msawvdrtar kgkvvevgtg egkplrwtlp agsptvqgrk
      601 dpmgdthygi mattgavdas tlpgaqitaq irvdrsvpdv aeyvrntaar idpgmrfvtl
      661 dsverdrqyd siqtglkvga svvllliaas mlvsqveqlr erkrllsvlv afgtrrttmg
      721 wsvlwqtavp vflglvvava gglglgavla wmiaesvsdw wlflpltgvg aglillvtaa
      781 smpslwrlmr pdglrte
//
LOCUS       WP_457658058             471 aa            linear   BCT 27-JAN-2026
DEFINITION  class II fumarate hydratase [Streptomyces griseus].
ACCESSION   WP_457658058
VERSION     WP_457658058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..471
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49539
     Region          12..470
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mgdtsgatsd gsgfriehds mgevrvpaha kwraqtqrav enfpvsgqrl erahiealar
       61 ikgaaakvna elkvldpdia aaiqeaaaev asgrwdehfp vdvfqtgsgt ssnmntnevi
      121 atlaterlgr evhpndhvna sqssndvfps sihiaataav tadlipaldh ladslgrksa
      181 efaevvksgr thlmdatpvt lgqefggyaa qirygverlr aslprlaelp lggtavgtgi
      241 ntppgfsaav iaevaeatgl plteardhfe aqgardglve tsgqlrtiav sltkisndlr
      301 wmasgprtgl aeialpdlqp gssimpgkvn pvipeavlmv aaqvtgndat vatagatgnf
      361 elnvmlpvia knllesvrll anasrlladr tvdgitadve rarayaessp svvtplnkyi
      421 gyeeaakvak kslkdgttir etvlasgyve rgdltleqld ealdvlrmtr p
//
LOCUS       WP_457658062            1106 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Streptomyces griseus].
ACCESSION   WP_457658062
VERSION     WP_457658062.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1106)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1106
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=114261
     Region          1..>1099
                     /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 mrddriavig talrfpgadt peeywrdira gtgrvhrftr aefaaagipa aeyerpgfgg
       61 asglltgvdg fdagffgmsg reaeltdpqq rlfleccfha ledggyagge gryagggdgg
      121 svrigvygss gyrlyslhsy laanlaaeag sgdwmtakqv qvgnypdfta traafrlglt
      181 gpaltvstac ssalvsvhla cqalragdad lmlvgsaalh lpqvsghtpv kgstlsptgt
      241 vrafdagadg tvggngaaav llkplerala dgdtvhavil gsavtndgah kggfaapgva
      301 gqrdavlgal raadvdaasi gyveahgtgt lkgdpiefaa lteafrahtg rtgfcalgst
      361 kpaighldsa aglaglikav evlrhgvvpp lvnysrpnpa lalddspfll pvrerawpla
      421 gvrragvhsi gmggtnahvi leqapeagpv saaptaapap vpallplsaa dgdalrayav
      481 alrdhlagga rpspadlltt aalgrrllph rlvvtaedpv agldaflsga pageayttgv
      541 agsvrrpvfl fsgqggghpg mgtelaarfp vvaevletca rvyaeetgrd dfldrivggq
      601 gperwdtafa qpalfalqia qarmwerlgv tpsrvaghsv gayaalcvag aldtedamrl
      661 vcgrgrlmre rsapgamvsa fvprsrvrel laavpglela vvngaghhvl ggppgavdaa
      721 kvllaargea yevlavdraf htalldpale efrvladkve llplhtefvd gidgsvrpag
      781 wrpdaaylva qarrtadfaa vldrlagppl deppsgeppl teppsdgsss pgaapllelg
      841 psavltgmvr rslpdavcvp trqweravaa lhcagagvdw aalldgcggr rvrlptypfr
      901 rrshwrgpap ytppapaapr tprttprtph tedrmteqav ldrvleltar hlghrldeva
      961 adrtfvglga dslqligmvr qleaefgtei smreileeag tprltaelia grrapaisas
     1021 aeptpaadvp tpapvsvpvt aapapvaqvp apasppapde pgyatraeva alseqirqla
     1081 etqaamltql seavalltar tgtetr
//
LOCUS       WP_457658063             469 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658063
VERSION     WP_457658063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47932
     Region          33..431
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(43..44,47..48,51,83,136..137,139..141,144,164,
                     167..168,171,247,250..251,254..256,259,295,299,359..360,
                     364,368,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtsgideadg pkaneaggga gkdrdtavse rrfrflvagy avssygtfln mvalnlfvye
       61 ttgralamgl fmavrlasgf vaglvvggll arfsaksiml wanvgqgsvm lvlilapesl
      121 vtgalmavsv vigacgtlfm valrssipem vgedrrawan slsitgrsla mvagfasagv
      181 vvslvgytaa flldmatfvv cavtvallpi aggkgatnaa gasdtekagk gekaeksgpr
      241 wrpvaflala aapglglmva lrgvdafgss shnaalpiys tsldasnpav fvsafwcvwa
      301 lgnigaqqvi qryaqrtgrs vgalgfgygt vvmsaafiaa fagfplavta vialiagaad
      361 gltevaytsh lqtlpatlrg hafglsatfe nlgfgvgmil vaaaldrftp lavvgwshga
      421 aivvavvfll rvaglrraer tgrvglrkee avegrpdrgd rdgaevsrg
//
LOCUS       WP_457658064             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658064
VERSION     WP_457658064.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29351
     Region          29..268
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mmnyeqgaap ttpqgppdpt pdpppppaie ahdltvvrgv rtvlraldft vrpgsitgll
       61 gpsgcgkttl mravvgtqdk vtgtldvlgh pagdpalrpr igyvtqapsv ytdltvrqnl
      121 dyfaavlhpg rahrdarnda vtraigdvdl tthadalaga lsggqrsrvs lavallgtpn
      181 llvldeptvg ldpvlrrdlw dlfhrlaadr gtallisshv mdeaerchrl llmrdgrila
      241 edtpdalrrs tgtatveeaf lrlvdeaapi teeasr
//
LOCUS       WP_457658067             223 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457658067
VERSION     WP_457658067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..223
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24772
     Region          2..162
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 maqgevlafe dyvrtrqeal lrsarrlvpd pvdaqdllqt alvrtygrwd giadkslada
       61 ylrrvmintr tewwrarkle evpteqlpda svedgseqra drallmdilg ilapkqrsvv
      121 vlrhweqmst eetaaalgms agtvkstlhr alarlrqele sreldsreav aretgshrsa
      181 apavsarvpa qrspvtsarg arahtsaqrn grhdergmer caa
//
LOCUS       WP_457658070             842 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Streptomyces
            griseus].
ACCESSION   WP_457658070
VERSION     WP_457658070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..842
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92935
     Region          1..806
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mferftdrar rvvvlaqeea rmlnhnyigt ehillglihe gegvaakale slgisleavr
       61 qqveeiigqg qqapsghipf tprakkvlel slrealqlgh nyigtehill gliregegva
      121 aqvlvklgad lnrvrqqviq llsgysggke aataggpaeg tpstslvldq fgrnltqaar
      181 eskldpvigr ekeiervmqv lsrrtknnpv ligepgvgkt avveglaqai vkgevpetlk
      241 dkhlytldlg alvagsryrg dfeerlkkvl keirtrgdii lfidelhtlv gagaaegaid
      301 aasilkpmla rgelqtigat tldeyrkhle kdaalerrfq piqvaepslp htieilkglr
      361 dryeahhrvs itdealvqaa tladryisdr flpdkaidli deagsrmrir rmtappdlre
      421 fdekiagvrr dkesaidsqd fekaaslrdk ekqllaakak rekewkagdm dvvaevdgel
      481 iaevlatatg ipvfklteee ssrllrmede lhkrvigqkd aikalsqair rtraglkdpk
      541 rpggsfifag psgvgktels ktlaeflfgd edalisldms efsekhtvsr lfgsppgyvg
      601 yeeggqltek vrrkpfsvvl fdevekahpd ifnsllqile dgrltdsqgr vvdfkntvii
      661 mttnlgtrdi skgfnlgfaa qgdvktnyer mkvkvneelk qhfrpeflnr vddtvvfhql
      721 teediiqivd lmlakvderl kdrdmgiels aeaktllakk gydpvmgarp lrrtiqrqie
      781 dilsekilfg elrpghivvv gtegegddka ftfrgeeksa lpdvppieqa aggagpnltk
      841 da
//
LOCUS       WP_457658073             380 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit D [Streptomyces griseus].
ACCESSION   WP_457658073
VERSION     WP_457658073.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..380
                     /product="NADH-quinone oxidoreductase subunit D"
                     /EC_number="7.1.1.-"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=41969
     Region          16..380
                     /region_name="NuoD"
                     /note="NADH:ubiquinone oxidoreductase 49 kD subunit (chain
                     D) [Energy production and conversion]; COG0649"
                     /db_xref="CDD:440414"
ORIGIN      
        1 mtettigigg aaentdmvln igpqhpsthg vlrlrivldg ervqhaepvi gymhrgaekl
       61 feardyrqiv mlanrhdwls afsnelgvvm avermlgmev peravwtrtl laelnrvlnh
      121 lmflgsyple lggitpvfha frereelqav meevsggrmh ymfnrvgglk edvpagwagr
      181 vrdavasvrs rmdvyenlvl gneifrgrtr dvgvlsaaav haygvsgpia rasgvdfdlr
      241 rdepylayge lqdtltvvtr tegdclarfe clleqtlnal dladacldrm ahlapgpinq
      301 rlpkvlkape ghtyawtenp lgvngyylvs kgektpyrlk lrsasfnniq altellpgtl
      361 vadmvailgs lffvvgdidk
//
LOCUS       WP_457658074             373 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658074
VERSION     WP_457658074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..373
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39776
     Region          34..369
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltstavla vvavlavalf aatvrfwprl arpgaaavsg riglllatql tlfaavglaa
       61 nnaflfygsw adlfgrqqel gvvsdhagng pgprhmtrid sqhpdvpggr vpavggridk
      121 vvvsgrtsgi espayvylpp eyfqaayagr kfpavvvltg ypgtaenllk glrypqtahe
      181 rvkagkaqpm ilvmlrptva pprdtecvdv pkgpqtetff akdlpeaiag syrvgkrarn
      241 wgiignstgg ycalkiglhh pdryaasagl sayykaaedp ttgdlfhgqg elrdradlmw
      301 tlenrppsgg sflvttsreg ednlgdtmtf iekvkapakv ssivldsggh nfttwrreip
      361 palewlsarl gen
//
LOCUS       WP_457658078             432 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658078
VERSION     WP_457658078.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44818
     Region          18..413
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(29..30,33..34,37,72,119..120,122..124,127,151,
                     154..155,158,244,247..248,251..253,256,287,291,343..344,
                     348,352,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mapstsvrsv rparvhrawl maavagaaiv tagafttvpg llvtplheey awergqiala
       61 asvnmvlfgl tapfaaalmd rigarrvvvg alllvaagal ltgvmtrpwq lvaywgvlig
      121 lgsgcltmtf aagvtarwfd rrrglvtgal gsashlgqll flpllawsvd rfgwrppvvt
      181 lalvalavaa avflllrdhp adagvepyga pefvprpapa pgaamrtlkv laraarggpf
      241 wllagmfalc gastngimws nwapaahdhg mrataaasll slvgvfsalg avlagwltdr
      301 fdprrlltvc favraltlla lplvfassvt apmllfvavy glvdvatvpp vielarrvyg
      361 adgpvvfgwt naahqlgaga saflgatard vfgtydvvwa alaagclvaa llapavrvra
      421 hrpavrepgg lp
//
LOCUS       WP_457658081             566 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658081
VERSION     WP_457658081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..566
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57496
     Region          41..519
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,166,
                     169..170,173,298,301..302,305..307,310,338,342,395..396,
                     400,404,420,423..424,427..428,448)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mstnqpgpvs vdpddaprls gadegegvld arrrrtillt vclalmavia svsglnvaqp
       61 dlavafgasq stilwiiniy tlglaalllp lgaigdrlgr kpvlvaglvv fgvasaaagl
      121 apsaevmlga rllsgvgaam impitlavit ttfpenergr aigvwtgvag gggvlgmfls
      181 aalvdvadwr wlfvlplvlg aaalvmtlrf vpdsreafrh gfdaagalts avavvglifv
      241 lqegpergws spvtliglvv gvlagvgfvv qelrrgdaal ldvrlfrera laggsvtllv
      301 vfgvqagifv vlfpflqavl gwsgllstsa lmpmavlmmm asglaphlaa rvgaratmat
      361 gillagagla lmagivsvdg gylsvlpgml amglgmglam tpsteaitga lprerqgvas
      421 alndvtrefg talgvallga llsagyrgai dsrlagvpdg padsaregva naveaangag
      481 pyaqeliraa rqsfvdgwqn amwagvavma alflyvlfrg plrparaaeg phlaesthla
      541 esartaegts rpvgpdaper adatas
//
LOCUS       WP_457658082             438 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658082
VERSION     WP_457658082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45812
     Region          30..406
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(40..41,44..45,48,81,136..137,139..141,144,164,
                     167..168,171,248,251..252,255..257,260,284,288,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 magqepagqq tarqqsagqe rarpelgrsf gwlwaaftas tagtwlgfga fpliaiqvlh
       61 vgpaevsala aaglavgall alplgpwvea rrkkpvmvvt dlvrfgallt iplahftgtl
      121 tytqllivcv igaaaniaft saagaylqql vrpdhllvan srfetttwta tavgptlgga
      181 aisllgpavt vianaagfll salgigairq reaepehart ekfraadlaq gwkfihadpl
      241 lrslfrntva vnalimatep lmavlllddl gwaawtygla fglpcvggfv garaaprlea
      301 rygrrrvmgt sgvlralwpv glffvmsgtg gvflviavel alitcmgvfn plfaterlqr
      361 vpadrvgrvl tawqvtgvga ialltalwgv laaltdarta igvagvllla tpwlllrgde
      421 gqgrprpggl eepaltta
//
LOCUS       WP_457658084             337 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658084
VERSION     WP_457658084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..337
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35152
     Region          8..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtgaarphlv avvafddvql ldvtgpaevf ttanghggry dvrivsvtgk dvrtsggvrl
       61 gvdgtldslp grlgtllvpg rrdwrqavad aaltagvrdl aersrrvasv cagafvlaea
      121 gllngrraat hwrlagelaa aypavtvepd plfvrdgpvi tsagitagmd lalslveedh
      181 gadpardtar elvvfmarpg gqsqfsarlr preathpvvr aamdavsadp agrhspatla
      241 rrgkvsarhl srlfrseagl tpaqyiesvr leaaqallas gtdpvevvad gagfgsaetm
      301 rrafqqtlgl sptqyrarfr ttttvagtag ttvragh
//
LOCUS       WP_457658087             188 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658087
VERSION     WP_457658087.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20058
     Region          6..186
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mrtskrtqil daatrvvqre gvksvtfdsv aaeagltkgg llyhfasrdd lvqaihqhla
       61 drweadlvaa agkpapeatr derlaaytrv aiqsatrael llmlegstnt ahaavweavt
      121 erwapppppt sasasasasa sadpaaldrf ilrlaadglw lyesltsdrl dpamrqavae
      181 riadaldq
//
LOCUS       WP_457658088             515 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658088
VERSION     WP_457658088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18440193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..515
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53416
     Region          5..264
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          301..>419
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtvfilvaga ftgphvwrdt aarlaadgav vriaaltglg grtggpggsg rtvdlethid
       61 dvlavidavv aeaepggeiv lvghdygihp vlgaadrrag viarivhlda gmpqdgvpal
      121 aavpdqrlre evaeraagsg egagggelpp pdrdawsrwg staglsdaal dgltalaapq
      181 plgtllqplr ltgavagvpv tgvlctgngp gigmlqimvd vgdralrala darvaffelp
      241 tghwpmlscp aelaatliea aagaghrlts atdgaeppah lrpflldvpe rprertgntd
      301 lyppdgpgph pavvfvhggp vpaearptpr dwptltgyar yvagrgavgv tldhrlrsva
      361 dygtaagdva davervradp rvdadrvalw ffsgggplaa dwlakppawl rcvaanypil
      421 eplpswgltd trfnpvrtvs gaghlpfvlv ragremaeia atveefltea arceanveii
      481 dvpegrhgfe tldptdeare avhravdtvl arlkg
//
LOCUS       WP_457658089             220 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658089
VERSION     WP_457658089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24073
     Region          21..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnqsvgrpa hsrarprtpr spearqrqqd ilaiamdafa argynnasla eiadrvgltq
       61 agvlhyfrsk allltsvlel rdqrdiehlg pdrpqgldfl rhlvstalln aeregivrly
      121 avlsaesvtd dhpaqdyfrd ryhglrafvs dalreacelp adraeltdna anaiiavmdg
      181 lqvqwllspe svdmaastdl vvtsllakld perfgphaag
//
LOCUS       WP_457658091             158 aa            linear   BCT 27-JAN-2026
DEFINITION  RrF2 family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658091
VERSION     WP_457658091.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..158
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16267
     Region          1..137
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 msggvewalh ccvvltatee papaarlael hdvspsylak qlqalsragl vqsvqgkagg
       61 yvltrspali tvldvveavd gpgpafvcte irqrgpmatp peactapcai nramgraeaa
      121 wrealrsvtv adlaadvtsd ygtgalgris twlnpaka
//
LOCUS       WP_457658092             373 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Streptomyces griseus].
ACCESSION   WP_457658092
VERSION     WP_457658092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..373
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38880
     Region          41..329
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mssplsstkt aaalrtsarv saelllvlva aavalwvlgr mwsvlwpliv alflttltwp
       61 larflrrhgw rpalaasavt vfsllvgagi valiavpvad qsgelagrvv dgieklrewa
      121 agpplnigdd qitgaldtat sklqdsvgsv vttavtgvst vvnglvtavl avflmffflk
      181 dgtrflpwlt rqlpgrlatd ipevasrswd tlgafvrsqa fvglldavfi glglwildvp
      241 lvlplavltf vsafvpivga lfagfvavvi alvsngpmda livlgiiivv qqlegnvfqp
      301 miqsrglglh aatillavtl ggslagvvgs llavplaall gvawnylreq lseeprepea
      361 eagdlpadap vpt
//
LOCUS       WP_457658093             233 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658093
VERSION     WP_457658093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..233
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24420
     Region          38..202
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mntargqspa pppapesgpa rsggtpasvp gagtkgvpra rreaqilaaa meefgrhgha
       61 sasmasiarr vgvtkpmlyt yfgskdglyl acleqiaprl rsaieeamtp dppgvtpass
      121 nvpprvlaav fdvleeqrea wfvlydrtlk pgsdlhaaah ahrsaidela asgtadvlhg
      181 rgnrdpldad alkhvwtgtv galvgwwish peqsatemaa rcarllaair tps
//
LOCUS       WP_457658098             310 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator ArgP [Streptomyces griseus].
ACCESSION   WP_457658098
VERSION     WP_457658098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11480010
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..310
                     /product="LysR family transcriptional regulator ArgP"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33570
     Region          4..287
                     /region_name="PRK03635"
                     /note="ArgP/LysG family DNA-binding transcriptional
                     regulator"
                     /db_xref="CDD:235144"
ORIGIN      
        1 mmfelpldqv rtllavvdeg tfdaaagvlq ltpsavsqrv kaleqrtgrv llmrtkpvrp
       61 tesgevvvrf arqlsrlerd artalgmagp dgptplsiav nsdslatwfl palrrvpeel
      121 dlcyelrred qdhtaallre glvmaavtss peavtgcsvr rlgrmrylpv aspafadrwl
      181 erragtalhe ligdapvigf drrddlqdaf vrrlglgpra sarrhlvpts egfvnavaag
      241 mgwgmvpevq aepllgdgrl vrlapddtpg rsvvvplywq qwkldspala avadavaaea
      301 tealdgdrpd
//
LOCUS       WP_457658102             534 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces griseus].
ACCESSION   WP_457658102
VERSION     WP_457658102.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 534)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..534
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59486
     Region          12..474
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(67,70,107,110,155,173,177,209,259,320..321)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(209,259,321)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          455..532
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 maavppsrtd twwrdaviyq iyprsfadgd gdgtgdlagv rahlsylaal gvdavwftpw
       61 ylsplvdggy dvadyrtidp afgtldeaek liaeaagfgi kvivdivpnh lsdqhvwfts
      121 alaagpgspe relfhfrpgr gengelppnn wpsqfsgdtw trvpdgewyl hlfapeqpdl
      181 nwshptvrre hedvlrfwfe rgvagvrids aalltkhpdl pdftegvdph pyidqdeihd
      241 vyrswrtiad aydgvfvgev wlpdserfar ylrpdelhta fnfnflscpw dperlrrtid
      301 dtlaehapvr apatwvlcnh dvtrtvtryg rtdtafdfat kefgtpadle lgtrraraaa
      361 lltlalpgsv ylyqgeelgl peadipldri qdpmhfrsgg tdpgrdgcrv plpwaaaepy
      421 ggfgsttepw lpqpadwpty avdrqdadpa smlslyraal rlrretsgfg dgpmtwlpse
      481 dgvlafartd glvcvvnlld rsvelpvhee pllasgplda dgrlpsdtav wlrr
//
LOCUS       WP_457658103             311 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658103
VERSION     WP_457658103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34463
     Region          19..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mqtltiepkr psrpprrpaa qrkrtvrani taygflcaal fcfamfawwp iirqvvlsfq
       61 etnlvdeptw vglanfrtvv adpafgqawk ntvvftllal vcgyvipfav aivlnelrha
      121 rgylrfvvyl pvmlppivsv llfrwfydpg pglfnqvldf aglpalswld ssdtalislv
      181 avstwmnmgs gvliylaalq nipgdlyeaa eldgagifkr iwnvtvpqtr lilllmlmlq
      241 ivatmqvfie pymltgggpe natvtvaylm yqyafvyggn ygagsalglm lmlvllavaa
      301 vqlrltrdek r
//
LOCUS       WP_457658106             677 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658106
VERSION     WP_457658106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..677
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73466
     Region          4..673
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mgnlpvvtts fvgrdselvs veralrdhrl vtltgpggvg ksrlalrtae rardryadgv
       61 wwadlshlhd ehllattvcd gvglldhspr rpvaalgewl seknlllvld ccerivgpcg
      121 qlvaellaaa pgltvlatsr epldaadelc vevpplsage dgddavrlfh eraaavapgl
      181 algdpgstaa vaeichrldg iplavelaca qlrdsspqei tgrlasrmen ltddtlwprr
      241 hralrttigw shelcapler llwarlsvfr gvittadaea vcaggpldte avapalerla
      301 dqsvlrrtgd gyrmldtlre ygamwlaela edalladrha rhfahvsvqa yagwlgpsqv
      361 lwyhriadsh adlcaaldhl laedpemame magcvglfws ccghlhqart ylqrvlalpl
      421 sagphrtral walgitmtlq gdheaarrtg eecghaarrd edpeamllaa hsvsftylmm
      481 grpltahsvs dralrlhpgd padapsqlrc rvirlfalsa lgrldeayee amrlqrislr
      541 fgehwaraya dhqlalihll qgrprhaesh aramlaskhe lhdslgialg ldllagaiaa
      601 qgngvaaara sgtghaywrm ighphrgtpe lgaireqwel rarqaagdsa yerayrhasa
      661 ddaerglaha lergqpg
//
LOCUS       WP_457658107             167 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658107
VERSION     WP_457658107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..167
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18136
     Region          4..141
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mtsisrlrpd haeallafer enrayfaasi pdrgddyfaa faerhrella eqsaglhhfh
       61 liedddgavl grinligvrd asaelgyria ekaagrglat wavqqvcvla vgeyglttlr
      121 aettldntgs ravlartgfe pledvmfgdr pgrryvldls ggappvr
//
LOCUS       WP_457658108             671 aa            linear   BCT 27-JAN-2026
DEFINITION  PTS fructose transporter subunit IIABC [Streptomyces griseus].
ACCESSION   WP_457658108
VERSION     WP_457658108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 13938247
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..671
                     /product="PTS fructose transporter subunit IIABC"
                     /EC_number="2.7.1.202"
                     /GO_function="GO:0005351 - carbohydrate:proton symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0022877 -
                     protein-N(PI)-phosphohistidine-fructose phosphotransferase
                     system transporter activity [Evidence IEA]"
                     /GO_function="GO:0090563 - protein-phosphocysteine-sugar
                     phosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=67974
     Region          1..144
                     /region_name="PtsN"
                     /note="Phosphotransferase system
                     mannitol/fructose-specific IIA domain (Ntr-type)
                     [Carbohydrate transport and metabolism, Signal
                     transduction mechanisms]; COG1762"
                     /db_xref="CDD:441368"
     Region          175..654
                     /region_name="FrwC"
                     /note="Phosphotransferase system, fructose-specific IIC
                     component [Carbohydrate transport and metabolism];
                     COG1299"
                     /db_xref="CDD:440910"
ORIGIN      
        1 mselitaelv dldlsaatkd aaarslaerm vaadrvtdld gfladvaare aqmptgldgg
       61 igiphcrseh vsaptlafgr saagidfgaa dgpadlifli aapagadddh ltilsalarr
      121 lmdpeftaal ragtdpgava alirgeepte npdpepepep eeddataaaa apfrivavts
      181 cptgiahtym aaeslaaagr aegvevtvet qgsagfkkld pavvaaadav iwahdvevre
      241 kgrfrgkplv dvgvkaginr paeliaearr kaergeiaav sedggstdpg dgdgggsgad
      301 hahfgvrlrt ylmsgvsymv pfvaagglli alsfaiggye iasaksvadh fvwgeadswa
      361 allnqigsaa faflvpvlag yiaygmadrp alvpgfvgga ialtvnagfl gglvagllag
      421 avvmaiqrvp vhatlrgimp vlvipliasa vvgflmfivv gkpiaslqna ltdwlnglsg
      481 snavilgvvl glmmcfdmgg plnkvayafa vggladptdg slkvmaavma agmvpplama
      541 lattvrkklf tkterengra awvlgasfit egaipfaaad plrvipsvma ggavtgalsm
      601 afgatlraph ggvfvvplig qpflyllaia agtlvatalv vllkgarrta sdpageaeat
      661 gsddsrvtva a
//
LOCUS       WP_457658113             336 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658113
VERSION     WP_457658113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..336
                     /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=36074
     Region          19..320
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpktsarlla llsllqarrd wpgsllaerl qvsprtvrrd vdrlrelgyp iaafkgpdgg
       61 yrldagaqlp pllfdddqav alavalrtaa atgagigeaa aralttvrqv mparlrhrvd
      121 alqvtavert ggrtqpqadp rvpltlsaav harevlrfdh spayvpaead aapvvrrvep
      181 hrlvtwggrw ylvawdldra dwrtfradri tprtptgprf tprevpggdv aafvaarfqg
      241 sdtpgewpcr geailaapas evaghlrhgi veehgpdrcr vilgawswpg laaelgrfdv
      301 dievvgpdal rdafahlarr yadaagagag aeadga
//
LOCUS       WP_457658118             476 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457658118
VERSION     WP_457658118.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..476
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51013
     Region          35..474
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpsplfadrp apqppahdav ddlihrtrrl rgdvdavrrd aalfdeddpq lrwqralcel
       61 avhhldnlde hlgqlragmp gprtegsapr ddeapagpea gsppnrvgsa ewnlltdess
      121 wsdelyeifg rppgstplsl ddlpsvllpe dqplltamvt gclvdgrpmd gefrivrpdg
      181 dtrtlhmtge pvldaegcta smwavlrdvs elrrseqavg rsrasvrrek hiqrtehrma
      241 velqetvlpp wrgslrlpar gpgaldiaah ylpsassgli ggdwydamel pdgrtlltvg
      301 dltghgipat samammlgal rgmavagiep gallghlnqv letsvqpalg salccrfdpd
      361 tsllswaqag hpapllfrdg sgrilpppdg mllgaasnvv feqddvrllp gdvlvlhtdg
      421 ltqrgdrgag peallalapr faeartaqec vrtvveefgg terpddacvl variga
//
LOCUS       WP_457658119             737 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces griseus].
ACCESSION   WP_457658119
VERSION     WP_457658119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..737
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79861
     Region          3..737
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mreeqefidr lharvdalrg vaadgveral tpvgtgqqar lerdilvaer sgllaaldav
       61 dgslcfgrid rsdglahhig rigireddte htpvlidwra pvarpfylat ghtpmglrrr
      121 rhittegrtv telhdeildl gdrdrtgfed pngdavllaa lnsartgrmg divrtiqaeq
      181 dgiiraphrg vlvveggpgt gktavalhra afllyehrel lakravlivg pnpaflryia
      241 evlpalgetg vllatqaelf pgvratgadt praatvkggg pmaealalav rdrqrlpepg
      301 aamviphedg gdlildweia yearqaardt rlphnlarph fvfrvidalt aqlverigad
      361 pyggpnflgp ddvallgrdv alskevhaav delwppltpe gfladyladp vyvpeedada
      421 irrpagagaw tpadvpllde aaellgvdds aeraaaeaar qervgyaqgv lelsrgsesy
      481 efedeesevl aahdiidaer maerheeadh rtaaeraaad rtwafghiiv deaqelspma
      541 wrllmrrapt rsltlvgdpa qtseeagvgs weeilrpyvg drfehvtlev nyrtpaeime
      601 laagvlrekd psftapvsvr stgekpwkra agedlagava eavveltpre grlaviapra
      661 lheeiaapld gvaageapdl thpvvlldpr qakglefdhv lvveparfgt sdlyvaltra
      721 tqrlgivhre elppalr
//
LOCUS       WP_457658121             255 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces griseus].
ACCESSION   WP_457658121
VERSION     WP_457658121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..255
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28408
     Region          81..242
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mnalhstsss avvtrlhdvg rsmeksgvtn vrgcvrstgr qhqtaaeqvr mpymavvdap
       61 kaaagaygea tgdrgnrten adaeaaftay vqerraslya tayhltgdrf eaedllqsal
      121 fstyrawdri sdkaavggyl rrtmtnlhis awrrrklney pteelpetvg dtdamrgtel
      181 ravlwqalar lpelqrtmlv lryyegrtdp eiasildisv gtvkssiwrs lrrlredevl
      241 sfgrdeqesf gelva
//
LOCUS       WP_457658122             158 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658122
VERSION     WP_457658122.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..158
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16179
     Region          44..>87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msiratnqad viplrpipta aspaipatpe lpglpreplw rdlvgevlrr erqaqgrtlk
       61 evseaarism aylsevergr keassevlaa aaqalglsla dvlalagerl vsltavrsrp
      121 rsgvgslgaa gghrsvrtag parrggpagp mggvllaa
//
LOCUS       WP_457658124             234 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658124
VERSION     WP_457658124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..234
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24601
     Region          22..143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          90..233
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 madretrqtt vwsrpargar gpapersrae ittaalalad aegltavsmr alaqrlgtgp
       61 aslyryvgsr delldlmada vaaeldlsad psgdwlddlv glarqskaah vrhpwladln
      121 drrgevlgph aidyldhalr ilapapgtpg qkleaigllv glatlfarre alavdtetpp
      181 araahlaava aegrhphlla alttagappt agpddrdalf vrllrrvlpa mltg
//
LOCUS       WP_457658143             349 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Streptomyces griseus].
ACCESSION   WP_457658143
VERSION     WP_457658143.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..349
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35318
     Region          58..343
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpapkpllpe sarraaawcg vvllvvgvaa vavwlvvalk tavtpvllal lgtallgpvh
       61 rrlialrlnr slaagltcaa lvavvggagy ivvtalvdsg dqivaslkda gqwvvdhldi
      121 agatdvddla dnaknlvekf gasaagglls gisligslva tsvlallltf fflrdsdrav
      181 slahavaprg tgdlveamgr rafeavegfm rgttfialid avcitvglli ldvpgavglg
      241 alvfvgayip ylgaflsgav avlvaladrg fvialwalgv vlavqvlegh vlqpmiqsrt
      301 vqmhpamimi altagasvag llgmllavpl caaafgvlge lrrpspsgv
//
LOCUS       WP_457658150            1140 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658150
VERSION     WP_457658150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1140
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=120322
     Region          <2..1014
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mtpalfgrdh pvgvlrseia ratdshgglv lvtgeagigk stlvtdaahe arrrgalvvg
       61 gscwdsdttp gywpwvqvlr glrrsataae waaaqeasdg rlavllgdpa kvvtggsdgp
      121 gpstlsapka aaggpdsgaa qggepgtatg tsppgdgspg hgspgggfpg ggaaegpeaf
      181 glfdavttal vtvsqsrplv vvlddlhssd paslrllefa aqhawferll ligtyrdvev
      241 eapghplqql ilplvsrats tltltglgrd evgalmtvtt grepapqlvd evhrrtggnp
      301 ffveqtarlw hsgapvstip pgvreavrqr lallpepvvs lltsaallgr efrrqvlavv
      361 hgapvphver llesavvarv vvprpsgqya fahdllretl yasldeagar aahaaavral
      421 dahggigdav gpgelarhah laggalerdr ridlllaaar dasgrlaeee avghyrrala
      481 vasgedpdlr raaligldla gqlrhagega eaqrlldgav artrelddpe llarvaitly
      541 rdgsmggghd astrdlllga hrgltgkegq enlsddrlaq elaihimala rggsddeala
      601 fslwarhdsv wglgsaveri eltdemtvig rrtrhqdmel hatsmrwval lelgdpafid
      661 qfrtfvrlae qtelprfalg iavdtslias lqgrfaeatt alqdealdpe nndhaafgfm
      721 ghhlrwalhl lqghfaeaee vlgrlpasgy pypgllesvt aveqgdptpa lrliaeqtdr
      781 dgpyprafmp lwlrllaqta avtgdrrlia raedeltpyt gqwivslygc diggpvdlwl
      841 gllaaarddq daavaaltea aassdrlgar pwavrarlgl arallarsga agsgdagggd
      901 agrarrllge vireageldl shlgaeasal rtapptaprt vavsdasaaa gtdtsaapga
      961 aefrrngpvw qlrwdgvtvh vpdakglrdl hsllglpgad vpavrllape ggelvaaagq
     1021 lggdpvldee akrrykerla rldaeidraa arddtrqvet ydrerqalld elrtaaglgg
     1081 rtrrlgdqte rarktvtari rdtlrkletl hpalaahlka svttgttcay rpehspdwrl
//
LOCUS       WP_457658162             306 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658162
VERSION     WP_457658162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..306
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31337
     Region          77..>165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhiqdthgqa alsrasedhg rlgsvgalgv mssadavrsa aavsaaalss agagqapnga
       61 ttagaagapr saplrvdaqr nlehvlraar evfgelgyga pmedvarrar vgvgtvyrrf
      121 pskdvlvrri aeeetsrlte qartalgqee kpwsalsrfl rtsvasgagr llppqvlrvg
      181 vdgeepgapa asgaasasga vdetrvpqqr qgvgqddfrv vgprsgsgde ldglgedsga
      241 vellevvgql vdrardsgel rrdvtvadvl lviataapsl pdaaqqaaas arlldilleg
      301 lrsrpa
//
LOCUS       WP_457658163             479 aa            linear   BCT 27-JAN-2026
DEFINITION  PrsW family intramembrane metalloprotease [Streptomyces griseus].
ACCESSION   WP_457658163
VERSION     WP_457658163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Ho,T.D. and Ellermeier,C.D.
  TITLE     PrsW is required for colonization, resistance to antimicrobial
            peptides, and expression of extracytoplasmic function sigma factors
            in Clostridium difficile
  JOURNAL   Infect Immun 79 (8), 3229-3238 (2011)
   PUBMED   21628514
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..479
                     /product="PrsW family intramembrane metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51739
     Region          56..324
                     /region_name="PrsW"
                     /note="Membrane proteinase PrsW, cleaves anti-sigma factor
                     RsiW, M82 family [Signal transduction mechanisms];
                     COG2339"
                     /db_xref="CDD:441909"
ORIGIN      
        1 msdpsvryqq arpavpvlhe qrldevlgaa pergqwryrp rrvgmvwrsk vfragaviva
       61 lvlcglvila lvreqtgpeg flvglglavl pvpllmaafr wldrvepgpw rnlifsfawg
      121 acaaalvaii ansfatrwia tatadpagad tlgatviapv veesakaaav lliflfrrre
      181 fggvvdgivv agftatgfaf tenilylgna fgedqqlgss gfasvtagtf fvrivmspfa
      241 hplftvltgl gfgfaavsar rhrgrrialp vlglllamgl halwngssaf gpygfyavyg
      301 ivmvpafglv twlaiwsrqr elrtlaaelp ayaaagwltp aeptalssmr argmardlar
      361 hwqqdrtrgr aaaravaeye sfatslaglr rrarhgaagp dfgarerell hhlwqrrdia
      421 apalthaarl tshrppahhr pppygngygn ghgygygygg pvpqqpysgp phshrrppq
//
LOCUS       WP_457658170             454 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658170
VERSION     WP_457658170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  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 454)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..454
                     /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=47419
     Region          202..416
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 migrvrgwrr gwhersklqr idlytrvtly sitwffavsw gllplgdald ngsvavalaa
       61 aflvanitqs vlsnrnlsaa fdhyrgagpf ppgrlrlpva lqvvmtgvlv alaavngvkd
      121 qglvllvldl pvafaipyvl lvpvrrylgl gavyaalvva llaavgvpga sligaasslv
      181 vvtllvlvst rpsiwslsvm wqaeeardmq arlavaeerl rfgrdmhdvl grnlsvialk
      241 selavelaqr gnaaavdqmv evqriarasq qevrdvvrgy readlptelm gargvlqaag
      301 itvtvegadg pagigapaav qaalgwvvre tatnvlrhgd prhcwirlar trdavvleve
      361 ndgagatdpl ggpddgggsg laglrerlga lggtlsagpa gedlfrvtat vpltaprptp
      421 sassslstps tpstpsapsv psspdtasap peer
//
LOCUS       WP_457658175             253 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658175
VERSION     WP_457658175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..253
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25540
     Region          3..252
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mpsplngrta lvtgatgglg saiasrlaad gatvalahld dglaaaelaa hitgsggaai
       61 slaadlrdae avralchqah dqlgpvdilv snagayprrt wtettpahwd aalasnltsh
      121 yllaheltpa mtaagggrii tigsvlatag rhdlagyisa kaglegltra larelgpvgi
      181 tancvapgsi rvpaedtvvd dpeamtarql arqcvqrrgr pediaaavaf lvtedagfit
      241 gqtlrvdggw ilg
//
LOCUS       WP_457658176             185 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces griseus].
ACCESSION   WP_457658176
VERSION     WP_457658176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..185
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20312
     Region          1..>149
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 madiwlmrhg ayeghrpgyh apheaaltqe greqvrrslp lpegvtaivt spiprarqta
       61 tlvshltglp ivatsgllae wrapsivlgr taetypptyr awrarrlanp slrcedgesl
      121 tdlhtrarhc atflhhtavr hgsllavsht lflgvlthlq egpaafvtaa kvpwrfaerr
      181 plpan
//
LOCUS       WP_457658183             369 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658183
VERSION     WP_457658183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..369
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=39035
     Region          1..367
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtgtatvvga gigglataig lrragwsvtv lerrtelery gaafgihpta qsaldrlgvg
       61 dalrdhavpy rdahirtpeg tpiarlpler ierkagrpel lisrpyllda lragleafgd
      121 vplklgervt dvdalaagqd lvigadgirs vvrtarfgdr sgprevgtva wigiadfpsp
      181 vhgetwgsgr ffgltpvepg rtnwyatape attaeelrgl fagwhdpipr ildatdpaaw
      241 iryemrhlyp alptfvsvdv rhapsaagps aagpdssaap valvgdaaha mtpnlgqgac
      301 taildadalt ralaaappgp agvtgalrvy drerrrsaqr tafasrtlhr fmstertrlr
      361 dgavrllpg
//
LOCUS       WP_457658184             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658184
VERSION     WP_457658184.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20795
     Region          2..193
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mnpdrrdrlr daaievlard ggrglthrav draaevppgt tknyfptrda vlravaercl
       61 elyvaltaql aahpgpadre gltalfrsll envagpgrar llavlelqae atrrpwlsgi
      121 ldpmatgdfa gfeaaqrsag lpvtrrraav vtlalhaavp hlltngpgtl aaaglddldr
      181 fvrdlldavy ppdata
//
LOCUS       WP_457658189             297 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658189
VERSION     WP_457658189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30476
     Region          11..293
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkqantttdp apvtvlglgd mgrslarafl aaghpttvwn rspgkgedvv glgavraasa
       61 eeavrasglv vvclvdydas dtvleplaea lrgrvlvnlt sdtparsrrt aawaekhals
      121 yldsaimvpv dvvgsadali fhsgdraafe ahetalkalg apatflgedh glaaaydmam
      181 ldffygamgg lvhafalara egidgaslap ylntiagilp piaaytatdi dsrtyvgegg
      241 nlammaagvd hilhtskdhg ldvsqlaglk svtdravaeg hgssswssiv eviaagr
//
LOCUS       WP_457658193             486 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658193
VERSION     WP_457658193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 486)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 486)
  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 486)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..486
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50756
     Region          165..485
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrsvraraai gatlvvaval vaaglavllv lranlidqad lqaevaarea agqlatgtpy
       61 edvelddeed hpvqvtdeed rvvivskdlk avtgtgasgv tpapsasaga tsspgddddg
      121 dddadddgde drgrpgrgev ssddpdfsdg tatvgrttad yrfaaveatt pdgvtltvya
      181 gaplaaeqea vntvrgamlt glplllvvva gvtwlvtrra lrpvegirre maaitasedl
      241 arrvpepgsr deiaalartt netltvleas verqrrfvad ashelrspia slrtqlevae
      301 ahpelldlpg avadtvrlqv laadllllar ldagekpgsa tvelgalvre evsqragdri
      361 avrvevpegg afevngsrgq lsrvignlld naqrhaeasv avsvaadghg vrvevrddga
      421 gvpeeereri ferfvrldda rsrddggagl glaiardvas rhggtltvhr aaeggaafrl
      481 wlprps
//
LOCUS       WP_457658195             243 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658195
VERSION     WP_457658195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  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 243)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..243
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25561
     Region          52..243
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 maavlltetr lflrepgslf wilafptvll vilgfvpafk eadenlggrr vidlyvpvsv
       61 llamimaglq amppvltayr ergilrrmst tpvrpsvllt aqitlhgaaa lgsallvvav
      121 grvgygvalp gqllgyalal llavaavlsl gaticalsrt tkaatavgsv aylammftag
      181 vwvpvqampd tlrrvvqltp fgaasqaldq aasghwpswa ylgvvalwtv ilgiaagrlf
      241 rwq
//
LOCUS       WP_457658198             543 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces griseus].
ACCESSION   WP_457658198
VERSION     WP_457658198.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..543
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58418
     Region          22..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msasdthisc aslafswpdg sevftgfdlt vgpgrtglig lngcgkstll rliagelapq
       61 dgvitvrgel gylpqtlald talrvdevlg iadrraalda vesgdvrdgh fevigddwdi
      121 eerslatlng lglghigldr tigemsggec vllrlaalll drpgvlllde ptnnldayar
      181 rrlydavdaw tgallvvshd rellervdri adlregsvtw yggnlsayee alaveqeaaq
      241 rmvraaesdv qrqkrelaaa hvtlarrkry gqkmwdtkre pkvvmgqrkr aaqvsagkhr
      301 ilhterlaaa eerldeaesa vredeeirie lpgtrvhpgg evlllrdpvp pygpalrgel
      361 mvrgperial tgrngagkta llrtiagdlt plsgeasplv atgflpqrln vlddassvvr
      421 nvarsapgst dnavrarlar flfkgaaadr pagtlsgger fratlatlll adpaprllll
      481 deptnsldla svrrlteale ayegalivas hdvpflesig itrwlrldge lrdttaeavr
      541 agg
//
LOCUS       WP_457658201             743 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457658201
VERSION     WP_457658201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 743)
  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 743)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..743
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79702
     Region          68..702
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mkqsgaaggt algtlahgaa gspvptggaa rellaraerl lesaravpad raaatdavrt
       61 vldplldalv dqelahipvg rlkdvtegrl rlgaleqagf gtvgqvhgtg ryelrqlpgv
      121 gahtadqala aagqiahavr dtvsvridvd apddtstalv ialhrlveag aearravdaa
      181 rrlgerlgpa vataapagsr lrmlfsgrek rarvrealda vrsavaeave relpvllaqa
      241 sadllrspas paeawvdfel rsaeyyslla elsgsgpdrd aaegflpagi adrvralrld
      301 dtrlrvslrg yqafgarfal tqkrviigde mglgktvqai aalahlaahg eshflvvcpa
      361 svlinwtrei rarstlravp vhgaerteaf aewresggva vttfdalhll pegaaaevrp
      421 gmlvvdeahf vknpearrsr avagwaerve rvlfltgtpm enrveefrsl vrqlrpelap
      481 svssthgaag srafrravap aylrrnqadv laelpalvqv deweefgaed raayreavas
      541 grfmrmrraa yaapgtsakl erlrelvdea rdnglkvvvf syfrevlatv gdalgpdafg
      601 plsgsvppar rqelvdafsa vdghavllsq iqaggtglnm qaasvvvlce pqikptlehq
      661 avarahrmgq vrtvqvhrll atdsvdqrlv ellarkdrlf dayarrsdla ettpdavdvs
      721 daelarrive eeqrrlvdds rrp
//
LOCUS       WP_457658211             432 aa            linear   BCT 27-JAN-2026
DEFINITION  MCE family protein [Streptomyces griseus].
ACCESSION   WP_457658211
VERSION     WP_457658211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Asthana,P., Singh,D., Pedersen,J.S., Hynonen,M.J., Sulu,R.,
            Murthy,A.V., Laitaoja,M., Janis,J., Riley,L.W. and Venkatesan,R.
  TITLE     Structural insights into the substrate-binding proteins Mce1A and
            Mce4A from Mycobacterium tuberculosis
  JOURNAL   IUCrJ 8 (Pt 5), 757-774 (2021)
   PUBMED   34584737
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Zhang,F. and Xie,J.P.
  TITLE     Mammalian cell entry gene family of Mycobacterium tuberculosis
  JOURNAL   Mol Cell Biochem 352 (1-2), 1-10 (2011)
   PUBMED   21258845
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Haile,Y., Caugant,D.A., Bjune,G. and Wiker,H.G.
  TITLE     Mycobacterium tuberculosis mammalian cell entry operon (mce)
            homologs in Mycobacterium other than tuberculosis (MOTT)
  JOURNAL   FEMS Immunol Med Microbiol 33 (2), 125-132 (2002)
   PUBMED   12052567
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Flesselles,B., Anand,N.N., Remani,J., Loosmore,S.M. and Klein,M.H.
  TITLE     Disruption of the mycobacterial cell entry gene of Mycobacterium
            bovis BCG results in a mutant that exhibits a reduced invasiveness
            for epithelial cells
  JOURNAL   FEMS Microbiol Lett 177 (2), 237-242 (1999)
   PUBMED   10474190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..432
                     /product="MCE family protein"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005548 - phospholipid transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /GO_process="GO:0044409 - symbiont entry into host
                     [Evidence IEA]"
                     /calculated_mol_wt=45585
     Region          42..118
                     /region_name="MlaD"
                     /note="MlaD protein; pfam02470"
                     /db_xref="CDD:426790"
     Region          122..344
                     /region_name="Mce4_CUP1"
                     /note="Cholesterol uptake porter CUP1 of Mce4, putative;
                     pfam11887"
                     /db_xref="CDD:432164"
ORIGIN      
        1 mrtsstrtar rrlagvtfll vpavlvwvsv svyqkdftdd atvtvrtgsv gnemhthadv
       61 klrgvvigqv rsiatdgega rltlaidrdk lgripadvta qmlpttlfga rfvalvppri
      121 ptgstlraga vipqdrssna ieleqvldnv lplltavkpe klsatlnavs qalegrgerl
      181 getlttldgh lkkfnpqlpt lnadikelvk vstlyadaap dvldaltdat vtsstladqe
      241 arlaglygtt taaaqdvtsf lrenkdnlir lsassrpslq llaeyaesfp ctlrtmagfv
      301 pamdkalgkg tdqpglhvsv kavaskgkyv pgkdtpvyds tggphcysvp yvgkhaptad
      361 trraadvtap pptpdkggdg tdtalglpns pqesrlvnel vapslkvrpg dladwssvli
      421 gpafrgaevk lk
//
LOCUS       WP_457658212             157 aa            linear   BCT 27-JAN-2026
DEFINITION  SCP2 sterol-binding domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457658212
VERSION     WP_457658212.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..157
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=16726
     Region          53..155
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 mdgtssgnlt dslagldfaa vgpeefariv kglsakqlae vmrgelrtri lgevfgrmrq
       61 qfrpeaaggl talirwkitg eddvvyetai adgvcrvtsg rsdaeprttl vmgdaeflrl
      121 vsgngnpvtm fmtrklkvag dvglasgltr yfdipka
//
LOCUS       WP_457658214             321 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658214
VERSION     WP_457658214.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34717
     Region          7..321
                     /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 makesshrvv mivsagsnpf emgvatelfg lrrpelpvgw ydftlcsptp tvrmhsgffq
       61 lsdvpglsav dradtvivpn rpdpleepdp dvlaairrah argarlvsfc tgaftlaaag
      121 vldgrratth wrwadsftar yprvdldpdv lfvddgqmit aagsaaaldt glhliradhg
      181 aetaaavsrr lvhpahrdgg qrqfvehpvp gtadaslapl ldwatehlad gldvaalaah
      241 aavspatlhr rfraqlgttp lawlteqrvt larrlmerge erldviaras glgtatslrt
      301 qlrrrtgltp teyrrrfapa p
//
LOCUS       WP_457658215             546 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658215
VERSION     WP_457658215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  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 546)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..546
                     /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=58824
     Region          151..374
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mvrvespptd reipvvrvvl lpvvlllgat aagaalvapa aripvavcga ittfvvavlt
       61 aalhrrrram rvqraeyeqr iaylehriqs hdaetvrltk dvmpaairrl rvgnspeevm
      121 rdivdadvan rhlpkalreq iyqvlevidn eearrdsaqr afvsvarrvq aivhrqasel
      181 remenhygrn pevfddllri dhgtaligrl adsiavlgga rpsrqwpkpv plfsvlrgam
      241 srileyqrvd lhsiakvaiv gtsvepliha caelldnatr ysppqtrvhv tavevqtgia
      301 ieiedggvsl seeararaen mlaqaqagin mndlgesprl gmavvgrlsr myqlqvslrq
      361 sayggvravl ivprdmittg papgiahgig atsrptssld msqlqhvvpp pgkrkpkpaa
      421 tgpvpsvaap vstgapaats rpavppaame ddvpvvtewt englpqrrsr graplgshnl
      481 pqqpppppap angfqpgpde gtdggrgeek ppglwleaft kavngvpqer khgedsddaw
      541 dkgdlk
//
LOCUS       WP_457658219             384 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Streptomyces griseus].
ACCESSION   WP_457658219
VERSION     WP_457658219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..384
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41699
     Region          80..331
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mesvlrpliv iggsvvitll igwladlllr radsrhhetp lwgllrrcrp plqvvvital
       61 lrgsyrqtri dwvwdhragi gqvltlvlig asawlvvria atvveasyar yaaatrdpar
      121 vrrvrtqvtl iqrvviavvt vvaiaamllt fppmravgts mlasagllgi vagvaaqstl
      181 gnlfaglqia fgdmvrigdt vvvdgewgti deitltflav rtwderritm pvsyftgqpf
      241 enwsrggvqm tgtvffhldh sapvaamrek lrdllgdiaa wdgrdwslav tdttpstiqv
      301 ravvtakdan diwtvrcavr eqligwlrdh hpyalpriat apavlppgeq waeptgagtd
      361 rpgrngtspp adrgdskapr tgrg
//
LOCUS       WP_457658220             556 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces griseus].
ACCESSION   WP_457658220
VERSION     WP_457658220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..556
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59669
     Region          30..524
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtsrhlpsps rrtvvraaaa saaavpvlat asvtsaapar aagapaflhg vasgdplpdg
       61 vllwtrvtpe pgaepgsglg adtpvrweva edreftrisa tgttiasaas dhtvkadvrg
      121 lrpataywfr ftagddtada vvspvgrtrt apatdaavsg irfgvvscan weagwfsayr
      181 hlaarpdlda vvhlgdylye ygtgeygtrg atlrahrpah eildladyrt rhgnyktdad
      241 lralhaahpv iaiwddhefa ndawsggaen htpvaegawe qrvaaakqay fewmpvrast
      301 egtvyrrlrf grlaelhlld lrsfrseqas vgsgavddpe rtvtgraqld wlkaglagsd
      361 aawklvgtsv mispvafgal pahlleplag llglpkegla vnvdqwdgyt ddrreliahl
      421 rdrgvadtvf ltgdihmawa ndvpvkaaty plsasaatef vvtsvtsdnl ddilrvapgt
      481 vsvvaaaavr aanrhvkwvd mdahgygvld vtaeraqmdy ytlsdktdre attawtrsyr
      541 trrgtqrver adrpvr
//
LOCUS       WP_457658225             421 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658225
VERSION     WP_457658225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..421
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45314
     Region          146..419
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpqvvrprig altgppptap lphrfrslad reavevlhra arvlvaslpa ltdrlvealy
       61 aqepgyraai esdraevwqe vhhslrhnvg sliqprefre sahrtsrwig eiraeqgvpl
      121 davlhafrmg gamvwqdlvd etarrdpddv rllvhvaadv wnfvdehcgi vadayrqaer
      181 rltwrrenrq rlmvaalldg tariadlada avmlglpeqg ryavlavatg saarpaltlp
      241 aapeavvlwh pgqdaefail plagapgels elaaaldvpp garagigsav eglaalgdar
      301 rlaetalrac pasggtvlld ehlpdalvvs spalagalad rvlgpldrld padrdvivet
      361 ltawldadgs aqragarlyc hrntvlnrlr rfeqltgrcl trprdavevs lalaarrllg
      421 a
//
LOCUS       WP_457658226             195 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces griseus].
ACCESSION   WP_457658226
VERSION     WP_457658226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..195
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21956
     Region          4..>80
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mpseerrrvs dldtlkaigh plrlklyral hikrtatasq laelvdeavs lvsyhlrkla
       61 dsgliepaeg qgtdgrerww qpssrgltfs dedfddapdk aavyaaanrm sfdqhvelyr
      121 ahqdsrhtwd tewrsaswss enllrltage laslsremga lidryeeagr ardeagdteg
      181 retvalhtyg fpfrp
//
LOCUS       WP_457658227             418 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658227
VERSION     WP_457658227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41602
     Region          19..406
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(28..29,32..33,36,67,122..123,125..127,130,150,
                     153..154,157,242,245..246,249..251,254,278,282,335..336,
                     340,344,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtttvecpvq pahrdpnvlr wlgaytasmi gdsvyfmala waaartgsas gtglvlaags
       61 lprallmlgg gvladrlgpr rvvigsdaar allvlslaav lvltaptvgv lvavallfga
      121 vdalflpavg alpprisgpg qlariqglra laargssiig aplggvavat ggpalafaaa
      181 gvlfalslpl llrlrirplp eptetsgeap aaektpnawh dlvdglryir rhpllgplml
      241 vialselgfv gplnlglill seqrgwgaag mgwivagfag gaagsalvla vrgrvpragt
      301 vmclmalvga tgiaalaqvp svalaaaiaa fvgltaglag alcgalvqta adpaylgrvt
      361 svstfftyai aplsypvtga avalwgtgpv favsaavcaa ggvmglavtt lrraelpr
//
LOCUS       WP_457658228             407 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces griseus].
ACCESSION   WP_457658228
VERSION     WP_457658228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43100
     Region          11..407
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msttaagpts ttaagpltgl kvidlatlfa gplaatmlgd fgadvikveh prkpdpsrgh
       61 gpakdgvglw wkllgrnkra ltldlsapgg rdvllrlaag tdvivenfrp gtlerwglgp
      121 eelhavnprl vlarvtgfgq fgpyahrpgf gtlaeamsgf aaitgepdgp ptlppfglad
      181 siaalataya vmaalagrek tgegqvvdla iiepiltvlg pqplwydqlg hvqprtgnrs
      241 rnnaprntyr tadghwvavs tsaqsvaerv mrlvgrpdli eepwfgagtt raehteeldg
      301 avghwisrhs rdevingfek aeaavapiqd vrevmedpqy ralgtiaevd dpelgplrmq
      361 nvlfrlsgtp ggirwagrph gadtdeilag lglsenriaa lrdqgal
//
LOCUS       WP_457658235             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658235
VERSION     WP_457658235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22974
     Region          11..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptkkkpqvt ptperrrell ataaevfaaq gynattvrri adeagmlags lyyhfdskes
       61 mideilstfl delwqgydav laaglgpret iealviesfr eidrhrpava iyqkeskhla
      121 tqprfaylvd sqtkfekawl gtlergvaeg vfrddldirl tyrfvrdtvw vaaswyrpgg
      181 hhspeeiarq ylsmvldgia lri
//
LOCUS       WP_457658237             548 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces griseus].
ACCESSION   WP_457658237
VERSION     WP_457658237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..548
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56930
     Region          81..451
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtsserserq drtprsrpar grgrgqgagp qaasngrgga prsrnqggsk paarrkpava
       61 qpaefalpet vtpalpsvea fadldmpaal lktlaaqgvt epfpiqgatl pnslagrdil
      121 grgrtgsgkt lafglallar tagrrsepra plamvlvptr elaqqvtdal tpyatavnlr
      181 matvvggmsi tkqsatlrrg aevlvatpgr lkdliergdc rldevsitvl deadqmadmg
      241 fmpqvvallk qveadgqrml fsatldknid rlvkmfltdp vvhsvdpsag avttmehhvl
      301 hvldetdkka vatkiaardg rvimfvdtkr aadrfakrll asgvraaalh ggrsqpqrnr
      361 tldqfktgev talvatnvaa rgihvddldl vvnvdpptdh kdylhrggrt aragesgsvv
      421 tlvlpeekre mtrlmqdagi aprttrvtsg daelsritga repsgvaivi evpqptppkq
      481 rarsggsags gsgggavrsg srgrgrrgsg gaggtgggag rsggagrsgg eargagrsga
      541 pargrraa
//
LOCUS       WP_457658240             326 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces griseus].
ACCESSION   WP_457658240
VERSION     WP_457658240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Nemeth,E., Kozisek,M., Schilli,G.K. and Gyurcsik,B.
  TITLE     Preorganization of the catalytic Zn(2+)-binding site in the HNH
            nuclease motif--A solution study
  JOURNAL   J Inorg Biochem 151, 143-149 (2015)
   PUBMED   25898772
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Veluchamy,A., Mary,S., Acharya,V., Mehta,P., Deva,T. and
            Krishnaswamy,S.
  TITLE     HNHDb: a database on pattern based classification of HNH domains
            reveals functional relevance of sequence patterns and domain
            associations
  JOURNAL   Bioinformation 4 (2), 80-83 (2009)
   PUBMED   20198175
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Mehta,P., Katta,K. and Krishnaswamy,S.
  TITLE     HNH family subclassification leads to identification of commonality
            in the His-Me endonuclease superfamily
  JOURNAL   Protein Sci 13 (1), 295-300 (2004)
   PUBMED   14691243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="HNH endonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35793
     Region          195..308
                     /region_name="COG3440"
                     /note="Predicted restriction endonuclease [Defense
                     mechanisms]"
                     /db_xref="CDD:442665"
ORIGIN      
        1 mteaetaasr aqgrawsflv tgddrqfqgn dgyediveks ysydstvsnh qhvavgdlvv
       61 vrngkealga gyvealqvlp dqekvrsrcr fcgntgfker atmrprfwcs rcknafddpt
      121 vetltvtafr ahyggtwqpl dgcldkvqls elspsrshqq sikkmhpdrt lkairdrgvr
      181 lpgpreagge rghrpqvlpg gsrratasvr rgqdgfrkal vrqyglicav tgaapaevle
      241 aahlrpfsdt qhhrveeglm lrsdvhrlfd sgllaidshl vvhiapslag helysslegt
      301 plhiahdapi dravvadhha atvatw
//
LOCUS       WP_457658244             225 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658244
VERSION     WP_457658244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24340
     Region          35..189
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqgqqgqddd rdrygargeg eppagaadpe prrgrprsaa aeraildavi alleagepla
       61 glsieriart agvgkatiyr rwsgkeelfv dvvrdmeptd ppvsgtagla dlrvmleslr
      121 trglaqrssv llvnifaqmk shpklweeyh gtviaprrva mleavrrava agelrddldv
      181 eliddlfvgp mlvrtvhrpd tslpddladr iitallqgla ptara
//
LOCUS       WP_457658245            1223 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658245
VERSION     WP_457658245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1223)
  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 1223)
  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   3  (residues 1 to 1223)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1223)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1223
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1223
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=128903
     Region          1..240
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          192..1058
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(917..918,920,943,946..947,950..951,953..954,980,
                     983..984,987..988,994)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          941..971
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          979..1008
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrycilgttr alrddgtava lggarlrall tvlalhpgrt vpagalvdev wdgdppadaa
       61 galqalvgrl rralgrsave svaggyrlaa ppdavdlhrf erlagegsra ladgdaasal
      121 avlgealalw ngpaladlpd rtatasrwea rrldarraaf gallalgrpd aalpelaalc
      181 dahpldeplq vlritalrda grpaealaay eevrtllddr lgtapgpalr alhadllhqe
      241 paepnpsgrt gpglpgpaap evsgpaapgp agpaapkfsg psaqgqtpdp aqggpepvpa
      301 pgavpgmegv papatgtapa patpttaqas pppppppppa ygnlrarlts fvgrdtdmaa
      361 lredlgrarl vtllgpggag ktrlsqeaae aaaeawpdgv wlaelapvdd pdtvpeavlg
      421 algaretvlr gagaeelraa drtgddplvr ltehcaprrm lllldncehv vgaaaaltdh
      481 llthcpqltv latsreplgv pgefvrpvep lpdpmalrll aergaaarpg frtdadeata
      541 aacaeicrrl dglplaiela aarlrmltpr qiadrlddrf rlltngsrtv lprqqtlrav
      601 vdwswdllda seravlrrls vfaggcslaa aeevcalpap adgvsvdald vapllgslvd
      661 kslvvaapge dgemryrlle tvgeytaerl aeageraavd rshlvhyrel vrttgpamrg
      721 sgqraaitvi rreyenlrta frhavaarde healclvlsl swywmlrdlr sdarhwadaa
      781 sslgpdpfar pgvrapslpe saidrpppmd dgqlaearrg valiqvasvd daisswsdaa
      841 gqerlriiad ayrpgqpqtc rmpgtfwiya imltgdmdrt rqaldetvrt srshgfewel
      901 aaalqlranf laghsghadl aradaeeslk lftrldddwg taealasrge anertghfpe
      961 aledyaaave yarkigarsq vallraryag plaelgrlpe aeaalrevcd egrpptpesv
     1021 aiarmhlafv lgaqgrptea reqvdmirar ltfgdvalfd gfvfgvlawl dnlegesasa
     1081 lgnaltalec srdrlsmmva pqmpsahlma iaralaglaa aggagsgaya daarllglqa
     1141 allppghvpt mierrnlaea eeaarvhlde eaytaayeeg ggltldeata laetyrptpp
     1201 prsdvwvrps sgtwpppaep spa
//
LOCUS       WP_457658249             360 aa            linear   BCT 27-JAN-2026
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457658249
VERSION     WP_457658249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=36938
     Region          86..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 gpdtgrtarr rparvraaaa ltaavafalv ltgcgggdgp apksasgkss
       61 adadrvepla appapklpvt vdsadgtkvt igstdrivpl tgslseivft lgfgkqvvar
      121 ditatfeqae klpvvtrahd vsaesvlslk ptivladttt gpseaidqir dagipllvve
      181 pakglddvgr ridtvaealg vpsagtelke rtekriadvq ksipdhadgk kprvaflylr
      241 gsasvyllgg aesgasslle aagavdagke sglnkdftai tsealakaap daillmtkgf
      301 esvggmdglv kipgiaetpa gmdrrvvtvd dgvllnygpr tdrvlteive qlyakggkgr
//
LOCUS       WP_457658251             331 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457658251
VERSION     WP_457658251.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34995
     Region          3..247
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgetvrwgvl atggiaatft advqklpdae vvavasrtet sarafaerhg igraygswae
       61 lvaddavdvv yvatphsahh aaaglalrag khvlcekaft lnsreavelv elarerglfl
      121 meamwtylnp vvrrltelvr dgaigeirtv qadfgfagdf apghrlrdpe lgggalldlg
      181 vypvsfahll lgepdriqad allspegvdl ntgmllgwds ganallscsi vghhptaatv
      241 igtagridip rdffhpdhav lrragaepet itsgpgpqgl sgmqyeaaev mravragete
      301 splvptagsl avmrtldavr drigvrypad r
//
LOCUS       WP_457658252             263 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658252
VERSION     WP_457658252.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..263
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27510
     Region          15..256
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnteqtaqte qarrtrrkva vvtgagsgig ravalalara gwslalagrr aeplaetaaa
       61 agdtealcvt tdvtdadeva alftavrdrf grldllfnna gtfgpggval eelaaedwra
      121 vvdvnltgaf lcaqaayrlm keqdpqggri inngsisaha prphsiayta tkhaitgltk
      181 slsldgrpyr iacgqidign aatemtermr tgilqangel avepvmdaad vartvahmae
      241 lpleanipfv tvlatnmpyv grg
//
LOCUS       WP_457658254             221 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658254
VERSION     WP_457658254.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..221
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23572
     Region          41..210
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 maapepehga apdsgptpgp ipgpapgpgp dpltvpsmsa gpdfvlrpwe msdltlvrea
       61 sldpyiplit tiparysdaa aeafvrrqwe raatgtgypf aivrsrdrrp vgaiglwlrd
      121 lpegraslgy wltasargqg varaalrtvt gwalrdlgvp rlqlfvepwn tasaqvaedv
      181 gfrregllrg wqqvgderrd mtvyallntd gpadgraaaa n
//
LOCUS       WP_457658255             303 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces griseus].
ACCESSION   WP_457658255
VERSION     WP_457658255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33491
     Region          5..258
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 msapsaprig vsivtmgdrp qaveallasv amqdvrptrl viigngtqlp dysstpglen
       61 ldggvttiel penlgcpggr neglrrlaei gdvdvvield ddgllvdkdv frrvrdhfaa
      121 ddrlgivgfr iadelgetqr rhvprlragd pmrggevtaf lggghafsmk mleqtglwpa
      181 effftheetd lawraldagw kvlyepelll qhpktsparh avyyrmtarn rvwlarrnlp
      241 lplvpaylgt wtlltlartr dpkglrawag gfaegvrtpc gerspmrwst vwqmtrlgrp
      301 pii
//
LOCUS       WP_457658256             337 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457658256
VERSION     WP_457658256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  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   2  (residues 1 to 337)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..337
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35793
     Region          7..337
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 maeelprrht tldevaalag vsrsvasrvi nhaphvsrak resverairk lgyvpdpkar
       61 alatrqagaa alvisrddpe vltdpffgqv iagvagalee adlnlmlcva atprgrerve
      121 rlvrsravdg vmltashedd plariakesp lpvvfggrpv dfeprwyvdi dnvggareat
      181 dhllargrtr vvticgpldt evarsrhrgy reamtlaglp prppeegdfs eaagaaamar
      241 lleahpdldg vfaandnmaa galralrgag rsvpgdvavv gfddlavaqv tepalttvhq
      301 pirglgrema rmlvgliagr tsgplilptr lvkrsst
//
LOCUS       WP_457658257             253 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658257
VERSION     WP_457658257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..253
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26802
     Region          1..101
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(49,52,56..57,66,86,90,96,100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrigeiaalv gvtsravrhy hhigllpepa rqangyrayt vrdavllari rrlteiglsl
       61 devrdvladd agrelgevlg eldadlarqe reiqerrqvl avlleapltp dgpllspala
      121 allekapatg spaaakdreh lalldaaggg agaevfaalr plaedpgvla lyerldelag
      181 agvddlriap laaelvaavp devlavipdg epspsgfgrv llddyppaqr evvrrvmval
      241 aergrlrvhr gtp
//
LOCUS       WP_457658262             462 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658262
VERSION     WP_457658262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46271
     Region          12..426
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,138,
                     141..142,145,269,272..273,276..278,281,309,313,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtsrqklvla lllgsqfmia vdfsilnval pvvgeglgfs lahlqwiats falaaagftl
       61 lfgrvadlvg rknlfiggma vlglssalgg lagspevllt arvlqglata avtpaglall
      121 ttafkegplr eralglngal msagftagai lgglltdlls wrwaffinvp vaalvlalap
      181 svitdsrper rprldvpgav tvtggllllv lgltragetg wttpatlaal aagavllaaf
      241 vrieqraaap lvpthilgrr svvwgntagl iafatetslv flltlylqev lgysalatgl
      301 afgvlgigtv vggllggrav grfgnrraiv lggavqaaaa lalvalgtsg awiwlllgat
      361 fvggvgnmlm ivgfmvtats glpdaeqgra tglatmtqqv gialgipvms avvtagtgaa
      421 tgpeavlsgv stailvnsal vlagallagy fltgegrgpk da
//
LOCUS       WP_457658271             699 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces griseus].
ACCESSION   WP_457658271
VERSION     WP_457658271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..699
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=73320
     Region          1..698
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mttrapqfpg apvvrreard kvtgsaryaa drtpsgclya wtvpatvaag ratavravda
       61 lavpgvhavl thdnaprlqe pddpilavlq ddrvphhgwp ialviadsle aartgagalh
      121 veyerdpfdv tltedhpgly tpeeanggfp avrvrgdver alagarvqvd atyrmgalhn
      181 hpmephaata vwedghltvh dssqgsdkvr gslarafgla sdritvvseh vgggfgskgt
      241 trpqavlaam aarhtgrpvk lvfpraqlae vighraptiq rvrlgagldg vltavshevv
      301 tqtstvkefv eqaavpartm yaspysrtah rvtaldvpsp swmrapgeas gmyalesamd
      361 elasalgldp velrlrnepe tepdsgrpfs srglaaclrd gaarfgwhdr dprpaarqeg
      421 rwligtgvas atypvlvsrs tasahaapdg alsiavnatd igtgartvla qiaadalgvd
      481 peavhidigs tdlptaplag gssgtaswgw avhkaaadla arlaehtgpl ptdgitttad
      541 teqetgeesp yarhafgahf aetavdavtg evrvrrllgv yaagrilnar tarsqftggm
      601 vmgigmalte dcgldpdfgd ftakdlaayh vpvcadtadi qahwieeddr hlnpmgskgi
      661 geigivgtaa aignavrhat garlrelplt pdtllpyll
//
LOCUS       WP_457658273             792 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Streptomyces griseus].
ACCESSION   WP_457658273
VERSION     WP_457658273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..792
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87287
     Region          10..792
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 msdtparssl sddelaalda hwraanylav gqiylmanpl ltrplvpedi kprllghwgt
       61 spglnlvhth lnrvikarel salcvwgpgh ggpavlansw legsysatyp dvgrdaagmg
      121 alfkqfsfpg gvpshvapet pgsiheggel gyalahayga afdhpdllva cvigdgeaet
      181 gplaaswhgd kfldpvhdga vlpilhlngy kianptvlar ipeeelghll rgyghdplfv
      241 tgddpaavhr alaaaldtal drigayqraa reggaterpr wpmivlrtpk gwtgpeevdg
      301 qpventwrsh qvplsgvrdd pghlrqledw lrsyrpaelf dadgrpteqv lacvpegesr
      361 lgstpyangg lllrdlplpd padhavrvdr pgttlheptk vlggllesvm aatadrrdfr
      421 vvgpdetasn rldalyratg kawqaetlpt dehlahdgrv mevlsehlcq gwlegylltg
      481 rhglfssyea fahivdsmvn qhikwlrtsr rlpwrrpias lnylltshvw rqdhngfshq
      541 dpgfvdhiln kspevvrvyl ppdantllsv adhalrsrdy vnvivagkqp tfdwltpeea
      601 rahcargaga wtwagtedga repdvvlaca gdvptqetla aadlirrhlp elavrvvnvv
      661 diarmmpdte hphgmpdsey dalftrdkpv ifayhgypwl ihrlayrrtg hahlhvrgyk
      721 eegttttpfd mvvrndldry rlvmdvidrv pglgvravav rqemadtrtr hhawirehgt
      781 dlpevvdwkw gg
//
LOCUS       WP_457658287             394 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658287
VERSION     WP_457658287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..394
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42593
     Region          158..384
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 msmpmgyvas tavltwctff avvaprrprp lasmsfwfgl ginevpfmgi yllvgstvla
       61 aaegdlrspg akvtaavaav aaaglalsaw rgvrtdrvvg aalrqglgad wreqvrvplr
      121 rhrpwarill lpalmwrrdv eripdirygp agrrnlldvy rhrgaprggp vlvhfhgghf
      181 tggaknrear pllyrlasqg wvcvsanyrl rpetsfpghq idakkviawa rehaadhggd
      241 psklfvagss agsnlaglca ftqndprfqp gfesadtsvt aaiclygyyg hyfgdrpdee
      301 pspnqpqgyl rsgappvlvv hgakdalatv eaarhfvgrl rrisddtvvy aelpgaqhsf
      361 dvfhsprfea vvdgveafaa rvladpgrts adtp
//
LOCUS       WP_457658288             383 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658288
VERSION     WP_457658288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..383
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40509
     Region          20..372
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mtttphhpia viggglgglt larvlhvhgv hatvfdleas paartqggml diheetgqaa
       61 lrearlyeef tarvhpggqa mrvldrhgvv rreepddgsg grpeidrgdl rdlllsslpd
      121 gavrwnakav scrpldgggh eveladgsvf ttgllvgadg awsrvrplvs patpaytgvs
      181 fveldlndad vrhpgaagli gggmffalge ekgflghret dgslhiyval radeswlgtv
      241 dftdtdaaka ilakhfdgwa palrdlidaa dgplvprhih alpaghrwpr tpgvtllgda
      301 ahlmspfage ganlalidga dlgrclaahp gdteaaltay eeimfpraed taresaegld
      361 vifdprapqp lvdmfarfdg eqh
//
LOCUS       WP_457658292             282 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658292
VERSION     WP_457658292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..282
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=29840
     Region          3..282
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 marklaviga glmgsgiaqv saqagwdvvl rdvtdaaltr grdgikasyd kfvskgklda
       61 adaeaalari ttttdldava dadvvveavf eklevkheif rtldkvvgeh tvlasntsai
      121 pitkiaavte rpervvgahf fspvpmmqlc elvrgyktsd etlatarefa esvgktcivv
      181 nrdvagfvtt rlisalvvea aklyesgvas aedidiackl gfghamgpla tadltgvdil
      241 lhatgniyte sqdekfaape lmrrmvdagd igrksgqgfy ty
//
LOCUS       WP_457658293             259 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658293
VERSION     WP_457658293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26658
     Region          4..248
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtvistagla rtfttpsgpv eavrsidlti rpgeivallg pngagktttl rmlttlltpt
       61 ggaatvaghd lladpaavra vcgyvaqsgg vdphltvree lvtqgrlyrl graeaaarae
      121 elaaalgldg llgrkavsls ggqrrrldia mglthrpavl fldepttgld pgsradlwel
      181 vrslreetgt tvvltthyld eadaladrli lidggtvvae gtpaelktry agspdaslqd
      241 aflaatgrpv tpadapvav
//
LOCUS       WP_457658295             399 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658295
VERSION     WP_457658295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 399)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..399
                     /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=41740
     Region          133..395
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mltslrpdrd avalavsgll gglllwllgl htqgghpfsa pwvtlvplta maaaellrrt
       61 aprtaltiga lalvadqltr gslatilmft dvmyaavlyg tpaaarrlpv atllvtvast
      121 igflawfrkp ealliglvig lvtfipaltg vsvrshrtaa daarlaaaqt arlaemdrtq
      181 aviaerarma relhdmvanh lsavaihsta alsiddpets rnalkviren sveglaemrr
      241 ligllregge drapaaaptl aaldtlieqt nvngvsgglv ctledtrdpa agalptpvel
      301 aayrivqesl tnalkhaapg pvvvrlgrtg elltvevtsv fgsrpgptap gsgaglvgmr
      361 ervallggti taraepdgge tkiwrvrael pvtertire
//
LOCUS       WP_457658308             485 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            griseus].
ACCESSION   WP_457658308
VERSION     WP_457658308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..485
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50919
     Region          <74..484
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 miryirraaa lcllllvall vnaarvqlfe adelddnpan rrnsiarydq prgnilvgdr
       61 pvtgnketre qlsfertylh gplyapvtgy asqtygttli enaedavlsg tdsllaplpf
      121 wneltrgrqp ggdvvttika smqeaaydgl rgrrgavaal dpstgailal vstpsydper
      181 lsgtgaavtd awtrlnaaks lpmlnrairq typpgstfki vtaaaaldsr avtdadaatd
      241 tpspyvlpgt sttlpnessg cenasladai rvscntvmah lgvqvgldgm vdaaerfgfn
      301 daglripsgv arsnfdtdms edqlaqssig qfntratplq mamvasavan ggdlrrphlv
      361 drvttndgdt vrqegsrpye ramnpstavq lqrmmvdvve sgtganaaid gvkvggktgt
      421 aqhgvdnsgl pyawfiswaq apdsgrpava vavvvedasa dradisgggs aapiaravme
      481 aalee
//
LOCUS       WP_457658312             395 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathionylspermidine synthase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658312
VERSION     WP_457658312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Sui,L., Warren,J.C., Russell,J.P. and Stourman,N.V.
  TITLE     Comparison of the functions of glutathionylspermidine
            synthetase/amidase from E. coli and its predicted homologues YgiC
            and YjfC
  JOURNAL   Int J Biochem Mol Biol 3 (3), 302-312 (2012)
   PUBMED   23097746
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Pai,C.H., Chiang,B.Y., Ko,T.P., Chou,C.C., Chong,C.M., Yen,F.J.,
            Chen,S., Coward,J.K., Wang,A.H. and Lin,C.H.
  TITLE     Dual binding sites for translocation catalysis by Escherichia coli
            glutathionylspermidine synthetase
  JOURNAL   EMBO J 25 (24), 5970-5982 (2006)
   PUBMED   17124497
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Bollinger,J.M. Jr., Kwon,D.S., Huisman,G.W., Kolter,R. and
            Walsh,C.T.
  TITLE     Glutathionylspermidine metabolism in Escherichia coli.
            Purification, cloning, overproduction, and characterization of a
            bifunctional glutathionylspermidine synthetase/amidase
  JOURNAL   J Biol Chem 270 (23), 14031-14041 (1995)
   PUBMED   7775463
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..395
                     /product="glutathionylspermidine synthase family protein"
                     /EC_number="6.3.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44023
     Region          1..395
                     /region_name="Gsp"
                     /note="Glutathionylspermidine synthase, CHAP domain [Amino
                     acid transport and metabolism]; COG0754"
                     /db_xref="CDD:440517"
ORIGIN      
        1 merrtteprp gwqetvesqg vvypltrypd dslrpywdes ayyvfslpev ealeevveel
       61 htmclaaaah iveqdrfadl gitdprlaal vaeswrrrae lpsvygrfdl rydgsgpakm
      121 leynadtpts lveaasaqwf wmedrfpgad qwnslherlv aawkrqapll ppgplhfvqs
      181 dgdeigedlm tvaylretaq qagidteals veeigwdrls grfvddrlrf irscfklypw
      241 ewlatdrfgp qvldtldngg gsgttcwiep awkmllsnka llailwelyp dhpnllpahl
      301 dgprelagpg gagyvskpll gregagvdih apgsppvlrd epccyqelap lpdidgnrvv
      361 lgawivedea aglgiresag pvtdeyarfl phvil
//
LOCUS       WP_457658316             391 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Streptomyces griseus].
ACCESSION   WP_457658316
VERSION     WP_457658316.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 391)
  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 391)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..391
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - obsolete lipid glycosylation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=40231
     Region          23..391
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mntasrpasa frlivtgggt gghtypalta irtlqarlaa sgrtldvlwi gtaeglearv
       61 tsaegipftt vatgkvrrha nplkmvspan vrdmarvplg vaqarsavsa frpdvvlatg
      121 gyvavpagla armcrvplvl heqtvrlgla nrklagsatr iavssestlp llpesvrsaa
      181 vvtgnpvrpe vltghpdkav talglhsfdr rlptvyvtgg aqgsqqindv vggelpwlle
      241 ranvvhqcgp ahqealsara aglpaplaar yhltpfvgpe lpdvlaladl visrsgagtl
      301 aeltalgkpa vfiplataag neqahnarhl eesgaavall geisggrlre avgpllddpe
      361 rrgamaaaar ahgrpdaaer lvdvilsaas r
//
LOCUS       WP_457658325             196 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457658325
VERSION     WP_457658325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..196
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21187
     Region          16..189
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 msaltvdpvp gpgqdwddlv riweetdape gckveiieei vtvspppskd hnttaellqr
       61 rlytvvpedw giyqtlglsl pgrggiyipd lvvvdrasat gpgntvpaee arlvveitsr
      121 ananhdrvsk vngyakagve lfllldpwhs grptatlyge pdggtyrvle tveygrkltl
      181 pepfglvldt gvfpis
//
LOCUS       WP_457658326             479 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Streptomyces griseus].
ACCESSION   WP_457658326
VERSION     WP_457658326.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 479)
  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 479)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..479
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49789
     Region          230..477
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mvfalvglvv lallgavhry lwrrfvgdtt apgsplrrag tvaafvlpll svgamtsgrv
       61 gapfwlqqvl awpgflwlac llyltlallv gevvrpvllr vlagrdrkad taesgapsat
      121 psgassapps gtlvevpeet rprteelvps rsagtsdaav rtatepqaep eteattgpea
      181 epstgpdtep aptpaaeapp apapnpsrrl fvsrvvggaa aaaglatvgy gtygvlrgps
      241 vrritvplak lpraahgfri avvsdihigp ilgrahtrri vdtinrtspd lvavvgdlvd
      301 gsvadlgsaa eplaalrarh gsffvtgnhe yfsgaeqwvd hvrelglhpl enarveiegf
      361 dlagvndvag etegqgpdfv kalgdrdrgr aavllahqpv vihdavehgv dlqlsghthg
      421 gqlwpgnlla elanptvagl erygdtqlfv srgagawgpp vrvgapsdit vvelasrqa
//
LOCUS       WP_457658336             466 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658336
VERSION     WP_457658336.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..466
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50327
     Region          31..410
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mstvstvvgg isfwyaqegt papreplpgd tsvdvcivgg gytglwtayy lkkavpflni
       61 tvleakfcgy gasgrnggwl yngiagrdry aklhgheaav rlqkamnetv gevvraaaee
      121 kidadihqgg vlevahtpaq larlkdlhsv eiafgetdrv lrgaretaer vhvtgavgss
      181 wtphgarlhp aklvkglada vealgvtihe stpvteikpk havtpygtvr apyvlrcteg
      241 ftaslkgqkr twlpmnssmi vteplpariw dtigwegret lgdmahayfy aqrtaddria
      301 lggrgypyrf gsatdndgrt rpatvaalrd llvrlfptaa gahidhawsg vlgvprdwca
      361 tvtldrstgl gwaggyvgsg vatanlaart lrdliqqdsg qagptdltal pwvdhkvrrw
      421 epepfrwlgv hgmyaayraa drrettsprp gtdriaqiad riagrh
//
LOCUS       WP_457658337             304 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658337
VERSION     WP_457658337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..304
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32724
     Region          2..304
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 midipeelae tqsrfngvag rafvaglpdl aarllerwgl rldgpsmygm calvlpvvre
       61 sdgrpaalkl qavdeetage pvalrawsaa gagavelldh dpesgallle rlderrplsg
      121 etdvreavkv lgsvlarlvv vpapeglrtl ggvaermlae apervgllad aadrrlladc
      181 aaavrevage pgdrllhwdl hydnvlagra eagragewia ldpkplagdp gfelfpaldn
      241 lfdadevmwr fdaltealgl erdreraraw tlgrvlqngl wgaeegkvrl apdhaeiarr
      301 llgr
//
LOCUS       WP_457658340             198 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658340
VERSION     WP_457658340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..198
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20862
     Region          <2..198
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          8..34
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(9..10,13..15,17..18,22,25,34,36,38,42..43,46..48,
                     50..51,55,58,67,69,71,74,79..81,83..84,88,91,100)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          36..67
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          69..100
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          102..134
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          136..172
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnaldhdllt aartgdpdrv rtaieggarv dvrdeelrtp lllavhgdhv eaarllvaag
       61 adpnaqdlre dspwlatgvt gsvamlhvll pagpdltlrn rfggtslipa serghvayvr
      121 evlrvtdidv dhvnrlgwta lleavilgeg glahqqvvel llaagatrdl pdgdgvtpla
      181 haerrgfael aallrtta
//
LOCUS       WP_457658342             469 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457658342
VERSION     WP_457658342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..469
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50209
     Region          53..460
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(167,169..170,301..305,320,323..324,327,342,346,398)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mnrprparrr tatasvllal allgggcsgg vegtpgavgl rdpyfpglgn ggydvthygl
       61 eldvdpaagr lrgtatitar atqdlsafhl dllgldvesa tvegrraavn ragkeltlrp
      121 apgaesrlrk grtftavvry sgspltvtdp dgskegwlpt adgavalgep tgsmawfpgn
      181 hhpsdkaayd igitvpegla aisngelvsr rtangrtayr wrtaepmasc latvavgrfa
      241 teesvtpdgi rlftavdpes aaasedvlar mpavlkwaag kfgpypfssa gaivertgds
      301 syaletqnrp vypgppdtal lvhelahqwf gnsvtpktwr dmwlnegfat yaewlwaadh
      361 eevpveesfr eayeddanwa fppadpptaa elseppvygr gamavhrirl avdddaaffa
      421 lvrgwtqkyr hgnaatddft ayveeetgrd lgrlwdawly ggsrppleg
//
LOCUS       WP_457658343             168 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces griseus].
ACCESSION   WP_457658343
VERSION     WP_457658343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..168
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18086
     Region          16..168
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; pfam01613"
                     /db_xref="CDD:460266"
ORIGIN      
        1 msndefraal arlaagvvli taqepplded grgedvgmta tafmsvslep plvmvslrng
       61 srmddlldeq plwavsvlaa sqrhiagrfa mkgrisdrll fedvpyvrge vthapligga
      121 latlecrteq rvvagdhtlv igrvltanlp saegepltyf kgryrqlg
//
LOCUS       WP_457658344             308 aa            linear   BCT 27-JAN-2026
DEFINITION  1-phosphofructokinase family hexose kinase [Streptomyces griseus].
ACCESSION   WP_457658344
VERSION     WP_457658344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..308
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31426
     Region          2..300
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltvtlnta ldvtytvdal vphgshrvge vierpggkgl nvarvlgalg hdsvvtgfag
       61 gatgtvlrdl laplpprdal vevagntrrt laitdrstgd ttqlnepgpq vspaewaafl
      121 rtyedllaga davalcgslp pgihvgayae lvriaraaav pvlldtsgep lrrgiaarpd
      181 lvkpnaeela rltgsreplr aagdarrrga havvaslgpe gvlaltpdgv wraappapvr
      241 gnptgagdsa vagllsalae gldwprrlar avalstatvl aptagefdaa ayaellprvt
      301 vephvpap
//
LOCUS       WP_457658348             201 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658348
VERSION     WP_457658348.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..201
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21708
     Region          43..182
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mtgaatvrag adgghedagy vlrtataddl ggaravmldt vyrdlrsgyv prwhadiidp
       61 eaaylrperc tllvvehrge ivatgavrdr gpqappnpqw vadrfpsgst aqlcriyvrp
      121 ehrrhglarr lvrelgefav raggytalyl htdpavpgae pfwrslarev cdertlpggg
      181 qgivhfelpm pvpgspgnpt q
//
LOCUS       WP_457658350             425 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658350
VERSION     WP_457658350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  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 425)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..425
                     /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=45014
     Region          181..420
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mehrsgspev aegsgisgis gsdpdarwla llmhaaffll lgaslarflm rhpgeartpw
       61 iialsitlav lyllgpvlgs rptprrltwl gvlvlvwmvl vvlapsfawc avplfytglr
      121 ilppraalal valltafvva aqlrlatgfd pnlvlappav aavatavfvh mqrqavrqre
      181 laarqrelid dllrtrrela aterregtla erqrlsmeih dtlaqglssq qmllqaadrt
      241 wtadpdaarr hvrtatgiae rnlaearrfv hdlapadlae gggleaalha laaresaqaa
      301 galtvhchve gtphaplpdr vqsallriaq galanvrehs gasaagltlt hlgdrvvldv
      361 gdngrgftve pggprptagv rghglpaira rvhqlggtlt iesapgegtv lsaevplptt
      421 peepa
//
LOCUS       WP_457658352             251 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658352
VERSION     WP_457658352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26360
     Region          12..248
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mvltplpdsr tepdgsavir vlsynvrslh ddtaalarvi sacapdlvlv qeaprffrwr
       61 kaaarlakss glvvlsggat aagplllcsl rasvertedv llpltpglhr rgfatavvri
      121 agarlgvlsc hlslqrderl aqadlllerl aamgvehava ggdlndvptg kafrrlagtl
      181 qdcravapws geltfppdap rkridavfat pgievlgcgv psglpgvsed dlraatdhlp
      241 vlaalrvpvt r
//
LOCUS       WP_457658354             332 aa            linear   BCT 27-JAN-2026
DEFINITION  2-hydroxyacid dehydrogenase [Streptomyces griseus].
ACCESSION   WP_457658354
VERSION     WP_457658354.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10187446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.28"
                     /GO_function="GO:0008720 - D-lactate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0070404 - NADH binding [Evidence IEA]"
                     /calculated_mol_wt=36163
     Region          1..327
                     /region_name="LDH_like_2"
                     /note="D-Lactate and related Dehydrogenases, NAD-binding
                     and catalytic domains; cd12183"
                     /db_xref="CDD:240659"
     Site            order(75..77,99,233,294,297)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240659"
     Site            order(99,104,150,152..155,172..174,203..206,210,213,
                     231..233,257..258,294,296..297)
                     /site_type="other"
                     /note="putative NAD binding site [chemical binding]"
                     /db_xref="CDD:240659"
ORIGIN      
        1 meilafgvqs dekpliekaf eglhevrcld vflnrdtapi aagheiists vnadlgslvl
       61 qtlaaggtqm iaqrstgfnn idlevaerla lrvarvsyys pysvaefawt lamavnrrii
      121 raasrtrdfd frldgllgrd mrgrtvgvlg tgkigeaftr iahgfgmkll gwdvarnpac
      181 velgmeyvdk drlfaeadli slhvpllpst qhiideaalk amkddailvn ssrgglidta
      241 alvtelragr flgvgldvye aeaglffldk slegidddtl arlvtfpnvv vtshqayyte
      301 davgqivdat vqnvtdylar rhsenvlvpr tp
//
LOCUS       WP_457658356             264 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Streptomyces griseus].
ACCESSION   WP_457658356
VERSION     WP_457658356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..264
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27463
     Region          1..255
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msddvfslgp aafgsrlimg tggapslevl ersliasgte lttvamrrld ptvqgsvlsv
       61 lerlsiqvlp ntagcftage avltarlare algtdwvkle viadertllp dtvelldaae
      121 tlvddgfvvl pytnddpvla rkledvgcaa implgspigs glgirnphnf eliveragvp
      181 vildagagta sdaaqamelg caavmlasav traqepelma gamrhaveag rlarragrip
      241 rrhfaeassp lagraafdpe rpaf
//
LOCUS       WP_457658358             504 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457658358
VERSION     WP_457658358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..504
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52458
     Region          24..496
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag tgamaaaarl avagnrvtvy ersasyggsv grfehegfvf dtgpgllhlp
       61 avqrdlfvkt gkesleqcvt liqvdpasrh lfadgtavsl pnasragvaa aldgalgaga
      121 garwsafmdr ardtwdrsrr plleeplrad hqvlgrdpyp avrqrrllrg arqagtvaei
      181 gaweladdrl aalldgyals hgldprsapa saallpymeq tfgswyvrgg mrelaravye
      241 rcvarrvefv fgaevvrvve kdgraagvel aggevaeadq vvlgvrprpd lvpgqqavga
      301 gdvpvragsg agaagrftvl lsvrgaread avhrtvvhsa qgaaeqeavf ggrvaghptv
      361 tvlrpddpat rpdaeheavt ltatvapqgp vdwrdaavrq rfadvlvera aaavpglrer
      421 ilhteirtpa eteaetgaeg gavpppalag aggsylhpgn ptrlpglyra ggwshpgggl
      481 ahagmsgtlv aglvvegddf rgsr
//
LOCUS       WP_457658361             805 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Streptomyces griseus].
ACCESSION   WP_457658361
VERSION     WP_457658361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..805
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83818
     Region          13..406
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          376..552
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          673..744
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 msgrarlalc ayaatllaag sliplvegig wlvqaamllg vqsgvgalar rvplartlti
       61 alqtlvtlvl ltlvfardha lfgllpgpga vmrlgellva ggedvgtyst papltdgikl
      121 mviggvvlig lvvdalavtf rsaapaglpl lalysvaagl sdggaswlwf llaasgylll
      181 llaegrdrls qwgrvfggaa rnagglsdgl agvgggtspv rtgrrigvla lgialvapla
      241 lpaldsgllg gsgpgngkgs gggtisavnp lvslqnnlnq pdnrevmtyr sniedpqsly
      301 lrilaldefn gsewrsstrr ltdvperlpq ptglsgdvsv tevrtnisas rsyqqtylpl
      361 pypasevrvg grwryepegr tlvgddgqtt rgaqyevgsl vveptadqla aagtppeelv
      421 reytrvpgsl pgvvadtaee vtegaanaye qavklqdwfa sdggftydtt vtsgtgssai
      481 arflrdkegf cvhfsfsmaa martlgipar vavgftpgtm kangatsvgl rdahawpely
      541 fegvgwtrfe ptpsrgsaps ytrpevptds asdvaepsad tsdapsaaps addscppqlr
      601 qeggcgpsqd agaalptdrg tpagtvllvi laavlavvlp lspllwrtrt rnrrlgsggr
      661 tpadaaartl aawreitdta wdhgigpdes ltprkaaari vrlgrldtga aeavhriags
      721 veqvlyapep rpaaglaeda pavraglras agrgarlrat llprssvrvv wavaerrtal
      781 aerwanrpga grwtarlrrl srqhg
//
LOCUS       WP_457658362             349 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces griseus].
ACCESSION   WP_457658362
VERSION     WP_457658362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..349
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37856
     Region          16..307
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mttyddrasl tdltttaerv rrsvesvieg kpevvrlslt vllaeghlli edvpgvgktm
       61 lakalarsid csvrriqftp dllpsditgv sifdqqrrdf efkpgaifaq ivigdeinra
      121 spktqsalle smeerqvtid ghsyelpdpf mvvatqnpve megtyplpea qrdrfmarvs
      181 igypspeael qmldvhggls plddlqpvah ahdivklida vrtvhvadav rryavelvaa
      241 trshpdlrlg aspratlhll raakasaals grdyalpddv qalatpvlah rllptaqaql
      301 nrrtaeqvvl giiqrtpvpt saggtappap agqepgrply nqqhgarrl
//
LOCUS       WP_457658366             565 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457658366
VERSION     WP_457658366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..565
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=60910
     Region          7..275
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(7,42..43,72,77,82..85,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,46,48,80,96..99,103,105,142,144,
                     146..147,149,162..163,166,183..186)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,46,48,80,96..99,103,144,146..147,
                     149,162..163)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(18,103,105,142,144,146,166,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(162..170,179..186)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mrpvgskyll eeplgrgatg tvwrarqret agaeaavagq pgetvaikvl keelandadv
       61 vmrflrersv llrlthpniv rtrdlvvegd llalvmdlid gpdlhrylre ngpltpvaaa
      121 lltaqiadal aashadgvvh rdlkpanvll derdggmtpm ltdfgiarla dspgltrthe
      181 fvgtpayvap esaegrpqts avdiygagil lyelvtgrpp faggtalevl hrhlseeprr
      241 pstvpaplwt vierclskdp errpsaenla rglrtvaagi gvhansaqia aadgvgalla
      301 pdpaptavpe tpgaadptqv lpsnagsydp aaatsvlpqt gpggqggpgg hadptavlpp
      361 vpqrpdgppq pdgphpwqsq lqaardrneq tqvqyldpsq dplrrrpqrq qpqqqyqqpq
      421 qpqrrqpppq hqqyppqrqq ppqrqqpqqh qpqryqqpqq pqrqqyappq pqqpqqpaar
      481 ppreprpprq rganpmripg lgclkgclft vvlliiagwl iweltplqdw vaqgkgywea
      541 igdaigkvtd wfsqlgdsag gsgga
//
LOCUS       WP_457658368             743 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces griseus].
ACCESSION   WP_457658368
VERSION     WP_457658368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..743
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=82631
     Region          1..213
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          355..710
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mprftvivpa frvqaylhac ldsvlsqsfk dyeiivvddc spdacgpiad eyarrdprvt
       61 alhlprnigl gparnagmar aggdylvfld gddtllpdal rtiadridat gepdvlmydy
      121 artywtgrsv rnvlaahlde ggparfrltd rpellqllmv vwnkayrrtf veaegfafpp
      181 gyyedtpwty pvlmaadsia vldavcvsyr qrrrgnilst ssekhfdvfd qydrvfafid
      241 srpelalwrp vmfrrmldhf salfasrdrl pphsrtaffr ratascrryh tpgapvprra
      301 llrhglmhlg arrtyralsv aqrlggrlrr aaeavrravr gaalrahyrt qlllplrprd
      361 avftarggrg yggspaaiea kvrelvpgar tywicravda htvptgsrhl apgtfahgta
      421 larstylvnd ssfdrglvkr rgqvlvqthe gtplrsvgtd lldrpaaarg tdfeqllrsv
      481 dtwdfslsan phstlvrera ypsayttley gsprndvyqr tgpaevarlr etlgipagst
      541 allyapthrd yrrvqrpald lerlvrilgp qfvilarapr ppgpggvrra phpriidvsa
      601 hrsvetlala sdalitdyas lmfdyvnldr pvvlhlddie ayeaargtyf ditafppgiv
      661 arsqdelfdi fatdhwrgsr saqlraafrd rfcpyddgya aervvrrvfl getdglplpv
      721 ppaarrtpaa lpaqdgagaa vgg
//
LOCUS       WP_457658372             394 aa            linear   BCT 27-JAN-2026
DEFINITION  CDP-glycerol glycerophosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658372
VERSION     WP_457658372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12052972
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..394
                     /product="CDP-glycerol glycerophosphotransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43687
     Region          30..390
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mpprasaasv krfvrrqamr avyradlhrp ldpglavyga ywnrgvacnp aaihakarel
       61 aphirgvwav ssrhrdrmpa gvpyviegsr pywraiatas ylvnnssfpg gftkrpgqry
      121 lqthhgtplk tmgldqrgyp alarktdfdk ilahvrqwdf slsanphste vwdrvypgay
      181 eridlgyprn dvyftatadd iakiraglgi aegqtallya pthrdyrtgf apdldperla
      241 rqlgpdhvvl vrahyfygrs agigdsvptg rvidvtahpr veelclaada liadyssltf
      301 dyacldrpiv vhapdwsayr aargtyfdll sgrpgdtpgp vtttpgqlae vfrtgewrsp
      361 asaalrtafr erfcpyddgh aaervvrrff apal
//
LOCUS       WP_457658373            1241 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces griseus].
ACCESSION   WP_457658373
VERSION     WP_457658373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1241
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1241
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=132719
     Region          3..220
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          859..1236
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mkspllsvvv pvhnveayla dclrsvaeqt laaievvmvd dgstdgsari aaefaardsr
       61 frlvrqqnag lsaarntgvr httptvpyla fadsddivvh dayermtasl estgsdlvtg
      121 nvwrltgqgr qqawqyrwlt gprsrthitr dprlladrva wnkvfrrsfw dahgfafpeg
      181 rlyedtpvmi pahylagavd vlaehvyywr vregsitrrr tdvtgvrdri aaceqvsafl
      241 ggrdaeqrra ydasclrddf gyfldglpmg geayraafle gagafvdrag pkaleglpve
      301 lrikwqlvre rrlaellevl aferangagt faveglpgrr raaypgvhga sarlagpdip
      361 avarlsearw gadgklrlrg yaylrnlpaa sarqrltvgm vraergrqvr pvpvrsvpap
      421 eatvnsgqel hdydhagfem tldpdrlpat agggwlvglv lagpgtvrrv avrapdagad
      481 qplthdlgdg rravldfrag rlrltvsrlr alaeghrtve aagsalditg rhiggsrpta
      541 lvltrdggee rsyeveyaeg gargengegg egredgargg sfrvrvplae laaappaphr
      601 apreveaang pesgarwrvr llladgsrvp lpaapdlppp ayadpagdlv ldlaglpyad
      661 evectpeggv rirgayagta aappsayggr lvlrhetlhe tvpvagavvd asgaeaerpa
      721 gaeaeaasgp rtdaatraga gaenyaasgt eagagnhtas gteadaavaa adgsaprpla
      781 ttapgrfsal vvpplpegrw elrldgrpvr vlgsvaarlp raggvegalr lerrhgdrls
      841 vvagpespav gigrsaygrr ilraahhgdr rttlplrdtv lyaggdspha vhaelvrrgt
      901 eaehlwvtgt tpgrtthvpp garavpvhsp awyealarsr rivtdeqlpg wferrpgqtv
      961 vqtwhgtplg rfgggladtl yadhqylatl pqrsaqwsvl vspsrfatpw lrrslayege
     1021 vleagspand vlfppvrdka aeevrrglgi pedhrvvlya ptyrdqlahp paasadrtap
     1081 gpyrwdpald phalaralgp ghtvlvrrhp rvtgdvpagp gvldvsghpg aaglllvadv
     1141 lvtdyaglmf dfaltgrpml fhtydlehyr dtvrgfcldf etrapgpllv ttdevaqalr
     1201 dtgslaarha dayesfrrdy cdlddggaaa rvadrlladg p
//
LOCUS       WP_457658375             263 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658375
VERSION     WP_457658375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..263
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27918
     Region          16..263
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 madtdnvsgd rrvptvvvdd vhitytvnga rtgrgsatsa lsrlttrrat pgarkvhavk
       61 gvsfaaykge aigligsngs gkstllkava gllpptrgrv htqgqpsllg vnaalmgdlt
      121 gernvvlggl amgmtreqir erydaivdfs ginekgdfit lpmrtyssgm garlrfsvaa
      181 akshdvllid ealstgdakf qrrskdrike lraeagtvfl vshsnksitd tcdralwlea
      241 gtlrmdgpak dvvaayeaft nrk
//
LOCUS       WP_457658376            1660 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-glutamate dehydrogenase [Streptomyces griseus].
ACCESSION   WP_457658376
VERSION     WP_457658376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1660)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1660
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1660
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=182982
     Region          48..1656
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mqtkldeaka ellagaakva edgpgggvgg pggaprarva aagadasdrp gqdtvlaylq
       61 ryylhtaped lsgrdpvdvf gaaashyrla enrpqgtanv rvhtptveen gwtcshsvve
      121 vvtddmpflv dsvtnelsrq grgihlvihp qvtvrrdvtg klievlsggp gtpkpgekae
      181 lphdalvesw ihvetdresd radlqqitad llrvlsdvre tvedwgkmrd aalriaddlp
      241 geplddlpde eveearellr wlaadhftfl gyreyelkds dalaavpgtg lgilrsdpqh
      301 sedeahpvsp sfdrlpadar akarehkllv ltkansratv hrpsyldyvg vkkfdakgnv
      361 vgerrflglf ssaaytesvr rvpvirrkva evvegagfsy nshdgrdllq iletyprdel
      421 fqtpvdqlrs vatsvlylqe rrrlrlylrq deygryysai vylprdrytt gvrlrlidil
      481 keelggnsvd ftawntesil srlhfvirvp agtelphltd adadriearl veaarswadg
      541 fqealnaelg eergaelqrq yghsfpegyk adhspraava dlvhletlkq gekdfalsly
      601 epvgagpger rfkiyrtgeq vslsavlpal qqlgvevvde rpyelrcadr thawiydfgl
      661 rmplangngg yladdarlrf qeafaavwkg eaendgfnal vlgaglnwrq amvlrayaky
      721 lrqagstfsq dymestlrnn vhttrllvsl fearmspgrq sagteltdgl leeldgaldq
      781 vasldedril rsfltvikat lrtnffqktd dgtphsyvsm kfdpqaipdl paprpafeiw
      841 vysprvegvh lrfgkvargg lrwsdrredf rtevlglvka qmvkntvivp vgakggfvak
      901 qlpdpsvdrd awfaegiaay rtfisalldi tdnmvagevv ppvdvvrhde ddtylvvaad
      961 kgtasfsdia nevavaygfw lgdafasggs agydhkgmgi targawesvk rhfrelghdt
     1021 qtedftvvgv gdmsgdvfgn gmllsehirl vaafdhrhif idpnpdaats yaerrrlfdl
     1081 prsswadydt gllsagggvh prsaksipln ahirealgid asvskmtpad lmqtilkapv
     1141 dlvwnggigt yikavsesna dvgdkandai rvngedlrak vvgeggnlga tqlgriefar
     1201 nggrintdai dnsagvdtsd hevnikilln glvrdgdmtv kqrnklladm tdevgalvlr
     1261 nnyaqnvals nasaqapsll haqqrflrrl erdgaldral eflpadrhir ellsnekgls
     1321 qpelavliay tkittadeli stvlpddphl qklvhayfps elrerfpeav dghalrreii
     1381 ttvlvndtvn tagstflhrl reetgasiee ivraqytare ifglssvwda vealdnqvaa
     1441 dvqtrirlhs rrlvergsrw llgnrpqpva iaetidlfrd gveqvwselp klvkgadldw
     1501 yhsildelta agvpdelavr vagfssafpa ldivaiadrt gkeplevaev yydladrlri
     1561 tqlmdriiel pradrwqsma rasiredlya ahaaltsdvl svgngastpe qrfvaweskn
     1621 aailarsrst leeiqgsdaf dlanlsvamr tmrtllrtha
//
LOCUS       WP_457658380             355 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658380
VERSION     WP_457658380.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..355
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36241
     Region          47..351
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtapptalrr rsaarkpqpe pnaartalrg ggllvlagll lllvvlstwi gtkdttlgqv
       61 wtalwnddga yatdvirqlr lprtlvglmt gaalgvagav mqavtrnpla dpgllgvnag
      121 asaavvfgig vvglagfgsl vwfsfvgaal ttvivyvlga sgragptpvr lalagaavsa
      181 slsgviaglt vfdsatydyl rfwmvgslag repelvvqll pfvavglvia lllarplnsl
      241 algeelgral gariartria aviavtllcg astaaagpig fvglvvplva rwltgpdlrw
      301 vlpysmllap vlllvsdiig rvalpgdele vgavtaviga pvfiamvcrr keasl
//
LOCUS       WP_457658381             383 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658381
VERSION     WP_457658381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..383
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39207
     Region          28..381
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtatdvrtap eksprasdaa cpvrwwsgrv sfrmhrrtal vsggalllaa llllvslcvg
       61 sypvpvpeva ralfygtgdr lavhfvnqer lpqallaila gcalgmsgai fqsvsrnala
      121 spdvigfnsg aatgailviv tfggaaasva agaivgglvt allvsvlasr gglhgirlvl
      181 iglgvtamlg svnsylltrs slndaqnahi wlvgtlngrg wssvqimava lvillpavll
      241 fgrrlrmmel gddlatglgv rvnrsrlalt vlgiglcgva vasagpipfi alaapqiavm
      301 vsrspgvslv sagavgaall saahlassqf fsalvwadrq igwiqvvees qrnnllpvgv
      361 ttavlggvyl gwvlfkrrgt gsa
//
LOCUS       WP_457658387             241 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces griseus].
ACCESSION   WP_457658387
VERSION     WP_457658387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..241
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26963
     Region          2..238
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mrritprmvr ltlggedlse fssngsdqhv alyfyepgve lprpftsdaa rallpvakpr
       61 lrrytirdhr pelrevdmdf vlhgpdqlas gwaervrpgd eviwfgpspa ypvapvtdwt
      121 lllgdetalp aigaileelp pghrvlaave vadraeeqpl ptradatvsw lhrhdrahge
      181 llrehavglq lpdgrgrvwg gaergvmrel rhhfvhvrgl dradthltay wtqgetqdse
      241 v
//
LOCUS       WP_457658389             572 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658389
VERSION     WP_457658389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 572)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 572)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 572)
  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 572)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..572
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60192
     Region          19..540
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mnapaeqprp yepttrdglr llagclrdrp glaalavlgg lvyqlalial pwfieravdq
       61 givhedrsal whwaliivga gilaalaemv lgwystllat tqgnrlyial adrvsrldar
      121 avarygegdl gmrgtrdvdl vrgwlsgvas fltgvtgfvv mivaimrldp llalicllcv
      181 pplvwintyw fpkrfgaant alsaahgsra daveellsas aavrglggep alvrrhhers
      241 atvtehtltt grvsagwaal spfvpalaig aglglggvav lrgtmsvggi vaftswmsml
      301 vlwvgvitlr isqlsqatta arrlqdvllp hptdrapgte plpatgdlta egvghraggr
      361 pilspvdltv rpgelvavtg ptgsgkttll rtlagllppt tgtvrfggrp leeadpaevh
      421 arlgyvpqrp vtisgtladn lrlgsahtdd elraacrtaa lddyleaapd gldtlvgerg
      481 stlsggqlqr lalaravlrk ppvlllddit saidtttert llerlrawsg etaivcathr
      541 ggfldaadrt ltlaqaeaaa pddmeervtt gg
//
LOCUS       WP_457658390             466 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658390
VERSION     WP_457658390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  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 466)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..466
                     /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=48945
     Region          199..449
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtppgprsay adramsssss pagppppadg llsaarrnlr elahglshas hpstpllaea
       61 pklwqrllpy vvvlalaatf ipvtitvlts qydvpgalag algvagaapl lmlahrplqa
      121 wwiifpadiv galvllahps eqhdvwpwip pvlvaylfll laiglretrr tavsvwvatc
      181 laglvlhlva padrstgsal llpilgavvl viggavrerg eatrrlaeqe tiseaeraqr
      241 tlleertria relhdvvahh msvitvqads apyripglpe paqqefaaia aaareslgem
      301 rrllsvlrsd gtegdltpqp gldrlqqlve atvraglpve lslaadlgev psavdlsayr
      361 ivqealanvv rhapgsrtqv svraaaghln vlvvngpapk paeplestgt ghglvgmrer
      421 vrltggtldt gplpdggfrv aarmplppat apsarpssvp plpedl
//
LOCUS       WP_457658392             274 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658392
VERSION     WP_457658392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30342
     Region          18..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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 maniqtldpd asplayygae lrrhreaqgl tqpqlgsaif ctgslvgqve ttkkvptrdf
       61 servdaalgt dgvfsrlvgl vlrsqlptwf qpyadmeaka ayisayqaqv vygllqtedy
      121 aravlatgmp ddlegllaar merqrilera kpplawavld eavlyrpigg nevmraqlqk
      181 lldyaarrwm riqvlpfeag ehasldgsft gmrfdsdpdi iytedlisgh mtansetvre
      241 aslryahlqa talsveesva risrvmeery garp
//
LOCUS       WP_457658395             335 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein [Streptomyces griseus].
ACCESSION   WP_457658395
VERSION     WP_457658395.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..335
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35620
     Region          25..332
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
     Site            order(76,87,112,182,184,241,281,300)
                     /site_type="active"
                     /db_xref="CDD:185696"
     Site            order(182,300)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185696"
ORIGIN      
        1 mttssdtaty tedfgvladg spvrrwtler dgvrvrilty gaivqsvetp ardgsrapva
       61 lglpevagye efpnpyfgav vgryanrigg asfvldgrth rltaneggnh lhggtrgfdk
      121 rvwdavavpd gvrmslvsad geegypgrld fsvtytlgpg gelrlgyrav tdaptvlnpt
      181 shlywnlaga esgsalgqql riaagritpv daasvptgaf apvaggrfdf remravgsgy
      241 dqnfvldera egadgvaael ydaasgrvlt vrtsepglql ytadhfdgrp fgpcagiale
      301 tqhfpdspnr pefpstvlrp geefvsrtay afsvr
//
LOCUS       WP_457658402             207 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658402
VERSION     WP_457658402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18555887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.-.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22302
     Region          35..180
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
     Region          99..169
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtttpppdpt dspnspspsp siasasassd spgpvlirpc lptdldiler hmpspgrtrr
       61 hadrfdrqeq glstfltawi ddvpvgtaqi lwqgcaapev qarfpgcpel nglgiwppdl
      121 rsrgigtali raveqrvrea ghdliglgvd ddnhraaaly lrigyretgc ryldryayld
      181 adgvrqevad parflvrslg easagpk
//
LOCUS       WP_457658405             433 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457658405
VERSION     WP_457658405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 433)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..433
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47713
     Region          28..418
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(65,72,101..102,109,113,120,247..248,251,255..256,
                     259,297,302..303,306..307,309,332,359..361,364..365,
                     367..369,373)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(72,95,97,100,102..103,185..186,196,246..247,
                     250..251,255,303,306..308,408)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mndtpacphs atpesgpelf twefatdpyp ayawlrehrp vhrtalpsgv eawlvtrygd
       61 arqaladarl sknpanhaes phakgktgip gerkaelmth llnidppdht rlrrlvskaf
      121 tprrvaefap rvqeltdrli defiekgead lihdlafplp iyaicdllgv predqddfrd
      181 wagmmirhgg gprggvarsv kkmrgylael ihrkrenpgd dlisgliras dhgehltene
      241 aaamafillf agfettvnli gngtyallrh peqrdrleas ldagesalla tgleellrfd
      301 gpvematwry atealtlgge eiaagdpvlv vlaaadrdpe rfadpdtldl arsdnqhlgy
      361 ghgihyclga plarlegqta latllrrlpd lrlagepddl rwrgglimrg lrtlpvefep
      421 gsrseksdtl stl
//
LOCUS       WP_457658410             843 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658410
VERSION     WP_457658410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 843)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 843)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 843)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..843
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87292
     Region          2..843
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mfrtalrnvl ahkarllmtv lavmlgvafv sgtlvftdtl gnafrnqsak sydnvavsve
       61 tyagddeknp gideatleki rgldgvasat grvsgfagva dpdgkligng wsntganfap
      121 gkdgkdtqyv ftdgsgpakd gavaldkdta ekgkyrvgdp vrvatngpvk eytlagiftt
      181 edgavnaggs lvlfdtataq qlylkpgvfk datvtaagdv sdqklldeit pllpedataq
      241 tgkalaeqqa kdiesglngl ntmllafagi alfvgiflia ntftmlvaqr trelalmrai
      301 gatrrqvkrs vlleaafvgv lasvigfalg lglatglrsa mgvmggkipa gplvvsptav
      361 isafavgili tvlaawlpar raakiapvaa mssvhatasv kslvvrnsig gviallgsag
      421 ivggaasggt sgrqlvaaga ffaligviil ipllsrpvia lvrpllkkvf gvsgklasqn
      481 avrnprrtga tasalaiglt lvtgisvlgv tlgqaidkmt tdnikadymv tmasgdslde
      541 saltalskad gvsalspqqa awfevdgehh sasgvtpgdv ekvfslttes gslaslkdgq
      601 vavgsktaks ngwktgdtlp vkfddekkge ltigatyeen eflspfvipk qladqhsass
      661 rpeireiwik tdggasqane qsivdalgdn pamsvmdrqd irdmfggfin talnimygll
      721 amalliavlg vvntlamsvf erqqeigmlr aigldrgrvk rmirleavvi svfgavigvg
      781 lgvflgwaig rtlsgdipgy alvipwdrlg iflllaglvg vlaslwpars aaklnmltai
      841 kte
//
LOCUS       WP_457658411             321 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces griseus].
ACCESSION   WP_457658411
VERSION     WP_457658411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..321
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31967
     Region          13..298
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mhtpvasalp vgrgllylvv agvawgtaga aaslifrvsd lgplalsfwr caggllllag
       61 alalrprrap rkpeprrrrl lrilgtgigl tvfqsayfaa veatglavgt vvtlgagpvl
      121 iavgarlllg erlgggglaa vtgaltglvv lvlggeggdv vpagvllall saagyaaitl
      181 ltrwlgrdgd ggdalttsaw afgigavgll pmalaeglvp htaetgqvlw llvyvaavpt
      241 alayalyfag aaavrsatvs vimllepvsa aviavtvlre rlttatvlgt lmlltavagl
      301 alaeargaaa arrkeavgva v
//
LOCUS       WP_457658415             434 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658415
VERSION     WP_457658415.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44519
     Region          24..419
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,75,130..131,133..135,138,158,
                     161..162,165,252,255..256,259..261,264,288,292,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mqfpasspsp spsptpslwr dadfrrlwvg qtasqlgeht tlvvlplfav ltldagagrl
       61 gvlravgqap vlllsllaga wvdrwrartv mvltdagrav algaaavagl lgllglpalf
      121 vvafavgals vlfdvayqas lvrmvrrdql vrgnsalegs rsaaqiggpa lggalvslls
      181 apfaaasgal ffavsflslr rirrpesvpp vcgerpedrp cpepaprirh riheglrfva
      241 gnpwlravcl asaafqfsla atmtvyllfl pralhlpgat vglalaatgp gallgsvlaa
      301 rlpgrfglga vlvsaavlgn gallcvpalh gsstatvlal lavnvvfgaf sqlvnvtvms
      361 vrqavtpdgm qgraaatitf vgmgltplgs llggflaqew glragllmaa agmmlspavm
      421 aasplvrlgr rltp
//
LOCUS       WP_457658416             273 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces griseus].
ACCESSION   WP_457658416
VERSION     WP_457658416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..273
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28342
     Region          1..270
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mririvdaft drpfsgnpag vlllesgafp aaerlqeiaa evnlsetafa hplppggtad
       61 walrwftpaa evdmcghatl atahvlhttg latgpvrfaa rcgiltatah pdgsltldfp
      121 tsplaeepvp ygladalgad pvsvhatgeh igdllvelrd eatvralapd faalvahsrr
      181 gviataeaed ptrgydyvsr gffpgvgide dpvtgsahta lapfwsarlg rddlaglqas
      241 arsglvrtal rgertlltgs avtvidgell tal
//
LOCUS       WP_457658419             518 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces griseus].
ACCESSION   WP_457658419
VERSION     WP_457658419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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 11434433
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..518
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=55180
     Region          <422..518
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          422..449
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          452..480
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 maedreapdg tvvgvgnsvs gggfhapvvq tgtfsggvht yygppahssl ppvpewpqlg
       61 taepialgvr rtrrlpgesp lppyverdcd ralgsrvrea vrsgglvvvt gaplsgktrt
      121 awaalfsnls gttrifapsp gadlrglpal lrergeqvcv lwlddleghl gehglttavl
      181 aelvrlrvpv latmddgayd arrfgtadra rvlsgaepve lqrewsesel grlaasdqep
      241 rlraaaarhg vhtvpeylav gpelleewrr arrpdahprg hllvraaidl grcgvsrvsa
      301 rpllkaqely pkeaaaaeae sfedalawat girhgvtgll slvpgvrpat wsvfgslvad
      361 vegrpdappv pigmwsfafa vasdkgerwa vrwraheelv pladtdpeip allghinavm
      421 gdvetamhwf rraadaghae saadigqlli grdpeasryl eqaaeagvvr aqyqlgmlla
      481 graqswltra aeaghttagq alpalrtvtd tppdnvka
//
LOCUS       WP_457658422            1049 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658422
VERSION     WP_457658422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1049
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=115325
     Region          250..1031
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          842..858
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          864..886
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          887..909
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          933..977
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          978..1000
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 msgtevavlr lattvivaaa kalltpkpga rlvpspvrpl prpakpdrla evlagrmags
       61 fadlpeherl aavasvqdtf aaagepdagr lfaldldpdr lsaelsapaa glseravdly
      121 edllgdccah lveqltahps faaraaveqv ratgrtrelv edvrarvgpr pdaadlefer
      181 ryaefmatan srmglfgltl grsasewple tayislsvsg yeaagppvlg gpvrtsvsgy
      241 egshahgpde pvrttariee algertrlll rgpagsgktt lvqwlalnaa rrtfgtelad
      301 wnrcvpfvlr lraftardal papadflraa gvplhgsapd gwadrlmleg ralvlvdgvd
      361 evpdrlrrrt erwlkdlita ypraryvvtt rpsavpeswl sgsgfephtl lamrrddiha
      421 fighwhraar secrsdeera eletyesalr ravgtrrdla rlatnplmca llcalnrdrr
      481 mqlprarkel ydaaldmllv rrdnerevsg vegvdltree qttllqrlay wlirndlvqa
      541 aqdeavslia dwlrsmsqvr gtpeqvfthl lnrsgllrep vpgavdfvhr tfqdylgaka
      601 avevrdfgvl vrhahedrwd dvvqmavgha rpderaallt sfleradaep ghehrlilla
      661 aaslghapel dpsvreavea rterllppds qesidqlaev gdlalellss mldglserea
      721 asvvrtaaav ggetayelvr qfrddersli tyevsmawer fdperyarev lagpgwedty
      781 vyvksdrhls alkhvprahs vnlsgdrhdl spvtsrtdvr rvfvwhnarl igvrqlaamp
      841 glrelglsnc prirtiepla rtglewlslv qlhpeldpap ladlpalryl alghpflmes
      901 vgelpacpqv trldllaesr yldlegledw tglrdltlyg gtqfrqlvrt palhglrdlg
      961 liripaldln ltapltglrv ltlaecalas glaplaelps lttlrlsgka ecydlaplaa
     1021 sehltvhlah dtpvtgaell pperivrlp
//
LOCUS       WP_457658431             368 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Streptomyces griseus].
ACCESSION   WP_457658431
VERSION     WP_457658431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..368
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37602
     Region          13..365
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 mthpffdlpp ltadrfaaie rsvarllate qdvvitqgea llplegcirs garpgstaln
       61 vvtgpygqtf gnwlrdcgaq vvdlavpfht avtagqvaea laahpeidfv slvhaeaatg
      121 ntnpvaeige vvrahgalfm ldavasvgae pllpdawgvd lcvigaqkam ggpagvsavs
      181 vsarawerma anpaaprrsy lslldwkerw idggrkalph apaqlemlgl eacvariedt
      241 gldtvmarha saaaatraga valggglepy vhatrdaapv attlrapagt daaalvahal
      301 aadpslplva gggalskemi rvnhygadat rdavlsslaa lgsaltdagl rvdidaaraa
      361 vsetwpgr
//
LOCUS       WP_457658435             483 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            griseus].
ACCESSION   WP_457658435
VERSION     WP_457658435.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..483
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50537
     Region          <74..483
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnktirrasv fcllmvlall vratwvqgye akaladdehn rrntiaryaq plgdiivags
       61 pvtgskgtsg gdlrykrtyt qgelyaavtg yssqaygatq legihgdvld gtddrlknpe
      121 dlitggqakp gnvlttidpg vqkaayealg ddkgaavaid pktgrilgmv stpsydpski
      181 sgttdgdawq kllddpdkpl vnralrqpla pgstfklvva aaalenglyg svdertdspd
      241 pytlpgtstv lrnenasapc enatlrtalr yscnnvfaka aadlgqdkvk emadafgfdt
      301 ekldvpvraa ksvyptgmde aqtaltgigq fevtatplqm amvsaalang gelaaphmvs
      361 qvtdgdgtvl eetedgetkr vveegtaeql rsamvtvvee gtgtnariag aevggktgta
      421 qngvdnsntp yawftsytkd dssgkevava vivedsgsar sevsgnglaa pvaqkmmkaa
      481 ler
//
LOCUS       WP_457658439             190 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457658439
VERSION     WP_457658439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..190
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          <1..187
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 glavggttak mglrtaplst lhldgcripa drvlgrvggg llvldhvmkr eilfgftvql
       61 gemrhrlert vgyarerraf ghpigdyqav shrvvdmkir tdtaakwlyd taerlaaged
      121 vtadlaitki laseaalsts lsavrvfgga gylaevglek evraavagtl ysgtndiqyn
      181 hvasalglgg
//
LOCUS       WP_457658440             217 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457658440
VERSION     WP_457658440.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23122
     Region          5..182
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mnaspraltl tkkthscvri ekegrvlvid pggfseddaa lgadavlvth ehpdhfnear
       61 lragleanpa aeiwtlrsva eqlsaafpgr vhtvgdgdaf taagfdvtvh gelhavihpd
      121 ipritnvgfl vdgsvfhpgd altvperpvd tlllpvmapw skisevidyv reveprraid
      181 vhdalltdla rpiydhqiga lggadhgrla pggttel
//
LOCUS       WP_457658450             214 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658450
VERSION     WP_457658450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22839
     Region          1..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 medgtplrer lvdigvemva tegiaalglr eiarragvsh gaprryfpth rsllsaiagr
       61 gfdalkdrld talrpdgdpr tqlcllvegy vgfavehrpm felmfrhdll dggdeadgrp
      121 rlrektlplf gslvalvarh lqdsarlssa gpgpapdvva aalwanvhgi aqlwswgsls
      181 ltlgapspgd ardreslapl iartvdahlg paqp
//
LOCUS       WP_457658453             507 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces griseus].
ACCESSION   WP_457658453
VERSION     WP_457658453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 507)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..507
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51551
     Region          71..486
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msagtlpapg aqgvraglla ggadgpgrlr glttivldtl ddaprarggp lpaggpgava
       61 lstralcspv lpeegvgpea aladvvrava egaadpadpa cvahlhcppl avavaaelag
      121 aalnpsmdsw dqapaagvie elttaalarl vhpaapapda litsggtesn lvalllarer
      181 atpgplrvvt ganahhsvhr aawmlglpap tvvacrdgvi dpdaldralt glagapllvv
      241 atagttdegr idplpeiari aerhtarlhv daayggpllf serlaplltg leradsvtfd
      301 lhklgwqpva agvlavadag mltplslrad ylnadddtea glpdllgrsi rttrrpdavk
      361 mavtfralgr rglgalvehc vrtahefgea vdarpalrrr pggigistvl frpavadtlp
      421 eeagdavvaa vrrillaegr avlgravaed sdgrrrlwlk atllhpnaat adllplldlv
      481 taaadravse aqaaegtqap gaerlsp
//
LOCUS       WP_457658454             465 aa            linear   BCT 27-JAN-2026
DEFINITION  lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family protein
            [Streptomyces griseus].
ACCESSION   WP_457658454
VERSION     WP_457658454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Visca,P., Ciervo,A. and Orsi,N.
  TITLE     Cloning and nucleotide sequence of the pvdA gene encoding the
            pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in
            Pseudomonas aeruginosa
  JOURNAL   J Bacteriol 176 (4), 1128-1140 (1994)
   PUBMED   8106324
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790239
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..465
                     /product="lysine N(6)-hydroxylase/L-ornithine
                     N(5)-oxygenase family protein"
                     /EC_number="1.14.13.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50847
     Region          1..453
                     /region_name="IucD"
                     /note="Lysine/ornithine N-monooxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3486"
                     /db_xref="CDD:442709"
ORIGIN      
        1 mtpgprtppl dllgvgagpf nlslaaladg vpglrtvfhe qraafhwhpg lliegatlqv
       61 pfladlvslv eptspwsyln yikirrrlfp fyfaerfhil rsefdsylrw vstelpatrf
      121 ghrvdtvawd pgqgafavef trldpdgqpl stgltharnl algvgtaphi peplrelvqd
      181 paavvlhsad ylaqrdrlla arhitvvgsg qsgaevlldl lrarpegaeg ltwlartpaf
      241 apmeyskigl eqftpdytry fhglpqatrd rllprqwqly kgvsgdtlgd ihdelyrrsl
      301 gggwpdvtlt pgievtgaat taegriglsv ehgqqetrgr lvtdavvlat gyrerpvdtl
      361 laaldpyivr dgagrpqvda aqrlvlapei agsvfvqnae rhthgvgapd lglaawrsav
      421 ivnaltgkef yplpertaft tfglegqdre dvdpppsraa eeerr
//
LOCUS       WP_457658455             466 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658455
VERSION     WP_457658455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46717
     Region          1..393
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(3..4,7..8,11,43,93..94,96..98,101,121,124..125,128,
                     255,258..259,262..264,267,295,299,351..352,356,360,376,
                     379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mivaldgsvl fvaqpslqrd lsaslaqvqw tstayllava sllvlagrlg dryghtrlll
       61 tgslgfgaas lgiavvpsvg wvialravqg vfgallqpat lallrqvypp drlglpvalr
      121 tsaigvaaaa gpllggflva qfgwrsvfvv nvpvalligl fclaarvpkg aavrtsgrrl
      181 eiggglllaa alallvnala evelhgwadr rtvggllcsa avaavlvrhe rrgrdplvpa
      241 avarsvpvta smamllftas glfgalfvst yflqyalgla pldsalralp mtalmivgap
      301 vagrllrvlg arttalggtl lvvlgigwla gtdsttgpva mgaafavlga gyatvmvtat
      361 gtvvgdappg yagvvgglkq tavnigpvlg iavaagllpa agagqaerwe gamgpalmvl
      421 aataalalip aallpgtrrr tgppprdagr grpesaapcl tspsev
//
LOCUS       WP_457658456             481 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457658456
VERSION     WP_457658456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..481
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52323
     Region          46..462
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(153,155..156,286..290,315,318..319,322,337,341,401)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mphltrrlra allatasatl vaatlpapep lgigdrlfpe lgnpgydvla ydialtyhgs
       61 ntepldavts ikarttapld rinldfargt vrgvevnghs vdfgsknedl vlqaprrlpa
      121 gvplnitvrh tsdpsgsged ggwvrtadgl amanqadaah rvfpsndhps dkayftfrit
      181 apekltavag glpvgktrhg atttwtyrte hpmatelaqv sigssavahr tgphglpvrd
      241 vvpaadrkkl epwlkktpah ltwmeeqvgr ypfetygvlv adspigfale tqtlslfgks
      301 fftepgypqw yvesvmihel ahqwfgdsvs paswsdlwln eghaswyear yaeengggtl
      361 errmrqayel sdgwradggp pahpdgpapg qklslfrpvm ydgsalvlya lrqeigeaaf
      421 drlertwvra hrdstattad ftrlasgiag rdltaffdgw lygkktppmp ghpdwssakp
      481 a
//
LOCUS       WP_457658457             721 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Streptomyces griseus].
ACCESSION   WP_457658457
VERSION     WP_457658457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 721)
  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
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..721
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=77502
     Region          34..716
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msaeaadpga plrrrsrpri dlrrlgrval rgpvsrdrlp daighvaeah rahhpdadlt
       61 ilhrayvlae sshrgqmrks gepyithpla vtlilaelga etttltasll hdtvedtevt
      121 ldqvreqfgd evcylvdgvt klekvdygaa aepetfrkml vatgndvrvm sikladrlhn
      181 mrtlgvmrpe kqariakvtr dvliplaerl gvqalktele dlvfailhpe eyehtralia
      241 aaagpdapld tiavnvrhtl rdagisaevl irprhfvsvh rvrrkrgelr gtdfgrllvl
      301 vgedadcyav lgelhtcftp visefkdfia apkfnlyqsl htavvgpega vaevlirthr
      361 mhkvaeagvv algnpyaqdh aaaqhaepsd eradptrpgw lsrlldwqes atdpdtfwtt
      421 lrddlaqdre itvfrtdggt lglpagascv daayaqygdr ahtsigarvn grlatlstvl
      481 sdgdtvqlll aqdtasgpsp dwldhvrtpa ariaitgwlt dhpdeakpap smmtsvdaga
      541 pgpvglaper daqitapart rsgpratgvv vegaggpvrl agcctpvppd eltgfvvrgg
      601 avtvhrrecp avaamqeigr dpvgarwada egresdagcr vtlvaesfgr prlladltea
      661 iataeaaivs atveppseqr vrhtytlqlp daaglpalmr amrevagvyd vsraqhpapa
      721 g
//
LOCUS       WP_457658462             313 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658462
VERSION     WP_457658462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..313
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33100
     Region          43..273
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(46,49..51,54,62,64,94,113..116,207,209,211..212,214,
                     224..225,228,243..244,247)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(46,50,54,62,64,94,113..116,207,211..212,214,
                     224..225)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(49..51,207,209,212,225,228,243..244,247)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 mtdadaetei engteaeaga eitaelvrdl lreqhpdlag lavrevaggw dnqqwrigde
       61 lavrmprter apdlqrkerr wlpvlaprlp lpvpnpvrtg epsalfpkpw tvmtwvpgep
      121 ldhasisrgd haaealagfl ralhveapag apissdrgah psgctdgfdg ffeavapgdi
      181 adairavwad avaapawegp pvwvhgdlhp anvvvsdgtl sgvidfgdlf agdpawdlaa
      241 awvilpagta srffdayaha degtirrarg lavlkglvlm lvgrngdrgl pggkpawgpa
      301 graaldrale tar
//
LOCUS       WP_457658464             304 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces griseus].
ACCESSION   WP_457658464
VERSION     WP_457658464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..304
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=32928
     Region          2..299
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpegdtvlqt aarlhealag qvltrsdlrv prfatadltg rtvldvtarg khlltriegg
       61 ltlhshlrmd gawrvyapde rwrggpghqi railgnaeht avgyrlpvle llrtseesra
      121 vghlgpdllg pdwdpglamd hllaaperpl gealldqrnl agignvykce lcflarvtpw
      181 lpvgalpdgv lprlvalaer llhanrdrpt rtttitselr tppgpntspg paprpapapg
      241 tapsptppag lrprtrppvr vqerlyvygr arrpclrcgt pvrladqddr ptywcpgcqs
      301 gptp
//
LOCUS       WP_457658465             943 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA translocase FtsK [Streptomyces griseus].
ACCESSION   WP_457658465
VERSION     WP_457658465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..943
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=99494
     Region          395..933
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 masrtsgkgs qgtagtakrv grtsgpvkka apakktapkk saapvkkapa kkaaakkpap
       61 kpapsptggi yrlvravwlg aahgvgalfr sigrgakgld pahrkdglal lllglaliva
      121 agtwsnlqgp vgdlvemlvt gafgrldlla pillgamavr lilyperpea ngriviglsa
      181 lvigvlgqvh iacgspgrde gteamqdagg lvgwatskpl ifmmgevlav pllvlltvfg
      241 llvvtatpvn aipqrlrqlg vrlgiveplp eagegdendd erydeqwrea lperhqrrga
      301 rrtdpdadpv ydhdqaeaea ltkrrrsrrp aaqpamnrpl davdvaaaaa aaldgavlng
      361 mppspivadl tqgvsvdrer tgtpvpgare aerdgagksg agrrsgdtde ptggdrsggt
      421 sdrsgavpdl tkpaperseg lparaeqlql sgdityslps ldllerggpg ktrsaandav
      481 vasltnvfse fkvdaavtgf trgptvtrye ielgpavkve kitalaknia yavaspdvri
      541 ispipgksav gieipnsdre mvnlgdvlrl adaaeddhpm lvalgknveg gyemanlakm
      601 phvlvagatg sgksscincl itsimvratp ddvrmvlvdp krveltayeg iphlitpiit
      661 npkkaaealq wvvremdlry ddlanfgyrh iddfnhavrn gkckapegse relspypyll
      721 vivdeladlm mvaprdveds ivritqlara agihlvlatq rpsvdvvtgl ikanvpsrla
      781 fatssladsr vildqpgaek ligkgdglfl pmgankptrm qgafvtedev aavvqhckdq
      841 mapvfrddvv vgtkqkkeid edigddldll cqaaelvvst qfgstsmlqr klrvgfakag
      901 rlmdlmesrn ivgpsegska rdvmvkpdel dgvlavirge sap
//
LOCUS       WP_457658467             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658467
VERSION     WP_457658467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33811
     Region          66..310
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mseallvqea gaapavapas garlflrrlr aqraacaaal vvlllvlval aaplltalag
       61 qdpnayhpdl vdsaaggvpi gsfggisaeh wlgvepqtgr dlfarvvyga rvslgvalva
      121 tvlqialglv iglaaalgsr wvdqllgrit dvnvalpvmv ialallaivp esfprpvlia
      181 lviggigwsg tsklvraqal tlksldfvsa arlsgrgkws iarrellpsl aapvityaal
      241 afptniivea alsflgvgik pptpswgqml teadtwyqaa ptyllipagl lfitvlaltv
      301 lgegirtald praasrlrvg ttrkgeat
//
LOCUS       WP_457658470             529 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658470
VERSION     WP_457658470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..529
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55755
     Region          209..>341
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          425..524
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrahrraqra tvttgaalla agllagcgls epdadvpadg rpghtsaapt pagptdsprt
       61 pelpseltsq rldwkrctap rggnapgsaw rcarvdvpld yadpsgetls valirkeard
      121 kgrrlgsllf nfggpggsgv atlpraagsy aklntrydlv sfdprgvaas sgvrcrtdke
      181 qeqahrnvdl tpdtaaeeaa fiedaaefga gcerrsgtvl phvgtgnaar dldlirrvlg
      241 deklsyfgfs ygtelggtya hlfphsvgrt vldaavdpta dgigharnqt vgfqraleny
      301 lkdrgqspke gseriarlla ridrsplptd sgrelsesla itgivtplys esswpaltaa
      361 ldeaenngtg ngllrladsy ngrdeqgryd tqshsqrais cadstsrptv dearallpef
      421 rklspvfgpf lawdtagwca ewpvegehet petsapgagp vlvvgttgdp atpyegarrm
      481 adelgegvgv lltnkgeghg aygsndcvts tiddyfldgk vpadgrtcg
//
LOCUS       WP_457658471             530 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658471
VERSION     WP_457658471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..530
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55517
     Region          122..>357
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          426..523
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrtspalraa alaatatvll plaacsddgd gegsstptga stasptatae dlasqklews
       61 pcpppntsqg ggespsplpg gvvwecsfmd vpldyakpdg rtielalvra kakerqrrig
      121 slvfnfggpg asgvatlpaf gteydrlrtr ydlvsfdprg vgrsegvqca ddaqldafyq
      181 edatpddaae ekqfvqgqkd fiaaceessg delpfvgttn aardmdllrt vlgdeklhyf
      241 gisygtelgg vyahlfpdkv gravfdavvd ptkdaeqssl gqaegfqlal dnftkdcaer
      301 ddcalpgatq qeveqfiadl laeleeqpvd glgdraltqt lattgiasal ysketwplle
      361 qgldeadgkn gglllalads lngrsedgry dnsnaaniai ncadskqrfs leqtkaalpa
      421 frkasplfgd ylgwglmsct gwpvagawqt pdvsapgaap ilvigntgdp atpyagakam
      481 veklgkgvgv eltykgeghg aynskdacvq rtvdgyllng kvpesgtvcg
//
LOCUS       WP_457658472            1131 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Streptomyces griseus].
ACCESSION   WP_457658472
VERSION     WP_457658472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1131)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1131
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=121984
     Region          53..863
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          866..1126
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mythahpris tgpaihvsss strhsphres rprttgayrl vrtppgsvdp plldagqrav
       61 vdhpggpllv lagpgtgktt tlvesvaarv nrgadparil vltfsrkaav elrdrmaarl
      121 gaargpqatt fhsycyalvr ahqdadlfad plrllsgpeq dvtvrellag qldlekegla
      181 hvrwpdelrs clttrgfade vravlarsre lglgpdalaa faartgrpdw saaaqflaey
      241 ldildaqgvl dyaelvhrav llaerpevaa elagrydavy vdeyqdtdpa qvrllhalag
      301 nrgrgedpsg grtliafgdp dqsiytfrga dvngildfpd tfrradggpa pvgvlttsrr
      361 sgagllaatr lltrrmpltr lpgdtvrahr dlhavrdggr vetytyptts teleniadll
      421 rrahledgvp wqemavlvra ggrslpavrr altsagvple vdgddlplrh epavapllta
      481 lrtvataalh hrpveteaed qpeagptswl dtetaltllt splgamdaad lrrlgralrd
      541 eeraagirvp apsddllara laeperlvth dpayahgaqr lgallrkare llqgggtaee
      601 alwilwngtp wpgrlaraal rggaggrnad rdldavcalf dtaaraeert ggrgalnfle
      661 evdaqdiaad tlsrrtarpd avrlmtahrs kglqwrlvvv agvqegvwpd lrrrgsllea
      721 drigrdglae pltpgallae errlfyvaat rardrlivta vkapaddgdq psrfltelgv
      781 eprdvtgrpr rplavaalva elrattvdpa asaalreaaa hrlarlaalt ddegqplvpa
      841 ahpyrwwgle eptrsavplr drdqpvtlsg saldqlantc alqwflgrev kadapataaq
      901 gfgnvvhvla devassrtpa dldvlmerld svwnglafda pwkseqekdq araalerflh
      961 whvldrggrt ptasehdfdv tleageyavr irgsmdrveq daegrayvvd fktgkgaptk
     1021 devaahpqla vyqlavrega vdevfdgrrp epggaelvql rqpapkkegg dafpkvqaqe
     1081 plagewvsdl lataagkvld erftpttgth cahcafrasc saqpegrqvv e
//
LOCUS       WP_457658474             484 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC1 kinase family protein [Streptomyces griseus].
ACCESSION   WP_457658474
VERSION     WP_457658474.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..484
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=52670
     Region          1..449
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 msdlprkavt rtaklaalpl gfagratwgl gkriggksae lvarevqqrt adqlfktlge
       61 lkggamklgq alsvfesalp eevagpyraa ltklqeaapp lpartvhevl ttrigedwre
      121 yflefddtpa aaasigqvhr avwhdgreva vkvqypgage allsdlaqls rfarllgplv
      181 pgvdvkplik elrdrvseel dyeleaqaqr ehaeefagdp dvvipqvvhq sdqvlvtewi
      241 egiplseiia dgtpeqrdra gqllarflfs gpartgllha dphpgnfrll pedekeqged
      301 ggaagswrlg vldfgtvdrl pgglprnigd slrltlegda agvyaklrqe gfvkesidld
      361 pdevldyllp iieptqveef tfgrgwireq aariadprsp ahqlgrqlnl ppsyvlihrv
      421 tlstigvlcq lgatvrlree leawlpgfla eeaeaqapea eyagttehae eegepepege
      481 tvqa
//
LOCUS       WP_457658476             217 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658476
VERSION     WP_457658476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22826
     Region          38..151
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mgdsqgrvde ghgspaaavf dalgaeyeqa fassaahres lerlladlap gsrvldvgsg
       61 tgrptartla daghrvlgvd vspvmtalaa rqvpgaefrc adirdlplte sefdavcvyf
      121 sllqlsrgeq gellerlars lrpggllava tvpvdvadvd avfmgqpvrv ssfgaeefta
      181 lteragvivk wthsalftpd hpagapephf fvhgrri
//
LOCUS       WP_457658477             489 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces griseus].
ACCESSION   WP_457658477
VERSION     WP_457658477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..489
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50310
     Region          9..483
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 misakelknp hvvrrdllas lvvflvalpl cvgvavasgv paelglvtgi vgglvvgflp
       61 gsklqvsgpa agltvlvfea vkefglstlg pivlaagllq vvlglarfgr wfraisvsvv
      121 qgmlagigli ivlgqvyama dteqpgsgla klaglpglaa eivtdqealt afglgagtva
      181 vlllwprlpa tvrivpapla avalatavas laglrpavad vngllhaidl pggaefgrla
      241 dvavigtvla faliasaesl fsaaaidrmh dgprtdydke lvaqgvgnti cgalgalpmt
      301 avivrsaanv qagattalsr iahglwlllf aallpaavgi iplaalagil vhagcklvpa
      361 kefgplwreh qgeavllait aiaivvtnlf egvvlgllla vvksawetsh vqltthqltg
      421 grvvvtltgn atflrlpril eqleqlpqdq pieldltglr hldhacrval enwarrhnna
      481 eiepvtirr
//
LOCUS       WP_457658478             481 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457658478
VERSION     WP_457658478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..481
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49888
     Region          218..457
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mndptaglpl sapealtvlg alvlvaarwl perlrgpaal aagallagsv tvlvmtglrw
       61 qlvpvvvaaa vvgafllapv varrsgrtpw rarwwlavpg svvcaaliaa gpvsvwafpv
      121 pnfpapsgdf pvgtealews arpagagpda eprtlvvqlw ypagrsgpda rrarylgrte
      181 aeahtvssal adyagvpgfl ldslprarsh avpgapvadg ggrfpvvvfs pglggvrtqn
      241 tawaeelash gyvvaavdhp ydsaavvlsd grtlrtrvsa tgdrakdraa aegwtrtrtg
      301 dlravlsrle rldrgegegp lagridtgrv aaaghslgga aalraarqdr rfdavvdldg
      361 fphgpvgdrf eqpvlaltqe igprtdpdyl prltrvlels dtagyrltvp gaahltftda
      421 plylppvpgv igspgrtegp ritagatrsf ldatlrgtav dlpaalsayg evtvhrpega
      481 g
//
LOCUS       WP_457658482             261 aa            linear   BCT 27-JAN-2026
DEFINITION  glutamate racemase [Streptomyces griseus].
ACCESSION   WP_457658482
VERSION     WP_457658482.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10002726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..261
                     /product="glutamate racemase"
                     /EC_number="5.1.1.3"
                     /GO_function="GO:0008881 - glutamate racemase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26095
     Region          1..245
                     /region_name="MurI"
                     /note="Glutamate racemase [Cell wall/membrane/envelope
                     biogenesis]; COG0796"
                     /db_xref="CDD:440559"
ORIGIN      
        1 mkialmdsgi gllaaaaavr rlrpdaelvl ssdpgsmpwg prtpedvtar alavaraaaa
       61 hrpdaliiac ntasvhalpt iraelepalp vigtvpaikp aaagggsvai watpattgsp
      121 yqrgliaefg gsaevaevpc pgladavehg deaaidrava aaaaltppdv ravvlgcthy
      181 elvatrirda vqrpgrppla lhgsagavaa qalrrigadp aptaepsgtl tvlrggrpaa
      241 lpetaltyae grilaaaapv r
//
LOCUS       WP_457658484             446 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces griseus].
ACCESSION   WP_457658484
VERSION     WP_457658484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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..446
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..446
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=46454
     Region          15..446
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mgatmtmqkg tnvpvpagtv rvavgwhtap gtpdvdasgl llvagkvrsd adfvfynqpa
       61 hasgavrheg kqtaadrvtd tllvdfgkve pgierivvaa sadggtfgrv sglsvrvtda
      121 angaelarfd stdatvetaf ilgelylrqg awkfravgqg ystgleglat dfgisvdepq
      181 qaapapaaap tppapqppaa pahswpaapa papvapappv ppapmppapp apapvrltkv
      241 tltksapsvs lakqggtsga lrvnlnwevr kqfkgwgakl gravamhadl dldlcalyel
      301 adgrkgvvqa lgnafgslrq ppfihldgdd rtgavstgen mtinldhkdl lrrvlifvti
      361 yegarsfadl hatvtlqpqn gapidfslde ctvpstvcal alitnnggdl tvqrearylv
      421 pdrgvspqrt idaaygwgmn wtpgrk
//
LOCUS       WP_457658488             283 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            griseus].
ACCESSION   WP_457658488
VERSION     WP_457658488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..283
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29512
     Region          8..271
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msenqnllae qrralildev rrrggvrvne ltrklnvsdm tirrdldala rqgviekvhg
       61 gavpvveast hepgfeaksa lelsakedia rtaaalavpg saialsggtt tfalarhlld
      121 vpdltvvtns vrvadvfhda qrpaggrgar pgaatvvltg gvrtpsdslv gpvadraids
      181 lhfdvlflgv hgisaeagls tpnlaeaetn rrfvraarri vvvadhtkwg tvglssfatl
      241 devdtfvtda glapetraei gehlpgllva gddpaeaapv teg
//
LOCUS       WP_457658496             251 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces griseus].
ACCESSION   WP_457658496
VERSION     WP_457658496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..251
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27252
     Region          28..225
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mqiaehiasl sgegrllaaa aeragpgasv ptcpgwqirh llrhtgmvhr waaafvtegh
       61 tayqpdggep aldgaelltw freghdhlvr sleeapsdld cwtflpapsp lafwsrrqlh
      121 ettvhrvdae salggpltpv paeravdgid elltgfharp kskvrsrkpr tlrvravdte
      181 atwtvrisea ppeavrtaap dapedgvdce lsgtaeglyl tlwnrlplaa lslrgdrsva
      241 rhwtdnaavt w
//
LOCUS       WP_457658497             432 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658497
VERSION     WP_457658497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  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 432)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..432
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=45376
     Region          <220..416
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdeqrpphrg ggppcglpgr sgrpggrggp ppwlsgarsr taaglpwlst avllvfvmvg
       61 tgfaehgqdr rpldlvarll lfvavgvlll rhrrpvlavv ttcavtlgyl aagypygpvf
      121 vavavgcfsa ivaghreaaw wslgglwagh vlvahwlyrw lppdgdpaap waqegfitaw
      181 vvavvaaael lrvrreqwaa araereaaer rradeerlrm arelhdvlah sisvinvqag
      241 vglalldsdp eqartaltti kgaskealde vrqvlanlrt pgdaptapap gldrlpelvd
      301 qaaaagltvt vesegdpaav ppgaglaafr ivqealtnvv rhsgsrtalv hiahdsgrvr
      361 lriddggpat gddaggsgng lvgmreraaa lggtieagpr pdggfrvrae lpftapdhdr
      421 rqdppepaee ap
//
LOCUS       WP_457658500             228 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces griseus].
ACCESSION   WP_457658500
VERSION     WP_457658500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..228
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24408
     Region          9..210
                     /region_name="yflN-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis yflN; MBL-fold metallo hydrolase domain; cd07721"
                     /db_xref="CDD:293807"
     Site            order(64,66,68..69,151..152,170,209)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293807"
ORIGIN      
        1 mdlvevlpql hmfrfrigqa ylwrdgpelt lidagdvesa aaiedairsl ghaparirri
       61 vlthghrdhf gaareladry gaeiiahtld apvirgerpv pepdlldwer plhahgltcp
      121 eapptrvdre vtggeelpfg dgarvvhapg htpgsialhl prhgvlftgd tvasvervml
      181 gvfnvdraga aatfrrlaal aprtvcfghg dpltenaaal meaaanga
//
LOCUS       WP_457658501             182 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658501
VERSION     WP_457658501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..182
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19332
     Region          5..167
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mrrnpapael glveefcnta thlhgeddla rpesaarwlg ahgfpalsdp gdltslaear
       61 etvraflver tspeavdaln rlvataagap avrpdgaltl rpasggavaq vmrpvleall
      121 fhgltgrhat rlkacaapec rwvfydraps snglwcdmdv cgarhkmray rarggaaarr
      181 da
//
LOCUS       WP_457658507             208 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658507
VERSION     WP_457658507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..208
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22075
     Region          44..122
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkakstyrkr wgvpggpdll dqvpdlldqv pdlldripgw vdamtanglr dtvlrilsgg
       61 prsgaeliee igtlrgrpqi taeqlyplld qltdenlvta gtkdrpraya lteegreaaa
      121 rrdgsgafgp fgsfdpfasa gsagsagssg ssdssgarpg eahrllgdvl maagrlewsg
      181 darrreqaaa vlaearrely rlladeec
//
LOCUS       WP_457658508             726 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457658508
VERSION     WP_457658508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..726
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75959
     Region          9..691
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mfgrigqsav rhpwltivaw iiaavalmsl apqlkptgdq adflpshyes vqvgevqkra
       61 fpqqeqpasi avfqrgdkaa ltpedrqdlr kvvaglddag lkkvkqiatd eqsvsadgkl
      121 alasimattk dpydadlmas veelreiavp llksteltmg itgqtatgvd tmkssgntda
      181 mimmatmvli vvlllaifrs pliaflplli islvfmvang liatvsdlgg lktdasissi
      241 livvlfgvgt dyllfllfry rehlrsgqep kqamadavgk vgetiasaag avivaflall
      301 lstlgmfram gpalaiavav tllaaltlvp avfsllgaka fwpskawrkq pqhriservg
      361 altgrrpglv aaasggllav laigalgfnp vfdtgsslpk elesvkamed lqhsfpsgqt
      421 dpvwimvrse dggkldpaal eaygkelaal dgvgsappav lapagdvaql svlidhrptg
      481 daaidlvsgp lrdlahdkap dgtealvggt savladvqha vnrdytlvfp aaglaimiil
      541 glllrsvvap wylmlavglg fgatlgstvw lfqdvrgesg llftlpvily lfvvaigtdy
      601 nilmiarlre eirrgsspae ataravvsta stitaaavil agtfgvllla enamlqqmgf
      661 avafgillta fvmamllvpa ltalfgrraw wpggradapr tgedapdgpd aadgsaderk
      721 padvtg
//
LOCUS       WP_457658509             515 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces griseus].
ACCESSION   WP_457658509
VERSION     WP_457658509.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..515
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55580
     Region          3..512
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 meqealtela viraealrgp serateaqha kgkltareri ellldagsfr eveqlrrhra
       61 tgfgleakkp ytdgvitgwg tvegrtvfvy ahdfrifgga lgeahatkih kimdmaisag
      121 aplvslndga gariqegvsa lagyggifqr ntrasgvipq isvmlgpcag gaayspaltd
      181 fvfmvretsq mfitgpdvvk avtgeeitqn glggadvhae tsgvahfayd deetciaevr
      241 yligmlpsnn renpptarsd apadrrsdvl ldlvpadgnr pydmhqviee lvddgdylei
      301 herwarniic amarldgqvv givasqplal agvldinaae kaarfvqlcd afniplvtlv
      361 dvpgflpgva qehggiirhg akllyaycna tvprislilr kayggayivm dsqsigadlt
      421 yawptneiav mgaegaanvi frrqiadaed peamrtrmvk eykaelmhpy yaaerglvdd
      481 vidpaetrev liaslamlrr khadlpsrkh gnqpa
//
LOCUS       WP_457658511             205 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658511
VERSION     WP_457658511.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..205
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22373
     Region          7..191
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          121..191
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtppppvlrp yrpedrealf dicvrtgheg gdarhlypdp dllpnifaap yaalepglaf
       61 vvedggravg yilgtadtas fvdryraewl pgladrhpap arepatpaea maalmhtper
      121 milpelagyp ahlhidllpt hqraghgrrl metflaalhe qgvkavhlsm ltantraraf
      181 ydrvgfheia vpdpgpvtyl gratr
//
LOCUS       WP_457658512             219 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658512
VERSION     WP_457658512.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006587
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..219
                     /product="DsbA family oxidoreductase"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24070
     Region          4..200
                     /region_name="FrnE"
                     /note="Predicted dithiol-disulfide isomerase, DsbA/YjbH
                     family (virulence, stress resistance) [Posttranslational
                     modification, protein turnover, chaperones]; COG2761"
                     /db_xref="CDD:442047"
ORIGIN      
        1 madpvkikiw sdyvcpfcml aegpleeaid digaevevew mpfelrphpq ptlrpeddyl
       61 pdiwkravyp marrlgvdit lpdvspqpyt alafegyqya aehglgtayt rrmfraffqe
      121 sqdlgqvdvl vtlageigld eagfraalad gayrarhqea lreaaahrvq avptlligdt
      181 riegvprpaq lrkaildaqa rqaedavvyg aacgidgsc
//
LOCUS       WP_457658513             378 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH:flavin oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658513
VERSION     WP_457658513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..378
                     /product="NADH:flavin oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39466
     Region          26..352
                     /region_name="OYE_like_FMN_family"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02803"
                     /db_xref="CDD:239201"
     Site            order(40,42,75,118,198,246,336..337)
                     /site_type="active"
                     /db_xref="CDD:239201"
     Site            order(40,42,75,118,246,336..337)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239201"
     Site            order(196,198)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239201"
     Site            198
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239201"
ORIGIN      
        1 mpgtaagpsg astgqtrahp alaacrfagl dlcnrfavap mtrvsatedg ratpemaayy
       61 aafaeggfgl litegtytdr afsqgylfqp gitdeaqaaa wrpvveraha agtrivlqlm
      121 hagavsqgnr frdraagpsa vrplgeqlak yrgsgrwpvp meltrrqiae avegfaaaav
      181 rardagfdgv eihaangyll dqfltpytna rtdeyggdve erlrlvrevt agvraatgpg
      241 ftvgvrlsqg kindpgwqwp ggdaeartvf taaatagady lhlagsgrdr fprgrslpal
      301 aravtglpvi angglhrdev arrvldegha dllaigtaal anpdlprrva agtaraafdp
      361 galeplatlg narahaha
//
LOCUS       WP_457658514             255 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658514
VERSION     WP_457658514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..255
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25722
     Region          7..254
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mpggpllsgk valitgassg igaaaarhfa degaavvlva rraglveeva erirkdggra
       61 vavpgnvtvr admeqavata vdrfgrldca fnnagyasag tvlhelpdev fdrtmdvnlr
      121 gvwnclraqi pamlpagags vvntssvagv ratsvsapyv aakhaviglt raaaaeygeh
      181 girvnalvvg stdtemmdgv latgptvrag fgskaiqqrl adpaeiaraa awlcsdassf
      241 ttgsalavdg grtak
//
LOCUS       WP_457658516             446 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658516
VERSION     WP_457658516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44119
     Region          15..414
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(25..26,29..30,33,65,118..119,121..123,126,145,
                     148..149,152,248,251..252,255..257,260,288,292,341..342,
                     346,350,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mknpplmdaa trrwraalfl fmlatgvsma swvartpavr dalevstgsm glvlfglsig
       61 smagvlvsgg lvrrhggrsv ialgagllva glaviaggaa leasagvfgg lalfgagmgl
      121 aevafniega avertlgrpv lpvlhgcfsl gtvvgalagm altavrfpvg whlaavavav
      181 taagvwtvra vpagtgraea eadaqdpgsg pgsetgtgqg aggertggvr gqlavwrdrr
      241 lvliglivla mafaegsand wlpllmvdgh gtsatagslt fmlfavamtt grfaggpllv
      301 rygpaavvra salvaavgva lvifsssall agaavvlwgl gaslgfpvti saagegarpa
      361 dasarvaavs tagyaaflvg ppslgfladh vglrnamvvv lvllggaali tralrfpvpe
      421 regpgtgaaa sregrprtgs dqpdlv
//
LOCUS       WP_457658518             172 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457658518
VERSION     WP_457658518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..172
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17880
     Region          18..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mrdgdgdgdg teagagdtps qqellsraal tvfrlngqfl svadelarpg gltaawwqvl
       61 gavlpeplpv agiaramgit rqsvqriadl lverglaeya enpahrrakl lrvtgagrea
      121 vsrigpshae faarlvgelg vegvveavrv lerlsqtldt lttadragpp ga
//
LOCUS       WP_457658520             182 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces griseus].
ACCESSION   WP_457658520
VERSION     WP_457658520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..182
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20141
     Region          6..177
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 msteefeela rrapelvrle fiqgqvrvkp vpdgnhgaiv mwllrqcmrr rpelslfpdq
       61 glaietyrkg rarpdgvlap dehfagagew aapngvlmtv evtsrdadtn rrdrvekpdg
      121 yaaagipvyl lvdreassvt vftepekgty rsattrpfga vvelpepvgf aldteklkey
      181 ad
//
LOCUS       WP_457658519             281 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658519
VERSION     WP_457658519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29219
     Region          2..208
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mtmvvtgatg nigrellrql smdgrgadvr altrdaarag aavpdgvavv egdlgrpasl
       61 ksalggarsl flvsgvgdda gvldaardag vehvvlvssi tvethphlgp aqanlaverr
      121 lresgmewtv lrptqfasnt lwwadsvrda svvrvpyadv glpavhpadi asvaraaltg
      181 pghrgrtypl tgperitprq qagelgrvlg revacvgigr eaaygpmaam mgaevansvl
      241 dlmggdvnda llavhdtvar vtgsparpyr rwaeenadaf r
//
LOCUS       WP_457658532             247 aa            linear   BCT 27-JAN-2026
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658532
VERSION     WP_457658532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..247
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0017169 - CDP-alcohol
                     phosphatidyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25943
     Region          10..155
                     /region_name="EPT1"
                     /note="sn-1,2-diacylglycerol ethanolamine- and
                     cholinephosphotranferases [Lipid transport and
                     metabolism]; COG5050"
                     /db_xref="CDD:444050"
ORIGIN      
        1 mgstgtvlre lrgaqksakg vslysryvnr pagrvlaaga yragmtpnqv tftsalftyg
       61 alasvalvep swtlavlvya alavgfafds adgqlarltg rggpdgewld hvvdcgklvl
      121 vhaavlisfy rfgelpsdaw lllplgfqla tvvtfcagll reqlgkaaas argpswaepa
      181 tpaqpvsrvr avvllpadyg vfclvflllg apgafragya alavvhtlfl aafltkwfre
      241 lkalrag
//
LOCUS       WP_457658534             401 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457658534
VERSION     WP_457658534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42062
     Region          4..367
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtafslepeq tawceelrtl avrelrplae kgepgqvnrp llaalgelgl lermfgsgal
       61 dlcllresla rgcteaetal alqglgatpi vqagtpahre rwlpevragr avaafalsep
      121 gagsdaaals laaehtpagw altgrkcwis napeadfavv farttpgags rgitaflvps
      181 drpgltgsal dmlsphpigt lefdgvpvta ddvlgepdrg frvamntlnl frpsvgafav
      241 gmaraaldat lehtahrtaf ggplsdlqav shqvaematr teaarllvya aaaaydages
      301 gvprraamak lyatetaqyv vdaavqlhga ralrrghlle hlyrevrapr iyegasevqr
      361 tiiakelyan aaqppgphqp paatpeppaq qpasptqepp a
//
LOCUS       WP_457658536             276 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658536
VERSION     WP_457658536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..276
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28989
     Region          193..268
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtwtftddvd vflasagpsl aarpvkhtva ltvterlrrs gphhygaddp vlgwwrgadg
       61 avagtlvrtp phgalltavp aeavgplvaa lgpgpdlddv tadrdtaaql aallpghrtv
      121 qeqrlyrlgt lrppcpapeg raraatradr allvvwvrgf adatgqakss aewlvdegtd
      181 rgsftlwesg gapvalagrs rmlagtvrvt svytppefrg rgyaaavtae asraalaega
      241 aevllftdla nptsngvylr igyepvadrv qlrrnt
//
LOCUS       WP_457658543             119 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide pyrophosphohydrolase [Streptomyces griseus].
ACCESSION   WP_457658543
VERSION     WP_457658543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Requena,C.E., Perez-Moreno,G., Ruiz-Perez,L.M., Vidal,A.E. and
            Gonzalez-Pacanowska,D.
  TITLE     The NTP pyrophosphatase DCTPP1 contributes to the homoeostasis and
            cleansing of the dNTP pool in human cells
  JOURNAL   Biochem J 459 (1), 171-180 (2014)
   PUBMED   24467396
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Galperin,M.Y., Moroz,O.V., Wilson,K.S. and Murzin,A.G.
  TITLE     House cleaning, a part of good housekeeping
  JOURNAL   Mol Microbiol 59 (1), 5-19 (2006)
   PUBMED   16359314
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Moroz,O.V., Murzin,A.G., Makarova,K.S., Koonin,E.V., Wilson,K.S.
            and Galperin,M.Y.
  TITLE     Dimeric dUTPases, HisE, and MazG belong to a new superfamily of
            all-alpha NTP pyrophosphohydrolases with potential 'house-cleaning'
            functions
  JOURNAL   J Mol Biol 347 (2), 243-255 (2005)
   PUBMED   15740738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..119
                     /product="nucleotide pyrophosphohydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009143 - nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=13169
     Region          10..100
                     /region_name="NTP-PPase_RS21-C6_like"
                     /note="Nucleoside Triphosphate Pyrophosphohydrolase (EC
                     3.6.1.8) MazG-like domain found in mouse RS21-C6 protein
                     and its homologs; cd11537"
                     /db_xref="CDD:212144"
     Site            order(12..13,16,19..20,22,28..29,32..33,35..36,39,42..43,
                     46..47,67..69,71..73,75..76,78,81..82,84..85,87,89..90,
                     92..94,96..97,99..100)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:212144"
     Site            order(13,38,41,70,73,77)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:212144"
     Site            order(25,29..30,32..34,36..37,40..41,43,46..47,77)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:212144"
ORIGIN      
        1 mtdidvaelq qrlaafaaar dwgqyhtpkn laaalsveas elleifqwlt peqsarimek
       61 pesahrvade vadvlayllq fcevlgidpt aaladkiern ekrfpvpgap elrdrhsse
//
LOCUS       WP_457658544             265 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            griseus].
ACCESSION   WP_457658544
VERSION     WP_457658544.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..265
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27753
     Region          1..265
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msrdarwdal lelvgkhgrv dveeaatald vsaatirrdl dqlaeqhllt rtrggavahg
       61 vsyelalryk tgrhapekqa igravsglva vgevvgltgg ttvtevaral avrqdivgep
      121 taagghptlt vvtnalnias elairpqikm vvtggvarpq syeltgplav gvmneitldv
      181 avlgvnaidi ergayvhheg easvnrllae raqrvvvaad sskigkrafa rvcdlelvdv
      241 lvtdsniaae ardrfgeagv qviav
//
LOCUS       WP_457658545             341 aa            linear   BCT 27-JAN-2026
DEFINITION  iron-siderophore ABC transporter substrate-binding protein
            [Streptomyces griseus].
ACCESSION   WP_457658545
VERSION     WP_457658545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Braun,V. and Braun,M.
  TITLE     Active transport of iron and siderophore antibiotics
  JOURNAL   Curr Opin Microbiol 5 (2), 194-201 (2002)
   PUBMED   11934617
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Clarke,T.E., Tari,L.W. and Vogel,H.J.
  TITLE     Structural biology of bacterial iron uptake systems
  JOURNAL   Curr Top Med Chem 1 (1), 7-30 (2001)
   PUBMED   11895294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..341
                     /product="iron-siderophore ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0005524 - ATP 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:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36730
     Region          56..316
                     /region_name="FhuD"
                     /note="Fe3+-siderophore binding domain FhuD. These
                     proteins have been shown to function as initial receptors
                     in ABC transport of Fe3+-siderophores in many eubacterial
                     species. They belong to the TroA-like superfamily of
                     helical backbone metal receptor proteins...; cd01146"
                     /db_xref="CDD:238566"
     Site            order(97,116..117,138,220)
                     /site_type="active"
                     /note="siderophore binding site [active]"
                     /db_xref="CDD:238566"
ORIGIN      
        1 mlgftrvrrh tlaatattva lavalvgcss eeggdkkkde aavtiksslg tatikgkper
       61 ivtlgqgsae taialgqtpv giesypwgsd ksgylpwine avkksgdklp kqftggeeid
      121 feaitelepd vilapwsgit qkqydvlkdi aptvaypdqa wstdwdqqmd iigkalgrtk
      181 dtdalkkkie kqladaaatr pnykdvtfsy iynsgpgtlg vfkpeeqrvk mvsslglkvd
      241 pvvngfketp gtdsaligle naeklkdsdl iftfytdekn rkeiegqkly gaipaikkga
      301 vvasddnsfv tassiinplt vpwtierylp iidqavktag k
//
LOCUS       WP_457658546             164 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457658546
VERSION     WP_457658546.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..164
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17955
     Region          39..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtaaqpsrpt spsrdpegge reryfsrlar erpdialcra ttlvartvde elsglrltva
       61 qhlvlkmlnd vgpcsqqels eqlridrsvm vgcidgleds glvrrerhpr drrayavtlt
      121 peagpalaea eggvprlldr afgsltaaer rtltrlvgki ldvn
//
LOCUS       WP_457658548             447 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457658548
VERSION     WP_457658548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..447
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47379
     Region          4..439
                     /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 mkdfrsvadl vaaeiaagrl ragerlppqr efarryaian stavrvyqel arrgltvgqv
       61 grgtfvtdap gapapapals epadsrvdle lnhpvvpeqa gllaaglekl vrsdhlesvl
      121 rpvgpdgtaa areaaaevla rgggrpdper ilfagngrqa isaavaaltr pgarlgveef
      181 typvlkaiaa rlgvtlvpla mdedglvpea veeahradpl havyvqpvlh nplsvtmpgr
      241 rldrladvll tagihaieda vwaflrddlp plasrapeht vlvdslskrl spglslgfav
      301 apaasagrva galrsggwtp mrfpleamvr wqadgtvdtl vrakqrevra rqeiadrhlg
      361 dfrtrsdpvs cyrwwelpgp wradtfvaaa arhgiavtpa aafaagrprg phairlglas
      421 ptrdvlsral atladlarst pddlagd
//
LOCUS       WP_457658549             215 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces griseus].
ACCESSION   WP_457658549
VERSION     WP_457658549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22165
     Region          3..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mvelsgvlgv alvalgmvlt pgpnmiylvs rsitqgrrag vvslggvavg flvyllatnl
       61 glsvvflavp elyvavklag agylaylaws alrpggisvf apkdlphdss rrlftmglmt
      121 nllnpkiaim ylslipqfis leagnvllqg fllgsvqiav altvnlcivl aagaiavfla
      181 rrpswlraqr clmgtalgll avsvamdssa paasg
//
LOCUS       WP_457658552             248 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658552
VERSION     WP_457658552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..248
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26204
     Region          3..198
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mttilvtgat gtlgrqvaer lrtegadvrg lsrrspsyav dlrdgkglda avegadvivh
       61 cataprggdd vaagflidaa kragtphlly isivgvdrlp lgyytvkhrv ermiedsglg
      121 atilrttqfh dlalrilsga aklpvlpvps gvalqpvdsg evadrlttla lgapagrvpd
      181 lggpevrelt dlagaflrst grsrrivpvr lagkayagyr rgdhlapeha lgtvtfekfl
      241 dhrrrrpa
//
LOCUS       WP_457658560             487 aa            linear   BCT 27-JAN-2026
DEFINITION  PepSY-associated TM helix domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457658560
VERSION     WP_457658560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..487
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51803
     Region          38..439
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msnrtehiar hdhgptdppa gtpdgkparp arswsevrhl lvrlhfyagv lvapfllvaa
       61 ltglaytltp qldrlvhgdq lrvervgeev rplseqiaaa rsahpegtla svitppgped
      121 ttrvvlavpe lgenqrtvfv dpytaevrge lttwfgstpl ttwlddlhrn lhlgdtgrly
      181 sevaaswlwv avagglvlwl grargrraks argvllpdrt akgvrrtrsl haatgvwlal
      241 gllflsatgl twsqyggerf grlldaadgn apaldtalpg aeapaedhse haghggsgga
      301 tadadpadfd aalaaargag lggivevtpp adasrawvva qtdntwpvhy drvavdttsg
      361 eitsrtrwad hpalnklskl gvqghmgvlf gvvnqialal lalgltaviv wgyrmwwqrr
      421 ptrgdrsapv grapergawr riplpalvlg ipavaalgwa lpvlgvtlag flvvdavvga
      481 vrrrrta
//
LOCUS       WP_457658555             156 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658555
VERSION     WP_457658555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..156
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16771
     Region          69..141
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 msaprpelpa lpvtfrpilt rvvllsvgla mflvitvial mlerlnpger vsfifvaalf
       61 fgvlallsrp rvtaddsgvt vvnltrsrrl aweeilrvnl rsgdpwvfld lsdgtslpal
      121 giqpglakqq airdaralrd laetrgtgnd dtpgsg
//
LOCUS       WP_457658565              70 aa            linear   BCT 27-JAN-2026
DEFINITION  FmdB family zinc ribbon protein [Streptomyces griseus].
ACCESSION   WP_457658565
VERSION     WP_457658565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 70)
  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 10021090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..70
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6753
     Region          1..46
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpryefrcrt cgdtfelsrp marssdpasc paghddtvkl lsavavggta gsapapsggg
       61 ggccdggccg
//
LOCUS       WP_457658567             221 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Streptomyces griseus].
ACCESSION   WP_457658567
VERSION     WP_457658567.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Ko,T.P., Lin,J.J., Hu,C.Y., Hsu,Y.H., Wang,A.H. and Liaw,S.H.
  TITLE     Crystal structure of yeast cytosine deaminase. Insights into enzyme
            mechanism and evolution
  JOURNAL   J Biol Chem 278 (21), 19111-19117 (2003)
   PUBMED   12637534
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Carter,C.W. Jr.
  TITLE     The nucleoside deaminases for cytidine and adenosine: structure,
            transition state stabilization, mechanism, and evolution
  JOURNAL   Biochimie 77 (1-2), 92-98 (1995)
   PUBMED   7599282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..221
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22638
     Region          22..137
                     /region_name="nucleoside_deaminase"
                     /note="Nucleoside deaminases include adenosine, guanine
                     and cytosine deaminases. These enzymes are Zn dependent
                     and catalyze the deamination of nucleosides. The zinc ion
                     in the active site plays a central role in the proposed
                     catalytic mechanism, activating a...; cd01285"
                     /db_xref="CDD:238612"
     Site            order(39,56,75..77,102,105)
                     /site_type="active"
                     /note="nucleoside/Zn binding site [active]"
                     /db_xref="CDD:238612"
     Site            order(73,78,82,103..104,107..108,111..112)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238612"
     Site            order(75..77,101..102,105)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:238612"
ORIGIN      
        1 mpderddedf gqawdaapea vrrslglaye aweagglavg svlvdaagav laegrnhayd
       61 tgpgngplrg tplahaelna lgsartewdl gattlwstqe pcsmcsaaas ftgvgavryl
      121 apdpwalatg negsssgtca tgggwlvaan amflksvsea aeggeepatl arnrllepet
      181 arlhdglppg lptfpsvraw lseawpgiie agaarrlrtg g
//
LOCUS       WP_457658569             277 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces griseus].
ACCESSION   WP_457658569
VERSION     WP_457658569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..277
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26967
     Region          1..203
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlesvaalts spwiyavval svlldvflpl lpsgvlvita ataaaagttt vsgaggstgg
       61 qvpslvvlil caatasvlgd lvayrlawrg gdrldraiar srrlstaqer lgaalsrggg
      121 alviiarfap agrsvvslga gaahrrkrdf lpwsalagla wagysvglgy fggrwlgstw
      181 fgtavsvlal fvagalaafv vkrpatrtat pagiaaeaaq ppvptrtdtg tetragagtg
      241 agtvtgagap avaptgptgp tgpggpaavg apapaap
//
LOCUS       WP_457658571             606 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces griseus].
ACCESSION   WP_457658571
VERSION     WP_457658571.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 606)
  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 606)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..606
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=65337
     Region          125..508
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(131,173,176,235..237,241..242,453,455)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(131,173,176,235..236,241..242,453,455)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 maglrlgpll ryvdwetgst atvwveasrp ctvevrcadg asgssptfav aghhyalvvv
       61 tgltpgstta yevligsrrv wppddarlpp stittppvat astttattat atatahagae
      121 ppgvrisfgs crwaaapggg hdpvgpdalv tlaarlaadp aaerpdvlll lgdqvyadet
      181 saatrrrlaa rrdlreppga eiadyeeyty lydeswrdpe vrwllstvps cmifddhdvi
      241 ddwntsaawq rdmratpwwh erivsglmsy wvhqhlgnls paelaadpvy aavraspdgt
      301 ealrrfaaet dadpartrws yrrvfgrvrl vmvdtraarv laeeqramld aeeagwlrea
      361 vlddptsydh lligsslpwl lpplihdaeh wnaalcagvr grrwarfgek lrrasdlehw
      421 aafpesfdrf tellreagsg pdapatvcvl sgdvhhayia eprwpdtgpr rpdtgpapat
      481 gsgpgstags gvapasrvlq ltcspvhnsi prsirtgfrf gwsragrwig ralarhgltg
      541 appvtwsrag gpwfgnqlmt ltllgrksal tlvqatagsa gaqletvler sltpeseals
      601 ghstec
//
LOCUS       WP_457658572             380 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457658572
VERSION     WP_457658572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..380
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36987
     Region          303..372
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mtghacpecg rrtagepgte hrvpcrcgag agaapltede qraartaeia aaedfdplri
       61 rpyvtltdld aragggglae sggsaatsgp gtseaatapv gtpsapgaag apgatettmp
      121 lflgddgpga gvgtgvdtgt gtvagasapa gpggrrrsag aepvfapdpv qprrrrpfga
      181 lavgaavaav vgtaafaggl fggddsrdea lpeattsvpd tedepaasva pspsasaaps
      241 rtpsasatps aspsasaspt rsqeptptat asasptasap atpdggggas sappaeappa
      301 elagpslrpg drgpevaelq nrlmevwlys gpsdanyndr venavavyqs ykaiqgdpag
      361 vygphtrral eaetsgrgrr
//
LOCUS       WP_457658575             709 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase 87/phosphatase PAP2 family protein
            [Streptomyces griseus].
ACCESSION   WP_457658575
VERSION     WP_457658575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12100807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..709
                     /product="bifunctional glycosyltransferase 87/phosphatase
                     PAP2 family protein"
                     /EC_number="2.4.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=76382
     Region          85..320
                     /region_name="GT87"
                     /note="Glycosyltransferase family 87; pfam09594"
                     /db_xref="CDD:430703"
     Region          466..649
                     /region_name="PAP2_3"
                     /note="PAP2 superfamily; pfam14378"
                     /db_xref="CDD:433919"
     Site            order(541,549,588..590,625,631,635)
                     /site_type="active"
                     /db_xref="CDD:239481"
ORIGIN      
        1 merwegrrsv vnadhsvrgd aaadagartg lirallwlva aalavrqvaa vlrqppgerl
       61 ldletwigen gvlhltgsly esgrftgtpf aglvlkplts saqqtlgvvw tfgslllvva
      121 lgivaaralp tpvghrtall aapvaislfm lslpvrnalh lgqtsilpvl lvllacfvvr
      181 ehraagvlvg laaafqpvll lfaallwltg rrqasvgaga tfalatavaw vagpkdswty
      241 wvhhlagagl gerpdslanq slhgallrlg legpleialf lvlaaavvav glrravryaq
      301 dgqlllavav tgcvvvavsp tawqhqllwv llavvgrvgk rasdrlvwps vvvlvvtlpg
      361 tmllpnlepl fpvrdnvlll valgaaclap flprtspywq hpvptdyakp vgarwrrvpl
      421 lpfwrrvltr pnlllellli rvvydayaqv rlaaragrpl aeehgrqiha ieqwlhidie
      481 hwvnhtvvqi twlreffdyy ystfhfivpl tilgvlyvrr padyrwvrss igfatllalv
      541 gfwlyplapp rlmpglgfid tvhgvqdfak pdygtlttvt nqyaampslh fgwslwcgvv
      601 ivmlapklwm kalgllhplf tiaaivatan hwvldaagga lvvslgfglt yllsgprrlv
      661 agereaaaea esveqppaep aepaeaadsa epeadaepvp agkaagtss
//
LOCUS       WP_457658584             316 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658584
VERSION     WP_457658584.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 316)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..316
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34129
     Region          36..316
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mkttdtppsg psgppsdaea amvpaqragt vskgssapvk ssegqvlnvf shgmlilwai
       61 mvvlplfwav mssfktdsdi fntpwslpss lnfdswgraw sqahmseyfl ntilvvggsl
      121 vgtlvlgsma ayvlarfefp gnrfiyflfv ggmsfpimla lvplfyvmdn mgllntihgl
      181 ilvyiayslp ftvffltsff rtlptsvaea siidgashtr tffqvmlpma kpglisvgif
      241 nflgqwnqym lptvlntdpe krvlaqglve lassqgykgd ysglfaglvi amlpvlaayi
      301 ifqrqvvsgl tagalk
//
LOCUS       WP_457658588             187 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658588
VERSION     WP_457658588.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..187
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19990
     Region          12..162
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mpelgsvpwp pvpiaterll lrepeardrp afvellsspe vgaylggarp rdeleraipa
       61 aparrsglfv vdldgamigq vtltrdsghl araagraelg ylflpqawgy gyaaeacaav
      121 lgwfagavpg epvvlatqta narsmrlaer lgfieaerfe aygaeqwfae wssgttpgrt
      181 pvrgtwa
//
LOCUS       WP_457658590             217 aa            linear   BCT 27-JAN-2026
DEFINITION  TMEM175 family protein [Streptomyces griseus].
ACCESSION   WP_457658590
VERSION     WP_457658590.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Brunner,J.D., Jakob,R.P., Schulze,T., Neldner,Y., Moroni,A.,
            Thiel,G., Maier,T. and Schenck,S.
  TITLE     Structural basis for ion selectivity in TMEM175 K+ channels
  JOURNAL   Elife 9, 53683 (2020)
   PUBMED   32267231
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Cang,C., Aranda,K., Seo,Y.J., Gasnier,B. and Ren,D.
  TITLE     TMEM175 Is an Organelle K(+) Channel Regulating Lysosomal Function
  JOURNAL   Cell 162 (5), 1101-1112 (2015)
   PUBMED   26317472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007546
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="TMEM175 family protein"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0022841 - potassium ion leak channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23172
     Region          13..200
                     /region_name="COG3548"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442769"
ORIGIN      
        1 msadraaaeq adeksadrlt tlsdgifaia mtllvldlhi epgldkdeft davrqalpdl
       61 gayalsfail agfwrdhrli vrlvprfegv slrfallwlg aialvpfpta llseyaarpl
      121 tvavyagmva vtnllepamf ltgrratehg tdaargdvgr aviadlasta alfaatvpvs
      181 ylvspvaamw crlalvpvkl glahrkrata rrhgrad
//
LOCUS       WP_457658592             487 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces griseus].
ACCESSION   WP_457658592
VERSION     WP_457658592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Singh,R., Goyal,V.D., Kumar,A., Sabharwal,N.S. and Makde,R.D.
  TITLE     Crystal structures and biochemical analyses of intermediate
            cleavage peptidase: role of dynamics in enzymatic function
  JOURNAL   FEBS Lett 593 (4), 443-454 (2019)
   PUBMED   30582634
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Wilk,P., Uehlein,M., Piwowarczyk,R., Dobbek,H., Mueller,U. and
            Weiss,M.S.
  TITLE     Structural basis for prolidase deficiency disease mechanisms
  JOURNAL   FEBS J 285 (18), 3422-3441 (2018)
   PUBMED   30066404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..487
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53380
     Region          51..192
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          223..469
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(286,303,315,399,430,454)
                     /site_type="active"
                     /db_xref="CDD:238520"
ORIGIN      
        1 msdarqgqav adepdenrar knglygevss elaenmrqgw adterhdlgp vaqaaytahr
       61 raalsarfpg ellvvpagnp kvrandtnyp frpssdyvhl tgdqsqdsvl vlepgpggeh
      121 raiayllprs drengefwrd yhgelwdgrr nsltenerll glpcrdvrtl terlatasgp
      181 vrllrgydag vdaalhdrvt aerdaefrat lselrlvkda feiadlrhac ratvrgfedv
      241 vralgtdtpt pervvegtfw mraridgndv gyasvcaagp hattlhwgrn dgearpgell
      301 lidagvesrn lytadvtrtl pvdgrftpvq rrvydavyaa qsagvaavrp gakyrdfhha
      361 aqrvlaehla swglfggrsv deayglglhr rwtlagtghm lgldvhdcak artelyvdgt
      421 laagmvltve pglyfqpddl tvpeelrgig vrieddflvt edgsenlsag lpraadevea
      481 wmarlrg
//
LOCUS       WP_457658593             480 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces griseus].
ACCESSION   WP_457658593
VERSION     WP_457658593.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Singh,R., Goyal,V.D., Kumar,A., Sabharwal,N.S. and Makde,R.D.
  TITLE     Crystal structures and biochemical analyses of intermediate
            cleavage peptidase: role of dynamics in enzymatic function
  JOURNAL   FEBS Lett 593 (4), 443-454 (2019)
   PUBMED   30582634
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Wilk,P., Uehlein,M., Piwowarczyk,R., Dobbek,H., Mueller,U. and
            Weiss,M.S.
  TITLE     Structural basis for prolidase deficiency disease mechanisms
  JOURNAL   FEBS J 285 (18), 3422-3441 (2018)
   PUBMED   30066404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..480
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51446
     Region          52..187
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          216..463
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(281,298,310,393,424,448)
                     /site_type="active"
                     /db_xref="CDD:238520"
ORIGIN      
        1 meqrdgsrga rshdrqapav vaevfrqgwa dtglrlppvs gaasaakrra avserfpger
       61 ivvpagglrt rsndfdyafr phsafihlta eqgtsavpds vllfepagsg hevtlftrpr
      121 sprdagpsgs efysdrqhge fwvgrrrtlr etadalgvea aardgleral gggvptrvvr
      181 gtdafvdalv ppsapadael lsflselrlv kdaweieqlr aavghtvagf rdvvgelpra
      241 trlargerwv egtfnrrarl egyglgfeti aaagahacvl hwmhndgpvr egelllldag
      301 veadsfytgd vtrtlpvggr ftdvqrrvyd lvfaaqsagi aalrpgapyg afhdaatrvi
      361 aegldawglr pgggaiphep dlyrrytvcg tghmlgldch dcaaarsgty pggvleeghv
      421 ltvepglyfq pddltlpeel rgigvriedd fvitaegalc lssdlprgad gieawmdasr
//
LOCUS       WP_457658595             281 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658595
VERSION     WP_457658595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..281
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29048
     Region          23..268
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 mtsepttaap asaaatvppp pvldltrltr rygtltavdd vslrlpagar havigpngag
       61 kttllnliag tdrpdhgtia ldgaditrts tarrsrlgia rsfqqpsvis elsvldnvvl
      121 agwphhpkrr gawrspsryr qhtesagrhl etvgladlar rpastlshgq rrmldlaaal
      181 agaprlllld epaagltdgd igrllgilgg lpasvavilv ehhvevvaqi astvtvlaag
      241 rvlatgetqe vlahpevrda yhgtgpgaaa teaapvtear g
//
LOCUS       WP_457658596             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658596
VERSION     WP_457658596.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25074
     Region          1..235
                     /region_name="LivF"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivF [Amino acid transport and
                     metabolism]; COG0410"
                     /db_xref="CDD:440179"
ORIGIN      
        1 mleltgltag yhggtvlhal dlsvsagtvh avvghngagk ttlvhtvagl mrpsagtvtl
       61 ngrevtgrpa hriaragigl vpqgrrvfag ltveehlrls yrpprrgdtt rpsvwtparv
      121 lellprlger rgnrgtdlsg geqqmlalar allgsprvll ldepteglap vlvrqvhelv
      181 ttlaaegiav llvspspaqa aecartltvl tsgrvtlrms gadaradata lhaalelapt
      241 aa
//
LOCUS       WP_457658597             525 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658597
VERSION     WP_457658597.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..525
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57089
     Region          8..518
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msearpvpaf dyvvvgggta gaviaarlte dpdvtvcvle agpsdvgdds vlrlerwmal
       61 lesgydwdyp vepqergnsf mrharakvlg gcsshnscia fwapaedlda wgalgctgws
      121 aadcfplyrr letndapgdh hgrsgpvtir tvpprdpcgt alleacaaag iptvpfntgs
      181 tvirgahwfq inaredgtrs sasvsylhpv lgkrpnlevr tglqakrllf dgdrcsgvey
      241 lepdtvhsga vharrevivs cgaidspkll mlsgigpagh lrdtgvdvrv dspgvgshlq
      301 dhpegvimwe arqpmvttst qwweigifad tepgldrpdl mfhygsvpfd lntyrrgypt
      361 sdnafcltpn vtrarsrgtv rlrtrdfrdk prvdpryftd ehdvrvmtyg lrlarqivar
      421 pemaawagae lapgpgvttd aelfdyiret hntvyhpagt vrmgpvedve spldpqlrvk
      481 gvrglrvada svmpflptvn pcittmmige kcadlikegp lpvta
//
LOCUS       WP_457658601             516 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces griseus].
ACCESSION   WP_457658601
VERSION     WP_457658601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..516
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54555
     Region          128..516
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mghveipetd lsgpvglrga prprtaasrn rtavleqlwr aptaqrdpar paparrrrap
       61 gpalaaltdl lglagpawll lragdqprpv aaaavaglmw aglrgargry adppgaepgg
      121 algavgdwlv ligllavlht aagspvdpat avvavapgll vatavaglrr wplsgrrdhr
      181 vrrvllvgda agvdraaell nsrtdhdfsl vavvpvgaar leldgvqmpg rlascpaddd
      241 vstvlggvya haadlvlvap gpqltgdrlr rlgwglhdgg vslsvlsels gvaaervrpv
      301 taagltllhi applrggpqa vfknvldrtg alfglltlap lllavalsvr lssrgpvfhr
      361 qvrqgqhnrp ftmwkfrtmv adaeelkaql aaanevdgpl fkmrgdprvt pvgrllrrts
      421 idelpqllnv llghmslvgp rpplpeeasr yderehrrla vkpgltglwq vsgrsdlswq
      481 etvsldlwyv dnwsvaadlg llartvravt dgrgay
//
LOCUS       WP_457658602             327 aa            linear   BCT 27-JAN-2026
DEFINITION  GDP-L-fucose synthase family protein [Streptomyces griseus].
ACCESSION   WP_457658602
VERSION     WP_457658602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..327
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          22..320
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(27,29..32,52,55..58,78..80,82,102,121..123,152,156,
                     179..180,182)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(99,123,152,156)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(123,152,181,200,217,225)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mttelpvppq estrsllrpg srifvaghrg lvgsavarrl addghevltr grdlldlrda
       61 artetylkev rpdvvvlaaa kvggimanst ypvqflednl riqlsviaga haagterllf
      121 lgssciyprl apqpiredal ltgeleptne ayalakiagi vqtrsyrrqy gasyisampt
      181 nlygpgdnfd letshvlpal irrfhearrd gapevtlwgs gsprreflhv ddlaaacvrl
      241 leaydgdepi nigcgedlti relaetvrdv tgyqgrigwd tskpdgtprk lldvtrlssl
      301 gfkpqiplre gvartyawwl gqlpsgq
//
LOCUS       WP_457658604             369 aa            linear   BCT 27-JAN-2026
DEFINITION  methionine ABC transporter ATP-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457658604
VERSION     WP_457658604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 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   5  (residues 1 to 369)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..369
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39056
     Region          1..332
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mitttgltkv yqsrdrevta ldgvdlhvre gevygvigqs gagksslirc vnllerptsg
       61 tvtvagqdlt alagrgrras aelrrartri gmvfqhfnll dsrtvldnve lpleilgvsg
      121 qartrkarel ldlvgladka kaypgqlsgg qkqrvgiara lagdpqvlls deatsaldpe
      181 ttrsilqllr dlnqqlgltv llithemdvv kticdsaalm rrgrivesgt vgellatpgs
      241 elahelfpvg gtasgpdrtv vdvtfqgesa sqpvisqlsr tynidisilg aamdtvagkq
      301 igrmrielpg rfeenvvpig flreqglqae vvedetgpka taeaagttap aapavpeqtp
      361 aaitkevvk
//
LOCUS       WP_457658612             273 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class IV [Streptomyces griseus].
ACCESSION   WP_457658612
VERSION     WP_457658612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  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   2  (residues 1 to 273)
  AUTHORS   Denessiouk,K.A., Denesyuk,A.I., Lehtonen,J.V., Korpela,T. and
            Johnson,M.S.
  TITLE     Common structural elements in the architecture of the
            cofactor-binding domains in unrelated families of pyridoxal
            phosphate-dependent enzymes
  JOURNAL   Proteins 35 (2), 250-261 (1999)
   PUBMED   10223296
REFERENCE   3  (residues 1 to 273)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..273
                     /product="aminotransferase class IV"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28967
     Region          1..273
                     /region_name="IlvE"
                     /note="Branched-chain amino acid
                     aminotransferase/4-amino-4-deoxychorismate lyase [Amino
                     acid transport and metabolism, Coenzyme transport and
                     metabolism]; COG0115"
                     /db_xref="CDD:439885"
ORIGIN      
        1 mriwvngglr daddarlsvl dhgltvgdgi fetvrtsegr pfaltrhldr ltrsarglgl
       61 pepdhdevrh avaavvdanp valgrlrity tgglsplgsd rgdhgtslvv aldgvsrrpd
      121 stavitvpwt rnergalagl kttsyaenvv alarareqga sealfpntvg rlcegtgsnv
      181 fvvldgriht ppvasgclag itralavewt gaeetdlpmd vlaeadevfl tstlrdiqav
      241 hrvddrelap etgpvtakam rifaeragdd ldp
//
LOCUS       WP_457658613             312 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457658613
VERSION     WP_457658613.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31482
     Region          16..303
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(46,256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(196,226,254,257..258,261)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtesavpgaa pdpcavlvlg ealvdlvpad gdsgvltaqp ggapanvavg larfggrpsf
       61 vgglgddafg grieawltga gvdlslsars alptalavad lgahgntyhf hlqdtatfrl
      121 pdrapeaarf gavyvgglaa vvepaagvva ataraasrag llvvdpnvre drtldpvrsl
      181 drlrelcsla qvvkasdedl vrlwpdappe escrrlagqg rlvvmtrgar gatayvhdap
      241 avsvpalpvr vvntigagda fmagmltwlg aeagwdpals agrtkamley avgtaasvca
      301 ragteptapl gv
//
LOCUS       WP_457658614             400 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces griseus].
ACCESSION   WP_457658614
VERSION     WP_457658614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=43641
     Region          30..396
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(35,63,259..260,284)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 mandikdiah aveaaavmgl faspprmltl gepthgvdap lrlrnalfrq lveregyrti
       61 aiesdcvagl lvddhvttga galdevleqg fshglgasaa nrelvrwmra fndgrpscdr
      121 lrfagfdgpl emayaasprh tltrlhrcla dhvdpdllpc taetldrllg addrwtepaa
      181 mldpsasfgr saearelrll addlgallda wtprliaets rdafdrarly artasgllry
      241 hfwmadtsps rlsrltglrd rmmadnllal aergpvlvha hnghlqrdms smrmggrrle
      301 wwsagsivea rlgeaygfla tafgtmrhqg vdvpppdtle galyalpeea glldasrlad
      361 aldatgpvrr tspyfgyapl dpahlaridg vvfmkdvpen
//
LOCUS       WP_457658615             169 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457658615
VERSION     WP_457658615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..169
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18530
     Region          24..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msgtegpmsg tggheddeel rwldeqekaa wtglislvll lpgklesplr qehgltlfey
       61 lvlshlseap grklrmgela flasgslsrl snvvkrceqr gwvarspdpa dgrytlaelt
      121 dagfdivrla apthlrsvrr tvldslnttd qkalvriaek lrivpndfg
//
LOCUS       WP_457658617             127 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces griseus].
ACCESSION   WP_457658617
VERSION     WP_457658617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..127
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13905
     Region          8..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 misvlqnvai dcanayqlar fwsgvtgrpl hpedgpgsre tqvllaegpv lhfnqvpeak
       61 tvknrihlcl rpdttrdrev erllelgatf vadhrnpdgs gwailadpeg nefcvlrses
      121 draamds
//
LOCUS       WP_457658619             415 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Streptomyces griseus].
ACCESSION   WP_457658619
VERSION     WP_457658619.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..415
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=44835
     Region          131..400
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mtdtsdtqpt eaeaeasrqn rlrrlmrylp liapvllwtv pcwvllyggq hwppavalag
       61 talfvlglvg mplamvrghg rrqqdaaaii gdtllgacwv lftwsvlfgv llrlvltvag
      121 vaesqdrari vtwavlgvsa allawgyaea rrvprvrrld vrlprlgagl dglrvvlitd
      181 thygpldrar wsarvcetvn sleadlvcht gdiadgtaer rraqavplgt vqatrarvyv
      241 tgnheyysea qgwvdlmgel gweplrnrhl llerggdtlv vagvddvtae ssglaghgah
      301 lagalsgadp dlpvlllahq ptfvdraaag gidlqlsght hggqiwpfhh lvridqpala
      361 glsrhgartl lytsrgtgfw gppfrvfaps eitllvlrsp rqtdgeaqtg rvrae
//
LOCUS       WP_457658620             522 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658620
VERSION     WP_457658620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..522
                     /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=56094
     Region          154..493
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mntaeprrrw wprsvrarta lavastaavi lvaigwwlhh dvyrqsaria edqardplla
       61 ladqlregvi psrrsavpye vvatgrgtpv asgggmdvfa pgarpvlpap palsepvdtg
      121 sgwyyttidm ripertaddp tdgfdlagrt ypvlytdiwa gelssaeaaa lgvdadatlr
      181 vhvvvlphta eaithnmdll llraglvslv lisavtyftv rnalrpveai rvitasvtan
      241 dprervtvpa tgheiaalat tinttlqrld eaaarqrrfv adaahelrsp lttllaslev
      301 alaypertdw pgavataarq tgrlqtlaed llllarldsh apttaggsid laalvrrlve
      361 eyeqpgrpva ltadasgpay vhgspgdher llrnlvdnaa rhavnrvrvt vrnqdeqvvl
      421 svhddgpgvp aeeaerifer fvrrddarsr dhggtglgla iarelahrhr gtldlvpsdr
      481 gacfrlrlpa qrqpdspvdg gpeatgysap dvspadegtg er
//
LOCUS       WP_457658621             503 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 39 protein [Streptomyces griseus].
ACCESSION   WP_457658621
VERSION     WP_457658621.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  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 503)
  AUTHORS   Ernst,J.F. and Prill,S.K.
  TITLE     O-glycosylation
  JOURNAL   Med Mycol 39 Suppl 1, 67-74 (2001)
   PUBMED   11800270
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 503)
  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 503)
  AUTHORS   Gentzsch,M. and Tanner,W.
  TITLE     The PMT gene family: protein O-glycosylation in Saccharomyces
            cerevisiae is vital
  JOURNAL   EMBO J 15 (21), 5752-5759 (1996)
   PUBMED   8918452
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474915
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..503
                     /product="glycosyltransferase family 39 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53076
     Region          31..354
                     /region_name="COG5305"
                     /note="Uncharacterized membrane protein PF0508, contains
                     N-terminal glycosyltransferase domain of PMT family
                     [General function prediction only]"
                     /db_xref="CDD:444104"
ORIGIN      
        1 msldvrapav pttrtvpsrp saartpstpa ralaviapaa ltaalgvwgv rrqntmwgde
       61 avtyqlahre lsqiwntaqh vdlvhalyya vmrvifdlfg agllslrlps vlamsaaaga
      121 vgllglrlag prvglpaglv fpllpqvqky aqegrsyamv caliawatyv lvdnvprrsr
      181 wrwavygctm llacllhefa vlalaahgvt livsrppkgv lrawsvtaag vvigllplav
      241 vsagqseqvs wiggpvrpdh llvamvvgva caraaprgqg pvslaalavp mlvlpgalll
      301 taslvkplfv dryvlfsnig ialllgacld hvrrlprwsp avyvatvaal ialvplslsl
      361 rtpqsrsnda tavgaavrea grpgdgllyl sgrqrmltaa dpedtrllvd lalaqdpvas
      421 ntlagvelaa peiaarmref driivvravg vhapgdsqee akettlrrhf rvqgtaevng
      481 arvsvhvreg ssrpvrrsgg gsp
//
LOCUS       WP_457658623             267 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658623
VERSION     WP_457658623.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27925
     Region          15..250
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mterntqqdl rytdhfgprg pavrgtvlvv pgrgethdty arfgkrlaad ayrvrvvdaa
       61 rldaedpdgs ltrlggriad avagtadpdg avvhpvilvg adtgavavaa llgredgaga
      121 aglrpdavvl aglpahtsas ptgswddeld vrtfcpahrs tltddaafgr galdevvpep
      181 llaaayasea dvpvlilagd adpladrdal trtakslpra rlsvvrdahh dvlndmqhrs
      241 vaaeivtfle tlrnelvplv tvessaw
//
LOCUS       WP_457658624             299 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658624
VERSION     WP_457658624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..299
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31877
     Region          32..>282
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msplspdtlt srpadtdrpa adapdappae pvlalhdvri tdrvtdreiv hgvtfdltpg
       61 kavgivgesg sgktltcraa lgilpphfev sggridlags diatltprrw telrgatisa
      121 vfqdpasyln paikvgaqia evvrvkqglk rraarrrave llaavrlrdp elvygqypye
      181 lsggmlqrvl iaaaiavepr aliadeatta ldvtvqaeil dllaelrtrt glalvvvshd
      241 lavvaqlcde vlvlrqgevv eqgptravlh dpqhdytrll iaehdsygld kflapqgas
//
LOCUS       WP_457658625             296 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658625
VERSION     WP_457658625.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30737
     Region          28..265
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mvrrvlalts griavvilav iallallgpw lapqnplats dnalaaysgs hwlgtdylgr
       61 dvlsrlldgs risvlgslev alvalvvgav pgilsvylgr afewftlria dtlvalpfll
      121 faiaviallg ngitqamlvt galvsplfyr vsraatlava rspyveaaiv sgasigwivr
      181 rhvlakvlpp iavalaqtig vgfvivsslt flgigvqppe ptwggllasd lgylshrpwa
      241 pvapallimi tvwacnllad airdvsgeag ralandrkar anrraaagll paggsr
//
LOCUS       WP_457658626             330 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658626
VERSION     WP_457658626.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006587
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..330
                     /product="DsbA family oxidoreductase"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35174
     Region          35..259
                     /region_name="FrnE"
                     /note="Predicted dithiol-disulfide isomerase, DsbA/YjbH
                     family (virulence, stress resistance) [Posttranslational
                     modification, protein turnover, chaperones]; COG2761"
                     /db_xref="CDD:442047"
ORIGIN      
        1 mtdapertpp aaggatsrpp sarrtapged pppllevvey tdplcpwawg sepvfrrlra
       61 slagrvhwrr ayailfdddd dpppdpaaet awyarhladi gthtlaprah ilsrvaassw
      121 psslaakaae lqgpevadgv lrrlresvfv lgepadtpas alrcvqgvpg ldadrlarda
      181 assgvrqqvr adraearrpv pevlsvraes phpgtaketp ggeiryalpt llfrtpaghr
      241 avpgwrpfea yagavdalap gllrtappld pagaleryrs ltdperlvla egvwpppgav
      301 rvdtgqgplw lhpheaqlhp avtpdgsapr
//
LOCUS       WP_457658634             295 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457658634
VERSION     WP_457658634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..295
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30709
     Region          13..280
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msgptaravt ldadgvpisg llaepphgpp ravvvalhgs gmsagyfdnr agpglsllal
       61 gaelgytvls ldrpgygasa rqlplgqnla dqtgtlgaal aafrrshdhg aglfllahsn
      121 ggrlalstaa aehappdlig ldvsglgsml avgpgqlpgs gargawrrhw galrlyppga
      181 flegqrlvrp vpdlearetl lwprmyaala arvrvpvrft faeqeqwwrs deeavralla
      241 plagvpaevv gqpdaghnis lgraartyhl ralafleecl laresaapvp raaqt
//
LOCUS       WP_457658633             356 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658633
VERSION     WP_457658633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..356
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39042
     Region          32..353
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkfgivffpt vgpadksglq yfdealrlvd laeelgfdhv kmvehyffpy ggyspdpvtf
       61 laaaagrter vrlgtsatip afqhpvklag klamldnisg grvdaafgra flpdefkafg
      121 vpideskdrf vegvgaikrl wseedvvvdg rfhrfgpvtl lprpvqqphp pvfvttarsa
      181 escaeagrag hnlqsvpnvm steelqnrlg vyraewaasg rtpgteqihl sypcvmaedg
      241 eearakgryd dernstaird avaswadtrs daypgyeklv eatktshfek klsekkllig
      301 speqvrdqle qisawfgddi tislgvhsgh lsfedaattm rlmaeqvipk lkagra
//
LOCUS       WP_457658635             329 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces griseus].
ACCESSION   WP_457658635
VERSION     WP_457658635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..329
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34595
     Region          1..251
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 meplrigvlg cagiarrrml pafracpgte lvavasrdrl rsretaaeak ceavhgyael
       61 lartdidavy lplpaalher waraaleagk hvlgekpltt dpaatarlaa laaasglalr
      121 envmfvhhpq haavaqlvad gaigdvrsfr aeftvprlpd ddirydpalg ggalfdtgvy
      181 pvraalhflg dglelvgavl thgvphrsvd tagvallrda agtgvqltfg ldhgyrsrye
      241 ilgsagaltv draftppaga rplvrwergt gteqldlpah dqvlasvaef aeavrtgapp
      301 dpalfrqadl lariradarv vtgpagpar
//
LOCUS       WP_457658637             436 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658637
VERSION     WP_457658637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43950
     Region          9..359
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mgpgpvgppa vrrtpwplvc vlaatmlvda levsaavvsa pvvgdaldlt pavlfwlvgg
       61 faagfaavlp waaalgrrfg rrrvqlvala vfalasaasa aadsggwlil gravkggcaa
      121 ltaptglaii laavpdgpdr rravsgyalc gtagfcggll laglltgvdw rlvpalpvpa
      181 allllvlaar lvprdppvrr rarprgrpgr psagprvlwr crplrraalt aaafngayvv
      241 lllvtawqlh hrggwtplrt alvflpaaap aaltalwsar iavrlgpdrs aaagavlavv
      301 gcllvprdag aagsgaagll pasavlglaf llaftalhlq avdavpeelr paatafyqtw
      361 vqsgpvllta paaalvtaga digpalwlvt avaaagalva vtgllpsgpp gppstprprs
      421 shddpstlpy vrdggr
//
LOCUS       WP_457658640             776 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces griseus].
ACCESSION   WP_457658640
VERSION     WP_457658640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..776
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79574
     Region          22..774
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msahsattas tatgseagtt avelaiggmt cascaariek klnrmdgvea tvnyatekak
       61 vtyqgaevsv ddliatveat gytarppapp appassggng tetagaagta gpaaesaedd
      121 glttlrqrlv tavllsvpvi amamvpalqf dywqwlsltl aapvvtyaaw pfhraawtna
      181 khgaatmdtl isvgtsaafl wslwalffgt agmvgmthpf eltiarsdga gniyleaaag
      241 vtafilagry fearskrkag aalkalmelg akevtvlrdg vettiptaal qvgdrflvrp
      301 gekiatdgtv vegssavdas mltgesvpve vsvgdtvtga tlnaggrlvv eatrvgadtq
      361 larmarlved aqngkasaqr ladrisavfv pivialalat lgfwlgndag ltaaftaava
      421 vliiacpcal glatptalmv gtgrgaqlgi likgpevlet trrvdtivld ktgtvttgrm
      481 tlqtthttdt tteaevlrla galenasehp iaqavataat datgplptpe dfqnvpglgv
      541 qgvveghavl vgreqllaew eirlpaplae akkaaeaagr taitvawdge aravlevada
      601 vkdtsaeavr rlrdlgltpi lltgdnrava esvaaevgid evyaevmpqd kvdvvkrlqa
      661 egrsvamvgd gvndaaalaq adlglamgtg tdaaieagdl tlvrgdlnaa adairlsrrt
      721 lstirtnlfw afaynvaalp laaagllnpm iagaamafss vfvvgnslrl rtfkga
//
LOCUS       WP_457658644             211 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent F420 reductase [Streptomyces griseus].
ACCESSION   WP_457658644
VERSION     WP_457658644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..211
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21706
     Region          3..203
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mrigllgtgn varalahgwr aaghdvllgs rrpkertdlg lpaasldeta ahaealvnat
       61 pggvsvdllr sigapalagt llidvgvgls ddfsalthpn sslgeliqea fpltpvvktl
      121 ctmdsttmta pgeltepgtv flsgddaeak rttgrlltdl gwpessqldi ggittargqe
      181 hfaflfmgia ggvgshtfni kvvtrpsadt r
//
LOCUS       WP_457658643             111 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658643
VERSION     WP_457658643.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..111
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12178
     Region          29..>77
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mnhsrwklqh ereltsglge seesraerae irlamafaka vydrrkelgl sqkdvaerag
       61 ltqakisrie gadavptlll lrrlalalda slnialdenq eevafvahta a
//
LOCUS       WP_457658645             122 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Streptomyces
            griseus].
ACCESSION   WP_457658645
VERSION     WP_457658645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Jurenas,D., Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Biology and evolution of bacterial toxin-antitoxin systems
  JOURNAL   Nat Rev Microbiol 20 (6), 335-350 (2022)
   PUBMED   34975154
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Kamruzzaman,M., Wu,A.Y. and Iredell,J.R.
  TITLE     Biological Functions of Type II Toxin-Antitoxin Systems in Bacteria
  JOURNAL   Microorganisms 9 (6) (2021)
   PUBMED   34208120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Rocker,A. and Meinhart,A.
  TITLE     Type II toxin: antitoxin systems. More than small selfish entities?
  JOURNAL   Curr Genet 62 (2), 287-290 (2016)
   PUBMED   26597447
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Goeders,N., Dreze,P.L. and Van Melderen,L.
  TITLE     Relaxed cleavage specificity within the RelE toxin family
  JOURNAL   J Bacteriol 195 (11), 2541-2549 (2013)
   PUBMED   23543711
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Ramage,H.R., Connolly,L.E. and Cox,J.S.
  TITLE     Comprehensive functional analysis of Mycobacterium tuberculosis
            toxin-antitoxin systems: implications for pathogenesis, stress
            responses, and evolution
  JOURNAL   PLoS Genet 5 (12), e1000767 (2009)
   PUBMED   20011113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..122
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=14101
     Region          1..>83
                     /region_name="COG4679"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:443715"
ORIGIN      
        1 mhvievepev rdwlellpek hyrkveeyag llasmgtstp mpfsrplrdg vyelrptlng
       61 eatritywfa sehrivlltv frktrmreta qveravqart lceaehdpah ttytrgesre
      121 ts
//
LOCUS       WP_457658648             253 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457658648
VERSION     WP_457658648.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..253
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27553
     Region          9..247
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mstagtapvl rmeavrksfg tslvlrdvdl avaphtvtal igasgsgkst llrcanllee
       61 vddgaiwleg eeitdprada davrrrigvv fqaynlfphl tvlqnitlap rrvhglsrtr
      121 aeaearelle rlglgakaee ypdrlsggqq qraaivrala vrprllllde itaaldpelv
      181 gevlglvrev kedgmtmvia themafarev adqvcfldag vvlergtpee vfgapreert
      241 qrflrrimea grl
//
LOCUS       WP_457658652             374 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            griseus].
ACCESSION   WP_457658652
VERSION     WP_457658652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 374)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..374
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39408
     Region          19..347
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msgvtihqva aaagvsastv snvlngrtdr mqaatlarve etierlsyrp nraarmlrtg
       61 rikviglivp svanpfwgsl areleaiala egyhvllcns erdparelky geelladgvs
      121 gvvlcsslps lehvepllsr glkmvafdrt aqagdppsla sisvdnamga elatrhllel
      181 ghrrlafvsg svnsvnrrer lrgfraaleg agldpadatv wpgadtsefg dkdaaelgrn
      241 aarellsgpr pptafvaind mcaigicrga kdagrtagrd vsvvgfddil ladlfepplt
      301 tvrqplpema aetfqqlrar iesapsagrs llirprlvvr estapvpgse pasadtgtpd
      361 aphavapdev aptv
//
LOCUS       WP_457658657             324 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces griseus].
ACCESSION   WP_457658657
VERSION     WP_457658657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..324
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35268
     Region          1..322
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mlfdmdlerl reyrpepqep adfdafwakt laeaarhdvd arfvpyetgl atvdvldvtf
       61 rswegqpvka wlmlpkqrsg plpavvqyig ynggrgipya wltwsafgya hlvmdnrgqg
      121 gggkntadtp digpeghgss spgfltrgie dphrhyyrrl itdavravda araheavdag
      181 rvavlggsqg gglalavagl rddvsaavad vpflchyrra sqitdsgpya eiarwlsghr
      241 frieeametl syfdgvnfaa rasapawfsv glmdrvcpss tvfaayhrya geaeievfpy
      301 ngheggaeyd lprklgalrg vfga
//
LOCUS       WP_457658658             539 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457658658
VERSION     WP_457658658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..539
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56684
     Region          30..539
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mpapqtpasr tsagqpatrg ssgpgapard rydavivggg hnglvaaayl aragqsvlvl
       61 erlgttggaa istrpfagvd arlsrysylv sllpdkivrd lgldfavrkr tvssytpavr
      121 dgrptgllva gegtresfaa ltggereyaa wqrfygmtrr vaervfptlt eplpgrdalr
      181 eriddadawr mlfeeplgva veenftddlv rgvvltdali gtfadahdts llqnrcflyh
      241 viggstgdwd vpvggmgalt dalagaaraa gaeirvqhea triesdtsaa evtvrtpdge
      301 hvvaarrvlv naspqalaal lgetppppae gaqlkvnmll trlpklrdrs vdprqafagt
      361 fhiaegygql adayrdaaag rlpaappsei ychsltdpsi lgpdlvargy qtltlfglha
      421 parlfaadnd aaraallkat laeldahlee pvtdclalda ngepcieakt pldlerdlrl
      481 pgghifhrdl sfpyaqegtg rwgvetahan vllcgagavr gggvsgvpgh naamaalgr
//
LOCUS       WP_457658659             383 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces griseus].
ACCESSION   WP_457658659
VERSION     WP_457658659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..383
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=39732
     Region          187..378
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(194,229,267,361,364)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(194,361,364)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(194,229,267)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msgrgparrg vlyaaaaaga aavattatda raagttgpar srwttswata qtaptptdpv
       61 ayngltdgdc tavlrlsagg avrlryantf gtapvlvgpv tadgrpvtfa grsqewlaag
      121 anltsdpvag lrvadgarle vrtrvpgptg plsfhrntha whtvdgvrtr svllltgvet
      181 tgargpvvav fgdsiaegvg tpddadlrwp dqlarrlpgs avanlgisgn rlllddvrfg
      241 pggqarfdrd vlglpglrtv lvhlgvndlq qppgqsgpdp vlsgyrqlal rargaglrvv
      301 gatitpfegw trwspeldav rerinravrt grifdgvadf daalrdpdrs srmlpahdsg
      361 dglhpgpsgh aalaaavdrr hll
//
LOCUS       WP_457658672             250 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces griseus].
ACCESSION   WP_457658672
VERSION     WP_457658672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..250
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26950
     Region          54..224
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(59..62,112..117,150,152..153,174,180..181,204,206)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(61..62,112,116,152..154,174,204,206)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mplsgmglaa alvtaltltl sgcsmdttap gsargeaasd akgsfgpvdc rkakcialtf
       61 dagpgkdtpr lldilkekkv hatffllgkh hvikhpdvvq riedegheva nhtwthqvlt
      121 drkpdeirae lektqlaiek itgkkprlmr ppqgrtddtv seiskdlgls qvlwsatakd
      181 ystndsalik erildqaskd giillhdiyk gtvpavpgii dalqkdgytf vtvpelmapa
      241 epepgtiyrp
//
LOCUS       WP_457658675             271 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658675
VERSION     WP_457658675.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..271
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26641
     Region          27..271
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msstasrvss gsssgplsgt apatlptglp praalvtggs rgigaaialr laqdgadvav
       61 tyvqdeaaar avvakiegfg rrgvalrcda adadaaadav hraadalgrl dvlvnnagig
      121 ilgpiaalag pdvdrtltvn vravflacra aaerladggr visvgsalsr yaggpgstly
      181 glsksaltgl tkplarelgp rgitvnviqp gavdtdlnpa dgplaegqra analgrfgtt
      241 eeiaslvayl vsteagfitg telvvdggha a
//
LOCUS       WP_457658676             304 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces griseus].
ACCESSION   WP_457658676
VERSION     WP_457658676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..304
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31067
     Region          17..295
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mpavapprra watdlpvlav avvwgasyla akvittthtv vavlvlrfai vlpvlvatgr
       61 rrlraltgaq wrgagllglv lsgifllety gvvhtsatna gliisltmif tplaeaavtr
      121 vrpsagfvaa aglsvtgvvl ltqgggftsp sagdllmlla alartvhvla marikavrna
      181 dslslttvql ggavavfavl aavpgtgalp wsaaadfgar ewaglvflsv fctlfaffvq
      241 mwsvrrtsps rvslllgtep lwaaavgisl ggerlgllga agavlvlagt awgrrdadle
      301 raga
//
LOCUS       WP_457658678             390 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457658678
VERSION     WP_457658678.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 390)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..390
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=42988
     Region          16..390
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,79..80,87,91,98,224..225,228,232..233,236,269,
                     274..275,278..279,281,304,331..333,336..337,339..341,345)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(60,73,75,78,80..81,163..164,173,223..224,227..228,
                     232,275,278..280,380)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mavldlrnlp dfivdpypyy aklraegpvh tvrteemeri wlivgyeear aaladqrfgk
       61 dwrtsgrwte sdaalsanml eldaphhtrl rrlvvreftp rriealrpri tevtaqllda
      121 mvprgsadlv dalafplpmt vicellgvpd idrdafrals ngivtptpeq readpvgamn
      181 tylvdliedk rrspgedlls alirardegg dslssaelvg mafvllvagh ettvnliang
      241 vralldhpeq lallradpgl ldnaveemlr ydgpvetatf rftrepvtvg dtviprdqav
      301 lvalasadrd parfpapdtf dirrepqghl gfghgihycl gaplarmear iaigallerc
      361 pdlardpsgg eldwlpgllm rgarglpvrw
//
LOCUS       WP_457658679             400 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457658679
VERSION     WP_457658679.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 400)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43329
     Region          20..400
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(57,64,84..85,92,96,103,233..234,237,241..242,245,
                     278,283..284,287..288,290,314,341..343,346..347,349..351,
                     355)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(64,83,85..86,170..171,179,232..233,236..237,241,284,
                     287..289,390)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mttpplidla algeqftrdp ypayaalrek gpvhrvripe gadawlvvgy eagralladq
       61 rlskhwsras palgvskvsa gssmlgsdap dhtrlrklva reftprrmer laprvqemtd
      121 glldsmlaap drtadlveal sfplpmsvic ellgvpfldr edfrtwsgqa vssldpalra
      181 sstqamtayi agllddkrek pgddllsali htadedgdgd rlsgeeligm awlllvaghe
      241 ttvnlitngv hnllahpdql aalradfsli dnaveeilrf egpvetptyr fttdpievgg
      301 tvipgggelv lvamsdanrd parypdgsrf ditrdarghi afghgihfcl gaplartear
      361 iairsllerc pdlrltadpa tlawrtgmlm rgplslpvaw
//
LOCUS       WP_457658681             250 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658681
VERSION     WP_457658681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces griseus"
                     /db_xref="taxon:1911"
     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=26256
     Region          51..231
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 miervvpegv araeafddal pglpdprela llrgrpeatv rrfaaaraca hqcldrlava
       61 pgpllrtaag gpawpagvvg sithcagyrg avaaraevwa algvdaepar plptglldlv
      121 atdperrmva glsrsspevp wdrllfsake svykawhpat grwigtlave vaftadglft
      181 arvrpertep pparrrpaat grgvprpvgg aypypgrwhv gggllltava vpgpanrrpg
      241 vsrptarlsv
//
LOCUS       WP_457658685             254 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457658685
VERSION     WP_457658685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>254
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          5..>252
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mrnrdadqea lcagmaqwgk ilseghiead arsafepdrw rsladsgvlg lpfpqqwgga
       61 gqsllttlhv letlgetcre sglnfcatts mastgvplta fgsdalrery lpgicsgeli
      121 gahaitepds gsdamamttr aerdgthyvl tggkafvsng piadvfvvya rtrpeggplg
      181 ttaflvdrdt pglavggtta kmglrtapls tlhldgcrip adrvlgrvgg gllvldhvmk
      241 reilfgftvq lgem
//
LOCUS       WP_457658691             154 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457658691
VERSION     WP_457658691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..154
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17091
     Region          9..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnatpcwltp eqqaawdgfi rmqekligrl srqvqadssm saadfivlak lteaggrmrf
       61 mdltklvewe ksrmshqvgr makrglvake ecpddgrgsf ivatpagyqa iegaapihve
      121 hvrrlfidal tedeldtltk isrrvvahle aqpd
//
LOCUS       WP_457658692             340 aa            linear   BCT 27-JAN-2026
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces griseus].
ACCESSION   WP_457658692
VERSION     WP_457658692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..340
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36059
     Region          58..333
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mqrtparrlt vlatigalll tgcgtkpaap eaerttasad grtiraqklm qltrthtetg
       61 mtllegpvfg kdgglyvvdv tapegkpkvi rvdvtrktsr avhtdgkgay tsaqfspydq
      121 rlylsdfahg evvslapggg dlrtffsgei dgarmnpddi vfdqegnlyv sdsrglsegk
      181 algrvvrigr eggqatilae nlaapngisf dadhrglwfs eltenrisyl rfdergavls
      241 rhtairvdag iaqtdsiavd adgnlyqglh graamavydr hgerlatvev psraeglesa
      301 tnvaitpggt kaymtvsgpa ggylytfdal aegirqsngg
//
LOCUS       WP_457658693             602 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces griseus].
ACCESSION   WP_457658693
VERSION     WP_457658693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..602
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=66433
     Region          81..544
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mtnphlpaph epaalreryr yererrvrld gaaqyrdada efgyyaadpy ikeprrrgpc
       61 hdtvdvavig ggfggilaga hlrqqgverv rfvekggdfg gtwywnrypg vhcdveshvy
      121 lpmldetgyv pewkyapgde irrhavriad afglytdtlf stgvtsltwe etsgtwivat
      181 drgdafraty vvnatgtltd pklpgipgie kftghtfhts rwdyaytggt pqggmtrlad
      241 krvgivgtga tgiqvipmla qdaahlyvfq rtpstvdvra nrrttaqdvg adhdgwargr
      301 renylrivsg entdhdlvad rwtasaglle kllpsfrrhg draafeaaye aadaakmnel
      361 rtrveqsvtd petaeklkpw yryackrptf sdlyypafnr dnvtlvdtad thgiehiteh
      421 gvtvgaatye ldclifatgf nvgtsaistg klpvhgrggt qllhawarrg prtlhgftsn
      481 gfpnlvhlga lqnassvnft hildeqarha aaliaaaeda aalieptpea edawtavlaa
      541 dapdhewfha ectpgyynre grgrpngpfa yphsavafha llarwraesi qeilrdrtgh
      601 ps
//
LOCUS       WP_457658694             226 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces griseus].
ACCESSION   WP_457658694
VERSION     WP_457658694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  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 226)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..226
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24097
     Region          11..126
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          164..224
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdseqrepvr vvivdddqlv rmalrlvidg epdltvvaea adgraaitvv deqrpdvvlm
       61 dvrmpvldgl satrellthp vpprvlmltt fdsddlvlga lragalgfvl kdtqpsrild
      121 avrtvadgnp vlspaatarv iaaatgpqss htrdasrraa rdrlsalter eretagaiae
      181 glgnpeiaer lhisvatvka htgslfskla vqnrvqvall vrdaee
//
LOCUS       WP_457658695             394 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658695
VERSION     WP_457658695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..394
                     /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=42016
     Region          133..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mntdgaprlg wwqqtwrlaa aavlsvpiwl yigvllhnqg vgpdpwfrig dplvalaclt
       61 vlpwrrrfpl avamtvtias tasalatgaa llalgsistr rrpveigavv layvtatqfv
      121 ggfypvqnpp gtfwfqlalp altagiavav gmaigarrve vrslrdraes aereqaaraa
      181 qarvlernri aremhdvlah rislvamqag vldhrgdlra eenrllvrgi aegshqalee
      241 lrdvlgvlra dpghpeppqp sldripdlva darasgldvt ltttvtgtpa davgrtcyrv
      301 vqegltnaak hapgarvhia vegrsgdglg vsvrnspatd rpaqrppasg fgllglterv
      361 dlaggtlhhc ptpdhgyvlt vrlpwpapth ekrt
//
LOCUS       WP_457658699             402 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457658699
VERSION     WP_457658699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..402
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43838
     Region          27..401
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrvllvgagg vgtaitriaa rrsffdhmiv tdydlsraea avaalgeeqa rftalrvdas
       61 dreavtallt eqrcdilvna tdprfvmplf eatlaagvdy ldmamslssp hperpyeecg
      121 vklgdgqfer aaaweeagrl alvgvgvepg lsdvfaryaa delfdtveei gvrdganltv
      181 dgydfapsfs iwttieecln ppvvwekdrg wfttapfsep evfdfpegig pvecvnvehe
      241 evlliprwve srrvtfkygl gdefidtlkt lhklgldrtd kvsvpggdvs prdvvaaclp
      301 dpaslgdrmh gktcagtwvk gtkdgaprev ylyhvvdnqw smreygsqav vwqtainpvi
      361 alelvangvw sgvgvlgaea ldprpfldll vaygspwglr eq
//
LOCUS       WP_457658696             491 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces griseus].
ACCESSION   WP_457658696
VERSION     WP_457658696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..491
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52746
     Region          94..>316
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          387..481
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrkslslala agavavaaam pgasaatpgt aragsdtvrw gpcpedvaap rlqcstldvp
       61 ldyrrpdgrr ieiaisrlas enpskrrgvl ltdpggpgga gldypavlaa sglpqevlds
      121 ydvigfdprg vgrsspvtch ltqeqqyrgn fapyahtaad vareagyart varqcatsrt
      181 awmlphitta ntardmdrir valgerkisy lghsygtylg avyttmfprr gdrvvldsnl
      241 gpggydvtam rlfargledr fpdfaefaaa rpeyglgstp eqvtakffdl akrlerkpvr
      301 gvdgtafrga tfehlyadal mphlaelwqa ldtdrplpps lplpanlenl maarfyvicg
      361 darwpgtvre yqrnaavdrv rypmlggsta sigpcafwpt gqveppvrig drgpsnvlmv
      421 qnerdpgtpl agarelrraf gqravmvtad qgghgvypfd dnvcangtvt rflmtgqrpa
      481 rdldcaaepg a
//
LOCUS       WP_457658705             403 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            griseus].
ACCESSION   WP_457658705
VERSION     WP_457658705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..403
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=42384
     Region          <127..379
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 maqkqtrkqr gvrhrsgaap gpdagtasvs rsrignwtlf gglvlltvlv vfldirtgnd
       61 lrvvpllvvv palasvycsl rqtiwvavwi ttvvvgfrvg adgtfwdflf gigfavlaca
      121 lgvaacaari rhatemarlr saavtlqrqi lrplpvvtgh vlahglyepi eedrfvggdi
      181 yevvespygt rviigdvqgk glaaigagfa aiaafreaai reptltgvve aledavvrhn
      241 vfsaqtgeae rfvtalvlgf dgsglveavn cghlpprllh dgrasavtlh rtyvplglag
      301 lsresrates fafppgatll vvtdgvtear dtagafypld ervgawagrg pselldalrv
      361 dledfsggvr rddiaalals hapvggggrs ettgedalrv vav
//
LOCUS       WP_457658707             635 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces griseus].
ACCESSION   WP_457658707
VERSION     WP_457658707.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..635
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66794
     Region          12..626
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mhpqrdraql amkdvskayg drsvldqvtl tvrpgektav igengsgkst llrllagaeq
       61 pdtgeitvrf pgstgylaqt ldldpsdtvq davdaalael rdlehrirea eaglsgrksg
      121 dpeptdaelt aygdlltaye drdgyraear teaalhglgl ahltrdrala tlsggeqsrl
      181 alacvlaaap elllldeptn hldaravgwl edhlrahrgt vvaithdraf lervtsvile
      241 vdrdlrtvtr ygdgwdgyrt akaaarrrwa qeheeyvadl arteelveaa garlaatgrd
      301 pkqgfgkhrr sheaklsgqv rsararldal rrspvppppr pltftgrptv ttatagaeha
      361 gstgstgstg stgstgstgs tgstgstgst gaagaagtte aagtagttea agtagipgta
      421 eatgtaeaad aigmpdrtrp lvelddvsvg drlrlpslrv apgarllvtg engagkttll
      481 rvlagdlapd tgtvtrhari gylpqelpar ptrrtllatf aagrpgfpde yadellalgl
      541 frpedlgvpv aslsvgqqrr lalarlvtrp adllvldept nhialslvee leqaldqyrg
      601 avvvvshdrs frsrftgdvl elragrqvgt vpapa
//
LOCUS       WP_457658706             267 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658706
VERSION     WP_457658706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..267
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26636
     Region          20..266
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mststdhsst paaapgsasd efagrtalit ggasgiglal arrlaaggaa vvvadydeen
       61 arkaaaeles sgaraaavam dvtdpasvea gvrfavdtfg alhlavnnag iagpssptga
      121 ypvedwnrvv atnlsgvfhs mryelpaiva agggaivnms silgtngfag spayvaakhg
      181 vvgltktaal eyagqnvrvn avgpgfidtp llrntdpaar ehlislhpag rlgtaeevae
      241 laafllsdka sfihgsyhlv dggysap
//
LOCUS       WP_457658709             730 aa            linear   BCT 27-JAN-2026
DEFINITION  Hint domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658709
VERSION     WP_457658709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Burglin,T.R.
  TITLE     The Hedgehog protein family
  JOURNAL   Genome Biol 9 (11), 241 (2008)
   PUBMED   19040769
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Perler,F.B.
  TITLE     Protein splicing of inteins and hedgehog autoproteolysis:
            structure, function, and evolution
  JOURNAL   Cell 92 (1), 1-4 (1998)
   PUBMED   9489693
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10051399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..730
                     /product="Hint domain-containing protein"
                     /GO_process="GO:0016539 - intein-mediated protein splicing
                     [Evidence IEA]"
                     /GO_process="GO:0016540 - protein autoprocessing [Evidence
                     IEA]"
                     /calculated_mol_wt=76954
     Region          470..611
                     /region_name="Hint"
                     /note="Hedgehog/Intein domain, found in Hedgehog proteins
                     as well as proteins which contain inteins and undergo
                     protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In
                     protein splicing an intervening polypeptide sequence - the
                     intein - is excised from a protein; cd00081"
                     /db_xref="CDD:238035"
     Site            order(470,543,610..611)
                     /site_type="active"
                     /note="protein-splicing catalytic site [active]"
                     /db_xref="CDD:238035"
     Site            order(470,540,543)
                     /site_type="other"
                     /note="thioester formation/cholesterol transfer"
                     /db_xref="CDD:238035"
ORIGIN      
        1 msqqnsasgd geprtgpvst tgpvhawwqr lsswqrialp agiltlviav iaaaalnsgg
       61 asegsratap dlqpfreavd glaeapglry kdtstlgite nditvtadgs qfgttssgrs
      121 dsgrdvlrig gkkftrwqvd paprktvaad ekappsewiv glddgselmd ealartvapp
      181 qlaavldkal adlekspppa ngsktpgtpg qrpltvngtp algidtsagr llvteekphr
      241 vlrleaydlr dgladmkdql engetpsapr tvttgplaag gaegmdltpv ladaadkmfd
      301 tlveyadqle datdrgitft ldgagemdcs adgctatqsf tgevtsiark ervtkgkvta
      361 vmgatftidg kpagectspq rtfpvrgnnv sgtlkcsnpa agplyasvaa rvqaqaqada
      421 drcgckvrlt yplrastlid aralakveaq klaaqakser dradcvkphs fpsgtqvlla
      481 dgttraiedi rvgdrvatsd prsasaatrp vtntfatdgd kdftritvtt drgpttvtat
      541 dnhpfwltdd qrwknagdlr vgdelrttdg tgvavtevrd qqgrhrthdl tvdelhtyyv
      601 lagrtpvlvh nnngcpphvt gkgddplvpe lvkdinaryp ghvraqgvdi vgangkaltd
      661 fdivtrnavv qvktgsgkga lkqalrtqsl tdypvivylp qgrgsviksl eqagimvtrd
      721 knvlldalap
//
LOCUS       WP_457658710             519 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Streptomyces griseus].
ACCESSION   WP_457658710
VERSION     WP_457658710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..519
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=54719
     Region          28..337
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mtgasdsvrv vvvwvpdfpv lacgtrdgap vavahrgavv acsasaraag vrrrmrlraa
       61 qarcpglrvv erdlaaevrm feqvvhrvea evvprlevir pgliaaparg aarywggeaq
      121 lsvrladtvt alglparvgi adstfaaala arrgdgvivp adgnaaflap ypvgvlgvpg
      181 ladllkqlgi rtvgdfarlp agrvaerlgt egvgahrvar ggqarpvsvr taaqdhtvrr
      241 lfevpeqqtd avvfvavala delherlaaa gvvcarveav vgtadgrtlt rifrhegrls
      301 sravaervrg vlaawsekgl ldaggtepgi rrlalrpdgi spdtgsqgaf dgerdtpvev
      361 eraaarvqav lghravtrii evggrgpgdr irlvpvgdvp ddgaramgae gapwpgrlpa
      421 phpaavypvr rparltgtdg apvgvagrle lsaepaflav dgrrragvng wagpwpvleq
      481 wwtrdsgrri armqvttddg hawlllvdrg rwwveahyg
//
LOCUS       WP_457658713             303 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658713
VERSION     WP_457658713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  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 303)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31100
     Region          <107..200
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msttvpssgp aapaaagpad taasagapdt heaaadsvya sdtparrgpl rtapwgadpy
       61 analrtgrgp lflrrsdgwl lpldverwcs dagsadlsal hrcegpvldi gcgpgrlvae
      121 laslghralg idvseaavar trglggaall rsvfdplpge grwgtlllld gnigiggdpa
      181 alldraadll gagglliaet apvdldervr vrlddgrggp dgrtapvaag devaepflwa
      241 rigtpallrh artggwrtad qwgaegrtfv slrrperers artssqsaes ansapvissq
      301 lpr
//
LOCUS       WP_457658714             253 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces griseus].
ACCESSION   WP_457658714
VERSION     WP_457658714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  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 253)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..253
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26958
     Region          23..191
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(26,28,99)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(52,98..99)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            97..99
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mtdssaalpf ppaphtglpk adivlpclde aaalpwvldr ipvgwraivv dngstdgsae
       61 larslgasvv teerrgfgaa chagllaaea efvcfcdcdg sldplllagf vrriadgecd
      121 lllgrrrpeg rgawpphara gnlalarmlr rrtglrlhdl gplraarrad llaldltdrr
      181 sgyplqmvvr asdaglrvae sdvpyrprtg kskvtgtwrg twhavrdmrg vlreppadrt
      241 pdsaapagtg alr
//
LOCUS       WP_457658715             367 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658715
VERSION     WP_457658715.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..367
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37858
     Region          2..346
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvlvtggag figshvvaal taaghesvvl dallpsahpg atppglpgdr vvvgdvrdre
       61 avadalagvd avchqaamvg lgkdfadapl yvgcndlgta vllaemaaag vrdlvlagsm
      121 vvygegrydc prhgtvrpgp raeadlrsgd fephcpdcga eltpglvaed apadprnvya
      181 stklaqehla aawaratggr avslryhnvy gpgmprdtpy agvasffrsa largeaprvy
      241 edgrqrrdfv hvhdvaaana valaavrerr pasfaayntg sgephtigem aaalaaahgg
      301 pgpvvtgeyr lgdvrhvtad sralreelgw rprvsfaegm adfaaaplrg aagrrdeded
      361 avtlsga
//
LOCUS       WP_457658717             265 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457658717
VERSION     WP_457658717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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
REFERENCE   2  (residues 1 to 265)
  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 10007540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..265
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29229
     Region          1..263
                     /region_name="YcgL"
                     /note="Predicted nucleotidyltransferase YcgL [General
                     function prediction only]; COG3541"
                     /db_xref="CDD:442762"
ORIGIN      
        1 mttaiddlla raglpvtdlr pdlehapgpl afatvsgahl ygfpsrdsdv dlrgvhvlpa
       61 edllglhepe etrtrmwerd gveldlvthd lrkfvrlmlr pngyvleqll splvvhtgpl
      121 hteltalspg vltrnhahhy rgfavtqwrl ygntgelkpl lytfralltg ihlmrtgevl
      181 ahlptliegt dapaylpdli aakaeaehgt attgpdeetl vrdvtelhrv ldeartrsrl
      241 pdavtvlqdl hdlvvrarla alrdv
//
LOCUS       WP_457658738             300 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658738
VERSION     WP_457658738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31417
     Region          8..>147
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdlvgacraf vsvseyggft dgaaaagmsq svasrrvaal eerfgeqlfe rtsrravltp
       61 fgrdmlaaag qlvqaadvll eeaeavkhkp wrlavpavcs asalarlvad arghgvrldl
      121 rtagparrre lvqaqqvrag llavpaegap wsvplglaga rdggvrriyv etlrlgrvaq
      181 gparrvwiqp eddvphirdp ltrlrdavgl rpaqvlaapd vtaaaaevlc sddlllcsra
      241 qaaelaltwh pigemtprrg yaltvvadgn plpmearlge aiarclgadd paaagggkaa
//
LOCUS       WP_457658740             332 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658740
VERSION     WP_457658740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34967
     Region          13..318
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtdarentvv paldvrdlsv rfrmrggrdi aavtdarfsv apgeclalvg esgcgksvla
       61 sallgllpan aattgsavlg gdtdlltade rtlartvrgr riglvpqspa ahltpvrtvr
      121 aqleeslrel tgvrgselrk aavaaadras fpdghldryp helsgglaqr aatalaligd
      181 apllladept tgldrdlver tvdelrrhtd egralliith dlaaaeriad rvavmyagri
      241 veiadaprff gapgprhpya kglldalper dfapipgmpp elgalpegca faarcayada
      301 rcteeqpafd adlachhalt grtyplkeaa da
//
LOCUS       WP_457658743             372 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457658743
VERSION     WP_457658743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..372
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37770
     Region          12..365
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mttpaqppat pdllysqdee dlrsavrall tdradaptvi aatesdmpyd pqlwaslagg
       61 igaagllvpe klggqgashr evavvleelg rsvapapylt ssvvatetll algaedgpaa
      121 allgelasga rtavlavpfa tppagadaal aapdgtvrgv adaaaadvll vptaeglyav
      181 evsdpgvavs plvpldltrp laavtltgaa gtlladadts atavrrglla gagllaseql
      241 giaewcltet vrytrerhqf nrpvgsfqsl khrmaqlwle vvsaraaarn aadalathsp
      301 daplavavaq aycsgvavha aeecvqlhgg igmtwehpah lylkrakads iaygtagshr
      361 qavaelaelp ap
//
LOCUS       WP_457658744             199 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658744
VERSION     WP_457658744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Rosinski,J.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 14302692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..199
                     /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=21678
     Region          18..91
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          107..181
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(112,114,126,129,133,167,169,181)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mkendrddpe leavltgvgp rlrrlrkdrg vtlaalsaat gisvstlsrl esggrrpsle
       61 lmlpiarahe vplddlvgat pvgdprvrak pivqhgrtml pltarpgglq aykliqepgs
      121 ggppeqrthe gyewlfvlsg klrlllaehd lvlgpgeaae fdtrlphwfg paedetvefl
      181 slfgpqgerm hvrakpkrv
//
LOCUS       WP_457658745             274 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457658745
VERSION     WP_457658745.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..274
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29407
     Region          11..271
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mstvptvtln ngvaipqlgf gvfqvpddet taavsaalea gyrsidtaai ygnevgvgra
       61 laasgipree lfittkvwna dqghdatlaa fdaslaklgl dhvdlylihw ptpahdlype
      121 swraleklva dgriraagvs nfqpahlsrl letgtlvpav nqvelhpglq qaelrafhae
      181 hgiateawsp laqgallkee tlvsiaerhg kspaqvvlrw hlqlgnivip ksvtperirq
      241 nidvfdfels dadmdavaal drgmrtgpdp dtln
//
LOCUS       WP_457658747             487 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658747
VERSION     WP_457658747.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48824
     Region          32..471
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mavmpdvsap vsappapari rpstwavvla actgqflvvl dvsvvnvalp smradlglsa
       61 aglqwvvnay siafagfmll ggraadiygr klmflvglgv ftaaslaggl aqegwqllaa
      121 raaqglgaav lapatltilt aavpegpart kaigtwmavg agggaaggli ggvltdalsw
      181 rwvllinvpv galvliaaal riaegragdr rridllgavl attglaavay givqteaegw
      241 taaatlvpll sgiavlvafv lveartavpl iplrvfsara vssanvsmll mgsatfsmwy
      301 fmtvyaqnvl gytplkagla liptsaavvi gsklaprlmv rtgakslava gvlitaagfg
      361 wqstmgvdgs yltaiclpgv lmmagaglas tplatlatsg aepgdaglvs glvntsrtmg
      421 galglavlst vaaartagsg daaevtagya lafrtasgvl lagvivmliw lpnhraprte
      481 rhpetvi
//
LOCUS       WP_457658749             737 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Streptomyces griseus].
ACCESSION   WP_457658749
VERSION     WP_457658749.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..737
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77419
     Region          14..372
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
     Region          369..733
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(454,484,486,517,519,715..717,719,721)
                     /site_type="active"
                     /db_xref="CDD:173841"
ORIGIN      
        1 mgrgtaigtg igiteehral ahsvrgwlar aappgevrkl ldahgpadtg vrpahweala
       61 aqgltgihlp eaygggggdl ldlavvleea aygslpgpyl atalvgavlr ravgpgtgdl
      121 lralaagdrt aafaltpgtl tatpapgghr ldgtappvlt geaadllllp aadasggvlw
      181 flvdagtdgl tvrphrsvdp trptaevrad avpvpahrnl pldatlvrdl aavllaadac
      241 gtaarsldta vahaavreqf grpvgafqav khlcadllvr leqaraltwd aaraaderpe
      301 vrgltaalaa atapeaaytc akdaiqilgg igftwehdah lqlrravlar qllgpadlhr
      361 lravrlaeag arreltlelp peaarhraea rphlaaargl aprearrala gtgyaaphlp
      421 apyglgagpv qqlaiqqesh eqgirlsdls vatwvvpsli aygteeqrer ylpatlrgdl
      481 qwcqlfsepe agsdlaalrt ravrtdegwr itgqkvwtsa artadhgill artdpdapkh
      541 rgltyflvdm rkargidirp lkeitgdslf nevyfddvll padavvgevg ggwrvardtl
      601 gnervhmadq mtfdsgletl iarsagldep vrartgalaa eahalgcigl rttlqqvsgr
      661 epgagasvrk lvqtrhqqkv aeltlellgp dgavdepaag gralhgflms rcltiaggtt
      721 qiqlnvvaer ilglprd
//
LOCUS       WP_457658750             514 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658750
VERSION     WP_457658750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..514
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52646
     Region          28..470
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide)-like multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17504"
                     /db_xref="CDD:341047"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,152,
                     155..156,159,283,286..287,290..292,295,329,333,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341047"
ORIGIN      
        1 mrrtqrirha eelpeprkar sgpivpvlaf agitvavmqt llvpvikdlp vllstdpana
       61 twvmtatlla gavstpimgr lgdlygkrrm llaslavmvi gslicastdd lvvmitgral
      121 qgfamgaipl gigimrdelp reklgsamal msssigvggg lalpaaalva qhadwhalfl
      181 gsaglgvlam altytlvpep plrapgtfdv igalglslgl vllllpvtkg gdwgwtsapt
      241 lgllaasvat lllwgrfelr tpaplvdlrt tarrevlltn lasimvgvaf yavslvlpql
      301 lqlptstgyg lgqsmvvagl cvaplgvtmm fvaplyaris arrgpkstlm lgmlviavgy
      361 gaglgllsaa wqtvliavvl gagiglayss lpaliigavd psetgaangl ntlmrsigts
      421 vssavigmvl antsvtmgsa qvpsmegfri sfliatgavl iglvlaaflp aqrpsahpvl
      481 lassaedaqa aedaraaeda rsvvsaperr taap
//
LOCUS       WP_457658759             276 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces griseus].
ACCESSION   WP_457658759
VERSION     WP_457658759.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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 276)
  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 276)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..276
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27534
     Region          36..276
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mprpvvralt gvlaltaaaa vlpfaspapa aadsvivggr papvadspwa valssrdrfg
       61 garsgqfcgg vavaptkvlt aahclsdeal ggpanrvkdl lviagrerls dsggqeipvr
      121 siwvnpaydp vsnagdlavl tlsralpkng vipmarggda ayragtaadv ygwgdttgsg
      181 tyasvlrsar vrvlpdsdca raypggqega ykasamvcag dpaggrdacq gdsggplvar
      241 grliglvswg sgcgragspg vytrvsaale waagri
//
LOCUS       WP_457658761             643 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces griseus].
ACCESSION   WP_457658761
VERSION     WP_457658761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..643
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=71286
     Region          22..637
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mptypasrds aespqlfspp eldrqiwdra aarllakmlg efayekiiep vpgpgtdglh
       61 rltlddggvl afaarrgvyg swrvdpdsie itarppaaap tdapsngtpa ttgsvdapsn
      121 gsatatgprp frdpltflar arellgldgt tlghlirelt rtlsadarld htaltadrla
      181 aldyaelegh qtghpwlvas kgrlgfsaad aarftpetrs plrlpwiavs triaqyrgvg
      241 rlttpgrlya geldrdvqda fakelrsrgh dprdylylpv hpwqwdewiv plfapaiadg
      301 divalhtdgd arlpqqsirt fanverperh tvklplsiln tlvwrglpte rtlaapavta
      361 wvqglcegdp flrdtcrvvl lgevasvave hplydhlpea pyqykellga iwreplpprl
      421 apgerartla sllhtdpagr aftaelaers glspetwlkr lfaallppll hflyrygtvf
      481 sphgenaivv fdendvpvrl aikdfvddvn isahplpehd ampeevravl lteepsfltq
      541 fihsglfvgv frylsplcee qlgvsedtfw slvraeivrh hgrfpelker felfdmltpe
      601 ierlclnrnr lhvdgyrdra srphaaihgt vpnplhpsar ire
//
LOCUS       WP_457658762             269 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658762
VERSION     WP_457658762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..269
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28511
     Region          106..251
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mppadasaet dasaepdaap vdhgsapaag pgsaersgsg agehnavedt ldlklteell
       61 aliaeerntg adrardrvpq ellgdpgawp paattagefa llpvrperdl pvlsrwmnep
      121 avaafwelag pesvtadhlg pqlegdgrsi pclgvldgtp msyweiyrad ldplarhypa
      181 rphdtgihll iggvnnrgrg vgttlirava dlvldnlprc grvvaepdlr ntpsvsafls
      241 agfrfsaevd lpdkraalmi rdrtyrdql
//
LOCUS       WP_457658766             428 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658766
VERSION     WP_457658766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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 428)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..428
                     /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=44861
     Region          162..414
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msadvpleep arrltgagga rdsdvwvrsl ppwdgyfavv wavtlavvlg aaepswpvra
       61 aaaaivalnl pwyvlvgrpa mlddsgsegp arryvvgall lflptamlvg etqlvtfala
      121 pqcfmllrlr dalwvlggmg avpfvgwtll whptagdaaf rlllavatfa fsaflgrwtm
      181 riiaqsrera aliaeleagr eeiarlstah galaererms reihdtlaqg ftsllmlsqa
      241 veselehdlp qarlhvalmt rtarenlaea ralvaggspa dlagnslada lnrltdrhta
      301 qtgapaaltv tggvrplpta yevvvlracq ealantrkha gpsapvavvl tyasdaltls
      361 vrdegcgfdp rapregygld gvraraeeag ggaairsapg agtsvtvtlp lppavpsaga
      421 tstpgrnl
//
LOCUS       WP_457658767             455 aa            linear   BCT 27-JAN-2026
DEFINITION  replication-associated recombination protein A [Streptomyces
            griseus].
ACCESSION   WP_457658767
VERSION     WP_457658767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..455
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=48230
     Region          10..450
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mepdlftaaa edrqekdpss splavrmrpr tldevvgqqh llkpgsplrr lvegsggpag
       61 assvilwgpp gtgkttlayv vskatnkrfv elsaitagvk evraviesar ratggfgket
      121 vlfldeihrf skaqqdsllp avenrwvtlv aattenpyfs iispllsrsl lltlepltdd
      181 dlrsllrral tgerglggav tlpedaeahl lriaggdarr altaleaaag aaiatgeaei
      241 sletveatvd raavkydrdg dqhydvasal iksirgsdvd aalhylarmi eagedprfia
      301 rrlmisased igladptalp tavaaaqava migfpeaalt lshatialal apksnaatla
      361 isaaqedvrk glagpvpahl rdghykgaak lghaqgyvyp hdvqggiaaq qyapdavrdr
      421 ryytptryga earyadvver vrerlgrsge sgeqt
//
LOCUS       WP_457658773             130 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658773
VERSION     WP_457658773.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..130
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13247
     Region          <11..>125
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(21..23,25..26,30,33,42,44,46,50..51,54..56,58..59,
                     63,66,75,77,79,83..84,87..89,91..92,96,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          44..75
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          77..102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msetpdpevv elatkvfdla ragdtealta yveagvpanl tndrgdtllm laayhghaat
       61 vaalvardad pdrandrgqt plagavfkge davidallvg gadpaagtps aldtarmfgk
      121 adllerfgar
//
LOCUS       WP_457658779             787 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 31 protein [Streptomyces griseus].
ACCESSION   WP_457658779
VERSION     WP_457658779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 787)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 787)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 787)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 787)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11605349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..787
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85021
     Region          160..285
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            196
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          268..712
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
ORIGIN      
        1 mdgrdlvrrv rlvgsvrglr tvrsawrrrs adaaalparg perarvpgal tgaepgpggg
       61 vvrfarselr irvsvggavf wawdgaeplp syavpgeapa pdpravlepd kdggwqvvse
      121 rltvvvsrtg avelrtpggl llrrelpprw wepvgggpvr wvqrsevpad arffglggra
      181 ggprlrdgvy glwntdpggr fgpeddplyl tmpvqvvvsd agthlafhdn swagrvvlre
      241 geegagsghd rpgtcevrme ggplrcwvva gtparvlqgw taltgapalp pswalgpqha
      301 rwgfggerev rrvvagyrer glplsvlhld idhfdghrvf tvdrerfpgl palakelred
      361 gvrlvsivdp avkaepgdav fdagrsvger gayvrdargr vvvgevwpga svypdftdpl
      421 vrdwwgslye erlaqgfsgv whdmnepvsf aafgdpslpr sarhalegag gdhreahnvy
      481 alamaragye gllrfrpeer pflfsrsgwa gmqryggtws gdvstgwpgl raslslvvgl
      541 glcgvpysgp dvggfdgfps pelyvrwfql gaylplfrth satgagrrep wefgpealea
      601 araalverer lrpyfvtlsh varltgapyv rplwwgapgd ralrecedaf llgdallvap
      661 vlepgarrra vrlprgrwyd tvtgrayegp gqvlvdapls rvpvlaraga vvpvrgadgg
      721 pelevwapap grtggglvvr dpgdgwaeae veryvtrweg drvvverdga eggvdcpvrv
      781 rgvaegv
//
LOCUS       WP_457658785             390 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces griseus].
ACCESSION   WP_457658785
VERSION     WP_457658785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..390
                     /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=40571
     Region          17..360
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msglvariea atpprrdrav dalralailg vvgghwlvta lvadsgtvrg asplahlpel
       61 tpvswvfqtl avfflvggvv aagswasark rgvpygawvg grlarlfrpv aavlvvwala
      121 aavmlvagvg estvralakl vwsplwfllv faaltaltpl varlhplwpl vvvlhvdlvr
      181 lglggprelg winvvagwlv pyclgamvar gglrgragrw gllsggasaa aglvlwagyp
      241 apmvgvpggr vsnldppsla avafglaqcg aallllgplr rvlrrpavwa vvavvnlsam
      301 tvflwhqtam iivtasalll adgplpglht vpddagwvva rllwlpvfal allgcwaafr
      361 gyeqggrrgg ggslvvresa perkgrarra
//
LOCUS       WP_457658792             442 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658792
VERSION     WP_457658792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  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 442)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..442
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=46865
     Region          183..426
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgavtssrav rlraavrrap ralyeevwaa padrvprmge pdapvwrpsl lvlliiaaac
       61 favprtnelv teasngvsgw avlaalaqsv vlvagmirpv gawwaatals vttvlvtepv
      121 mspdrlfpws imgmvfqgga lfllalrvpl rratgalalt llagmaltlh qtqrhnldld
      181 rsapvfvval vlgaalrslr larkdlvvqa eltaeerarr tlleernria relhdvvahh
      241 msvisiqaqv aphlvehpte elrenltgir enalealael rrvlgvlrse dapaqsarha
      301 pqpdldgida llatvrsagl avtvsttgap rplspgvels ayrivqeals nvmrhapgas
      361 aevvighrst gltvrvvntp pdrpatpsag vrhgllgmre raamlggdla tgptpdggwe
      421 vtailpagtg ttepdttted tp
//
LOCUS       WP_457658794             415 aa            linear   BCT 27-JAN-2026
DEFINITION  phospholipase D-like domain-containing protein [Streptomyces
            griseus].
ACCESSION   WP_457658794
VERSION     WP_457658794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   McDermott,M., Wakelam,M.J. and Morris,A.J.
  TITLE     Phospholipase D
  JOURNAL   Biochem Cell Biol 82 (1), 225-253 (2004)
   PUBMED   15052340
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Waite,M.
  TITLE     The PLD superfamily: insights into catalysis
  JOURNAL   Biochim Biophys Acta 1439 (2), 187-197 (1999)
   PUBMED   10425395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..415
                     /product="phospholipase D-like domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /calculated_mol_wt=46549
     Region          47..415
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 msataaeatd rpgpddragp ddrpglddrt ceerslrlrr rlerligiaa tegnalvplr
       61 ngdaifgaml aairgaehtv dlmtfvywrg diartfaeal adraragvrv rlmldgfgsr
      121 lieqdqldlm daagvtvtwf rkplylsplk qnhrchrkvl vvdertaftg gvgiaeewcg
      181 darnehewrd thvqvtgpav dglaaafaqn waechaelfd erdrfiaeeh hgdavvqvvr
      241 gsasfgwqdm qtlirvvles aeerirltta yfapdayftg llcdaarrgv eveillpgph
      301 tdkrvcqlag qrfyeeltgc gvkihqyqpt mlhtktltvd rvasligstn fnrrsldhde
      361 evmlavldrd ftatldghfe edraksvlie hgrwkrrdll qrareaavvp irrfl
//
LOCUS       WP_457658795             455 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658795
VERSION     WP_457658795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..455
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46632
     Region          8..70
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(14,18,43)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(17,42)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(24..25,36,39,43..44)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 matpeaehfa allkelkgrs grsygvlagr lhvststlhr ycngdavpne yapierfarl
       61 cgasgdelve vhrrwivada arrrtpagaa epvgvpdavp gggeaseppp vslepelsrv
      121 pelsvtsgga gpgsrwsrls rrtrlliava gvaallvpgt vvavdlagsg kegggsaadr
      181 vedaggdlaa apegsasgtp rpsaspspsg ssasasgsps gppsgkppag ggsgpgqsqs
      241 gggggtglga pptvtissyn weepcgqhyl vnqgpdkldp ppapqdrrgw aesyggveag
      301 nallqltvqg tsreavvlkr mnvrvlsrna plswsaykmg ngcgsgitpq tfaahldagh
      361 ptlrpvpgtq gdvevpavdf pykvtsedve vfnldmeavn ydvtwflele wssggnegtl
      421 riddhgkpfr lsgmkgrpey vyggpgygwe pagqp
//
LOCUS       WP_457658796             188 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces griseus].
ACCESSION   WP_457658796
VERSION     WP_457658796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..188
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21591
     Region          3..183
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mnrivtsisl sldgffegpd qdidwhtvde evhqhfndyf rtmggfvegr vtyelmeefw
       61 ptadqdpene gpmaefagiw rdmpkfvfsr tlesvgpnat llhevdpeqv rglrdaasgd
      121 lvvggsdlle sfrqadlide yriyihpvvl grgrpffrdt eerqmlrlme trtfvngvvl
      181 lryetvra
//
LOCUS       WP_457658801             401 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658801
VERSION     WP_457658801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41154
     Region          10..381
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,137,
                     140..141,144,216,219..220,223..225,228,256,260,309..310,
                     314,318,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtdaglrygr aslglsfgvq gvafallvtr ipaiqdqygi sdgllpvfla avpvlagags
       61 vatekvvarv rpgvvlrwaq plvllallgv gagrevwhva valgvfglav galdasmnml
      121 gvslqraygr simlgfhaay slggiagasl awvgarwdls lfvsylpvvv vllpaalags
      181 rwytegkgpa eearsggggs ggglsftlll plclvmtfay igdstvsnws akylqdvlgs
      241 seqlatvpyn vymvttllgr avgdlgvrrf gavavvrggs llaaggfavv alapgawvgm
      301 lgftmlgfgl cvivpqtfaa agrmfpensd aavarlnifn yvgfligspl vgalgdawsy
      361 rgamlvpmgl vlvtlvyara fgpdparygg gherartadv g
//
LOCUS       WP_457658802             261 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658802
VERSION     WP_457658802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29169
     Region          1..57
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          81..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mklvgkllar frieagmtqv elalaagvqe dtiasieqgr rslvpdlaet iddlldtkga
       61 latavdnmpe ydliplwaeh ylnmeheala lswydnqvip gllqtkayad avfsnkipvy
      121 speevetqta trlqrqqild rkkpptismv iwepvlmmkl tsdedhreql rhlyamaqlp
      181 gvclqvlpld srahaglngp ftlletpdhq hvaytetqrg shlisdrnei silaqkyaml
      241 raqaltpvet lrllarllge t
//
LOCUS       WP_457658807             311 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658807
VERSION     WP_457658807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34228
     Region          11..301
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtpsvrssar irigsapdsw gvwfpddpkq vpwqrfldev aeagyawiel gpygylptdp
       61 arladetrsr gltvsagtvf tglhhgpdvw drtwahvadi aaltramgae hlvvipsfwr
      121 ddktgevled rtltpaqwrd ltaqterlgr evrerfglri vvhphadthi dteenvnrfl
      181 datdpdlvsl cldtghyayc ggdsvkliet ygerigylhl kqvdpeilaa vvaeevpfgp
      241 avargvmcep pggvpalepv ldaaraldvd lfaiveqdmy pcppdkpfpi arrtreflrt
      301 cggtrspgpa s
//
LOCUS       WP_457658808             260 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces griseus].
ACCESSION   WP_457658808
VERSION     WP_457658808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..260
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27981
     Region          33..213
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mdrnvrtadd vlalmdglfa peadrwtagg aswwdafyad rskpvpffad kpdenldayl
       61 rqgwiapgra lelgcgpgrn alhlaslgfd vdavdlspaa ldwareraek agagsirfhl
      121 gdafaltaag aplagpydli ydsgcfhhlp phrrisylal lerclvpggh faltcfaage
      181 ggmgselpds elyltgglhg glaytddelr hvfsgltett etegmeevel rrmndeapgs
      241 plfgepflwt alfrrvagqg
//
LOCUS       WP_457658809             780 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces griseus].
ACCESSION   WP_457658809
VERSION     WP_457658809.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..780
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=80873
     Region          19..725
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 msevnrsapp svggwtrfvt arprlallaa lvitalavfa gsgvadrmgs ggwqapdaes
       61 tyatealare fpasqpnlll lvdsgsatvd dpavaaeaar lverleaeqg isgigsywgt
      121 qapalrsedg heaiiaarig gdektagetl driapafage rgpvtvsigg pvavqhemqt
      181 iiqedllrae lialpvtlvl lvmvfgsava amlplgvgiv ailgtnavlr glteftdvsv
      241 famnlttalg lglaidyalf ivrrfreela ggadprtavg ttlrtagrtv lfsaltvavs
      301 lsamlvfpqy flrsfayagi avvllaaaaa lillpaalvl lghrinsldl rrllrrhkkd
      361 tstegdfagt gtganagaga spgrgwakla alvmrrapvf avvttvglll lglpflgvkf
      421 gtaddrqlpa gaesrvvqeh irdgfpgspg gglevlaegq gspaeyadlk srieqlpgvl
      481 rvdgpvtads vayysvlpeg eavgeetqql vrdlravpsa asldtsvtgt aavlvdskda
      541 iadrlpwala iivvvtlllv flltgsvlip lqavvlnals ltamfgavvw vfqdghlsgl
      601 laftstgdie ttlpvlmfcv afglsmdygv flisrikeey drtgdhehsv tfglrhtggl
      661 itaaavilav vmvaigtsrv tntkmlglgi alavlmdamv vrsllvpavm klmgrstwwa
      721 paplrafhrr fglsegdaap agpaapetpg drggpggpgp taeveersga gaeiaeparr
//
LOCUS       WP_457658811             798 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces griseus].
ACCESSION   WP_457658811
VERSION     WP_457658811.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..798
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81928
     Region          15..797
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mastaaadhp aadaseaelm iggmtcasca arvekklnrm dgvtatvnya tekarvtfge
       61 glelgdlvat vektgytarp vtrperkapa aaapaaeaap apnaeakaka gaeaetetkp
      121 epepeaeaea eaardgvaep dastgsdslr qrlvvsavla vpvvllamip alqfdfwqwl
      181 sltlaapvvv wgglpfhraa wtnakhgaat mdtlvslgtl aafgwslwal flgdagmpgm
      241 rhgfdltvsr adatstiyle vaagvitfil lgrylearak rksgaalral mhlgakdvav
      301 lkagrevrvp agelvvgdrf vvrpgekiat dgtvvegssa vdasmltges vpvevsvgdt
      361 vtgatlnagg rlvveatrvg adtqlarmar lvedaqngka saqrladrts avfvpivial
      421 alatlgfwlg ndagltaaft aavavliiac pcalglatpt almvgtgrga qlgilikgpe
      481 vlettrrvdt ivldktgtvt tgrmtlqtth ttdttteaev lrlagaleha sehpiaqaia
      541 taatdttgpl ptpddfanip glgvqgtveg rtvlvgrprl ladaaiplpa elsealaeag
      601 rhgrtavvva wdgeargvfg vadavkdssa eavaelrtlg lrpvlltgdn ravaaavare
      661 vgidevhaev lpedkvnvvk slqaegrvva mvgdgvndaa alatadlgla mgtgtdaaie
      721 asdltlvrgd lkvtadairl srrtlatirg nlfwafgynv aalplaasgl lnpmiagaam
      781 afssvfvvtn slrlraft
//
LOCUS       WP_457658812             189 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457658812
VERSION     WP_457658812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..189
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20422
     Region          28..168
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtngpgadrr rrgadgpggv dgpgggdrea vrvdrvmdgl rafganytef trrfaawlgl
       61 hstdaaalve ilyaedqgtp lsparlserv slssgatail lkrleraghi vrtrestdrr
      121 vvtlrsspai rpramaffgp ysermaeamq ayspqeiqrf eqflgtlrst mdgllaneye
      181 nggptplap
//
LOCUS       WP_457658815             400 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658815
VERSION     WP_457658815.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41531
     Region          <158..358
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgestgpavm vlgalpslva vgtlgwavac rrvaarqrlg rlarpttvca vlsltisfal
       61 pqagsgwklv eaalllllva vvtrwsplre latalpaaal avtlwplplv tgesflesig
      121 igafwllpvv gavavgaypr rqelrrrrav aearstqrlq lsrdlhdfva hdisgivvqa
      181 qaarfvaatd pshavlaler iekaglsala amdrtvrmlh gpeaaatepl pglsrlpflv
      241 ndftaagate ayldlpptat ealsreagsa ayrivvealt nirrhapgas ratvvftpta
      301 ttveievtnd rgageasarr gsrgglgipa ltehaqalgg tlsagphgdg gwrltavlpa
      361 dvpavppavp pavrpvalpk dlpvelpedq pvalpkektp
//
LOCUS       WP_457658817             477 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 76 protein [Streptomyces griseus].
ACCESSION   WP_457658817
VERSION     WP_457658817.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Thompson,A.J., Speciale,G., Iglesias-Fernandez,J., Hakki,Z.,
            Belz,T., Cartmell,A., Spears,R.J., Chandler,E., Temple,M.J.,
            Stepper,J., Gilbert,H.J., Rovira,C., Williams,S.J. and Davies,G.J.
  TITLE     Evidence for a boat conformation at the transition state of GH76
            alpha-1,6-mannanases--key enzymes in bacterial and fungal
            mannoprotein metabolism
  JOURNAL   Angew Chem Int Ed Engl 54 (18), 5378-5382 (2015)
   PUBMED   25772148
  REMARK    Erratum:[Angew Chem Int Ed Engl. 2016 Feb 5;55(6):1949. doi:
            10.1002/anie.201511540. PMID: 26836331]
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008866
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..477
                     /product="glycoside hydrolase family 76 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50803
     Region          144..474
                     /region_name="COG4833"
                     /note="Predicted alpha-1,6-mannanase, GH76 family
                     [Carbohydrate transport and metabolism]"
                     /db_xref="CDD:443861"
ORIGIN      
        1 mlgalpavan pastavpapg aaaevcnkhc dardpasata drvpvhasvh grsialhlsd
       61 ndvmgwasid dgaagdetwl drsfdggrtw asgsklgats vpsgrtgwrs qmynvddwnt
      121 ggigalracg kagdrseiac tgwarvnwna gsrstaaata lmmnydrnsg kfagwwtsat
      181 altslidnir ishmpsytya isntyeklig aeggdftnsy lddtgwwgla wvaaydltge
      241 qryldtarkd adhmaaywtg tcgggvqwat dkpyknaitn elyiqlsaal hnriagdtty
      301 lrraedgwnw fkgsgminsg ntindglsen sdgtcsnngd ttwtynqgvv laalaelnra
      361 tgdaslldsa rtladastts sylnpggtlh epyepdsdct tdgdsfkgay arglgilnka
      421 lpdrpysayl drqadtahek nrnsldqyga hwagpltrtg ngcqhsaldl mnaaqdr
//
LOCUS       WP_457658819             617 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces griseus].
ACCESSION   WP_457658819
VERSION     WP_457658819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..617
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=61785
     Region          325..616
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mddgkptgpq akwwsrpsaa gpaaedrtpa aedrepvaed rgpavedrep aarsqipapv
       61 pvpvpaqpsd gsgrpdehgq evpgprpsgq plhepdeyst ppyggpgpwa pappvqrptp
      121 ahgtvvppga ggpppqyaap naagpqapap aaapppqpap adafappqga tpaggftpph
      181 arpadafaap qpapndafap ppphphpgpa apaqqqhtqw lqydpwgapg qpltrpgppe
      241 gmepggrkkr rggafmgvll ltlvasgigg gvgayierng glttvelpqa trdsgdrape
      301 svagiaasal psvvtlhvsg taesgtgtgf vldgqghilt nnhvvapags sgditvtfss
      361 getasaelvg kdsgydlavv rvrgvsglkp lplgnsdnvq vgdpvvaiga pfdlsntvts
      421 giisakqrpi taggekgdgs disyvdalqt dapinpgnsg gplvdtqahv iginsairaa
      481 dsgrgpeagg qsgsiglgfa ipinqgkrva eelistgkat hpvigvtldm kytgdgakvg
      541 tkgadgtpav akdgpadkag iksgdvitqv egqrvhsgee livkirahrp gddldlkltr
      601 ggkertvtlk lgsasgs
//
LOCUS       WP_457658822             194 aa            linear   BCT 27-JAN-2026
DEFINITION  suppressor of fused domain protein [Streptomyces griseus].
ACCESSION   WP_457658822
VERSION     WP_457658822.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Das,D., Finn,R.D., Abdubek,P., Astakhova,T., Axelrod,H.L.,
            Bakolitsa,C., Cai,X., Carlton,D., Chen,C., Chiu,H.J., Chiu,M.,
            Clayton,T., Deller,M.C., Duan,L., Ellrott,K., Farr,C.L.,
            Feuerhelm,J., Grant,J.C., Grzechnik,A., Han,G.W., Jaroszewski,L.,
            Jin,K.K., Klock,H.E., Knuth,M.W., Kozbial,P., Krishna,S.S.,
            Kumar,A., Lam,W.W., Marciano,D., Miller,M.D., Morse,A.T.,
            Nigoghossian,E., Nopakun,A., Okach,L., Puckett,C., Reyes,R.,
            Tien,H.J., Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T.,
            Xu,Q., Yeh,A., Zhou,J., Hodgson,K.O., Wooley,J., Elsliger,M.A.,
            Deacon,A.M., Godzik,A., Lesley,S.A. and Wilson,I.A.
  TITLE     The crystal structure of a bacterial Sufu-like protein defines a
            novel group of bacterial proteins that are similar to the
            N-terminal domain of human Sufu
  JOURNAL   Protein Sci 19 (11), 2131-2140 (2010)
   PUBMED   20836087
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Merchant,M., Vajdos,F.F., Ultsch,M., Maun,H.R., Wendt,U.,
            Cannon,J., Desmarais,W., Lazarus,R.A., de Vos,A.M. and de
            Sauvage,F.J.
  TITLE     Suppressor of fused regulates Gli activity through a dual binding
            mechanism
  JOURNAL   Mol Cell Biol 24 (19), 8627-8641 (2004)
   PUBMED   15367681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..194
                     /product="suppressor of fused domain protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /calculated_mol_wt=20679
     Region          29..189
                     /region_name="SUFU"
                     /note="Suppressor of fused protein (SUFU); pfam05076"
                     /db_xref="CDD:461543"
ORIGIN      
        1 maeilalvea rlisalgepd aradvtflgt drievlrfld gdivryatlg msgqpmadpt
       61 spladpvkgp raelilsvrg gladtdqvlr plavlaaspq veglivaaga sldlgeplwt
      121 gapftsvlva esgglvedle ldepmdpvrf lpllpmtrne aawkrvrgaq elqerwlthg
      181 tdvrdplrts vpld
//
LOCUS       WP_457658823             412 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658823
VERSION     WP_457658823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42175
     Region          23..346
                     /region_name="MFS_YfmO_like"
                     /note="Bacillus subtilis multidrug efflux protein YfmO and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17474"
                     /db_xref="CDD:341027"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,150,
                     153..154,157,225,228..229,232..234,237,261,265,314..315,
                     319,323,338,341..342,345..346)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341027"
ORIGIN      
        1 mreadpfdeg atgagilrqp kavwatagas vvafmgiglv dpilpsiarg ldasasqvsl
       61 lftsyflita famlvtgfvs sriggrrtll aglalvvvfa alsgtsssva elvgfragwg
      121 lgnalfvsta lavivgaaag gsavaillye salglgmacg pllgallgda swrypffgta
      181 almaigflci aaflkeqpkp avktslldpv kalghgglas vaasaffyny afftilaftp
      241 fvldmtpyks gavffawgll lavfsvlvap rlqrrfgslk vlgaslvlla adllvlgygs
      301 hgtaivativ sgafigmnnt vftelalgvs daprpvasag ynfvrwfaaa aapflapkie
      361 ewtdlhipfv vaalaalvga avvgvrrtal theaeepapv haqedgvaaf ad
//
LOCUS       WP_457658824             288 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658824
VERSION     WP_457658824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30136
     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 vgghkqaida lpegltlvtg
       61 aelscrvdgv gmhllaylfd padtelerar elvrddrvpr aqemvrklra ldvpitweqv
      121 ariagdgsvg rphvaaalve lgvvrtvsda ftpewlgngg rayaekhefd pfeavrlvka
      181 aggvavfahp aaakrgavvp estiaalaea gldgvevdhm dhddpararl rglardlgll
      241 ttgssdyhgs rktvelgact tdpeiygeit rratgafpvp gaggagrr
//
LOCUS       WP_457658826             271 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457658826
VERSION     WP_457658826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..271
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27615
     Region          87..266
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 maftratgkh rapsrltrrs aqaagiaala ttgvigslss palaadteta riadtgltqa
       61 isldatladq idaqaqaqkq qaeavarakt kaaaeareka akakakaeaq rkaearakei
      121 reekaraara aerarlnafh lpvagshvtt gyktggslws sgshsgvdfm aasgssvvav
      181 gagtvveagw ggaygnnivl rmsdgtytqy ghlssigvsv gqsvssgqqi glsgstgnst
      241 gphlhfeart tpdygsdmdp vgylrshgln v
//
LOCUS       WP_457658833             579 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein/permease [Streptomyces
            griseus].
ACCESSION   WP_457658833
VERSION     WP_457658833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 griseus"
                     /db_xref="taxon:1911"
     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=60334
     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 antarrplgl atallaavta thlaqavlla lvlsriaqgq taalapllta
       61 viavvlvrag lgraqrlaav tagatvrvgl rdtllrrlga lgptaitgar agavratlvd
      121 gvegvdayis rylpqslvtc avpplllvav alvepyaala lgpalllalf gprwwdrlla
      181 rrgrehwdsy ealaadylea lqgmptlrta gavgrvrerl errsaalhrt tvaklrvslv
      241 dtgltdlavq ggtvaavlva cssaatgrta atgtylllll asecfrpvrd lsrewhagyl
      301 gvsaadgiaa lrtaeaavpd rgtraavwkn apeirfedvh fthpgstrpa ldgvsftaap
      361 grttavvgps gagkstlvsl llrqrdpdrg rltvagtdta aytlaslrrg iavvsqetyl
      421 fhatiaenlr iarpaatdeq lraaartagi dqeiarlpdg yatlvgerga tlsggqrqrl
      481 alarallada pvlildeats avdergqtri vreltaagrg rtcvvvahrl davrhadhiv
      541 vldagrvaaa gdhttllagg gvyaslvaag rtaqeeraa
//
LOCUS       WP_457658834             821 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces griseus].
ACCESSION   WP_457658834
VERSION     WP_457658834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 821)
  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   3  (residues 1 to 821)
  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   4  (residues 1 to 821)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..821
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=87279
     Region          37..261
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          251..693
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          704..817
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 masadegspa epgplpsgdg rgpastaada aaviagdgtv igwtrgaeal lgypaaevvg
       61 rsaarlltgp pdprrtaava arcragsgws glvplrnrdg rsldidvrat asfpiagqeg
      121 flvsgreltp hwtmggsvld dfltrspvgm avldpelryl wlndtlerfg gvpreqrlgr
      181 rpgevlpgal aapierlmrq vlstgeavtd yeylgwswad phrrrayass ffpladaqdr
      241 rigigyvvld vtdrwnarrl lalvneagaa igstldvhrt aqeladfavp rfadfvfvdl
      301 letpfggdrp gaaapaeger pamrraglss vregcpeavv rvgeavdfvp pphdahflld
      361 gapvllpvld pdghgwtveq paraarlref glhslisvpm rardtvlglt tfmrsqnpvp
      421 fdeddvapar elvaraavcv dnarrytreh taalvlqrsl lphtlrggta ldvassylpa
      481 dakdgvggdw fdviplsgar vglvigdvvg hgigaaatmg rlrtavqtla dmdlppdell
      541 arlddlvlrl seeepatgpv erggttvvga tclyavydpa sgcctmarag hpppvivtpd
      601 gavsfpdlps gpplglgglp fesqeielpe gsllglytdg liegtdkdme sgmgrlgrav
      661 srgglpledl cpavvkellp vpqpddiall larthilspe hlvswevpvd paavgetrak
      721 vsrqleawgl telsmtteli vselvtnair yasgpvrlrl lfqsaltcev sdasntsprl
      781 rharttdegg rglflvaqla hrwgtrytpr gkiiwaeqpl p
//
LOCUS       WP_457658835             409 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 26 protein [Streptomyces griseus].
ACCESSION   WP_457658835
VERSION     WP_457658835.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Kaira,G.S. and Kapoor,M.
  TITLE     How substrate subsites in GH26 endo-mannanase contribute towards
            mannan binding
  JOURNAL   Biochem Biophys Res Commun 510 (3), 358-363 (2019)
   PUBMED   30717976
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,X.X., An,X.M., Gui,L.L. and Liang,D.C.
  TITLE     From structure to function: insights into the catalytic substrate
            specificity and thermostability displayed by Bacillus subtilis
            mannanase BCman
  JOURNAL   J Mol Biol 379 (3), 535-544 (2008)
   PUBMED   18455734
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..409
                     /product="glycoside hydrolase family 26 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45034
     Region          25..332
                     /region_name="ManB2"
                     /note="Beta-mannanase [Carbohydrate transport and
                     metabolism]; COG4124"
                     /db_xref="CDD:443300"
ORIGIN      
        1 mpakrrlivs ciaaaalsll agggiagqsp pgtdsvdsaa pgppgsgsgt ahgayldygp
       61 agvsrmaels rwlggaelrv ghtylpgdlw vniegtpdfl dawadwkrad edrmfvlnvp
      121 mlerneervp drevrgllra gasgeydqhf tklaerlvel gvpdtvivlg wemngttyth
      181 rcgpdptswk aywerivtam ravpgqefrf dftpsrgrda vpwtecypgd dvvdiigmds
      241 ydqppgetfd dqvndpyglq khvdfaaehg kpisfpewgl frngdnpeym rrmlewidrh
      301 eplyqtvtdy cphgvwqcrs nprsskvfrt mmtemaapaa papsptptpt ptptdpapsp
      361 tvppaaqpsp vtptppgtgt pptrrwcvtv pfgdwlgqwl kerkicfry
//
LOCUS       WP_457658837             582 aa            linear   BCT 27-JAN-2026
DEFINITION  murein biosynthesis integral membrane protein MurJ [Streptomyces
            griseus].
ACCESSION   WP_457658837
VERSION     WP_457658837.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     gene            1..582
                     /gene="murJ"
     Protein         1..582
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=59646
     Region          81..565
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 msesgtgtet garpadpaav ppplpasapa ppllpapgag pegplspgaa pgtesgeapr
       61 lgsflaraaa atavltvlga vlglvrdqai aryfgasdas dafliawtvp emaatllied
      121 gmalllvpaf slaltrraea gktpgsdpvr dlvaatlprl flllsggaal liagapwvvg
      181 vlapgladpr lavdctrlta vtvltfgitg yfsaalrahr sflppagvyv aynlgiigmt
      241 lalhsvwgvr aaavgvavgs almiltqlpm flrlvplarp rlprlgrpgr ravrtapllg
      301 favlapvvlf vvsrqsqvlv erflastlpa gaishlnyaq kvaqmpmvls lmictvtfpv
      361 vaqamaagdr ekarlrverd lalagmvvll gtavvlgyap qiievlfqrg afdvadtdst
      421 aqvmrvyalg llghclvgal srpffssgrp twfpafamgt gllvtmgagy altyrfgvdg
      481 iatanaigis ttallllmgl gtrvvpirtp avalslgrlt gaslaagaag wacaplvpdp
      541 vlslaagcll vpavfflsgl alrspevvsl laltrrrfld gr
//
LOCUS       WP_457658838             457 aa            linear   BCT 27-JAN-2026
DEFINITION  O-antigen ligase family protein [Streptomyces griseus].
ACCESSION   WP_457658838
VERSION     WP_457658838.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..457
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O-antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=46406
     Region          180..441
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 maavltrpap apssapravs rprrggwrsr wpllplvatv llpalpygvs gggggpavgp
       61 adlasgiavl lcvgrllylr rrplsaaaal vlglpvvgfa vatvtaadpa aalpglvryl
      121 qvfvlvpvav fllvedaygf rvvagalvll avvqgvtgvh qyvtgtgasy mgediravgt
      181 fgpsdimgma tvvaygllaa tacalrtpga apswlrpata vlavalivpl tlsfsrgvwi
      241 ataaavlaal alagrrqalt slavlgaagv vvvggfgigs emiadraasv trvtstpdrs
      301 vsdryamwsa agamwrerpa agvglkgfpd hrdghasigl ssgsdtagag qefrrqalls
      361 phnmyllvlg eqgligltal vgswaailvg avrrlrlars rghaamdcgl vavalmtwqs
      421 vnflyadigg pttvlsgvvl glaawwalae pdrvsaa
//
LOCUS       WP_457658839             493 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces griseus].
ACCESSION   WP_457658839
VERSION     WP_457658839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..493
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52532
     Region          55..489
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mtmesapvpg sgqatavqah tvhpprrsgg gaqvrpgerr tirygrsvpl lgvdalapav
       61 tfalvvpvsw pwllvaaqav vqvllfaqrg lyrmrlsssa lselpaltgl tllqwyvtme
      121 vldvwapqha igwavlayga gtqtaltcag raaayrarrr aavrrplstl vvgqgplarq
      181 vtaalydhpa yglrpvglva apaagdekqp agsdtvplpv lgspqevgra vvqnsvrhav
      241 ftappeatpd gaalftlltg hgcrvwlvtg pgavagppag grpdhlwgft aqplhdgsdr
      301 plghgvkram davlaavgll laapvmaaca lavrlsdgpg vifrqervgr hgrpfvllkf
      361 rtlrpadvqe satrwnvasd grmsrvgrvl rrtsldelpq lwnvlrgdms mvgprperpf
      421 fvaqfsrahp gyqarhrmpv gitglaqvng lrgdtsieer arfdnryiet wslwqdacvl
      481 artagslfrl ggs
//
LOCUS       WP_457658842             606 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658842
VERSION     WP_457658842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 606)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 606)
  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 606)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..606
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62028
     Region          28..604
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 maptpappft stppqtpapp saptpetgal rsllpvlgah ratvlrtcla alvdqaalva
       61 lvtlaaytvg tavtehrppa pgtiallagl vllralatwr emdlshdlay rvlaelrvrv
      121 fdglarsapa riagrrsgdl aatalgdvea leffyahaia qllasgvvfa vsaavlaalg
      181 pwlllavvpa allliwsplf eargraerga rtrsalaevs setvesvdgl rellmagaln
      241 rrrarlrsag rrlaraqrae qswetgagaa rdllvvaavi avvaaaahaa sagrldgawa
      301 paamalalga lapvaesaaa lgragglraa aarvraavha pagapapaap rpvppgplgl
      361 rlrglrfgyg ggavldgvdl tvrpgetval vgasgagkst cahllarywd paegavelvp
      421 rapahpvdlr dlteedlrat vsvvgqeapl fhgtlaenlr lgapdataqe vgavartcgv
      481 dviadalpdg ldtavgerga tlsggqrarv alargllsgp rvlvldetta hldhrgdael
      541 aralaadsat rttlviahrp atvrradria vleggrivee gtwdelirag gpltrlfare
      601 eatals
//
LOCUS       WP_457658845             287 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphodiesterase [Streptomyces griseus].
ACCESSION   WP_457658845
VERSION     WP_457658845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Tehara,S.K. and Keasling,J.D.
  TITLE     Gene Cloning, purification, and characterization of a
            phosphodiesterase from Delftia acidovorans
  JOURNAL   Appl Environ Microbiol 69 (1), 504-508 (2003)
   PUBMED   12514034
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Richter,W.
  TITLE     3',5' Cyclic nucleotide phosphodiesterases class III: members,
            structure, and catalytic mechanism
  JOURNAL   Proteins 46 (3), 278-286 (2002)
   PUBMED   11835503
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Imamura,R., Yamanaka,K., Ogura,T., Hiraga,S., Fujita,N.,
            Ishihama,A. and Niki,H.
  TITLE     Identification of the cpdA gene encoding cyclic 3',5'-adenosine
            monophosphate phosphodiesterase in Escherichia coli
  JOURNAL   J Biol Chem 271 (41), 25423-25429 (1996)
   PUBMED   8810311
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..287
                     /product="phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28953
     Region          5..236
                     /region_name="MPP_GpdQ"
                     /note="Enterobacter aerogenes GpdQ and related proteins,
                     metallophosphatase domain; cd07402"
                     /db_xref="CDD:277347"
     Site            order(10,12,48,51,78..79,152,191,193,213)
                     /site_type="active"
                     /db_xref="CDD:277347"
     Site            order(10,12,48,78,152,191,193)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277347"
     Site            order(21,24,27..28,31..32,51,54,63,156,158..159,186,188,
                     195..199,202..204,206,234)
                     /site_type="other"
                     /note="homohexamer interface [polypeptide binding]"
                     /db_xref="CDD:277347"
ORIGIN      
        1 mtlsvahlsd phittgpgav apaaglraal rrvlaldplp dcavitgdlt ergepgeyaa
       61 lreevgafpl plhlvagnhd apqalvevfg gtrflgggtl tsyvvehpal tvvvldsrva
      121 gapggrlgag qlsrldrtla rrpgvpalvc lhhppvpvgi pfldamglad gpalaevvaa
      181 yprvvrvlag hvhrpvtapf agstvavaps tyrqsglvlr eglpgypdep pafllhlrpe
      241 appgglpgts psarpgaspd aargaspgpg aawvthtvpt apaaprg
//
LOCUS       WP_457658849             409 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces griseus].
ACCESSION   WP_457658849
VERSION     WP_457658849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10993447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..409
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=41960
     Region          <27..161
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cl18957"
                     /db_xref="CDD:473128"
     Region          227..403
                     /region_name="TerZ"
                     /note="Stress response protein SCP2 [Signal transduction
                     mechanisms]; COG2310"
                     /db_xref="CDD:441884"
     Site            order(264,266,310)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mtamtpgsni plsaarvavd vaapvrldvs gllltadgkv rsdddfifyn qpsgpgvtyr
       61 sgggsapdai vvdtaavppg iekivvtasp datgqtfqgi eptatvrnad dgsalatftp
      121 pqlgaetalv vievyrrngv wkaravgqgy anglagiatd fgvsveepaa paappvpvap
      181 apvappappa aapvdpriap pappappaap aappvgsgki nldkgrvslq knqtvslvkg
      241 gapllsrvrm glgwepafrg kdidldasvi aygpnrnhld scyfgkltil ngaikhsgdn
      301 ltgegagdde tivvdlgrip aeatglvftv nsftgqkfne vakaycrlid dasgeelvrf
      361 dltgaepqtg vmmaklikqf tgewemtamg dfvksrtvrg mvkpaaqal
//
LOCUS       WP_457658850             269 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658850
VERSION     WP_457658850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..269
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28863
     Region          6..229
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtaprtvllt gaagglgtlm rgllpaygyd lrlfdlvpve depqaitadl ndrkalreav
       61 rgvdaiihla gislestfdk ilnaniqgth alyeaareeg vrrivaassn hvigytprpg
      121 pgdplipldt prrpdtfygl skcfgedlaq lywdkhgvet vsvrigscfp eptsvrmlsv
      181 wmspadgarl fhaalsaegv ghavvhgssa ntrlwwdlts aralgyapqd dsepyaakli
      241 aeqgeldpdn pahacvgghf ltdppiwph
//
LOCUS       WP_457658852             410 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658852
VERSION     WP_457658852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40569
     Region          20..378
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(28..29,32..33,36,67,120..121,123..125,128,148,
                     151..152,155,231,234..235,238..240,243,267,271,323..324,
                     328,332,348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mggvggsavg rvlrdrtagr clagvvvsgf gtsamwltag iwvksltgsn slaaltvcam
       61 wapvlagpal galadrmdrr allvrvnlav acllatlvlv dsagtvwlvf vvlvlygaag
      121 vlldaaeaal vartvpasll adfnglrmta negmklvapl agaglytrfg gpavalldaa
      181 tcalaalvfa rlpvrsplrd papaaarrge lavglrrira savlrplvaa gaatmllagv
      241 ngavtfayvd dvlgrgpaya gvlyavqgag svavgllvgp llrrlpervf aaggialfal
      301 gvgartvspd avalaasaai gcglpcvlia amtavqretp davlgrtaat agslmtapna
      361 valalgaglv avvdvrvlta vagaagvlaa vvlasgarrq hrrapvspqp
//
LOCUS       WP_457658856             172 aa            linear   BCT 27-JAN-2026
DEFINITION  SixA phosphatase family protein [Streptomyces griseus].
ACCESSION   WP_457658856
VERSION     WP_457658856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..172
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18851
     Region          9..170
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 msvetprriv llrhakaews qasdherpla ergrkdapva grrladsgid fdlalcssaa
       61 rtretwklav hefsqrprtv yeerlyeasl gelialfnet pdevrnllvi ghnpgmhgaa
      121 dalsgsadgd tlarmtrdgf ptaayavvel pgswksvehg agklteywtp nd
//
LOCUS       WP_457658859             447 aa            linear   BCT 27-JAN-2026
DEFINITION  S-adenosylmethionine:tRNA ribosyltransferase-isomerase
            [Streptomyces griseus].
ACCESSION   WP_457658859
VERSION     WP_457658859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Van Lanen,S.G. and Iwata-Reuyl,D.
  TITLE     Kinetic mechanism of the tRNA-modifying enzyme
            S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)
  JOURNAL   Biochemistry 42 (18), 5312-5320 (2003)
   PUBMED   12731872
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..447
                     /product="S-adenosylmethionine:tRNA
                     ribosyltransferase-isomerase"
                     /EC_number="2.4.99.17"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051075 - S-adenosylmethionine:tRNA
                     ribosyltransferase-isomerase activity [Evidence IEA]"
                     /GO_process="GO:0008616 - tRNA queuosine(34) biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47762
     Region          4..431
                     /region_name="Queuosine_synth"
                     /note="Queuosine biosynthesis protein; pfam02547"
                     /db_xref="CDD:460587"
ORIGIN      
        1 mrvpdglsar vpaeqrgagr ddvrllvsrg ravshrafre lpgelragdv lvvntsmtlp
       61 aavngrvgge rvvvhfstlg adgrwavelr apgaagvtgp rpggpagavv rlpggrtlvv
      121 eeplgpasra rlwwarvpep msmslsgprs vpqsvpgaes mpgpertrpv prpewrptsv
      181 pkrdpmpesr seaesaqglv pglvreseae eeeearsmrg pvpdsvpefl rrygrpiryg
      241 yterdqplsa yqtvfaapsp dgsgsaemps aarpftaalv aelvrrgvlf aplslhtgva
      301 saeaheppyp erfsvppata wlvnavraar ggdrttggrv iavgttavra lesaagadgl
      361 vrpvagwtdl vvtprrgvrv vdglltglhe prashllmle avagrealrl gyeaalqery
      421 lwhefgdvhl llrdeernap dcssnew
//
LOCUS       WP_457658862             164 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces griseus].
ACCESSION   WP_457658862
VERSION     WP_457658862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..164
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17655
     Region          18..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnpptdartd qapadpgatd dqlatqpigy wsgrvhadvt erlrdamari dvtqpqywvv
       61 ncvhggpdap sreevvsrlt pladgpheia rvvdqlthrg wlrtdagqrl hltdageaar
      121 vrvralatev ravvhegisd aeyvaalkvl rrmaanvegg sarg
//
LOCUS       WP_457658866             350 aa            linear   BCT 27-JAN-2026
DEFINITION  iron-siderophore ABC transporter substrate-binding protein
            [Streptomyces griseus].
ACCESSION   WP_457658866
VERSION     WP_457658866.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Braun,V. and Braun,M.
  TITLE     Active transport of iron and siderophore antibiotics
  JOURNAL   Curr Opin Microbiol 5 (2), 194-201 (2002)
   PUBMED   11934617
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Clarke,T.E., Tari,L.W. and Vogel,H.J.
  TITLE     Structural biology of bacterial iron uptake systems
  JOURNAL   Curr Top Med Chem 1 (1), 7-30 (2001)
   PUBMED   11895294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..350
                     /product="iron-siderophore ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0005524 - ATP 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:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37462
     Region          68..331
                     /region_name="FhuD"
                     /note="Fe3+-siderophore binding domain FhuD. These
                     proteins have been shown to function as initial receptors
                     in ABC transport of Fe3+-siderophores in many eubacterial
                     species. They belong to the TroA-like superfamily of
                     helical backbone metal receptor proteins...; cd01146"
                     /db_xref="CDD:238566"
     Site            order(114,132..133,154,238)
                     /site_type="active"
                     /note="siderophore binding site [active]"
                     /db_xref="CDD:238566"
ORIGIN      
        1 mslhrttlvk pwqrlaavls aatlgvglla gcgsdsaddk kkddapaaae gafpvtveha
       61 fgstevtkap qrvvtvgytd dqavlafgik pvgmvdqypn pagrtpdint qwpwvkdkwg
      121 dtrpevvmkn gdagpnfeki aslrpdliia vysevdkaay eklskiaptv grtkgekelf
      181 sapwqdnavh iakalgkeke gvelvkgiqt kldaakkahp efggqkaval swykdsisaf
      241 tstdvrgrlv tgtgftyqte idkvadggfs aelsperidl idvdrifvin dkadtdalkk
      301 felftnlpav kngkvsylld segpavgaam sqgtllslpy aidelvesvk
//
LOCUS       WP_457658867             352 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658867
VERSION     WP_457658867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..352
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35723
     Region          45..348
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvttaverpa pggttdirgr rlaglgvlav tlvaaaavsl avgaralspg evwhglftdp
       61 epdqklteir livqtvrvpr tvlavvagla lgvggaliqg ytrnpiadtg llgvnagasf
      121 avvsviavfg ftnpfqyvwf afvgagvagv vvfglasigr gagnpltlal agqgitvfla
      181 amttavaltd qkslnalrfw nagsvagvgf dviwpvtgfi avglvlalit lpalnllnlg
      241 ddvarglgvn iaasrtlgiv avtllagaat aacgpiaflg lmvahvaryl tgpdyrwlvp
      301 yagllgscvl lvcdivgrlv vrpgelesgv vvallgapff avlvwrgkfk ka
//
LOCUS       WP_457658864             566 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces griseus].
ACCESSION   WP_457658864
VERSION     WP_457658864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 566)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 566)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 566)
  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 566)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..566
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59363
     Region          16..560
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mktpdttrpr pgaailrtal rrnvgamiag tvlmglyqaa etafpialgl ivehtmqdrs
       61 lgslgvsigs laviittvsl swrfgmrvlq kantteahrw rvqvaacglq pvardvdlks
      121 geiltiated adqtadiiev vpllisslva vvvaavalsl adlrlgllvi vgtvailsvl
      181 avmskrigas tqeqqarvar agakvadlii glrplhgfgg nhaafgayrk vstdakrqai
      241 tvarvngtya gtalalnavl aaavsltagw lafegrisig elvmavglaq fimeplkmfs
      301 empkyvmmar asaermalvl nappvtapgp erpepggdle vddvrhgtlq gvtfsvrage
      361 fvaiaayqqr aaaelasvla mnvapqaygg avrvggrevg elsieavray llvnpydgei
      421 fagtlrtnid psgsgrsiae aveasmltdv valhregldh vvrdrganls ggqrqrlsla
      481 ralaadteml vlhdpttavd avteqliarn iaklrrgrtt lvltsspall daadrvlvld
      541 ggaitaedth rnllasdeay clavar
//
LOCUS       WP_457658868             684 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658868
VERSION     WP_457658868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..684
                     /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=70366
     Region          <95..566
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <379..680
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mgrargqgar aegpgrarlp lrrsllgrll avsalvaacs vaatawiavq ttsgaikqeq
       61 gqnltadari ydtlleyaar nptwdgvgat vrelaresgr rvalttqsrq pladsataat
      121 apalppqasa vvdplsvdtv laargtdgqr taadridpra vgpfrlstad stalrrtada
      181 evaclnragi asdvvvgasg rprvqivgnd peralgtrcd laaldtptrs eqkaldalta
      241 ladaclkrqg regvrlnndl swgdpaavev pgeagplspr pvpgpaprda pvteaepsav
      301 prertgendr aiascvgtar seqlssyvas pallfigdeg gatlpgfdls pantakiaga
      361 aalvlaltvg asvfagtrlv rpllaltgaa qrmrdgeqpa svpvsgddev grlaaafndm
      421 sahrarleeq rkamvsdvah elrtplsnir gwleaaqdgl adpdpafvss lleeavqlqh
      481 iiddlqdlaa adagvlqlhp epvgirells qvaaahqara enagvaltva vaatdpepal
      541 radpvrlrqa vgnlvsnavr htpeggrvtl sayasdasda sdasdasdgg gegdaegkac
      601 dgtvvievqd tgsgipaedl phvfdrfwra eksrsrrtgg sglglaivrk lveahggave
      661 atstegegst falrlpagpe psgp
//
LOCUS       WP_457658870             417 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces griseus].
ACCESSION   WP_457658870
VERSION     WP_457658870.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 417)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..417
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45499
     Region          29..416
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(63,70,99..100,107,111,118,248..249,252,256..257,260,
                     293,298..299,302..303,305,328,357..359,362..363,365..367,
                     371)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(70,92,95,98,100..101,187..188,197,247..248,251..252,
                     256,299,302..304,406)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mncphaeaaq adrnagviti dpmvqdldge tarlrdagvl aridllgvpa wtvtrhaear
       61 qllvdprlvk didawglwqs gvvtrawpli gmidagrsmf tvdgsehrrl rtktsqaltp
      121 rrleairpdi ekfteellda ldaaqgedgv vdlkavfaqp lpmkvvgmlm gvdesqhaml
      181 trqykaffsm ltpqderlsl laeldvfytd lvrektarpa ddltsalila eeggdpltee
      241 evvgnlkamv aaghettigl vlnavralls hpdqlrsvla geigwdavve etlrwdtptt
      301 hllmrfated lavgdevirk gegvvisyra igrdteqhgp dadafditrp trnrhmtfgh
      361 gphicpgaal srveagialp alfgrfpglr lavpdeeitk lpvmtqndma afpvllg
//
LOCUS       WP_457658869             433 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces griseus].
ACCESSION   WP_457658869
VERSION     WP_457658869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Manikandan,P. and Nagini,S.
  TITLE     Cytochrome P450 Structure, Function and Clinical Significance: A
            Review
  JOURNAL   Curr Drug Targets 19 (1), 38-54 (2018)
   PUBMED   28124606
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Guengerich,F.P., Waterman,M.R. and Egli,M.
  TITLE     Recent Structural Insights into Cytochrome P450 Function
  JOURNAL   Trends Pharmacol Sci 37 (8), 625-640 (2016)
   PUBMED   27267697
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Pochapsky,T.C., Kazanis,S. and Dang,M.
  TITLE     Conformational plasticity and structure/function relationships in
            cytochromes P450
  JOURNAL   Antioxid Redox Signal 13 (8), 1273-1296 (2010)
   PUBMED   20446763
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   5  (residues 1 to 433)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Degtyarenko,K.N. and Archakov,A.I.
  TITLE     Molecular evolution of P450 superfamily and P450-containing
            monooxygenase systems
  JOURNAL   FEBS Lett 332 (1-2), 1-8 (1993)
   PUBMED   8405421
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Nelson,D.R., Kamataki,T., Waxman,D.J., Guengerich,F.P.,
            Estabrook,R.W., Feyereisen,R., Gonzalez,F.J., Coon,M.J.,
            Gunsalus,I.C., Gotoh,O. et al.
  TITLE     The P450 superfamily: update on new sequences, gene mapping,
            accession numbers, early trivial names of enzymes, and nomenclature
  JOURNAL   DNA Cell Biol 12 (1), 1-51 (1993)
   PUBMED   7678494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15334917
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..433
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46546
     Region          51..423
                     /region_name="CYP_unk"
                     /note="unknown subfamily of actinobacterial cytochrome
                     P450s; cd20623"
                     /db_xref="CDD:410716"
     Site            order(121,125,132,176,252..253,256..257,260..261,264,297,
                     307,309,332,362..364,368..370,373..374,377..378)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410716"
     Site            order(197..198,252,255..256,260,305..308)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410716"
ORIGIN      
        1 mtnpssampe sttgagggcp mgagtgavql ggpgftaepq elyrsmrreh gpvvpvelpg
       61 gfpawlvigy relhqvtsdg elyprdvslw nqwenipadw pllpmvgtpm psiyftagae
      121 hrrhvemvvp alegadpfei rqhceqladr lidavcsrgt adlvaefaep lpvlvlarlv
      181 gfpddegadi arvlkdladg gpdaqkahlr fgehmhrlva akrarpgddv tsrmlahpep
      241 ftdeeyaldl maitaaghlt tadwignstr lmltedqfad alsggrhsva eamnevlwed
      301 gptqilagrw aardsrlggr niargdmlll glgaanadph irqqvtasav rsgqggnsah
      361 lafshgeyrc pfpaqeiaei iartgievll drlpdlelav padelvrrps aflrgttalp
      421 vrftpvrttg dal
//
LOCUS       WP_457658872             362 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces griseus].
ACCESSION   WP_457658872
VERSION     WP_457658872.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  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 362)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 362)
  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   5  (residues 1 to 362)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..362
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38741
     Region          88..>312
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtgptsaapp ppwwvfhatg rapegeppel papppwrtfp geplqppppq ddraadrrlg
       61 riqdgpqlrr eetdavnaal llrrpllitg ppgvgkstla yllarelglg rvlpwsvvsr
      121 stlrgglyay daigraqaia awraadtgnp hgpapdgtga dageggatge gppalgdfvt
      181 lgplgtalla yerprvllvd eldksdidlp ndllhvleng syeipelvrs neesatvftd
      241 dprgtarieg grvecaqfpv vvitsngere fpaafrrrcl plemeppgre qligivvshl
      301 rqrpegveal vdefvnrqrg ggtqsidqll navqlttagg fqpdadgrkl vemllrdlsk
      361 gr
//
LOCUS       WP_457658876             400 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            griseus].
ACCESSION   WP_457658876
VERSION     WP_457658876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 400)
  AUTHORS   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 400)
  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 400)
  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..400
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..400
                     /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=42323
     Region          25..359
                     /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 mtgtdtlkat epngntgatg vdenavfsvr nlwkvfgpka dripgsehaa lppaelreat
       61 gctaavrdvs fdvrkgevfv vmglsgsgks tlvrcltrli eptsgtlsid gedvlamdra
      121 rlrelrrhra amvfqhfgll phrtvldnva ygleiqglgk aerrakaael vakvglagle
      181 drrpsqlsgg qqqrvglara lavdpsvllf depfsaldpl irremqdevv rlhreegrtm
      241 vfithdlsea lrlgtrialm rdggivqlgt peeivgspan dyvrefvrdv preqvltvat
      301 amrpalages ergpavrpda tvseaieavs rsgdpaarvm dggrlvgvvd haclldvvag
      361 tsgpgeattt atapgastvt dapdapdapd apdgsrevtl
//
LOCUS       WP_457658877             661 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658877
VERSION     WP_457658877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 661)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..661
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67893
     Region          56..334
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          375..651
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 masaqatgar avpagarrgp vaalrdrpaa akllllalva avvvpvvhgr wgggvwpdal
       61 tadlsaplgd vtdwivsnrd shplflyffg hisnavvlsv rgvylvllal gwagvtvfaa
      121 avawrvaglr laltaavsfl vcgllgmwvp tmqtlalmvv avlasvvlgl llglaaglsd
      181 rvfrilrpvl dtmqvlpafa yllpvvlvfg igvpgavlat vvyaappmar ltalglrgad
      241 sgvmeavasl gatgrqrlls arlplarkel llglnqtimm alsmaviasv igagglgdrv
      301 yqalssvdvg aalaagipiv llavvldrtt eaagrrigae ptgpaflrgw rgwtlaavvt
      361 aavavvgrat dgrvwpedvt vaiagpvnta kdwmvdhlyt gvpvvggtad lashftsgvl
      421 nplrsgltgl pwwsvlliva alawtigtwr taatavlama aigvlgvwep smdtlsqvla
      481 avavtlvigf gvavgaarse rlerllrpvl dvfqtmpqfv ylipvvalfg vgrapaaaaa
      541 vvyalpavir ittqglrgvd paamecarsl gatpgqqlrq vqiplarpsl llavnqavvl
      601 vlavviiggl vgsgalgyev vlglaqgdla tglvagaaiv clglmldrvt qpttrrqrqe
      661 s
//
LOCUS       WP_457658880             245 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphocholine cytidylyltransferase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658880
VERSION     WP_457658880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Jackowski,S. and Fagone,P.
  TITLE     CTP: Phosphocholine cytidylyltransferase: paving the way from gene
            to membrane
  JOURNAL   J Biol Chem 280 (2), 853-856 (2005)
   PUBMED   15536089
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kwak,B.Y., Zhang,Y.M., Yun,M., Heath,R.J., Rock,C.O., Jackowski,S.
            and Park,H.W.
  TITLE     Structure and mechanism of CTP:phosphocholine cytidylyltransferase
            (LicC) from Streptococcus pneumoniae
  JOURNAL   J Biol Chem 277 (6), 4343-4350 (2002)
   PUBMED   11706035
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Kent,C.
  TITLE     CTP:phosphocholine cytidylyltransferase
  JOURNAL   Biochim Biophys Acta 1348 (1-2), 79-90 (1997)
   PUBMED   9370319
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..245
                     /product="phosphocholine cytidylyltransferase family
                     protein"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26743
     Region          3..243
                     /region_name="COG1213"
                     /note="Choline kinase [Lipid transport and metabolism]"
                     /db_xref="CDD:440826"
ORIGIN      
        1 miglvlaaga grrlrpytdt lpkalvpvdg dktvldltla nfaevgltev aivvgyrkea
       61 vyarkaelea tygltltlid ndkaeewnna yslwcardvi krgvilangd tvhpvsveki
      121 lldargkgqk iilaldteks ladeemkvit aegkgvqrit klmdpatatg eyigvtliea
      181 eaaeeladal kttferdpdl yyedgyqelv nrgftvdvap igtvtwveid nhddlkkgre
      241 iacqy
//
LOCUS       WP_457658885             382 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces griseus].
ACCESSION   WP_457658885
VERSION     WP_457658885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..382
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=37698
     Region          16..337
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mthppalpta agpgayvigv dsggsglrva lgrvglpgpl attvcaepvr tgpggidagh
       61 lldqllpaar elleraaess adgapagegk atvgevaala igaagmatlg erlraelpga
      121 ladalgvrrl alaadavtay agavgqrpga vvaggtgmia lgtdlaewhr adgwghllgd
      181 sgggawigra gldaamrahd grrggspall drlravfgpa delpgllypr sdrpavlasf
      241 apevaacaga dpvaagilra aaghiaeaaa avcptaarpa taepddggde lgeggevalt
      301 gglfrmgepl laplreelah llpgarvtsa egdpltgalr iaralaagdl rlprhptmlf
      361 vplehatgqr vgtaardepr sg
//
LOCUS       WP_457658889             326 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658889
VERSION     WP_457658889.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..326
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35663
     Region          4..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mltnvaalll devhpfelgv lcevfgldrs deglpvhdfa vvsaegpvln thagftittp
       61 hglerleead liavpagshf mrreypeevl dalrraverg srvlsvcsga yvlgaaglld
      121 grrctthwrh taelsrrypk avvepdvlyv degpvissag taagidaclh lirqeygqda
      181 antlarrmvv pphrdggqaq yisrplprna cdtvgstlaw meqhldqems veqlaaqahm
      241 sprtfarrfq qetgttpyrw llrqrvllaq hlletsdrti dtiagqtgfg taatlrhqfv
      301 rslgttpnay rrtfrgpaat avpdva
//
LOCUS       WP_457658887             169 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658887
VERSION     WP_457658887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..169
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18255
     Region          5..163
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mdltirvaep aeyavlggii aeaylgddll dgpqdpyllk lraveqraae aevlvaldad
       61 gtvlggvtya apgtpwrdia gpdeaefrml avaragrgrg vgealvraci erarsadgvr
      121 alvlstqpgm lsahriyrrl gflrtperdw epvpglrlmt frlwletts
//
LOCUS       WP_457658891             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658891
VERSION     WP_457658891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22424
     Region          5..>106
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptarqalld aalralddgp wcavrmvdva alagvsrqtl hnefgtkdgl aeallrraad
       61 gylagvdral tapapdrpaa valwtvraar gdalvkallt ghwaeglprp drrpgsrgrp
      121 aavrppptpg qllalvrdrm aaatpgaadg rgeialrlal scvivpvpgd daadsrvlrl
      181 vreasrpvvq gavtqgpvvq gpaglsarsp taggrshr
//
LOCUS       WP_457658893             318 aa            linear   BCT 27-JAN-2026
DEFINITION  anti-sigma factor family protein [Streptomyces griseus].
ACCESSION   WP_457658893
VERSION     WP_457658893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..318
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32820
     Region          73..>122
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msdqqwqpfg prppgprtps gpsrppytag pahpsgpahl pgpggpigpg gptgpggpfg
       61 vepegsehda aaayvlgild daqasafeah lagcarcaah ldefasmepm lamlseapsa
      121 vpgarpvphv pekpaprvlg glmdevarkr hrrtrrsryl vaaaaaliig gpvaafavta
      181 gddrgggsva vgephptspa edaffehmte kvsatdpttq vgatvgmeek awgthtvlel
      241 knvkgpqkcn liavsktgee evvtswsvpq wgygiegatn ptakaplyvh ggaamdrkdi
      301 arfevrtfdg erlveiga
//
LOCUS       WP_457658894             222 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658894
VERSION     WP_457658894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..222
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23312
     Region          10..185
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 msrtagrsar twrfdagric ldlvaterad gvpgtceqld gpahlaqwlt aaglvppgtv
       61 ltglddtwva rfhelrsavs rlmaaqlggp etggalelln slasgappgp ravrgadggl
      121 vrvlsaapdc agllavvard avdlltdpva raalrrcqge achrlyldts rggrrrwcsg
      181 evcgnrerva rhrrrtsgtt daygretpga ygpekeippg ve
//
LOCUS       WP_457658895             217 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces griseus].
ACCESSION   WP_457658895
VERSION     WP_457658895.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..217
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23336
     Region          20..167
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 meyegelrmd rtgrydgsdv igsgglrlrr wreedlpall rayedpamhr wlatqvsgpd
       61 gaadwleaqr tgwasgtrfa favteggqed eplgnavlkr pdpvsdlaev gywttasarg
      121 rgvapralaa ltdwafttfa eqgltrlell hqvdnkascr vaekcgypla rvipalppdy
      181 pldghvhare apaaalsrpa grrgeaagtd ggrasgr
//
LOCUS       WP_457658896             390 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces griseus].
ACCESSION   WP_457658896
VERSION     WP_457658896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..390
                     /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=43204
     Region          27..373
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtaptaptvp agpflappaa akkpgrdryl dllrtialvr vviyhifgwa wltvlfpsmg
       61 vmfalagslm arslsrpalg virgrirrll ppmwvfalvv vpmmfalswq pvkseglwwf
      121 vklawyvfpv gappfpwssg draglledtw avqaagplwy iraylwfvla splllrafrk
      181 lpwatllapl gltavigtgl vtipgetgna lsdfavfgsc wvlgfahhdg lfkdvprylt
      241 islasivmgf glwwasghlt adgwdlndip laqaawslgf cvillqyaps wqelpgrlvr
      301 fdrlvtlann ravtiylwhn llilatvpli dllwkipyvd ahlgstveag ytllmtlliw
      361 pllalvivav gwvedvaarr rprlwpdgrr
//
LOCUS       WP_457658897             459 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Streptomyces
            griseus].
ACCESSION   WP_457658897
VERSION     WP_457658897.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 459)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..459
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=48704
     Region          28..435
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 msvstavlds svcaplpvlg qdvtvplvtg gevtyaaldy aasapalqrv wddvaayapy
       61 ygsvhrgagy lsqlstdlfe nsrrtvaefl gcraedqvvf trsttdslnl laaaipadcq
      121 vfvyetehha sllpwrdaqv tylnaprtpa qavetleral adrdpygpal vcvtgasnvt
      181 gelwpvrela aaahahgari vldaaqlaph hpvdideldv dwvafsghkl yapfgsgvla
      241 gradwlqeae pylagggasr kvarradggv dvdwhttaar heagspnvig vysiasacka
      301 lteagfdslv areqelvgrv reglaavpev qvlslfgdda prvgvisfvv rgwnsshfaa
      361 alsaeygigv rdglfcahpl vrtllgsdpq dpgecgapea epgerslnai rasfgagtpd
      421 ehidrflrav telvregaqw kyrtedgrcv pdrgeaaqv
//
LOCUS       WP_457658903             359 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457658903
VERSION     WP_457658903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085931
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..359
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37378
     Region          1..>42
                     /region_name="Flavin_utilizing_monoxygenases"
                     /note="Flavin-utilizing monoxygenases; cd00347"
                     /db_xref="CDD:238209"
     Region          31..358
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mrigtfvlaa qfpgqgpgea lhravrstea aeesgldsvw laehhfvpyg vcpsattlaa
       61 lllgrtrrir vgtavsvlpn hhpvalaeqa allhltsggr fslgvgrggp wvdlevfggg
      121 ldayengfpe alglvlawlr earvagrger fgfrevavvp radellegpa davpgasgpg
      181 asvpgasgpe vvvactspks vrlaarqalp mllgmhcgde ekaemvalwr taareaghpp
      241 evvegaahvs agvaqiadga rdatemlvka mpgwlrqgld ahvtvdgrhr vmrdpvayte
      301 llcglhpvgp pqlaadrlaa taertgitrf allvegtgdl aateenvrrl gadvlpllt
//
LOCUS       WP_457658906             311 aa            linear   BCT 27-JAN-2026
DEFINITION  1-aminocyclopropane-1-carboxylate deaminase/D-cysteine
            desulfhydrase [Streptomyces griseus].
ACCESSION   WP_457658906
VERSION     WP_457658906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Thibodeaux,C.J. and Liu,H.W.
  TITLE     Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase:
            characterization of an unusual pyridoxal 5'-phosphate-dependent
            reaction
  JOURNAL   Biochemistry 50 (11), 1950-1962 (2011)
   PUBMED   21244019
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Nagasawa,T., Ishii,T., Kumagai,H. and Yamada,H.
  TITLE     D-Cysteine desulfhydrase of Escherichia coli. Purification and
            characterization
  JOURNAL   Eur J Biochem 153 (3), 541-551 (1985)
   PUBMED   3908101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..311
                     /product="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32229
     Region          17..299
                     /region_name="Acd"
                     /note="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase, PLP-dependent ACC
                     family [Amino acid transport and metabolism]; COG2515"
                     /db_xref="CDD:442005"
ORIGIN      
        1 mnsppdrpsr ldallrprvp splpavqder farhgvtlll krddlihpdl pgnkwrklvl
       61 nleaaagrpv ltfggaysnh lrataaagrl lgfptigvvr gdelahrpln pslarcaadg
      121 mrlhfvdrtt yrakaspevl agllsrygdv evipeggsna laaqgctalg relageadva
      181 avacgtggtl aglaaglapg qralgvpvvg ggflagever lqreafggpa gswtlderfa
      241 fggyarstpe laafaadfed rhglpvervy vakllfaltv lagegafapg srvaavitga
      301 paplqessvs r
//
LOCUS       WP_457658909             507 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces griseus].
ACCESSION   WP_457658909
VERSION     WP_457658909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..507
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52382
     Region          18..>372
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mttlvsttdt vtrdalavlq pgftgttapd wllrrvgegl asvglfgrni tspeqltalt
       61 grlrserddv lvaideeggd vtrlevthgs sfpgnfalgs vddvhltrav aqelgrrlae
      121 cgvnlnwaps advnsnpgnp vigvrsfgad trlaarhtaa yieglqaagv aactkhfpgh
      181 gdtavdshla lpridvdldt lharelvpfr aaiaagsksv msahillpal dpdrpatlsp
      241 qiltgllrqe lgydglivtd avemdaiagt ygiergsvla laagadaicv gggladeetv
      301 lrlrdalvaa vrsgelteer ladaaarvra laswtqrarg dvpepgaavq egtapgtgvs
      361 sdiglvaarr avrvtgsgdr lteaayvasf savaniavgd etpwgiaael drilpgtgtd
      421 tyteeteava dailaaager rivavvrdeh rhawmgaald allaarpdtv vvemglpqsd
      481 prgalyiath gaarvcgtaa aealtgr
//
LOCUS       WP_457658910             488 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces griseus].
ACCESSION   WP_457658910
VERSION     WP_457658910.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..488
                     /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=53215
     Region          1..486
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mndlvrqhta lsdtdlewlh llvsewqlls dlsfadlvlw vptrdgtryv svaqmrpntg
       61 ptsyqddmvg hlvprgrrpl ldaaldegri vregdpewre evpvrvesip vrregrvlgv
      121 iarntnlltv rtpsrlelty lqsasdlaqm iaagsfpfpg qqvdmdaspr vgdglirlda
      181 dgivqyaspn glsayhrlgl asdlvghhlg tttaelapsr gpvdealvkv asgyaprefe
      241 vecaggviql raiplkpkgv rigslvllrd vtelrrrere litkdatire ihhrvknnlq
      301 tvaallrlqs rrmdseqgre alneavrrvg siaivhetls qnldervefd eiadrviamv
      361 seispgkvtc rrtgrfgild aevatplsmv ltevlqnale hafavadhgt vevsavrggs
      421 padgrllitv tddgrglpeg fdpkqagnlg lqivrtlveg elggafgmvp apergtqvvl
      481 dlpvradk
//
LOCUS       WP_457658911             208 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658911
VERSION     WP_457658911.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21872
     Region          16..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtekpttrrr aagmspdrrr emiveaaipl iaaygaavtt aevaraagig eatifrvfad
       61 keelldacmt eamrhdhavr elmsvpadlp iadrlveaad aleahldrmg aiagslhasg
      121 hrrrdapage qargmgrees maairsavae llapdaasfr lpveqaaalf lgllftrphp
      181 gdparltgsg laevflhgal aptpgadr
//
LOCUS       WP_457658928             359 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent amine dehydrogenase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658928
VERSION     WP_457658928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Bennett,M., Ducrot,L., Vergne-Vaxelaire,C. and Grogan,G.
  TITLE     Structure and Mutation of the Native Amine Dehydrogenase MATOUAmDH2
  JOURNAL   Chembiochem 23 (10), e202200136 (2022)
   PUBMED   35349204
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Sharma,M., Mangas-Sanchez,J., Turner,N.J. and Grogan,G.
  TITLE     NAD(P)H-Dependent Dehydrogenases for the Asymmetric Reductive
            Amination of Ketones: Structure, Mechanism, Evolution and
            Application
  JOURNAL   Adv Synth Catal 359 (12), 2011-2025 (2017)
   PUBMED   30008635
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Knaus,T., Bohmer,W. and Mutti,F.G.
  TITLE     Amine dehydrogenases: efficient biocatalysts for the reductive
            amination of carbonyl compounds
  JOURNAL   Green Chem 19 (2), 453-463 (2017)
   PUBMED   28663713
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Somack,R. and Costilow,R.N.
  TITLE     2,4-diaminopentanoic acid C 4 dehydrogenase. Purification and
            properties of the protein
  JOURNAL   J Biol Chem 248 (2), 385-388 (1973)
   PUBMED   4684685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467356
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..359
                     /product="NAD(P)H-dependent amine dehydrogenase family
                     protein"
                     /EC_number="1.4.-.-"
                     /GO_function="GO:0016638 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors [Evidence IEA]"
                     /calculated_mol_wt=37719
     Region          1..350
                     /region_name="COG3804"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443017"
ORIGIN      
        1 miptvvwgtg nvgraairav aahpaltlaa vlvhdpakvg rdagelgglg rtlgvaatdd
       61 iaavlasrpr avvyaasgdi rpddaltdig rairagavvv tpslyplydq rnappelrdp
      121 vlaavaeggg slfvsgvdpg wgndvlpllv sglgtevdvi rcqeifdyst yeqeesvrhl
      181 igmgnpmeye plmlaesvpt mvwggqirlm aralgvelde iretldrral etavttrtmg
      241 afaagtqgav rfevqgivdg epriviehit rihpscapdw psppdgvgah rvviegrpri
      301 evtveasdeg enrsaggnat avgrlvsaid wlvdakpgly daldvplrpa vgrlgrrpa
//
LOCUS       WP_457658929             160 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658929
VERSION     WP_457658929.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..160
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17841
     Region          19..152
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 miidvpegqe pigyvwgemv pgigmaaatf smsvyehttl glrefeaarl rvaqingclf
       61 cldwrterdg akveeefaga vtewrttdaf dertrlaaey aerytldhhg lddafwermt
      121 thysqaeive ltmsigswla fgrlnhvlgi davcvlpghg
//
LOCUS       WP_457658932             460 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces griseus].
ACCESSION   WP_457658932
VERSION     WP_457658932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..460
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47340
     Region          14..417
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstpgtpttg dtespggspp lkralgpkll ilfvvgdilg tgiyattgdv agkvggalwl
       61 pfaigfvval ltaasyvelv gkypkaagaa lytqkafkvp fltfvvafmv mcsglssasa
      121 aarafsgdyl geftdavppt liailfilal aainlrgvae svkanvvltl vevtglavil
      181 aigayavlgg egepsrltqi etggtgyali tgvlgatalg ffafvgfeds vnmaeetknp
      241 ardfpraifi gvgvtgtiyv lvalvssllv dsrtlagssg pllevvkagg vdfppklfal
      301 ialfavtnsa linimmasrl cygmaneril ppamgkvlag rrtpwvgivf vsvlaiglvs
      361 tgeieglgdt tsflllcvfa vvniavlvlr kdrvdhrhfr tptalpvlga ltslilaspl
      421 adrgsdvyvr agillligig lwalnravmt areksaapda
//
LOCUS       WP_457658936             319 aa            linear   BCT 27-JAN-2026
DEFINITION  COG1470 family protein [Streptomyces griseus].
ACCESSION   WP_457658936
VERSION     WP_457658936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11444751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..319
                     /product="COG1470 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33052
     Region          28..>240
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mspptprlrr allvltavla allcaltstp aaaddgpadw tarpaggsgd rdarpyvyle
       61 gtpgtvlqdr lavtnsgrap ltvrlrgdgr agawirfaad tvtvpartra evplaltvpp
      121 davpgdasge vvavdggees rvpvrvrigg ptlaaltved vgisgetlry alvnrgnall
      181 rprlavrvdg vfgtlldrpe rplplelapg rrveltepwp dapaldavtv rlrvtapgga
      241 rdeaeasaty lpvlpavggg llvlgvlall gsgayrrrrr tgrgapeppd teaeaetkae
      301 aeaeaetdtr plakagaek
//
LOCUS       WP_457658945             786 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces griseus].
ACCESSION   WP_457658945
VERSION     WP_457658945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..786
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81882
     Region          40..778
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msgdaataan atstglprid alsggpgggp dqgqeqprmg lgaslpaada raktegtfpy
       61 aadlwaegll waavlrsphp harivsidts aaeempgvra vvthedvpgd snygrhvvdr
      121 pvfasdlvrh hgepiaavaa dhpdtarlaa aaiavryevl epvtdpekaf aaeplhpdgn
      181 lirhiplryg daeatgevvv eglyrigrqd papigaeagl avprpdggve iytastdpht
      241 drdliaacfg lepdrvkvvv tgvpgatgdr edpgfqiplg llalrtgcpv klaasreesf
      301 lghthrhptl lryrhhadae grlvkveaqi lldagayada sseslaaala facgpyvvph
      361 afiegwavrt nnppsghvrg egamqvcaay egqmdklaak lgidpaelrl rntlstgdil
      421 ptgqtvtcpa pvaellqavr dyplpalpkd apeddwllpg gpegagepga vrrgvgyglg
      481 mvhmlgaegt devstatvrv hdgvatvica avetgqgftt larqivqetl gveevhvaav
      541 dtdqppagpa thgrhtwvsg gaveraakmv rtqllqplah kfgmstellq iadgkitsyd
      601 gvlsttvtea ldgkelwata qcrphptepl desgqgdafv glafcavrav vdvdielgsv
      661 rvvemavaqd vgrvlnpaql airieagitq gigaaltenl rtarglirhp dltgyalpts
      721 ldapdirivk lveerdvvap fgakpasavp vvtapaavas avrsatgrpv nrlpirpqaa
      781 vatpkp
//
LOCUS       WP_457658951             742 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate--CoA ligase family protein [Streptomyces griseus].
ACCESSION   WP_457658951
VERSION     WP_457658951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 griseus"
                     /db_xref="taxon:1911"
     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=78220
     Region          50..738
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt tgfrarvvac geephaavvs lptasapggl dvsgrplhlt vpdldrffrp
       61 rsvavvgasd aegrpntgit rqlvdwagrv garlhpvhpt rrtvfgrdcf asvaaipdpv
      121 dlavllvadp lpvieelgea kvpfavafas gfaetgeaga aaqarlaaav ersglrllgp
      181 ntnlnaferf redldgpaia litqsghqgr plhalqelgi rlshwaptgn eadletadfl
      241 ayfaqlpevg aiacyveglk dgrsfllaad raaragvpvv avkvgrteag artaashtgk
      301 ltgadqvvda amrqfgvvrv dgldelqdta allararppk adgvavysis ggtgahfadl
      361 ataagltlpt lspakqdelh twipeyltva npidngghpv gdwrgrkiid ailadpsvgv
      421 licpitgpfp pmsdrlaqdl adaaeatdkl vcvvwgspvg tedayrttll gssrlatfrt
      481 arncvtavka yldhhrftdr yrspfedapr tpspsfrkaq nllrpgqqls ehaakqllra
      541 ygirvpreql vtsaaaavra agpvgypvvm kasgprlahk telglvkvgl tsasqvrday
      601 reltdiarye svdldgilvc qmidrgvemm vgvthdalfg ptvtvglggv lvevlhdtav
      661 rvppfgeqqa rdllgelrgr allegvrggp pvdvdalvev vlrvqrmale lgddlteldi
      721 nplvvlgrgq gavaldalav cr
//
LOCUS       WP_457658952             198 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658952
VERSION     WP_457658952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..198
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21681
     Region          4..198
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mphpsgtdpr pltgeplald llntrwidgd grhdlldsva glalwlvspp vrehlrptea
       61 apappadrtt ldrllltraa ldalvtttar hdpatpedat hlnevlshgr irrtlgpdga
      121 pestvetddp swipawyaad nwlhliadrp drirpcanha cilhfydvsk ngtrrwcsma
      181 gcgnrakaqr hyakrtga
//
LOCUS       WP_457658954             456 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658954
VERSION     WP_457658954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..456
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46303
     Region          66..444
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(76..77,80..81,84,116,171..172,174..176,179,197,
                     200..201,204,281,284..285,288..290,293,315,319,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mekptgrasi pdaardtrts pvpnpdrrpn pspapldggg pggtgpgagp ffgsapgrag
       61 lwnrnfryff vartvalfgd gmipvaltag llgagrpass vgfalaawmg plavfvlfgg
      121 vladrftprr mmiiadalrl igasvlavtf atgnpplwav yvlcsvagvg aalfqpgvas
      181 tvprvstdvq ranavlrvae almtmagpaf agalvglasa gavyaanaat favsgaclfl
      241 mrlapaphdd avrgtfaael vdgwrefrar swlwgviavw tvygfavlgp mlpltavlvt
      301 eahgsgaygm lmavngagsv vggllalrlr pshplaagav alplvavsll vlalglpvpv
      361 laagqllagg aaafwlvmws ttvqthvppe alnrlhaydv agsllmvaag ralagpvaea
      421 vgapellvaa avinmgvvav llvarpirrl krighi
//
LOCUS       WP_457658957             199 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces griseus].
ACCESSION   WP_457658957
VERSION     WP_457658957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..199
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=20511
     Region          52..194
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 maatavrylr svgaattaap qtpaealprp vlravrdgeg lpvapdefrr vlghfasgvt
       61 vitardadgp tgfacqsfas lsldpplvsf mvartsttwp riaragtfcv nvlgaqqgal
      121 crgfavsgad kfagvayeda patgspllds vpawidcrih avhtggdhli vvgrvealga
      181 teegdpllfh rgafgrfsg
//
LOCUS       WP_457658961             454 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658961
VERSION     WP_457658961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46127
     Region          11..393
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(17..18,21..22,25,57,112..113,115..117,120,142,
                     145..146,149,231,234..235,239..241,244,267,271,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mghrtplaat laansistag tsltligvpw fvlettgsag ragvvafcat lpivvaalig
       61 gpvidrigrr rvavvsdavc alaiaaipll hfagvldfwm lcalmalngf ahtpgntary
      121 vlipdlaeha gttlaraasl fdavsrgarm vgaalagvli afvgaesvll ldaatfglsa
      181 llvaagvrgi raaeprkaet pvsvraygte lregyshlfs nrlllsvvvm vmfmngldqg
      241 wyavllpvha eaelggatdi glltavfgag gltgallyga vghrfprrav ftacvilcga
      301 prylvaavtg ttlplavtml lggiaggvln pilttviyer vpdrlrsrvs galtagcefa
      361 mplgglaagl lvegagatga lvamggiyll atlsplvfps wrtlddqvve esgpvpgtpe
      421 teeakesges gkpgdpsvpp rvsssapsrp tpgp
//
LOCUS       WP_457658968             381 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            griseus].
ACCESSION   WP_457658968
VERSION     WP_457658968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..381
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41082
     Region          1..375
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mihlfqpqtg deelaavsev fadrwlghgp rtkafeaefa ahvgvepehm iflnsgtagl
       61 flaleclglg egdevvlpsl sflaaanail atgarpvfcd vdprtlnata ahieaaltdr
      121 tkavivlhyg gypgdieava alcrdrgvpl vedaacspgs rvdgrtvgsf gdlamwsfda
      181 mkvlvtgdgg mlyvrdaela vrarrlayhg lvqasgigha kvshrwweld vpeigrrvig
      241 ndmtaaigrv qlrrlpefla arrrivelyd relagtpgvl tppplpdgqe styyfywvqf
      301 eqdelrdiia sellaadiyt tfryaplhkv aayghdgral pssdhaavrt lclplhpgls
      361 dddvrtvaat lrkavaahgg e
//
LOCUS       WP_457658969             918 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces griseus].
ACCESSION   WP_457658969
VERSION     WP_457658969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..918
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=97524
     Region          117..800
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msehrrkspq pqgggraaar raaqqstgrr aapsrratsa sptespyesh ggeerqygsr
       61 aearraaqrg grrrgadagg agggggrrrg ggggsdgpgg rgrdnggpgk krfidyprhg
      121 kygfrrwvps wklvsglclg flgvlmgvgg vsyalvskpn ineaaeaqnn vyywadgtqm
      181 vatggvvnrq ilkyeqipea mrnavisaen ksfdsdrgid pmgigralyn matggetqgg
      241 stitqqyvkn smlsqdqtlk rkfqelfitl kvageekked vmagylnvsy ygrgasglqa
      301 aartyynkda gelnasecaf latllkgasy ydpagapdid kanatkaknt krakerwewi
      361 ldeqvkdgrm saadrakytk fpmplppkkd aklggqtgyl vdlakkyfla nnnqgidakk
      421 lelggyeiht tfqkkrvqel ekavnkvyka kirpkerpet dthvefggas vdaktgaiia
      481 tyggqdatth ftnnadatga qvgstwkpfv laaamqygvr dpsggreqse sqrtqvsqes
      541 iyngdnllri kdytgkiwln qdneewrqtn dggkdygeid lrtameqsan spfvqlgmdv
      601 gtdkvkdvav asglkddsfm adatvpsfsi gtsspsairm agsyatfats gqqndtysvt
      661 evkkggetvf khqkrtkral stdiadnvtd vlknvvengt gtpaqlegrd vagktgttdg
      721 nrsawfvgyt pqistaismf rldddetnke reflkmfgtg geqkihgasf pasiwhdyms
      781 damkgkksia fpepkdlgev vwgggavsps ptpsptpset asedpsptpt ptqttpsptp
      841 tptkscgffd pncqesnggq nagadgggqn ggadgggdtt gttdgsdngg ttdgsdngga
      901 qgangnpggt gsiwgtsg
//
LOCUS       WP_457658970             422 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces griseus].
ACCESSION   WP_457658970
VERSION     WP_457658970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44281
     Region          23..392
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,69,123..124,126..128,131,151,
                     154..155,158,244,247..248,251..253,256,284,288,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvardlrml lrlrnfrrll tvrllsqsad gvyqvalaty vvfspekqts aaaiasamav
       61 lllpysligp fagvlldrwp rrqvflygnl lraalacsta llilasvpdw lfyasalcvt
      121 avnrfvlagl saalprvvdt drlvvansls ptagtlaata ggglafvvrl vadesdaavv
      181 llgsmlylls alaslslpra llgpdtdesp lrlraalavt arglvaglrh laqrdhaara
      241 laamtvirfc ygaltvmvlm lcryawsdte sdglallgla vgvsgagffv aavltpwavg
      301 llgrygwivs cagaaavlvp alglsfapvp mliaafvlgv vtqgskiatd tvvqtsvdds
      361 frgrvfslyd vlfnvafvsa agvaalmlpp dgrsvsvvav vsvlyavvav tmfhwrrtda
      421 rr
//
LOCUS       WP_457658977             228 aa            linear   BCT 27-JAN-2026
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            griseus].
ACCESSION   WP_457658977
VERSION     WP_457658977.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..228
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25587
     Region          133..>193
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mialdpdngf vtaidwltld endrdgqakl ldllrpgade rggpgrvssa lhaahrragv
       61 adfaqwrsve elrahhddpa rqdellrigg lttgvrllaa elvsvqhapa vtggvdvspd
      121 rddwtsvaiq wvrpeeqgal vaeltrpree wvhllpgyrs hsvlrgldgt fvvnyaqwes
      181 eeaywafhdv pehtwpldvr asrdrarklt rtweyntfrv vharveak
//
LOCUS       WP_457658982             328 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457658982
VERSION     WP_457658982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..328
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34479
     Region          31..327
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mrhkdpdgfa glgrtadaha gtgvqsagpa dlnllrtfla vhrsgsftaa arllglsqpt
       61 vtaqmraler qvgrelferl prgvapspya delaarivap ldalaevtgd tvpagerpaa
      121 pvhlagpael mclrvlpala plvadglllr aatgltdpll delragrhdl viattrprgr
      181 alsavplmde efvltaaphw aartggperl aaegpgalhg lplvtyaedl piarrywrhv
      241 fgrrldcraa vtvpdlrgvl aavvagagft vlprylcade lasgalvely apedppinta
      301 ylvqrpgsav npqvarvrdl ltgaaraw
//
LOCUS       WP_457658988             330 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces griseus].
ACCESSION   WP_457658988
VERSION     WP_457658988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  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 330)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 330)
  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 330)
  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 11430362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..330
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35385
     Region          4..323
                     /region_name="PdxI"
                     /note="Pyridoxal reductase PdxI or related oxidoreductase,
                     aldo/keto reductase family [Coenzyme transport and
                     metabolism, General function prediction only]; COG0667"
                     /db_xref="CDD:440431"
ORIGIN      
        1 milmeqrtlg rtgrdvsvvg qgtwqlggdw gevaeddafg lldaavasgv tffdtadvyg
       61 dgrseqligr ylknrpdadv fvatkmgrrl dqvpenyvld nfrtwndrsr anlgtdtldl
      121 vqlhcppsav yssdavfdal dtlvaeqria ayavsvetca ealtaiarpg vasvqiilnp
      181 frlkpldevl paavaagvgi iarvplasgl lsgrytketv fgpddhrtyn rhgeafdqge
      241 tfsgidyatg vaaaaefael apegatpaqt alrwiiqqpg vtsvipgars veqaranaaa
      301 adlpplpqst ldavrelydr siraevhdrw
//
LOCUS       WP_457658993             301 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces griseus].
ACCESSION   WP_457658993
VERSION     WP_457658993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10007665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..301
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33641
     Region          1..285
                     /region_name="COG3662"
                     /note="Uncharacterized conserved protein, DUF2236 family
                     [Function unknown]"
                     /db_xref="CDD:442879"
ORIGIN      
        1 mssatdarta eppqpggakd peppppggvl wslsgdiral lmlpaaltlq vahpavgagv
       61 dehsvfrtdp wgrgerslrs lqlwvyggae aaeegrrlrr lhrtirgtdt rgrpyhaltp
      121 anyawvhstg fpvyqhaary lirpmtpaqe ralyaewlrv grilgihdrd mpqtieefwp
      181 ywqkmlagei eattvvrelv dvdqpvpppd rgpwplrvvl ralwpvllpp larfrrfvti
      241 gfmppdaraa iglpwtddqe krlrrmcavl rvvvpalper vrylpraraa raarrtamsg
      301 g
//
LOCUS       WP_457658994             522 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457658994
VERSION     WP_457658994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..522
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56513
     Region          46..456
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(154,156..157,290..294,314,317..318,321,336,340,395)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mhrrfivpsa laatlllatp aaaapgtvga pgigdpyypa sgnggydvsh ydlrlkyqpv
       61 tdllegtati latttqelsr fnldfgldvs evrvngrkar fatsgdhele vtpadplakg
      121 kdvsvvvrya gkpselking wtawartpdg gvaaqepesa vwwypsndhp ldkatydvsv
      181 svpdgtqais ngvlqsqssk lgwtrfnwrs dkpqatyltt laigrfditt drtadglpvl
      241 nayskdlgan agaarasier ttevaewlte vfgpypfnal ggyvpnvtsg faletqtrpf
      301 ysprqfanga nvsvvvhela hqwygdsvsv dgwkdiwine gfarysqwlw sekegegtaq
      361 eladyayaqh paddpfwqvk pgdpgpdnqf diavydrgal alqalrnevg ddtffellkg
      421 wpaehaygna nvgdfvryae rvsgkplaal fdtwlyrpar paapaaadag laeaalsars
      481 aarverpasw kkiaatntvh dhsdhgdhta sahrsegghe hr
//
LOCUS       WP_457658995             461 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Streptomyces griseus].
ACCESSION   WP_457658995
VERSION     WP_457658995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 461)
  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 10154696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..461
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49920
     Region          127..352
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06242"
                     /db_xref="CDD:349461"
     Site            order(135,138,185,194..195,224..225,229,316)
                     /site_type="active"
                     /db_xref="CDD:349461"
ORIGIN      
        1 mthrvaralr mlsphpwlap vtgparpese pprrgaramr rtavaatlaa lalpfaiapa
       61 eaahrpprtg fetsdgarwt geaeeqaflt avdrgsdrvs vdrigtteqg rplrlvrvgq
      121 erpdattvll icsqhgdepa greaclttvr dlafaedraa raflarttll vlptanpdgr
      181 aadtrgnadg vdinrdhial etsearaiaa vvrderpqvi ydlheygatp pyydkdlfal
      241 wprnlnvddr vhdasrtlse ryvrpaatag gyssghygiw tdpatgdpik qvagdgqeri
      301 lrntsglkha vglliesrvd alsdaekddp alnhrrrvhs qrtalgglfa ftdeqrarlr
      361 tatalsrltg ladrgpvylg gadndpaepa eiladppcgy rldaaqyarv kdelalhgvr
      421 arpdgdgafv slrqsarsli pllldqraty hltngqarta c
//
LOCUS       WP_457658997             395 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658997
VERSION     WP_457658997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..395
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38991
     Region          22..308
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrrppvallc lgavalvsav calslgtpyv pparlpatlg sdglaglvvt elrlprmvla
       61 llagaclgaa glvlqealrn plavpemlgv ssgaalgvaa plvlalsvpl glqpflalag
      121 aaigglltlv aagfgrspsa vlltgaavaa alqagllvlm vmadqldlql iyryllgsls
      181 artwddvtgl lpwlavavpa lvlcvpvlgv lrlgdddara lgvrverarv aalgiavvli
      241 apvvavcgpv awvgflaphl arrlrpdgga agwlvrsavc gaivvlcadq parlalapve
      301 tpvgawtalv gvpvgvvllk rgrrpagdpg pealsasgss pepgtaagpv gppvpgsrsv
      361 sgsspvpggp sasgipsapr gpqdvpgavl rkaer
//
LOCUS       WP_457658998             331 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457658998
VERSION     WP_457658998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..331
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32815
     Region          20..327
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mggllvlvav vacadlfagr gvtpegvrav lfgagddpta ehivlqlrlp rllvalvaga
       61 clgvaglvlq salrnplagp evtgvtpgav lgavaatglg lagwesptav vvaacvggfa
      121 gagllwllag rdrgdpeqta vygvlvsavl agltavvllv apgelgsvvq wligstegrv
      181 wqhwnllwpw aafwgaaawl lagpltllrc gdeqaaaagl atgrgrgaal vcavaltaga
      241 vsavgalgfv gllvphlala vfgadlritl pgaalfgaav vcgadaaaql lsrllatale
      301 adrltlpvga lttfvgaall mvvarrrade r
//
LOCUS       WP_457658999            1112 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457658999
VERSION     WP_457658999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1112
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=115565
     Region          122..593
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava aavavalaag mtqtavaqpd pkgasgtrak drevrhltli tgdrvtvdaq
       61 grpvafrpak grenipvqrm snkghtlvip adahrlivsg kldrrlfdvt elsrpenlra
      121 hkdglklivg yrgkqaaaak aqvrgaggte vgrsltslna esvttptada pdiwkaltdr
      181 gtdgervtta agidrvwldg vrrasldksv pqigvpaawk agftgkgvki avldtgtdtt
      241 hpdlkgqvla eknfsdakdt kdrvghgthv asiaagtgak sggkfkgvap dakllagkvl
      301 ddegygddsg ilagmewava qgadivnlsl ggmdtpevdp leaavdklsa ekgvlfaiaa
      361 gnegdgagtv gspgsadaal tvgavddkdq ladfssrgpr igdgaikpdv tapgvdttaa
      421 ippgsliare vgekpagyat isgtsmatph vagaaallkq qhpdwtyael kgaltastkp
      481 gaynpfqqgs griavdraia qtviaepvsv sfgvqqwpha ddkpatekvt yrnlgtsdvt
      541 ldlkatgtnp kgkpapagff tlgadrvtvp aggtaevtlt adtrlggtvd gtysaylvat
      601 gggqtvrtaa averevesyd vsikhlgrdg rpaayadstl frfgvesgnp flspqvvdgt
      661 akirvpkgty vanstvykdp ddvtkgadwi aqpkvavtkn tsltfdarka kpvkvtlpda
      721 kakgelfspd yvveaandav sfgwvmdspa girtlhvgpk itdgslaqhw sgtwskgast
      781 eydiavggtv kqlatgfdrk ftsaqlakvk iamgsaapkk kgsitafpfl ptqgggwats
      841 idqklpgtrt lyvstadkva wtfdfdqqgp ldadgwptye anyqvgreaa ykagktypks
      901 vntgvfgplv dkdygvareg neitgslpll adgqgnaggm vftsastvly rngkklgqnt
      961 dpvtgfesfk vpagaadykl tttvrhsakv splstrvdaa wtfrskktaf tmlpvstvrf
     1021 tpavgadgrv kagktvsvpv kvhgaaagkn lkslktyvsy nggktwkkvt vkkgkitvkn
     1081 pakgkaisfs akvtdkkgnt ssvkiysayl gk
//
LOCUS       WP_457659001             310 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces griseus].
ACCESSION   WP_457659001
VERSION     WP_457659001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..310
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=32240
     Region          12..301
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mtvvadvivv gggvvgltta vtlaerglrv rvwsrdpaga ttsavagalw wpyriepaer
       61 vgdwsletla vyeelsgape etgvrrvagl hagerfaalg dwaaglkdav evpeglrvtl
      121 plldmpvhla wleqrlvaag gaverrtvkg fdeaaelgav vvnctglgar elapdagvrp
      181 vrgqlvaven pgieewytaa dpasaattyf fpqpgrlvlg gtaeaddrrt epdpetarei
      241 varcarirpe iagapvlghr vglrpareag vrieaealpg ggllvhnygh ggagvtvawg
      301 caraaaalvd
//
LOCUS       WP_457659004             427 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces griseus].
ACCESSION   WP_457659004
VERSION     WP_457659004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  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 427)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..427
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46419
     Region          3..374
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(15,209..211,275,297)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 mhisfllhna ygiggtirtt ftlartlaeq hdveivsvfr hrdapvlgap egvtmrhlvd
       61 lrkksatydg edaeharpav vfprgdsrhk qysrltdari aahlrtvead vvvgtrpgln
      121 vhisrqarrg pvrvgqehlt ldshgyrlrr eiahrytlld alttvtrada ddyrsrlklp
      181 glrietipna vpepagppag gdlkwvvaag rlhrvkrydl lvrafaqvsa arpdwrlriy
      241 gggdatgneq aslralidel glhsqvflmg svnpmeaewp kgsiaavtse resfgmtive
      301 amraglpvva tdcphgpaei iedgadgrlv pvgdpdataa allqliedde lrhrmgaaal
      361 assarfdpar iaerheslyt ellargsqgr ghsalstalh rtrgsvldga yalrykaada
      421 lrgkrsa
//
LOCUS       WP_457659005             512 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457659005
VERSION     WP_457659005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..512
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52210
     Region          68..510
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mahlasrrtr alavpvglal taslgflpta tataaptgeq aaasvrtdgp klsyvvntrg
       61 ghgtvknvkk aiakaggtvv vayeqigviv vhsqnpafge tirrargves agatrtnpiv
      121 pqatkdvgsi aqpltaeqaa aaaaqatage dpleplqwsl paikadkahq ktlgskkvtv
      181 avidtgvddt hpdlapnfds rasvncvsga pdttagswrp aagesdhgth vagtiaaakn
      241 gvgvtgvapg vkvsgikvsn pdgffyteav vcgflwaaer gvdvtnnsyy tdpwlfnckn
      301 dpdqralvda ltravkyaer kgtvnvaasg nsrhdlalda iedttspndt epvtrtidps
      361 acpdiptmlp gvvtvsatga kglkssysny gkgiidvaap ggdstvyqtp eppavnglil
      421 stlpggkfgy kagtsmasph vagvvaliks khpyaspaav kalltlqada kacgepydin
      481 gdgvidavce ggknyngfyg agvvdaldav rw
//
LOCUS       WP_457659009             197 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457659009
VERSION     WP_457659009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21034
     Region          7..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtartprkda vrnraavlaa adelfarses patitmadia aaagvgkatl frgfgdrtgl
       61 irelfatrle pirtavedgp pplgpgtaph rripalldav lclkldnrhl alaledtgda
      121 gpyraehyer whqvlremld ridgladsaf aahallaatr adlvehlvaq qgmtheeira
      181 hlawytaqvi gagapaa
//
LOCUS       WP_457659017             120 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein, partial [Streptomyces griseus].
ACCESSION   WP_457659017
VERSION     WP_457659017.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..120
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <1..82
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 lalldetaec lgaaladlin lflperilig gwaglligpr llpeirryan eyalrhaaar
       61 ttiemgrlgp davtvgaatl pladfltrgg srpatgvtgt pprtaaqavr erhrtststt
//
LOCUS       WP_457659025             206 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase, partial [Streptomyces griseus].
ACCESSION   WP_457659025
VERSION     WP_457659025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>206
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
     Region          8..>204
                     /region_name="Oca4"
                     /note="Protein tyrosine/serine phosphatase Oca4 [Signal
                     transduction mechanisms]; COG2365"
                     /db_xref="CDD:441932"
ORIGIN      
        1 mqtartvpaa tvvnlrdlgg ialgrdrrvr qgllfrsgql seldpasdra vsalgirtvv
       61 dlrtaderrw apdrlpdrar lfvadvlgdh pgvaparlrs lladpveaer tlgggraeel
      121 faetyrkmvl spgaaaayra fletvadsga rpvlfhctag kdrtgwaaav llmilgaara
      181 tvrsdfvavn pavraafapy vakfld
//
LOCUS       WP_457658990             230 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces griseus].
ACCESSION   WP_457658990
VERSION     WP_457658990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..230
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24130
     Region          13..212
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtsrpvtasg lhvifdldgt lvdsepnyye agrrllaryg vrdfgweana rfigistlet
       61 ltvlraeygi eapleellag knalylelag astevfpqmr vlverlyaag vpmavasgss
      121 raaieavlav tgldayiply vsadevahgk pepdvfleaa rrlgvtpadc vvledapaga
      181 aaahaagmrc iavpyvpeta sdpafkaadl lfaggqsaft aeaayhrmlg
//
LOCUS       WP_457658989             407 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces griseus].
ACCESSION   WP_457658989
VERSION     WP_457658989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..407
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43220
     Region          1..244
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(1..2,4,17,19,50,66..69,73,75,112,114,116..117,119,
                     129..130,133,152..155)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(1..2,4,17,19,50,66..69,73,114,116..117,119,129..130)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(13..14,42,47,52..55,67)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(73,75,112,114,116,133,152..155)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(129..137,148..155)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgevwratde vlgravavkl llgdqadass tarfrleaqt aarlshphlv avfdfgawed
       61 rfflvmelve gqslgdllaa qervhpeqva liagqaaagl aaahrqgivh rdikpgnlml
      121 dadgsvkigd fgiaqfvddp stalttaghi vgtslylape ralgrtadsa sdmyslgcvv
      181 yqlllgqppf ksdtatatly qhvdtppvpl rqhgvdisaa fdsyllglla kkpeerptaq
      241 qvadwfrtda wrgrpeplpm qttppshras apmapkpspa appapvgptt yrlpgptgrr
      301 rqaptrsapa rrrstreair rrprvasaia gtatflaavy lgmvlfspds ssagtpdqsp
      361 ssgpsqdvrd gggqqpdqqg qqgqqgqeng ngnghdgdsd edderdd
//
LOCUS       WP_457659029             278 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase, partial [Streptomyces griseus].
ACCESSION   WP_457659029
VERSION     WP_457659029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  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 278)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>278
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          28..223
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mnepipvire vdcgtarllp dvdrdrawll tvddapqsyv dlddpsylef eyvrrlahvv
       61 dgaaepgapl dvlhlgggal tlpryvavtr pgsrqdvvea drallrlvre hlplpdgsgv
      121 slhaadarqr leatapasvd lliadvfggs rvpahltsve yaraagralr edgvyaanla
      181 dsapfaflrs qlanfaavfp elaligepav lrgrrfgnvv llashapidv dplvrgcaad
      241 afparvthga altrflggar pvadadavas peppdgaf
//
LOCUS       WP_457659034             333 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease, partial [Streptomyces
            griseus].
ACCESSION   WP_457659034
VERSION     WP_457659034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..333
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          28..330
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 ctsrtgaart afllllglva laialcasvm fgsrstsfgd vldvlrgsad pnitviiesr
       61 yprtvlgvla glclavagtl mqgvsrnpla epgllginag asasivaata wlgasgatdt
      121 mwwalpgalv agilvhvigs agtgtsvvrl vlagavltav lmafiqavtl skpqvfdsyr
      181 ywvvgalggr dfdvfwsvlp faavgfllal algpglnala lgdatavalg shpgrtrggg
      241 llaatllsaa ataavgpiaf vglavphvvr alvgvdfrvr ilfsallgpt lllfadvvgr
      301 vvmrptelmv gvvtafigap alliavrrmr gts
//
LOCUS       WP_457659003             545 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces griseus].
ACCESSION   WP_457659003
VERSION     WP_457659003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..545
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58596
     Region          7..544
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mtatlvakdl aaghgdrtlf agldlvvapg dviglvgvng agkssllrll agldrpeege
       61 lrlspptatv ghlpqeperr dgetvaafla rrtgvadaqr tmdeatealv agapgadday
      121 sdalerwlal ggadlderae qvaaelgltv gldrpmtals ggqaaragla slllsrydvf
      181 lldeptndld ldglerlerf vsglragtvv ishdreflmr tvtkvleldl aqqqinlygg
      241 gyaayleere tarrharegy eeyadkkasl earghmqrsw mdkgvknarr katdgdklgr
      301 narseasekq aakarqtqrm ierldvveep rkewelrmei asaprsgsvv atlrdarvar
      361 gdftfgpasl qidwadrvai tgangagkst llaallerlp ldsgdatlgs gvvvgevdqa
      421 rklflgaqsl ldafcaavpd tepaevrtll akfglradhv mrpatslspg ertraalall
      481 qgrgvnllvl deptnhldlp aieqleaale tytgtlllvt hdrrmleavr ttrrievtdg
      541 qvkev
//
LOCUS       WP_457659028             303 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457659028
VERSION     WP_457659028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..303
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=30336
     Region          31..275
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 msaaaagggl lvvgdvvtdv varygsalah gtdtaarirt vpggaganva cwaarsgcpd
       61 vrllaragae sadwhrrale ragvraflav ddelptatvi alvdeaaert fltdggavlr
      121 laaedfapsm ldgvgrlhls gyllfaatsr aaallalrta vergvpvsvd pasagflgel
      181 gpkrflefae gaelllpnad earlltglpg peaaaaelsr wfprvvvtlg argavvaarg
      241 evtgrapapp vrepvdstga gdaftggfla allagahdlt aaaagcraga eavatvggrp
      301 pvr
//
LOCUS       WP_457659040             434 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces griseus].
ACCESSION   WP_457659040
VERSION     WP_457659040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..434
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=45322
     Region          27..432
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mpagagsvvr gavrrwaaaa padrarllrr favvvdehie elaqlevrea ghtignarwe
       61 agnvrdlldy saggaerllg rqipvaggid ftvleplgvi gviapwnfpm piaawglapa
      121 laagnavllk paettpltal rlaelaleag lpdglfqvlp gegpvagsal vehpgvakiv
      181 ftgstrtgkh imtrcaervk rltlelggks pnlvfadadv aaaaaaapms fldnagqdcc
      241 artrilvers vydrflellv pavaavvvgd padektqmgp lisalqlerv rgfvdgdrga
      301 dgvrtllgta pegpgfwypp tvltgvspda pvaveevfgp vavvlpfede qdalrlanat
      361 eyglagsvwt rdvgralrvg qglragnlsv nshssvryst pfggykqsgl grelgpdala
      421 aftetknvfi stea
//
LOCUS       WP_457659044             274 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457659044
VERSION     WP_457659044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>274
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          24..271
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtmpkqqttp rapsaagagp aagvrltdva vrfrskkrdv talsevsldv apgefvaivg
       61 psgcgkstll klvaglltas sgdvllgger vtgprhdigy vfqraallew rsalrnillq
      121 aeirhmepaq argradelir mtgltgfeda yphelsggmq qrvalcrall heppvllmde
      181 pfgaldaltr eqmntelnri wrttgttvll vthsiseavy ladrvvvmsp rpgtvteiie
      241 vglpaerdys etlgrpefra aaahirdllg avsa
//
LOCUS       WP_457659045             310 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces griseus].
ACCESSION   WP_457659045
VERSION     WP_457659045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..310
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32016
     Region          8..295
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(35,240,243)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(180,211,238,241..242,245)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mldrldalvi gecvadivrl pgeadrvhpg gspanvaygl arlghdttll tqlgqdgygr
       61 lvrdhltaag vevrtddatg ptpsaavald dqghatytfd vdwtlgpval draplhvhtg
      121 siaavvepga atvlaavesl ragatvsydp nvrpelmger apavarverc vvlsdvvkas
      181 dedlrwlypg edvervavrw laagpalvlv trrgagaval fdggraavea lpvtvadtvg
      241 agdafmsgtl halaahgllg pdarerlrav drdtvadvlr havasaavtv sraganppgp
      301 delrealayn
//
LOCUS       WP_457659046             330 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces griseus].
ACCESSION   WP_457659046
VERSION     WP_457659046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..330
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35557
     Region          64..327
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtcpthppal tgrpggaagg gdgsraarpp rrgrsvspkg hsgwtpwlyl lpalvllagl
       61 lvypiyqlgl isfleytqaq vsggepttfq gfgnyatlfn dsqfwqvlla tvlfaaacvv
      121 stlvvgcala vlltriralp rlalmmaalg awatpaitgs tvwvflfdpd fgpvnkvlgl
      181 gdfswtygry safalvllev lwcsfpfvmv tvyagiraip tevleaasld gasqwriwrt
      241 imapmlkpil ivvtiqsiiw dfkvftqiyv mtngggiagq nlvlnvyayq kafassqysl
      301 gsaigvvmlv illavtlvyl rlvrrqgeel
//
LOCUS       WP_457659053             532 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase, partial [Streptomyces griseus].
ACCESSION   WP_457659053
VERSION     WP_457659053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>532
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          81..440
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtsserserq drtprsrpar grgrgqgagt qaasngrgga prsrnqggsk paarrkpaaa
       61 qpaefalpet vtpalpsvea fadldmpaal lktlaaqgvt epfpiqgatl pnslagrdil
      121 grgrtgsgkt lafglallar tagrrsepra plamvlvptr elaqqvtdal tpyatavnlr
      181 matvvggmsi tkqsatlrrg aevlvatpgr lkdliergdc rldqvsitvl deadqmadmg
      241 fmpqvvallk qveadgqrml fsatldknid rlvkmfltdp vvhsvdpsag avttmehhvl
      301 hvldetdkka vatkiaardg rvimfvdtkr aadrfakrll asgvraaalh ggrsqpqrnr
      361 tldqfktgev talvatnvaa rgihvddldl vvnvdpptdh kdylhrggrt aragesgsvv
      421 tlvlpeekre mtrlmqdagi aprttrvtss daelgritga repsgvaivi evpqptppkq
      481 rarsggsags gsgggavrsg srgrgrrgag gaggagggag rsggagrsgg ea
//
LOCUS       WP_457659055             374 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein, partial
            [Streptomyces griseus].
ACCESSION   WP_457659055
VERSION     WP_457659055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>374
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
     Region          2..301
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlgatgqigr aavralaadg wevtaasrgg grdegwdagv ravaldrdee galakalgdg
       61 cdvlvdmvaf dgaharqltg lagrigsavv issgavyede rgrsfdtqae pdgfprypvp
      121 lpesqatvap gdatygtrkv qlerelpaag ealpvtllra gavhgpycrt prelyvvkrl
      181 ldgrrrrvla yggesrfhpv hvsnaaelir laarkpgsrv lnaadpeapt vaeiasaida
      241 vlgretetvl idgpapegqv getpwsgahp vvydmtaage qlgyrpvtgy aeslpetvew
      301 lagelaerdw reafpkmlkn ygeglfdyaa edawlagggp gaprggagga ppggaeagvg
      361 ggggaaqkdr pgvp
//
LOCUS       WP_457659063             446 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase, partial [Streptomyces griseus].
ACCESSION   WP_457659063
VERSION     WP_457659063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..446
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          21..437
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 segravartq tllkgsngig tvrrtvlpgg lrivtetlps vrsatfgiwa nvgsrdetpt
       61 lngathyleh llfkgtakrt aldisaaida vggemnafta keytcyyarv ldtdlplaid
      121 vvcdmltgsl iapedvdaer gvileeiamt eddpgdcvhd lfahtmlgdt plgrpvlgtv
      181 dtinalnrgq iarfykkhyd pthlvvaaag nvdhatvvrq vrkafekaga lsrtdaapma
      241 pregsrtlrt agkvellnrk teqahvvlgm pglartddrr walgvlntal gggmssrlfq
      301 evrekrglay svysytsgfa dcglfgvyag crpsqvhdvl kicrdeldrv aahgldddev
      361 araigqlsgs tvlgledtga lmnrigksel cwgeqmsvdd mlariaevtp ddvrevagel
      421 lthrpslsvi gplkdkqadr ldeavs
//
LOCUS       WP_457659068             288 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator, partial
            [Streptomyces griseus].
ACCESSION   WP_457659068
VERSION     WP_457659068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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   2  (residues 1 to 288)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>288
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [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          10..288
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 maaarvrsgg rptleevaar agvgrgtasr vingsprvsd atreaveaav aelgyvpnra
       61 aralagnrtd aialvvpepe trffaepyfs aivrgvgaal adtemqlllt lvgndrerrr
      121 laqyltahrv dgvllvavha ddplpelleq lgmpcvisga rhaaetlpsv dsdnfegara
      181 avdhlvargr rqvatitgrl evygaqrrld gyraalsaag lapderliap adfteeggar
      241 amrdllarrp dldavfvasd vmaagarqvl readrriped valigfdd
//
LOCUS       WP_457659069             391 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter, partial [Streptomyces griseus].
ACCESSION   WP_457659069
VERSION     WP_457659069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..391
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          5..369
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(16..17,20..21,24,60,107..108,110..112,115,138,
                     141..142,145,216,219..220,223..225,228,258,262,312..313,
                     317,321,337,340..341,344..345,348)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 vrsrpraalp alcatqitsw givyyafpvl npqittatgw ptgattaafs aallvsaiag
       61 irvgriidrh gprtvmttgs vlgvtsilii asapnlpvft agwllaglam aatfyqpafa
      121 altrwwapdh vraltivtla gglastafap ltatlashls wrttyvvlal ilaavtipah
      181 alalkapwpe pftptglhdd vgvekvtrtr pfwmlattlt lsaftvsaav ialvplmier
      241 gytsteaawa lglggagqtl grtlyatlar htspttrtit lvalgaltta alaitpgpya
      301 mlvalsiaag tvrgnltllq atattdrwgt thygrlsgll aaptttaaai apfagtaiaa
      361 plggypqlfi alaaisaaac italkttpsr a
//
LOCUS       WP_457659070             155 aa            linear   BCT 27-JAN-2026
DEFINITION  urease accessory protein UreF, partial [Streptomyces griseus].
ACCESSION   WP_457659070
VERSION     WP_457659070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..155
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
     Region          <2..155
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 ldplaldeaa dartpapalr atarklgrqm mraaratwps peldalarar prgahqpvvl
       61 gltaraaglg pvdaahcvay etvsgpatav vrllsldpfh atavlarlap eldrvaeqaa
      121 eaarqgidal paasaplldi taeahaawpv rlfas
//
LOCUS       WP_457659074             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor, partial [Streptomyces
            griseus].
ACCESSION   WP_457659074
VERSION     WP_457659074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 242)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..242
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [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          <171..227
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 prelpaavgv gggadrsvgq raagagrtsa alpaalmegr aeplsrliga lrsyhhaave
       61 pywphirasi eadravrgra lldggadgll gtlppmirwr spvleadypv drdlhldgrg
      121 lllqpsffcr gtpvvyrdps lppvlvypvt npgapvfaep gpwlgrlvgh trsavlssig
      181 sgcttselar ragvslasas qhasvlreag lvltlrhgss vlhtltplgg sllrggapla
      241 lp
//
LOCUS       WP_457659075             217 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein, partial [Streptomyces griseus].
ACCESSION   WP_457659075
VERSION     WP_457659075.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..217
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
     Region          2..178
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 gdrtnlrygp aggglavldl rggirepggr vlvvnpldpa hpllasllrt lnppsksrfr
       61 sgtsakawir qygrdaeerh ldtliergll rretrrflgv lpyqrhfpad pdltgaarrr
      121 fgqaealgfp drrnralaal vsaiglagtl spdgragrit mkairrtqwa atavhhnvrq
      181 trssggdsgg ggwgdgglgd sdggsgcggs scggggd
//
LOCUS       WP_457659081            3125 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase/type I polyketide synthase
            [Streptomyces griseus].
ACCESSION   WP_457659081
VERSION     WP_457659081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 3125)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 3125)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   3  (residues 1 to 3125)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 3125)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 3125)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 3125)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   7  (residues 1 to 3125)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
REFERENCE   8  (residues 1 to 3125)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   9  (residues 1 to 3125)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18690202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3125
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..3125
                     /product="non-ribosomal peptide synthetase/type I
                     polyketide synthase"
                     /EC_number="1.14.-.-"
                     /EC_number="6.-.-.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=336592
     Region          10..1402
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1283..1684
                     /region_name="KR_2_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 2, complex (x); cd08955"
                     /db_xref="CDD:187658"
     Site            order(1450..1451,1453,1473..1476,1514..1517,1543..1545,
                     1566..1567,1589..1590,1604,1631..1632)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187658"
     Site            order(1567,1591,1604,1608)
                     /site_type="active"
                     /db_xref="CDD:187658"
     Region          1722..1805
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1817..3045
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 madannralr nkvaiigmgc rlpggasdhr tywrnlmagk dcitptppdr ydvrtlgsrf
       61 rdkpgrlvgg rggyidgfde fdpaffgisp readhmdpqq rkllevawea ledggqrpad
      121 laggnvavyv gaftldykil qfadlgftsl aahtatgtmm tmvsnrisyc fdfrgpslsi
      181 dtacssslva vhlacqalnn gesdlalagg tllhmapqyt vaetkggfls pegrsrtfda
      241 aadgyvraeg vglvalkrld davrdgdrih aviagsgvnq dghtngitvp nadaqvdlir
      301 rvcaeagitp gdlqymeahg tstpvgdpie analaralai grapgarayv gsvktnight
      361 esaagiagli ktvlsiqhrt vpphinlenl npaidpatlp yeiptrptaw pahegparag
      421 vnsfgfggtn ahvvleeapp pppktgaapp agrpwsilpl sarnpdalve laagirgela
      481 gdngpavald dlghtlahrr qhlperlsvv ystrasldea ldahgrgeph prvvhgrare
      541 sadrrlvwvf tgmgpqwwgm grqllaeepv frvaveacdr alrefadwsl ieemtadesv
      601 srmsetwlaq panfavqval aalwrshgvr pdavvghstg eiaafhaagv yslrdaariv
      661 vhrsrlqqtl agtgamlavs lsedeaerrv rpyrdrvsva avnsptaitl agdeaaltll
      721 aeelraeqqf akfltvevpy hsvgmerikd ellaelaple prparvplyl tgvegtargg
      781 eldaaywwkn vrdrvrfrsa vdriaadghq lfleigphpv lghairecle aggttgltlp
      841 sirrrenege rfaaslgslh tlgvtvdwdv lqptgrpvtl prhpfrrdrh wteprpvaqv
      901 rqghrdhpll grrtdrtept wqarldtedl pyladhriqd tvvfpaagyl emaaqavlrl
      961 tggttavlad idlrkalflp dgedrtvevs lslenaafti asptgddger avhasgivrt
     1021 gqrrrtappl dapairarsl rhlegpdcyt alaalgyhyg pafqaveevw igagevlari
     1081 rppeaigdda aghhlhpvll dacfqtlltp lipptpegpa pgtgirlpls vdevalepig
     1141 dqpfwahatl lpgdadttlg nialyaddgt plgrvhgfra advekaatav arttidswla
     1201 epawteappl paedtardhd wlvladnggv adafaalaaa rgercrlvrr gaaytasgdg
     1261 vtftvdpasd adlrrlladl draggpfrga vlhlwnldap aladcdraal rdhagagayg
     1321 lialarllla rggggrlhiv trgaqpalpg egpeplgapa wgigrvlrhq elinhpgkli
     1381 dldprrrpgp dgdraeaeal laevlsgdee eialrdggrr tsrlrpaehl trplplrlra
     1441 dgsylvtgaf galgrllcht lvrrgarriv lvgrtpvpar ekwagtdpat aegravallr
     1501 elealgaqpv latlditded altgwldahr qsgappvrgv fhlagqvrdt lvadldraaf
     1561 davhdpktvg ahllhrhlrd eplehfvlfa siasllttag qtnyaagnaf ldalahhrra
     1621 qglpalsldw gpwatgmiee lglvehylhs rgmsslspdt gmavlervig qdhaqlvvat
     1681 vvdwpaflaw yptppplvad laaaaappgd aasgngfldt fraadeetrr alvaerfaal
     1741 satvlrtgtd ridpatglge lgldsllame lrarihaelg valpvvalls gtpagelaaq
     1801 lhdglsalaa adtpdgaaga velhrderqy pltqnqkalw flkhlnpdgy ayniggavev
     1861 nvalepdlmf davrrliarh palrtnfllv dgqavqrvse daatdlalfd vqgedwdsih
     1921 ativqeyrkp ydlahdplvr frlfkrgpdr wiimkavhhi vsdaistftf ieellavyea
     1981 lrrnqepqlp pvearyldfl nqqnaflagp eaagmldhwr ahlpaevpll dlpvdkprpa
     2041 vqthngasef fvlddalsar vhalarahgv tpfmvllsay ylllhrysgq dhivvgspvt
     2101 grtrqdfasv ygyfvnplpl hadlsddptv aellqqvrrt vlggldnqey pfvllveelg
     2161 lqhdpsrsav fqamfillth kvateqygyr leyielpeee gqfditlsay edeaegrfhc
     2221 vfkyntdlfl petmrrmaah ytrlldrmth apgeqpasrl emlgdqerar ligqwsrpal
     2281 patgsreepf aavqtliart aaehpaavav ttpsphggah rltyaelerr aadsaarlrt
     2341 lgigegsvvv lcldkspeli vallavlkag aaylplrpdq padrlahlvt atgaalvlva
     2401 ddagpeqtga lavptltlga lartaphpdg psdeagpesp ayiittsgst grpkavrvsh
     2461 rnlasahaaw rqeyrletdv rvhlqmaeps fdvftgdlvr alcsggtlvl adrdllfdtt
     2521 rlyrtmrqer vdcaefvpav vrglmdhcar eglrldflkl lvvgsdawsv geyrrlaelc
     2581 gpgtrlvnsy glteatidsa sfegpvddle pgamvpigrp lpnsalhvld ahgepvppgv
     2641 pgelwiggdg valgyagdpe qtearfvtrt lsrsadgdar perlyrtgdi arwdahgrvh
     2701 llgrtdgqvk lrghrieige ieahlaqwpp laravvtvra dtggeaalca ycvpapgatl
     2761 dgralrrhla rslpsymips hfvelpalpl tangkvdtaa lpapraetgd rpyeepvtly
     2821 eisvarhwkt llgreqvgle ddffelggss ikliellhql rtefgvgvpv srlyqvttlh
     2881 gmaatvedvl hgtsadelps ltfnagqhpa lfcfppaggh glvyrglaah lpdhtligfn
     2941 ylpgddkvar yadlieaarp dgpyrllgys lggnlafeta kelerrgrsv ahvvildsrr
     3001 iltayepdas giavfeaela dhlrkhtgse avtretlaha aeylafcgrt pntgtvaatv
     3061 svitdeekaa lyaagehgtw hgsstgatav lrgsgvhadm ldakhlprna elvrsvltgd
     3121 pahgg
//
LOCUS       WP_457659083             270 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator, partial [Streptomyces
            griseus].
ACCESSION   WP_457659083
VERSION     WP_457659083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>270
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          10..79
                     /region_name="HTH_MERR"
                     /note="helix_turn_helix, mercury resistance; smart00422"
                     /db_xref="CDD:197716"
     Site            order(11..13,27,44..46)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 matgtdeptl tvdelaarag vtvrtvrfys trgllpppvi gprrvgrygp dhlsrlalie
       61 elqqqgmtla aieryleqlp pdlsahdlai hralvaswap dktedfsrae lerrtgrals
      121 epdverlaam gvlvrpqeag gayrvdlgll rlgvelldvp vahetilaar tvllehtrsa
      181 aqemtrlfrd evwnpyrere gdpehvaamk slsadmqpiv vqalvtafqr slkeelraag
      241 thqgrgdrpp aragprdvgg wlcpnnpklp
//
LOCUS       WP_457659085             485 aa            linear   BCT 27-JAN-2026
DEFINITION  HAMP domain-containing sensor histidine kinase [Streptomyces
            griseus].
ACCESSION   WP_457659085
VERSION     WP_457659085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Dunin-Horkawicz,S. and Lupas,A.N.
  TITLE     Comprehensive analysis of HAMP domains: implications for
            transmembrane signal transduction
  JOURNAL   J Mol Biol 397 (5), 1156-1174 (2010)
   PUBMED   20184894
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Hulko,M., Berndt,F., Gruber,M., Linder,J.U., Truffault,V.,
            Schultz,A., Martin,J., Schultz,J.E., Lupas,A.N. and Coles,M.
  TITLE     The HAMP domain structure implies helix rotation in transmembrane
            signaling
  JOURNAL   Cell 126 (5), 929-940 (2006)
   PUBMED   16959572
REFERENCE   6  (residues 1 to 485)
  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   7  (residues 1 to 485)
  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   8  (residues 1 to 485)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20436658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..485
                     /product="HAMP domain-containing 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=50471
     Region          184..241
                     /region_name="HAMP"
                     /note="HAMP domain; pfam00672"
                     /db_xref="CDD:459898"
     Region          <238..459
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msgvrrsgar wrrrrplrtr lavaasaava lvavgvcaaa ffviryellh qldlsltqsa
       61 trviqenrge gpqtvagecr ylsapacaqi vpadpaadpd tayllpvsip vrevaagkra
      121 pyysnvsrfg qplrmlttpf gdgralqval radpvekgvr qaavllaavg gagvllagll
      181 ghavsrtgla pvarltstae riaatrgprh rmeetpgppr padevtrlaa sfntmlgele
      241 qsvssqrrlv adashelrtp ltalrtnael largdrltpe qrerasgalg rgirevtglv
      301 ndlielarde eplslleevr iaevaehtva tarthwprtp fllevgpgaa qtirpgvpar
      361 larlltnlld naakfsppgt pvevalsayg sgreggggpg sggglvltvr dhgpgipaad
      421 lpyvfdrfyr aeaaralpgs glglamarqi arahgaelta gaapgggalf tltfgpggpp
      481 ggggp
//
LOCUS       WP_457659086             476 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces griseus].
ACCESSION   WP_457659086
VERSION     WP_457659086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..476
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49887
     Region          1..472
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mttaivvgsg pnglaaavvl arsgarvtvl eaadeigggt rsgeavmpgl lhdhcsaihp
       61 maagsaflrs ldperhgliw rrpeidcvhp ldggeagvlh rsveetaagl grdgsrwrla
      121 fagpaarfdl laedvmgpll rlpghplala rfglpallpa savarlftte rgralfggva
      181 ahafrplhhp lsaaiglgii taghrhgwpv aaggsrsiaa alasalaehr gtietgvevr
      241 rvqdlppadi tmfdlaprav adivgdrlpa rvarayrrfr hgpgafkvdf aveggvpwtn
      301 pdarragtvh lggpyaetaa aerdvhagrm perpfvlvgq qyladprrsv gdihpvysya
      361 hvphgytgda tgavidrier fapgfrdrvv ghvarsttam qahnpnyvgg divtgakdpr
      421 qlvlgprstl spydtgvpgm yicsaatppg pgahgmcgan aaeaalrhlt rrprdr
//
LOCUS       WP_457659090             393 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter, partial [Streptomyces griseus].
ACCESSION   WP_457659090
VERSION     WP_457659090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..393
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          7..371
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,62,109..110,112..114,117,140,
                     143..144,147,218,221..222,225..227,230,260,264,314..315,
                     319,323,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 tgvrsrpraa lpalcatqit swgivyyafp vlnpqittat gwptgattaa fsaallvsai
       61 agirvgriid rhgprtvmtt gsvlgvtsil iiasapnlpv ftagwllagl amaatfyqpa
      121 faaltrwwap dhvraltivt lagglastaf apltatlash lswrttyvvl alilaavtip
      181 ahalalkapw pepftptglh ddvgvekvtr trpfwmlatt ltlsaftvsa avialvplmi
      241 ergytsteaa walglggagq tlgrtlyatl arhtspttrt itlvalgalt taalaitpgp
      301 yamlvalsia agtvrgnltl lqatattdrw gtthygrlsg llaaptttaa aiapfagtai
      361 aaplggypql fialaaisaa acitalkttp sra
//
LOCUS       WP_457659099             145 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter, partial [Streptomyces griseus].
ACCESSION   WP_457659099
VERSION     WP_457659099.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>145
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          37..>144
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 msapceprat apasalpppv psapparrpa ldwrirfaal sliwgfsfll ikvgtegyap
       61 fqvtfgrlla gtavlvaama mrrerlprsa rtwghltvaa fllnalpfsl fsyaeltips
      121 tlagicnats plwgmalsvv alsed
//
LOCUS       WP_457659100             286 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase, partial [Streptomyces griseus].
ACCESSION   WP_457659100
VERSION     WP_457659100.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>286
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
     Region          28..223
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mnepipvire vdcgtarllp dvdrdrawll tvddapqsyv dlddpsylef eyvrrlahvv
       61 dgaaepgapl dvlhlgggal tlpryvavtr pgsrqdvvea drallrlvre hlplpdgsgv
      121 slhaadarqr leatapasvd lliadvfggs rvpahltsve yaraagralr edgvyaanla
      181 dsapfaflrs qlanfaavfp elaligepav lrgrrfgnvv llashapidv dplvrgcaad
      241 afparvthga altrflggar pvadadavas peppggavsv gwgarr
//
LOCUS       WP_457659102             172 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457659102
VERSION     WP_457659102.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>172
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          30..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 meidrpglaa flrrrrellq pedvglprgq rrrtgglrre evavlchmst dyyarlerer
       61 gpqpseqmia siaqglhlsl derdhlfrls ghmppargtt gehispgllr ildrlddtpa
      121 eivtelgetl rltplgvahk ggptpdtrrp rpqgypgvsp ppppppdggg gp
//
LOCUS       WP_457659103             526 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase, partial [Streptomyces griseus].
ACCESSION   WP_457659103
VERSION     WP_457659103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>526
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          81..440
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtsserserq drtprsrpar grgrgqgagt qaasngrgga prsrnqggsk paarrkpaaa
       61 qpaefalpet vtpalpsvea fadldmpaal lktlaaqgvt epfpiqgatl pnslagrdil
      121 grgrtgsgkt lafglallar tagrrsepra plamvlvptr elaqqvtdal tpyatavnlr
      181 matvvggmsi tkqsatlrrg aevlvatpgr lkdliergdc rldqvsitvl deadqmadmg
      241 fmpqvvallk qveadgqrml fsatldknid rlvkmfltdp vvhsvdpsag avttmehhvl
      301 hvldetdkka vatkiaardg rvimfvdtkr aadrfakrll asgvraaalh ggrsqpqrnr
      361 tldqfktgev talvatnvaa rgihvddldl vvnvdpptdh kdylhrggrt aragesgsvv
      421 tlvlpeekre mtrlmqdagi aprttrvtss daelgritga repsgvaivi evpqptppkq
      481 rarsggsags gsgggavrsg srgrgrrgag gaggagggag rsggag
//
LOCUS       WP_457659104             237 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter, partial [Streptomyces griseus].
ACCESSION   WP_457659104
VERSION     WP_457659104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..237
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <8..180
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 vvalsedrpt rrrvaglglg flgvltvlga wqgfsgldlp gtgmallasf cypvgwiyvr
       61 rtlagtgsst laltgsqlfl gtvqlavvtp lftsaptsfp llptlsvlal galgtglavl
      121 lqyglvqevg pttaqmvtyf ipviataagv allgerlswn tpvgalivlv gaaltqsrar
      181 pattavpkep aghpaaappe aaatavpdep tghpaatasp repagppgad aprlsrs
//
LOCUS       WP_457659105             326 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase, partial [Streptomyces
            griseus].
ACCESSION   WP_457659105
VERSION     WP_457659105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>326
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          22..>326
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msahsattag tatgseagtt avelaiggmt cascaariek klnrmdgvea tvnyatekak
       61 vtyqgaevsv ddliatveat gytarppapp appassgsng tetagaagpa aesaeddglt
      121 tlrqrlvtav llsvpviama mvpalqfdyw qwlsltlaap vvtyaawpfh raawtnakhg
      181 aatmdtlisv gtsaaflwsl walffgtagm vgmthpfelt iarsdgagni yleaaagvta
      241 filagryfea rskrkagaal kalmelgake vtvlrdgvet tiptaalqvg drflvrpgek
      301 iatdgtvveg ssavdasmlt gesvpv
//
LOCUS       WP_457659110             227 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein,
            partial [Streptomyces griseus].
ACCESSION   WP_457659110
VERSION     WP_457659110.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>227
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          3..>227
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 maevlvlvdh vdgavrkptl elltlarrvg dpvavalgag aeatagvlge hgavkvltad
       61 apefadylvv pkvdalqaay eavspvavlv vssaegkeia arlalrvgsg iitdatdlea
      121 gekgvvatqa afaasyttks rvsrgvpvit vkpnsapvep aaaagaveal svsfgatatg
      181 tkvvsrtare stgrpeltea aivvsggrgv ngaenfpvie aladslg
//
LOCUS       WP_457659113             426 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Streptomyces griseus].
ACCESSION   WP_457659113
VERSION     WP_457659113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 426)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 426)
  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 426)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>426
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          135..409
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkrsvlrrla dasklphtti rtrialvygg vflvlgtall atvnlasrag tetdaraias
       61 saavgppgyv tgppgyvvap pghlvngpvi srssvasptv yeitdhvsda agkqlmnwsf
      121 aallvmtaga vgvgwwiagr vlrpvhamta karrlsertl heriassgpd delkelgetl
      181 dallgrleka fdsqrrfian ashelrtpla tqraaiqvgl ddpspedlvr trqtlldtnr
      241 rserliegll vlarsergla tderesvrld hvvreetarh pavrgpiggp eerradggpa
      301 vkvtvagcsv rgnrlllaql vanllanavt ynvpggsvev slsgegallv rntgpvvsea
      361 diagffepfr rgegrdrmgp gsglglsivr siamahggtv tarpgpeggg lavnvrhtvd
      421 qaaepa
//
LOCUS       WP_457659121             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator, partial
            [Streptomyces griseus].
ACCESSION   WP_457659121
VERSION     WP_457659121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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   2  (residues 1 to 298)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>298
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [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          10..298
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 maaarvrsgg rptleevaar agvgrgtasr vingsprvsd atreaveaav aelgyvpnra
       61 aralagnrtd aialvvpepe trffaepyfs aivrgvgaal adtemqlllt lvgndrerrr
      121 laqyltahrv dgvllvavha ddplpelleq lgmpcvisga rhaaetlpsv dsdnfegara
      181 avdhlvargr rqvatitgrl evygaqrrld gyraalsaag lapderliap adfteeggar
      241 amrdllarrp dldavfvasd vmaagarqvl readrriped valigfddsv varhmhpa
//
LOCUS       WP_457659123             597 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein, partial
            [Streptomyces griseus].
ACCESSION   WP_457659123
VERSION     WP_457659123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..597
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
     Region          42..582
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 vtssrkermr entgvismgl vpaarmplra rlrllaeptl gvgsfldhar avspdpsapf
       61 llaqhaggpe edglerlsld rlteirdaya swyheagvrk gdpvgvyage gidaflhfla
      121 lsslgaiaal vngrmkpava aeyltrigvy glvgtaegid rlresgglpk tlafekdlrt
      181 fprtrsarps lpgvfpyrhg eddlvmlcht sgttgppkav tfghrqffrg krhrlvsfpd
      241 agsnrmlsal pqthsagisy lmtatllglp tlvmadssge avhdaagwfr ptlvvafpqt
      301 yaelarldls psavgnvhtw intgdsahea hikalirhgr rpggrsgrlp vtlpggwpgg
      361 rssragsrfi dglgssemgm alfrkvsepe rqdydrcvgr pvkvveratv ldpdgrqlgp
      421 gragrlgvis ptrtpgywgn teltgkssvs gfwltgdivy rdrrgrffhl drvpdvieta
      481 egpvyslpme eaillglpev adcavvavda ppplgkqapf atvllkpgak apadllatln
      541 dvlrarglts lsaavlatep ehfptgatgk vlkrslrehf advlvrpssp gteesss
//
LOCUS       WP_457659124             413 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein, partial [Streptomyces
            griseus].
ACCESSION   WP_457659124
VERSION     WP_457659124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         <1..413
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
     Region          1..411
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 adragllrrf avvvdehiee laqlevreag htignarwea gnvrdlldys aggaerllgr
       61 qipvaggidf tvleplgvig viapwnfpmp iaawglapal aagnavllkp aettpltalr
      121 laelaleagl pdglfqvlpg egpvagsalv ehpgvakivf tgstrtgkhi mtrcaervkr
      181 ltlelggksp nlvfadadva aaaaaapmsf ldnagqdcca rtrilversv ydrflellvp
      241 avaavvvgdp adektqmgpl isalqlervr gfvdgdrgad gvrtllgtap egpgfwyppt
      301 vltgvspdap vaveevfgpv avvlpfedeq dalrlanate yglagsvwtr dvgralrvgq
      361 glragnlsvn shssvrystp fggykqsglg relgpdalaa ftetknvfis tea
//
LOCUS       WP_457659130            2349 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Streptococcus pneumoniae].
ACCESSION   WP_457659130
VERSION     WP_457659130.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pneumoniae
  ORGANISM  Streptococcus pneumoniae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 2349)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2349
                     /organism="Streptococcus pneumoniae"
                     /db_xref="taxon:1313"
     Protein         1..2349
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=260353
     Region          2255..2305
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mmlarglwas gtfrpsgagt aktidvsdsp vtgfdkairl tssnardqig iaqdgfyisq
       61 gtytmscwvk grrgqkvklq tywqvndnsg ispiftlkde nwtklsftsa rnragvasig
      121 yvylvnaevg eyldvlapql edgslatssk eapediegqi stvesnfkqr adsleagvsr
      181 lteglrtkad isslnvtaen irqsvkslet dtqnklnqkl sqaefevrag sirqeilnat
      241 kdkankselt qtaeelasri asvqasgrnl flnslfkqdi sktgiwttst ytatidsesk
      301 ylghkalkii glnpsgrdgg npkvtypalg qfgkvipgst tnqdvtisfy akankngiml
      361 rsrlgnigyk tgnvtlstei kryvvhipkg wtneskqttn ewlfnfnqeg tiwiwmpkfe
      421 isdvdtsyse apediegqis tvesnfkqra dsleagvsrl teglrtkadi salnvtaeni
      481 rqsvksletd tqnklnqkls qaefevrags irqeilnatk dkankseltq taeelasria
      541 svqasgrnlf lnslfkqdis ktgiwttsty tatidsesky lghkalkiig lnpsgrdggn
      601 pkvtypalgq fgkvipgstt nqdvtisfya kankngimlr srlgnigykt gnvtlsteik
      661 ryvvhipkgw tneskqttne wlfnfnqegt iwiwmpkfei sdvdtsysea pediegqist
      721 vesnfkqrad sleagvsrlt eglrtkadis alnvtaenir qsvksletdt qnklnqklsq
      781 aefevragsi rqeilnatkd kankseltqt aeelasrias vqasgrnlfl nslfkqdisk
      841 tgiwttstyt atidseskyl ghkalkiigl npsgrdggnp kvtypalgqf gkvipgsttn
      901 qdvtisfyak ankngimlrs rlgnigyktg nvtlsteikr yvvhipkgwt neskqttnew
      961 lfnfnqegti wiwmpkfeis dvdtsyseap ediegqistv esnfkqrads leagvsrlte
     1021 glrtkadisa lnvtaenirq svksletdtq nklnqklsqa efevragsir qeilnatkdk
     1081 ankseltqta eelasriasv qasgrnlfln slfkqdiskt giwttstyta tidseskylg
     1141 hkalkiigln psgrdggnpk vtypalgqfg kvipgsttnq dvtisfyaka nkngimlrsr
     1201 lgnigyktgn vtlsteikry vvhipkgwtn eskqttnewl fnfnqegtiw iwmpkfeisd
     1261 vdtsyseape diegqistve snfkqradsl eagvsrlteg lrtkadisal nvtaenirqs
     1321 vksletdtqn klnqklsqae fevragsirq eilnatkdka dktlvvseag klreefskmk
     1381 vggrnlwiks ktvgaviekl penhvtgqke cyrlennstl tfnlepdfss rlyqkvtfsa
     1441 wikyenvvqg rnfwnvfncf khylfrknse tgvqsgpdya tlgmykgsad wkyitftydy
     1501 sektnfdqlk tslrfnlega tsgtawvtgi kveigsvatd wspapedadg liteakatfe
     1561 rtaqglrtdl saiqeyvnkd gqrqealqry treesarqat avrelvnrdf vgkatyqedv
     1621 kginqrieav ktsankdias qiasyrqsvd gkftdissqi ttykqdvggq isglsnrlts
     1681 seqgtttqis nlsnrinsnk qgtdnqisnl ktqvatnkdn aerqmgrisd qvsankanad
     1741 sqfanvtnql arkvettdfq rvketsklye rilgntengi adkvarmalt nqlfqvevgk
     1801 vakggrnyir ngqfkngskn wleyqsvnfg lnfnyqhsqn pnnrnrpglh fyhdsqdvan
     1861 ffgiqqsfaf dgvrgekvsv sllvskdggd snsglkvalh yiknkniigq ewqnipspqi
     1921 tskykrftft ftlsddvenl nlmlfgekgk tinlyvtdvq lergsvatdy keapedtdea
     1981 irsvqsqlag swavqninsa gdiisginlg anghnrfvgk lthitgetli draviksamv
     2041 dklktanfea gsvtttilea eavtaeklkv dnalikklta tdafiyelis krifstkves
     2101 vissstflea yqgriggftl gqfdqgggrw isgvnqfsvg mgngagygvr tafwanwgnn
     2161 wnyagpkawn vntdgkmycr nevgfydqvd fsnssranfy gnttfsrspv fsngielgsk
     2221 dvlgdgwnpk ggrnavvwwn qvgsgsvkyw meqksdrrlk enitdtavka ldkinrlrmv
     2281 afdfienkkh eeigliaqea etivprivsr dpenpdgylh idytalvpyl ikaiqelnqk
     2341 iekmektia
//
LOCUS       WP_457659134             818 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces griseus].
ACCESSION   WP_457659134
VERSION     WP_457659134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 818)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..818
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87361
     Region          34..808
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mavvaavavm stlaatgsta tgaaaaeagp drptirytey giphiiasdw eglgtgygya
       61 aaednictla dtylmvdarr srhlgpdgra spgqnqntts nlnsdlyfqr lkddrvverl
      121 ldqpapdgpe pevreairgy vqgynrylae tgvdgisdpa crgadwvrpi temdvyrhah
      181 aeiimgsada lldgqvnaap pgasaaaqpk aasgepapra sspeetaaki rdamaasreq
      241 gmgsnalavg sqgvsggtam llanphfpwq gknrmwqsql tipgkvnvsg asllgfpavn
      301 ighnenvaws htvatvapfg lfdvqvdpln pttylvdgaw ermtsqrvev dvlkpdgsla
      361 kagrtlwstr ygpvttsmqg iplpwvvsah avrdvnlhnl ralnswfrld raedvhdvvn
      421 ilettqgvpf fntvaadrtg nalyadiqat pnitdqhaes cltatgrllf dqslrlpnvp
      481 pisildgkrs acdwpddpna aapglldphq qprlirsdfv gnandspwla npaqplsfpr
      541 vmgdtaaprs lrtqelilta qkriagtdgl pgkgftpetm gqllfadnsr aadlaldatv
      601 tmcqnvpfgh ilvdgnlvdv reacpvlaaw kshdyttdsr gswlfanywa fllngqgvek
      661 lpwrvpfdpk dpvhtpnsld sgssavrdaf gravlalrka niplnaplsd iqkvtrggeq
      721 ipihgslgql gvlnvitpgq vdgapdivfg ssfiqqvrft atgppqalsv maysqsadpn
      781 sphhadqtkl fsaggwvter fteeqiaasp qlrttvln
//
LOCUS       WP_457659137             188 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces griseus].
ACCESSION   WP_457659137
VERSION     WP_457659137.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20341
     Region          6..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 milstserkg sarerllarl ldafgealps pemslrevaa rietshallr yhfgslpgvl
       61 aamltaqrsr dnealleaaq qgtfddfvva iwrtytrpeq lsrargffyv aglaaygped
      121 frafvesigd ltemlsslae regldatear dtaavtvaai rglllqevla pgtrpedava
      181 lilrmsgs
//
LOCUS       WP_457659139            1112 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457659139
VERSION     WP_457659139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1112
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=115519
     Region          120..593
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava aavavalaag maqtavaqpd pkgasgarak drevrhltlv tgdrvtvdaq
       61 gkpvafrpak grenipvqrm snkghtlvip adahrlivsg kldrrlfdvt elsrpenlra
      121 rkdglklivg yrgkqaaaak aqvrdaggte vgrsltslna esvttptada pdiwkaltdr
      181 gadgervtta agidrvwldg vrrasldksv aqigvpaawk agftgkgvki avldtgtdtt
      241 hpdlkgqvla eknfsdakdt kdrvghgthv asiaagtgak sggkfkgvap dakllagkvl
      301 ddegygddsg ilagmewava qgadivnlsl ggmdtpevdp leaavdklsa ekgvlfaiaa
      361 gnegdgagtv gspgsadaal tvgavndkdq ladfssrgpr igdgaikpdv tapgvdttaa
      421 iapgsliare vgekpagyat isgtsmatph vagaaallkq qhpdwtyael kgaltastkp
      481 gaynpfqqgs griavdraia qtviaepvsv sfgvqqwpha ddkpatekvt yrnlgtsdvt
      541 ldlkatgtnp kgkpapagff tlgadkvtvp aggtaevtlt adtrlggtvd gtysaylvat
      601 gggqtvrtaa averevesyd vsikhlgrdg rpaayvdstl frfgvesgnp flspqvvdgt
      661 akirvpkgty vanstvykdp ddvtkgadwi aqpkvavtkn tsltfdarka kpvkvtlpda
      721 kakgelfspd yvveaandav sfgwvmdspa girtlhvgpk itdgslaqhw sgtwskgast
      781 eydiavggtv kqlatgfdrk ftsaqlakvk iamgsaapkk kgsitafpfl ptqgggwats
      841 idqklpgtrt lyvstadkvt wtfdfdqqgp ldadgwptye adyrvgkeaa ykagktysks
      901 vntgvfgplv dkdygvareg neitgslpll adgqgnaggm vftsartvly rngkklgqnt
      961 dpvtgfesfk vpagaadykl tttvkhsakv splstrvdaa wtfrskktaf tmlpvstvrf
     1021 tpavgadgrv kagktvsvpv kvhgaaagkn lkslktyvsy nggktwkkvt vkkgkitvkn
     1081 pakgkaisfs akvtdkkgnt ssvkiysayl gk
//
LOCUS       WP_457659144            2695 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Streptococcus pneumoniae].
ACCESSION   WP_457659144
VERSION     WP_457659144.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pneumoniae
  ORGANISM  Streptococcus pneumoniae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 2695)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2695
                     /organism="Streptococcus pneumoniae"
                     /db_xref="taxon:1313"
     Protein         1..2695
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=299418
     Region          2601..2652
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mdvlkrtian dirpkqaqae aeiakqvevl srtknelsgv ksaqatyeet ttrrlseltn
       61 langkaskse ltqtaeelas riasvqagss rnyfrnsrsr tfttggqavy dyrtfivpdf
      121 wknsdrfkrd yvrisfdvtf pvalvndmpa mvhfsahpwy ayrnlifkgg tverqhfeft
      181 idlssssedy qtnnvfirfg tnygfpaglq vvienamlsv gnyfpayqpa yedqedrvsv
      241 vesnfkqrad sldagvsrlt eglrtkadis slnvtaenir qsvkrletdt qnklnqklsq
      301 aefevragsi rqeilnatkd kaskseltqt aeelasrias vqasgrnlfl nslfkqdisk
      361 tgiwttstyt aaidseskyl gynalkiigl npsgrdggnp kvtypalgqf gkvipgsttn
      421 qdvtisfyak ankngimlrs rlgnigyktg nvtlsteikr yvvhipkgwt neskqttnew
      481 lfnfnqegtv wiwmpkfeis dvdtsyseap ediegqistv estfkqrans leagvnrlte
      541 glrtkvdisa lnvtaenirq svksletdtq nklnqklsqa efevragsir qeilnatkdk
      601 askseltqta eelaskiasv hlgrrnllkg tkelarykpv seyngfkvir tvagatryqd
      661 syvertvipt agteyiaify arasendypv rchfynpntv vssenssgyk srssdglsii
      721 rlstdwqlcw vkwtqtatdq aktviigrhg pqvggkegvw veicapaife gnlagdwspa
      781 yedqdervsa vesnfkqrad sleagvsrlt eglrtkadis slnvtaenir qsvksletdt
      841 qnklnqklsq aefevragsi rqeilnatkd kaskseltqt aeelsskias vqvggrnyir
      901 gtkrmmlarg lwasgtfrps gagtaktidv sdspvtgfdk airltssnar dqigiaqdgf
      961 yisqgtytms cwvkgrrgqk vklqtywqvn dnsgispift lkdenwtkls ftsarnragv
     1021 asigyvylvn aevgeyldvl apqledgsla tsskeapedi egqistvest fkqranslda
     1081 gvrslteglr tkvdisslnv taenirqsvk rfetdtqnkl nqklsqaefe vragsirqei
     1141 lnatkdkask seltqtaeel asriasvqas grnlflnslf kqdisktgiw ttstytaaid
     1201 seskylgyna lkiiglnpsg rdggnpkvty palgqfgkvi pgsttnqdvt isfyakankn
     1261 gimlrsrlgn igyktgnvtl steikryvvh ipkgwtnesk qttnewlfnf nqegtvwiwm
     1321 pkfeisdvdt syseapedie gqistvestf kqransleag vsrlteglrt kadisslnvt
     1381 aenirqsvks letdtqnkln qklsqaefev ragsirqeil natkdkasks eltqtaeela
     1441 sriasvqasg rnlflnslfk qdisktgiwt tstytatids eskylghkal kiiglnpsgr
     1501 dggnpkvtyp algqfgkvip gsttnqdvti sfyakankng imlrsrlgni gyktgnvtls
     1561 teikryvvhi pkgwtneskq ttnewlfnfn qegtiwiwmp kfeisdvdts yseapedieg
     1621 qistvestfk qransldagv rslteglrtk vdisslnvta enirqsvksl etdtqnklnq
     1681 klsqaefevr agsirqeiln atkdkadktl vvseagklre efskmkvggr nlwiksktvg
     1741 avieklpenh vtgqkecyrl ennstltfni epdfssrlyq kvtfsawvky envvqgrnfw
     1801 nvfncfkhyl frknsetgvq sgpdyatlgm ykgsadwkyi tftydysekt nfdqlktslr
     1861 fnlegatsgt awvtgikvei gsvatdwspa pedadglite akatfertaq glrtdlsaiq
     1921 eyvnkdgqrq ealqrytree strqaiavre lvnrdfvgka tyqedvkgin qrieavktsa
     1981 nkdiasqias yrqsvdgkft dissqittyk qdvggqisgl snrltsseqg tttqisnlsn
     2041 rinsnkqgad nqisnlktqv atnkdnaerq mgrisdqvsa nkanadsqfa nvtnqlvrkv
     2101 ettdfqrvke tsklyerilg ntengiadkv armaltnqlf qvevgkvakg grnyirngqf
     2161 kngsknwley qsvnfglnfn yqhsqnpnnr nrpglhfyhd sqdvanffgi qqsfafdgvr
     2221 gekvsvsllv skdggdsnsg lkvalhyikn kniigqewqn ipspqitsky krftftftls
     2281 ddvenlnlml fgekgktinl yvtdvqlerg svatdykeap edtdeairsv qsqltgswav
     2341 qninsagdii sginlgangh nrfvgklthi tgetlidrav iksamvdklk tanfeagsvt
     2401 ttildaeavt aeklkvdnal irkltandaf idqliskrif stkvesviss stfleayqgr
     2461 iggftlgqfd qgggrwisgv nqfsvgmgng agygvrtafw anwgnnwnya gpkawnvntd
     2521 gkmycrnevg fydqvdfsns sranfygntt fsrspvfsng ielgskdvlg dgwnpkggrn
     2581 avvwwnqvgs gsvkywmeqk sdrrlkenit dtavkaldki nrlrmvafdf ienkkheeig
     2641 liaqeaetiv pkivsrdpen pdgylhidyt alvpylikai qelnqkiekm ektia
//
LOCUS       WP_457659159            1117 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces griseus].
ACCESSION   WP_457659159
VERSION     WP_457659159.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..1117
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=116221
     Region          126..597
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrtacipava tavavalaag mtssavarpg pgassdtraq drsqdrelrr ltlvtgdrvt
       61 vdaqgkpvaf rpakgrenip vqrmsdqght lvvpadahrl itsgkldrrl fdvtelsrpe
      121 nlraqrdglk livgyrgkqt atakaqvrga ggtevgrslt slnaesvttp tadapaiwka
      181 ltdrragger lttaagidrv wldgvrrasl drsvpqigap aawqagftgk gvkiavldtg
      241 tdathpdlkg rilaeknfsa spdtkdrvgh gthvasiaag tgarsggkfk gvapdaella
      301 gkvldddgyg edsgilagme wavaqgadiv nlslggtdtp evdpleaavd klsaekgvlf
      361 aiaagnegdg agtvgspgsa daaltvgavd dqdkladfss rgprvgdgav kpdvtapgvd
      421 ttaaipsgsq iakevgenpa gyatisgtsm atphvagaaa llkqqhpdwk yrelkgalta
      481 stkpgaynpf qqgsgriavd raiaqsvvae pvsvsfgvqq wphtddvpvg ekvtysnlgt
      541 tdvtldlkvt gtgptgkpap agfftlgadr vtvpaggtad vtltadtrlg gtadgtysay
      601 lvatgggqtv rtaaaverev esyevtvkhl grdgrpaaya dstlyrfgve sgdpflsprv
      661 vdgtakirvp kgtyvvnstv yndpddvtkg adwiaqpkla itkntsltfd arkakpvnvt
      721 vpdakakarl fspdyvveea ndavsfgwlm espagirtlh agpkitdgsv aqhwvgtwsk
      781 gasteydiav ggpvkqlatg fqrkfttaql arvkvamgsa aprktgsita fpflptqggg
      841 watsidqklp gtrtlyvsta dkvawsfdfd qqgpldaegw ptyeanyqig eeaaykagks
      901 yaktvntgvf gplvdnenyg varegnditg tlplladgrg naggmlftsa etvlyrngkk
      961 lgrngdpvtg gesfrvpaga adyrltttvr hsakvnplst rvdaawtfrs kktaftmlpv
     1021 stvrftpavg adgrvkagkt vsvpvkvhga aagknlkslk tyvsynggkt wkkvtvkkgk
     1081 itvknpakgk aisfsakvtd kkgntssvki ysayfgk
//
LOCUS       WP_457659162             601 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase, partial [Streptomyces griseus].
ACCESSION   WP_457659162
VERSION     WP_457659162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseus
  ORGANISM  Streptomyces griseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Streptomyces griseus"
                     /db_xref="taxon:1911"
     Protein         1..>601
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
     Region          2..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          31..>601
                     /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 mseeqklrdy lgrvtaqlkq akrtlqnlea aqnepiaivg macrypggvr spedlwrlvd
       61 sgedaisefp anrgwdldal fdtdpdrsgt sytreggfly dadefdadff gvspreatat
      121 dpqqrllles awqvlesaai rpdslrgsdt gvfvgvmsqe ygpsllhpsv dgtdgflltg
      181 nqnsvasgri aytlgfegpa vtvdtacsss lvgvhlavqa lragecslal aggvavmstp
      241 gffiefsrqr glspdgrsks faaaangtgw segvgmlala rlsdaerlgy rvlglvrgsa
      301 inqdgkssql sapngpaqqr vmrqalasar ltasdvdvve ahgtgtvlgd pieaqaviat
      361 ygqdresplw lgslksnigh tqaaagvggi ikmimamrhg vlprtlhvde ptphvdwsag
      421 svelltkarp wpelerprra gvssfgisgt nahvvleavp vaepaepges vepggaarvp
      481 ylvsartpda lraqidrlrh hldrhpglsp advgfslaer tqfthraall gdatlaegqa
      541 grgglaflft gqgsqrtgmg relyetypvf realdaalta lgiqdefftg dldrtrltqp
      601 a
//
LOCUS       WP_457659171             361 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces microflavus].
ACCESSION   WP_457659171
VERSION     WP_457659171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..361
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36721
     Region          106..153
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          174..357
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(206,231,265,268..272,274,282..286,289,293..296,298,
                     307,312..317,332..334,339,343)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(206,294,296,298,312..317,332..334)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mkhrrisrkr atvagsavva lvvagftfqt anasdevpqf tvkmlsadaa gklattldrd
       61 lgadaagsyy dtktkalvvn vvdetaaeqv rqaggkarvv ehslaelksa rqtltdkati
      121 pgtswavdpv tnkvlvtads tvdgaawkkl savveglggk aelnktagef kpliaggdai
      181 wgsgsrcslg fnvvkdgepy fltaghctes vtswsdtqgg seiganegss fpendyglvk
      241 ytsdiahpse vnlyngstqa itqagdatvg qavtrsgstt qvhdgevtal natvnygngd
      301 ivngliqttv caepgdsgga lfagdtalgl tsggsgdcss ggttffqpvp ealaaygaei
      361 g
//
LOCUS       WP_457659177             307 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            microflavus].
ACCESSION   WP_457659177
VERSION     WP_457659177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..307
                     /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]"
                     /calculated_mol_wt=32843
     Region          14..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msprppdlag fgawprepgt vmrrasavpa gasapfviis efhvpgvpte wephthplhe
       61 lvwvrggtlm srvadqvftv segqglwmpa gvvhggrlta gvefydaffa pertpvafdg
      121 ptaismtpll esllthlart dldagarara esvvfdvllp serqftlqlp gdaridtiae
      181 alledpadsr sleewaralg tsdrtvaraf rhstglsftq wrqtlrvhra ltllsegwdv
      241 qsvgealgya qpstfiaafr rvvgttpgaf fstatgaefr saadrgsrag edaprgvrna
      301 vsgvsss
//
LOCUS       WP_457659178             321 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            microflavus].
ACCESSION   WP_457659178
VERSION     WP_457659178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..321
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33458
     Region          2..320
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 midipdelia sqyayngaag rafvaalpgl agrfleewgl rrdgaamygm calvlpvvre
       61 adgvpaalkl qlvdeetvge pvalrawgaa gagavgvlgh dpgtgallle rldegrplsg
      121 maggggvpgg srlvgevada rravavlgev larlaavpap eglrtlgdav ermlaaapet
      181 vgrladeeer rlladcaaav revagepgdr llhwdlhydn vlagradagr agewvaldpk
      241 plagdpgfel fpaldnlfda gevvwrfdal tealgmerdr grarawtlgr vlqnavwavg
      301 dgerelapdh aeiarrllgv g
//
LOCUS       WP_457659180             430 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces microflavus].
ACCESSION   WP_457659180
VERSION     WP_457659180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42668
     Region          18..412
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,66,121..122,124..126,129,149,
                     152..153,156,248,251..252,256..258,261,284,288,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpespaehrp ahrdgnvlrw laaytaslig dsvyfvalaw saqkvagpae vglvmaagaf
       61 prallmlggg vaadrfgvrr ivlgsdtvrc vlilavaagv avtapavwil valalafgav
      121 dalfvpavga lppritgpdq larvtgmrtl smrisqisgp plgglamglg gasaafavag
      181 alfalslpll ltvrlrppgg asdatdvqge adpapssapa pgsawqdlig glryvrrhrl
      241 igpliavlai selgltgtln vgmvllnger gwgpsgygwi isgfgagatv gallltvagr
      301 lpragptlag tllagcagaa tialvptlpl avavaltvgl amgicgtlan slvqtaadpt
      361 ylgrvtsvvm ltsvglapls ypvvgaaiga wgsapvfigc gafgslgvgv algsgavrra
      421 elprlrpvka
//
LOCUS       WP_457659181             301 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces microflavus].
ACCESSION   WP_457659181
VERSION     WP_457659181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..301
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32643
     Region          36..298
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 msapdqavpa yapgelaala arhgltvsga rpslpayvrq lwgrrhfiaa fatakltaqy
       61 sqaklgqvwq imtpllnatv yyfifgvlln tkngvedfvp flvtgvfiwt ftsssitagt
      121 raisgniglv ralhfprasl pvalalqqlq qllfslgalt lillafgqyp rpswllaipa
      181 lalqavfntg vsmavarlta ktpdiaqltp fvlrtwmyss gvmwsldhll kgervphavm
      241 vtleynpaal yidlmryali dsysaaqlpp hvwaaaagwa llcgvagfvy fwkaeetygr
      301 g
//
LOCUS       WP_457659185             185 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            microflavus].
ACCESSION   WP_457659185
VERSION     WP_457659185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..185
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20133
     Region          1..145
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdtfaargyn naslaeiadr vgltqagvlh yfrskalllt svlelrdrad ieqlgpdrpq
       61 gldflrhlvn talrnaereg ivrlyavlsa esvtddhpaq eyfrdrydgl rvfvadalre
      121 acelpadrad itedaanaii avmdglqvqw llapdsvdma astdlvvtsl latlapgrfg
      181 psahr
//
LOCUS       WP_457659195             241 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            microflavus].
ACCESSION   WP_457659195
VERSION     WP_457659195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..241
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25330
     Region          55..226
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(60..63,113..118,151,154..155,177,183..184,207,209)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(62..63,113,117,154..156,177,207,209)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mvlccgrrpg gagvwvgapa pptpyasata paaptgprrf pgqpalithg prdrprvalt
       61 fegrgdpdla raalariera garvtvlavg swldahpgma rrildgghei gnhtqshrdl
      121 atldertaye eitacarrlr rltgsmgtwf rpspgpattp lvqrlarrag yphvlsydve
      181 sldhlaggvp avtrkvagel rngsvvglsl arpvtvaalp lllaeigrrg lravtatell
      241 s
//
LOCUS       WP_457659197             288 aa            linear   BCT 27-JAN-2026
DEFINITION  terpene synthase family protein [Streptomyces anulatus].
ACCESSION   WP_457659197
VERSION     WP_457659197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Segura,M.J., Jackson,B.E. and Matsuda,S.P.
  TITLE     Mutagenesis approaches to deduce structure-function relationships
            in terpene synthases
  JOURNAL   Nat Prod Rep 20 (3), 304-317 (2003)
   PUBMED   12828369
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16077446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..288
                     /product="terpene synthase family protein"
                     /EC_number="4.2.3.-"
                     /GO_function="GO:0010333 - terpene synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0046246 - terpene biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32626
     Region          27..222
                     /region_name="Terpene_syn_C_2"
                     /note="Terpene synthase family 2, C-terminal metal
                     binding; pfam19086"
                     /db_xref="CDD:465972"
ORIGIN      
        1 mirtrpelwi slifpkatqe hldlfcqwlf waflvddefd dgpagrdplm cetaitrlvd
       61 vfdgaapngp meralaglrd rtcrgrspqw nrqfrrdtaa wlwtyyaeav eraagqvpsr
      121 aefakhrrds vamqpflclh eitagidlpd sarslpayia lrnavtdhsg lcndicsfek
      181 eaalgyehna vrliqrdrgc tlqeavdeag iqlariaerv hraerelide ieaagiggpt
      241 rtalercvqd yrglvrgdfd yharaerytr pdlveldere slsqyfaa
//
LOCUS       WP_457659198            1117 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces anulatus].
ACCESSION   WP_457659198
VERSION     WP_457659198.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..1117
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=116136
     Region          126..597
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava tavavalaag mtssavaqpd prgasgaraq drsqggesrq ltlvtgdrvt
       61 vdaqgkpvaf rpakgrehip vqrmsdkght lvipadahrl ivsgkldrrl fdvtelsrpe
      121 nlraqrdglk livgyrgkqa atakaevrda gstevrrslt slnaesvttp tadapaiwka
      181 ltdrragger vttaagidrv wldgvrrasl dksvpqigap eawkagftgk gvkiavldtg
      241 tdathpdlkg qilaeknfsa akdtkdrvgh gthvasiaag tgaksggkfk gvapdaklla
      301 gkvldddgyg ddsgilagme wavaqgadiv nlslggpdtp evdpleaavd klsaekgvlf
      361 aiaagnegsg agtvgspgsa naaltvgavd dqdkladfss rgprigdgav kpdvtapgvd
      421 ttaaipsgsl iakevgenpa gyatisgtsm atphvagaaa llkqqhpdws yselkgalta
      481 stkpgaynpf qqgsgriavd raiaqtvvad pvsvsfgvqq wphtddepat ekvtyrnlgt
      541 sdvtldlkvt gtgpagkpap agfftlgtdk vtvpaggtae atltadtrlg gtadgtysay
      601 lvatgggqtv rtaaaverev esyevtvkhl grdgrpavya dstlyrfgvd sgdpflspqv
      661 vdgtakirvp kgtyvvnstv yndpddvtkg adwiarpkva vtenttltfd arkakpvkit
      721 vpdakaksrl fspdyvveea nsavsfgwlt espadirtlh sgpkitdgsl aqhwvstwsk
      781 gasteydiav ggtvkqlatg fdrkfttaql akvkitmgsa apkkkgsita fpflptqggg
      841 watsieqklp gtrtlyvsta dkaawsfdfd qqgpadadgw ptyeanyqvg aesrykagkt
      901 yaktvntgvf gplldnknyg ivregnditg alplladgrg naggmlfssa ktvlyrngkk
      961 lgqngdpvag gesfrvpaga adyrltttvk hsakvnplst rvdaawtfrs kktaftmlpv
     1021 stvrftpava adgrvkagkt vsvpvkvhga aagknlkslk tyvsynggkt wkkvtvkkgr
     1081 itvknpakgk aisfaakvtd kkgntssvki ysayfgk
//
LOCUS       WP_457659206             408 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Streptomyces anulatus].
ACCESSION   WP_457659206
VERSION     WP_457659206.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..408
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45544
     Region          67..397
                     /region_name="XerC"
                     /note="Site-specific recombinase XerC [Replication,
                     recombination and repair]; COG4973"
                     /db_xref="CDD:443998"
ORIGIN      
        1 mtgkrgngeg siypykngfa ayvwvtkpdg krarkyaygk trdevhdkwl nlhaeakkgp
       61 vatrhrtlav flaywldsiv kpnlapltyv syegyvrlyi apqlgakwld kltvrdvrew
      121 ltrlatlcqc caqgkdakra pgrrkccavg dccesypsrr vvqgsrdalr aalshavaee
      181 eisknvaslv kvpkprrrri kpwsaaeasl fladaaardd hlfaawvlvl tlglrrgevl
      241 gltwksidfe tgelyvdhqi qragreilhr etktedsddf lplpavclka lrmrcaqqlg
      301 drkaagelwq gshdlvfttk ygtpiepgnl trmfalrsrr aglrviplrn trhttgsllv
      361 vlkvhpkvaq rilrhsqiam tmdvyadaad eevreaigkl sdamggtg
//
LOCUS       WP_457659208             361 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces microflavus].
ACCESSION   WP_457659208
VERSION     WP_457659208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..361
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36704
     Region          106..153
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          174..357
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(206,231,265,268..272,274,282..286,289,293..296,298,
                     307,312..317,332..334,339,343)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(206,294,296,298,312..317,332..334)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mkhrrisrkr atvagsavva lvvagftfqt anasdevpqf tvktlsadaa gklattldrn
       61 lgadaagsyy dtktkalvvn vvdetaaeqv rqaggkarvv ehslaelksa rqtltdkatv
      121 pgtswavdpv tnkvlvtads tvdgaawkkl savveglggk velnktagef kpliaggdai
      181 wgsgsrcslg fnvvkdgepy fltaghctes vtswsdtqgg seiganegss fpendyglvk
      241 ytsdiahpse vnlyngstqa itqagdatvg qavtrsgstt qvhdgevtal natvnygngd
      301 ivngliqttv caepgdsgga lfagdtalgl tsggsgdcss ggttffqpvp ealaaygaei
      361 g
//
LOCUS       WP_457659213              69 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces microflavus].
ACCESSION   WP_457659213
VERSION     WP_457659213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..69
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=7544
     Region          1..52
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 mffpigttgp aliqieeaka vcrrcpsmeq clqwalengq dqgvwgglse derralkrra
       61 argrgrlsa
//
LOCUS       WP_457659215             371 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            microflavus].
ACCESSION   WP_457659215
VERSION     WP_457659215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..371
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=38999
     Region          7..359
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtvtgsalrp spaprsadee rrlaavdryq ildtppdgtf dkgaalaari frtpaaaitt
       61 adgyhlgtvn vldtrprqvt aeqlaalqnl aalvmdqlem rlsairtvta erqmrtaaer
      121 lartlqrtll ppalpqvpgl raaaayhaas adevggdfyd lfplddgrwa fflgdvcgrg
      181 aeaaaltslt rytlraaaiy gpdpcavlan ldtvlkgeyp gtdprhctav fgvlgrtedg
      241 sftltlaggg hppasavrad gtiqplpvtg gqligllpep rftqtsthla pgdalllytd
      301 glteartpsg pmrqeeglaa hlaagtwdda ddlvagirrl ldhlgtgvnd dtallalsvp
      361 ihppapaqet r
//
LOCUS       WP_457659218              95 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Streptomyces microflavus].
ACCESSION   WP_457659218
VERSION     WP_457659218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces microflavus
  ORGANISM  Streptomyces microflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Streptomyces microflavus"
                     /db_xref="taxon:1919"
     Protein         1..95
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0097351 - toxin sequestering activity
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045927 - positive regulation of growth
                     [Evidence IEA]"
                     /calculated_mol_wt=10098
     Region          7..86
                     /region_name="StbD"
                     /note="Antitoxin component YafN of the YafNO
                     toxin-antitoxin module, PHD/YefM family [Defense
                     mechanisms]; COG2161"
                     /db_xref="CDD:441764"
ORIGIN      
        1 mnwevamrtv sceefladca gtldtvgedg egvvvtrpgh epvvivplae yaslketvhl
       61 lrsprnarrl lasinrlesd gdaardadgr rpaag
//
LOCUS       WP_457659228             313 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Streptomyces anulatus].
ACCESSION   WP_457659228
VERSION     WP_457659228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..313
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=34159
     Region          104..240
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(109,111,173..174,177)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            111
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(172,221..222,224..225,229)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(178,182..183,217,220..221,224..225,228,231)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(200..202,217..218,221..222,225,229,232,236)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(200,222,225,229,232,236)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(230,236..237)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          252..303
                     /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(253..255,297..298,300..302)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mespgsdsfr gitdeqfdal aaierhpcps cdvpagsacr tgagktavky htrrlqlvpr
       61 vaeelhvptp pdrgpgkrwa lgpepdgvdp tesaplaagi tavrigyarc statqelqsr
      121 ldalepvcle vfhekvstrv kiwpeyekav amarrfkrlh pevqviltvh efrrlgrgtd
      181 llftvedlrk agialeflsg pitglydpgd rhgqgailfg viaalsgaer tytrektleg
      241 qesarkrgrt ggrppsldad qieyaltlra kgtpmkeiqq ktvitrgkhk gkhpslptly
      301 rtlseaaaer tdt
//
LOCUS       WP_457659231            1128 aa            linear   BCT 27-JAN-2026
DEFINITION  ALF repeat-containing protein [Streptomyces anulatus].
ACCESSION   WP_457659231
VERSION     WP_457659231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            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 10510034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..1128
                     /product="ALF repeat-containing protein"
                     /calculated_mol_wt=113805
     Region          62..95
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
     Region          200..238
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
     Region          <513..>614
                     /region_name="PRK12472"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:237110"
     Region          617..651
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
     Region          758..791
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
ORIGIN      
        1 megksvlsps lwsrrrilst vagaaavpal psiltlsatp ahaapaapga pdnglpdtdq
       61 gravwayktg gravregaaa allgtpaalt aflatelpva raednrfavl sslsgagrsv
      121 qqtasaalsa gdeavagflr dgfaapvled lrvsvfsald nggtamkrea tkalntntke
      181 sletflrttq htaqqedeqa avfailstas pevkkyaera ltdgspaair lflssgqhia
      241 rardeetati eqlveivere gkraklttdk avafsarake aaekakiaal eaaaeakaaq
      301 qdvrksataa nnaasaarga aaaantaisa srtaqaassr aaqaaqaaaa aaasagnaaa
      361 rayhaaigas kdaskasaar daavgarnaa arartaakaa dqaaiassqa ssagsaaasa
      421 arnaaaaasa sadaaasaga aqaqaakarq aaaeanaaaa ratraagtaq alanraaaaa
      481 rvardaansa aahadkaaaa aeeaaanagk aieyakrste yakqavdaan tavdavrean
      541 eveaaarkae tdriaedtel gvlearlqaq aetedaarve kqrtqvsqts eevkglista
      601 eaalaagnta savtvgrkaa lrlldssgsw trgaaefals gsehdvvnwi dadrllaqqq
      661 ddrenvlala qsstaavaaa aeraladsdp naatvfletg aieaaaadnr vlvfqvlsqd
      721 pgkavkakaq aalnagtaga lhhfltvels eatkeddrve lfrlldtggp ymrsaaqial
      781 egsarmrraf virdkfniar ldhdhathis airatlahaa rvaakaleda araskaaaea
      841 rqaaqeaaew aakadgyakd alasaaeaka nadaadksaa saaqsakdar aaattargaa
      901 rtanysmrqa sasakqavaf aveaqasasr aaasaqqagq daraaaaaas qahaiaaqkr
      961 raeaaaaark aaeearqnqq ngtnpsdkpe ndddgdtkwl glwpedmkdp kdwasatghw
     1021 stlfgtasvv lgvgallfpp aapvlgplal gagviswglq gvsaglsgwg ygwdssefht
     1081 alglfvvggv ffgkgrlfsk fgvaeeigak vsgvvsdgat avigwltw
//
LOCUS       WP_457659235            1116 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces anulatus].
ACCESSION   WP_457659235
VERSION     WP_457659235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..1116
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=115777
     Region          126..597
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava tavavalaag mtssavaqpd prgasgaraq drsqdgesrq ltlvtgdrvt
       61 vdaqgapvaf rpakgrehip vqrmsdkght lvipadahrl ivsgkldrrl fdvtelsrpe
      121 nlraqrdglk livgyrgkqa atakaqvrda gstevrrslt slnaesvttp tadapaiwka
      181 ltdrragger vttaagidrv wldgvrkasl drsvpqigap eawkagftgk gvtiavldtg
      241 tdathpdlkg qilaeknfsa akdtkdrvgh gthvasiaag tgaksggkfk gvapdaklla
      301 gkvldddgyg edsgilagme wavaqgadiv nlslggpdtp evdpleaavd klsaekgvlf
      361 aiaagnegdg agtvgspgsa naaltvgavd dqdkladfss rgprigdgav kpdvtapgvd
      421 ttaaipsdsl iakevgenpa gyatisgtsm atphvagaaa llkqqhpdws yselkgalta
      481 stkpgaynpf qqgsgriavd raiaqtvvad pvsvsfgvqq wphtddepat ekvtyrnlgt
      541 sdvtldlkvt gtgpagkpap agfftlgadr vtvpaggtae atltadtrlg gtadgtysay
      601 lvatgggqtv rtaaaverev esydvtvehl grdgrpavya dstlyrfdag agdpflspqv
      661 vdgtakirvp kgtyvvnstv yndpddvtkg adwiaqpkva vtknttltfd arkakpvnvt
      721 vpdakaksql fspdyvvetg tdavsfgwvm qspagmrtlh agpqitdgsl aqhwagtwsk
      781 gasteydiav ggkvkqlatg ysrkftagql aevkiamgas apkkkgeita wgnlptqggn
      841 wataieqklp gtrtlylsta dkvawsfdfn qigpadadgw ptyeanyqig keakykpgka
      901 yaktvntavf gplvskefgi iregneiggv lplladgrgn aggvalssvk tvlyrngkkl
      961 gqnsdpltgg evfrvpagaa dyrlttsvkh sakisplstr vdaawtfrsk kttstmlpvs
     1021 tvrftpavga dgrvkagrtv svpvkvhgaa asknlkslkt yvsynggktw kkvavkkgri
     1081 tvknpakgka isfaakvtdk kgntssvkiy saylgk
//
LOCUS       WP_457659238             440 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces anulatus].
ACCESSION   WP_457659238
VERSION     WP_457659238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..440
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46760
     Region          18..351
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
     Region          <319..439
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mritrsvagr rlragyvatt gltvtalllt gcggssdsdk gadadgnitl tladfgqfgy
       61 keaglfekyh elnpkitvke dttaeeknyy pkllqqlnsg sgladvqgie vgrikeivdt
      121 kadsfadlsk aigvdewvsw kakqatapdg avigagtdig pmslcynrel fekaglptdr
      181 aevakltegg wedflalgeq ykkkapegty fmdsasamfn avvssspeqy ydasgkpiye
      241 ksasvekgwk laaeaaskkl tqglaqfedq wqaalrkstv atvvcpawma gqistyagda
      301 nkgkwditsa pgntsanwgg sflavpksgk nvaeatklvk wltapeqqaa vfkaigvfps
      361 nqgaydlpdv knatlpyfnd apigqiyadg aksipeavlg pkdgvikdsi stqinnmeqr
      421 gtspddawda avrtidkaig
//
LOCUS       WP_457659240             126 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine kinase, partial [Streptomyces anulatus].
ACCESSION   WP_457659240
VERSION     WP_457659240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  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 126)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..>126
                     /product="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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          2..>126
                     /region_name="KdpD"
                     /note="Osmosensitive K+ channel His kinase sensor domain;
                     pfam02702"
                     /db_xref="CDD:460656"
ORIGIN      
        1 mgrgilriyl gaapgvgkty amlseahrrv ergtdcvvaf vehhdrprte vmlhglellp
       61 rreleyrgsv ftemdvdavl erapavalvd elahtnvpgs rnakrwqdve ellragidvi
      121 stvniq
//
LOCUS       WP_457659246            1117 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces anulatus].
ACCESSION   WP_457659246
VERSION     WP_457659246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..1117
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=116122
     Region          126..597
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava tavavalaag mtssavaqpd prgasgaraq drsqggesrq ltlvtgdrvt
       61 vdaqgkpvaf rpakgrehip vqrmsdkght lvipadahrl ivsgkldrrl fdvtelsrpe
      121 nlraqrdglk livgyrgkqa ttakaevrda gstevrrslt slnaesvttp tadapaiwka
      181 ltdrragger vttaagidrv wldgvrrasl dksvpqigap eawkagftgk gvkiavldtg
      241 tdathpdlkg qilaeknfsa akdtkdrvgh gthvasiaag tgaksggkfk gvapdaklla
      301 gkvldddgyg ddsgilagme wavaqgadiv nlslggpdtp evdpleaavd klsaekgvlf
      361 aiaagnegsg agtvgspgsa naaltvgavd dqdkladfss rgprigdgav kpdvtapgvd
      421 ttaaipsgsl iakevgenpa gyatisgtsm atphvagaaa llkqqhpdws yselkgalta
      481 stkpgaynpf qqgsgriavd raiaqtvvad pvsvsfgvqq wphtddepat ekvtyrnlgt
      541 sdvtldlkvt gtgpagkpap agfftlgtdk vtvpaggtae atltadtrlg gtadgtysay
      601 lvatgggqtv rtaaaverev esyevtvkhl grdgrpavya dstlyrfgvd sgdpflspqv
      661 vdgtakirvp kgtyvvnstv yndpddvtkg adwiarpkva vtenttltfd arkakpvkit
      721 vpdakaksrl fspdyvveea nsavsfgwlt espaairtlh sgpkitdgsl aqhwvstwsk
      781 gasteydiav ggtvkqlatg fdrkfttaql akvkitmgsa apkkkgsita fpflptqggg
      841 watsieqklp gtrtlyvsta dkaawsfdfd qqgpadadgw ptyeanyqvg aesrykagkt
      901 yaktvntgvf gplldnknyg ivregnditg alplladgrg naggmlfssa ktvlyrngkk
      961 lgqngdpvag gesfrvpaga adyrltttvk hsakvnplst rvdaawtfrs kktaftmlpv
     1021 stvrftpava adgrvkagkt vsvpvkvhga aagknlkslk tyvsynggkt wkkvtvkkgr
     1081 itvknpakgk aisfaakvtd kkgntssvki ysayfgk
//
LOCUS       WP_457659277             370 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces anulatus].
ACCESSION   WP_457659277
VERSION     WP_457659277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..370
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41215
     Region          71..363
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgsffkdcgc akptrcphpy sirfrdalgk qreesgygtq ddaierltqv yaekkttapt
       61 vaaarrelgq ltvgeyakqw rprqrkmtdy stgehvdssi nvhivprlgs rklnsvtpiv
      121 verfldemeg dgvgrgnqvn ifrvlktvlr dayakgamad dpvkgvqepe yvrgtvaips
      181 layvtkalav adedlaleiv mmagcglrng earavnvnni vaqdvyrvre qihsntlkpa
      241 klkhrktgef revplprsvr eaieryvekh gttkdgyllr gpggyftegm errrvkklfa
      301 dlppedgvgm ygfrhyfasn algngipitd vaewmghksi eetyrtyrhl mpgsitkaar
      361 ildaglwqaa
//
LOCUS       WP_457659284             577 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces anulatus].
ACCESSION   WP_457659284
VERSION     WP_457659284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  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 577)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..577
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=61840
     Region          103..479
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(109,151,154,213..215,219..220,431,433)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(109,151,154,213..214,219..220,431,433)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 mlgrggarap rggggggrgg gggggggppp pasgasptfs vaghhyalvv vtgltpgstt
       61 ayevligsrr vwppddtslp pstittpsaa apespgatpd gvrisfgscr wasapggghd
      121 pvgpdalvtl aarlaadpaa erpdvllllg dqvyadetsg atrrrlaarr dlseppgtei
      181 adyeeytyly deswrdpevr wllstvpscm ifddhdvidd wntsaawqrd mratpwwher
      241 ivsglmsywv hqhlgnlspa elaadpvyaa vraspdgtee lrrfaaetda dpartrwsyq
      301 rvfgrvrlvm vdtraarvla egeramldae eadwlrdavl ddpssydhll igsslpwllp
      361 plvhdaerwn aalcagvrgq rwarfgeklr rasdlehwaa fpesfdrfte llreagsgpd
      421 apatvcvlsg dvhhayiaep rwpksdpglg sgpgtdsgpa pggtpasrvl qltcspvhns
      481 iprsirtgfr fgwsragrri grllsrhgrt gaspvtwhra ggpwfgnqlm tltlhgrksa
      541 ltlvqakask qgaqleavle rsltpeseai fghstec
//
LOCUS       WP_457659290             540 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase, partial [Streptomyces anulatus].
ACCESSION   WP_457659290
VERSION     WP_457659290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..>540
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          2..403
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtlpvalsgs dvigqaktgt gktlgfglpl lervtvpadv eagrakpeql tdapqalvvv
       61 ptrelcqqvt ndlltagkvr nvrvlaiygg rayepqveal kkgvdvivgt pgrlldlagq
      121 rkldlshirg lvldeademl dlgflpdver iitmlppkrq tmlfsatmpg avislarrym
      181 sqpthinats pddegttvkn tvqhvyrahn mdkpemlsri lqadgrglam ifcrtkrtaa
      241 diaeqlekrg fasgavhgdl gqgareqalr afrngkvdvl vctdvaargi dvegvthvin
      301 yqspedekty lhrigrtgra gakgiaitlv dwddiprwql inkaldlkfp dppetystsp
      361 hlfeelgipa gtkgvlprae rtraglraee vedlgetggr grkaaapapa reereprtrt
      421 prqrrrtrgg svaeegaatv papaketspv asvapagdaa sddaprtprr rrrtrvsaae
      481 avaeaavava eapaaraphk aphpprgrhp ppparahasg ppglalrlga vgprppvpaa
//
LOCUS       WP_457659307             474 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein, partial [Streptomyces anulatus].
ACCESSION   WP_457659307
VERSION     WP_457659307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  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 474)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18742127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         <1..474
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          91..218
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          108..140
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(109..110,113..114,116,148,151..152,155..156,
                     158..159,182,185..186,189..190,193)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          146..176
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          181..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          186..452
                     /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          214..239
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          253..279
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(255..256,259..260,262,286,289..290,293..294,
                     296..297,319,322..323,326..327,330)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          284..314
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          318..341
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          422..451
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 gpnsaapara prssniehsg gksvhpdhte ppyqppsspr rsrrlrsilf tlalgaamfa
       61 agavmlapdq ttasrpsgqg qpagapprgs iealqarvar lpedsggwaa lgmayvqqar
      121 ttadpatydr aekalrtsft vqaegntdae igmgalsaar hdfptalrwa rkattsgpys
      181 ssaygvlada ytqlgryeea dkavqkmtdl rpdaaslara syafelkget draralmrrs
      241 laaaatladt sfahnvlatl dlqdadpraa larartglra apgdsallet rarahmalgn
      301 ttkaiadfra aiaiaplphy llglgeleqs lghreqaeaq ytllraqdri raaagdpadt
      361 dailfeadhg dprravtmag qtlrtrpfva vqdayawalh ragrdaealv qadralatgm
      421 psalfhyhra aihhalgdte aarrdltral repgfhplha daahdllqri dttp
//
LOCUS       WP_457659288             320 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces anulatus].
ACCESSION   WP_457659288
VERSION     WP_457659288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..320
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34677
     Region          4..319
                     /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 mkqrtvlvvl fdgiqsldat gpmevfagas rspgvsydlr tasldggpvr stcglalvpd
       61 ssladapaph tllvpggqgt rgshpeltgw lrehgpraer lvsvctgall laeaglldgh
      121 rvtthwnyce rlardypavr vdpepifvrd grlatsagvt agidlalalv eedhgrdlal
      181 diarhlvvfl rrpgnqaqfs aqlsaqtarr eplrevqhwi tqhpdadlgv dalaararls
      241 prhfarafra etgttpgryv ervrleharr lledtadgve riarasgygt peamrrafvk
      301 tlatapaeyr rrfrtpasst
//
LOCUS       WP_457659318             227 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator, partial
            [Streptomyces anulatus].
ACCESSION   WP_457659318
VERSION     WP_457659318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  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   2  (residues 1 to 227)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..>227
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [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          1..>194
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 makvtrddva rlagtstavv syvinngprp vapatrervl aaikqlgyrp drvaqamasr
       61 rtdligmivp darqpffaem ahaveqaaae rgkmvlvgns dyrderevhy lraflgmrvs
      121 glilvsqgps eraaaeieaw darvvllher peaiddvavv tddvggaqla trhllehgna
      181 yvaclggtee tpagggprap praggrraqa qwgrgppgrr vpgpghp
//
LOCUS       WP_457659323             286 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Streptomyces anulatus].
ACCESSION   WP_457659323
VERSION     WP_457659323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..286
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29600
     Region          3..256
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 msiadegagp ygitagpdga lwltfahsgr iarltldgel heypleppgc rptviapgpd
       61 galwftrsqd hrigritvdg etesfpvptp dsgpfgitag pdgamwftem ntdrigrits
      121 tgeitefalp ctgaypsait agpdgalwft lnqanaigri tvhgdivihp lptpsaapvg
      181 itsdgaalwf veiaagqigr isvdgtveef plpdraarph aivavstgdc wftewgansm
      241 gritgsgkvt eyglpspsse phgialgpdg alwaalesgg varlep
//
LOCUS       WP_457659362             403 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces anulatus].
ACCESSION   WP_457659362
VERSION     WP_457659362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..403
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45213
     Region          71..380
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 magarrrnpn gsgtvtlrsd gryqtavyvp qpdgtrkrkf aygktfdecd rkrrdlldra
       61 aagvptptrd mtlgqwfdyw levivkpnlk yrswetyeqa vrnhlrpllg skvmlklgvk
      121 elrgdvqrla eakgaktakh alrvlsaalt aamvediglt rnvaklvhvr astdsgkswd
      181 avtvlrflaa arrltvyypa fllicllglr raevcglrwe nidldnrvvw ieqqrqrasa
      241 gtidvspkse tskavlplpa qciaplrwtr mrtamlrera isrgrpwfed pekhvfisrt
      301 gqpllasnly ltmqrilria glgkmnlkgl rkscgtllvh lkvhpriika vlrhsriatt
      361 ldiyaealdp dvveavaqld rllrqpsrll eldttasegp dag
//
LOCUS       WP_457659363             534 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein, partial [Streptomyces anulatus].
ACCESSION   WP_457659363
VERSION     WP_457659363.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Plisson,C., White,H.E., Auzat,I., Zafarani,A., Sao-Jose,C.,
            Lhuillier,S., Tavares,P. and Orlova,E.V.
  TITLE     Structure of bacteriophage SPP1 tail reveals trigger for DNA
            ejection
  JOURNAL   EMBO J 26 (15), 3720-3728 (2007)
   PUBMED   17611601
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         <1..534
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
     Region          <1..261
                     /region_name="COG5412"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444167"
ORIGIN      
        1 dpigflgnlv kavgaglnlf itniadhlkt gvvswllgta vkagldlpar fdlkgiiqli
       61 gsmlgltwdn irtrvtrkgv pdeamsavet svpvaknlaa egpagavkei qaeagdlkat
      121 ilgklttyli ptvliagitw iisllnpasa fvravkgiid ivtfivtqga qiadfvnavl
      181 daviaiangg qagvpkliea alassvplli gflaallgig glankvksvf qsvsrpvtra
      241 idkivdfiak kgkalwdklk kngkegaapa vdnkknpggk pkgrdgeqqk kpirfafamq
      301 gephrltltr sgrllmassr eqallakiea amgsvsdqdq ieslsnlwrl tsallgrgen
      361 atqeqvreha relekygdqy gkddiapesd epgrpnrtpv erpakkdrks tprllklade
      421 hrgagcvail tvdsrtyegw sagrpesdld sqalsdirsh spahtlgcae vhcisqaygk
      481 eykknvnelp veftaiemvh adryekpnsw yqkpfpacsh cspmleglki ttmn
//
LOCUS       WP_457659369             215 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane protein [Sinorhizobium medicae].
ACCESSION   WP_457659369
VERSION     WP_457659369.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..215
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22680
     Region          75..215
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mirnvlvaif aafmlggkah aadlaqppep tptvetvhsf vwtggylglq ggggwlnsdl
       61 svpggggskr fsggllgafa gynyqhgdwv vgvegdvsyn wndetvtvfg tntdvgmdvs
      121 gsvrarlgyt vndrtllyat ggwavtrgfv dvagapkeke tfngwtiggg vdygftdsvf
      181 graeyryndf sdkdvggvnv dldqhqftig vgvkf
//
LOCUS       WP_457659387             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659387
VERSION     WP_457659387.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77114
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklseg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457659376             307 aa            linear   BCT 27-JAN-2026
DEFINITION  SEL1-like repeat protein [Sinorhizobium medicae].
ACCESSION   WP_457659376
VERSION     WP_457659376.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 307)
  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 307)
  AUTHORS   Mittl,P.R. and Schneider-Brachert,W.
  TITLE     Sel1-like repeat proteins in signal transduction
  JOURNAL   Cell Signal 19 (1), 20-31 (2007)
   PUBMED   16870393
REFERENCE   5  (residues 1 to 307)
  AUTHORS   D'Andrea,L.D. and Regan,L.
  TITLE     TPR proteins: the versatile helix
  JOURNAL   Trends Biochem Sci 28 (12), 655-662 (2003)
   PUBMED   14659697
REFERENCE   6  (residues 1 to 307)
  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 12218275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="SEL1-like repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33225
     Region          7..36
                     /region_name="SEL1"
                     /note="Sel1-like repeats; smart00671"
                     /db_xref="CDD:214772"
     Region          26..56
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          54..293
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          63..92
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          99..128
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          138..164
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          171..200
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          207..236
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          243..272
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mlvaltvkaq vnlgglyfdg egvaqdyaea arwfrkaaed gaaalaelnl gvmyehgrgv
       61 apdpaeaarw ygraaehgda qaqhrlglmy fkgegvkrdh vqaarwyraa aaqgnpsaqf
      121 hlgsmylqgq gvpkepseaf rlfrgagglg henaqynlgl mylngigvqk dldksvrwfr
      181 aaaeqksalg qynlalmyan gtgvaknsee aarltslaah qglamaqhnl giayisgagv
      241 ekdsaaavhw fqkaaqqgha raqfnlammy argegvarnd alafewmqka anqlpearqy
      301 ldrtrke
//
LOCUS       WP_457659391             175 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457659391
VERSION     WP_457659391.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 175)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..175
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=18726
     Region          4..>106
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mpairkldir nfrgiknlsw tpspgfncli gpgdsgktsv ldaidlclga rriaaftdad
       61 fhdvdvsqpi sitvvlgale dalksidayg dflrgynagk neledepasg lettlclrlt
      121 vaqdlepvws lessraaakg ldrnlkwadr erlsplrlga ggrqssgmas riave
//
LOCUS       WP_457659392             274 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457659392
VERSION     WP_457659392.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 274)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..274
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=28898
     Region          <28..210
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mnklsdekpn tsgvlsaaar earttfgdka kdqlkdaidi vnatakhlgi svgstataml
       61 dihsvafgsg sislhdesgi plrgmgtgsk rlltaglhke asksksiali deietgleph
      121 rivrflkslg skdteptmqv fatshspial qelsshqvfi vrqdkaggqt lvlsapsevq
      181 galratsssf laksvliceg kteigfirgi dlfrtevrgk esidaagvlv trlrwgignt
      241 airkgegvsg agisrrdlhr qrqacsgsrg edvc
//
LOCUS       WP_457659398             596 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease [Sinorhizobium medicae].
ACCESSION   WP_457659398
VERSION     WP_457659398.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..596
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..596
                     /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=62805
     Region          7..520
                     /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 miefvaenla pimfvslivf lllgypvafs laangllffi igvelaplsn sinlswplln
       61 alperfwgvm sndtllaipf ftfmgivler sgmaedlldt igqlfgpvrg glayavifvg
      121 allaattgvv aasviamgli slpimlrygy drrvasgvia asgtlaqiip pslvlivlad
      181 qlgrsvgdmy agalipglil tslymgyill msflkrdsmp alpleartlg sgvtsllval
      241 vvaagiayaa hvyfsptqge nadilgatvg vlfiylvala drafkinals rlaqqviivl
      301 ipplaliflv lgtiflgiat pteggamgav galvmaaakg rlsmeviraa lasttrlsaf
      361 vlfiligarv fsltfygvng hlwvehllta lpggeigfli avnvlvffla ffldffelaf
      421 iivpllapaa dklgidliwf gvllginmqt sfmhppfgfa lfylrsvaar vpyldkvtgk
      481 rmqpvttgqi ywgavpfvci qiimvaltlm fpqmvlhykg tgsevdpsti kievpgfgsg
      541 gggltlpdng gglglpgglq lpggspldes rqpaqpdtap kqnntapdls appsfn
//
LOCUS       WP_457659402             538 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659402
VERSION     WP_457659402.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..538
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59055
     Region          41..514
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mrnlllagvc aaalmgnpaf addikqggem tvtykddvst ldpaigydwq nwsmikslfd
       61 glmdyvpgtt elrpdlaeay eisgdgkift fklrqgvkfh ngreltaedv kysiervvnp
      121 ttqspgagff ssikgfedvs agrggdlsgi avqdphtirf elsrpdatfl hvmalnfahv
      181 vpkeevekhg adfgknpvgs gafklaewtl gqrlvferfa dywneglpkl dritfevgqe
      241 pvvallrlqn geidvpgdgi ppakfvevtk dpnfkeliiq ggqlhtgyvt mnvkmapfdk
      301 vevrkavnma inkdrilrii ngravaanqp lppsmpgyak dykgyaydpe gakklleqag
      361 lgdgfstely vmntdpqpri aqaiqqdlka igitasiksl aqanviaagg eenqapmvws
      421 ggmawiadfp dpsnfygpil gcggavpggw nwswycneel dkkaaeadai vdpakaaere
      481 amwrdiyvki medapwapif neerftirse riggddklfv dpvhipvhyd qvyakdvq
//
LOCUS       WP_457659411             306 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659411
VERSION     WP_457659411.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..306
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34110
     Region          18..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mkslfrqrsg vfskittvpf lllvigvggy swaqvivmaf srlrieagqf vwspagfdnf
       61 rdilandval ysvavttifv iatvwlsvll glllallvqr skrfnrlaqv vllwpamvap
      121 vvvsliwlli lspnigvlnk lldtfmlptq dwlgmevgai vaivivdvwh wtpvaflmly
      181 talcavdeea veaarcdgan ewqviryvki pmlmpailgt ifiravmgvk afdemyllta
      241 ggpnnattlv slhirdvffd qlnygygsaf svlivllmsl iialvltvrt lrhsrffmre
      301 vqndrr
//
LOCUS       WP_457659427             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659427
VERSION     WP_457659427.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77129
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvakypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drrgkpkkqk wlsrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslggayrwg vpywtdeewd aiadrlgrle apqqgdledr lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457659412             510 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfatase [Sinorhizobium medicae].
ACCESSION   WP_457659412
VERSION     WP_457659412.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Stam,M., Lelievre,P., Hoebeke,M., Corre,E., Barbeyron,T. and
            Michel,G.
  TITLE     SulfAtlas, the sulfatase database: state of the art and new
            developments
  JOURNAL   Nucleic Acids Res 51 (D1), D647-D653 (2023)
   PUBMED   36318251
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Ghosh,D.
  TITLE     Three-dimensional structures of sulfatases
  JOURNAL   Methods Enzymol 400, 273-293 (2005)
   PUBMED   16399355
REFERENCE   3  (residues 1 to 510)
  AUTHORS   O'Brien,P.J. and Herschlag,D.
  TITLE     Functional interrelationships in the alkaline phosphatase
            superfamily: phosphodiesterase activity of Escherichia coli
            alkaline phosphatase
  JOURNAL   Biochemistry 40 (19), 5691-5699 (2001)
   PUBMED   11341834
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Parenti,G., Meroni,G. and Ballabio,A.
  TITLE     The sulfatase gene family
  JOURNAL   Curr Opin Genet Dev 7 (3), 386-391 (1997)
   PUBMED   9229115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..510
                     /product="sulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0008484 - sulfuric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58951
     Region          1..352
                     /region_name="sulfatase_like"
                     /note="uncharacterized sulfatase subfamily; cd16148"
                     /db_xref="CDD:293767"
     Site            order(9..10,49,94,96,200,278..279)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293767"
     Site            order(9..10,49,94,96,200,279)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293767"
ORIGIN      
        1 mraifvlfds lnrtavgryg anavktpnfd rfaerattfd shfvgslpcm parrdlhtgr
       61 lnfmhrswgp lepfdnsfpe llgkcgvhsh litdhlhyfe dggstyhtrf rtwdfirgqe
      121 ddpwkamvqp plerfkemys ekhydfddpw krmqsavnre fvrgeheypg prcfksalef
      181 ldlnraaddw flmvecfdph epfaaperfk eqyatgwegg vldwpkyekv vdspeeiaei
      241 ranyaalvtm cdeyfgrlld yfdehdlwkd taiilstdhg fllaehdwwg knrmpyyaei
      301 sqipliiyhp ehaggggarr saltqtidlm ptfldlfgid vpqevqghsl lpllkedrsm
      361 rdvaifgvfg gpigstdgry tyylypedly gpdlheytlm pmhmtslftp eelktsalta
      421 gfnftknmpv lridalrdar ripnndrvgw svdlgttlyd lhldrtqmrp frdseielrl
      481 segirsvlia hdapeeyyrr yglaamdvgs
//
LOCUS       WP_457659415             264 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659415
VERSION     WP_457659415.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..264
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30315
     Region          <20..64
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(21..22,33,36,40..41)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mpqddifatn lrfacatrrs isqvcreigi nrqqfnryis gearpsahnv ariaaffgls
       61 addfllppkl fearmirper hrleagqlle gfpgdaaalr rhfgyyqtyh lslswpgfvv
      121 cscahiyeeg gsirvksier irdraneieq fskyvglvtf wrnrifiaer tvgqaamlaq
      181 tilmpfelhq rvylrgttmg vswrkenlpy asrmiwrhig qdpdkrqmls rcglvpfgar
      241 hlpsavrrfl evpeaevlti pvey
//
LOCUS       WP_457659416             743 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Sinorhizobium medicae].
ACCESSION   WP_457659416
VERSION     WP_457659416.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 743)
  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 743)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..743
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81385
     Region          2..475
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mlggelsrta lalwphqhaa ldtveayfvs asaraclvnm ptgtgktgvm atiarqraqv
       61 rpvlvvcpsa alveqliaqf edrfwdkiga spvwkpdrvw nvlpsdiesl tkrldghgge
      121 rvivvgtvqa iqqidadgki dqlhgrigti lfdeghrepa pswarvvrgf avptvlfsat
      181 pfrgdlkifd vdddhihflg fadavdqgli rgveideqpl plspddyala liarvdalva
      241 egrftaankv ivrcdseelv temhqaltag lagraagvla ihhnfrerpd dgifdavprd
      301 laaraerfli hqfmliegid dprctmlaly epftntrmlv qqigrlirhp gpigdaapaa
      361 yvlapkgrdi anewnsflaf daaskangnk pfvrndatil enliaalptl dyvmgrfrer
      421 pdlddpglhd dlrfpsaava ftiepdldld elqkaikael iredrhealt grtadgncry
      481 hitlrltpsp flsgslfqap sleatiyakk nkrlfffdsa glwineldgi gprvnaktlr
      541 allpdgydns isfmsvkntd lgplalrsrs lsarsldrsg vfmgehlnvv tratgyihpk
      601 aaedgirrav gfsrsrvrdg kgndltaqqa aicrlvrhgr cparrrrpds iglhplrrsr
      661 ygscghdaaq hsrrhgrdgr svrsqgadrg gqdrgsvcrg rgghrpqgag avpfppacrw
      721 rgasgldrle rqegkilagv awt
//
LOCUS       WP_457659428             300 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457659428
VERSION     WP_457659428.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..300
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31554
     Region          3..284
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtriqanlfl lfsgaiwgag fvaqstamea igplwfiglr faiaalvalp lallekrqaa
       61 tplprhamln fvfiglalfg gavtqqygll tttvtnsgfl tglyvvfvpv ltvvflrrrp
      121 hwviwpaall atfgifllsg galsaltggd mltivcalfw avqlmlvgif apatgrpmll
      181 smtqfavcai agcvlaglfe plslaaikga lpqilyagvf ssgiaficqv vgqryttapq
      241 aaiflsseal faalfgvlll getitpvgyv gcaviflaml avelipeltk krreaakaav
//
LOCUS       WP_457659429             183 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Sinorhizobium medicae].
ACCESSION   WP_457659429
VERSION     WP_457659429.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..183
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20224
     Region          40..178
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mstkltyiav cfvtayrskg ndcvagqtkn kslginndpe ddegtidfei iellffayrd
       61 ftgdpdaile ksgfgrahhr vvhfvnrepg mtvadlldtl kitkqslarv lkqlidsgyi
      121 rqvtgpedrr qrmlyttteg ralaralaep qsrriadala kagpgaretv krflanmmnd
      181 tvg
//
LOCUS       WP_457659431             310 aa            linear   BCT 27-JAN-2026
DEFINITION  ribose-phosphate pyrophosphokinase [Sinorhizobium medicae].
ACCESSION   WP_457659431
VERSION     WP_457659431.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Becker,M.A., Smith,P.R., Taylor,W., Mustafi,R. and Switzer,R.L.
  TITLE     The genetic and functional basis of purine nucleotide
            feedback-resistant phosphoribosylpyrophosphate synthetase
            superactivity
  JOURNAL   J Clin Invest 96 (5), 2133-2141 (1995)
   PUBMED   7593598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..310
                     /product="ribose-phosphate pyrophosphokinase"
                     /EC_number="2.7.6.1"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004749 - ribose phosphate
                     diphosphokinase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0006015 - 5-phosphoribose 1-diphosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009156 - ribonucleoside monophosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0009165 - nucleotide biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33375
     Region          1..310
                     /region_name="PRK01259"
                     /note="ribose-phosphate diphosphokinase"
                     /db_xref="CDD:234929"
ORIGIN      
        1 mkvfagnsnr llaeaicnyl nlplgkatvr rfadqeifve igenvrgedv fivqstsfpt
       61 ndhlmellim idavrrssar ritavlpyfg yarqdrkpgp rtpisaklva nliteagadr
      121 vltldlhagq iqgffdiptd nlyaipilar dvkenynlkn vmvvspdvgg vvraralakr
      181 ldcllaivdk rrdrpgesev mnvigevngk dclliddivn sggtlcnaae allkngatsv
      241 tayithgvls ggavarvtss mlkelvitds iqpttavqsa hnvrvistaa llgeaisrts
      301 qeesvsslfd
//
LOCUS       WP_457659434             542 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659434
VERSION     WP_457659434.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..542
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59655
     Region          1..527
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mttdklltvc glslevagsg hqvvksvsfd lapgeifgiv gesgsgktla trslisllpp
       61 nitvtggsvt ykgrdvlklk ekelrhlrga eigvvfqepm tslnpsmtig rqleeglvlh
      121 tkapaqerrl cildmlkrvg irdpegalas yphefsggmr qrimlasvml lkpalliade
      181 pttaldaviq rdvmelmvel traegtavll ishdlpmvar ytsrivvmek gaiveqgrte
      241 dlltapqhpy trkllsslpf rgeprridts kapmisarei ivdyagrksl frknkpkral
      301 hgvsidiyeg evvalvggsg sgkttlgrti aglvkedegr iqfqgrlrte nwadyrlncq
      361 mvfqdpyssl dprmtiqalv eealrlvpgl dgnakrkrsl etleevglgm eyagryphel
      421 sggqrqrvai araiarrprf liadepvsal dvtvraqvld lfsdlqkryg fsclfishdl
      481 gvveqvadrv vvmqdgriie egardsifds pkeaytrrll saipaldqne nggvtlkwrl
      541 en
//
LOCUS       WP_457659438             181 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine hydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659438
VERSION     WP_457659438.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..181
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19085
     Region          5..161
                     /region_name="nicotinamidase_related"
                     /note="Nicotinamidase_ related amidohydrolases. Cysteine
                     hydrolases of unknown function that share the catalytic
                     triad with other amidohydrolases, like nicotinamidase,
                     which converts nicotinamide to nicotinic acid and ammonia;
                     cd01014"
                     /db_xref="CDD:238496"
     Site            order(10,85,118)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238496"
     Site            113..114
                     /site_type="active"
                     /note="conserved cis-peptide bond [active]"
                     /db_xref="CDD:238496"
ORIGIN      
        1 mskravivvd lqkdylasgk falvgmdaai enaarivama rrsgdlvinv rhegptdapf
       61 fvsgtegaei vpamtpqege avitknypna fretnladll ssaaiedvti igamshmcid
      121 ataraaadlg ykttiiqdac atrdleyrge avpaakvhaa fmsalafgyg kvlstdeyla
      181 k
//
LOCUS       WP_457659440             433 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457659440
VERSION     WP_457659440.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45526
     Region          30..371
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(58,108..109,111..113,116,136,139..140,143,210,
                     213..214,217..219,222,246,250,301..302,306,310,326,
                     329..330,333..334,337)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mrnnllpvaa lllgtlflfl gnglqglllp vrgtaegypt tilglfgtlw atgfvlgcff
       61 apnivkrigh vrafsvftal iaivslltgi lidpiwwlal ravtgfstag tsmiieswln
      121 eratnesrgl ifslyiaitl fgvvggqmmi pfgetsttff fmicgilycv amlptlmsra
      181 aspqplkqvr ldlrglysns pvsflgilli giangafgtl gavfgrqagl sdstvaamms
      241 vaifsgavmq lpagrisdrv drryvlaala gigalagllm flvepsqvwi vltliaiyga
      301 aanalypiav shandfatae dfvkvsggll llygvgtiig ptiggplmta sgpyglfmit
      361 acahmlitay aivrsrrrap vpaadrenfs pvnagtattp eslqlspraa pmeelaegga
      421 gdpqeeeksn epv
//
LOCUS       WP_457659442             500 aa            linear   BCT 27-JAN-2026
DEFINITION  xylulokinase [Sinorhizobium medicae].
ACCESSION   WP_457659442
VERSION     WP_457659442.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..500
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53498
     Region          6..494
                     /region_name="XylB"
                     /note="Sugar (pentulose or hexulose) kinase [Carbohydrate
                     transport and metabolism]; COG1070"
                     /db_xref="CDD:440688"
ORIGIN      
        1 mqpderyvig ldsstqsvka vawtadgtpr aegraphris tphplkaeqn aedwwsaacd
       61 alssllrqid shrvdgvais nqretmvllg vdrkplspat lwldrraqdi vqpfadefgs
      121 erlhaisgkp idvipcvyrl ryyrqhepel ldraaqilsv hdfltqkltg eaaaswtsad
      181 pfgildteak qwsreildhl diplsklppl hrpgtligrv tadaaaatgl aagvpvyagg
      241 gdghcaglgv nviepgvvyl nlgtavvggc wtptrklsry wrtlvspsge gyllescqrg
      301 gayfvnwlld tfaggrsdpa iferleaeaa sldvgsggvt vcsylmgcmd phwdadarat
      361 fsgmgpetgm ghlyrasmea itlefvrsls emksmgvaad rifvigggag salwrqmiad
      421 asglpvirsl sneasalgag msaaigagwy ghfgeaagam srlaeqidpr paaaqawaal
      481 srrqanlyqa trrldaydgp
//
LOCUS       WP_457659445            1116 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces anulatus].
ACCESSION   WP_457659445
VERSION     WP_457659445.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..1116
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=115825
     Region          126..597
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrnacipava tavavalaag mtssavaqpd prgasgaraq drsqdgelrq ltlvtgdrvt
       61 vdaqgkpvtf rpakgrehip vqrmstkght lvipadahrl ivsgkldrrl fdvtelsrpe
      121 nlraqrdglk livgyrgkqa atakaqvrda gstevgrslr slnaeslttp tadapaiwka
      181 ltdrragger vttaagidrv wldgvrkasl dksvpqigap eawkagftgk gvkiavldtg
      241 tdathpdlkg qilaeknfsa akdtkdrvgh gthvasiaag tgaksggkfk gvapdaklla
      301 gkvldddgyg edsgilagme wavaqgadiv nlslggpdtp evdpleaavd klsaekgvlf
      361 aiaagnegdg agtvgspgsa naaltvgavd dqdkladfss rgprigdgav kpdvtapgvd
      421 ttaaipsdsl iakevgenpa gyatisgtsm atphvagaaa llkqqhpdws yselkgalta
      481 stkpgaynpf qqgsgriavd raiaqtvvad pvsvsfgvqq wphtddepat ekvtyrnlgt
      541 sdvtldlkvt gtgpsgkpap agfftlgtdr vtvpaggtae atltadtrlg gtadgtysay
      601 lvatgggqtv rtaaaveree esyevtvkhl grdgrpaaya dstlfrfgag agdpflspqv
      661 vdgtakirvp kgtyvvnstv yddpddvtkg adwiaqpkva vtknttltfd arkakpvnvt
      721 vpdakaksql fspdylvete tdavsfgwvm dspagmrtlh agpqitdgsl aqhwsgtwsk
      781 gasteydiav ggkvkqlatg ysrkftagql akvkiamgas apkkkgeita wgnlptqggn
      841 wataieqklp gtrtlylsta dkvawsfdfn qigpadadgw ptyeanyqig keakykpgka
      901 yaktvntavf gplvskdfgi fregneiggv lplladgrgn aggvalssvk tvlyrngkkl
      961 gqnsdplagg evfrvpagaa dyrlttsvkh sakisplstr vdaawtfrsk katstmlpvs
     1021 tvrftpavga dgrvkagktv svpvkvhgaa agknlkslkt yvsynggktw kkvtvkkgki
     1081 tvknpakgka isfaakvtdk kgntssvkiy saylgk
//
LOCUS       WP_457659455             286 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Streptomyces anulatus].
ACCESSION   WP_457659455
VERSION     WP_457659455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..286
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29540
     Region          3..256
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 msiadggagp ygitagpdga lwltfahsgr iarltldgel heypleppgc rptviapgpd
       61 galwftrsqd hrigritvdg eiesfpvptp dsgpfgitag pdgamwftem ntdrigrits
      121 tgeitefalp ctgaypsait agpdgalwft lnqanaigri tvhgdivihp lptpsaapvg
      181 itsdgaalwf veiaagqigr isvdgtveef plpdraarph aivavstgdc wftewgansm
      241 gritgsgkvt eyglpspsse phgialgpdg alwaalesgg varlep
//
LOCUS       WP_457659458             331 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Sinorhizobium
            medicae].
ACCESSION   WP_457659458
VERSION     WP_457659458.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..331
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.94"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=33722
     Region          11..326
                     /region_name="gpsA"
                     /note="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase; PRK00094"
                     /db_xref="CDD:234629"
ORIGIN      
        1 mkmknpktgp kivvvgagaf gtalaavaad kanvtllarr eeaaeecrrt grneaalpgi
       61 plpaglsyss qaaalgdahi vlfampsqah rdaarrygda igakaivvtc akgmeqstgr
      121 lltdvldeel pgrrigvlsg pgfaadiakg lptamviaap draiatelae vlsgrtfrly
      181 psadrtgvql ggalknvlai acgivegagl gdsaraalis rglaemsrfi varggdadtv
      241 rglsglgdlv ltatshqsrn lrfgitlgks graegsgelv egafaasvaa rvagelgidm
      301 pitkavaaiv dgkldvrsal eqlmsrpith e
//
LOCUS       WP_457659472             370 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces anulatus].
ACCESSION   WP_457659472
VERSION     WP_457659472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..370
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41540
     Region          71..363
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgsffkdcgc akptrcphpy sirfrdalgk qreesgyatq ddaierltqv yaekkttapt
       61 vaaarrelgq ltvgeyakqw rprqrkmtdy stgehvdssi nvhivprlgs rklnsvtpiv
      121 verfldemeg dgvgrgnqvn ifrvlktilr dayakgamad dpvkgvqepe yvreqvaips
      181 layvkkaltv adedlaleia mmtgcglrng earavnvnnv vakdvyrvre qihsntlrpa
      241 klkhrktgef revplprsvr eaieryaeky gttkdgyllr gpngyytepm errrvrrlfa
      301 dlppeegvgm ygfrhyfasn algggipitd vaewmghksi eetyrtyrhl mpgsitkaar
      361 ildaglwkaa
//
LOCUS       WP_457659464             317 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659464
VERSION     WP_457659464.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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   4  (residues 1 to 317)
  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 10006830
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..317
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32432
     Region          21..306
                     /region_name="COG2984"
                     /note="ABC-type uncharacterized transport system,
                     periplasmic component [General function prediction only]"
                     /db_xref="CDD:442223"
ORIGIN      
        1 mrsllialaa tvalslpara devtvavtai vehpaldaar dgvkdalaaa gykegenlkf
       61 iyelaqgnpa taaqiarqfa geapnvivpi stpsaqavvs strdipvvft avsdplgaql
      121 vkdmekpggn vtglsdlspv aehvalikei lpnvktigfl ynsgeansvs llavlkeeae
      181 kaglsviesa atksaevqga aralvgradv iyiptdntii salegavava eesklplfta
      241 dtdsvsrgav aalgfnyydv gkqtgevvvr vlkgenpgdi avkvaagtdl vinkgaatrm
      301 gitlpesvvg ratrtie
//
LOCUS       WP_457659462             325 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar-binding transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659462
VERSION     WP_457659462.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..325
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35105
     Region          11..312
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 msedddalmv raawfyyvgg lnqemtaarl gltrarvnkm laearesglv sisidhrrvg
       61 vlpledrlrt rfgldfcist pafgfhdtsk qdsevrkqia fravgvaaan hlktllsend
      121 sltvgtgwgr tieqmtlhla gvrapharfi simgsltann aynpfevvhs larrtggegy
      181 flpvpfians vddkkvlisq rsvvkaleia rsasvcfisa gelteesllr rqgmisgtel
      241 eslrqagavg dtngiffdse grqvdhelne rtialgfeel kalpvlllia glekiqaara
      301 llrsgvvngl iidgdaaeal aalge
//
LOCUS       WP_457659473             429 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457659473
VERSION     WP_457659473.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..429
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47928
     Region          6..334
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdnkrrfalv gtgnrgttmw gkdllagwrg lvdlvaiadt nslraerart miatnapiyd
       61 svdsmlaetr pdlvivctpd dthddivvra lesgadvite kpmsttveki rrileaekrt
      121 grrvdvsfny rfaptaarik ellnageigr itsvdfhwyl dtrhgadyfr rwhayaersg
      181 slfvhkathh fdllnwylds dpdsvgafad lqmygrkgpf rgprcklcph ksecdfyldl
      241 eadpfldaly eepseingyf rdgcvfredi dipdtmvani ryrndvhvsy slntfqpieg
      301 hhiafngtkg rielrqyedq pweappedvi llvrnfpkgk aaveritvph sagghyggdd
      361 rlrntlfkpg atdplgqrag aragamsvlc giaalesark gkvvrladlm pelfveetqa
      421 vsrlaanga
//
LOCUS       WP_457659465             322 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659465
VERSION     WP_457659465.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..322
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33351
     Region          8..304
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mnavtssakl hdcrdafvtv lerlsadnpr ivavcndfvg ssklggfrar wpdrlvnvgi
       61 aeqnmvgvga glanggllpf vcgaacfltg rsleqikadi aysnanvkli gissgmayge
      121 lgpthhsied fawtrvlpnl pviapcdsve taaavewaah ydgpvflrls rvgvpdllps
      181 ghtfelgkan llrdgdaitl vangtvthri lkaadllaae giearvlnma tvrpldldav
      241 vaaaretgai ltaeehstfg glgsavaelv vaeapvpmki lgvpgifapt gsaeflldef
      301 gmspaaiaea avaliarkps ra
//
LOCUS       WP_457659460             286 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Sinorhizobium medicae].
ACCESSION   WP_457659460
VERSION     WP_457659460.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..286
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30986
     Region          1..275
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mkpqdtftth hrghgiflar gadpkrmmae iggketgycr gkggsmhiad malghlgana
       61 ivgggipavi gaglssrhlk qdsvsiaffg dgamqqgily esmnmaslwn lpvlfvcinn
      121 qygmgtridq atrntafdqr akafglngav vdgldveevq aaarwlvdea ragkpgflsv
      181 evyrffghar mdkspyreea eelegrkkdp vlfarnklid tgieeerild eldkaiaaem
      241 datidfaves kapplgsmfk dvyaagepep esvraridrv lardda
//
LOCUS       WP_457659476             304 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659476
VERSION     WP_457659476.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32877
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..296
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(102,104..105,109,167,206,271)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(103,106..107,110..111,114..115,117..118,121..122,
                     124..128,130,193,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 mpkpdlnllv tldvllaegs varaakrlrl spsamsralq rlrettgdpl lvragrglva
       61 tpralelrer vgrlveeaea vlrpqgklei erlvrtftlr tsdgfvenfg ptllsrlgae
      121 apgvrlcfvq kpnkdsgplr dgsvdletgv laettgpelr tqalfrdrfv gvvrkghgls
      181 rgevtpelya agrhilvsrr gldkavtgid valgaigler eivttvggfs salamarasd
      241 lvasvperht svlragmhsf plpfqvpqit vsllwhprlh adpahrwlrg cirevcgsva
      301 vcrl
//
LOCUS       WP_457659474             488 aa            linear   BCT 27-JAN-2026
DEFINITION  CpaF family protein [Sinorhizobium medicae].
ACCESSION   WP_457659474
VERSION     WP_457659474.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..488
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53615
     Region          88..473
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mfgkrgnegp gkggargftp apsipavela vverpsapdy gepaappsrp qaaappqrrr
       61 paraedyydt ksqvfsalid tidlsqlskl diesareeir divndiitik nfamsiseqe
      121 ellddicndv lgygplepll arddiadimv ngagqtfiev ggkveeleir frdngqllsi
      181 cqrivsqvgr rvdesspicd arlpdgsrvn viapplaidg taltirkfkk dkltleqlvr
      241 fgsvtpeaav llqiigrvrc nivisggtgs gkttllnclt ryidsnerii tcedsaelql
      301 qqphvvrlet rppniegege itmrdlvknc lrmrperiiv gevrgpevfd llqamntghd
      361 gsmgtihant preclsrmes miamggytlp artvreiisg svdviiqasr lrdgsrrith
      421 itevvgmegd viitqdlmry eidgedangr ivgrhvstgi grphfwdrar yfnedkrlaa
      481 tldamekq
//
LOCUS       WP_457659483             336 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457659483
VERSION     WP_457659483.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35296
     Region          10..315
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mslppilsgk vrlpivgapl fivshpklti aqckagiiga fpalnarpqs qldewlseit
       61 etlaahdady perpaapfav nqivhksnar leqdlmlcvk ykvpvvissl gavpevnaai
      121 hsyggivlhd vinnrhansa irkgadglia vaagagghag tlspfalvqe irawfdgpll
      181 lsgaiatgda ilaaqamgad mayigspfia teearasday kqmivdsnaa divysnfftg
      241 ihgnylkpsi laagmdpsnl peadpskmdf gqaaegakaw kdiwgcgqgi gavheigtva
      301 rlvdrleqey dtararlgla sgadirrgke fstsrn
//
LOCUS       WP_457659480             761 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent malic enzyme [Sinorhizobium medicae].
ACCESSION   WP_457659480
VERSION     WP_457659480.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Bologna,F.P., Andreo,C.S. and Drincovich,M.F.
  TITLE     Escherichia coli malic enzymes: two isoforms with substantial
            differences in kinetic properties, metabolic regulation, and
            structure
  JOURNAL   J Bacteriol 189 (16), 5937-5946 (2007)
   PUBMED   17557829
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Voegele,R.T., Mitsch,M.J. and Finan,T.M.
  TITLE     Characterization of two members of a novel malic enzyme class
  JOURNAL   Biochim Biophys Acta 1432 (2), 275-285 (1999)
   PUBMED   10407149
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Yamaguchi,M.
  TITLE     Studies on regulatory functions of malic enzymes. IV. Effects of
            sulfhydryl group modification on the catalytic function of
            NAD-linked malic enzyme from Escherichia coli
  JOURNAL   J Biochem 86 (2), 325-333 (1979)
   PUBMED   225306
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..761
                     /product="NADP-dependent malic enzyme"
                     /EC_number="1.1.1.40"
                     /GO_function="GO:0004470 - malic enzyme activity [Evidence
                     IEA]"
                     /GO_function="GO:0004471 - malate dehydrogenase
                     (decarboxylating) (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=82140
     Region          13..761
                     /region_name="PRK07232"
                     /note="bifunctional malic enzyme
                     oxidoreductase/phosphotransacetylase; Reviewed"
                     /db_xref="CDD:235976"
ORIGIN      
        1 mpgidrsdra mtsvtaqeal dfhsqgrpgk leisptkpma tqrdlslays pgvavpvkai
       61 aedpataydy targnmvavi sngtailglg nlgalaskpv megkavlfkr fadvdsidle
      121 vdtddvdefv ncvrflgpsf gginledika pdcfiieqrl revmdipvfh ddqhgtaiia
      181 aaglinaltl tgrdfkstkl vcngagaaai acieliksmg fnpaniilcd tkgviykgrt
      241 dgmnqwksah avetdrrtla ealngadvff glsakgalsa dmvrsmgerp iifamanpdp
      301 eitpeevadi rndaivatgr sdypnqvnnv lgfpyifrga ldvrastind amkiaaaeal
      361 anlakedvpd dvaaayqgnr prfgpqyiip vpfdprlisa ipmavakaam etgvarkpie
      421 dlkaygeqls arrdpiastl qrivervrrq pkrivfaege evqmmrsaia yanqqlgtal
      481 llgreevmre taeregidld ragiqivnar lskrvgaytd flysrlqrkg ylfrdvqrli
      541 ntdrnhfaas mvalgdadgm vtgltrnyst aledvrrcid pkpghrvigv sialcrgrtv
      601 lvadtavhdm ptseeladia eeaaglakrl gyvprvamla ystfghpsge rservreavk
      661 ildrrrvdfe ydgemaadva lnarvmeqyp fcrlsgtanv lvmpafhsas istkmlqelg
      721 gstvigpllv gldksvqias msakdsdlvn laaiaaynag t
//
LOCUS       WP_457659486             385 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457659486
VERSION     WP_457659486.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..385
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43079
     Region          60..348
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mplklvqrkg sdfyyirgtv rgqslfestg trdrevaeai riktesrlln esvhgkkali
       61 tfeeaaesyi asggserfli kvspstgkvs givahfrgkl lknltqsdld aaarilfpta
      121 saetrnrqcy tpfiavwnha agnqwaevrq wkrprkakgt nivklkvrag tkptsydraa
      181 qfvaamspap aqlmtalfyt gmrpiemfll easdvnmpgr witldasktg eprgipihef
      241 lvplfealva rggvlfrshk gdpyppteef ggqissaitg arnrlkkrgv sivdiapyta
      301 rhtvstqlvi nrihpyikdq ilghaaddms rhythvpqqp lidaintlpv pqlwrdqeww
      361 sdpvywsrrl vkwgdpakrr vqkvg
//
LOCUS       WP_457659487             122 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659487
VERSION     WP_457659487.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 122)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..122
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13963
     Region          51..98
                     /region_name="HNH_3"
                     /note="HNH endonuclease; pfam13392"
                     /db_xref="CDD:433169"
ORIGIN      
        1 mssrrdqire kimarvmidp vtgcwnwtgp tsgktgrgkd yprmwlsgqt vpvhlvmwtn
       61 ehgyipgkrq ldhkcrnrlc vnpdpkhtel vthkenqkrr draraamirh nggpplecae
      121 vl
//
LOCUS       WP_457659507             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659507
VERSION     WP_457659507.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77101
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempvia klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkvfki stpmvspgck itsnyqegtq etyhvpcphc
      241 qelqelrwen mrdhidpahp eqahfvcihc gceihehhre wmvkpengak wvakypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnra
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvid
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtvdrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457659509             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457659509
VERSION     WP_457659509.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32108
     Region          78..292
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(85,126,163,178,180,188..191,240,265..267,269,272)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(105,112,138,204,206..210,238,242)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            163
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrnypeiasr mfgtplmlhp skgdiiaraf gprvlgspda pahvaggeem gllgeklrna
       61 tdwdgeriyp gpdlvasgia lieiegslvn kgkwigkscg mtsyegisaq vqdcierddi
      121 kavvfevdsy ggevtgafdc aeqifelsqa kptiavltdh acsagyllas pcrqlvipqt
      181 gicgsigvis mhvdmsawla keglkvtilk agehkadfnp yeaipddvlq qelaeleelr
      241 vefaatvary ragrltqqsa latearvyrg qkavdaglad avarpsqvle afeaelsrta
      301 g
//
LOCUS       WP_457659531             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457659531
VERSION     WP_457659531.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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 301)
  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 301)
  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 301)
  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..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /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=31959
     Region          45..184
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mkgyvsllls iaaisllgst fafaaavert ivyiecalge rtsrgtgvvv spqghiltak
       61 hvifdpnarc qasigvadpn sarlvirqpa nppnevdval irfadqqqye ymrfcsledw
      121 mirrkifvag fpagtetgsp sfregvlstv fpnqkgliet dgqtiagmsg gpvfsnnlag
      181 lvglvigakf dpgtglvnny ailpvsdyaa ifnltvsdvp cyhrgnevel paglahwtsd
      241 sgpkklgvrv eqgicfltsi ggmfngpnar vsievengey vlsgvnptgq vgasvrciwy
      301 d
//
LOCUS       WP_457659536             352 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457659536
VERSION     WP_457659536.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..352
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39633
     Region          60..330
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtivrvkgvk ryfepksgkw yayhrktgkr ikaefgtpef fvelaalndg skdvgskpgt
       61 lgalitsyrn sagfkslagr tradyqkimn ylqkyaespl adlthgalsr frdkvfeekk
      121 rkfanytltv lsilfehaie memasvnpvt kvkrvrktkd taeanrpwtd eeretveavl
      181 pvhmrlpval mmycgldpqd alklprtavs dgmidtrrgk tgvpvwmpmp dpvkdvlaga
      241 pkhdattlca nsygkpwtyn gfstnwhrlk vkleekgdiq pgltlkglrh tvatilremg
      301 kdpatianml gqkteamakh ysrradmskk mtetvddfsa evnrrrtkvs rk
//
LOCUS       WP_457659537              80 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659537
VERSION     WP_457659537.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..80
                     /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=8734
     Region          10..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mrvaandnfp hrlltksqaa qycglsvatf ggicpvkpia lgdgvrmhry dvrdidrwid
       61 gfkaggaapr skfeelmekl
//
LOCUS       WP_457659549             247 aa            linear   BCT 27-JAN-2026
DEFINITION  LexA family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659549
VERSION     WP_457659549.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Giese,K.C., Michalowski,C.B. and Little,J.W.
  TITLE     RecA-dependent cleavage of LexA dimers
  JOURNAL   J Mol Biol 377 (1), 148-161 (2008)
   PUBMED   18234215
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Erill,I., Campoy,S. and Barbe,J.
  TITLE     Aeons of distress: an evolutionary perspective on the bacterial SOS
            response
  JOURNAL   FEMS Microbiol Rev 31 (6), 637-656 (2007)
   PUBMED   17883408
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Rosinski,J.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 12213969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="LexA family transcriptional regulator"
                     /EC_number="3.4.21.88"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27675
     Region          8..60
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(9,13,38)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(12,37)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(19..20,31,34,38..39)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          116..234
                     /region_name="COG2932"
                     /note="Phage repressor protein C, contains Cro/C1-type HTH
                     and peptisase s24 domains [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442176"
ORIGIN      
        1 msrltdtlsk klteadipqa elarrvgltq qainnlfagr vvsstawrei arelhidede
       61 mrrlmidagr dpvrntrmps slpglishfr evrsgvepna tigaettier hkkkllpvlg
      121 eavggedgey ifngsvldyv dcppslenvp nayavyidge smvprfrpge tvwvhptkpp
      181 rrgddvvvqi hrdeedegap prgfvkefvg wtanklvlrq ynpdkkieft rqqvvsahpi
      241 ilagkyw
//
LOCUS       WP_457659551             203 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659551
VERSION     WP_457659551.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..203
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22179
     Region          14..59
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(19..20,31,34,38..39)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 msrlsqmlln eqakrgltdy kaakeigvlq qtysswkhgs iprpnryaai agwlhisidm
       61 arelceeava stgstklprt veqpagrisd rkegrfkfdp vstgskrips sryavavdtk
      121 vmepallvgt kawldpsvwp kvgnevmvha rggvawlgrl eslengkaei sryalgnrit
      181 iddvqavhav vlservagqe lns
//
LOCUS       WP_457659552              85 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659552
VERSION     WP_457659552.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 85)
  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 85)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Rosinski,J.A. 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 85)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10622089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..85
                     /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=8876
     Region          <3..31
                     /region_name="HTH_38"
                     /note="Helix-turn-helix domain; pfam13936"
                     /db_xref="CDD:433591"
ORIGIN      
        1 mniqemhqsg lsmreiggrv gvshmtvari lwgarssnri pvaandnkiv kmmphnggcs
       61 ttsglvpvsl prvggmgphp yevaa
//
LOCUS       WP_457659557             269 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659557
VERSION     WP_457659557.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 269)
  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   2  (residues 1 to 269)
  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 10605537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..269
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=29664
     Region          14..234
                     /region_name="AAA_24"
                     /note="AAA domain; pfam13479"
                     /db_xref="CDD:433243"
ORIGIN      
        1 msvfdklrss krktppvlal ygiggvgktt lagefpdaly lhtsgeetpv dldipaieie
       61 sydemieafs tlltethpyk sviidsldaf ekmlwaatca rmgwdtidsn dkgsptafgk
      121 gyleadndwl eymggarals rsgvnvvqil hckvksfndp lldpydryrp klqdratdii
      181 meksdallfm skrasikqvd kgfgkkenka vgmsgservi ytderagfla knrlnmpati
      241 pyvkgkgyda lsayfytphd vtaaedeaa
//
LOCUS       WP_457659563             159 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-70 family RNA polymerase sigma factor [Sinorhizobium
            medicae].
ACCESSION   WP_457659563
VERSION     WP_457659563.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Davis,M.C., Kesthely,C.A., Franklin,E.A. and MacLellan,S.R.
  TITLE     The essential activities of the bacterial sigma factor
  JOURNAL   Can J Microbiol 63 (2), 89-99 (2017)
   PUBMED   28117604
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Campbell,E.A., Westblade,L.F. and Darst,S.A.
  TITLE     Regulation of bacterial RNA polymerase sigma factor activity: a
            structural perspective
  JOURNAL   Curr Opin Microbiol 11 (2), 121-127 (2008)
   PUBMED   18375176
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Mooney,R.A., Darst,S.A. and Landick,R.
  TITLE     Sigma and RNA polymerase: an on-again, off-again relationship?
  JOURNAL   Mol Cell 20 (3), 335-345 (2005)
   PUBMED   16285916
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Wosten,M.M.
  TITLE     Eubacterial sigma-factors
  JOURNAL   FEMS Microbiol Rev 22 (3), 127-150 (1998)
   PUBMED   9818380
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Helmann,J.D. and Chamberlin,M.J.
  TITLE     Structure and function of bacterial sigma factors
  JOURNAL   Annu Rev Biochem 57, 839-872 (1988)
   PUBMED   3052291
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11495650
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..159
                     /product="sigma-70 family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18011
     Region          11..156
                     /region_name="sigma70-ECF"
                     /note="RNA polymerase sigma factor, sigma-70 family;
                     TIGR02937"
                     /db_xref="CDD:274357"
ORIGIN      
        1 mtattaprpp eidamllanw nklrkyalrm tpnvdeadsv msdmteailt hwatyrpdgd
       61 fltwckltir srasnrrrmi rhryehvevd seklvygagq dhlvdlksal qsidsdtrrl
      121 vmlaaegyth aaigkmigrt gervcqrlkh arakmrgda
//
LOCUS       WP_457659595             225 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457659595
VERSION     WP_457659595.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..225
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25394
     Region          79..165
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msiamhnali esetrqakll felawqvddp styilddvtt prerstkmra eyyqelhdgn
       61 dayqannwlv aekasilkak pktlvevgcg ngafslsaae nvekvfavdw alspkfcdrp
      121 envefvqada tqdrlpradv vcsadvlehf tpwnvtrvle ncasaaglqy hviacyddgh
      181 shitvmrpsa wlasfwryfp darltridcr rekhtqlvcv itnie
//
LOCUS       WP_457659601             238 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Sinorhizobium medicae].
ACCESSION   WP_457659601
VERSION     WP_457659601.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..238
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24176
     Region          63..>236
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mrfkrtltas aflaaagavf apdaaayinr antppamtva ieraayrapv tdaatvminr
       61 pngrgtgfhi gggriiaaah vvdgaktvsl ksidgrissa tvvkvdtatd vavlqtnmrl
      121 laaeldcgtv pvgtvisaig nplgqefita fgriagaprd lgksgpayvt dmttvmgqsg
      181 gpvfadgrvi gvvsavmtap felvgkvpqd sgiyarslvg fgyvvpsaev crllgeva
//
LOCUS       WP_457659621             503 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659621
VERSION     WP_457659621.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..503
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=54019
     Region          1..498
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mkpaialegi sksfpgvral sdvslalypg svtalvgeng agkstlvkil tgiyqpdaga
       61 irladrettf ptalaasrag vtaihqetvl fdelsvaeni flghaprnrf glidwkklna
      121 daktllnrag adfdptirlr dlgiakkhlv aiaralsvda rvvimdepta alshkeihel
      181 yalierlkan gkailfishk fdeifriadr ytvfrdgami geglianvsq ddlvrmmvgr
      241 avgsvypkke vaigqpvltv sgyrhptefe dinfelrrge ilgfyglvga grsefmqsli
      301 gitrpsagav kldgevlvir spaeairagi vyvpeergrq gaiigmpifq nitlpslsqt
      361 srsgflrlaq efalareyts rldlraasld qdvgtlsggn qqkvviakwl atrpkviild
      421 eptkgidigs kaavhafmse laaqglsvim vsseipeimg msdrvivmre grvagrfers
      481 eltaeklvra aagietqagg gaa
//
LOCUS       WP_457659624             338 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659624
VERSION     WP_457659624.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..338
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37584
     Region          71..332
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 meqliaailt mvagvlvcaa yfwssnllld wifpskgkfg aaasrnlrfa nmvrpwlfla
       61 pallalaiyl vypviksvll sfndrggqdf vglrnylwmi ndgefrqsif nnflwllvvp
      121 alstffglii aaltdriwwg niaktlifmp maisfvgaav iwkfiydyra agsdqiglln
      181 alvvalggep qawitlpfwn nfflmviliw iqtgfamvil saalrgipee tieaavidga
      241 ngwqiffkim vpqiwgtiav vwttitilvl kvfdivlamt ngqwqsqvla nlmfdwmfrg
      301 ggdfgrgaai avvimilvvp imiwnirnat retggalr
//
LOCUS       WP_457659625             428 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457659625
VERSION     WP_457659625.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..428
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46994
     Region          31..395
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mswqspispg yswyeatipe rpafpvmpgs rradvaiigg gytglqaayn larsgtdvtl
       61 inscrfgdga sgrnggqfgt gqrlwaeeae emlgreraqr lfdmaenakr yvlgfaeeha
      121 idiefmpgql svshkksler dyrdhveamt erfgyphlsf mdreetvsrl gsshyhfgir
      181 dvgtghihpm klvvgltrqa araganlyeq tkalriekkg glvviettsg titadralia
      241 cnayignlep vtaahvmpir sfigatsvla dhpevlpgge svddsrfvvr yfrkskdgrl
      301 lfggreayta dnprdisahi rrqiceiypa ladievthaw ggsvgitmpr qpfcrdvmpg
      361 itsiggysgh gvmlanycgk lyadlalgka teldllkelk ipafpggtrf rsallflalt
      421 wyalrdrm
//
LOCUS       WP_457659626             380 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659626
VERSION     WP_457659626.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..380
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41627
     Region          19..380
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkslgsirrs fapwadpask pfisfknvtk kfsdftavdd lslniytref fallgasgcg
       61 kstllrmlag feqptsgeii ldgqsltgip pyrrpvnmmf qsyalfphmt vennvafglk
      121 qdrmpkadia ervaqmlklv klekfakrkp hqlsggqrqr valarslakr pkvllldepl
      181 galdkklree tqfelmdlqq elgltfvvvt hdqeeamtma driavmshgk vvqvatpaei
      241 yeapnsrfva dfigdvnifd gsvtsagdgy vviettgais vrmasaekpa kgaraavair
      301 pekirlsrqa pahaptnaae geiwdigylg dmtvfhirlk dgkvikassl navravedpl
      361 gydqqvwvsf gedagvvlkd
//
LOCUS       WP_457659628             538 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659628
VERSION     WP_457659628.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (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   3  (residues 1 to 538)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..538
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58107
     Region          <1..215
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          257..529
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 mailghwigg rklallggla taylaifglw teamktvsiv ivivplavta gfalglwafr
       61 nrrfekllnt cfdimqatph maylapvvvl fgfgqvpali atfifalppm grctilgmrt
      121 vqpdvieagh msgctkrqll wkvqtpaaqq tlllgvnqvv mqtlamvvia slvgaaglgq
      181 kllfslqqlq vgkaveqgva itliavvldr msqsymrrip ahreagkiph khllafgvlv
      241 iaavvisrfl pavlvlpkdl tfsygapinq avrwisrelf syvkpvrdti tiwallplrd
      301 fclwlpwpvv lgslaaigwv lgglrlallp vallgimllt gfwtqlmltv ylvasttvls
      361 iligtpigiw aarrpfaari vnticdtlqt fpsfiylipv imlfqtsdls nvlamlayat
      421 vpmiryaqlg lkrvpqatve aavasgttpf qrlvkvelpi afpellmgin qtimmalamv
      481 aitaligsqd lgqeiykalp gadtgrglla glgiafigit anrflgawaa kinrnlgm
//
LOCUS       WP_457659633             289 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659633
VERSION     WP_457659633.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..289
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30744
     Region          65..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mnkpvitqam idaydeythl tldrrrfmek ltalagtaaa aaaiapmlaa nsakaeiiae
       61 tderikgedi typggdgemk gylvkpaems gklpavivih enrglnphir dvarrmaleg
      121 flalapdfls peggtpgded karemigald asatnanatv aflkghaest anvgaigfcw
      181 ggglvnrlav napdlkagva yygaqpkaed vpkikaalll hyaglderin agieayrkal
      241 tengkdatiy vyegvnhafn ndtsaarydk eaadlawqrt veflkakla
//
LOCUS       WP_457659635             204 aa            linear   BCT 27-JAN-2026
DEFINITION  2-dehydro-3-deoxy-6-phosphogalactonate aldolase [Sinorhizobium
            medicae].
ACCESSION   WP_457659635
VERSION     WP_457659635.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..204
                     /product="2-dehydro-3-deoxy-6-phosphogalactonate aldolase"
                     /EC_number="4.1.2.21"
                     /GO_function="GO:0008674 -
                     2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0034194 - D-galactonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20419
     Region          1..199
                     /region_name="PRK09140"
                     /note="2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
                     Reviewed"
                     /db_xref="CDD:181670"
     Site            order(8,33,37,62,122,124,150)
                     /site_type="active"
                     /db_xref="CDD:188632"
     Site            order(37,62,64,83..86,106..109,111,115,124..125,136,
                     140..141)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:188632"
     Site            122
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188632"
ORIGIN      
        1 mkrpliailr glkpeeaegv vgalietgfe aieiplnspd pfrsietavk mapagcliga
       61 gtvlttaqvd lladaggrlm vspnvepavi rlaaakgmvt mpgvftptea laaaaagasg
      121 lkffpasvlg psgiaairav lpgdveiaav ggvsevnfad yaaigirsfg lgsslykpgm
      181 saadvrqrai atlaaydavy ggqq
//
LOCUS       WP_457659636             391 aa            linear   BCT 27-JAN-2026
DEFINITION  cell wall hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457659636
VERSION     WP_457659636.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Bagyan,I. and Setlow,P.
  TITLE     Localization of the cortex lytic enzyme CwlJ in spores of Bacillus
            subtilis
  JOURNAL   J Bacteriol 184 (4), 1219-1224 (2002)
   PUBMED   11807087
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ishikawa,S., Yamane,K. and Sekiguchi,J.
  TITLE     Regulation and characterization of a newly deduced cell wall
            hydrolase gene (cwlJ) which affects germination of Bacillus
            subtilis spores
  JOURNAL   J Bacteriol 180 (6), 1375-1380 (1998)
   PUBMED   9515903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="cell wall hydrolase"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42926
     Region          254..386
                     /region_name="CwlJ"
                     /note="Cell wall hydrolase CwlJ, involved in spore
                     germination [Cell cycle control, cell division, chromosome
                     partitioning, Cell wall/membrane/envelope biogenesis];
                     COG3773"
                     /db_xref="CDD:442987"
ORIGIN      
        1 mrkgikfpgk frltfsrwra pamiglaifl gfpsaaaysd iatflsginr ggerwrtylt
       61 qspagslhev emvftdpvtt galdggagmt lpdggrvavt aeskhhgtpd edrvtrklkk
      121 krivavtpat ppkdfsagsi lertsslmvp sldgsekmif akpkikgkei viatafyrka
      181 ppkpepgisp mlaklvtndk pdilatayvr pepdyaresp fdsilrdden agrfipeiap
      241 ddhtwaatal pptvfskeeq tclaegiyfe argesvkgqa avaqvilnrv rnptypktic
      301 gvvyqnkawr nrcqfsfacd mirdliysrg hwktakeval avtsgkvwls evgsathyha
      361 tyvkpawakt mkrvgkiglh ifyrtygggw s
//
LOCUS       WP_457659637             797 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457659637
VERSION     WP_457659637.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 797)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..797
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=87007
     Region          86..769
                     /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 mtlgkralil ifpvvlagyl laafsvhvaq srsiraleha klsqrlehaa avfqnevrrs
       61 rgalnallsg nalrqyvaet drkyratafg vrlqeslksl lddpagylsf avlntrlete
      121 yyfenswdpf aeidqaqldl arqlangskl gdwtyvdatg erprivyslf vdpitfgrps
      181 psnrknallm qvavqpdrfl klqaalekey gadivlqpwp lavtddlsas vplgpslhat
      241 ltvsdthfna qmlrqkvlla lgalamslfs iwlivvlirr fitgpiatld anvmavmaae
      301 reeiakvgga geigrltgni relhrqsvqs lqlvqrsswt daltginnra rfnilaaqav
      361 retvasgdkc sllfididnf kfvndkhghd vgdellktla ariahdvgai tggrgqepai
      421 larlsgdefa vllrsqpgdg vvretcaail alfsdgfels gkrypvtasi gvavcphdas
      481 svaelisnsd aamyqaksag knrsarfsra lndkrtrqrq iqdelrsldp dqqfhlvymp
      541 ivdaggkvng ceallrwysp vlgnvtpdef vpiaessglf tkidwwvvdk amsdcrqlka
      601 lfgpdtvlai nissaelhsk aisehlsdcl arhnleaqsi dieltetfav qisdqlrlrm
      661 delrskgfrl siddfgagyt svqqiigyaa dtikldrelv snlnasesla vlravialch
      721 akgmavvgeg vdtpeklaml kaagcdrfqg yliskplpla elaiwalsrv ahavekpads
      781 sfrpesktpe darkiag
//
LOCUS       WP_457659638             271 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659638
VERSION     WP_457659638.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Khuri,S., Bakker,F.T. and Dunwell,J.M.
  TITLE     Phylogeny, function, and evolution of the cupins, a structurally
            conserved, functionally diverse superfamily of proteins
  JOURNAL   Mol Biol Evol 18 (4), 593-605 (2001)
   PUBMED   11264412
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   8  (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 14398393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29821
     Region          31..121
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          32..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpisdgsylp klpdadhfrs lewiekanap vlaigkdyac glvvpphshs rtqlwwarsg
       61 vvlvytsggr wmippghall ipagiehsae mvsdvrmhst yippeasear rplvlemspl
      121 vgslideliv agneastekr eslimelllt eiprlsqrpl glpfprdrkl aiicrqfvea
      181 psasasidaw aasmgisrrs ftrlfrqetg vsfgtwrqqa cifaslpria dgepittval
      241 dagyenvaaf ttmfrrmlga ppsvylrdqr t
//
LOCUS       WP_457659639             397 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659639
VERSION     WP_457659639.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..397
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=40971
     Region          12..363
                     /region_name="thiolase"
                     /note="Thiolase are ubiquitous enzymes that catalyze the
                     reversible thiolytic cleavage of 3-ketoacyl-CoA into
                     acyl-CoA and acetyl-CoA, a 2-step reaction involving a
                     covalent intermediate formed with a catalytic cysteine.
                     They are found in prokaryotes and...; cd00751"
                     /db_xref="CDD:238383"
     Site            order(30,57,69,72,76,87..90,98,105..106,109,124,275,277,
                     279,299)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238383"
ORIGIN      
        1 mnalpdptrt pvliaalrtp vcrvngslaa iepaslaall iekivantgi drgeiddvlv
       61 gnaansagnl arlaaleagl pisipgvtvd rqcgsgleai vlaarqiqag agrfyiaggt
      121 esasrahirl rppltrgeel qpvkrarmap nsigdpdmgv aaeyvatacg isrdrqdrfa
      181 leshrravaa enagrfarei vpvstaagti ardecprana saetlsrlkp afveggtvta
      241 gnacpvndga amvlvtnlae aqrlgarfgl vfadaatagi dpnllglgpv pamaklrarn
      301 paldpagvdf iefneafasq vlgsldrldi aperinregg aialghpyga sgailvvrlf
      361 sqmlttssrt eglavmgigg gmgivahfrs yrpdqtl
//
LOCUS       WP_457659640            1128 aa            linear   BCT 27-JAN-2026
DEFINITION  ALF repeat-containing protein [Streptomyces anulatus].
ACCESSION   WP_457659640
VERSION     WP_457659640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            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 10510034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..1128
                     /product="ALF repeat-containing protein"
                     /calculated_mol_wt=113988
     Region          <23..146
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          62..95
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
     Region          200..238
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
     Region          <513..>614
                     /region_name="PRK12472"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:237110"
     Region          617..651
                     /region_name="ALF"
                     /note="Short repeats of unknown function; pfam03752"
                     /db_xref="CDD:461040"
ORIGIN      
        1 megksvlsps lwsrrrilst vagaaavpal psiltlsatp ahaaptapga pdnglpdtdq
       61 gravwayktg gravregaaa allgtpaalt aflttelpva raednrfavl sslsgagrsv
      121 qqtastalsa gdesvaaflr dgfaapvled lrvsvfsald nggtamkrea skalntntke
      181 sletflrttq htaqqedeqa avfailstas pevkkyaera ltdgspaair lflssgqhia
      241 rardeetati eqlveivere gkraqlttdk avafstrake aaekakiaal eaaaeakaaq
      301 qdvrksataa nnaasaarga aaaantaisa srtaqaassr aaqaaqaaaa aaasagnaaa
      361 rayhaaigas kdaskasaar taavgarnaa arartaakaa dqaaiassqa ssagsaaasa
      421 arnaaaaasa sadaaasaga aqaqaakarq aaaeanaaaa ratraagtaq tlanraaaaa
      481 rvardaansa aahadkaaaa aeeaadnagk aieyakrste yakqavdaan tavdavrean
      541 eveaaarkae tdriaedtel gvlearlqaq aetedaarte kqrtqasqts eevkglista
      601 eaalaagnta savtvgrkaa lrlldssgsw trgaaefala gsehdvvnwi dadrllaqqq
      661 ddrenvlala qsstaavaaa aeraladsdp naatvfletg aieaaaadnr vlvfqvlsqd
      721 pgkavkakaq aalnagtava lhhflsvels eatkeddrve lfrlletggv ymrsaaeivl
      781 egsarmrraf virdkfniar ldhdhathis airatlahaa rvaakaleda araskaaaea
      841 rqaaqeaaew aakadgyakd alasaaeaka nadaadksaa saaqsakdas aaattargaa
      901 rtanysmrqa sasakqavaf aveaqasaas aaasaqqagq daraaaaaas qahaiaaqkr
      961 raeavaaark aaeearqnqq ngtnpsdkpe ndddgdtkwl dlwpvdmkdp kdwakatghw
     1021 stlfgtasvv lgvgallfpp aapvlgplav gagviswglq gvsaglsgwg ygwdssnfhe
     1081 alglfvvggi ffgkgrlfsk fgvaeeigak vsgvvsdgat avigwltw
//
LOCUS       WP_457659642             140 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Sinorhizobium medicae].
ACCESSION   WP_457659642
VERSION     WP_457659642.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..140
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15116
     Region          1..138
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykkiivpia mdqlehgesv lgiavklide ggeiillnvv edlnayaqgy mivdfplemi
       61 eelrkhavkt lealrtkhgi ngrveirtgg aagsinalak eenadlviia shrpglidyf
      121 igstasrvvs hcpcavlidr
//
LOCUS       WP_457659647             411 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457659647
VERSION     WP_457659647.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43797
     Region          10..370
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,135,
                     138..139,142,209,212..213,216..218,221,245,249,300..301,
                     305,309,325,328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 msqirplipl lvtagiligg nglqgtfisl raldegfsts ligvvgagyn igfaigciyv
       61 trilraighi rtfsamaaia saaaismvli idpwfwflmq lvagicfasl fatveswlna
      121 svtnanrgrt lsvyrlvdlg svtaaqyaip gigiggfelf aiismaltls lvpisfadrs
      181 spvtpeairf dvktlwnisp latigcivvg ltnaafrslg piyaqeigls vtaiatfmsa
      241 giiggvvlqy plgyysdrid rrliillatf gsllaglfla fgagsdewln fagifafgaf
      301 amplfslcsa qandhaaegq halvsagmlf fwslgaiigp lfasflleif apqvlfiyta
      361 ailgafmlyt llrmtarkpv pteersmrfr nllrtssffn klaggharke p
//
LOCUS       WP_457659654             291 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457659654
VERSION     WP_457659654.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..291
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31464
     Region          35..276
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mskdktgdks ardthyanlr rahrdgrrer geiptprqdk rgkpsadwkp palapdqvll
       61 yglhtvraal dnperriirl svtqnaaarl dlgdsaalpf pvetvtpqel drilgpdaih
      121 qgvmletrpl phrklealrd cplilvldqv tdphnvgaim rsavafdaga littmrhspt
      181 elgvlaksas galelipyiq isnladtide lhalgfmtig ldsegpqple gtfagdkial
      241 vlgsegkglr qktrqtvkal arldmpgaik slnvsnaaai amyaarhhlk e
//
LOCUS       WP_457659657             340 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457659657
VERSION     WP_457659657.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133569
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..340
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=37929
     Region          2..325
                     /region_name="GT4_GT28_WabH-like"
                     /note="family 4 and family 28 glycosyltransferases similar
                     to Klebsiella WabH; cd03811"
                     /db_xref="CDD:340839"
     Site            order(13,174..176,232,254)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340839"
ORIGIN      
        1 mkvshfhfgk dggaerffvh lvnalaergv eqtatirpgr swrrdiegva kvreshfrnl
       61 sldrillplk vkhmarrekp dvlmawapra selmpnyrga fkisrlgdyp trlsyfrntd
      121 civcntpgia ervrdlgwtr evrvisnfta tgrveavdra kldtpadapv vmsmgrfver
      181 kgfhtlieav arlpgvylwl lgdgeegdnl hklssdlgvs drvrfagwqk dtrpylaaad
      241 ifamssshep lgnvileswa qgtpvvstrs egpkwfmrdg engvmveigd aegfahaigq
      301 ivadptlgtr laerghetli rqfskeaitd aylrlfaskt
//
LOCUS       WP_457659668             370 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces anulatus].
ACCESSION   WP_457659668
VERSION     WP_457659668.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..370
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41218
     Region          71..363
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgsffkdcgc akptrcphpy sirfrdalgk qreesgygtq ddaierltqv yaekkttaps
       61 vaaarrelgq ltvgeyakqw rprqrkmtdy stgehvdssi nvhivprlgs rklnavtpiv
      121 verfldemed dgvgrgnqvn ifrvlktvlr daytkgamad dpvkgvqepe yvrstvaips
      181 layvtkalav adedlaleiv mmagcglrng earavnvsnv vaqdvyrvre qihsntlkpa
      241 klkhrktgef revplprsvr eaieryeakh gttkdgyllr gpggyftegm errrvkklfk
      301 glppvegvgm ygfrhyfasn algngipitd vaewmghksi eetyrtyrhl mpgsitkaar
      361 ildaglweaa
//
LOCUS       WP_457659693             296 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457659693
VERSION     WP_457659693.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..296
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31768
     Region          1..285
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mmvlsvllsp lidifsklav atvpsaeita irfllqvafi lpivllrgtv ldltwrksal
       61 halrggllvv tmlsfvtalk vmevadaiai ffvepiilti lgsiflketi gwrrytacgv
      121 gflgsllviq psmqevglia llpivaafgl affllvtrmv aqsedpwsmq fhagiwgglf
      181 clvllwcgeg tgsavfdpvw pdgralyhll gvgvvatiag vlgvyayraa pasvlaplqy
      241 leivsatifg wlvfgdlpda lkwlgiaiii gsglyiiwre rqahktasip pvspai
//
LOCUS       WP_457659700             221 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457659700
VERSION     WP_457659700.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 221)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..221
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23870
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maligsligd paranmltal mggqaltate laaqagvtlq tasshlakle agglltqrkq
       61 grhryyalse devglmlesl mgfaagkglt rsrpgpkdpa lrkarvcynh lagdygvrml
      121 dsliaarqie mtddddlalt dagrirvesl gvdyaalrks rrpicrtcld wserrshlag
      181 slgealltlf iengwakreq nsrailftaa gekaflelfp r
//
LOCUS       WP_457659701             320 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces anulatus].
ACCESSION   WP_457659701
VERSION     WP_457659701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..320
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34737
     Region          4..319
                     /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 mkqrtvlvvl fdsiqsldat gpmevfagas rspgvsydlr tasldggpvr stcgltlvpd
       61 ssladapaph tllvpggqgt rgshpeltgw lrehgpraer lvsvctgall laeaglldgh
      121 rvtthwnyce rlardypavr vdpepifvrd grlatsagvt agidlalalv eedhgrdlal
      181 diarhlvvfl rrpgnqaqfs aqlsaqtarr eplrevqhwi tqhpdadlgv dalaararls
      241 prhfarafra etgttpgryv ervrleharr lledtadgve riarasgygt peamrrafvk
      301 tlatapaeyr rrfrtpasst
//
LOCUS       WP_457659702             285 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457659702
VERSION     WP_457659702.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..285
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29995
     Region          23..263
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtglgglals fdiplirsad gevwsilavr slstflaala twvvinhllg rrvalipgka
       61 gliagllygi nsftfllavf ntstanvvfi laftsmfaai lswiflkerp snatfltmgv
      121 mlvgvgvivs dglesghlfg damaacsafl laaaitisra sgrdmslvpl ttaifpaiag
      181 fmllpagglt iaepayilfn glvmiplaff clatgpryls apevgmfyll etilapiwvw
      241 ivfsetpssp tllggtilil alvghslwqi rmraararla cevag
//
LOCUS       WP_457659708             323 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein, partial [Sinorhizobium
            medicae].
ACCESSION   WP_457659708
VERSION     WP_457659708.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..>323
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
     Region          23..135
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(41,44)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 malqmdnpap apkvqnwlrg splanfqlgk vyvvhfwatw wtpcatfmhg lmqlqekyrd
       61 rgvevvavaa demaaaadev qahvdawlte klprlnfrvg ldctgemkrl wmeasfsfgi
      121 plsfvvdgdg ciafighpaq layvlpkald gswrtsdqak aadgeriang reealkrsil
      181 dkfsaaieme dwkaalsaik egttlmpdsi qlraahadtl lhkmrdmktg llvlrelvre
      241 aidrnaedwl leamnqlfna eydytdfpsv erfaigkels ehilaltgle ddvkaysyql
      301 varyyhesgn raraeellkl alk
//
LOCUS       WP_457659709             691 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659709
VERSION     WP_457659709.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..691
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=77727
     Region          13..402
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mnafsplppa llkrkavvyv rqssqsqvmq nlesqrrqyd lvdaarqhgf rrvevidddl
       61 glsasgavar pgferlvawl cagdvgavlc fdasrlarng rdwhhllelc glvdarvidq
      121 dgvynpcspn drlllgmkgt isefelgiir armldaarak arrgelrisv pigyiwyrda
      181 glnfdpdlrv qeavrlifsr frelrsgrqv llsltedklc fprptdgrnt ttfdwtpiry
      241 rnvisvlknp fyagvyaygk sekrteiidg rarktyghgk pkeewevflk dhhdgyiewd
      301 eyernqalla anaygqkgga ksgrggrall sgllscgrcg rrlcvaytgk tprpvyrcer
      361 pnlmlglnrc lgfggpridk avaaellrvv qpmaieaamq aehmqseara errraaeldl
      421 qkaqyeaala erryaacdpd nrliaatlek nwevalkrle acktrldaeq lpdtpaklpd
      481 ldglaedlqa awnapgvstr arqrlarali kdiiadvdee ardvvltihw qggqhsqlrv
      541 rkpktgehgc ntsedalevm rsmagrwsds diaatlnrmg irtgfnhtwt ahrvssirrv
      601 ndihayfsae ksgkwltmte aatklgvtnh virnlikaki lpaeqvvpra pyqikavdie
      661 rediieainn rrrkrpyrdp rqialpinsi t
//
LOCUS       WP_457659711             427 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457659711
VERSION     WP_457659711.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..427
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45897
     Region          4..426
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtifitpsla tttyasrlqr vkspggieaw lledhtlpvl wtsfcfrgga afdpegkpga
       61 sallgsmlte svgdlhaggf qrrldekvih lsfgarraal hgslrtltqn vdeafdllgm
      121 avsdpafqql dferthakra aslrmgmaqp drvahqvfda iafaghpfsr pasgcyetig
      181 svelsdvval hsrmiarhnl eivavgalga dafvaaldra fsklpvsaea svlpapflgl
      241 geevlthlds pqstmifgrp cisvddpdfm aakvvnhclg ggtfssrlft elrekrglcy
      301 sihtrldatr nvsrligyts trndrlyeal dvirsefahl vsnkisaeev emaksylmgs
      361 falqldtssa iartllstkv gglqpdfide rnariasvtr dtvadavdrl igdgallvsi
      421 agnpath
//
LOCUS       WP_457659712             453 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457659712
VERSION     WP_457659712.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..453
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49695
     Region          14..436
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mfnsfhsenl qldspvgekh etspdmvftg rlgngmdviv irdhrrpiat hmvwyrngsa
       61 ddpigksgia hflehlmfkg trnhpaghfs gllasvggne nastsrsytn yyqrvpqdyl
      121 ktcmayeadr mtgliltdei vdmerqvvla ergmccdsnp rdilhealha gafspdpcgr
      181 piigwqheie tlgredalay yrrfytpena ilvvagdadp davmdmaeti ygaitptgas
      241 fkrpvvrapp vrtqrlltlv denvhqpaft rihvvpsmma tgphaaalev lalllgggkt
      301 sylhealivn nrmaisvgas yggdvsrgla sfqigacpap gvslthldda ienalemlrr
      361 tgfsaddiqr vksrivanai yqkdnhfnla yqygvaaslg lsvedvalwh drikgvtted
      421 irnaltller stgivgyltp prnrrlnrkg fls
//
LOCUS       WP_457659719              67 aa            linear   BCT 27-JAN-2026
DEFINITION  cold-shock protein [Sinorhizobium medicae].
ACCESSION   WP_457659719
VERSION     WP_457659719.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6865
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 matgtvkffa qdkgfgfitp dsggpdvfvh isalgfggsl qngqkvsyel gqdrktgksk
       61 aenvsal
//
LOCUS       WP_457659723             230 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659723
VERSION     WP_457659723.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..230
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=24065
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavd warapngcpi feqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarggyftpt vaakanssaa ggemgavavl
      181 erhgalfplg ddnlslpsys agggdpaktl asqleqlgls vhdwfslldl
//
LOCUS       WP_457659720             197 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457659720
VERSION     WP_457659720.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 197)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..197
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /calculated_mol_wt=22154
     Region          63..191
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
ORIGIN      
        1 mkllqrelrr dvlcgfynrf sgkdislitq hpswcaamkk adrylarlap hasslmngga
       61 ahqigaicyr snetgavevl littrdsgrw tipkgwpikn lkphqaaere aweeagvagk
      121 akkralgyft ylktlgdgqt tpsvvevfrl kvdelhlefp ergerevawl spveaarrvq
      181 epelkgllmr mlkqslr
//
LOCUS       WP_457659730              93 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659730
VERSION     WP_457659730.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10120
     Region          1..93
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mvrqsfsnvw dalentpaaa asmamrsnll iaieqrvrsw qvtqaeaarr lgitqprlnd
       61 llrgritnfs ldtlinlasq agltvrldia eaa
//
LOCUS       WP_457659736             699 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457659736
VERSION     WP_457659736.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..699
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77732
     Region          132..526
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mtkqlqafyl lfcvgiafvv wmlgyglglq lfykdgrile ttitsnpfap iqqfwhykts
       61 palqkvalgs mlpallaagl vayiglkpts splgdaafqd maslrrgkwf rkqghifgrv
      121 grnilrtrdd rhhliigptr sgkgagyvip nalmhegsmi vtdlkgevfk atagyrrqng
      181 sqvfllapgs ektnsynpld firpergnrt tdiqniasil vpentesens vwqataqqvl
      241 agaisyites pfyrdrrnla evnsffnsgv dlqalmkyik ekepylskft vesfnsyial
      301 seraaasall diqkamrpfk nerivaatnv tdmdlramkr rpisiylapn itditllrpl
      361 ltlfvqqvmd iltlehdpns lpvyflldef rqlkrmdeim tklpyvagyn iklafiiqdl
      421 knldeiyget srhsllgncg yqlvlgandq ataeyasral gkrtiryqse srtielmglp
      481 rrtkveqire rdlmmpqevr qmpenkmill iegqrpifge klrffqtqpf ksaeafsqan
      541 ipqvpevdyl spkpvpattp eyanggdpsv etpspapvtg ekpltaaaee avpvkaetaa
      601 aetpeapakr tvnkkalrsk pretpantgg aeastsldam eariraveeg lkpkvaqlke
      661 vverkaeklg ensptkrrni mdifsatvpd pvepgvaae
//
LOCUS       WP_457659758             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659758
VERSION     WP_457659758.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30581
     Region          53..285
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtflsntsaa atagrphrss laaarrhplv ligggllvll vllalaapfy vgdpsnmdpf
       61 vrlqppsaeh wfgtdnlgrg vfartiygar vslmvglisa alaacvglli gvvagyvrsv
      121 dnvvmrvmda lmsiptilla ialialtgpg vgiliiaval petpsvtrlv rsvvlsvrer
      181 pyveaaicgg arlpkilwrh vlpstipplm vqsamvcasa imteaglsfl gvgvppeips
      241 wgnmisssrl ylvtapltif apgiflavtv lavnllgdgl ralfdprakr rr
//
LOCUS       WP_457659761             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659761
VERSION     WP_457659761.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35282
     Region          1..327
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mkgpllkven lvkhyplggg ifnkdplvvr avqdvsfsve tgetlcivge sgcgkstvar
       61 llmrlsepte grvllegtdi aslnahalrd grrrmqmvfq dpysslnprl tagqiitepv
      121 enferlsrrk realaaellq kvglapeimh rlpsdlsggq rqrvsiaral slkpaiiiad
      181 eavsaldvsv qaqilnllmd iqeelgvafv fishdlgvve highrvavmy lgrivelasc
      241 ealfanpvhp ytealiaaap apdhtkapha vpiegevpss vspptgcafh prcplaeerc
      301 rvevpaltpm pdgrlvachv rapaeasv
//
LOCUS       WP_457659760             340 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659760
VERSION     WP_457659760.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..340
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37384
     Region          17..337
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mlmqnvvkdk tiandvlldv rdlethffge esvtralggv sfrvrkgetl gvvgesgcgk
       61 svtalsilrl lpkltartvg gevrfdgrnl ldlseremrk irgdkiamif qdpmtslnpv
      121 ytvgrqiaea vqihtgasrs samakaeeml rlvriadper riknyphems ggmrqramia
      181 malicspell iadepttald vtiqaqilrl ivdlkqrtgt avmfithdlg vvaetcqrvi
      241 vmyagrivee asvtnlfarp ahpytkalmg svpdrrrgte rrlpeipgiv pslrepmagc
      301 sfaarcpfvt dicreqtpll eqvgtehaaa cwrskevmsa
//
LOCUS       WP_457659763             483 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457659763
VERSION     WP_457659763.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 483)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..483
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51940
     Region          3..479
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 mrifmaslat etntfspipt nlrsfveggy srrdgtrsen gassvaltew rhaaesdgld
       61 ivesitayaq pagttnrsty eelrdyildd lrnaqpvavv lldlhgamia dgyddcegdi
      121 iahtralagp evkigvsldh hchltqamvd gadilvayke yphtdmreca rdvydltmsv
      181 qrgglkpvka vhdcrliglw pttrepvrsf vdrmralesk ngvasislih gfpwgdvadv
      241 gakvlviada nqtradalas qlgaefwamr eeartpyltv dealarvqen tanapvvlad
      301 vadnagggaa sdntaimqrv ldlgirdial gcfwdtvavq mcfgagigat lalriggkvg
      361 rnsgqpldvv atvrglspeh kqpglsgsrs plgpsayiev egvhiivsti reqvfspelf
      421 teigcsisdk rgivvksaqh fynnfesias eiqyvaapgs vapdfaqiay tklqrsvwpr
      481 sda
//
LOCUS       WP_457659768             373 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanine--D-alanine ligase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659768
VERSION     WP_457659768.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1021533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..373
                     /product="D-alanine--D-alanine ligase family protein"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008716 - D-alanine-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=41581
     Region          10..353
                     /region_name="DdlA"
                     /note="D-alanine-D-alanine ligase or related ATP-grasp
                     enzyme [Cell wall/membrane/envelope biogenesis, General
                     function prediction only]; COG1181"
                     /db_xref="CDD:440794"
ORIGIN      
        1 mppktkarev sfifggiste ydasisslth iissylaiph eerpfsvkhl yhvsrhdslv
       61 riipfrsdft iaelqayisd dsivpghrll aifdkirlsn eyivnllhgq fgedggiqtl
      121 aalsglmgtf gdphvasltm nkyamssfvt slfptevvkv pktkvvkpqd ihnavqiats
      181 fggpivvkpn slgaslfaap fsdpstsete ilallraifr ydntalmqef ilgdeyscgc
      241 liasptvisl pvvkieadgr ffghkekhsy glslervvdn qddelvqrln misrriassi
      301 dlfnmarfdf mvtessdiwf lecnyipglm knsifpkmia hygmtvidli vwieansgry
      361 skknhlfkyd ile
//
LOCUS       WP_457659766             407 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457659766
VERSION     WP_457659766.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..407
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45352
     Region          222..400
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(256,352,355..356,387)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mkrsalyrkl vygpyrefar vyaakmsneg lgrrctwrsl slfrdlmnwh vgnghdpqdl
       61 revhvdrfle hrfkhwspdt gdrsalrrll salreeglip aalpverteh eqivdvfaay
      121 lsnerglaas tvrshkllsh rflrevcpag adgfaaltpe siigyverha ldgsadsgka
      181 mcvvvraflr ylhlkgfist aladcvpsir rwrlaglptf lppekvqkvl dacdrttamg
      241 hrdyavlmil aklglrasev atlnlddidw qagtilvhgk grrqaimplr hdvgtaivay
      301 irhgrpasac rrlflrtlap hvgfasgcai tmiakqaler agvdgyahhg ahlfrhslat
      361 dllrsgasfa eigqllrhrs idstriyakl didklrelsl pwpggvq
//
LOCUS       WP_457659769             245 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659769
VERSION     WP_457659769.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..245
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27320
     Region          8..232
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mialnyfkrv glvggvswas saeyykrlni lladsdapgi vlvdlnfrhv raaqeqyvvd
       61 teaelvtdgi drsvnagaei ilvcsnttsr tldslkrrpn vevvslidcv sthldhqkyn
      121 etlllgtryt merdfyrsam lgqnrtirtp dgpdrmkihe iiydelcrgi ilpksknwic
      181 nmlefysrkf pnldsiilgc telsllgvsq tvnqctvidt isvhidsalr sasigviptl
      241 idqnp
//
LOCUS       WP_457659772             104 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein, partial [Streptomyces anulatus].
ACCESSION   WP_457659772
VERSION     WP_457659772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..>104
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          2..>69
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mrawgepaer ieaaalivte lvtnavqhtt trkircrllr sadgvricvw nrgraripsp
       61 aspgdsaglp vargpgaarp eddgkrdppg gvgpglrlgh aaag
//
LOCUS       WP_457659779             246 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457659779
VERSION     WP_457659779.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..246
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26778
     Region          9..234
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 miglprvgit pdineivape teyvlrinya davskagglp lilpygdqie eylaaidgll
       61 itggmfdidp vlygqtarks yvikpvrtaf erdliqgalt rhipilgicn gmqllavcld
      121 gqlvqdipte idgalehkpa qsatvaqhev efsgasrhlr iqngqtlrvn svhhqavlss
      181 eryetlarap dgvvealeak eggfavgvqw hpeygvaeid tivfddflak areysqrkkc
      241 sndfna
//
LOCUS       WP_457659770             381 aa            linear   BCT 27-JAN-2026
DEFINITION  integrase catalytic domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659770
VERSION     WP_457659770.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..381
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - obsolete endonuclease activity,
                     active with either ribo- or deoxyribonucleic acids and
                     producing 5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=42419
     Region          22..117
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 mssavrrsvp vrtfgdwndp lpgyvevdfv ahsgtsssgs faqtmvltdi atgwtecvpv
       61 rtresglvia aikqarsqfp fpllgvdfdn dsafmnelvv cwcrsqglev trsrayrknd
      121 qawveqknga ivrrlvgygr fvgaeattal arlyevvrlh gnlfqpsfkl rektrigarv
      181 ikryhppvpp varvlahsgv aeadkdrlqa mlesadpvil fagiraaqee lgrrvdrrgl
      241 narseepvav dlqrftlslk tawqvgekrp thrrpyrrtk pypkrqsmle pfepqirawl
      301 eadpavsaas vlerlmsadp srftkkslrt vqmavkawri etagqiildg dwmeratlss
      361 haaagedngh lsaqrfgnip g
//
LOCUS       WP_457659784             407 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659784
VERSION     WP_457659784.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..407
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44690
     Region          58..311
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          325..401
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 markalilve ghrsngplyi qaakslglhp islsrdptqy dylvskkhea irvdtdsyda
       61 mievcsriqa mydisgitgf tgldeslyvt vanlcqyfgl pgpnpasieh ccdkfiqref
      121 laesgvempa yrlavnatei eeaaaeiglp viikpaigsg ssgvrmcrnv eevkehttyl
      181 lggthrwrss prilveecae gnsysaqmmg nemigvtgnv fgppphfvyr eftypavlsd
      241 yeqkriadis lrslqalalg wgpanievrl tkrgpvviev nprlagdpql vhlahgvdlv
      301 rehiklaigd ewnlrrtrsh taavrflvpd rdgtlewtns dsraaavpgv vevkfykqpn
      361 tpitlkgdyr dcighviavs psgartasil qhavdlvsws itpfsnr
//
LOCUS       WP_457659785             288 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA dioxygenase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659785
VERSION     WP_457659785.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32394
     Region          16..272
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mrdeidvtki viphadvvkc strigaeirn iklsadlpdd tiaaihglvl ehkviffrdq
       61 ghlddaeqer falrfgkpsp ypqgtmpile idsagediqa diwhidwscm daypkisvlr
      121 gvviplvggd tvwsntaaay ldlpaplqrl andlwavhsf pgaynsryve nfvgpkiete
      181 hpvvrvhpet gertlvlgsy varfvgvskq dsqrlfdlfe shitaqentv rwkwkqgdva
      241 mwdnratmhc atkdysdqrr vvrratiege vpvsvdgrys varfkfrg
//
LOCUS       WP_457659793             387 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 aminoacylase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659793
VERSION     WP_457659793.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 10145370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..387
                     /product="M20 aminoacylase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /calculated_mol_wt=42251
     Region          13..383
                     /region_name="M20_Acy1-like"
                     /note="M20 Peptidase aminoacylase 1 subfamily; cd05666"
                     /db_xref="CDD:349916"
     Site            order(103,105,138,164,359)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:349916"
     Site            order(187,209..210,214,217,220,237..243,247..248,250,
                     256..258)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:349916"
ORIGIN      
        1 mhkidtfnsl akdviawrrh lhqypelgyq lhktarfvad klksfgvdqi etgiaetgiv
       61 aaikgklgdg ptiglradmd alpiseasdk pwtsrtsglm hacghdghta mllgaakhlt
      121 etrdfrgrva fifqpaeedg rgalrmveeg vmdrfnvsrv fgmhnepgie vgkfgicygt
      181 imaaldefdi ivtgkgghaa ephrcidpvv iaaqvilglq tlvsrntnpl dslvisvttl
      241 naggayniip ervqlsgtvr tlrsdlrdfa elrihqaaqa iahgfggqie fkyrrlepvt
      301 rnhreetsla ievarnlvge davddkfpps mgtedfcyms earpaayilv gngetaalhn
      361 psydfndeav rygvaywvdl vekalaa
//
LOCUS       WP_457659795             154 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659795
VERSION     WP_457659795.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17457
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meldradlal lkavqrnnry tsdelaqlvn lsptacqrrl rklreegvie advsivspka
       61 vgrqltmivl vslereradi vdrfkasirk tsevmigyyi tgdadfilvv tavdmegyeq
      121 ftrrffyenp dikgfktmvv mdrvkasfaf pige
//
LOCUS       WP_457659798             393 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457659798
VERSION     WP_457659798.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40675
     Region          4..392
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mstpsivias agrttvgsfn gafantpahe lgaavikgvl eragveagev devilgqvls
       61 agegqnparq aarkagipqe atawgmnqlc gsglravalg mqqiaagdan iivaggmesm
      121 smaphcahlr ggvkmgdfkm idtmikdglt dafygyhmgl taenvarqwq lsreeqdafa
      181 lasqnkaeaa qkagrfaeei ipfivktrkg dltidqdeyi rhgatidqmt klrsafdkeg
      241 tvtagnasgl ndgaaatllm tetqaskrgi qplarivswa tagvdpqvmg tgpipasrka
      301 laragwaigd velveaneaf aaqacavnkd lgwnpeivnv nggaiaighp igasgarvls
      361 tllfemkrrg iskslatlci gggmgvamcv eam
//
LOCUS       WP_457659802             217 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659802
VERSION     WP_457659802.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..217
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23014
     Region          1..212
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mnttyaylpy lvqgvtesva lggasflvat ifglvlalir dnssrfiqtl itvyisvfra
       61 lpelltillt yygsivvtrs vglpdlnpfa aalialgvqi gsyacqifsd ayravprgli
      121 eaghavgmps ykinvriavp lmlrlaapsl gsllnvvikf taiasvigvt eltrraqivv
      181 gathdplaaf gcaaviylai savltifqrr letakql
//
LOCUS       WP_457659806             948 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase, partial [Streptomyces anulatus].
ACCESSION   WP_457659806
VERSION     WP_457659806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 948)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..>948
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
     Region          2..947
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 magveelars agattpmvvq aalavllhrl gagddltlgs piagrideal ddlvgffvnt
       61 wvlradlsgn ptfarlleqv rgkalaaydh qdapferlve llnpdrstaf hplfqvmfaw
      121 qntaplelrl pglhvsdvpv ppltakfdll fnlgpdadgg aggaieyatd lydratveri
      181 aerlprvlah vvaaphtrva avdvlneder allfgemndt atelpadtia elfhrramrt
      241 seaaavlcre eeisygdlha raarlarvla argvgpetvv avalprnphl lvallavlms
      301 ggtylpldpa hpvrrtaall adarphlvlt eqdtagtlpl dgltvlttda wadapgqdpa
      361 pvlpdalayv mytsgttgtp kgvgithkal angvlalapt agvsegtrvl sgtsvtfdvs
      421 lfetltalca ggtvelvrda lvlgerdvwr ggvlstvpsv ltallpeiag rvradtvvla
      481 gealtaraar qvrtalpgar lvnaygqses fyasaftvad aealpagdvi pvgrplanmr
      541 myvlgpglap vppgvvgely vggpvgrgyr gravltaerf vpdpfgppgs rvyrtgdlar
      601 vgpdgqivcv gradtqvkvr gvriepgeie taltghpgva eavvvacdgd pgagpgarrl
      661 vgyvvpvgsg alddvdltag lsvaelrghl varlpdymvp aafvlldrvp lnangkldrs
      721 alpepepaap ggyrapgspe eeilavvfae vlgldrvgvd ddffaaggds irsiqvvars
      781 rgrglllspr qvferrtvaa lapvarpart aapvlaelpg gdegwmpllp mahyllhlgg
      841 dhdryamslv lelpsdites gllttltalv erhavlrsrl tmtpepglva gpassvdvas
      901 wlrvveaaap eareeqlaae cdaaagrlgp svgvmgqfvw vrpvvgvg
//
LOCUS       WP_457659811             138 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Sinorhizobium medicae].
ACCESSION   WP_457659811
VERSION     WP_457659811.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..138
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15090
     Region          15..136
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msietlkava hpwlcdamgh mnvrfytaff ddassyfvgg lgggvdqlad ahlgwadvrh
       61 vvefreevrs gallrvctrv tkigrtsltf qheltgpngn lhatmevvsv mfdlekrqav
      121 plpdtirsaa eqllgqhp
//
LOCUS       WP_457659814             288 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659814
VERSION     WP_457659814.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31642
     Region          1..>231
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdigllrtft avaalgsfsg aaqrlnmtqs tvsqqiarle ehlgkqllir ttrrcrlthd
       61 gdelmerasq vvalvdemen afrpelssgt vvvgvvddsy lfapltrala efverrptin
      121 ieiragmsad lvrelkarni elallrvdpe veragllqts klvwisapdw qvpangvipl
      181 avvggtcnyh kvaletlrra nlqsrrvvtc sslegvlevv raglavsvvp egelrngmei
      241 vndrrlprlp htglkisfse qepslaakql arvientlqn rvpmkrqa
//
LOCUS       WP_457659817             239 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457659817
VERSION     WP_457659817.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..239
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=26048
     Region          9..234
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mphlprigit pdindlvape teyvvmqnya davskagglp fllpyrehvd dyldaidgll
       61 vtggmfdidp alyrqtarkd yvmkpartnf eralieaals rgmpivgicn gmqllavclg
      121 galvqdipae iegalehkpn qsasiahhqi yisgtsrylq tpqgelhqvn svhhqsvlps
      181 dayqviavsp dgvvealekk dggfaigvqw hpeygladid tiifeaflak ardysekkk
//
LOCUS       WP_457659820             376 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457659820
VERSION     WP_457659820.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41988
     Region          29..135
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(41,44)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mvlkmestap alevqdwvrg rplanfepgk vyvvdfwatw cgpcvsampd lmllqekyrd
       61 sglevvgvaa dekavaadev rayldtwlte rfpklnfrig ldctgemnkl wmepsssfgi
      121 pssfvvdrds riafighpae lddvlpkvld gswrtsdqak sadreriaag redvflykvl
      181 aavkiedwkt alsaieegta lmpdslhlra ahadtllhkm rdiqaglpvl rqlvrdaidr
      241 nnedwllqam nqlfnpaydy tdfpsverla mgkelsehil altgledsvk assyrliapy
      301 yyesgnkara eellelalkl vdglpfpdni kkrflgdlll slakyrgqkv cygdvcaape
      361 drdtpkakei knnsat
//
LOCUS       WP_457659828             388 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457659828
VERSION     WP_457659828.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Goodwin,T.J. and Poulter,R.T.
  TITLE     A new group of tyrosine recombinase-encoding retrotransposons
  JOURNAL   Mol Biol Evol 21 (4), 746-759 (2004)
   PUBMED   14963102
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..388
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42374
     Region          190..387
                     /region_name="INT_Cre_C"
                     /note="C-terminal catalytic domain of Cre recombinase
                     (also called integrase); cd00799"
                     /db_xref="CDD:271180"
     Site            order(206,220..221,223,299..301,315,317,335..337,372)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271180"
     Site            order(215..216,343,347)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271180"
     Site            order(220,262,337,340,372)
                     /site_type="active"
                     /db_xref="CDD:271180"
ORIGIN      
        1 makslpspse dvhrradeld aldailpfdr rdqlaalltd ddvatlkhla qegmgentlr
       61 alasdlgyle awcrlatgdp lpwpapeall lkfvahhlwd pvkraedpth gmpievesgl
      121 raghllkalg phapatvrrr ltswsiltrw rglsgafgap slksalrlav rasnrprqrk
      181 skkavtldil tklleacagd rlvdardral llaafasggr rrsevaalrl edladeepvr
      241 anpadenspp lpclsirlgr tktataddde hvllvgrpvt alkrwlaeaq ikggpvfrri
      301 dqwgnvdrra ltpqsinlil karceqagld palfsahglr sgylteaanr giplpeamqq
      361 slhksvtqaa syynnaerkh graarliv
//
LOCUS       WP_457659823             294 aa            linear   BCT 27-JAN-2026
DEFINITION  ArdC family protein [Sinorhizobium medicae].
ACCESSION   WP_457659823
VERSION     WP_457659823.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Gonzalez-Montes,L., Del Campo,I., Garcillan-Barcia,M.P., de la
            Cruz,F. and Moncalian,G.
  TITLE     ArdC, a ssDNA-binding protein with a metalloprotease domain,
            overpasses the recipient hsdRMS restriction system broadening
            conjugation host range
  JOURNAL   PLoS Genet 16 (4), e1008750 (2020)
   PUBMED   32348296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Belogurov,A.A., Delver,E.P., Agafonova,O.V., Belogurova,N.G.,
            Lee,L.Y. and Kado,C.I.
  TITLE     Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa
            has a high similarity to the 'protein transport' domain of TraC1
            primase of promiscuous plasmid RP4
  JOURNAL   J Mol Biol 296 (4), 969-977 (2000)
   PUBMED   10686096
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..294
                     /product="ArdC family protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33699
     Region          2..>201
                     /region_name="ArdC"
                     /note="Antirestriction protein ArdC [Replication,
                     recombination and repair]; COG4227"
                     /db_xref="CDD:443371"
ORIGIN      
        1 mqsikdiyqr itdtiieqle agtkpwirpw rgssrgslvp rratgeayhg invlmlwlas
       61 elasyeentw mtyrqaqdlg gqvrkgekgs lvvkygtftp keredddera ipylkgytvf
      121 naeqiedlpd rfyrpaadlp atpvphletv atfvrntgaa ityggtsacy rpapddilmp
      181 dracfvdevh lystvlhets hyavrrimph gqvwrllcll lamwqfgiir afrgrravrr
      241 egvlimllvl vlpsrlyarv akliwqlrlw prnvpvaslf hasarhagyr ewfr
//
LOCUS       WP_457659835             161 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659835
VERSION     WP_457659835.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 161)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17916
     Region          36..102
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mslmsarglv eitdpefdrp vfrqpgfdgt lsakemdeki sawlkktrea kgisradlah
       61 llglsvsvyg ryergsearl siprlihlce imgfmpldvi fdaaphlwgk tleeaedrlt
      121 ltklieelpq dtmrdlirll rrmtpgepaa dtvatsmseg c
//
LOCUS       WP_457659837             405 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659837
VERSION     WP_457659837.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..405
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44392
     Region          59..310
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          326..400
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mattralilv egdpagnglv yvqaarrlgl hpiilsadpa qydslaaekv eairvdtkdl
       61 dalirecsrl rasydiagit cakewvcatv gklcryfelp gpnpasveec cdkfaqrell
      121 akagvpmpay rvathvteve raaaemglpv ilkpvvgngs sgvrlcrtvd evaehttyll
      181 ggthiwrssp rilvedfaqg thyiahtmgh evigieaadf drpphfvfrq svfpavltse
      241 ehkriadvsl sclralalgw gpanielrwt krgpvvievn prlagdpdlv klaygidlat
      301 ehiklvigek cdlrrkhsht aiwrnlipdr dgtldwiqgt sraaavpgvv evklfvepkt
      361 pivrkgdfqd sighvivtsr crtqtttilq raidliswsi tpfde
//
LOCUS       WP_457659845             428 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659845
VERSION     WP_457659845.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..428
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46001
     Region          23..343
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mllnrrgfma gaagaaagva lgsrttlaae svqlramwwg sndrskrtla vaklfeeanp
       61 diriigesls gdgywtklat qmagrsiadi fqlepstisd yskrgacmal dpfissaldv
      121 dafgqdvlkl ttvdgklwgv glglnsfalf ydadafarag idppgidttw aeyaeiavem
      181 tkavgkksag ggpygaryay vfdawlrqrg sslytdsglc fgveeakewy ayweelrkrg
      241 gtvgadiqtl dqntidtncl algysamgma ysnqmvgyql imksklgigm lpraekggps
      301 ghyyrpaliw sigastehge eaakfinffv ndveagkilg vergvpmspi vreailpsln
      361 ptetetvkyi nglkdqvgsy pspaplgate fdqrvlrpia delaferisi gdaatrlvee
      421 gratvrag
//
LOCUS       WP_457659852             226 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659852
VERSION     WP_457659852.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24757
     Region          1..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msplieahgl trilqetvpv tlvkdidlti gegefvavtg lsgsgkssll yllglldrpt
       61 rgmlrvrgrd tepmsetsra etrlstmgfv fqfhfllpef tarenveipm rkvarlgrde
      121 mraratells slglvdhlnk rpdqlsggqr qrvavarala ndpplilade ptgsldstss
      181 eqvfaildgl vrergktvva vthdfgmaar mdrrihlvdg evskee
//
LOCUS       WP_457659847             318 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659847
VERSION     WP_457659847.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33392
     Region          1..317
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mvgenplhvf atllrgafgs tdriagsllq atpiiicgva acialrgglf nigvegqlyl
       61 ggfaaawvgf sfamppvihv vvavaaaila gclwilipal frakfgtnev vttilanyia
      121 vlltsyltis vfkrpggwse tdpiavtarl pqllpdsrln iglfigigla iglhlflrht
      181 sagyamgamg anpkfaeygg vrtrrnvfli llasgavggl aggvetlgvh hrfmegfapg
      241 fgfdgviaal langnpigmi gtalffgalr agsllmevet nasreiitvi qafiilcvsa
      301 qilirrrsgr tgerrwkf
//
LOCUS       WP_457659856             611 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457659856
VERSION     WP_457659856.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 611)
  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   5  (residues 1 to 611)
  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 611)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18652649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..611
                     /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=66094
     Region          28..324
                     /region_name="COG2984"
                     /note="ABC-type uncharacterized transport system,
                     periplasmic component [General function prediction only]"
                     /db_xref="CDD:442223"
     Region          310..611
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mvlrirpqtv ivtmfaliag tlvchstepr rvlliyeses tlvaamqlas gfqeymeand
       61 pghveyytey ldtlrfsspe hslrlagfle akyrqlnldv vvaagpgalr fvletrerfa
      121 ndvpvvfgav tessvtgnlp pdvkgvvsrf dvgktvqlas rlqprarkvv vmygsapfdr
      181 kwgdtatavl geryagldve yvsglsldgf rktaaelpsd aalviltvfe daegmkfvpr
      241 daaraiaaas gapvygvyss ylgfrvlggy vgtfpsigaq maalsldvmr gdlsaprttp
      301 aqetalvdwr evqrlgiddv lipedaeils yapsvweryr lpisaallvi aaqmltiaal
      361 vyqnrrgrrl eatlaserve lahlsrrsql gelsgafahe ltqpltsila naeagqrlat
      421 etapdmneir aifddivadd rrassvisql rsmmlkgeas qeildlndav rqtvalahae
      481 mlarrtevev knelasvrvk anlvqlqqvi lnllvnaada madippkqrk veiavdrsnn
      541 gycelsvadm gpgipagmqg evfkpfvssk kgglglglai crsiveaqgg klffddgvkr
      601 garaiiilps a
//
LOCUS       WP_457659862             301 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659862
VERSION     WP_457659862.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /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]"
                     /calculated_mol_wt=33373
     Region          <185..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 malhqesnav dsqgpiirsi tsgdisvtrv csdrydlkaa patpcaeafs vivqlrdfea
       61 hrlwkagklv yegghsrasl aitdlrdrwq cnhlspfdni rfqipfarms afakqagrne
      121 ylglasvqgr idpvmyglaq allpslespe tasslfleqi nlavlahlsq tygglhfpig
      181 kkgtlapwqe rlateflanh fnkpfslgel arlcelsrsy fnkafkesfg rtpsrwlsey
      241 rtgrvkelll qdvpiaeaai acgfadqshl trvftgltge tparyrrknr carpameqls
      301 g
//
LOCUS       WP_457659864             287 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659864
VERSION     WP_457659864.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..287
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30253
     Region          1..286
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpfeyyepa tlaeasellr rlgkdasiia ggtdllvelk edlrsahhiv nikkipgltd
       61 faydpanglr fgalvtvrei etspavngny pnlakavsll gsiqvrnrat vvgnicrasp
      121 sadtipplia dgaslsvysg gtersiplde fftgpgrtvl vpgdivtgis mpaprptsgr
      181 ayikhgrrka melatvgvav smehvagqcs dirialgava ptvirarrte dllrgrmida
      241 allaeaaesa mqeatpignv rasaayrhdm vgvltrraig yamggvq
//
LOCUS       WP_457659866             158 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659866
VERSION     WP_457659866.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..158
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15783
     Region          8..>157
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mntatvypae aprslkaril gspsagpllv lfgfcvifal tnprflathn lsiilqqtvv
       61 igalaigqtl viltagidla vgaicvlgti vagklanlgy dpvlsmgiav lictaagfaa
      121 gglvsglrlp pfivtlgilg iltaalrlis eggrlpga
//
LOCUS       WP_457659868             424 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659868
VERSION     WP_457659868.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..424
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=45092
     Region          60..318
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 malnivhrgr valatagnpl rhvfraerva rhapelagvg prpirsaavi gggtmgtgia
       61 aalcnaglpl viverdeaam egalarlrai fdgavkrrri saglaaerla rvtgatdyav
      121 laeadliiea vfedldvkrd vfrnvgaacr hdavlatnts yldperiadg iasperflgl
      181 hffspaqvmk lleivptgat apealatgfa larmlnkipv ragisdgfig nrilkvmrsq
      241 aerllvtgat psavdaamra fglpmgpfea qdlggldiaa fqrraararg lpvfapvadr
      301 lcaiarfgqk sgggwydyvp ghrtplpsea varlieeeaq gwprldwdea siidcilwpm
      361 vneaarived gtalrpsdid lveihgygfp rwrgglmhha qsqgldriva algafaekgl
      421 adpp
//
LOCUS       WP_457659867             172 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659867
VERSION     WP_457659867.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..172
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18394
     Region          <3..172
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mrdpflawtg ntmklggfvl tygvlimfil yasvwyllnq tkwgrhvyai gnnveaarlv
       61 gipvrrhlls vyvlagliyg iaawlalgri pnadpnamqs anldsitavv iggtslfggr
      121 gglvgtliga livgvlrngl tlagidplwq dlitgilvii avaldqlsrr rr
//
LOCUS       WP_457659873             856 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457659873
VERSION     WP_457659873.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 856)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 856)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 856)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..856
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=89738
     Region          80..856
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 mpdispgrts faasdralrr lsilnahvlp gapsassdri rcefnklllg svasialfcs
       61 ldsearaacv etspgaydcs gtgpgptftg qsvtinadpt asftsdvsit gpgtstlnnn
      121 gtltnslrat dndrftlnnr glidgtiflg gsganviiny agddvqngvt stgdshdtvi
      181 nrgffagsiv lgdgndvlgl iegtvqtsvd mgagddqftw lvgniaatvq mgegddravf
      241 gsltqqnlsa gkrvdgglgi dtlvwenttn ddgggsgdhp enivnweeie lrngsemtfi
      301 ystgnltlgd sasgtgtlsi detsavragn sfgygvrafd psqlvtvyna giidmtndtv
      361 nvgdllhdtf tvygnyvgqq gglqlhtvle sddapsdklv isgtgasasg gtsilitnvg
      421 gqgaltladg irvvdataga ttegtaftlg apvaagifey qlyrgglted pdndddwflr
      481 sggvsppppp pppppppppp pppppppppp pppppppppp ppppppgpsp itpsvrpeip
      541 gyilkpalmq kmgvaaigtf herqgdqfll nsngylpgaw grlfgesfdq swsskisrfe
      601 fevspsfsge lwglqagqdl igalhddgsq drvgvffayt gtsgsnggnt lgrlqvesgs
      661 idlhansiga ywthigadgw yvdsigmysw ldggsssdrg igvdtsgnst alsieagypf
      721 rfdngwvlep qgqliwqhvd lddandrftg idyesfgtwt grlgvrlean ttmndvpvqp
      781 fasvnlwhdf dqdykvsfnr vpvvteleqt llelnvgfsa qmsetvsvyg glqfatgldd
      841 ddnrgyggni glrikw
//
LOCUS       WP_457659876             342 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659876
VERSION     WP_457659876.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37654
     Region          3..338
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mphraffafi mpsllamllf ialpivsvav qslyveherv vtevetcapf agcttetrvd
       61 aeateklrda eplgrfngfg tyldrnhlat aemnailtdn agfadvasri ynlpfyrala
      121 ftltytfvvt plamllgfci algvnaippf ykgpviffsl lpmivtplvg aliiywmssp
      181 qgilgatlqs llnnstlslk ssavltwvtl lvygvwhnap fsfvvfyagl qtvphdtles
      241 amidganrwe rirfvviphl mplatfvalv qlmdnfrvfe pivgfsaean atslswsifn
      301 dlrgqvdqlf gsaaatsmlt ivgvvillsp vlvrtwrefn rr
//
LOCUS       WP_457659877             328 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659877
VERSION     WP_457659877.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33152
     Region          6..222
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mavivgstgy dilqgtdead hiwglhggdt idagggddfv dggdlsdvlt sssgydrlhg
       61 gagddqivlt gtggavtggl gfdrltvdms mlsdqlvfng asghgiigyg sagerhvffh
      121 dvewlsivsg sgndrivgta ghdristgag idvvvagagn dvitntggqd rleggdgndr
      181 fvlvgtgstv fggtgddtlt ldlaatsgdi vfnantghai iasrtpderh vfahhseier
      241 ievitgsgnd rvqgttfgdv iktdagddvv dggagddsii dgrganhlsg gdgsdlittt
      301 lysasvdggs gqgfganrgt vtyerrrh
//
LOCUS       WP_457659878             360 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659878
VERSION     WP_457659878.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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..360
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..360
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35817
     Region          80..328
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msdvaidfvs gtastgtvfr nietaslalg agndtvittd flasfvdaga gddrlvggag
       61 sdafhgedgn dridsgagnd tittglgddv asggegddsl andggkdild ggagddwiad
      121 aipgsgslgd gsvmlggdgn dafrasftge vdggdgrdll qlrlgslsaa idfdatqgai
      181 qtgltfanie dftvttgvan dvlrggdgnd efdslsgndl leghggndil rgysdwdrlf
      241 ggdgddrleg gphddllsgg ngtdtliggs gadtflwsde vagqsgidhi vdldfgdlia
      301 fsaaasertg ihdhagfvaa atntadgvyv afngsaadgi lienasiaal taddlvfgla
//
LOCUS       WP_457659879              88 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Sinorhizobium medicae].
ACCESSION   WP_457659879
VERSION     WP_457659879.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 88)
  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 88)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..88
                     /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=9365
     Region          3..83
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mtqtikdkvr tfvienflfg dtayeladda sliendiins tgvlelvafi eddfgiamad
       61 adivpqnlds larisafiea kgavpvsa
//
LOCUS       WP_457659880            1065 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457659880
VERSION     WP_457659880.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1065
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112116
     Region          1..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 miseifidrp rfaavisivl tlaglialtr lpvaqfpdiv ppqvsitasy pgagadvvea
       61 tvaqpieskv vgvddmlymk stsgadgtys ltvtfavgtd pdiatvnvqn rvalaepvlp
      121 aevkqsgvsv qkrssslmqv iaihgendef dnlflsnyat invldtikrv pgvgdatlfg
      181 aqdysmrivl didrltnlgl tptdvinalk aqnvqaaigr igaqpmtddp lfqlniqtqg
      241 rltdpaqfgd vvlragadgs fvrirdvahv elgsvssnst aringkpvam igtyqapgan
      301 alaategvqq alerlsaafp egltytvsyd tsdfvqasve nvehtlleaf alviivvflf
      361 lgnwratlip liavpvalvg tfavilamgf slntvsllal vlaigivvdd aivvvenver
      421 vteenpgmsa aeasrlamge itgaivaitl vllsvfvpva fipglsgqlf qqfavavsvs
      481 mvisainalt lspalcaill kphhgpkrgv lgwisrgidr trngyahlag giarrailgl
      541 vllavaigas gwlfrvvptg flpsedqgaf faeirlpega sfnrtdavvr qvesllgsie
      601 gvanvttvtg ysfldgiaks ssafaivtmk pfaereseta svnaaiatvm aqgaairnaq
      661 vfafnlppii glgtgsgfey qlldlqgrsp aelaataggl mvaanqnpql gptfstysas
      721 spqlyldldr drlqalgvsv sdlfatlqgt lgsyyvndfn lfgrswkvtm qaaetdrdav
      781 edisrlhvrn aagdmvpvas varvnyivgp qsivrynnyr sitlngqpap gvssgqalaa
      841 meqisaatlp pgysfewtgt alqeleaagq ttvilalavf faylflvaly eswtipipvl
      901 lsvsvgvaga lvavllagls fdiyaqiglv vlialaskna ilivefakfq rekgvpivda
      961 avegartrfr avmmtsfafi vglvplvtae gagmlsrrav gtgvaggmla asllgifiip
     1021 alyvvfqwlr erghklagls shaaveaprk geleesierd rnvad
//
LOCUS       WP_457659881             253 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659881
VERSION     WP_457659881.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26586
     Region          4..245
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mvslalkdvg atygrrvvls dintgvlkgg qltavigpna agkstlfkri aglaagpglv
       61 hlsdtakgse aicympqdtg anavltvyel vllsakqgsa wkvkdgelqe idrvlaalki
      121 nelafrglge lsggqrqlvs iaqalvrkpe vllmdeptsa ldlfrqievl gfmkrlaaqs
      181 gmavlialhd lnhalryced tivisdgsvv asgpthavvt admlktvyrv earveacsrg
      241 rpviivddsi alg
//
LOCUS       WP_457659882             485 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659882
VERSION     WP_457659882.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..485
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52332
     Region          8..460
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
ORIGIN      
        1 mmdsfgqnap rptvaiiggg ftgamvamhl ardramggwq iavfeprvrl gcglaydtae
       61 pahrvnvpaa rmsidpddpd dfarwlalqs elrddpevla gdghlyprrq lfgryvaeav
      121 vpfvrsgriv hhrerviave regaawavrg eggtlnrada lvvatthpap eapagigavl
      181 tghpryvpds tepgaldkir tddrvliigt gltsadviat lrtrghmgpi tafsrrglrs
      241 rghadraqdp fgdfvaqpwr saaellaqvr rtisdaeaeg ftwhavldal raqggeiwrn
      301 lpvderrrlv rharpfwdvh rfrvapqida ivstglkdgd irvragsiah laragenvav
      361 tfrgrraggt eewefdavvi ttgpahrsil qsqpwleslg aagylrpdtv glglacseas
      421 raldgeggev ddlfvagpla rgtfgelmgl pqvndhaifv aaqiaalaqa rraesvrsrr
      481 eeaat
//
LOCUS       WP_457659884             338 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457659884
VERSION     WP_457659884.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..338
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37404
     Region          15..313
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(149..151,211,233)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 mpdlttnsir gsrsnvsvcr rskagrfrag llvlrriyrl rsairhsqpd fvlsfltrtn
       61 vltllatigl pvpvvvsern npalqpfgvf wkwiqrrlyp rafglvtmtr galdyfpqkm
      121 rsrgwviana vdlpgewqkr rgnniltavg rltrqkgfdl lieafariaw rhpewklviw
      181 gegddrksle alrdaldmtd rvempgvtqr pglwvetadv fvlssryegw givlleamaa
      241 glpvvsface wgpsdmvehg edgllvpsnd vdalaealsr vladgelrsr laanaeasak
      301 rylpdrilsq wdavalsalk htardhaaaa svvgagsa
//
LOCUS       WP_457659887             312 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659887
VERSION     WP_457659887.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=33738
     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 miqieevtkr ygdttvvngv tltvalhtvt vivgtsgsgk ttllrminrl veptagivki
       61 dgednrsipg yelrrrigya iqghglfphr tvaqniatvp tllgwekdrt eakveellkl
      121 fqldpadfgp ryphelsggq qqrvgvaral aaepnvllmd epfgaldpii rskaqedlaa
      181 iqkhfgttii lvthdmeeaf hladkiavmd kgevvqyatp aemlvkpatp fvetlvgase
      241 rpfrllgiet vgeavepgsa egrpvpevls qrdalsellw sgrsalpvaa angeilgrvt
      301 lqaivkraar pr
//
LOCUS       WP_457659888             287 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659888
VERSION     WP_457659888.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..287
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31317
     Region          1..273
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdifatlqee kgrlsqsenr iadillndfe favnasiiel agkadvsppt vtrfcrrlgc
       61 esfsdfkvql artpyvgmry lkpepksqep gdvaqdiitk aqnallllhr sldlaaiera
      121 adqlaqaemi yafgsggnss miagefqnrl frlgmritss sdhsmqmmma aaarpadviv
      181 gssfsgrnae lvrafilare akvptialtq sgspvaqaad itvpvdlpeg nniyrptstr
      241 iaylalldiv asfvayrvqp qatvtlrrik qqlvvhrdgd drqlmgd
//
LOCUS       WP_457659895             305 aa            linear   BCT 27-JAN-2026
DEFINITION  N-formylglutamate amidohydrolase [Sinorhizobium medicae].
ACCESSION   WP_457659895
VERSION     WP_457659895.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..305
                     /product="N-formylglutamate amidohydrolase"
                     /EC_number="3.5.1.68"
                     /GO_function="GO:0050129 - N-formylglutamate deformylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006548 - L-histidine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34656
     Region          35..222
                     /region_name="FGase"
                     /note="N-formylglutamate amidohydrolase; pfam05013"
                     /db_xref="CDD:461519"
ORIGIN      
        1 mdapaeamnm npgpeplnla pcaasdwwtq hrgdspvvat aihdghavrd avqrlcalde
       61 aerlreedpf teflirdfsn rivvhrsrfe vdinrpraga vylrpeqawg ldvwaeeppq
      121 avvdaslsmh deyyemlksf lagierchgr fvvldvhsyn hrragrkaea apaadapdin
      181 igtismdrrk wacvvddfma alrsfdfpgg sldvrenvaf qgrgeqtrvs rpegfhlpas
      241 rrtvreplds hrshqanrfv pnacqctkrp rlsrascrkn cearvlwnrk rlyfriiqal
      301 sfrlm
//
LOCUS       WP_457659890             232 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457659890
VERSION     WP_457659890.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bondos,S.E., Swint-Kruse,L. and Matthews,K.S.
  TITLE     Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox
            Proteins
  JOURNAL   J Biol Chem 290 (41), 24669-24677 (2015)
   PUBMED   26342073
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Ravcheev,D.A., Khoroshkin,M.S., Laikova,O.N., Tsoy,O.V.,
            Sernova,N.V., Petrova,S.A., Rakhmaninova,A.B., Novichkov,P.S.,
            Gelfand,M.S. and Rodionov,D.A.
  TITLE     Comparative genomics and evolution of regulons of the LacI-family
            transcription factors
  JOURNAL   Front Microbiol 5, 294 (2014)
   PUBMED   24966856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Swint-Kruse,L. and Matthews,K.S.
  TITLE     Allostery in the LacI/GalR family: variations on a theme
  JOURNAL   Curr Opin Microbiol 12 (2), 129-137 (2009)
   PUBMED   19269243
REFERENCE   4  (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   5  (residues 1 to 232)
  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   6  (residues 1 to 232)
  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 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   8  (residues 1 to 232)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   9  (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
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
REFERENCE   11 (residues 1 to 232)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
REFERENCE   12 (residues 1 to 232)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..232
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25098
     Region          23..68
                     /region_name="HTH_LacI"
                     /note="Helix-turn-helix (HTH) DNA binding domain of the
                     LacI family of transcriptional regulators; cd01392"
                     /db_xref="CDD:143331"
     Region          83..>187
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mgkgnggngs pkdagggrpt mtdvariagv sqssvslvln emsgarisae trarvrdaar
       61 kigyrlpntr qdldhapaie kdtiafivde istsphpvvs ldgirdyafe qgllvsahat
      121 rsnpdlesav lrsvlrdpai agviyatift rkvsvprele nvptillncy aeprqhmaiv
      181 pgevagglrg drashvsrap ahrlhqrrtl dgrryrpaqr lqaslgdrry rl
//
LOCUS       WP_457659899             537 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659899
VERSION     WP_457659899.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 537)
  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 537)
  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 537)
  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..537
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..537
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54841
     Region          <63..243
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <123..>179
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
     Region          259..503
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matityhfpa glypnqynpp lsgvsvnpsf gelvdmstas rstttstsvl yrldnglkmk
       61 lvgtgfsfda sgdavggtit sievllnngt gliqtisglf qdasaafdss gleswlasgn
      121 dtingslgnd eiwgrlgndv lngnagndlv tggggadtyd ggagfdilnf qdaydsptai
      181 rginlnatag tvvdqfgfse tfqnfeefrg tqfsdsmmgs svdetffgfg grdninggag
      241 idtvrydrdf qrgatkgvsi dlstgiatdg fgsrdtltsi eniratefkd tivgssaanf
      301 lrtfagndsi nggggsdnmr ggigndtyfv dntgdivdea adsgagtdtv qstvsfnlgn
      361 tavakggven lvllgtgnin gtgnalnntl sgntgnntfs gfagndtidg glgndlingg
      421 lgndsltgga gldtfnfsna ldatnnvdti ngfvvaddti rlenavftgi vgtgtltaaq
      481 fvtnttglaa daddriiyds dtgrllydsd gdgaggsvhf atvgtnlgmt asdffvv
//
LOCUS       WP_457659900            1013 aa            linear   BCT 27-JAN-2026
DEFINITION  AsmA family protein [Sinorhizobium medicae].
ACCESSION   WP_457659900
VERSION     WP_457659900.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Prieto,A.I., Hernandez,S.B., Cota,I., Pucciarelli,M.G., Orlov,Y.,
            Ramos-Morales,F., Garcia-del Portillo,F. and Casadesus,J.
  TITLE     Roles of the outer membrane protein AsmA of Salmonella enterica in
            the control of marRAB expression and invasion of epithelial cells
  JOURNAL   J Bacteriol 191 (11), 3615-3622 (2009)
   PUBMED   19346309
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Deng,M. and Misra,R.
  TITLE     Examination of AsmA and its effect on the assembly of Escherichia
            coli outer membrane proteins
  JOURNAL   Mol Microbiol 21 (3), 605-612 (1996)
   PUBMED   8866482
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Misra,R. and Miao,Y.
  TITLE     Molecular analysis of asmA, a locus identified as the suppressor of
            OmpF assembly mutants of Escherichia coli K-12
  JOURNAL   Mol Microbiol 16 (4), 779-788 (1995)
   PUBMED   7476172
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1013
                     /product="AsmA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=105055
     Region          1..460
                     /region_name="AsmA"
                     /note="Uncharacterized conserved protein AsmA involved in
                     outer membrane biogenesis [Cell wall/membrane/envelope
                     biogenesis]; COG2982"
                     /db_xref="CDD:442221"
     Region          <426..788
                     /region_name="AsmA"
                     /note="Uncharacterized conserved protein AsmA involved in
                     outer membrane biogenesis [Cell wall/membrane/envelope
                     biogenesis]; COG2982"
                     /db_xref="CDD:442221"
ORIGIN      
        1 mrrvilcvlg avalavtaia ilpslissdw mraelgrqls satgssiafn gpvkfsafps
       61 lavvaedvtl saeaqgvtae faqvtgsvaf sslwadrlri eeisldrpvi ildekaadet
      121 tpaqegsgea rssdplpdla allersavds vsitsgtfir rsaarpeevv sdveltlsvp
      181 diddtfslsa sarmgernye asftistlrs llgrqpadld ltveadpapa pgltslsasg
      241 kvtlnangsy qirggkvetg eqafglnalf vpgkrarfla dldadrldlt pfvdttpaas
      301 pskvlstgtk tdvgnrvglq flasfdadvs inaaaitfge msasdvsvsa elkdgnlave
      361 lgqlgidagv vtadvatdvr sddpvfrgrl ssegldigsl saladrsvpv sgaliidadf
      421 afrgldadsi rktidltgtv glrdasfalp lsdeamqevk akkisaries lrkpvrlegr
      481 lewrnkpvdv dlqipaadtl ltgdlasqgi plklqmqmpd arlsldgraa lpgtyagrld
      541 fsvadlsafl sgfgqsgaes igplafsgnv vsgaqgfsfd kasvsvngie atgngsvefa
      601 tplkietsld fteldlarla gagapapqpk akakakavig advpldlssl rsvdatigin
      661 aeklgygrvf agpvttmlvv segvasltlp espfygghvv aslkadgsqp epsivfqasi
      721 srassapllt dmagfryleg alnarfdvtg aggttktlak slqgtaevtf adgairgidi
      781 advynnlvrl mssgfkqdds kattftelga sfaieggvar tediklvgpl vrmtgegaad
      841 laqstlnfrl eprivaslqg qgaeistdgv gvpvvvegsf aapriypdls dllknpdaal
      901 aklkdfglpi dklpigdlln gdgagaavad llggtldkal kdkafkqeeq qlsieeiigg
      961 dpapkpdeaa aevppneeaa kadapteqpa ngteepseea dgpmegffkq llr
//
LOCUS       WP_457659904             214 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659904
VERSION     WP_457659904.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..214
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23673
     Region          3..214
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mhraiksgay kpderlpteh elatefevsr pivrealrrl reqgliysrr gagsfvratg
       61 lreplgfgql envadllncy efrltlepaa aaaaalrhde tslaairral ellrdatnrq
      121 shredadfqf hlaiaraaqn syfstameal kehiavgmkf hgisvkreas glsrvfaehe
      181 aiadaiaagn aedarilmlk hltgsrdrlf lasq
//
LOCUS       WP_457659905             490 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457659905
VERSION     WP_457659905.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 490)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..490
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53367
     Region          3..479
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 mriftaalat etntfspici drrafeasly aspgkhpetp tlctapitvg rrvaaekgwi
       61 liegtaawad paglvnrrty edlrdeildq lraalpidav ilglhgamva dgyedtegdl
      121 lqrvrelvgp evlvcaeldp hshltnrrva aadffvffke fphtdfvera edlwrvavdt
      181 legrvtpvms vfdcrmidvf ptsrepmrsf vdrlmqierh dadvlslsvv hgfmagdvte
      241 mgtkmlvvtn gkaekgkala relglelfsr rgtyrmpeid ahqavaqaia apsgpvviad
      301 mwdnpgggta gdatvvleel larkatdtav gtiwdpmavq icmaagegae iplrfgaksa
      361 pgtgrpidgi veviklvrna emrfgesiap fgdaahirlr gidiilnttr aqsfdpslfs
      421 amdidpgskk ilvikstnhf yasfskiase ilycsagtpy pndpaktpyr rarrdiwpmi
      481 adphgpdqgv
//
LOCUS       WP_457659908             180 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659908
VERSION     WP_457659908.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..180
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=19961
     Region          <10..175
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtfqgrvssm etvilrfsht qnadelldpd sffsgprffl rpkikqqeaf gnrtaadllr
       61 aadpgrpalv ltrnengrpf kmhitdtrdm argvllalsh pkaaggvfnl gatdpvdfae
      121 vlpvmadrig wplvtvdlpg sgvwyhtsnq rirealgfep kwpimrmlde avaawttrqs
//
LOCUS       WP_457659920             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659920
VERSION     WP_457659920.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34764
     Region          5..323
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtmplleidn lhvcfdtrag tvqalrgvsl svapgetlgi vgesgsgksv taqavmglid
       61 vpgrisggei lwqgqplagv dvtraargiw greitmifqn pmtslnplmt igaqiaevve
      121 lhmgfdrraa rqraaellsa vgiagaerrl dqyphefsgg mrqrvmiamg iacepkllia
      181 depttaldvt iqaqilella elqekmelai vlithdlgiv aglchrvavm yagqivetgp
      241 vdaifenpsh pytqglirst pgldadeerl taidgappgl lrppsgcafl prcpigdegc
      301 rapqrlravg sgtvacrkag eqawreav
//
LOCUS       WP_457659922             476 aa            linear   BCT 27-JAN-2026
DEFINITION  CpaF family protein [Sinorhizobium medicae].
ACCESSION   WP_457659922
VERSION     WP_457659922.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..476
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51694
     Region          75..458
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mfgkksisek qiseaavqsv ienepqaapa lvqvlkptqv aatarfdkae qyyslkkeif
       61 saliatidva alsnmdveqa rgeigaiind ivaakkagis maeqnnllsd icndilgygp
      121 lepllarddi adimvnganq vfievngrvq etgvrfrdne qllnicqriv sqvgrrvdes
      181 spicdarlad gsrvnviapp laidgptlti rkfekekltl dqlvrfgsis qegaevlkii
      241 grvrcnvlis ggtgsgkttl lncltgyidh gervitceda aelqlqqphv vrletrppni
      301 egqgeitmrs lvknclrmrp eriivgevrg peafdllqam ntghdgsmgt lhanspream
      361 arveamitmg gsslpartir emlvssvdvi vqaarlrdgs rrithitevl gmegdvittq
      421 dlfiydilge dekgniigrh rstgigrpaf wdraryygee grlaaaldaa emkaaa
//
LOCUS       WP_457659927             128 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457659927
VERSION     WP_457659927.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..128
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=13613
     Region          <24..>124
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mifgrtdkrl sertskmpad rtgtfvanvs srrdcdalva etverfgrvd tlvnaagmnl
       61 vgtieetsde dweecitsdl sgvfymsraa vphlketkgs ivnigsvssl gggwshaayn
      121 aakavspi
//
LOCUS       WP_457659928             216 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Sinorhizobium medicae].
ACCESSION   WP_457659928
VERSION     WP_457659928.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..216
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23396
     Region          <4..211
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mralqgisar lntmvsfwlv vllyvilgll evsdlgarir rltdddaari isgfelaasr
       61 irryllirti msaatgiavw alatafglrf aaewgivaft lnyipfigpa fatilptcya
      121 laqfqspqsa livfaclsta qfiigsyiep rvagntlgis pslvlfsvfl wtflwgifga
      181 figvpitiav lsfcaqfast rwlaellgke timdga
//
LOCUS       WP_457659929             592 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Sinorhizobium medicae].
ACCESSION   WP_457659929
VERSION     WP_457659929.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..592
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65420
     Region          52..481
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,316..317)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,317)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mkpisesrfg ataaaiarsq gwkafalagt ilvssvvtts spasaqdapg kpnilvifgd
       61 dvgqfnlsty sfglmgyktp nidriadegm kftdyyaens ctagrssfit gqtpkrtgls
      121 kvgipgapvg lqdrditiaq alkplgyatg qfgknhlgdr deylptahgf deffgnlyhl
      181 naeeeperpy wpkddlayvk ansprgvihs yadgriedtg alnakrmeti ddettsaaie
      241 fmkkqveqkk pfftwmnttr mhvfthvrps mlgqsgmpgn eyadgmiehd ghvgkllkal
      301 ddmkiadnti viyttdngpn qfswpdaatt pfrsekdtnw egafrvpami rwpgkikpga
      361 vsnemfsgld wfptllaaag egdikekllk gtdvagkqfk vhldgynqlp yltgeteqga
      421 rqefayfndd gklvafrykd wkavfcemka pggfrvwyee fdclripklf nlrmdpmera
      481 dtvsdqyddw riknaymmgw mtfhaaqfle tfvdyppsqt pasftidqie adverrsaek
      541 aggeqivhga crlsstrpis ssgasplpar ssgsttrsnl qdgsspqthk np
//
LOCUS       WP_457659931             484 aa            linear   BCT 27-JAN-2026
DEFINITION  TrkH family potassium uptake protein [Sinorhizobium medicae].
ACCESSION   WP_457659931
VERSION     WP_457659931.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..484
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52589
     Region          68..481
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 msasllrhai hiasilglyl sgamlipaml dlyyghtdwq vfataafvtn glsattfmat
       61 ragpppfskk fgfllvnvlw stfaligalp lwmssldldf aqalfesvsa itttgstviv
      121 glddappgvl mwrslicwlg gvgivvlglf iipylrvggm sffkmessdt nekpfarltt
      181 fsrafftvyv gitllcaigy nltgmnrfda inhamstvat ggfsthdasf ayfgsipllw
      241 tatffmtlcs lpfsilivfv argrldalrd pqifvflayl tvfalsaaiy hrltngvefh
      301 ialahsffnf ssilstagym sedyqlwgpf vvmaafiatf mggcsgstag gikayrfivl
      361 fnaihsglrk liypaavypi rygrnsldad tlraillffv tyillwilgs ltmaalgydf
      421 ltsvsavitc lsnvgpglgn ivgpagnfss lkdpelylls lmmmmgrlev lsvlviltpv
      481 fwkq
//
LOCUS       WP_457659940             179 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome b/b6 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659940
VERSION     WP_457659940.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..179
                     /product="cytochrome b/b6 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19518
     Region          1..178
                     /region_name="CytB"
                     /note="Cytochrome b subunit of Ni2+-dependent hydrogenase
                     [Energy production and conversion]; COG3658"
                     /db_xref="CDD:442875"
ORIGIN      
        1 mtstvkvwdr pirlfhwsla gsvalcwlta delqslheva gyavaglvgl rlalglagtr
       61 yarfsqfirs prrtllyagd mlrhkepryl ghnplgavmv vllllmvggi altgwmqttn
      121 aylgvewvee thealaelll vaialhvvgv ihaslrhhen lvlamitgrk rapaggdil
//
LOCUS       WP_457659941             633 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Sinorhizobium medicae].
ACCESSION   WP_457659941
VERSION     WP_457659941.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 medicae"
                     /db_xref="taxon:110321"
     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=68766
     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 mtigaigvvy gdigtsplya frealrpfgp dgveraevvg
       61 lvslmlwtlt iivtfkyvlf llradndgeg gtlsllallm kkapryttlm fmagilgaal
      121 figdamitpa lsvlsavegl klvtpafhdy vlpisvgimv llfavqsrgt gavsiffgpi
      181 tliwflvlga agvahigddl ailaafnpvn avtflwnagf vgfivlgavf ltvtgaealy
      241 adlghfgrgp iqaawfavvf paltlnylgq galvlshpea vsdpfflmfp nwallpvvll
      301 ataatiiasq avitgafslv rqainlgflp rfeicftset qtgqiylpfv nnallagviv
      361 lmfmfgsses lataygisvt gamvvttvla fefarhqwgw stltatavll pllvlelffl
      421 ganlfkiydg gyvpiliagt lmttmwtwrk gvsllrekta rqdiplsqfm amverkseha
      481 pvevpgtaif ltatpdttpa vllhnikhnh vlhqhnvilt iktarvpyvp ekdrytiekl
      541 sdrfsllelr fgfmddqnvs ralarcrkeg fkfeimstsf ylgrrkliaa pqsglpqwqd
      601 klfiamadsa idpteyfhlp pnrvvelgeq vvi
//
LOCUS       WP_457659954             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659954
VERSION     WP_457659954.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39254
     Region          1..357
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mskpflqirg irkeygpvta vqdvnldvaq gefltflgps gsgksttlyi lagfedptgg
       61 dillngesll stpshkrnig mvfqrytlfp hlsvgeniaf plkvrrlpka eidakvrqml
      121 klvrlegfed rkpaqmsggq qqrvalaral aydppvllmd eplsaldkkl reeiqheirr
      181 ihqqtevtil yvthdqeeal rlsdriavfs kgvidqigtg pelyanpatr fvaefigdsd
      241 flpcnvvsag ngraeiaice tmtvadiplh gtassgskaa lmlrperlll skrqsefglp
      301 vtvsditflg nnvhvatkts kgnnlsvrlp fgheaisgln rgdavwlkfd aesahvfgq
//
LOCUS       WP_457659955             385 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457659955
VERSION     WP_457659955.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..385
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41774
     Region          2..369
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(154,169,203,229,255,278,305,330)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mkisnvriyr veggglrpvi ieietdegis gfgeagvayg ygapavagml edmalrlsgr
       61 npleirriwq dlydqsfwak gggaisfaai saielalwdi kgkaaglpvh dllggamrgd
      121 vklyangwnh ehddvvnwak aaarpladgy ralkaypfay elpdgtfrhv sarmlddgrf
      181 rqaiekvkal rqevgpdiel mldlsgglcd dqllrfldvc rdlditwiee pldpfnlngl
      241 srvaarsgip ialgervygr ggfrnvldtg avsivmpdia ncggmleavq iagmadtynv
      301 rvsphncass lctaaslslc vaipnamnle vypyfansnt yvqvlenppe qavrrdgklq
      361 ansmpglgii vdrrrieafm sfalv
//
LOCUS       WP_457659956             247 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659956
VERSION     WP_457659956.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 247)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26894
     Region          11..247
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mwsspirgvp aslnprlypt slsagienir rvlsetgylr ayyvsvaytv ltiagvllig
       61 smaafefalf rfpgarilfa lvmlslmvpt aatliptylv vaklgwlntm qglvvpglas
      121 afglfmltqf mksipqemle aarldgathf qlywfialpl sktalvtlai ltfmktwgnf
      181 iwplvisqkp elftvsqvvs lfnaplshtt vdvvmtanll aaipplvffl ifqrqivegi
      241 assgtkg
//
LOCUS       WP_457659958             259 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659958
VERSION     WP_457659958.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..259
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29114
     Region          1..238
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvpalentia vlqylngtap heaslteive algiskthch silktlvhfe wlkydqrskt
       61 yrlhsgifts assllnspvl davrrhltal vhrvdipcll tqpmndgayi vidkfngpts
      121 melsfpvghr fprdacaqmr aylawqsper idawfrnwqp trytsrsplt eedvragiea
      181 trrrgyavsk geftegimai alpifdrdge vsyvfncsfm idrflplees varemlvalr
      241 dihrdtlarp paapaftgp
//
LOCUS       WP_457659959             264 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659959
VERSION     WP_457659959.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..264
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28327
     Region          3..251
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnvvsavnls ksfgalevlk gidldiakge vvciigpsgs gkttflrcin qlefisggal
       61 wvngelagyr iigeriqpld eheialqrra tgmvfqrfnl fahltaeqnv algpievlgq
      121 dpaqalgtar dlltrvglsh klksypaels ggqqqrvaia ramamnpqvl lfdeptsald
      181 pelvgevlkv mqevattgit mvvathelnf ardvsdrvvf madgrilevg speriltepk
      241 eprlktflsa lsgsraesgd shaq
//
LOCUS       WP_457659961             291 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659961
VERSION     WP_457659961.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..291
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32336
     Region          26..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mhsrpclttw lylsplhlll lamltvpsly vfwlslngss ygtgltwvgl enyravfddp
       61 yfwraalntf lvvngvvyve llfglalaal fvsgvpfrgv mfacilmpya isevvavlvw
      121 kmmmdpniga iartieelgl grvnwsasps tglvlvgvin iwthlpftfl miyaglltid
      181 gslyeaarid gasrwqrflr itlplliptl litlifrlif afrmfsevwl ltkggparls
      241 evlavylyqh gfrygdfgma aatgwlmvlg slllasvflf amqrgikgge r
//
LOCUS       WP_457659963             130 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Sinorhizobium medicae].
ACCESSION   WP_457659963
VERSION     WP_457659963.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..130
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=14466
     Region          31..114
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mglkslliia asiiaplavq pvvaqeangp viriaeleid paqmaaysaa vkeemeesir
       61 vepgvlalya vsikgqpnhl rffemyadqa ayefhresph frkyvettkd mitsrklfet
      121 dnfqlsakqr
//
LOCUS       WP_457659964             329 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Sinorhizobium medicae].
ACCESSION   WP_457659964
VERSION     WP_457659964.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..329
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36251
     Region          9..306
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(18..20,50,55,80,125..126,155..156,175,203..209,260,
                     277..282,285,288..289)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(50,55,80,125)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mqkrklgqgl evsalslgcm gygkardipd rpqmiellrr avdlgmdffd taevygpwtn
       61 eemvgeafag mrdkvkiatk fgwdidqstg ehrggvnskp tqirsavegs lkrlrtdfid
      121 llyqhrvdpd vpmedvagtv kdliaegkvr yfglseagae lirrahavqp vaalqseysl
      181 wtrepeaeii ptleelgigl vpfsplgkgf ltgkidasta faandfrsqi prfapearea
      241 nqalvdlirs vgerrsatpa qvalawlmaq kpwivplfgt rklerleenl galsvtlsdd
      301 dleqievgaa airiegaryp eemlrrsgr
//
LOCUS       WP_457659965             108 aa            linear   BCT 27-JAN-2026
DEFINITION  Csu type fimbrial protein [Sinorhizobium medicae].
ACCESSION   WP_457659965
VERSION     WP_457659965.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Pakharukova,N., Malmi,H., Tuittila,M., Dahlberg,T., Ghosal,D.,
            Chang,Y.W., Myint,S.L., Paavilainen,S., Knight,S.D., Lamminmaki,U.,
            Uhlin,B.E., Andersson,M., Jensen,G. and Zavialov,A.V.
  TITLE     Archaic chaperone-usher pili self-secrete into superelastic zigzag
            springs
  JOURNAL   Nature 609 (7926), 335-340 (2022)
   PUBMED   35853476
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Pakharukova,N., McKenna,S., Tuittila,M., Paavilainen,S., Malmi,H.,
            Xu,Y., Parilova,O., Matthews,S. and Zavialov,A.V.
  TITLE     Archaic and alternative chaperones preserve pilin folding energy by
            providing incomplete structural information
  JOURNAL   J Biol Chem 293 (44), 17070-17080 (2018)
   PUBMED   30228191
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..108
                     /product="Csu type fimbrial protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=10700
     Region          <2..108
                     /region_name="SCPU"
                     /note="Fimbrial subunit ScuA/B, ScuA/B/SCPU domain
                     [Extracellular structures]; COG5430"
                     /db_xref="CDD:444182"
ORIGIN      
        1 mssnidatgr atvtctpata ytvglsngms gtsptnrrmt lggaavvygl ykdagrsqpw
       61 gdgatpgstv agtgtgaakg ytvygrvppq ttptpgtysd tvvvtvty
//
LOCUS       WP_457659967             325 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457659967
VERSION     WP_457659967.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 325)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..325
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=35609
     Region          19..309
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 marefyeedl pllaikmadv rqggdnpdye irlfvdgqik hvrvvgriir hldgtmecig
       61 avqdvsaqri aelgrdklrs elsqlarvts lstmaasiah evnqplagii mnasaslrml
      121 canppnitga vetakrtird gnrasdvilr lrnlfkrgva tvewldlnda ireliglaas
      181 dlqrgrilli eelsdpppfv lgdrvqlqqv imnllrnsid amtdtaqtqk kifvrtvvgl
      241 gevrvvvedh gvglegtdve rlfdafhttk phgmgiglsv srsiieahkg kiwaeprpsg
      301 gaifgfalpf dkdsvdrpsp pemkt
//
LOCUS       WP_457659968             363 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659968
VERSION     WP_457659968.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..363
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40894
     Region          58..307
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mlieklgvng kvgvlvagst vssfpteedr illhvaacqa alaiteairf rhdtravaer
       61 elnriadaip vmawstlpdg radffnehfl tflgitseqa agwgwaasih pddsralqsv
      121 wmellasgmp getearlrrw dghyrwflfr anpvysdega vvrwygtntd iddrkrfeee
      181 mrrsaalmaq aqrltvtgsv wwrpatndiy wsdeayrvag qdvgitpsve mmldrchped
      241 lpriqklisn amnrgenvdv ehrllmtdga vkyvhvvlqn ignnpadpef igavaditer
      301 klaeeqlrrs dvllregqri sqtgtfswkv etdeitfsee lnrifgfesg rvvdfdaigq
      361 rvl
//
LOCUS       WP_457659970             601 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457659970
VERSION     WP_457659970.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 601)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..601
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66510
     Region          228..590
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msyqalsadg tlrwleaqvv qiriqngela gycvlqtdvq dsrdsshllg qemeilemva
       61 rgapsasvlq rlcdvvadlv pdlvcgflel sldrklfrmg aatrlagefr eifdgrsvis
      121 dknpcstaal tkrtveianm aesdqretsm geimlangln yckaipilsp ygntagilai
      181 lrhqqadlgp reqqivdrak hiaaisidrt rheealvrre tqveqsqaql vaaqrisstg
      241 sftsdiqrde niwseefyri fdldpkleps idavrervhp edldlfdfem krgfagedad
      301 fvfriirtdg tlrfirglar vthyigdhpv fmgtvqdite trraedalrr geealakare
      361 elayvsrvmt isalttsiah evsqplsgil ananacvrll aldppniasa tdtarrtird
      421 tmratevikr lramfsrqsp pmekidlnei arevialsar dmrekfivle arlapelppv
      481 tgdriqlqqv ilnmvlngie amaeteerpr rllvrtalvs ediltlsisd agvgiaaeaa
      541 dkmfepfftt krdgmgigls isrsivenhg grmwamsndg pgatfafslp slgkptdrsa
      601 t
//
LOCUS       WP_457659971             141 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457659971
VERSION     WP_457659971.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10062837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..141
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=15533
     Region          13..98
                     /region_name="PAS"
                     /note="PAS domain; PAS motifs appear in archaea,
                     eubacteria and eukarya. Probably the most surprising
                     identification of a PAS domain was that in EAG-like
                     K+-channels. PAS domains have been found to bind ligands,
                     and to act as sensors for light and oxygen in...; cd00130"
                     /db_xref="CDD:238075"
     Site            order(29,33,39,52..55,76,81)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(49,53,61,64,88,90)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
ORIGIN      
        1 mgpttakesl nslpglvwtt detgalcyan srfteftglm idqggsrqwa sylhpddhll
       61 vvpaqkggaq lfaarlrrrd gkfewfnlsa spmkgfgevc wlaterleri dnqfgnadrd
      121 frsflrfpvt pgastnafpg t
//
LOCUS       WP_457659972             336 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457659972
VERSION     WP_457659972.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  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   2  (residues 1 to 336)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36893
     Region          1..326
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msritlqdia dhtglskfav scslsgkpgv sdttrkrvqd aavqlgyqrl kpaeerreit
       61 lifhdqvdsv syelrtmlqd gmqreahrlg qpvrlqwthd anrveamvkd sagiilvgph
      121 eqktldilra sgvpvvrlgw vapleqadhv ggtdheagia vgeyliglgh rdiaflqgee
      181 gyrgrmeryh glresieqyp darlhnlhfk edggfipalq slqtmgiapt alfcahdgla
      241 ltavsellar gyripedmsv vgfgdfsaat qispqlttik vqglemgata lrllleriet
      301 qgntvparri liastfverr ssgpapkhgk sldrrk
//
LOCUS       WP_457659988             288 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659988
VERSION     WP_457659988.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31529
     Region          4..287
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 magmvafvrt vetgsfsaaa kslgltpsaa sksvsrlell lgaklfrrst rtlslthegd
       61 afyglvmplm rqiesatevv rpkhqasghl rvglpgdlgi qilkpvftef msehpaisfe
      121 isttdrhvdi lrekfdvvfr vgevqqnali srtiahldma lvaspifvaq wglvedvrrl
      181 qklpfarytm agrhypirfv ngteivpegr vdldsasair eavisgvgag hlvrrlvqed
      241 idqgriiell psmklqtvpl qaihvsgnmp phrltllvnf vagamrra
//
LOCUS       WP_457659977             720 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457659977
VERSION     WP_457659977.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 720)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..720
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77049
     Region          449..675
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 miknisfgff paaatahfwt spfalvillv lqraswaqst gdpppekvrq flelarnpev
       61 kawlgeklaa paaapsssia eaissweaav dgriaalaka fprvpaelan afavsvrdvn
      121 sgtpglvvgi lalllgvgfg tewltrralt rartpgergd agqtvlsdav alltfalasv
      181 gsflafewpp llrkvvltll lafiafrfvy tiarllvafg gagsgssyqp vpvaetdaag
      241 rfwlrrvsls agflligwav vslmpsfgfs idvarlasla fgfgilaiai etvwrrpgki
      301 tspvvrslls lylivlwlaw vaglfgllfi giyslvlpal trgvgrvaqv fanrvqltga
      361 lgvmlnsmiv rsaralviaa avawlayvwr fsaaalagse igiivingvl ntvvvllvad
      421 llwqsskali ayrmdlaeha ggtedqvars grlrtllpif rntlavfica vavlailsgl
      481 gvqiapliag agifgvaigf gsqtlvkdvl sgvfymldda frigeyiqsg sykgtvesfs
      541 lrsvrlrhhr gpiftvpfge lgavqnlsrd wvidkmtlnv tydtdvelar klikkvgqel
      601 aadpefaadt lqplkmqgvd sfgdfaivlr lklmtkpgtq faikrrafmm ikkafdengv
      661 kiavptvhve gsgepataah qleqvvkkap mtesaetcqp ykapqalkgp khietideaq
//
LOCUS       WP_457659989             291 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659989
VERSION     WP_457659989.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32414
     Region          5..277
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mklenwddlr lflhvaeqgg lagaaeragv saptigrrml aleraigral fvrartgyel
       61 apdghvller vkamyeaaqd ihnwqelvhs lpmvrllsds tlscftaasf nrlwspsdsf
      121 rvcfktseai ldltyreadi glaaerpetg nvaarrsvri ayapycaqgf dqqrnnnwvs
      181 lgtdvanqrw krwtfehrgq fitnwvnapr smfdlvkaga gvgvlpcfig drdpgflrag
      241 hvidelshhl wivlhddere resvravadr lsallaanap lfcgftgqdp l
//
LOCUS       WP_457659990             113 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457659990
VERSION     WP_457659990.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..113
                     /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=12727
     Region          6..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpsvserpvk rsirrnelre ivpladstiy emeqrgefpr rfglsprcvv wdlaeveacl
       61 esrrtrsipr akhpdvtqrk frpvkgqgra qalgmvgggg srvtgdlmrv klr
//
LOCUS       WP_457659991             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457659991
VERSION     WP_457659991.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35869
     Region          6..325
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtkplqktpa ltvdhlvktf dvsapwlnrv verkprqylq avndisftvp aggclsivge
       61 sgcgkstvar lvtglhrpts gamrfapgks gaalsaqmif qapyaslnpr wrvknivaep
      121 lremklrkta aevterveel lhtvglspsd gekfphefsg gqrqrisiar alasepeflv
      181 cdeptsaldv svqaqvlnlm rrlqdelglt ylfishdmsv vrqmsdriav mylgriveeg
      241 dteqlfaepr hpytqlllqt ipniaapnrn repasgevps plkppsgcaf hprcpvaigr
      301 cskevpevrv lpngtrvach lvedglak
//
LOCUS       WP_457659999             301 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457659999
VERSION     WP_457659999.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33691
     Region          6..297
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matvvmtsld srsraasrgl sdikicnlfi iptilflivf nifpliyslg ysftdfrass
       61 napanfvglq nyrellndpf iwanfaitak yvivsvtgqv vvgfgtamll nraipfkgli
      121 ttllllpmml smavvglfwk llydpsfgii nyalglgtfe wlanpdmaly avaitdiwmw
      181 spfvmllsla glsavprhly eaaaidragp fytffritlp lvapilmiai ifrtmeafkt
      241 fdlayiltsq pttevisirl ykmafqewqt grscalayiv limvlaitni yvkylnrvke
      301 r
//
LOCUS       WP_457660006             216 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660006
VERSION     WP_457660006.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..216
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=22692
     Region          6..147
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mlreafgafp tavtvitasd pagrpvgfta nsftsvsldp plllvcvakt ardypamtaa
       61 ehfainilse aqkdvsikfa rpledrfaav dwargpngcp ifeqvaawfe csmhdvieag
      121 dhvmmvgrvt afessglngl gyarggyftp ganssaagge igavavlerh galfplddqn
      181 lalpsysags gdpktlasql eqlglsvhdw fclldl
//
LOCUS       WP_457660007             421 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660007
VERSION     WP_457660007.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..421
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45360
     Region          1..344
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 milclafvvl sgcgghpkgv ltpvadsapt sskvdmlitt trgrsevpge mftgeraraa
       61 afanitvsip pvrkvgevaw pkklpsnpat dfatlkaddl trdgaktwln ttvnkspdrs
      121 vlvfihgfnn rfedsvyrfa qivhdsgiks apvlvtwpsr gsllaygydr estnytrnal
      181 eslfqylaad kevkevsila hsmgnwltle alrqmairnd glpakfknvm laapdvdvdv
      241 frsqiedmgs qhprftlfvs rddralafsr rvwgdiprlg sidpeadpyk qelanneitv
      301 idltkikagd gmhhgkfaes pevvrligar isegqpltds rmglgdhlia gttgaaaaag
      361 saaglilaap vavidphtrd nyanhfgaam gqldgkqkia vtdcasrpsa erdpacrvpq
      421 n
//
LOCUS       WP_457660016             118 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB N-terminal domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660016
VERSION     WP_457660016.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 706361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..118
                     /product="ParB N-terminal domain-containing protein"
                     /calculated_mol_wt=13619
     Region          5..73
                     /region_name="ParB_Srx_like_nuclease"
                     /note="ParB/Srx_like nuclease and putative transcriptional
                     regulators related to SbnI; cd16400"
                     /db_xref="CDD:319257"
     Site            order(15,50..53)
                     /site_type="other"
                     /note="Ca-Po4 binding site [chemical binding]"
                     /db_xref="CDD:319257"
     Site            order(19,21,50,53..54)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:319257"
ORIGIN      
        1 mryyllqpnd ltpteevdcr qvleleeeil qakfwktpia vhkgelfvmd ghhrlavakr
       61 lqlrilpaml ldyhgvrvea wrpgevvtpe iifamarsgr kfpakttkhv felsvprm
//
LOCUS       WP_457660019             372 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660019
VERSION     WP_457660019.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..372
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40338
     Region          3..372
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mgperskssg siindpqvrg ifyqaitiii ltaliywivd ntvdnlrran iasgydflrs
       61 ragfdvgqsl isftsdstyg rallvgflvg igrlshnwii aklslayvev frnippllvi
      121 ffwysgvlsi lpqardalal pfdiflsnrg vafprpvage gaeytllafi iaiaasvfft
      181 rytrqrqlat gerlpvlwtv lgliiglpli tflvtgapig fdvpvagkfn ltggsvvgpe
      241 fmslflalsf ytaafiaeiv ragirgvskg qteaahalgi rpslttrlvv vpqamriiip
      301 pltsqylnlt knsslavaig yadlvavggt ilnqtgqsie vvsiwlivyl slslatslfm
      361 nwynarmalv er
//
LOCUS       WP_457660025             765 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660025
VERSION     WP_457660025.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..765
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86445
     Region          17..>469
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mldstiewie sfgdgfltil gdfgggkttl lrrleyeyss lflekrtrhr plyftlkdys
       61 fydgldefia ssvrqkyqrn mpasvfwtla keagflflld gfdeiitgsd radraktfls
      121 lhrlitcgsp viltcrpayf vsneelndli rqvnsktgqk naglparwda hlfnigetnt
      181 lartnqflfd kynttldpll dlsstvanld vfrpaqidey lakfdedfqk vsnsswsdvk
      241 seiekiydlt dlmkrpimls mikdtilqgq idirrnnvig gafslydayt slnlkrdwgk
      301 skgrkllnek qrqeyaqlia ltmfkrasle vehseivqva kkltsalelp adlnqynpeq
      361 iaadiqvttf lsrqgssfrf thksfmeffv aksvvdrlnn hrlaksslae pypreiisfi
      421 geavsinpkl ltsalsafrs qtnaarksde srlikrnvlg illssseait tdylsdvhvw
      481 elsvrkrtmd glairgttwd ycgwhlvtls nssisqssft gwrveggnwl nssfngrlqd
      541 chfedlelsd cvtvastekt vfhtcrfvdg tltvrgefqi nsssfhnttl svevavgais
      601 rltacnfenc eiadlngpqn rpvmiercsf adcqfvgfsp sskfiersly eneifskklt
      661 vddektivvd rcagvllide lderikigkq gfksvgnlfl vaqsalqnkp ksraafikai
      721 hsrlekkype llaklkatyp aifmppngrh esekgvprrs pivqa
//
LOCUS       WP_457660030             596 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457660030
VERSION     WP_457660030.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 596)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..596
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=65024
     Region          1..446
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrlsklgirn frnfkfvdip lhgnivllge nrvgksnllf airlildpal pdaarqlrls
       61 dfwdgcpadf sqpievhldi adfagdpalv alltdfrvah dpsiarlsyv frkkaevtgp
      121 aqssedcefl vygggvetrt vpgkvrrria idvldalrda egqlatwrts pirhlleeav
      181 agisradlda vaaeldkatk sleafptika ledelragil hlsgkahdvd arlrfapsdp
      241 lrlfraiamf idggkrgiae aslgsanval lalklaefaw rrrknernfs llcieepeah
      301 lhpqlqrsvf kkllneasaa qtmvvtshsp tlaavsplrs iiqlrtrdra tqayslanlp
      361 vtpeelddle nyldatraem lfargvihve gdaeealvpv faaslgfnld dlgitvcnva
      421 gtnfgpyvkl tealgvpwsv itdwdpmdgs qppkpplgrk rvidlwqdil avrgkapmap
      481 etranweakp yaelvdaavr tgiylneqtf evsvantpgl laplldilse qgfgsirtkr
      541 iaswrsgtav dpaqllamva digkgrlssr lakksaglvp pkyiadaiqh vvsrvq
//
LOCUS       WP_457660031             593 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Sinorhizobium medicae].
ACCESSION   WP_457660031
VERSION     WP_457660031.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..593
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65670
     Region          17..572
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 msssdvllra ieelkanpeq skavletghc vvlagpgsgk tktlttamar tlsqdvvdpr
       61 gvacitynne caieletrla glgivpgdra figtvhsfal sqviapyarc isiglpaelk
      121 iatkaqaraa veaayesaid ggenphdrwg fasekrkrdv drtrpewvar npelvtfieh
      181 yerelrrqgl idfddmplla yrmikenawi reaiwarfpv lfvdeyqdlg halhelvlll
      241 cfgggirlfa vgdadqsiyt faganpalle sltqrpdvet iklrfnyrsg gklikaslga
      301 lgeerdyrev dgapegeisf waapmgldtq admiatsvip hlvskgiahg eiavlyraaw
      361 lgdkvadalk qagipfvrtd tnalvrrssr larfiedcar wvtggwhdae ppfsrllsqa
      421 talvfgshas eaeqdalsrq lilffessig spatthawlq rfdrelitsw ralarnteqe
      481 weicaemisg tdptkdldvp laqfagrads agrvtlstlh sakgrefdav imygvnngdf
      541 pnkrdlktea glrearrsfy vgvtrprkel clvfqehhhs pwvqelfnrs qrk
//
LOCUS       WP_457660051             358 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Streptomyces anulatus].
ACCESSION   WP_457660051
VERSION     WP_457660051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..358
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39140
     Region          92..357
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkirafehgm diqdaaehai nawysaenlp eaktdgaktw gtflpvgepd rfkaacsdrg
       61 vtyiqglaqa ltlwldnhps pssplvsqpv vrvivanqkg gvgktfissg maqalaeagh
      121 rvlivdydpq ghltaelgfe dvmyeddvet llmhmdgtak ghigellval dqerfgerlh
      181 llpasddafl rdvalskvsf seaalerale pleadydvii idgppslgln mdtalyyvrr
      241 rdgeladrsg vitpvwanka shrafrllqs qkedlcrkgr iqvdylglvv naydsrrgkl
      301 vkankdqwel stspavlavi gdlkegreaa dgeiplleya pdsehaqamr dlakelav
//
LOCUS       WP_457660015             318 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase domain-containing protein, partial [Sinorhizobium
            medicae].
ACCESSION   WP_457660015
VERSION     WP_457660015.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Schneider,A. and Marahiel,M.A.
  TITLE     Genetic evidence for a role of thioesterase domains, integrated in
            or associated with peptide synthetases, in non-ribosomal peptide
            biosynthesis in Bacillus subtilis
  JOURNAL   Arch Microbiol 169 (5), 404-410 (1998)
   PUBMED   9560421
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         <1..318
                     /product="thioesterase domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
     Region          <18..304
                     /region_name="EntF2"
                     /note="Thioesterase domain of type I polyketide synthase
                     or non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG3319"
                     /db_xref="CDD:442548"
ORIGIN      
        1 aqalalgmkv sasnifdapi lkdlapkiel dsshytpgvl pvrtigsqap vffvptgygd
       61 csyvfrlvre mdidcpvyal pwppfeearr aslediatkv ahavrkvqpr gpyrfagyss
      121 gavlayalae rllyleetvs fmafidvpip amspamtdte ialqmifepl eslgdeafev
      181 lrqsagqssv eqlfdkarqi gavvgrpdly ydalryaqfh qavhsyemps lpvsvhqfya
      241 lehspsrgar lpagpdansp mrgwdrilga efiqavpvpg dhvtmmavpe nrrvlarqls
      301 aalnnsptth pnrnldvk
//
LOCUS       WP_457660052             539 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660052
VERSION     WP_457660052.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..539
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=57949
     Region          467..511
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mglygsapea pdpqetasaq tatnigtava nnvmgnvnqv tpdgnltyty ttqkwkdpis
       61 gkeydlqvpt atqslsqqqq aiknqtdaae lnmatlannq sgklndllgk piniggapag
      121 gnagaiglpq yqqfgsgpql qtslgnygnv qssiagagni qkqvadsgqi qnqlgnagdi
      181 trsyetdfsa drqkvedalm qrlnpqmerd raaletrltn qglqpgseay nraideanrs
      241 stdarlgail sagqeqsrla glanqsatfq nsaqqqaynq llgsgqfans aqaqqyaqna
      301 nnmqmgnaaq qqqfgqnqaq qqanntaqqq kfsqglagaq fgndalqqqy hnqntatagn
      361 nalqdqsfns qqskfnmqnq qraqylnely aqrnqpinei iglmsgaqvn spsfvptqsn
      421 pmptvdyagl vqqdyankmg aynqqqagmq smfggmlgfg gqlaslsdkr akkdikkvge
      481 lkghglyeys yrgkhddgkk higvlaqeve kkrpdavsrr pdglrqvnyg alfnagrkr
//
LOCUS       WP_457660061             257 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660061
VERSION     WP_457660061.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28070
     Region          60..195
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maakpsgpqg drprrlrasp qsappqsapp qsaspesapp esgssksleg prtepslsld
       61 rivaaavell dtrgvdglkm rqladrlgag amslywhven kemvfdlald svlayrgppq
      121 kaksrdwrge vfhmledwra smlrhpwsas llprralgpn ilsrlellsn tlsragvada
      181 dlnaaiwslw nyvigatvtr asfvlsdedr svaqqrltgl gehyptiers rllldddwdg
      241 afrkgldfll dglaprs
//
LOCUS       WP_457660065             219 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660065
VERSION     WP_457660065.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..219
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22630
     Region          <3..217
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mppthllswl afagaltmsl aiyalswnsg ssslriilig iglsslagag anfistfgnp
       61 qavqramvwl sgsiynstwd kirtlatwlt igiagsalia remdllilgd etarargqpv
      121 eliravmfvl cavlsgaava aaglvafvgl iaphiaralv ghshglmlpv talaggllvv
      181 gadlaartlf tpaplpvglm tailgapffa ylmwrkkna
//
LOCUS       WP_457660067             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660067
VERSION     WP_457660067.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=39217
     Region          6..356
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 miinsikrrt llgaglagas vlampsvlra qdrslkvgvy ggyfkdsfdk nifpeftkas
       61 giaiesvaep tgeawlvqle qaaragqapa dvsmmsqvam lkgqatdlwt pidmakikng
      121 snlierfvnk ypdgriagig avswyitlvt ntdsykeapt sweafwdpan adklgllalv
      181 snsfllevta ktfmggtnal dteegilkaf eklaevkpnv rlwyrdeaqf eqalksgeip
      241 mgqyyhdvtg laaadghpvr stfpkeggiq dsgcwavsra sqkveeahif idymcqpavq
      301 atlsrkvgts ptikrestdl tdkefagvss diepivpryd lyqtksdwln qkwtelivg
//
LOCUS       WP_457660068             290 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660068
VERSION     WP_457660068.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..290
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31425
     Region          9..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matlhtrsaa rlmiapsvll llawmivpla mslyfsllry nllmpgmeef agltnytyfl
       61 tdpaffqaif ntlaivlgvl fitvvggtal allldqpmfg qgivrilvia pflimptvaa
      121 lvwknmfmnp vnglfawlak llglqpfdfl anapllsiil ivawqwlpfa tlilltalqs
      181 ldeeqkeaaq mdgagavsrf iylvlphlsr aitvviliqt ifllsvfaei lvttnggpgt
      241 qstnltflvy aqallqfdvg gasaggiiav ilanivaffl mrmigktlea
//
LOCUS       WP_457660069             310 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Sinorhizobium medicae].
ACCESSION   WP_457660069
VERSION     WP_457660069.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..310
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32843
     Region          4..269
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(29..30,33,88,101,103,133,167,256,259)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 magkmlsige cmvelmqaeg gmlrkgyagd sfntayyarl flpadwtvdy ftavgtdivs
       61 qelltfiest gvgtshirki egrmpglymi hlkdgersfs ywrsasaakl laddpdrlra
      121 aieavnvvff sgitlailsp laaetllael rrakaggrnv vfdpnirprl wddaarmrat
      181 ieagarsatm vmpsyddeat hfgdasveat ieryrslgae nvvvkdganr valsfagder
      241 vhvpasqvsa vvdttsagds fngsflarla sgdssaaaaa faarvaaavi ghhgaligrd
      301 klpagsaqfa
//
LOCUS       WP_457660074             171 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator substrate-binding protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660074
VERSION     WP_457660074.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10144261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..171
                     /product="LysR family transcriptional regulator
                     substrate-binding protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19861
     Region          <19..156
                     /region_name="PBP2_LTTR_substrate"
                     /note="The substrate binding domain of LysR-type
                     transcriptional regulators (LTTRs), a member of the type 2
                     periplasmic binding fold protein superfamily; cd05466"
                     /db_xref="CDD:176102"
ORIGIN      
        1 menwtwwylq pprdlsqfpe hfrftritti rsqmfvregh pilaqeriry edlanypwim
       61 yqqdpeiier vatllkdlgv nppriaieas slmavlellr sgdflaclaa pilgvvqdvg
      121 irpvpidrei wsfpagityh raieqstpfe llrqmltdev tklgldrteq r
//
LOCUS       WP_457660075             192 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660075
VERSION     WP_457660075.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   3  (residues 1 to 192)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..192
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21130
     Region          15..>183
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mlkflfcenr ygfvmdlfrh vgllrsflmv aregnvtaaa eklgisqpal trsirrlede
       61 tgfrlfdrht rgvtptiygk allrhaqlid tecrfassel ealrsghrgq ikigggpfwg
      121 aallpravar lhsllpklqv nlqigvnnvl hpklldgeld lvvsaapprs iaisgafply
      181 sdhdhtepdv cp
//
LOCUS       WP_457660077            1023 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660077
VERSION     WP_457660077.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1023
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=111647
     Region          13..1023
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlrdsrtktp rkapergqgs ggssvrgger rivtalcydl vgstdlmhvm diedyqelms
       61 afqfaskqei ashsgvmqhe agdggvalfp ieleardaas lairaglgiv eackrvgrea
      121 gqddlqvrvg iatsvalvre asregwaqep vtgaalamaa rlqaiaapss vlvceetrhl
      181 agrsysfvfe gskelkgftt pekvwralgh kvgidrfyaf grlggplinr enelntigri
      241 wdgvlagqgs vvliegdagi gksrllreir rrtrgrrskl lffqclpggf rstlhpllnn
      301 lpgsvsgggq mgptaaavaa lferngirda evvdifayll gaqgsrqpss kdpkairera
      361 hrallralea mcrsgpavva vedihwidpt sqdllgeaar iigqfpillv ttsrpasase
      421 wldiasptrl plrpldpdet rlaikakwpe hrldllpdlf daterisggv plfieeicqw
      481 vsqnvepdtm rlsesanpth vsafesilas rlqqlgtare varaaavagt qvtlpllral
      541 lpdfgksala naadtlcetg fltrirlpgr taygfrhtli qetiyksvlr kqrqvlhrrl
      601 fttvnqnrgi aawidtgala ehaeraglle eaaplfitag kesssrsami eakqflehal
      661 dlcgqlgesd taeplklsaf talgpiliga vglsseparr lyedaveiar qrplseqsqw
      721 fpiywgwwlt gsnfrvmhdr alevrsmlsk anepeiqlqv nhciwaidfn lgrhretqea
      781 ikaglalyde krakesrtef gghdakvcgl gqlalslwlt grtkasdaal srmiafadri
      841 ahahskahsl dteavsafyr ddfegltris lrmadfaqrh kmqslsglsn lfggwaeahr
      901 tsfasghalf qsglsqlrel gavadlpiyl cmhatllgla griepainvv neaigkgeet
      961 ghaywlaelh rcraillart gerkevvaad lrcaieiaes qgatallrra rkstrelgiv
     1021 irh
//
LOCUS       WP_457660079             232 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660079
VERSION     WP_457660079.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..232
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25636
     Region          88..221
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgemtmsqef pkisvgrrkf gkallllgfc liplaalaqt qiynsktkkw vnydkrkarq
       61 yfsrnnqvpe afrrqmvpfr taevpgtiii dgnqhflylv qpggqairyg igvgregfgw
      121 agivrvgrra ewptwtppae mvardpnaak waggmpggpd nplgaralyl yegdsdtiyr
      181 ihgtvepwti gldvssgcir mnndniidly srvdvgakvi vlmqgaalyk gv
//
LOCUS       WP_457660092             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660092
VERSION     WP_457660092.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77165
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcirc gceihehhre wmvkpengak wvakypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnkt
      361 idwevlrdra eehgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appimqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457660098             440 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457660098
VERSION     WP_457660098.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 440)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..440
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46466
     Region          2..435
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 madalkigia glgtvgaslv rilqdrhetl attcgraiei tavtardrsk drgvdlagit
       61 wfddavslas qggidvfvel mggtgdpaya svkaalthgv hvvtankall aahgielaei
      121 aekhgallny eaavaggipv ikalresmtg ntisrvygim ngtcnyiltk mekeglsfea
      181 clkeaqrlgy aeadpafdie gndtahklsi ltslafgtai aaddiylegi tnisiediqa
      241 aadlgyrikl lgvaqrtesg ieqrvhptmv phdtviaqvd gvtnavaies dilgellmvg
      301 pgaggdatas avlgdiadia ksrpgaqhvp afgrpanall pykrarmqsh eggyfirlkv
      361 vdrtgvfanv akqmadndis lefimqhskh yadpaepkti ilvthatfea svrkaivsik
      421 aegylvgepq virierpkaw
//
LOCUS       WP_457660108             405 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457660108
VERSION     WP_457660108.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..405
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=43988
     Region          18..397
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mgshtrnalt vksitaskav klrdggglwl vtkgggrywi fsytfagmrr emglgplhtv
       61 gladarekae earamvrrgl dpiaarkdeq adtpklttfg ayadafidaa vkagrwrgak
      121 tearwrnlle nhakpmraks lasirtkdvi avlnpiwgsk qetaeklrea iervldaakv
      181 eghragenpa awkgnleham hkpnqlaats hhaampyvel pafmktlsev ggvsaralel
      241 ailtacrsge argavwsevd lkakvwtiqp armksgklhr vplsdeavrl lkkmkeqsin
      301 dlvfpgirdk kplsdmslak alksagggay tvhgfrssfr dystevahap reiaeaalah
      361 avgdtversy arsdalerrr almqawadyl aspsaiaspt npsvs
//
LOCUS       WP_457660101             376 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457660101
VERSION     WP_457660101.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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 376)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40866
     Region          72..367
                     /region_name="RepA"
                     /note="RecA-family ATPase [Replication, recombination and
                     repair]; COG3598"
                     /db_xref="CDD:442817"
ORIGIN      
        1 makreppaep drvihdpqtg evrldynppq angatepkan gadnpksngk gktppppkii
       61 sgadlarlkf dpidyiipgy iapgmtllag kpkigkswlv ldwalavawg gvamgtveve
      121 qggvlylgle dnqrrlqarl kqlagdrsip dcihfgtewp rvdnhgadii raelkrikkp
      181 rlvvvdvigk lrprvhakdi yaadyaaiep lkrlvdertd laivachhvs kridaadpfd
      241 lvsgstgltg aadtvailsr dsngmrlygr grdieefdta vnfdatrgsf salgnsadvf
      301 rsdqrnailk ilaetpyals pkeiaavggl rddnvrkllg kmvaagevek ttrgqyrlcd
      361 rssdrtshng rwngyq
//
LOCUS       WP_457660120             137 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF3168 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660120
VERSION     WP_457660120.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10568396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..137
                     /product="DUF3168 domain-containing protein"
                     /calculated_mol_wt=14687
     Region          11..130
                     /region_name="DUF3168"
                     /note="Protein of unknown function (DUF3168); pfam11367"
                     /db_xref="CDD:431845"
ORIGIN      
        1 maspelelqg aivarlkadv glmalvngvy dqppdtafat pkesyvtige aqflrddatc
       61 vnggevyltl hawsrnvgyp vakqiadava vslhlapltl atnrlisimh rqtrvfrdtd
      121 gltshavidf vanvekp
//
LOCUS       WP_457660118             118 aa            linear   BCT 27-JAN-2026
DEFINITION  head-tail adaptor protein [Sinorhizobium medicae].
ACCESSION   WP_457660118
VERSION     WP_457660118.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Chaban,Y., Lurz,R., Brasiles,S., Cornilleau,C., Karreman,M.,
            Zinn-Justin,S., Tavares,P. and Orlova,E.V.
  TITLE     Structural rearrangements in the phage head-to-tail interface
            during assembly and infection
  JOURNAL   Proc Natl Acad Sci U S A 112 (22), 7009-7014 (2015)
   PUBMED   25991862
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Lhuillier,S., Gallopin,M., Gilquin,B., Brasiles,S., Lancelot,N.,
            Letellier,G., Gilles,M., Dethan,G., Orlova,E.V., Couprie,J.,
            Tavares,P. and Zinn-Justin,S.
  TITLE     Structure of bacteriophage SPP1 head-to-tail connection reveals
            mechanism for viral DNA gating
  JOURNAL   Proc Natl Acad Sci U S A 106 (21), 8507-8512 (2009)
   PUBMED   19433794
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009478
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..118
                     /product="head-tail adaptor protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098005 - viral head-tail joining
                     [Evidence IEA]"
                     /calculated_mol_wt=12892
     Region          6..118
                     /region_name="COG5614"
                     /note="Phage head-tail adaptor [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444345"
ORIGIN      
        1 mvrkasagrm hqrlhfqkrs ivddsygnev agpfetvftt aaeliplrgg epvqaarlvg
       61 vqpytvrirs caaarevtts wrivdarnas rvmnirtgtn pdqknawldl lvddgvat
//
LOCUS       WP_457660113             572 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Sinorhizobium medicae].
ACCESSION   WP_457660113
VERSION     WP_457660113.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..572
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64168
     Region          9..567
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mqydidaeky phvaagyrya ldvvggripa ceyvqqacqr qlddiarsis aegwlyyfdh
       61 daaervckft cflphikgpl agqnltlepw qsfilttafg wlrhdngkrr frraytevpr
      121 gngkttlsdg palycgfgek eggaevysaa rtrdqakvaf saaqamlrra talrtalgid
      181 veahriiqmr snsyfealsa dadsldgknv hfalidelha hrdrsvydai etgagkrnqs
      241 mvwaittaga dktgicyehr aytinilkgt aqddtyfgii ytidkdddwt deatwrkanp
      301 nygisvepeh iaalcrkams spasqanflt khlnvwiqtn ealydmrawd rcfdeeidie
      361 dfagepcria vdlaskvdia avvalfergd kvypfarfyv peqaiiesrn dsyrgweaeg
      421 kliatpgdvi didrieqdil emssrfhvle iaydpwqaqq manhlaeqga nvveyrqtvq
      481 nfseptkeld almrsgkiah pygprdplsw mignvvghyd akenvyprke rpenkidgai
      541 alimnlglhl rssggaqaps pwedpnfkia vv
//
LOCUS       WP_457660137             193 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660137
VERSION     WP_457660137.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..193
                     /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=21818
     Region          28..78
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mplrpmgrri gafgiagval gglpmndspr ligrkeaaey cgisptcfsm wvashkmppa
       61 ipgtrkwdkr aidakldeis gllslhaptt atvherntfd wwkarqaerd khrphhrldv
      121 reerilrfml ahpehttvdl ipragektle altkvgvvgp ggkdhrgfrt wfvtdegrae
      181 idrtdtwrnw kfe
//
LOCUS       WP_457660138             110 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660138
VERSION     WP_457660138.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..110
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12610
     Region          24..72
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mpaatvfpfl evhmpptvsl dkiyttdeaa erlrvarrtm iklgrdlgyc srigreyffs
       61 erdlldiwqa qramptssqg ravkvkglls dvrlqrslvs lsrkkqrwkl
//
LOCUS       WP_457660139              89 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Sinorhizobium medicae].
ACCESSION   WP_457660139
VERSION     WP_457660139.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..89
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10332
     Region          <13..71
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mdtraaryfk wllfwqqqgr ccycgehvvl tyrpydaarp yaatlehlqr radggtghps
       61 nlamsckhcn ntrgerdwls yasqrrsef
//
LOCUS       WP_457660150             177 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660150
VERSION     WP_457660150.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..177
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=19454
     Region          78..124
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mkpahrtefl tvpsspvntn tntptntnnp tntntnnptn tntnnptntn tntsmptntn
       61 tntntndnap epdaneasdr rlkrdiarla elanglgvyr frylwsdevf vgvmaqevle
      121 vmpeavvigs dgymrvnytk lgiemlsleq wtsrlvagvp ssralrmdhr slalasr
//
LOCUS       WP_457660156             336 aa            linear   BCT 27-JAN-2026
DEFINITION  heparan-alpha-glucosaminide N-acetyltransferase [Sinorhizobium
            medicae].
ACCESSION   WP_457660156
VERSION     WP_457660156.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10544557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="heparan-alpha-glucosaminide N-acetyltransferase"
                     /EC_number="2.3.1.78"
                     /GO_function="GO:0015019 - heparan-alpha-glucosaminide
                     N-acetyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0007041 - lysosomal transport [Evidence
                     IEA]"
                     /calculated_mol_wt=36202
     Region          23..247
                     /region_name="HGSNAT_cat"
                     /note="Heparan-alpha-glucosaminide N-acetyltransferase,
                     catalytic; pfam07786"
                     /db_xref="CDD:377915"
ORIGIN      
        1 msdssatttp eaqvpadatg akrialldal rglalvamav yhfvwdleff gyvaagtagt
       61 ggwrmfarli assflflagy slvlgqypkf rprafamrfa eiagaaalis vgtwfafrhs
      121 fiffgilhsi aaaslvgllf lrlpaatsfl aaaaafaapy ylrssyfdtp alwwvglset
      181 iprsndyvpl fpwlapflvg lgcakllhpv lsarrrsrgs atgnavlits lafagrhsll
      241 iylahqplll avvylfsiav papapdstei yrrnceqacg sensgiscsn fcgctldrlk
      301 eqdlfddlnl gkidvttder iariagqctm esrsvd
//
LOCUS       WP_457660158             291 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457660158
VERSION     WP_457660158.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..291
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31391
     Region          35..276
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mskdktgdks ardthyanlr rahrdgrrer geiptprqdk rgkpsadwkp palapdqvll
       61 yglhtvraal dnperriirl svtqnaaarl dlgnsaalpf pvetvtpqel drilgpdaih
      121 qgvmletrpl phrklealrd cplilvldqv tdphnvgaim rsavafdaga littmrhspt
      181 elgvlaksas galelipyiq isnladtide lhalgfmtig ldsegpqple gtfagdkial
      241 vlgsegkglr qktrqtvkal arldmpgaik slnvsnaaai amyaarhhlk g
//
LOCUS       WP_457660160             192 aa            linear   BCT 27-JAN-2026
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660160
VERSION     WP_457660160.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Parey,K., Brandt,U., Xie,H., Mills,D.J., Siegmund,K., Vonck,J.,
            Kuhlbrandt,W. and Zickermann,V.
  TITLE     Cryo-EM structure of respiratory complex I at work
  JOURNAL   Elife 7, 39213 (2018)
   PUBMED   30277212
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   5  (residues 1 to 192)
  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 10012723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..192
                     /product="NuoB/complex I 20 kDa subunit family protein"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=20906
     Region          27..186
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 melasgttlv apqpkgildp atgkpigsnd affgeinnel adkgflftst delitwartg
       61 slmwmtfgla ccavemmqms mprydaerfg faprasprqs dvmivagtlt nkmapalrkv
      121 ydqmpepryv ismgscangg gyyhysysvv rgcdrvvpvd iyvpgcppta eallygvlll
      181 qkkirrtgti er
//
LOCUS       WP_457660204             630 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660204
VERSION     WP_457660204.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Scheurwater,E., Reid,C.W. and Clarke,A.J.
  TITLE     Lytic transglycosylases: bacterial space-making autolysins
  JOURNAL   Int J Biochem Cell Biol 40 (4), 586-591 (2008)
   PUBMED   17468031
REFERENCE   2  (residues 1 to 630)
  AUTHORS   van Asselt,E.J., Thunnissen,A.M. and Dijkstra,B.W.
  TITLE     High resolution crystal structures of the Escherichia coli lytic
            transglycosylase Slt70 and its complex with a peptidoglycan
            fragment
  JOURNAL   J Mol Biol 291 (4), 877-898 (1999)
   PUBMED   10452894
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     'Holy' proteins. II: The soluble lytic transglycosylase
  JOURNAL   Curr Opin Struct Biol 4 (6), 810-813 (1994)
   PUBMED   7712284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12989934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..630
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /EC_number="4.2.2.n1"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008932 - lytic endotransglycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=69037
     Region          458..612
                     /region_name="Slt70-like"
                     /note="70kDa soluble lytic transglycosylase (Slt70) and
                     similar proteins; cd13401"
                     /db_xref="CDD:381604"
     Site            order(485,494,496,498,503..505,508,539,558..562,594)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381604"
ORIGIN      
        1 mprvadlksg ldalsdrqpa raiairdrmp agtldrhila waiavsgqkg ipsydiaaaq
       61 gelggwpglk slrahseral yrespppadv vaafgatrpe ttegaialar alvaqgrtss
      121 aatqlrafwl neildketet kilsefshll taedhrrrme mllyrarvdq aerfgtlgra
      181 qslfrawaav irdgsnaasl idavdpswrs qpaylfirie hlrkrqkyae aaelldqmpk
      241 ddtalvnpge wwveqrivsr glldsgdfrg ayriaanhaa rratdlvdae fhagwyalrg
      301 leeaetaarh frkildassr pisasrawyw lgraaeaggp gdareyfnna arysatfygq
      361 laaarlghsk ldmsypsptq edhirlegre avkaigrlea aghgwraesl yralaeelts
      421 pgelailaar aekagnhqls lqigkiafgr gievaalafp igvippsadi dgagkalaya
      481 iarqesafnp aaisvanarg llqllpgtak gvanryglay skdrltsdag ynatlgahyl
      541 geqidsfggs yiltfiayna gprrvpdwla rygdprgkpi devvdwieri pfeetrnyvq
      601 rvmenyqvyk srlgqetdiv sdlrigreap
//
LOCUS       WP_457660208            1153 aa            linear   BCT 27-JAN-2026
DEFINITION  chromosome segregation SMC family protein [Sinorhizobium medicae].
ACCESSION   WP_457660208
VERSION     WP_457660208.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1153)
  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 1153)
  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 1153)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1153
                     /product="chromosome segregation SMC family protein"
                     /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=127525
     Region          1..1152
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mkftklrllg fksfveptef iiergltgvv gpngcgksnl vealrwvmge nsyknmrasg
       61 mddvifsgsg nrparntaev glyldnsdrt apaafndsde iqvtrriere qgsvyringk
      121 earakdvqll fadastgars psmvgqgrig eliaakpqar rqlleeaagi sglhsrrhea
      181 elrlkaaetn leqlddvtsq lesqieslkr qsrqanrfkm lsaeirrhea ilfhirwiqa
      241 keaeaeatsq lnqvtalvae taqsqmeaak aqaitslklp elrqneakla aalqrlqiar
      301 aqleedagri lrrreelqrr laqlsediar eerlvadnag ilarldqeee elrdalaead
      361 drslearerl eeaneklaas egalarvtae raeaqaarnq ieralrdlse rqarlarqla
      421 dqarelddld grmaslpdpd ekreqvehae asmeeaeaav saveeslaea raaetatrpp
      481 vdqararlng ieteartirr mleaagastf pavveslkve rgfeaalgaa lgddldssle
      541 qaapahwrmp gddaddpalp sgvlplidfv qgpealrrtl rqiglvqsed eaeqllpflr
      601 agqrlvtrqg avwrwdghva gseapsaaal rlaqknrlfe legeaeaasg alskaeadla
      661 aagarirged erlrlsreaq rmrarqlaea rdalaiaera sgdlarrrav laetklqieg
      721 qaeeiaeqie vaneafadqp dpaeldrhls drtaevatdr aaaaearaah dglarenner
      781 hrrlmaiage retwgaraas aenhiatlre reaeaqeeve elleapdafd ekrralmnel
      841 qkaeasrrea adnlaeaesr qresdrqaat alselaeare krgraeerlv sarerrleie
      901 arilealsca phevmrltgl aanealpdmr svereverlk iererlgavn lradeeqkel
      961 serlaallke rddvieairr lrsaiqnlnr egrerliaaf dvvnvqfqrl fthlfgggta
     1021 elqliesddp leagleilar ppgkkpqtmt llsggeqalt amalifavfl tnpapicvld
     1081 evdaplddhn verycnlmde malstetrfv iithnpitma rmnrlfgvtm aeqgvsqlvs
     1141 vdlqtaermr eav
//
LOCUS       WP_457660209             797 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457660209
VERSION     WP_457660209.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 797)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..797
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=86971
     Region          86..769
                     /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 mtlgkralil ifpvvlagyl laafsvhvaq srsiraleha klsqrlehaa avfqnevrrs
       61 rgalnallsg nalrqyvaet drkyratafg vrlqeslksl lddpagylsf avlnarlete
      121 yyfenswdpf aeidqaqldl arqlangskl gdwtyvdatg erprivyslf vdpitfgrps
      181 psnrknallm qvavqpdrfl klqaalekey gadivlqpwp lavtddlsas vplgpslhat
      241 ltvsdthfna qmlrqkvlla lgalamslfs iwlivvlirr fitgpiatld anvmavmaae
      301 reeiakvgga geigrltgni relhrqsvqs lqlvqrsswt daltginnra rfnilaaqav
      361 retvasgdkc sllfididnf kfvndkhghd vgdellktla ariahdvgai tggrgqepai
      421 larlsgdefa vllrsqpgdg vvretcaail alfsdgfels gkrypvtasi gvavclddas
      481 svaelisnsd aamyqaksag knrsarfsra lndkrtrqrq iqdelrsldp dqqfhlvymp
      541 ivdaggkvng ceallrwysp vlgnvtpdef vpiaessglf tkidwwvvdk amsdcrqlka
      601 lfgpdtvlai nissaelhsk aisehlsdcl arhnleaqsi dieltetfav qisdqlrlrm
      661 delrskgfrl siddfgagyt svqqiigyaa dtikldrelv snlnasesla vlravialch
      721 akgmavvgeg vdtpeklaml kaagcdrfqg yliskplpla elaiwalsrv ahavekpads
      781 sfrpesktpe darkiag
//
LOCUS       WP_457660210             391 aa            linear   BCT 27-JAN-2026
DEFINITION  cell wall hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660210
VERSION     WP_457660210.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Bagyan,I. and Setlow,P.
  TITLE     Localization of the cortex lytic enzyme CwlJ in spores of Bacillus
            subtilis
  JOURNAL   J Bacteriol 184 (4), 1219-1224 (2002)
   PUBMED   11807087
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ishikawa,S., Yamane,K. and Sekiguchi,J.
  TITLE     Regulation and characterization of a newly deduced cell wall
            hydrolase gene (cwlJ) which affects germination of Bacillus
            subtilis spores
  JOURNAL   J Bacteriol 180 (6), 1375-1380 (1998)
   PUBMED   9515903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="cell wall hydrolase"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42923
     Region          254..386
                     /region_name="CwlJ"
                     /note="Cell wall hydrolase CwlJ, involved in spore
                     germination [Cell cycle control, cell division, chromosome
                     partitioning, Cell wall/membrane/envelope biogenesis];
                     COG3773"
                     /db_xref="CDD:442987"
ORIGIN      
        1 mrkgikfpgk frltfsrwra pamiglaifl gfpsaaaysd iatflsginr ggerwrtylt
       61 qspagslhev emvftdpvtt galdggagmt lpdggrvalt aeskhhgtpd edrvtrklkk
      121 krivavtpat ppkdfsagsi lertsslmvp sldgsekmif akpkikgkei viatafyrka
      181 ppkpepgisp mlaklvtndk pdilatayvr pepdyarksp fdsilrdden agrfipeiap
      241 ddhawaatal pptvfskeeq tclaegiyfe argesvkgqa avaqvilnrv rnptypktic
      301 gvvyqnkawr nrcqfsfacd mirdliysrg hwktakeial avtsgkvwls evgsathyha
      361 tyvkpawakt mkrvgkiglh ifyrtygggw s
//
LOCUS       WP_457660212             326 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660212
VERSION     WP_457660212.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34696
     Region          48..299
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(63,150,152,154..155,182,231,252,255,268,270,299)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mafqlkrrtl fsagagalaa psllaglaga qetmekdgma kgvdfktlkl gsfkvtvisd
       61 gtrasdnphe ifgtnqpaes vatlleqnfl ptngfvngfa pvlvdtgsev vlfdtglgeg
      121 greagmgkla eglktagyap dqvtvvvlth mhgdhigglt eggkpafana ryvtgqveyd
      181 fwkdaarvgt aaenghkavl akvvplaeki tfiadggevv pgisamaafg hspghmiyrl
      241 efdgramilt adtanhyvls lqrpdwevrf dmdksgasas rkmvfdmiat drlpfigyhm
      301 pfpavgfaer qdqgyrfvpa syqfdi
//
LOCUS       WP_457660216             608 aa            linear   BCT 27-JAN-2026
DEFINITION  AsmA family protein [Sinorhizobium medicae].
ACCESSION   WP_457660216
VERSION     WP_457660216.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Prieto,A.I., Hernandez,S.B., Cota,I., Pucciarelli,M.G., Orlov,Y.,
            Ramos-Morales,F., Garcia-del Portillo,F. and Casadesus,J.
  TITLE     Roles of the outer membrane protein AsmA of Salmonella enterica in
            the control of marRAB expression and invasion of epithelial cells
  JOURNAL   J Bacteriol 191 (11), 3615-3622 (2009)
   PUBMED   19346309
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Deng,M. and Misra,R.
  TITLE     Examination of AsmA and its effect on the assembly of Escherichia
            coli outer membrane proteins
  JOURNAL   Mol Microbiol 21 (3), 605-612 (1996)
   PUBMED   8866482
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Misra,R. and Miao,Y.
  TITLE     Molecular analysis of asmA, a locus identified as the suppressor of
            OmpF assembly mutants of Escherichia coli K-12
  JOURNAL   Mol Microbiol 16 (4), 779-788 (1995)
   PUBMED   7476172
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..608
                     /product="AsmA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=64014
     Region          45..505
                     /region_name="AsmA"
                     /note="Uncharacterized conserved protein AsmA involved in
                     outer membrane biogenesis [Cell wall/membrane/envelope
                     biogenesis]; COG2982"
                     /db_xref="CDD:442221"
ORIGIN      
        1 mtrkmlhilr dsglrsrlrp rhlvwsaaig valaaaynaa lpllvsttea raamermldd
       61 wsggkstisg epevrfwpep lltlpmativ tsgpeqrpla eigritasfs vlsalrgeqa
      121 leevtlvepv itlergadgt vnwqkprwlv ppdttipqde apvgditien grvriidrma
      181 angggidiag isgtlkwpsf ggrlstqfsa tiggeqigwa fvceeplalf agrnaalkts
      241 ltsapltfsf egtgnlppql fasghlqmsa pslarlaawy rnvpdaglpa ggfsidtkvd
      301 tsetalkled lqlaiggdaa tgvldvqlgs gkrprvegtl afdridlngl plaalkpaqe
      361 ddrvsqmvqa vvggwrldvr lssqevlagp lhltdvaagv midgrrvsld igdstyangr
      421 lsgravlsek gleqggklqa slknadfaav ldrfglkgpl ptgrgvlsid latgrplwet
      481 gitdvfgrld ysltdgslag fdvraftdlv rkgeffslsq asdgtldfrt adieasfggg
      541 tarldraaft gpagtisvtg vvpyrsgsla lagtlaspad ddeplqffig gswpnavisp
      601 lsvllgpn
//
LOCUS       WP_457660220              97 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660220
VERSION     WP_457660220.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..97
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10197
     Region          11..86
                     /region_name="STAS_2"
                     /note="STAS domain; pfam13466"
                     /db_xref="CDD:433231"
ORIGIN      
        1 masrntagkt lklapvldln eatvlherll alkgeavtid asgverlgal cvqvlmaaak
       61 sweedrlsft faeasdafvk ttqligaeig plmakei
//
LOCUS       WP_457660225             152 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Sinorhizobium medicae].
ACCESSION   WP_457660225
VERSION     WP_457660225.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..152
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=15610
     Region          1..145
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit G (CoxG);
                     cd05018"
                     /db_xref="CDD:176853"
     Site            order(3,5,7,16..18,20..21,26,30,36,42,44,46,48,50,55,59,
                     63..65,68,74,76,78,90..92,94,96,105,107,109,111,125..129,
                     131..133,135..137,140)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mnmsgeeria agreavwrgl ndadilkrci pgcqslelis ptelaavvki kigpvsasft
       61 gmvvlsnlnp pasytisgeg kggiagfakg gadvtlvdeg aetvlrydvk aeiggklaql
      121 gsrlvnstar klaqqffadf nlavsgeaqa as
//
LOCUS       WP_457660226             601 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660226
VERSION     WP_457660226.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..601
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65024
     Region          541..596
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mlvalsacna saadnivvkq ataegaafaf vsvngniiai plsirlspts etpfilqkql
       61 sqfgtrfvls gnltfsldtd sakllsaakk lelspedisa aadlqyktyi gqwdgdtekh
      121 lkiqvdggii sagssmvvsf sktfddgeql tgflrntnal lllmelrtgf qvrliqankd
      181 ideivakyfr ehtvppimpi tsvfvsikee ypeqveknpl yalnaisdvv srlelkvned
      241 gnvvyevpdd itmmgspets srimdgavts lnldicgnpd rlllidlgkt gcdsvkdllg
      301 gavimwkfya viafllsamt tgaqvvspsp gpadelvyfd apvgfptfrd vtvyhawgdp
      361 kvffllpngi qsdggftlhy krangrings ltltmkpime gedvkeitsy lqntvsgakf
      421 thsepvasew eilgagfrrt vsplyssnpl lhsssvsmdi psdlteillk ggssyataiv
      481 vrykfavrgi eldssasprv ttrwftrgvs fpggcsvtpe ryvdiatgrv gcishitfna
      541 divreiqtll nevdqaslsv dgvagsktrl airrfqsrss mpqdgqvssi llhklrdaak
      601 g
//
LOCUS       WP_457660236             155 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Sinorhizobium medicae].
ACCESSION   WP_457660236
VERSION     WP_457660236.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..155
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17426
     Region          11..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mafnrmesat ylasllargf sralqergqk lgfapgqfpv llelwseegl tqrqlldrld
       61 ieqatmantl armerdglii rrkhpndkrs qqifltdrar kmetaakeaa aaaeqsllsg
      121 fhrfekelml eymrmalans arqggdfltr gppai
//
LOCUS       WP_457660240             281 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660240
VERSION     WP_457660240.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..281
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30024
     Region          1..272
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mrrliaqlah dwelllgvvl fglivllavf ggwlwredpl rvdilnsllp pdlahpmgtd
       61 dvgrdvlarf irgaqvsmgv aisvtiagtl vggtlgllag liggwfdvvv srimdailaf
      121 pplilamava iglgqgivsa gigvilaaip wyfrllrsev lrlrtlmyve saqalgassf
      181 rlirlhilpq ttstifiqas svfgfsiltl aalgfvglgi qpptpewgtm iteglayalt
      241 gqwwlgffpg lgifilavsa nliadrlrdi ydpksgarls i
//
LOCUS       WP_457660241             264 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Sinorhizobium medicae].
ACCESSION   WP_457660241
VERSION     WP_457660241.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..264
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28595
     Region          7..259
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mfgpknriit ianqkggvgk tttainlata laaigekvli vdldpqgnas tglgiqrrar
       61 hlssyelmmg thsiaeiaqd tavpnlsivp stmdllgvem eiakeldrvf rlrkalgsae
      121 alaysyilvd cppsfnlltm namaaahsvl vplqceffal eglsqlletv dqvrrtvnpa
      181 ldiqgivltm fdsrnnlaqq vvsdvrlhlg dkvyhtlipr nvrvseapsy gkpailydlk
      241 cagsqaylql aseviqrerq rkaa
//
LOCUS       WP_457660242             296 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Sinorhizobium medicae].
ACCESSION   WP_457660242
VERSION     WP_457660242.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..296
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32723
     Region          39..294
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnddsskrrl grglaalige mdqplqtgsa pvspvsadrr ipiefisrnp rnprrqfdea
       61 elqdlassir qhgivqpvvv rtigsdryei iagerrwraa qlagfteipv ivrdvddrta
      121 leiaivenvq rsdlnpleea lgyeqliaeh gytqndlgdi igksrshvan slrllklpep
      181 vrdmlsdgsl sagharalip tsdpvalara vvakglsvre verlaqndir sqndpnyaka
      241 rqrdekdadt lalertlsds lglevtvnhk asgghlkity ktldqleeic rllerr
//
LOCUS       WP_457660244             629 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457660244
VERSION     WP_457660244.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..629
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67310
     Region          20..615
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(33..34,37..38,41,79,137..138,140..142,145,165,
                     168..169,172,258,261..262,265..267,270,298,302,541..542,
                     546,550,566,569..570,573..574,577)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 manvvtaggt kagpmtgeek kvifasslgt vfewydfyly gslavyigat ffsqypettr
       61 nifallafaa gflvrpfgal vfgrlgdlvg rkytflvtil imglstflvg vlpgaasigi
      121 aapiilialr llqglalgge yggaatyvae haphgrrgyf tswiqttatl glflslvvil
      181 lvqymlgkea faewgwripf llsfvllgvs vwirlkmnes pafkkmkeeg kgskapltea
      241 fghwrnakia llalfgavvg qavvwysgqf yalfflqsil kvdgqsanlm vaaslllgtg
      301 ffvffgwlsd kigrkpiima glllamltyf plfkaltwag npalaeaqqs vratvtaapg
      361 dckfqfnptg takfttscdi atafltrnsv pydvvtsaaa gtpatvkige ttitsydaia
      421 agdkakaeea afgkqinmal qssgyplvrg aakvpeskld afvaanpela ldaaavrage
      481 ktmvpadklv adklltqeev gsatemavys idkggaftmv adparvnwtv iiavltvlvi
      541 yvtmvygpia allvelfptr irytgmslpy higngwfggl lpatafamsa tkgdiyyglw
      601 ypivfagitl vigllflpet kdrdihtme
//
LOCUS       WP_457660246             185 aa            linear   BCT 27-JAN-2026
DEFINITION  SixA phosphatase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660246
VERSION     WP_457660246.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..185
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20012
     Region          12..174
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mpddarpaar rllllrhaks awpddvhdhc rplsqrgrka apalgafmar qgfapdlalv
       61 starraqetw efvagafpqr itardtadiy evdapaifgv irkvepsvet lllvghnpgm
      121 adlalllagr gdeagleqlr ekfptaglav idfeagswse largtgrlvr fvtprllkqe
      181 qsgla
//
LOCUS       WP_457660247             702 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660247
VERSION     WP_457660247.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..702
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74612
     Region          382..668
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msnalpirig flllavapil fwmllgvswa qqapvgvppe kaqqflglls dpevrtwleg
       61 kipsaaaepp aaspadtiss weaairdrig gllgavprip eelasgaavv srdvnsgrpg
      121 lvvsilavli aaglgaewli rrvfararks gtkeeagqei lsevaalltf alasigsflv
      181 fewppllrki iltllvaliv fravraiskf lfavsgsngi adqpmsalas daaprfwlwr
      241 islvagfllf gwaivslmpe lgfsievvrl taflvglgil atavevvwrr pdkpaslvvk
      301 slltlylvvl wsawvmgllg vlwlgiysll lpalvrgvgd vaqalatraq rtgapgivlg
      361 vlivrgaraa viaaavawla yiwriraaal agsepgaivi pgllngiial lvadllwqms
      421 kaliayrmgl gpkdgsnade larsgrlrtl lpifrnvlav figavtvlti lsglgvqiap
      481 liagagifgv aigfgsqtlv kdvlsgvfym lddafrvgey iqsgsykgtv esfslrsvrl
      541 rhhrgpiftv pfgelgavqn msrdwvidkm tlnvtydadv dlarklikkv gqelaadpef
      601 aadtieplkm qgvdsfgdfa ivlrmklmtk pgaqftmkrr afmmikkafd engiriavpt
      661 vhvsggsdna aaaqqalnms kaaelaakap vaplkrkngg ls
//
LOCUS       WP_457660249             469 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease/ATP-binding protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660249
VERSION     WP_457660249.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Holland,K.A. and Holland,I.B.
  TITLE     Adventures with ABC-proteins: highly conserved ATP-dependent
            transporters
  JOURNAL   Acta Microbiol Immunol Hung 52 (3-4), 309-322 (2005)
   PUBMED   16400872
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..469
                     /product="amino acid ABC transporter permease/ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50596
     Region          6..221
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
     Region          228..466
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnlintffnv kvlldslpql lwglavtlqi gitsilcgla gglflavarl ysppfcqfli
       61 rtyvdvfrsi pllvllivvy yalpfvgirl spflsavtsl slvsaaytae ifragieaip
      121 hgqfeasaal glsnrhtmvd vilpqavriv ippltnncin vlkdtalasv vampdllkqa
      181 tqaqalaanp tpligaaiiy vmllwpmviv vgrletifsr getmmaalis irglkkafgr
      241 fmvlhgidld iaegevvcvi gpsgsgkstl ircinhlegf ekessvtvdg vrveqgaala
      301 kvraevgmvf qsfnlfphmt vlrnvmlapm rvrgtppaea krkaldllar vgiseqadkf
      361 psqlsggqqq rvaiaralam epkvllfdep tsaldpemvg evldamrkla gtgvtmivvt
      421 hemgfarqva drvifmdggr iveagtpsdi fdspreertr gflravlnh
//
LOCUS       WP_457660253             411 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457660253
VERSION     WP_457660253.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45664
     Region          65..408
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msvrkrtwtt pkgveksawv vdyfdmagkr rlktftkkkd adafaatakv evregvhvad
       61 sasatieeag klwlasaraa gleratiedy erhlrmhivp higasklpsl siakirsfed
      121 qlreagrsaa mikkvlvslg slladaqerg lvarnvvrdm kgrrgngekr qekrqkgrlk
      181 vgvdiptree vkalvgiltg rwrpliltat fcglraselr glrwqdvdle krevrvhqra
      241 drfndigrpk sisgertvpa ppmvinalre wklscpkkds gktdasgeki mvldlvfpng
      301 tgkveqlnni lrrglhpawv aagvavdsge vdedgkpvla pkytgmhalr hfyaswcinr
      361 rkdgglelpp kvvqerlghs simmtmdvyg hlfprsddad emaeaerafl a
//
LOCUS       WP_457660259             530 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660259
VERSION     WP_457660259.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..530
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=56728
     Region          463..506
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mglygsapea pdpqetasaq tatnigtsva nnvmgnvnqv tpdgnltyty ttqkwkdpls
       61 gkeydlqvpt atqslsqqqq aiknqtdaae lnmatlannq sgklndllgk piniggapag
      121 gnaaavglpq yqqfgsgpkl qtslgnygnv qssiagagni qkqvadsgqi qnqlgnagdi
      181 trsyetdfsa drqkvedalm qrlnpqmerd raaletrltn qglqpgseay nraideanrs
      241 stdarlgail sagqeqsrla glanqsatfq nsaqqqaynq llgsgqfans aqaqqyaqna
      301 nnmqmgnaaq qqqfgqnqaq qqannaaqqq kfgqglagaq fgndalqqqy qnqntatagn
      361 nalqdqsfns qqskfnmqnq qraqylnely aqrnqpinei iglmsgaqvn spsfvptqsn
      421 pmptvdyagl vqqdyankmg ayqqnqagig slmgglagmf tlsdktakkd ikkvgglyey
      481 rykgegknap krigvmaqev ekvrpdavrk gadgfrrvny galfdagrkk
//
LOCUS       WP_457660269              48 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660269
VERSION     WP_457660269.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 48)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 48)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 48)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..48
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..48
                     /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=5489
     Region          <1..41
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mgsstiyrrm kagkfpkpkr lseacvrwre seiekwmsel pttgsmnk
//
LOCUS       WP_457660271             130 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660271
VERSION     WP_457660271.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..130
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14520
     Region          37..91
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mtrraiisne ttkqreregg taatkgdqrl sqttdrlltp eqaaeflavs trqlrdlada
       61 ghlafvnigl gerptrrylp adiaafiesr rvapelreqa ratiksstaf kiadfaalrd
      121 elrqkrrskr
//
LOCUS       WP_457660274              82 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660274
VERSION     WP_457660274.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..82
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8476
     Region          5..>37
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mlttgnqlka aralagleqk dvaekagvnv ntirnmeaag agqiagraqn vqnvqrvleq
       61 egivflnhgq pgvrlvkaqs tg
//
LOCUS       WP_457660275             177 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457660275
VERSION     WP_457660275.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..177
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19273
     Region          50..166
                     /region_name="VapC"
                     /note="VapC family ribonuclease, contains PIN domain
                     [Defense mechanisms]; COG3742"
                     /db_xref="CDD:442956"
ORIGIN      
        1 mnaltamiaa rsrsengmkq sgtrpkslas lndrrgfiry hcdhvrwrge asaciaalqk
       61 srsrlisavn dvetgtvmag rvrsgdrcea iadldafltv fridiapvdd rtaraamkar
      121 idygqgfgtr gglnfgdcfa yalekqrsap llyagndfgm tdinpalkap slrrtkr
//
LOCUS       WP_457660278             297 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660278
VERSION     WP_457660278.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33137
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtltriraf idvvdaegfs aaarrigksk allskyvrel edelgallln rttrqfslte
       61 aghtyyrsas eilkeidnla dlvrasnsdl kgklritvpr tfvdadigqs lidfgkehpe
      121 lsleivsddr fvdlveesfd vairitrled stliarkldd fqvlvcaspd fisradplih
      181 pselsklpci ldtngrsyss wrfvekdgsp ftvsvsgqie vnsplgaara avtgigvavl
      241 pdfiarpkia sgelvtlfdd flpkdrgiya iyphrrylpt kvrtfvdflh nwfrstr
//
LOCUS       WP_457660279              88 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Sinorhizobium medicae].
ACCESSION   WP_457660279
VERSION     WP_457660279.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 88)
  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 88)
  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 11434433
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..88
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=9665
     Region          <6..88
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          28..57
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 msklgkegnl eaaaalgefy frqehpltyk lsfewnewaa rrgdagsqgr latiyheglg
       61 vernpqrafa fwllaakqgh sgaramlg
//
LOCUS       WP_457660290             202 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease H family protein [Sinorhizobium medicae].
ACCESSION   WP_457660290
VERSION     WP_457660290.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 202)
  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 202)
  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 202)
  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 202)
  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..202
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..202
                     /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=21744
     Region          32..172
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(36..39,70..72,75,98,156)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 mnsyrkffkr pagrpakkhq pldvalfskg thvfcdgace pnpgaggwaf avyqdgiett
       61 caaggevett nnimeltgml ravewaaakg atvtiwcdsq yvvngcndwr kkwkangwrr
      121 ggpnakpens kvmnlelwke idaalesaga lvtiawvkgh ngtagnerad elsligrqqa
      181 ieasadsrge dldaqfrgim ag
//
LOCUS       WP_457660292             224 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457660292
VERSION     WP_457660292.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..224
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25123
     Region          75..161
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mkspsqiads esdqhtaevp yrvqfyenwr hspasclvpq aiseieekgf agregpalpi
       61 lkspcvaaig kdgkamglli yhlggsrwyi tlsytapehr rkhihtalfe alrdeglqqg
      121 nivsidcrth vnnlaaqaaf eaqgrtkefi eytfrlkdev vtaeemrmmp eylvepfdtg
      181 pdglksmqaf inektaegye lhqviersty qwvlffkleg gagk
//
LOCUS       WP_457660294             165 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660294
VERSION     WP_457660294.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18201
     Region          23..158
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mhrhfvcnnr hfagafnsgr rrrkidavdr tilsilsrea ripmkslagr iglsrsatae
       61 rvarlekagv irgyradigq leegqieafl lvtlqrtpsl gvldrlagfs svrrvssvsg
      121 qldlivevev asinalnelr nevaqldnve dlstsivlrr dierg
//
LOCUS       WP_457660302             542 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660302
VERSION     WP_457660302.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..542
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57986
     Region          22..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdqnkpdlkr henpalthhe vsddfdfivc gagssgsvia arlaqcgsar vllleaggdd
       61 vaesvrdpaq wplnlgtsrd wgfvgepape lygrrlplsm gkglgggssi nvmvwarghm
      121 edwnyfaaea gdeawgyesv lgyyrriedw rgtpdtvrrg aggpvyvaqp rspqpiaeal
      181 lnaasaigip vfdtpngelm esgggasiae lrirdgkres vfgsyvrplm srpnltvltd
      241 alvtriifdg iratgvdvlv ngqrcaftar cetvlslgai ntpkvlmqsg igprdelkah
      301 gisvvqhlpg vgrnhqdhla fgctwayrkp egiggggcea klywksdsrl sqpdilqcql
      361 efavpspvet gletpahgwt mfsglaqpks rgrlrlsgpn tndpiliepn slsepedvaa
      421 alaavelcre lgnsdaftpl vaceavpgtr dragmidfir ksavtywhqs ctakmgrdsm
      481 svvnnelkvy gveslriada simprittgn tmapcvvige ragdlirkth gladssgvap
      541 fa
//
LOCUS       WP_457660301             408 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660301
VERSION     WP_457660301.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..408
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43562
     Region          7..406
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 meqvsgrlvv vgggqaafal vaklralkdm rpitvvaaea slpyqrppls kkyllremtl
       61 drllyrpetw yaeheidirl sttvtrvdra trqvvlsdgs tlgyetlafa tgatprrlpa
      121 avggdlagvy vvrdfrdadl laeemqpgrr vlvvgggyig leaaavaris glevtviema
      181 drilqrvasa atsaivreih sahgvhireg tglhrlighn grvtaaelsd gsvipvdivi
      241 vgigvtandd lahdagieta ngivvdshgr tsdpavfamg dcavlpwdgm rirlesvqna
      301 gdqaeavaav lagssvpyap kpwfwsdqyd vklqiagfgl ghdetlvrpg qregsvsvwy
      361 frqgkliavd aindakayvt gkklleqgvt pnralladpq vdlktlla
//
LOCUS       WP_457660307             533 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660307
VERSION     WP_457660307.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..533
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=58695
     Region          1..398
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkraaiyary stdlqndqsv edqfrlcrah aerlgfnvve efsdraksga smfgrpglan
       61 liqaaeraef dvlvseapdr isrdiadlah ihktlkfrgi emncvnggam dtvqigmygv
      121 igqmqreega kkvrrgmagv vrsgrnpggk aygyrpifgr kgeleivede aatvrriyel
      181 yaggmaprsi aailneenvp aprgerwnas tingsgqrgn gilrnpiyag rivwnriqmv
      241 kdpstgrris rvnpesehee vaaphlqivd sglfeivqhr keatggadra kgprskrils
      301 gllrcgacgg gmalvgpdrs gnriqcstfr esgtcnnsrr yyverietev vdglrrqfad
      361 tsiieayvea yqveqkrlrg daqrarasaq ralqeakdgi tkivekiskg liedeeaaal
      421 laplraerdr qkailgttee ppnvieiqpk avkrfrenie slaqivrekd geaspeiaap
      481 frqlvaavvi nptekgqpye inikgylssl idselsvikm vaeegfeppt qgl
//
LOCUS       WP_457660311             391 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660311
VERSION     WP_457660311.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42263
     Region          2..391
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mrperskssg siindpqvrg ifyqaitiii laaliywivd ntvdnlrras iasgydfvrs
       61 ragfdvgqsl isftsdstyg rallvgfint llvaitgiit atiigflvgi grlshnwiia
      121 klslayvevf rnippllvif fwysgvlsil pqardalalp fdiflsnrgv afprpvageg
      181 aeytllafii aiaasvfftr yarqrqlatg erlpvlwtvl gliiglplit flvtgapigf
      241 dvpvagkfnl tggsvvgpef mslflalsfy taafiaeivr agirgvskgq teaahalgir
      301 pslttrlvvv pqamriiipp ltsqylnltk nsslavaigy adlvavggti lnqtgqsiev
      361 vsiwlivyls lslatslfmn wynarmalve r
//
LOCUS       WP_457660317             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660317
VERSION     WP_457660317.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27107
     Region          13..195
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 myshheaklg wgsslgdkay kalkyivvnc happgtrlda taistvlnms atpvrdaliq
       61 leieeyiarf pgsgyytrkl dpkrlsdefg vtrtilqeai rgkldelhrr lpilqttprw
      121 ndyelarefl evfykqitea lnnermlyyv hesnirtryv rwldvqrpgr lscirddmse
      181 llelldkrdk ngaianvdrq fsaiintvpd lvlqgndrag nmkeswlgtl ssfaves
//
LOCUS       WP_457660320             402 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660320
VERSION     WP_457660320.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..402
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44445
     Region          33..144
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(51,54)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mshklpstsa pvlqmdslap elkvrdwirg eplasfqpgk lyilefcvtw ceacegamln
       61 lielqetykd sgvevvtvaa hesaasagea qahldawlaq fkklnfrvgl ddtgtmdtlw
      121 mqpsfsveip qafvidrdgy iafighpddl pdvlpqvlgg twrtsaqana aereriaene
      181 pkaakealkk qikdkiaaae eiedwktara aieegvaldp nslffrhahv hlllhnmhdi
      241 qtglpmlckf vrdaintnye ymlqlafgll fdpaydyskf psverfamgk elsehilaqs
      301 rlnddydkvc syemvaayyn asgnkdraie llevalklld gpdpdmdglk egflphllqt
      361 lanykgetvc sgdvcvapee iapdgvtpma eqenpadrga le
//
LOCUS       WP_457660324              79 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660324
VERSION     WP_457660324.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..79
                     /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=8676
     Region          <4..73
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mecldlsadv prltarqkec lswvlkgkss wdigiilgit sntvdfhikg amkrlgavnr
       61 mvaakkaeql gliephwlf
//
LOCUS       WP_457660329             577 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Sinorhizobium medicae].
ACCESSION   WP_457660329
VERSION     WP_457660329.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..577
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=60344
     Region          29..566
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mkvstdrqse apgfaelytp kfltilregy glphlradai agltvaival plsmaiaias
       61 gatpaqglys aivggffvsl fggsrfqigg pagafivlva atvaqhgmdg lilatflsgl
      121 mltavgllrf gtfikfipfp vtvgftagia viifasqikd lfgltldhep gellqkfpvl
      181 wgakdsvasg avgisittia vilglrrwrp rwpgmliava lsstatalla lpvetigtkf
      241 ggipsalpfp qlpdlsmdri vavlpaalsf tllgsiesll savvadgmtg rrhrsncelv
      301 aqgaanigas lfggfcvtgt iartatnira gahgpvagml hsafllifmv iaaplaayip
      361 laalagvlav vawnmiekpa iaillrsgwg eatvlgatff ltvfrdlsea ivvgfalgsv
      421 lfihrmsrtt avtthvpfva rdeaddahpr kaynesaaan pdvvvyritg alffgatasi
      481 gsvldriqdn qkalvvdfsa vpfldstgan mieglahkah khgvtlwltg ttrdirrvll
      541 kheikrplvr yaatveaais alqrarttlr agptqaa
//
LOCUS       WP_457660327             303 aa            linear   BCT 27-JAN-2026
DEFINITION  Fic/DOC family protein [Sinorhizobium medicae].
ACCESSION   WP_457660327
VERSION     WP_457660327.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Veyron,S., Oliva,G., Rolando,M., Buchrieser,C., Peyroche,G. and
            Cherfils,J.
  TITLE     A Ca2+-regulated deAMPylation switch in human and bacterial FIC
            proteins
  JOURNAL   Nat Commun 10 (1), 1142 (2019)
   PUBMED   30850593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Kinch,L.N., Yarbrough,M.L., Orth,K. and Grishin,N.V.
  TITLE     Fido, a novel AMPylation domain common to fic, doc, and AvrB
  JOURNAL   PLoS One 4 (6), e5818 (2009)
   PUBMED   19503829
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="Fic/DOC family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /GO_process="GO:0018117 - protein adenylylation [Evidence
                     IEA]"
                     /calculated_mol_wt=33731
     Region          13..225
                     /region_name="FIDO"
                     /note="Fido, protein-threonine AMPylation domain [Signal
                     transduction mechanisms]; COG2184"
                     /db_xref="CDD:441787"
ORIGIN      
        1 msfamaderp kgsytypnts ddpdrtnvlk nrwgiethse lrvkeyrata vrlqeiaegd
       61 vpqgnfdkah leaihgyifq dvyewaghtr nespivegqr vepigglskg gtsflpgsri
      121 emgldealkp irdpqalrna tpeefaerag rvlselnyvh pfregngraq eafiselgrh
      181 ygheidfsai tkprmieasi ettsdpsspv mkhviedams pgrreairsa fedlrevgee
      241 plhhhvrtar ageeitgqil ghdnrvaslv tdqgivvadr adlpeklpde deitftarrt
      301 fpg
//
LOCUS       WP_457660330              85 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Sinorhizobium medicae].
ACCESSION   WP_457660330
VERSION     WP_457660330.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..85
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=9884
     Region          1..83
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mklewtrkav sdlgrlhdfl asvnrqaaar tvqsltsapa rlleqprige rleefdprev
       61 rrilvghyem stiyvlrlwh tresr
//
LOCUS       WP_457660336             457 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457660336
VERSION     WP_457660336.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47827
     Region          12..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(24..25,28..29,32,71,129..130,132..134,137,157,
                     160..161,164,246,249..250,253..255,258,286,290,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msnvkpagsp akvalasfig tsveyydffi ygtaaalvfp riffpeaspl mgtllafatf
       61 gvgffarpvg gvvfghfgdr vgrkkmlvis lvgmglstvl mgllpsygti gilapilltl
      121 lrliqgfcvg gewggavlma vehapkgkkg ffgafpqmga pagtglatfa fmlvagmpde
      181 qfyswgwrlp flisallvlv gliirmkvde spafeelrkq nqavkipaie airthpreil
      241 lvagiylsqg vfayismsyf vaygtsvvgi prgaalqavl vaaviatily plfgalsdri
      301 grkttymiga aamaasigpa lllintgepl yfmaalalvf glamspagga tgslfsmifs
      361 pqvrysgasi gytlsqiags afapliasal ygayqstlpl fvymlgmsli siialtlvpg
      421 pwgrkeaamq danseqsagh rdsaaasqpd glghlka
//
LOCUS       WP_457660341             321 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660341
VERSION     WP_457660341.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 321)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (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   4  (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   5  (residues 1 to 321)
  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   6  (residues 1 to 321)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (residues 1 to 321)
  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   8  (residues 1 to 321)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   9  (residues 1 to 321)
  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   10 (residues 1 to 321)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   11 (residues 1 to 321)
  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 10156897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..321
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33720
     Region          53..319
                     /region_name="PBP1_ABC_unchar_transporter"
                     /note="type 1 periplasmic ligand-binding domain of
                     uncharacterized ABC-type transport systems predicted to be
                     involved in uptake of amino acids, peptides, or inorganic
                     ions; cd06325"
                     /db_xref="CDD:380548"
     Site            order(69,71)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380548"
     Site            order(101..103,121..122,124,180,232,255)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380548"
ORIGIN      
        1 mngcsryaav lataawvgaa sfpvqaqdkk vptvgfvaga ggypkmaitn qtffdalaek
       61 gykdgstmrv vfrsaegdmg kmpdlvrqvl sknvdvlvvs sspgcaaaaa atadtpvlci
      121 svqddpvreg ltdslergrg nvvgvhshla dgikqqldgl lamkpgatri gvlfnpenkt
      181 hlrllelwks saaakhvqvv emrvtkaadl daalktalae ktdlaigllg adtyairkei
      241 aenaakqrlp ivmdtpgsyt dmggvatlgv divplyrega ikqmvpmleg krpsdlawig
      301 pgrisakfng evvrsfglta d
//
LOCUS       WP_457660345             144 aa            linear   BCT 27-JAN-2026
DEFINITION  reverse transcriptase/maturase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660345
VERSION     WP_457660345.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inouye,S. and Inouye,M.
  TITLE     Structure, function, and evolution of bacterial reverse
            transcriptase
  JOURNAL   Virus Genes 11 (2-3), 81-94 (1995)
   PUBMED   8828137
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..144
                     /product="reverse transcriptase/maturase family protein"
                     /EC_number="2.7.7.49"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0003964 - RNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006278 - RNA-templated DNA biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15773
     Region          <11..113
                     /region_name="RT_G2_intron"
                     /note="Reverse transcriptases (RTs) with group II intron
                     origin. RT transcribes DNA using RNA as template. Proteins
                     in this subfamily are found in bacterial and mitochondrial
                     group II introns. Their most probable ancestor was a
                     retrotransposable element with...; cd01651"
                     /db_xref="CDD:238828"
     Site            22
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238828"
ORIGIN      
        1 maesrvygar vfhdtysgtp qggvigplla nialhgmeaa vglkyisrgd nvgkrclily
       61 addfvvfces eedarnarse lsvwlasrgl alsdektris ylsdgfdflg fnirryrape
      121 nsvrleivhq alseigevae ssdr
//
LOCUS       WP_457660346              98 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Sinorhizobium medicae].
ACCESSION   WP_457660346
VERSION     WP_457660346.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..98
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11258
     Region          1..95
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mivefsdeae sdleqiadyi akdnprhals fvqelrskce rlgdtpkgfp lvpryeeygi
       61 rrrvhssyli fyriegeqiv ivhvlhgamn yaailfes
//
LOCUS       WP_457660351              92 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Sinorhizobium medicae].
ACCESSION   WP_457660351
VERSION     WP_457660351.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     New connections in the prokaryotic toxin-antitoxin network:
            relationship with the eukaryotic nonsense-mediated RNA decay system
  JOURNAL   Genome Biol 4 (12), R81 (2003)
   PUBMED   14659018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..92
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0097351 - toxin sequestering activity
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045927 - positive regulation of growth
                     [Evidence IEA]"
                     /calculated_mol_wt=10063
     Region          4..67
                     /region_name="PhdYeFM_antitox"
                     /note="Antitoxin Phd_YefM, type II toxin-antitoxin system;
                     pfam02604"
                     /db_xref="CDD:460615"
ORIGIN      
        1 mtstvtaaav sknfgayqda avrepviitk ngrprtvlia yedylrlsrr drrveatadl
       61 sdddlaavek semepgfdhl ntqlltdkha ad
//
LOCUS       WP_457660352             139 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457660352
VERSION     WP_457660352.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Clissold,P.M. and Ponting,C.P.
  TITLE     PIN domains in nonsense-mediated mRNA decay and RNAi
  JOURNAL   Curr Biol 10 (24), R888-R890 (2000)
   PUBMED   11137022
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..139
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=14638
     Region          5..131
                     /region_name="PIN_Pae0151-like"
                     /note="VapC-like PIN domain of the Pyrobaculum aerophilum
                     Pae0151 and Pae2754 proteins and homologs; cd09873"
                     /db_xref="CDD:350221"
     Site            order(9,38..40,42..47,49..51,67..68,70..71,84,87..88,
                     90..91,95..99,101,116..119,123)
                     /site_type="other"
                     /note="homotetrameric interface [polypeptide binding]"
                     /db_xref="CDD:350221"
ORIGIN      
        1 msvfvldast aaawllpeeh seiaeqliag isgqcpvpgl fwhearsilv taerrqriaa
       61 gqaltamtrl rripledaga gqdgsviela tvqglsayda aylelaiars lplatldrkl
      121 aaaaraekvp vlgpfgneh
//
LOCUS       WP_457660353             675 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457660353
VERSION     WP_457660353.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 675)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..675
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=75529
     Region          1..532
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mqlhkisvkn frllhdvevl leprttvivg rnncgktslt evvkrllhdk tavfrledfa
       61 fcchnkfwea flafknaaee qdvrlllpsi eikltftygp adplgllsef vidldpdcse
      121 avvvgrytlk pammtslfag ledteatgkd elfrllreri pnlfgldlfa vdpndatntk
      181 aielsllrsl aasgfisaqr glddeskedr vvigkvlenl fmtaknnpad aashemakel
      241 egavheiqdk igtdfnskln almpalslfg hyptagdstl ltettlnvdk lltnhtrvry
      301 sgvngihlpe tynglgarni ilillqlrqf fkqylamepk pavqvvfiee pevhlhpqmq
      361 evfirklsei adlfgeehkl lwpaqfvvst hsshvanear fdairyflak ldaehgslkt
      421 tikdlrkglt gkgtpeeqef lhqymtltrc dlffadnail iegtterlll pkiiemidvg
      481 qpagkklksq ylsimevgga yahmffdlld flelrtlivt dldsvrqnda kkwvgcpvhl
      541 gsktsnaclk swfhaevtpd qlvlvpdeyk ivdkkriayq ipeadglacg rsfedafmla
      601 ntalfplvgt etekaqtawd nakdekksef alrhalrven wtvpryireg ivwlaepdtp
      661 plivaaeaap adiaa
//
LOCUS       WP_457660355             184 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660355
VERSION     WP_457660355.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 184)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..184
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20302
     Region          <5..176
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 maplrggvhn glwfwalsge rtflncdnpt qrrplpgetv slmswtvang mhaenertva
       61 igplpepckr afeaileire avdplikpgt lwrdlfektr egleargyga htpgrighsi
      121 glgpherasi daksqlvlep gmiitfephi ripgtcqtqi sdtvlitktd reyltrargg
      181 ylei
//
LOCUS       WP_457660361             362 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660361
VERSION     WP_457660361.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..362
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=38684
     Region          <86..198
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mrmspalwvi salwlgasgt ahsqvpvldg kvletdtkrd qttteiektd sdrhtvsksv
       61 tcsmyrpgrs gdaasaatgn peitglvkrv aqeegvdesl fmalvyqesr fnpcakspvg
      121 aiglsqlmpg takdlgvnpy dmednlrgga rylkqqlrrf ngntnlalaa ynagpgnvqk
      181 wggippfket qgyvanitqk wlpafggsdv anipanyggg staftgmrds tinsmatsqa
      241 igessgnvas wlqqlgamss gtiqdswdhn tgarnanlem mnqvirlgtt madlmnsrsa
      301 vdvgnlsgas rtsdfknddd dadrettgvc dpreglewsp tekacvqkre reanvdlmlt
      361 aq
//
LOCUS       WP_457660365             227 aa            linear   BCT 27-JAN-2026
DEFINITION  B3/B4 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660365
VERSION     WP_457660365.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Roy,H., Ling,J., Irnov,M. and Ibba,M.
  TITLE     Post-transfer editing in vitro and in vivo by the beta subunit of
            phenylalanyl-tRNA synthetase
  JOURNAL   EMBO J 23 (23), 4639-4648 (2004)
   PUBMED   15526031
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Mosyak,L., Reshetnikova,L., Goldgur,Y., Delarue,M. and Safro,M.G.
  TITLE     Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
  JOURNAL   Nat Struct Biol 2 (7), 537-547 (1995)
   PUBMED   7664121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..227
                     /product="B3/B4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=24965
     Region          4..225
                     /region_name="B3/B4"
                     /note="B3/B4 domain (DNA/RNA-binding domain of
                     Phe-tRNA-synthetase) [General function prediction only];
                     COG3382"
                     /db_xref="CDD:442609"
ORIGIN      
        1 mfespvider ikeiapgfra msihvdatna gkgslhtgll tdacdyvlrg gpawadahlt
       61 swadaytrfg akpnrtpcsa qalrkrvlkn gmipsinpiv dlynavslky avpvggenyd
      121 ayagrplltv adgrerfetv mngevvienp lpgeviwrdd agvtcrrwnw rqgtrtrlda
      181 tdrrmwfvle sletmpvgal aeasdmlveg lktlmpdclv faqriav
//
LOCUS       WP_457660372             236 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660372
VERSION     WP_457660372.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..236
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25751
     Region          1..229
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 miqsierall ileiiaregg aaklkhisek akltkstthn ilktfaslgy vkrgicdtqy
       61 ylgagiqnis ratgddnalk gllrptlhri aeksketvyl avlngdevcc ldavettqmr
      121 trpigerepv srsavgqifl afvpglferl kadpnelitk eiqeqvakva nmgfsvalet
      181 ihpgmncvav pwrqrgevra aiglsgpsar lsnkalisha lmmireveqs farttn
//
LOCUS       WP_457660373             303 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660373
VERSION     WP_457660373.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=32811
     Region          <134..255
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mctiwvqisy aqdghksadi ittrstwtie rkaelatnfd erwrgsekef vlgadgavkq
       61 enavqnkadk gphdlgglhh tdadlnnfap ssnvpnrvde pqvftgsiqh ivavrqinds
      121 nndmyecgps plspeevksl vvqtarryrv devfataiaw aesgfdqsrn spkgargtmq
      181 lmpataarfg vtdicdptqn ieggmkylrf lldefqnpll vaaaynsgeq riyqhggipp
      241 fqetvgyvak vvnyqlglpm psakgkarpa aapqavsdas dsgdagviav kktgkfvggv
      301 mhf
//
LOCUS       WP_457660381             226 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660381
VERSION     WP_457660381.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23593
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavg wgrgpngcpi faqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarvgyftpg anssaaggei gavavlerhg
      181 alfplgdqnl alpsysagsg dpaktlasql eqlglsvhdw fslfdl
//
LOCUS       WP_457660390             215 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660390
VERSION     WP_457660390.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24235
     Region          1..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mitlydyels gncyklrllm smlgieyntv pvdfypgreh ksdwflrlnp lgqlpviedd
       61 glvlrdaqai lvylaskydp sgtwyprsdp allgeisqwl afadgitgta saarlhdglf
      121 ydldvelara gahrlfrild ehlwfgeqer rdwicsgqhp tvadiacfpy vmlseeggvs
      181 rqdypairrw cdrvkrikgf tvmsgifpag paraa
//
LOCUS       WP_457660391             369 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660391
VERSION     WP_457660391.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40144
     Region          1..362
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtqielrnie krfgavqvik nlnlaiadne fivllgqsgc gktttlraia gletidegdv
       61 lidgqpvqhm kasardiafv fqsfslyphm tvfeniafpl ratrgnrsei erevqavakt
      121 lqithllskr psalsggdmq rvaigralvr rpkamlmdep igaldaklre emraeikrlh
      181 ikqgsttiyv thdqveamsl adrivvmheg vlqqvatphe vyahpsnmfv aqfvgspvmn
      241 maevtvseaa qhaqvllrga ptafnlpstl taqlaaagae ngnltlgirp egvlvsrepr
      301 egfvtaeahi ieplgshdii dlqlgdqmlr artksgfvqr pgvavwarln paqahffkss
      361 tgasfgirl
//
LOCUS       WP_457660393             400 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660393
VERSION     WP_457660393.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..400
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44243
     Region          2..380
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(173,175,217,243,269,292,319,344)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mkitsfetvr vrdfpnilwv rihtdeglvg lgetffmaqt vetyihevva pkllgrdple
       61 idriskdltg ylgfrstgae mrgnsavdig lwdlfgkatn lpiaqllggf srreirtynt
      121 cagntymrda rgqqtanygi ggprrdyddl ngfleradel aedllsegit amkiwpfdia
      181 aeksggqyis gpdlrkalep fekirkrvgd lidimvefhs mwqltpaiqi aralepyatf
      241 whedpikmds lsslkryaaa sraplcaset latrwafrdl metdaagvvm ldlswcggvs
      301 eakkiatmae awhlpvaphd ctgpvvlaas thlslnapna lvqesvrayy ktwyaelttq
      361 lptvtngmit ippgaghgvd lapdldrkfe vsrrssevqp
//
LOCUS       WP_457660394             154 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660394
VERSION     WP_457660394.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..154
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17784
     Region          11..>90
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mshrinfatk spdimkkfva ffvaskqnav eesirdlvnv riaqlnactf sldmyvkqak
       61 rdgerelrly hlaswrgvtl fsprerasla gpkssrrcli skfrtnsttr vypvereart
      121 srlrwpqmlg rvsmpasklf lahrmrcsds trwd
//
LOCUS       WP_457660395             137 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457660395
VERSION     WP_457660395.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..137
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14823
     Region          8..>118
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mhslshitva ivdddqflle slhdffamsi psktyrsaee flksgdaqwv hcvladfkmp
       61 gisglqllet lvreggppvc imtsfaddrt raavhsggav gllekpissa nllnfisask
      121 rkvtgvlppr yppsrdq
//
LOCUS       WP_457660399             103 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660399
VERSION     WP_457660399.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..103
                     /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=11399
     Region          6..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpsvserpvk rsirrnelre ivpladstiy emeqrgefpr rfglsprcvv wdlaeveacl
       61 esrrtrsipr akhpdvtqrk frpvkgqgra qalgmvgggg gag
//
LOCUS       WP_457660400             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660400
VERSION     WP_457660400.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34869
     Region          8..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mgdmqepvve vrnlrvdfpg rhgtvtalsg islsirsgei lgvvgesgag ksmtglaiqg
       61 lleapghiag gkvwlgesri dtlddramek irgreigaif qdpltslnpl ftvgaqlvet
      121 irrhlglgka eararavqll rdvgipsped rvnqyphqfs ggmrqrvvia lalaaspklv
      181 iadepttald vsiqaqiisl lrklckekqt avmlvthdmg viaeaadria vlyagrlvei
      241 gpveqvlhqp rhpytqglma sipslgarve rlnqidgsmp rldaipdgca fnprcsmagp
      301 rcrreqpelv faghsasacw lnaggta
//
LOCUS       WP_457660405             195 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660405
VERSION     WP_457660405.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..195
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21692
     Region          2..172
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mytpgeliva hgesgrdvff ilegrarvtl fsengreify gdrgpgdiig evsaidgkar
       61 sasvvalept raarlpapaf rrlvtdhpdf swallehlss girhmtdrvy qfstlvvrrr
      121 lilellrrad drdestsrvf idpapthfel aasisthrea vsremsvlak ggphremrtq
      181 apavrpycsg iarrr
//
LOCUS       WP_457660411             576 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660411
VERSION     WP_457660411.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 576)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..576
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62266
     Region          131..393
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mssldrklvr elwrlkaqvl aialviasga allimaltti ealeettaay yertrfadvf
       61 aqakrapehl grdiaeipgv rlvetriveg aildmpgfae pvvaqllslp ergpellnal
      121 virsgrltdp arpnevvvse pfaeahdlkp gdsfsavlrg rkrtlqvvgt alspefvyai
      181 apgglmpdde rfgvmwmghd avtaafdlka sfnsvtlgll pgadekdvis rldgllapfg
      241 gigaygradq tsnwflesei aqqknmsrim ptiflavaaf ltnmviarli eterheigll
      301 kafgysnlai gwhyakmvlv igtigiligs llgawlghwn telytkfyrf pfllyrpgpa
      361 gfviagaisl gaalagslaa vrraarlppa eamlppsppi yrrswasrta lagaldepsr
      421 miirriirwp vraflaslgl amsiavlima lqwvdaidal aetafergqh qdatvafndl
      481 lpihtagdyk hlpgvlaaep yrhasarish ghlverqgii gvppgailsp vfdvergrid
      541 vppgglvlsr klaellqvsa paiawasnsw rgarpd
//
LOCUS       WP_457660412             224 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660412
VERSION     WP_457660412.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..224
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24652
     Region          3..223
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mgvellegrq arlslpvaqv fetylgtpay mdmeelnrls gdgrvasglh ilvdapsrts
       61 llaklkdipn vaavlfrqaa idtfyqtmge tififvgffv afsmtlsvgv tynsirials
      121 erarelatlr vlgfsrwets yillgevgil twiaipfgai vgyglawymt safetelyrv
      181 plvlrdatyg kaalialaat lvcaafvrrr ldrldliavl ktre
//
LOCUS       WP_457660419             303 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Sinorhizobium medicae].
ACCESSION   WP_457660419
VERSION     WP_457660419.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31403
     Region          15..295
                     /region_name="ribokinase_group_B"
                     /note="Ribokinase-like subgroup B. Found in bacteria and
                     plants, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01945"
                     /db_xref="CDD:238920"
     Site            order(55,251,254)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238920"
     Site            order(192,222,249,252..253,256,278,281)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238920"
ORIGIN      
        1 mmgavaipde ahpeviclgl saldriwrve klfasgseki ragehltepg gmaanaavav
       61 arlggivsfw gragdddagr iladgfaaeg vdienfrlfe ggassvsgvi vdtagerqiv
      121 nfrgrypadp swlpladlaa dcvladprwp egaealfraa rsrgiptvld gdvadvevfe
      181 rllpltdhai fsepglrgfa gdeiepalah aatfgcrmva vtrggdgvtw regsdlvhlp
      241 apkvpvvdtt aagdvfhgay afatgagfgi sdalcfagav aafkctrsgg raaipfvdel
      301 kss
//
LOCUS       WP_457660423             184 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457660423
VERSION     WP_457660423.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..184
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19558
     Region          6..>177
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mknqalkgaa lvvlamtlyi qndvatkllt erfdtlqvmm vrgaigaasl lvllrftgtt
       61 yswkhalmpa vmirsacdgl aslafvfala emplatltai mmlapvisag igalifrerl
      121 tgrlaisvml gftgvlifar pvstgvnfpm flacsatlll sardlftrht sadvgsvlkv
      181 lqih
//
LOCUS       WP_457660425             394 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660425
VERSION     WP_457660425.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  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 10009251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43280
     Region          1..334
                     /region_name="COG5397"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444156"
ORIGIN      
        1 mlktvdliyq tmlaeigqra mddawtldfp pigrfvkvkv kereywyfdq sdgeggqkrk
       61 yvgpaedpei skrvedfsrt ksdyrirrrl vssltrdggl laadrtsgli vetlaaaglf
      121 rlrtvlvgtl afgtysgllg vrmpsaaimt gdadfaqdya isaevmdslp pilellqsad
      181 ptfravptfd ggattafvng egyrvefltt nrgkdeyldk padmpalgga saqplrfinf
      241 lirepvravl lygagvsvlv pdparyavhk liiasrrhah salkrdkdlv qaailveall
      301 qtkrspdlam ayveawergp awqeaieiga amlsvehkdr lrecleagga gnrregdiav
      361 lrshgsskmv irsfftpevk vgsssrpqri tktn
//
LOCUS       WP_457660432             394 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660432
VERSION     WP_457660432.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 394)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42737
     Region          123..391
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 maeverllgg rtrdirlkge lgrlfeersw srtakiiraw miwvtlldvl tlglnaillp
       61 navalsmlpp acilppaala tafiwrkprg vglqrvslva glflillsva lvgvsaggef
      121 yerhlnimlf vaitaiiifs iplawtvava sfalalylif qlrnpmldtg savagtlfft
      181 sgivatvvar rtmtilaqkt fllelrdkrr vaeladanar lerlaktdpl tgianrrwmm
      241 etlnrlwgag aerpagtaml mcdiddfksl ndrlghaegd rclvkvagii qssvrrnrdh
      301 varyggeefl vvlpgadvqa alataerira sveaaslpnp asrvapyvtl sigvaaqgaa
      361 geiigperlq nqadtalyla kkagrnrvvl frpe
//
LOCUS       WP_457660436             313 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660436
VERSION     WP_457660436.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..313
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35389
     Region          4..>231
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 mklkrlsigt fnlynlnepg lsiytdktgw sqeeydrkie wtsrtirllq pdifgfqelw
       61 hsasieralt qsgiagdydl ivpenadgkr ivcaaivrkg lmisepqwik rfpekftlks
      121 sgddpqtpai tvsipsfsrp vlhfsvrpre dhepihvyvc hfkskgptkv fqedwfeadg
      181 alykkhatsi gaaistirrt aeaaalrfil teqmkgtrtp vivlgdindw paqqhrqhpd
      241 raaalsgrrf swrrrcqplh rsdpagipqh arcllhtcps ghhgvarphs gqrgilrqlt
      301 ttgvdvrwhd gqq
//
LOCUS       WP_457660439             216 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Sinorhizobium medicae].
ACCESSION   WP_457660439
VERSION     WP_457660439.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..216
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23395
     Region          <4..211
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mralqgisar lntmvsfwlv vllyvilgll evsdlgarir rltddnaari isgfelaasr
       61 irryllirti msaatgiavw alatafglrf aaewgivaft lnyipfigpa fatilptcya
      121 laqfqspqsa livfaclsta qfiigsyiep rvagntlgis pslvlfsvfl wtflwgifga
      181 figvpitiav lsfcaqfast rwlaellgke timdga
//
LOCUS       WP_457660445             469 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457660445
VERSION     WP_457660445.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 469)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..469
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=51136
     Region          <34..464
                     /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 mkatapvlli sglllftlts glsvvlrrrs rrlqesqael nhlarhdplt glanrasfnq
       61 slaqavassa adqanallyl dldrfkqvnd tlghpvgdrl mvavakrlme tasagvisri
      121 ggdeftivve rtrqeevekl cdsliaairq pfeidgqpil iglsigvava tgndadpvei
      181 trkadialyh aksagrnrya vfghhmdeli rtkrdleqdl raaldagnql evfyqpvysa
      241 qsreisslea lvrwrhpskg aiapdvfvpl aetaglidrl gafvlkeacs tarefpsldi
      301 avnvsaielg qrhyaaqvfs llrqfsvepw rleleiteta lldeagvcek nitalrdfgv
      361 kfalddfgtg fssfgrlqrl evdrikidrs fvhafdrpgg gvavvqsivg vahakglrit
      421 aegveteeqs eilrnlgcde lqgfhlskpv pksslrqllg aetakrtss
//
LOCUS       WP_457660461             116 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Sinorhizobium medicae].
ACCESSION   WP_457660461
VERSION     WP_457660461.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..116
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11706
     Region          33..>100
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 maygspplqq tsagaaggpv sncgsahais raaqqadggp lfrqrcatch avdpgenkag
       61 pclasiagrp aasvdgahys kalksagitw drqsldafla tepfslrhtn dgphpr
//
LOCUS       WP_457660462             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660462
VERSION     WP_457660462.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36107
     Region          1..329
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mssppliear titqrfgarp dlaakialgl klakpapvvh aldgvslsir sgevvglvge
       61 sgcgkstlgr viagiatptg gsvfwkgvdr ntmsaaeqke aglatqmifq npmaalnprm
      121 tieeliweap kthgmatate casyvdnylt lagfdpsmkt ryphqfsggq rqrvniaral
      181 avqpkflvcd esvaaldvsi qaqvinlfmd lrerldltyl fvshdlgvve hisdrvaimy
      241 lgriveeapv edvfrrpnhp ytrallaevp rietgkrrfk avegelpspl dppkgchfhp
      301 rcpfamercr vevpvrkeia pkhlsachln g
//
LOCUS       WP_457660464             362 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660464
VERSION     WP_457660464.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39258
     Region          1..361
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 magisiqnvy knygalnvlk efsleisdge fvvlvgpsgc gkstmlkila glepasggki
       61 ligdkdvtdl apgdrdiamv fqnyalyphl tvgqnigfgl kmrgmpkaei dkrvhavaki
      121 lavehlldrr pkalsggqrq rialgraivr epraflmdep lsnldaklrv htraeisalh
      181 krigvttvyv thdqieamtm adrvvimrdg viqqiadpdt lfarpanlfv agfigspgmn
      241 fmsarieggr ltlfgqnfat qkgardgevi vgirpehlsl gqgdvtfavr ptlveslgse
      301 kyiyfdpgen aygeaardee rgkgliaria hsgpvregde ltlsfdpsei hlfdpkteka
      361 vd
//
LOCUS       WP_457660466             534 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660466
VERSION     WP_457660466.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..534
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58194
     Region          5..534
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mnphpnetyd fivvgagsag cvlanrlsad prnrvlllea ggsdryhwvh vpigylycmg
       61 nprtdwmmrt aaepglngrs lpyprgkllg gcssingmiy mrgpaadydg wrqagnagwg
      121 wddvlpyflk sednhrgtsa mhgaggewrv erqrlswpil dafrdaaeel gipktedfni
      181 gdnegsgyfe vnqrggvrwn ttkaflrpam krpnlkvltg aeterlifeg rrtkgirfrl
      241 hgrirearat revilsagai ntpkilelsg vgrpdvvsaa gielvhdlpg vgenlqdhlq
      301 irtvfriega ktlnqlyhsv fsrmgmgley mlrrsgplsm apsqlgifar sspsvatadl
      361 eyhvqplstd rlgeplhkhp avtvsvcnlr pesrgsvhvt tgdasaapdi rpnylstagd
      421 rllaaqairh arslmatkai arfkpaemlp gaefqsedel irqagdiatt ifhpvgtckm
      481 gsdpmavvdp slkvhgldgl rvvdasimps ivsgntnspv imiaekaada ilrr
//
LOCUS       WP_457660468             315 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660468
VERSION     WP_457660468.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 315)
  AUTHORS   Tomii,K. and Kanehisa,M.
  TITLE     A comparative analysis of ABC transporters in complete microbial
            genomes
  JOURNAL   Genome Res 8 (10), 1048-1059 (1998)
   PUBMED   9799792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..315
                     /product="ABC transporter permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=33213
     Region          11..299
                     /region_name="NupQ"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     subunit NupQ [Nucleotide transport and metabolism];
                     COG1079"
                     /db_xref="CDD:440697"
ORIGIN      
        1 mevlekifnf aliaatlrtt apillvslgg sfttkagifn iglegqmlvg affgvlgsiw
       61 tgsalggllc gvlaavvmaa tfsllvvtlr anevvvglal nilaggltis ltkaifgtrg
      121 sivsgdivgl ppidipfied lgrfgrvlsg ytplvylafv mvfvvwvvly rtklglyirv
      181 tgekpeaaea lgiptalmqh iasllcgvla glagahlslg yitmfaenms sgrgfmavav
      241 lifsngdplk vllgcllfgf sdaaslrlqt fgfpsyivlm vpylvtlgal faltyrqrpk
      301 viretlesls llrrt
//
LOCUS       WP_457660470             155 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Sinorhizobium medicae].
ACCESSION   WP_457660470
VERSION     WP_457660470.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..155
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16554
     Region          5..143
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mrlpervlti vvvtvmsgli ivptaqvimr gvfrlpfiga eeltrfllic lvflsyplvv
       61 ghgenivmge lkaampmkar aivnvaisvv aiavtgfigw vtasnitrnl anatptlgip
      121 fwiflgatlf gfaaaalihl lhlrkppqad knvav
//
LOCUS       WP_457660471             422 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660471
VERSION     WP_457660471.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..422
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45191
     Region          21..392
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 mgnvnscggr lrvaktgstt vsalvalvll agcgghakgv mapvalaqps atsqvdmlva
       61 ttrepsgdaa tlfsgerspt lsmtdvavsi ppdsrrkpgt vqwprklppn petdfavtrv
      121 rklasndear dwfqvhnegg hvllfvhgfn nryedavfrl aqivhdsgaq atpilftwps
      181 rarlfdynyd kestnysrta ledtlrtlas aprvkditil ahsmgtwltm eslrqmgird
      241 ggiapkienv ilaspdidld vfakqwvdmg karpkftifv sqddralavs rlisgdvsql
      301 gaidptaepy rtqletagit aidltkvqtd dglhhgkfae speivqligq riikgqtltd
      361 sdislgegit avvagtaknv gtvaaatita pvtiieqrgt prkkvnleet ltssenagnt
      421 ar
//
LOCUS       WP_457660472             120 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457660472
VERSION     WP_457660472.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (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   3  (residues 1 to 120)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..120
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12934
     Region          <1..107
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mkagavdflt kpveaaalle avdvalqrar srreteekka nvamridrlt aretqvmhlv
       61 vsgllnkqia adlgtvekti kvhrgrmmsk lgvrtvadlv rlvsgaetmh ggigpksnyd
//
LOCUS       WP_457660473             360 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457660473
VERSION     WP_457660473.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..360
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38889
     Region          1..349
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrllilgtgg manshakafa eiegvemvga vdvdpsrara fasthgiert ftsldeaiaw
       61 gefdaatnvt pdkahhpttl aliaagkhvl cekplaenye kaaemaaaae raglvtmvnl
      121 tyrnvaplqk arelvvagei glvrhleasy lqswlvskaw gdwaseskwl wrlstkhgsn
      181 gvlgdvgihi ldfagygans svervfarlk afdkapgnrl geydldands famtaefeng
      241 amavihasrw atghlnelrl rlhgdkgale vihtpdgssl raclgadvek avwrtvdagt
      301 vptnyqrfve avkagrtvep gfrhaadlqk vlhlaieter errelgvpdi davvqeravg
//
LOCUS       WP_457660475             330 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660475
VERSION     WP_457660475.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Gonzalez-Duarte,R. and Albalat,R.
  TITLE     Merging protein, gene and genomic data: the evolution of the
            MDR-ADH family
  JOURNAL   Heredity (Edinb) 95 (3), 184-197 (2005)
   PUBMED   16121213
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
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..330
                     /product="MDR/zinc-dependent alcohol dehydrogenase-like
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35673
     Region          17..327
                     /region_name="Zn_ADH9"
                     /note="Alcohol dehydrogenases of the MDR family; cd08269"
                     /db_xref="CDD:176230"
     Site            order(48..50,53,128,132,152..157,175..176,180,207,
                     220..221,223,243..244,268..270)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176230"
     Site            order(48,72..73,128)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176230"
ORIGIN      
        1 mnirmsqrtd tmsaaivtgp gtvrierlpl pqpgrgqvri rlegcgvcas nlvpwagpew
       61 mrfptepgal ghegwgvida vgegvhgfsp gdrvaalsyn ayathdiadq saiarlpasl
      121 adqpfpgepl gcafnilrrs aitpgetvai igigflgvll telvsaagar viaisrrpss
      181 laaakqagas dvipmddhwr iieevkqltd grfcdcviea vgkqwpldla geltrergrl
      241 viagyhqdsp rqvnmqlwnw rgldvinahe rdpavymrgm reaieataag risparlyth
      301 rfpleelgaa lditrdrpeg fikalviche
//
LOCUS       WP_457660479             278 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660479
VERSION     WP_457660479.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10452004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..278
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30391
     Region          84..126
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          153..269
                     /region_name="TetR_C_7"
                     /note="AefR-like transcriptional repressor, C-terminal
                     domain; pfam14246"
                     /db_xref="CDD:433807"
ORIGIN      
        1 mgslpvrpag frlkqskrqf apddsnawyr rcsatqrilk ppqdlrstep enwmaeeefa
       61 ededdqeaas grsgkrdarr eeflraatev flssgfsgas vdsiiakagg skrtiysyfg
      121 kkdqlfttvi keitgrvmgp fpaaniagad ldtvlyrsgs hyldavmspe alqlyrivvg
      181 egarfpgvar affengpgra saalasilee gadnwgipkr saaklaehfi gmirddlhlk
      241 vvlglcdppt paearssvrd avdvfvygir kteltrsr
//
LOCUS       WP_457660481             161 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660481
VERSION     WP_457660481.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16936
     Region          5..157
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mnrlvsmtvn gepcelsval nrtlldalrn egsltgtkkg cdvgdcgact vimdgrpvna
       61 clvlaaeaeg aaietieglq paydkphalq qkfmefggaq cgfctpgiim makalldenp
      121 vpsedeirfa lagnicrctg ytkiidavra taeelrragt l
//
LOCUS       WP_457660482             240 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660482
VERSION     WP_457660482.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26182
     Region          9..215
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msgpeaehrv vqviveaimd hrvapgarli erelaiasga srsairnglm rlahaglvel
       61 spnkgasiam cspdearqif darivietaa vkklagtige gelerlrafv edereayerg
      121 rmedarhlsr rfhvllaema gndvltgvir dlinrqplls wsrpeteprf cgnhahseiv
      181 eaiasrdger aahlnmehlr alerelgaer aaamqelrsa qaadgpdgna rqadespvvd
//
LOCUS       WP_457660484             302 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660484
VERSION     WP_457660484.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..302
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32716
     Region          2..293
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msadtsfakr snraailfls pallfvfafv aspvayagwl slfrwdgasm pvflgagnfv
       61 rlagdaifwq alfrnilval saivlqvfla laiayclvri vpafsriflf fylvpvmvse
      121 icigllwrfm ynpyfglvna glsaiglggl krgwlgeset aftavvvvms ftylglyvll
      181 fvaavrnvpe svyeaaeidg agdfrkffsi tvpmvwdavr ansllaiigs lktfslvfvl
      241 tnggpnhase vvstylykmg fgsfemgyaa aigfaqmvlt algawiafry mkrigagaga
      301 ws
//
LOCUS       WP_457660486             495 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660486
VERSION     WP_457660486.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 495)
  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 495)
  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 495)
  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 11458748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..495
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48497
     Region          124..382
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <272..411
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 mdggsgsdti dfgdktaavv ltlagvantt atvggvaedt vrnienifgg agadvltgdg
       61 nsntirggag adgldggagv dtadyrdkvt svvvtlsgan aalvkvggln edtirnfenv
      121 aggsagdtlv gddlanvllg ndgadtlkgg lgsdvldggn gidtadylek adaisvtlng
      181 ttnatvlvgg vaedvirgve nilagsgadt lvgdgasntf rgalgadfid ggagsdtady
      241 rekaaavdvt lfgagdtfvf vggvaedtir nienvfggkg ndtltgddsa ntlngndgkd
      301 lltggggadi ldggaasdta nyrdksasvs vtlngaasta vmvggvaedt vrnienvwgg
      361 tgndslsgdg nanllsgggg sdmlsggaga difqfdfalg asnvdmvldf tagdrlflsk
      421 svftslsggs lasnqfyaaa gateaqgvnq rvvydtttga lyydadgnls ghtavqfavl
      481 stqpgltagd fvlvv
//
LOCUS       WP_457660489             357 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660489
VERSION     WP_457660489.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38961
     Region          1..356
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msnlqlsqvr ksygglevik gvdldiksge fvvfvgpsgc gkstllrmia gleeitsgel
       61 sidevrmndv dpskrgiamv fqsyalyphm tvrenmgfal rfagvpkaei ekrvneaadi
      121 lelgtlldrk pkqlsggqrq rvaigraivr hpkiflfdep lsnldaelrv hmrieiarlh
      181 kqlattivyv thdqveamtl adkivvmrgg vveqigspln lyddpanlfv agfigspkmn
      241 flkgtteive grtyarlpdh ggskipisle aiapdtpvti grrpehfnea gpavldltid
      301 mlehlggetf ayarhgngal ivvetkngre lkagdrlaar fdpasalvfd gegkrlr
//
LOCUS       WP_457660490             754 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 2 protein [Sinorhizobium medicae].
ACCESSION   WP_457660490
VERSION     WP_457660490.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..754
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83862
     Region          9..>547
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          654..743
                     /region_name="Glyco_hydro2_C5"
                     /note="Glycoside hydrolase family 2 C-terminal domain 5;
                     pfam18565"
                     /db_xref="CDD:436582"
ORIGIN      
        1 mrsvtsfnds wvfsagftaa dagtlqagqp islphnaiel pfnyfdetcy qraftyqkvl
       61 awrpdfsgre vslvfdaama davvylngee ivahkdgytp iearltgrlr egdnlitvki
      121 dgsenpeipp fggridyltf agiyrdvwlk itdpvsiani kietrdvlsd artvsvrcdl
      181 anpqglsftg tvsallkdaa gdvlaevage tagggvtvqm dglkglslwd iddpvlyeve
      241 velrtgrgsd rvaahfgfrt aeftnegfrl ngrllkirgl nrhqsfpyvg yamgrtaqer
      301 daeimkhtlh cnlvrtshyp qskwfldhcd rigllvfeei pgwqhiggea wkeeailnva
      361 rmierdwnhp siviwgvrin elqdshdfya ktnrlareld ptrqtggvry itdsefledv
      421 ytmndfilgn eelpgsnrpr talrpqqect glsrkvpyli tefgghmypt kiydqeqrqa
      481 ehvrrhlevl naaygdpsis gaigwcmfdy nthkdfgsgd ricyhgvmdm frepkfaayv
      541 yasqcdpsee vvmkpvtfwa rgerniggvl plivltncde velkygslvk rigpdrenyp
      601 hlphppvvid hrhftkdelg vwgmkwesae ftgfidgkpv agrrmvadpv pttleieadg
      661 ktlraggrds irimlraldq agnvlpflnd avaievhgpa rvvgptrlvf qggstgfwle
      721 stgaagaivv tavssrlggv klelvamaeg ewna
//
LOCUS       WP_457660493             347 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457660493
VERSION     WP_457660493.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 347)
  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   2  (residues 1 to 347)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..347
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          6..320
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mvggankaat irevaalagv apgtvsnvlt gkklvaeplr kavldaiaql dyrpnhlass
       61 lrfgrtksig ivvpdmtnpf fsglvrelel kaaksgfqil lmssyeeaae ereriralvs
      121 rqvdgliisp srdsietsph saisgiptvl vdrafavegf dtvsadneqa tlmgarhlie
      181 lghkritfla tapglanmee rvsgyrkamq dagvsdanvv ygglsiescr saieqelrra
      241 grptavfasa yvatlgaaka iraldlafpq dvsllgfdds dwmtvlrpyv stieqpldel
      301 ghacwellqr rmkkmdvppr pqadrlhlar kgvdpphpak ieatlal
//
LOCUS       WP_457660495             439 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457660495
VERSION     WP_457660495.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..439
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46782
     Region          <2..439
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 msggqgaltl adgirvvdat agattegtaf tlgapvaagi feyqlyrggl tedpdndddw
       61 flrsggvspp pppppppppp pppppppppp pppppppppp pppppppppg pspitpsvrp
      121 eipgyilkpa lmqkmgvaai gtfherqgdq fllnsngylp gawgrlfges fdqswsskis
      181 rfefevspsf sgelwglqag qdligalhdd gsqdrvgvff aytgtsgsng gntlgrlqve
      241 sgsidlhans igaywthiga dgwyvdsigm yswldggsss drgigvdtsg nstalsieag
      301 ypfrfdngwv lepqgqliwq hvdlddandr ftgidyesfg twtgrlgvrl eanttmndvp
      361 vqpfasvnlw hdfdqdykvs fnrvpvvtel eqtllelnvg fsaqmsetvs vygglqfatg
      421 lddddnrgyg gniglrikw
//
LOCUS       WP_457660496             435 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Sinorhizobium medicae].
ACCESSION   WP_457660496
VERSION     WP_457660496.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..435
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46371
     Region          21..413
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 matdgvteqr gykpflpmlm syvasggslv lgsaaqlltf ailarwlgvh efsvfvaita
       61 vaniavhlcg lgameclvrr vardraiypq mlghniilts gsgaalvllg avvlpffftl
      121 spdrmtnvav itlmlvtnil lvrvivlteq ifiahtdfas ankvvvgfaa artvaaalac
      181 iafgattvas wavwqflchv lvavccmwsv rllgapsyrl vreelpqgly fsipfilral
      241 rqnadllvls fvttaeivas ysvarriles sylsvealnr liypgsarat aaglhhalqr
      301 vrrvlaaatv islaaavtvf vlapilpylf gkeylslvgf artlcwvvvp lamwsvavea
      361 lgasgdhaar aavmgfgsia gtglaawasw yappagtfis fyvieiamvv aswsvflhfv
      421 rrdrqaaitf gsgsa
//
LOCUS       WP_457660502             396 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457660502
VERSION     WP_457660502.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 396)
  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 396)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..396
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43496
     Region          19..371
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(31,207..209,269,291)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 msensnspav vagnmsgarv tiilpslgag gtehvvklva nhwaqlgckv tlitlelpha
       61 rpyyefdpri aierlglppq qggkiwagll vlrriyrlrs airhsqpdfv lsfltrtnvl
      121 tllatiglpv pvvvsernnp alqpfgvfwk wiqrrlypra fglvtmtrga ldyfpqkmrs
      181 rgwvianavd lpgewqkrrg nniltavgrl trqkgfdlli eafariawrh pewklviwge
      241 gddrksleal rdaldmtdrv empgvtqrpg lwvetadvfv lssryegwgi vlleamaagl
      301 pvvsfacewg psdmvehged gllvpsndvd alaealsrvl adgelrsrla anaeasakry
      361 lpdrilsqwd avalsalkht ardhaaaasv vgagsa
//
LOCUS       WP_457660505             386 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457660505
VERSION     WP_457660505.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..386
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42585
     Region          1..372
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkvgiielgf rlgylgyvfk aideafeiag yvdpepagla tltekgisag kayatpeeli
       61 agetldllmi gspnhlhldh irigleaglk vfcekplvst ieqslelaal lskhgpdrlm
      121 vglvlryapl yrdlraaqaa gtlghvvsie aaehiepyhg affmrdwrry gryagsfmle
      181 kcchdldlyn gvvgarperv asfggrksfi pandptrdgi ndlqlfhrkp sgwrgsdrvf
      241 dsdgdiidyq vaiieyangv amnfhtnlnv pdqfrrfcvm gsrgmaegdf irgyldvhev
      301 lsgkkvvekq yaketalsqh ygadeqmaae iiahvrdggp lpvspldale agilalsmde
      361 armkrtvvdl rplwdrfdea lhdraa
//
LOCUS       WP_457660508             343 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660508
VERSION     WP_457660508.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12124374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..343
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37286
     Region          <1..37
                     /region_name="OppC_N"
                     /note="N-terminal TM domain of oligopeptide transport
                     permease C; pfam12911"
                     /db_xref="CDD:463747"
     Region          <122..339
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 magcvmlvli glfsfvgplf sphsydqvfp syvtigpsle prpdsstlqg vmegvasrar
       61 vrltefaved qsftatvtsd apidpratry fdranefent kvvategdgr tlkvegdvar
      121 eyfpfgtdsn grdllvrvml ggqisiavgl laslvslgig vlygatsgyi ggrvdnvmmr
      181 fveilyslpf vflvvvlvvf fgrsfilifl vigavewldm arivrgqtla lkrrefvgaa
      241 qalgltdwqi irrhiipnti gpvivfvtvv vpkvillesf lsflglgvqa pltswgalis
      301 eganniqsap wllifpaiff vltlfslnfv gdglrdaldp kdr
//
LOCUS       WP_457660509             200 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660509
VERSION     WP_457660509.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..200
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21460
     Region          13..199
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mpdhgymhkl kagspggpil fvfhgtggde nqffdfgaql lpkatvvspr gdvsehgaar
       61 ffrrtgegvy dmadlarate kmagfvkala seyeaseiig lgysnganil anvlieeglf
      121 dkavlmhpli pfrpkantal agrkilitag erdpicpapl tqalgdylsq qnaavelkwh
      181 sgghdirqne iaateeflrv
//
LOCUS       WP_457660515             416 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457660515
VERSION     WP_457660515.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..416
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45632
     Region          78..408
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mhakmprvll agllfllvps qgfgldlprs nhpvfdrvvt lvvdnfhdpa aldgfgaavr
       61 relndrqpln sespgpqvdt aiekilasle ashtarfkqd tiayyeladi frfairhdmk
      121 rlfppngaat yagvgmvtrm englrfvsdv yddspadkag irvgdevlsv dgapyreids
      181 frdrigrtve irlrreagtq pfkatvaver lrplptfeka idnsvalhee ggrsigylrl
      241 wtlsspdgld ivarelatgr lkdadgvivd lrgrwgggpp daaelfvgdt pnfrliprsg
      301 kdmlanvrwr rpvvaiideg srsglelfay alkangiplv gtrtagalla grayllpdds
      361 ilelavsdav idddvrlerr gvepdiiatf slpyaagrdp qreaafeemr riltkd
//
LOCUS       WP_457660518             604 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660518
VERSION     WP_457660518.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 604)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 604)
  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 604)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..604
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65902
     Region          10..594
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 maftrltarn raflsvfrfs wahwkrqpvr laalltavlf stladvltpl ysgrlvdavv
       61 sgaasdeiaw naamaafmml malslgaivl rhvtfmgivs ltlkmmsdia aaafhhiqrf
      121 ssdwhansfa gstvrkvtrg mwaldllndt llvalfpsvv mlvgstalma wywpmmgvii
      181 glgsivfivv tvslslgyva pmaslanswd trlggalada vscnpvvkaf gaegredarl
      241 akvlrkwenr trrtwsrgtl ngtaqgamll vlraavigfa lllwargqat agditfvlts
      301 ffilqgylre vgmhirnlqr sindmeelva ihdqslgved rpgakpirit eggiefrdvt
      361 fhygahrapl yqgfsvsiaa gervglvghs gsgkttfikl iqrlhnlnag eiridgqnia
      421 dftqaslrqq iaivqqepil fhrslaenia yarpgatqrd ieeaarlasa hdfitelpkg
      481 yatlvgergv klsggerqrv aiaraflada pilildeats sldsesevli qqamerlmtg
      541 rttlvvahrl stvraldrll vfdrgriaee gdhgalirvk ggiyrslfer qaleltkgli
      601 lseg
//
LOCUS       WP_457660519             434 aa            linear   BCT 27-JAN-2026
DEFINITION  O-antigen ligase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660519
VERSION     WP_457660519.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..434
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O-antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47197
     Region          150..393
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mriskaslvr pgandvfgtf alalsvfvfa ysarfgqvsi layyglwlpl vlvdyrkvlg
       61 nyasylwils ftifacltif wsaapslslr tgiqylshvv caliamrtid irtltrgmia
      121 gvaivllysl lfgsyhydpl dgtysfvgaf asknqlgfya slgiyfafaa vfvlgerglw
      181 mgaaggggll aaycllmsqs atsvlttaav iglclgmrai ttlrpasrki lftaasvfgg
      241 vaavaiiyag gidmilgafg kdstltgrty lwqqgieaak asplvgigyq aywvqgfsea
      301 erlweefyig sragfhfhnt fietavetgf iglvlltmvl attffgqlkr llsedrdpel
      361 mvlfgvgall lvrafveidi ltpyhigsfl lyftagklti prrraaallw ppqlhpapyg
      421 raftpmmqrp genr
//
LOCUS       WP_457660520             219 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660520
VERSION     WP_457660520.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..219
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24088
     Region          1..219
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mirfeqatky arakgikkpi iedasltlnr gksvgllgrn gagkstllrl iagaikldkg
       61 riirrgkisw plgfagsfqs smtgeqnvrf variygvdte qligyvedfa elgpffkapv
      121 gtyssgmkar lafglsmgvn fdyylvdeit avgdanfkkk cqavfetrlq dldvvmvshs
      181 tgtirdycdc gvvlekgkmt yyenvedair ahdknmkes
//
LOCUS       WP_457660522             387 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660522
VERSION     WP_457660522.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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..387
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..387
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38995
     Region          5..264
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <255..>320
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 milkgtnlad tirgfladda iwgyegddyl ygdagndrif ggsgndfina glgndyaegg
       61 dgndrleggl gddtldgglg ndtfdggngn divkggdghd qilggrghdt iyggageeyi
      121 dagdgddviy agsgndgfnn rinpatgklt qqavgggagn dtiygeegnd alkgqagndk
      181 vyggigddiv dggngdnfld ggdgndvlds eggidvaygg vgkdkiavga gndlaygddg
      241 ddilsgeaga dvlhggtgnd liyggngndi vrgdvgkdtl vgeagsdilw ggadsdrfvf
      301 kgtptlsgqd svmdfqdgfd ilvienlgvt rysssgangt vfaydttggd vlikgndsvg
      361 rvfsilvddp igtlsaaqfs kadflfa
//
LOCUS       WP_457660525             332 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660525
VERSION     WP_457660525.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..332
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35272
     Region          2..319
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mltggtwcad ynrtvshwpg edglaelfee erhgggsgcn laldikhldp aipvetiglv
       61 gddddgrylr ataaaagidt sqmmvtaaaa tqfcdayvsl sshrrthifh agsgalltpd
      121 hfdfsstrmr ylhlglpgvh rildapwhde angwvvvlkk araagletnl elasvdralm
      181 arlvapclph ldflivndle igaiagveti vrdapdqaac mraaravler galklvavhc
      241 pafaiavtrw gegvvlpsva ipkqeikgan gagdafaagm lygihegwsv gqslrlahat
      301 aaaslrsist tgavlpwrdc laladkwdsr dy
//
LOCUS       WP_457660526             257 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660526
VERSION     WP_457660526.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 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   4  (residues 1 to 257)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28990
     Region          18..246
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 marqenlpde rpidrnhpda lyaqlrnllr gmierrelav ndklpserel vavygvsrit
       61 vrqaikelen lgylqtrpgk giyvtepapv yelevvrsft qtahannrkp gmrllraeia
      121 radpevarpl slptgaevvf leelrlldgv pvvvqrdwfs asltpgildi dwtvenrsly
      181 defenrygil psrgqstlsa rlasdleasl lqldrpaavl tldqiaydsh nrtvnisaaa
      241 yhptryplsl tqshrrf
//
LOCUS       WP_457660531             367 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660531
VERSION     WP_457660531.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..367
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40908
     Region          36..308
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(43,178,244,268,270)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 msilisrrri mqasfavava tlatpvvnas aqtagelrvl tyggqlgkfv ieayakpfea
       61 etgikvipvt qdfelaqlel mqktnsvtid vgpmsqgaal eaaqkgylek idysifrked
      121 ieglvpnvkh dfgvgfffyt ynlvyntkky padklrpnnw aefwdtekfp gvrylvsgqy
      181 gsegpweeal ladgvapdki ypmdidrifa sldkikphvr kwwtagseiq qlmlsgagdv
      241 mmsydgraas aiaqgaalel nrnqakmtwd ywvipknsps aknaqkfvef vsraenqasf
      301 aklypegptn rnafklisee lgltlpshpk ylekaillng awyaevgpdg lsniqrlvqr
      361 wsdwvir
//
LOCUS       WP_457660532             373 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660532
VERSION     WP_457660532.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..373
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41198
     Region          33..373
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msksahlrsd ehpvaklpkq aitedqelke rvpaqiefrd vtkmygpvaa vtelsltvrr
       61 gefltilgps gsgkttalmm lagfesptkg dilisgksva avpsygrdqg ivfqsyalfp
      121 hltvrrnlef plemrgmkas eraplverml krvhldtfge rmpsqlsggq qqrvalaral
      181 iadppillld eplgaldrnl reqmqgeikg lhrefgktti cvthdqeeal tlsdrivvmr
      241 ggrieqldtp ealydrpatr fvanflgean vldspelgfn dqnfrgkvpm vrpervrisa
      301 vnspapaelg esqvvtgive emiyvgplrk yqvrvgdksl vvrqhvasgq evfatggsvr
      361 ldwlradvrl lde
//
LOCUS       WP_457660538             389 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660538
VERSION     WP_457660538.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 389)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..389
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42040
     Region          20..389
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mampqgpqaf prseylrrla avkqemerrd vgalvvvlps nityltgyta ksgyvpqgli
       61 vslndeeptf itrrmdapaa vhqmfvdrsq vigypeslia npdkdgwdai idhlreagfg
      121 kgnigieeqa lssqtvkkfh ararpasvvg fgntvcwirg iksdleialm reaaaiadag
      181 mlrarevmrp gvseadaaae iiaqlvrgag gkqgtdvadf tlcasprtst ahikwaedef
      241 tngsqiniel agvrhgytsa lmrtfsigkp sdvlqrlheg evagleaala vvkpgatcge
      301 vatafndtlk kfgfekesrc gyaigidwte ptasfkigdp tilkpnmtfh lmlgnwided
      361 lgyaisetlr vtdvgaetfs alpreiiqi
//
LOCUS       WP_457660533             591 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457660533
VERSION     WP_457660533.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 591)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..591
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63777
     Region          1..267
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          324..582
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqtfqrigra pvilvlpama lllvvfgvpt vqlfleslna pnfsiqnyss flgqysnirv
       61 llqtleisai atmicllvgy ptaylistas krarmvlivl vvipyltsgl artyswvvil
      121 gdnglinsvl mnwgmisnpl pliynraavy vgmvhimlpm milplvsvml gintsliaaa
      181 ksmgakpsta fwriyfplsm pgvrsgtllv fviclgfyit paalgglgda mlstfiasqv
      241 stgfnmgsvs assfvllaia vvmlsvfgln lsgtqdsapk lrkgfmerfs llrvvkqyln
      301 elslasrskq wskalyqaqg dggwsrfags ltltlviffl lfpevvviim sfssdatlqf
      361 ppsgfslqwy gsffgdeawy gaawasikig lavaalstvl gtlaayglsr iasdirgwlt
      421 mvilapitip vivvgvasyf glvnlgiigt etgivlahti gaisyvvviv satlanfdrr
      481 leqaaksmga rpftafmrvt lplirpgiig galfafihsf devvvtslvs gysvrtlplk
      541 mwenirneid ptvaavasll tllpilwmia lyvtwwrars ssqnmvieat a
//
LOCUS       WP_457660542             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660542
VERSION     WP_457660542.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44154
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          327..403
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 makralilie gsrgngplyv qaaqrlglhp itlaadpaqy dylaaenses irvdtadlda
       61 lihkcsqlga tydivgitgf tgldesgyvt ivklcqhfgl pgpnlaaieq csdkytqrkl
      121 laaagipipa yrlaanatev esaaaeiglp vivkpaegsg stgvrlcrda devaehtkyl
      181 lsgahvwrss prilveefaq gsfysadamg ntviavgasd fnrpphfvpc esmfpapltd
      241 eeyiiiadvs lsclralglg wgpaniefrw tkrgpvviev narlpgwttp rlihlaygvd
      301 lvtehiklii geecnlrarh shtaaarflv adrngtldri egtnlaaavp gvvdvrfyve
      361 pkapivrkgd yrdmighvia aspsgtqtka ilqravdlis wsitpfptld e
//
LOCUS       WP_457660543             408 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660543
VERSION     WP_457660543.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 408)
  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   4  (residues 1 to 408)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..408
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44016
     Region          57..310
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          324..400
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mpkkalille gtenngplfl qsaqrlglhp itlsadptqy eylaaedses irvdtadlda
       61 lihkcsqlsa tydiagitsa reevyataak lcqhfglpgp nptsielcln kftqrqllae
      121 agvpipayrl aanateaksa aaemglpviv kpaegsgstg vrlcrdadev aehtkyllsg
      181 ahvwrsspri lveefaqgpy fgahtmgnev igieagdfgp lphfvyreyt ypalltdheh
      241 khiadvslsc lralslgwgp adiefrwtkr gpvvievnpr iagaadpqlv qlasgvdlvt
      301 ehiklvigek cdlrsthsht aatrflvadh dgildriegt slaaavpgva evkvylepkt
      361 pivrkgdyrd cigyviatsp crtqtaailq ravdliswsi tpfptlde
//
LOCUS       WP_457660546             393 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660546
VERSION     WP_457660546.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  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 393)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42010
     Region          15..390
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mtsltnnlls ktecdavlel rhamhrepel snnewktqkr iiealeafgl agaktfhntg
       61 vyidiegtas gpgrsvvlrg didalpihee rddlpyksev pgvmhacghd vhgsialgta
      121 lafhrmrpnf sgkariifqp aeeaeplggr svaeaelldg fdlavglhvh tdipagsyga
      181 ragavtkssd qfevefigim ahgakpnagv daisiaaafi nevqkvvsre mpvddgaiit
      241 igtihggeat niicpsvtvt gtirtssser rtllvrrvge iadgvasmhr grarfsslag
      301 eppiindsdm vdrfrdtvik vagedkfvqp passgsddfg yysdllpsiy fwigsqepgn
      361 dtgvhtptfg asdkivipat elavqycldl ire
//
LOCUS       WP_457660548             128 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660548
VERSION     WP_457660548.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..128
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=14099
     Region          19..120
                     /region_name="Ser_Recombinase"
                     /note="Serine Recombinase family, catalytic domain; a DNA
                     binding domain may be present either N- or C-terminal to
                     the catalytic domain. These enzymes perform site-specific
                     recombination of DNA molecules by a concerted, four-strand
                     cleavage and rejoining...; cd00338"
                     /db_xref="CDD:238206"
ORIGIN      
        1 mfgslrrirs ctiakqrlqy amrerlaalg wshietvddd lgrsaaggva ragfdrmvae
       61 vclgkvgava arevsrfarn srdwqqliem crvvdtvlid qeavyaprqg ndrlllglkg
      121 kfrgnppp
//
LOCUS       WP_457660554             294 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660554
VERSION     WP_457660554.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..294
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32422
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlqkgplhsh iierfddmse qlqqaarhil ehpqevalvs mrelarnagv qpstmtrlak
       61 flgfpgyedf rvqhadvirv nadgfaaram qrdeagande glahrmlqsi saqiarlcep
      121 etlsrlndla vrlatarrvy vlglrschsv awhfhyvmtl lgertihlds pagtggdali
      181 rattddvlla vsinpysryt levaeaaiek glsvlaitds evsplfmiae havlfptesh
      241 tffhtltpal aisevlcgll asqdrkvalk elkrvdgyls smntysasip rrki
//
LOCUS       WP_457660555             220 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660555
VERSION     WP_457660555.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 220)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..220
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24449
     Region          17..>216
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mrkelhfelt efhtrlaavk nemarrgidi lllseppnqn yltgynaysf ytpqmvivaq
       61 dhdepiwvgr fmdrvsatmt tylaednira ypdtyvqsaa lsaydfmaei vkelggnnar
      121 igvemggyyy parghvdltr alpdaefvda dllvawirlv kspaevaimr qagqladvam
      181 krvvdmvvag vrecdiaati yhqqvsgtae fggdypccpp
//
LOCUS       WP_457660556             250 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660556
VERSION     WP_457660556.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 250)
  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 10099437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..250
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27697
     Region          16..>140
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cd01066"
                     /db_xref="CDD:238514"
ORIGIN      
        1 mnatsrrqsi inkcparqns gatipvappd lcigersiap haawtddrlp dstvvnlels
       61 gcrhryqvnl artivvgkps psfqdlseia iealnvglea vspgrtcsev esdfrqalar
      121 hgiekesrig yptgigfppc lgrthckhsq grrnspqtrh gfphdarlva rqrrdhhhte
      181 lcglrlwlra sdddpaktvr qitsvlkmne rindldfcep kssrrfprfp vafpglpnss
      241 iahlnevntl
//
LOCUS       WP_457660559             154 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660559
VERSION     WP_457660559.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17450
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meldradivl lgavqennrl tseelaeran lsptacqrrl krlraegvie advsivspka
       61 vgrqvtvvvl vslereradi idrfksairk trevmigyyv tgdadfllvv takdmedyeq
      121 ftrrffyenn dikgfktmvv mdrvkagfvf pies
//
LOCUS       WP_457660565             470 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457660565
VERSION     WP_457660565.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..470
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51505
     Region          8..470
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mqvssagfle svdqnfrham sflalpegla eritqcnsty tvrfgvrlrg rmysfigwrs
       61 vhsehcepvk ggiryasnad aeevealaal mtlkcslvdv pfggskgalk idprewtpqe
      121 leritrrftq elnkrgligp gvnvpapdig tgeremawmm defrranptd vvnaracvtg
      181 kplskggiag rteatgrgvq faiqsflrdt rtvgldgrrd lkgasvivqg fgnvgyhaak
      241 flseedgarv tvvaerdgyv anpeglaiee lkqhqirtgs ilgfeggtsf agemtgieqp
      301 cdvlipaame naihvenaer ikahlvveaa ngpvsfeadk ilrsrgvtll pdlyvnaggv
      361 vvsyfewvkn lthipfglme rrrrerrnqt iatalermtg kefpadirde fleggaeidl
      421 vrsgledvmr stwarigdlm akqpelgdyr taayvasirq iaeayeaigi
//
LOCUS       WP_457660567             324 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660567
VERSION     WP_457660567.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..324
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35797
     Region          105..322
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mlyqdtvete vlvhkpsviv sifvvvlaaf lmfnltdttf gelmrlvige plqsgfygrf
       61 aiafviavmf clnlvligfa alrlqiaivw lellllflgf vksfnlnlpf isenlpylit
      121 qgvmttiyvs tvslifasli aiiaaiakls sngfaygias fytsffrglp llmqiyliyl
      181 glpqlgivid avpsgilals vcagaymtei fragiqsidr gqweasrsmg fgfgltmrki
      241 ilpqafpvii ppmgnefiam lknsslvsvl gvweltflar tlgqptfnhm emlisasiiy
      301 wilsaclevi qsrlerhfsr skvr
//
LOCUS       WP_457660569             321 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660569
VERSION     WP_457660569.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..321
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35669
     Region          16..312
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mgfmmrpyee rfiwrldwnl lrtftvvvek ggitraaefl tlsqptvssa lkrledtlek
       61 rlldrrpghf altpagetly rescllflav srlpgllaaa esvvtghiti amtshvvcph
      121 fdevlaqfnh efpevtysia itdsaevlsr vkqnqatlgl clmrdadpll essvlfreff
      181 glfcgpshpl fgikgiapaa lsgepsvsfq teiengplyl vrqlrervnl qseprgvsan
      241 lpevrrmivn glgigalpvh varrdvdagl lwqlppwdel aqidihlvvn prrslnpaes
      301 afitalqeli aetpfndrty s
//
LOCUS       WP_457660573             436 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate aminotransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660573
VERSION     WP_457660573.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Kafala,B. and Sasarman,A.
  TITLE     Isolation of the Staphylococcus aureus hemCDBL gene cluster coding
            for early steps in heme biosynthesis
  JOURNAL   Gene 199 (1-2), 231-239 (1997)
   PUBMED   9358061
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..436
                     /product="aspartate aminotransferase family protein"
                     /EC_number="5.4.3.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46444
     Region          27..430
                     /region_name="HemL"
                     /note="Glutamate-1-semialdehyde aminotransferase [Coenzyme
                     transport and metabolism]; COG0001"
                     /db_xref="CDD:439772"
ORIGIN      
        1 mtpqspahqn ssldaallec reryaakrpq saalnreaik vlpggntrtv layapfptam
       61 argegcrlwd vddntyldlc geytaglfgh sdsriraalh dalarglsla avgeaeqrfa
      121 rilcsrfrsi dmirftnsgt eanlialsva qvvtgrsrii afrggyhgsl lyypatgssp
      181 itapfpvtlc dyndtdgtva airsaagela avivepmlgs ggciaaeptf laaiaeaarg
      241 vgaisifdev mtsrmseggl qerlgilpdm ttlgkyiggg msfgafggrr dimelfvskv
      301 phagtfnnnv msmaagitam gevftaaeaa dlfalgeglr delnvmsdka gaplqfcglg
      361 slatahfrrd qinrpyaitp reealkelff fdmlnagvyi arrgmtalsl ptterdlvqf
      421 ktavsdflda rapllr
//
LOCUS       WP_457660574             414 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660574
VERSION     WP_457660574.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..414
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45302
     Region          63..408
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtvskqwfaa stsaevndas glpgakshqp tpdqlefgaa erfsaiddrr ekatmlqaka
       61 qvlvsnlvrv dgapgatayi iapkldleig vaagliekse geplttahpv rissvtkpfv
      121 aaailrlwem gkielalsid sylpadhisi lksggydakv itvrhllsht aglrdvfhtg
      181 afaqmlpklm sgqvrhcftl eeqlkmameg gprfppgdaf eysdtgylll gailekvtgn
      241 smaaatrelv sfdrlgltst wwevlevere gvftrahqye yacgwdsyde dpphdlfggg
      301 gmistprdla tffhalfhgq vferpetihv misvaktttp rnqnddlygh gpqihsvgdl
      361 taythggwwg ldvgyvpeld mtlsvvglrr dirprysvaf delileaarl hikl
//
LOCUS       WP_457660577             357 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660577
VERSION     WP_457660577.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..357
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40884
     Region          108..337
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfrylarrhd rkhifrslqr qkrtdrrsie fgfdtrlafa vneaediyas sgelafrkis
       61 eaelffspil ppeplkeeqn svtfqsditt adeenntfec vvtdsglkdh alvvfhhwya
      121 rnryhsfskf faakgitvie atlpyhfsrg syeyseeqff nanigrtvrs irqavldgrk
      181 ivrwlhsrgy nkisvvgmcl ggtvagliaa qeekvdkavl mvspgspadl vwtaetmksl
      241 rdriervmsl edlrvawgli nlemhlfglt rpqldmmfvl geddtitrpa asdrviellt
      301 kcnrspevlr lncghssvgi fpyniiaark vlrflketpt laelwdirgf rydfsev
//
LOCUS       WP_457660581             230 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660581
VERSION     WP_457660581.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..230
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23908
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgfaan sftsvsldpp lllvcvarta
       61 rdystmtaae hfainilsea qkdvsiqfac paedrfaavd wargpngcpi faqvaawfec
      121 smhdvieagd hvmmvgrvta fkssglnglg yarggyfaps vaakanssaa ggeigavavl
      181 erhaalfplg ddnlslrscs agggdpaktl asqleqlgls vhdwfslldl
//
LOCUS       WP_457660583             412 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Sinorhizobium
            medicae].
ACCESSION   WP_457660583
VERSION     WP_457660583.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46269
     Region          18..399
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtanptsirq lldrrlsgfs leqpfyvspe vyaldlehif ymewlyavpa cqlaktgsyv
       61 tlrvgayevv ivrgrdgevr afhnscrhrg slickarqgq vaklvcpyhq wtyeldgkli
      121 wandmgpdfh askyglkpvn lrsldgliyi clsdtppdfq tfaqlarpyl evhdlkdakv
      181 aftstiiekg nwklvwennr ecyhcssnhp alcrsfpldp evagvqadgg vseklqahfd
      241 lceaagtpaq fvlagdgqyr larmplqeka lsytmdgkaa vsrhlgrvap pdagtllmfh
      301 ypstwnhflp dhsltfrvmp isptetevtt twlvhkdave gvdydlkrlt evwiatnded
      361 reivetnqqg ilspayvpgp yspgqesgvm qfvdwyaawl ervlaprqva ae
//
LOCUS       WP_457660585             241 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Sinorhizobium
            medicae].
ACCESSION   WP_457660585
VERSION     WP_457660585.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..241
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25708
     Region          21..197
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mdnqhraggy dslrinrdgq aeafdaigah ydeafpnkqg qvlagdwlir slptgarvld
       61 lgcgtgvpta rqlvasgfev vgidlsggmv klarecvpga tfhqmdiadl rpggprelgq
      121 fnavaaffsl lmlpraeipl alltirnllv pgglfalsmv eadvddfsip flgnnirvsg
      181 ylredlraii aeagfqivee tsysyatavg vppeeqiflc crkgfsrsgs mrissvgksa
      241 m
//
LOCUS       WP_457660593             696 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660593
VERSION     WP_457660593.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..696
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=77487
     Region          12..421
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mntkitpdhl graavvyvrq stmtqvtgnl esqrrqydla gaaattgfas vsvidddlgr
       61 sssgsmerpg ferlvaqvcs gnvgavycie asrlarngrd whhlidlcal agtlvidpdg
      121 aydprlvndr lllglkgtms eyelslmrqr gnaardskag rgelrfmlpp glcwsevgki
      181 eidpdehvae tirlvfakfr elgsgrqvfl wlrsadikmp vvlrnvdvck lvwkapayhs
      241 vmqilhnply agayafgrra qrtrivdgra rkatgvrkpr dewsvllrdn hqgyiswrey
      301 eenhkllten ahmkkncdrk sarggrallt glmrcgrcgr mmrvfygsak gnahryqcrg
      361 ddahvgvglc igiggvrvdr avamqileav sdraveaaif asdqversrr dviaaierdl
      421 egaryealla srryelvdpa krhvarelea rwndalervg vlerkikdls alsaarpvid
      481 rgrllqlaqd lptvwnapst etrtkqrlih ilvqeiicdl ddatneavll ihwtggrhte
      541 vrvarvktgr ypaelapsav ealrklgghw pdrelavsln rmlcktgdge swttvrvrdm
      601 rerlgipeyd atkvdvpmis lmkaaeklgi cvgsakslvq rgilpatqil pgspwmvpve
      661 alsseavrig vqgvvdrrpk fyedyqydkv vrlpgi
//
LOCUS       WP_457660599             429 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457660599
VERSION     WP_457660599.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..429
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48452
     Region          39..389
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdniiaassi tiqerrsaeg ldahvpmilr dgalydpdld rffrdlplng vrsrhslray
       61 gydvlvwvrf lseacaktvw qadrhdvlay hrvrrraeag qrisaaswnr avaclerlyr
      121 wgvhekliae apfthqsawr qgyagrraqi aarndayeps arradvsfvt lddyrifrdv
      181 glrgllpdgg tragardrng irnalfsdll vttglrleea sflfasdlsf tdqqpgrqvw
      241 ldlpdaltkg drgrqilipa rlleqvrayi rvervhavak fqgrsgwrsf drpilvhrer
      301 snsrlrprdg gdialdllsp eergriiica ddgtpeepav lwlseiglpv qtnswevifa
      361 rasercrsfg fdvnisphql rhtfavhmla mliqhrlrda alpagpmedt grfsailfsr
      421 sngslvmpt
//
LOCUS       WP_457660610             211 aa            linear   BCT 27-JAN-2026
DEFINITION  NYN domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660610
VERSION     WP_457660610.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..211
                     /product="NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22215
     Region          10..115
                     /region_name="PIN_LabA-like_N_1"
                     /note="uncharacterized subfamily of N-terminal LabA-like
                     PIN domains; cd11297"
                     /db_xref="CDD:350237"
ORIGIN      
        1 masdtlalla kivtgllaei anygvatvkr ingdctgpnl kgwkdclleh siqrvqqfay
       61 ttgknatdga miieamdlly tgrfsgfciv ssdsdfarla arlreqgvtv cgigerktph
      121 pfvtacdfdv lsgaapeaea pvapqrtvrk pvaaaetaap iarpapakpa ldraaldmla
      181 kavtgsaded prqprrrrra pgqtgsglrc p
//
LOCUS       WP_457660617             264 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660617
VERSION     WP_457660617.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27630
     Region          14..262
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mttentgvrr smnlhsklal vvggygaigt sisemlavag atsviagrng drarelaral
       61 tekglaaegv evdachagav relsaslaqr hgsidilvnc igfnkeqkll evteeafdev
      121 ysrtlragmf laqavashqi afgrggsqih ilsvrsslgf rdrgysafca akgglaillk
      181 qhatelapyg itvngvapgm vrtykntkal qdaeifqrav sdvplarlat pndvagavhf
      241 fasplsrfvt gqilyvdggl tasa
//
LOCUS       WP_457660618             377 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660618
VERSION     WP_457660618.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..377
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40919
     Region          <15..344
                     /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 metnldqgdc gplveqpisl irstpptpqw lgealievlr diensgniat llryhtfsgs
       61 eadrstaslw leerfgqrvd pgriivtngt qsalfltlrt vvgagnhilt edlsyygfrr
      121 laallgitat gvamdangai peafdkacrq hppraiflqp tlhnptaiim sterrkalae
      181 varrhgvaii eddvygslps lapppvaaia peltwfatgp akcmgpglri gylvapseee
      241 akhatsafdt istwhtnpls aaimerwvan gtlmrvrnav raeiaerqki arkqlagldf
      301 sthpesvylw lalptgldqe allssllkkg vvlrsgemfl vdpkrragrv rvvvgspetr
      361 telqtalsii rselspa
//
LOCUS       WP_457660622             277 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660622
VERSION     WP_457660622.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 277)
  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 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..277
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30685
     Region          7..276
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 msdllpcdth vhlfpskhev pvpanrhpea aatindlrkv aephgvarfv ltqpsflgfd
       61 nsiilstiaa dpdrlrgviw mepstppkql hdlpakgvag lrfplmfptg qgaplalaaa
      121 ppdwsacrel lqeaqriglh velgmeghll qqaveeispt gvniviahfg mfdrtlgpda
      181 detfrfllea arsghvwfkl sqsyrsqpgf igrafellle aagperlvwg sdwphvgnrl
      241 drlktypsav qwiekmisds slrrqiwcln pailyny
//
LOCUS       WP_457660619             157 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457660619
VERSION     WP_457660619.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17354
     Region          <43..143
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 msiidvepvs epvilrlvgr sagetlrnvv lrskdtawla dcdmdsdhfh vaascgrdvi
       61 stasfmrenl ediiaqeagm hwrlraiate plyrsqgigg rvlefgiaei mkrggalvwc
      121 ngrvsaegfy rrhgfepfgp afenpgtglh lrfvrri
//
LOCUS       WP_457660609             349 aa            linear   BCT 27-JAN-2026
DEFINITION  Shedu immune nuclease family protein [Sinorhizobium medicae].
ACCESSION   WP_457660609
VERSION     WP_457660609.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Doron,S., Melamed,S., Ofir,G., Leavitt,A., Lopatina,A., Keren,M.,
            Amitai,G. and Sorek,R.
  TITLE     Systematic discovery of antiphage defense systems in the microbial
            pangenome
  JOURNAL   Science 359 (6379) (2018)
   PUBMED   29371424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10624091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..349
                     /product="Shedu immune nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39702
     Region          163..322
                     /region_name="DUF4263"
                     /note="Domain of unknown function (DUF4263); pfam14082"
                     /db_xref="CDD:433703"
ORIGIN      
        1 msfdrfaaps qaltvsplwl fmakaekgtq lyappeyvlg ikrfhalkre ltrianrfrr
       61 earnekqdri ydallhsadr erfprkdrkl kpdaisqltq gyatdagisk rdrrtavrlv
      121 rqsvdtlakd ephallalks eielvtlkgl idrfnemltk elpesrwqaf lrdnpfilsm
      181 afsapaimiq enayvggkrf ngsngkfadf lmatastgnl alieikrpqt nlltqsayrg
      241 tdvygpsael ngaiyqvldq rfrlhknlpl fkdeterndi hahavrcivi agtsaqethl
      301 kksfeiirna fsevtiitfd elrsrlteih nalssppket varpwrddf
//
LOCUS       WP_457660624             196 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660624
VERSION     WP_457660624.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..196
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22135
     Region          1..>158
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mklasfnvhy cvgkdgrydp yriaelmrdi divglqevev nwdrsgnsdq paalaaalph
       61 hftawgpgvd mlktsdeplt ptsarrrqfg nmilskypil tvrnlylprr gavdalyfqr
      121 salevvvdtp ngamrvycth lcnlstnrri dqlsylldmc ananregsmf vgrhrdlsws
      181 segdapkppr rrrdpr
//
LOCUS       WP_457660626             371 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660626
VERSION     WP_457660626.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..371
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40005
     Region          <40..371
                     /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 msihvqaqnr epislirttp ptpnwmgkav setlleisgr enldtllryh rfagteadrl
       61 agagwlakrf gqapdidgvi vtngtqnall ialvnavgsg gllltenlsy yglrriagfl
      121 nidvkgiemd engalpdafe eacrtlrpka lfltptvhnp ttmimsldrr laladvarry
      181 gisiieddvy gllpneappp iaalapdvtw yaaglakcva pglkiayllp psveaaaaaf
      241 drfqvtstwh vaplsalvaq swikdgtadr ilravrdeas arqsiarslf anatyvskpe
      301 slhmwltlps rwtqasfiaa aahvgvvlrp gsmfaldeek apnairivvg spetrsalee
      361 altvlkplve e
//
LOCUS       WP_457660628             319 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660628
VERSION     WP_457660628.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..319
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34702
     Region          19..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mgdvmslpnr kreargrgas pasangrstr lsdmiaawtl agpalflliv lfflpvlavf
       61 vialtdwqfg astlsfvgla nfeevfadrg fraslfntva yvaivvpgti vlglgvalli
      121 esgksfrafy raihflpyma tlaamsiawe allhptiglv nqtlaglglp tanwlrdett
      181 vlpvlaaigi wqnlgfamvl flaglksipq dlyyaaevdg adlwldrlrt vtlpmlgpvf
      241 mfvfivvalk afetfdtvhv ltqggpghas emlmftlyre sfeffrtgyg aavtvvflli
      301 avaltlfqas fmdkkvhyq
//
LOCUS       WP_457660629             506 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660629
VERSION     WP_457660629.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..506
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54031
     Region          2..434
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mkfliasfdg lrpdliskel tpniarvqel gvtlarhntv ypsetraafp slvtgaapvr
       61 hgmvgnkfvd rkstperyid tsdavlldrl nkesggrlmt aptlgellaa sgkslavlat
      121 ntpgttrlfh hkaedfghir lsghfpeact padalaqiei efefgklppa paigqpdfsg
      181 qewitsvfln yvwprlspdv ailsygepdt tshfhgtgsa ttreiiaycd aqfgrvleww
      241 eaegrsagiq lmlasdhghi tahtrvsvmd dlraagfapg rapdpdvdvv vvpgqvgaly
      301 lrdrsvdqvs rlveammdqp wcgpiftspr nevegiapgs fasslvlcdh drapdvyfaf
      361 raddgldqfg laggtfydnd riaglgvhgg lhakelaavg ivagshfrgd gsvsaipsgi
      421 cdlaptilhg lelavpstmt gralrevlas atqdslephv eteefeaglg sfrqtlrrnv
      481 idgtvylvgg aasndatatr kleaae
//
LOCUS       WP_457660630             412 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Sinorhizobium
            medicae].
ACCESSION   WP_457660630
VERSION     WP_457660630.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44382
     Region          1..395
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,235,237..238,246)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,244..246,275,278)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mtliskrlaa vrpsatkamt araaalreeg ndvvtlsqge pdfdtpdnvq laginairng
       61 ktrytavagv kplreaiqhk lqrdngleyd ideitvgcga kqvvfnalfa sldprdevii
      121 ptpcwvsypd mvrlaggepv lveaaerhgf klrpaeleaa itprtkwlml nspnnptgav
      181 yskaelaala evlrrhahvh vlsddiyekl vydvpfatma saapdlceri ltingvskst
      241 amtgwrvgyg agpkalikam ntvqgqtssh tssisqyaai eaiggpqdyl dafvaelkkr
      301 rdlvvdrvrq mpglrcrvpe gafyvfisca gvlgkltasg kviesdmdfa mylledfgva
      361 vvpgsgfmas pyirisyass veeleracsr ilaacvalse gvqtheqvka ia
//
LOCUS       WP_457660632             376 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660632
VERSION     WP_457660632.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40839
     Region          14..369
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maintrpmcs lsaggvvgas iayglaaega rvgildaeds dfsasrgnfg misisnkgfn
       61 nlayfrlsya ssrlwpefas tlreqtgidp afdlkgkiyl svgdaefaah tekvaeyarr
      121 vgadyrhdil nqadlqhmlg kvrlgervag gsfspldgla eplrlysgll naiqrhggwi
      181 lrdhrvdrie hqggmftahg qwgsfsaprl viaaglgtpd lasqvgisvk vrpqrgqmmv
      241 terveqsfpy pisgllrqnp egtimigvst eevgyddrtt vsvlkslark averlpalrs
      301 vqinrcwaal rprtedgypv yqesreypga fvitchsgit laalherllp kwilggrkda
      361 llepfglgrl qnasaa
//
LOCUS       WP_457660634             946 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660634
VERSION     WP_457660634.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..946
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=103120
     Region          36..472
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          525..944
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mshkmecsaa wrflatvala sfassafadt sstswpqtqs dikadtdvhf gtlangmrfa
       61 imrnatppgq aairfrigsg sldendnqqg lahvlehmaf kgsthvaegd iirilqrkgl
      121 afgpdinast sydetaytld lpevdadtis tglmlmreta seltldasaf drergvilse
      181 erlrdtpqyr asleimnsll agqratmrap igkadiisna pvdlvrdyyr anyrpdratl
      241 ivvgdidpaa meveirqrfg dwkavgpapt kadlgapvtk gesaevivvp ggmtsiqiaw
      301 trpydaapdt fakrraelie nlglrvlnrr vstiaskada pfisadvgsq dlldsahvvl
      361 vaansepdkw qaaltaidqe qhriqefgva qaeidreire yrsalqaaaa gaatrmttdi
      421 asmlarsvdd dqvftspaed lsmfetmmng vtadevnral qrafsgngpq vvlqadqspe
      481 ggadtvrqvy dasnaiavsa psgatdvawp ythfgepgav verravedlg ltmvrfsngi
      541 rltvkptrlr vnevlvredi grgrldlphd rsaaiwaapa vvlsgvkamd yqdiqkalta
      601 nifsvdfsvg dssfrfdght rtedlatqlq lmtaytsdpa yrpeafkrvq qaylsgldqn
      661 daspggvvsr dfaglvhsgd prwtfpdraq lsaakpdefe alfrpmvsng piditivgdv
      721 tvddairlta etfgalpprp etassndrdd vhfpattekp vlqthsgrad naaaavgasi
      781 gdllsdlprs ftaniatqif qnrlidqfri aegasyaprg evdlsrevpg ygyayfyaet
      841 dpakvarfya lvdeiandlr shevsedela rarepivetl khqqqsngyw ieylhhaqtd
      901 srrldrirdn lsgygkvtag dirafaatyf spekfwkfev lpaavr
//
LOCUS       WP_457660639             376 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457660639
VERSION     WP_457660639.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39383
     Region          5..373
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(15..16,19..20,23,55,105..106,108..110,113,132,
                     135..136,139,207,210..211,214..216,219,247,251,301..302,
                     306,310,326,329..330,333..334,337)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mitpwrsiaa gflingvlfg twaghiarvk dqfglsdqnl sklllllglg allsfsfagr
       61 lcdsmgapri traaacallv atvflgfaqt vqqlglslfl fgmchglldv ainkwgseve
      121 khmersvmss fhamfslgag lgaangyvaa vyhdqmntdf litavltggi lgpfllldwq
      181 stvlknvkga velalprgal llvgliafss glgegmvahw gsvhlkqvfk tmeesailgy
      241 vvfcaamvsi rltvdslvtr lgpvmvtrls gvsatcgisl vlagsseplv slvgfvlmgv
      301 gyaaimplaf kwaatyhvvp pgqaiatvat faygamtlgp pafgwlseal spkygmcivg
      361 ifamlvavla palehk
//
LOCUS       WP_457660641             252 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660641
VERSION     WP_457660641.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..252
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28641
     Region          81..245
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mtteseagna fsifihqmle etsidhmven vslfarrfnc ssisygpqph vqtvqresri
       61 klptlltypk ewqehcfksg ydrlapglrv spfqsspilw dqaykdpntt drerrifdea
      121 kefglqtgvt iplrgrlddf pimsfvqset sglskfavsw ltsaaflfhd rvegrvelka
      181 dvpsltarek ecltwvrqgk sswaigtile isphtvdfhi khaksklgae nrrvaameae
      241 rlglikpkfw ll
//
LOCUS       WP_457660640             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660640
VERSION     WP_457660640.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44295
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          327..403
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 maskalilie ghrsigplyv raaqrrglnp itmstdptqy dylaaegvea vqvntndlda
       61 mksvysrlkl thdiagltgf sgldesvyvt vgklcrhfgl pgpdpasikq chdkftqrql
      121 ledaglpipd yrvatnatev esavaeiglp vvikpvvgsg ssgvqmcrtv devaehtrhl
      181 lggghmwqar pqilveefaq gqyltadmmg gclvgigtgh fgppphfvyr eysypallsn
      241 desariadvs lsclralglg wgpaniefrw tkrgpvviev nprlagtpdp eliqlaygvd
      301 lvdehiklvi geecdlrarh srtasarflv pdrdgmlevi egagraaalp gvaevkmyvh
      361 pntpivrkgd yrdlighvia asptrdqtaa llqqavnlvs wtitpfgpkg g
//
LOCUS       WP_457660643             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660643
VERSION     WP_457660643.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44212
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          327..399
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 matkalilie ghrsngilyl rkakrlglnp itlsanpaqy dylaaegtda isvdtsdlea
       61 lirvcsrlga thglagitgf agvdeslyvt vgklcqhfnl pgpnpasieq csdkftqrql
      121 laqagvpmpe yrlaanamev esaageiglp vivkpavggg sigvrlcrda kelaehatql
      181 lsgtppsqss prilveefae gtfyetttmg daviadgsan fhhpphfvpc esmfpavlty
      241 derkriadis lsclralgld wgpanielrw tnrgpvviev nprlpgwtip wliqlaygvd
      301 iikehiklii gdecdlrakr sntaaarflv pdrdgilgrn egtslaaavp gvvdvrfyie
      361 pgtsivrkgd yrdmighvia aspshaltea ilqravgsii wpitpfprfn k
//
LOCUS       WP_457660648             399 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457660648
VERSION     WP_457660648.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..399
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40996
     Region          16..396
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,66,121..122,124..126,129,149,
                     152..153,156,230,233..234,237..239,242,267,271,324..325,
                     329,333,349,352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mqqqysyrsl lqipglfpli laailarlag rmfiltlvlf vlahfsspsl agwltfgaia
       61 pgliaspaag vlldrmgpti avridliasa vfiaaisfag wvgyfsppvl filvmlfsmt
      121 gplgaagtrt llprlvppga lgqanaldta vyaivdvvgp amagvivawf gpeiamsmia
      181 aaytgaaicl crvqclpgla stntpflrqt vegiqmvarh ptlrglavsy slyeitwgvl
      241 nvavpvfvag rcatgcsslt gllwaamgia ggvgalfagh mritgrerrv maagmvvtaf
      301 aawpvaaefg fgglilgltl agmvsglisv avltlrqrrt epqqlgrvms ismslntagf
      361 plgsaiagta iseslsssfv lagiasvvaa aatlfipad
//
LOCUS       WP_457660649             331 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanine--D-alanine ligase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660649
VERSION     WP_457660649.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12229933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..331
                     /product="D-alanine--D-alanine ligase family protein"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008716 - D-alanine-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=36403
     Region          1..321
                     /region_name="DdlA"
                     /note="D-alanine-D-alanine ligase or related ATP-grasp
                     enzyme [Cell wall/membrane/envelope biogenesis, General
                     function prediction only]; COG1181"
                     /db_xref="CDD:440794"
ORIGIN      
        1 mrvaivsnyd yagvinrfgq pcpeqyrsde mvgrvvaalq egghetllce gdkglltale
       61 rfmppdpeac psgivfnlae giqgeyryth vpamlemagv pytgssllgh gltndklvtk
      121 rlirdygvpt pnfrvmrsgt estgdlrfpv vvkprveecs lglqlvhepa qlrraveaiv
      181 sqysqdalve eyidgreici allgneemev lplveqdfgg ratrlmtwea kysaapvpki
      241 cpaqigsgle tvlrdisiat fracmcrdya rvdvridrag rpfvleinsm pglathssyv
      301 qaaraagytf pslvnrilnv ahkryfgidm s
//
LOCUS       WP_457660656             405 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457660656
VERSION     WP_457660656.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..405
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44419
     Region          77..382
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlrhvdfepg kpefvadvsr ggvqvppnpe aagslgghgp lirpifdenc katrlaehdr
       61 avdgmcagki fdgfavlapl lesyfrrrlt kqrnatpatv asyrdalrml ilfaaarlrk
      121 kpaalaledl drdlvlafld eleekrnnav atrnarlaai rsffhhvaaa dpasfgvaqr
      181 vltipikrah ievthhltka evdaliaapn prtsrgrrdr tfllflartg arvseatgvn
      241 andlqlersh pqvllrgkgr rdrvipipqd laraltalla ehgianhepr pifigarner
      301 ltrfgathiv rravaqavti rptlaqkpis phifrhslam kllqsgvdll tiqawlghaq
      361 vatthryaaa dvemmrkgle kagvsgdlgv rfrpndavlq llnsi
//
LOCUS       WP_457660658             294 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660658
VERSION     WP_457660658.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..294
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32212
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlqkgplhah iiehfdqmse qlqraarhil ehsqevalvs mrelarnagv qpstmtrlak
       61 flgfsgyeef raqhadvirv nadgfaaram qrdestsnge glairmlqsv svqitrlcep
      121 dalsrlekla drlssarriy vlglrschsv awhfhyvmtl lgektvhldg pagtggdali
      181 ratpddvlla vsinpysrdt levaeaalek gmgvvaitds evsplatiae lsvlfptesh
      241 tffhtltpal aisevlcgll ashdrkaale elkrvdsyls smntycasip rrki
//
LOCUS       WP_457660659             193 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660659
VERSION     WP_457660659.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..193
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20678
     Region          43..176
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msvfgstssp cppfadedwp seiadmrdgf agalnvyram ahhpallkaw aplrqhvvke
       61 salgavrsel vilrathrmd sayewthhvs raralgiadv riqamrgmpg gedgliaqav
      121 dslfanhrls ssilnaldst igteaifdli atvgfystlg filntyetpi dpavaeelka
      181 rplaqaelah gta
//
LOCUS       WP_457660662             297 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660662
VERSION     WP_457660662.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..297
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31733
     Region          13..286
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtdataspss akrnrftaaf kilafdkaas igclivltfc lvalfaplia pfdpteqhil
       61 dslkspnavy wlgtdeygrd lfsrmiygtr palfvgvlsi vvsiaigvpi glvagyrlgw
      121 fdrvigwlid vmlsfpslll almmvtllgs smvtlvavig fsyvpvfvrl trssalvvsn
      181 lefvaasrsf gasdlriiwr hilpnvlgpi ivmgslsiag airdeaslsf lgmgiqppsp
      241 swgnlirdgi gvilqspwva vapglaltls vlafnmmgds lrdmldprdl assgekk
//
LOCUS       WP_457660663             491 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457660663
VERSION     WP_457660663.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 491)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..491
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=52927
     Region          3..480
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 mkvaiagfel esvtflptvt tleefkqaes rgsaiverhr rtntvmggfi dvcerervem
       61 vpivdtsrga agpadeeafl yycdaivegl rahrgaldgv llslhgactt psrldpdgdl
      121 vrlvrkevgp dtpvmlvldy hanldassis datatfgyhy sphidmgdtg rraaeclvkt
      181 lqgeivpvta iarpgvmvps ifsatnlqpl dsfvarsiel pqtvpglldv sifagfsyad
      241 vpncgfsvvv iangdrdlaq rtadelsksi yqsrrelhvp glvrgledgv gyaleralsa
      301 kapivlleha drlndstyvl relirhrarr vavpylwdpd saaaalrage gktvelnlgg
      361 rssprsggpv vvrakilqvg kksysttgpm ghgtkvdlgl talldvdgii vsvttkpdta
      421 idedaflqfg mraqdfsiiv lrskthfrav yeplaeeivi vdtpdwgpad lttlpylhap
      481 iatafpfvdn d
//
LOCUS       WP_457660664             337 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660664
VERSION     WP_457660664.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..337
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36782
     Region          8..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtnkkkplls vrdlsvslai srgggipile svsfdvaegd vlgivgesgc gksltalsil
       61 rllpksavvt sgqilfqgsd llhksesemr atrgndiami fqepmtslnp vltvgeqile
      121 aiiyherttr laarkraiet ldivgipspd rriddyphqm sggmrqrvmi amalatnpkl
      181 liadepttal dvtvqaqile llrklradlg msviiithdl gvisdfadrv mvmysgrvve
      241 esttrdlfdr plhpyteglm rsiphidedv arlhtiegiv pslgewpqgc rfhprcpyst
      301 aackgavpel vgyapdhsva cvryepskqp rsqlasr
//
LOCUS       WP_457660665             329 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660665
VERSION     WP_457660665.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36090
     Region          14..329
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 misnarllnv apcllevrgl vkhfpiakns lfsremavvh avdnisfdir kgetlglvge
       61 sgcgksttsr lvvrlldpta gsihydgedi aslsasklrt rrkdfqiifq dpysslnprm
      121 rvnellsepm aiagfrsaer dsrvyelldm vglarrhasr fphefsggqr qrigiarala
      181 lrpkfvvcde pvsaldvsvq aqivnllkdl qaemgltylf vahdlsvvrh isdrvavmyl
      241 gkivemaaks slfsdplhpy tkalisavph arprspskaa plkgdvpspi tppsgcrfht
      301 rcplavercr leepvlrdvg tqsvachlv
//
LOCUS       WP_457660667             263 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660667
VERSION     WP_457660667.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29898
     Region          1..68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msnsfseklr slcahyrsvs evcrmlglnr qqfdryltgr vrpsqhnlqr iaegfgvevs
       61 elidpareig rparlkvesg rdrmtslidr afpgdlkrlr imlgyyhthf lipsdpdevt
      121 rslvylyeqe grvcsktier tgpheevkei lkyegmatfl gncifllefe tlsadtives
      181 ilypsyrksl diltgltfgm tsqvyrqpfa apiawkylgr tvdlkeqlav cgsykrtdvr
      241 idprirkyln aaglsgtlsl gpm
//
LOCUS       WP_457660668             474 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660668
VERSION     WP_457660668.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 474)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 474)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..474
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51905
     Region          3..454
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 mvvasregst tdstdpgllt ngyqwylaya ftstlteilp dgtvgpalae awdssdaqtw
       61 sfklrksvtf hsgkpmtsad vvasinhhrt kdstsfvapi anqivelnvd glhgvtikla
      121 qpnadfpasl ntvgftiypa sgngvdwqsr dgtggyvlke hepgvrsflt rnpnywrddr
      181 afadeveflt iadatarina lvtgqvnaid avdlktvsml qrqsgitvee nagplhysfp
      241 mrvdldpfkd vnvrlamkha inrqeildki llghgtignd tpigpsyryy dsslaqntyd
      301 pekakfhlkk agmssldidl stseaafaga tdaailfaeq arpasininv irepddgywd
      361 niwlkkpica aywggyptes emlaigyapg apwndtfwse phfeklrlea aaeldaskrk
      421 amyselqtil rddggalifa fansltarnq siahgtvgsr afdgnriaer wwlv
//
LOCUS       WP_457660671             293 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660671
VERSION     WP_457660671.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31306
     Region          25..281
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mkilseypat nlkrssktia vilrratpsa wfgaaiifly vlvaifashi apygetevvs
       61 svpygpwtqq tflgtdqlgr dvfsrlifga rntigislaa tmitfvvgvs lgitaavlgg
      121 svdmvvsriv daimalpqlv vilvmlsvvg ssvfnliili giagatnvfr larsvslnvt
      181 vmdyvedarm rgeslvwivf revlpnilpt lvaefgmrfc fvvltisals flglgiqppt
      241 adwgamvres atlisygdvt pllpaaaiav laigvnfvvd wflhcasglr ddh
//
LOCUS       WP_457660676             246 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660676
VERSION     WP_457660676.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..246
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27474
     Region          5..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msdivieaan vskwygtfra ltdvnltvrk gerivicgps gsgkstlirc fnrleahqag
       61 eitvngmrlh skmrnvtevr knvgmvfqhf nlfphmtvlm ncmaapmwik gvpeaqarkt
      121 alqflervri peqankypaq lsggqqqrva iarslcmeps vmlfdeptss ldpemvaevl
      181 etmsslardg mtmvcvthem gfaravadrv ifmdagqvve eaapdnffnn prhertkffl
      241 sqilkh
//
LOCUS       WP_457660678             392 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660678
VERSION     WP_457660678.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 392)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..392
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40922
     Region          1..391
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrdavivsta rtpigkayrg afnatqgpvl aahamraald ragveggevq dftlgcaltq
       61 gtsginvarh aifaaglpeg vpaatidrqc asglsaiaaa anqirsgdce vvlaggmdsv
      121 slvqntdwng tnyrvptire gyympmlata dliarkyhvn rasqdeyalt sqmrtsaaqe
      181 agrfaheivp vqakqllknr etgeenfvfv tlardecsrp gttseglael tpvmgegstv
      241 tagnssqlsd gasacvlmsa seaasrnitp lgvfrgmltv gcapeemgig palaippllk
      301 rhglsvddid lfeineafaa qlvycrdelg ldpaklnvng gaisighpyg msgarlvgha
      361 llegrrrrar yavvsmcigw gmgaaavlev vs
//
LOCUS       WP_457660680             161 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660680
VERSION     WP_457660680.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 161)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17889
     Region          36..102
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mslmsarglv eitdpefdrp vfrqpgfdgt ltakemdeki sawlkktrea kgisradlah
       61 llglsvsvyg ryergsearl siprlihlce imglmpldvi fdtaphlwgt tleeaedrlt
      121 liklveqlpq dtmrdlirll rrmtpgepaa davatstseg r
//
LOCUS       WP_457660681             144 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660681
VERSION     WP_457660681.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..144
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15721
     Region          <34..87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mlnpnpdkmk gkpepvdvhv grrirmrrir mqvtltalad aigvtfqqvq kyekgtnrvg
       61 asrlqqiada lvapvsyffe dmpgaapvgg dnrsgqkklq peiiefassd vglalirafs
      121 qitdkrvrnr ilglvnalak qdpa
//
LOCUS       WP_457660682             421 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660682
VERSION     WP_457660682.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..421
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45436
     Region          1..344
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 milclafvvl sgcggnpkgv ltpvadsmpa tsrvdmlitt trgrsevpge mftgerarap
       61 afanitvsip pvrkvgevaw pkklpsnpat dfatlkaddl trdgaktwln ttvnkspdrs
      121 vlvfihgfnn rfedsvyrfa qivhdsgiks apvlvtwpsr gsllaygydr estnytrnal
      181 eslfqylaad kevkevsila hsmgnwltle alremairnd glpakfknvm laapdvdvdv
      241 frsqiedmgs qhprftlfvs rddralafsr rvwgdiprlg sidpeadpyk qelanneitv
      301 idltkikagd gmhhgkfaes pevvrligar isegqpltds rmglgdhlia gttgaaaaag
      361 saaglilaap vavidphtrd nyanhfgaam gqldgkqkia vtdcasrpsa erdpacrvpq
      421 n
//
LOCUS       WP_457660687             278 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660687
VERSION     WP_457660687.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 278)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..278
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30221
     Region          12..278
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mksmglstps aivcqalllc tsaiillpfv wmgslsikpp geifrvsfal lpehfygien
       61 ysqaltaapl trymvngllv csailtlqvl vcapcayala klqfrgrdml fglvliglli
      121 phqvlalplf ifgyqigiln tyaalilpfi vspfgiflfr qffkaipddv vhaarldgls
      181 efaivwriil pmalpaviaf sifsvvghwn dlfwpliavr dqdlmppsig ivtfrdaesg
      241 sdygplmaas viviapllic flaaqryfie gltaggvk
//
LOCUS       WP_457660688             216 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660688
VERSION     WP_457660688.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..216
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23578
     Region          <1..200
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mdeplsnlda klrvqmraei kelhkrlgvt fiyvthdqae amtlsdrvav mldgellqva
       61 pprdiyadph drrvaefigs pkinmldgav ierglmatsg aklsvpesia pgtkltvgir
      121 peafslitqp dtpnviegsv hliehmgsdl fvhlrvegmn ealiarlhae raphigsghr
      181 lvvgvkpaqm ilfdetgyrl qtasvsnrvt pireta
//
LOCUS       WP_457660689             412 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660689
VERSION     WP_457660689.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44999
     Region          58..314
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          328..404
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mpknalilie gskmgtgqmy vqaakglglh pitlsadpar ydylatennd airvdtddld
       61 alirecsrlr eiyhiagitg fpnpgeavya tvaklcrhfg lpgpnpesie rccdksaqrq
      121 llaeagvpvp ayrmatnaae iemaaaeigl pvilkpavgn gstgvrlcrg aeelaehmvy
      181 llggtyewqt sprilveefa qgpyfvadim gntiieigag dfgpppnfvy reytypaplt
      241 dyqrariadv slsclralal rwgptniefr wtergpvvie vnprlacspd pqliqlangv
      301 dlvtehiklv ignewdlrkr hwqtatarfl vpdrdgtldr iegadqaadv pgvaeitwyi
      361 kpptpiimkg dsrdcighvi aasptptqts tilqravdsi twsitpfpti de
//
LOCUS       WP_457660696             509 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457660696
VERSION     WP_457660696.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..509
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53959
     Region          4..433
                     /region_name="ASKHA_NBD_FGGY_EcLyxK-like"
                     /note="nucleotide-binding domain (NBD) of Escherichia coli
                     L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar
                     proteins; cd07802"
                     /db_xref="CDD:466805"
ORIGIN      
        1 mgryllglda gntvikavif drdgseiasa aaeghsrmps pghverglde lwqnarrvir
       61 tcideaeida geigaigcag hgnglyaldr dgrpllaiqs ldtraaalvd ewksqgvger
      121 typigrqrpw psqtptllaw lkrhrpevfa slgtvflckd fivnrltgar vsdvsdmtgc
      181 gllnlagrhy daalmaaygl sdsmdllppl vesadiagrl teaaaaetgl aagtpvvggl
      241 fdvvasaigs gvtrtgaasi iagtwsinqv iiegpeldgp vfmsstfdrd rymaiessat
      301 saanlewlvr effsdirceg rspfdlccel asssepasdd plyhpflyga qqdgsaragf
      361 ygiagwhtkg hlvravlegv afghrqhiea irkagadfde ailsgggsrs lvwpqifadv
      421 lgvpvsvars retgalgaai aagtgvgifs dfaegaaamv ktdrhyrpnt arephyarry
      481 alyrdiadam aplwrrlsai eattagaaa
//
LOCUS       WP_457660697             479 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Sinorhizobium medicae].
ACCESSION   WP_457660697
VERSION     WP_457660697.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..479
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=51349
     Region          14..476
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mtavallqwv lasvpeiivv tgacillivg elvrkgrdel llwasvaivl laavatlmla
       61 geirpayagm fisdsfavff klvfylatvl tfflsrkyae iegigrseyy vlllfallgm
      121 mimasaidll siyvglelmv lctyvltgfl rkerrsneaa lkyvilgavs taiflygvsl
      181 iygltgttql drmaeavsgg pldpalllav vfivaglvfk igavpfhmwv pdvyegaptt
      241 itafmsvapk aagfavilrv flnplveasn awiivaaiav atmalgsfva lvqdnfkrll
      301 ayssiahagf aifgvvaggq dgiasvmlyl liyafinlgi fgavimmrng dfsgeviddy
      361 agfakfhpgl allmllylfs lagipptagf fakfyvlval vergfvalav iaallsviaa
      421 yfyirivmvi ymrepertfd paltplvrat laftavgtig iglfpawflr laqqaafgg
//
LOCUS       WP_457660699             333 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660699
VERSION     WP_457660699.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..333
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35398
     Region          2..302
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mhslirthat efsllgvivv isavlffata nflslgnafd llnissvnii favgllvvli
       61 aggidisfav aasvvqygta ialgwigggg wlsgfviaas lgvllgcvna llihrfriis
      121 ivatiatfni yfgllmfftr gvsiydlpdw ltdrvilfer empdgtwiei tlpvlvmiic
      181 vvatwtlitr ttigrqlfaf gdnpegarrf ginigamqfi afgwlglmag igglvqahya
      241 qevvpnalyg reldvlaavv lggarlgggk gtvlgcvlgv llisitqngl nlmgvspfaf
      301 kmiigaiili aitlsntrle rllpfagwkg trr
//
LOCUS       WP_457660700             517 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660700
VERSION     WP_457660700.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 517)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 517)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..517
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56529
     Region          28..501
                     /region_name="PBP2_DppA_like"
                     /note="The substrate-binding component of an ABC-type
                     dipeptide import system contains the type 2 periplasmic
                     binding fold; cd08493"
                     /db_xref="CDD:173858"
     Site            order(393,397,413..416)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:173858"
ORIGIN      
        1 mkrlirsamv laalafagta gaqtppdvlv vgqiaepqsl dphtvtatnd frilvnvydg
       61 lvrfkdgtle vepalaeswe isedgktytf klrqgvkfhd gsdfnaeavk fnfdrmlkkd
      121 hpfygtgpfp lsfnfssvds vnvldehtve fklseafapf lsnlayptgl ivspaavseh
      181 gkeygrspsg tgafkfvewl snqrvvvern pdywdgaakl qavvfrpitd antrvaemma
      241 ggidvmvevp pdnlatfrqd anfavaeqag phvwfailnt kegpfadkrv rqaanyavnk
      301 etlandvlqg tatvaagpip pafnwvessv kpyaydpeqa ksllaeagfe npqvtfyvte
      361 ggsgmldpit mgaaiqadlq avgfkvkiet yewntflgrv npglqgkadm aemawmtndp
      421 dtvpyltlrt dampdkggfn sgyysnpkld ellekarkst dqaergklyg evqsivhdda
      481 pwlfvanwkq navttaavkg felqpsflld lhgvtke
//
LOCUS       WP_457660701             269 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660701
VERSION     WP_457660701.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..269
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27727
     Region          1..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 madfsgktvl vtggagvigk saaklflerg anvvladida gkletaaeal nggervstip
       61 gdlsetetak aavdhavgvy gkldilfnna gisgkvapvh lldvdawddi vkvnlrsmfl
      121 mlkfaasnmv arksgsiinm assmsgwdvl sggagyastk hgvvgltkva aldlaryrir
      181 vnaicpgvie ttlgvpglge dkgssavehf adriplrrig qpadvaevvl flasdaarhv
      241 ngaawlidgg qtlqsfsnap kegvyples
//
LOCUS       WP_457660702             365 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660702
VERSION     WP_457660702.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 365)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..365
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38006
     Region          22..364
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mttnssatks svvpaadrkg ppgwaeglig qllaialslv ggaviilmvg enplhvfatl
       61 lrgafgstdr iagsllqatp iiicgvaaci alrgglfnig vegqlylggf aaawvgfsfa
      121 mppvihvvva vaaailagcl wilipalfra kfgtnevvtt ilanyiavll tsyltisvfk
      181 rpggwsetdp iavtarlpql lpdsrlnigl figiglaigl hlflrhtsag yamgamganp
      241 kfaeyggvrt rrnvflilla sgavgglagg vetlgvhhrf megfapgfgf dgviaallan
      301 gnpigmigta lffgalrags llmevetnas reiitviqaf iilcvsaqil irrrsgrtge
      361 rrwkf
//
LOCUS       WP_457660705             352 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457660705
VERSION     WP_457660705.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..352
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38331
     Region          1..341
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 madlkgalig cgffavnqmh gwrdaegari vaicdrdper lravgdefai trrylsvddl
       61 fadggfdfvd iattvgshrs lvelaarhgi aticqkpiap tmedaeamve acakagvpfm
      121 vhenfrwqsp iraikaaids gtvgevfwgr vsfrsgydvf sgqpylatgk rfiiedlgih
      181 aldvaryifg datavtartr rvnpaiaged vatmlldheg aitsivdcsy atrlpiepfp
      241 etlievdgsk gtlrlsqgyh ltmhskdgtk vtnveppvls waappwhniq esvsriqqhw
      301 vealragrep dtsgldnlet falveasyls aaegrtvsla evigrrpsqf sr
//
LOCUS       WP_457660707             552 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Sinorhizobium medicae].
ACCESSION   WP_457660707
VERSION     WP_457660707.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..552
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60593
     Region          59..480
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(67..68,108,161,163,268,320..321)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(67..68,108,161,163,268,321)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 msfpdadkrk naqgsisidr rslllggtil aaaaaangav avgsakaqeq ssagsgktpn
       61 ilvifgddig ipqisaytmg lmgyrtpnid riaaegaift daygqqscta grasfilgqe
      121 pfrtglltig mpgdphgiqd wmptiadvmk skgyatgqfg knhlgdrdeh lptnhgfdef
      181 fgnlyhlnae eepegyfypk deefrknfgp rgvikssadg kiedtgalnt krmetvdeef
      241 laaakdfidr qakadkpffc wfnstrmhvf thlkpesmgk tgkgihadgm vehdghvgql
      301 lqqlddlgit entivlyttd ngaelalwpd gamtmfhgek gttweggfri pmmvrwpgvv
      361 kpgtqindpv tlmdwmptfa taagipdvke emktgfksgd ktfkvhldgy dltallqgea
      421 eeppreavyy fdqggnlnai rwndwklsfa vnsegniata tretpswani anlrmdpyer
      481 gtkegggame fiarnmwllv piqskikeff qdfdqypyqp gstlnasgin ynllqqqaal
      541 krlgdlerla pr
//
LOCUS       WP_457660708             201 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Sinorhizobium medicae].
ACCESSION   WP_457660708
VERSION     WP_457660708.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (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   4  (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 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..201
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22024
     Region          11..183
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mnqsvepply araiialsea llsleklvva glmgvllali llnvvtrysg hplywvdesa
       61 vyamvwlafi ggsaltrlrl dfsvtlltdy lpaaaarwmr agstllvllf alalaafcwl
      121 wmdpvgifra gfdtkafaae sfnflyters qtlnwpiwai slviplfavt mtvhcaanlv
      181 edlglspqqk rrelssaegv n
//
LOCUS       WP_457660711             837 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660711
VERSION     WP_457660711.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 837)
  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 837)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..837
                     /product="TRAP transporter permease"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89030
     Region          3..693
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
     Region          645..822
                     /region_name="DUF3394"
                     /note="Domain of unknown function (DUF3394); pfam11874"
                     /db_xref="CDD:432151"
ORIGIN      
        1 mtglillcta vawslfqlwy asplpfvfgf gilndteara ihlgfalflt flaypalrss
       61 prdrvpladw vlaalgafag aylfifygdl agrpgqpstl dlvtgtigil llleatrral
      121 glpmvivagv fifytfagqy mpdviqhrga slvkfinhqw lttegvfgia lgvstsfvfl
      181 fvlfgtllek agagnwmmqi siallghlrg gpakvavvss alngvvsgss vsnvvsggif
      241 tiplmkrtgl sgvkagaiea sasingqimp pvmgaaaflm veyvgipyse ivkhallpav
      301 fsyiallymv hlesvkldmq pipqrptpar krwirmglgl tgsvlavcll yygilgiraa
      361 fganapllla iggaalyiat iwyssrypdl elddpnapil elprawdvtr tgldflipia
      421 vllwclmveq lspglsafwa tvtilaivat rkplmaifrk edfassvgaa awdlvdglal
      481 garnmigiav atatagivvg titltglglm mtelvefisg gnvimmlili aaislvlgmg
      541 ipttanyilv atlmapvvve lgsqaglaip liavhlfvfy fgimaditpp vglasfaaaa
      601 iskedpiatg fqgalyslrt ailpfvfifn pailligvdt wahtiwvaai slaaillfsa
      661 atmnwfvtks rlwesavlll acfslfrpdw wvnqisppye elpaseflrt vqeapakari
      721 nfvvqgidlm gddvrktvnv plgepgeplq rlraigltvt pagdslmisn vafgsyakri
      781 gldvgydvva vlkkadqpst aipvsialil tagiaglqfa rkradrsgas lrgtark
//
LOCUS       WP_457660712             449 aa            linear   BCT 27-JAN-2026
DEFINITION  uracil-xanthine permease family protein [Sinorhizobium medicae].
ACCESSION   WP_457660712
VERSION     WP_457660712.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..449
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46269
     Region          2..442
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mtgkkidsid ptdqalpprs lilfglqhvl vmaaspitav flvskalgfs daltvslisa
       61 tflicglgti lqsfgpagfg arlpfimvpg gapiaiflai aqqtdiqtav gaviltagfy
      121 flalpvfrrl lryfppivvg tmlllvsvnl vriyggtitg kqgsegfadp mnvglalati
      181 altvifarif tgtfqrisvm lgliagsmia fgagymdlsg ifdgpviavp allpfgmpkf
      241 difaalpliv fsiismaeat gqtvataeiv grrgdahaiv patirgdava slvgglfgts
      301 liitsgenvg ivratnvksr yvtamagvil vliallapvg rlanalpgpv vggtavivfs
      361 iigvigidll rrvdlrehgp mftlaaalsm gllpilvpgv ysqfpqwsqm ilanglaagt
      421 itavivnaff qhmpsgsaqk aaagveaei
//
LOCUS       WP_457660717             497 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Sinorhizobium medicae].
ACCESSION   WP_457660717
VERSION     WP_457660717.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..497
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52358
     Region          13..488
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mkltftsykr ewfsnirgdv lsgivvalal ipeaigfsvi agvdpkvglf asfaiacvsa
       61 ftggrpgmis aataatavlm vtlvkeygle ylfaatllmg liqiaagflk lgrvmrfvsr
      121 svitgfvnal aimifmaqlp eligvphvty amigaglaii ylfpyvtkav psplvaiaal
      181 taiavwtgmd irtvgdlgel psslpifalp qvpltfetlq ivfpysmgla avgllesllt
      241 aqivddmtdt tsnksqecig qggsniasgl iggmggcami gqsvinvtsg grgrlstfva
      301 galllflilv lddivriipm aalvavmimv sigtfswrsi ldlrrnplps svvmlatvvt
      361 tvgthdlakg vlvgvllsgi ffagkvarlf hvrsildqsg rertyyvdgq iffastegfv
      421 gafdfaepld kvvidvsgah lwditavgal dkvvlkyrrh gvavevigln easahmldrf
      481 avhdkseeag aaltpah
//
LOCUS       WP_457660718             306 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660718
VERSION     WP_457660718.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33622
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="PBP2_LysR_opines_like"
                     /note="The C-terminal substrate-domain of LysR-type
                     transcriptional regulators involved in the catabolism of
                     opines and that of related regulators, contains the type 2
                     periplasmic binding fold; cd08415"
                     /db_xref="CDD:176107"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176107"
ORIGIN      
        1 mgltlrqiev iravmiagti agaarlmnva qpgvsrtmkh iesalgiklf vrkagryvpt
       61 aeardvfaql qevhrkvddl qfsigqlerg rgvelalgsv psianamvpq aiatlmrrhp
      121 dirinfdilr ieeaidylll gkgelvamsy hlshpsitfe plsrghlvci aarehpiaer
      181 tsisareiag hpligldprd pygaiiagif esegleyytp irarfgttvc alvrrnlgia
      241 vvdaftvgdm tdqglavipi deetgfqtyv ayradavlss yaerfvktlr rvmnesvrrl
      301 prptel
//
LOCUS       WP_457660720             224 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660720
VERSION     WP_457660720.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24470
     Region          7..212
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mriepvflfd ldgtlvdsvy qhvlawkeal daegidlsvw rihrkigmsg glfadqllre
       61 tnmeisaerv grlrqyhaaa ykrqadsirp lpgarelltw ltdakisyai atsgrmetaa
      121 vnlaalgtdp avvpvvtrdl vkyakpdpdl flaaaeqlga pietavvvgd siwdmlaavr
      181 cralaiglls ggygheelrh agayrifedp admlhhidev ggrr
//
LOCUS       WP_457660722             528 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660722
VERSION     WP_457660722.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..528
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=56527
     Region          18..518
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mrdavptllg dsvtteparp ilaaeavsks fggvaalkdv rfdlrsgdih almgengagk
       61 stlmkvlsgv yadyegtvrv dgeiarfssv rdaeaagiai ihqelnlvpe lgvadniflg
      121 rervvaglfv drkasleaar gllnrlgiel dpearvgqlr vgeqqlveia kalsvearil
      181 imdeptsals sgecrrlfki vrqlaadgvg ivyishride vmqlsdrvtv frdgrhvwtr
      241 pmagldedti iaamvgrnll dahpvnrpkg aepvlsvsgl slavagrhgw rdmlkgvsfd
      301 vhageilgig gllgagrtei letvfasndg vrggeirldg iavdirsprd arrlgfalvt
      361 edrkakglhl qesirdnval plvgrlarfg lrsfereral asravealgv rcagtdqtag
      421 tlsggnqqkv vigkwlatgp rvllldeptr gidvgakrei ydlvfklaad glaivvvsse
      481 lpelllladr ilvmaegrqt glisreease erimqlaapr stfgrsva
//
LOCUS       WP_457660728             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660728
VERSION     WP_457660728.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36409
     Region          3..335
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msntaflsle kltlaygdtv avkdldlsir qgelvaflgp sgcgktttmr siagllrpqs
       61 grisldgadi trvaankrsv glvfqsyalf phltvfenva fglrlkglsg telesrvdag
      121 lksvgltsfa arkpaelsgg qqqrvalars mvmepkvlll deplsnldar lrlemraelq
      181 rvqketgvtm ifvthdqgea lsladrivvm lngaieqigt pediynrpas afvadfvgfe
      241 nifaiengrl ragngpiela mplphdaagl awrprmvtlg sgpfqgtvrg aafsgstreh
      301 lldtplgalk aevdaaapah sagttlafdl pvekaakler fn
//
LOCUS       WP_457660730             377 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660730
VERSION     WP_457660730.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..377
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41674
     Region          5..355
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mqvvrdqqld glravavtmv lyahffaadg shwghlgvrl ffvlsgflit rllldardaa
       61 rfepstalks fyarralrif ppyfavlaav flldlerste vmawhglyls nfwyalqnew
      121 spwvlchtws lsieeqfylv wplvvlllpr rsiagvcigv ivcslvyrfy wpftgtpsla
      181 rdllppasmd alavgallaa rpswrvawpr waelswipls iasfalvwlk pvpmtpviaw
      241 lawiglevvp llplamlvgn cskgivgiag rvvalspvaa lgrisygvyl fhavvlavvv
      301 qaqpfipvnv tnqgvgrfvv agaltlmlas aswilfekpl nglkrhfpyv rpegaagpva
      361 avprvrrdea lqtpplr
//
LOCUS       WP_457660731             207 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660731
VERSION     WP_457660731.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..207
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22257
     Region          13..199
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mpdhgymhkl kagspggpil fvfhgtggde nqffdfgaql lpkatvvspr gdvsehgaar
       61 ffrrtgegvy dmadlarate kmagfvkala seyeaseiig lgysnganil anvlieeglf
      121 dkavlmhpli pfrpkanaal agrkilitag erdpicpapl tqalgdylsq qnaavelkwh
      181 sgghdirqne iaateeflrv lkreatq
//
LOCUS       WP_457660736             827 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Sinorhizobium medicae].
ACCESSION   WP_457660736
VERSION     WP_457660736.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 827)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 827)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534137
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..827
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86120
     Region          18..80
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(24..26,29)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          83..151
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          176..822
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(471,473,778)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(515..517,580,596..598,627,667..669,689,692,695,714,
                     717)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(779,807,811)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mtalkqteks tslpmsfdfd iegmtcascv rrvekaiaav pgvasanvnl ateratvqfn
       61 gvpettsvlr avekagyapr ivteeiqieg mtcascvsrv ekalkavpgv adasvnlate
      121 katvrlvsgs aeisalaaav kgagygirka tpaeamkedv dhrtaelrsl ksavtisslm
      181 tlplfllemg shfipgvhdf imgtigmrnn lylqfalttl vlfgpglrff rkgvpnllrw
      241 tpdmnslvvl gttaawgysv vatfvpailp sgtanvyyea aavivtlilv grylearakg
      301 rtsqaikrlv glqpktafvl rsgefvetei tevvtgdvir irpgekipvd gtvtdgssyv
      361 desmitgepv pvqkatdsav iggtinktgs itfkatkvgs dtllaqiirl veaaqgsklp
      421 iqapvdrvta wfvpvvilaa vvtfaawyvl gpfpalsfal vnavavliia cpcamglatp
      481 tsimvgtgra aelgilfrkg ealqslrdad vvavdktgtl tkgspeltdl faaegfepde
      541 vlclvaslet lsehpiaeai vsaaksrgla tvavsafeas pgfgvsgtvs grrvlvgadr
      601 alvkngidit gfadeaerlg sggksplyaa idgrlaaiva vsdpvkestp qaikslhalg
      661 lkvamvtgdn rrtaeaiark lgidevvaev lpegkvdavr klrqggrsva figdgindap
      721 alaeadvgia vgtgtdiaie sadvvlmsgd lngvakalal skatirnikq nlfwafvyni
      781 slvpvaagvl ypvngtllsp ifaaaamams svfvlgnalr lksfdpa
//
LOCUS       WP_457660739             281 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660739
VERSION     WP_457660739.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..281
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29941
     Region          65..278
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkflrygepc qekpgllgsd giirdlsgqv pdlaagaldp skltelakld vealpavngn
       61 pklgpcvagt gkficiglny sdhaaetgat vppepiifmk atsaivgpnd dlilprgsek
      121 tdwevelgiv igrtakyvse aealdyvagy ctvhdvsera fqterhgqwt kgkscdtfgp
      181 tgpwlvtkde vedpqnlamw lkvngetmqd gstktmvygv aylvsylsqf mslhpgdvis
      241 tgtppgvgmg mkpprylkag dvvelgiegl gsqkqrvrad d
//
LOCUS       WP_457660743             412 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Sinorhizobium medicae].
ACCESSION   WP_457660743
VERSION     WP_457660743.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=45016
     Region          1..402
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mndrftlavt gqslikhdir dipapafrev qsllrqadls ftnfegtilg thggwplkgs
       61 ffgcsdpavl dalgaigfqa lslsnnhafd lgpsgvlstl eevekrgflh aglgrnarev
      121 srasiatinq rrialvamdg gpgpdfmyaa dadenrperp gvnrlrlsql levddvafeq
      181 iravrdkigy taidlandsq pddpprldpq aevaiarcvf krsdrygrgv ridevdmarn
      241 laaiasaard ealviaylhh hhwasdwyql pewvsgvakr cidagasmfv shgapvlqpv
      301 eiyrgrpify slgnfifhvq sekstwtaae vwesvvgvcs fasdnslini sfhpvvigge
      361 hgledgvler rlvpqlvtrd savrilgrlq eqsarlgahi eisgnvgrlq ar
//
LOCUS       WP_457660745             265 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Sinorhizobium medicae].
ACCESSION   WP_457660745
VERSION     WP_457660745.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11999121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..265
                     /product="potassium channel family protein"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29661
     Region          37..220
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          157..228
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mdmtdqprah sklnsirlal qrlergrdpw alrwqallai idlsilaffi lgpylragps
       61 yliidyiiaa wigceliara faapsvkrfl rrpmtwvdvv ilgtllfpdl lfnfaflrvm
      121 riwaigkspl lleglrragw shlqevvrac lnflaflfvv tgfvyttffy hreggegfvd
      181 avyftvatit ttgfgditlp gtlgkltsvv tmivgislfv rlaqavvrpy kvnfpcpqcg
      241 lqrhdtdavh ckacgymlni pdegd
//
LOCUS       WP_457660746              84 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Sinorhizobium medicae].
ACCESSION   WP_457660746
VERSION     WP_457660746.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 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 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=8922
     Region          1..79
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mkdkvrtfvi enflfgdtay eladdaslie ndiidstgvl elvafieddf giamadadiv
       61 pqnldslari safieakgav pvsa
//
LOCUS       WP_457660748             423 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660748
VERSION     WP_457660748.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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 423)
  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 11458748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..423
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43364
     Region          99..380
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <290..422
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 mgsfdfsaiy ygwsyvqsgt lfrvdygdga seefrgtgfr yntsgeptag tvtsyaafyn
       61 gqrlfyvegg avaatkivta artystsddl rvvaevlkgn dtisggnyad vlygfdgndf
      121 vagnggndtl yghagndtih ggsegdying gtgvdsasya gsnrnvmasl snpnintnda
      181 igdqyasien ligtnysdal ygngsantle ggsgndtlag gagadkllgg agidtvsyan
      241 asaavtakll yastntgdal gdtyssveni igsiyadkly gsdgansitg gsgndglvgn
      301 ggndvlfggq gadhlygsvg adtfvfkaan esigsaydti fdfltseqdr idlsaidani
      361 sasgnqafsf lgtaaftgva gelrydklss dtyiyadvng dkladlkirl ddavtltdgy
      421 fvl
//
LOCUS       WP_457660750             295 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660750
VERSION     WP_457660750.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32393
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqreelgdlm aflavaeees ftkaaarlgt sqsslsliik rlearlgvrl ltrttrsvap
       61 taageqlfst lapafgtiea qlsalsefrd kpagsfrita gqhaidtiiw pklsaflvdy
      121 pdikvelvae saltdivaer fgagvrlgdq vekdmiavri gpparmivvg apscfraqpp
      181 pktpqeltay rcinlrlpsy ggfyawefer dggevrvrvd gqvafngvpq vvraaldgyg
      241 ltyvhedvvr eylddgrlvq vlddwtppfp gyhlyypsrr hpspaftllv ealke
//
LOCUS       WP_457660751             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660751
VERSION     WP_457660751.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41316
     Region          1..302
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mskpflqirg irkeygpvta vqdvnldvaq gefltflgps gsgksttlyi lagfedptgg
       61 dillngesll stpshkrnig mvfqrytlfp hlsvgeniaf plkvrrlpka eidakvrqml
      121 klvrlegfed rkpaqmsggq qqrvalaral aydppvllmd eplsaldkkl reeiqheirr
      181 ihqqtevtil yvthdqeeal rlsdriavfs kgvidqigtg pelyanpatr fvaefigdsd
      241 flpcnvvsag ngraeiaice tmtvadiplh gtassgskaa lmlrperlll skrqsefwla
      301 chgqryhlpr qqrpcgdedq qrqqsvgppp irprgnlrpq srrrclaeir rrvgarlrpi
      361 vaagmprrpa ng
//
LOCUS       WP_457660752             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660752
VERSION     WP_457660752.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36298
     Region          24..286
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(31,159,222,246,248)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 mrnifilaat vatiatsapa taadlvfssw ggttqdaqka awadkftekt ginvlqdgpt
       61 dygklkamve anavtwdvvd vegdyaaqag kkdllekldf siidkskldp rfvtdysvgs
      121 fyysfvigcn kdavdacpkt wadlfdaqkf pgmrafykws apgvieaall adgvspdkly
      181 pldldrafkk ldtiksdiiw wsggaqsqql lasaeapfgs vwngrmtala qsginvetsw
      241 eqnitaadsl vvpkgaknke aamqfialat saeaqaelan ltgyapinld spelmdadla
      301 ktlpdaqtas qvnadmnywa enrdaigerw yawqak
//
LOCUS       WP_457660753             346 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660753
VERSION     WP_457660753.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..346
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38937
     Region          32..346
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkfslfvhme rldpsqdhks lyeefvalce iadkggmhai wtgehhgmef tiapnpfvti
       61 adlarrtknv rlgtgtviap fwhpiklage aamtdlicdg rldigiarga ysfeyerllp
      121 gldawsagqr mrelipavkg iwagdyaheg efwkfpatts spkplqkpyp piwvaardpn
      181 shefavangc nvqvtplwqd deevrslmar fndacakntd igrpkimllr htyvgsdead
      241 iaqaahemsv yynyffawfk nekpikqgli eripdeaiaa ntmlsgeamr rnnvvgtade
      301 aiarlktyea mgydeysfwi dtgmsferkk aslerfiaev mpvfae
//
LOCUS       WP_457660757             225 aa            linear   BCT 27-JAN-2026
DEFINITION  hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660757
VERSION     WP_457660757.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Colovos,C., Cascio,D. and Yeates,T.O.
  TITLE     The 1.8 A crystal structure of the ycaC gene product from
            Escherichia coli reveals an octameric hydrolase of unknown
            specificity
  JOURNAL   Structure 6 (10), 1329-1337 (1998)
   PUBMED   9782055
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..225
                     /product="hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24197
     Region          19..179
                     /region_name="YcaC_related"
                     /note="YcaC related amidohydrolases; E.coli YcaC is an
                     homooctameric hydrolase with unknown specificity. Despite
                     its weak sequence similarity, it is structurally related
                     to other amidohydrolases and shares conserved active site
                     residues with them; cd01012"
                     /db_xref="CDD:238494"
     Site            order(24,89,123)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238494"
     Site            order(27,30,76)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238494"
     Site            118..119
                     /site_type="active"
                     /note="conserved cis-peptide bond [active]"
                     /db_xref="CDD:238494"
ORIGIN      
        1 mtpanfdgtr piivaddaam llidhqsglf qtvgdmpmtt lrnhatalak matlcnmpvi
       61 ttasvpqgpn gplipeihen aphakyvarr geisawdnpd fvaavketgr ktliiagtit
      121 svcmafpaia avqegykvfa vidasgtysk maqeitlarv vqagvvpmdt aavaselqrt
      181 whrddamqwa eiytkifppy alliesykka qdvianneql dsarg
//
LOCUS       WP_457660758             115 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457660758
VERSION     WP_457660758.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..115
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12447
     Region          <26..95
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(45..47,57..58)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mletcsagst ssswsvegrn glgrpgrlra rqvreratgv lyydlavdeg yrrqgiatal
       61 irrlcdlaae rggwvvyvqa dlgdapaial yeklgvrqdv lhfdividak rvgps
//
LOCUS       WP_457660763              70 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660763
VERSION     WP_457660763.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..70
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7514
     Region          2..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 melkevmain lrrirhvkql tqeelavqsg lsaryigsie radvsatvtv lgqiaavlgv
       61 epaelvtksr
//
LOCUS       WP_457660769             307 aa            linear   BCT 27-JAN-2026
DEFINITION  arginase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660769
VERSION     WP_457660769.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Dowling,D.P., Di Costanzo,L., Gennadios,H.A. and Christianson,D.W.
  TITLE     Evolution of the arginase fold and functional diversity
  JOURNAL   Cell Mol Life Sci 65 (13), 2039-2055 (2008)
   PUBMED   18360740
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Ash,D.E.
  TITLE     Structure and function of arginases
  JOURNAL   J Nutr 134 (10 Suppl), 2760S-2764S (2004)
   PUBMED   15465781
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Cederbaum,S.D., Yu,H., Grody,W.W., Kern,R.M., Yoo,P. and Iyer,R.K.
  TITLE     Arginases I and II: do their functions overlap?
  JOURNAL   Mol Genet Metab 81 Suppl 1, S38-S44 (2004)
   PUBMED   15050972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="arginase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016813 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear
                     amidines [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32571
     Region          8..289
                     /region_name="Arginase-like_1"
                     /note="Arginase-like amidino hydrolase family; cd09999"
                     /db_xref="CDD:212523"
     Site            order(95,117,119,121,134,224,226,269)
                     /site_type="active"
                     /db_xref="CDD:212523"
ORIGIN      
        1 mptlpyaile apstlglatd gvehlpdqll glglaeriha rradrlavls keptpdaetg
       61 ilnaraiaaw spkladavea vldarefpvv lggdctivlg smlafrrrgr yglffidgna
      121 nffqpeaepn gegasmdlal vtgygpshlt diegrgplvr pedavafayr dhkdqeeygs
      181 qplpkelkai dlpavramgi eaaarkavdh ltrealdgff ihldadcldd vvmpavdfrv
      241 pgglswdelg valrvalasg kavgieitiy nprldadgsa grgladvlaa algtaaplvd
      301 rrradir
//
LOCUS       WP_457660778             370 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660778
VERSION     WP_457660778.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..370
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39442
     Region          31..360
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mstenreacs ppsgraamkk elpkqfqdyr nvwvfieleh gqvhpvsiel lgegrkladk
       61 lgvhlagvvi gppggqgtan aiadafayga dlsylvespl lahyrnepft kaltdlvsan
      121 kpeilllgat tlgrdlagsv attlktglta dctelnvdsd gslaatrptf ggsllctiyt
      181 lkcrpqmatv rpsvmampqr vnkptgsiir helkmleeei atkvlaffsd gdsntanlay
      241 advvvagelg lgavqnlqll kdlartlggd fgcsrplvqk gwmpvdrqig qtgntirpkl
      301 yiaagisgav qhrvgvegsd livaintdpn apifdfahlg vvadaisflp altevftkrl
      361 eprnlekfvq
//
LOCUS       WP_457660788             348 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660788
VERSION     WP_457660788.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..348
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36152
     Region          26..348
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msieqskpaa sqaipssagv reaairygfl vllagmilyf slvrggfasp qsavfilqsv
       61 sitgilalgv tatlvvggfd lsigsiatta mmassyvmvv lggdaltatl vcfsigvlig
      121 lingiiivym rvpdllatlg mmflllglqr iptegrsiaa gmtlpdgtva pgtfspafla
      181 lgrhrfdfvl pnlvpvsvvv liilavviwf fleytrfgrm myavgsnera aslagapvna
      241 ykiwayiisg vfasiggill aarlgrgdia sgnnllldav aaaligfavl gatkpnafgt
      301 avgalfvgil lqgltmmnap yytqdfvkga vlvialiftf alskrgrr
//
LOCUS       WP_457660787             755 aa            linear   BCT 27-JAN-2026
DEFINITION  cation-translocating P-type ATPase [Sinorhizobium medicae].
ACCESSION   WP_457660787
VERSION     WP_457660787.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   5  (residues 1 to 755)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 755)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..755
                     /product="cation-translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0043169 - cation binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /calculated_mol_wt=78929
     Region          38..100
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          126..735
                     /region_name="P-type_ATPase_FixI-like"
                     /note="Rhizobium meliloti FixI and related proteins;
                     belongs to P-type heavy metal-transporting ATPase
                     subfamily; cd02092"
                     /db_xref="CDD:319782"
     Site            order(406,408,698..699,720,724)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319782"
     Site            order(450..452,511,527..529,547,587..589,609,612,615,634,
                     637)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319782"
ORIGIN      
        1 msccsgiavp itagagdksa raeeirlasr dlgdglrqti ltlpdvhcaa ciaaveralr
       61 kisgvelarv nlssrrvtin wrgnddessd faaelakigy ashlasieed gqdpvlssll
      121 kalavagfsa mnimilsvsv wsgadpatrh afhlisaala lpaivysgrv fyrsawealr
      181 hgrtnmdvpi svgvllafal svydtlhnaa yayfdastsl lfvllagrtl dhlmrgrars
      241 avgalerlap rganviradg aidyvplsei kpgmhllvaa gervpvdgvv vkgaseldcs
      301 lvsgesawkr aepgsalqag vmnvgnpltl latvsadgsf laemtrmmea aesgrstyrr
      361 iadraaslya pvvhgvalls mfgwfygtgd lhksvtiaia vliitcpcal glavpmvqvv
      421 aarrlfergi mardgsafer lndidtvlfd ktgtltlgem rlvnagdlqp rllslaaama
      481 rvsrhpasta ialagagrht apvefdslee vhgcgiegra gdavyrlgrp swasnatqvd
      541 lgtssatvls kdgettavfa feesvrpgac elvqtlrsag vsvrifsgdr saavssiagq
      601 leieafsael lpdekveair alaakgrkvl migdglndap alaaahvsia pssatdvgrs
      661 asdfvflgqs llavrdiilt aaradvlirq nfamaiaynv vsvpfaiagl vtplaaalam
      721 slssivvvgn alrlgarvkk gprtfgatkp atvki
//
LOCUS       WP_457660792             491 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660792
VERSION     WP_457660792.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..491
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53828
     Region          4..435
                     /region_name="SsnA"
                     /note="Cytosine/adenosine deaminase or related
                     metal-dependent hydrolase [Nucleotide transport and
                     metabolism, General function prediction only]; COG0402"
                     /db_xref="CDD:440171"
ORIGIN      
        1 mdgllllhgt ivtvddkrri iedgalavdn dkivdigtsq alaprhagkk vidcrgkvii
       61 pglidahgha ghalirsiga dtnalwmriv tptyyhyvtr dywyadglvs glerlragvt
      121 tsasivtsmp rsddpvfain harayselgl reiicvgpag lpwpqsvtrw esgkperrsv
      181 sfeammegae avieslngts egrikvfltp ftivpsveps nastpdfavn lteddrmqar
      241 riretarkwg vrihsdafag qirmawqdre nallgpdvhl qhcwgishee idilaetgth
      301 vthappgrst pvmqmmargv svaitsdgaa pschfdmfqi artaqatqhi lhnhdryilp
      361 pgkifemiti daaraigmgh eigslevgkk adiavidmrk phltpnwmpv hrlihqvlgs
      421 dvdtvivdgr iimeegkvlt admyealafg eaeakalver aglqahmhdp gwgqlhrtfe
      481 rpvplptppd c
//
LOCUS       WP_457660795             555 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Sinorhizobium medicae].
ACCESSION   WP_457660795
VERSION     WP_457660795.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..555
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61288
     Region          34..485
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(42..43,84,137,139,263,316..317)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(42..43,84,137,139,263,317)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mnrrimrgvg afaastvlwc tasslqaqea rpkpnilfiv sddtgygdlg pygggegrgm
       61 ptpnidrlad egmtffsfya qpsctpgraa mqtgripnrs gmttvafqgq ggglpaaewt
      121 lasvlkrggy qtyftgkwhl geadyalpia qgydemkhvg lyhlnaytya dptwfpdmdp
      181 elramfqkvt kgslsgkagg evkedfking qyvdtpvidg kegvvgipff dgyvekaaie
      241 fldsaakkpd qpffinvnfm kvhqpnlpap efqhkslsks kyadsvveld trigrildkl
      301 retgmdkntl vfyttdngaw qdvypdagyt pfrgtkgtlr eggnrvpaia kwpgkikars
      361 knhdivggld lmatfaavga vplpdkdred kpivfdsydm spillgtgks arelwfyfte
      421 nelspgairv nnykfafnir gddgastggl avdtnlgwkg aekyvatvpq vfdlwqdpqe
      481 rydifmnnft ertwmgvvmg eelkkimaty vqypprkpqs ltyngpitls dyerfqwvrd
      541 slakegvsis lptgn
//
LOCUS       WP_457660797             397 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457660797
VERSION     WP_457660797.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..397
                     /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=42554
     Region          <10..397
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 meaakvskpd vaavytvdls qrpvppsdaa qekaallqla grmhdgpgev lpkfvelame
       61 ltgaisagvs lleqtepfpv frghnlrgil spfngattpr dyspcgitld rgaptlaihp
      121 ervydwipsg lslpevllvp lyigrteplg tlwvvadrig yfhcghgatl qeladfigva
      181 lkmarseqel lqaleqqell tremshrlkn lftivdgmvr isarstnskd dlvsllsgrl
      241 halaaahslv kpsfsdvqga asnladlisi viephkpaai fgrsrfsleg pailcgeqsv
      301 nglalvfhel ttnaakygal rgdngrvdiv wqvngddlsi twsedggeit sppvskgfgs
      361 tlvdatvtrq fggilsydwr ktglsvnivl plsrlaq
//
LOCUS       WP_457660798             220 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457660798
VERSION     WP_457660798.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..220
                     /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]"
                     /calculated_mol_wt=24750
     Region          2..211
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maitlsrlas slrhvevvdh qrlrlgraaq ilivdcrqrq rdehkptels sellhlalvs
       61 esslhrdaif asgysdyllw pliqqevlrr lascvaeier rsaglffsad plvqkscdll
      121 aqrinqqtal selarlvgtn rttlvnrfea sfgcgpitwl rhfrmaeaaq rlrsgeesva
      181 kiaetlgyen snnfstafka ihglpplsyr kiafrrekpv
//
LOCUS       WP_457660802             207 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457660802
VERSION     WP_457660802.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..207
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22931
     Region          2..193
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mytpgeliva hgesgrdvff ilegrarvtl fsengreify gdrgpgdiig evsaidgkar
       61 sasvvaleat raarlpapaf rrlvtdhpdf swallehlss girhmtdrvy efstlvvrrr
      121 lilellrrad drdestsrvf idpapthfel aasisthrea vsremsvlak ggliercgrr
      181 lllcdltala llagdeeepv fsrreks
//
LOCUS       WP_457660806             277 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Sinorhizobium medicae].
ACCESSION   WP_457660806
VERSION     WP_457660806.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29686
     Region          153..276
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtyktvllii gandqendla aaadlsaaag ahlsvlvvql aappavgdya alsvawlder
       61 aedmkqldea vkraratlkd lgisfdangi ycetawaddd vgsraryadv tligaslqad
      121 pslrnraidg alfysarpvl lsanrqsvtl rpkkillawn stmesaraar eamelmenae
      181 evnvvlvdps aaparngeel gadiatylar hvvnvtvdrl ssagrrveev lnqhaidtsa
      241 dlivmgaygh trlrerifgg vtkamierpi vpvlmvh
//
LOCUS       WP_457660808             280 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660808
VERSION     WP_457660808.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 280)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..280
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31362
     Region          1..280
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtattarrln aigliiavit vfcaiiwafp lywavvsslk pehevvrpyi elwpetftvs
       61 hyvfaltqte igrwyvnsiv tatavtvltv ssslfcgyai sqlnfplrnv lwwlilasfm
      121 ipmqtlivnh felvadlgli ntwsgivlpq lihpviiivy kqffdgvpkd freaavmdna
      181 sewriltkvy ipmnwgvtta lsivcfiwsw naflwpflav tktdmmtitv gitqvndafg
      241 vyyarqltaa vlaglpvama ylifqrrvte aitlsagikg
//
LOCUS       WP_457660807             535 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660807
VERSION     WP_457660807.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 535)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 535)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..535
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58128
     Region          57..514
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 mnditnwtrs ddamietair rgatrrellq mmlaggaals agslmlgrag navaatpvag
       61 gtlkaagwsa stadtldpak aslstdyvrc csfynrltfl dkggtpqmel aeaietkdak
      121 twtvklrkgv tfhdgkplta ddvifslkrh ldpavgskva kiaaqmtsfk avdkqtveit
      181 laspnadlpt ilsmhhfmiv adgttdfskg ngtgafvrev fepgvrsvgl knknywksgp
      241 nvnsfeyfai sddssrvnal lsgdihlaat inprsmrlve sqgdgfvlsk ttsgnytnln
      301 mrldmepgsk rdfvegmkyl vnreqivksa lrglgevgnd qpvspanfyh npdlrphafd
      361 pekakfhfek agmlgqsipv vasdaansai dmamiiqasa aeiglkldvq rvpadgywdn
      421 ywlkapihfg ninprptpdi lfsllyssea pwnesqykse kfdkmliear gsldqekrka
      481 iynemqvmva seagtiipay isnvdaitak lkgleanplg gqmgyafaey vwlea
//
LOCUS       WP_457660809             408 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional alpha/beta hydrolase/OsmC family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660809
VERSION     WP_457660809.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Marchot,P. and Chatonnet,A.
  TITLE     Enzymatic activity and protein interactions in alpha/beta hydrolase
            fold proteins: moonlighting versus promiscuity
  JOURNAL   Protein Pept Lett 19 (2), 132-143 (2012)
   PUBMED   21933125
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18542801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..408
                     /product="bifunctional alpha/beta hydrolase/OsmC family
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43768
     Region          9..253
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
     Region          271..408
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mafktqrlqf sghsgatlsa rldlpngplr ayalfahcft cskdlaaarr iavelaregi
       61 avlrfdftgl gssegefast nfssnvadll saadylrqhy eapavlighs lggaavltva
      121 gdipevraaa tigapadvgh vlknfgasld eiekngeadv dlagrtflvk rqfvedtrah
      181 rikdavaglk rpllvlhapl dhtvgienat eifvaarhpk sfisldkadh lltdpedaaf
      241 agriisewlt rylaadtpqa tgpieyvrvr etgegkfqna vqagghrlfa depesvggld
      301 sgpspydfla valgactsmt lrlyaghkql klgriavdvs yakthakdce ectelersgs
      361 gridrfervi sidgevseel rekigeiagk cpvhrtleav tkiktvvk
//
LOCUS       WP_457660811             342 aa            linear   BCT 27-JAN-2026
DEFINITION  D-cysteine desulfhydrase family protein [Sinorhizobium medicae].
ACCESSION   WP_457660811
VERSION     WP_457660811.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="D-cysteine desulfhydrase family protein"
                     /EC_number="4.4.1.-"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35746
     Region          5..341
                     /region_name="PRK03910"
                     /note="D-cysteine desulfhydrase; Validated"
                     /db_xref="CDD:179673"
     Site            order(56..57,85,201..205,297,326..327)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107202"
     Site            57
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
ORIGIN      
        1 mtdrdplqsf prerlmkgpt piqrlarlee vlgersrgvs iwakrddlme lggggnklrk
       61 lefllgqaka egcdtlvvtg gvqsnfarla aaacarsgla celvlaqmvp rtteiyqdng
      121 nvlldrlfga svhildpgdd agayarrrvd eiaetrrkal laplggstti gclgyvdcaf
      181 elarqsaetg vafeqiiipn gsggmhagla agmfvggshp sriaaytvls padkclpata
      241 dkinavlerl asdarvtadd lrissaqlge gygvptsgmi davellarse gllvdpvygg
      301 kalagllsdv esgaiapqsn vlfimtggsp glyayadvlt sk
//
LOCUS       WP_457660816             716 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660816
VERSION     WP_457660816.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..716
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76580
     Region          445..671
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msfgffpaaa tahfwtspfa lvillvlqra swaqstgdpp pekvrqflel arnpevkawl
       61 geklaapaaa psssiaeais sweaavdgri aalakafprv paelanafav svrdvnsgtp
      121 glvvgilall lgvgfgtewl trraltrart pgergdagqt vlsdavallt falasvgsfl
      181 afewppllrk vvltlllafi afrfvytiar llvafggags gssyqpvpva etdaagrfwl
      241 rrvslsagfl ligwavvslm psfgfsidva rlaslafgfg ilaiaietvw rrpgkitspv
      301 vrsllslyli vlwlawvagl fgllfigiys lvlpaltrgv grvaqvfanr vqltgalgvm
      361 lnsmivrsar alviaaavaw layvwrfsaa alagseigii vingvlntvv vllvadllwq
      421 sskaliayrm dlaehaggte dqvarsgrlr tllpifrntl avficavavl ailsglgvqi
      481 apliagagif gvaigfgsqt lvkdvlsgvf ymlddafrig eyiqsgsykg tvesfslrsv
      541 rlrhhrgpif tvpfgelgav qnlsrdwvid kmtlnvtydt dvelarklik kvgqelaadp
      601 efaadtlqpl kmqgvdsfgd faivlrlklm tkpgtqfaik rrafmmikka fdengvkiav
      661 ptvhvegsge pataahqleq vvkkapmtes aetcqpykap qalkgpkhie tideaq
//
LOCUS       WP_457660822             252 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660822
VERSION     WP_457660822.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..252
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26349
     Region          11..249
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mkeiigtfrp dlfagkdili tggssgigla iaqgfarlgg tvialgsses klkaaaadpe
       61 nkgirfervd vrdpeminaf aktlgkldvl ingagiarpe aefedatyme vmdvnlnsqm
      121 rfamavlpll kasrgvilnt asmlsyvsdp lvpaygasks gvlgltrhla hafgpdgirv
      181 naispgyhkt dmtsglwtdp vpaekiaqrs alkrwgtvdd lvgtalflas paaefitgad
      241 lpvdggfvvg sf
//
LOCUS       WP_457660825             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457660825
VERSION     WP_457660825.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..320
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34314
     Region          38..314
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mslaprntpp pkhppetrpm srrewllsdr pqsrtqarlg raymtwrrfs anrlavlglc
       61 illalifvai fadalapynp vignlagarl lppgsegyll gtddqgrdil srlihgsrlt
      121 llvvllvaii aapvglivga vagyaggwid avlmritdif lafpklvlal afvaalgpgi
      181 enaviaiait swppyariar aetltvrhsd yiaavrlmga splriifrhv mpmcmssliv
      241 rvtldmagii ltaaglgflg lgaqpplpew gamiasgrrf ildqwwvatm pgiailivsl
      301 gfnllgdglr daldpresgq
//
LOCUS       WP_457660832             308 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanine--D-alanine ligase [Sinorhizobium medicae].
ACCESSION   WP_457660832
VERSION     WP_457660832.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..308
                     /product="D-alanine--D-alanine ligase"
                     /EC_number="6.3.2.4"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008716 - D-alanine-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33413
     Region          1..308
                     /region_name="ddl"
                     /note="D-alanine--D-alanine ligase; Reviewed; PRK01372"
                     /db_xref="CDD:234948"
ORIGIN      
        1 msskhvavll ggfsserpvs lssgtacada legegyrvtr vdvgpdvaav lqelrpdvvf
       61 nalhgpfged gtiqgileyl eipythsgvl asalamdkaq akhvakaagi pvaeavvmdr
      121 rsfgnqhpmk ppyvvkpvre gssfgvvivk edqshppqvi tssdwrygdr imveryvagr
      181 eftcgvmgdv algvteiipq ghafydydfk yvkggskhvi paqvspniyq kiqtlalkah
      241 qaigcrgvsr sdfrfddrgd gegeliwlei ntqpgmtpts lvpemaqhag lrfgeflrwm
      301 vedasclr
//
LOCUS       WP_457660835            1044 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457660835
VERSION     WP_457660835.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1044
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110925
     Region          20..1023
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnigmgghhp gggqggktgf talfirrpif alvvntlivv aglaawngve irelpqvdqp
       61 vvsvttefdg aspetidrev tsvvegavsr vqgikdisst ssfgrsrvtl efsdttdigq
      121 aandvrdalg ritgqlpdda deprivkads dsqpimrlal tsdtmsmddm tllveneisd
      181 rlaavegvad vtvygdqeki fridvnqakl agrgvtvanl realanasyd vpagsltsan
      241 qdisvratad lqtpeqfenl mlgnnvrlrd vatvtlgpdt gtsalrsngr egiglgiirq
      301 aqsntvdisq gvrsvvnais sdilppgtel kvtsddavfi ngaiheveia lfvavfivtl
      361 viylflldwr atliptitmp ialigtvaai ylagfsinil tllaivlatg lvvddaivvl
      421 enivrrraeg lgpraaavhg tlevffavla ttatlaavfv plsflpgqtg glfrefgfvl
      481 afsillssfi sltlcpmlas rmltkerkeh qgvmqrfgqr asafyrvtlg aclnaplivf
      541 avaafftaag algfltlkse ltpnedrsqv mlrinapqgv sleytqaqir rieeglqpll
      601 ksgeisnvfs isgqggsans gfmvltlaqw eerdrtqsqi vadinrmtak ipslraftiq
      661 anslgirgag sglqvalvgn dytklgdaaa kllramedsg rfenvrlnye anqaqlsvti
      721 drerasdlgv digglswalq amldgssvvd ifvegeaypv kllsstepln dptdlqnifi
      781 kagdgrivpm ssiatieeka vapqlsresq lravslsagl ksdlalgeal smveemaepi
      841 lppgsrimpl aeaatldena nglfvtfgfa iviiflvlaa qfesfvsgli imstvplgla
      901 caifamiltg ntlniysqig lvmlvgimak ngilivefan qlrdrgqdvr saienaanir
      961 lrpvmmtmia tvvgavplvl asgagaeari algwvlvggl glavivtlyl tpvaylviag
     1021 ftkphadeer kleeemkaae vlki
//
LOCUS       WP_457660836             171 aa            linear   BCT 27-JAN-2026
DEFINITION  SspB family protein [Sinorhizobium medicae].
ACCESSION   WP_457660836
VERSION     WP_457660836.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..171
                     /product="SspB family protein"
                     /calculated_mol_wt=18841
     Region          1..170
                     /region_name="SspB2"
                     /note="SspB-like protein, predicted to bind SsrA peptide
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3814"
                     /db_xref="CDD:443026"
ORIGIN      
        1 mgqdhirydi laqdalrgvi rkvlaevsat ghlpgdhhff itfltgapgv risqhlkaky
       61 peqmtivvqh qfwdlkvtet gfeiglsfsd tpeklvipyn airgfydpsv nfelefdvaa
      121 seeqetdsae itaypveets esvtdentek pdgpkgggas ivslnsfrkk n
//
LOCUS       WP_457660840             368 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660840
VERSION     WP_457660840.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..368
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42229
     Region          1..368
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 mslrlatfni enlmswfdfs gfrnhlkqdr vlrlfdvrse aeyqrleear tiahtddvrq
       61 msalaiadcd adilclqead nmaalqafey gylfrmvgng yrqkylvegn dtrgidvavm
      121 mreetrdgqk ieclevksha altyedldlf ndelaltnrp rdrifkrdcl evdvriggrp
      181 ltlyvvhlks mgparegldg rqatmavrra evkavrhiie grfgsgdtad kifavcgdmn
      241 dyqekvnvlg drrngyefvp yeetssaldv lshdgfvvnp mlrrpvldrw tlfhsrgpee
      301 rhlcqldyiw lsqelarrna arvpevirag qpyrtifpag qeveryprtg wdrpkasdhc
      361 pvvmtldi
//
LOCUS       WP_457660847             399 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457660847
VERSION     WP_457660847.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..399
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43352
     Region          21..379
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(178,180,213,244,270,293,320,345)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mtahlssats vpgfdappml rissvacvpl vgeapkggwa seirpedsih aliavhtedr
       61 psgygsvftn ghlarealqv lkpllegana letgrtteil hqntfwmgrg gtithvisgi
      121 nialwdilgk vtglpvstll ggrhierirp ycsllmdepe imrdtlaryr eqgykafkig
      181 wgpfgrresy rsdeaiiaaa rselpegydl fvdagasdaf wpnglkwalr taemlrahev
      241 gwfeealvpd dvegfvtlra naglpitgge vltrrqafqp fiergafdii qpdvtkvggi
      301 seqklirema achgveyvgh gwntalglaa dlqmaaafpn trfveyiggs ayvdgllarp
      361 felnaegyle ipftpglgva idaekvrrya pdaddlrla
//
LOCUS       WP_457660845             158 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660845
VERSION     WP_457660845.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..158
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17061
     Region          6..127
                     /region_name="FabA"
                     /note="3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier
                     protein) dehydratase [Lipid transport and metabolism];
                     COG0764"
                     /db_xref="CDD:440527"
ORIGIN      
        1 mlleyfqmid riesvdlaag rlvarsnvpe kspvfeghfp gyplvpgvll ietmaqasgf
       61 lvlaatnfaa mpflmtvdga kmrsfvepna eleiealleh egsgfavtka riasvgkkic
      121 daklklrtip fdqvplgdiv rkraeelglm artagsek
//
LOCUS       WP_457660851             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660851
VERSION     WP_457660851.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77119
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspddpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 qelqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklseg krneiidmln
      601 qslvgayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457660855             307 aa            linear   BCT 27-JAN-2026
DEFINITION  SEL1-like repeat protein [Sinorhizobium medicae].
ACCESSION   WP_457660855
VERSION     WP_457660855.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 307)
  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 307)
  AUTHORS   Mittl,P.R. and Schneider-Brachert,W.
  TITLE     Sel1-like repeat proteins in signal transduction
  JOURNAL   Cell Signal 19 (1), 20-31 (2007)
   PUBMED   16870393
REFERENCE   5  (residues 1 to 307)
  AUTHORS   D'Andrea,L.D. and Regan,L.
  TITLE     TPR proteins: the versatile helix
  JOURNAL   Trends Biochem Sci 28 (12), 655-662 (2003)
   PUBMED   14659697
REFERENCE   6  (residues 1 to 307)
  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 12218275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="SEL1-like repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33254
     Region          7..36
                     /region_name="SEL1"
                     /note="Sel1-like repeats; smart00671"
                     /db_xref="CDD:214772"
     Region          26..56
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          54..293
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          63..92
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          99..128
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          138..164
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          171..200
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          207..236
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          243..272
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mlvaltvkaq vnlgglyfdg egvaqdyaea arwfrkaaed gaaalaelnl gvmyehgrgv
       61 apdpaeaarw ygraaehgda qaqhrlglmy fkgegvkrdh vqaarwyraa aaqgnpsaqf
      121 hlgsmylqgq gvpkepseaf rlfrgagglg henaqynlgl mylngigvqk dldesvrwfr
      181 aaaeqksalg qynlalmyan gtgvaknsee aarltslaah qglamaqhnl giayisgagv
      241 ekdsaaavhw fqraaqqgha raqfnlammy argegvarnd alafewmqka anqlpearqy
      301 ldrtrke
//
LOCUS       WP_457660853             603 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Sinorhizobium medicae].
ACCESSION   WP_457660853
VERSION     WP_457660853.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Collins,K.D., Lacal,J. and Ottemann,K.M.
  TITLE     Internal sense of direction: sensing and signaling from cytoplasmic
            chemoreceptors
  JOURNAL   Microbiol Mol Biol Rev 78 (4), 672-684 (2014)
   PUBMED   25428939
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Alexander,R.P. and Zhulin,I.B.
  TITLE     Evolutionary genomics reveals conserved structural determinants of
            signaling and adaptation in microbial chemoreceptors
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2885-2890 (2007)
   PUBMED   17299051
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12182596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..603
                     /product="methyl-accepting chemotaxis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004888 - transmembrane signaling
                     receptor activity [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=65161
     Region          36..189
                     /region_name="sCache_2"
                     /note="Single Cache domain 2; pfam17200"
                     /db_xref="CDD:435780"
     Region          166..591
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrririsarl yalvafallt maaaltfglv qaqdrlvaer kamlaamnen aitvfnayhg
       61 qekagrvsrk eaqsraleav ramryqesgy fwvndmhptm vmhpikpeld gadltqnkdp
      121 ngkflfvefv ktveahgkgf vdyywpkpga depvlkyshv agfepwgwvv gtgvyaddla
      181 amfrerawqm agilaaaala ilmaalaivr svvrpieklk ismrataden lsldvpetdr
      241 adeigqmakv lvvlrdsvke rlelrsreae qqdrldserr gneelqrkta aiqaeametl
      301 gaalerlasg dltaevaria peytklkddf ntaaaalrdv igaisqstei vhgsaadise
      361 aannlsrrte qqaaaleeta aaldeitstv rhasdrahea rdmvdetkas aaksggivrn
      421 aidamgriea sssrisqiig videiafqtn llalnagvea arageagrgf avvaqevrel
      481 aqrsagaake ikdliatsvk evgagvelvr stgdalmeie slvnrvneqv asiataareq
      541 atglqevnta vnsmdqmtqq naamveetta asqtlaqesr elkallgqfr lqegaqpayg
      601 raa
//
LOCUS       WP_457660859             440 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457660859
VERSION     WP_457660859.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 440)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..440
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46524
     Region          2..435
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 madalkigia glgtvgaslv rilqdrhetl attcgraiei tavtardrsk drgvdlagit
       61 wfddavslas qgdidvfvel mggtgdpaya svkaalthgv hvvtankall aahgielaei
      121 aekhgallny eaavaggipv ikalresmtg ntisrvygim ngtcnyiltk mekeglsfea
      181 clkeaqrlgy aeadpafdie gndtahklsi ltslafgtai aaddiylegi tnisiediqa
      241 aadlgyrikl lgvaqrtesg ieqrvhptmv phdtviaqvd gvtnavaies dilgellmvg
      301 pgaggdatas avlgdiadia ksrpgaqhvp afgrpanall pykrarmqsh eggyfirlkv
      361 vdrtgvfanv akqmadndis lefimqhskh yadpaepkti ilvthatfea svrkaivsik
      421 aegylvgepq virierpkaw
//
LOCUS       WP_457660860             356 aa            linear   BCT 27-JAN-2026
DEFINITION  BMP family ABC transporter substrate-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660860
VERSION     WP_457660860.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  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 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   3  (residues 1 to 356)
  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 356)
  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 356)
  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   6  (residues 1 to 356)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 356)
  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 14448206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="BMP 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:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38454
     Region          28..306
                     /region_name="PBP1_BMP-like"
                     /note="periplasmic binding component of a basic membrane
                     lipoprotein (BMP) from Brucella abortus and its close
                     homologs in other bacteria; cd19963"
                     /db_xref="CDD:380618"
     Site            order(34..35,43,117,163,191,236,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380618"
ORIGIN      
        1 mkkllvalat tvavlgiapa asaqekakic fiyvgsktdg gwtqahdigr qelekelgdk
       61 ietqflenvp egpdaeraie rlarsgcgli fttsfgfmda tikiaakfpd vkfehatgyk
      121 tapnvatyns rfyegryiqg qiaakmsekd vagyiasfpi pevvmginaf vigaravnpd
      181 fkikvvwant wfdpgkeada akalidqgvd iitqhtdtta pmqvaaergi kafgqasdmi
      241 aagpqtqlta ivdtwgayyv krtkafldgt wstssswdgl kdgiltmapy tnmpddvkam
      301 aeeteakikt gelkpftgpl nkqdgspwlk egetaddatl lgmnfyvegv ddklpq
//
LOCUS       WP_457660878             225 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457660878
VERSION     WP_457660878.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..225
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25231
     Region          74..160
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mkspsqiads esdqhtakgp ycirfyencs hspaswlvpq alseteengf vdrspalpif
       61 eepcvaaiga dgkamality yyvpgrcnit lgytksdhrr kgihtalfna lvervtkrgd
      121 ifsifsrtha knlaaqaafe aqgrtkeyie yffhlkdavv gveptveemr vpeylvepfd
      181 tgpgglksmq afinektaeg yelhqliers tyqwvlifkr qpdrg
//
LOCUS       WP_457660879             203 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase small subunit [Sinorhizobium medicae].
ACCESSION   WP_457660879
VERSION     WP_457660879.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Oliveira,L., Tavares,P. and Alonso,J.C.
  TITLE     Headful DNA packaging: bacteriophage SPP1 as a model system
  JOURNAL   Virus Res 173 (2), 247-259 (2013)
   PUBMED   23419885
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Benini,S., Chechik,M., Ortiz Lombardia,M., Polier,S., Leech,A.,
            Shevtsov,M.B. and Alonso,J.C.
  TITLE     The 1.58 A resolution structure of the DNA-binding domain of
            bacteriophage SF6 small terminase provides new hints on DNA binding
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 69 (Pt 4), 376-381
            (2013)
   PUBMED   23545641
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Zhao,H., Kamau,Y.N., Christensen,T.E. and Tang,L.
  TITLE     Structural and functional studies of the phage Sf6 terminase small
            subunit reveal a DNA-spooling device facilitated by structural
            plasticity
  JOURNAL   J Mol Biol 423 (3), 413-426 (2012)
   PUBMED   22858866
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..203
                     /product="terminase small subunit"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0051276 - chromosome organization
                     [Evidence IEA]"
                     /calculated_mol_wt=22391
     Region          25..180
                     /region_name="Terminase_2"
                     /note="Terminase small subunit; pfam03592"
                     /db_xref="CDD:427384"
ORIGIN      
        1 mpvlknarhe kfaqalakgk taddayaeag fkpdrgnasr lqqkdnirqr vaelleweqt
       61 verkatekai dklaitkerv laelakigfa dirkaikwqg tlvteednqd ggdvlviknv
      121 vtnnvqliss deidddtaaa iaeisqnstg gikikfhdkk galvdigkhl gmfverhehs
      181 gpdgapiqte trtwrevlrs kks
//
LOCUS       WP_457660906             209 aa            linear   BCT 27-JAN-2026
DEFINITION  CatB-related O-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457660906
VERSION     WP_457660906.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..209
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=22557
     Region          37..186
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(40,42,60,72..73,78,80,82,120,122,125,144,160,168)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(42,44,71..72,74,83..84,122,125,142..143,148,156,
                     158..159,161,165)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(42,44,71,83..84)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100040"
     Site            order(72,74,111,122,125,130,142..143,148,156,158..159,161,
                     165)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 magststiak sasikqktiv edpihvgagc avmadrigry cfinnntcif dgvrigrfvt
       61 farncqigga ehpihylstg ffrisrnwfp ddhvaqtael vpltrvpsrs rganieignd
      121 vwfgasclvl kgvtigsgav igagavvtkd vppyaivagn pakvvkyrfd ektisrllas
      181 kwwdrdmavi eklplndvqe slrileaap
//
LOCUS       WP_457660907             274 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 108 protein [Sinorhizobium medicae].
ACCESSION   WP_457660907
VERSION     WP_457660907.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..274
                     /product="glycoside hydrolase family 108 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /calculated_mol_wt=28932
     Region          9..166
                     /region_name="ZliS"
                     /note="Lysozyme family protein [General function
                     prediction only]; COG3926"
                     /db_xref="CDD:443130"
ORIGIN      
        1 maretlpval elmfgdeggy snvktdrggp tkygvthvtl aahrgvkavt ahqvkamsre
       61 eaediyrrsy wgqsggnllp pgldyaafdf gvnsgparav ktlqkvvgvr edgqvgeqtl
      121 aavrkypggv stlirdycda rmrflrsltn aktgfpvngr gwtirvtgkd pkgqwanqpg
      181 vignalrlaa dasgrtvekn dappeggaka dtrdtglgev lkkpeawgpl ggllsaagal
      241 fagngpvqwa laaamvaavl vglwyfvrrv reag
//
LOCUS       WP_457660909             534 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660909
VERSION     WP_457660909.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11458748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..534
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54467
     Region          23..>483
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          259..506
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <384..513
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 matvtyhfpg glypsqynpp lsgvsvnptf gelvdmsesa rstttstdvl yrldnglklk
       61 lvgtgfsfds sgdavggtit siqvllnngt tlvqtisgln lslelfqdaa aafdnaklen
      121 wlmsgadtin gsagdddisg rggndilngn dgddtitgge gddtydggng fdalsfqday
      181 gattatqgis lnatngtvtd qfgfsetfqn feeyrgtqfs dtingssise sfmglggrdk
      241 isggagvdti rydrdfqlgg tkgvnvnltt gvatdgfgsq dtlsgienvr gtglkdtiig
      301 nsasnflrgf agadtlngwg ggdtmrggsg ndsywvdntg divdenqdsg agidvvqssi
      361 sfnladtaav kgsverltli gsgaingtgn algnlltgns aantfdggag ddhiygalgn
      421 dtligsagqd lfvfntalna ssnvdtivdf viaddtirle ngiftavvgt galtaaqfas
      481 nttglaadad driiyesdtg nlfydadgdg aggsvqfatl taniaitagd flit
//
LOCUS       WP_457660915             373 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Sinorhizobium medicae].
ACCESSION   WP_457660915
VERSION     WP_457660915.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..373
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39862
     Region          4..352
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,230,306,326,328..330)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,99,106,178,181,183,230,237,306,326,
                     328..329)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,99,178,181,183,329)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            183
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 maslfdpisi gdivlknrvv mapltrnrsp qavpndlnva yyeqrasagl liteataish
       61 qgqgyadvpg lykpealagw rkitdavhka ggrivvqmwh vgrisheslq sqggkpvaps
      121 airaksktyl inpdgtgtfa etsepralel aeipgivedy ckaaraaiea gfdgveihaa
      181 ngylidqflr sgsnertday ggsienrarf lfevvdavtg eigagrvgir ispvtpanda
      241 fdpdpqplft yvveglaryp layvhviega tggardhqqg drpfdyaalr nayaaaggka
      301 awmtnngydr dlalrtvesg eadlvafgkp fianpdlvrr lrdnvalnap dqatfyggga
      361 kgytdypsle nva
//
LOCUS       WP_457660920             938 aa            linear   BCT 27-JAN-2026
DEFINITION  Rne/Rng family ribonuclease [Sinorhizobium medicae].
ACCESSION   WP_457660920
VERSION     WP_457660920.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 938)
  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 938)
  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 938)
  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..938
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..938
                     /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=103901
     Region          3..647
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 maekmlidas hseetrvvvv rgnrieefdf esehkkqirg niylakvtrv epslqaafvd
       61 yggnrhgfla faeihpdyyq ipladrqall kaeaeearre ddiepmetsa erksasstds
      121 vaevvaqaea aeaageaaea qaaaekpkak pkrtrrakpk aseetaasqe seapeggpse
      181 dgesdksema aivetdsise dvdarrqrdd dddddnhdge keiiesvgae dameevaerq
      241 frkprkqyri qevikrrqil lvqvakeerg nkgaalttyl slagrysvlm pntargggis
      301 rkitnlqdrk rlkeiargld vpqgmgvilr taganrtkve ikrdfeylmr lwenvrtltl
      361 nstapclvye egslikrsir dlynkdisei vvsgeegyke akgfmkmlmp shakvvqpyr
      421 dvhpifsrsg ieaqldrmlq pqvtlksggy iiinqtealv sidvnsgrst rehsiedtal
      481 qtnleaaeev arqlrlrdla glividfidm eekrnnrsve kklkdclknd rariqvgris
      541 hfgllemsrq rirasvlest mqtcphcngt ghirsqssva lhvlrgieeh llkntthdis
      601 vrttpdialy llnqkrssit dyeqrfgvsi fieadahvga qhfaidrgep venpvridqi
      661 lqfepepeee eeeeevliee elddeeaeet aaehqdqqkg qpddqggrkr krrrrrrgkg
      721 agqgadavsa esadaaedea gdeaaaddae deldaadsln gdseqkrkrr rrgkrggrrn
      781 rqeelagseg etgataetve epgeesvdst aaeipavsaa eeapadvaaa aavegvaeep
      841 kpakprrsrk kttkteepav nadevaekvv eaqpepaepa pqiveeaved legakparsn
      901 rdlsaiaskp vvtsskgese eeptkpkkgg wwqrrgff
//
LOCUS       WP_457660924             413 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457660924
VERSION     WP_457660924.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..413
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43806
     Region          6..408
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mphdgivivg sghagaraaq slrangwqhr isvidgegca pyerpplska vlsgksrped
       61 avlfpqdfve qhgidfrsgv ravgidrdtr qvrlsnddav sygrllltpg aeprlldipg
      121 relegvfslr tavdacglsg qllpgadvvi vgggliglev aasaiqrgcs vtvieagprl
      181 mtravppela elirllhetr gvrfilgrqa vallgsqrie alrmddgstl actaalisig
      241 vtprtdlala agleiengia vdcflktsdp fiyaagdaca fkngdgsrlr lecwknaedq
      301 galaarnmmg anepytpmpw mwsdqydrtm qiaghpelgd lhvarhcpdg sllvyhldan
      361 daivgvsgfg slreiargvr tgqmlmqrgi hpakealqnp kidlkaaakv aag
//
LOCUS       WP_457660933             478 aa            linear   BCT 27-JAN-2026
DEFINITION  protein adenylyltransferase SelO [Sinorhizobium medicae].
ACCESSION   WP_457660933
VERSION     WP_457660933.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..478
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52760
     Region          2..478
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mpanfygrvq ptpvtepwli kfnrplaeel gldvraiecd gaaifsgnli pegaeplama
       61 yaghqfgtfv pqlgdgrail lgevtdtsgr rrdiqlkgag qtpysrrgdg raalgpvlre
      121 yvvseamhal gvpttralaa tvtgqpvyre qilpgaiftr vaashirvgt fqffaargdm
      181 dsvrmladyt idrhypelkd deraylalfk aiaarqasli arwlhvgfih gvmntdnmti
      241 sgetidygpc afmdgydskt vfssidqfgr yayanqpaig qwnlarlaet mvklfdpvad
      301 tavnlandal geygtifqkh wldgmrrkig litdededld lvqslltlmq kgkadftltf
      361 rrlaasaenv gadmelaslf eepeatspwl erwrrrltre pqmeieraas mravnpafip
      421 rnhrveqain aatedadfsl fealvdvtsr pyedqpgrsa yaappkpgee vlqtfcgt
//
LOCUS       WP_457660929             126 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Sinorhizobium medicae].
ACCESSION   WP_457660929
VERSION     WP_457660929.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..126
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13931
     Region          22..110
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mallaceata saqgaveiea pivrifefvv vsddleafmv agrknvqtsv rdepgvlsmh
       61 cvadksdptk lyvvevyede dayrshvela hfrdfinaik gkvisrrvie tnpkmvgskq
      121 fawteq
//
LOCUS       WP_457660939             255 aa            linear   BCT 27-JAN-2026
DEFINITION  SURF1 family protein [Sinorhizobium medicae].
ACCESSION   WP_457660939
VERSION     WP_457660939.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..255
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial respiratory chain
                     complex IV assembly [Evidence IEA]"
                     /calculated_mol_wt=27488
     Region          42..255
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mrapvkstva dghmpafrrl fgrvagvvlv laalavlval gtwqmqrlqw kealigaiae
       61 rrsapavple qieamaaagg didyrtvhas giydhgrerh ffathegrtg fyvftplmla
      121 daralfvnrg fvpfekkdss krsegpvagk vtvnglarpk lsgkpsslvp dndpaknify
      181 wkdlgamans tgissdrvvp ffidadaapn pgglpvggvt qfdlpnnhlq yaltwyglaa
      241 alvavsgvfv yrrrr
//
LOCUS       WP_457660941             391 aa            linear   BCT 27-JAN-2026
DEFINITION  cell wall hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660941
VERSION     WP_457660941.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Bagyan,I. and Setlow,P.
  TITLE     Localization of the cortex lytic enzyme CwlJ in spores of Bacillus
            subtilis
  JOURNAL   J Bacteriol 184 (4), 1219-1224 (2002)
   PUBMED   11807087
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ishikawa,S., Yamane,K. and Sekiguchi,J.
  TITLE     Regulation and characterization of a newly deduced cell wall
            hydrolase gene (cwlJ) which affects germination of Bacillus
            subtilis spores
  JOURNAL   J Bacteriol 180 (6), 1375-1380 (1998)
   PUBMED   9515903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="cell wall hydrolase"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42922
     Region          254..386
                     /region_name="CwlJ"
                     /note="Cell wall hydrolase CwlJ, involved in spore
                     germination [Cell cycle control, cell division, chromosome
                     partitioning, Cell wall/membrane/envelope biogenesis];
                     COG3773"
                     /db_xref="CDD:442987"
ORIGIN      
        1 mrkgikfpgk frltfsrwra pamiglaifl gfpsaaaysd iatflsginr ggerwrtylt
       61 qspagslhev emvftdpvtt galdggagmt lpdggrvavt aelkhhgtpd edrvtrklkk
      121 krivavtpat ppkdfsagsi lertsslmvp sldgsekmif akpkikgkei viatafyrka
      181 ppkpepgisp mlaklvtndk pdilatayvr pepdyaresp fdsilrdden agrfipeiap
      241 ddhawaatal pptvfskeeq tclaegiyfe argesvkgqa avaqvilnrv rnptypktic
      301 gvvyqnkawr nrcqfsfacd mirdliysrg hwktakeval avtsgkvwls evgsathyha
      361 tyvkpawakt mkrvgkiglh ifyrtygggw s
//
LOCUS       WP_457660943             326 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457660943
VERSION     WP_457660943.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34727
     Region          48..299
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(63,150,152,154..155,182,231,252,255,268,270,299)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mafqlkrrtl fsagagalaa psllagfaga qetmekdgma kgvdfktlkl gsfkvtvisd
       61 gtrasdnphe ifgtnqpaes vatlleqnfl ptngfvngfa pvlvdtgsev vlfdtglgeg
      121 greagmgkla eglktagyap dqvtvvvlth mhgdhigglt eggkpafana ryvtgqveyd
      181 fwkdaarvgt aaenghkavl akvvplaeki tfiadggevv pgisamaafg hspghmiyrl
      241 efdgramilt adtanhyvls lqrpdwevrf dmdksgasas rkkvfdmiat drlpfigyhm
      301 pfpavgfaer qdqgyrfvpa syqfdi
//
LOCUS       WP_457660950             117 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660950
VERSION     WP_457660950.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..117
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13136
     Region          49..105
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(73,75..77,79,92..93,97..98,101,105)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 manritacgc svpkgtkcah eqtrttarqk andvargtaa ergydkdwwr lrhaflqahp
       61 tccvpgceak athvdhiksi rdaprlrlve snlrsmclpc hsrrtardqs qnwgrkr
//
LOCUS       WP_457660946             540 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Sinorhizobium medicae].
ACCESSION   WP_457660946
VERSION     WP_457660946.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..540
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60184
     Region          12..531
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mtttttpsga sshlawifdd spildphgkg eaavnfikal rhpksvlpgr sfqldrwqer
       61 iirrvygdtk pdgtrkiktv faliprgnrk ttlgaalclv algperipgs qvvssavdre
      121 qarialeemk gvigahprld eafqiqdtkn rithrksgaf yramsadaat ahgrspvfal
      181 vdelhawkkr dlwdaiktgl vktpgsllvi tttagvgren vaydmyayar qvasgaiede
      241 aflpilfead adedwrdeav wrrvnpglsc nppypdidgm rqmvreaehr padremfrql
      301 hlnvwldgaa npewdlgiwd eghepidlpa legrkawiav dlskridlsa vacaielddg
      361 rfalhvmgft peaqlrkrad ndsapyalwa ehgwltvclg divdrliiee yirdlcrrfd
      421 vqecvfdval arelmenlea dgipvaafpq tlmnfakpvd tfedmflnrr lvhdspllrw
      481 avgnvvmmrd qndnrrpakn ksadridpav aaimstarav qgatgrssye dasdlsmfvv
//
LOCUS       WP_457660956             628 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457660956
VERSION     WP_457660956.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 628)
  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 628)
  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 628)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 628)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..628
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69796
     Region          254..>463
                     /region_name="RepA"
                     /note="RecA-family ATPase [Replication, recombination and
                     repair]; COG3598"
                     /db_xref="CDD:442817"
ORIGIN      
        1 mtaaqrkefi etherrtawk efsgfcwqls gdavlmpfkd gepvwenatr dnlervnhws
       61 dftdediprl avltdsftrf igkgndvsvl thwrygtpei rqidgepcer avdlimeaia
      121 ddlfiedmlg lpladplkpl admppskmsl kleaiasrfe esrtapvaan dnqpsyderl
      181 lpyleafggk dtiltadgvy gavvdnkagq irlmpdgral fvnklfsryi elpevpkplt
      241 anpfslddpt tlpqrdwlfg rhyirryvta svgpggggkt ahsisealam vtgrplldag
      301 gpltkplrvw winaedpqde inrrfhaaak hfsvtneqig grlftdsgrd qhfiiarqeg
      361 rdlkvvepfi gdmvaeihrr eidvviidpf vstheaqend ngamqrvaaa wtrvadeanc
      421 nielvhhvak nqgevtadsa rgggafkdkv rsmrvfnvmt keeaekagve nhrsyfrvdf
      481 gkinmiasgn sqwrrfvsvp lmngkglvks gdeigvveaw rwpskdavae kakaerasli
      541 anvpaetlag lkvrlgasdf kasdqatnwa gnlvgeffdl nvkdkdskrq vkamlsawid
      601 ageleivqiq dayrrvsphv kpaaapqn
//
LOCUS       WP_457660960             394 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457660960
VERSION     WP_457660960.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42790
     Region          64..378
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mairhrewvt ekgtkgsawv vdyyaqtgkr hvksfakkkd avafdaktri evngkvhvad
       61 setvtvaeag klwlaacdgl erstvaqytq hlnlhiapli gkkklteiti pavrafldkl
      121 kaegrsdamv ravrvslgsl lsdaqerglv irnavkdigr akgkakaaar hkeqvivgvd
      181 iptpkevram lakaegkprv fmmtaaltgm raselrglrw sdvdlkkaev tvrqradayh
      241 eigspksakg rrtiplpanl vaalkewqke cpsgdlglvf psgtgniefh anivkrwyhp
      301 pqiaagvsvn tgdldkdgkp ivaakysglh alrhfyaswl inrpedgglg lppkvvqerl
      361 ghssiqmtld vyshlfpkgd dagtmdnaas sllg
//
LOCUS       WP_457660962             364 aa            linear   BCT 27-JAN-2026
DEFINITION  polyamine ABC transporter substrate-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660962
VERSION     WP_457660962.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Kroger,P., Shanmugaratnam,S., Scheib,U. and Hocker,B.
  TITLE     Fine-tuning spermidine binding modes in the putrescine binding
            protein PotF
  JOURNAL   J Biol Chem 297 (6), 101419 (2021)
   PUBMED   34801550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..364
                     /product="polyamine ABC transporter substrate-binding
                     protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     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_process="GO:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40355
     Region          27..357
                     /region_name="PBP2_PotF"
                     /note="The periplasmic substrate-binding component of an
                     ABC putrescine transport system and related proteins;
                     contains the type 2 periplasmic-binding fold; cd13659"
                     /db_xref="CDD:270377"
     Site            order(33,238,241,270,272,308)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270377"
     Site            order(44,47..48,296..297)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270377"
ORIGIN      
        1 msklivatlt aavlagstml asaqervvnv ynwsdyidds iladftketg ikvvydvfds
       61 neiletklla ggsgydvvvp tayflqrqia agvfqkldks klpnlsnmwd mvmertaqyd
      121 pgneyavdym wgttgigynv dkmkeilgtd ekpnwdvifd peisakfkdc gihllnsptd
      181 impsalaylg lnpdsheqad lekaadllmk vrpnirkfhs seyinalang diclavgfsg
      241 difqardraa eanagvtvdy sipeqgaqmw fdmlaipada phvaeahefi nymmkpevia
      301 kasnyvfyan gnkasqqfld kevledtaiy psdavmeklf tttpfeakeq rvltrlwtri
      361 vtgq
//
LOCUS       WP_457660961             531 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660961
VERSION     WP_457660961.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..531
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59055
     Region          25..514
                     /region_name="PBP2_DppA_like"
                     /note="The substrate-binding component of an ABC-type
                     dipeptide import system contains the type 2 periplasmic
                     binding fold; cd08493"
                     /db_xref="CDD:173858"
     Site            order(409,413,427..430,432)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:173858"
ORIGIN      
        1 mkklttllaa talatlmagt awsktfvfcs egspegfdpg lytagttfda aahtvysrll
       61 efkkgttete pglaeswtis ddgleytfkl rpgvkfqtte yftptrelna ddvvfsierq
      121 wksdhpwhgy vtggsweyfa gmglpellef vekvddmtvk iklkrkeapf lanlampfas
      181 imskeyadkl qaegkmnqln qmplgtgpfa fvayqqdavi rykahpefwg gkqkiddlvf
      241 aittdaavrf qklqagechl mpypnaadve amkadpnlkv meqaglnvay laynttqppf
      301 dklevrkaln kainkeaivd avfqgqaqpa tnpipptmws yneqieddty dpeaakkmle
      361 dagvkdlsmk vwampvarpy mlnarraael mqadfakvgv kveivsyewa eylekskakd
      421 rdgavilgwt gdngdpdnfl dtllgcdavg gnnraqwcnq efdelvtkak easdvaertk
      481 lyeeaqvvfk reapwatldh slsivpmrkn vegfvqsplg dfafdgvdiv e
//
LOCUS       WP_457660971             120 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Sinorhizobium medicae].
ACCESSION   WP_457660971
VERSION     WP_457660971.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..120
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12786
     Region          12..95
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mntttpnehp saivkvdtsn fseevlqsae pvivdfwing cqpcdmiapf leqiatelag
       61 kvkvvtlnge espelveqyg vrgyptlalf kggevavaai dfrtgsfras isnalaslrt
//
LOCUS       WP_457660990             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457660990
VERSION     WP_457660990.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32172
     Region          78..292
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(85,126,163,178,180,188..191,240,265..267,269,272)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(105,112,138,204,206..210,238,242)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            163
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrnypeiasr mfgtplmlhp skgdiiaraf gprvlgspda paqvvggeem glvgeklrda
       61 sdywgdalyk gpdlvapgia lieiegslvn kgkwigkscg mtsyeaigvq vrdcierddi
      121 kavvfevdsy ggevtgafdc aeqifelsql kptiavltdh acsagyllas pcrqlvipqt
      181 gicgsigvis mhvdmsawla keglkvtilk agehkadfnp yeaipddvlq qelaeleelr
      241 vefaatvary ragrltqqsa latearvyrg qkavdaglad avarpsqvle afeaelsrta
      301 g
//
LOCUS       WP_457660992             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457660992
VERSION     WP_457660992.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77150
     Region          5..658
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempaia klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 qelqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vsywtdeewd aiadrlgrle apqqgeledh lnqiavktep aagqtataeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457660965             532 aa            linear   BCT 27-JAN-2026
DEFINITION  globin-coupled sensor protein [Sinorhizobium medicae].
ACCESSION   WP_457660965
VERSION     WP_457660965.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Hou,S., Larsen,R.W., Boudko,D., Riley,C.W., Karatan,E., Zimmer,M.,
            Ordal,G.W. and Alam,M.
  TITLE     Myoglobin-like aerotaxis transducers in Archaea and Bacteria
  JOURNAL   Nature 403 (6769), 540-544 (2000)
   PUBMED   10676961
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12110371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..532
                     /product="globin-coupled sensor protein"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=57362
     Region          14..171
                     /region_name="Protoglobin"
                     /note="pfam11563"
                     /db_xref="CDD:431935"
     Site            order(23..25,55,113..115,117..118,121,124,155..156,
                     159..160,163,167)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381256"
     Site            order(62,65,75,78..79,82,102,105..106,111,115,119..120,
                     169)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381256"
     Region          255..491
                     /region_name="MA"
                     /note="Methyl-accepting chemotaxis-like domains
                     (chemotaxis sensory transducer); smart00283"
                     /db_xref="CDD:214599"
     Site            order(279..280,283..284,287,290..291,293..294,297,
                     300..301,304,307..308,311..312,315,318..319,321..322,326,
                     328..329,332,335..336,339..340,343,346,349..350,353,357,
                     360,367,371,374,377..378,381,384..385,388..389,391..392,
                     395..396,409..410,413,416..417,420,423..424,426..427,
                     430..431,434,437..438,441..442,444..445,448..449,451..452,
                     455,458..459,462)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206779"
     Site            349..382
                     /site_type="other"
                     /note="putative CheW interface [polypeptide binding]"
                     /db_xref="CDD:206779"
ORIGIN      
        1 mkqeaseqar rgqaasller lcfagldeda callrdhrqa lsprielalr alshrlqthp
       61 daarhfdsdr qvdrlhdlqs shwnvltdar fdglyaervk vladtesrmg ldprwqiash
      121 avvlehlimg aiedawpksi islgkarkke lrdlvaalvr tafvdteiav slrfnalrqq
      181 hqrqlsqsrr dgeaelqalf adflnalaeg dltarlpeda petympivag lntalgeirn
      241 allaaderaa aaeaivsdlr gsaadlsska gaevktldqh latlvsater irsgsiriga
      301 teakasetri aversgeiag qaisamadie asaekigqii gvideiafqt nllalnagie
      361 aaragesgrg favvaqevra laqrsgeaar eikqlvtgtk gqvaagvetv grtqhaissi
      421 aeqvisinea vtgiareaey qvrdlssaas eigavaeamn rstalaeval assgdlhdvi
      481 melgetvrrf hlerearsga rflpsrveat ddqnempfge aaserhfagw rr
//
LOCUS       WP_457660998             337 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457660998
VERSION     WP_457660998.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..337
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36363
     Region          1..328
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkiwkigtal aasllastas aetvrfwyhf dnpenpmadl iakfeaanpg ieieaenvpw
       61 nsyydnlyta lvggnapdaa mvklfaqprl iemgaleplg eridgwagka dlldnlldln
      121 kgsdgqqyyl piqyvvlyly yradlfdaag lkppatcdaf rdaaikltkq patygfglrg
      181 gkggwdqwga fvlsqgakle pgglttpqai aanqwlidlf qkdkvippsa pndgfqeita
      241 afkkgttamt ihhvgssndm vkalgdkvsa vpvpecgggr wtsygdesla ifsssevkds
      301 awkwisflae gennvalqqg drandgdqer fgkldaa
//
LOCUS       WP_457661010             517 aa            linear   BCT 27-JAN-2026
DEFINITION  hydantoinase B/oxoprolinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661010
VERSION     WP_457661010.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Watabe,K., Ishikawa,T., Mukohara,Y. and Nakamura,H.
  TITLE     Cloning and sequencing of the genes involved in the conversion of
            5-substituted hydantoins to the corresponding L-amino acids from
            the native plasmid of Pseudomonas sp. strain NS671
  JOURNAL   J Bacteriol 174 (3), 962-969 (1992)
   PUBMED   1732229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..517
                     /product="hydantoinase B/oxoprolinase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56439
     Region          2..516
                     /region_name="HyuB"
                     /note="N-methylhydantoinase B/oxoprolinase/acetone
                     carboxylase, alpha subunit [Amino acid transport and
                     metabolism, Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0146"
                     /db_xref="CDD:439916"
ORIGIN      
        1 mldfaaaiyd kevrllsqap slpmfmgtls fciieavkan ggpetlkpgd aliynwpfgt
       61 gshpqdvvii mpvffrdeel igytaikghw ldigakdpyc tdttdvfqeg vifpgvkiyk
      121 envlnddifr mimantrvpq mvrgdldaqv tgcrvgvksl ievierfgle tyraavddmf
      181 dhgerivrsy fekipdgryv gkgemdnngv ttdripfevv levrasdvil dfsgvpdeqa
      241 gptnsplptt isasrvaitm lagygeaphe ghfrplkvit rpgsmfdplp papsfiygwp
      301 glqaieviyn avahampkav paqsggcics vvawgsrees gepwadgtpl ptgqgawdgg
      361 dggimlhiae satrftpaev wehrnpwiie qlalaedsvg pgkwrggpgl nldirmtedt
      421 littvfdrtl napwgllggk earpnncfak mpdgevhsia ksthfhmpkd svlqtrtgsg
      481 ggygdpaerp vemvkrdlad gyitedyark hyphafs
//
LOCUS       WP_457661016             412 aa            linear   BCT 27-JAN-2026
DEFINITION  multidrug effflux MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457661016
VERSION     WP_457661016.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="multidrug effflux MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43253
     Region          12..387
                     /region_name="MFS_MdfA_MDR_like"
                     /note="Multidrug transporter MdfA and similar multidrug
                     resistance (MDR) transporters of the Major Facilitator
                     Superfamily; cd17320"
                     /db_xref="CDD:340878"
     Site            order(21..22,25..26,50,53..54,111,142,145..146,228,231,
                     350)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340878"
ORIGIN      
        1 mtlrmserrt siigaflval gpismalytp ampelvrafa sseaaikmtl slyfggfafa
       61 qlvsgtlsdv igrrrttlif maiylagslm aafapsipvl lagrlvqgig asvgmtvsra
      121 lvrdqftgtt aarimnmigm mlalgpavsp tlggialglf gwqsifllmv gfaltaclvv
      181 qffmvetatp drskghlali faaycqlmsd srfmsstlvi agavgalyaw atmlpfvlis
      241 qvgltptafg igmlmqsglf fsgtvtmrlm mrrftpqalv pvglsfigaa slalaftmha
      301 leptflsvmt pigiyafgia fvmpymmtaa lapfphiagi asammgfiqm sagllggala
      361 alvgvpalal gtiipsfglv slasylwyrr avrlrplaap taeqdpivqa ae
//
LOCUS       WP_457661017             342 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Sinorhizobium medicae].
ACCESSION   WP_457661017
VERSION     WP_457661017.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37110
     Region          9..331
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mdapvntnll elyrtmrrir tfeervgelf vrgqsagsml hlsigeessa agvcaamkpq
       61 dtftthhrgh giflargadp krmmaeiggk etgycrgkgg smhiadmalg hlganaivgg
      121 gipavigagl ssrhlkqdsv siaffgdgam qkgilyesmn maslwnlpvl fvcinnqygm
      181 gtridqatrn tafdqrakaf glngavvdgl dveevqaaar wlvdearagk pgflsvevyr
      241 ffgharmdks pyreeaeele grkkdpvlfa rnklidtgie eerildeldk aiaaemdati
      301 dfaveskapp lgsmfkdvya agepepesvr aridrvlard da
//
LOCUS       WP_457661018             702 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661018
VERSION     WP_457661018.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..702
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74621
     Region          382..668
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msnalpirig flllavapil fwmllgvswa qqapvgvppe kaqqflglls dpevrtwleg
       61 kipsaaaepp aaspadtiss weaairdrig gllgavprip eelasgaavv srdvnsgrpg
      121 lvvsilavli aaglgaewli rrvfararks gtkeeagqei lsevaalltf alasigsflv
      181 fewppllrki iltllvaliv fravraiskf lfavsgsngi adhpmsalas daaprfwlwr
      241 islvagfllf gwaivslmpe lgfsievvrl taflvglgil atavevvwrr pdkpaslvvk
      301 slltlylvvl wsawvmgllg vlwlgiysll lpalvrgvgd vaqalatraq rtgapgivlg
      361 vlivrgaraa viaaavawla yiwriraaal agsepgaivi pgllngiial lvadllwqms
      421 kaliayrmgl gpkdgsnade larsgrlrtl lpifrnvlav figavtvlti lsglgvqiap
      481 liagagifgv aigfgsqtlv kdvlsgvfym lddafrvgey iqsgsykgtv esfslrsvrl
      541 rhhrgpiftv pfgelgavqn msrdwvidkm tlnvtydadv dlarklikkv gqelaadpef
      601 aadtieplkm qgvdsfgdfa ivlrmklmtk pgaqftmkrr afmmikkafd engiriavpt
      661 vhvsggsdna aaaqqalnms kaaelaakap vaplkrkngg ls
//
LOCUS       WP_457661020             311 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine recombinase XerC [Sinorhizobium medicae].
ACCESSION   WP_457661020
VERSION     WP_457661020.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..311
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33638
     Region          10..311
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(151,165..166,236,238,257,292)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271179"
     Site            order(165,257,260,283,292)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mnelliighp evmaerkrwl aslaeerrls gktveayerd trqfltfltg hlagpprlsd
       61 iralrpadlr gflaqrrkgg agartlgrgl aglrsflryl eknglanaag agavrspkqp
      121 kslpkplter dalkvvttds qlaeepwiaa rnaavltlly gcglriaeal dltpadftet
      181 arslrvtgkg gktrivplia aaaeavttyr klcpyhieag epifrgarga klqpaiiqre
      241 mqklrsalgl pdsatphalr hsfathllag ggdlrtiqel lghaslsttq vytgvdsarl
      301 leiydrahpr a
//
LOCUS       WP_457661021             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661021
VERSION     WP_457661021.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38225
     Region          1..352
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mlemkniskv vggemhihpt dlvlergsln vllgptlsgk tslmrlmagl dkpasgsihl
       61 dnadvtgvpv qkrsvamvyq qfinypamav yeniaspmri kgadaatidr evrkaaellk
      121 ltpyldrtpl nlsggqqqrt alaraivkna dlvlldepla nldyklreel reelpkifsa
      181 sgaifvyatt epsealllgg ntatmsegri tqfgrtidvy rqpvdivtar tfadpplnti
      241 dllksgshfa legkpvlpvp vhlgavadgp ctvafqphhl sfdppngsdq plavktaise
      301 itgsesfihv afagarwvml apgiheiepd atlkvfvdtr hlmafgpdgr avggra
//
LOCUS       WP_457661023             122 aa            linear   BCT 27-JAN-2026
DEFINITION  PRC-barrel domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661023
VERSION     WP_457661023.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=13539
     Region          10..89
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mvnpdlhesh dliasdkvvg tavydmngen vgsieriile krggrvayav msfggilgig
       61 hehyplpwem ldydtslggf qvnitkeqve gaprypagqd ydwspesgrr vydyygiapy
      121 wv
//
LOCUS       WP_457661026             255 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661026
VERSION     WP_457661026.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..255
                     /product="glycerophosphodiester phosphodiesterase family
                     protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28093
     Region          4..239
                     /region_name="GDPD_pAtGDE_like"
                     /note="Glycerophosphodiester phosphodiesterase domain of
                     putative Agrobacterium tumefaciens glycerophosphodiester
                     phosphodiesterase and similar proteins; cd08565"
                     /db_xref="CDD:176508"
     Site            order(7..8,34,36,49,102,104,106,139,159,211,231)
                     /site_type="active"
                     /db_xref="CDD:176508"
     Site            order(7,49)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176508"
     Site            order(34,36,104,106)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:176508"
ORIGIN      
        1 mtkiighrga rnlwpenslt gfrnalrlgv daiefdvhls dsgellvihd stlertvhat
       61 gpvrrltpqg riatrlrdtd esvptlsevl dilatregps lhveiksder gspypgvagr
      121 vaeelrrfgv dhrshltsfd isvledcrlh aphvarlvsv naggaarqgg larflagaga
      181 lveivaihhe lmaaewdlir rtvpleqlcv wtlnekedic rwfekgigyl tsdrpdlald
      241 lrqivhapar aeeis
//
LOCUS       WP_457661028             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661028
VERSION     WP_457661028.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38516
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matveyqrig ksfgavtimr disfriedhe fvvllgpsgc gkttllrmta gleavsqgdl
       61 miggkrvndv hprdrsiamv fqnyalyptm kvydniafsl evakvppaei ksrveraaat
      121 lnltpylgry pkelsggqrq rvamgramvr eaevflfdep lsnldaklra hmrteirqlh
      181 nrlktttiyv thdqieamtm adkivvmrag kieqigspdd vydrpaskyv adfigsssin
      241 flpgtvvvdn ggpavdtttg rvsvepspal ksgqkvvlgl rptdvvvdag gplaakailt
      301 erlghdaqlf cegpegsfva vvdkaarfse gaevrfaipp skvhvfdaet eiri
//
LOCUS       WP_457661030             381 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Sinorhizobium medicae].
ACCESSION   WP_457661030
VERSION     WP_457661030.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..381
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=39785
     Region          1..378
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mrvdlnvpvk dgqvtdttri ervaptirel sekgakvvll ahfgrpkgep vadmslktia
       61 saveeildqr vyfapdcigd kaasaiadln dgevlllent rfhkgeeknd pafvtalaan
      121 gdiyvndafs aahrahaste glaqhlpaya grtmqaelea lekglgnpqr pvvaivggak
      181 vstkidllqn lvkkvdalvi gggmantfla aqgvdvgksl cehdlaetak ailaaaseag
      241 caivlpvdgv varefkagad nevvdvkaip adammldvgp ksidainewi sraetlvwng
      301 plgafeitpf dkatvaaakh aaartrsgsl vsvagggdtv aalnhaevad dftyvstagg
      361 aflewmegkp lpgvdilkqq r
//
LOCUS       WP_457661031             351 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661031
VERSION     WP_457661031.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..351
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=38593
     Region          1..>297
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkraviyary stdlqndqsv edqirlckah aerlglnvvg elfdraksga smfgrpglar
       61 lmqkadadef dvlvaehpdr isrdiadlah ihktlrfrri eincvnggam dtvqigmygv
      121 vgqmqreega kkvkrgmvgv vrsgrnaggr aygyrpvpgr kgeleiveee aevvrrifsl
      181 yasgiaprai aatlndesvp aprgkrwnas tlngngqrgn glllnpiyag kliwnrvhmv
      241 kdpstgrris rinpeiehee ieaphlrivd dalfeavqnr kasrggahsr stpkykrlls
      301 gllrcggcgg gmaingsdrs gprvicsthk efgqlrqwsa ilcredratg h
//
LOCUS       WP_457661032             122 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661032
VERSION     WP_457661032.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 122)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..122
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13824
     Region          51..98
                     /region_name="HNH_3"
                     /note="HNH endonuclease; pfam13392"
                     /db_xref="CDD:433169"
ORIGIN      
        1 mssrrdrira kimarvwidp itgcyvwtgp dsgkngrgkg yprmsldgqt vavhiamwtn
       61 ehgyipgkke ldhacrnrlc vrpekdhvem vtrkenakrr erakrsmigh nggpvlecee
      121 vl
//
LOCUS       WP_457661038             124 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661038
VERSION     WP_457661038.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..124
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14452
     Region          31..82
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mssrivyscn msnieqihan ktpvrihyip ewaerrnlsq advvreigad kslvsrwfag
       61 tlpkdeylek laglfgtdvh glfrhpdddw ltrffrdkte eqkeraieml rlffrehdkt
      121 gtdg
//
LOCUS       WP_457661047             681 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661047
VERSION     WP_457661047.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..681
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77192
     Region          5..627
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtmlfnpgrl alsvlaeice pppsvdyldw akrhivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempvva klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd peaqsdsrsk affnakvfki stpmvepgck itanyregsq esyhvpcphk
      241 ecgglqelrw enmrdhidpl hpekahfvci hcgceihehh rewmvrpeng arwvakyper
      301 arrhrsfriw mayspferwe nlareyislq aggpekrdng agaeqtffnd wlglayeadn
      361 kavdwevlrd raeangftrg vvpagvlslv igldvqgdrv ewllvgygrn rlravidhgv
      421 idsragghil gfrehsghis epevraaldl llarewrdda grkrvadlla idgnaytddv
      481 wnwvrkhprs rvimvrggns dnappiaqar eydkkgkpkk qkwssrfftf asssfklrly
      541 rdfkkedaeq agyisfargf eddlfqqats esrvaektrs ghtryiwklt egrrnevldm
      601 lnqslagayr lgipywtdeq wdviedrlgk lepprqgdle dhlnqvpqah pqpapppqte
      661 tpvrteqkkl taaealrqln r
//
LOCUS       WP_457661050             299 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457661050
VERSION     WP_457661050.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..299
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=31386
     Region          76..290
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(83,124,161,176,178,186..189,238,263..265,267,270)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(103,110,136,202,204..208,236,240)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            161
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mshypqiasq lfnrpllahr gtleqyaram aprifggsvt fggewqagli gepvrdavdf
       61 egnptytgpr migksgvavi evegalvpkg kwigamcdat syegihaqvs dcrsnkdirg
      121 vilevdsfgg avsgafscad aihqlaqekp vlailtehac saaylvasaa tgsvipktgl
      181 agsvgvimlh idyskamdka gvnitpifsg arkndyspye algeavykka vaeadtvrdm
      241 fidavagyrk gritadalrk teaetfmgad avkmglvdev gdpitaanaf ileigrkaa
//
LOCUS       WP_457661069             160 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457661069
VERSION     WP_457661069.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 160)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..160
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /calculated_mol_wt=17817
     Region          26..153
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
ORIGIN      
        1 mkkterylar laphastltk ggaahqigai cyrtneigav evllittras grwtipkgwp
       61 iknlkphqaa ereaweeagv agkakkrafg yftclktldd ghktasavev frlkvdelhh
      121 efpehgerqv awlspveaar rvqepelkgl lmrilkesrs
//
LOCUS       WP_457661076             247 aa            linear   BCT 27-JAN-2026
DEFINITION  methyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661076
VERSION     WP_457661076.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="methyltransferase family protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27856
     Region          54..167
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mlfdeiahqg nwlfrwrsyv llitvpvafl tlrqgepiel lfgdradfvy eafcivlaft
       61 glgiravtvg hapagtsgrn trrqkadsln ttgmyslcrn plyfgnaviy mavalftqgi
      121 yfviimalll viyleriiaa eeaflskkfg eqysewvqcv pvffprpsrw erpglpfsar
      181 nvlrreypgf faiiaafgai eafgdilfrg rllydpawig afiagasvyl allflkkrtr
      241 llnvqgr
//
LOCUS       WP_457661077             257 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661077
VERSION     WP_457661077.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28069
     Region          60..195
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maakpsgpqg drprrlrasp qsappqsapp qsaspesapp esgssksleg prtepslsld
       61 rivaaavell dtrgvnglkm rqladrlgag amslywhven kemvfdlald svlayrgppq
      121 kaksrdwrge vfhmledwra smlrhpwsas llprralgpn ilsrlellsn tlsragvada
      181 dlnaaiwslw nyvigatvtr asfvlsdedr svaqqrltgl gehyptiers rllldddwdg
      241 afrkgldfll dglaprs
//
LOCUS       WP_457661080             459 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457661080
VERSION     WP_457661080.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..459
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49229
     Region          7..454
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mlgddivlie rekmlpycrd whgdavssav avirprstdq vaaavkacra lgfsivpqgg
       61 ntglvlgaip daperqvvls lermnrirki daddfsavve agcilselkd avsekgmffp
      121 lalgaqgscr iggnvstnag gvnvlrygmt relvlglevv lpdgsilegl stlrkdnrgi
      181 dlkqlfigae gtlgiitavs ikltpypdqa atallglasl edaiklyrra rrdccdlmsa
      241 fefmpplaft laqeaisdlp ipisteypay vlmeisgsgl vdvddlmqrf legvleeglv
      301 ldgtiaasqt qarnlwlire ginegqakrg ahmrtdisvp lsqlasfvde aeravsealp
      361 gavsvsyghv gdgnvhlnvl ppsgstpeer iqliykaksv vnevldryag sisaehgigr
      421 lkrpdfdars petsrkllta lkhavdpeli mnpgcqlrf
//
LOCUS       WP_457661086             222 aa            linear   BCT 27-JAN-2026
DEFINITION  lambda exonuclease family protein [Sinorhizobium medicae].
ACCESSION   WP_457661086
VERSION     WP_457661086.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Steczkiewicz,K., Muszewska,A., Knizewski,L., Rychlewski,L. and
            Ginalski,K.
  TITLE     Sequence, structure and functional diversity of PD-(D/E)XK
            phosphodiesterase superfamily
  JOURNAL   Nucleic Acids Res 40 (15), 7016-7045 (2012)
   PUBMED   22638584
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Zhang,J., McCabe,K.A. and Bell,C.E.
  TITLE     Crystal structures of lambda exonuclease in complex with DNA
            suggest an electrostatic ratchet mechanism for processivity
  JOURNAL   Proc Natl Acad Sci U S A 108 (29), 11872-11877 (2011)
   PUBMED   21730170
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Kovall,R. and Matthews,B.W.
  TITLE     Toroidal structure of lambda-exonuclease
  JOURNAL   Science 277 (5333), 1824-1827 (1997)
   PUBMED   9295273
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16909715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..222
                     /product="lambda exonuclease family protein"
                     /EC_number="3.1.11.3"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24887
     Region          9..187
                     /region_name="PDDEXK_lambda_exonuclease-like"
                     /note="Uncharacterized nucleases similar to lambda phage
                     exonuclease; cd22343"
                     /db_xref="CDD:411747"
     Site            order(75,106,116,118)
                     /site_type="active"
                     /db_xref="CDD:411747"
ORIGIN      
        1 miqifdcdqn spewyqarag iptaskfhtv mapgrggges ktrkdylydl ageiitgept
       61 esysnshmer ghihepeare mysfitdaei qrtgfirngd kgaspdglvg ndgmfeaksk
      121 lprllieslm rdgfppehka qcqgalwvae rewidivvyw pkmplfvkra yrdgpyivsl
      181 asavkqfnee laeivdrvrr ygqepaptvt naellqhplm ag
//
LOCUS       WP_457661082             215 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457661082
VERSION     WP_457661082.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 215)
  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 215)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  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 215)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP 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 215)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..215
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..215
                     /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=23800
     Region          2..165
                     /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 mridaisvwt gkaaawlilc lmllvcgevf kryilnmpta wifdasnmly gslfmlagay
       61 alaqnahvrg dflysafrpr tqaaldlily ilfflpgiaa liyagydyaa lswrigehst
      121 vtaegpplyf fktvipvaga lvifqglaei lrciiclktg awparlkdve eidvvaeqla
      181 hsehldqetr etaleraqdi draarqrglg gesre
//
LOCUS       WP_457661081             113 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661081
VERSION     WP_457661081.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 113)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..113
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=11747
     Region          <2..113
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mfppalqeaa sidgaseart fwmimlplsm pslitsslft aimtwneflm gltmtsggtt
       61 splsvgiasl vqpyevrwgq laaagslavv pimiasvvas kriiagmtrg avk
//
LOCUS       WP_457661090             542 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457661090
VERSION     WP_457661090.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..542
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58030
     Region          22..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdqnkpdlkr henpapthhe vsddfdfivc gagssgsvia arlaqcgsar vllleaggdd
       61 vaefvrdpaq wplnlgtsrd wgfvgepape lygrrlplsm gkglgggssi nvmvwarghm
      121 edwnyfaaea gdeawgyesv lgyyrriedw rgtpdtvrrg aggpvyvaqp rspqpiaeal
      181 lnaasaigip vfdtpngelm esgggasiae lrirdgkres vfgsyvrplm srpnltvltd
      241 alvtriifdg iratgvdvlv ngqrcaftar cetvlslgai ntpkvlmqsg igprdelkah
      301 gisvvqhlpg vgrnhqdhla fgctwayrkp egiggggcea klywksdsrl sqpdilqcql
      361 efavpspvet gletpahgwt mfsglaqpks rgrlrlsgpn tndpiliepn slsepedvaa
      421 alaavelcre lgnsdaftpl vaceavpgtr dragmidfir ksavtywhqs ctakmgrdsm
      481 svvnnelkvy gveslriada simprittgn tmapcvvige ragdlirkth gladssgvap
      541 fa
//
LOCUS       WP_457661105             412 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Sinorhizobium
            medicae].
ACCESSION   WP_457661105
VERSION     WP_457661105.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46251
     Region          18..399
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtanptsihq rldrrlsgfs leqpfytspe vyaldlqhif ykqwlyavpv cqlakagsyt
       61 tlrvgayevv ivrgrdgevr afhnscrhrg slickarqgq vaklvcpyhq wtyeldgkli
      121 wandmgpdfd askyglkpvn lrnldgliyi clsdtppdfe vfaqlarpyl kvhdlkdakv
      181 aftstiiekg nwklvwennr ecyhcssnhp alcrsfpldp evagvqadga vseklqahfd
      241 rckaagapaq fvlagdgqyr larmplqeqa lsytmdgkaa vsrnlgrvap pdagtllmfh
      301 ypstwnhflp dhsltfrvmp isptetevtt awlvhknave gvdydlkrlt evwiatnded
      361 reivetnqqg ilspayvpgp yspgqesgvm qfvdwyaawl eralaprqla ae
//
LOCUS       WP_457661097             161 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Sinorhizobium medicae].
ACCESSION   WP_457661097
VERSION     WP_457661097.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17650
     Region          32..157
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mgtkphqndv esegapatpg ldlgrlgdll gfhlrmahva vyrdfaetma elaltqkqla
       61 vmellegnpg ssqiglahtl gtdratmmal vnrlasrnli erqpsaadrr rlelhltkag
      121 tailaqarkl idkheqrfit lfardemdal llalkriymg n
//
LOCUS       WP_457661110             396 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661110
VERSION     WP_457661110.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..396
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44821
     Region          9..74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          197..302
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mtalnelsaq eigrrlriar enanvrqdda aqfigvsrpt lvsiekgarr vriqeiqtla
       61 rhygvsvnal lrreavhtdl vprfrklret edehtleair lfndlikadv elenilgiqr
      121 rrnyppergi nvgdavslge ahakdlrdwl glgsgpiadi fsviehslgi rlyqrrlssr
      181 srvaglftyd dnvgacilln anhplprriq tasheighfy gtrqipevle ddekflsrde
      241 ryanafgral vtpgesfses frqlkeitgk ttrrlvilla dqygisrqac vlrleelglv
      301 krgtwswfes nggitddhar evlgsafdrr dagkadadrl vshrmslmah aawkrelmse
      361 gqlaellkig rvqlreivdq ieleeketdd llklpe
//
LOCUS       WP_457661115             391 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457661115
VERSION     WP_457661115.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Goodwin,T.J. and Poulter,R.T.
  TITLE     A new group of tyrosine recombinase-encoding retrotransposons
  JOURNAL   Mol Biol Evol 21 (4), 746-759 (2004)
   PUBMED   14963102
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42532
     Region          193..390
                     /region_name="INT_Cre_C"
                     /note="C-terminal catalytic domain of Cre recombinase
                     (also called integrase); cd00799"
                     /db_xref="CDD:271180"
     Site            order(209,223..224,226,302..304,318,320,338..340,375)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271180"
     Site            order(218..219,346,350)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271180"
     Site            order(223,265,340,343,375)
                     /site_type="active"
                     /db_xref="CDD:271180"
ORIGIN      
        1 mvdnhkaags dsqavhrrae qldaldailp fdrrdqlaal ltdddvatlk hlaqegmgen
       61 tlralasdlg yleawcqlat gtplpwpape plllkfvahh lwdpvkraed sahgmpaeve
      121 aglraerllr sdgphapgtv rrrltswsil trwggftgaf gapslksalr lavkasnrpr
      181 qrkskkavtl diltkllqac agdrlvdard ralllaafas ggrrrsevaa lrvedladee
      241 pvranpaden spplpclsir lgrtktttad gnehvlligr pvaalkawla eaqirdgpvf
      301 rridqwgnid rraltpqsvn lilkarceqa gldpalfsah glrsgyltea anrgiplpea
      361 mqqslhrsvt qaasyynnae rkngraarli v
//
LOCUS       WP_457661117             669 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Sinorhizobium medicae].
ACCESSION   WP_457661117
VERSION     WP_457661117.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..669
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=73346
     Region          4..>621
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mdedstnyni plgwrlqgrl drvawrrsld rlfarhealr ctfvageddp qvqilsgdrg
       61 lpvvehdlrd rpdaqaalld lcqeeartpf dlareplirg rlirladeeh vflltqhhiv
      121 sdgwslgvlv relsslyraf eageddplpp laiqypdyaa wqrqwlsger lqrqaqywrd
      181 tlsgaparla lptdrprpaq qsfagasvpv vidqvltrgl krlsrqhgtt lfmtvlaawa
      241 avlsrlsgqd divigvptan rrrreiedli gffvntlavr idlsgepsvs dllerarraa
      301 ltaqdhqdlp feqvveivqp praldhtplf qvglawqnnt ggsldlpglr vevagegldq
      361 vkfdlelnlg eqgeaiagtl gyatalfdra tierqcgyll allramlada eqpvseldil
      421 ppdersylle elnrtetdyp sdlcvhalfe aqvrrapdav alvfeeqsis ygalnadanr
      481 lahhliglgv rpdqpvaicv erspamvvgl lailkaggay vpldpaypse rlrqllddag
      541 prlllcdaag raalgaeaia dlsavdldta tawadqsadd pdphalglta rnlayviyts
      601 gstgtpkgvm vehaqivrhc lrrrgagtis tsamsgacfi lsrlrlsrfg qlwggaplww
      661 psgsrtgsi
//
LOCUS       WP_457661118             213 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457661118
VERSION     WP_457661118.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..213
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=23707
     Region          7..>193
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msehlllapl lesyfrrrlt kqrnatpatv asyrdalrml ilfaatrlrk kpaalaleel
       61 drdlvlafld eleekrnnti atrnarlaai rsffhhaaaa dpasfgvaqr vltipvkrah
      121 ievthhltea evdaliaapn prtsrgrrdr tfllflartg arvfeatgvn andlqlersh
      181 pqvllrgkgr rahppgsges tdslvgrary rep
//
LOCUS       WP_457661120              85 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Sinorhizobium medicae].
ACCESSION   WP_457661120
VERSION     WP_457661120.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..85
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=9878
     Region          1..83
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mklewtrkav adlgrlydfl asvnrqaaar tvqsltsapa rlleqprige rleefdprev
       61 rrilvghyem stiyvlrpwh tresr
//
LOCUS       WP_457661128             161 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661128
VERSION     WP_457661128.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 161)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17952
     Region          36..102
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mslmsarglv eitdpefdrp vfrqpgfdgt ltakemdeki sawlkktrea ngisradlah
       61 llglsvsvyg ryergsearl siprlihlce imgfmpldvi fdiaphlwgk tleeaedrlt
      121 lmklveqlpq dtmrdlirll rrmtpgepaa davasstseg r
//
LOCUS       WP_457661161             288 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA dioxygenase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661161
VERSION     WP_457661161.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32420
     Region          16..272
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mrdeidvtki viphadvvkc strigaeirn iklsadlpdd tiaaiyglvl ehkviffrdq
       61 ghlddaeqer falrfgkpsp ypqgtmpile idsagediqa diwhidwscm daypkisvlr
      121 gvviplvggd tvwsntaaay ldlpaplqrl andlwavhsf pgaynsryve nfvgpkiete
      181 hpvvrvhpet gertlvlgsy varfvgvskq dsqrlfdlfe shitaqentv rwkwkqgdva
      241 mwdnratmhc atkdysdqrr vvrratiege vpvsvdgrys varfkfrg
//
LOCUS       WP_457661165             299 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457661165
VERSION     WP_457661165.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  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 299)
  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 299)
  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 299)
  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..299
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..299
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33216
     Region          27..188
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mirfdpcliv rrlvvkrgvh vayderfhag vnvvrgdnss gkstilnfif fglggdlskl
       61 dwsghallcd hvwvevelng npavlrrkid aatqsdmeif ggryeaavea pieswlrysy
      121 srsqnkesfs qalfrllgmp dvavegtssi tmhqilrlly adqlsptdsl frfegydpen
      181 lreaignllc gafdtaiyes qqlrrvkere lqevsaelrs ifrvvggees lglgwisqkr
      241 aslladrerv lesitqkeel fyssaasdrl tpdsakgalq crpkiaagac sgtgsfkrd
//
LOCUS       WP_457661167             228 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457661167
VERSION     WP_457661167.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 228)
  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 228)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..228
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25641
     Region          3..209
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mgkklilive dneklrsslk qhlleagfrt dcaadgvvgf srfrllkpdl vflkddlprq
       61 tgfellfdir ldsdtpvima sawnswktel kcfkqgaddf ihmpynnhvv terikkvlrr
      121 sganqlirvg rltinpdart acvddptgei klhptpseyk llvcmatspg rvftrlelie
      181 hcfpqselle stinthmhnl rhkltaagig nyldgrrgvg yaltdrlg
//
LOCUS       WP_457661169             445 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661169
VERSION     WP_457661169.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..445
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48554
     Region          14..445
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mfnsfhsenl qldspvgekh etspdmvftg rlgngmdviv irdhrrpiat hmvwyrngsa
       61 ddpigksgia hflehlmfkg trnhpaghfs gllasvggne nastsrsytn yyqrvpqdyl
      121 ktcmayeadr mtgliltdei vdmerqvvla ergmccdsnp rdilhealha gafspdpcgr
      181 piigwqheie tlgredalay yrrfytpena ilvvagdadp davmdmaeti ygaitptgas
      241 fkrpvvrapp vrtqrlltlv denvhqpaft rihvvpsmma tgphaaalev lalllgggkt
      301 sylhealivn nrmaisvgas yggdvsrgla sfqigacpap gvslthldda ienalemlrr
      361 tgfsaddiqr vksrivanai yqkdnhfnla yqygvaaslg lsvedvalwh drikgvtted
      421 irnaltller stgivgyltp patda
//
LOCUS       WP_457661171             303 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661171
VERSION     WP_457661171.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=32650
     Region          <134..255
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mctswgqisy aqdgqkssgt eakrstwtne rkadlatnfd erwrgsekef algadgvvkq
       61 enavrnkadk sphdfgglhh vdadlssfap fndvpnrvde pqvptgsiqh igavrqiddd
      121 tknvyecgss plspeevksl vvqtarkyrv devfataiaw aesgfdqsrn spkgargpmq
      181 lmpataarfg vndicdpaqn ieggmkylrf lldefqnpll vaaaynsgeq riyqhggipp
      241 fqetvgyvak vvnyqlglpm psakgkarpa aapqavsdas dsgdagviav kktgkfvggv
      301 mhf
//
LOCUS       WP_457661172             157 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661172
VERSION     WP_457661172.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 157)
  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 10099437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..157
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=17397
     Region          <3..144
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cd01066"
                     /db_xref="CDD:238514"
     Site            order(17,28,90,120,134)
                     /site_type="active"
                     /db_xref="CDD:238514"
ORIGIN      
        1 mawsdgefqh gsqvnlelgg trfgytaalm rtmiigepsd rlkrmheaev agleaalaaa
       61 rpgntchdva nafytelkkf rfekdsrcgy pigidwleps aslqlgdqtl lernmtfhlm
      121 lgnwvdedfg yvisesfrvt gstaevlttt prslfqi
//
LOCUS       WP_457661179             572 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661179
VERSION     WP_457661179.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 572)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..572
                     /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=62416
     Region          52..>134
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mlkralpava viadahfhdl eadfgfdrve vegrkitmrs waetrkstrv fnesadafla
       61 alaevrrrgi rhvvllgdyt ddgqrattga lrnildehsa fgmsfyalpg nhdifgpqgr
      121 hhtkqfldca grgilvtsdv kragsgvtvs drmycegypa gldpmagfgy frkpeylhwe
      181 tpfgmsdaae dreyevaspd grnrynmmda sylvepepgl wllmidanvf epvngvyewg
      241 deaafidsts ggwnamlrck pfvipwiadv caraerlgkt llafshypvl dsfdgatgae
      301 galfgetnis rrtprraver allaaglslh fsghlhvegv trrgsggqsl tnvavpslva
      361 fppafkiahp gegnvavetv elsglpvhpr lrnayereaa llgeepddaf sapsygaflr
      421 ahkralvshr yfpeewprai vervadltle eiaclftges agsapklsal gqasaidiae
      481 lgrlpmielv adwyclrqga slalahiees rlplyrflad rfgcepqtch dspakgfvai
      541 flgalglfle ragnsqahiv vpsnparqda sa
//
LOCUS       WP_457661185             299 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661185
VERSION     WP_457661185.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..299
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33328
     Region          17..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 malvrragig ryydvngwlf vapalglial fmiypiawsl wmsfqsgrgm tmkfagfani
       61 vrlwndpvfi kaltntmtyf vvqvpimill alilasllnn pqlvgrglfr taiflpcvss
      121 lvaysvlfkg mfatdgivns tlqaiglvas pipwlthpfw akvlvilait wrwtgynmif
      181 ylaalqnidk siyevaridg vpawarfthl tipllkpvil fttiistigt lqlfdevynl
      241 tegkggpsna tltlslyiyn ltfrfmpnlg yaatvsyviv vlvallafvq ffaarerdr
//
LOCUS       WP_457661187             508 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661187
VERSION     WP_457661187.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..508
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55586
     Region          9..506
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mdpetvdaar vvlearrisk sfsgvqvlfs vnfelragei halmgengag kstlvkifsg
       61 feqpssgevl ldgervtfpa ngaaealgiv iihqefnlae hltvaeslfl grevtrfgml
      121 drkymraetr rvldllgcnv danaligsls iaekqmveia kaisrdariv fmdeptavls
      181 reetsflfrq vrklrdrgts fvfvshklde vieltdrvtv lrdgqwvkta ptsmldgesi
      241 aqlmvgrems slypaknepd vdeevvlrvd alstdyvkda sfevrrgeil gfsgmigsgr
      301 telmeavagl rhrlsgevai rgesvpsgdv haanrcglay mtkdrkakgl llnsgmtanl
      361 tlqslgrhar igylspasea aalerarrrf dirvrdgnvv arrmsggnqq klllakvmet
      421 epdiiiidep trgidvgtkq qiyhfisala rdgssiivvs sempeviglc trvavmregr
      481 ivgmlegdei seqeimryaa glkkmaaa
//
LOCUS       WP_457661195             613 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Sinorhizobium medicae].
ACCESSION   WP_457661195
VERSION     WP_457661195.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=66644
     Region          1..613
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 madsldhapa qannlpqfla mtigaigvvy gdigtsplya frealrpfgp dgveraevvg
       61 lislmlwtlt iivtfkyvlf llradndgeg gtlsllallm kkapryttlm fmagilgaal
      121 figdaritpa lsvlsavegl klvtpafhdy vlpisvgimv llfavqsrgt gavsiffgpi
      181 tliwflvlga agvahigddl ailaafnpvn avtflwnagf vgfivlgavf ltvtgaealy
      241 adlghfgrgp iqaawfavvf palalnylgq galvlshpea vsdpfflmfp nwallpvvll
      301 ataatiiasq avitgafslv rqainlgflp rfeicftset qtgqiylpfv nnallagviv
      361 lmfmfgsses lataygiwgw stltatavll pllvlelffl ganlfkihdg gyvpiliagt
      421 lmtvmwtwrk gvsllrekta rqdiplsqfm amverkseha pvqvpgtaif ltatpdttpa
      481 vllhnikhnh vlhqhnvilt iktarvpyvp ekdrytitkl sdrfsllelr fgfmddqnvs
      541 ralarcrkeg frfeimstsf ylgrrkliad pqsglpqwqd klfiamadsa idpteyfhlp
      601 pnrvvelgeq vvi
//
LOCUS       WP_457661199             313 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457661199
VERSION     WP_457661199.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 313)
  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 313)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..313
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34771
     Region          75..179
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mdhlqtsgsh hrakskseiq atvrrlapfh haidlpfgls tfvpelsrqt rertrlqtfl
       61 dhawgsilta cggslkgkrv ldiacncggf svhaansgad yvfgididah yveqasfvgd
      121 alglsnvefq qldlldldps thgkfdlvlc lgilyhlenp vlsmkrisav tgdvlvvdtt
      181 lmkvpiinpv ldrwplwhmr rvsgttsdat nistsrwrpd efcqfspnsp avrnlleycg
      241 fteiarlkak aknlekryys grratfiaqr rrssqggrfp hsyggmnmpr hhpetnrags
      301 dkarpflagr sgr
//
LOCUS       WP_457661205             336 aa            linear   BCT 27-JAN-2026
DEFINITION  S8/S53 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457661205
VERSION     WP_457661205.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="S8/S53 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35295
     Region          99..305
                     /region_name="Peptidases_S8_S53"
                     /note="Peptidase domain in the S8 and S53 families;
                     cd00306"
                     /db_xref="CDD:173787"
     Site            order(123,164,273)
                     /site_type="active"
                     /db_xref="CDD:173787"
     Site            order(123,273)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173787"
ORIGIN      
        1 mvkgkavhfv deeqsdrrff mhktqwfpvg fvaglvalaa pgfagdlgaa vsgkgttgsp
       61 aaessssgcp qnadgtfcwm spdigqawas gfigsgvsin vsddftgqpi dgdlgrgtqr
      121 qrhgdwvaqi agmvapgani fkydyleefs ivlqdglnvi nasygmwepl sqhpreqaiv
      181 gaawagtaiv tksadnhsre vgqphvgdfd eltigligap savfvgaleh ngtpenkarl
      241 epysnyagsn pevqnhfltv gvereeigqr gtsfaapvva gyaailgskf tsatpiqitn
      301 qlldtartdt lvnynpaayg rgeaslsral apvsih
//
LOCUS       WP_457661206             507 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457661206
VERSION     WP_457661206.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 507)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..507
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=54004
     Region          4..451
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mpairkldir nfrgiknlsw tpspgfncli gpgdsgktsv ldaidlclga rriaaftdad
       61 fhdvdvsqpi sitvvlgale dalksidayg dflrgynagk neledepasg lettlclrlt
      121 vaqdlepvws lessraaakg ldrnlkwadr erlsplrlga ggdshlawrr gsllnklsde
      181 kpntsgvlsa aarearttfg dkakdqlkda idivnatakh lgisvgstat amldihsvaf
      241 gsgsislhde sgiplrgmgt gskrlltagl hkeasksksi alideietgl ephrivrflk
      301 slgskdtept mqvfatshsp ialqelsshq vfivrqdkag gqtlvlsaps evqgalrats
      361 ssflaksvli cegkteigfi rgidlfrtev rgkesidaag vslldcdggs etrpferaka
      421 fqalgyrvai fidndrpvpa veaktfveng gelfhwsegq siedaiicsa tgsvilaile
      481 aaervnpedl elldskiksa sggetgf
//
LOCUS       WP_457661207             361 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661207
VERSION     WP_457661207.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..361
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39719
     Region          1..361
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtsvsvrdls lnfgavtvld rlnldidhge flvllgssgc gkstllncia glldvsdgqi
       61 fikdrnvtwe epkdrgigmv fqsyalypqm tveknfsfgl kvakippaei drrvaraaei
      121 lqiqpllkrk pselsggqrq rvaigralvr dvdvflfdep lsnldaklrs elrveikrlh
      181 qslkntmiyv thdqiealtl adriavmksg viqqladpmt iynapenlfv agfigspsmn
      241 ffrgevetkd grsfvrvggv afdvtdypgq aklrtgqkvv lglrpehvkv deardgeath
      301 qavvdieepm gadnllwltf agqsmsvria gqrryppgst vrlsfdmgva sifdagsenr
      361 l
//
LOCUS       WP_457661212             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661212
VERSION     WP_457661212.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37810
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maflqltniq ksfgpvqvvh nfdmgidkge fvsflgpsgc gkttilrmia gfetpsggti
       61 fidgkdqgal kpnqrnigmv fqayalfpnm nvhdnvafgl kvagnskpei dkrvkqmlgl
      121 iklehladrf pyqlsggqqq rvalaralav kpqvllldep lsaldakirv slreeirqiq
      181 qqlgittvfv thdqeealsi sdrivvmnag radqigtpfe iyntpatrfv asfvgtlnii
      241 egkvadpaig avtiggqqis lsepitgakg gdsislalrp eagsiaegar gdtalpgkvv
      301 srsflgsvir tklrvgedii sfdmfndpgm ippvagesvt lrfaakdllv ire
//
LOCUS       WP_457661211             582 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661211
VERSION     WP_457661211.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..582
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=62617
     Region          36..566
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 msflsrimvl kskahfsagg dhrttdggln vtfegtrkrs asraksrvai miasfgvvya
       61 viggrlvqyg laqpetvssi gradtlmasr pdildrngev latdirtvsl yaephkivda
      121 deaverlatv lpdlnareiy nklksdsrfq wlrrqltpkq qseilalgip gigfrpekrr
      181 fypggptaah ilghvnidnr gvagmeryid eqgladlaai gmtsdaklep vrlsidvrvq
      241 nivrdvvdsg mknyeaiaag avvldvhtge vlamasvpdy dpnrpaegae egwmnrmsng
      301 tfemgstfkt ftiamglnsg kvtlndsfda trpiriggft ikdfhgkrrv ltvpeifqys
      361 snigtakiad ligipghkef ltrmglltrl ptelpevksp sqprewkkin sitisfghgv
      421 sttplqtava gaalvnggkl ippsflprse eeaselasav vkkstsddmr yllrrngiag
      481 sgkralvpgf nvggktgtad kvvngryasd lnfnaflaaf pidnpkymvl tfidapktge
      541 gggrtagsna apmvrdiisr sapllgvepk fgedgsallv sy
//
LOCUS       WP_457661214             307 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661214
VERSION     WP_457661214.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34560
     Region          1..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 masvthssar rsrfriskrv lpyvlslpal lvcigilipf ftaviysfqr yrlsqpwarq
       61 fnwgdnylnf ftdpgfwntl kisllyagvt vtlelllglg ialllqrrst vnnfisimll
      121 lplmtapala almwklmtnp gfgilsylas liglenfrwa sspdtalltv vlvdiwvytp
      181 fimilllagl rslptqpfea aaldgvprsf vffritlpml tpyiltatlf rllnsiqqfd
      241 iiyamtqggp gdtltvfqve aylnffqstn vgrsaallii lwaityilsn ifiknwlrlr
      301 erargea
//
LOCUS       WP_457661215             275 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661215
VERSION     WP_457661215.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..275
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29328
     Region          22..261
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mnlrtipfsa wigiigiaia ifcalfapll apfgerevvg dvwlpaggdf llgtdnlgrd
       61 llsrliygar ttifvalaat visfalgmil sftaavtggf vdqffsrfnd lmmavptlif
      121 alvvlavlpq hlwilvlvma vlnstrvfri gravaldvav mefveaarlr gegtvwiifr
      181 eilpntlspl laefglrfaf silflstlsf lglgiqppaa dwggmvkdnk dgiifgisaa
      241 lipggaiaal aicvnlvvdw lmkrtsslkg grgda
//
LOCUS       WP_457661217            1103 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457661217
VERSION     WP_457661217.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1103
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=119879
     Region          1..1036
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnfsawsirn pvapilaffv lvvlgwqsfn slpitrfpni dvpivsiavt qsgaapaele
       61 tqvtkeieda vagvtgvdhi estitdgist tavifrmevp ttqavqdvkd aidrirsdlp
      121 tsieepivsk vdvegqaiqt fsvsspgmtl eelswfvddt ikraiqgqtg igrvdryggs
      181 drevrvelde drlnsfgisa advnaqlrrm nmdlgsgrgq vggseqairt lgdtrdvtal
      241 adtmialpng rfvrlselgk vidtyeepks farfngqpgv tfavfrakga sevsvaetva
      301 ktlddirakh pdvsiemvdn svyftygnye aaihtliega vlavivvmlf lrnwratlis
      361 avalplsaip tfwvmellgf slnlvsflam tlatgilvdd aiveienier hirmgkspyr
      421 aaieaadeig laviattfti iavfvpvsfm pgipgqyfiq fgltvavsvf fsllvarlit
      481 pvmaaylmkp sdasghddde gfmmrqytrl vrfttkrwyt rystllaail lsvgsviall
      541 vfvpgsflpp edssrvslsi elppdamlad tdrttteiyn rikdvegven vfvlggaspk
      601 gdlelrraav tvllrkldhs linkvvndvi grtpligeyl pklppagrii pqsaiereif
      661 arlrsipdvr vtklndrger dlsfnllsnn eadldkavat leadlrrdpl lanvspegal
      721 prpelqirpr deqmsrlgit taqiseviri atigdidaql tkialdgrli pirvqlnrdf
      781 rtdlaairnl kvqtasgatv plssvadiny aegpssikry dryrvvklga dlpagvaldt
      841 asarfrqiaa daelpatvqf lesgdaevqa emqesfgnam llglmmvlvv lillfkdviq
      901 pftilfslpl aiggvaaali ltqnalsmpv ligilmlmgi vtknaillvd fgiemmhhgm
      961 drtlamieag rkrarpivmt siamsagmlp salgvgeggs frapmaiavi ggiivstvls
     1021 lvvvpsffli mddlsrllaw tfgrfigkkd eeelpldqea lsklaaeqgs tiesleervk
     1081 aledekrrks drkvishpal aae
//
LOCUS       WP_457661219             257 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661219
VERSION     WP_457661219.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28071
     Region          60..195
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maakpsgpqg drprrlrasp qsappqsapp qsaspesapp esgssksleg prtepslsld
       61 rivaaavell dtrgvdglkm rqladrlgag amslywhven kemvfdlald svlayrgppq
      121 kaesrdwrge vfhmledwra smlrhpwsas llprralgpn ilsrlellsn tlsragvada
      181 dlnaaiwslw nyvigatvtr asfvlsdedr svaqqrltgl gehyptiers rllldddwdg
      241 afrkgldfll dglaprs
//
LOCUS       WP_457661221             177 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457661221
VERSION     WP_457661221.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..177
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19364
     Region          50..166
                     /region_name="VapC"
                     /note="VapC family ribonuclease, contains PIN domain
                     [Defense mechanisms]; COG3742"
                     /db_xref="CDD:442956"
ORIGIN      
        1 mnaltamiaa rsrsengmkq sgtrpkssas lndrrgfiry hcdhvrwrge asaciaalqk
       61 srsrlisavn yvetgtvmag rvrsgdrcea iadldafltv fridiapvdd rtaraamkar
      121 idygqrfgtr gglnfgdcfa yalekqrsap llyagndfgt tdinpalkap slrrtkr
//
LOCUS       WP_457661223             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661223
VERSION     WP_457661223.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39580
     Region          1..346
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 marinlehir haygakpkse sdyalkevhh ewndggayal lgpsgcgktt llniisglin
       61 psegrilfdg tdvthlttqq rniaqvfqfp viydtmtvyd nlafplrnrr vpetevdrrv
      121 keilemtglv swakktargl tadqkqkisl grglvrsdvs ailfdepltv idpemkwvlr
      181 sqikrlhkqf gftmvyvthd qtealtfadk vvvmydgqiv qigtpaelfe rprhtfvgyf
      241 igspgmnvlp aeiagstasi gdqrialdfr pevkagtkte lgirpefisl gregmpvavt
      301 kvedigrhkv vrarfadrpi siivdedgei paeprvtfdp kainiyansw rvggea
//
LOCUS       WP_457661228             342 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Sinorhizobium medicae].
ACCESSION   WP_457661228
VERSION     WP_457661228.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37082
     Region          9..331
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mdapvntnll elyrtmrrir tfeervgelf vrgqsagsml hlsigeessa agacaamkpq
       61 dtftthhrgh giflargadp krmmaeiggk etgycrgkgg smhiadmalg hlganaivgg
      121 gipavigagl ssrhlkqdsv siaffgdgam qqgilyesmn maslwnlpvl fvcinnqygm
      181 gtridqatrn tafdqrakaf glngavvdgl dveevqaaar wlvdearagk pgflsvevyr
      241 ffgharmdks pyreeaeele grkkdpvlfa rnklidtgie eerildeldk aiaaemdati
      301 dfaveskapp lgsmfkdvya agepepesvr aridrvlard da
//
LOCUS       WP_457661235             503 aa            linear   BCT 27-JAN-2026
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661235
VERSION     WP_457661235.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..503
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52893
     Region          2..503
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mpegasgvtf vfggvriega avlpeaklla dwphkagdtv rvdeifalae sisqayreag
       61 yalsfamvpq qqidggvfri qvvegfverv vikgdlseav radmqafadr ilasrplrta
      121 dlerylllin dmpgvtasgv lspaaveaga vltleaahep vagsvgynsf mpdtlgthvl
      181 easggmqgvl tgsgsvsltv rrslmpdayl gvsgdasvgi gteglrvgvs glwsridprd
      241 illdvidykg slvsaqlygf ypiirsreen lsigasfsld ndnstilttd fvddrlrsvs
      301 vwgrydfvdq travtslrga lthgvdlfga tgnsrangvv kytkveldaq rnqpladvlg
      361 galslqatah aqaalgsgal fsapecsfgg rrfgrgfdsg iltgdhcamg svelhwvrsv
      421 dfpdlgapvf ldfyafvdgg vvwqkgevls gepgrghaas lglglsvqft aeasgllevs
      481 rpvslsvgtp detrilgals frf
//
LOCUS       WP_457661244             159 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-70 family RNA polymerase sigma factor [Sinorhizobium
            medicae].
ACCESSION   WP_457661244
VERSION     WP_457661244.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Davis,M.C., Kesthely,C.A., Franklin,E.A. and MacLellan,S.R.
  TITLE     The essential activities of the bacterial sigma factor
  JOURNAL   Can J Microbiol 63 (2), 89-99 (2017)
   PUBMED   28117604
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Campbell,E.A., Westblade,L.F. and Darst,S.A.
  TITLE     Regulation of bacterial RNA polymerase sigma factor activity: a
            structural perspective
  JOURNAL   Curr Opin Microbiol 11 (2), 121-127 (2008)
   PUBMED   18375176
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Mooney,R.A., Darst,S.A. and Landick,R.
  TITLE     Sigma and RNA polymerase: an on-again, off-again relationship?
  JOURNAL   Mol Cell 20 (3), 335-345 (2005)
   PUBMED   16285916
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Wosten,M.M.
  TITLE     Eubacterial sigma-factors
  JOURNAL   FEMS Microbiol Rev 22 (3), 127-150 (1998)
   PUBMED   9818380
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Helmann,J.D. and Chamberlin,M.J.
  TITLE     Structure and function of bacterial sigma factors
  JOURNAL   Annu Rev Biochem 57, 839-872 (1988)
   PUBMED   3052291
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11495650
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..159
                     /product="sigma-70 family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18071
     Region          11..156
                     /region_name="sigma70-ECF"
                     /note="RNA polymerase sigma factor, sigma-70 family;
                     TIGR02937"
                     /db_xref="CDD:274357"
ORIGIN      
        1 mtattaprpp eidamllanw nklrkyalrm tpnvdeadsv msdmteailt hwatyrpdgd
       61 fltwckltir srasnrrrmi rhryehvevd feklvygagq dhlvdlksal qsidsdtrrl
      121 vmlaaegyth aaigkmigrt gervcqrlkh arakmrgda
//
LOCUS       WP_457661250             270 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457661250
VERSION     WP_457661250.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..270
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29558
     Region          1..255
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mhekerhrii lsavqekpva tvpelvdltg sseatirrdi aalhvqkrlr rvrggaeain
       61 ppqfvglagr pfrvneglha rekqaiarea valcqdgepi iinggtttfq mvhflanrrm
      121 qvftnsfpia ehllkhsknt vmlsggtiyr eqniilspfe ndvtrnfyar rmfmgaqglg
      181 plglmeadpl liqaeqklid qaddlvvlvn sskfhrrssl ilcglkriat vitdagiedr
      241 hasmlenagv slivaaqsar adaekastsa
//
LOCUS       WP_457661254             369 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661254
VERSION     WP_457661254.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39733
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtglllknir ksygavdvih ginleikege fvvfvgpsgc gkstllrmia gleeitggdm
       61 fiagervndv ppskrgiamv fqsyalyphm tvydnmafgm riareskeei drrvraaadm
      121 lqltpyldrl pkalsggqrq rvaigraicr npkvflfdep lsnldaalrv atrieiakls
      181 eqmsdttmiy vthdqveamt ladrivvlsa ghieqvgapl elyerpanlf varfigspam
      241 nvipaaitat gqqtavtlag gksvtldipt nasengktas fgvrpedlqv tgtddflfeg
      301 tvsivealge vtllyieglv enepiiakmp giaqvgrgdk vrftadkakl hlfdtrgakl
      361 sgvvqrggg
//
LOCUS       WP_457661255             289 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661255
VERSION     WP_457661255.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..289
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30718
     Region          65..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mnkpvitqam idaydeythl tldrrrfmek ltalagtaaa aaaiapmlaa nsakaeiiae
       61 tderikgedi typggdgemk gylvkpaems gklpavivih enrglnphir dvarrmaleg
      121 flalapdfls peggtpgded karemigald asatnanatv aflkghaest anvgaigfcw
      181 ggglvnrlav napdlkagva yygaqpkaed vpkikaalll hyaglderin agieayrkal
      241 tengkdatih vyegvnhafn ndtsaarydk eaadlawqrt veflkakla
//
LOCUS       WP_457661259             116 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661259
VERSION     WP_457661259.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..116
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12260
     Region          <1..>108
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mglipaiddd glvlteslan nlylarkhgg plapadvree gqignwtmwa atevepyave
       61 ivlaydkgie ntpegqteia acaraleraf avleahlagr dhvvggslyc cgpqsr
//
LOCUS       WP_457661261             743 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661261
VERSION     WP_457661261.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..743
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=82022
     Region          57..675
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mrqnlrdmkt vqeprkednr pkrrhiflri dswidstvws agfrlaewwe dttiffrrfr
       61 vrgwkkalfe vlgegmtlga agsvlmlala lpafeettgn wraqsdfavt fldrygneig
      121 hrgiihedsv pidelpdhli kavlatedrr ffdhwgidfl glaramtena raggvvqggs
      181 tltqqlaknl flsnertier kikeaflavw lesnlskkei lrlyldraym gggtfgaaaa
      241 aqfyfgkait dvnlaesaml aglfkapary aphvnlpaar aranevlsnl vqgglmtegq
      301 viaarltpas vvdraqvkap dffldwafee vqriaapfaq hslivrttid mglqqaaeea
      361 velglrqyge tykvkqgalv mvehggavra mvggrdyges qfnratralr qpgssfkvyt
      421 yaaamekgmk petvvvdapi twrgwspqny arkyagrvtl mnalarsint vpvrlakdkl
      481 gteiiaetak rmgietpirt dktmplgtse vtvldqatay avfpaggfqs rrhgisqiln
      541 ydgdilydfg rdatparrvl seeaassmnr mltqipvigt arraaldngi vtggktgttq
      601 ayrdawfvgf tgdyttavwf gnddytstde mtggslpamt fkrlmdyaeh giehraipgi
      661 eapsepakqq paetakkddn alpplvrprs lsadvtrllk kiggtfekaq plkarerpgg
      721 kvavletpsq gshirplrnt tnn
//
LOCUS       WP_457661263             104 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Sinorhizobium medicae].
ACCESSION   WP_457661263
VERSION     WP_457661263.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..104
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11795
     Region          2..88
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mrifefvvvs ddleafmvag rknvqtsvrd epgvlsmhcv adksdptkly vvevyededa
       61 yrshvesahf rdfinaikgk visrrvietn pkmvgskqfa wteq
//
LOCUS       WP_457661268             251 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457661268
VERSION     WP_457661268.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..251
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26059
     Region          4..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mklgleekia ivtgggsgig aavsrqlgge gaevivadrd adaartvaae irsnggkard
       61 ftvdvansaa veqmvafavr ecgglhlavn nagvegprra tadypledwr rlievnlngv
      121 fycmkyeiaa mlgkgggaiv nmssilgava lptasaytaa khgvvgltka agieyarmgi
      181 rinavgpgwi etpllsehse laktrrleal qplgrrgkpe evaslvcfll seqasfitgs
      241 yhpvdgafta h
//
LOCUS       WP_457661271             164 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661271
VERSION     WP_457661271.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   3  (residues 1 to 164)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..164
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17694
     Region          2..>155
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mvaregnvta aaeklgisqp altrsirrle detgfrlfdr htrgvtptiy gkallrhaql
       61 idtecrfass elealrsghr gqikigggpf wgaallprav arlhsllpkl qvnlqigvnn
      121 vlhpklldge ldlvvsaapp rsiaisgafp lysdhdhtep dvcp
//
LOCUS       WP_457661276             484 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457661276
VERSION     WP_457661276.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 484)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..484
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=52769
     Region          1..446
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mrlsklgirn frnfkfvdip lhgnivllge nrvgksnllf airlildpal pdaarqlrls
       61 dfwdgcpadf sqpievhldi adfagdpalv alltdfrvah dpsiarlsyv frkkaevtgp
      121 aqssedcefl vygggvetrt vpgkvrrria idvldalrda egqlatwrts pirhlleeav
      181 agisradlda vaaeldkatk sleafptika ledelragil hlsgkahdvd arlrfapsdp
      241 lrlfraiamf idggkrgiae aslgsanval lalklaefaw rrrknernfs llcieepeah
      301 lhpqlqrsvf kkllneasaa qtmvvtshsp tlaavsplrs iiqlrtrdra tqayslanlp
      361 vtpeelddle nyldatraem lfargvihve gdaeealvpv faaslgfnld dlgitvcnva
      421 gtnfgpyvkl tealgvpwsv itdwdpmdgs qppqapagpe arhrplaghi ggaresthgp
      481 rdtr
//
LOCUS       WP_457661292             569 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661292
VERSION     WP_457661292.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 569)
  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 569)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 569)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 569)
  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 569)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..569
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63034
     Region          26..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
     Region          297..569
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mhsrpclttw lylsplhlll lamltvpsly vfwlslngss ygtgltwvgl enyravfddp
       61 yfwraalntf lvvngvvyve llfglalaal fvsgvpfrgv mfacilmpya isevvavlvw
      121 kmmmdpniga iartieelgl grvnwsasps tglvlvgvin iwthlpftfl miyaglltid
      181 gslyeaarid gasrwqrflr itlplliptl litlifrlif afrmfsevwl ltkggparls
      241 evlavylyqh gfrygdfgma aatgwlmvlg slllasvflf amqrgikggr amsdafspie
      301 rfarglllgf iliwsvapil fivsssfkrq vdifvyppki vfiptfdnyl kltsqwqdff
      361 tsmgnsliaa igatvlagiv sffggyaysr yrsritawsa vymiavrvlp pivvtlplfp
      421 vadllglgdt hlllillyat fwvslntmim knffdqipye ldeaayvdga sewqlvsqil
      481 arltlqgmta gsifvfvfsw neylfamift tnqaktapli lselmgavdg tewgvlfagv
      541 slqllpvvll vtlarrylia gltagavkg
//
LOCUS       WP_457661298             494 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661298
VERSION     WP_457661298.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..494
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55011
     Region          189..438
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 megvlgerss rqllnndmpd mvmvasener lrrcmndils vtalpaawtg gtvdgicsal
       61 ldalrsildv dflvvnvags gdqaevlker srtnfvdaga viisdlvrtl ganiavwpre
      121 tnvehgeadl rvlieklgvn gkvgvlvags tvssfpteed rillhvaacq aalaiteair
      181 frhdtravae relnriadai pvmawstlpd gradffnehf ltflgitseq aagwgwaasi
      241 hpddsralqs vwmellasgm pgetearlrr wdghyrwflf ranpvysdeg avvrwygtnt
      301 diddrkrfee emrrsaalma qaqrltvtgs vwwrpatndi ywsdeayrva gqdvgitpsv
      361 emmldrchpe dlpriqklis namnrgenvd vehrllmtdg avkyvhvvlq nignnpadpe
      421 figavadite rklaeeqlrr sdvllregqr isqtgtfswk vetdeitfse elnrifgfes
      481 grvvdfdaig qrvl
//
LOCUS       WP_457661301             642 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661301
VERSION     WP_457661301.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 642)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 642)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 642)
  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   6  (residues 1 to 642)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 642)
  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 10170692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..642
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72047
     Region          54..618
                     /region_name="PBP2_NikA_DppA_OppA_like_4"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08500"
                     /db_xref="CDD:173865"
ORIGIN      
        1 mqefsrrafl lastaavllp vmpvialans akepamleal akagslpava drlplnpmvv
       61 tpldrvgthg gdwnsaivgg gslsmlfryq ayepllryap dwsgvvpnva ehyesnadat
      121 eftfrlrkgm kwsdgepftt edilfwyedi fnyeglndvg qnhlraggkk arfeavddvt
      181 fkvifaapng lfplrlawan ddqttrapkh ylkqfhikyn pnaeeeaktk gasgwiqlfq
      241 reaglvvdne ffqnsqrpvi hawkvaiapg qstdravaer npyywkvdte gnqlpyldri
      301 vyqmvsdpqv lllkamqgei dlmdqyiatp anravlydsq eqgkfgfytl tstetnemvf
      361 qlnlnhpnev krklynnkdf raalsmaldr qaiidtvfig qgtisqpavr addplynerl
      421 atqytqydpd ranalldkil ptkdsegfrl deggkrvsii feidqaratf ldifqlalpt
      481 fravgldvqm rsmdrslwev rvrqgieyda tahrfggngg iaaildpryf ipnttealya
      541 kgwqlwyrds qsqgaveppq pvrnalalyd rvlasadpde qkklmaeile iaadqfyvfg
      601 iclpadsygv vkndmqnvpe ampnswgypt pgpanpetff kv
//
LOCUS       WP_457661314             510 aa            linear   BCT 27-JAN-2026
DEFINITION  malonate--CoA ligase [Sinorhizobium medicae].
ACCESSION   WP_457661314
VERSION     WP_457661314.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..510
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55421
     Region          1..502
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(159,162..167,169..170)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(162,202..203,206..208,248,250,254,276..278,297..302,
                     306,321,381,393,401,404,407,436,472)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(162,276..278,297..302,321,381,393,401,407)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(202..203,206..208,248,250,254,276,298,300..302,306,
                     404..406,436,472)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 msnhlfdair rasrpdfvfi laadervwty gdmlehsgrl asalvslgvq pgdrvavqve
       61 kspealmlyl aclragavyl plntaytlte ldyffgdaep rlivcapaak egiskiaayr
      121 sagvetlddk gggslielal getpdfsdld rraddlaail ytsgttgrsk gamlthdnll
      181 snavtlrdhw rftaddrlih alpifhthgl fvasnvilla gasmfflpkf danevlslmp
      241 rsttmmgvpt fyvrlvqnpg ltrevtagmr lfvsgsapll aethrtfahm tghaileryg
      301 mtetnmntsn pydgeriagt vgfplpgisl rvadpesgkp lpngdtgmie vkgpnvfkgy
      361 wrmpektqae fradgffitg dlgkidergy vhivgrgkdl visggyniyp keveteidqm
      421 pgvvetavig vphpdfgegv tavvvrkpga tiderailgg legrlarykq pkrvifvedl
      481 prntmgkvqk nvlreayadl yaeagagari
//
LOCUS       WP_457661325             187 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661325
VERSION     WP_457661325.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 187)
  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 187)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 187)
  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 10583968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..187
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20549
     Region          2..>167
                     /region_name="Ferritin-like"
                     /note="pfam12902"
                     /db_xref="CDD:403953"
ORIGIN      
        1 mqlalelewa tlppylvall sikgpqnrea adlirgvame emlhfalvan vinaiggrpv
       61 vakencptyp mrmtfegrpf adrtfpinlg cfskesistf mkieqpqepv iktawldtvi
      121 dvpaptigef yeeiksilre ldaalpeglf vgdpahqlgg dffwgggrrn qgghrsrlra
      181 ggtrdrg
//
LOCUS       WP_457661327             523 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661327
VERSION     WP_457661327.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..523
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57117
     Region          1..358
                     /region_name="SsnA"
                     /note="Cytosine/adenosine deaminase or related
                     metal-dependent hydrolase [Nucleotide transport and
                     metabolism, General function prediction only]; COG0402"
                     /db_xref="CDD:440171"
ORIGIN      
        1 mdttfnvfad givwieanri iavadagask pvgfehiqpv vtggtifpgl ielhnhlayn
       61 vlrpwdvpkp yanreewrdd edykaivndp mnvlgkssgv apaiarytea kcllagttts
      121 qgitlssnlg mkryyrglir nveesldsnl pdakaripny rpkdkeqflk dlkdyecfll
      181 hlsegigdda rsyflgleie pgswaiapsl tgihctalka edferlaqng agmvwsplsn
      241 lmlyggtadi kvaraagiri algsdwspsg sknllhemkm awrysefsgg ifsrreivam
      301 stisaagllr wdrylgslet gkyadlivir gdqsdpyeal lnadetsidl vvvdgvprsa
      361 rpalaagfsk tselvafane rrminfddaa adqavaglsl saaekilkea maglgnplai
      421 lakvspysqw radlpptqee wtivldeeee nghdtvpqfd gsakipeilr dakhtspmap
      481 lstplkpqel dkltvagddd yypsflaqkn ipetiklalf pgq
//
LOCUS       WP_457661330              99 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661330
VERSION     WP_457661330.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..99
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=10359
     Region          <11..98
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mlppaelppa hpirfgtgvh vgevmygnig skrrldftvi gpavnlasrl egltndlkrp
       61 vlvsgdfvta agcsaktdcl glhsikgfdd alevhalrl
//
LOCUS       WP_457661346             565 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661346
VERSION     WP_457661346.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..565
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=61591
     Region          <1..>501
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlldregplk vllaagrsaa lghgsivvve geagigktsl lrefaehsdn gcrvlwgwce
       61 alftpcplgp lqdmgqlldp rvaallkqaa pperlfpall nalqhsgdti ilifedvqwa
      121 dnatldlvky lgrrisllpt vlvltlrsde igadhplthv lgdlpsasvs rialqplsre
      181 avaalteqsg rcaddlyrit egnpffvtel lasetepgri phsirdavwa rlsrltager
      241 kalevisivp ggvepwlvra llgveadtll dqclargllr rdgqgavmfr helarqatle
      301 rlppslqrsl hsiveaaisq lvttkapall vrrvhhaasa edgarvlela pqaaahaahl
      361 gahrdaashl atalryiaqa tpeqaaqlye dwayeaglal dvyepvieah hraidiwrel
      421 griekigpnl crlsrlhwrr gegkaaedca dqavcemerl ppgpelamay strsqlhmlh
      481 yrfdeaiewg lraialadql gqietrvhal nnvgtallfs drpggrdrtr rnacagarar
      541 vprpcgpslh qlrgmrgivq rlrag
//
LOCUS       WP_457661348             531 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457661348
VERSION     WP_457661348.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..531
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58667
     Region          6..436
                     /region_name="YSH1"
                     /note="RNA processing exonuclease, beta-lactamase fold,
                     Cft2 family [Translation, ribosomal structure and
                     biogenesis]; COG1236"
                     /db_xref="CDD:440849"
ORIGIN      
        1 maieptirfh gaagtvtgsc qlvefgatki lvdcglfqgs ktekelnyrp fpfdpktida
       61 vilthahidh tgllpklarl gyegpifatp attdlcsvml pdsahiqese vdqlnrrnlr
      121 rgrqtvtpiy tardaaaait lfrqvrlgsw eqagggirfr fwnaghllgs asvemeissg
      181 plplrvlfsg digprhkllq fdakapigwd yvicestygd vereeagdaa rrhvlrsevl
      241 taahpngall ipsfavertq elltdlvylm etgavpkcpi iidsplatra seifrrhape
      301 lengdalvrg ielknvrfte taeqskavdf irgfhiviaa sgmceagrir hrlknwlwrd
      361 eatvllvgyq angtlgrlle egatavriqd ddirvrarir kldiysghad gseladwvra
      421 rqpisagvfl vhgedealeg irerlstflp qdhlirprld safrlgshga vqiseavapp
      481 ridpvragst dwhndfqklv ldlqdelaka addkargvvi rrlrralqee l
//
LOCUS       WP_457661350             125 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Sinorhizobium medicae].
ACCESSION   WP_457661350
VERSION     WP_457661350.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..125
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12814
     Region          42..>109
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 miygrrhdpl aygspplqqt sagaaggpvs ncgsahaisr aaqqadggpl frqrcatcha
       61 vdpgenkagp clasiagrpa asvdgahysk alksagitwd rqsldaflat epfslrhtnd
      121 gphpr
//
LOCUS       WP_457661359             285 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661359
VERSION     WP_457661359.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..285
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31253
     Region          1..284
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mvafvrtvet gsfsaaaksl gltpsaasks vsrlelllga klfrrstrtl slthegdafy
       61 glvmplmrqi esatevvrpk hqasghlrvg ppgdlgiqil kpvftefmse hpaisfeist
      121 tdrhvdilre kfdvvfrvge vqqnalisrt iahldmalva spifvaqwgl vedvrrlqkl
      181 pfarytmagr hypirfvngt eivpegrvdl dsasaireav isgvgaghlv rrlvqedidq
      241 griiellpsm klqtvplqai hvsgnmpphr ltllvnfvag amrra
//
LOCUS       WP_457661360             286 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase [Sinorhizobium medicae].
ACCESSION   WP_457661360
VERSION     WP_457661360.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 286)
  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 286)
  AUTHORS   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..286
                     /product="nitroreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32042
     Region          73..282
                     /region_name="PnbA_NfnB-like"
                     /note="nitroreductase similar to Mycobacterium smegmatis
                     NfnB; cd02136"
                     /db_xref="CDD:380313"
     Site            order(74,91,94..96,98..101,103..107,109..115,199..200,
                     202..208,211..212,215..216,218..219,223..224,232,235,237,
                     254,273..276,278,281..282)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380313"
     Site            order(74..76,78,101..105,188,209,212,229..233,255,273,275)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380313"
ORIGIN      
        1 msqdgcdrse aaraisfesl gpcvqadell ktrrrnslls aqknergavm hanakweesv
       61 vdrstiidqv mierrakrgf lkdpvsldtv rdilnaarha psssntqpwk chvltggard
      121 rittkavdif ragpdklape ypffpqplhd pfiarfnlfr gqlgdavgvp rsdkygrlkd
      181 verqfrffea pvgmiftmdr klewasficy gcflqtlmla akargldtca qqiwslqhnm
      241 lreelglads dmvvaglslg yadnslaenn manhrldiee fvtfvs
//
LOCUS       WP_457661364             326 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661364
VERSION     WP_457661364.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34310
     Region          36..319
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mkrflkiyld kpelaglall ivlvlvfqak sngillsfen irgvmgllpe malvaigvtl
       61 lmicgefdls vgsvfalmpm smavilnsgv pftaavllgl micgavgfin gyvtlqfsip
      121 sfittlgmlf iarsltivis ggfppllppd lptwlftdyi ggspfrmsfl wfvviaalva
      181 allsltnfgn wiratggfne aaasmgipvk rvkiacfmlc svlagfagll qvlrlgsplp
      241 sigeglelqa vaaaviggta laggigtvfg aivgtllirt idnglvlsrv danwfkfaig
      301 vltmfavian awmgkmsrki kveaqk
//
LOCUS       WP_457661365             295 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661365
VERSION     WP_457661365.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..295
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32934
     Region          1..245
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mhlsthnwmr aeplavtlkr ikkygyesie isgepaqydi kdtrallkeh gircwgavtl
       61 tlgernlaak desqraksvd yvksvitmvs elegeivtlv patvgklipd ateeeewtwv
      121 vdatkecfah aqkkgvrlav eplnrfetyl fnraaqaial adavspecgv cldafhlnie
      181 eediydairl agnrlldfhv adnnrfaagl ghldwpkiva tlkeigydga ltnefvapvd
      241 rtpaakypdm vertpvdipp eqlkfiqdhg sslltekfyd dqmritaeti lplik
//
LOCUS       WP_457661366             580 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoethanolamine transferase [Sinorhizobium medicae].
ACCESSION   WP_457661366
VERSION     WP_457661366.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Needham,B.D. and Trent,M.S.
  TITLE     Fortifying the barrier: the impact of lipid A remodelling on
            bacterial pathogenesis
  JOURNAL   Nat Rev Microbiol 11 (7), 467-481 (2013)
   PUBMED   23748343
REFERENCE   2  (residues 1 to 580)
  AUTHORS   O'Brien,P.J. and Herschlag,D.
  TITLE     Functional interrelationships in the alkaline phosphatase
            superfamily: phosphodiesterase activity of Escherichia coli
            alkaline phosphatase
  JOURNAL   Biochemistry 40 (19), 5691-5699 (2001)
   PUBMED   11341834
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..580
                     /product="phosphoethanolamine transferase"
                     /EC_number="2.7.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016772 - transferase activity,
                     transferring phosphorus-containing groups [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0009244 - lipopolysaccharide core region
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=64158
     Region          44..576
                     /region_name="OpgE"
                     /note="Phosphoethanolamine transferase for periplasmic
                     glucans OpgE, AlkP superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2194"
                     /db_xref="CDD:441797"
ORIGIN      
        1 mlnadiatld apfrslsafs fsasdlriha reeagllnki kthrprlrse wlsilttvyl
       61 lfflnatfwd ksflylkgqg falvalaigl laafvaltvt fsakylikpa lifmvlasva
      121 sawfmdrfsv iidtemirna letnraeagh litgafvlhi ilfgvlpslf iawvevihra
      181 ilkkvmvnlv iivpsllvfa gaglsnggtf ifstrehrdw frtlnpifpv gsaasflvdq
      241 sreqsiilqp igtdakvada lpsadrrprv tivvvgetar aqnfqlggya retnpeltkr
      301 diiyfkdtss cgtatavsvp cmfsvydrkd yshakalate nlvdvlshag iktewwdnnt
      361 gdkhvadrik ktdlfksndl rfcdggecld qilvdgldaw ldkvngdavl vlhqlgnhgp
      421 ayylrypeef rkfmpdcrsa dfdtctpeti tnaydnglly tdhilaevid tlsahgdrld
      481 tamiymsdhg eslgenglyp hgapymfapt qqthvpfvlw ispglqqstr iekpclaaka
      541 dvphshdnlf hsvlglmqvk tqvhdpaldi faacrdgvss
//
LOCUS       WP_457661374             229 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiX family flavin prenyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457661374
VERSION     WP_457661374.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 229)
  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..229
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..229
                     /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=24272
     Region          31..212
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mgtracyagg scregrsild rtgpgrsami kerivvgvsg asgaalalrv verlaeipsv
       61 ethlivsaaa krtllhevgp halhqllaia drtyqvgdig aatasgsfrt agmivvpcsm
      121 rtlaaiaagv adnlivraad vhlkerrrlv lmtretplhl ghlrnmtavt emgavvlppv
      181 pafyhrpksi eeiidhlaar aiglfglpge pfatewdpqs hrphcavar
//
LOCUS       WP_457661390             571 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Sinorhizobium medicae].
ACCESSION   WP_457661390
VERSION     WP_457661390.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..571
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63204
     Region          52..481
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,316..317)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,317)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mkpisesrlg ataaaiarsq gwkafalagt ilvssvvtts spasaqdapg kpnilvifgd
       61 dvgqfnlsty sfglmgyktp nidriadegm kftdyyaens ctagrssfit gqtpkrtgls
      121 kvgipgapvg lqdrditiaq alkplgyatg qfgknhlgdr deylptahgf deffgnlyhl
      181 naeeeperpy wpkddlayvk ansprgvihs yadgriedtg alnakrmeti ddettsaaie
      241 fmkkqveqkk pfftwmnttr mhvfthvrps mlgqsgmpgn eyadgmiehd ghvgkllkal
      301 ddmkiadnti viyttdngpn qfswpdaatt pfrsekdtnw egafrvpami rwpgkikpga
      361 vsnemfsgld wfptllaaag egdikekllk gtdvagkqfk vhldgynqlp yltgeteqga
      421 rqefayfndd gklvafrykd wkavfcemka pggfrvwyee fdclripklf nlrmdpmera
      481 dtvsdqyddw riknaymmgw mtfhaaqfle tfvdyppsqt pasftidqie adverrsaek
      541 aggeqivhga crlsstrpis ssgasplpar s
//
LOCUS       WP_457661383             510 aa            linear   BCT 27-JAN-2026
DEFINITION  malonate--CoA ligase [Sinorhizobium medicae].
ACCESSION   WP_457661383
VERSION     WP_457661383.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..510
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55405
     Region          1..502
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(159,162..167,169..170)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(162,202..203,206..208,248,250,254,276..278,297..302,
                     306,321,381,393,401,404,407,436,472)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(162,276..278,297..302,321,381,393,401,407)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(202..203,206..208,248,250,254,276,298,300..302,306,
                     404..406,436,472)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 msnhlfdair ralrpdsvfi ltadervwty gdmlehsgrl asalvslgvq pgdrvavqve
       61 kspealmlyl aclragavyl plntaytlte ldyffgdaep rlivcapaak egiskiaayr
      121 sagvetlddk gggslielal getpdfsdld rraddlaail ytsgttgrsk gamlthdnll
      181 snavtlrdhw rftaddrlih alpifhthgl fvasnvilla gasmfflpkf danevlslmp
      241 rsttmmgvpt fyvrlvqnpg ltrevtagmr lfvsgsapll aethrtfahm tghaileryg
      301 mtetnmntsn pydgeriagt vgfplpgisl rvadpesgkp lpngdigmie vkgpnvfkgy
      361 wrmpektqae fradgffitg dlgkiddrgy vhivgrgkdl visggyniyp keveteidqm
      421 pgvvetavig vphpdfgegv tavvvrksga tiderailgg legrlarykq pkrvifvedl
      481 prntmgkvqk nvlreayadl yaeagagari
//
LOCUS       WP_457661392             188 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661392
VERSION     WP_457661392.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20480
     Region          2..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marikefdke evldaaiavf rehgfegtst emlvramnig rqslydtfgd kwklyrlave
       61 rysaeetray iellrgtpra ldgirsmmar vvenagqacl gvnsicefgq srpdltalhh
      121 aadlrlkkva iervreaqda gdiavslsae avadflfani tgiriaargg agpeqlqsls
      181 glalraii
//
LOCUS       WP_457661405             247 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661405
VERSION     WP_457661405.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 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   3  (residues 1 to 247)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27451
     Region          50..>230
                     /region_name="Csa3"
                     /note="CRISPR-associated protein Csa3, CARF domain
                     [Defense mechanisms]; COG3415"
                     /db_xref="CDD:442641"
ORIGIN      
        1 mtkeskpdrl rqmgalnpkp egvrapwfre agffdpldlv qvkyemlrha reegtnkada
       61 aalfglsrqt yyqaeaafer dgmsgllprt rgpksahklt gevmrlveeh ldangqlqar
      121 sladlvharl gisvhprsie ravarkkktm ksrrtqspcr raarmfyeal radvicgtac
      181 arrmgaivfh glwrglavli aphqsavarq qsaprfktts mvahdrqlvh mlanmvlaae
      241 tggshvy
//
LOCUS       WP_457661406             226 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661406
VERSION     WP_457661406.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23617
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavd warapngcpi faqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarggyftpg anssaaggei gavavlerha
      181 alfplgdqnl alpsysagsg dpaktlasql eqlglsvhdw fslldl
//
LOCUS       WP_457661416             386 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661416
VERSION     WP_457661416.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 386)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..386
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41599
     Region          25..383
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mattnpaipv tgipfpnsey ehrqqkvlea mvraeldavl vtayghqeyl tgydgnggyf
       61 apfplilvpg rapifvaref dldtvraesc ieeiipysqq ndfapvcadv lrrldlqsrr
      121 vgmelgcwnl apadvnaiqa llpdlkivda srlvssvsav ksdleiqair samtttdlvv
      181 ttfqrslhig vteaemlafi tdelgksgge lcpaptllfg ertrlphgtp kkhpignnes
      241 afmemgtlkh kyaaglcrsa iigrnpales lhnlaeeale aaiaairpgq tagaidaaar
      301 gvieragrah vfrhrtgyqi ginwtergdl slepgakeil qtgmtlhmpi ilfdegghgi
      361 gcsetvlvte ggvevlsstp htlyra
//
LOCUS       WP_457661417             592 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457661417
VERSION     WP_457661417.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 592)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..592
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63790
     Region          1..267
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          323..580
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mvpflklsrl sigltlpama illavfgvpm vlllltsfna paftlanyqa fvdqpanlrv
       61 lsqtieislv ttalcvvigy ptayviaass kqlratligf vvisyltsll artyawilil
      121 gdrglinnfl ldlglisspl pliynrtavy igmvqimlpv mvlplisvtv gidkslmaaa
      181 rsmgarpfta frrvffplsl pgvrsgsvlv fvlclgfyit paalggvrda mlstfiaaha
      241 ksslnlgsta asslillaia mivisligld lsgspsrtpk parktwlrll pssglitryl
      301 nelavpcrak rwtaqlyrag tddrllkiag amfvvfvmlf llfpglvviv msfspgtfle
      361 fppsglslqw yrsffsdasw yaaawtsiqi giavtilsti vgtlaaygls htfprlrtvl
      421 smviltpitf pvivvgiaty lglvqlglig tkvgiilaht igatayvvvi vsatlanldr
      481 rlenaaksmr aspfkafmrv tlplirpgva ggavfaflhs fdevvttslv gglsirtlpl
      541 kmwenmrhql dptiaavasl lmllpvvwli vlyvtwwksk pqalrairda as
//
LOCUS       WP_457661418             368 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661418
VERSION     WP_457661418.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..368
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40341
     Region          37..309
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(44,179,245,271)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 mtilinrrhf iqattsafaa gtlssvagna laqppkelrv ivgggdygta vvnafvkpfe
       61 aetgvkvtsi tdqtdlaqle lmvtsnsvsi dvatlgygea laagargrle eidysiykke
      121 eldgiaefar dphsvgalmy ayvlaynikk ypadkqapqs wadfwdveef pgtrtlvsgq
      181 ygdggpweea llangvaada iypinidqvf aslnkikphi rkwwgtgsei qqmmhdgtvd
      241 laqtfdgran llidlgapia inwnqakavl dswvipkgsp nlehaqrfie fatrsdrqaa
      301 faqlipygpt nlnafkripe nigrklashp dnlaksvrtd yrwyaevgtd glsnierlvq
      361 rwnawile
//
LOCUS       WP_457661421             286 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661421
VERSION     WP_457661421.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31752
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mekikerqat fskaesaiaa hlvtnirdip fetaasissk lklspmtvgr flrslgyenl
       61 aalkeelgst ihqiawlvge ryermtsaer srneadsaah drsasldlel kavisayeqa
      121 gteifgevae mvakadrvyv agfqtvrgla mdfalrleya rpnvrfmdgv sgtyselfad
      181 qtgkpllivv dvrryakqai llarqasqan vnlviitdsv cywaqeltdn vfrvatdvdm
      241 fwesnapvtt flgllvdevi lrlgplvkkr sermqklqdn fgsfad
//
LOCUS       WP_457661422             376 aa            linear   BCT 27-JAN-2026
DEFINITION  DmpA family aminopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661422
VERSION     WP_457661422.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Bompard-Gilles,C., Villeret,V., Davies,G.J., Fanuel,L., Joris,B.,
            Frere,J.M. and Van Beeumen,J.
  TITLE     A new variant of the Ntn hydrolase fold revealed by the crystal
            structure of L-aminopeptidase D-ala-esterase/amidase from
            Ochrobactrum anthropi
  JOURNAL   Structure 8 (2), 153-162 (2000)
   PUBMED   10673442
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Fanuel,L., Thamm,I., Kostanjevecki,V., Samyn,B., Joris,B.,
            Goffin,C., Brannigan,J., Van Beeumen,J. and Frere,J.M.
  TITLE     Two new aminopeptidases from Ochrobactrum anthropi active on
            D-alanyl-p-nitroanilide
  JOURNAL   Cell Mol Life Sci 55 (5), 812-818 (1999)
   PUBMED   10379365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10115574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="DmpA family aminopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39015
     Region          23..361
                     /region_name="DmpA"
                     /note="L-Aminopeptidase D-amidase/D-esterase (DmpA)
                     family; DmpA catalyzes the release of N-terminal D and L
                     amino acids from peptide susbtrates. DmpA is synthesized
                     as a single polypeptide precursor, which is
                     autocatalytically cleaved to the active...; cd02253"
                     /db_xref="CDD:239071"
     Site            order(80,100..101,265,269,272,315..319,321)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:239071"
     Site            order(85..88,90..92,94,96..97,100,114,117,125,149,
                     272..273,284..288,320,324,327)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:239071"
     Site            order(149,221,251,289..290)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239071"
     Site            250..251
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:239071"
ORIGIN      
        1 mettqclasd asakprardl glpfsgktgs ynaitdvagv evgystvisd apasgrgpar
       61 tgitailprg rsgplrapvw agfhslngng emtgthwike agyftgpiai tnthslgtvh
      121 qsilewmiyk pnpgfgpykf ilpvvgetsd aylndmdafh vtgthvkeal dgassgplae
      181 gnvgggtgmi cfefkggtgt ssrivdllgs pytigclvqa nfgirpllki lgvpvgehlt
      241 snrlfageqg siiavlatda plmptqlerv arraglgigr tgtpvgdgsg dlclafstan
      301 ltasesatap avghlaflpn nrldplfeat aqaveeaiin amvaaesmvg qedrlvaaie
      361 hdavkevmrn ygrlnv
//
LOCUS       WP_457661424             412 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661424
VERSION     WP_457661424.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44023
     Region          58..315
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          330..404
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mrpralilie gartgnglly vqaaqrlglh pitlsadlaq ydylaedgtg airvdtgdlg
       61 alirecsrll vtfdivgiig fagldesvnv tvgrlcrhfg lpgpspasie hcydkfaqrr
      121 llaqagvsip ayrvaanare vvsaaaeigl pvvlkpivgs gssgvrlcrd vdevaehtsy
      181 llggthvwqc sprilveeya qgpyciantm gnevigvaag efgpppyfvf retifpaplt
      241 dneykrivqn svsclqalsl dwgpaniefr rtkrgpvvie vnprisgapd pqliqlacgv
      301 dlitehvkla igeevdlrks hsqtaaarnl vpdcdgtldw ieganraaav pgvievklyv
      361 epkspivlkg dyrdwighii aaspsaaqta aildravgll dwsitpfpip gs
//
LOCUS       WP_457661433             393 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457661433
VERSION     WP_457661433.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40613
     Region          6..390
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mstlsifias agrtavgsfn gsfantpahe lgaavikgvl eragveagev devilgqvls
       61 agegqnparq aamkagipqe atawsmnqlc gsglravalg mqqiatgdar iivaggmesm
      121 smaphcahlr ggvkmgdfkm vdtmikdglt dafygyhmgt taenvarkwq lsrddqdqfa
      181 lasqnkaeaa qkagrfadei ipfivkgrkg dvtvdqdeyi rhgatldsma klrpafdkes
      241 tvtagnasgl ndgaaatllm teaeagrrgi qplarivswa tagvdpqimg tgpipasrka
      301 lekagwsvad velveaneaf aaqacavnkd lgwdtsivnv nggaiaighp igasgariln
      361 tllfemkhrg vskglatlci gggmgvamcv dat
//
LOCUS       WP_457661441             393 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661441
VERSION     WP_457661441.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  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 393)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42965
     Region          11..391
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mkmpinelts eaereaivrm rhamhrepel snnewntqkq iietlarfgl tkvkmfhktg
       61 vyvdvegaar gpnrsivlrg didalpiqee rddlayrsqv pgvmhacghd vhgsialgta
      121 lafhrmrenf sgrvrvffqp aeeaeplggr tvaeehlldg fdaavgfhvr tdipvgsyga
      181 rtgavtkasd qftleltgtm ahgakphlgv daisiaaafi nevqkvisre mpvddraivt
      241 igtiqggeai niicpsvkig gtirtasaer rhqlvqrvrd vaegvavmhr gkaafiaqmg
      301 eppvvndham vehfrqlvae svgpdkyvdg qattgsddfa fysscvpsiy fwfgsrepgy
      361 esgvhtptfa vsdkvliptt elavrycwkl lhs
//
LOCUS       WP_457661442             126 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661442
VERSION     WP_457661442.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 126)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..126
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=13414
     Region          <2..126
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mgnpspafqn lskiavealn vglealrpgt tcsqvegefr ralarhgiqk esrigyptgi
       61 afppasgert asirtgdetv lvpgmvfhmm pglwldnvgi tttqsfvvsd tgfepltatp
      121 revfik
//
LOCUS       WP_457661443             305 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661443
VERSION     WP_457661443.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 305)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..305
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33594
     Region          19..>241
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mnmikelhfe qgefqarlaa vkqemshrgi dilllseppn qnyltgynay sfytpqlviv
       61 aqdhdepiwi grfmdrvsas mttylaeeni raypdtyvqs atvsayvfma divkelggek
      121 vrigvemggy yyparahadl thalpnaefv dadllvgwir lvkspaevam mrqagllada
      181 amkrvidtvg agvrecdiaa aiyhqqisgt pefggdypsc ppdlcigers iapharldgr
      241 taaelhrrqs gtvrmppqva gqscshdcrg qsftsfpksi enscrstecw prstpsgdnv
      301 fagrr
//
LOCUS       WP_457661444             183 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661444
VERSION     WP_457661444.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..183
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19946
     Region          43..172
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msishetksp cppiadenwp aeiadmkagf agdlniyrtm ahhpallraw aplrqhivrd
       61 salgpvrsel vilraahrmg sayewahhvs raralgisda rirdlraspv gedgliarav
      121 dalfdagrlt adiereisaa fgkqavfdlm atvgfysvlg yilmtfdtli ddcvadeiak
      181 rpi
//
LOCUS       WP_457661446             294 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661446
VERSION     WP_457661446.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..294
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32039
     Region          1..281
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlqkgplhah iierfddmse qlkqaarhil ehpqevalvs mrelarnagv qpstmtrlak
       61 flgfsgyedf raqhadvirv sadgfaaram qgeeagange glayrmlqsl taqigrlcep
      121 ealsrlnqla erlakarkiy vlglrschsv awhfhyvmtl lgektvhldg pagtggdali
      181 rataddvllt vsinpysryt leiaetalek gmgvvaitds evsplvaiae hsvlfptesh
      241 tffhtltpal aisevlcgll ashdrkaalq elkrvdsyls santyaasip rrki
//
LOCUS       WP_457661450             413 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457661450
VERSION     WP_457661450.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..413
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45990
     Region          228..406
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(262,358,361..362,393)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mnasdylkrs alyrklvygp yrefarvyaa kmsneglgrr ctwrslslfr dlmdwhvgng
       61 hdaqdlrevh vdrflehrfk hwspdtgdrs alrrllsalr eeglipaalp verteheqiv
      121 dvfaaylsne rglaastvrs hkllshrflr evcpagadgf aaltpesiig yverhaldgs
      181 adsgkamcvv vraflrylhl kgfistalad cvpsirrwrl aglptflppe kvqkvldacd
      241 rttamghrdy avlmilaklg lrasevatln lddidwqagt ilvhgkgrrq aimplrhdvg
      301 taivayirhg rpasacrrlf lrtlaphvgf asgcaitmia kqaleragvd gyahhgahlf
      361 rhslatdllr sgasfaeigq llrhrsidst riyakldidk lrelslpwpg gvq
//
LOCUS       WP_457661453             590 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457661453
VERSION     WP_457661453.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 590)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 590)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..590
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63679
     Region          1..263
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          322..578
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mktmqkmssm pilltmpalg vllavfgipl illfltslna palslvnyvv ffeqrsyvai
       61 llltleisav ataiclligy ptaylivvsg rarpvlmvlv fltwltsalv rtyawtvvlg
      121 dnglinslll nvglidsplp liynrfavyv gmvhimlpmm ilpiisvmms idsslmaaar
      181 smgakpftaf lrvyfplsip girsgcilvf vvclgfyitp qalgglgdtm lsalinsqlt
      241 tsldlaptaa asfillaitv vvlsavgvnl agahsqagsp alklrqdrlr vltrairyln
      301 efvlprrarr wtaklyqtqh htslwkivga ifiaivmfyl llpgviviii sfnsgeflef
      361 pprevslrwy ysffsdpswi aaawnsfqfg livsglstii gtmaafglsr cssglrsslt
      421 mviltpitip vivvgvavyl glaklgligt stgiilghti gaigyvvviv matlsgfdrt
      481 leqaamsmra gptqtfmrvt lplirsgiig galfaflasf devivtsfvg gyaiptlplk
      541 mlenlkqqvd ptiaavgsll tllpivwlvv lyftlwrnqg tlgkpamnpt
//
LOCUS       WP_457661454             606 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457661454
VERSION     WP_457661454.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..606
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65962
     Region          37..573
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 msivnqsstk tgalssatid ksqetqpsif gldlrgkpkr scevgslesv yvstrdgvrl
       61 aldvtrpmgd gecakrdtil vmtcywrgqn gepsnryadl fvphgyavvv gdvrgtgasf
      121 gewpghrtrd eildfsdvld wiaaqpwstg nvvgyglsyt ansatwmasl gnpalkgvva
      181 rfvdysiyed idfpggirnl tqlqwdsqlk nlnhnvsskn tgesqpsrgv rpvgeaaela
      241 aalsehekap srprlqqsmd kdeyfgmdps gfdwspqtaa ecisrsgvpi qnwggwfdsv
      301 saegsirqfl lqsnpasiii gpwnhgataa tdplrpagee vapllatqea nwvrfaagcf
      361 ageaadeggk vlhyytlgeg awkstrswpi patrqrwyta sgsrllssst dktgfetlqv
      421 dpeladvisn rwetnggale fmdkvdygdr refdaarlvy tsepltrgle vtghpvvqld
      481 itstredgaf fvyleavrpd gvscyitegn lrarhrkvwt dsplsvlgpq hsylsedaep
      541 ltpgksails ftlqpisali pagyslrlvl agsvkgtfan vpedgpppfl kfhhpgcyid
      601 lpiier
//
LOCUS       WP_457661455             547 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457661455
VERSION     WP_457661455.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12067979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..547
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58428
     Region          14..530
                     /region_name="MFS_3"
                     /note="Transmembrane secretion effector; pfam05977"
                     /db_xref="CDD:399164"
     Site            order(32..33,36..37,40,72,127..128,130..132,135,155,
                     158..159,162,237,240..241,244..246,249,273,277,330..331,
                     335,339,355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mqhvdphqsg sailaplrng vfrsiwtasq isslgwfvqt vaiswlmati svsdlmvalv
       61 qaastlpvff lsilggaiad nfsrrwmmfa ghcllalgst tlvisvgigf ispwlilglg
      121 flagcgfaln dpawhasigd ilhkrdipaa vtltsvgyni vrsvgpalgg vilaffgplt
      181 afafaalcdl tplgaiwrtk whvrasplpr ekittaihdg lrftamsfei rsavaratlf
      241 glasisilal lpivvrdqla sgpivygill agfgsgafva gmsnsflrri msqsklvava
      301 svacaaccls laltssvava afalalggag wliswtgidv svqlasprwv vgrtlsiyya
      361 lsaggmaags wiwgtvaqny sltwalegaa aalllvaaag ilfpvrpwee adqessdfnp
      421 pelalalkpr sgpigvkiey sipeenieaf lscmrarryv qsragarnwt lhryletpsv
      481 wietfrtptw mdflrlnhrl taadkdvvqh lqalhdgklp pqtvlsiert tdaartdpss
      541 sfgralr
//
LOCUS       WP_457661457             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661457
VERSION     WP_457661457.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44310
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          327..403
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mpkralilie gskgngplyv raaqrlglhp itlatdpaqy dyleaegsea irvdtndlea
       61 lirecarlla tydiagitgf pgleeslyvt vaklcrhfal pgpdpasieq ccdkfvqrql
      121 laeagvpmpa yrlaanardv egaaaeiglp vivkpavgsg ssgvrlcrta devadhatyl
      181 lggtyvwqsa prilveefaq gplystdtmg ktviaaglad fnglphfvpc gsmfpapltd
      241 deharivdvs lsclqalglg wgptniefrw trhgpvviev nprlpgwttp rlihlaygid
      301 linehiklvi gkecdlrarh srtaaaqflv pdrdgildri egtsraaavp gvvdvrfyva
      361 pstpilrkgd yqdmighvia vstspartke ilqravdlis wsitpfpaid e
//
LOCUS       WP_457661458             410 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661458
VERSION     WP_457661458.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..410
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44080
     Region          57..312
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          326..400
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 makralilie gsrvagplyv raaqrlglhp itlatdpaqy aylaakgsea irvdtndlea
       61 lirecarlrv tydivgitgf pnpgesvfvt igklcrhfdl pgpdpasieh ccdkfvqrql
      121 laqagvpmpa yrsaanakev edaaaeiglp vivkpavgng ssgvrlcrta devakhakhl
      181 lggtyvwqsa prilveefae gsyyganimg ieviavgtga fgppphfvfc eylfpaqltd
      241 deharivnvs lsclqalglg wgptniefrw trrgpvviev nprlaigese lvqlafgidl
      301 inehiklvig decdlrarhs rtaaaqflvp drdgildrie gtslaaavpg vvdvrfyvep
      361 ntpilrkgdg ndmigqvias stspaqtkai lqravdlisw pitpfpalde
//
LOCUS       WP_457661462             252 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661462
VERSION     WP_457661462.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..252
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28504
     Region          81..245
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mtteseagna lsifihqmle etsidqmven vslfarsfnc ssisygpqph vqtvqresri
       61 klptlltypk ewqehcfksg ydrlapslrv spfqsspilw dqaykdpntt drerrifdea
      121 kefglqtgvt iplrgrlddf pimsfvqset sglskfavsc ltsaaflfhd rvegrvelka
      181 dvpnltarek ecltwvrqgk sswaigtile isphtvdfhi khaksklgae nrrvaameae
      241 rlgliepkfw ll
//
LOCUS       WP_457661463             236 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457661463
VERSION     WP_457661463.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 236)
  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 236)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..236
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26665
     Region          3..218
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mhtklilive dneellcsle rhlsehgfrt isasdgfkgf krfqtekpdl vvldhgpprv
       61 ngyqllekir hfgdtpvima ttwnshddel rcrylgaddy lprpihnavl tervrtllrr
      121 gedrgairpi hyrkltidpd eytafvdgpl gaielkltns elkllahmar cpgqvferad
      181 liyacfpdsn mllrtidshv snlkgklaga gidgyletvr gvgyrmrnln tnpmda
//
LOCUS       WP_457661464             368 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661464
VERSION     WP_457661464.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..368
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41313
     Region          29..135
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(41,44)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mvlrmespap alevqdwirg eplpnfqpgk vyivafwatw cgpsvstmps lielqqkykg
       61 sgvevlavaa deeaatayev rgyldawfte kfpklnfrig ldctgemkkf wmqaslsmgi
      121 pssfvvdrds rvafighpae lddvlpkvld gswrtsdqak tadreriarg reevflfkvs
      181 qaikmedwkt alsvieeaia lmpdsiqlra ahadtllhkm rdmhtglpvl rqlvrdaidr
      241 ndenwllgam nqlsnpaydy tgfpsverfa mgkelsehil alkelkddvk aysyqlvary
      301 yhesgnkara eellalalal vdglylavni kqrwvadllq tlanyrgqkv cynamsavpe
      361 nhakpkan
//
LOCUS       WP_457661466             602 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661466
VERSION     WP_457661466.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..602
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=66867
     Region          13..412
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mmhekigahh lerkailyvr qssahqvlhn ressalqyam rdrlaalgws hietvdddlg
       61 rsaaggvara gfdrmvaevc lgkvgavaar evsrfarnsr dwqqliemcr vvdtvlidqe
      121 avyaprqgnd rlllglkgsl neyeldllrq rslsaryeka rrgelvvtvp igflkagdri
      181 ekdpdrriqe aialvfdkva elgsarqall wfleqgldlp vryangdvtw rrpnyatihr
      241 mianpiygga yaygksrsvp gydgrsgirr kardewlali pdahegyvsw eraeeirkmv
      301 sdnvptsrhh gapkhgdall aglfrckrcg rkltvrytgs nhnipryscw rglldngepr
      361 ciafgglrvd daieeallgv vepgaiaaav eadrnmasqr dqvqdallrd leaaryaadr
      421 afrqydaadp enrlvtsele arwnkalarv geieakiakh rtvapqpipm sasqlvalag
      481 nlravwtaps tdarlkkriv rtlihevvad lddvaseivl vihwvggvht elrlpkrrrg
      541 qrnatpddiv eavrqlvlia nddviagvln rnglttghss targsmdlqp fktrvprsas
      601 dp
//
LOCUS       WP_457661468             273 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661468
VERSION     WP_457661468.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..273
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=30669
     Region          13..>266
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mmhekigahh lerkailyvr qssahqvlhn ressalqyam rdrlaalgws hietvdddlg
       61 rsaaggvara gfdrmvaevc lgkvgavaar evsrfarnsr dwqqliemcr vvdtvlidqe
      121 avyaprqgnd rlllglkgsl neyeldllrq rslsaryeka rrgelvvtvp igflkagdri
      181 ekdpdrriqe aialvfdkva elgsarqall wfleqgldlp vryangdvtw rrpnyatihr
      241 mianpiygga yaygkssfra rirwpvwnss qga
//
LOCUS       WP_457661469             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661469
VERSION     WP_457661469.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27417
     Region          13..217
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 myrhredklg wdksktgqvy kalktlvvnf wvppgtkfna kaiskvmkks vtpvrdaliq
       61 leaeeyivsn hgsgyyakkl dtkrlsdefg vtrtilqdvi rgnldelhrr spvlqttpsw
      121 ddyesvrefl evfyekiaaa snndrmlyyv hesnirtryv rwldvqrper llcirddmse
      181 llelldkrdk ngaianldrq fsavistipk lvregnerae ntkeswldtl ssisves
//
LOCUS       WP_457661474             326 aa            linear   BCT 27-JAN-2026
DEFINITION  Fic/DOC family protein [Sinorhizobium medicae].
ACCESSION   WP_457661474
VERSION     WP_457661474.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Veyron,S., Oliva,G., Rolando,M., Buchrieser,C., Peyroche,G. and
            Cherfils,J.
  TITLE     A Ca2+-regulated deAMPylation switch in human and bacterial FIC
            proteins
  JOURNAL   Nat Commun 10 (1), 1142 (2019)
   PUBMED   30850593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Kinch,L.N., Yarbrough,M.L., Orth,K. and Grishin,N.V.
  TITLE     Fido, a novel AMPylation domain common to fic, doc, and AvrB
  JOURNAL   PLoS One 4 (6), e5818 (2009)
   PUBMED   19503829
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="Fic/DOC family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /GO_process="GO:0018117 - protein adenylylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36359
     Region          8..221
                     /region_name="FIDO"
                     /note="Fido, protein-threonine AMPylation domain [Signal
                     transduction mechanisms]; COG2184"
                     /db_xref="CDD:441787"
ORIGIN      
        1 madqhpkdsy typntsddpd rtnvlknrwr iethselrvk eyratavrmq eiaegdgpqg
       61 nfdkvhlkai hgyifqdvye waghtrnesp vvegqrvepi gglstggtsf lpgsriemgl
      121 dealtpirdp qalrnatpee faeragkvls elnyvhpfre gngraqeafi selgrhyghe
      181 idfsvitkpr mieasiettn dpsnpamkha iedamnpgrr ealrsafedl revgeeplqh
      241 hvraaragee itgtvlghdn rvasvvtdqg ivvavrtdlp erlpddeeit ftarsdfsrv
      301 rrdqsaqvaq sqpaparqpq knvtrs
//
LOCUS       WP_457661476             443 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661476
VERSION     WP_457661476.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..443
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48368
     Region          12..443
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtfhsenlql dspvgekhet spdrvftgrl gngmdvivir dhrrpiathm vwyrngsadd
       61 pigksgiahf lehlmfkgtr nhpaghfsgl lasvggnena stswsytnyy qqvpkdylkt
      121 cmayeadrmt gliltdeivd merqvvlaer gmrcdsnprd ilhealhaga fspdpcgrpi
      181 igwqheietl gredalayyh rfytpenail vvagdvdpda vmdmaetiyg aitptgasfk
      241 rpvvrappvr tqrlltlvde nvhqpaftri hvvpsmmapg phaaalevlv lllgggntsy
      301 lhealivnnr matwvgasyw gnvsrglasf qigacpapgv sladlddaie naldmlrrsg
      361 fsaddirsak srivanaiyq kddhsnlalq ygvaaslgls vedvalwqer ikgvttedir
      421 naltllerst givgyltppa tda
//
LOCUS       WP_457661477             400 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457661477
VERSION     WP_457661477.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..400
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42948
     Region          4..377
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtifttpsla tttyasrlqr vkspggieaw lledhtlpvl wtsfcfrgga afdpegkpga
       61 aallgsmlte svgdldaggf qrrldekaih lsfragrdal hgslttltqn vdeafdllgm
      121 avsdpafqql dferthamha aslrmgmaqp drvarqvfna iafaghpfsr pasgcyetig
      181 svelsdvval hsrmiarhnl eivavgalga dafvaaldra fsqlpvsaea svlpapflgl
      241 geevlthlds pqstmifgrp cisvddpdfm aanvvdhclg ggtfssrllt elrekrglcy
      301 sihtrldatr nvsrligyts trndrlyeal dvirsefahl vsdkisaeev emaksylmgs
      361 falqldtssa iaqtllstkv ggapaglhrr aqcshclchp
//
LOCUS       WP_457661482              91 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Sinorhizobium medicae].
ACCESSION   WP_457661482
VERSION     WP_457661482.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..91
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=10677
     Region          1..90
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mklewtskav adlgrlydfl apvnrqaaar tvqsltsapa rlleqprige rleefdprev
       61 rrilvghyei ryeirqstiy vvrlwhtred r
//
LOCUS       WP_457661483              54 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457661483
VERSION     WP_457661483.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 54)
  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 54)
  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
REFERENCE   3  (residues 1 to 54)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 54)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
REFERENCE   5  (residues 1 to 54)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 54)
  AUTHORS   Clissold,P.M. and Ponting,C.P.
  TITLE     PIN domains in nonsense-mediated mRNA decay and RNAi
  JOURNAL   Curr Biol 10 (24), R888-R890 (2000)
   PUBMED   11137022
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..54
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..54
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=5576
     Region          <2..46
                     /region_name="PIN_Pae0151-like"
                     /note="VapC-like PIN domain of the Pyrobaculum aerophilum
                     Pae0151 and Pae2754 proteins and homologs; cd09873"
                     /db_xref="CDD:350221"
ORIGIN      
        1 miklatvqgl saydaaylel aiarslplat ldrklaaaar aekvpvlgpf gneh
//
LOCUS       WP_457661484              86 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457661484
VERSION     WP_457661484.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..86
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=9427
     Region          4..>57
                     /region_name="VapC"
                     /note="RNA interferase (RNase) VapC, contains PIN domain
                     [Defense mechanisms]; COG4113"
                     /db_xref="CDD:443289"
ORIGIN      
        1 msvfvldatt aaawllpeeh seiaeqlias isgqcpvpgl fwhearsnlv taerrqragv
       61 fkwkapqsgh crqgltrcda pvrtdr
//
LOCUS       WP_457661485              80 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Sinorhizobium medicae].
ACCESSION   WP_457661485
VERSION     WP_457661485.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Garcia-Pino,A., De Gieter,S., Talavera,A., De Greve,H.,
            Efremov,R.G. and Loris,R.
  TITLE     An intrinsically disordered entropic switch determines allostery in
            Phd-Doc regulation
  JOURNAL   Nat Chem Biol 12 (7), 490-496 (2016)
   PUBMED   27159580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..80
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /calculated_mol_wt=8847
     Region          4..>44
                     /region_name="Phd"
                     /note="Antitoxin component of toxin-antitoxin stability
                     system, DNA-binding transcriptional repressor [Defense
                     mechanisms]; COG4118"
                     /db_xref="CDD:443294"
ORIGIN      
        1 msvtvkvaea kahlsellar veageeviis rgsdpvarls rihkdnelgv lmaevraarl
       61 rakpvtndei ldwkreeqqf
//
LOCUS       WP_457661496             161 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661496
VERSION     WP_457661496.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 161)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18005
     Region          36..102
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mslmsarglv eitdpefdrp vfrqpgfdgt ltakemdeki sawlkktrea kgisradlah
       61 llglsvsvyg ryergsearl siprlihlce imgfmpldvi fdaaphlwgk tleeaedrqt
      121 lmklieelpq dtmrdlirll rrmtpsepaa dtvatsmseg c
//
LOCUS       WP_457661497             332 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661497
VERSION     WP_457661497.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36469
     Region          2..331
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mygaitavkd laltvrqgef ltilgpsgsg kttalmllag fispsegdil iggrsvaavp
       61 syrrdqgivf qsyalfphlt vrrnlefple mrgikasera nrvdrilkrv hlkdfggrmp
      121 sqlsggqqqr valaraliad ppvllldepl galdrnlreq mqgeikslhk efgittvcvt
      181 hdqeealtls drivvmrggv ieqvdtpeal ydrpatlfaa nflgeanlle etgsdvqaer
      241 srpfgmvaii rperlristr gaprspdadq rqsvigmvtd tvyagaqrky hvqagtrmlt
      301 vrehvasgqq vyspgdqvrl ewlrsdvrfv tp
//
LOCUS       WP_457661520             632 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661520
VERSION     WP_457661520.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..632
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69836
     Region          159..563
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mnpallllgl liatatavfv aslayaglyy tfdnstwmlq alqddllasy kaarldlyag
       61 ewhrpaiaag agfvagaaml itlatgkkks tdarflstme aralgltrtg gvfvgriggs
      121 likvpggftq rgsgrrrltk pklfggkklw idgddvggfv igpprsgkga slivpncllw
      181 pdsivvldmr getyeatagh rskfsrvlrf spadengdte cynpldfvai npdqrdidin
      241 siatallptp kgdaywisda ralfagvtsw vlenpdipdk dknlgtvlnv veggdqplre
      301 wleevanpel raewissfty ttiarfavma gkqfdgvygs laaavrpfkn nrilratars
      361 tfdiramrre nmslyldfri qqvasigpif nvlmvqfmdy msrnmmtrge rrvlvlldef
      421 qnlgklenal tvatvlggyg ipcwffvqsl rsidnvytre grqtlvnsar aqiflgaqdp
      481 edqryvsqll gerkevtvdk avstgvtlfd rkgatmsyrt amrplmrpde lgamnetrci
      541 iklrnqqpif glrnfyyadd elmkrawlpi aatneqhrmt rtpevvvehi dpcpsnqaaq
      601 stvapgekfa lkapprsrsg ldqdakrtkp kk
//
LOCUS       WP_457661524              70 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661524
VERSION     WP_457661524.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..70
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7799
     Region          7..67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mamtmerere krglnkkema slceitspyy lqildgsanp slqvitrist nlkiplqalm
       61 mgqksevkvd
//
LOCUS       WP_457661530             431 aa            linear   BCT 27-JAN-2026
DEFINITION  type VI secretion system Vgr family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661530
VERSION     WP_457661530.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..431
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=47842
     Region          20..>421
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvqhttenpl krnrfaavts aafqpndvtl rwlrgterlg qpfhyevkla ittpiqnfas
       61 vpgqsltagl klkgggtrff ngvitrfeyv glddtehlny laelrpwvfl lnyrtnsrif
      121 qnktsieiit aifqenkgnf knrtmgrfpr rifcvqhget dldfvsrlme qdgiyyyfeh
      181 gqdrhdlvlv dnlssheacm penvethhnl rpagnlhrdd vildwseivs lqpntvvlkd
      241 ydhekpaael tsvarvptvr iggippakda rqrlsgaprv asqtanagas sklhatfnyp
      301 gcykekwhgd fyatvraeel acstyrarie ttarqittgs tfkaanpyny gdvgarpkst
      361 qrfmaiandf tilgelgggp trsatghkae cflyhsavei ipastqyrpp aphtvagdqg
      421 aadggrrgsa g
//
LOCUS       WP_457661534             363 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457661534
VERSION     WP_457661534.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 363)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 363)
  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 363)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..363
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40343
     Region          36..361
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msakarvgiv rvagwirlds ktndveppyd reitliinni drlqmlgflr pqeisllhqt
       61 rdlvmahimp iavsgrgydq alryadevee nlarisdvaa vhrrevkeka efkrtlrrry
      121 fafvlilvvl isgailitqn aefekrrngy vrsvallhsh mtrsriaalr lfldyfndqr
      181 spapemlraa leavkeleai nsglvrivns erdahtealg ellqgirvpl dteigleies
      241 nakylqvsai qvhliveelv nnavtavagk qtkqitirar llnrhfsfan klliqvadrg
      301 ggmtsdildk aatpffstra gshvglglts ciemvkamqg kvkidstpgv gtvvsvllpl
      361 nqr
//
LOCUS       WP_457661541             406 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein, partial [Sinorhizobium medicae].
ACCESSION   WP_457661541
VERSION     WP_457661541.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 406)
  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 406)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         <1..406
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
     Region          1..396
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 lavtgqslik hdirdirtpa fqdvqsllrq adlsftnfeg tilgrhggwp lkgsffgcsd
       61 pavldalgai gfqalslsnn hafdlgpsgv lstleevekr gflhaglgrn aqevsrasia
      121 tinqrrialv amdggpgpdf myaadadenr perpgvnrlr lsqvlevddv afeqiravrd
      181 kigytaidla ndsqpddppr ldpqaevaia rcvfkrsdry grgvridevd marnlaaias
      241 aardsalvia ylhhhhwasd wyqlpewvsg vakrcidaga smfvshgapv lqpveiyrgr
      301 pifyslgnfi fhvrsekstw taaevwesvv gvcsfasdns lidisfhpvv iggedgledg
      361 vlerrlvpql vtgdsavril grlqeqsarl gahieisgnv grlqar
//
LOCUS       WP_457661548             461 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate aminotransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661548
VERSION     WP_457661548.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..461
                     /product="aspartate aminotransferase family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50239
     Region          1..460
                     /region_name="PRK06105"
                     /note="aminotransferase; Provisional"
                     /db_xref="CDD:180401"
     Site            order(117..119,151..152,154,225,258,260..261,287)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(118..119,151..152,225,258,261,287)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            287
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mndrpnslha ldkqslvhpy tnlavhqetg phvitggngi yvvddegkry ieglaglfca
       61 glgfseqrlv eaamrqlktm pfyhsfahks tepgirlaek llsiapvpms kvffagsgse
      121 andtaikliw yynnalgrpd kkkiisrrka yhgvtvatas ltglpfnhrd fdlpianilh
      181 tdcphywrfa eigeteedfa trmadnleat ileegpetia affaepvmvs ggvitppkty
      241 fekvqavlrk ydillvadev icgfgrtgnm fgsetyglkp dmiscakqls aaympisalm
      301 inqkiadalv dqsrkigtfs hgftygghpv aaavalealt iyeeidivgh vrsvapvfqd
      361 rvrklgehpl igeargvglv agfefvedka trenfppawq vanqagkfat argvltrglg
      421 dmvslcpami idegqiddlm trmglalddt lawaraqghv a
//
LOCUS       WP_457661550             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661550
VERSION     WP_457661550.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..354
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36726
     Region          21..321
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mttatttttp tdaasgsvll tlmklrtfia lfaviaffsi fapnflstan lilmskhval
       61 naflamgmtf viitggidls vgsivglcgm vagglilngi dlqfgytiyf nvvevclitl
      121 avgivigavn gllitklnva pfiatlgtly vargfallss ggqtfpnlvg kpelsttgfa
      181 flgsgrllgl pvsiwilivv alaaaylary tpigrhifav ggneraarms girvnrvkmf
      241 vymfsgfcaa ivglvissel mashpatgns felnaiaaav lggtsmsggr gtiggtiiga
      301 fvigilsdgl vmmgissfwq mvikgiviiv avvvdqaqrr lqqqvtlmql akkg
//
LOCUS       WP_457661551             334 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457661551
VERSION     WP_457661551.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..334
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36589
     Region          64..328
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mfqvtrrsam kiaalaaaas smgqaafaae psilpswvdg gakariidfv sattaeggpd
       61 fvepadrvav fdndgtlwge qpmyvqlafv ldrvkqqapq hpewqttepf ksvltgdmag
      121 vaasgergll elvaathagm steefekivs dwmesarhpa sgkpytahif kpmvelidyl
      181 ksnqfevfiv sgggvefmrp wtkrvygipp envvgssikt kyelrdgvpa imrlpeidfi
      241 ddgpgkpvgi nkfigrrpia afgnsdgdfe mlewttagpg rrfglivhhd daerenaydr
      301 dshfgrlarg ldeapardwt vasikddwkl vype
//
LOCUS       WP_457661553             421 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease [Sinorhizobium medicae].
ACCESSION   WP_457661553
VERSION     WP_457661553.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..421
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44309
     Region          1..421
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mlttaaflaf mlvgvpigvc lclgsivyil asgnpllfqs fptqlfggvd nyglisiplf
       61 vligeimngg gitrriidmt mafvgamrgg layvnllanm fvasilgsat aqvavmaqmm
      121 vpemekkgyd ktfaagisay agmlgpiipp simfvvysvl aqvpvsdmla agivpgvllt
      181 vafclviaam glvynyprge rmklkdrvri vldalptlli pfvivgsils glanateaaa
      241 vgavaavlvg rfwigelrfa dlprmmlrag iysavvlflv aaaavfswvl vygmvpqqva
      301 gwvqtvasdp vtfmllvnii lliigtvidg apglimtvpi llpiatevyg idpihfgvvv
      361 vvnlvlgfls ppvglcffva aavtgakpgk mflvtlpfff vsclmlvlls lipslstffv
      421 r
//
LOCUS       WP_457661554             217 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661554
VERSION     WP_457661554.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..217
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23570
     Region          1..217
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mfdtaltwnd laflaqgagm tlavtavavt agtllgilfg virfqlgpyw aapltllldv
       61 frsvplliql vlgnafqsiv klgwgaftts gvvlslytaa fcaeivrggi ssvpvttrra
      121 arslgmtwwq dmryivapla trvslpswig ltlgvmkdsa lvlwlglvel lrasqilvtr
      181 lqeplfilli ccaiyfllsf pvarlggyle krwspyd
//
LOCUS       WP_457661487             451 aa            linear   BCT 27-JAN-2026
DEFINITION  integrase catalytic domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661487
VERSION     WP_457661487.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..451
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - obsolete endonuclease activity,
                     active with either ribo- or deoxyribonucleic acids and
                     producing 5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=50305
     Region          92..187
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 malweasdrl cskrlkplip illpalerhg rlelnsalrd kllmvsaatm drllsevrvv
       61 arggqrrrag mssavrrsvp vrtfgdwndp lpgyvevdfv ahsgtsssgs faqtmvltdi
      121 atgwtecvpv rtresglvia aikqarsqfp fpllgvdfdn dsafmnelvv cwcrsqglev
      181 trsrayrknd qawveqknga ivrrlvgygr fvgaeattal arlyevvrlh gnlfqpsfkl
      241 rektrigarv ikryhppvpp varvlahsgv aeadkdrlqa mlesadpvil fagiraaqee
      301 lgrrvdrrgl narseepvav dlqrftlslr tawqvgekrp thrrpyrrtk pypkrqsmle
      361 pfepqirawl eadpavsaas vlerlmsadp srftkkslrt vqmavkawri etagqiildg
      421 dwmeratlss haaagedngh lsaqrfgnip g
//
LOCUS       WP_457661558             772 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Sinorhizobium medicae].
ACCESSION   WP_457661558
VERSION     WP_457661558.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..772
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=83240
     Region          12..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mntheridrd lserdftvvg ksvkrsdtle kvtgaaryag dvalpgmlya kmkrsniaha
       61 riksidtska lalqgvkavl thqdvprvlh agsphprsas vtkdqyilde rvrywgegva
      121 avaavseeia eravalieve ydplpglfti eaasdpaapp ihenglgqny vlppvfvtrg
      181 dvdkgfeead lviereydlg rptpaymepn vcvsqwdgng kltmwtstqs afmvrgtlae
      241 vlgvplnkvr vivdhmgggf gakqdlfqne flcallarrt grpvkmefsr ketflggrsr
      301 hpgkiwlkqg ftrdgrivar earvtfnsga ygshgpgvtn vgtaaltsly rcenvrlegr
      361 ciytnspiag afrgygvvqt yyaldlmmde aaeklgfdpa efklmnavre gdmapsghpi
      421 vghglvdcir rvmeetnwhe lrrrekpetv krrgigigce mhgssaypgi keqgnaivkm
      481 nedgtvtlit gtaglgtgah talsqivaee lgvpfeavsv vqgdtdivpw digafashtt
      541 ylggraaqla aadvrrqvle haapllkaea gdlairdgfv vvangsnqsl rlseavgpqr
      601 gmpavqlvgv gtymptksys faahfaevev dtetgevavl evvpvheigr vihpiaaagq
      661 ieggiqqgig htlsedyvid ltdgrslnps fvdykmplsm dmpsirtiii etapdpggpy
      721 gakgvgedpi iaigpaiana iydaigvrfh hypitpeqvl nalktkanet rq
//
LOCUS       WP_457661561             365 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457661561
VERSION     WP_457661561.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..365
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38657
     Region          <22..365
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 mfklenpnst laatgedsit qgayayalrk ggggdwylqs ellagpvdpv dpvptfnqga
       61 gvyetyaqdl laftrlpslr qracieeggl warsegetad ivpqvssagv sgydrdigri
      121 eagidgllhe sgqgkliggv sahygsggss vasfhgggei dsraygmggt ltwygqngfy
      181 advqgrlnwf ssdlasallg nlasgndgfg yglsleagqr faigdnwalt pqaqlsyasv
      241 dfdgftdpfa arvsledgds lrariglsid yeniwqgqqg dtrrmqvygi anvihdmsgr
      301 trarmsdvtl dsrpdswtge iglggsynwg ddkyalygel raatgvtdfg dshaqggtvg
      361 lrvkf
//
LOCUS       WP_457661562             551 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457661562
VERSION     WP_457661562.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 551)
  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 551)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..551
                     /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=60690
     Region          342..548
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maitrndatl rvnrpakefa gaarewllrt dperliclgr vitavfaila iyldptrpns
       61 mlyesrlvlg lylllavalv ffplrfsfvs pvhllihgvd aavvgwltfl tnelaspffs
      121 ilpfvilamt mrwglkgasl galialivql vvglpdlldg daelnifimr siyfvliaat
      181 lgyfgayrer srqrlaqlaq wpsgaigedr lswlsivlqh asgvlgdahl lviwreqefe
      241 sgcaafwtsg rlqladlrdp efwrrhdpdg derhsrsgea lnglfadlpq ihanagrpnc
      301 kvvsaafssl ryrgrvfvis fanstddmkd ltqiiatrvg telervaliq aaraegrmrl
      361 ardlhdsvlq nltaarlklk ligeafpdga rqklmevgsl ileqqqcvrk fvdenrpgee
      421 gnlarldqdl pefldllrmq wscsidvsig spgmmvprwm lfeimqlise avanavrhgr
      481 atvvrigfig saglleldis dngtgiadgl tskkpfslsq riaelggsla icrsspglgl
      541 titlplkpgl r
//
LOCUS       WP_457661563             497 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Sinorhizobium medicae].
ACCESSION   WP_457661563
VERSION     WP_457661563.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..497
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52415
     Region          13..488
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mkltftsykr ewfsnirgdv lsgivvalal ipeaigfsvi agvdpkvglf asfaiacvsa
       61 ftggrpgmis aataatavlm vtlvkeygle ylfaatllmg liqiaagflk lgrvmrfvsr
      121 svitgfvnal ailifmaqlp eligvphvty amigaglaii ylfpyvtkav psplvaiaal
      181 taiavwtgmd irtvgdlgel plslpifalp qvpltfetlq ivfpysvgla avgllesllt
      241 aqivddmtdt tsnksqecig qgasniasgl iggmggcami gqsvinvtsg grgrlstfva
      301 gafllflilv lddivriipm aalvavmimv sigtfswrsi ldlrrnplps svvmlatvvt
      361 tvgthdlakg vlvgvllsgv ffagkvarlf hvrsildesg rertyhvdgq iffastegfv
      421 gafdfaepld kvvidvseah lwditavgal dkvvlkyrrh gvavevigln easahmldrf
      481 avhdkseeag aaltpah
//
LOCUS       WP_457661565             339 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661565
VERSION     WP_457661565.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..339
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37483
     Region          12..325
                     /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 mpeaalrska eiglmlypgc qmamvhgmtd liniagqfsa erggavarvs hwglqddgcl
       61 arcfdthpel gsrempeill vpgrltgpme aeeaapyarw lldrhaqgat lastcggtfv
      121 laatgllkgr patthwlfan afrdrfpdvr ldtdkivied gdivtagglm awtdlgmrlv
      181 drlfgptvtv etgrfllidp agreqrhyss fsprlnhgde vilkvqhwlq arearavsva
      241 qmakvvamee rtflrrfkaa tgmrpieyaq hlrvgkarel leftrrsveq vawavgydys
      301 aafrklfhri vglspgdyrh rfavagegfs rpghrlgtn
//
LOCUS       WP_457661567             299 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661567
VERSION     WP_457661567.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..299
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33270
     Region          17..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 malarragig ryydvngwlf vapalglial fmiypiawsl wmsfqsgrgm amkfagfani
       61 vrlwndpvfi kaltntmtyf vvqvpimill alilasllnn pqlvgrglfr taiflpcvss
      121 lvaysvlfkg mfatdgivns tlqaiglvas pipwlthpfw akvlvilait wrwtgynmif
      181 ylaalqnidk siyevaridg vpawarfthl tipllkpvil fttiistigt lqlfdevynl
      241 tegkggpsna tltlslyiyn ltfrfmpnlg yaatvsyviv vlvallafvq ffaarerdr
//
LOCUS       WP_457661569             154 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Sinorhizobium medicae].
ACCESSION   WP_457661569
VERSION     WP_457661569.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 154)
  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..154
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..154
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17412
     Region          7..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 mnasslkeen altitrvvna prdlvfkvwt tqehlsrwwg pkdftvaamt tdfrkggawr
       61 ccirapegqd ywahgiyrei eqpnrivfsf aweeegaidt litvtfedvs ggtaltfhqt
      121 pftsvesrds haegwsegid rladyvaark eevq
//
LOCUS       WP_457661571             245 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661571
VERSION     WP_457661571.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..245
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27161
     Region          3..243
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 malrdlsksf ringrplsvl rnltldirsg eclaivgasg sgkttllrvl aglespdsgr
       61 vlvdgrpvtg vgreravifq eprllpwltv lgnvafglev rgedpgrade rarhyialvg
      121 ladfqdaypk qlsggmaqrv glaraltvqp eillldeplg aldamtkltm qqeleriwre
      181 envtmvlvth dleealylad rvlilpkqkd asprligidl prprdrsear fvryrqellr
      241 efglh
//
LOCUS       WP_457661572             365 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457661572
VERSION     WP_457661572.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 365)
  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   2  (residues 1 to 365)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..365
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39278
     Region          6..320
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mvggankaat irevaalagv apgtvsnvlt gkklvaeplr ktvldaiaql dyrpnhlass
       61 lrfgrtksig ivvpdmtnpf fsglvrelel kaaksgfqil lmssheeaae ereriralvs
      121 rqvdgliisp srdsietsph saisgiptvl vdrafavegf dtvsadneqa tlmgtrhlie
      181 lghkritfla tapglanmee rvsgyrkamq dagvsdanvv ygglsiescr saieqelrra
      241 grptavfasa yvatlgaaka iraldlafpq dvsllgfdds dwmtvlrpyv stieqpldel
      301 ghacwellqr rmkkmdvppr pqadrlhlar kgvdpphpak igatlalrsl sgyenvtrvs
      361 arrag
//
LOCUS       WP_457661576             273 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661576
VERSION     WP_457661576.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..273
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29246
     Region          19..269
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdasgkgkrg rkagenatpa svqvldrsls llaiiaegdg stlttlsers gmapstvhrl
       61 ltslaqhgma tndtetgtwt vgvkafeign aflrfrklgt isrpflkrlm desgetanig
      121 ieddgdvvfi sqveshapmr affrpgrrgp ihasgigkai lstwsdteia ktlngkplpc
      181 ftgrtlatlp dlirnvqeir frgwsiddee htlgmrciaa plfneygeai ggisisgpsv
      241 rvdderlvvl gpavrrtade ltraigghrp eeg
//
LOCUS       WP_457661574             468 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457661574
VERSION     WP_457661574.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..468
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49229
     Region          <2..468
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 msggegaltl adgirvvdat agattegtaf algapvaagi feyqlyrggv tgdpdndddw
       61 flrsggvspp pppppppppp pppppppppp pppppppppp pppppppppp pppppppppp
      121 pppppppppp ppppppppgp ppitpsvrpe ipgyilkpal vqkmgvaaig tfherqgdef
      181 llnsngglpg awgrlfgesf dqswsskist fdfevspsfs gelwglqagq dligalhddg
      241 sqdrvgvffa ytgtsgsngg ntlgrlqves gsidlhansi gaywthigad gwyvdsigmy
      301 swldggsstd rgigvdtsgn stalsveagy pfrldngwvl epqgqliwqh iglddandrf
      361 tgidyesfgt wtgrlgmrle anttmndvpv qpfasinlwh dfdqdykvsf nrvpvvtele
      421 qtslelnvgf saqmsetvsv ygglqfatgl ddddnrgygg niglrikw
//
LOCUS       WP_457661580             479 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457661580
VERSION     WP_457661580.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 479)
  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 479)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..479
                     /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=51914
     Region          202..462
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrflvraddl irrwnsqpla rqfliiggsv aaaamlvvsa fvtslieeav trnsaattal
       61 yvdsviapll pdmqttqvld dsvaraldet lgqgalgdrl asfrlwradg tvlyssekam
      121 vgqkfelgpe lttafdgdmv arfmpldead geterlsnsp lleiynpllq pwsgevvavs
      181 efheiadefq qslnrarlht wlavagftla ffialsaivl rgsrtiekqr qtlgqrveel
      241 sallaqneal rgrlrqasqr atalnetllr rigadlhdgp aqlvayaslr ldsnklvsps
      301 tpedvrerei aaikgsldea mneirtlcsg lvlpqietag lreilercvr aheqrtgttv
      361 dlsmigppir lsasakiciy rfvqealnna yrhgggvaqr vtqstngdki tvevadggpg
      421 fdpgevqpts lglaglkgrv eslggtfein anapgtivrm algleemehd dgnpssrdr
//
LOCUS       WP_457661582             435 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Sinorhizobium medicae].
ACCESSION   WP_457661582
VERSION     WP_457661582.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..435
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46383
     Region          21..413
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 matdgvteqr gykpflpmlm syvasggslv lgsaaqlltf ailarwlgvh efsvfvaita
       61 vaniavhlcg lgameclvrr vardraiypq mlghniilts gsgaalvllg avvlpffftl
      121 spdrmtnvav itlmlvtnil lvrvivlteq ifiahtdfas ankvvvgfaa artvaaalac
      181 iafgattvaf wavwqflchv lvavccmwsv rllgapsyrl vreelpqgly fsipfilral
      241 rqnadllvls lvttaeivas ysvarriles sylsvealnr liypgsarat aaglhhalqr
      301 vrrvlaaatv islaaavtvf vlapilpylf gkeylslvgf artlcwvvvp lamwsvavea
      361 lgasgdhaar aavmgfgsia gtglaawasw yappagtfvs fyvieiamvv aswsvflhfv
      421 rrdrqaaitf gsgsa
//
LOCUS       WP_457661588             305 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457661588
VERSION     WP_457661588.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..305
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32094
     Region          1..295
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mlarlapaif vllwstgwvv akyaaffadp ltflalrysf aillfvcfcl lsgarwprsp
       61 taighaivsg iflhglylga vwwaigqgvp aaisgiiagl qplmtaavap wligeklngq
      121 qklglvlgfc gialavapkm laidasatpi hllplavnva gmaavtygtl yqkrylqngd
      181 lrsiaalqyv galivtipla lmlenlhvtw nlelvaalaw svlglsmgai alllylirrg
      241 qvsraasliy lvpplaagea alffgealtv pmilgtniav agvyltnrna aepapsavld
      301 tqrpl
//
LOCUS       WP_457661594             629 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661594
VERSION     WP_457661594.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 629)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..629
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67921
     Region          7..571
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtsgadllrv eglritfsvl gggveavrga sfrilpgrvt alvgesgsgk saisqaimgi
       61 lpsvasvtgr vvfndptgnk pvdllsldsg greiqdirga riskifqepm tslsplhtig
      121 nqisevlkiy tdidkagrre rteqllgyvg fsdpkraydm ypfelsggmr qramiamali
      181 cspalliade pttaldvtvq aqilqllrgl qsklnmamll ithdlgvvan madevvviyh
      241 geiveagpvd aifrnpqhpy lkglmaavph fdmkpgerlk alrevpvqag giigdrdvrk
      301 aggpnvlvsv rnlsktfstr ssgwfgsgsa frhravdnvs fdirrgeclg lvgesgcgkt
      361 tiskilmrav tpdkgtitfd dgegaldvlk ldgaelkalr akiqmvfqdp vsslsprmtv
      421 knilseplei hgrgtpksrv etvrsllqav gldqrfinry phsfsggqrq rigiaralal
      481 vpqllicdep vsaldvsvqa qilnllkdlq kelgltmlfi shnlavvdym adriavmyag
      541 rivelaprev lmsdpihpyt ksllaavpyp dldrkldfdl lqvsggsdqq rwgvqfadgg
      601 ddealvpadl ggghfvlark svdarelrp
//
LOCUS       WP_457661590             452 aa            linear   BCT 27-JAN-2026
DEFINITION  NfeD family protein [Sinorhizobium medicae].
ACCESSION   WP_457661590
VERSION     WP_457661590.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..452
                     /product="NfeD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46961
     Region          20..450
                     /region_name="NfeD"
                     /note="Membrane-bound serine protease NfeD, ClpP class
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1030"
                     /db_xref="CDD:440653"
ORIGIN      
        1 marilfllfs llsafmlpvs papaaerkai vlhvngaisp ataeyvtrgl rrardrgval
       61 vvlqmdtpgg ldtsmreiir aildspvpva sfvapsgara asagtyilya shiaamapgt
      121 nlgaatpiai ggglfgdder dgeetpgepd kqeprkpada geaklindai ayirglaelr
      181 grnidwaera vreaaslssa aaareqvidf tainlndllk qahgrsvrig qsdvrldtag
      241 lfiedlppdw rtqllsvitn pnvalllmmv giyglifefl spgtvvpgti ggislllgly
      301 alavlpvsya gvalillgag llvaeahaps fgvlglgsav alvlgaailf dtdvpglqvs
      361 wpvlsgigfa slafgllvar lallssrhki ltgaeemigi sgkvdswegv ggyviahger
      421 wsavsneplg pgedvmvvgr qgltlevark pt
//
LOCUS       WP_457661598             367 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Sinorhizobium medicae].
ACCESSION   WP_457661598
VERSION     WP_457661598.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..367
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41255
     Region          4..214
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mplplvsvll pvyngepyia aalesvlrqd yqrveviaid dgstdrsrdi lerygktdpr
       61 lsiisrenrg lvaslnegla lakgeliarm daddiaypsr lsrqvalfge eprlalcgtg
      121 idmlignrii rgrpnpiyrp gslrtlsmff tifmhstvvy nrtiipdeml rydsnyvhae
      181 dfdlfrriad rfpvhmidep lvayriheds vtskhkrqmr rthlsivaen lardalldds
      241 aalealgaav tgetvarlad cvlaleraia arpvevrgay edgalcffyf lyqliadeeq
      301 prlthefltr tgkwglirrr erygllaatr apwcsrisla asrrvdrlar hlqsvpaatv
      361 lpehglt
//
LOCUS       WP_457661602             451 aa            linear   BCT 27-JAN-2026
DEFINITION  O-antigen ligase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661602
VERSION     WP_457661602.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..451
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O-antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49671
     Region          159..387
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mliilfvtai avpwiipvga lrmsayrmtl civvipclvh wlsgragpir fsdfaiilfa
       61 fwkglslavl hgeeavqaig isfvetlgpy flarccvrsa edfevfakal fvviaallpl
      121 illetvtgwk atlrifafvl ptypddpmmr agfwraqgpf ehpilcgvvc svgfvlaflv
      181 lgyarppldr yskagtiaft valslsagpl lgialqslli awkrladaig prplwfmtvt
      241 lsalalctsw itgrslvalv grltfdpmsy wsrnliwevg wvsvsnhpaf gtglgrwdrp
      301 ewmvssidnf wlstavthgl pallfiiasv aiclvavgrk tglheklrey rsayvisvfs
      361 wcavgqtvhl wdgalvivlf llgsglwlld vdaneahpyp asdrlrrkri dsvgvrrpgh
      421 rrpprgsrrs pnlaehrfga tipkhypgps e
//
LOCUS       WP_457661606             185 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661606
VERSION     WP_457661606.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..185
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=19854
     Region          20..>168
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtvaseafar vletsilrla lddsdkshlg slgfiprryp ahavitrqgd eedrifvvhs
       61 gwgcictnli ngerqildfp lkgevvasra fegeglesft ahtevmlfea paksisagla
      121 hstslaagll gaiarekail sqhltnlgrr salvrtahfl lelgtrleka eaakshgfec
      181 ppnpi
//
LOCUS       WP_457661610             193 aa            linear   BCT 27-JAN-2026
DEFINITION  CatB-related O-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457661610
VERSION     WP_457661610.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..193
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20918
     Region          50..185
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(55,57,76,89..90,95,97,99,144,146,149,168,184)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(57,59,88..89,91,100..101,146,149,166..167,172,180,
                     182..183,185)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(57,59,88,100..101)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100040"
     Site            order(89,91,119,146,149,154,166..167,172,180,182..183,185)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 mkeevvaalg rhrvtfmgqp rdtrfgfgfk kdpialepfi qfrggafdvw kigaftylgc
       61 rmtvfrhvds igrfcsiapn vtvgaaehat rmlgthsmfn gqwdkqwpel fsefglttdq
      121 iavgrqaana qlaaragrvk igndvwigdg afisrgvtig dgaviaarsv vtkdippyai
      181 vggrpcaryp isi
//
LOCUS       WP_457661608             434 aa            linear   BCT 27-JAN-2026
DEFINITION  O-antigen ligase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661608
VERSION     WP_457661608.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Faridmoayer,A., Fentabil,M.A., Mills,D.C., Klassen,J.S. and
            Feldman,M.F.
  TITLE     Functional characterization of bacterial oligosaccharyltransferases
            involved in O-linked protein glycosylation
  JOURNAL   J Bacteriol 189 (22), 8088-8098 (2007)
   PUBMED   17890310
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..434
                     /product="O-antigen ligase family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0008754 - O-antigen ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008755 - O antigen polymerase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47152
     Region          150..393
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mriskaslvr pgandvfgtf alalsvfvfa ysarfgqvsi layyglwlpl vlvdyrkvlg
       61 nyasylwils ftifacltif wsaapslslr tgiqylshvv caliamrtid irtltrgmia
      121 gvaivllysl lfgsyhydpl dgtysfvgaf asknqlgfya slgiyfafaa vfvlgerglw
      181 mgaaggggll aaycllmsqs atsvlttaav iglclgmrai ttlrpasrki lftaasvfgg
      241 vaavaiiyag gidmilgafg kdstltgrty lwqqgieaak asplvgigyq aywvqgfsea
      301 erlweefyig sragfhfhnt fietavetgl iglvlltmvl amtffgqlkr llsedcdpel
      361 mvlfgvgall lvrafveidi ltpyhigsfl lyftagklti prrrvaalpw ppqlhpapyg
      421 raftpmmqrp genr
//
LOCUS       WP_457661614             365 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457661614
VERSION     WP_457661614.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..365
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39846
     Region          9..361
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mmlglrgipn vqggvekhve mlssrltghg wevevvgrrr ylpvsgphlw ngvrvsplwa
       61 prmmaleaii htflgicfaa mrrpdvlhih avgpallvpl arlmrlnvvv thhgydydrq
      121 kwgafakkml rtgermgmrl ahgriaisre iaatmgeryr vpvafvpngv avshcdvetg
      181 vlgefgltrr ryillaarlv pekrqidlik ayaklgntgf nlvlaggaef esayedevra
      241 lasrvpgvvl tgfqtgdrla elfanaalfv lpsshegmpi alleamahgl pvlasdivan
      301 rqldlpagdy fplgdidala saisektats ldeqevlaqt ervesaysws svalktldvy
      361 ravtk
//
LOCUS       WP_457661616             257 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661616
VERSION     WP_457661616.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 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   4  (residues 1 to 257)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28935
     Region          18..246
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 marqenlpde spidrnhpda lyaqlrnllr gmierrelav ndklpserel vavygvsrit
       61 vrqaikelen lgylqtrpgk giyvtepapi yelevvrsft qtahannrkp gmrllraeia
      121 radpevarpl slptgaevvf leelrlldgv pvvvqrdwfs asltpgildi dwtvenrsly
      181 defenrygil psrgqstlsa rlasdleasl lqldrpaavl tldqiaydsh nrtvnisaaa
      241 yhptryplsl tqshrrf
//
LOCUS       WP_457661617             374 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661617
VERSION     WP_457661617.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41041
     Region          14..370
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mllrsrhrrp kpggrslfql aalrfrrnrp amagcvmlvl iglfsfvgpl fsphsydqvf
       61 psyvtigpsl eprpdsstlq dvmegvasra rvrltefave dqsftatvts dapidpratr
      121 yfdranefen tkvvategdg rtlkvegdva reyfpfgtds ngrdllvrvm lggqisiavg
      181 llaslvslgi gvlygatsgy iggrvdnvmm rfveilyslp fvflvvvlvv ffgrsfilif
      241 lvigavewld marivrgqtl alkrrefvga aqalgltdwq iirrhiipnt igpvivfvtv
      301 vvpkvilles flsflglgvq apltswgali seganniqsa pwllifpaif fvltlfslnf
      361 vgdglrdald pkdr
//
LOCUS       WP_457661618             228 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661618
VERSION     WP_457661618.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..228
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24983
     Region          2..227
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mvvdelgqav vggefsvgdt lpgdtdlaar fnvsrtvlre amktlaakgl vvprarigtr
       61 vlpkahwnlf dsdvltwhfg agvdekflrh vsevrlalep yaaalaarra sdadiarmmr
      121 lavamgdagh sphtlaqadl efhlrlleas lnpfmrtvgs lieaaligvf qltsptadet
      181 eidrvaiahi riveeirrrn edgarrameh virvgqerli lnlkerqg
//
LOCUS       WP_457661619             299 aa            linear   BCT 27-JAN-2026
DEFINITION  Fic/DOC family protein [Sinorhizobium medicae].
ACCESSION   WP_457661619
VERSION     WP_457661619.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Veyron,S., Oliva,G., Rolando,M., Buchrieser,C., Peyroche,G. and
            Cherfils,J.
  TITLE     A Ca2+-regulated deAMPylation switch in human and bacterial FIC
            proteins
  JOURNAL   Nat Commun 10 (1), 1142 (2019)
   PUBMED   30850593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Kinch,L.N., Yarbrough,M.L., Orth,K. and Grishin,N.V.
  TITLE     Fido, a novel AMPylation domain common to fic, doc, and AvrB
  JOURNAL   PLoS One 4 (6), e5818 (2009)
   PUBMED   19503829
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..299
                     /product="Fic/DOC family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /GO_process="GO:0018117 - protein adenylylation [Evidence
                     IEA]"
                     /calculated_mol_wt=33212
     Region          9..221
                     /region_name="FIDO"
                     /note="Fido, protein-threonine AMPylation domain [Signal
                     transduction mechanisms]; COG2184"
                     /db_xref="CDD:441787"
ORIGIN      
        1 maderpkgsy typntsddpd rtnvlknrwg iethselrvk eyratavrma elaegdgpqg
       61 nfdkahlkai hgyifqdvye waghtrnesp ivegqrvepi gglskggtsf lpgsriemgl
      121 dealkpirdp qalrnatpee faeragrvls elnyvhpfre gngraqeafi selgrhyghe
      181 idfsaitkpr mieasietts dpsspvmkhv iedamspgrr eairsafedl revgeeplhh
      241 hvrtaragee itgqilghdn rvaslvtdqg ivvadradlp eklpdedeit ftarrtfpg
//
LOCUS       WP_457661627             444 aa            linear   BCT 27-JAN-2026
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Sinorhizobium medicae].
ACCESSION   WP_457661627
VERSION     WP_457661627.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..444
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=48757
     Region          13..443
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mskkfdkseh wahpataalh agfrndpstk avcvpiyqns ayelegdlsk ianvynvked
       61 gytytriinp ttralerrfa avdnatdsla vasgqaatfi alanlcsgrp gdnivaspfl
      121 ygnswnllhn tfrrfgietr taensdpaaf erqiddrtic lfgecisnpi ldplplrslv
      181 eigrrrgvpv vvdntttplv crpaklgadm atysatkyvc ghgttlggii sdygsfpfqq
      241 hpesfplfsn pdeahggilw heavrevqdl gksatllkar mtwlrdvgac aspfnsfqll
      301 qgletlhlrm rqhcanaqtv aemlrnhpkv akvtyplfft gqkkeladdl fdrsygygam
      361 lmfevgdarn grtlienidl lyhvsnvgda rtlithpvst thttvprdkr iaagitdgti
      421 rlcvglehad diigdlekal saiy
//
LOCUS       WP_457661629             262 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661629
VERSION     WP_457661629.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..262
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=28935
     Region          6..255
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mplvgvtanr lvedevhrew vrrryidtle tlakveivvl ptqstndrvg irkiadrldg
       61 lvltgdesnv npdyvsrsna rrlfltesgy rrgesdhyrd vmasgflsaa lerglpilgi
      121 crglqemnvf fggalfedis srkdmlrhre dvslprdrqy dpvhdviiqp ggkfasifgc
      181 gtlikvnslh nqgisslgng ltceavapdg lieaisvana dalqlavqwh pewhaaedph
      241 skrlfgafgk acadygskrp rq
//
LOCUS       WP_457661632             472 aa            linear   BCT 27-JAN-2026
DEFINITION  alanine/glycine:cation symporter family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661632
VERSION     WP_457661632.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 472)
  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 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..472
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49341
     Region          1..447
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mntiiaflnt ilwgyvliyg llavglffti rlglpqiihf gemfrvlssg gskdtsgisp
       61 fqalmvslas rvgtgnlagv avalylggpg atfwmwmval vgmatayaes alaqlykvrn
      121 edgqyrggpa fyiahglnap waaaifslcl iisfglvfna vqansiadav qgafgvpklt
      181 vgfglavlsg vvifggirqi arvaeiivpf mavayllmav yvlianaalv phvlwtivss
      241 afglqeaagg vtggiaaaml ngvkrglfsn eagmgsapni aavatpvphh pssqgfvqsl
      301 gvfidtilic tatsvmills gtldpgsnit gtqltqaamn vhigaagtyf iaiaifffaf
      361 tsiignysya enaltylgag nrlgltimrc atlvmvvwga yesiatvfda adasmglmat
      421 inliaillls gtiakltkdy fkqrkqglap vfhaadypel qgkidhgiws rv
//
LOCUS       WP_457661640             391 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457661640
VERSION     WP_457661640.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Goodwin,T.J. and Poulter,R.T.
  TITLE     A new group of tyrosine recombinase-encoding retrotransposons
  JOURNAL   Mol Biol Evol 21 (4), 746-759 (2004)
   PUBMED   14963102
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42744
     Region          193..390
                     /region_name="INT_Cre_C"
                     /note="C-terminal catalytic domain of Cre recombinase
                     (also called integrase); cd00799"
                     /db_xref="CDD:271180"
     Site            order(209,223..224,226,302..304,318,320,338..340,375)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271180"
     Site            order(218..219,346,350)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271180"
     Site            order(223,265,340,343,375)
                     /site_type="active"
                     /db_xref="CDD:271180"
ORIGIN      
        1 mvdnhraags dsqavhrrae qldaldailp fdrrdqlaal ltdddvatlk hlaqegmgen
       61 tlralasdlg ylegwcqlat gaplpwpape slllkfvahh lwdpvkraed pahgmppdve
      121 vglraerllr sdgphapgtv rrrltswsil trwrgfagaf gapslksalr lavkasnrpr
      181 qrkskkavtl diltklleac asdrlvdvrd rallltafas ggrrrsevaa lrvedladee
      241 pvranpaden spplpclsir lgrtktaaad ddehvllvgr pvtalkrwla eaqikdgpvf
      301 rridkwgnid rraltpqsin lilkarceqa gldpalfsah glrsgyltea anrgiplpea
      361 mqqslhksvt qaasyynnae rkngraarli a
//
LOCUS       WP_457661644              91 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein, partial [Sinorhizobium medicae].
ACCESSION   WP_457661644
VERSION     WP_457661644.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..>91
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          3..>91
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 marigyarts ttdqnlaaqi aalrnagcev ireeqksgas legrpqlmti ldfihagetl
       61 vitridrlar slrdlqvivd rlkakgahlv a
//
LOCUS       WP_457661645             119 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Sinorhizobium medicae].
ACCESSION   WP_457661645
VERSION     WP_457661645.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..119
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=12572
     Region          <1..118
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mgvsnwfass srgdssklsg gtfssglrmg tlveltnpkg iafflglyav sippdaaisv
       61 kltvlaggfi lemlwysfvt mlmssppaqa vyrtsgawid rfvgtlligf gikllserl
//
LOCUS       WP_457661650             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457661650
VERSION     WP_457661650.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32150
     Region          78..292
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(85,126,163,178,180,188..191,240,265..267,269,272)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(105,112,138,204,206..210,238,242)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            163
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrnypeiasr mfgtplmlhp skgdiiaraf gprvlgspda pshvaggeem gllgdklrna
       61 tdwdgeriyp gpdlvasgia lieiegslvn kgkwigkscg mtsyeaigvq vrdcierddi
      121 kavvfevdsy ggevtgafdc aeqifelsqa kptiavltdh acsagyllas pcrqlvipqt
      181 gicgsigvis mhvdmsawla keglkvtilk agehkadfnp yeaipddvlq qelaeleelr
      241 vefaatvary ragrltqqsa latearvyrg qkavdaglad avarpsqvle afeaelsrta
      301 g
//
LOCUS       WP_457661658             451 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661658
VERSION     WP_457661658.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 451)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..451
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48830
     Region          1..354
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mksmlkkgll aaalmastap aamaqecada drvpitwsti agfytdamae lvsgfeaghc
       61 vkvnvvnidn sqlynkqvie mvgqtgaydv vtletsekae faengfilpm teyfadkkaq
      121 lddvaptlaa lttqykddvw glpyytytag yiyradlfdd ptekeafkkr fnydlavptt
      181 waqhrdiaef ftrkagetlk gekltkdfyg vglmagpfpe iqdemsgvlw sqgadwltde
      241 gkvpvdavek amndylelvk yappaaltvt ydgvmnqmkd gqiaqtysff ldqwpnavqt
      301 etsvagakmg vaeapekkay iggfllavsa ssahpkeamd fvahigghda qmefakaggt
      361 stlmsvlsdp afaapesrgk tghfstllei fnsmkgfrsn lfdtpfgaki yntmqiplqs
      421 aaagqisarq aaeqlaveve kicggpcpig k
//
LOCUS       WP_457661659             494 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661659
VERSION     WP_457661659.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..494
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=53644
     Region          5..494
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mnqheillkl eniekrfpgv valksislev ragevqvllg engagkstlm kipagehppt
       61 dgtivvggrk vpaltptlat elgiglvhqe lslipalsvt eniflgrmpr nafgkinwsk
      121 ahadarhale algvfidpaa evrtlevaeq qlveitrvle rgprilllde ptsalsdger
      181 srlfdvirll kqrghgiiyi shhlseipli adrvtvlrdg ivvktlpadq adeetviglm
      241 vgrrleeqfp kekvelgtpv lvvenlasgt tlkdlsftlr rgeilgvygl mgagqaeias
      301 alfglqavka gsvevegkra nfrhssdaia aglglisrdr rqslvpmqpv gpnlslswla
      361 gksllsrldl trereegsry isdlrirpas tthklfffsg gnqqkvilar wmssgarili
      421 fdeptrgidv gakaevfavm srlvsegasi lmisselnel igmadralvm rggrlsaelp
      481 rkeisqqnll ryas
//
LOCUS       WP_457661660             311 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661660
VERSION     WP_457661660.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..311
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34201
     Region          11..281
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mayaarhegl pairpplmer iadasapyly tapalilivt vmlvplvlgi syafrdiqll
       61 npfsggfvgl dhfralaqdq affrslrntl wwtgasvflq fafglilall ldkpfhgrav
      121 aqalvflpwa vpsflaglnw awlfnpvvgp lphwlfamgi msqptnilsd pqlamwgpiv
      181 aniwwgipff aitllaalqa iprdlyeaas idgagplqrf lsitlpflap tiaitillrt
      241 vwisnfadli ivmtnggpad rtqivasyif tqafkrldfg yasaialvll alllayslli
      301 vilrqwllsk d
//
LOCUS       WP_457661662             345 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661662
VERSION     WP_457661662.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..345
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36769
     Region          1..345
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msglalqnvv kefgsfravn dvdltvphgt fvcmlgpsgc gkttllrmia gldlptsgai
       61 gldgeditrv pthkrnlgmv fqslalfphl tvgeniaypl rirgapkenq rkrvdellsm
      121 ihlsgyadrp vsklsggqrq rvaiaralai spklflldep lsaldaklre amqvelrqlq
      181 qklgittivv thdqreamtm adtvvvmngg eirqaaspie iyrrpadsfv adfigqtnlv
      241 eaetdrsgrv tvfgqpvpgl dlpagaakam lsirpedvhl tapgagaltg tvtfvrdlgs
      301 tietfvdvag rqivavstpr arpqvtvgqq vgigltpdvc vvlak
//
LOCUS       WP_457661663             263 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661663
VERSION     WP_457661663.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..263
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29125
     Region          3..260
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtsnsasvvs arnlgltfet sdgpvnaltg vdldvakgdf vsfigpsgcg kttflrviad
       61 lekptagsit vngmtpeear rrraygyvfq aaalypwrti ennialplei mgysredrka
      121 riertlelvn lsgfgkkypw qlsggmqqra siaralafda dlllmdepfg aldeivrdhl
      181 neqllmlwar tnkticfvth sipeavylst riivmsprpg rvtdviestl prerplgire
      241 tpefleiahr vreglraghs yee
//
LOCUS       WP_457661664             528 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457661664
VERSION     WP_457661664.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..528
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=57544
     Region          4..523
                     /region_name="ASKHA_NBD_FGGY_D-RBK"
                     /note="nucleotide-binding domain (NBD) of D-ribulokinase
                     FGGY and similar proteins; cd07782"
                     /db_xref="CDD:466800"
ORIGIN      
        1 mreyvvavdi gtgsaragvf dgrgrllara dqpiamnrpe enhaehdsed iwaavcgavr
       61 sarekaavpa esvaaigfda tcslvvrdrd gaplsvnrqg earwdtivwl dhralaeadf
      121 ctatrhqvld hsgkvmspem empklmwlkr nlphqwekag yffdladyms wratgspars
      181 rctltakwny lahekrgwqq dyleqigled llargglpee tlpveravgr lnasaaeelg
      241 ldaecrvapg lidayagalg vlggfagdka klerqlalig gtsscivafs kdmkpgfgmw
      301 gpyfeavlpg lwlieggqsa tgalldhivr lhggglpptt ethakiierv qelralhggp
      361 gfadrlhvlp dfhgnrspla dphalgvisg laldssfdal crlywrtcva ialgirhile
      421 mmkevgyeld tlhvtgghvr nsllmeldcd vtgcrvvape tpdavllgta mtaavagkly
      481 pdlasagpam ssagkerlpd atrrrdydrd yrrflalyrh reelesie
//
LOCUS       WP_457661665             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661665
VERSION     WP_457661665.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35432
     Region          1..330
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maavffdnvs ryfgavravd rvhltiaege ffamlgpsgs gkttclrlma gfeqptgghi
       61 eifgetaegv ppyrrsvntv fqdyalfphl sildnvaygl mvkgigreer rkaaedalam
      121 vklpgygtrr pgqlsggqrq rvalaralvn kpkvllldep lgaldlklre qmqeelkilq
      181 kslgitfvfv thdqgealsm adriavfneg riqqlgspee vynrpqtrfv adfvgssnvl
      241 sedlcrslgl kasfaslrpe avaiappseg alslagtvas qsflgatnri vidvegvria
      301 vaspaargvp avgspvtisf aahdlhpmed a
//
LOCUS       WP_457661666             416 aa            linear   BCT 27-JAN-2026
DEFINITION  D-amino acid dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457661666
VERSION     WP_457661666.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..416
                     /product="D-amino acid dehydrogenase"
                     /EC_number="1.4.99.-"
                     /GO_function="GO:0008718 - D-amino-acid dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0055130 - D-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44648
     Region          1..415
                     /region_name="PRK00711"
                     /note="D-amino acid dehydrogenase"
                     /db_xref="CDD:234819"
ORIGIN      
        1 mkvivlgagi igvtsayqls raghevtvid rqpgpalets fanagevsfg ncspwaapgi
       61 pmkalkwlfm qhaplilrpr idaamlswma kmlsnctsrr yavnksrmlr ladysrtsla
      121 alreetaity dermqgtlql frteaqldas akdisalaad gipyevldrd gciraepalg
      181 rvrdkivggl ltpqdetgdc fkfanalagr aeklgvcfdy gteiralevd ggrvhgvvts
      241 kgrraadavv valgsyspll vrrfgirlpv ypvkgyslti piadasrapv stvmdetyki
      301 aitrlgdrir vggmaeisgy tndlgiarrr tlehsvmdlf pggdaakgsf wsglrpmtpd
      361 gtpvigptri aglflntghg tlgwtmssgs arviadlvsd rkleidatdl aiaryg
//
LOCUS       WP_457661667             326 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661667
VERSION     WP_457661667.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36806
     Region          15..317
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mlkflfcenr yvfvmdlfrh vgllrsflmv aregnvtaaa eklgisqpal trsirrlede
       61 tgfrlfdrht rgvtptiygk allrhaqlid tecrfassel ealrsghrgq ikigggpfwg
      121 aallpravar lhsllpklqv nlqigvnnvl hpklldgeld lvvsaaprdl sqfpehfrft
      181 rittirsqmf vreghpilaq eriryedlan ypwimyqqdp eiiervatll kdlgvnppri
      241 aieasslmav lellrsgdfl aclaapilgv vqdvgirpvp idreiwsfpa gityhraieq
      301 stpfellrqm ltdevtklgl drteqr
//
LOCUS       WP_457661668             191 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457661668
VERSION     WP_457661668.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..191
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21442
     Region          5..181
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 miiheterlk lrawleadrd lfaeinsdpk vveffpfrrn radadalfds nnrnihetgf
       61 gffalalren dapigfcgla rtdlkphlpd gtveigwrla arhwgkgyvt eaagalpdyg
      121 feerklgeiv aiavatntrs iavmkrigmy cdpsrgfehs gvpdthpqlr phvlyaitad
      181 rrqrngetak r
//
LOCUS       WP_457661669             184 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Sinorhizobium medicae].
ACCESSION   WP_457661669
VERSION     WP_457661669.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..184
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21029
     Region          22..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mphgrdglkn gagetisspd pfedkilalm palrrysrsl arsdtdgedl lqdcvekvla
       61 rrmqwrgvnl rawaftimtn lyrnghrhra rhpevefdqa ldlraeenna dplerqrlvh
      121 aleqlsadnr avlmlvvieg yryqdvadmm eipigtvmsr lsrarrqlae amkddnvial
      181 rrpk
//
LOCUS       WP_457661694             500 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457661694
VERSION     WP_457661694.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..500
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=52594
     Region          414..>498
                     /region_name="Lipase_GDSL_2"
                     /note="GDSL-like Lipase/Acylhydrolase family; pfam13472"
                     /db_xref="CDD:463889"
ORIGIN      
        1 madeirdafa vawpdgpasd pvepdkstir sigpvidkki antaadlqmq ineveliaea
       61 asaglvqkgt wtalaaivgt tngqagrvag pdagthtdpv vggtvanege yawstspagw
      121 qrvgdllvsk vaqvaasfhd nlgfvgmqlq tdgslrqnpp ersfeigdtr ssaellavqd
      181 efgfkalslt atefrapgvs ggedegfnsg fdaspliggh lvafdgaeth lytrnilpar
      241 sdisrvrasl yseaatdgsr ptysrlgdde lvvdltkcgg tvylqtrlde vnpdirhqat
      301 msvvtppvap gslntarvlm igdsitnrqm aarmnaaaaa kgytltfvgt lngagigqis
      361 sdvtgplgeg regwefgdft yavadrvsiv tpgdeatyla sdkatkqtkn pflrvaaggd
      421 dpsvvrngnv fdfdfyldrf tladphvvfi glgtndirdl nspdlgpait dgltimcgqi
      481 qaarpgtkiv iwfppgftlk
//
LOCUS       WP_457661698             534 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661698
VERSION     WP_457661698.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11458748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..534
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55193
     Region          42..>178
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          166..425
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <284..>334
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
     Region          <385..533
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 matvtyhfpg glypsqynpp lsgvsvnptf gelvdmsesa rstttstdvl yrldnglklk
       61 lvgtgfsfsp sgdalggtit sievllnngt tlvqtisgls lsledfqnas aafgnlelea
      121 wllnradtin gsaghdnlsg hfgndvlngn ggddfitggn gddtydggag hdilsfqday
      181 gsplatngvn lntatgtvtd qfgfsetfqn feeyrgtqfa dtmigssane tfmglggrdt
      241 lngwtgsdlv rydrdaqfgg tlgvkvdlaa gtakdgfgre dtlisienvr gtdfadsivg
      301 nwaanflrgf agndwinggt gsdtmrggkg ndtytvdrsg dvvdenadsg agvdtvrstv
      361 sfnlgnaavv kgsvenlvlt gtwdvsgtgn glnnsltgns gnnslngsdg ddvingdlgn
      421 diltgsvgld sfrfntalde atnvdtvtdf tvaddtiqlq asiftgivgt gtltdvqfva
      481 natgtaetae nriiydvdtg elfydsdgng aggavhfatl gtnlsitaad ffvi
//
LOCUS       WP_457661744             343 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Sinorhizobium medicae].
ACCESSION   WP_457661744
VERSION     WP_457661744.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11488572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..343
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=37284
     Region          24..339
                     /region_name="rluA_subfam"
                     /note="pseudouridine synthase, RluA family; TIGR00005"
                     /db_xref="CDD:161659"
ORIGIN      
        1 mndpfkqapg nrkvltagdd asgrldaflt ealggefsrn rikglieqga vsvnaltvte
       61 skrkvhpgdt fqialpeped pepkgeaitl dvlyedqdli vlvkpaglvv hpgagnwtgt
      121 lvnalihhcg dslsgiggvk rpgivhrldk dtsgvmvvak ndaahrhlsd qfadhgrngp
      181 lerayravvw grprqlkgti daplgragdr tkravkrdds ddareaithy evvdryhekp
      241 dgtslasave chletgrthq irvhmahigh pligdpdyga afrtkanllp erartavnrf
      301 prqalhafml qfehpstget mhfeaavpsd mqelvdalrm aap
//
LOCUS       WP_457661751             518 aa            linear   BCT 27-JAN-2026
DEFINITION  formate dehydrogenase beta subunit [Sinorhizobium medicae].
ACCESSION   WP_457661751
VERSION     WP_457661751.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11555116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..518
                     /product="formate dehydrogenase beta subunit"
                     /GO_component="GO:0009326 - formate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54302
     Region          3..94
                     /region_name="TRX_Fd_FDH_beta"
                     /note="TRX-like [2Fe-2S] Ferredoxin (Fd) family,
                     NAD-dependent formate dehydrogenase (FDH) beta subunit;
                     composed of proteins similar to the beta subunit of
                     NAD-linked FDH of Ralstonia eutropha, a soluble enzyme
                     that catalyzes the irreversible oxidation of...; cd03063"
                     /db_xref="CDD:239361"
     Site            order(4,6,40..42)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239361"
     Region          100..508
                     /region_name="NuoF"
                     /note="NADH:ubiquinone oxidoreductase, NADH-binding 51 kD
                     subunit (chain F) [Energy production and conversion];
                     COG1894"
                     /db_xref="CDD:441498"
ORIGIN      
        1 mtvrifiprd aaalalgaes vveaisgeia araldativr ngsrgmhwle plveietadg
       61 rvaygpvkag dvaslfdagl tsggahplcl gkteeipflk rqtrltfarc gvidplsldd
      121 yrahgglrgl eravvmqpaa ivaevtesgl rgrggagfpt gikwktvlet pgarkyivcn
      181 adegdsgtfa drmimegdpf vliegmaiag iatgatkgyi ytrseyphai avmsaaveia
      241 raagvlgtsv lgsahafdme vrtgagayvc geetsllnsl egkrglvrak pplpahkglf
      301 drptvinnvi slasvpvild kgagyyrdfg mgrsrgtipl qiagnvrhgg lfetafgltl
      361 geivdeiggg tasgrpvkav qvggplgayf pralfdtpfd yeafaardgl ighagivvfd
      421 dtadmlkqar famefcaies cgkctpcrig sirgvevada iaagiepekn rvlladlcnt
      481 mkfgslcalg gftpypmmsa mthfpedfsp vpmveaae
//
LOCUS       WP_457661756             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661756
VERSION     WP_457661756.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..330
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34235
     Region          15..328
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnatsqtlag akgvtasrgr kdwllrystl falivlflgf aitvdrflta snllniiqqi
       61 smltivgagl tfgfaaremd lsvgymvgls gilvplllis gvplplalla gvgagfavga
      121 vnsalvtlvg gpsliatlat gsilyginfl ttggraiygg lpdaylwmgq grllgipvla
      181 yamvlfvlla wflmertifg ryiyaaggnl raaelsgvng rfyraaalvv cslfaavaga
      241 llaarlgsgq pnagerylld glatvfigmt mirpgtatvt gtffgalfig vinnglnlvg
      301 mdtyiqsivk gliilvavai vsrttklkll
//
LOCUS       WP_457661758             489 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457661758
VERSION     WP_457661758.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..489
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51484
     Region          1..479
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mttailaidq gttnskavlv sttgeilsrg aspvgiehpq pgwveqnplr iwesvqeaia
       61 aclqkgprsd ilgiaisnqr esvtaweaat gkplgpvvsw qcrrsapaca elsaaghaer
      121 vraltglpid pmfpgpkmkw lldrippghe vrlgtidawl ihcftagaih acdagnaars
      181 qlydlnrraw sdelcdlfgv pksalpevcd saarfgvtkn vpglkdgipi asaigdshaa
      241 lfghgafkpg dgkvtfgtgs simttlprfi apeqgittti awsiagrpty afegnilvsa
      301 aalpwmaeml glshvedlid laataeprgp gfvpafvglg apywhadara lfsgitfntt
      361 raqmaravtd smafqvhdvf kamsaqsptp lgrlyadggp skntflmqcv adtlnhvitq
      421 cdapeasalg aaylaglslg vwpdlaavas lpragkpvlp rpcdaadrlm vwqdaiyrst
      481 vpgpsimse
//
LOCUS       WP_457661762             372 aa            linear   BCT 27-JAN-2026
DEFINITION  murein transglycosylase A [Sinorhizobium medicae].
ACCESSION   WP_457661762
VERSION     WP_457661762.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   van Straaten,K.E., Barends,T.R., Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     Structure of Escherichia coli Lytic transglycosylase MltA with
            bound chitohexaose: implications for peptidoglycan binding and
            cleavage
  JOURNAL   J Biol Chem 282 (29), 21197-21205 (2007)
   PUBMED   17502382
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Powell,A.J., Liu,Z.J., Nicholas,R.A. and Davies,C.
  TITLE     Crystal structures of the lytic transglycosylase MltA from
            N.gonorrhoeae and E.coli: insights into interdomain movements and
            substrate binding
  JOURNAL   J Mol Biol 359 (1), 122-136 (2006)
   PUBMED   16618494
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Lommatzsch,J., Templin,M.F., Kraft,A.R., Vollmer,W. and Holtje,J.V.
  TITLE     Outer membrane localization of murein hydrolases: MltA, a third
            lipoprotein lytic transglycosylase in Escherichia coli
  JOURNAL   J Bacteriol 179 (17), 5465-5470 (1997)
   PUBMED   9287002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     gene            1..372
                     /gene="mltA"
     Protein         1..372
                     /product="murein transglycosylase A"
                     /EC_number="4.2.2.-"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40855
     Region          5..365
                     /region_name="MltA"
                     /note="Membrane-bound lytic murein transglycosylase [Cell
                     wall/membrane/envelope biogenesis]; COG2821"
                     /db_xref="CDD:442069"
ORIGIN      
        1 mpfdlepvsf selpgwfadd papviaslrr chrhvttvkp yktgslglsv edmlpafeaa
       61 ggdfanaaaa raffeawfvp frirpkgkra gfvtafyepe ievreepdan frfplyrrps
      121 dlvdindanr pegmdpyfaf gclrdgriee ypdrcaieeg flagrgleia yarskvdvff
      181 vhvqgaarln ypdgsrrrit yaaktghrft aigkllierg eidaatvsma sirewlaahp
      241 drtdevlrhn rsfiffreap vekddlgpva aakvplepgr slavdrliht fgvpfyiase
      301 tlthldggns fgrlmlaldt gsaivgparg diftgsgdaa gdlagsvrne adffilvpla
      361 aaaryrrqss hg
//
LOCUS       WP_457661769             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661769
VERSION     WP_457661769.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36626
     Region          10..342
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mteppmsipl levtglktsf ttprgkvksv ddvsfsiaag ktlgvvgesg sgksvtslsi
       61 mrlvgrgggv iddgairlnl pgqpgldira ldekamrkvr gndiamifqe pmtsldpvws
      121 igdqiieair lhqdvsknea rekaiemlrl vgisapesrv ddfphqlsgg mrqrvmiaia
      181 lscrpallia depttaldvt iqaqildlir rlqkeigmsv lfithnlgvv aeiadkvavm
      241 yagqvveegp vrtifsaprh pytvgllksi pmpggmrvdd agsrrldtig gmppnplalp
      301 agcrfaprcs laiedchkap pplvqagdeh gvrcirwqea sk
//
LOCUS       WP_457661771             336 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Sinorhizobium medicae].
ACCESSION   WP_457661771
VERSION     WP_457661771.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36694
     Region          141..333
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mfgiditvlg laglvalaaa alaygllypr ietekktegr llrvsaaetd rtkikaardr
       61 vnemskrrks vqdslkelek kqqeksansa psmkkrllqa nlsisvaqfy lfsalfglft
      121 fvvvflagag aliaagvwlt aaaglprwiv gsrikrrcrk fldefpnald vmvrsiksgl
      181 plndalrlia sdgqepvrte frrvvesqqv glnvpeacar mihsiplpev nffaiviaiq
      241 aqaggnlsea lgnlskvlre rrkmkakvna lsmeakasac iigalpfiva tlvyltspay
      301 mailftdprg hlimgasavw msigiwmmrn minfdi
//
LOCUS       WP_457661770             528 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661770
VERSION     WP_457661770.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 528)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..528
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57262
     Region          30..515
                     /region_name="PBP2_NikA_DppA_OppA_like_7"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08512"
                     /db_xref="CDD:173877"
ORIGIN      
        1 mrignkrglq fatallscma gfagpasaqs sdlvvnsava pstldpawac glqeisflqn
       61 fyvrlvqngt aegpegtgav dyskiepyla kswevsedgl vytfhlkegy tfesgkpvda
      121 davryslqrv ldmagcgrff ltdghidpvi fksieavdpl tveitlnkpn gnmlgdlath
      181 aasivdpsiv eanggvtpgq pneymaanvt esgpflldsy tanqnarlva npafageapa
      241 skainvnwit alptlllqar tgqaditfgl akqavktmvs nagtrviays spfaqqmilp
      301 ntkapwnnkl frqavahavp yesivsrvay gygtqyygpi ppslpgfkae lskpvpfdld
      361 rakvliaesg vatpvdvevm iqegdatqqq latilqstwk dlgitlkirv apaaefqdls
      421 qghrvqslmr ldgpgvfevg yywgydavcg npnnlteycn kdmdalierl rassdpaerq
      481 timdqateiw radypkilff edqpvvvlsd avtkftfspl pdyrywak
//
LOCUS       WP_457661772             319 aa            linear   BCT 27-JAN-2026
DEFINITION  2-hydroxyacid dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457661772
VERSION     WP_457661772.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kutner,J., Shabalin,I.G., Matelska,D., Handing,K.B.,
            Gasiorowska,O., Sroka,P., Gorna,M.W., Ginalski,K., Wozniak,K. and
            Minor,W.
  TITLE     Structural, Biochemical, and Evolutionary Characterizations of
            Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two
            Distinct Subfamilies
  JOURNAL   Biochemistry 57 (6), 963-977 (2018)
   PUBMED   29309127
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..319
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34730
     Region          15..314
                     /region_name="GDH_like_2"
                     /note="Putative glycerate dehydrogenase and related
                     proteins of the D-specific 2-hydroxy dehydrogenase family;
                     cd12164"
                     /db_xref="CDD:240641"
     Site            order(54,73..75,98,234,282)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(74..75,92,98,102,146..150,168..171,173,199..201,
                     205..206,232..234,258..259,282,284..285)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240641"
     Site            order(101,103..105,107..108,111..112,115,117,120..121,
                     123..124,128..129,131,134,137,161,256,260,263..265,267,
                     271..272,274,277,279..281,283..284,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240641"
ORIGIN      
        1 msakspvivd lkfireevea alagafpdre vidladpvhr grdlsgidya vvwksapdlf
       61 srapdlkvvf sggagvdhvl tlpglpdvpl vrfvdrtltt rmsewvvmqc llhlrqhhay
      121 ealanrhewr dlsqpeaadv tvgimgmgvl gqdaarklav mgfkvigwsr skrviegvet
      181 ydaagldafl gqtdflvgll pltpetrgif ngalfaklsr rgpfgapvfi nagrggsqve
      241 adilecidss mlagasldvf ereplpqesr fwdlpnvyvt phvaassdvr alfvhvehqi
      301 arfesglple hvvdkvagy
//
LOCUS       WP_457661523             219 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Sinorhizobium medicae].
ACCESSION   WP_457661523
VERSION     WP_457661523.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..219
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24443
     Region          6..>184
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mttiiielnk ldadpknvrk tysadsiaal aasikvngvl qnlvvrtaek kgryfvtage
       61 rrrralllll eqgeiqknha veckvrdsed ateisltenv mredmhpvda yeafsalade
      121 gkaipdiaar fgtteiivrr rlalakvspk lldlyrkeem tfeqlsaftv sddherqeqv
      181 wnglstwdrh asriksnllt devastdrrv kfvggagcl
//
LOCUS       WP_457661777             500 aa            linear   BCT 27-JAN-2026
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661777
VERSION     WP_457661777.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..500
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=52721
     Region          4..500
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mlrgvtfvfg gvriegaavl peaklladwp hkagdtvrvd eifalaesis qayreagyal
       61 sfamvpqqqi dggvfriqvv egfvervvik gdlseavrad mqafadrila srplrtadle
      121 rylllindmp gvtasgvlsp aaveagavlt leaahepvag svgynsfmpd tlgthvleas
      181 ggmqgvltgs gsvsltvrrs lmpdaylgvs gdasvgigte glrvgvsglw sridprdill
      241 dvidykgslv saqlygfypi irsreenlsi gasfsldndn stilttdfvd drlrsvsvwg
      301 rydfvdqtra vtslrgalth gvdlfgatgn srangvvkyt kveldaqrnq pladvlggal
      361 slqatahaqa algsgalfsa pecsfggrrf grgfdsgilt gdhcamgsve lhwvrsvdfp
      421 dlgapvfldf yafvdggvvw qkgevlsgep grghaaslgl glsvqftaea sgllevsrpv
      481 slsvgtpdet rilgalsfrf
//
LOCUS       WP_457661778             326 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I NDUFA9 subunit family protein [Sinorhizobium medicae].
ACCESSION   WP_457661778
VERSION     WP_457661778.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  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 326)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=34854
     Region          10..279
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(14,16..19,38..40,82..84,97,119..121,132,136,
                     155..158)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(132,136)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mtlsnlpplv tifggsgfvg rhvvralakr gyrirvavrr pdlaghlqpl gnvgqisfvq
       61 anlryrnsvd ravdgadhvi ncvgvlfeng rntfdavqdf garavaeaar atgatlthis
      121 aigadarsds syartkgrae aaileilpta vilrpsiifg pedgffnkfa emarfspvlp
      181 ligggntrfq pvyvtdvaea varsvdgkla ggtiyelggp qvlsfrecld imlktidrkr
      241 sfvslpfgia slmgsvaslv pfieppltad qvvllksdnv vsamaetegr tfagigiept
      301 mlelilptyl vryrphgqyt rtgraa
//
LOCUS       WP_457661785             518 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Sinorhizobium medicae].
ACCESSION   WP_457661785
VERSION     WP_457661785.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..518
                     /product="trypsin-like serine 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=53658
     Region          259..515
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrnlaqvlal lflagttiav aqdgggfggg ggfggggggf ggggfgrggg gegfggggge
       61 gfgggpfgae afqsldtlpi etqravevlr skepydgstv pdyidgvpft lglkfpkelp
      121 peiapdgvpi rnpsivdlen cpscvpsdps iglatfsglp dvtlpnrlqr assgagdgve
      181 ksqieqcgaa vqalrapvsp msgnmiddfy saclkeleve typqlddiak qevsaclaah
      241 ilyeqsclqh ldtivdkrvv grigmlfniv dkdnprpact atlltetliv tarhcytaea
      301 lglpggtdgt aalaftpnpi llaatnvqsm payievagev tlagehevdv vpetpqpsed
      361 vialrlktpv alesprleii wanlelgkel tligfqelal rrtllearik nvgltsgksl
      421 ieegafsafl rvdhgpmciv gdltpgqfgh ycqsfngtsg apiflgnlal pqnsgfsval
      481 vgfqsrgnas dmpdkevigp pntaaqvtsd latllglr
//
LOCUS       WP_457661783             326 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457661783
VERSION     WP_457661783.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33906
     Region          91..299
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msaapdlsrl spemaalllr vaaetgpqvd pttlppaegr slseegnrrw nvglpemaav
       61 geafveadaa igsarlrlki lvppgagsga vvfvhgggfv fcspesherc arvlalecgl
      121 pvllpdyrla penpypaglm dvvatirnaf avsapfgvaa gplllsgdsa ganlalaall
      181 heaaagrprm agallfygty agdfrtesyr nfengpgltt akmqrywrwy vgdrdvsadp
      241 lacpllasde alaalpplhl maagvdplls dsialhqrlk qlgrgealmv vpgvthgflq
      301 ntldlaaare alakagaear rmagan
//
LOCUS       WP_457661786             389 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457661786
VERSION     WP_457661786.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..389
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43449
     Region          60..348
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mplkltkrgn sdnwyirgtv rgqsvfestg tcdreiaeai riktegrlln esvhgkkali
       61 tfeeatesyi asggserfli kvspktgkvs giaahfrgml lkemtqsdld aaarilfpna
      121 spetrnrqcy tpfiavwnha asnqwaevrq wkrprkvkgt nvvklktrag tkpttydraa
      181 qfvaamspap aqlmtalfyt gmrpielftl easevnvpgr witldasktg eprgvpihef
      241 lvplfealla rggilfrthk gepypptedf ggqissaitg arnrlqkrgv aitdispyta
      301 rhtvstqlvv ngihpyvkdq ilghaaddms rrythvpqqr lldaintlpv pqlwrdqeww
      361 qdpvywsrrl irwgqasgns raqslqssn
//
LOCUS       WP_457661796             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661796
VERSION     WP_457661796.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77161
     Region          5..663
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 hdlqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvakypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghiser evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklseg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesataeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457661799             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457661799
VERSION     WP_457661799.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32109
     Region          78..292
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(85,126,163,178,180,188..191,240,265..267,269,272)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(105,112,138,204,206..210,238,242)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            163
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrnypeiasr mfgtplmlhp skgdiiaraf gprvlgspda pahvaggeem glvgeklrda
       61 tdyrgdalyk gpelvapgia lieiegslvn kgkwigkscg mtsyeaigvq vrdcierddl
      121 kavvfevdsy ggevtgafdc aeqifelsqa kptiavltdh acsagyllas pcrqlvipqt
      181 gicgsigvis mhvdmsawla keglkvtilk agehkadfnp yeaipddvlq qelaeleelr
      241 vefaatvary ragrltqksa latearvyrg qkavdaglad avarpsqvle afeaelsrta
      301 g
//
LOCUS       WP_457661817             273 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661817
VERSION     WP_457661817.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..273
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29735
     Region          3..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mekwsrfnia svvlgfgfly lpivllvifs fnelklvtvw agfstkwygq lwqnqsllda
       61 awvtirvall satcatvlgt maalalvryt rfrgrvlfsg mvyaplvmpe vitglsllll
      121 fvaigfdrgf wtitlahitf tmcfvavvvq srllsfdqsi eeaaldlgat pvrtffaitl
      181 pviapavfsg wilaftlsld dlviasfttg pgattlpmki ysqvrlgvtp einaictili
      241 gvvalgviva sivtrrreaq rekderaafa aig
//
LOCUS       WP_457661818             275 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661818
VERSION     WP_457661818.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..275
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31116
     Region          75..264
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          203..259
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mqktdvpdls tiasivgqig rptlpealde mlakvarfdl saifgfpfds rplllhdgyr
       61 qhaepaalna yldgaylfdp fytacarsfp aglwrmrela pdhffnsefy ssrevhpcis
      121 mragslveei gflipleggf navyslmrsh gapfsgdemd glkqieplvr etvrshwrdv
      181 raserqlrld dlmetafasf cedrltyqqr rivqlilrgn snyaigqils vtegtvklhr
      241 qniykrlnis sqrelfamfv erllpplple esarg
//
LOCUS       WP_457661823             347 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457661823
VERSION     WP_457661823.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..347
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35810
     Region          18..346
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtidtassks ttkdqasmqh evapqksvir rlldgpelmi fgsliiiiai ftvmaptafl
       61 sginlrnmai easmmmilav gmtyviitsg idlsvgavlv fssvasliam ratgsdapwv
      121 pvlglavala sgafwglvng lliararltp livtlasmgi alglarlmtg gvdltgvprs
      181 ivtsigigri ggipvivlia cvfasvagia lhmtrfglyt yavgsneqga rragikvdrh
      241 pisiyvfsgv caglagyltl trfssttisg hamdnlkait avvlggaslf ggigsmygta
      301 agvfipvvla sgliivglps fwqevavgiv llaavlldqy rrrtrss
//
LOCUS       WP_457661825             236 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457661825
VERSION     WP_457661825.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..236
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24629
     Region          7..234
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mpvlkpiagi lfdkdgtlld yvkswvpvny elariaakgd edlahvllra ggmdpdsghv
       61 vpdsllaagn tveiatgmvg agapftveel tslfdglfaq sahyavpvtd lasffavlha
      121 kgyrlgvass dnersireta krfgfenylh yiagydsgyg tkpepgmvlg fcaatglapd
      181 evavvgdnnh dmhmgrsagv gmtvavltgt gsrqslaaas dhcladitel etvltv
//
LOCUS       WP_457661829             227 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457661829
VERSION     WP_457661829.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 227)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..227
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24519
     Region          2..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkegpdiali gsligdpara nmltalmggq altatelaaq agvtlqtass hlakleaggl
       61 ltqrkqgrhr yyalsedevg lmleslmgfa agkgltrsrp gpkdpalrka rvcynhlagd
      121 ygvrmldsli aarqiemtdd ddlaltdagr irveslgvdy aalrksrrpi crtcldwser
      181 rphlagslge alltlfieng wakreqnsra ilftaageka flelfpr
//
LOCUS       WP_457661835             710 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin-containing oxidoreductase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457661835
VERSION     WP_457661835.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hille,R.
  TITLE     Molybdenum and tungsten in biology
  JOURNAL   Trends Biochem Sci 27 (7), 360-367 (2002)
   PUBMED   12114025
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Hille,R.
  TITLE     The Mononuclear Molybdenum Enzymes
  JOURNAL   Chem Rev 96 (7), 2757-2816 (1996)
   PUBMED   11848841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..710
                     /product="molybdopterin-containing oxidoreductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77815
     Region          1..710
                     /region_name="BisC"
                     /note="Anaerobic selenocysteine-containing dehydrogenase
                     [Energy production and conversion]; COG0243"
                     /db_xref="CDD:440013"
ORIGIN      
        1 mpyrkamnva spvrqektig hsvcphdcps acaldidlta egrigrvrga aentytagvi
       61 cakvaryser iyhpdrlmvp qrrtsakgeg rwqeitweaa ldeiaahfvk aeqkygselv
      121 wpyfyagtmg qvqrdsierl rhakrysgff gsictnmawt gvsmatgalr gpdpremaks
      181 dcvviwgtna vatqvnvmth avkarkdrga kivvidvydn ptikqadmgl vlkpgtdaal
      241 acavmhiafr dgyadrayma kfaddpagle ahlktrgpew asaitglpie eieafarlvg
      301 ttprtyfrlg ygftrqrnga vaihaaasia tvlgswkheg ggafhsnndi frldkrelvg
      361 talhdpevrm ldqsqigrvl tgdaealrhr gpvtalliqn tnpvnvapeq rlvkrgflrd
      421 dlfiavhehf mtdtaqladi vlpatmfleh ddlyrggghq hillgpkvve ppptvrtnlf
      481 vieelakrlg vadcpgfglt erqhidrlla nygigydgmk erkwldcqpn fdeahfldgf
      541 ghpdgrfrfk adwtgtpapn rppkamgpqg phgklpefpd hvdlievade rhpfrlatsp
      601 arsflnstfa etpssiqkeg rpevmihaed aaelgvaegd vvrlgngrge irlhakiggg
      661 arrgvvvaeg lwpnsahldg eginvltgad avapyggaaf hdnrvwmrra
//
LOCUS       WP_457661837             147 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Sinorhizobium medicae].
ACCESSION   WP_457661837
VERSION     WP_457661837.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..147
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15666
     Region          8..144
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtlqpvmtve elnrfldtdf pqvhtdgkvf avtdtgpgfg tmrldpnerh irpggtvsgp
       61 tlfaladvsa yialiahigp valavttsln inflrkpepe plectcrilk lgkrlavlda
      121 sikpvagpdl vahatatysi pprrdav
//
LOCUS       WP_457661850             530 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661850
VERSION     WP_457661850.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..530
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=56669
     Region          463..506
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mglygsapea pdpqetasaq tatnigtava nnvmgnvnqv tpdgnltyty ttqkwkdpis
       61 gkeydlqvpt atqslsqqqq aiknqtdaae lnmaslantq sgklndllgk piniggapag
      121 gnaaaiglpq yqqfgsgpql qtslgnygnv qssiagagni qkqvadsgqi qnqlgnagdi
      181 trsyetdfsa drqkvedalm qrlnpqmerd raaletrltn qglqpgseay nraideanrs
      241 stdarlgail sagqeqsrla glanqsatfq nsaqqqaynq llgsgqfans aqaqqyaqna
      301 nnmqmgnaaq qqqfgqnqaq lqannaaqqq kfgqglagaq fgndalqqqy qnqntatagn
      361 nalqdqsfns qqskfnmqnq qraqylnely aqrnqpinei iglmsggqvn spsfvptqsn
      421 pmptvdyagl vqqdyankmg ayqqnqagig slmgglagmf tlsdktakkd ikkvgglyey
      481 rykgegknap krigvmaqev ekvrpdavrk gadgfrrvny galfdagrkk
//
LOCUS       WP_457661839             555 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease J [Sinorhizobium medicae].
ACCESSION   WP_457661839
VERSION     WP_457661839.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..555
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60268
     Region          3..555
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 maqneelvfl plggvgeigm nlglygygrp gsrqwimvdc gvtfpgpdlp gvdlvlpdia
       61 flaeerrnlk aiiithahed hygalndlwp glnvpvyasp ftagmleakr afeksrseip
      121 itifkqgdri nvgpfsveav gvnhsipepm aliirtrlgt vvhtgdwkid lepslgpltd
      181 ekrlrqigee gvlalicdst nalregvsps erqvseslsk iiadaegrvg ittfssnvgr
      241 irsvaqaaea agrevlllgs smkrvvdvar dvglmeglrp flaedefgyi prdkvvvilt
      301 gsqgepraal akiardemrn vafsagdtiv fssrtipgne kaindikngl ieqgihiitd
      361 sealvhvsgh prrnelqqmy qwvkpqivvp vhgeaahlta haelalqsgi psvprlrnge
      421 mlrlapgpae vvdqaphgri ykdgtligdf eemgigerrk lsfaghvsvs vvldnrydfl
      481 gdpdvvpigl peyddegesm edtlydavlg avesiprakr kdlamlqeav rravrstanq
      541 vwgkkpvvtv fvtkv
//
LOCUS       WP_457661854             166 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457661854
VERSION     WP_457661854.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..166
                     /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=18568
     Region          105..162
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mslttqfwsr vpselsfplf pqggkdrcap aqflpalagp hergpmsqsa neallafvrd
       61 larrqaridi eleaqrrsdp gslqpeappm delpassrsf qlrgdrllkl revismtslg
      121 sstiyrrmka gkfpkpkrls eacvtwrese iqkwmcelpt nrgvsk
//
LOCUS       WP_457661858             441 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457661858
VERSION     WP_457661858.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..441
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..441
                     /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=47846
     Region          37..148
                     /region_name="FAD_binding_4"
                     /note="FAD binding domain; pfam01565"
                     /db_xref="CDD:426326"
ORIGIN      
        1 mrmddfesaa rsgrrprpsi spddyedatg svaamaflpv gnglslgdvc rneggtpids
       61 rklnrtltfd sgsgaircea gvslaellar aaphrfflpv tpatglvtvg gavandihgg
      121 nhhargsfgn hvrrltllrs sgerlvctpe enaelfaati gglgltglil dvelrlmkvp
      181 sphvqrhvlr fdsleqyfal aeraaeehey cvawldqlat grragrgvlf aadhadgace
      241 lpdvlkrpkl avpvsppfsl fnrltlraln eyrfrkagtg etvstedwps yfhrldavgg
      301 wgrlygrrgf cqhhsvypaa tapettarll eaarraghas vrttlqrfgd iasrgllsfa
      361 rpgftlildf anqgratvkl ldtldeivis aggavnpcqd frmsravfea sfpswkrlea
      421 lrdpaivsdf wrrtalatgt t
//
LOCUS       WP_457661860             295 aa            linear   BCT 27-JAN-2026
DEFINITION  LpxI family protein [Sinorhizobium medicae].
ACCESSION   WP_457661860
VERSION     WP_457661860.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..295
                     /product="LpxI family protein"
                     /calculated_mol_wt=31311
     Region          13..286
                     /region_name="COG3494"
                     /note="Uncharacterized conserved protein, DUF1009 family
                     [Function unknown]"
                     /db_xref="CDD:442717"
ORIGIN      
        1 msvaiyrlpq skgrlaiiag agalphhvae aarrqgenpf iialsreada dwtgfdhtvc
       61 aigdfaaish tfeaekidrv vlsgavrrrp ewrdirptlk tlakvprvfr tlmsggddav
      121 lrmvieliea sgahvigahe vvpglladvg plgrhapmde dqrdiragia aanalgaldv
      181 gqgavavggr vvalegaegt damlarvsdl rkdgrisvrr rgvlvklckp qqderadlps
      241 igpstvaeah aaglagiaie agralvlert rlveaadrsg mfvlgiernl rrere
//
LOCUS       WP_457661886             298 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457661886
VERSION     WP_457661886.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..298
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32069
     Region          61..275
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(68,109,146,161,163,171..174,223,246..247,250,252,
                     255)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(88,95,121,187,189..193,221,225)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            146
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrythilmav aseywaided kfdqivsfla lqasgekfss eelqarisrq terdvarreg
       61 avavlpfrgv lanrmslmsd isggtsyegf artfdaavsd pevkaiildv dspggvvsgv
      121 delsqrifsa rgkkpiiahv nstgasaayw titaadevil npsaevgsig vmmvhddisa
      181 alekagvkrt liaagkfkge gapfqqlsde arefrlqrae fyydkfvgri asnrgvsvsa
      241 vksgfgqgrm vtakeavaqk madgiatlee tiarfgvsaa kpsrsnfare rekramai
//
LOCUS       WP_457661905             320 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Sinorhizobium medicae].
ACCESSION   WP_457661905
VERSION     WP_457661905.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..320
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34013
     Region          1..312
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 maeitglvlp ffgliflgyl tarlvdhpge amgwlntfiv ylalpalffk lvsrtpveel
       61 tradfiltsv gttyvvfall faislflrrn tvaeatmqgf agaygnigym gpglallalg
      121 etaavpvali fcfenaahft vapammaaag gsrrkpaara lgiarriafh pfilstfagv
      181 aaaflsfepp lplqrlidyl aqaaapcalf amgvtlalrp lkripaeigy ivpaklvlhp
      241 vlmylalslg gaydpiwvqt avllaslpta tnvfvighqy gvwqerasat ilittllsva
      301 tvtgllylir sgalpadlfp
//
LOCUS       WP_457661918             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661918
VERSION     WP_457661918.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77102
     Region          5..662
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 hdlqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvakypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklseg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesaaaeq
      661 qsplvaaala ratraaqrnr
//
LOCUS       WP_457661966             408 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Streptomyces albidoflavus].
ACCESSION   WP_457661966
VERSION     WP_457661966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..408
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45657
     Region          67..396
                     /region_name="XerC"
                     /note="Site-specific recombinase XerC [Replication,
                     recombination and repair]; COG4973"
                     /db_xref="CDD:443998"
ORIGIN      
        1 mtgkrgngeg siypykngfa ayvwvtkpdg krarkyaygk trdevhdkwl nlhaeakkgp
       61 vatrhrtlav flaywldsiv kpnlapltyv syegyvrlyi apqlgakrld kltvrdvrew
      121 ltklatlcqc caqgkdakrd psrrkccavg dccetypsrr vvqgsrdalr aalshavtee
      181 eisknvaslv kvpkprrrri kpwsaaeasl fladaaardd hlfaawvlvl tlglrrgevl
      241 gltwksidfe tgelyvdhqi qragreilhr etktedsddf lplpavclka lrmrraqqlg
      301 drkaagelwq gshdlvfttk ygtpiepgnl trmfalrsrr aglrviplrn trhttgsllv
      361 vlkvhpkiaq rilrhsqiam tmdvyadaad eevreavgkl sdamggtg
//
LOCUS       WP_457661904             356 aa            linear   BCT 27-JAN-2026
DEFINITION  BMP family ABC transporter substrate-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457661904
VERSION     WP_457661904.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  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 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   3  (residues 1 to 356)
  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 356)
  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 356)
  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   6  (residues 1 to 356)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   7  (residues 1 to 356)
  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 14448206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="BMP 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:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38439
     Region          28..306
                     /region_name="PBP1_BMP-like"
                     /note="periplasmic binding component of a basic membrane
                     lipoprotein (BMP) from Brucella abortus and its close
                     homologs in other bacteria; cd19963"
                     /db_xref="CDD:380618"
     Site            order(34..35,43,117,163,191,236,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380618"
ORIGIN      
        1 mkkllvalat tvavlgiapa asaqekakic fiyvgsktdg gwtqahdigr qelkkelgdk
       61 ietqflenvp egpdaeraie rlarsgcgli fttsfgfmda tikiaakfpd vkfehatgyk
      121 tapnvatyns rfyegryiqg qiaakmsekd vagyiasfpi pevvmginaf vigaravnpd
      181 fkikvvwant wfdpgkeada akalidqgvd iitqhtdtta pmqvaaergi kafgqasdmi
      241 aagpqtqlta ivdtwgayyv krtkafldgt wstssswdgl kdgiltmapy tnmpddvkam
      301 aeeteakiks gelkpftgpl nkqdgspwlk egetaddatl lgmnfyvegv ddklpq
//
LOCUS       WP_457661900             249 aa            linear   BCT 27-JAN-2026
DEFINITION  alanyl-tRNA editing protein [Sinorhizobium medicae].
ACCESSION   WP_457661900
VERSION     WP_457661900.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..249
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA deacylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) deacylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=27485
     Region          1..241
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mtrsvtalfr edfylstcea svtailedgg ieldqtcfya tsggqpgdkg fleredgsri
       61 diidtrhgat kdiilhipae garmpdvgek lvlhidwprr yrlmrmhtac hllsvvcpfp
      121 itgaavgeee srvdfdmsel idkdqvtaal mklvhenhpv yvqwitdeel vanpaivksk
      181 nvrppmglgr vslvcigens svdsqpcggt hvsetqevga ihiakiekkg kenrrfrirf
      241 aapedrafa
//
LOCUS       WP_457661889             573 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Sinorhizobium medicae].
ACCESSION   WP_457661889
VERSION     WP_457661889.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..573
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63536
     Region          16..566
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mgyassirae wqfscpdwve rlregrslvp dlpldhaegn ravqifnklr lpdvpgqpam
       61 adaagdwfrd ivravfgsid engrrqvgrv fglvpkknsk ttggagimvt allmnkrpra
      121 eflligptqe iadtayqqav gmieadeyla krfhaiehkk tivdrlnkak lkiktfdmkv
      181 ltgtkpagvl ldelhvmssf syasrvlgqi tgglipnpes fliiittqsd eppsgvfkte
      241 ldyargvrdg rvtrggllpi lyefpeemqt spekpwqdpa nwpmvlpnlg lsitidrlle
      301 ewqeakekge eeqrrwasqh lnveiglalh tnrwtgadyw laaadksitl eyilehsdav
      361 tvgadvggld dlwglavigr hhetrhwmcw tkawcqtdvf karpeiaekl ndfakdgdlv
      421 icerttqdae eaaeiigqir dsgllpeeda igvdswgvta lvdelamyei eepqirsvpq
      481 ggklsaaffg lerklkdgtc khngsammaw cvgnarleqr attamidkks psskidplma
      541 lfnaamlmam npvalgisvy etrgileiev dsl
//
LOCUS       WP_457661967             228 aa            linear   BCT 27-JAN-2026
DEFINITION  B3/B4 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661967
VERSION     WP_457661967.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Roy,H., Ling,J., Irnov,M. and Ibba,M.
  TITLE     Post-transfer editing in vitro and in vivo by the beta subunit of
            phenylalanyl-tRNA synthetase
  JOURNAL   EMBO J 23 (23), 4639-4648 (2004)
   PUBMED   15526031
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Mosyak,L., Reshetnikova,L., Goldgur,Y., Delarue,M. and Safro,M.G.
  TITLE     Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
  JOURNAL   Nat Struct Biol 2 (7), 537-547 (1995)
   PUBMED   7664121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..228
                     /product="B3/B4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=25137
     Region          5..228
                     /region_name="B3/B4"
                     /note="B3/B4 domain (DNA/RNA-binding domain of
                     Phe-tRNA-synthetase) [General function prediction only];
                     COG3382"
                     /db_xref="CDD:442609"
ORIGIN      
        1 mldfpvidke iasiapdfra isifvdikdd argtmarsml eeacdfvrag gpvwseahlt
       61 swaeaysrfg akpnrtpcsa qalkkrvekd gripsinpvv dlynavslrf aipvggenfd
      121 ayvgkprlsv adgteafdtm mkgeavtenp skgeviwrdd vgvtcrrwnw rqgtrtrlet
      181 lggrmwfile slatmpeeal eeaanmlvgg lrqlapgcev yrhkiiaa
//
LOCUS       WP_457661968             253 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661968
VERSION     WP_457661968.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 253)
  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 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   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 253)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27887
     Region          8..253
                     /region_name="HisP"
                     /note="ABC-type histidine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4598"
                     /db_xref="CDD:443652"
ORIGIN      
        1 mhierlkpal vvndvhkcyg ahkvlkgisl saekgdvvsi igssgsgkst flrcinflei
       61 pdqgtfqing edvvfrkgrd gkchpanwrq ierlrsglgm vfqsfnlwph mtilqnviea
      121 pihvlrierk aaiekaeall akvglydkkd typaflsggq qqrasiaral cvdpavmlfd
      181 eptsaldpel vgevlkvirg laeegrtmvm vthemrfard vstrvmflhq gqveelgppt
      241 qvfgaptsar cke
//
LOCUS       WP_457661973             336 aa            linear   BCT 27-JAN-2026
DEFINITION  SIS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457661973
VERSION     WP_457661973.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35734
     Region          7..322
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 mtqfafdkqi asqadavrta lttgeipqld pkrpvifagi gtslhackva aywatelsgg
       61 rirpavveth dyalrgaiaa edqiivvshr gtkrfphhlf eraktagast iaiaghgakn
      121 pggdvvlrtc ddelssthtv syttalavla rlvgklvgge aavkfaaald tvpaaiaetl
      181 tkpapinvlp rlinkepifl tgygideltv leaalkikeg aylwaeamsi elalhgtpav
      241 fearhaaiva vpeeddggrt eafltllndl niesvtlgag dfdlsfakvd ylvrpfvsii
      301 plqrlvaela rrrgsnpdtt rgdvepyksa idrisl
//
LOCUS       WP_457661974             254 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661974
VERSION     WP_457661974.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..254
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26787
     Region          55..229
                     /region_name="PBP2_peptides_like"
                     /note="Peptide-binding protein and related homologs; type
                     2 periplasmic binding protein fold; cd13530"
                     /db_xref="CDD:270248"
ORIGIN      
        1 mkisrkvqrg fihatlvsaa lalgsisasa dtigkcevtg tkgestfkaa qagqltvvtn
       61 lpspgwwngd taetiadgye ycfaaniahr agfdkvnvvn vpfdaivaar vkdfdlalaq
      121 isitdarkkv vdfsipyfss digvvvkkgt tvnsesikqm rvgvkqattg aqfitdkvkp
      181 asvkvfpdsa glfaalmagq idvavhdtsi vlgqaaqskg klevagqyle lppkdrtcsg
      241 lrlradelar rlis
//
LOCUS       WP_457661975             311 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457661975
VERSION     WP_457661975.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..311
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32357
     Region          1..291
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mllgivaglt tcalwgltfi apraivpfta wdltiarygi fglaclllma drrfrpvgfa
       61 hsrlligrsl ggigyvgyfi saafavqlag aavppvvigt mpvflaiian irerstpwna
      121 lalplaliai gvaivnaati stadgadtps illgvlastm alviwiaygl anaavmrsad
      181 apdglqwtgl qgigaaigsl fllplasfdl lntasgaeaa rfvawallmg lagswfatwc
      241 wvvasrrlpl alaaqlivae tifglaygfm fesrfpspae migavlqfag vcsaiavfsr
      301 prtltaiqea t
//
LOCUS       WP_457661977             227 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Sinorhizobium medicae].
ACCESSION   WP_457661977
VERSION     WP_457661977.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Lutkenhaus,J.
  TITLE     The ParA/MinD family puts things in their place
  JOURNAL   Trends Microbiol 20 (9), 411-418 (2012)
   PUBMED   22672910
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Szardenings,F., Guymer,D. and Gerdes,K.
  TITLE     ParA ATPases can move and position DNA and subcellular structures
  JOURNAL   Curr Opin Microbiol 14 (6), 712-718 (2011)
   PUBMED   21963112
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Surtees,J.A. and Funnell,B.E.
  TITLE     Plasmid and chromosome traffic control: how ParA and ParB drive
            partition
  JOURNAL   Curr Top Dev Biol 56, 145-180 (2003)
   PUBMED   14584729
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..227
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=24684
     Region          1..167
                     /region_name="ParAB_family"
                     /note="partition proteins ParAB family; cd02042"
                     /db_xref="CDD:349760"
     Site            order(8..11,19,40,42,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349760"
     Site            order(9..16,38,40,88,91,112,114,116,148)
                     /site_type="active"
                     /db_xref="CDD:349760"
ORIGIN      
        1 mivtianpkg gtgkttlvra lsgtaahagn dvflidadsr antirwvtms kqmnvwpdrl
       61 eaescldpnr iykmalehhf egklvfvdie gttnenlfag lycadivlip lqttqddvva
      121 gmqlalnhip vveedqkrkl pamivinqhd lvtgrakahe plreilresg valssqpiar
      181 rasyqsigaa gtlqtvaksd qkaiaemetl lgelltlyrs takeall
//
LOCUS       WP_457661980             382 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457661980
VERSION     WP_457661980.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Goodwin,T.J. and Poulter,R.T.
  TITLE     A new group of tyrosine recombinase-encoding retrotransposons
  JOURNAL   Mol Biol Evol 21 (4), 746-759 (2004)
   PUBMED   14963102
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..382
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=41483
     Region          182..379
                     /region_name="INT_Cre_C"
                     /note="C-terminal catalytic domain of Cre recombinase
                     (also called integrase); cd00799"
                     /db_xref="CDD:271180"
     Site            order(198,212..214,286..288,303,305,331..333,365)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271180"
     Site            order(207..208,339,343)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271180"
     Site            order(212,249,333,336,365)
                     /site_type="active"
                     /db_xref="CDD:271180"
ORIGIN      
        1 mtsiveqnse nhapepsaps lsttlsgnhs vfqrpdaasp plpahlqdlg erardyveaa
       61 ssantrraya adwkhfsawc rrqnlsplpp dpavvglyit acavgsavvt gsgsaigtat
      121 rngraesvst ierrlsaigw nyaqrgkkld rkdraiatvl agirnkhaap prqkeaimpe
      181 eliamlqtle sgtlrgmrdr amlligfagg lrrseitgld lgrdqtedsl gwieifdkga
      241 lvtlrgktgw reveigrgst datcpvaale twisfarlak gplfrrvtgk gkdvgperln
      301 dqevarlvkk aalaagvrpd lteterlekf sghslragla ssaevderyv qkqlghasae
      361 mtrkyqrrrd rfrvnltrgs gl
//
LOCUS       WP_457661986             298 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457661986
VERSION     WP_457661986.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..298
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32359
     Region          1..276
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msnavlsiqk leagygskav vrdfsldvaa gefvsllgps gsgkssvlra iagflpamgg
       61 rillegrdit getperrnvg ivfqnyalfp tmtafeniaf alrvakrpqa evekrvrdma
      121 tlsgideqlt rnpaemsggq qqrvaiaral vtgsrvllfd eplsnldakv rvtmrreikr
      181 mqrevgftai fvthdqedal tmsdrivvln ggraeqighg rtlyrqpatp ficqfigasn
      241 elsppvarrl lgakgegrsf vrledvliae ngggggachc qpyrvswlaq prlhdrrg
//
LOCUS       WP_457662012             206 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662012
VERSION     WP_457662012.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..206
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=22288
     Region          107..153
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mkpahrtefl tlpvaagvpa avaqvianra dgeritvsns nssspvntnt ntptntnnpt
       61 ntntnnptnt ntnnptntnt ntsmptntnt ntntndnape pdaneasdrr lkrdiarlae
      121 langlgvyrf rylwsdevfv gvmaqevlev mpeavvigsd gymrvnytkl giemlsleqw
      181 tsrlvagvps sralrmdhrs lalasr
//
LOCUS       WP_457662016             942 aa            linear   BCT 27-JAN-2026
DEFINITION  Rne/Rng family ribonuclease [Sinorhizobium medicae].
ACCESSION   WP_457662016
VERSION     WP_457662016.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 942)
  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 942)
  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 942)
  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..942
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..942
                     /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=104328
     Region          3..647
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 maekmlidas hseetrvvvv rgnrieefdf esehkkqirg niylakvtrv epslqaafvd
       61 yggnrhgfla faeihpdyyq ipladrqall kaeaeearre ddiepmetsa erksasstds
      121 vaevvaqaea aeaageaaea qaaaekpkak pkrtrrakpk aseetaasqe seapeggpse
      181 dgesdksema aivetnsise dvdarrqrdd dddddnhdge keiiesvgae dameevaerq
      241 frkprkqyri qevikrrqil lvqvakeerg nkgaalttyl slagrysvlm pntargggis
      301 rkitnlqdrk rlkeiargld vpqgmgvilr taganrtkve ikrdfeylmr lwenvrtltl
      361 nstapclvye egslikrsir dlynkdisei vvsgeegyke akgfmkmlmp shakvvqpyr
      421 dvhpifsrsg ieaqldrmlq pqvtlksggy iiinqtealv sidvnsgrst rehsiedtal
      481 qtnleaaeev arqlrlrdla glividfidm eekrnnrsve kklkdclknd rariqvgris
      541 hfgllemsrq rirasvlest mqtcphcngt ghirsqssva lhvlrgieeh llkntthdis
      601 vrttpdialy llnqkrssit dyeqrfgvsi fieadahvga qhfaidrgep venpvridqi
      661 lqfepepeee eeeeevliee elddeeaeet aaehqdqqkg qpddqggrkr krrrrrrgkg
      721 agqgadavsa esadaaedea gdeaaaddae deldaadsln gdseqkrkrr rrgkrggrrn
      781 rqeelagseg etgataetve epgeesvdst aaeipavsaa eeapadvaaa aavegvaeep
      841 kpakprrsrk kttkteepav nadevaekvv eaqpepaepa pqiveeavee avedlegakp
      901 arsnrdlsai askpvvtssk geseeeptkp kkggwwqrrg ff
//
LOCUS       WP_457662019             710 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin-containing oxidoreductase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662019
VERSION     WP_457662019.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hille,R.
  TITLE     Molybdenum and tungsten in biology
  JOURNAL   Trends Biochem Sci 27 (7), 360-367 (2002)
   PUBMED   12114025
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Hille,R.
  TITLE     The Mononuclear Molybdenum Enzymes
  JOURNAL   Chem Rev 96 (7), 2757-2816 (1996)
   PUBMED   11848841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..710
                     /product="molybdopterin-containing oxidoreductase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77815
     Region          1..710
                     /region_name="BisC"
                     /note="Anaerobic selenocysteine-containing dehydrogenase
                     [Energy production and conversion]; COG0243"
                     /db_xref="CDD:440013"
ORIGIN      
        1 mpyrkamnva spvrqektig hsvcphdcps acaldidlta egrigrvrga aentytagvi
       61 cakvaryser iyhpdrlmvp qrrtsakgeg rwqeitweaa ldeiaahfvk aeqkygsesv
      121 wpyfyagtmg qvqrdsierl rhakrysgff gsictnmawt gvsmatgalr gpdpremaks
      181 dcvviwgtna vatqvnvmth avkarkdrga kivvidvydn ptikqadmgl vlkpgtdaal
      241 acavmhiafr dgyadrayma kfaddpagle ahlktrgpew asaitglpie eieafarlvg
      301 ttprtyfrlg ygftrqrnga vaihaaasia tvlgswkheg ggafhsnndi frldkrelvg
      361 talhdpevrm ldqsqigrvl tgdaealrhr gpvtalliqn tnpvnvapeq rlvkrgflrd
      421 dlfiavhehf mtdtaqladi vlpatmfleh ddlyrggghq hillgpkvve ppptvrtnlf
      481 vieelakrlg vadcpgfglt erqhidrlla nygigydgmk erkwldcqpn fdeahfldgf
      541 ghpdgrfrfk adwtgtpapn rppkamgpqg phgklpefpd hvdlievade rhpfrlatsp
      601 arsflnstfa etpssiqkeg rpevmiyaed aaelgvaegd vvrlgngrge irlhakiggg
      661 arrgvvvaeg lwpnsahldg eginvltgad avapyggaaf hdnrvwmrra
//
LOCUS       WP_457662022             736 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662022
VERSION     WP_457662022.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..736
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=81108
     Region          50..668
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mktvqeprke dnrpkrrhif lridswidst vwsagfrlae wwedttiffr rfrvrgwkka
       61 lfevlgegmt lgaagsvlml alalpafeet tgnwraqsdf avtfldrygn eighrgiihe
      121 dsvpidelpd hlikavlate drrffdhwgi dflglaramt enaraggvvq ggstltqqla
      181 knlflsnert ierkikeafl avwlesnlsk keilrlyldr aymgggtfga aaaaqfyfgk
      241 aitdvnlaes amlaglfkap aryaphvnlp aararanevl snlvqgglmt egqviaarlt
      301 pasvvdraqv kapdffldwa feevqriaap faqhslivrt tidmglqqaa eeavelglrq
      361 ygetykvkqg alvmvehgga vramvggrdy gesqfnratr alrqpgssfk vytyaaamek
      421 gmkpetvvvd apitwrgwsp qnyarkyagr vtlmnalars intvpvrlak dklgteiiae
      481 takrmgietp irtdktmplg tsevtvldqa tayavfpagg fqsrrhgisq ilnydgdily
      541 dfgrdatpar rvlseeaass mnrmltqipv igtarraald ngivtggktg ttqayrdawf
      601 vgftgdytta vwfgnddyts tdemtggslp amtfkrlmdy aehgiehrai pgieapsepa
      661 kqqpaetakk ddnalpplvr prslsadvtr llkkiggtfe kaqplkarer pggkvavlet
      721 psqgshirpl rnttnn
//
LOCUS       WP_457662026             405 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662026
VERSION     WP_457662026.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..405
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42660
     Region          3..257
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mtrfrlalat iavlffgtaq avagsaslvv dartgrvlsa enpdtlnhpa sltkmmtlym
       61 tfealhrgql awktpvpmsa taarkpptkl gvrpgetitv qeavygmivr sandaaaama
      121 erlggteegf armmnakarq lsmnrtffvn asglpaseqv ttardmarla valmrhypre
      181 yrlfsvqsfa frgrvirghn nlmyryqgmd giktgytras gynlvsavae gnrrligvvl
      241 ggrsarsrde kmaalldqhl grvsspgrpm iesanaprla dvaslpgvsl syagtkpave
      301 alaapaaaap ttvpaavaaa sapsfsngwr iqlstaptae garkmlveaq saggaallgg
      361 tphseaagka yrvgfvgfvs reaaaiacdv lkkrsydcvl lpdeg
//
LOCUS       WP_457662030             211 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase I [Sinorhizobium medicae].
ACCESSION   WP_457662030
VERSION     WP_457662030.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..211
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=23784
     Region          10..201
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 maakglitgd dgldrcawhg nledyrryhd eewgrpvadd hrlfekicle gfqsglswlt
       61 ilrkreafra afagfafdrv aefgeedver cladagivrh rgkivstinn arrakelrse
      121 fgslaayfws hepesserpa vvdhaalian pttpasiris kdlkkrgwtf vgpttvyafm
      181 qamglvndhi eacfcrapie elrrrftrpa a
//
LOCUS       WP_457662035             529 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Sinorhizobium medicae].
ACCESSION   WP_457662035
VERSION     WP_457662035.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..529
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59257
     Region          17..496
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mtfsifddee ipdpfgyger avrflralrh pkstlpglsf dlspwqeriv rkiygprhad
       61 grrivrtvai mlprgnrkts lgaalallht igpeaipgge cmaaasdrsq ariayeealn
      121 iircdsrmdg rlhlvdsknr iknpkvgsff eaisadakta hghtpvfalv delhawpkrd
      181 lweaiksglv kvpgsllvvi stagrgqenv awefyeyark vargevndpt wlpilfeter
      241 dadwhdeqvw yaanpglayg ypdieglrql areaaeipae rdafrqlnln vwldhsaspf
      301 vdmlvydega ypvdpvnleg epcwigvdls snrdltavva cwrdgddgya vypwffcpad
      361 nlraradrdg vpyptwaeqe fiiptpgnvv dyravedhir elcarfevre iafdphmarn
      421 imnnllednl pavemrqgwv tmapaikeme raiigrrfrh gghpvlrwnf dniaievdka
      481 gniafhkgks kdridgavaa amavarcaag dsglsvydsa dwsdemayf
//
LOCUS       WP_457662038             137 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF3168 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662038
VERSION     WP_457662038.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10568396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..137
                     /product="DUF3168 domain-containing protein"
                     /calculated_mol_wt=14963
     Region          11..129
                     /region_name="DUF3168"
                     /note="Protein of unknown function (DUF3168); pfam11367"
                     /db_xref="CDD:431845"
ORIGIN      
        1 msvensvqvg irsrliatag vivlvpaghi ldrsqrpiid psiilgegla vededslard
       61 rwrvfstlhi wkkedslagv raiawairma irparlelgv dfhcadcrvs svryvrdpdg
      121 vtshgiltie tlaetve
//
LOCUS       WP_457662045             428 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662045
VERSION     WP_457662045.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..428
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47020
     Region          31..395
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mswqspispg yswyeatipe rpafpvmpgs rradvaiigg gytglqaayn larsgtdvtl
       61 idscrfgdga sgrnggqfgt gqrlwaeeae emlgreraqr lfdmaenakr yvlgfaeeha
      121 idiefmpgql svshkksler dyrnhveamt erfgyphlsf mdreetvsrl gsshyhfgir
      181 dvgtghihpm klvvgltrqa araganlyeq tkalriekkg glvviettsg titadralia
      241 cnayignlep vtaahvmpir sfigatsvla dhpevlpgge lvddsrfvvr yfrkskdgrl
      301 lfggreayta dnprdisahi rrqiceiypa ladievthaw ggsvgitmpr qpfcrdvmpg
      361 itsiggysgh gvmlanycgk lyadlalgka teldllkelk ipafpggtrf rsallflalt
      421 wyalrdrm
//
LOCUS       WP_457662048             519 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease family protein [Sinorhizobium medicae].
ACCESSION   WP_457662048
VERSION     WP_457662048.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12545973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..519
                     /product="HNH endonuclease family protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58323
     Region          44..105
                     /region_name="DUF262"
                     /note="Protein of unknown function DUF262; pfam03235"
                     /db_xref="CDD:427209"
     Region          <474..515
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 matrvnldam ipradfated ntdytidlft nfpianleng npirtllrkp dfqretnhwd
       61 prqiatfias fldselipsl ilwksssyif vidgghrlsa lrawieddyg dgpisqkfyn
      121 ndisddarra arrarqlveq kvgrfsllks ivnnashgde lqtrragrlf trslnlqwvq
      181 gsasvaetsf fkinsqgtpl ddteemllrn rrkpiaigar ailrsgtghk ywsafepglq
      241 kqiensaeel fkllfepevd qpvktldlpl ggsvspvdal sllieflsia nstqtetkni
      301 sayeddatge etasilkrsi evtrritgnd kgslglhpav yfynergkhs rflflgmvtl
      361 mtskirnndk effrrftlar rkleaflien kslvgillqn mskrtrvskm rdlveflvak
      421 fsadqevrie qaiehlgarg riydittaaq nasfseeaks amyvkravas aiscnlcggl
      481 ldpqksvsyd hivrvreggk gdvengdlth pycnqslkn
//
LOCUS       WP_457662067             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457662067
VERSION     WP_457662067.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32191
     Region          78..292
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(85,126,163,178,180,188..191,240,265..267,269,272)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(105,112,138,204,206..210,238,242)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            163
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrnypeiasr mfgtplmlhp skgdiiaraf gprvlgspda pshvaggeem glvgeklrda
       61 tdywgdalyk gpdliapgia lieiegslvn kgkwigkscg mtsyegisaq vqdcierddi
      121 kavvfevdsy ggevtgafdc aeqifelsql kptiavftdh acsagyllas pcrqlvipqt
      181 gicgsigvis mhvdmsawla keglkvtilk agehkadfnp yeaipddvlq qelaeleelr
      241 vefaatvary ragrltqqsa latearvyrg qkavdaglad avarpsqvle afeaelsrta
      301 g
//
LOCUS       WP_457662070             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662070
VERSION     WP_457662070.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77144
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaqice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempaia klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra eehgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledr lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457662079             270 aa            linear   BCT 27-JAN-2026
DEFINITION  sterol desaturase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662079
VERSION     WP_457662079.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..270
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30064
     Region          94..255
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlyfgfsepv wrlgafaaaf aalaalellh prlerpeltr tlkarrwitn lsilvlssll
       61 lrvafptaat gvaiwaqayg ygllpalgla psaagliafv aldfaiwleh vvfhkvpilw
      121 rihrvhhadp gvdvttalrf hpveillsmv wksavivllg apalavllfe ivlnagamfn
      181 hanlrlpkaa dqllrrfivt pdmhrihhsv ekgetdsnyg fnlsvwdrmf styiahpsrg
      241 ddaietglkv ygrsepmkll wslvlpfrrr
//
LOCUS       WP_457662078             385 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457662078
VERSION     WP_457662078.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..385
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42892
     Region          60..348
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mplklvqrkg sdfyyirgtv rgqslfestg trdrevaeai riktesrlln esvhgkkali
       61 tfeeaaesyi asggserfli kvspstgkvs givahfrgkl lkdltqsdld aaarilfpaa
      121 saetrnrqcy tpfiavwnha agnqwaevrq wkrprkakgt nivklkvrag tkptsydraa
      181 qfvaamspap aqlmtalfyt gmrpiemfll easdvnmpgr witldasktg eprgipihef
      241 lvplfealva rggvlfrshk gdpyppteef ggqissaitg arnrlkkrgv sivdiapyta
      301 rhtvstqlvi ngihpyikdq ilghaadgms rhythvpqqp lidaintlpv pqlwrdqeww
      361 sdpvywsrrl vkwgdpakrr vqkvg
//
LOCUS       WP_457662084             216 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457662084
VERSION     WP_457662084.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..216
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23446
     Region          5..215
                     /region_name="Nnt1"
                     /note="Protein N-terminal and lysine N-methylase,
                     NNT1/EFM7 family [Posttranslational modification, protein
                     turnover, chaperones]; COG3897"
                     /db_xref="CDD:443104"
ORIGIN      
        1 mrtdpesfvr antgilmpph vpeirlhlas eahelwlkte eeleqiglpp pfwafawagg
       61 qglarfildh petvrgrrvv dfasglvaia akmagadevv aadidpwcet aarlnaelng
      121 vslafaaadi vgseraadvy lagdvfydks faalllpwfd aleragavvl vgdpgraycp
      181 rermtplaty evpvtraled cevkrttvwr fgqaas
//
LOCUS       WP_457662087             588 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662087
VERSION     WP_457662087.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 588)
  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   2  (residues 1 to 588)
  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   3  (residues 1 to 588)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   4  (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 11573933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..588
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64872
     Region          6..168
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(10,12..17,52,54..56,59,109..111,115..116,119..120,
                     157)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(12,56)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(17,28,31..32,35,40,52..53,104,110..113,116,157)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          181..314
                     /region_name="TolBN"
                     /note="TolB amino-terminal domain (function unknown)
                     [Signal transduction mechanisms]; COG5616"
                     /db_xref="CDD:444347"
     Region          351..576
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          414..442
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(415,418..419,422..423,425,449,452..453,456..457,
                     459..460,483,487..488,491..492,495)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          447..477
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          482..506
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meqrlaavla admagysrlm eadeagtlar lrthrielid paieknkghl ikttgdgmlv
       61 efqsvtdavk caveiqsrmk rrnadvaqdr riefriginl gdiifedddi fgdgvniaar
      121 ieqladvggi cvtaavamqv adrlevsied lgekmlknis rpihlfrval egtlpvfpet
      181 adarrsvskp aivvlpfdnm sgdpdqeffa dgltediite lsrrhelfvi srnssfvykn
      241 qpvnvrevae klgaqylveg svrkigdrvr vtvqlidavn dahiwadkyd rrlddifaiq
      301 devtsaiaat lpgrveaaqr dllartkpan maayecalaa kvlhhrstva dnrqaralid
      361 ravaldpgya hahawracil gqawvhgwcd dkdaawaeiv seldralald dndadvhril
      421 aavnvnnnal ttaryhqera lslnpnydlv vvqqgellmw lgrpeegiew ickamqlnph
      481 hperfwshlg kacfsarqyg esieafmhls vmdhaqhafv aacygclgdd iaaqahmakv
      541 ralapefdid aflatqhyvq esdlqrlrng lvkagagsgs vaseiaaq
//
LOCUS       WP_457662090             251 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662090
VERSION     WP_457662090.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..251
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27958
     Region          12..249
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mptsidtasl eitlsgvhkw ygqyhalddi nlsiaprekv vicgpsgsgk stlircvnrl
       61 eahqqgrivv ggvevgeder kvdairrevg mvfqqfnlfp hltilencil apmwvkripr
      121 aqateiamdy inrvripeqa nkypgqlsgg qqqrvaiara lcmnpkvmlf deptsaldpe
      181 mvkevldtmv slanegmtmv cvthemgfar qvadrvifmd qgriveegep deffahpktd
      241 raslflsqll h
//
LOCUS       WP_457662092             259 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662092
VERSION     WP_457662092.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..259
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28634
     Region          1..>177
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mpdkpliait gassgigeav arafsraghp llliarrldr lealglpnal lkkadvrdra
       61 alaaavgeae arfgpvdmmf anagiarlgd iarqapeewd emidintkga mnsvhavlsg
      121 migrkhgtlv mmssiagrkv ypdhtvycgt kffvhavses lreylaphdv rvivvsprhy
      181 rygsagsceg rddarqlqge qsgdrrrhfr rrrrrshprr lsaaaasdrp gnrhhadpte
      241 iltqrsrrrr dgrperrme
//
LOCUS       WP_457662093             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662093
VERSION     WP_457662093.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38532
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matveyqrig ksfgavtimr dvsfriedhe fvvllgpsgc gkttllrmta gleavsqgdl
       61 miggkrvndv hprdrsiamv fqnyalyptm kvydniafsl evakvppaei ksrvewaaat
      121 lnltpylgry pkelsggqrq rvamgramvr eaevflfdep lsnldaklra hmrteirqlh
      181 nrlktttiyv thdqieamtm adkivvmrag kieqigspdd vydrpaskyv adfigsssin
      241 flpgtvvvdn ggpavdtttg rvsvepspal ksgqkvvlgl rptdvvvdag gplaakailt
      301 erlghdaqlf cegpegsfva vvdkaarfse gaevrfaipp skvhvfdaet eiri
//
LOCUS       WP_457662101             506 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662101
VERSION     WP_457662101.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..506
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55933
     Region          16..500
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 malittrylg vtmgaplfsq ldlaispgdr igivaangrg kstllrciag aldattgdvi
       61 rarglrighv eqsippglse irfrdavrqa lpdeqaqted wrvdvaldsl dvpqalrqlp
      121 igrlsggwqg lallarvfvt dpdallldep tnhldlekil rletwllnlp rdmpvliash
      181 drafldattn rtlflraeqs yafslpysra rnaldeidas derryrkdmk tvqqlrrqaa
      241 klnniginsg sdlltvktkq irqraerled aarpafhers sgairlanrg thakvlitld
      301 dtpvetpqgt llfrtgrqwi rhgdrivllg rngagkshlv hlirtaiaep enpeatikat
      361 pslmlgysdq alaelagdet plttitrrfe igdqrartll vgaglgielq trpvgvlsgg
      421 qksrlamlvl rltnpnfyll deptnhldie gqealetelt aqkascllvs hdrsfaravg
      481 nrfwlienrr llevgdpddf fkglre
//
LOCUS       WP_457662100             199 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662100
VERSION     WP_457662100.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..199
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=22260
     Region          <121..183
                     /region_name="djlA"
                     /note="co-chaperone DjlA; PRK09430"
                     /db_xref="CDD:236512"
     Region          155..>198
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mcvmkldsky fdrirtrprg qarvepsapv cqwdgcdeta vhrapvgrna egeyfmfcfe
       61 hvkaynkgyn yfsglsdtei aryqkeavtg hrptwtvgvn knarnaptqs qtrsgtagaq
      121 armrdpfgff neararqarh eprmrklktl eakafetlgl aasatsadik aaykelvkkh
      181 hpdanggdrg sedrfravi
//
LOCUS       WP_457662102             312 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662102
VERSION     WP_457662102.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 312)
  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   4  (residues 1 to 312)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..312
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33888
     Region          25..>312
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mqpflgctai aivatavsig pgtriamaqd atpsdedaat tlapiiitge kfgrdqfttf
       61 tsvevftgge lhdlvrptln dalnsspnir afmsgrgnsd ivirglsseg vtapsrsnpv
      121 isvvvddaeq gveatrrgtr glwdveqvev lrgpqstlqg rnalagsvii ktkdptytpe
      181 asiegligtd eyksgafavs apivedelaf risgqifrrd ndidyvdpsi sdvgeeefee
      241 irgkllwepa eipglrglft vsrthdkpaw alvsgpdffa rrfddttaer rdtyvnryia
      301 dltyeinedw ki
//
LOCUS       WP_457662103             384 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor [Sinorhizobium medicae].
ACCESSION   WP_457662103
VERSION     WP_457662103.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..384
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42506
     Region          <3..366
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 meitspqtpt lqqfqlirdd treggdfsqd irltygsaes qfsgvfglfa grstfdldsn
       61 irvvadpvtp filpfqqlqa knksettaly adtryefvdr wtllaggrlv hdkvsanytg
      121 slldastfgy vpltennsvs nteflpkigl afeldenqnl aatiskgyrp gyseliigtt
      181 dintvrpesl wayelayrsk wledrlqvng nvfyydytnq qvpiefdprf paqtislnaa
      241 eshsygaeie vrygfdsgle lfsglglmks kfdkgdfkgk efpeapslta sfggvykhes
      301 gffaggdvsf tdgyyskgdv knvraldsft vvnanigyek dnlkitafar nlfdeeylts
      361 issngnlati gdgrsfgvrv natf
//
LOCUS       WP_457662104             194 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662104
VERSION     WP_457662104.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..194
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20067
     Region          <12..192
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mahrtefltv piligiglss lagaganfis tfgnpqavqr amvwlsgsiy nstwdkirtl
       61 atwltigiag saliaremdl lilgdetara rgqpvelira vmfvlcavls gaavaaaglv
      121 afvgliaphi aralvghshg lmlpvtalag gllvvgadla artlftpapl pvglmtailg
      181 apffaylmwr kkna
//
LOCUS       WP_457662105             193 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662105
VERSION     WP_457662105.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..193
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20046
     Region          18..>147
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mrsvlilsgf svvililala igdhhvsiaq ilavltdspa adaqsiqiir dirlprvilg
       61 flvgaslata gmiaqsvlrn plaepgligv nagaalaavi vivrfevppt hllswlafag
      121 altmslaiya lswnsgsssl riilmgvsgi lcggpvssve eplakddgel clcldpfprr
      181 pfpllgrvvk nei
//
LOCUS       WP_457662107             296 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662107
VERSION     WP_457662107.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32517
     Region          9..288
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 maefnsrrle idalralwai rhhggitraa eamglsqsav shkikrlets ldcdllsrrs
       61 ggpvftsage dlldyagril glhdeallsl sktqlagria lgltedttct dlarilgrfr
      121 rlhphvsvhi kvrmslvlra mlergeldaa ivqvfshevr ptdvvlfren lhwvkhpdlc
      181 lpqngpipfl sfddecfyrk waldvgqdgg tiletvfeca saagivaavk salgvallse
      241 rhlraemqiv tdrlpappal vyvvrrarka ripaldtlia eiehetsrhg gliltg
//
LOCUS       WP_457662108             290 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662108
VERSION     WP_457662108.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..290
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31469
     Region          9..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matlhtrsaa rlmiapsvll llawmivpla mtlyfsllry nllmpgmeef agltnytyfl
       61 tdpaffqaif ntlaivlgvl fitvvggtal allldqpmfg qgivrilvia pflimptvaa
      121 lvwknmfmnp vnglfawlak llglqpfdfl anapllsiil ivawqwlpfa tlilltalqs
      181 ldeeqkeaaq mdgagavsrf iylvlphlsr aitvviliqt ifllsvfaei lvttnggpgt
      241 qstnltflvy aqallqfdvg gasaggiiav ilanivtffl mrmigktlea
//
LOCUS       WP_457662110             157 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662110
VERSION     WP_457662110.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..157
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17798
     Region          22..97
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msraelaagk kreaekhael ielgkrirfl rkeilgyhrq tdfadrlgvt rgavgnweig
       61 vgmkrdhlmm iakefniswv wlaegkgtpi akpsidarme llppeeyetl yehfqamidn
      121 rlralgrkeq ggdkasglnl hevtkageys krrkptl
//
LOCUS       WP_457662123             379 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin family protein [Sinorhizobium medicae].
ACCESSION   WP_457662123
VERSION     WP_457662123.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..379
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42382
     Region          9..151
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mylsmesqap aikaqnwigg eplanfqpgt vyvleffstt cphcvapmln liqlqekyrd
       61 rglevvgvaa eeraatadda rahldpwlte nvpklnfrvg idctgemekl wkeasfsfgv
      121 pysfvvdrds riafighptd ldsvlpqvld gtwrssdqak avereriakg rddaqlnpil
      181 dkftaaiemk dwmtalpaie eaialmpddi dlrtthvetl lykmrdmqag ltvlrrlvrd
      241 aidrndqewl lnaldqlfnp deydythfps aerlamgkel sehilaltgl kdevkasyyr
      301 avapyyyesg nkaraeelle lalkladglp rlnpswlegv lqtlatykge kvchgapcva
      361 pkenvpngat rqaekknpa
//
LOCUS       WP_457662127             562 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Sinorhizobium medicae].
ACCESSION   WP_457662127
VERSION     WP_457662127.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..562
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61662
     Region          4..553
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mtgwnfacpd weqrllagks lipdlpldea eaaravdifn klrlpdvpgq pllrdaagew
       61 qrdivraifg smvgdtrmvq elfcmvpkkn nkttggagvs ltallmnsrp haefiyvgpt
      121 hevsdqafqq avgmieaddy lskrfhiahh tktildrrnk arlkvktfdm kvvtgskpvf
      181 vlldelhlms smaaaariiv qirngmpape svlvmittqs deppagafkt elryargvrd
      241 grikesrmlp ilyefpeemq rsgvwrdpav wplvnpnlgr sitleklkss yqaavekgde
      301 dlrlwasqrl nveigvalhd drwlgadywe saadpsvsln sliaesdaiv fgidgggldd
      361 lfglaaigrc krnrsewrlw shawahkdvl srrkeiadrl hdfqrdgdlt icetptqdfe
      421 dvadiiarvr dtgllpekag vgldpvgvan mvdalavrgi tgdqvvaipq gyrlsgviqg
      481 terklkdgtl whagaplmaw cvgnakveqr gnavlitkqv agkakidplv aafdaamlms
      541 knpeavgagm dsyfrslaga aa
//
LOCUS       WP_457662140             276 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 108 protein [Sinorhizobium medicae].
ACCESSION   WP_457662140
VERSION     WP_457662140.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..276
                     /product="glycoside hydrolase family 108 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /calculated_mol_wt=29296
     Region          5..165
                     /region_name="ZliS"
                     /note="Lysozyme family protein [General function
                     prediction only]; COG3926"
                     /db_xref="CDD:443130"
ORIGIN      
        1 matssfkaal arvlvheggy vnhprdpgga tnqgiiqrty dayrrskklq prsvqkltap
       61 erdaiyrrqy wdaikgdklp agvdyvvfdg avnsgpkqsi kwlqralgsa yrgqidgvig
      121 latfaaleat edhdalidri cdrrmvylra ldtwsyfagg wtrrvqnvra agkamaderk
      181 devaavhiag aetkarieda rkapskapad aatgggigag giagtlqslq eqltplsvag
      241 dwitttvvvl altggvlaig gdrlsllgqa ergglg
//
LOCUS       WP_457662142             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662142
VERSION     WP_457662142.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77151
     Region          5..663
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehrre wmvkpengak wvakypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvid
      421 hragshlada kehsghisep evraaldrml qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesataeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457662158             288 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662158
VERSION     WP_457662158.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31139
     Region          27..257
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mrsatntkrn lvtaalvapa aawlavflvl pfmamlvfaf gerapeggyq aaftfkqfan
       61 lptraaafwn tlllapagal lclliaypva yylavkadpr yrlilvslvv vpfwtsllvr
      121 tyawmyilgs rgipnllsmi diedvrmlnt pgavllgivy gylplmimpi yvslekldrr
      181 lleasadlgg kpvstffgvt lplslpgvmt gvalvtilll geylipqllg ggkvfflgna
      241 lvdlflqsrn wpfgsaiavt lvavvvvvlm vamrvawkva gtrqvdlv
//
LOCUS       WP_457662159             309 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662159
VERSION     WP_457662159.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..309
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34530
     Region          20..301
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maftlslntn plvnrfaead dlidtiadki righvqlthe fvnpgwpast inkalrqfrt
       61 alartgvkit sgmtgpygrl nhfghpdsdv rryyvdwfkt fadisaelga sgmgtqfaif
      121 tlrdyddpar reeliaiaid cwrevaqhak aaglsylfwe pmsvgrefgh tiaecraldq
      181 rlatagfsip mkmmvdidhg dvtspnaadv dpyawaqafp kqspiihikq ssmnkgghwp
      241 ftaaynkdgg itperlldav rrgggtdnei clelsfrere ptdrnvvemi resvefweph
      301 idtgfnnpk
//
LOCUS       WP_457662160             377 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457662160
VERSION     WP_457662160.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 377)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..377
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41116
     Region          18..367
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 manypaitst erqtrisrlr atlsernvgg lllgsteslr yytglewhas erflgalitg
       61 sdliyiapaf elsrvetlsr epgeirawqe eessaalvas llppeatlav ddslplfayn
      121 alvgeigarr lidggplira qrrlksaaei eiiqfamnlt levhrrahkf ikpgisasev
      181 rryiddqhrl lgapggssfc ivsfgdatal phgaegeqvy kpgdvvlvdt gcriggyhsd
      241 ltrtymiddp tpefariwai ereaqlavfe aahigatcgs ldsaardvlv rnglgpdykl
      301 pglphraghg igleiheepy ivrnnhfals egmcfsvepm ivvpeafgvr ledhiymskd
      361 gpvwftapae gptepfa
//
LOCUS       WP_457662139             739 aa            linear   BCT 27-JAN-2026
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662139
VERSION     WP_457662139.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Jenkins,J., Mayans,O. and Pickersgill,R.
  TITLE     Structure and evolution of parallel beta-helix proteins
  JOURNAL   J Struct Biol 122 (1-2), 236-246 (1998)
   PUBMED   9724625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..739
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=79227
     Region          39..>302
                     /region_name="NosD"
                     /note="Nitrous oxide reductase accessory protein NosD,
                     contains tandem CASH domains [Inorganic ion transport and
                     metabolism]; COG3420"
                     /db_xref="CDD:442646"
ORIGIN      
        1 minlgsaeia dlrvgasqva rvylgediiw qpnfdslpaa iyfsaagndd tgagtqaapf
       61 ktlkmanava ragktlyfrg gdtftgtlla rpgciynsyg tgkatinsgn aeavlldnad
      121 saqvrrliaq gsgttvngth girainshae giqiddvvid gcevrgygrn gifatvanyp
      181 sgltglqitn nivedctqnd erghtggiiv aaeeadfwgl athpashrdv vvtgntvrrc
      241 kgkrdapnhv gsgiivaqte gglvennlae dcgenstnqa gpvgiwawda igvvirkntv
      301 lrqrsarsdg ggfdldggck dcvleynfsm gctgpgiiif sfddtaypan klldysgnia
      361 rynlsvrdgq tvrsefgmfi gtmrpvasdf qnirvynnti vvdtvgafsp tclsiqtfgg
      421 vdfshatgvi anniflqkga gllcdvrtta mqihgncfhs vqgtamrsfa fdwetvdqwi
      481 sasgnkeflh gthtifvdnp qlvndsgtnp edfrpaddsp lygvgmdina efgiarpted
      541 flgnalpatq vfftpgamep dtplpnllts pnvlntgwel ndvdlisgll gmfggtsaqn
      601 irvdaegaav gqlrtftagt ekifrrggfv kpaadviaaa ignrqpdind ywwtwfdiva
      661 gelddadawg ayldsvprfr mqkrpngfwl imhemkvpst wtqdkfwaqp saphplrggi
      721 neglgrglih dgffefrvg
//
LOCUS       WP_457662162             301 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662162
VERSION     WP_457662162.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33485
     Region          18..284
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mkslfrqrsg vfskittvpf lllvigvggy swaqvivmaf srlrieagqf vwspagfdnf
       61 rdilandval ysvavttifv iatvwlsvll glllallvqr skrfnrlaqv vllwpamvap
      121 vvvsliwlli lspnigvlnk lldtfmlptq dwlgmevgai vaivdvwhwt pvaflmlyta
      181 lcavdeeave aarcdganew qviryvkipm lmpailgtif iravmgvkaf demylltagg
      241 pnnattlvsl hirdvffdql nygygsafsv livllmslii alvltvrtlr hsrffmrevq
      301 e
//
LOCUS       WP_457662164             362 aa            linear   BCT 27-JAN-2026
DEFINITION  AbrB family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662164
VERSION     WP_457662164.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Sullivan,D.M., Bobay,B.G., Kojetin,D.J., Thompson,R.J., Rance,M.,
            Strauch,M.A. and Cavanagh,J.
  TITLE     Insights into the nature of DNA binding of AbrB-like transcription
            factors
  JOURNAL   Structure 16 (11), 1702-1713 (2008)
   PUBMED   19000822
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Daley,D.O., Rapp,M., Granseth,E., Melen,K., Drew,D. and von
            Heijne,G.
  TITLE     Global topology analysis of the Escherichia coli inner membrane
            proteome
  JOURNAL   Science 308 (5726), 1321-1323 (2005)
   PUBMED   15919996
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..362
                     /product="AbrB family transcriptional regulator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0010468 - regulation of gene expression
                     [Evidence IEA]"
                     /calculated_mol_wt=37603
     Region          19..362
                     /region_name="AbrB"
                     /note="Uncharacterized membrane protein AbrB, regulator of
                     aidB expression [General function prediction only];
                     COG3180"
                     /db_xref="CDD:442413"
ORIGIN      
        1 mkpeqpstpt lprngglgrl splwqwglla llsavfagil emigipagll mgpmiagavi
       61 gmnggtirlp rqlffcvqvi lammiaasms pdllatfsgh wplflgivls vigvstlcgw
      121 titrmgilpg ttaiwgssag aastmllmad aygadarlva fmqylrvvfv agtativshl
      181 wvsgaeapta vrwfapiagv pffmtlaigi iggflgkmlr vpagaflvpf aigsalsitg
      241 tltielpqwl lalsfamlgw niglgftrsi laharrallp tivsilvlis fsgllallli
      301 eaagidplta ylatspggld siaviaassn vdlpfvmalq tarllvitli gpalarfvad
      361 ra
//
LOCUS       WP_457662166             678 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662166
VERSION     WP_457662166.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 678)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..678
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70897
     Region          126..639
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mrvsdeiarg rrkatnapav dtdaevrsgs rmlerplrvl akarcwqwlr lasggakddg
       61 segergparv rlpkeltral rgfdlppppy adevrvpetr sakagprrrs syfrfrgkrm
      121 sgvgepawll afvcgavfll svlplihlgw aglkglegge aasvlleaat faalrntlva
      181 aaggmvislv vgalfafvva ltdirgklal sfafmlpmmi ppqvtalawv emsgpsspll
      241 ktlglapplg spqplyslag ialllgvqha plvflaikag lathprdgve aarlsgaspw
      301 rvfrdivlpl acpaliagga iafisgignf gipailgipa sietlptlif akfasfgsst
      361 fgeiavlsti iasisaggll lqqralkgrd yrligltgar aaftlgrlri avetllwgtl
      421 alvlvaplla lvasslvpay gvpltlhtvs lqaygevlfr qtvtltalkn svflasaaav
      481 gllvialpag yllaarrgrv anllailiei pyalpgivla vafilafaap lpvigvsiyg
      541 tiwiilaayl ssffavslkp vmsaflqmdp sleeaarlag agflrrmrdv llplvapaag
      601 asvilvflia aneltvsall wsagtqtlgv aifnlddsgs snlasalsvl vvavviglma
      661 tlevlakylp egvlpwrn
//
LOCUS       WP_457662170             564 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457662170
VERSION     WP_457662170.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 564)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..564
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=62378
     Region          1..475
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mqiakleien frgiregvvr fsphtvlvgs nncgkttvve alallfgrdr mvrqltehdf
       61 ygsnpqpvdr irlvatvidf dgddpaqhmd wfrddrgivk wwnpvdgavm partdpswkl
      121 acqvtfaarf hrpslevetl ryfhdddvvg dvfadesata fsarlirdig fffvpaartw
      181 drtvsfgsel frrvvaageg qpsesvlser drlrmpearl eqderlapiv nrlnqelrgf
      241 frtaptlhlr vtatdsdgll esvvshyahe gadlplparr hgsgllslqh lllllqfghm
      301 raeanegfwm aleepelhvp palqrrlvhr iqalsrqtfv sthspmvaal adpkgvavlr
      361 ndggvltaip lltstlpadt pnsvrklfqv nrvetiaavm hefvlvpegr tdyewlgllv
      421 ravdlhqswa aadecrfdaf vgvipthdga vvttveamap lhprvvamvd gdlegvgyaa
      481 tlvaagspns gvilrwadgq mledtigwii dadsnaclpa iqinqpattv aelvarlknd
      541 nraaggaeeg hvhlrnhrgr drrq
//
LOCUS       WP_457662183             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662183
VERSION     WP_457662183.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77115
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykerv dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wlsrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslggayrwg vpywtdeewd aiadrlgrle apqqgdledr lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457662203             336 aa            linear   BCT 27-JAN-2026
DEFINITION  S8/S53 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457662203
VERSION     WP_457662203.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="S8/S53 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35339
     Region          99..305
                     /region_name="Peptidases_S8_S53"
                     /note="Peptidase domain in the S8 and S53 families;
                     cd00306"
                     /db_xref="CDD:173787"
     Site            order(123,164,273)
                     /site_type="active"
                     /db_xref="CDD:173787"
     Site            order(123,273)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173787"
ORIGIN      
        1 mvkgkavhfv deeqsdrrff mhktqwfpvg fvaglvalaa pgfagdlgsa vsgkgttgsp
       61 aaessssgcp qnadgtfcwm spdigqawas gfigsgvsin vsddftgqpi dgdlgrgtqr
      121 qrhgdwvaei agmvapgani fkydyleess ivlqdglnvi nasygmwepl sqhpreqaiv
      181 gaawagtaiv tksadnhsre vgqphegdfd eltigligap saifvgaleh ngtpenkarr
      241 epysnyagsn pevqnhfltv gvereeigqr gtsfaapvva gyaailgskf tsatpiqitn
      301 qlldtartdt lvnynpaayg rgeaslsral apvsih
//
LOCUS       WP_457662208             307 aa            linear   BCT 27-JAN-2026
DEFINITION  SEL1-like repeat protein [Sinorhizobium medicae].
ACCESSION   WP_457662208
VERSION     WP_457662208.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 307)
  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 307)
  AUTHORS   Mittl,P.R. and Schneider-Brachert,W.
  TITLE     Sel1-like repeat proteins in signal transduction
  JOURNAL   Cell Signal 19 (1), 20-31 (2007)
   PUBMED   16870393
REFERENCE   5  (residues 1 to 307)
  AUTHORS   D'Andrea,L.D. and Regan,L.
  TITLE     TPR proteins: the versatile helix
  JOURNAL   Trends Biochem Sci 28 (12), 655-662 (2003)
   PUBMED   14659697
REFERENCE   6  (residues 1 to 307)
  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 12218275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="SEL1-like repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33287
     Region          7..36
                     /region_name="SEL1"
                     /note="Sel1-like repeats; smart00671"
                     /db_xref="CDD:214772"
     Region          26..56
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          54..293
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          63..92
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          99..128
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          138..164
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          171..200
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          207..236
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          243..272
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mlvaltvkaq vnlgglyfdg egvaqdyaea arwfrkaaed gaaalaelnl gvmyehgrgv
       61 apdpaeaarw ygraaehgda qaqhrlglmy fkgegvkrdh vqaarwyraa aaqgnpsaqf
      121 hlgsmylqgq gvpkepseaf rlfrgagglg henaqynlgl mylngigvqk dldesvrwfr
      181 aaaeqksalg qynlalmyan gtgvaknsee aarltslaah qglamaqhnl giayisgagv
      241 ekdfaaavhw fqkaaqqgha raqfnlammy argegvarnd alafewmqka anqlpearqy
      301 ldrtrke
//
LOCUS       WP_457662209             617 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662209
VERSION     WP_457662209.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 617)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 617)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 617)
  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 617)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..617
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68185
     Region          21..604
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mfgwfesrln pypteeptlp pkglfafcwh ytkpaapwlf imslctmlia igevalfqfl
       61 gnivdwlssa dretflsaeg grlawmaali liglpglval dsfvmhqvll gnypmiarwq
      121 mhryllrqsm tffanefagr vatkvmqtsl avretvmkil dvfvyvvsyf atmlivvaaa
      181 dwrlvmplgv wlviyivivt yfvprlqkis keqadarsmm tgrivdsytn igtvklfsha
      241 greetyarsg mdeflgtvhr qmrrvtlfhi fvyanncval fsvgalgiyl wltsgisvga
      301 iavaiglamr vngmsqwimw evstlfenig tvydgmgmmt kahdivdkpn aatlradkga
      361 irfqdvrfhy gkakgvidql sldirpgeki glvgrsgagk ttlmnlllrf ydlesgairi
      421 dgvdistvtq dslrsqigvv tqdtsllhrs irdniayghp qasdadiiaa akkanawdfi
      481 qalednmgrq gldaqvgerg vklsggqrqr iaiarvflkd apilildeat saldseveaa
      541 iqenlfalma gktviaiahr lstltemdrl vileagrive tgshaelvar rgiyadlwsr
      601 qsggfiadev ekeaaae
//
LOCUS       WP_457662210             398 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662210
VERSION     WP_457662210.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..398
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41898
     Region          224..378
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(259,302)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(264,267..268,272,276,298,300..303)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(294,322)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mggaisllav nfviaqifva aflviavksr rgraaawcaa gfaiaslaai ceavlpftpv
       61 pkffavgafa svlagfcllr fglglfygvp akpaalaafl ivsvvvdlli ydlprgtlqh
      121 affyqmpffl iqawtaaaim rsprrsyadr ilvgllvlna lhflgkvyaa iapgagstas
      181 dylqspfali sqalgaaliv gtgvailgvm vkdivdaara sseidslsgl wnrrgfierv
      241 apwllsrnak spgaliltdl drfkgvndty ghhtgdevir qfarvlldli psraaaarlg
      301 geefavflpg vdladarvva qgmraaiast piadlpetat itasfgvaai apgkslemal
      361 qradkalyva kaagrnrvec aeptarvvtp vvsqwmrq
//
LOCUS       WP_457662211             285 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457662211
VERSION     WP_457662211.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..285
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31482
     Region          75..179
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mdhlqtsgsh hrakskseiq atvrrlapfh haidlpfgls tfvpelsrqt rertrlqtfl
       61 dhawgsilta cggslkgkrv ldiacncggf svhaansgad yvfgididah yveqasfvgd
      121 alglsnvefq qldlldldps thgkfdlvlc lgilyhlenp vlsmkrisav tgdvlvvdtt
      181 lmkvpiinpv ldrwplwhmr kvsgttsdat nistsrwrpd efcqfspnsp avrnlleycg
      241 fteiarlkak aknlekryys grratfiaqr rrssqgdasp tltaa
//
LOCUS       WP_457662218             160 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457662218
VERSION     WP_457662218.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 160)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..160
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /calculated_mol_wt=17895
     Region          26..154
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
ORIGIN      
        1 mkkterylar laphastltk ggaahqigai ccrtneigav evllittras grwtipkgwp
       61 iknlkphqta ereaweeagv agkakkrahg yftylktldd grktasivev frlkvdelhq
      121 kfpergerqv arlspveaar rvqepelkgl lmrmlkesrs
//
LOCUS       WP_457662219             633 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Sinorhizobium medicae].
ACCESSION   WP_457662219
VERSION     WP_457662219.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 medicae"
                     /db_xref="taxon:110321"
     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=68767
     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 mtigaigvvy gdigtsplya frealrpfgp dgveraevvg
       61 lislmlwtlt iivtfkyvlf llradndgeg gtlsllallm kkapryttlm fmagilgaal
      121 figdamitpa lsvlsavegl klvtpafhdy vlpisvgimv llfavqsrgt gavsiffgpi
      181 tliwflvlga agvahigddl ailaafnpvn avtflwnagf vgfivlgavf ltvtgaealy
      241 adlghfgrgp iqaawfavvf palalnylgq galvlshpea vsdpfflmfp nwallpvvll
      301 ataatiiasq avitgafslv rqainlgflp rfeicftset qtgqiylpfv nnallagviv
      361 lmfmfgsses lataygisvt gamvvttvla fefarhqwgw stltatavll pllvlelffl
      421 ganlfkihdg gyvpiliagt lmttmwtwrk gvsllrekta rqdiplsqfm amverkseha
      481 pvqvpgtaif ltatpdttpa vllhnikhnh vlhqhnvilt iktarvpyvp ekdrytitkl
      541 sdrfsllelr fgfmddqnvs ralarcrkeg frfeimstsf ylgrrkliad pqsglpqwqd
      601 klfiamadsa idpteyfhlp pnrvvelgeq vvi
//
LOCUS       WP_457662221              88 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662221
VERSION     WP_457662221.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9802
     Region          3..>47
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mdlrawrten gltmseaatl lsiesartyq ryetgenrpd aplverirsv sgglvmaedl
       61 hrqrlewlks nkpetvasli dmvaeaae
//
LOCUS       WP_457662224             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662224
VERSION     WP_457662224.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77099
     Region          5..662
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykerv dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evrtaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklgeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagqsaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457662228              81 aa            linear   BCT 27-JAN-2026
DEFINITION  TFIIB-type zinc ribbon-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662228
VERSION     WP_457662228.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Elsby,L.M. and Roberts,S.G.
  TITLE     Interaction of the TFIIB zinc ribbon with RNA polymerase II
  JOURNAL   Biochem Soc Trans 36 (Pt 4), 595-598 (2008)
   PUBMED   18631123
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Hahn,S. and Roberts,S.
  TITLE     The zinc ribbon domains of the general transcription factors TFIIB
            and Brf: conserved functional surfaces but different roles in
            transcription initiation
  JOURNAL   Genes Dev 14 (6), 719-730 (2000)
   PUBMED   10733531
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..81
                     /product="TFIIB-type zinc ribbon-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9690
     Region          <1..40
                     /region_name="COG3809"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-finger domain [General function prediction only]"
                     /db_xref="CDD:443022"
ORIGIN      
        1 mserqgieid ycpkcrgvwl drgeldkiie rssaeesqpr fvermqrdqh reepkyrddd
       61 rkygsqrpqk kksllgeifd f
//
LOCUS       WP_457662236             384 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662236
VERSION     WP_457662236.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..384
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41575
     Region          3..371
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrmkwlaavg flaaivsgqa vaqtpafdtk akqiylvdae tgtvlfsrde dapvppasla
       61 klmamkvvfe aldkgeltpd tnflvsehaw rtggapsgts tmfaaiksri rvadliqgat
      121 vqlandacii laegmagsep afaermtkra reiglpvatf knatglphpg ntitmrelva
      181 larhlyeahp nyyplysqpe fewnkilqrn knpliaakig vdglatgfae gfgfsvaasm
      241 qrgerrvyla msgleseker ieesrrvldw amtafakrri fsdgetigea svyggadsrv
      301 alvaggpvdv llpvknserl tarivykwpl napvaagqqv gvvklwngdk llrevpveta
      361 ravdpgtlts raldalqell ffwl
//
LOCUS       WP_457662238             542 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662238
VERSION     WP_457662238.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..542
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57969
     Region          22..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdqnkpdlkr henpapthhe vsddfdfivc gagssgsvia arlaqcgsar vllleaggdd
       61 vaesvrdpaq wplnlgtsrd wgfvgepape lygrrlplsm gkglgggssi nvmvwarghm
      121 edwnyfaaea gdeawgyesv lgyyrriedw rgtpdtvrrg aggpvyvaqp rspqpiaeal
      181 lnaasaigip vfdtpngelm esgggasiae lrirdgkres vfgsyvrplm srpnltvltd
      241 alvtriifdg iratgvdvlv ngqrcaftar cetvlslgai ntpkvlmqsg igprdelkah
      301 gisvvqhlpg vgrnhqdhla fgctwayrkp egiggggcea klywksdsrl sqpdilqcql
      361 efavpspvet gletpahgwt mfsglaqpks rgrlrlsgpn tndpiliepn slsepedvaa
      421 alaavelcre lgnsdaftpl vaceavpgtr dragmidfir ksavtywhqs ctakmgrdsm
      481 svvnnelkvy gveslriada simprittgn tmapcvvige ragdlirkth glanssgvap
      541 fa
//
LOCUS       WP_457662239             278 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA adenine methylase [Sinorhizobium medicae].
ACCESSION   WP_457662239
VERSION     WP_457662239.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Lobner-Olesen,A., Skovgaard,O. and Marinus,M.G.
  TITLE     Dam methylation: coordinating cellular processes
  JOURNAL   Curr Opin Microbiol 8 (2), 154-160 (2005)
   PUBMED   15802246
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Cheng,X.
  TITLE     Structure and function of DNA methyltransferases
  JOURNAL   Annu Rev Biophys Biomol Struct 24, 293-318 (1995)
   PUBMED   7663118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..278
                     /product="DNA adenine methylase"
                     /EC_number="2.1.1.72"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009007 - site-specific
                     DNA-methyltransferase (adenine-specific) activity
                     [Evidence IEA]"
                     /GO_process="GO:0032775 - obsolete DNA methylation on
                     adenine [Evidence IEA]"
                     /calculated_mol_wt=31280
     Region          12..266
                     /region_name="Dam"
                     /note="DNA-adenine methylase [Replication, recombination
                     and repair]; COG0338"
                     /db_xref="CDD:440107"
ORIGIN      
        1 mqeifqftav rpvsppaayl ggkkqlaari asmleqiphs lyadpfvgmg gvflrrslip
       61 ktevindrsg dvitlfrilq rhypqfmevm kfqltsrref erlvatgpst ltdleraarf
      121 lylqrlafgg kitgrsfgvd ttgparfnig rlgilleevh erlsgvvien ldwrefidry
      181 drpgalfyld ppyfgnegdy gkdvftrnrf qemarllgti kgrflislnd rpevreifsa
      241 fpiarvdlty tiaggggkdv gevlimdgke pavenlpi
//
LOCUS       WP_457662246             113 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Sinorhizobium medicae].
ACCESSION   WP_457662246
VERSION     WP_457662246.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..113
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12412
     Region          12..108
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mnttipnehp taivkvdisn fpeevlksae pvivtfwarw cppcellqpi feqiatelag
       61 kvkivelsdn envelaaqyg vrsfprlamf kggavadiyv egslrswish ama
//
LOCUS       WP_457662247             393 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662247
VERSION     WP_457662247.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43406
     Region          24..135
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(42,45)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mrscrwshgp palkvrdwvr geplasfqpg klyilefcgt tcdgcdraml nlielqesyk
       61 dsgvevvava aheraasaee vrskleawla kfpelnfpfg lddtgamdtl wmepsssivi
      121 prvfvidrdg slafighprd lhevlpkild gtwrtsarak ateseriagd epkarkhall
      181 qpirgklraa ceigdwktal aaveegiald pdnynlratq vdllldkicd metglavlwq
      241 fvreaidrgg ahwlvtammq ifhpvvgcqs lpaaerfamg kelsehilal dfaqcnqpas
      301 lvfpevaryy heignkdrav elielalksl dgpdpdmhgl kkdlkpyllq tlanykgeev
      361 cygdvcvvpr tntssgatpk aetknlderg ale
//
LOCUS       WP_457662248             120 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Sinorhizobium medicae].
ACCESSION   WP_457662248
VERSION     WP_457662248.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..120
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12736
     Region          12..95
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mntttpnehp saivkvdtsn fseevlqsde pvtvdfwkng cqpcdmiapf leqiatelag
       61 kvkvvmlnge espelaeqyg vrgyptlalf kggevavaai dfgtgsfras isnalaslrt
//
LOCUS       WP_457662252             269 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662252
VERSION     WP_457662252.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..269
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29193
     Region          7..254
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 migiepalcs vtfrkmpade ivalavearl aavewagdah vspgdlpaar avarrcenag
       61 lktsygsyia pptddfaafk saletavalg asniriwagt rerdssnysa eerrhaaeai
      121 rqmgaeaarh gvtvsleyhp qsltdetlsa qslieavghp nvylywqprp glplkealte
      181 iaqvgehish vhvfawdrcr nrfalataad ywrtvltalp qsrwrgrrfa mlefvagddp
      241 aafladagtl rqvlrvelsl rtsgdadgd
//
LOCUS       WP_457662254             200 aa            linear   BCT 27-JAN-2026
DEFINITION  BMP family lipoprotein [Sinorhizobium medicae].
ACCESSION   WP_457662254
VERSION     WP_457662254.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 200)
  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 200)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 200)
  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 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   5  (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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..200
                     /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=22009
     Region          25..>147
                     /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 mntafkrila gpvvaaavac gsgaaqaepl kiaavsgyfs qgfgisivng lerakkdlgv
       61 elkivdtgnr aldyeeqfnn lakggqydli fvmgwelvda lqksnktypd qrfifidgvl
      121 dsptmtyidf veeegsflag alagmltsge srrlrqfvgs glprwprhsr hqklhvgnga
      181 grrqgrirrh gerrlrrylr
//
LOCUS       WP_457662255             160 aa            linear   BCT 27-JAN-2026
DEFINITION  BMP family lipoprotein [Sinorhizobium medicae].
ACCESSION   WP_457662255
VERSION     WP_457662255.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 160)
  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 160)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 160)
  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 160)
  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 160)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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..160
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..160
                     /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=16207
     Region          <1..157
                     /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 msgmeqgvak vasdvtvngv fagtfddpak gselamtlyg qgvdiiyqaa gptgegvlqa
       61 akaarkyaig vdidqcgtap gailasmlkr advavydlik geaegnkikp gavafgvkag
      121 gvelkicdev kdkvpaeiva kleelrqgva dgsvavklnq
//
LOCUS       WP_457662258             230 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662258
VERSION     WP_457662258.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..230
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25352
     Region          14..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprvkkspdv rtneliecaq rlffeqgyen ttvndvirea nvskgafyhy fvskeallea
       61 vasrmahqsl kelqalfedp tldaagqlna lfagsrrlkv emapqlkntf nalfkpeniv
      121 lyhridaavs avtlpyltgl lerghkegsl dapdpeatal mllnlrlgva ktmhralqqt
      181 eagdldgaar ildgwmrtyg laverllkip egaieitepg farafleatv
//
LOCUS       WP_457662260             400 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter outer membrane beta-barrel domain-containing
            protein [Sinorhizobium medicae].
ACCESSION   WP_457662260
VERSION     WP_457662260.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510333
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..400
                     /product="autotransporter outer membrane beta-barrel
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43964
     Region          285..>397
                     /region_name="Autotransporter"
                     /note="Autotransporter beta-domain; pfam03797"
                     /db_xref="CDD:461054"
ORIGIN      
        1 maylgntrga arsvwlsgts agsfgleaaq gnqmvdtwsk skrglhlsls pvvsngnggt
       61 hklldlsggk pclldtqnqv rdfippdftw pqgrpdigpi rffdfdlpeg rpdtgpirvf
      121 pdfdrpagrp dtgpirvfpg fdrpdgrpdt epvrvfpgfd rpderpdndl prippdrpdg
      181 rpdndlprvf pgfdppspsp nptavrggrv vgartaqnci dprsvgsdqr rdvpicpefv
      241 aeeaatqgag qsrgvpltpg rdlpapslwn fwsdirftdi sderydrdsd tfartldmgl
      301 drritddlvv gmsfslqdss thafhdsldi dsdgfsfgpy aayrlskhwa idasltygry
      361 nndvelsvls gkydserfag eislngqykf dpttsvrkhp
//
LOCUS       WP_457662261             319 aa            linear   BCT 27-JAN-2026
DEFINITION  formylglycine-generating enzyme family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662261
VERSION     WP_457662261.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Appel,M.J., Meier,K.K., Lafrance-Vanasse,J., Lim,H., Tsai,C.L.,
            Hedman,B., Hodgson,K.O., Tainer,J.A., Solomon,E.I. and
            Bertozzi,C.R.
  TITLE     Formylglycine-generating enzyme binds substrate directly at a
            mononuclear Cu(I) center to initiate O2 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (12), 5370-5375 (2019)
   PUBMED   30824597
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Knop,M., Dang,T.Q., Jeschke,G. and Seebeck,F.P.
  TITLE     Copper is a Cofactor of the Formylglycine-Generating Enzyme
  JOURNAL   Chembiochem 18 (2), 161-165 (2017)
   PUBMED   27862795
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bojarova,P. and Williams,S.J.
  TITLE     Sulfotransferases, sulfatases and formylglycine-generating enzymes:
            a sulfation fascination
  JOURNAL   Curr Opin Chem Biol 12 (5), 573-581 (2008)
   PUBMED   18625336
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510263
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..319
                     /product="formylglycine-generating enzyme family protein"
                     /EC_number="1.8.3.-"
                     /GO_function="GO:0016670 - oxidoreductase activity, acting
                     on a sulfur group of donors, oxygen as acceptor [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35391
     Region          13..316
                     /region_name="FGE-sulfatase"
                     /note="Sulfatase-modifying factor enzyme 1; pfam03781"
                     /db_xref="CDD:397722"
ORIGIN      
        1 mkaslnsvve lepaaemvwv pgatfmmgsn dhypeeapah pvtvdgfwid eapvtnrqfl
       61 efvnatghvt faekkpraed ypgappsnlr agslvftppk rplqgndisq wwiftlganw
      121 rhplgrkssi gaildhpvvh iayddakaya ewagkelpte aewelaargd ldeaefawgd
      181 elvpdgkhma ntwqgkfpie namedgfart spvrfyppng yglydmignv wewttdywsv
      241 rhpeaaakpc cipsnprnad veasvdpaag vkvprrvlkg gshlcapnyc rryrpaarha
      301 qeidtttshv gfrcirrvs
//
LOCUS       WP_457662262             456 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Sinorhizobium medicae].
ACCESSION   WP_457662262
VERSION     WP_457662262.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..456
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47950
     Region          <88..123
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 mtiaaprlyr llavlfcwls tqgpalsadp laraalqsqg tlyagqqilv dvdvlvpnyf
       61 lqspqfpaid ipgaivtldd gralnlneti dgtpysgirr tyiivpqaag dftlppvpit
      121 fgyaavppqa trgevtfppl rftvrsapgt agdspgivaa kvsvsqeldq dpaqlkagdt
      181 mvrtvtvrae glrammipep dftapqgvrl yrqdpslsee tdrngqsiag lrkdvasylf
      241 qdagnyvlpa vtvswfdpas aktqsatapa vsvtvsaaaa lspalappap epqrdafdwl
      301 hlaliggdra shrllalgcr qrivpagslv arapleraav gagffpasga gvqkrprrrd
      361 rararrlvaq sgsdaartla walrgcrdqa glpglaenal rfsasipavr srlasarpee
      421 gsgslvdagn gsarpqagla spqpdyavtr rmkadl
//
LOCUS       WP_457662263             526 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662263
VERSION     WP_457662263.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 526)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..526
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55994
     Region          21..523
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mqstiiaeqk mpsveaqggg tpflevrnle krfggvralk gvsftiergr tyhlmgengc
       61 gkstlikiis gaqpadggel aingkktegl taigalaagi etvyqdlsll pnlsveenva
      121 ltqqlvasng rlarrldlkv lretsiralk evglptepaf lstpveelpi atrqliaiar
      181 aiasdaglvi mdepttaltr revdnlirvv hglhakgvsv lfvthkldec kaiggqaiim
      241 rdglkvaecd vstqskselg fwmtgkklde tryrvdahgd etllsveqlg gsgfdnvsfa
      301 vakgeifgit glldsgrnel alslagvepa rrgsvlmggk aadlsspasa iaagigyvpe
      361 drlseglflg ksirenivma vldrlrgafg lldsrraral aqktvddlqv atpdidnpvt
      421 slsggnqqrv ligrwltiep sllilhgptv gvdvgskdti friiqrlagd gmsviiisdd
      481 lpellqncdr vmvmrkgrva dvftaeglee dviyksmmae agqgvq
//
LOCUS       WP_457662265             837 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662265
VERSION     WP_457662265.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 837)
  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 837)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..837
                     /product="TRAP transporter permease"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89074
     Region          3..693
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
     Region          645..822
                     /region_name="DUF3394"
                     /note="Domain of unknown function (DUF3394); pfam11874"
                     /db_xref="CDD:432151"
ORIGIN      
        1 mtglillcta vawslfqlwy asplpfvfgf gilndteara ihlgfalflt flaypalrss
       61 prdrvpladw vlaalgafag aylfifygdl agrpgqpstl dlvtgtigil llleatrral
      121 glpmvivagv fifytfagqy mpdviqhrga slvkfinhqw lttegvfgia lgvstsfvfl
      181 fvlfgtllek agagnwmmqi siallghlrg gpakvavvss alngvvsgss vsnvvsggif
      241 tiplmkrtgl sgvkagaiea sasrngqimp pvmgaaaflm veyvgipyse ivkhallpav
      301 fsyiallymv hlesvkldmq pipqrptpar erwirmglgl tgsvlavcll yygilgiraa
      361 fganapllla iggaalyiat iwyssrypdl elddpnapil elprawdvtr tgldflipia
      421 vllwclmveq lspglsafwa tvtilaivat rkplmaifrk edfassvgaa awdlvdglal
      481 garnmigiav atatagivvg titltglglm mtelvefisg gnvimmlili aaislvlgmg
      541 ipttanyilv atlmapvvve lgsqaglaip liavhlfvfy fgimaditpp vglasfaaaa
      601 iskedpiatg fqgalyslrt ailpfvfifn pailligvdt wahtiwvaai slaaillfsa
      661 atmnwfvtks rlwesavlll acfslfrpdw wvnqisppye elpaseflrt vqeapakari
      721 nfvvqgidlm gddvrktvnv plgepgeplq rlraigltvt pagdslmisn vafgsyakri
      781 gldvgydvva vlkkadqpst aipvsialil tagiaglqfa rkradrsgas lrgtark
//
LOCUS       WP_457662273             343 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457662273
VERSION     WP_457662273.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 343)
  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   2  (residues 1 to 343)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..343
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37038
     Region          4..337
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msdstpatie dvariaevsi atvsraihtp ekvakstrlk vnqaiaitgy ttnamarslr
       61 lgrsnmilvv apdigdpnfs silvglenea rshgygvlig htqndaqrav eylkflnsnq
      121 aaglilftgi lpfghetiaa rlppsvgife pvfnggipyv gvddeegark vvdlllaegh
      181 rkiafignsr trlaykrrra gydaglnsag vpaelrlvqe gdgtlesgra averlfvrdt
      241 lptafmcvnd qtalgvmigl kargydiprd fsvtgfddvp qatfmtpalt tirqprtlig
      301 khamalllel lsnglpaeme illrpdlvvr nsvstpsprw rer
//
LOCUS       WP_457662279             758 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Sinorhizobium medicae].
ACCESSION   WP_457662279
VERSION     WP_457662279.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..758
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81500
     Region          1..755
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtenaqrrtt sggdqfigka vdrvdgprkv tgtapyayei aegpppaygy ilgaaiakgr
       61 ilkidaelae rapgvlyvmt hlnaprqqef gpavtpavre vftrarpvlr gdhvhfydqp
      121 vglvvaetfe aaraaaalik iryqetagdf gleehlaaay apkrtnagfe tdsavgdfet
      181 afaeaevrid vsyrtpyqhh npmephatla iwqgddvtih tsaqtlsnfr aglaatlgrp
      241 vervrvvsry igggfgskli vhadsvfaal aarilkrpvk itltrqqmfa naghraemlq
      301 qvrfgaradg rlialghdvw satarveefc eqtavfarsl yaasnrltrh rlvpvdlnrg
      361 ewmrspgeap gmlalecamd elaehldldp ielrirnepd qdperrvpfs trnlvacmqe
      421 garrfdwgrr spepgrlreg rklvgigmaa airpnyigaa aawvridaeg qvtarldmtd
      481 igtgtytilt qiaadtlgvp laavaielgd srfpltagsg gswgaasagt allracealk
      541 ekilaaarvh gapvrnaadv smaagavrfg nraedlkdvl rrvapeglda rgsveagagt
      601 eayqafsqhs ygahfaevsv dcdtgeirtr rllavidagr ilntktarsq ilggmtwglg
      661 aalmektvld grygrfvnhd laeyhipvng dvpdldvvfl eenddkanpl gakglgelgv
      721 cgagaaiana vynatgvrvr efpltldkll pgltafvl
//
LOCUS       WP_457662280             232 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457662280
VERSION     WP_457662280.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bondos,S.E., Swint-Kruse,L. and Matthews,K.S.
  TITLE     Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox
            Proteins
  JOURNAL   J Biol Chem 290 (41), 24669-24677 (2015)
   PUBMED   26342073
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Ravcheev,D.A., Khoroshkin,M.S., Laikova,O.N., Tsoy,O.V.,
            Sernova,N.V., Petrova,S.A., Rakhmaninova,A.B., Novichkov,P.S.,
            Gelfand,M.S. and Rodionov,D.A.
  TITLE     Comparative genomics and evolution of regulons of the LacI-family
            transcription factors
  JOURNAL   Front Microbiol 5, 294 (2014)
   PUBMED   24966856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Swint-Kruse,L. and Matthews,K.S.
  TITLE     Allostery in the LacI/GalR family: variations on a theme
  JOURNAL   Curr Opin Microbiol 12 (2), 129-137 (2009)
   PUBMED   19269243
REFERENCE   4  (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   5  (residues 1 to 232)
  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   6  (residues 1 to 232)
  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 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   8  (residues 1 to 232)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   9  (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
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
REFERENCE   11 (residues 1 to 232)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
REFERENCE   12 (residues 1 to 232)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..232
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25015
     Region          23..68
                     /region_name="HTH_LacI"
                     /note="Helix-turn-helix (HTH) DNA binding domain of the
                     LacI family of transcriptional regulators; cd01392"
                     /db_xref="CDD:143331"
     Region          83..>181
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mgkgnggngs pkdagggrpt mtdvariagv sqssvslvln emsgarisae trarvrdaar
       61 kigyrlpntr qdldhapaie kdtiafivde istsphpvvs ldgirdyafe qgllvsahat
      121 rsnpdlesav lrsvlrdpai agviyatift rkvsvprele nvptillncy aeprqhmaiv
      181 pgggcgglrg drashvsrap ahrlhqrrtl dgrryrpaqr lqaslgdrry rl
//
LOCUS       WP_457662284             226 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662284
VERSION     WP_457662284.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24861
     Region          1..226
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mdelgqavvg gefsvgdtlp gdtdlaarfn vsrtvlream ktlaakglvv prarigtrvl
       61 pkahwnlfds dvltwhfgag vdekflrhvs evrlalepya aalaarrasd adiarmmrla
      121 vamgdaghsp htlaqadlef hlrlleasln pfmrtvgsli eaaligvfql tsptadetei
      181 drvaiahiri veeirrrned garramehvi rvgqerlimn lkerqd
//
LOCUS       WP_457662287             132 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Sinorhizobium medicae].
ACCESSION   WP_457662287
VERSION     WP_457662287.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..132
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14720
     Region          <2..115
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mvsryvfpqp aawtyelamm afaylvffga vagvrlgtha aidvlvaalp dgwqkavawf
       61 nylmlalffm vmtilfawqa wtsrhvhtia ldlsralsya plalasagml lqhliaerpw
      121 svrlhrnpes li
//
LOCUS       WP_457662290             311 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662290
VERSION     WP_457662290.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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 311)
  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 11458748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..311
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31356
     Region          5..268
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <178..289
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 mdlmatilsl etggndtlyg hagndtihgg segdyinggt gvdsasyags nrnvmaslsn
       61 pnintndaig dqyasienli gtnysdaldg ngsantlegg sgndtlagga gadkllggag
      121 idtvsyanas aavtakllya stntgdalgd tyssveniig siyadklygs dgansitggs
      181 gndglvgngg ndvlfggqga dhlygsvgad tfvfkaanes igsaydtifd fltseqdrid
      241 lsaidanisa sgnqafsflg taaftgvage lrydklssdt yiyadvngdk ladlkirldd
      301 avtltdgyfv l
//
LOCUS       WP_457662293             412 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Sinorhizobium medicae].
ACCESSION   WP_457662293
VERSION     WP_457662293.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44853
     Region          1..402
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mndrftlavt gqslikhdir dipapafrev qsllrqadls ftnfegtilg thggwplkgs
       61 ffgcsdpavl dalgaigfqa lslsnnhafd lgpsgvlstl eevekrgflh aglgrnarev
      121 srariatinq rrialvamdg gpgpdfmyaa dadenrperp gvnrlrlsqv levddvafeq
      181 iravrdkigy taidlandsq pddpprldpq aevaiarsvf krsnrygrgv ridevdmarn
      241 laaiasaard salviaylhh hhwasdwcql pewvsgvakr cidagasmfv shgapvlqpv
      301 eiyrgrpify slgnfifhvq sekstwtaae vwesvvgvcs fasdnslini sfhpvvigge
      361 hgledgvler rlvpqlvtgd savrilgrlq eqsarlgahi eisgnvgrlq ar
//
LOCUS       WP_457662309             147 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457662309
VERSION     WP_457662309.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..147
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16170
     Region          3..144
                     /region_name="VapC"
                     /note="VapC family ribonuclease, contains PIN domain
                     [Defense mechanisms]; COG3742"
                     /db_xref="CDD:442956"
ORIGIN      
        1 mlfidasviv avlageedvp tlidrleqdg gpyyvsavvr meatlsltrr laeasgrdrp
       61 atsemmekar rlveqfisdl dckeamisgd vgakaldaaq qfgkimnhpa klnmgdcfty
      121 acarayrtri aykgddftyt dlgwhsh
//
LOCUS       WP_457662312             223 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein, partial [Sinorhizobium medicae].
ACCESSION   WP_457662312
VERSION     WP_457662312.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..>223
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavd warapngcpi faqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarggyftpg anssaaggei gpvavlerhg
      181 alfplgdqnl alpsysagsg dpaktlasql eqlglsvhdw fsl
//
LOCUS       WP_457662322             412 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457662322
VERSION     WP_457662322.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10315023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=46057
     Region          116..200
                     /region_name="Phage_int_SAM_1"
                     /note="Phage integrase, N-terminal SAM-like domain;
                     cl12235"
                     /db_xref="CDD:472283"
     Region          227..405
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(260,357,360..361,392)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mlefyfsygr vlkrlrsgal ggemdrlaeh ffrlgykras akiylsriar fsrfagtrcg
       61 pmpihqdvvd sylrtfptdt prigamsalg harrvaperf iisvpseedd pdapllasfs
      121 dylrrvrgle pksregvllg grrfldwcrh hhpgqdieal takqvlaave yrlslsttsg
      181 srtaatshir tflrflywag rhhqdlariv prtpswrwah lpprlawndv rhaidaigat
      241 tpvgirdrav llllattgir ngelrairlr didwrtgevf vrrtkgkrdr vvplleetga
      301 aladyilrar prvdspylfl sftppvgpfk caapvsrivr krlrhggvel grvagahllr
      361 hslatqlvgq rrpinevadl lgqrsintta lyvkvaasql aevalpfpgg va
//
LOCUS       WP_457662328             444 aa            linear   BCT 27-JAN-2026
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Sinorhizobium medicae].
ACCESSION   WP_457662328
VERSION     WP_457662328.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..444
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=48687
     Region          13..443
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mskkfgkseh wahpataalh agfrndpstk avcvpiyqnt ayelegdlsk ianvynvked
       61 gytytriinp ttralerrfa avdnatdsla vasgqaatfi alanlcsgrp gdnivaspfl
      121 ygnswnllhn tfrrfgietr taensdpaaf erqiddrtic lfgecisnpi ldplplrslv
      181 eigrrrgvpv vvdntttplv crpaklgadm atysatkyvc ghgttlggii sdygsfpfqq
      241 hpesfplfsn pdeahggilw heavrevqdl gksatllkar mtwlrdvgac aspfnsfqll
      301 qgletlhlrm rqhcanaqtv aemlrnhpkv akvtyplfft gqkkeladdl fdrsygygam
      361 lmfevgdarn grtlienidl lyhvsnvgda rtlithpvst thttvprdkr iaagitdgti
      421 rlcvglehad diigdlekal saih
//
LOCUS       WP_457662331             489 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA carboxylase biotin carboxylase subunit [Sinorhizobium
            medicae].
ACCESSION   WP_457662331
VERSION     WP_457662331.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Chou,C.Y. and Tong,L.
  TITLE     Structural and biochemical studies on the regulation of biotin
            carboxylase by substrate inhibition and dimerization
  JOURNAL   J Biol Chem 286 (27), 24417-24425 (2011)
   PUBMED   21592965
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Mochalkin,I., Miller,J.R., Evdokimov,A., Lightle,S., Yan,C.,
            Stover,C.K. and Waldrop,G.L.
  TITLE     Structural evidence for substrate-induced synergism and half-sites
            reactivity in biotin carboxylase
  JOURNAL   Protein Sci 17 (10), 1706-1718 (2008)
   PUBMED   18725455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..489
                     /product="acetyl-CoA carboxylase biotin carboxylase
                     subunit"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52220
     Region          3..458
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
ORIGIN      
        1 mtikrvllac rgeialrfir takrlnieti svytdeerqa sfvlaadhrv rsdaanpyas
       61 peallaiakn wkadaiapgy gplaenadfa aacgsaglif igphpdalll agdkvrardl
      121 ardaglpvip ggavatleaa ivlaeeigfp vllkavaggg grgirlattl qnletawkev
      181 dlesriafgr sgiyierylg ddirhveiqi vadqsgnvfs lgdrgcsvqr rrqklveeap
      241 apgippalrh eisaaatafa kaasytsagt veflldtear fyfiemngri qvehpvteai
      301 tgvdiveqmf riangdslev vgeethrgha ielricaedp hrdfrpgggt vsacefpagp
      361 gvrvdagikt galqpsryds lcakliiwgr drteaigrar qalsetriag fptnvifyrw
      421 lldqpdfvag tydlsiastf vpnaapttll rdvaiaaalq khltvstass pvqanpaskw
      481 qrvnnggga
//
LOCUS       WP_457662334             402 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Sinorhizobium medicae].
ACCESSION   WP_457662334
VERSION     WP_457662334.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..402
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44458
     Region          19..143
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mshklpstsa pvlqmdslap elkvrdwvrg eplasfqqge lyilefcgtc cdscegamln
       61 lielqetykd sgvevvavaa henaasagea qahldawlaq fkklnfrvgl ddtgtmdtfw
      121 mqpsfsieip qafvidrdsr iafighpgkl pevlpkildg twrtsaqaqa aereriaede
      181 pkarnealkt qikgkiaaae eiedwktala aseegvaldp ddlsfryahv hlllhrlhdm
      241 qaglpalrqf vrdaintnye cmlqlafgll fdpaydyskf psverfamgk elsehilaqs
      301 rlnddydkvc syemvaayyh asgnkdraie llevalklld gpdpdmdglk egflphllqt
      361 lanyegeevc ygdvcvvpqt nipngatpna eqenpaerga le
//
LOCUS       WP_457662337              85 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Sinorhizobium medicae].
ACCESSION   WP_457662337
VERSION     WP_457662337.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..85
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=9852
     Region          1..83
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mklewtrkav adlgrlhdfl asvnrqaaar tvqsltsapa rlleqprige rleefdprev
       61 rrilvghyem stiyvlrpwh tresr
//
LOCUS       WP_457662341             536 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662341
VERSION     WP_457662341.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Solano,F.
  TITLE     On the Metal Cofactor in the Tyrosinase Family
  JOURNAL   Int J Mol Sci 19 (2) (2018)
   PUBMED   29473882
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Xu,Y., Bartido,S., Setaluri,V., Qin,J., Yang,G. and Houghton,A.N.
  TITLE     Diverse roles of conserved asparagine-linked glycan sites on
            tyrosinase family glycoproteins
  JOURNAL   Exp Cell Res 267 (1), 115-125 (2001)
   PUBMED   11412044
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447028
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..536
                     /product="tyrosinase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58385
     Region          70..311
                     /region_name="Tyrosinase"
                     /note="Common central domain of tyrosinase; pfam00264"
                     /db_xref="CDD:425566"
ORIGIN      
        1 mtrtrfltvs rrsfvkgata aagtalfaps ilraatkhrr knmtsadgqk dlqsymdavt
       61 amlklppsdp rnwyrngfih lmdcphgdww ftswhrgylg yfeetcrels gnpdfalpyw
      121 dwtanpevlp plfgtildpv nssayipdhn rfqdimqepi kacwdslssa qlqqqnlrgy
      181 pdfdalwsda masfanqpna rfltaqnpkl npatqtavdi dtikaslapt tfandagapg
      241 lafnspvsss hqvapvgfsi legqphnrvh msvggqsapy glmsqnlspl dpifflhhcn
      301 idrlwdvwtr kqqamglpvg ptadqqtqyd pepylfyvna dgspvsdktr aadylaigaf
      361 dydyepgsgd evipvatagr sapipaleaa vpasaavain kpatakltvs qelvdvaakp
      421 seqsrqfakv siappmdvgg lnflvfispe gttpdlnpdg pdfagsfeff gvrhhhtdtv
      481 sftipidkal drliddgrlk agepidfnvv vaqagkrieg smpakarltd iqvgsf
//
LOCUS       WP_457662350             699 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662350
VERSION     WP_457662350.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..699
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77415
     Region          132..526
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mtkqlqafyl lfcvgiafvv wmlgyglglq lfykdgrile ttitsnpfap iqqfwhykts
       61 palqkvalgs mlpallaagl vayiglkpts splgdaafqd maslrrgkwf rkqghifgrv
      121 grnilrardd rhhliigptr sgkgagyvip nalmhegsmi vtdlkgevfk atagyrrqng
      181 sqvflfapgs ektnsynpld firpergnrt tdiqniasil vpentesens vwqataqqil
      241 agaisyites pfykdrrnfa evnsffnsgv dlqallkyik ekepylskft vesfnsyial
      301 seraaasall diqkamrpfk nerivaatnv tdmdlramkr rpisiylapn itditllrpl
      361 ltlfvqqvmn iltlehdpds lpvyflldef rqlkrmdeim tklpyvagyn iklafiiqdl
      421 knldeiyget srhsllgncg yqlvlgandq ataeyasral gkrtiryqse srtielmglp
      481 rrtkveqire rdlmmpqevr qmpenkmill iegqrpifge klrffrtqpf ksaeafsqan
      541 ipqvpevdyl spkpvpattp eyakggdasv eipspapvte ekpltaaaae aapvkaepaa
      601 aakaaapakr tvnkkallpk pkatatktgg aeasasldam earikaieeg lkpkaaqlke
      661 vvetkaeklg dksptkrrni ldifsatvpd pvevgvpae
//
LOCUS       WP_457662359             378 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Sinorhizobium medicae].
ACCESSION   WP_457662359
VERSION     WP_457662359.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..378
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40095
     Region          2..>337
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mqriyqlvdp gsfaeidalv ehdcihfsad rrrvsgdglv vgharidgrp vgiyahdaaf
       61 lggsssrmha lkitkildla lkagmpvlgl ndssgirihe gvdagvqfge vfyktvrasg
      121 vipqisillg dcaggaayap altdfiimvr dkstmfltgp tvikqatgei vskeeiggpi
      181 lhavttglah fladsvddal eiarellsfl panncvsqss sqpadvsgss aiaklipqva
      241 tqpydvldvi geivddrhfl evhrlfapnv ltgfarlggl tigivanqpk vlagcldvas
      301 sekaarfirf cdafsipilt lldvpgylpg lkqeaggdyw sgskaaprll rgyrpedrpg
      361 paqgiwrrps yacqslgd
//
LOCUS       WP_457662364             303 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662364
VERSION     WP_457662364.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=32522
     Region          <134..255
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mctnwvqisy aqdgqksani itnesawptd dkaalatnfd erwrgsekef vlgadgvvkq
       61 enavqnkadk spynlggshh idaalsnfap sndvpnrvde pqaptgpiqh igsvrqiddd
      121 tkdvyecgps plspeevksl vvqtarkyrv devfataiaw aesgfdqsrn spkgargpmq
      181 lmpptaarfg vedicdpaqn ieggmkylrf lldefqnpll vaaaynsgeq riyqhggipp
      241 fqetvgyvak vvnyqlglpm psakgkakpa aapqavsdas dsgdagviav kktgkfvggv
      301 mhf
//
LOCUS       WP_457662366             369 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite oxidase [Sinorhizobium medicae].
ACCESSION   WP_457662366
VERSION     WP_457662366.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Hsiao,J.C., McGrath,A.P., Kielmann,L., Kalimuthu,P., Darain,F.,
            Bernhardt,P.V., Harmer,J., Lee,M., Meyers,K., Maher,M.J. and
            Kappler,U.
  TITLE     The central active site arginine in sulfite oxidizing enzymes
            alters kinetic properties by controlling electron transfer and
            redox interactions
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (1), 19-27 (2018)
   PUBMED   28986298
REFERENCE   2  (residues 1 to 369)
  AUTHORS   McGrath,A.P., Laming,E.L., Casas Garcia,G.P., Kvansakul,M.,
            Guss,J.M., Trewhella,J., Calmes,B., Bernhardt,P.V., Hanson,G.R.,
            Kappler,U. and Maher,M.J.
  TITLE     Structural basis of interprotein electron transfer in bacterial
            sulfite oxidation
  JOURNAL   Elife 4, e09066 (2015)
   PUBMED   26687009
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Barber,M.J. and Neame,P.J.
  TITLE     A conserved cysteine in molybdenum oxotransferases
  JOURNAL   J Biol Chem 265 (34), 20912-20915 (1990)
   PUBMED   2249998
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Campbell,W.H. and Kinghorn,K.R.
  TITLE     Functional domains of assimilatory nitrate reductases and nitrite
            reductases
  JOURNAL   Trends Biochem Sci 15 (8), 315-319 (1990)
   PUBMED   2204158
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Neame,P.J. and Barber,M.J.
  TITLE     Conserved domains in molybdenum hydroxylases. The amino acid
            sequence of chicken hepatic sulfite oxidase
  JOURNAL   J Biol Chem 264 (35), 20894-20901 (1989)
   PUBMED   2687265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..369
                     /product="sulfite oxidase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41535
     Region          35..335
                     /region_name="SO_family_Moco_dimer"
                     /note="Subgroup of sulfite oxidase (SO) family
                     molybdopterin binding domains that contains conserved
                     dimerization domain. This molybdopterin cofactor (Moco)
                     binding domain is found in a variety of oxidoreductases,
                     main members of this family are nitrate...; cd02110"
                     /db_xref="CDD:239028"
     Site            order(36..37,39,41,85,157,186,191,199,202,204..205)
                     /site_type="active"
                     /note="Moco binding site [active]"
                     /db_xref="CDD:239028"
     Site            85
                     /site_type="other"
                     /note="metal coordination site [ion binding]"
                     /db_xref="CDD:239028"
     Site            order(244,275,279,281,290,292,324,329..331,335)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239028"
ORIGIN      
        1 mptperpsli vrqkspqnie fpfaslsdwl iptelffvrn hfaspdldar dwrlrvggav
       61 erpieldlds ikamrsttft avvecagngr vyyeppkegl qwqngavgna awtgvllrei
      121 lemagvkrta revllvgads gvvdankkta spgpiafars lplekamahs tilaysmnee
      181 altrdhgypl ravvggwfgm awvkwithit vveqpflgyw qardyfrwer slaeprlvpl
      241 aemevkaqia rpvqgahlia gqpyrifgaa wsgeavirqv qvctgdgrgw regrlleter
      301 pfawrlweym wtpeevgryv lrcraidgag rvqpelprsd cesyaanwiv pvevtvvpep
      361 qtyeeefvi
//
LOCUS       WP_457662367             301 aa            linear   BCT 27-JAN-2026
DEFINITION  class II glutamine amidotransferase [Sinorhizobium medicae].
ACCESSION   WP_457662367
VERSION     WP_457662367.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31773
     Region          2..295
                     /region_name="GlxB"
                     /note="Glutamine amidotransferases class-II
                     (Gn-AT)_GlxB-type. GlxB is a glutamine
                     amidotransferase-like protein of unknown function found in
                     bacteria and archaea. GlxB has a structural fold similar
                     to that of other class II glutamine amidotransferases...;
                     cd01907"
                     /db_xref="CDD:238888"
     Site            order(2,149..150,175..176,200)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238888"
ORIGIN      
        1 mcgivglflk dkrlepqlga llsdmlitmt drgpdsagia iyggtadgka kvtiqsadpa
       61 tdfagldadl vnagidaavt vksthaviei aasrlgeira ilgeirpntr imgsgesvei
      121 fkeiglpkdv vsrfdvrsmg gthgightrm atesavttlg ahpfstgadq clvhngslsn
      181 hnnlrrelir egmsfetqnd sevaaaylta emakgkdlgq altgalddld gfftfvvgtk
      241 sgfgvvrdpi ackpavmaet dqyvafgsey ralvnlpgie tarvwepepa tgyfwdheka
      301 a
//
LOCUS       WP_457662370             511 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662370
VERSION     WP_457662370.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 511)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..511
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55486
     Region          1..500
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 miprlelhni tksypgivan edislsiqpg evhavlgeng agkstlmkii ygaaqadsge
       61 ifchgrriea hnpaisrslg iemvyqhfal fesvsvveni alaikgvfdl drlaaeiktl
      121 sarygmpidp hrrvhdlsvg erqrveivrc llqspkllil deptsvltpq avvklfetlr
      181 qlasegcsiv yishkldevq elcdtatvlr ngrvtgvarp kettslelar mmvgsqlpem
      241 hvspsvpsek pvlevrglsa pardeygtel tnisfdvhgg eivglagvsg ngqaeliall
      301 sgerthsrse tiliggrpsg hlgagerrkl gmafvpeerl grgavpphcl wenalltahr
      361 tglvrkglve rgqardfarr iidrfkvkan gpqssaqsls ggnlqkfivg reltleprll
      421 lvsqptwgvd vgaaafirqt lvdlsragaa vlvvseelde lfeicdrllv isngrvsppl
      481 irkqtnreei gllmtrvghg earrsevale n
//
LOCUS       WP_457662379             270 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457662379
VERSION     WP_457662379.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 581040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..270
                     /product="MBL fold metallo-hydrolase"
                     /calculated_mol_wt=29725
     Region          60..238
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Site            order(115,117,119..120,172..173,194)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mtiflcsacg tsfdegeylp ktcricader qyvpasgqaw ttmedlaldh rntwlqlepd
       61 liaiqtvpaf aineralllr tpagnvlwdc ialldeatna iihalgglta iaishphyyt
      121 tmqdwavafd apiylhaadk dwicrpsdhi rlweedalvl sssvtlvhgg ghfgggtvlh
      181 wtgedghgvl lagdivqvtp gadhvsfmws ypnmlplsaa evrsvadrla pwrferiyga
      241 fshqnvrqgg hdmvarsahr yieriqgpgr
//
LOCUS       WP_457662384             221 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662384
VERSION     WP_457662384.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..221
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24577
     Region          8..198
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtrspnflsm lgeaavaalf khwivrlytp gelivahges grdvffileg rarvtlfsen
       61 greifygdrg pgdiigevsa idgkarsasv valeatraar lpapafrrlv tdhpdfswal
      121 lehlssgirh mtdrvyefst lvvrrrlile llrraddrde stsrvfidpa pthfelaasi
      181 sthreavsre msvlakggph remrtqapav rpycsgiarr r
//
LOCUS       WP_457662389             287 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662389
VERSION     WP_457662389.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..287
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30693
     Region          23..278
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtmthsetks arisgtrlgy rfnivgmvgl siilfwalva vfapliipyp vgeivdldyf
       61 gpmsrdfwlg sdylgrdmls rilmgarytv gislaavtia cfsgvvlgmi aavaggwldt
      121 ilsrlldaln sipsklfglv vvaavgssip vliltlsvvy ipgayrfara lavninamdf
      181 itvarirges tlylirseil pniigpvlad lgirfvfsvl llsglsflgl gvqppyadwg
      241 alvrenigal pfgapavifp sfaiasltis vnllidnlpq kirdrse
//
LOCUS       WP_457662390             430 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662390
VERSION     WP_457662390.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..430
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47641
     Region          38..141
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          104..>272
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msqiqaqvtr rtllaaaata gavgmipqaf aateapvikp fkfratdeql idlhrrvaat
       61 rwpdeenvad dsqgvrleti kklakhwkhh dwrnvearln afpqftteid gldihfihvk
      121 skhenalpii ithgwpgsvi eqlkiikplt dptayggtea dafhvvipsl pgygfsgkpr
      181 etgwnppria kawavlmehl gytkyvaqgg dwgnavtelm avqqppgllg ihtnmaatvp
      241 aeiskslaag tppeglsade rrawdqlddf nknglgyaie mnnrpqtlyg ivdspiglaa
      301 wmldhdirsy rmiarsidge keglspddvl dnvslywltn taissarlyw dnahhpsggf
      361 fdrrgvkipv avsafpdeiy qapqswakra ypklihynrl pkgghfaawe qpalftselr
      421 asfkslrdqi
//
LOCUS       WP_457662394             264 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662394
VERSION     WP_457662394.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..264
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28297
     Region          3..251
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnvvsavnls ksfgalevlk gidldiakge vvciigpsgs gkttflrcin qlesisggal
       61 wvngelagyr iigeriqpld eheialqrra tgmvfqrfnl fahltaeqnv algpievlgq
      121 dpaqalgtar dlltrvglsh klksypaels ggqqqrvaia ramamnpqvl lfdeptsald
      181 pelvgevlkv mqevtttgit mvvathelnf ardvsdrvvf madgrilevg speriltepk
      241 eprlktflsa lsgsraesgd shaq
//
LOCUS       WP_457662398             307 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662398
VERSION     WP_457662398.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33265
     Region          2..302
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(116,131,165,191,217,240,267,292)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 matappavag mledmalrls grnpleirri wqdlydqsfw akgggaisfa aisaielalw
       61 dikgkaaglp vhdllggamr gdvklyangw nhehddvvnw akaaarplad gyralkaypf
      121 ayelpdgtfr hvsarmlddg rfrqaiervk alrqevgpdi elmldlsggl cddqllrfld
      181 vcrdlditwi eepldpfnln glsrvaarsg ipialgervy grggfrnvld tgavsivmpd
      241 iancggmlea vqiagmadty nvrvsphnca sslctaasls lcvaipnamn levypyfael
      301 ehlrpga
//
LOCUS       WP_457662400             445 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydroorotase [Sinorhizobium medicae].
ACCESSION   WP_457662400
VERSION     WP_457662400.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Gojkovic,Z., Rislund,L., Andersen,B., Sandrini,M.P., Cook,P.F.,
            Schnackerz,K.D. and Piskur,J.
  TITLE     Dihydropyrimidine amidohydrolases and dihydroorotases share the
            same origin and several enzymatic properties
  JOURNAL   Nucleic Acids Res 31 (6), 1683-1692 (2003)
   PUBMED   12626710
REFERENCE   2  (residues 1 to 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 10784973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..445
                     /product="dihydroorotase"
                     /EC_number="3.5.2.3"
                     /GO_function="GO:0004151 - dihydroorotase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006221 - pyrimidine nucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=46726
     Region          16..436
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 msrrkehtpa gwpsggekia eigagaapsa atvvdygdcl ilpgsidgqt hatnskglvg
       61 fapasasala ggvttivdmp ydmplpldip erlaakisav aahslcdval yatvtkesgl
      121 dhvealiegg vvafkissfe sspvrfprid ealtldllek lvgrdlplgl hnedqeivrs
      181 rtakaraagr dgigahsdsr plaaelaatg qflalgqavg ahahivhish eegfaqvgaf
      241 agigapvtge lcvhylcfdp ahdgdllgar mkvnppirpd aidglwrale cgtvafvssd
      301 haswpidnkl avsiyeagag ipgletlvpa ffsaaqargh daarltaeyl aarparffgl
      361 sgrkgalapg ldadfcvleq gefiwdaaka hdglnwspfd grrfdvrvaa twlrgkpawn
      421 gsqillsqgn gqylrrhglg wfpth
//
LOCUS       WP_457662399             279 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662399
VERSION     WP_457662399.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..279
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31110
     Region          8..276
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maldernisv mnfhyvrhtm drfladvcda gvsrielwaa aphfyiddkt laharalgrk
       61 vrgmglniva ftpeqciypi nisarepelr drslryfles mefatecgap allvtagggy
      121 rdepteqale rcvdsmgilc draqklgihl wmeslpdsfa niirsareir elmdklkspa
      181 lhavydvaga vmthetpedy ftqlaghvah vhftdsdagg shlawgdgvi dldklvaylr
      241 sqnyegslti eltnwkynvd ptpplkqcie amrtalara
//
LOCUS       WP_457662404             295 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662404
VERSION     WP_457662404.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..295
                     /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=32678
     Region          5..289
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mdkivnilhi sdihldaags fsqdvvlnaf ledipkldgl glkpdllvis gdlakvadhd
       61 daynnflnfi lrlfdvfaid edklilcpgn hdvsrkvagp slpaiqawrk eaedrdkant
      121 lqlnpayagh vyktfegyyq ladsfsqksv vstgtsytsy ffrefglsvi svntatlsta
      181 glisprdder klviperllv dafatvprds hklvvghhpt swlsetneem vrrllgqsgh
      241 mymcghihia rpetvsgllg schyaqtgal yewrdrwngy cvyqivpgsp ltchg
//
LOCUS       WP_457662403             739 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662403
VERSION     WP_457662403.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..739
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83755
     Region          7..>511
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mvysppaare ffaglrlrvs phdlekwrte tllpalidec kkslapvpie eafvppefqr
       61 evakspdeld laakkevitf daainsqsny visatgqsgk stllrqwair larksalean
      121 wtapvlisfs elrnyaayve svasrqlppi peklggagrl leqglltffi ddvdfqdrqk
      181 lkalaefmek fpncryvvas vdmlfegasv spvitgalpf thvqlrplkr kdllslihgh
      241 nvvdsdlsad allervtrea kglnvplnpv tasfliqifs tepdrilvnr atlveryiel
      301 llqkfsrpdv elrsfdfklk rdllskiaqh mvdeeeqepl yndvlrivld yvnhygfpqd
      361 atsilnhfvs crilekvere egvclrfpls sffhyfvafr mtedesfrlr ifdplnylaf
      421 aeeisfyaal arndkklley vftafsrcse emwvdsseel ragtfletfv epnadatedd
      481 lfaineviks neqieaareh hlngdvdtrs rnpkvkrpty ktvgdqwtah lflssqvlkh
      541 melipndlkk kyltdvirgw lqfcafsltl vprlvkdktv eingvlykln wnthepmgem
      601 arrislvmpi aasfmatsai gseklrlqla eglgtdelsp seqlmralll adigvpgiar
      661 ifedtskava vspylrkvll rklydvairf rlnkndveav rglagnllas iagaekgsrk
      721 resvienlrr qrllldldk
//
LOCUS       WP_457662413             594 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457662413
VERSION     WP_457662413.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 594)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..594
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=64679
     Region          3..589
                     /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 mplvaklqer laagdeagts dqvlsigesd lvriggrpai vsakpivsdt gdivqepgre
       61 flhlairfld gdfltrlgad ygfddlrfsv spdpgrnrsy apivrssgep igyfswlpfr
      121 pgaavmkata pvllisglll ftltsglsvv lqrrsrrlqe sqaelnhlar hdpltglanr
      181 asfnqslarv varsaadqan allyldldrf kqvndtlghp vgdrlmvava krlmetasag
      241 visriggdef tivvertrqe eveklcdsli aairqpfeid gqpiliglsi gvavatghda
      301 dpveitrkad ialyhaksag rnryavfgph mdelirtkrd leqdlraalh agnqlevfyq
      361 pvysaqsrei sslealvrwr hpskgaiapd ifvplaetag lidrlgafvl keacstaref
      421 psldiavnvs aielgqrhya aqvfsllrqf gvepwrlele itetalldea gvceknital
      481 rdfgvkfald dfgtgfssfg rlqrlevdri kidrsfvhaf drpgggvavv qsivgvahak
      541 glritaegve teeqseilrn lgcdelqgfh lskpvpkssl rqllgaetak rtss
//
LOCUS       WP_457662406             394 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662406
VERSION     WP_457662406.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 394)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42798
     Region          123..391
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 maeverllgg rtrdirlkge lgrlfeersw srtakiiraw miwvtlldvl tlglnaillp
       61 navalsmlpp acilppaala tafiwrkprg vglqrvslva glflillsva lvgvsaggef
      121 yerhlnimlf vaitaiiifs iplawtvava ffalalylif qlrnpmldtg savagtlfft
      181 sgivatvvar rtmtilaqkt fllelrdkrr vaeladanar lerlaktdpl tgianrrwmm
      241 etlnrlwgag aerpagtaml mcdiddfksl ndrlghaegd rclvkvagii qssvrrnrdh
      301 varyggeefl vvlpgadvqa alataerira sveaaslpnp asrvapyvtl sigvaaqgaa
      361 geiigperlq nqadtalyla kkagrnrvvl frpe
//
LOCUS       WP_457662415             510 aa            linear   BCT 27-JAN-2026
DEFINITION  malonate--CoA ligase [Sinorhizobium medicae].
ACCESSION   WP_457662415
VERSION     WP_457662415.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Pohl,N.L., Hans,M., Lee,H.Y., Kim,Y.S., Cane,D.E. and Khosla,C.
  TITLE     Remarkably broad substrate tolerance of malonyl-CoA synthetase, an
            enzyme capable of intracellular synthesis of polyketide precursors
  JOURNAL   J Am Chem Soc 123 (24), 5822-5823 (2001)
   PUBMED   11403625
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..510
                     /product="malonate--CoA ligase"
                     /EC_number="6.2.1.76"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0090409 - malonyl-CoA synthetase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0090410 - malonate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55336
     Region          1..502
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(159,162..167,169..170)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(162,202..203,206..208,248,250,254,276..278,297..302,
                     306,321,381,393,401,404,407,436,472)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(162,276..278,297..302,321,381,393,401,407)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(202..203,206..208,248,250,254,276,298,300..302,306,
                     404..406,436,472)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 msnhlfdair rasrpnsvfi laadervwty gdmlehsgrl asalvslgvq pgdrvavqve
       61 kspealmlyl aclragavyl plntaytlte ldyffgdaep rlivcapaak egiskiaayr
      121 sagvetlddk gggslielal getpdfsdld rraddlaail ytsgttgrsk gamlthdnll
      181 snavtlrdhw rftaddrlih alpifhthgl fvasnvilla gasmfflpkf danevlslmp
      241 rsttmmgvpt fyvrlvqnpg ltrevtagmr lfvsgsapll aethrtfahm tghaileryg
      301 mtetnmntsn pydgeriagt vgfplpgisl rvadpesgkp lpngdtgmie vkgpnvfkgy
      361 wrmpektqae fradgffitg dlgkiddrgy vhivgrgkdl visggyniyp keveteidqm
      421 pgvvetavig vphpdfgegv tavvvrksga tiderailgg legrlarykq pkrvifvedl
      481 prntmgkvqk nvlreayadl yaeagagari
//
LOCUS       WP_457662418             549 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662418
VERSION     WP_457662418.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 549)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..549
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60591
     Region          4..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtasdkpilr idgltvdfls egdpvravdn vsfdvcpget lvilgesgsg ksvstgtvmg
       61 lidcppgdiv sgtlvfdgtd lsrldnegrr elngrriami fqdplaylnp vytvgrqiae
      121 vfeshgageg gamrgrvvrl lervgipeae trvdyyphqf sggqrqrvmi amaialepdi
      181 liadepttal dvsvqaqild llrdlqretg malimithdl evaaamadri ivmnagkvve
      241 sgraedvftn prhsytrrlm savphgdpkk rsrpveqevl lqvadlskhy klgsgpfapk
      301 refkavddvs ftlrrgetvg ivgesgsgks siarmllrln eptsgsalfa gedifklegr
      361 alngfrrkvq mvfqdpfgsm nprmnvrsii sepwaihrdi lprqrwnerv vellelvglk
      421 pehaeryphq fsggqrqris iaralasepe livcdeavsa ldvsiqmqvi glladlrqrl
      481 glsyifithd lpivrqfadr ilvmqrgkiv eegetealfv sprheytral lnavpqpkwl
      541 qrdptplag
//
LOCUS       WP_457662426             145 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662426
VERSION     WP_457662426.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Domitrovic,T., Raymundo,D.P., da Silva,T.F. and Palhano,F.L.
  TITLE     Experimental Evidence for a Revision in the Annotation of Putative
            Pyridoxamine 5'-Phosphate Oxidases P(N/M)P from Fungi
  JOURNAL   PLoS One 10 (9), e0136761 (2015)
   PUBMED   26327315
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
REFERENCE   3  (residues 1 to 145)
  AUTHORS   di Salvo,M.L., Safo,M.K., Musayev,F.N., Bossa,F. and Schirch,V.
  TITLE     Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate
            oxidase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 76-82 (2003)
   PUBMED   12686112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467517
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..145
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15965
     Region          1..136
                     /region_name="YzzA"
                     /note="General stress protein 26 (function unknown)
                     [Function unknown]; COG3871"
                     /db_xref="CDD:443080"
ORIGIN      
        1 maamsleels ekirkidfcm lstreagdgi strpmsnngd veydgnswff sfedtrkvaa
       61 igsdprvsls lsappsllgk pgifvaidgr asiirdkamf eehwvaeler wfpqgtktpg
      121 lvlikvhagr ieywdgedne vvtvs
//
LOCUS       WP_457662442             402 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662442
VERSION     WP_457662442.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..402
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=44447
     Region          12..389
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mntkitpdhl graavvyvrq stmtqvtgnl esqrrqydla gaaattgfas vsvidddlgr
       61 sgsgsmerpg ferlvaqvcs gnvgavycie asrlarngrd whhlidlcal agtlvidpdg
      121 aydprlvndr lllglkgtms eyelslmrqr giaardskag rgelrfmlpp glcwsevgki
      181 eidpdehvae tirlvfakfr elgsgrqvfl wlrsadikmp vvlrnvdvck lvwkapayhs
      241 vmqilhnply agayafgrra qrtrivdgra rkatgvrkpr dewsvllrdn hqgyiswrey
      301 eenhkllten ahmkkncdrk sarggrallt glmrcgrcgr mmrvfygsak gnahryqcrg
      361 ddahvgvglc igiggvrvdr avamqileav vgfhaelsrl ga
//
LOCUS       WP_457662445             391 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457662445
VERSION     WP_457662445.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Goodwin,T.J. and Poulter,R.T.
  TITLE     A new group of tyrosine recombinase-encoding retrotransposons
  JOURNAL   Mol Biol Evol 21 (4), 746-759 (2004)
   PUBMED   14963102
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=42655
     Region          193..390
                     /region_name="INT_Cre_C"
                     /note="C-terminal catalytic domain of Cre recombinase
                     (also called integrase); cd00799"
                     /db_xref="CDD:271180"
     Site            order(209,223..224,226,302..304,318,320,338..340,375)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271180"
     Site            order(218..219,346,350)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271180"
     Site            order(223,265,340,343,375)
                     /site_type="active"
                     /db_xref="CDD:271180"
ORIGIN      
        1 mvdnsktags dsqavvrrae eldaldailp fdrrdqlaal ltdddvatlk hlagegmgen
       61 tlralasdlg yleawcrlat gsplpwpape alllkfvahh lwdpvkraed aahgmpadve
      121 aglraerllr spgphapgtv qrrltswsil trwrgltgaf gapslksalw lavrasnrpr
      181 qrkskkavtl diltkllqac agdrlvdard ralllaafas ggrrrsevaa lrvedladee
      241 pvranpaden spplpclsir lgrtktttad enehvlligr pvtvlkrwls daqikdgpvf
      301 rridqwgnid rraltpqsvn lvlkarceqa gldpalfsah glrsgyltea anrgiplpea
      361 mqqslhksvt qaaryynnae rkngraarli v
//
LOCUS       WP_457662458             317 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662458
VERSION     WP_457662458.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..317
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=35045
     Region          1..>294
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mqraaiyarf stdlqsersv ddqielcref airqgfivar syfdkarsga sifgrdglls
       61 lmddaregkf divivealdr lsrdqedlag lhkrltfagv qiiavhdgaa daiqvgirgl
      121 vstlfladlk hkirrgmtgv iregrhaggr aygyrptlgq pgvlqifepe aeivrkiyae
      181 viegslprei aaglnrdkva pprgvawnas tilgsaqrgn giirnplycg rivwnrirmv
      241 rdpetgkris rpndasehre aeaphlaivn qqtyeaalai legrakkvrg garraeakat
      301 sfrppalrpv rwwhvda
//
LOCUS       WP_457662476             244 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662476
VERSION     WP_457662476.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..244
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27946
     Region          28..>84
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msmphladlv mylvrkishi gfmspnpnki aeirrrkklt qqqlaerlgv htitvskler
       61 gvmqltsswi erlakameva qselwmitdl mrfeangqvs dgdrvqvvdp sengfstfrh
      121 plgdptskwl hvqddsllpf agegdllqfs llqmdeieks dllngrlcmy vlegteeirl
      181 airekwhsdr lldlrsmngr lmkncrveav wyfsgyqpnw gvvahfdtdr knnvamaerg
      241 seei
//
LOCUS       WP_457662467             539 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662467
VERSION     WP_457662467.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..539
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=57881
     Region          467..511
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mglygsapea pdpqetasaq tatnigtava nnvmgnvnqv tpdgnltyty ttqkwkdpis
       61 gkeydlqvpt atqslsqqqq aiknqtdaae lnmatlannq sgklndllgk piniggapag
      121 gnaggiglpq yqqfgsgpkl qtslgnygnv qssiagagni qkqvadsgqi qnqlgnagdi
      181 trsyetdfsa drqkvedalm qrlnpqmerd raaletrltn qglqpgseay nraideanrs
      241 stdarlgail sagqeqsrla glanqsatfq nsaqqqaynq qlgsgqfans aqaqqyaqna
      301 nnmqmgnaaq qqqfgqnqaq qqannaaqqq kfgqglagaq fgndalqqqy qnqntatagn
      361 nalqdqsfns qqskfnmqnq qraqylnely aqrnqpinei iglmsgaqvn spsfvptqsn
      421 pmptvdyagl vqqdyankmg aynqqqagmq smfggmlgfg gqlaslsdkr akkdikkvge
      481 lkghglyeys yrgkhddgkk higvlaqeve kkrpdavsrr pdglrqvnyg alfnagrkr
//
LOCUS       WP_457662478             505 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662478
VERSION     WP_457662478.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..505
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=55658
     Region          1..398
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkraaiyary stdlqndqsv edqfrlcrah aerlgfnvve efsdraksga smfgrpglan
       61 liqaaeraef dvlvseapdr isrdiadlah ihktlkfrgi emncvnggam dtvqigmygv
      121 igqmqreega kkvrrgmagv vrsgrnpggk aygyrpifgr kgeleivede aatvrriyel
      181 yaggmaprsi aailneenvp aprgerwnas tingsgqrgn gilrnpiyag rivwnriqmv
      241 kdpstgrris rvnpesehee vaaphlqivd sglfeivqhr keatggadra kgprskrils
      301 gllrcgacgg gmalvgpdrs gnriqcstfr esgtcnnsrr yyverietev vdglrrqfad
      361 tsiieayvea yqveqkrlrg daqrarasaq ralqeakdgi tkivekiskg liedeeaaal
      421 laplraerdr qkailgttee ppnvieiqpk avkrfrenie slaqivrekd geaspeiaap
      481 frqlvcclse isgrrrecpg lsgnc
//
LOCUS       WP_457662489             301 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662489
VERSION     WP_457662489.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32110
     Region          8..284
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mssaattrvl isggtgfvgr fivehllang yhvtvggrsp ppagfysqpv shvplrldpd
       61 adqagafdni cyfvhaafvh vegryrggeg qdpegfrran legsvrlfee artagvrrcv
      121 flssraaygd tappvvaets pvapdtlygq vklaaenalk smtghhfvta nlritgvygp
      181 agegrqhkws dlfadylagr tvldrigtev hgddvakavr lmleteparl sgqvfnvsdv
      241 ltgnreilsi lqaatacpnp lptaaaaeft tmsteklral gwvpggrekl altirelagr
      301 r
//
LOCUS       WP_457662491             203 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Sinorhizobium medicae].
ACCESSION   WP_457662491
VERSION     WP_457662491.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..203
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22478
     Region          28..>185
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          83..111
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(84,87..88,91..92,94,118,121..122,125..126,128..129,
                     152,155..156,159..160,163)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          116..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          151..179
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpamrvfsnl ilaclamcat tvdstplvaa epspqtevaa lttpkervda lftdlkreve
       61 eekarqvaer irlewqdsgs atvnllmqwa nkaiaeekqt aaldlldqvi alspdyvegw
      121 nrratlhyqm gnfrksmsdi nrvlaleprh fgalagmatm leaagkeela mrawqqfldv
      181 ypsdrkaqeq lgelaeklag srt
//
LOCUS       WP_457662497             177 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457662497
VERSION     WP_457662497.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..177
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19305
     Region          50..166
                     /region_name="VapC"
                     /note="VapC family ribonuclease, contains PIN domain
                     [Defense mechanisms]; COG3742"
                     /db_xref="CDD:442956"
ORIGIN      
        1 mnaltamiaa psrsengmkq sgtrpkssas lndrrgfiry hcdhvrwrge asaciaalqk
       61 srsrlisavn yvetgtvmag rvrsgdrcea iadldafltv fridiapvdd rtaraamkar
      121 idygqrfgtr gglnfgdcfa yalekqrsap llyagndfgt tdinpalkap slrrtkr
//
LOCUS       WP_457662498             531 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662498
VERSION     WP_457662498.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..531
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58373
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdtfdyiivg agsagcvlan rlsenpdrrv llleaggsdn yhwihipvgy lycinnprtd
       61 wcfttaaeeg lncrslgypr gkvlggcssi ngmiymrgqa rdydlwrqlg cagwswndvl
      121 plfrkcedhh rgademhgag gewrvekarv rwavldafqk aateagipet ddfnrgtneg
      181 sgyfdvnqrs girwntakaf lrpamrrrnl tiltkahvrr lvlddrrvsg vefqhdgvtk
      241 svlarrevvl sagaigsphi lelsgigrpd vlrengievr helpavgenl qdhlqlrlay
      301 kvtgvptlne katslfgkaa igleylvrrs gpmamapsql giftrsgpek etpdlqyhvq
      361 pvtlekfgep vhpfpaitas vcnlrpesrg svhlkspdfa aapdirpryl saeadreaav
      421 kairltrriv sqpafarykp vefkpgpsye tdedlkraag eigttifhpv gtcrmggdqa
      481 svvdpelrlr glaglriada simptitsgn tnsptimiae kaaemilaad r
//
LOCUS       WP_457662501             338 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662501
VERSION     WP_457662501.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..338
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36946
     Region          19..335
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
     Site            order(66,77,103,174,176,238,277,303)
                     /site_type="active"
                     /db_xref="CDD:185696"
     Site            order(174,303)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185696"
ORIGIN      
        1 mttdmeifgh lasgepvhrv tlkgggltas vitwgsviqd lrldghappl vlgfedfpsy
       61 pahssyfgat pgrnanrigd grfsldgray qlernekgvt hlhggsdnia rrnwtivgrd
      121 edsvtlkitd pdgragypgn ctitctyrlk pggtlnvvye tetdaptlan vcqhsyfnld
      181 ggsdafghdi mvaadhflpt derqiptgei rpvdgtafdl remtslkrql dgdrigydhn
      241 fclspermqk rsvalvrsin sgvslevltt esgvqlytge kldvavpgle grryggfagf
      301 cletqiwpda vnhegfpnai lrpgetlrqe tdyvftrn
//
LOCUS       WP_457662502             502 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457662502
VERSION     WP_457662502.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..502
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53569
     Region          3..492
                     /region_name="ASKHA_NBD_FGGY_L-RBK"
                     /note="nucleotide-binding domain (NBD) of ribulokinase
                     (RBK) and similar proteins; cd07781"
                     /db_xref="CDD:466799"
ORIGIN      
        1 mgyfltadgg teslrarlyd ltgnclgsaa vpyetrfsag araeqnpedw wrafveasrr
       61 tiseadvepa aieaitlatt sctvvaldre gkalrpaiiw mdvrasdead avlatgdeal
      121 isngagrgpv saewmipkal wiarnepeif eeahticeyq dfmtlrltge raaslnnvtl
      181 rwhyqtdrgg wartlveklg lsalldkwpq rvvapgevvg tlspaaaqel glstrvklvq
      241 ggadaligmi glgvakpgql alitgsshlq fgvtesavha pgvwgtyrdc vypnryiveg
      301 gqtstgsiia wlgrlmngtm dldelnrkaa alepgcdgll vqdhfqgnrt pytdalsrga
      361 ivgltlahep hhifraimeg mgfgtraild amaeagyrgs eitvgggaga selwlqihad
      421 taglpvcvpa srdapsvgaa vlaahgagyf asidegisam vrpgkriepr preaalydgi
      481 yqqyralypa lkslrdrgge pr
//
LOCUS       WP_457662503             245 aa            linear   BCT 27-JAN-2026
DEFINITION  Bax inhibitor-1/YccA family protein [Sinorhizobium medicae].
ACCESSION   WP_457662503
VERSION     WP_457662503.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Guo,G., Xu,M., Chang,Y., Luyten,T., Seitaj,B., Liu,W., Zhu,P.,
            Bultynck,G., Shi,L., Quick,M. and Liu,Q.
  TITLE     Ion and pH Sensitivity of a TMBIM Ca2+ Channel
  JOURNAL   Structure 27 (6), 1013-1021 (2019)
   PUBMED   30930064
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Watanabe,N. and Lam,E.
  TITLE     Bax Inhibitor-1, a conserved cell death suppressor, is a key
            molecular switch downstream from a variety of biotic and abiotic
            stress signals in plants
  JOURNAL   Int J Mol Sci 10 (7), 3149-3167 (2009)
   PUBMED   19742129
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Zhou,J., Zhu,T., Hu,C., Li,H., Chen,G., Xu,G., Wang,S., Zhou,J. and
            Ma,D.
  TITLE     Comparative genomics and function analysis on BI1 family
  JOURNAL   Comput Biol Chem 32 (3), 159-162 (2008)
   PUBMED   18440869
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Reimers,K., Choi,C.Y., Bucan,V. and Vogt,P.M.
  TITLE     The Bax Inhibitor-1 (BI-1) family in apoptosis and tumorigenesis
  JOURNAL   Curr Mol Med 8 (2), 148-156 (2008)
   PUBMED   18336295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..245
                     /product="Bax inhibitor-1/YccA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26245
     Region          15..244
                     /region_name="YbhL"
                     /note="Integral membrane protein YbhL, putative Ca2+
                     regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic
                     ion transport and metabolism]; COG0670"
                     /db_xref="CDD:440434"
ORIGIN      
        1 madlrnyqtr mspagaqaga videglraym lkvynlmalg laitgvaayg tyalaasnpa
       61 faqliyaspl kwvvmlapla lvfflsfrin smsvatalmt fwvyaalmgl slssiflvft
      121 gqsivqtffv taasfgalsl ygyttkkdls glgsflimgl fgviiasvvn iflassalgf
      181 aisvigvlif agltaydtqk lkemyfegdd alvagrkaim galtlyldfi nlfmfmlqfl
      241 gnrne
//
LOCUS       WP_457662504             205 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent Clp protease proteolytic subunit [Sinorhizobium
            medicae].
ACCESSION   WP_457662504
VERSION     WP_457662504.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Yu,A.Y. and Houry,W.A.
  TITLE     ClpP: a distinctive family of cylindrical energy-dependent serine
            proteases
  JOURNAL   FEBS Lett 581 (19), 3749-3757 (2007)
   PUBMED   17499722
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..205
                     /product="ATP-dependent Clp protease proteolytic subunit"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22877
     Region          1..197
                     /region_name="clpP"
                     /note="ATP-dependent Clp protease proteolytic subunit;
                     Reviewed; PRK00277"
                     /db_xref="CDD:178955"
     Site            order(35,37,46..47,50..51,54,69,76,80,83,86..87,91,99,121,
                     123,129..132,146,149,151,153,176,178)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132928"
     Site            order(102,127,176)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132928"
ORIGIN      
        1 mreamqlvpm vveqssrger sfdiysrllr eriiflngev ndvvsalvca qllfleaesp
       61 tkpiqlyins pggvvtsgfa mydtmryira pvhtlcmgta rsmgsfllma geaggraalp
      121 ntsilvhqps ggfqgqasdm lihaeeirrt khrmtrlyae hcgrtyeefe ramdrdrfmt
      181 aeealewgli drivtervag aerdg
//
LOCUS       WP_457662510             579 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457662510
VERSION     WP_457662510.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 579)
  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 579)
  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 579)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..579
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65680
     Region          108..433
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 mlkellarps sdntypslrs sapypsaayl ltsrigreir rqtkrklnla paaigsaiar
       61 lsrdgdaypi ifsaieevrr qdenrglphs vaieeklpkp eidlnqprik hvrihnfksl
      121 esidfsmkaq mpevavamsv pnefsdvpda pcllilgena tgkssileai altciptqlr
      181 nqlqespadl lldpeymgsa ghapinrgsi evefhndtpt lklvldreng ifsdnsdahh
      241 plifaygahr lfdreqrddv vrhidtlfrr dqvisnpepw lielskrspe slnevvsalr
      301 hiiqidghfr nievgrdqdg keycainier knpdgllrqr lsvvssgyra vlavvcdifs
      361 rllelsnydp raarhgraii lideieahlh prwkmqivsg lrralprstf iltshdplcl
      421 rgmfagevmm lnryrnrdqt adsssmnevv eqisdfanie nltidqllts difqlfstdd
      481 rrieatfaev pailkkeeef lrtreerwrl sereqtilrs frdeisnglp ygktevsrlv
      541 qeavaeyvag rrvrdkssne ekreraknai ksylgdllg
//
LOCUS       WP_457662526             521 aa            linear   BCT 27-JAN-2026
DEFINITION  integrase catalytic domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662526
VERSION     WP_457662526.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..521
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - obsolete endonuclease activity,
                     active with either ribo- or deoxyribonucleic acids and
                     producing 5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=58349
     Region          162..257
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 matrteliea iieryrsscr adkhrildef vavtgyhrkh airvlrhrgs eppsarqhav
       61 qygpdvreal valweasdrl cskrlkplip illpalerhg rlelnsalrd kllmvsaatm
      121 drllsevrvv arggqrrrag mssavrrsvp vrtfgdwndp lpgyvevdfv ahsgtsssgs
      181 faqtmvltdi atgwtecvpv rtresglvia aikqarsqfp fpllgvdfdn dsafmnelvv
      241 cwcrsqglev trsrayrknd qawveqknga ivrrlvgygr fvgaeattal arlyevvrlh
      301 gnlfqpsfkl rektrigarv ikryhppvpp varvlahsgv aeadkdrlqa mlesadpvil
      361 fagiraaqee lgrrvdrrgl narseepvav dlqrftlslk tawqvgekrp thrrpyrrtk
      421 pypkrqsmle pfepqirawl eadpavsaas vlerlmsadp srftkkslrt vqmavkawri
      481 etagqiildg dwmeratlss haaagedngh lsaqrfgnip g
//
LOCUS       WP_457662527             290 aa            linear   BCT 27-JAN-2026
DEFINITION  lysozyme [Sinorhizobium medicae].
ACCESSION   WP_457662527
VERSION     WP_457662527.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Holtje,J.V.
  TITLE     Bacterial lysozymes
  JOURNAL   EXS 75, 65-74 (1996)
   PUBMED   8765294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10091405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..290
                     /product="lysozyme"
                     /EC_number="3.2.1.17"
                     /GO_function="GO:0003796 - lysozyme activity [Evidence
                     IEA]"
                     /GO_process="GO:0009253 - peptidoglycan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31038
     Region          5..133
                     /region_name="lyz_endolysin_autolysin"
                     /note="endolysin and autolysin; cd00737"
                     /db_xref="CDD:381599"
ORIGIN      
        1 mlaeeaivla syndgtgtmt igaghtaaag ppvprsgmti slteainiyr ndlaktenqv
       61 qsavravlsq hqfdalvswh fntgaissat ltrklntgdv agaaaefarw nkskgkvleg
      121 liarrdreta mflngdygnp kvrvleskgg gpeeiftgdq ieallggavs sedeqsteel
      181 lanpmsqllp lhrpkqtigi tkavlqkfhd lipadgrdda vavvavrgyy lntmgkegan
      241 drgvyddaif vvervkrsee ltppiasprd vtealcaema vifscrgvrr
//
LOCUS       WP_457662534             320 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457662534
VERSION     WP_457662534.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..320
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35155
     Region          96..298
                     /region_name="COG1223"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440836"
ORIGIN      
        1 marsdllisl vragasgdra mlksatealv aeeraqnhhi vadrlerals tvavtppalt
       61 aasspagsgk dtileleprl qlnqlmlplp veqggrqlie ehtradvlra hgyeprhrvl
      121 lsgppgngkt sfaeavaeal glpffvvryd aligsylget narlrklfdy vrtrpsvlff
      181 defdsigker gdthetgeik rvvsfllmql dqlpsyvvvi aatnhaelld ravwrrfqmr
      241 lafpapdrqr igvfldriis qwpdapkaaa nsiakklgtv sfaealdfcq nvrrrqilgl
      301 ggafhqrcts frtgplgnks
//
LOCUS       WP_457662535             791 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457662535
VERSION     WP_457662535.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..791
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=84529
     Region          242..585
                     /region_name="Peptidases_S8_Subtilisin_like_2"
                     /note="Peptidase S8 family domain in Subtilisin-like
                     proteins; cd04847"
                     /db_xref="CDD:173793"
     Site            order(248,281,331,352,387,539)
                     /site_type="active"
                     /db_xref="CDD:173793"
     Site            order(248,281,539)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173793"
ORIGIN      
        1 mlqrdpagla lrtdpsalap erllvfevrg siaafarain nvpglelide eelpddedka
       61 pvayllvpdl ralqqieslw rtwvagrvlp qgftpwrdvf aclrglrvwg padrvqplda
      121 dvlaqeiegr edneliplei elvfrasaea gaigeatvag airqsggqll srarlddiay
      181 havlaelpva avrtvvertp gslagvepim hirpqsvvtg idtndllpaa ptrapgpvaa
      241 apilalldgv plaghpllqp hlsvedhfgl epnalvsqrf hgsamasliv hgdrnrpepp
      301 lprqvhcipv lgnndrfppd rliidliyqa virmragdqp saphviivni slgnvrrpfy
      361 gqlspwarll drlafrfgil flvsagnita hfpvaafanr vafedanadq rargvinava
      421 aqvadrrlls pseainglti garnldwvpa aeralaranv npyseldtan pssalgpgfa
      481 gsvkpdilmp garehlrvva saesimvapa sasrgaglrv aapprpglen aegftngtsa
      541 atalasrtah rihdaleaay gqeflqltnv qravlvkall vhparwpnaa aglvkellgp
      601 cgkgqaprqk dnirrflgyg vfdsddavac aadratfwcv gslgrersvd vlvpipaaig
      661 gqarahsisa tlawftpvvp grksyravrm kildpaeiag lgvsadawqp dgnqtdrgtv
      721 ftrvwsgaqa avvadgmnlr lkiqrepdpa spiddlvpfg lavtlampge lrlydqvrsr
      781 vqprpaqraa p
//
LOCUS       WP_457662542             303 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662542
VERSION     WP_457662542.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33165
     Region          1..294
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdrsirafia iakhgnvtia ardigmaqss ltkklrqiei efgaplferl prgmrltnyg
       61 qalyrhaiei drsysqakee ivaiktghvd llrigtgpsf sllymsrvla qlrsefpktr
      121 lilsspanss ynkrllagdl dvvvgrieae hlsnkitstt latfehclvi gdrkgiahdp
      181 ptaadlldfa wisysessep epaltnffha yglqppplav stssfntalq lvaagkyami
      241 vpnqfqpive tsgavaypie tplhayevgv svrsstaryp ivkrlaeilk ielafgsklg
      301 ver
//
LOCUS       WP_457662543             535 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfatase [Sinorhizobium medicae].
ACCESSION   WP_457662543
VERSION     WP_457662543.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Stam,M., Lelievre,P., Hoebeke,M., Corre,E., Barbeyron,T. and
            Michel,G.
  TITLE     SulfAtlas, the sulfatase database: state of the art and new
            developments
  JOURNAL   Nucleic Acids Res 51 (D1), D647-D653 (2023)
   PUBMED   36318251
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Ghosh,D.
  TITLE     Three-dimensional structures of sulfatases
  JOURNAL   Methods Enzymol 400, 273-293 (2005)
   PUBMED   16399355
REFERENCE   3  (residues 1 to 535)
  AUTHORS   O'Brien,P.J. and Herschlag,D.
  TITLE     Functional interrelationships in the alkaline phosphatase
            superfamily: phosphodiesterase activity of Escherichia coli
            alkaline phosphatase
  JOURNAL   Biochemistry 40 (19), 5691-5699 (2001)
   PUBMED   11341834
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Parenti,G., Meroni,G. and Ballabio,A.
  TITLE     The sulfatase gene family
  JOURNAL   Curr Opin Genet Dev 7 (3), 386-391 (1997)
   PUBMED   9229115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..535
                     /product="sulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0008484 - sulfuric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61762
     Region          1..367
                     /region_name="sulfatase_like"
                     /note="uncharacterized sulfatase subfamily; cd16148"
                     /db_xref="CDD:293767"
     Site            order(9..10,49,94,96,216,294..295)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293767"
     Site            order(9..10,49,94,96,216,295)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293767"
ORIGIN      
        1 mrtvfvlfds lnrlalecyg gqgiptpnln rfaergvtfd rhyvgglpcm parrdlhtgr
       61 ltfmhrswgp lepfdnsfpk ifsehgtysh misdhqhyfq eggfgyintf dswefirgqe
      121 edtwvamvqp plerfremfd drhyplsrip kraetvtrgn tqlkawkhls niknreryke
      181 eaefpcvkcf taalefldgn kdadnwflmi etfdphepfh aperfkklfa tgytgkildw
      241 pvyekvtnsa eeiaeirany aalvtmcddq fgrlldafde gglwedtalv vttdhgflls
      301 ehdwwgknrt pyyeeiship lmiyhpdyaa nggerrsalt qqtdlmptfl dfasaetppe
      361 vtgcslrrvl eadepvrddl ilgmfggpic atdgrytyyl fpdsltgegf neytvmpthl
      421 rsyfdvrefe gaemsepfef tknmpvmkik ardfaeripw meqqggfadv gtvlydltad
      481 pkqerpvevp eivaalrrsi trhlarhdap reayvryglt qeksamqrer vgkvi
//
LOCUS       WP_457662545             319 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662545
VERSION     WP_457662545.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..319
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34608
     Region          20..317
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtstlvskta vpgiaqqqga assrgtrvld lfdrhfrlit iapaallils ltvapaielv
       61 rmagtkiaft ndgvertaaf aenigcland wiywrallnt lafvitstla elvlglvlal
      121 aaqrmtrakg ivrtlmlmpi lippvaignm wrlmynpefg iiaylvdqva gvrldmlgst
      181 stallaviiv dvwhwtpfmf lillaglegl peevmqashl dganslqrlr fivlpilwpa
      241 iavafvfrsi gafkvfdqiy lltsggpggs tevlslyvfk vffqnnelgy gallslvtia
      301 ivcsylavfr iaqrrkgal
//
LOCUS       WP_457662547             118 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662547
VERSION     WP_457662547.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 118)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..118
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12427
     Region          <1..118
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mmsafenipr eleeaavvdg crtltaffvi llplalpgli aagllsflfs wsefsialnl
       61 ttketytipv aiasyagene imhgqmaaas vlstipavvl mffgqrfilg gltagavk
//
LOCUS       WP_457662551             694 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662551
VERSION     WP_457662551.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..694
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=78940
     Region          18..427
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mstdnamkis adhlrrdafl yvrqsslrqv fentestkrq yalrdraval gwpiervhvi
       61 dndlglsgaq sqdrdgfqrl vtevamghag ivlglevsrl arnnadwhrl lelaamsrtl
      121 imdedgvyda asfndrmllg lkgtmseael hilksrlqgg ilnkarrgel elplpiglvy
      181 tpdmrvvldp drqiqdtvrm lfdtfrevgs acavvrrlrn ekilfprrir rgigkgdvlw
      241 seidhsrviq ilhnpryaga faygrtrtiy naklksvqqk mprsdwqvli pqahegyisw
      301 defernqtsl eqnavgfspg lrgrmprqgn gllqgrvlcg rcgarmrvhy eqfegnlrpy
      361 yicneavvrh agkacqwarg paideavsal lleamaptai evalavqeei sqrveqaasl
      421 rdkqlqrary eaelarrryl kvdpdnrlva daleadwngk lrdldtlqre herqnetdqs
      481 lldgamqeri ralaadfpri wnnkrtspve rkrmlgllie dvtllvdeqi nmhirwrggr
      541 tqslavarpr pmavirktpe avvalinell etdndqqias rlnalghrnw rgeaftlkkv
      601 mlvrrayglk trferlresg mltgeevarr fgvsattvhq lgrdgvlkrh ryatnhryly
      661 eppgnvrlak gvggrygsrq prlidaqqiq qgas
//
LOCUS       WP_457662553             381 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457662553
VERSION     WP_457662553.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..381
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39929
     Region          10..378
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,137,
                     140..141,144,212,215..216,219..221,224,252,256,306..307,
                     311,315,331,334..335,338..339,342)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mrvpklitpw rsiaagflin gvlfgtwagh iarvkdqfgl sdqnlsklll llglgallsf
       61 sfagrlcdsm gapritraaa callvatvfl gfaqtvqqlg lslflfgmch glldvainkw
      121 gsevekhmer svmssfhamf slgaglgaan gyvaavnhdq mntdflitav ltggilgpfl
      181 lldwqstvlk nvkgavelal prgalllvgl iafssglgeg mvahwgsvhl kevfktmees
      241 ailgyvvfca amvsirltvd slvtrlgpvm vtrlsgvsat cgislvlags seplvslvgf
      301 vlmgvgyaai mplafkwaat yhvvppgqai atvatfayga mtlgppafgw lsealspkyg
      361 mcivgifaml vavlapaleh k
//
LOCUS       WP_457662560             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662560
VERSION     WP_457662560.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27271
     Region          15..195
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 myrhhedklg wdqilankvf kalkklvveg qvppdtrlgi rlisdglkts vtpvrealih
       61 leaeryivgs prngyytikl dtqhisdqyg vtkiilqdvf rgspdelqrr lpvlqtipsw
      121 ddprsvsefl esfcervaet tnneimadlv hesnirtryv rwldlqrper lscirvdmse
      181 llelldkrdk neaianvdrq fsaiintvpe lvlegnyrag ntkeswletl lsnwaes
//
LOCUS       WP_457662561             340 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457662561
VERSION     WP_457662561.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 340)
  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   2  (residues 1 to 340)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..340
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36774
     Region          3..334
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mgsrvrlsdv akragvgvgt vsrvlnrsak vsaitrkkvl daiaelgyrp nlvarslaan
       61 rtgliaaiip eigytqhsei ilgmtdvlha nemnlmigtc gysdegelkv ieallsrrpd
      121 aiyvtgvrht eavrtalers gipvvegtnl tdhpidtvvg ysnfnasadl trllidhgyr
      181 hiwhvtvnkd fscrsddrlk gfqwatstea glevnvirce nsfdggaeav rlvtapgvkv
      241 ealtfttdvm avggllecqr rgiavperla iagfddltia rsinpppltt vkvdrvglgr
      301 kaaeiivsrl kgndhysrvv dvgfevvere strrsdrgah
//
LOCUS       WP_457662578             410 aa            linear   BCT 27-JAN-2026
DEFINITION  group II intron reverse transcriptase [Sinorhizobium medicae].
ACCESSION   WP_457662578
VERSION     WP_457662578.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20045434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..410
                     /product="group II intron reverse transcriptase"
                     /EC_number="2.7.7.49"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46979
     Region          <8..262
                     /region_name="ps-ssRNAv_RdRp-like"
                     /note="conserved catalytic core domain of RNA-dependent
                     RNA polymerase (RdRp) from the positive-sense
                     single-stranded RNA [(+)ssRNA] viruses and closely related
                     viruses; cl40470"
                     /db_xref="CDD:477363"
     Site            order(33..38,82..83,121,123..124,170..171)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238828"
     Site            order(33..38,82,123)
                     /site_type="other"
                     /note="putative NTP binding site [chemical binding]"
                     /db_xref="CDD:238828"
     Site            83
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238828"
     Region          326..395
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mgsgqdggch daiariynva tpvrrrkwvl dadikgafdn idhefllkav gdfparelir
       61 qwlkagymer gvfhdtdsgt pqggvispll anialhgmea avgvkyisrg dnvgkrclir
      121 yaddfvvfce seedarnars dlsvwlssrg lalsdektri shlsdgfdfl gfnirqyrap
      181 esrwgwklli kpsrksvksl karmvrewrg mdgqniitvl trlnpiirgw snyyrsvvsk
      241 rlfaqldswn fgkevrwark ahpkkpwywv rrkywgklhp krmdywvfgd aageggrlik
      301 fawtpivrhi lvkggaspdd ptlqdywkwr rsrhhvelsg rqqalakeqg gvcfrcgetl
      361 hndealcahh iraprlggkr tldnqrlmhl ychlqalaae kserdskrfa
//
LOCUS       WP_457662579             223 aa            linear   BCT 27-JAN-2026
DEFINITION  ArdC family protein [Sinorhizobium medicae].
ACCESSION   WP_457662579
VERSION     WP_457662579.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Gonzalez-Montes,L., Del Campo,I., Garcillan-Barcia,M.P., de la
            Cruz,F. and Moncalian,G.
  TITLE     ArdC, a ssDNA-binding protein with a metalloprotease domain,
            overpasses the recipient hsdRMS restriction system broadening
            conjugation host range
  JOURNAL   PLoS Genet 16 (4), e1008750 (2020)
   PUBMED   32348296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Belogurov,A.A., Delver,E.P., Agafonova,O.V., Belogurova,N.G.,
            Lee,L.Y. and Kado,C.I.
  TITLE     Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa
            has a high similarity to the 'protein transport' domain of TraC1
            primase of promiscuous plasmid RP4
  JOURNAL   J Mol Biol 296 (4), 969-977 (2000)
   PUBMED   10686096
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..223
                     /product="ArdC family protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24146
     Region          <35..222
                     /region_name="ArdC"
                     /note="Antirestriction protein ArdC [Replication,
                     recombination and repair]; COG4227"
                     /db_xref="CDD:443371"
ORIGIN      
        1 mngtasglle pcagklastv lrgrgsgdaa llpdqelggn vrkgekgtlv vyanaierte
       61 tdeegeever ripfmkgygv fnadqidglp qhfsavesep tngegiqrid aadrffanlg
      121 adirhggnra fyhaagdfiq mppfkafvsa ethagtlahe cihwtmnstr lnrnldrqkw
      181 gdegyareel vaelgsvfls adlgiaiepr edhaayiasw lks
//
LOCUS       WP_457662584             470 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457662584
VERSION     WP_457662584.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..470
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51601
     Region          8..470
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mqvssagfle svdqnfrham sfldlpagla eriiqcnsty tvrfgvrlrg rmysfigwrs
       61 vhsehcepvk ggiryaynad aeevealaal mtlkcslvdv pfggskgalk idprewtpqe
      121 leritrrftq elnkrgligp gvnvpapdig tgeremawmm defrranptd vvnaracvtg
      181 kplskggiag rteatgrgvq faiqsylrdt rtqgldgrrd lngaavtvqg fgnvgyhaak
      241 flseedgarv tvvaerdgyv anpegvsiea lkqhqirtgs vlgfegansf agdmtgieqr
      301 cdvlipaame ntihadnaer ikahliveaa ngpvtfeadk ilrscgitil pdlyvnaggv
      361 vasyfewvkn lthipfglme rrrrerrnqt iaaalermtg kefpadirde fleggaeidl
      421 vrsgledvmr stwvrigdli ekqpelgdyr ttayvasirq iaeayeaigi
//
LOCUS       WP_457662586             394 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl-CoA C-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457662586
VERSION     WP_457662586.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 394)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41131
     Region          4..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mstpsivias aartavgsfk gafantpahe mgaavikgvl eragveaqev devilgqvlp
       61 agegqnparq aamkagipqe atawgvnqic gsgfrtvalg lqqiitgdak vivaggqesm
      121 smaphcahlr ngtkmgdmkm idtmikdglt dafhgyhmgi taeniarqfk ltreeqdqfa
      181 lasqnkaeaa qkagrfadei ipfivkrrkg ditvdqdeyt rhgatldsmt krhpafdkeg
      241 tvtagnasgi ndgaaatllm tgqdairrsi qpplapivsw atagvdpkim gtgpipasrk
      301 slekagwkis dldlveanea faaqacavnk dlgwnpdivn vnggataigr pigasgarvl
      361 ntllfemkrr gakkglstlc igggmgiamc veam
//
LOCUS       WP_457662591             393 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457662591
VERSION     WP_457662591.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43784
     Region          18..392
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mseeklrfdl seyqarldka rrsmdhagld llvvtdpanm gwltgydgcs yyvpqcvvvs
       61 kdkdpmwfgr rmdangcrrt ayigedrikw ygdeyvqsdt lhamsllgqi iqdegygact
      121 igvekdswcl sassfehlsk slpnakfkna drlinwqrlv kspreieymr gagkiveamy
      181 drigqvlrpg akqsdviael syvgtrgvds wwgdypacvp nlgagadasa phltwtdrpi
      241 radesiffel agvhkryhcp lsrtyylgkp tqqildaeka vlegvqagle kavagnrced
      301 iaiaysgala rygfektsrs gypigmgypp awgensasfr agdktelqpg mtfhfmsglw
      361 ygdwgieite silitdgdve flsnvprrll vid
//
LOCUS       WP_457662594             164 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662594
VERSION     WP_457662594.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..164
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18844
     Region          3..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mteldpmdia llqavqknnr ltseelaeiv hlsptacqrr lrrlrtegvi esdvsivspk
       61 avgrhitmiv lvslererad ivdrfktair ntrevmigyy vtgeadfmlv vtardmegye
      121 qftrrffyen adikgfktmv vmdrvkasfa fpieaqhrds srhy
//
LOCUS       WP_457662595             204 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662595
VERSION     WP_457662595.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..204
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22434
     Region          43..175
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mktvrstety cppitdedwp tciadmksgf agalnvyrtm ahnpallkaw apirqhivkd
       61 stlgpirsei vilrsahrmg styewahhvs raralgisdk rirdicgtpe gedgliarav
      121 dalfdlsrlp pdvetelaal mgrqavfdli atvgfysilg yivmtygtpi dgevamqlsd
      181 hpleqaancd stfvsssriy hrdk
//
LOCUS       WP_457662596             294 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662596
VERSION     WP_457662596.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..294
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32107
     Region          1..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlqqgplhar iverfdemse qlqqaarhil ehpqevalvs mrelarnagv qpstmtrlak
       61 flgfpgyedl rgeyadvirv ntdgfaaral qrqeggange glayrmlqgl saqiarlcep
      121 ntllqlgama erlgkarriy vlglrschsv awhfhyvmtl lgektvhldg pagtsgdali
      181 rassddvlla isinpyalqt lelaeaarek gmeivaitds qvsplvtiak hvvlfptesq
      241 tffhtltpal avsevlcgll asqdrsaale elkradqhls smntyaasip rrki
//
LOCUS       WP_457662600             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662600
VERSION     WP_457662600.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44093
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          327..403
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mpkralilie gskgngplyv qaaqrlglhp itlatdpaqy nylaaegsea irvdtsdlea
       61 lirecarlla iydiagitgf pgleeslyvt vgklcrhfal pgpdpasieq ccdkfvqrql
      121 laqagvpmpa yrlaanardv agaaaeiglp vivkpavgsg ssgvrlcrta devadhaayl
      181 fggtyvwqsa prilveefaq gplystdtmg kaviaaglad fngpphfvpc gsmfpapltd
      241 deharivdvs lsclqalglg wgptniefrw trhgpvviev nprlpgwttp rlihlaygid
      301 linehiklvi geecdlrarh srtaaaqflv pdrdgilnri egtsraaavp gvvdvrfyva
      361 pdtpilrkgd yqdmighvia tstspartka ilrravdlis wsitpfpald e
//
LOCUS       WP_457662603             411 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662603
VERSION     WP_457662603.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..411
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44500
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          329..404
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 makralilie gsrgngplyv qaaqrlglhp itlttdpaqy dylaaegsea irvdtndlea
       61 lirecarlrl tydiagitgf pspdetlyat igklcryfdl pgpnpasier ccdkfaqrql
      121 laqagvpipa yrlaanaiev eraaaeiglp vivkpaegig ssgvrlcrdv selaehtthl
      181 lggkhiwrss pqilveefaq gpyycahttg nevvgiasad fgppphfvfr qtifpapltd
      241 eeyiniadvs lsclqalglg wgptniefrw tkrgpvviev nprlagapds qliqlsygvd
      301 linehiklvi gdkcdlrkrh shtaaarnlv pdrdgtldwi kgtslaaavp gvvdvrffva
      361 petpivrrgv yldcigyvia aspsraqtea ilqravdlis wsiapfpald e
//
LOCUS       WP_457662604             126 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662604
VERSION     WP_457662604.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
REFERENCE   3  (residues 1 to 126)
  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..126
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..126
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14151
     Region          34..90
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 mlaprflrcl srnkspsptl sylrtqecgg pmdlrhlrcv vvaarntnfn aaghelnvrq
       61 piiskrirel edelgvflfd raisgarltp krngcrrahq fslfsrtptp larcapqtdt
      121 snypmq
//
LOCUS       WP_457662608             252 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662608
VERSION     WP_457662608.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..252
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28288
     Region          84..248
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mtteseiara fdifirqmse gksvdqmvkn isvfarifkc ssiaygpqts vrnmqikcki
       61 klptlptilt ypeewqehcl kngydrlaps irmghsqssp llwddaykdp nttdrerrif
      121 deakelglet gvtiplpgrl gnfptmsfvq sersglseta vsylkfaaqa fhekvegcvd
      181 wkagfpslta retecigwva kektswaiai ilgitshtvd fhiknvlkkw glesrkdaam
      241 laehlglidp qf
//
LOCUS       WP_457662609             230 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457662609
VERSION     WP_457662609.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 230)
  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 230)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..230
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25603
     Region          6..211
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mnnrlilive hnealrssvd ehlshvgfri vcasdgavgl shfrrlkpdl vvlgdelprl
       61 dgfevlneir rysdtlvimt smwstpshel rcltlgadnl llkpydndvl terikkllrr
      121 ggggrahrir vgkliidpda qsacvdaptg ekelnltise ykllahmarf pgrvflrsdl
      181 idacfsgdgp lettlnthmc nlrakltdag igdylkcrrs vgyrlvdkrg
//
LOCUS       WP_457662610             368 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662610
VERSION     WP_457662610.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..368
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41379
     Region          23..135
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(41,44)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mvlrmespap vlevqdwvrg eplanfqpgk vyivdfwatw cgpclsvmps lmqlqekykg
       61 sgvevlavaa deeadtadev qayldawlte kfpqlnfrig idctgemhkl wmepsfsfgi
      121 pssfvvdrds riafighpae lddvlpkvld gswrtsdqae aadreriarg rervflskis
      181 aavkmedwtt alsvieeaid lmpdsiqlra ahadtllhkm rdmhtglpvl rqlvrdaidr
      241 naenwllgam nqlsnpaydy tgfpsverfa mgkelsehil alkelkddvk aysyqlvary
      301 yhesgnkara eellalalkl vdglyladni kqrwladllq tlanyrgqkv cyndmsavpe
      361 nhakskan
//
LOCUS       WP_457662612             408 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662612
VERSION     WP_457662612.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 408)
  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   4  (residues 1 to 408)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..408
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44100
     Region          57..313
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          327..403
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 maskalilie ghrsmgplyv raaqrrclnp itmstdptqy dylaaegvea vqvdtndlda
       61 mksvysrlkl thdiagltgf sgldasvyvt vgklcrhfgl pgpdpasikq chdkftqrql
      121 ledagvpipd yrvatnatev ksavaeiglp vvikpvvgsg ssgvqmcrtv devaehtkhl
      181 lggghmwqss prilveefaq gqyltadmmg gclvgigtsd igppphfvyr eysypallsn
      241 desariadds lsclralglg wgpaniefrw tkrgpvviev nprlagtpdp eliqlaygvd
      301 lvdehiklvi geecdlrarh srtasarflv pdrdgmlevi egasraaaip gvaevkmyvh
      361 pntpivrkgd yrdlighvia aspsrdqtea llqqavdlvs wtitpsrt
//
LOCUS       WP_457662622             521 aa            linear   BCT 27-JAN-2026
DEFINITION  integrase catalytic domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662622
VERSION     WP_457662622.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ballandras-Colas,A., Maskell,D.P., Serrao,E., Locke,J., Swuec,P.,
            Jonsson,S.R., Kotecha,A., Cook,N.J., Pye,V.E., Taylor,I.A.,
            Andresdottir,V., Engelman,A.N., Costa,A. and Cherepanov,P.
  TITLE     A supramolecular assembly mediates lentiviral DNA integration
  JOURNAL   Science 355 (6320), 93-95 (2017)
   PUBMED   28059770
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (5), 302-307 (2001)
   PUBMED   11774877
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and
            Davies,D.R.
  TITLE     Crystal structure of the catalytic domain of HIV-1 integrase:
            similarity to other polynucleotidyl transferases
  JOURNAL   Science 266 (5193), 1981-1986 (1994)
   PUBMED   7801124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10461024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..521
                     /product="integrase catalytic domain-containing protein"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016893 - obsolete endonuclease activity,
                     active with either ribo- or deoxyribonucleic acids and
                     producing 5'-phosphomonoesters [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=58373
     Region          162..257
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 matrteliea iieryrsscr adkhrildef vavtgyhrkh airvlrhrgs eppparqhav
       61 qygpdvreal valweasdrl cskrlkplip illpalerhg rlelnsalrd kllmvsaatm
      121 drllsevrvv arggqrrrag mssavrrsvp vrtfgdwndp lpgyvevdfv ahsgtsssgs
      181 faqtmvltdi atgwtecvpv rtresglvia aikqarsqfp fpllgvdfdn dsafmnelvv
      241 cwcrsqglev trsrayrknd qawveqknga ivrrlvgygr fvgaeattal arlyevvrlh
      301 gnlfqpsfkl rektrigarv ikryhppvpp varvlahsgv aeadkdrlqa mlesadpvil
      361 faairaaqee lgrrvdrrgl narseepvav dlqrftlslk tawqvgekrp thrrpyrrtk
      421 pypkrqsmle pfepqirawl eadpavsaas vlerlmsadp srftkkslrt vqmavkawri
      481 etagqiildg dwmeratlss haaagedngh lsaqrfgnip g
//
LOCUS       WP_457662636             270 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Sinorhizobium medicae].
ACCESSION   WP_457662636
VERSION     WP_457662636.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..270
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=30102
     Region          32..268
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mkqlkgnfvl psvateksfd asycsdnppp vvisafadgr yagnpaavaf ydrfpkasec
       61 ldlakrlrqp vtaflrplre sghyqirwft qnveldlcgh atlaatywlf hcglnetdrv
      121 vyhsrsgply awleddivkl slpaiemspa nsadyeavqr cmgvrakeiw kayddyvvvv
      181 dgeaivldfq pdierirqie crgialssav dpigalqefd ivsrffspri ainedevcvs
      241 ahcklypywa kvtgkkhlra lqashrgggp
//
LOCUS       WP_457662640             392 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457662640
VERSION     WP_457662640.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10315023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..392
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=43377
     Region          100..182
                     /region_name="Phage_int_SAM_1"
                     /note="Phage integrase, N-terminal SAM-like domain;
                     cl12235"
                     /db_xref="CDD:472283"
     Region          209..385
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(242,337,340..341,372)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 masyivpfae wlgdrgyglv smrnqvlmaa gfskwlghkg ielsdisgdh arrylldraq
       61 rpklgdaaal rhllaflrsq naiaeeiead hnpspveqhv qayewylrda ralaretiin
      121 yrpvvrefln yrfgdgevsl aqlraddvtk fvpqkvsrln lrrakittta lrsflsyarf
      181 rgdvtsdlaa avpivanwsl ssipraigrd evsrllasid rdtpigcrdy amilalarlg
      241 lrssevvtle lddidwvage ihvvgkngqr ndlplpadvg eaiadylrks rprnasrrvf
      301 lrdkapirgf tgqcglgsvi rrslkragid aptmgthqfr hglasemlrg gaslgeigev
      361 lghrhvqtta iyakvdldal rtlalpwpge aq
//
LOCUS       WP_457662642             332 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457662642
VERSION     WP_457662642.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10315017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..332
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=37547
     Region          15..100
                     /region_name="Phage_int_SAM_1"
                     /note="Phage integrase, N-terminal SAM-like domain;
                     cl12235"
                     /db_xref="CDD:472283"
     Region          127..309
                     /region_name="INT_RitC_C_like"
                     /note="C-terminal catalytic domain of recombinase RitC, a
                     component of the recombinase trio; cd01182"
                     /db_xref="CDD:271183"
     Site            order(162,259,262..263,294)
                     /site_type="active"
                     /db_xref="CDD:271183"
ORIGIN      
        1 mtkhaslapl lerffiqrlm qqrqasphti ssyrdtfrql lkfaartlhk ppsrlnfeev
       61 daplilafld dlenrqgisv rsrnlrltai hsffryaafe apehsaqiqr vlaipskrft
      121 rtlvnfltrp evdallaapd qstwsgrrdh afllvavqtg lrlseitglk rddlffgtga
      181 hlrvigkgrk erctsfakst tavlrnwlke pqrgdqgilf psargerlsv hgvqymlnkh
      241 rqtasaicls lkgkrvtvhr lrhtmamdll qagvdravia lwlghesvet tqiyleatla
      301 mkeaalaktp pysgkssrfr pddsllefln rl
//
LOCUS       WP_457662644             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662644
VERSION     WP_457662644.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35975
     Region          2..322
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mlltvnnlsi eiatsagklk vvqgvsfdis kgetlcivge sgcgksital slmgllpkaa
       61 rpsaeellfd gidlqkinsk dlralrgnri smifqepmts lnplhtigrq lsdvyrahrq
      121 atrkeaeara vhllqevgis naaqrllqyp helsgglrqr iviamalmce pdlviadept
      181 taldvtiqae llrllkdlqk rfgmgiimit hdlglvsria drvivmyagq vvesaparql
      241 fdrpahpytr allgsvpdps harmqplpsi pgnvpslltp mdgchfydrc syaseacrrq
      301 inlrevsdqh qarcimvdet saplrvmk
//
LOCUS       WP_457662647             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662647
VERSION     WP_457662647.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29611
     Region          9..262
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mfsyrkptpl awvgigivtm filiaifapv vapfneaetv gdtwtgmsah hllgtdnigr
       61 dmlsrliyga rmtigvtlvt tvlsfgigtl aglfasisgp widqalsrfv dvmlsipllv
      121 falvvlsvfg ssistlilti aildstrvfr vsravasnia vmeyveaarl rgegtwwvmr
      181 reilpnalpp miaefgmrfc fnllfvagls flglgiqpph adwggmvrdn skaisfglpa
      241 plwpaaaial mtigvnlvvd wllsinarps gasaem
//
LOCUS       WP_457662650             451 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457662650
VERSION     WP_457662650.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..451
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49446
     Region          3..451
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msfldlpegl aeriiqcnst ytvrfgvrlr grmhsfigwr svhsehcepv kggiryasna
       61 daeevealaa lmtlkcslvd vpfggskgal kidprewtpq eleritrrft qelnkrglig
      121 pgvnvpapdi gtgeremawm mdefrranpt dvvnaracvt gkplskggia grteatgrgv
      181 qfaiqsflrd trtagldgrr dlkgvsvivq gfgnvgyhaa kflseedgar vtvvaerdgy
      241 vanteglpie alkqhqirtg silgfegaks fagdmtgidq pcdvlipaam enaihvenae
      301 rikarlvvea andpvtfead kilrsrgvti lpdlyvnagg vvvsyfewvk nlthipfglm
      361 errrrerrnq tiatalermt gkefpadird efleggaeid lvrsgledvm rstwarigdl
      421 lekqpeigdy rtaayvasig qiaeayeaig i
//
LOCUS       WP_457662652             470 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662652
VERSION     WP_457662652.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..470
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50423
     Region          6..328
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mklnsakiqv dltdalerhr vagasiailh egalamaaag yanistgvgl ttdtmmhigs
       61 itkvlnatlv iqlvdeglld levpvsqylp dfrvkdpsat eeitvkmlin htsgidgdtt
      121 idhghdeetv ekavarmsty sqifppgadc sysnaatvva ghlaarvtgv swyeliknri
      181 fkplnmrcsv vlpedvllar asmghfldwq tnrhirssha flplgfapag htammspsdl
      241 vifaqmhlsn glgpdgspml saesarlmre tttpgigrmp ygvglgwmty gngvvghggg
      301 gpgvvgrlya sprhqfaiai ltnsdngdsl iedfaapylq evcgfeiphs sasdvlpnat
      361 idnanyvgcf edswmsytia eksdglvlst rtkiaiydvi steptdsavm lpvgddqfvv
      421 kptdqqrnan reafpqagdv litfrnkdsl grpqhlasgs rlyrrageql
//
LOCUS       WP_457662659             542 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662659
VERSION     WP_457662659.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..542
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59282
     Region          1..533
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtdtilsvrd lsvafhqgge tslavdrisf dikrgetval vgesgsgksv sansilrllp
       61 ypaashpsge ivfngkdllk vgedelrhvr gndvtmifqe pmtslnplht ieqqigeile
      121 ihqnlkgaaa rartlelldq vgireaekrl gayphqlsgg qrqrvmiama lanrpallia
      181 depttaldvt vqaqilellk slkdehgmsm lfithdlgiv rkiadrvcvm tkgkivetgp
      241 taeifanpqh dytrhllase prgepppsdt sspivveasg mkvwfpikag flrrvvdhvk
      301 avdgidltlr agqtlgvvge sgsgkttlgl altrlisskg riafvgenid ahsfremrpl
      361 rnrmqvvfqd pygslsprms iadiigeglk ihekaltdne rdgrvaaale evgldpatrw
      421 ryphefsggq rqriaiaram vlkpqfvmld eptsaldmsv qaqvvdllrd lqrkhnlayl
      481 fishdlrvvr alanevivmr lgkvveqgpa erifdapaed ytralmaaaf nleavnlaav
      541 hq
//
LOCUS       WP_457662661             254 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Sinorhizobium medicae].
ACCESSION   WP_457662661
VERSION     WP_457662661.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..254
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25212
     Region          71..174
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mnpyvnmgvg allgtvfvlm tvsiasegif hseapekegf aivaeetage agaaggeeak
       61 sepigpllas adapageavf kkcaschtve kggpnkvgpn lwdivnrpia shegfsysag
      121 mqtfseggkv vwdydhlsyf leapkkhvpg tamgfaglkk tderanliaw lrehsdnpap
      181 lpeagagste aapaegqapa aaegnaapap aegtsapadt aapppaegga apapavgeta
      241 pagqtgapap apan
//
LOCUS       WP_457662666             326 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I NDUFA9 subunit family protein [Sinorhizobium medicae].
ACCESSION   WP_457662666
VERSION     WP_457662666.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  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 326)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=34729
     Region          10..279
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(14,16..19,38..40,82..84,97,119..121,132,136,
                     155..158)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(132,136)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mtlsnlpplv tifggsgfvg rhvvralakr gyrirvavrr pdlaghlqpl gnvgqisfvq
       61 anlryrnsvd ravdgadhvi ncvgvlfeng rntfdavqdf garavaeaag atgatlthis
      121 aigadarsds syartkgrae aaileilpta vilrpsiifg pedgffnkfa emarfspvlp
      181 ligggntrfq pvyvtdvaea varsvdgkla ggtiyelggp qvlsfrecld imlktidrkr
      241 sfvslpfgia slmgsvaslv pfieppltad qvvllksdnv vsamaetegr tfagigiept
      301 mlesilptyl vryrphgqyt rtgraa
//
LOCUS       WP_457662667             761 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent malic enzyme [Sinorhizobium medicae].
ACCESSION   WP_457662667
VERSION     WP_457662667.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Bologna,F.P., Andreo,C.S. and Drincovich,M.F.
  TITLE     Escherichia coli malic enzymes: two isoforms with substantial
            differences in kinetic properties, metabolic regulation, and
            structure
  JOURNAL   J Bacteriol 189 (16), 5937-5946 (2007)
   PUBMED   17557829
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Voegele,R.T., Mitsch,M.J. and Finan,T.M.
  TITLE     Characterization of two members of a novel malic enzyme class
  JOURNAL   Biochim Biophys Acta 1432 (2), 275-285 (1999)
   PUBMED   10407149
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Yamaguchi,M.
  TITLE     Studies on regulatory functions of malic enzymes. IV. Effects of
            sulfhydryl group modification on the catalytic function of
            NAD-linked malic enzyme from Escherichia coli
  JOURNAL   J Biochem 86 (2), 325-333 (1979)
   PUBMED   225306
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..761
                     /product="NADP-dependent malic enzyme"
                     /EC_number="1.1.1.40"
                     /GO_function="GO:0004470 - malic enzyme activity [Evidence
                     IEA]"
                     /GO_function="GO:0004471 - malate dehydrogenase
                     (decarboxylating) (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=82155
     Region          13..761
                     /region_name="PRK07232"
                     /note="bifunctional malic enzyme
                     oxidoreductase/phosphotransacetylase; Reviewed"
                     /db_xref="CDD:235976"
ORIGIN      
        1 mpgidrsdra mtsvtaqeal dfhsqgrpgk leisptkpma tqrdlslays pgvavpvkai
       61 aedpataydy targnmvavi sngtailglg nlgalaskpv megkavlfkr fadvdsidle
      121 vdtddvdefv ncvrflgpsf gginledika pdcfiieqrl revmdipvfh ddqhgtaiia
      181 aaglinaltl tgrdfkstkl vcngagaaai acieliksmg fnpaniilcd tkgviykgrt
      241 dgmnqwksah avetdrrtla ealdgadvff glsakgalsa dmvrsmgerp iifamanpdp
      301 eitpeevadi rndaivatgr sdypnqvnnv lgfpyifrga ldvrastind amkiaaaeal
      361 anlakedvpd dvaaayqgnr prfgpqyiip vpfdprlisa ipmavakaam etgvarkpie
      421 dlkaygeqls arrdpiastl qrivervrrq pkrivfaege evqmmrsaia yanqqlgtal
      481 llgreevmre taeregidld ragiqivnar lskrvgaytd flysrlqrkg ylfrdvqrli
      541 ntdrnhfaas mvalgdadgm vtgltrnyst aledvrrcid pkpghrvigv sialcrgrtv
      601 lvadtavhdm ptteeladia eeaaglakrl gyvprvamla ystfghpsge rservreavk
      661 ildrrrvdfe ydgemaadva lnarvmeqyp fcrlsgtanv lvmpafhsas istkmlqelg
      721 gstvigpllv gldksvqias msakdsdlvn laaiaaynag t
//
LOCUS       WP_457662668             650 aa            linear   BCT 27-JAN-2026
DEFINITION  CHASE2 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662668
VERSION     WP_457662668.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 650)
  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 650)
  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..650
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..650
                     /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=69421
     Region          33..613
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkasrqlrls srraklaala alvaalvslv sltgswslvd lraydylsil grpslpedgp
       61 vivaidepsm aeigsqwpwp ralharliqs lraagarava ldvifaepaa apendralae
      121 vlgpdvvlag detlirtpqa eqfvrteplp vflergakvg vasvtlsgdg ilrqipsysd
      181 gfattiasva gadlarppgr almqtfgpar typtvsyyqa ldpeaflpeg tfrdrivivg
      241 lslqnapsia gggidafats dtvfsrgrva gaeihatiyd nlvhrlfveq agvtvaiaai
      301 ilatlaasla vlrstswktl gygalalasi flasyalmrl ghvfvsplap alafvgvavg
      361 qagldyaeer rrrreitsaf sqylspalve rlasdpsqlk lggerrtltv lfcdvrgftt
      421 isedmkddpe glttlinrll tplseavlnr rgtidkyigd clmafwnapl ddpdhavhav
      481 qaardmlaal aklnaeleae akaagrppkt lrigigintg ecvvgnmgsa rrfdysalgd
      541 avnlasrleg asknygvpll lgertaalaa sefpvaeldr itvkgrsavs pvftvvegas
      601 eaelarhrty larkydgdlp adndlldelk salpplrryy ererekfrag
//
LOCUS       WP_457662672             471 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome ubiquinol oxidase subunit I [Sinorhizobium medicae].
ACCESSION   WP_457662672
VERSION     WP_457662672.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..471
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51334
     Region          5..447
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mfesfdatvl ariqfaftvs fhiifpafsi glasylavle alwlwkkdev ylelfnfwkt
       61 ifavafgmgv vsgivmsyqf gtnwsvfsdk agpvigplmg yevltaffle agflgvmlfg
      121 lnrvgpklhf fatamvalgt lisgtwilav nswmqtpagf svneagqfip ddwwavifnp
      181 sfpyrlvhmv laaylttafv vgacgawhll rktaprrart mfsmamwmaa ivapiqifag
      241 dqhglntleh qpakvmameg hyqshpdgap lilfgipnsa ekridyalei pklsslilkh
      301 sldaplagld tipeerhppv aivfwsfrvm vaigfamlgl glwslwcrvr gtldsnaalh
      361 rtavlmgpag fvavlagwit tevgrqpyti yghlltadsi spieapavaa slvafiivyf
      421 lvfgagtfyi lrlmarlprd tmpeldegpl rtagvtpgpa spkapggqhg l
//
LOCUS       WP_457662676             380 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662676
VERSION     WP_457662676.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..380
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41579
     Region          19..380
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkslgsirrs fapwadpask pfisfknvtk kfgdftavdd lslniytref fallgasgcg
       61 kstllrmlag feqptsgeii ldgqsltgip pyrrpvnmmf qsyalfphmt vennvafglk
      121 qdripkadia ervaqmlklv klekfakrkp hqlsggqrqr valarslakr pkvllldepl
      181 galdkklree tqfelmdlqq elgltfvvvt hdqeeamtma driavmshgk vvqvatpaei
      241 yeapnsrfva dfigdvnifd gsvtsagdgy vviettgais vrmasaekpa kgaraavair
      301 pekirlsrqa pahaptnaae geiwdigylg dmtvfhirlk dgkvikassl navravedpl
      361 gydqqvwvsf gedagvvlkd
//
LOCUS       WP_457662679             254 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF899 domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662679
VERSION     WP_457662679.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28964
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtahatgtre ewlaarvdll aaekdltrrs delarwrrel pwvridqayr fetdegeasl
       61 rdlfkgrsql lvyhfmfgpd ytagcpscsa iadgfngivp hlenhdlafy avsraplakl
      121 taykqrlgws fpwaasndge fnrdfcvwft eqqqregaie ynfrreppll epgesrgpaa
      181 eiaamagtdv atftrdrpgv safvledgiv yhtyssyarg ldglwgmyqw ldrapkgrne
      241 ngiwwrrhde yarg
//
LOCUS       WP_457662677             560 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662677
VERSION     WP_457662677.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 560)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..560
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60159
     Region          13..559
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mhfttktlrq ryarsgtglh hplltgwagl asivvlmpil siawlaisgg sadwphlien
       61 vvpratgrtl llvlftctas aiigilaawl vatyefplrr ilsaalvlpl aipaylsaya
      121 fgelltfagp vqglvrslfg fqtsrdywfp dvrslggavl vlssvlypyv ylacrsmflm
      181 qgraaadvar tlgagpvrvf frvqlpmarp aimigltlva metlndigav eflgvqtltf
      241 sifntwlnrg slagaaqiac vmlvfvialm mieraarrrq rfasqkttaa ihdvarlkls
      301 gwkkwaataa cfvpilsgfa vpflvlgdya mrrldqflap rllsalansv lvsgltalat
      361 vllgfvlaya arsgrsritd iaarlasfgy gvpgtvlaig vlfpiaaldn aidaqmraff
      421 gistgllmtg tgfaivyact vrfltmaegt lgagfqklsp hldmaaralg rtsgqtlrsv
      481 llpmmrpavl taallvfiet mkelsatiml rpfnfntlat lvyedasrar vedasvaami
      541 iviagmvpvi lvsrslerrt
//
LOCUS       WP_457662681             391 aa            linear   BCT 27-JAN-2026
DEFINITION  cell wall hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457662681
VERSION     WP_457662681.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Bagyan,I. and Setlow,P.
  TITLE     Localization of the cortex lytic enzyme CwlJ in spores of Bacillus
            subtilis
  JOURNAL   J Bacteriol 184 (4), 1219-1224 (2002)
   PUBMED   11807087
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ishikawa,S., Yamane,K. and Sekiguchi,J.
  TITLE     Regulation and characterization of a newly deduced cell wall
            hydrolase gene (cwlJ) which affects germination of Bacillus
            subtilis spores
  JOURNAL   J Bacteriol 180 (6), 1375-1380 (1998)
   PUBMED   9515903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="cell wall hydrolase"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42956
     Region          254..386
                     /region_name="CwlJ"
                     /note="Cell wall hydrolase CwlJ, involved in spore
                     germination [Cell cycle control, cell division, chromosome
                     partitioning, Cell wall/membrane/envelope biogenesis];
                     COG3773"
                     /db_xref="CDD:442987"
ORIGIN      
        1 mrkgikfpgk frltfsrwra pamiglaifl gfpsaaaysd iatflsginr ggerwrtylt
       61 qspagslhev emvftdpvtt galdggagmt lpdggrvavt aeskhhgtpd edrvtrklkk
      121 krivavtpat ppkdfsagsi lertsslmvp sldgsekmif akpkikgkei viatafyrka
      181 ppkpepgisp mlaklvtndk pdilatayvr pepdyaresp fdsilrdden agrfipeiap
      241 ddhawaatal pptvfskeeq tclaegiyfe argefvkgqa avaqvilnrv rnptypktic
      301 gvvyqnkawr nrcqfsfacd mirdliysrg hwktakeval avtsgkvwls evgsathyha
      361 tyvkpawakt mkrvgkiglh ifyrtygggw s
//
LOCUS       WP_457662684             399 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662684
VERSION     WP_457662684.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 399)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..399
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..399
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46260
     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 mtirlsnrda rriflakqgl saaphralgk dgllqlihei gfvqvdsiat verahhqilf
       61 srnqtyrreh laellekdge lfehwthdas iipstffvyw khrfkweset lrerwrkwrg
      121 dgfdascdet yeriaangav msrdlkeegh qsggwwnwhp sktalevlwr qgklaiarre
      181 nfqkvydlte rvipvrhyeg evaheefidw acrsalerlg fathgeiaaf wdlvspdeak
      241 gwvaahrdel cdivielang gkprpsyafa hfpdglgdip eppgrirvls pfdpllrdrn
      301 raerlfdffy rievfvpepk reygyyvfpl legdrligri dmkadrrggs ldvrrlwler
      361 gvrassgrme klmaeldrva rfagvekvkl leswnaals
//
LOCUS       WP_457662687             339 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Sinorhizobium medicae].
ACCESSION   WP_457662687
VERSION     WP_457662687.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..339
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37589
     Region          22..203
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(25,27,112)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(58,111..112)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            110..112
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mnhieepakp mtevlegvel sivvpvfnee esvgplvtri rtamagflep welilvddgs
       61 tdrtlpnark elshqelrlk iielqknfgq taamqagida aagrlivtld gdlqndpadi
      121 phmvaaieer gldllvgwrq nrrdalilrk ipswcanlli gkitgvklhd ygcslkiyrg
      181 svikqvklmg emhrfipawv agvvpssrig empvthharh ygtskygisr tfrvvldlla
      241 vlflmrykar pghffgsigl aagglsalil fylaidkfil gndigtrpml ivgvmlflss
      301 iqlittgils emmarayfrd neptsyivrq tfvreppha
//
LOCUS       WP_457662690             572 aa            linear   BCT 27-JAN-2026
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662690
VERSION     WP_457662690.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 572)
  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 572)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..572
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=58004
     Region          408..554
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 miknkaswva lgvlaiatal mvfvvqpnlr esdkeavaqs gtggqparpa atdagsssav
       61 plgtaakqaa agspnqvass asdpatawvv pgfdvlrvep dgstvvagra qpntkleils
      121 gdavvgtadv gaggdfaavf dkplptgdhq ltlrsvgsag qsksseevat vsvpkdasgq
      181 llamvsrqgk asrlittpda epkpvqeava tgmapsgetg gasdtsaapa tvpglqvtav
      241 eiegsmmyva gnakpgalvr iyandqllge veaddkghfv vdgpielsig shiiradmmn
      301 edaskvamra svpfdrpega qvaaiagttl gaptagldrl kaeagkaltl lkglfsggkq
      361 psteqlaaar satefalqsl aefkpadtsd palaaaaaea sdaastalaa lkaspqdaas
      421 vaaavekvdg algsaltrqn vstsvasaep lamptselsr taappaagda aapaaepaaa
      481 tglnaateqp etieqaplke sktsviirrg dtlwqisrrv ygaglrytti ylanreqien
      541 pdlirpgqvf gvpdemltee esreihrkhm rh
//
LOCUS       WP_457662692             371 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662692
VERSION     WP_457662692.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..371
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40287
     Region          53..319
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(60,190,253,278,280)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 mneafqrdci eiladkvkrg emtrrrfaql aamlvagapl alrtggaaaq akqlvfvnwg
       61 gdaitaydka ygqpfleeag itvrqdgsgp tegaitaqfk sgapswdivd adpfsaitlg
      121 kqgmieeidy svvdknkmrp gfgwdyaass yffsyviayd sekygdnppk gmadffdvka
      181 fpgkrslykw gsaiweaall gdgvapekly pldlkrahdk iaafkenvva ywgggsesqs
      241 llldgeasma liwstrasli eqdsggrikf iwdqgllspg amavikgnpg grdaamkfia
      301 saqdpqkqlv mfdllrqgpa npaadalipe eqkrqnsvdp anmskqipln mewyaehygp
      361 alneftkivs a
//
LOCUS       WP_457662694             289 aa            linear   BCT 27-JAN-2026
DEFINITION  23S rRNA (adenine(2030)-N(6))-methyltransferase RlmJ [Sinorhizobium
            medicae].
ACCESSION   WP_457662694
VERSION     WP_457662694.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Punekar,A.S., Liljeruhm,J., Shepherd,T.R., Forster,A.C. and
            Selmer,M.
  TITLE     Structural and functional insights into the molecular mechanism of
            rRNA m6A methyltransferase RlmJ
  JOURNAL   Nucleic Acids Res 41 (20), 9537-9548 (2013)
   PUBMED   23945937
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..289
                     /product="23S rRNA (adenine(2030)-N(6))-methyltransferase
                     RlmJ"
                     /EC_number="2.1.1.266"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008988 - rRNA
                     (adenine-N6-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0015976 - carbon utilization [Evidence
                     IEA]"
                     /GO_process="GO:0070475 - rRNA base methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=32424
     Region          1..280
                     /region_name="RlmJ"
                     /note="23S rRNA A2030 N6-methylase RlmJ [Translation,
                     ribosomal structure and biogenesis]; COG2961"
                     /db_xref="CDD:442201"
ORIGIN      
        1 mnyrhiyhag nfadvlkhav varlvtyleq kdkafrvldt hagiglydls seeaqktgew
       61 regigrliea elpapvaaml kpylsavrel npkgglafyp gspklvrmlf rpqdrlsame
      121 lhpedyealh rlfegdfqsr itlldgwlal gahlppkekr glvlvdppfe aegeydrlvd
      181 glakayrrfs ggifclwypl kkaapvkafh eslkaleipk mlcaelsvrs drettglsgs
      241 glvivnppft lkgeldillp ylksqlaqdr fasgrcfwlr geeplkrrp
//
LOCUS       WP_457662695             300 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457662695
VERSION     WP_457662695.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..300
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31625
     Region          10..278
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtpstdadrh rrglaitglg glalsfdipl irsadgevws ilavrslstf laalatwvvi
       61 nhllgrrval ipgkagliag llyginsftf llavfntsta nvvfilafts mfaailswif
      121 lkerpsnatf ltmgvilvgv gvivsdgles ghlfgdamaa csafllaaai tisrasgrdm
      181 slvplttaif paiagfmllp aggltiaepa yilfnglvmi plaffclatg prylsapevg
      241 mfylletila piwvwivfse tpssptllgg tililalvgh slwqirmraa rarlacevag
//
LOCUS       WP_457662698             367 aa            linear   BCT 27-JAN-2026
DEFINITION  COX15/CtaA family protein [Sinorhizobium medicae].
ACCESSION   WP_457662698
VERSION     WP_457662698.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..367
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=40847
     Region          27..347
                     /region_name="COX15-CtaA"
                     /note="Cytochrome oxidase assembly protein; pfam02628"
                     /db_xref="CDD:460629"
ORIGIN      
        1 mahaelateq tllreigrte rnrrhirrwl avvlfalfal vlvggatrlt esglsitewk
       61 pvhgvippls aqeweeefrl yqripqyeqi nkgmtvddfk tifwwewahr llargigvif
      121 alplfffwvt grverrlrlp llailalggl qgfigwwmvs sglaertavs qyrlathlti
      181 acvifaacmw iyrglcphsd dapptkasqk maaviaifsl fqiylgaiva gldaglsynt
      241 wplmdgaivp gglfvqqpaw inlfenpktv qfvhrlgayl llalvlwhmi aalrsapett
      301 harrsvllfa lvvvqaaigi ttlllqvpig wgvlhqggal vvlgfaiahw rgfvgaypkd
      361 taievra
//
LOCUS       WP_457662702             413 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662702
VERSION     WP_457662702.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..413
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43835
     Region          6..408
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mphdgivivg sghagaraaq slrangwqhr isvidgegca pyerpplska vlsgksrped
       61 avlfpqdfve qhgidfrsgv ravgidrdtr qvrlsnddav sygrllltpg aeprlldipg
      121 relegvfslr tavdacglsg qllpgadvvi vgggliglev aasaiqrgcs vtvieagprl
      181 mtravppela elirllhetr gvrfilgrqa vallgsqrie alrmddgstl actaalisig
      241 vtprtdlala aglelengia vdcflktsdp fiyaagdaca fkngdgsrlr lecwknaedq
      301 galaarnmmg anepytpmpw mwsdqydrtm qiaghpelge qhvarhcpdg sllvyhldan
      361 daivgvsgfg slreiargvr tgqmlmqrgi hpakealqnp kidlkaaakv aag
//
LOCUS       WP_457662707             341 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter substrate-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662707
VERSION     WP_457662707.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..341
                     /product="amino acid 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=36667
     Region          27..262
                     /region_name="PBP2_BztA"
                     /note="Substrate bindng domain of ABC
                     glutamate/glutamine/aspartate/asparagine transporter; the
                     type 2 periplasmic binding protein fold; cd13692"
                     /db_xref="CDD:270410"
     Site            order(41,44,88,103,110,154..155,196..197,226)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270410"
     Site            order(50,54,178,181)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270410"
ORIGIN      
        1 martiltalv saavvgvgsy aasaatlddv kakgfvqcgv ntglagfaap nasgdwsgfd
       61 vdyckaiaaa vfgdatkvky tplsakerfp alqsgevdvl arnttwsinr dtalgfnfrp
      121 vnyydgqgfm vrkeldvksa lelsgaavcv qtgtttelnl adyfkannlq ynpvvfekle
      181 evnaaydagr cdvyttdqsg lyslrltlsk pddhivlpei iskeplapav rqgddqwfdi
      241 vswvhyalvq aeefgvtqan veemkksanp dvqrflgvea dskigtdlgl tnewavnivk
      301 avgnygevfd rnigagsplk ierglnalwn kgglqyappv r
//
LOCUS       WP_457662715            1025 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Sinorhizobium medicae].
ACCESSION   WP_457662715
VERSION     WP_457662715.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1025
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=112404
     Region          2..475
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mlggelsrta lalwphqhaa ldtveayfvs asaraclvnm ptgtgktgvm atiarqraqv
       61 rpvlvvcpsa alveqliaqf edrfwdkiga spvwkpdrvw nvlpsdiesl tkrldghgge
      121 rvivvgtvqa iqqidadgki dqlhgrigti lfdeghrepa pswarvvrgf avptvlfsat
      181 pfrgdlkifd vdddhihflg fadavdqgli rgveideqpl plspddyala liarvdalva
      241 egrftaankv ivrcdseesv temhqaltag lagraagvla ihhnfrerpd dgifdavprd
      301 laaraerfli hqfmliegid dprctmlaly epftntrmlv qqigrlirhp gpigdaapaa
      361 yvlapkgrdi anewnsflaf daaskangnk pfvrndatil enliaalptl dyvmgrfrer
      421 pdlddpglhd dlrfpsaava ftiepdldld elqkaikael iredrhealt grtadgncry
      481 hitlrltpsp flsgslfqap sleatiyakk nkrlfffdsa glwineldgi gprvnaktlr
      541 allpdgydns isfmsvkntd lgplalrsrs lsarsldrsg vfmgehlnvv tratgyihpk
      601 aaedgirrav gfsrsrvrdg kgndltaqqy adwcvtvdaq ldaaartasv ftrfavpdtv
      661 padtmplnil vdmvemadqf vakgqtaavr iedlcvavee dtdpkapalf rfllhvdgee
      721 hpvwidwnak kakywlvspg lsriktkdnp kisltrrlnq lqpfriitrd lahtyvggdf
      781 yrldldltdp kgaaslvldl itaipglgav tsekgvlvdg hvdywadgsl fefldkalrp
      841 drgpalfgrs fpdlvcddlq devgdflgld etsasqaava vagkwksgnp gvsasafydv
      901 caqglknlay mksdgvvlpg sqtrfdgrwr lskrnspitq tvdrkrhgrg stafrgafqr
      961 lraapttdra iwlvcsggml slaklkaefa kpqpephvlq fyhlvlstys acqsvgvqlr
     1021 ifcae
//
LOCUS       WP_457662716             120 aa            linear   BCT 27-JAN-2026
DEFINITION  thioredoxin family protein [Sinorhizobium medicae].
ACCESSION   WP_457662716
VERSION     WP_457662716.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459707
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..120
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12802
     Region          12..95
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mntttpnehp saivkvdtsn fseevlqsne pvivdfwkng cqpcdmiapf leqiatelag
       61 nvkvvtlnge espelaeqyg vrgyptlalf kggevavaai dfrtgsfras isnalaslrt
//
LOCUS       WP_457662718             356 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA disulfide reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662718
VERSION     WP_457662718.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=39889
     Region          27..138
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(45,48)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mesnkilsve srapalkvrd wvrgealasf qpdrvyvlef fgtscgycve amsdlielqe
       61 sykdrgvevv avaagesaas adevrsqiaa wlaqfpelnf rvgfddtgam dtlwmdpsfs
      121 veipqtfvvd rdgylafige pdklhdvlpq vldgtwrtsa qaqaaereri aedepkarke
      181 alkkqirakt aaaeeiedwk talaaleegv aldpddfsfr cahvhlllhe mhdmqtglpa
      241 lrqfirdain tnyeamlefa frelfdpayg ysqfpsverf amgkelsehf laqarlqddy
      301 dravsylmva wyyhasgnkd ravellelal qpldgpgpdg lkddllqtla dykgek
//
LOCUS       WP_457662731             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662731
VERSION     WP_457662731.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77089
     Region          5..663
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra eehgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hcagshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesataeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457662735             178 aa            linear   BCT 27-JAN-2026
DEFINITION  transcription termination/antitermination protein NusG
            [Sinorhizobium medicae].
ACCESSION   WP_457662735
VERSION     WP_457662735.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 178)
  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..178
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     gene            1..178
                     /gene="nusG"
     Protein         1..178
                     /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=20034
     Region          6..178
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mkvtemnpen arwyclhvks gkefdvenal tkanveafmp rervvlvrhg rkiesdrpff
       61 psyllvrlvp tpeafhglry qkdvldfvgg pagyhvinda dvvvfkrlsd gveaprvatd
      121 ksfrdgdqad ivlgpfagfr cvvtavkwcr qakasvridv qgrpfdiesm plaflrkl
//
LOCUS       WP_457662736             433 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662736
VERSION     WP_457662736.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 433)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..433
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..433
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47358
     Region          <26..68
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msiaimsqlf kahlgstnrk mlavrladfa dddgkgiwpt vgrlaqetel sersvqrila
       61 efveegllvv vrkggsrpge atrydfnmaa larlkapkta sdgchgvthd tvspvtaatp
      121 mgdtddvdgc hgdtqtviep piepserega regdlkdhdd pakfgkrvka lemgtannpw
      181 pgaiasstaw alqqfeklta eerrlaeerr daylaeckaq kvknvalgvy lrdkkffais
      241 plagkvqats tkipvapfgp vwagirvlal ldgpepvemp lgvrdrirqt fetlmrtsea
      301 rarsyvggkg vsvgpggeli fpddfdqael rrrvvesgyp randlhaqak nrdrtvaear
      361 fealadlcep vpvgselfer wrdyheaagw pfvpdpgsmp vvyfpkggpe rlhhfetaar
      421 aalrqersnd haa
//
LOCUS       WP_457662743             355 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457662743
VERSION     WP_457662743.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..355
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40489
     Region          70..344
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mvvkvklegl nvvsargkwy vyvrdtkekl lvgfegsrad ldkrmampdf iakynsrrvr
       61 dlrrtypdgt lgalvewyen ecpkyqslae atkndyteaf kylrpefdya ladinqadly
      121 dirdkcakek wprfadkmis aissmftqav krkkmlgnpa lgidkchkad pnanrewren
      181 ewvyvaanap phlltpmmia rhagyrgqti vklrwndyqp dprfgkcfri itaknkelvw
      241 ipatdelqgy ldkldrpaln ictrsdgtpw esevqmqtsv shylrdleea ghigggttlh
      301 glrttyaadl krsgaetgdv aaalgdkser mgahytrhve neakvirafe gkkkr
//
LOCUS       WP_457662748             639 aa            linear   BCT 27-JAN-2026
DEFINITION  LTA synthase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662748
VERSION     WP_457662748.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Sunden,F., AlSadhan,I., Lyubimov,A., Doukov,T., Swan,J. and
            Herschlag,D.
  TITLE     Differential catalytic promiscuity of the alkaline phosphatase
            superfamily bimetallo core reveals mechanistic features underlying
            enzyme evolution
  JOURNAL   J Biol Chem 292 (51), 20960-20974 (2017)
   PUBMED   29070681
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Pabis,A. and Kamerlin,S.C.
  TITLE     Promiscuity and electrostatic flexibility in the alkaline
            phosphatase superfamily
  JOURNAL   Curr Opin Struct Biol 37, 14-21 (2016)
   PUBMED   26716576
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..639
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=72583
     Region          34..618
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 maridsavss sdvyangqvs saryartlss arsalftlll aisvvftiel ivrwswpdtv
       61 ayftdpmrpa wttvavffla mlgvdalfgr ehkaallvap lavvpafisq qkqvflsdpl
      121 yptdflfgrq imelmpvlvk drpwtavgvv agiiiaivvs vlllrfawrn fpkltrrerm
      181 ariafalpll vafwnimdyn qfswirdrlr vipimwdqte nyrhngfala fainlpmanv
      241 sapagymada ieripvkplp agtshrgkpd vivlmsesfw dptrlpkvkl tpdpmptire
      301 lqggnvfspe fggmtanvef ealtgfsnaf lpygsipyqq yirnpipsla tffrsegyvs
      361 raihpfqgwf wnrnavykaf gfdmfkseen mppmakrgif asdesltkei irqadeledp
      421 ffffavtlqg hgpyeanrya kntikvegel sdadrqvlat yaqgvkeadd slkmlmdwak
      481 erdretiivl fgdhlpplnt vysstgymkg itaerkgpkd qikaehetpl vvwsnktgpk
      541 kkigtispaf lsyqilkqag yehpyytgfl gkvydhyrvl drymlirkng kdvadwlrqr
      601 kipaslrdyr flqhdmmfgk rysterffqs hadlysagl
//
LOCUS       WP_457662750             227 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457662750
VERSION     WP_457662750.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..227
                     /product="HAD family hydrolase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=24445
     Region          1..222
                     /region_name="PRK13222"
                     /note="N-acetylmuramic acid 6-phosphate phosphatase MupP"
                     /db_xref="CDD:237310"
     Site            order(9..13,113..114,146,170..171,174..175)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 mslplvvfdl dgtlvdtapd lvaslnhavt qvglepvtya dlthlvghga ramiertfal
       61 rgrtiaedel trqmnvfvef yhgsmpgesl pypglveald rlqdagmkla vctnkpemla
      121 krlleglgll drfaaisggd tfsvrkphad hllstvanar glperavmvg dslndilvar
      181 naavpsivvp fgysdmpies llpdriighf deltpdlvea vlsrkpk
//
LOCUS       WP_457662685            1153 aa            linear   BCT 27-JAN-2026
DEFINITION  chromosome segregation SMC family protein [Sinorhizobium medicae].
ACCESSION   WP_457662685
VERSION     WP_457662685.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1153)
  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 1153)
  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 1153)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1153
                     /product="chromosome segregation SMC family protein"
                     /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=127539
     Region          1..1152
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mkftklrllg fksfveptef iiergltgvv gpngcgksnl vealrwvmge nsyknmrasg
       61 mddvifsgsg nrparntaev glyldnsdrt apaafndsde iqvtrriere qgsvyringk
      121 earakdvqll fadastgars psmvgqgrig eliaakpqar rqlleeaagi sglhsrrhea
      181 elrlkaaetn lerlddvtsq lesqieslkr qsrqanrfkm lsaeirrhea ilfhirwiqa
      241 keaeaeatsq lnqvtalvae taqsqmeaak aqaitslklp elrqneakla aalqrlqiar
      301 aqleedagri lrrreelqrr laqlsediar eerlvadnag ilarldqeee elrdalaead
      361 drslearerl eeaneklaas egavarvtae raeaqaarnq ieralrdlse rqarlarqla
      421 dqarelddld grmaslpdpd ekreqvehae asmeeaeaav saveeslaea raaetatrpp
      481 vdqararlng ieteartirr mleaagastf pavveslkve rgfeaalgaa lgddldssle
      541 qaapahwrmp gddaddpalp sgvlplidfv qgpealrrtl rqiglvqsed eaeqllpflr
      601 agqrlvtrqg avwrwdghva gseapsaaal rlaqknrlfe legeaeaasg alskaeadla
      661 aagarirged erlrlsreaq rmrarqlaea rdalaiaera sgdlarrrav laetklqieg
      721 qaeeiaeqie vaneafadqp dpaeldrhls drtaevatdr aaaaearaah dglarenner
      781 hrrlmaiage retwgaraas aenhiatlre reaeaqeeve elleapdafd ekrralmnel
      841 qkaeasrrea adnlaeaesr qresdrqaat alselaeare krgraeerlv sarerrleie
      901 arilealsca phevmrltgl aanealpdmr svereverlk iererlgavn lradeeqkel
      961 serlaallke rddvieairr lrsaiqnlnr egrerliaaf dvvnvqfqrl fthlfgggta
     1021 elqliesddp leagleilar ppgkkpqtmt llsggeqalt amalifavfl tnpapicvld
     1081 evdaplddhn verycnlmde malstetrfv iithnpitma rmnrlfgvtm aeqgvsqlvs
     1141 vdlqtaermr eav
//
LOCUS       WP_457662758             609 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457662758
VERSION     WP_457662758.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 609)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..609
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=66595
     Region          7..480
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mggttvqiak leienfrgir egvvrfspht vlvgsnncgk ttvvealall fgrdrmvrql
       61 tehdfygsnp qpvdrirlva tvidfdgddp aqhmdwfrdd rgivkwwnpv dgavmpartd
      121 pswklacqvt faarfhrpsl evetlryfhd ddvvgdvfad esatafsarl irdigfffvp
      181 aartwdrtvs fgselfrrvv aagegqpses vlserdrlrm pearleqder lapivnrlnq
      241 elrgffrtap tlhlrvtatd sdgllesvvs hyahegadlp lparrhgsgl lslqhlllll
      301 qfghmraean egfwmaleep elhvppalqr rlvhriqals rqtfvsthsp mvaaladpkg
      361 vavlrndggv ltaiplltst lpadtpnsvr klfqvnrvet iaavmhefvl vpegrtdyew
      421 lgllvravdl hqswaaadec rfdafvgvip thdgavvttv eamaplhprv vamvdgdleg
      481 vgyaatlvaa gspnsgvilr wadgqmledt igwiidadsn aclpaiqinq pattvaelva
      541 rlkndnraag glkkdtstye iiagaigase accararall naitdvvkgv hnplfaadaa
      601 npairvfqp
//
LOCUS       WP_457662761             299 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662761
VERSION     WP_457662761.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..299
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33283
     Region          29..263
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(34,37..39,42,50,52,82,101..104,198,200,202..203,205,
                     215..216,219,234..235,238)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(34,38,42,50,52,82,101..104,198,202..203,205,
                     215..216)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(37..39,198,200,203,216,219,234..235,238)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 msdtdmpvid avlarrliat qfpqwadlpv rpvefggwdn rtfrlgkhmt vrlpsaahya
       61 lqvekeqewl prlapslplp vpvplamgrp gegypwhwsv yewrhgeiat raqiadlsrf
      121 attigeflaa lqridaqggp ppgqhnffrg galtvydret rwaldalegr idvhaarlvw
      181 eaalasawdr apvwfhgdva agnllvengr lsavidfgts gvgdpacdls iawtmfeets
      241 ctafraalrl degtwargrg wtlwkaliva aempgtdrre veksrriida vlsdhrrya
//
LOCUS       WP_457662766             307 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662766
VERSION     WP_457662766.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34548
     Region          1..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 masvthssar rsrfriskrv lpyvlslpal lvcigilipf ftaviysfqr yrlsqpwarq
       61 fnwgdnylnf ftdpgfwntl kisllyagvt vtlelllglg ialllqrrst vnnftsimll
      121 lplmtapala almwklmtnp gfgilsylas liglenfrwa sspdtalltv vlvdiwvytp
      181 fimilllagl rslptqpfea aaldgvprsf vffritlpml tpyiltatlf rllnsiqqfd
      241 iiyamtqggp gdtltvfqve aylnffqstn vgrsaallii lwaityilsn ifiknwlrlr
      301 erargea
//
LOCUS       WP_457662764             416 aa            linear   BCT 27-JAN-2026
DEFINITION  D-amino acid dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457662764
VERSION     WP_457662764.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..416
                     /product="D-amino acid dehydrogenase"
                     /EC_number="1.4.99.-"
                     /GO_function="GO:0008718 - D-amino-acid dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0055130 - D-alanine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44725
     Region          1..415
                     /region_name="PRK00711"
                     /note="D-amino acid dehydrogenase"
                     /db_xref="CDD:234819"
ORIGIN      
        1 mkvivlgagi igvtsayqls raghevtvid rqpgpalets fanagevsfg ycspwaapgi
       61 pmkalkwlfm qhaplilrpr idaamlswma kmlsnctsrr yavnksrmlr ladysrtsla
      121 alreetaity dermqgtlql frteaqldas akdisalaad gipyevldrd gciraepalg
      181 rvrdkivggl ltpqdetgdc fkfanalagr aeklgvcfdy gteiralevd ggrvhgvvts
      241 kgrravdavv valgsyspll vrrfgirlpv ypvkgyslti piadasrapv stvmdetyki
      301 aitrlgdrir vggmaeisgy tndlgiarrr tlehsvmdlf pggdaakgsf wsglrpmtpd
      361 gtpvigptri aglflntghg tlgwtmssgs arviadlvsd rkleidatdl aiaryg
//
LOCUS       WP_457662751             361 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457662751
VERSION     WP_457662751.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Van Houdt,R., Leplae,R., Lima-Mendez,G., Mergeay,M. and
            Toussaint,A.
  TITLE     Towards a more accurate annotation of tyrosine-based site-specific
            recombinases in bacterial genomes
  JOURNAL   Mob DNA 3 (1), 6 (2012)
   PUBMED   22502997
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..361
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=41679
     Region          175..339
                     /region_name="INT_Rci_Hp1_C"
                     /note="Shufflon-specific DNA recombinase Rci and
                     Bacteriophage Hp1_like integrase, C-terminal catalytic
                     domain; cd00796"
                     /db_xref="CDD:271177"
     Site            order(184..185,188,209,212..213,253,255,257,307..308,
                     311..312,314..315,325,335,338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271177"
     Site            order(217,302,305..306,337)
                     /site_type="active"
                     /db_xref="CDD:271177"
ORIGIN      
        1 mgtiterksk ngkksytaqi rlkrdkvvvh sesqtferka vatawikkre telrepgaid
       61 rlkenstlah aidryikesk kkigrtkaqv lakikdefei anmackeies adivkfatel
      121 shgrqpqtvg nyishlssif aiarpawkid lnysamedaq vvlkrlglia kstqrdrrpt
      181 leelwklmeh ysdretryaa hipmrrliaf aifstrrqee isritwsdye denkrvlvrd
      241 mknpgekign dvwcdlppea iriiaamprt kvkeifpyea rsvsasftra csllgiedlh
      301 fhdlrhegvs rlfelgwnip hvatvsghrs wnslkryshi kqrgdkyegw kwldivapak
      361 q
//
LOCUS       WP_457662762             671 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662762
VERSION     WP_457662762.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..671
                     /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=72813
     Region          1..338
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          406..655
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 meyrrdidgl raiavlpvvl yhagipgfsg gfvgvdiffv isgflitgil hkelaegrfs
       61 lvrfyerrar rilpalfvvl atclvagvll llpdmlvgla rsalatmlfa sniwfwfsts
      121 dyfapsadle pllhtwslav eeqfyivlpl llwwlhgkpr rtvlgalagl cilsfvlsaw
      181 atgpypqesf yfaptrawel glgvllalga fpacrnarlv eavalsgiaa ifisvvfysa
      241 atsfpglaaa lpcfgalall wsgeqrrtiv arllsgpvpv aiglasysly lwhwpiivyf
      301 rltlgtldlp haqaliaigl sfvcafasly fverpfrrgp pagfsprliv asglagavtl
      361 slvsaavnig eglperlpqd vrlayagsrd vdtrrgrceg rlpseglcri egevsspadl
      421 rndvllwgds hagalmsgld fvmddrklgg avafrgacpp ilgvqrvdqr hsrdcvafne
      481 aimtmlektd dfpvvvlsar wplaangkry pgetgrpavl drvdfkeash stagnyeifk
      541 seflktvrai rdtgrrvviv dgipeigwsv phalglhrli daelpppptr qavearsaka
      601 nsvlaiaded pgvqrvsavp llcnpicave kdgiplysdd dhlsvygamt lvprmfkdlm
      661 psetdrrlgp g
//
LOCUS       WP_457662767             455 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662767
VERSION     WP_457662767.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..455
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49300
     Region          52..442
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(166,168,293,295,327..329,372)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mknrsslvaa sgksrreflr ngatfaaagl agglsgfpfi nrlpvraqda plkfwqfyap
       61 ggqvkpqvew fertvadwna thdqkvelef ipnkeyingp klatafasgd gpdifiispg
      121 dflryynggv lqdltpyide karadfpesv lanrmvdgki fglpmevepm amfysikafe
      181 daglnendvp ktwdellelg kklttperyg llfqtapgyy qnftwypflw qgggefqnae
      241 gksafdspat vqalklwqda vnsgaaprqv lgngandsva nlasgycaiq nvgiwaisql
      301 knnakdfpyg vfrlptpang kyvtvgggwa fvanskgknp eaagqfcawa lasmvqgsid
      361 rvaswcteak sdmpprdsal kareaafseg iigqfakeih pgtraeprvp pevykiisda
      421 vqqamlggad pqatattasq rldaylasys gapil
//
LOCUS       WP_457662768             261 aa            linear   BCT 27-JAN-2026
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662768
VERSION     WP_457662768.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Grinter,R. and Lithgow,T.
  TITLE     The crystal structure of the TonB-dependent transporter YncD
            reveals a positively charged substrate-binding site
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 484-495 (2020)
   PUBMED   32355044
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Oke,M., Sarra,R., Ghirlando,R., Farnaud,S., Gorringe,A.R.,
            Evans,R.W. and Buchanan,S.K.
  TITLE     The plug domain of a neisserial TonB-dependent transporter retains
            structural integrity in the absence of its transmembrane
            beta-barrel
  JOURNAL   FEBS Lett 564 (3), 294-300 (2004)
   PUBMED   15111112
REFERENCE   3  (residues 1 to 261)
  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   4  (residues 1 to 261)
  AUTHORS   Buchanan,S.K., Smith,B.S., Venkatramani,L., Xia,D., Esser,L.,
            Palnitkar,M., Chakraborty,R., van der Helm,D. and Deisenhofer,J.
  TITLE     Crystal structure of the outer membrane active transporter FepA
            from Escherichia coli
  JOURNAL   Nat Struct Biol 6 (1), 56-63 (1999)
   PUBMED   9886293
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..261
                     /product="TonB-dependent receptor plug domain-containing
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27811
     Region          25..>251
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mqpflgctai aivatavsig pgtriamaqd atpsdedaat tlapiiitge kfgrdqfttf
       61 tsvevftgge lhdlvrptln dalnsspnir afmsgrgnsd ivirglsseg vtapsrsnpv
      121 isvvvddaeq gveatrrgtr glwdveqvev lrgpqstlqg rnalagsvii ktkdptytpe
      181 asiegligtd eyksgafavs apivedelaf risgqifrrd ndidyvdpsi sdvgeeefee
      241 irgkllwepa eipglrgavy r
//
LOCUS       WP_457662774             274 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 108 protein [Sinorhizobium medicae].
ACCESSION   WP_457662774
VERSION     WP_457662774.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..274
                     /product="glycoside hydrolase family 108 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /calculated_mol_wt=29027
     Region          9..166
                     /region_name="ZliS"
                     /note="Lysozyme family protein [General function
                     prediction only]; COG3926"
                     /db_xref="CDD:443130"
ORIGIN      
        1 mareilpval elmfgdeggy snvktdrggp tkygvthttl aahrgvnsvt anqvkamsre
       61 eaediyrrsy wgqsggdllp pgldyaafdf gvnsgparav ktlqkvvgvr edgqlgeqtl
      121 aavrrypggi stlirdycda rmrflrsltn gktgfpvngr gwtirvtgkd pkgqwkdqpg
      181 vvgnalrlaa dasgrtvekv esppeagaka dsrdtglgev lkkpeawgpl ggllsaagal
      241 fagngpvqwa laaamvaavl vglwyfvrrv reag
//
LOCUS       WP_457662786             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662786
VERSION     WP_457662786.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77167
     Region          5..662
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra eehgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wlsrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagqsaaaeq
      661 qsplvaaala ratraaqrnr
//
LOCUS       WP_457662791              78 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662791
VERSION     WP_457662791.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     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 78)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..78
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8195
     Region          <2..46
                     /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 maraalgwgi vefaeragvs tntlvrlerg delkkstldh lravfedagi efisaadhfg
       61 vlvkkistng svggrspv
//
LOCUS       WP_457662792             509 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662792
VERSION     WP_457662792.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..509
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55295
     Region          108..509
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 maiasaifgv liaallllas flihliggfe qgqisqivha vakqlplvfg vggffsafmt
       61 dapiaavfgs arwasgkelq klsakdagll igrdpttdkl lrydgpahll tlaptrtgkg
      121 vgtiipnllt adrsvicidp kgenasisgr areqfgpvhi ldpfgvagkh saafnpldml
      181 dpdgldiaed antladalvf depgmtgdah wneeakalia glilkiaiae spgrrnlsml
      241 reyltlaper flgllarmqd mdeangliar aanrhlgksd reaagvlsaa qrhthfldsp
      301 rmtavlgrsd fhfsdlkrnn atvflvlppd rlstysrwlr llisqsltdm ardpasparh
      361 vlylldefaa lghlapvera mglmagygvq lwpilqdihq lratygrrag tflsnaavlq
      421 vfgvndieta eliarsigkt daqyitrsws egkksssehi sardlinade imrlpedrmi
      481 vlrqgqrpaw vqklryyadp efkgtfdpa
//
LOCUS       WP_457662796             247 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662796
VERSION     WP_457662796.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27824
     Region          6..244
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msaekiieak nvskwygafk altdvnltvr kgerivicgp sgsgkstlir cfnrleahqe
       61 geitvngirl hnkmrdvtev rknvgmvfqh fnlfphmtvl mncmagpmwi kgipeaeakk
      121 talkflervr ipeqankypv qlsggqqqrv aiarslcmep avmlfdepts aldpemvsev
      181 letmtslard gmtmvcvthe mgfaravadr iifmdwgriv eegtpeefft rpqhdrtklf
      241 lsqilkh
//
LOCUS       WP_457662809             215 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457662809
VERSION     WP_457662809.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 215)
  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 215)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  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 215)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP 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 215)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..215
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..215
                     /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=23800
     Region          2..165
                     /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 mridaisvwt gkaaawlilc lmllvcgevf kryilnmpta wifdasnmly gslfmlagay
       61 alaqnahvrg dflysafrpr tqaaldlily ilfflpgiaa liyagydyaa lswrigehst
      121 vtaegpplyf fktvipvaga lvifqglaei lrciiclktg awparlkdve eidvvaeqla
      181 hsehldqetr eaaleraqdi drtarqrglg gesre
//
LOCUS       WP_457662810             286 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457662810
VERSION     WP_457662810.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..286
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31466
     Region          22..269
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mpflespfse plaerlraaa rgvrlywlgq agfviltsrf riaidpylsy slaekykgkr
       61 fehdrmmpap iapselgpvd lvlvthqhtd hmdpqtlvpi aeanpdcrfl lpraalgaaq
      121 erigvqserl vpidagesve plpgftvsai raahetlert pegwhrflgy vvatdgvrly
      181 hsgdtipheg lveevapfrv dlallpvngr raelteagia gnltldeacl ladrigapdm
      241 iahhygmfaf ntecpeaidt ksesadcrvr lhraklsvey rlsrag
//
LOCUS       WP_457662831             298 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457662831
VERSION     WP_457662831.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10647717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..298
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33556
     Region          32..>105
                     /region_name="HATPase_c"
                     /note="Histidine kinase-like ATPases; smart00387"
                     /db_xref="CDD:214643"
ORIGIN      
        1 msddtsfhsn lvrrvqnmal gpstpsnali pvfeavynsl haiqdrfkek wcdagrieig
       61 linldssrpt feirdngigl dtenyasfrt ydsdhkmkrg gkglgrlswl kvfegakves
      121 tflegdkclv rrfrmqldne qplaeyslaq eagrvpgtsv ilydmkveya rhvpskadti
      181 vrkvvahflp yliasarpti vietatesye laaylrekev slgtldlsln ldtslkldhn
      241 lleksvvegk aahriyfaah grvvadfdig feaprlcrrp qlvrsrvydk qddkqvfs
//
LOCUS       WP_457662839             220 aa            linear   BCT 27-JAN-2026
DEFINITION  3'-5' exonuclease [Sinorhizobium medicae].
ACCESSION   WP_457662839
VERSION     WP_457662839.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Viswanathan,M. and Lovett,S.T.
  TITLE     Exonuclease X of Escherichia coli. A novel 3'-5' DNase and Dnaq
            superfamily member involved in DNA repair
  JOURNAL   J Biol Chem 274 (42), 30094-30100 (1999)
   PUBMED   10514496
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..220
                     /product="3'-5' exonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24718
     Region          37..210
                     /region_name="DnaQ"
                     /note="DNA polymerase III, epsilon subunit or related
                     3'-5' exonuclease [Replication, recombination and repair];
                     COG0847"
                     /db_xref="CDD:440608"
ORIGIN      
        1 mdqnsiellp nttkkivlsn vpkmksernv dvyfsadiet dgpipgpysi lsfalvyags
       61 ydgqtftrpt sfdhsfyrel rpissefepe alavngldra rliregmrpe qamfeanewv
      121 ralagdgnpv fvayplsfdw twlywyfvrf sklgspfghs rcfdiktavs vktgfpiags
      181 grsrlplrll psrghthhal ddaieqaeif anvfewedga
//
LOCUS       WP_457662840             366 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457662840
VERSION     WP_457662840.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..366
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40681
     Region          119..332
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpkrlddklp kgvsldrdwr trearyyfra pgrkkvrlke tpgtdafdke vafarlgipy
       61 vpegtepppa gvtlkrdpae gtvdwlyaey krratisagv marratilee vcdykfgtar
      121 cgdlpyadmr krhvveirda vrdkpgsrnd vkkaisalfa wavesdlaqm npaakikllh
      181 sgdgfhtwtv devrqyeakh gagtkarlml hlalytglrl dslsivglqh irngqltirp
      241 ektrkssgvi vdipvlpelq ktidecptgn ltflvtefgk pfttnglgnk mrdwcdqagl
      301 fhctthglrk agatiaaeng atdeelmaif gwttknqttt ytkkarrkqi aagaiqkllp
      361 pkpepv
//
LOCUS       WP_457662849             268 aa            linear   BCT 27-JAN-2026
DEFINITION  LexA family protein [Sinorhizobium medicae].
ACCESSION   WP_457662849
VERSION     WP_457662849.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 268)
  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 268)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..268
                     /product="LexA family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=29978
     Region          40..267
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mtdfagsmsm geicdnrdfk sskirdirdi nfrvsrenvr mkdrrqeird wlqteldrkg
       61 ygakgqlakf lglrndgitr ilntapgkei revkadelvk mgeffgstpp gltgtltrse
      121 apinsvkvig riaantwmdv demdfgfddi etvpsvgdyp aawqfgllis gnclnkiasn
      181 gdrlvcldla kagldaqpdd lviverskfs gqmiertakr lrqsakgfel wpesndpahq
      241 dpiplyedgd ddielrivgk vlwilrkp
//
LOCUS       WP_457662861             124 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662861
VERSION     WP_457662861.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 124)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..124
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14000
     Region          51..98
                     /region_name="HNH_3"
                     /note="HNH endonuclease; pfam13392"
                     /db_xref="CDD:433169"
ORIGIN      
        1 mmsrreeire kimarvvvdp vtgcwiwqgp tsgskgrgkn yprmnlsgqt vavhlvmwtn
       61 ehgyipgkkq ldhkcrnrlc vnpdpkhtel vthkqnqkrr dqaraaaivg ykggpplece
      121 eitq
//
LOCUS       WP_457662870             472 aa            linear   BCT 27-JAN-2026
DEFINITION  alanine/glycine:cation symporter family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662870
VERSION     WP_457662870.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 472)
  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 10003022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..472
                     /product="alanine/glycine:cation symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005283 - amino acid:sodium symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006814 - sodium ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49441
     Region          1..447
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdtiigflnt ilwgyvliyg llavglyfti rlglpqiihf gemfrvlssr gskdtsgisp
       61 fqalmvslas rvgtgnlagv avalylggpg atfwmwmval vgmatayaes alaqlykvrn
      121 edgqyrggpa fyiahglnap waaaifsvcl iisfglvfna vqansiadav qgafgvpkli
      181 vgfglavlsg vvifggirqi arvaeiivpf mavayllmav yvlianaalv phvlwtivss
      241 afglqeaagg vtggiaaaml ngvkrglfsn eagmgsapni aavatpvphh pssqgfvqsl
      301 gvfidtilic tatsvmills gtldpgsnit gtqltqaamn vhigaagtyf iaiaifffaf
      361 tsiignysya enaltylgag nrlgltimrc atlvmvvwga yesiatvfda adasmglmat
      421 inliaillls gtiakltkdy fkqrkqglap vfhaadypel qgkidhgiws rv
//
LOCUS       WP_457662873             376 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662873
VERSION     WP_457662873.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38978
     Region          10..372
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkdntitsav ivgagifgvs tgvqlarrgi rvimlnegpp aggasgrsls wlnssrmrse
       61 pyhrlrmagi dryrtlsarf pdadwlrfeg gltwdaddas ngidaayrhe vslgydarhl
      121 sagevaaitp gvdtstitpq gaifnpgegw vdlpsligll lkefaalggt lvtdqgaaki
      181 vveggravga etaagnsfta davvlatgpa vpkmvaeage tigdatplal lvqtkplahp
      241 lravlntprv avrpapggtf sldadwaade glrlredggh didrtiveal laeaskvmeg
      301 npklkiasig vgskpipgdg epvvgalrai pgyhvafshs gatlgliige llahevatgs
      361 ehpmlatfrp erfasr
//
LOCUS       WP_457662877             104 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662877
VERSION     WP_457662877.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..104
                     /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=11456
     Region          6..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpsvserpvk rsirrnelre ivpladstiy emeqrgefpr rfglsprcvv wdlaeveacl
       61 esrrtrsipr akhpdvtqrk frpvkgqgra qalgmvgggg ggag
//
LOCUS       WP_457662878             136 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Sinorhizobium medicae].
ACCESSION   WP_457662878
VERSION     WP_457662878.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 136)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 139559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..136
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14390
     Region          16..126
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(105..108,110)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381122"
ORIGIN      
        1 mvgksedgrf leglkvlvve devwialdle aafvdvgaqv vgpcgtleta lvaakneala
       61 lavldirlgt attervidll nergipfffy sgqtlpdemr kksngavvmv kpamqqdivg
      121 kavevlmass mpisps
//
LOCUS       WP_457662879             362 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457662879
VERSION     WP_457662879.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..362
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39810
     Region          19..359
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mhtangftpd ppvrvnnyri gcigagmima echlaayrea gflvaaiasr teakareval
       61 rwdiptvhat psalisdtqc eiidiafppd qqpalirral raphvkaila qkplaltlee
      121 akalrdeaaa agkilsvnqn mrydqsmrvl kqildrrelg tiviatiemr aiphwqsfle
      181 gydrltlsnm svhhldvlrf lfgdpetitt vtrtdprttf dhkdgitvst ltfpngvlav
      241 smedvwagpr edgfdsdfyi kwrvegtdgv aqgsigwpdg spstltyasr kttggkwvtp
      301 ewqtmwfpha figvmeqlqy avnsgeppal svadnvktva lveagyrsia eartvrlsei
      361 ai
//
LOCUS       WP_457662880             172 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Sinorhizobium medicae].
ACCESSION   WP_457662880
VERSION     WP_457662880.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (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   4  (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 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..172
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19609
     Region          5..164
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mlpkllaigg wlrrraenll clmlltmfiv ftlqiifrya lnlsigwthe vsvalwiwtv
       61 lfgsafvvre vdeirfdliw sgasdrsrrv mqiicaaali flfgislpav idyvtfmkve
      121 staylkirfd ylysiyvifv ismilryiwl aiqairgrap dafdptkags gv
//
LOCUS       WP_457662883             292 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457662883
VERSION     WP_457662883.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..292
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=31660
     Region          <1..292
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mialvgvvsv lgfplsqsgp etpatlgtlg esvgrlfslp aylmravmlt liglttalam
       61 arsrrllare vsetarranl arflpaeiap lvgeddlatw rqgrrqqgti lfidirgfta
      121 yaekldparl sifissfrrr vmrateafgg vvdkfigdga lvvfgipepq sddctraiac
      181 ahrllslidr wnikrgfdpp vrvgigihsg elyyglvgdd hrleftvlgd tvnvaakieq
      241 atkrfdtall asetvvlrar qqpswqavcr eplggrgehv avfvytgtkp ag
//
LOCUS       WP_457662888             244 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662888
VERSION     WP_457662888.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..244
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25547
     Region          12..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtdpfsfppg fttviiggag digsaiaslf hargarviat ghdqacldrs plstnadval
       61 eildvrsdaa vnafaarfer vdalvncagi lardeefeie tfqrvldvnl tgtfrtstaf
      121 rrhlaasggs iiniasmnay salpripayc askggvvmlt kalalawaee girvnavapg
      181 yietsinaeg rkdtahrdri aartalkrwg tpeevagtvv flampaskya tgtvfavdgg
      241 flag
//
LOCUS       WP_457662889             231 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662889
VERSION     WP_457662889.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..231
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25269
     Region          <1..225
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 madgefwngl yvtfalyils mvlqlvagiy lamllfhskr lsgllrslli spfmmppvva
       61 gmmwlvildp slgaanyile svglppsewl aspvwvipti alidtwqwap yvalivlggl
      121 qslppsvyea aqidgassfr ifrritlpll lptivtaavl rsvdllrffd iiyittqggp
      181 gnasntlniy gfrvgfeffn igyssalmit lsvivlgavl mlnrlrnava w
//
LOCUS       WP_457662892             336 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662892
VERSION     WP_457662892.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35871
     Region          17..>310
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 maeklshsgv ndvasllaai vdgnearfid irrriheype iafeevrtaa lvaetlaslg
       61 iehqtgvgrt gvvghirgkr pgptllirad mdalpmqeet glayaskian rmhacghdlh
      121 tatvlavgav lkrledrlag nvrlifqpae eavggakemi adgvmegvdm alslhnrpei
      181 pvgqfgivhg yanaavdsfd itvhgkggha arpyaavdpi viaaqligql qtivsrdvra
      241 ldacvvtvgs ihagearnii percelkgtv rsrqpearda aeaglrrlce gvglsfragc
      301 eltyrrgtpp hlqrcghaaa hhgcdqraaw rrglrl
//
LOCUS       WP_457662893             245 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457662893
VERSION     WP_457662893.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..245
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25107
     Region          7..244
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtidkpvalv tgaasgigaa taadllgkgy ityaldrdsa mlsslgpsan lrcltvdvad
       61 eealaatvrq vieaegrlda vaavagislt asltemrsed wdavqrvnlr avyllgklta
      121 phleasgags fvavaselgt vgqlglaayg aakagvinlv rvmaleyatr gvrfnavapg
      181 gvatpmmere qkrlgltved aarnipmarl arpseiasvi vfllgreasf vtgatfvadg
      241 gytar
//
LOCUS       WP_457662903             120 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662903
VERSION     WP_457662903.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..120
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13809
     Region          3..>72
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtlelyghpf asfvwkplia lyergipftf kmidpdhpen qvriaalspt gqfpalidgd
       61 keitqsnavi ewdcqefcav ghddekerii twlsrknfwt sswldvihpr fsartvcwti
//
LOCUS       WP_457662904             139 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662904
VERSION     WP_457662904.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..139
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15817
     Region          <2..127
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpmipddprq alaarmmadv fddyvhvqmq rivgdalrsk eerdprgvtd ahalmdrsya
       61 wlelrlqgkq waacgrftia dcaaapalfy gdwvhpmaer fpvlaayrqr lltrpsvarv
      121 vdearpyrrf fplgapdrd
//
LOCUS       WP_457662906             230 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662906
VERSION     WP_457662906.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..230
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25940
     Region          14..230
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrvafaaere grgasirpss vvdgvydsiy hrlmsleiap gsriqidvfa rdlgvsqtpi
       61 realsrlere glvrkehlig ysaapqwtrk qfedlyvfrl lvepeaarla avnmtpdalr
      121 qlensaadmg hgeapvdrnt rysrfarada qfhdailkva gnevirstls nqhvhlhifr
      181 lmfhtrvtqe aleehenlla afragdpqaa fdamrihier srdrllsafe
//
LOCUS       WP_457662931              96 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Sinorhizobium medicae].
ACCESSION   WP_457662931
VERSION     WP_457662931.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Garcia-Pino,A., De Gieter,S., Talavera,A., De Greve,H.,
            Efremov,R.G. and Loris,R.
  TITLE     An intrinsically disordered entropic switch determines allostery in
            Phd-Doc regulation
  JOURNAL   Nat Chem Biol 12 (7), 490-496 (2016)
   PUBMED   27159580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008295
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..96
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /calculated_mol_wt=10650
     Region          1..65
                     /region_name="Phd"
                     /note="Antitoxin component of toxin-antitoxin stability
                     system, DNA-binding transcriptional repressor [Defense
                     mechanisms]; COG4118"
                     /db_xref="CDD:443294"
ORIGIN      
        1 mpqtsykise arkhfaevle ranqgeeiti mrgnevyari gpadggkrpf gllrqrglpd
       61 dlfdeddaeq aaidagdwnd dvgiwrgkpa erepkp
//
LOCUS       WP_457662938             442 aa            linear   BCT 27-JAN-2026
DEFINITION  caspase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662938
VERSION     WP_457662938.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 442)
  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 442)
  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 442)
  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 442)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 442)
  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..442
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..442
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47429
     Region          6..231
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 maivgalvvg igayrvggan fpplrfaahd agaiaqylke cwpsdrdlkl vwideskata
       61 ealkdgflsl arqgpfelcw iflsghgwvd etsagflvqp dgtgvdlpll hantldqlls
      121 eitaertilv ldccfaegvv rrmpfftalg psvarlyvas sreqqrtwed dgvqhgvfsa
      181 hlldllntgs aaqlgarktq ldvdaelfpt lceqvplyvl ehksgahqep vkggvsssav
      241 tlpvasaarr vrdrtalgta irrlrqimtg lavgsvalll ltytlvyyie pgatgtlivr
      301 hgtrwlqpll qilpytrvdt giavtdlssn gaaaaplqsg yasgvwthee ptsgyrvwft
      361 dvlagldpva aarystlvgd rpaalgaspp dlprsnvplg whlargelal lsrfspispv
      421 asaapanwyh frsttwtlrs st
//
LOCUS       WP_457662942             272 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Sinorhizobium medicae].
ACCESSION   WP_457662942
VERSION     WP_457662942.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Nemeth,E., Kozisek,M., Schilli,G.K. and Gyurcsik,B.
  TITLE     Preorganization of the catalytic Zn(2+)-binding site in the HNH
            nuclease motif--A solution study
  JOURNAL   J Inorg Biochem 151, 143-149 (2015)
   PUBMED   25898772
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Veluchamy,A., Mary,S., Acharya,V., Mehta,P., Deva,T. and
            Krishnaswamy,S.
  TITLE     HNHDb: a database on pattern based classification of HNH domains
            reveals functional relevance of sequence patterns and domain
            associations
  JOURNAL   Bioinformation 4 (2), 80-83 (2009)
   PUBMED   20198175
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Mehta,P., Katta,K. and Krishnaswamy,S.
  TITLE     HNH family subclassification leads to identification of commonality
            in the His-Me endonuclease superfamily
  JOURNAL   Protein Sci 13 (1), 295-300 (2004)
   PUBMED   14691243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..272
                     /product="HNH endonuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30211
     Region          132..266
                     /region_name="COG3440"
                     /note="Predicted restriction endonuclease [Defense
                     mechanisms]"
                     /db_xref="CDD:442665"
ORIGIN      
        1 mdelslpyed lgielpdykk edgsaasqpf srsshalfrr ktlksdgngv gprteyfkkh
       61 lvsifeqisr pvpyrfkdhl grkrsmdggc lkfvgpdgqd iaefveqdgy ivavkpkpvl
      121 iaqygamgpv aadlelltkd tslgetqrkq lidtrlgqgq frsavlamwq grcavtscsl
      181 pavlrashiv awrdathter ldpenglplv atldalfdtg lisfndqgel ltkaslqdhp
      241 nlvesgmrlc rspspkmrdy lcrhrkyngf ed
//
LOCUS       WP_457662947             382 aa            linear   BCT 27-JAN-2026
DEFINITION  exonuclease SbcCD subunit D [Sinorhizobium medicae].
ACCESSION   WP_457662947
VERSION     WP_457662947.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=41346
     Region          1..268
                     /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 mkilhtadwh lgrqfygqsl evdhdsildq vlravrtysp dvlviagdif drasppatav
       61 rqfnsfirmv hadcdtsivl iagnhdsgdr iasyasladp krllirgpls peerpliled
      121 eygpvafsgl pfgnefsare cygngsiscp advvaaqvac arthvpgnar wviaahvfva
      181 natpsesers lqiggietvp ssvfdgahyv alghlhrpqs aggehirysg splafgfdea
      241 gssksltmvd laadgsvtlq qlpinpprav rvlkgefeel rdigsrepse dfiklvltdk
      301 kllidpmgri rehypnalal iyerdesaep illrgssqar lddpvavvge flsqvrgedg
      361 tddemalvss glkqlnsvee ra
//
LOCUS       WP_457662950             942 aa            linear   BCT 27-JAN-2026
DEFINITION  UvrD-helicase domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457662950
VERSION     WP_457662950.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..942
                     /product="UvrD-helicase domain-containing protein"
                     /EC_number="3.1.11.5"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=102157
     Region          <171..938
                     /region_name="RecB"
                     /note="3#-5# helicase subunit RecB of the DNA repair
                     enzyme RecBCD (exonuclease V) [Replication, recombination
                     and repair]; COG1074"
                     /db_xref="CDD:440692"
ORIGIN      
        1 mvfsvaadaa iaakagvlnp laerfgyndp rrpdsgeppd wrrtvraivt lsrangldae
       61 gllasaersv etyrallpsp aadgaaldea laaalaaava arpaqpsata akdlptiraa
      121 herasrgevl nwpiwaklik vacartkdgp vyaealadli aaagrhvdhp rlrteteqfi
      181 retficaaea ltayhnwkae rglldftdqe alalevlkdp vrvgrlrehv grvfvdefqd
      241 ssplqlavft alaevaeest wvgdpkqaiy gfrgadtdlt qaaftgagda aepqdvlsks
      301 wrsrpgiiel snalfipafe rmglpaahha fssaarsdvg fdrppiawwp llgkvdeqaq
      361 alaegirrcl anasqwlveg arrehrplrs gdiavlcrtn tdvarfaral sraglpvave
      421 rsglartphv elvlaacrwv adasdrlala elarffgsdp gsddwlraaa sedapaalra
      481 qvpvadaler lrervlsltp aelvdsvlal ptmmahieqw gdpaihfddl ealrgfaaay
      541 egecaasgap atlqglllsl dgadpkrpps lardaiqvmt yhgakgrewp mtvltglawe
      601 pkarlfepva evdgeldwra plerrwirfw pwpygqsgkd salevaafts eigqaawrra
      661 vhedirllyv gvtrardylv fappakgtln wlklldepda aphvvppaad dnllsvgdqt
      721 fvadvrplaa idapeercpq lsfvrprsap versplylrp sqaeggdwrv vervslggrl
      781 pidgvadmaa lgealhaiia yddvcrdtaq rladadatla rwgvkgfaav daltaserlc
      841 awlrtrwpng nllhetpvta rfgdqlvqgr idllvsfedg saivdhksfp grvdqwegha
      901 lrhapqlgly geavaavsgr scdelwihmp vvgallrver te
//
LOCUS       WP_457662964             247 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457662964
VERSION     WP_457662964.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 247)
  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 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=27911
     Region          17..186
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 msmagdldpw qvscelrvdi flsqpreasv rlwnaardvl neeerqrarr fvfdrdrdmy
       61 vfshgllrll larymvadpr eltfasapgr rpelvspssa pirfnlshtd glvgciltqk
      121 adcgldveqi grvdyrhlvp tvlapeersa llglaeadrp drfceiwtlk eaylkgrglg
      181 isypirnisf sgfdgdrrcr vvgderddgs twhfwsrpfa gaysaaaavr tqrddvkfsa
      241 tfiedlp
//
LOCUS       WP_457662969             171 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457662969
VERSION     WP_457662969.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..171
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=19183
     Region          8..>159
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msdhnapsls tlvqrffleh lgqhravsre tvaayrdtlr lllgfaaqrl hrtpsaitll
       61 eldaplllaf ldhlekergn svrsrnarla airtflkyag hhdigalatl aipqkrferp
      121 mvgflsrdei rtiieapdak twagqrdram fstlyntgap rwctdrlavv v
//
LOCUS       WP_457662973             308 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457662973
VERSION     WP_457662973.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34156
     Region          28..75
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          107..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(120..121,123,127,129..135,226..231,237..238,
                     240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdelscrrkn lasvdlnllv alealleyrh vthagqhvgk sqpamsrald alrgvfnddl
       61 lvrgssgyvl tpegqrlael lpsalnmirr mvtndsstak ewrskttvam pdhqtmillp
      121 rlmqraphle ivpqslsksv lrgleqgdvd lavgqldavp pgylrrslyt dqfvsllrhd
      181 hpalarawti esfmalrhta vssnsnnqgs riydelpelq lpdhnpmrls hvltaamvva
      241 ttdlalmvpr raadlisaml pltavdppla lkpyevmliw herchhdprh kwlrgqfaaa
      301 vapgahce
//
LOCUS       WP_457662977             391 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662977
VERSION     WP_457662977.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42266
     Region          2..391
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mrperskssg siindpqvrg ifyqaitiii laaliywivd ntvdnlrran iasgydflrs
       61 ragfdvgqsl isftsdstyg rallvgfint llvaitgiii atiigflvgi grlshnwiia
      121 klslayvevf rnippllvif fwysgvlsil pqardalalp fdiflsnrgv afprpvageg
      181 aeytllafii aiaasvfftr yarqrqlatg erlpvlwtvl gliiglplit flvtgapigf
      241 dvpvagkfnl tggsvvgpef mslflalsfy taafiaeivr agirgvskgq teaahalgir
      301 palttrlvvv pqamriiipp ltsqdlnltk nsslavaigy adlvavggti lnqtgqsiei
      361 vsiwlivyls lslatslfmn wynarmalve r
//
LOCUS       WP_457662978             384 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457662978
VERSION     WP_457662978.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..384
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41643
     Region          172..383
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mstnqasfvr asmieaspap slesgvvswl rknlfatpkd taltiislli lawlvppaiq
       61 wlfidaawsg ggrgvcatls qggsqpegws gacwafvnak faqflsgryp lderwrpalv
      121 gilfvlllvp mlipripykg lnallllval pilsaillpg gwfgltyvet plwgglmvtl
      181 vlsfvgiavs lplgillalg rrsnmpvikm lctafievir gvplitvlfm asvmlplflp
      241 qgvtfdkflr aligvslfas aymaevvrgg lqaipkgqye gadslglsyw qkmgfivlpq
      301 alklvipgiv ntfiglfkdt slvsiigmfd llgivrlnfs dtnwasavtp ltglifagfv
      361 fwlfcfgmsr ysgfmerlld rsqr
//
LOCUS       WP_457662988             226 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662988
VERSION     WP_457662988.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23626
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavd wargpngcpi faqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarggyftpg anpsaaggei aavavlerhg
      181 alfplgddnl slpdygaagg dpaktlasql erlglsvhdw fslldl
//
LOCUS       WP_457662990             412 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Sinorhizobium
            medicae].
ACCESSION   WP_457662990
VERSION     WP_457662990.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46284
     Region          18..399
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtanptsihq rldrrlsgfs leqpfytspe vyaldlqhif ykqwlyavpa cqlakagsyt
       61 tlrvgayevv ivrgrdgevr afhnscrhrg slickaregq vaklvcpyhq wtyeldgkli
      121 wandmgpdfd askyglkpvn lrnldglvyi clsdtppdfq tfaqlarpyl evhdlkdakv
      181 aftstiiekg nwklvwennr ecyhcssnhp alcrsfpldp evagvqadgg vskklqahfd
      241 rceaagtpaq fvlagdgqyr larmplqeka lsytmdgkaa vcrhlgrvap pdagtllmfh
      301 ypstwnhflp dhsltfrvmp isptetevtt twlvhkdave gvdydlkrlt evwiatnded
      361 reivetnqqg ilspayvpgp yspgqesgvm qfvdwyaawl eralaprqva ae
//
LOCUS       WP_457662992             694 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457662992
VERSION     WP_457662992.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..694
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=78917
     Region          18..427
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mstdnamkis adhlrrdafl yvrqsslrqv fentestkrq yalrdraval gwpiervhvi
       61 dndlglsgaq sqdrdgfqrl vtevamghag ivlglevsrl arnnadwhrl lelaamsrtl
      121 imdedgvyda asfndrmllg lkgtmseael hilksrlqgg ilnkarrgel elplpiglvy
      181 tpdmrvvldp drqiqdtvrm lfdtfrevgs acavvrrlrs ekilfprrir rgigkgdvlw
      241 seidhsrviq ilhnpryaga faygrtrtvy naklksvqqk mprsdwqvli pqahegyisw
      301 defernqtsl eqnavgfspg lrgrmprqgn gllqgrvlcg rcgarmrvhy eqfegnlrpy
      361 yicneavvrh agkacqwarg paideavsal lleamaptai evalavqeei sqrveqaasl
      421 rdkqlqrary eaelarrryl kvdpdnrlva daleadwngk lrdldtlqre herqnetdqs
      481 lldgamqeri ralaadfpri wnnkrtspve rkrmlgllie dvtllvdeqi nmhirwrggr
      541 tqslavarpr pmavirktpe avvalinell etdndqqias rlnalghrnw rgeaftlkkv
      601 mlvrrayglk trferlresg mltgeevarr fgvsattvhq lgrdgvlkrh ryatnhryly
      661 eppgnvrlak gvggrygsrq prlmdaqqiq qgas
//
LOCUS       WP_457662993             241 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Sinorhizobium
            medicae].
ACCESSION   WP_457662993
VERSION     WP_457662993.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..241
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25698
     Region          21..197
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mdnqhraggy dslrsnrdgq aeafdaigah ydeafpnkqg qvlagdwlir slptgarvld
       61 lgcgtgvpta rqlvasgfev vgidlsggmv klarecvpga tfhqmdiadl rpggprelgq
      121 fnavaaffsl lmlpraeipl alltirnllv pgglfalsmv eadvddfsip flgnnirvsg
      181 ylredlraii aeagfqivee tsysyatavg vppeeqiflc crmgfsrsgs mrissigksa
      241 m
//
LOCUS       WP_457662997             400 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent nuclease [Sinorhizobium medicae].
ACCESSION   WP_457662997
VERSION     WP_457662997.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Akritidou,K. and Thurtle-Schmidt,B.H.
  TITLE     OLD family nuclease function across diverse anti-phage defense
            systems
  JOURNAL   Front Microbiol 14, 1268820 (2023)
   PUBMED   37840731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Schiltz,C.J., Adams,M.C. and Chappie,J.S.
  TITLE     The full-length structure of Thermus scotoductus OLD defines the
            ATP hydrolysis properties and catalytic mechanism of Class 1 OLD
            family nucleases
  JOURNAL   Nucleic Acids Res 48 (5), 2762-2776 (2020)
   PUBMED   32009148
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S.
  TITLE     Structural characterization of Class 2 OLD family nucleases
            supports a two-metal catalysis mechanism for cleavage
  JOURNAL   Nucleic Acids Res 47 (17), 9448-9463 (2019)
   PUBMED   31400118
REFERENCE   4  (residues 1 to 400)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..400
                     /product="ATP-dependent nuclease"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004527 - exonuclease 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]"
                     /calculated_mol_wt=44463
     Region          1..>390
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mhieslsirn frcfgdeavh inlaaginaf vgnngagkta alealkrlfs piaaerqirr
       61 sdvhfglged ihtikgsere ivieavfgfp gnttnaqvft dlffngidks lkvrvrleck
      121 ysranaiddd letkfyavrt ldpvpfgpdd erktplrgrp tqyaevvyip ahrdsrgvsq
      181 talrnllqrl ersadwdent kskskgfaed lqknlnetpa lkmvtqtleg fwaslhdghy
      241 dgkvelgvia tefqklirdl tlrfmkapgg glrqldelse gqtsllyfal satlhklmsd
      301 mqkaapkkle gfvvpdfiyp pltifaleep enhlapfylp klislldtln kdgtaqavvt
      361 shatsilsri pprhvryfrm epsfltsrvl alppsgkgig
//
LOCUS       WP_457663002             206 aa            linear   BCT 27-JAN-2026
DEFINITION  Fic/DOC family protein [Sinorhizobium medicae].
ACCESSION   WP_457663002
VERSION     WP_457663002.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Veyron,S., Oliva,G., Rolando,M., Buchrieser,C., Peyroche,G. and
            Cherfils,J.
  TITLE     A Ca2+-regulated deAMPylation switch in human and bacterial FIC
            proteins
  JOURNAL   Nat Commun 10 (1), 1142 (2019)
   PUBMED   30850593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kinch,L.N., Yarbrough,M.L., Orth,K. and Grishin,N.V.
  TITLE     Fido, a novel AMPylation domain common to fic, doc, and AvrB
  JOURNAL   PLoS One 4 (6), e5818 (2009)
   PUBMED   19503829
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..206
                     /product="Fic/DOC family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /GO_process="GO:0018117 - protein adenylylation [Evidence
                     IEA]"
                     /calculated_mol_wt=22967
     Region          9..205
                     /region_name="FIDO"
                     /note="Fido, protein-threonine AMPylation domain [Signal
                     transduction mechanisms]; COG2184"
                     /db_xref="CDD:441787"
ORIGIN      
        1 maderpkgsy typntsddpd rtnvlknrwg iethselrvk eyratavrma elaegdgpqg
       61 nfdkahlkai hgyifqdvye wagqtrnesp vvegqrvepi gglskggtsf lpgsriemgl
      121 dealkpirdp qalrnatiee fperteqvls eqnfvrpfre gnghaqeaci celgrlygre
      181 idvsvitkpr mieasiattn drpvpq
//
LOCUS       WP_457663005             434 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663005
VERSION     WP_457663005.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..434
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46541
     Region          1..420
                     /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 mahdiiegrl egndrlpphr dvayqlsigv gtvtkayavl errglirsek grgtfvaalp
       61 atsepvidls vntpprllse rmlsktltsi arninsdlft qyppdgghae hrrqmvqwla
      121 glgmlakvdq lllcngaqqa ltvafsvtse angiilteaq typgaisfar hnghclrgvk
      181 idregmrpda ldrvlqragg enkravvyvt ptlqnpttvt mgesrrrdiv svcrkhdvmi
      241 ieddvyslgs tglsplamla pertfyvnsl sktvspglri gslvapacfv gqaevvlsat
      301 ssmvspfsca vmaewlvngt aesvrrsiga essrrlelak sqlgdaaifp eyegfhiwlp
      361 melgtadsfv tasqavgilv tppsatavap dggdggirlc vggpelsdlk aaleklsliv
      421 mncgrrqqph rsyv
//
LOCUS       WP_457663006             342 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663006
VERSION     WP_457663006.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37198
     Region          38..320
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mrhtfpsklt fgifdhlded grdiaqqfad rltlaetcdr lgfyayhlae hhctphgrga
       61 spnlflssva qrtrqlrvgp lvmllslshp lrafeeicml dqlsggrlel gigcgslpie
      121 lsyfgigada vperytease ilvkamkggt lsyqgkhfel ndvpltlrph qrphpptwia
      181 tngpesaawa aanganiacl gpasvvrkit dafrshpeqn tdaddrapfl gllrmvvvgh
      241 sathahslaa paydrwvknf kflydvnaip vppnlpmtld aaieselcvv gtaafvrral
      301 ldqleeagan yllcqlafgd lslhasqnta laiqsgimdr vd
//
LOCUS       WP_457663011             424 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease [Sinorhizobium medicae].
ACCESSION   WP_457663011
VERSION     WP_457663011.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..424
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44904
     Region          22..419
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtlfhlagps llvvvlflls tpitwamaig alafflinmd mipltnfaqe vaegtqsvsl
       61 lalplfvlag cimnasgitr rlltladvlv ghmtgalaqm ctvlgtllgg ltasanadaa
      121 mlaktlgvem sergysrafa avitssaaii tslippsigr lfaagvvpgl llaaglmvtt
      181 yfiarkrgyk plrkqratra eatralidgl walsipvvif agtryglftt teagavvvvy
      241 vlfvavfgyr eftvrqvpev laeavrdsav vmimicaaaa fgfylaweqv pqamsgwlgd
      301 atdnpllmll linvllivig taiegsaali iltpmlipli dgvgidrvhf givfitnlti
      361 agitppvggl myissmvlkv pmmayarevl pylammmall vvlsmfpqls lwlpdlvygt
      421 savq
//
LOCUS       WP_457663016             445 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Sinorhizobium medicae].
ACCESSION   WP_457663016
VERSION     WP_457663016.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48255
     Region          14..421
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(27..28,31..32,35,74,132..133,135..137,140,160,
                     163..164,167,249,252..253,256..258,261,289,293,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mlntagstre sevrrvvfas ligatiewyd fflygviagi vfnqlyfpsh dplvsmvlay
       61 atfavgfvar plggivfghf gdklgrkqml vltilimgva tvligvlpty eqigvaapil
      121 llilriaqgi giggewggav lmayefaped krgyyasipq iglaiglcls sgvvallsll
      181 peaafmswgw rtafigsvvl ivvglyirlk vaetpdfasv keerqelkip fvelirtypr
      241 nillgmgary idgvffnvfa vfsivylskh vqvdrttalw lvclsalvmv vtiplfgkls
      301 drwgrpktya igslllalvt fpafmlmgsg slplialali apfgiiyamc ygpeaalfsd
      361 lfdvkvrytg isfvyqfsgi fasgitpiia tflisygdgs pwllaayvvf aalvsmvsam
      421 lirpvsqtrt tlphkplrps tvhts
//
LOCUS       WP_457663018             232 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457663018
VERSION     WP_457663018.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bondos,S.E., Swint-Kruse,L. and Matthews,K.S.
  TITLE     Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox
            Proteins
  JOURNAL   J Biol Chem 290 (41), 24669-24677 (2015)
   PUBMED   26342073
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Ravcheev,D.A., Khoroshkin,M.S., Laikova,O.N., Tsoy,O.V.,
            Sernova,N.V., Petrova,S.A., Rakhmaninova,A.B., Novichkov,P.S.,
            Gelfand,M.S. and Rodionov,D.A.
  TITLE     Comparative genomics and evolution of regulons of the LacI-family
            transcription factors
  JOURNAL   Front Microbiol 5, 294 (2014)
   PUBMED   24966856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Swint-Kruse,L. and Matthews,K.S.
  TITLE     Allostery in the LacI/GalR family: variations on a theme
  JOURNAL   Curr Opin Microbiol 12 (2), 129-137 (2009)
   PUBMED   19269243
REFERENCE   4  (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   5  (residues 1 to 232)
  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   6  (residues 1 to 232)
  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 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   8  (residues 1 to 232)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   9  (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
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
REFERENCE   11 (residues 1 to 232)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
REFERENCE   12 (residues 1 to 232)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..232
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25039
     Region          23..68
                     /region_name="HTH_LacI"
                     /note="Helix-turn-helix (HTH) DNA binding domain of the
                     LacI family of transcriptional regulators; cd01392"
                     /db_xref="CDD:143331"
     Region          83..>187
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mgkgnggngs pkdagggrpt mtdvariagv sqssvslvln emsgarisae trtrvrdaar
       61 kigyrlpntr qdpdhapaie kdtiafivde istsphpvvs ldgirdyafe qgllvsahat
      121 rsnpdlesav lrsvlrdpai agviyatift rkvsvprelg nvptillncy aeprqhmaiv
      181 pgevagglrg drashvsrap ahrlhqrrtl dgrryrpaqr lqaslgdrry rl
//
LOCUS       WP_457663020             377 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663020
VERSION     WP_457663020.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..377
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41658
     Region          5..355
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mqvvrdqqld glravavtmv lyahffaadg shwghlgvrl ffvlsgflit rllldardaa
       61 rfepstalks fyarralrif ppyfavlavv flldlerske vmawhglyls nfwyalqnew
      121 spwvlchtws lsieeqfylv wplvvlllpr rsiagvcigv ivcslvyrly wpftgtpsla
      181 rdllppasmd alavgallaa rpswraawpr waelswipls ivsfalvwlk pvpmtpviaw
      241 lawiglevvp llplamlvgs csegiggiag rvvalspvaa lgrisygvyl fhavvlavvv
      301 qaqpfipvnv tdqgvgrfvv agaltlmlas aswilfekpl nglkrhfpyv rpegaagpvt
      361 avprvrrdea lqtpplr
//
LOCUS       WP_457663022             593 aa            linear   BCT 27-JAN-2026
DEFINITION  adenine deaminase [Sinorhizobium medicae].
ACCESSION   WP_457663022
VERSION     WP_457663022.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Sterner,R. and Hocker,B.
  TITLE     Catalytic versatility, stability, and evolution of the
            (betaalpha)8-barrel enzyme fold
  JOURNAL   Chem Rev 105 (11), 4038-4055 (2005)
   PUBMED   16277370
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Roodveldt,C. and Tawfik,D.S.
  TITLE     Shared promiscuous activities and evolutionary features in various
            members of the amidohydrolase superfamily
  JOURNAL   Biochemistry 44 (38), 12728-12736 (2005)
   PUBMED   16171387
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Ribard,C., Rochet,M., Labedan,B., Daignan-Fornier,B., Alzari,P.,
            Scazzocchio,C. and Oestreicher,N.
  TITLE     Sub-families of alpha/beta barrel enzymes: a new adenine deaminase
            family
  JOURNAL   J Mol Biol 334 (5), 1117-1131 (2003)
   PUBMED   14643670
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Gerlt,J.A. and Raushel,F.M.
  TITLE     Evolution of function in (beta/alpha)8-barrel enzymes
  JOURNAL   Curr Opin Chem Biol 7 (2), 252-264 (2003)
   PUBMED   12714059
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..593
                     /product="adenine deaminase"
                     /EC_number="3.5.4.2"
                     /GO_function="GO:0000034 - adenine deaminase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006146 - adenine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61790
     Region          29..584
                     /region_name="AdeC"
                     /note="Adenine deaminase [Nucleotide transport and
                     metabolism]; COG1001"
                     /db_xref="CDD:440625"
ORIGIN      
        1 mnamqerndl ndaglrarav aaargdagfd vlvaggtvvd vvtgecraad igivgamias
       61 vhapgsrkea gtvieaagay lspglidthm hvessmvtpa vyasavvprg vttvvwdphe
      121 fgnvsglagv rwaadatrgl plravvlaps cvpsapglel agadfgaaei aemlswreig
      181 giaevmnmrg vidgdprmsa iveaglksgk svngharglt dadlqafvta gvssdhelvs
      241 gedliaklra glsielrgsh dhllpdfvra ldalghlpqt vtlctddvfp ddlhrdggld
      301 nvvrrlvryg lkaewalqaa tlnaarrlgr adlgliapgr radivlfedl rdfralhvla
      361 ngrlvasggt tlqaaavadv aplcgtmkig rlkeddfrip asgstarvat inrprftqwg
      421 evtamvsdgy vvppedttli avahrhgrad nrprvglleg wgawrgafat tvshdshnlt
      481 vfggnprdmt vaanavieag ggmavvsegr veallplplc glvsdaplad vaavfaaire
      541 aagrivewqp pylvfkacfg atlacnagph qtdrgiadvv tgtllespvl etf
//
LOCUS       WP_457663023             340 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663023
VERSION     WP_457663023.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..340
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36887
     Region          25..290
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(32,166,224,250,252)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 mknimlassa llligttaas aqeetltisv ygfaqdafke lvydpfeakc gcklvvetgn
       61 sverlakmea nkanpvvdma vvsmadalsa trsgliekid asklsnfdkl ydiakdpngd
      121 gmsvgytfya tsivyrsdrv evtswadllg dklaghvalp nvttnqgppt lymigealgq
      181 ntpdlkpaia avgekkddiv tfyvkssqlv qlmqqeeiwa apigrfsweg ftkmdlpikw
      241 atpkegqtgg mnvmvlakgs knqdlalqfm dfwlsteiqt alaeklvdsp ankevkvspe
      301 iaenltygee tvrnlklips avaldnrdaw lsewnakvgq
//
LOCUS       WP_457663024             465 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide sugar dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457663024
VERSION     WP_457663024.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..465
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=50592
     Region          39..452
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mvpaagppep hhrqqnwkpi ltsphhdrll esisrrtarv gviglgyvgl plavatarsg
       61 fqvtgfdvdp gkivaldagr syieavedes lareseagrf rsttdfsdlg lcdviiicvp
      121 tpltrhrdpd lsfventsrs iaaslrpgql vvlesttypg ttdgivrsil eetglrsgtd
      181 ffigfspere dpgnrsfktt sipkvvagdg plaaalmerf yaavvttvvp vssnataeav
      241 kltenifrav nialvnelki vydamgidiw evieaaktkp fgympfypgp glgghcipid
      301 pfyltwksre yelptrfiel ageinsampr hviarlaeal dkregkalsr ssvlvvglay
      361 kknvpdires pslklielie erggkaafyd phveeipatr eymalkgrrs vvfdeatvrs
      421 fdavliatdh davdytglag wsplivdtrn vfarrglaag hivka
//
LOCUS       WP_457663026             256 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663026
VERSION     WP_457663026.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..256
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28550
     Region          25..251
                     /region_name="CE4_u4"
                     /note="Putative catalytic domain of uncharacterized
                     bacterial proteins from the carbohydrate esterase 4
                     superfamily; cd10928"
                     /db_xref="CDD:200554"
     Site            order(29..32,82..86,132,134,180,218,220)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:200554"
     Site            order(31..32,82,86,134..136,220)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200554"
ORIGIN      
        1 mkmgsawqrc vdrldalqdg gqcidfwlrd ddavepspal drlldltgrf svpvtlavip
       61 astderlsrs lssrmhidva vhgwshrnha laiekrqelg ahrpretvaa dlragwarls
      121 alypaalapl lvppwnridp glvselqdig fealsvfgpe dgekcaafrd aglqlinthv
      181 dvmdwhgtrg crphgdilrd idrrldeven sggsvgilsh hlvhdesvwe flsklfeitt
      241 shpacrwrri telidr
//
LOCUS       WP_457663028             828 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457663028
VERSION     WP_457663028.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..828
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83609
     Region          2..828
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 mtlngdavvg sislgdgndm allrsgsaed vfgndgidai tldgarvngl idgggaadti
       61 sllsgsaatv aggldadnit ldgtstvtti wgdggavpgg gadtivlksg sartvdggdg
      121 gdgitltgas isgdilggag ddqigllsgt aaavdggtda dtitlgerar tgtingglgd
      181 dlitvdggvn tgfvngdaaa agagdgddrl vwtggaiggf fggngsdtad isglpvsgpe
      241 lvldggddva tadgmtdrlf vtgltyddai ganvrnwefi rldnaavtit dgalatgsda
      301 gmglfltrgs vldgldalal tgnldiekgs tftatgggag iyaisgnlrn agtidmvdgl
      361 tgdrltvagd ytgldnalrv dtylgddssp tdlvfvggdt mgtmdlfvns tdpaapgaqt
      421 dkgirvvdvg gasngvfkle npnstlaatg edsitqgaya yalrkggggd wylqsellag
      481 pvdpvdpvpt fnqgagvyet yaqdllaftr lpslrqragn rswampaapv cfadgqgren
      541 agnapaciee gglwarsege tadivpqvss agvsgydrdi grieagidgl lhesgqgkli
      601 ggvsahygsg gssvasfhgg geidsraygm ggtltwygqn gfyadvqgrl nwfssdlasa
      661 llgnlasgnd gfgyglslea gqrfaigdnw altpqaqlsy asvdfdgftd pfaarvsled
      721 gdslrarigl sidyeniwqg qqgdtrrmqv ygianvihdm sgrtrarmsd vtldsrpdsw
      781 tgevglggsy nwgddkyaly gelraatglt dfgdshalgg tvglrvkf
//
LOCUS       WP_457663031             226 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Sinorhizobium medicae].
ACCESSION   WP_457663031
VERSION     WP_457663031.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24684
     Region          <7..201
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mktfrepaav slglpaslky yrlkrlldcl lagtvfvlcl plmaatavvv waalglplff
       61 sqaragaemr vftvakfrtm tdarasdgtl lpddmrqtas tallrrlrfd elpqliavlc
      121 ghmsmvgprp lpvatvagfg elgrmrcrva pgmtgwaqvn gntrlsddek ialdlwyvah
      181 anlwldaril lltvktlvtg ervhavhlqe arvflsrrlg aepska
//
LOCUS       WP_457663032             452 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Sinorhizobium medicae].
ACCESSION   WP_457663032
VERSION     WP_457663032.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..452
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47971
     Region          28..437
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mafrkklfkk igglrqilsr ektmlerlqs iahlltgnil ssvigligfa ltaralgpag
       61 ygilalcfsy traverivsf qswqplikyg ahslsdnadd fkemqsllkf gllldvsaal
      121 agwliavlfi llaspwlgis adgaslaiiy ctvlpfqvsg mptavlrlyg rfmaiaygqv
      181 atsvlrvalc aigvamgagl feftliwmsa qiigtlvlvl falaelrrqg ilsgllsapl
      241 rgitarfpgl wkfaisanls ltirssanel dtllvgylad ptsaglyhia krigriaqqa
      301 gvqvqavlyp elarawaaka lgafhravaq mqalllacgl fligglylli gpllswaagp
      361 efaaagplvi vqsiavtmtl cgavirsall amgreneilr svtiaaigfh atafaliptm
      421 gamganvahi vmasiwlstm mlsyrrtpap gp
//
LOCUS       WP_457663034             408 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457663034
VERSION     WP_457663034.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 408)
  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 408)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..408
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=45150
     Region          35..400
                     /region_name="GT4_CapM-like"
                     /note="capsular polysaccharide biosynthesis
                     glycosyltransferase CapM and similar proteins; cd03808"
                     /db_xref="CDD:340837"
     Site            order(60,235..237,299,322)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340837"
ORIGIN      
        1 mtlvekvpra eadhiaegsa grgsaarfpq qkrviavvas ltaslvifrl ellkrlvaag
       61 hdviafapeh dprveqelaq igvrliripm artglnpled lrtfwalrrh farlkpdivl
      121 pytmkpiiya giaartlgir ercflvtglg hifsdaagas lkakairhlc vrlyrtalrg
      181 arvvfvynda dendirryrm lsghlsptmi sgsgvdldhf afstpprggp tflmvarllr
      241 dkgvveyvea arivrrsfpn arfqllghfd snptaisree idawahegil dylgttvdvr
      301 pylaacnafv lpsyyregip rsilealatg rpvittdlpg crdtvqpgkn glvvkardva
      361 alaeamttva knpelaeemg rrsrelaetr fdvhminrml fdgmhltd
//
LOCUS       WP_457663035             387 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663035
VERSION     WP_457663035.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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..387
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..387
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39077
     Region          42..296
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 milkgtnlsd tingalgnde lwgyagddhl dggdgndkif ggdgndfivg glgddyaegg
       61 agndrfdggl ghdtlkgglg ndifdggdgs dvldggdghd qilggrghdk ifggageeyi
      121 dagdgddiiy agsgddgfnn rvnpatgqvt qqavsggagh dkiygedgnd alkgqsgndw
      181 vyggigndiv dggdgnnyld ggegndvlds eggideahgg sgndkvvvga gddrvfgddg
      241 ddmlygeagn dvlnggnnyd rifggdgndt lrgdagqdvl vgeagsdilw ggtesdrfvf
      301 kgavalsgqd tvmdfqdgvd flvieklgik qysssgaagt vyaydatdgd vlvkgydaag
      361 tafsilvddp ngtlsaanfs ssdflfa
//
LOCUS       WP_457663036             308 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663036
VERSION     WP_457663036.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..308
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32010
     Region          2..295
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrlvvtgatg fvgarvidca lsrgyevtal ardperiatr kgsglrveqw tvgdplpplg
       61 rsdavlhlaa hipadlsdpr easrcfevnt ngalevamqa alqgvsrfvq fgsaqvyapg
      121 tgpasetspa fpvhrasyyl asklaaeicl lafgkasamp vtvlrlasvy gpgmhdagmv
      181 ptfvrtlgrg gsliiqdggr ytvdlvyvdd vvslaleaae raeggvfnag sgractslea
      241 ahivadavga eqhliavegg sidaappgfr pldvskaidg lnyaplsfre gieawrtmtg
      301 ltdfqdga
//
LOCUS       WP_457663040             293 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663040
VERSION     WP_457663040.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..293
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31460
     Region          21..288
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtgtwistra wllvlpllvv mtavigwpli dtvrlsftda kligteggfv gadnyarmlt
       61 gsnfqralit ttwfavisva aemvlgvlaa lllnqkfrgr tvlralmilp walptvvnat
      121 lwrliynpey galnagltqi gildsyrswl gepgtalaal ivadcwknfp lvalialaal
      181 qtvprdinaa sivdgagpfn rfrfvilpyl agpllvalvl rtieafkvfd iiwvmtrggp
      241 anstrtlsil vyqeafsfqr agsgaslali vtllvtilav ayavllrkaa gas
//
LOCUS       WP_457663041             281 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663041
VERSION     WP_457663041.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 281)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..281
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29486
     Region          3..281
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 merqsplfsv fihasalala ivilapvawl fimsispaad lsakplawwp sdidlsryrt
       61 llsavensag aafiasllns lkvagmatla avvvavpaaw avsrtpsvsw slyvviatym
      121 lppvalavpl ymglahfgll nsvfglalvy ltilapfttw llksgfdaip reiesaamid
      181 garldqilrl ltlplaapvm atsalfafll awdeffyall ftsdqraktl tvaiadlagg
      241 rvsdygliat agvlaalppv liglimqkal isgltsggvk g
//
LOCUS       WP_457663042             341 aa            linear   BCT 27-JAN-2026
DEFINITION  SIS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663042
VERSION     WP_457663042.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..341
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34724
     Region          59..341
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 mnmstskdrp aglvaidrem arqhgdavas yqeaaataqr iaaslnstgr llllgmggsh
       61 avgraveply ralgidaval plseqlgqpl piegktilvt sqsgesaevl rwfretdggt
      121 setfgltlee daflakavps lvgtggteqa faatrsltvt falhlailaa lgadpaealr
      181 alktpeapai ddalamltgv gaivtsgrrl qgiaeaialg vtelsrlpcf sleggqlrhg
      241 pmemlgpsma vilfraadpt aglvgamavs aaeagspvvv fdasgepaaa gattirfepa
      301 agmaaifaml pvaqslmiaf adahvenagt pvrstkvtrs e
//
LOCUS       WP_457663044             360 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663044
VERSION     WP_457663044.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39156
     Region          1..357
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msaleirnvh krygevetlk gidialesge flvllgssgc gkstllniia glsepsggdi
       61 ligersvlgv hpkdrdiamv fqsyalypnl tvarnigfgl emrrappaer dkavrdtarl
      121 lqiedllerk psqlsggqrq rvaigralvr dpqvflfdep lsnldaklrm emrtelkrlh
      181 qmlkttvvyv thdqieamtl atriavmrdg rieqlatpee iydrpatlyv agfvgsppmn
      241 ildaevtasg lkldgceevl plpaafdgta lagrrvkvgi rpeairlaae sedprltadi
      301 evveltgpel vttatvgrqr itaclpprta lgtgsvhaft fdetamhlfd pksgrslkvg
//
LOCUS       WP_457663045             283 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663045
VERSION     WP_457663045.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..283
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31461
     Region          23..271
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrsradlsgk edavadaddt inrrargldr afeildflrv qrqplrpnei aqgigaprss
       61 vyelvnlllr qnileyrgdd grvflgrkly flgaayaeqf dlmrecehll ariagetret
      121 aqmcqlegsk yavvlmnegs rpfristsig epvaipwtas grllvdhmsd eeiiafippe
      181 dfvlpdgtrl epaefiaqvr nakkegyftf nsivdsfthc favpvydaea iciatlclva
      241 pkedglrnre aylrvlidga gelseklgyr ndlaasvraa sar
//
LOCUS       WP_457663047             219 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663047
VERSION     WP_457663047.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..219
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23717
     Region          1..218
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mdvsfidqlw laripllkgl gisvsisfls ivagtvlgvf vglalvygyr pvrwivrgyt
       61 dfirgtpvlv lvlasyyvls aigidlgpfq agvlalavfc sshvgelvrg alqsipkgqt
      121 eaakaigltf aqtfayvlgp qalrqalpaw vntaaemvka stllsiigvg elllrthevi
      181 srtfmslefy ffagflyfvi nygierfgry verktavps
//
LOCUS       WP_457663049             885 aa            linear   BCT 27-JAN-2026
DEFINITION  nitrate reductase [Sinorhizobium medicae].
ACCESSION   WP_457663049
VERSION     WP_457663049.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Jacques,J.G., Burlat,B., Arnoux,P., Sabaty,M., Guigliarelli,B.,
            Leger,C., Pignol,D. and Fourmond,V.
  TITLE     Kinetics of substrate inhibition of periplasmic nitrate reductase
  JOURNAL   Biochim Biophys Acta 1837 (10), 1801-1809 (2014)
   PUBMED   24882638
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Najmudin,S., Gonzalez,P.J., Trincao,J., Coelho,C., Mukhopadhyay,A.,
            Cerqueira,N.M., Romao,C.C., Moura,I., Moura,J.J., Brondino,C.D. and
            Romao,M.J.
  TITLE     Periplasmic nitrate reductase revisited: a sulfur atom completes
            the sixth coordination of the catalytic molybdenum
  JOURNAL   J Biol Inorg Chem 13 (5), 737-753 (2008)
   PUBMED   18327621
REFERENCE   3  (residues 1 to 885)
  AUTHORS   Stolz,J.F. and Basu,P.
  TITLE     Evolution of nitrate reductase: molecular and structural variations
            on a common function
  JOURNAL   Chembiochem 3 (2-3), 198-206 (2002)
   PUBMED   11921398
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Thomas,G., Potter,L. and Cole,J.A.
  TITLE     The periplasmic nitrate reductase from Escherichia coli: a
            heterodimeric molybdoprotein with a double-arginine signal sequence
            and an unusual leader peptide cleavage site
  JOURNAL   FEMS Microbiol Lett 174 (1), 167-171 (1999)
   PUBMED   10234835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18697371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..885
                     /product="nitrate reductase"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0042128 - nitrate assimilation [Evidence
                     IEA]"
                     /calculated_mol_wt=95294
     Region          3..700
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
     Region          830..880
                     /region_name="Bfd"
                     /note="Bacterioferritin-associated ferredoxin [Inorganic
                     ion transport and metabolism]; COG2906"
                     /db_xref="CDD:442150"
ORIGIN      
        1 mahevkttcp ycgvgcgvia rlgddgavsv kgdpehpanf grlcskgsal aetldldgrl
       61 lhpeiggrra gwsealdlva erfshaiaeh gpesvafyvs gqlltedyyi anklmkgfig
      121 sanidtnsrl cmsssvaghr rafgsdtvpg vyedlelael vvltgsnlaw chpvlyqrls
      181 aakanrpemk ivvidprrtm tadiadmhla ispdgdvalf ngllahlaas gvidrnyvsk
      241 ctsgfdeava vasrldfpav snatgltqaq lrafyrlfet tenvvtcysq gvnqsaagtd
      301 kvnaiinchl atgrigrpgm gpfsltgqpn amggrevggl anmlaahmdi ekslhrdqvr
      361 rfwgapavan kpglkavdmf ravadgrika lwimatnpvv smpdadavea aikacpfvvv
      421 sdivrdtdta rhahvllpsl gwgekdgtvt nsercisrqr aflrgpgear pdwwqlaevg
      481 krmgfapafa ynsqaeifae haalsgfenn grrdfdisah aeiggtaydg lkpfqwpqtr
      541 gstpqqrrff adgryfhpdg rarfvaievp gprrrdaafp ftlntgrvrd hwhtmtrtgr
      601 sarlsghlae pfveihprda qaigvsgadl vtlesphgaa ivralvtdrq aegnlfvpmh
      661 wndqfasrar idalvapitd pvsgqpaskh mtvragrlaa avygfavsah rpaeldaayw
      721 aiaraeggwr melafaekei dwtdwcrktf giaseiepig ytdrtsgelr laffeedrll
      781 atlflspqpv avarnwavsq lrashhnlgk rfavvagrpg adtpdpgatv cscfsvgvnq
      841 itaavrvgch sveavgekls agtncgscra eirgiinacl tvaae
//
LOCUS       WP_457663051             458 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663051
VERSION     WP_457663051.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..458
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49650
     Region          2..433
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
ORIGIN      
        1 mhlardramg gwqiavfepr vrlgcglayd taepahrvnv paarmsidpd dpddfarwla
       61 lqselrddpe vlagdghlyp rrqlfgryva eavvpfvrsg rivhhrervi averegaawa
      121 vrgeggtlnr adalvvatth papeapagig avltghpryv pdstepgald kirtddrvli
      181 igtgltsadv iatlrtrghk gpitafsrrg lrsrghadra qdpfgdfvaq pwrsaaella
      241 qvrrtisdae aegftwhavl dalraqggei wrnlpvderr rlvrharpfw dvhrfrvapq
      301 idaivstglk dgdirvrags iahlaragen vavtfrgrra ggteewefda vvittgpahr
      361 silqsqpwle slgaagylrp dtvglglacs easraldgeg gevddlfvag plargtfgel
      421 mglpqvndha ifvaaqiaal aqarraesvr srreeaat
//
LOCUS       WP_457663055             410 aa            linear   BCT 27-JAN-2026
DEFINITION  urate hydroxylase PuuD [Sinorhizobium medicae].
ACCESSION   WP_457663055
VERSION     WP_457663055.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Doniselli,N., Monzeglio,E., Dal Palu,A., Merli,A. and Percudani,R.
  TITLE     The identification of an integral membrane, cytochrome c urate
            oxidase completes the catalytic repertoire of a therapeutic enzyme
  JOURNAL   Sci Rep 5, 13798 (2015)
   PUBMED   26349049
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..410
                     /product="urate hydroxylase PuuD"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45801
     Region          5..405
                     /region_name="COG3748"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442962"
ORIGIN      
        1 myefaiawew lafaarwlhv vtaiawigss fyfialdlgl vrrdhlppga ygeewqvhgg
       61 gfyhiqkylv apaampehlt wfkwesyatw lsgfamlciv yygsadlfli drhvldisat
      121 tailislasl glgwilydll ckspvgkstw glmallylvl vamawgytqv ftgraaflhl
      181 gaftatimsa nvffiiipnq kivvsdliag rtpdpklgaq akqrslhnny ltlpviffml
      241 snhyplafat afnwviaglv flmgvtirhw fnttharkgk ptwtwavtal lfilvmwlst
      301 vpeiltgeer aetapefqrf adnahfpavs etiatrcsmc haaepayegi vrppngvkle
      361 teaeiaarar eiyiqaglsh amppgnmtem tdeerrlvta wfesavgetr
//
LOCUS       WP_457663056             376 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663056
VERSION     WP_457663056.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40130
     Region          1..357
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mcevlivggg imglwaavma gragfttrll ersrigsgas ggflgalmph mpdrwnekkq
       61 fqfdalvsle geiaeleaat glsagyrrsg rvmpigkahl reiaqgrerd aaqnwrgpah
      121 qylwqvghgd aggwpaadaa pfgivqdtla arvaprnlla vlraaldqfp hvqceegaev
      181 vsiepargrl lladgraltf drmilaagve sfgfidgltq prrsasggav kgqaalfrad
      241 vdkalpiift eglyivphen rqvavgstse srfddpnftd rqldallara idiapvlrsa
      301 tvierwaglr pratglepmv grhpdheslf vltggfkvsf glahalarsv veeiagggmn
      361 alpesfqcah hvaalr
//
LOCUS       WP_457663058             305 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457663058
VERSION     WP_457663058.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..305
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32065
     Region          1..295
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mlarlapaif vllwstgwvv akyaaffadp ltflalrysf aillfvcfcl lsgarwprsp
       61 taighaivsg iflhgvylga vwwaigqgvp aaisgiiagl qplmtaavap wligeklngq
      121 qklglvlgfc gialavapkm vaidasatpi hllplavnva gmaavtygtl yqkrylqngd
      181 lrsiaalqyv galivtipla lmlenlhvtw nlelvaalaw svlglsmgai alllylirrg
      241 qvsraasliy lvpplaagea alffgealtv pmilgtiiav agvyltnrna aepapsavld
      301 tqrpl
//
LOCUS       WP_457663060             432 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663060
VERSION     WP_457663060.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..432
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=47637
     Region          150..423
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mdfvqifrpl eawfrtfvls ewtfyqlgii aagyifaslv asrtepalet rarrikgnpd
       61 llrviiafmr rlkwlfltvw lwlanvvltq stwpsqrwlv staltlaaaw fvisvltkii
      121 rnqtlsrvva vlswgylavy atglegpvls tldaaavnlg amrlsllivl kavvltvali
      181 wvavlagnvl shwvqrsgdl spsfkvlisk iikivlimva gaialsatgi dltaltvfsg
      241 avgvgvgfgl qkvvsnfisg iiilldksik pgdtitlgdt fgsirdlrar fvsvitrdgk
      301 eflipnedfi sqqvvnwsfs seyvridvdf gtsydsdphe vvriaietas avprvannyk
      361 apvcwmtgfg assldfrlrf wisdpanglt nvrgqvllal wdafkeakvs ipfphreiim
      421 ktpveiqrpp ra
//
LOCUS       WP_457663062             261 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663062
VERSION     WP_457663062.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..261
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28855
     Region          30..260
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mkkkpqrtdg taqqsdllld rlaaglseae dhspiymrla lalaeaidtg qlgrgrslps
       61 erllaehldi srvsvrraia eleregrvsr rhgartvvqt rvrkdlpnlt gfsddirarg
      121 mkpsfswisr gtaigtlqet malglpaqse virlirvrla dgspialera vvpksilpda
      181 mlvthslyet laslnampnh gfqriradvm speeaellqa apltpmliae rrcfledgra
      241 veftetryng kvydfisdlh l
//
LOCUS       WP_457663064             435 aa            linear   BCT 27-JAN-2026
DEFINITION  lipopolysaccharide biosynthesis protein [Sinorhizobium medicae].
ACCESSION   WP_457663064
VERSION     WP_457663064.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..435
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46220
     Region          21..413
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 matdgvteqr gykpflpmlm syvasgsslv lgsaaqlltf ailarwlgvh efsvfvaita
       61 vaniavhlcg lgameclvrr vardralypq mlghniilts gsgaalvllg avvlpffftl
      121 spdpmtnvav ialmlvtnil lvraivlteq ifiahtdfas ankvvvafat artvaaalac
      181 iafgattvas wavwqflchv lvavccmwsv rllgapsyrl vreelpqgly fsipfilral
      241 rqnadllvls lvttaeivas ysvarriles sylsvealnr liypgsarat aaglhhaler
      301 vrrvlaaaiv islaaavtvf vlapilpylf gkdylslvgf artlcwvvvp lamwsvavea
      361 lgasgdhaar aavmgfcsia gaglaawasw yappagtfvs fyvieiamvv aswsvflhsv
      421 rrdrlaaitf gsgsa
//
LOCUS       WP_457663066             328 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663066
VERSION     WP_457663066.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33153
     Region          6..222
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mavivgstgy dilqgtdead hiwglhggdt idagggddfv dggdlsdvlt sssgydrlhg
       61 gagddqivlt gtggavtggl gfdrltvdms mlsdelvfng asghgiigyg sagerhvffh
      121 dvewlsivsg sgndrivgta ghdristgag idvvvagagn dvitntggqd rleggdgndr
      181 fvlvgtgstv fggtgddtlt ldlaatsgdi vfnantghai iasrtpderh vfahhseier
      241 ievitgsgnd rvqgttfgdv iktdagddvv dggagddsii dgrganhlsg gdgsdlittt
      301 lysasvdggs gqgfganrgt vtyerrrh
//
LOCUS       WP_457663069             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663069
VERSION     WP_457663069.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35870
     Region          1..321
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maeirlknvs krwhnfvgvd nfdldiadre flvllgpsgc gktttmrmia glddisegei
       61 wlgdrmvnnl epkdrdismv fqsyglypnm svyenirfpl rvrkvpkelh hekvmqaarm
      121 velvdflerr paalsggqrq rvalgraivr qpaaflmdep lsnldaklrv straqiknlq
      181 htlkvttiyv thdqieamtl adrvvvmnkg viqqvgtptd iydnpantfv asfigspamn
      241 lvsgdiengt frgpgitigg lqtnvkgpvt lgfraedasl vseggelgae iysmellgdv
      301 vhaavpasic hlfdartgvr iartpgn
//
LOCUS       WP_457663071             421 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663071
VERSION     WP_457663071.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..421
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=46308
     Region          13..421
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mtitkpgead iamqsptepp silpggsegi wpvrrrriid wlvietrger fidnifvelc
       61 nrlveagvpv aratlhfrih hpqwlgaril wrkglseaql dtyaydveds ieyltsplre
      121 fnegaeevrg hlddpaaagk ayplydelra egltdyliwp lyhtlgkrha itfasdrpgg
      181 fgpddliflk dilpalalvs eirlknrfar tlletyvgph aseqilagat trgsgvtvga
      241 ailicdlrdf tklsdlwprd dviellngyf damsepierh ggeilkfmgd gllaifplsn
      301 pcacsqllga ideaqaalav lneenlrkgh dalgygigvh vgdvmygnig srrrldftvi
      361 gpavniasrl etltkelkrp vllskafvek agcagqlenl gsyvlrglde pvdvfafsgr
      421 r
//
LOCUS       WP_457663072             438 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457663072
VERSION     WP_457663072.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..438
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46315
     Region          <2..438
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 msggegaltl adgirvvdat agattegtaf algapvaagi feyqlyrggv tgdpdndddw
       61 flrsggvspp pppppppppp pppppppppp pppppppppp ppppppppgp ppitpsvrpe
      121 ipgyilkpal vqkmgvaaig tfherqgdef llnsngglpg awgrlfgesf dqswsskist
      181 fdfevspsfs gelwglqagq dligalhddg sqdrvgvffa ytgtsgsngg ntlgrlqves
      241 gsidlhansi gaywthigad gwyvdsigmy swldggsstd rgigvdtsgn stalsveagy
      301 pfrldngwvl epqgqliwqh iglddandrf tgidyesfgt wtgrlgmrle anttmndvpv
      361 qpfasinlwh dfdqdykvsf nrvpvvtele qtslelnvgf saqmsetvsv ygglqfatgl
      421 ddddnrgygg niglrikw
//
LOCUS       WP_457663073             366 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457663073
VERSION     WP_457663073.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 366)
  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   2  (residues 1 to 366)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..366
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39349
     Region          6..321
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mvggankaat irevaalagv apgtvsnvlt gkklvaeplr ktvldaiaql dyrpnhlass
       61 lrfgrtksig ivvpdmtnpf fsglvrelel kaaksgfqil lmssheeaae ereriralvs
      121 rqvdgliisp srdsietsph saisgiptvl vdrafavegf dtvsadneqa tlmgtrhlie
      181 lghkritfla tapglanmee rvsgyrkaam qdagvsdanv vygglsiesc rsaieqelrr
      241 agrptavfas ayvatlgaak airaldlafp qdvsllgfdd sdwmtvlrpy vstieqplde
      301 lghacwellq rrmkkmdvpp rpqadrlhla rkgvdpphpa kigatlalrs lsgyenvtrv
      361 sarrag
//
LOCUS       WP_457663074             693 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663074
VERSION     WP_457663074.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 693)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 693)
  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 693)
  AUTHORS   ter Beek,J., 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 693)
  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   6  (residues 1 to 693)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 693)
  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 10170692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..693
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77402
     Region          84..644
                     /region_name="PBP2_NikA_DppA_OppA_like_4"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08500"
                     /db_xref="CDD:173865"
ORIGIN      
        1 mkthrpnrta ylligisafa lqafasepti vpeqppfpaq gkityvsres ilefkalpey
       61 repewvtekf vkagklppls erlpkepmvf kagnmpdgmg vygdvmrhvi ggrpegwnys
      121 agqtqgwggi digmfecltr taplfqvead dmeplpnlak swewsedghk ltmhliegak
      181 wsdgdpfdae dvmfywednv ldpsvsplng atpetfgegt tlkevdkytv ewtfkeafpr
      241 qhlfamaygt fcpgpshilk tkhpkyagtt yneykngfpa eylnlpvmgg wvpvayrpdd
      301 iivlrrnpyy wkfdeagnql pylnelhykl stwadrdvqa iagsgdfsnl eqpenfvesl
      361 kraadesapa rlafgprvig ynmhmnfsgn gwgdpderak evrelnrsld frkavtmavd
      421 rkklgealvk gpftaiypgg lssgtsfydr nstmyyphdl egakallekv glkdtdgngf
      481 vnfpadklgg rdveivllvn sdystdrnla egivgqmekl glrivlnald gkqrdaanya
      541 grfdwmihrn taefasvvqn tpqlaptgpr tswhhrapeg geidalphet elvdivnkfi
      601 asndnderae lmkqyqkvat tnvdtvglte ypgaliinkr fsnippgapi fmfnwaedti
      661 irervfvaad kqgdfelype qlpgkpgesg pin
//
LOCUS       WP_457663077             259 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663077
VERSION     WP_457663077.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..259
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28876
     Region          35..168
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mdirnhhlkd direywskrs etfdlafghr iprgpefdaw aaavrsalga rplkvlelac
       61 gtgevtgvll slghdvtald fsetmlavar rkhagndkvr filadaertm epngtydavv
      121 crhlvwtlte peqalaewlr llkpggrllv fdgdwskptp lgrlaslava alegiigydp
      181 hydgamserh akimerlpfg dgltverlvp lieaagfeni llpsrrpiaa aqrrnadlrn
      241 rlrtffyrrf vlvcsrpsg
//
LOCUS       WP_457663079             320 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663079
VERSION     WP_457663079.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..320
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33598
     Region          16..281
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(19,50,53..55,141,166)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(50,53..55,141,166,214)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(54,59..60,91..92,115,122,126,279..280)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            166
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 meevlmqirl dyaasvvavp pialnadltv nadanaaiir hieeggvgil lyggnanlyh
       61 fgledyragm qaviaaaspe triitsigpd fgkalaqapi ardlglrnvm llptqfpadp
      121 agvangvrrl aavlghglvl ylkrenyvdp delgrlvseg avdfvkyave rpdpaqdayl
      181 daiiaaigkd rmasgmgetp ihdhlggrsl ttytsgavci apsaamellr lykagrgaea
      241 felsrpflef ekvraelggl qvlhdgmrla giadagplmp misnlnaekl gpvgvavkal
      301 qvaeadclrr agkpsvsala
//
LOCUS       WP_457663083             360 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457663083
VERSION     WP_457663083.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..360
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38925
     Region          1..349
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrllilgtgg manshakafa eiegvemvga vdvdpsrarv fasthgiert ftsldeaiaw
       61 gefdaatnvt pdkahhpttl aliaagkhvl cekplaenye kaaemaaaae raglvtmvnl
      121 tyrnvaplqk arelvvagei glvrhleasy lqswlvskaw gdwaseskwl wrlstkhgsn
      181 gvlgdvgihi ldfagygans svervfarlk afdkapgnrl geydldands famtaefeng
      241 amavihasrw atghlnelrl rlhgdkgale vihtpdgssl raclgadvek avwrtvdagt
      301 vptnyqrfve tvkagrtvep gfrhaadlqk vldlaieter errelgvpdi davvqeravg
//
LOCUS       WP_457663080             502 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663080
VERSION     WP_457663080.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 502)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 502)
  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   6  (residues 1 to 502)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   8  (residues 1 to 502)
  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 10170670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..502
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55383
     Region          28..498
                     /region_name="PBP2_NikA_DppA_OppA_like_12"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08491"
                     /db_xref="CDD:173856"
ORIGIN      
        1 miiryctcal alfaatllag aaiaaegevk ivlpeqpanl dpcrsirsdi griinsnite
       61 tltvidtekg tvgpwlaekw eqvdeltwrv hlksgvkfqd gaefnaeavv ksinrlmnpn
      121 itcdsrskfg dvkltpkavd aqtveissds pvpimptllg tvqivspnmp fdkesndpvg
      181 tgpyvvesks neqivlkrhd aywgakpdvt ratyvwrses airaamvesg eadmtpsiav
      241 qdatnaesdf aylnsettrm ridaqippld dvrirkalnm aidwdgmgea lfgkdvlras
      301 qmvvpgvrgh npdikpwtyn peeamklveq akadgapvdk eivligrngf fpnsaeslea
      361 irsmwqeigl nvsirqleaa dwvryldkpf pegrgptlfq qqhdnntgda gftapvmyls
      421 egqystiadk dldavlkkam aatgderekl fqevfakvhd eivadvpmyh migyvrvgsr
      481 ldwkpdlktn seialseihf kd
//
LOCUS       WP_457663088             516 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663088
VERSION     WP_457663088.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 516)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..516
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55929
     Region          9..512
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mimqardddd cilrledvtk vysgivavrh adlslrrgav nvlvgengag kstlmriiag
       61 vekpslgril ldgkevefhs padaqrhgig mvfqelnlfg nlsvaenifa treltrgfrg
      121 idhgaqvera tgfldrldag idaetlvedl pigqqqlvei akaisldtri lildeptsal
      181 saaevdvlfk virelkaqgv aivyishrle elmrigdyit vlrdgqitgh amvkdidtkw
      241 ivrsmigsda kdfaksiahr lgeeafraed iclprrtggl avdhvsislr agevlgiygl
      301 mgagrseffe cvmgqhrhss grvfvdgtev datdtagris aglalipedr qreglvqals
      361 iasnltlasl drfvrfgfhi vgareqasie aamrdlsika pnpdfevtsm sggnqqkvvi
      421 gkalmtkpkv llmdepsrgi dvgakadvfr tmrrlagegl ailfstsdle evmalsdria
      481 vmsngrlvtv vdradateem ivkasaeghk ttreha
//
LOCUS       WP_457663090             303 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore ABC transporter substrate-binding protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663090
VERSION     WP_457663090.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Delepelaire,P.
  TITLE     Bacterial ABC transporters of iron containing compounds
  JOURNAL   Res Microbiol 170 (8), 345-357 (2019)
   PUBMED   31678562
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kawano,H., Miyamoto,K., Sakaguchi,I., Myojin,T., Moriwaki,M.,
            Tsuchiya,T., Tanabe,T., Yamamoto,S. and Tsujibo,H.
  TITLE     Role of periplasmic binding proteins, FatB and VatD, in the
            vulnibactin utilization system of Vibrio vulnificus M2799
  JOURNAL   Microb Pathog 65, 73-81 (2013)
   PUBMED   24135791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..303
                     /product="siderophore ABC transporter substrate-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31238
     Region          4..299
                     /region_name="CeuA"
                     /note="ABC-type enterochelin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4607"
                     /db_xref="CDD:443657"
ORIGIN      
        1 masnklserl vaglvafala gacnaadivt aagtvtvekt pekiavfdia aidtldalgv
       61 kpdgipsnly lpelehlkdg aavvgdifep dleslselap dliivggrts araeaaakva
      121 ptidmtmdgd gllqearerl taygvlfgke aeanaaakal daavekaraa aagqgkalii
      181 mtngpkvtay gpgsrfgwvh saldlppavp dveaanhgea isfefiraan pdwllvldra
      241 aaigsedqga rttldnelva ettawkrgqv iylpagdlyi aaggvqalhr vftalsdafa
      301 kaq
//
LOCUS       WP_457663092             320 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663092
VERSION     WP_457663092.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..320
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33778
     Region          21..303
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(24,55,58..60,149,178)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(55,58..60,149,178,223)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(59,64..65,96..97,121..122,129,133,286..287)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 mvhnincksh ctdlimpltr ilpvlptpft esgvdiaamr rivrfaldag vagvvfpgfa
       61 sevemltgee rlalletvsa evdgrvpvia gasaatvddv vaygrqalal gitqlmiqpp
      121 ksigagadav aaflsasamq mpdaefilqn apaprgsdls peavlkvvrr vpavryvkee
      181 tlpagpaita iladapehll gviggggary ildeydrgac aampaleiad lhvaldrnyr
      241 agrggeartl yvkslpllal qavyrmrltk hvlglrgiid npivraptpd ldamavrdie
      301 rclqeceves fgrsnrgsga
//
LOCUS       WP_457663094             412 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Sinorhizobium medicae].
ACCESSION   WP_457663094
VERSION     WP_457663094.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=45001
     Region          1..402
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mndrftlavt gqslikhdir dirtpafqdv qsllrqadls ftnfegtilg thggwplkgs
       61 ffgcsdpavl dalgaigfqa lslsnnhafd lgpsgvlstl eevekrgflh aglgrnarev
      121 srasiatinq rrialvamdg gpgpdfmyaa dadenrperp gvnrlrlsql levddvafeq
      181 iravrdkigy taidlandsq pddpprldpq aevaiarcvf krsdrygrgv ridevdmarn
      241 laaitsaard ealviaylhh hhwasdwyql pewvsgvakr cidagasmfv shgapvlqpv
      301 eiyrgrpify slgnfifhvr sekstwtaae vwesvvgvcs fasdnslidi sfhpvvigge
      361 dgledgvler rlvpqlvtgd savrilgrlq eqsarlgahi eisgnvgrlq ar
//
LOCUS       WP_457663095             169 aa            linear   BCT 27-JAN-2026
DEFINITION  substrate-binding domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663095
VERSION     WP_457663095.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 169)
  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   2  (residues 1 to 169)
  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   3  (residues 1 to 169)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   4  (residues 1 to 169)
  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 10156839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..169
                     /product="substrate-binding domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18288
     Region          <2..151
                     /region_name="PBP1_sucrose_transcription_regulator"
                     /note="ligand-binding domain of DNA-binding regulatory
                     proteins specific to sucrose that are members of the
                     LacI-GalR family of bacterial transcription repressors;
                     cd06288"
                     /db_xref="CDD:380511"
ORIGIN      
        1 mgfingepwm daaidrlkgy kqalatadia ydeslvrngd wlplrgyeaa lellaidnpp
       61 taifcgndlm aigaleaase rglrvpqdls vlgyddqela rythpplstl vlpnyemgqk
      121 aaeilidmai hgknprpmti kvdgplvkrg ttaavperma grpfalreg
//
LOCUS       WP_457663096             404 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 aminoacylase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663096
VERSION     WP_457663096.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 10145370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..404
                     /product="M20 aminoacylase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /calculated_mol_wt=42882
     Region          29..400
                     /region_name="M20_Acy1-like"
                     /note="M20 Peptidase aminoacylase 1 subfamily; cd05666"
                     /db_xref="CDD:349916"
     Site            order(116,118,151,177,376)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:349916"
     Site            order(200,222..223,227,230,233,250..256,262..263,265,
                     271..273)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:349916"
ORIGIN      
        1 mgssrpfkgs rntcqcacpp giiddltflt alrrdlhahp elgfeevrts elvaklleea
       61 glrvhrglga tgvvgtlqvg ngtrtiglra dmdalampel adrpykstva gkmhacghdg
      121 htamllgavr hlaatrnfsg ivhfifqpae egrggarrmv edglfelfpc davyglhnmp
      181 glavdemavv pgpqlassds wrltfrgigt hgakphlgrd pitaagtfia slqtivgrvv
      241 dplqpavvsa cslqagdpka lnvipdtvei ggtaraytph vrdqleeeig rlaqgtaamy
      301 gieadyrfer rippvvndpd ataralsaar svfgektltr fppstagddf affaleapgc
      361 yvwlgngpav dgalhhnsay dfndeaigpg aafwtalveq elka
//
LOCUS       WP_457663098             257 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663098
VERSION     WP_457663098.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 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   4  (residues 1 to 257)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28921
     Region          18..246
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 marqenlpde spidrnhpda lyaqlrnllr gmierrelav ndklpserel vavygvsrit
       61 vrqaikelen lgylqtrpgk giyvtepapv yelevvrsft qtahannrkp gmrllraeia
      121 radpevarpl slptgaevvf leelrlldgv pvvvqrdwfs asltpgildi dwtvenrsly
      181 defenrygil psrgqstlsa rlasdleasl lqldrpaavl tldqiaydsh nrtvnisaaa
      241 yhptryplsl tqshrrf
//
LOCUS       WP_457663099             169 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Sinorhizobium medicae].
ACCESSION   WP_457663099
VERSION     WP_457663099.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..169
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=17791
     Region          <4..135
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 msddaplcrc gkfgcveara agwaiardls srgfraetar dvldlveqrk pealmllraa
       61 grtvgevisd vvsiinpsli vvggtlargg dlllsgirel vyqrclplat rnlsielsti
      121 rddsalygaa hlmlddifap tktgellary gaaaasthpq aptrattgt
//
LOCUS       WP_457663101             221 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter outer membrane beta-barrel domain-containing
            protein [Sinorhizobium medicae].
ACCESSION   WP_457663101
VERSION     WP_457663101.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510333
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..221
                     /product="autotransporter outer membrane beta-barrel
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24480
     Region          1..199
                     /region_name="Autotransporter"
                     /note="Autotransporter beta-domain; pfam03797"
                     /db_xref="CDD:461054"
ORIGIN      
        1 msfslqdsst dafhdsldid sdgfsfgpya ayrlskhwai dasltygryn ndvelsvlsg
       61 eydserfage islngqykfd ayyvrpkasv tlshvksday glsgslfnfp vsvslpgdsy
      121 nygvldmste vsrffrlpdg qpflvfaelg aqyeferpnd gkiltgdlse vspspwafsl
      181 rsglrmllne nlqieatggy lslgqddldv wegklhvsws f
//
LOCUS       WP_457663100             407 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663100
VERSION     WP_457663100.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11458748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..407
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40264
     Region          <30..>85
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
     Region          73..361
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <184..323
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 mtsvvvtlsg anaalvkvgg vnedmirnfe nvaggssgdt ligddlanvl lgndgadtlk
       61 gglgsdvldg gngidtadyl ektdaisvtl ngttnatvlv ggvaedvirg venilagsga
      121 dtlvgdgasn tfrgalgadf idggagsdta dyrekaaave vtlfgagdsf vfvggvaedt
      181 irnienvfgg kgndtltgdd santlngndg kdllsgggga dildggaasd tanyrdksas
      241 vsvtlngtaf tavmvggvae dtvrnienvw ggtgndslsg dgnanllsgg ggsdmlsgga
      301 gadifqfdfa lgasnvdmvl dftagdrlfl sksvfttlsg gslasnqfya aagateaqgv
      361 nqrvvydttt galyydadgn lsghtavqfa vlstqpglta gdfvlvv
//
LOCUS       WP_457663102             166 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663102
VERSION     WP_457663102.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 166)
  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   5  (residues 1 to 166)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..166
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=17820
     Region          5..164
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 mhqgffllfa tvsvvtaltl vlarnpvhsa lalmacflqi saifvmlgap llaviqifvy
       61 vgaimvlflf vimmvdvrea vlqrfmpggn lpalalllll gtemvvlvlw sdrliesppv
      121 aerggdairn lsktlysdyl lpfeiasvil laalvgaivl arkepg
//
LOCUS       WP_457663104             287 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663104
VERSION     WP_457663104.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..287
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30404
     Region          3..281
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mvsalkrrrh gpvltaskll lasyilvaia apliapqnpy dplqiygwea ssppgtrgsg
       61 gylyllgtdg lgrdivstil yglrislvvs ivssalaali gltagvsaay fgkwvdiaim
      121 rlvdlqlslp tilialiaiv tlgpgidrii laliiaqwat yariargval seankpymda
      181 arlmrlptsr iifrhllpns iapavtlipi evghavalea tlsflglgvp idkpslgsav
      241 angfqylltg qywislfpgl alfgliasin lvgedvrrsl dprnhsl
//
LOCUS       WP_457663119             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663119
VERSION     WP_457663119.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77103
     Region          5..657
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykerv dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkifki stpmvspgck itsnyqegtq etyhvpcphc
      241 helqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra edhgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvvd
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslagayrwg vpywtdeewd aiadrlgrle apqqgdledr lnqiavktep aagesaaaeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457663137             327 aa            linear   BCT 27-JAN-2026
DEFINITION  RecT family recombinase [Sinorhizobium medicae].
ACCESSION   WP_457663137
VERSION     WP_457663137.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Caldwell,B.J., Norris,A.S., Karbowski,C.F., Wiegand,A.M.,
            Wysocki,V.H. and Bell,C.E.
  TITLE     Structure of a RecT/Redbeta family recombinase in complex with a
            duplex intermediate of DNA annealing
  JOURNAL   Nat Commun 13 (1), 7855 (2022)
   PUBMED   36543802
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Muyrers,J.P., Zhang,Y., Buchholz,F. and Stewart,A.F.
  TITLE     RecE/RecT and Redalpha/Redbeta initiate double-stranded break
            repair by specifically interacting with their respective partners
  JOURNAL   Genes Dev 14 (15), 1971-1982 (2000)
   PUBMED   10921910
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..327
                     /product="RecT family recombinase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=36619
     Region          43..189
                     /region_name="RecT"
                     /note="RecT family; pfam03837"
                     /db_xref="CDD:397770"
ORIGIN      
        1 mnqlakaprr svlvdmaghf gmeadafemt vraqcsptpk kgeqfrpltr eefaafllva
       61 kkydlnpltr eifaypkrgg gvvpivsidg winlvnshpa cdgfqftwer dangdpisct
      121 cimhrkdrsh ptavteylae cwrdtepwkm khrmlrhkal mqcaryafgf agiydedegr
      181 riaedqnial lppaprapri gqqspageki qtaqgdatev esgtgqppve lglpplmtsp
      241 tpiarkwaas mptpprtrns ltncatgwpr rktppawrks gqsltrwrgs kaptlikrfa
      301 rrskragcai wkrrmgnead vrqcrpd
//
LOCUS       WP_457663140             377 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457663140
VERSION     WP_457663140.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 377)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..377
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41104
     Region          18..367
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 manypaitst erqtrisrlr atlsernvgg lllgsteslr yytglewhas erflgalitg
       61 sdliyiapaf elsrvetlsr epgeirawqe eessaalvas llppeatlav ddslplfayn
      121 alvgeiaarr lidggplira qrrlksaaei eiiqfamnlt levhrrahkf ikpgisasev
      181 rryiddqhrl lgapggssfc ivsfgdatal phgaegeqvy kpgdvvlvdt gcriggyhsd
      241 ltrtymiddp tpefariwai ereaqlavfe aahigatcgs ldsaardvlv rnglgpdhkl
      301 pglphraghg igleiheepy ivrnnhfals egmcfsvepm ivvpeafgvr ledhiymskd
      361 gpvwftapae gptepfa
//
LOCUS       WP_457663142             223 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663142
VERSION     WP_457663142.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..223
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24387
     Region          20..223
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mktsrltsnd ravllgsrlf anlpapaaea vlegatisrh eaqdvlfhqg daiehvffvv
       61 sglvrlygtg readiavfpr galfgekavf ldqratahaq avhpsiiakl dgprlcrlvr
      121 eeadvawall ellcrhgqmt ekrlaedrll tapqrvanyi lgqcpgdspa ftfrlpfqkn
      181 vlagklglap ealsrafstl rqsgvivkgr lieirdreal erf
//
LOCUS       WP_457663144             250 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663144
VERSION     WP_457663144.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..250
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28061
     Region          24..237
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mitegkfskg tpckecplrp lplfrsfeae eiafvsrfkt gelvfdsnam ilaegeeseh
       61 lftvlsgwgf rykmlddgrr qimnyvmpgd ivglqgtlmg emqhsiesls pvvlcvfqrs
      121 klaelyrchp elaydltwia areermlden llsigrrsal eraayliafl yqraaslelf
      181 rsgwsvipit qqhvadtlgl slvhtnktlk klaargllrw aekgcdvhdi dgllavagwd
      241 glcepkrpli
//
LOCUS       WP_457663146             115 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663146
VERSION     WP_457663146.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 115)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..115
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12784
     Region          <2..102
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpkepfeaae ldgastfrvl rtltfpmlkp vlflvlvlrt idsvrlydav avltrggpgt
       61 vtetmtfyly rtglklfrmd yastmaiffl yamlvaslfa lrplltqfss raseg
//
LOCUS       WP_457663148              57 aa            linear   BCT 27-JAN-2026
DEFINITION  Flp family type IVb pilin [Sinorhizobium medicae].
ACCESSION   WP_457663148
VERSION     WP_457663148.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 57)
  AUTHORS   Kachlany,S.C., Planet,P.J., Desalle,R., Fine,D.H., Figurski,D.H.
            and Kaplan,J.B.
  TITLE     flp-1, the first representative of a new pilin gene subfamily, is
            required for non-specific adherence of Actinobacillus
            actinomycetemcomitans
  JOURNAL   Mol Microbiol 40 (3), 542-554 (2001)
   PUBMED   11359562
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..57
                     /product="Flp family type IVb pilin"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=6043
     Region          1..55
                     /region_name="Flp"
                     /note="Flp pilus assembly protein, pilin Flp
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG3847"
                     /db_xref="CDD:443057"
ORIGIN      
        1 metlkrlfed rdgatvleyg llaalisvgl liglqnfssa lldmltfitg tleaawa
//
LOCUS       WP_457663149             424 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663149
VERSION     WP_457663149.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..424
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47288
     Region          55..352
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mignvhlpad angsadrllg glahsgldgl qsertlmigr pgrhlavypa ragyelqrel
       61 dflsnraieq nvfftgrfla pamprledrv vrlavirdqs eqssrirflm pfsiekpgfa
      121 igasiiraws npfgplgtpl ldaedaaeti snlyaalatp saglppvlvl pdirlngkfa
      181 qlaravaige nlpltvtdtf rrpmleslld gptylseaig pqrlrelrrq wnnlakqgsl
      241 tysvarrpdd irlrmeeflv leasgwkgre rsamimdrfr aafareaitn laeadsvrih
      301 tldlngkaia tiivlimage aytwktayde ryakyspgkl lfaeltewhl ddaniirsds
      361 cavpdhpvms rlwqereemg tlviglgqnr drdvrqvaaq lhlyrntrnm arllrekira
      421 lagr
//
LOCUS       WP_457663150              78 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase TusA family protein [Sinorhizobium medicae].
ACCESSION   WP_457663150
VERSION     WP_457663150.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Tanabe,T.S., Leimkuhler,S. and Dahl,C.
  TITLE     The functional diversity of the prokaryotic sulfur carrier protein
            TusA
  JOURNAL   Adv Microb Physiol 75, 233-277 (2019)
   PUBMED   31655739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..78
                     /product="sulfurtransferase TusA family protein"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /calculated_mol_wt=8737
     Region          10..77
                     /region_name="TusA"
                     /note="Sulfur carrier protein TusA (tRNA thiolation,
                     molybdenum cofactor biosynthesis) [Translation, ribosomal
                     structure and biogenesis, Coenzyme transport and
                     metabolism, Posttranslational modification, protein
                     turnover, chaperones]; COG0425"
                     /db_xref="CDD:440194"
ORIGIN      
        1 mpeeaklryd lrglkcplpv lktrkrmenm tagalieiet tdplavvdip hfcnedghrl
       61 ekaepvsggh rfvirkkt
//
LOCUS       WP_457663151             257 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663151
VERSION     WP_457663151.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28132
     Region          60..195
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maakpsgpqg drprrlrasp qsappqsapp qsaspesapp efgssesleg prtepslsld
       61 rivaaavell dtrgvdglkm rqladrlgag amslywhven kemvfdlald svlayrgppq
      121 kaesrdwrge vfhmledwra smlrhpwsas llprralgpn ilsrlellsn tlsragvada
      181 dlnaaiwslw nyvigatvtr asfvlsdedr svaqqrltgl gehyptiers rllldddwdg
      241 afrkgldfll dglaprs
//
LOCUS       WP_457663152             190 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663152
VERSION     WP_457663152.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..190
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21097
     Region          <1..60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mkrlselidv prrtlghwlt gtqpkpehlq kiadvtgvql hwlitgegpk kedpiskamq
       61 rllklsenpg gltndevaer yeeefragmq kfrgfeeegs sfatpkvsld iallqrlsdl
      121 aqsvfneckq sappraitae agnlynellq mvvdvhdeev veallpvlra rfkkrlqeaa
      181 sqpgsgkrsa
//
LOCUS       WP_457663159             680 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663159
VERSION     WP_457663159.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..680
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77119
     Region          5..663
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 mtvlfnperl alsvlaeice pppavdyldw akrnivfser itdhpgpyne dlvpffseil
       61 ralspedpcn ivslaksaqi ggticanift lgsldmapgd flyvhpteen aarwsktklm
      121 plvrempava klfsqnsrda snsvlykeri dgrgaiqaag anspaglsmi sprkqvqddl
      181 akwqmneagd pevqadsrsk affngkvfki stpmvspgck itsnyqegtq etyhvpcphc
      241 qelqelrwen mrdhidpehp eqahfvcihc gceihehhre wmvkpengak wvarypergr
      301 rhrsfriwma yspferwenl arewltvqag gpenrekgsg aeqtfwndwl glafeadnka
      361 idwevlrdra eehgfqrgvi paealalvlg mdvqgdrvew llvgygrnry ravidhgvid
      421 hragshlada kehsghisep evraaldrll qrewlddagr krtadrvaid gnaytddvwn
      481 wvrkhpksrv imvrggntea appivqtkey drkgkpkkqk wssrfftfna safkirlyrd
      541 ykkddpeqag yirfargfgd dfyqqatsea rvpektrsgh tryvwklaeg krneiidmln
      601 qslggayrwg vpywtdeewd aiadrlgrle apqqgdledh lnqiavktep aagesataeq
      661 qsplvaaala raaraaqrnr
//
LOCUS       WP_457663165            1058 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457663165
VERSION     WP_457663165.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1058
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114171
     Region          1..1046
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mrfahffvdr pifasvlsiv llivgsiayf qlpiaqypei apptivvras ypgadaetva
       61 ntvatpleqe ingvenmlym ssyatadgsm altitfklgt dldqaqvlvq nrvsiaeprl
      121 peevrrigvt ttksspdlmm vvhllspndr ydqlyvsnya rsrirdilvr ldgvgdvllf
      181 gereyalrvw ldpqklsayg mtagdvveal rqqnvqvsgg siggppmssd safqytvttd
      241 grfgdarqfr yvivkatdeg rlvqlqdvar ielgareyvt nsylngspav algifsrpgs
      301 nalaaadaiq atmadlsrdf pegleyriiy nptefisesi nevyktiaea allvalvvii
      361 flqswrtaii pivaipvslv gtfallfafg fslnmltlfg lvlaigivvd daivvvenve
      421 rnlakglspr eaahvtmdev gaaviaislv ltavfvptsf ipgisgqfyl qfavtiavat
      481 visainsltl spalaaillr phenhghesr npltrlgrgf angfnrgfdr madgyawtvr
      541 hlvttriala gslvvfvall gatwymaqiv prgfiptmdq gyaivviqlp dgaslertdk
      601 vvrraseiir evpgvkdava fagfngatft nasnsgvift pfnsfeerle rkqsseqiig
      661 qifgamqgiq eafiiavppp svrgignsgg fkmqimdrqs admrralgla hqmmgaanqt
      721 egltgvfttf sasspqffla idrdkaraln vpipnifetl sinlgtsyvn dfnafgrvyq
      781 vraqadqqfr leredilalk vrsatgalvp lgtlveirdt sgpalvqryn myvsvplqgn
      841 papgvstgda ldkmealagq ilpqgttfew telalqerqt gntavfifal svvfvflals
      901 aqyeswvlpl aiilivplav laallgvsir gfdnnvltqi glivliglaa knailivefa
      961 regeeegktp veaaidasrl rlrpivmtaf afilgvvplv iatgpgaemr qslgtavfsg
     1021 mlgvtflglf ltpvfyvalr slrrkrapaa eavpapge
//
LOCUS       WP_457663172             346 aa            linear   BCT 27-JAN-2026
DEFINITION  heme-dependent oxidative N-demethylase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663172
VERSION     WP_457663172.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Ortmayer,M., Lafite,P., Menon,B.R., Tralau,T., Fisher,K.,
            Denkhaus,L., Scrutton,N.S., Rigby,S.E., Munro,A.W., Hay,S. and
            Leys,D.
  TITLE     An oxidative N-demethylase reveals PAS transition from ubiquitous
            sensor to enzyme
  JOURNAL   Nature 539 (7630), 593-597 (2016)
   PUBMED   27851736
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..346
                     /product="heme-dependent oxidative N-demethylase family
                     protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=40479
     Region          53..286
                     /region_name="DUF3445"
                     /note="Protein of unknown function (DUF3445); pfam11927"
                     /db_xref="CDD:463399"
ORIGIN      
        1 maiafkqetf rddfsyrnsa enirrfpfpf drdeymyavn mephvkgqkg tafenlidvd
       61 ehyvaemrdr alvlkedplr yqalphmmaa qwdtlellme eravgfpehf tlarngdqwr
      121 winrplgidd tftfgdrstl pcepleyitr qaqgdfcivd qrdgnlwmda gmvttqadws
      181 ldfdigmnfm ewhgpvplah qmgvfdralk fllnlqqgkp trrfnwtmti nprldtspen
      241 yhkwgpdrat vttgnvgdkv hlrvevqslw rlprsnailf vircylmnmn elvtvpkwar
      301 rfprvlrtlp pelidykglt ryrqttidwl skfddgepts pgtfpd
//
LOCUS       WP_457663167             399 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Sinorhizobium medicae].
ACCESSION   WP_457663167
VERSION     WP_457663167.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..399
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41745
     Region          5..396
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mtfktlddlt diagkrvlvr vdlnvpvkdg qvtdttrier vaptirelse kgakvvllah
       61 fgrpkgepva dmslktiasa veeildqrvy fapdcigdka asaiadlndg evlllentqf
      121 hkgeekndpa fvtalaangd iyvndafsaa hrahastegl aqhlpayagr tmqaeleale
      181 kglgnpqrpv vaivggakvs tkidllqnlv kkvdalvigg gmantflaaq gvdvgkslce
      241 hdlaetakai laaaseagca ivlpvdgvva refkagadne vvdvkaipad ammldvgpks
      301 idainewisr aetlvwngpl gafeitpfdk atvaaakhaa artrsgslvs vagggdtvaa
      361 lnhaevaddf tyvstaggaf lewmegkplp gvdilkqqr
//
LOCUS       WP_457663173             240 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663173
VERSION     WP_457663173.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..240
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26529
     Region          9..239
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mndvtlklkp arrerladvl ygqileqias gqmaegaklp seahicrdfq vsrpvvreal
       61 mrlqadglvv srqgigtfvk srpsdkltsl aasaeiasyl rafeprlale tecaglaamr
      121 rtkaqlnqig ealsalegaf argetgweed fafhhavaea agnelfprll edlreilsgs
      181 mrmalgltrq gsadrrrrvl eehrkiysai sgqnrdlarl ymryhltesr aritgshgdl
//
LOCUS       WP_457663174             429 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Sinorhizobium medicae].
ACCESSION   WP_457663174
VERSION     WP_457663174.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..429
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47989
     Region          6..334
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdnkrrfalv gtgnrgttmw gkdllagwrg lvdlvaiadt nslraerart miatnapiyd
       61 svdsmlaetr pdlvivctpd dthddivvra lesgadvite kpmsttveki rrileaekrt
      121 grrvdvsfny rfaptaarik ellnageigr itsvdfhwyl dtrhgadyfr rwhayaersg
      181 slfvhkathh fdllnwylds dpdfvgafad lqmygrkgpf rgprcklcph ksecdfyldl
      241 eadpfldaly eepseidgyf rdgcvfredi dipdtmvani ryrndvhvsy slntfqpieg
      301 hhiafngtkg rielrqyedq pweappedvi llvrnfpkgk aaveritvph sagghyggdd
      361 rlrntlfkpg atdplgqrag aragamsvlc giaalesark gkvvrladlm pelfveetqa
      421 vsrlaanga
//
LOCUS       WP_457663180             391 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457663180
VERSION     WP_457663180.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44388
     Region          60..372
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 madirkrtgs kgttyqvrfp dpsaksgysy atfdtrkeal efrdgsanqk phisrgseir
       61 tveqavdkwl dvcekegrdg rdpvtaytmv gyrhraeiik sypwgkrlhd lsapdviefr
      121 swllqnrsrd qarkvlssfh slvlemvnrg vlahdvasgv girggsryde pvsipseyev
      181 rellaaadrl ansrnrqtqr tweryrpily laadtgmrpq eylvaarskl kdgtievdra
      241 ldgggneisv tkspsgrrvi dlspetydml aqyarkvhak nphdllfpts tgnwqsikhw
      301 rnrgfaaace eaglmesidd ggetilrpky vpydlrhfya smlieqrvnl kliqylmghr
      361 diqttlsvyg hliervemrs erntgliarl g
//
LOCUS       WP_457663182             304 aa            linear   BCT 27-JAN-2026
DEFINITION  ArdC family protein [Sinorhizobium medicae].
ACCESSION   WP_457663182
VERSION     WP_457663182.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Gonzalez-Montes,L., Del Campo,I., Garcillan-Barcia,M.P., de la
            Cruz,F. and Moncalian,G.
  TITLE     ArdC, a ssDNA-binding protein with a metalloprotease domain,
            overpasses the recipient hsdRMS restriction system broadening
            conjugation host range
  JOURNAL   PLoS Genet 16 (4), e1008750 (2020)
   PUBMED   32348296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Belogurov,A.A., Delver,E.P., Agafonova,O.V., Belogurova,N.G.,
            Lee,L.Y. and Kado,C.I.
  TITLE     Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa
            has a high similarity to the 'protein transport' domain of TraC1
            primase of promiscuous plasmid RP4
  JOURNAL   J Mol Biol 296 (4), 969-977 (2000)
   PUBMED   10686096
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..304
                     /product="ArdC family protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33844
     Region          4..304
                     /region_name="ArdC"
                     /note="Antirestriction protein ArdC [Replication,
                     recombination and repair]; COG4227"
                     /db_xref="CDD:443371"
ORIGIN      
        1 msdtnetprq dvysritnqi iealeqgvkp wtqpwsaaha aghvsrplrh ngqpyaginv
       61 ltlwasamtg hyaapiwmtf kqaielggnv rkgekgspvv yadtmrrtet deatgdeaer
      121 fipflkaytv fnveqieglp ahfhaqadni rnpderiaha etffgatrad irhggecayy
      181 spaldyiqmp afeafrdaqa yyatlaheat hwtrhntrld rdlgrkrfgd dgyareelva
      241 elgaaflcad lglrledrdd haayighwls vlkhdkraif aaaahaqraa dylsgfsqsq
      301 eaaa
//
LOCUS       WP_457663188             508 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663188
VERSION     WP_457663188.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..508
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56286
     Region          71..497
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mnafsneftr diprgvstrf lnqqkqpqac wmpidsilrs tamnydpqnp gaalmvgalg
       61 drllgindnr htlmvggsrs gksvslvnnl lfyrgsvlal dpkgelaslt aerraelgqk
      121 icildpfgiv perlapyras fnpltlldqa sdtiiedagl isdalvvagg kdphwdesaq
      181 nmieglllhv atdpqfegcr nlitvrrlin nalvpaggde dafalelaml knaarlsrnq
      241 stvdigdaie gaardfyerp anergsvlst trrqtklldy ramhrvlagh dfnlaelkta
      301 angmtiylcl panrmkkcnr wlrlfinlll damerektep acpvlvclde fpvlghmqql
      361 edaagqiasf gvklwvviqd wgqgvslykd rwetftgnag ilqffgnndl mtteyvskrl
      421 gktivtvtrq netapeqras gvdgrsesqe qydlltpdev srqfarddrl krqlviwagh
      481 hpmvlqrvey fdkaspvhgi fagkygap
//
LOCUS       WP_457663211             237 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457663211
VERSION     WP_457663211.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..237
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27614
     Region          4..230
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 miteldiggi svdvvfkdik nvhlsvyppt grvrisapsr mtienvrlfa isklgwikkq
       61 qgkllsqere aprefleres hyvwgrrfll rleeqgaagv elrhrdmvlr vepgaspqrr
      121 relvddwyrr elrlaaaplv hkwevalelq vsrffvqrmk tkwgssnpal rtirlnlela
      181 kkppecleyv ilhemlhflv pdhstrfqam ldermpgwrq lrqklneapl fygdsaa
//
LOCUS       WP_457663225             428 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663225
VERSION     WP_457663225.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..428
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46994
     Region          31..395
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mswqspispg yswyeatipe rpafpvmpgs rradvaiigg gytglqaayn larsgtdvtl
       61 idscrfgdga sgrnggqfgt gqrlwaeeae emlgreraqr lfdmaenakr yvlgfaeeha
      121 idiefmpgql svshkksler dyrnhveamt erfgyphlsf mdreetvsrl gsshyhfgir
      181 dvgtghihpm klvvgltrqa araganlyeq tkalriekkg glvviettsg titadralia
      241 cnayignlep vtaahvmpir sfigatsvla dhpevlpgge svddsrfvvr yfrkskdgrl
      301 lfggreayta dnprdisahi rrqiceiypa ladievthaw ggsvgitmpr qpfcrdvmpg
      361 itsiggysgh gvmlanycgk lyadlalgka teldllkelk ipafpggtrf rsallflalt
      421 wyalrdrm
//
LOCUS       WP_457663210            1016 aa            linear   BCT 27-JAN-2026
DEFINITION  type I restriction endonuclease subunit R [Sinorhizobium medicae].
ACCESSION   WP_457663210
VERSION     WP_457663210.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1016)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1016)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1016)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1016)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1016
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=114740
     Region          1..1010
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 msdigksers tqkrvielfr delgyrflgd wsdrdgnsni eddllsaslt krgysaaqis
       61 vaiyklhsea snnsrslyan nqavynllry gvgvkveagk atdtvhliew ddpakndfai
      121 aeevtlkggl errpdlvlyl ngiavgmiel knsrvtigdg irqalsnqkp efnqgffsti
      181 qfvfagndte glqygtigtp ekfflkwked eqddtrfkld kyllkmgrkd rvlelvhdfv
      241 lfdggvkklp rvhqyfgika aqeyarerkg giiwhtqgsg ksivmvllak wilennphar
      301 vvvitdrdel dkqiervfrd sgeqvkrtss grdlmtqlgq atprllcslv hkfgrkdvdd
      361 fdafirelea qpsktvgevf vfvdechrtq ggrlhramka mmpnavfmgf tgtpllkkdk
      421 qtsleifggy ihtykfseav ddevvldlvy eardidqslg sedkidqwfd aktkalndwq
      481 rdelkkkwgt mqnvlssrsr mdrvvsdivf dfsvkprlss ergnailvas siyeackyfe
      541 lfqktpfrnk calitsynpn aqdvtkeetg antdtdrqfi yntyvellkg veakgglskt
      601 evyeeaakal ftkepanmkl lvvvdklltg fdappctyly idksmqdhgl fqaicrtnrl
      661 dgedkdfgyi vdykdlfkkv enaiavytse ldhpddgpsp dvllkdrlkk grerlyqale
      721 giillcepve spkgeleyih ffcgnteias dlkerepqra alykatagll rayaniadem
      781 daagysvgdv arikkqvehy ldardtvrla snesldlkay eadmrhlidt yieayeprki
      841 spfdgmslle livktgiada issqlgglkg nkdaiaetie nnvrskiike hlndpafyek
      901 isalldeiia srkakaieye eylkqiaala rrveagqahd tpsslntpgk ralynnlgqd
      961 ealalkvdea vkssrpdswr gvqareqlik aalykilqdf aevervflii kaqkey
//
LOCUS       WP_457663229             206 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663229
VERSION     WP_457663229.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..206
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22627
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlklfytpgt cslashiale eagaayevhr vdfskaeqtk pdylsinpkg rvpalvtdrg
       61 iltetpaila yiaqsfpkar laplddpfef arlqsfvsyl cstvhvahah arragrwadd
      121 paaqeamkak vpqnmgdcfa liertmfagp fvlgdcysia dpylftiasw lefdgvdpar
      181 fprildhrnr mgerqavakv laavqa
//
LOCUS       WP_457663231             465 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457663231
VERSION     WP_457663231.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 465)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 465)
  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 465)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..465
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50659
     Region          132..463
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msrirvlfrt tavrlsalyl vlfslcaafl viyvtgmser llqqqtreai aaevnqisvv
       61 ydragingll rslerrarqp ganlyviagp ngeilagnva alepglldde gwksqpfryr
      121 rftdesqadr hvalaqvlvl dnglrllvgr dlqepekfra lvrqalmval gimglgalvi
      181 wfgigrnalr ridrmseast kimagdlsqr lpasgsgdef drlseslnam lerieklneg
      241 lkqvsdniah dlktpltrlr nkaeaaladg gedsrsgale qiiaesdqli rtfnallmis
      301 rveagsavae msevdlsriv edcvelyepl aedkdmriea eaapgvaisg nrelisqalg
      361 nlvdnaikya egaenplirv emkrsdrqvv ltvadhgpgi penirgevvk rfvrldesrs
      421 kpgtglglsl veaimelhrg sldlsatevg grgltvrmvf paaat
//
LOCUS       WP_457663232             554 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Sinorhizobium medicae].
ACCESSION   WP_457663232
VERSION     WP_457663232.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..554
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60469
     Region          31..349
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          451..552
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mteqqelper esmefdvviv gagpaglaaa irlkqvnpel svvvlekgae vgahilsgav
       61 vdpfgidrll pgwrdepdhp fktevtddhf lflgpagsvr lpnmlmpplm nnhgnyivsl
      121 gnvcrwlaaq aeglgveiyp gfaatevlyn degavigvat gdmgieqnge pgpnfargme
      181 llgkytlige gvrgslakql iarykldegr dvpkfgiglk elwevkpenh kpglvqhsfg
      241 wplgmktggg sflyhlednl vavgfvvhln yknpylfpfe efqrfkthpa irgtfeggkr
      301 lsygaraite ggyqavpkls fpggaligcs agfvnvprik gshnavlsgi laaeklaaai
      361 aegrandepi eiergwresa igqdlkrvrn vkplwsrfgt avgvalggld mwtnqlfgfs
      421 ffgtlkhgkt daqslepask hqkidypkpd gvltfdrlss vflsntnhee dqpvhlqvkd
      481 wdlqkrseye vyagpssryc pagvyewvek dgqptfvina qncvhcktcd ikdpnqninw
      541 vppqggegpv ypnm
//
LOCUS       WP_457663236             158 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Sinorhizobium
            medicae].
ACCESSION   WP_457663236
VERSION     WP_457663236.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12) (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..158
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17239
     Region          10..145
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mswppapvni rvqrddfdia veiaalcrdr tdigavvtfs glcrdeagal salelehypg
       61 maeaeieric qdaverfglq aataihrfgr mepganivlv iaaaphrqaa fdganfimdf
      121 lktsapfwkk ehrtdgsagd wisakdaddd ardrwarg
//
LOCUS       WP_457663235             496 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Sinorhizobium medicae].
ACCESSION   WP_457663235
VERSION     WP_457663235.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..496
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54857
     Region          13..465
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mrslydhrps haarsaqadl vltngqiytg dpglpwcral avaggrivar geradmehli
       61 gaqtevtdlg grfampglyd mhthpdlala pryaedldig lvdptpdqvr navlayaary
      121 pdrewiygqy fvrytfrqag lvpgrdwlda vmpdrpvall drmwgtmmvn seallragin
      181 adtpdpfngy ferdpvsgep tgllidgaya lihaampatp vavlraayrd giryqsargv
      241 vatkyvhvce nrlnalqsld qsgeltlrve aaiswqddif pvrrrwella gerhyyrsar
      301 ldasavkfhf dgtveprssy lmtpwdgans awrgklnltp ehladmiwdm drqgirviah
      361 ctgdaasdtf ldaveaarrr pgglgvrhqc ahstilhgsn lkrfrdlnvt aefspvawyp
      421 skfvsgarsg ygperlsray nikgvleagg vavvgtdwpv spprpvdrar nhghpresvg
      481 rgrgpvrrah lpysgy
//
LOCUS       WP_457663240             128 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663240
VERSION     WP_457663240.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 128)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..128
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15085
     Region          5..122
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(6..8,22,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(51,54,58..59,68,89,93,99,103,106..107)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 mnkyysitel trefgistrt lrfyedegli yperrgrtrl frpadrhlik eilrgrrigf
       61 tiaeireiiq vykdppgemg qlqllmkrve ekredlrqkr kdiedtltel dnveeacltr
      121 laeigvgt
//
LOCUS       WP_457663245             396 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin family protein [Sinorhizobium medicae].
ACCESSION   WP_457663245
VERSION     WP_457663245.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Schroder,E. and Ponting,C.P.
  TITLE     Evidence that peroxiredoxins are novel members of the thioredoxin
            fold superfamily
  JOURNAL   Protein Sci 7 (11), 2465-2468 (1998)
   PUBMED   9828014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..396
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43653
     Region          13..154
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mesnkilsve srapalkvrd wvrgeplasf qpgklyilef cgttcdgcdr amlnlielqe
       61 sykdsgvevv avaaheraas aeevrsklea wlakfpelnf pfglddtgam dtlwmepsss
      121 iviprvfvid rdgslafigh prdlhevlpk ildgtwrtsa rakateseri agdepkarkh
      181 allqpirgkl raaceigdwk talaaveegi aldpdnynlr atqvdllldk icdmetglav
      241 lwqfvreaid rggahwlvta mmqifhpvvg cqslpaaerf amgkelsehi laldfaqcnq
      301 paslvfpeva ryyheignkd ravelielal ksldgpdpdm hglkkdlkpy llqtlanykg
      361 eevcygdvcv vprtntssga tpkaetknld ergale
//
LOCUS       WP_457663251             165 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663251
VERSION     WP_457663251.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..165
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17481
     Region          3..147
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 miirpdtegd deairqitea afagqpyssq teariidrlr sedaltlslv aeeegeiigh
       61 iafspvtiap favgwyglgp vavrpdrqgh gtgsalvrrg ldmlrkagas grvlagdpaf
      121 ygrfgfrnep alvyegcapq yfmalplsga lvsgtvtyhp afgae
//
LOCUS       WP_457663252             406 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Sinorhizobium medicae].
ACCESSION   WP_457663252
VERSION     WP_457663252.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..406
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=42591
     Region          3..404
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 msllsveeal krilakarpp qrvervalhd clgrvlaedv aarlthppfd nsamdgyavr
       61 yediaaigte ltvigqsaag sgfrgqirsg eavriftgap vpagadtvii qedtenlpeg
      121 rirtlfapsk grhirlagqd fladdialta gtaldagrlt laagmnhpel pvlarpriai
      181 latgdellpp gsapgvdqii asnsfgvaai arengaevld lgivgdepaa iaaavskaha
      241 aeadvlvtlg gasvgdhdlv qstllgcgmt ldfwriamrp gkplmvgdld gmtvlglpgn
      301 pvsslvcall flepltrkla ylparsrlsq arlatplpan drrqdyirar ltreadgsfl
      361 ahpfprqdls mvsvfaqsdg livrppgape akigeacsvf klrdsv
//
LOCUS       WP_457663258             361 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457663258
VERSION     WP_457663258.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Van Houdt,R., Leplae,R., Lima-Mendez,G., Mergeay,M. and
            Toussaint,A.
  TITLE     Towards a more accurate annotation of tyrosine-based site-specific
            recombinases in bacterial genomes
  JOURNAL   Mob DNA 3 (1), 6 (2012)
   PUBMED   22502997
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10092408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..361
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=41569
     Region          175..339
                     /region_name="INT_Rci_Hp1_C"
                     /note="Shufflon-specific DNA recombinase Rci and
                     Bacteriophage Hp1_like integrase, C-terminal catalytic
                     domain; cd00796"
                     /db_xref="CDD:271177"
     Site            order(184..185,188,209,212..213,253,255,257,307..308,
                     311..312,314..315,325,335,338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271177"
     Site            order(217,302,305..306,337)
                     /site_type="active"
                     /db_xref="CDD:271177"
ORIGIN      
        1 mgtiterksk ngkksytaqi rlkrdkvvvh sesqtferka vatawikkre telrepgaid
       61 rlkenstlah aidryikesk kkigrtkaqv lakikdefei anmackeies adivkfatel
      121 shgrqpqtvg nyishlssif aiarpawkmd ldysamedaq vvlkrlglia kstqrdrrpt
      181 leelgklmeh ysdretryaa hipmrrliaf aifstrrqee isritwsdye denkrvlvrd
      241 mknpgekign dvwcdlppea iriiaamprt kvkeifpyea rsvsasftra csllgiedlh
      301 fhdlrhegvs rlfelgwnip hvatvsghrs wnslkryshi kqrgdkyegw kwldivapak
      361 q
//
LOCUS       WP_457663265            1155 aa            linear   BCT 27-JAN-2026
DEFINITION  indolepyruvate ferredoxin oxidoreductase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663265
VERSION     WP_457663265.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1155)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 1155)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 1155)
  AUTHORS   Siddiqui,M.A., Fujiwara,S. and Imanaka,T.
  TITLE     Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1
            possesses a mosaic structure showing features of various
            oxidoreductases
  JOURNAL   Mol Gen Genet 254 (4), 433-439 (1997)
   PUBMED   9180697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1155
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1155
                     /product="indolepyruvate ferredoxin oxidoreductase family
                     protein"
                     /EC_number="1.2.7.8"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043805 - indolepyruvate ferredoxin
                     oxidoreductase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=125751
     Region          7..1125
                     /region_name="PRK09193"
                     /note="indolepyruvate ferredoxin oxidoreductase;
                     Validated"
                     /db_xref="CDD:236404"
ORIGIN      
        1 mvsnsrllsg tdalvelllh qaefdkmrgl rtggfvsgyr gsplggldqa lwrrgselks
       61 rnihfqpain edlaatalig tqkvesepga tvegvfglwy gkgpgvdrsg dalkhgnayg
      121 tsphggvlvv agddhgcvss smshqsdlam qawsmpvlhp vsvsdyfhtg lwgwaasrts
      181 gawigfkais etvesastvh pvdypefilp aidsgpdglh wrwldlpgpq vewrlkykln
      241 aikafaqtnp idnllvpvsk prgliiivgk agldmlealr vaglsplala qrgiailqlr
      301 lvfplssttl slaalaervf iieekaavve aqlkheffni pagrrptiig krdsqgapil
      361 pddielrpel lagpvarwle sfgidmpvpl hwselpstsi vdlpkrtpyf cpgcphssst
      421 hvpsgsrarp gigchfmavw mdrqtagsvq mggegvdwmg tapftvtphi fqnlgdgtyf
      481 hsghlairqs vaagvnityk llfndavamt ggqpidgqvt vpqivklala egvkkvaiva
      541 edisryaarg elpagvtayp rddldavqre lrdiegvtvl iydqvcatel rrrrkrdksl
      601 rptaravind lvcegcgdcq tqsnclavvp ietslgrkra idqsacntdl sclkgfcpsf
      661 vtlegatpak rpvpatrdfd ldaavtalap pvptknhssp sdillvgigg tgvvtaagli
      721 aqaarldgng vrtlnftgfa qkggevlshv rfcsdetalh qariaqgead fvlvadivag
      781 vsekvltvfs sertrcianl hesqtgpmlr npdirigsnr lidlltsrsq ridmidagql
      841 aealvgdreq anilllgfsw qlgalpltll siqqaldglg ryasiarvaf qwgrlaaaip
      901 aqihdllgqs tgsraedlas lissrrdfli ayqdasyaqr yvervekirn aaqalgdtsl
      961 tevvaknffk lmaykdeyev arlhvetdfl asisdrfdgk tkfrfhfspp liapkdrrtg
     1021 ergkiafgpw iipvlrllar gkflrgtvfd llgrqaerra erqmlaeyeq hvdwiarilt
     1081 aerlplcrsl talpeqirgf ghvklrslnk vstrrrellq qiesslrnev pdtrpefsrg
     1141 rdapekekkl igqrp
//
LOCUS       WP_457663274             226 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663274
VERSION     WP_457663274.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23629
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavd warapngcpi faqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarggyftpg anssaaggei gpvavlerhg
      181 alfplgdqnl alpsysagsg dpaktlasql eqlglsvhdw fslldl
//
LOCUS       WP_457663280             496 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663280
VERSION     WP_457663280.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..496
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54394
     Region          159..>480
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mnpaillfgl viagaaaafv aslayaglyy afdnstwmfq alqddmlasy raarldlaag
       61 dwhrpamaaa agffaggaml vtamtgkkks tdarflstle aralgltrmg gvfvgriggs
      121 likvpggftq rgsgrrrfmk pmlfggkklw idgddvggfv igpprsgkga slivpncllw
      181 pdsivvldmr getyeatagy rskfsrvlrf spadengdte cynpldfvai dpdqrdidin
      241 siatallptp kgdaywisda ralfagvtsw vlenpdildk dknlgtvlnv veggdqplre
      301 wleevanpel raawissftf ttlarfavma skqfdgvygs laaavrpfkn nrvlratars
      361 tfdiramrre nmslyldfri qqiasigpif nvlmvqfmdh msrnmmkrge rrvlvlldef
      421 qnlgklenal tvatvlggyg ipcwffvqsl rsidnvytre grqtlvnsar aqiflgaqdp
      481 alprlncslr mgycli
//
LOCUS       WP_457663288             272 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Sinorhizobium
            medicae].
ACCESSION   WP_457663288
VERSION     WP_457663288.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..272
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31166
     Region          16..252
                     /region_name="SIR2-like"
                     /note="Sir2-like: Prokaryotic group of uncharacterized
                     Sir2-like proteins which lack certain key catalytic
                     residues and conserved zinc binding cysteines; and are
                     members of the SIR2 superfamily of proteins, silent
                     information regulator 2 (Sir2) enzymes which...; cd01406"
                     /db_xref="CDD:238697"
ORIGIN      
        1 mkehiqqivs alkrrhavlf vgagvsmsvg lpswktlvdh mlselrldef vmrdpdisyq
       61 tiaecyrleh gniaslcewm rhnwrisper ikrselhrli velgfpviyt tnydsnlesa
      121 ydvygkryak ishvrdiasa pagvtriiky hgdfddddtl iltetdyfnr lsfespldvr
      181 frsdaleatv lfvgysmsdl nirlllhriw stwqrsghek drpasyvfmy rpnpvqkavl
      241 gkwgvtvlag egddpqqsll aftrslrtel gg
//
LOCUS       WP_457663291             629 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663291
VERSION     WP_457663291.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 629)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..629
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67908
     Region          7..571
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtsgadllrv eglritfsvl gggveavrga sfrilpgrvt alvgksgsgk saisqaimgi
       61 lpsvasvtgr vvfndptgnk pvdllsldsg greiqdirga riskifqepm tslsplhtig
      121 nqisevlkih tdidkagrre rteqllgyvg fsdpkraydm ypfelsggmr qramiamali
      181 cspalliade pttaldvtvq aqilqllrgl qsklnmamll ithdlgvvan madevvviyh
      241 geiveagpvd aifrnpqhpy lkglmaavph fdmkpgerlk alrevpvqag aiigdrdvrk
      301 aggpnvlvsv rnlsktfstr ssgwfgsgsa frhravdnvs fdirrgeclg lvgesgcgkt
      361 tiskilmrav tpdkgtitfd dgegaldvlk ldgaelkalr akiqmvfqdp vsslsprmtv
      421 knilseplei hgrgtpksrv etvrsllqav gldqrfinry phsfsggqrq rigiaralal
      481 vpqllicdep vsaldvsvqa qilnllkdlq kelgltmlfi shnlavvdym adriavmyag
      541 rivelaprev lmsdpihpyt ksllaavpyp dldrkldfdl lqvsggsdqq rwgvqfadgg
      601 ddealvpadl ggghfvlark svdarelrp
//
LOCUS       WP_457663294             165 aa            linear   BCT 27-JAN-2026
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663294
VERSION     WP_457663294.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..165
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=18365
     Region          20..159
                     /region_name="RfbC"
                     /note="dTDP-4-dehydrorhamnose 3,5-epimerase or related
                     enzyme [Cell wall/membrane/envelope biogenesis]; COG1898"
                     /db_xref="CDD:441502"
ORIGIN      
        1 mggrkhpspr flqsrlkcsc rnelsdfgtg gsiaqinhtl trgrgtirgm hyqrprhdea
       61 kfvsclegvi fdvaidirpd sptnlqwhge ilsaenarsm mipggfahgf qtltencelv
      121 ylhdkpyape fegglnpldp rlaiswplem aqmserdraf afipg
//
LOCUS       WP_457663296              88 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Sinorhizobium medicae].
ACCESSION   WP_457663296
VERSION     WP_457663296.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 88)
  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 88)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..88
                     /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=9365
     Region          3..83
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mtqtikdkvr tfvienflfg dtayeladda sliendiids tgvlelvafi eddfgiamad
       61 adivpqnlns larisafiea kgavpvsa
//
LOCUS       WP_457663303             243 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663303
VERSION     WP_457663303.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..243
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26853
     Region          14..238
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mpekpliles laeappssya dqvygrilhd ilngvfqpga rlptenelae rfgvsrpvvr
       61 ealarlrvdg lvearrgsgt yvlsrpsqtl peladledis rflryqelrf hvegqaaala
      121 aerrtekqla aiveahetfa hevgrgaflp esdrrfhlai ceatgneffa kalegpevsl
      181 tsfmnvslal trsgsqarar rviaehaeiv eairtkdaaw arvamethii karrrmtdgt
      241 ids
//
LOCUS       WP_457663305             354 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide pyruvyl transferase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663305
VERSION     WP_457663305.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10514996
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..354
                     /product="polysaccharide pyruvyl transferase family
                     protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39224
     Region          14..288
                     /region_name="PS_pyruv_trans"
                     /note="Polysaccharide pyruvyl transferase; pfam04230"
                     /db_xref="CDD:427804"
ORIGIN      
        1 maklgvltfh rcinygsfwq trclvhglrs lgtdpvildh qstrvtraew rcamqpllpa
       61 rtarpdiply askirkfqsa laslptsasf alddpagaee cdilvvgsde vwnfrhpwyg
      121 gcslfygegl aakkkvsyaa tfgnhpaang lepywaerlr nfdgisvrde nsraiiekev
      181 greailvldp clqfpetisf gpnasasrpy mavyghsfps wfqnavrlwa garslplvsv
      241 gycnewadeq wldagpyefa awmagaeava tnffhgcvfs llnskpfvta lsdyrsnkia
      301 dlartagaer hvmsqetrpa eyeavlaegl dpaiihrlae lrrqsriylt dvla
//
LOCUS       WP_457663307             611 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457663307
VERSION     WP_457663307.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   4  (residues 1 to 611)
  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   5  (residues 1 to 611)
  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 611)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18652649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..611
                     /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=66068
     Region          28..324
                     /region_name="COG2984"
                     /note="ABC-type uncharacterized transport system,
                     periplasmic component [General function prediction only]"
                     /db_xref="CDD:442223"
     Region          310..611
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mvlrirpqtv ivtmfaliag tlvchatepr rvlliyeses tlvaamqlas gfqeymeand
       61 pghveyytey ldtlrfsspe hslrlagfle akyrqlnldv vvaagpgalr fvletrerfa
      121 ndvpvvfgav tessvtgnlp pdvkgvvsrf dvgktvqlas rlqsrarkvv vmygsapfdr
      181 kwgdtatavl geryagldve yvsglsldgf rktaaelpsd aalviltvfe daegmkfvpr
      241 daaraiaaas gapvygvyss ylgfrvlggy vgtfpsigaq maalsldvmr gdlsaprttp
      301 aqetalvdwr evqrlgiddv lipedaeils yapsvweryr lpisaallvi aaqmltiaal
      361 vyqnrrgrrl eatlaserve lahlsrrsql gelsgafahe ltqpltsila naeagqrlat
      421 etapdmneir aifddivadd rrassvisql rsmmlkgeas qeildlndav rqtvalahae
      481 mlarrtevev knelasvrvk anlvqlqqvi lnllvnaada madippkqrk veiavdrsnn
      541 gycelsvadm gpgipagmqg evfkpfvssk kgglglglai crsiveaqgg klffddgvkr
      601 garaiiilps a
//
LOCUS       WP_457663308             425 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter large permease [Sinorhizobium medicae].
ACCESSION   WP_457663308
VERSION     WP_457663308.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..425
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44734
     Region          1..423
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mgflvvlafl glfmigfpvv yaillpsily vlveglpfgl laqrityald sfplvavplf
       61 ifvgnlmnls gitdrifrfa ytlvgrvpgg laqvnvfgsl ifsgmsgaal adigglgrie
      121 idamkkrgfd psfagavtaa satlgpifpp siplivygsv tsvsivqllv agimpavlct
      181 allmltvliv airhgharae rwptagelva slvpalpail apvlmvggmt agaftpteaa
      241 aitavyvifi saalyreltp ahlwhsavlt arsssailii vasaalfgwi laveqvpqtf
      301 aatllgwskd plmlliianl iffiagmfln sttatlllvp iiapplvmag vdpvqlgivt
      361 ifnlmlgllt ppmglslflv sdiaqvsirq llralvpfyi plvstlvilt lakdltlwlp
      421 rliaq
//
LOCUS       WP_457663310             248 aa            linear   BCT 27-JAN-2026
DEFINITION  3-oxoacyl-ACP reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663310
VERSION     WP_457663310.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481062
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..248
                     /product="3-oxoacyl-ACP reductase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25238
     Region          6..245
                     /region_name="fabG"
                     /note="3-ketoacyl-(acyl-carrier-protein) reductase;
                     Validated; PRK05557"
                     /db_xref="CDD:235500"
ORIGIN      
        1 mttgalagka afvtggsrgi gaaiarklar egasvaltyv nsadqaqavv seielaggra
       61 iairadnrda esieravrha aetlgrldil vnsagiwhsa pldettvadl devmavnfra
      121 pfvairsasr hlgdggriit igsnlaelvp wpgislysas kaaligltkg lardlgprgi
      181 tvnivhpgst ntdmnpangd haeaqreria tggfgepqdi agfvawlagp dgkfvsgasl
      241 tidggana
//
LOCUS       WP_457663313             466 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663313
VERSION     WP_457663313.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..466
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51945
     Region          56..434
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mehqlarpia srkpfdptyd pirapnpgeg kdyaptywig tagkppsddg pvtcdmdvdv
       61 aivgsgytgl scaihlareh gikatvlean gvawgcstrn ggqaqisagr lkrsqwierw
      121 gvdiakklhv eiseafdlfr dlirspeidc daqdgghlyi ahrdkvmpal esesrllnev
      181 fgyrsrivgr eevhrdfvrd eeakgamyep dgmgihaakl afgylnlark lgawvhtasp
      241 vlscdwkngs yhlstpggtv raravciata gytspdlhsl trhrlmpils nsivtrplne
      301 eerselnfnt ripltdtrtl rhyyrimpdg rvqigsrsai tgrdavnpkh vgrlleglyr
      361 kfpvlkgiti dyswwgwvdv shdmmprifr pdpkqplfya mgyggngvmy saqagrrmaq
      421 mvagqggald lpiftsplps hglltpfrrl gqwgmyrwyy lkdeil
//
LOCUS       WP_457663319             633 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Sinorhizobium medicae].
ACCESSION   WP_457663319
VERSION     WP_457663319.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 medicae"
                     /db_xref="taxon:110321"
     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=68781
     Region          1..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mansldhapa qannlpqfla mtigaigvvy gdigtsplya frealrpfgp dgveraevvg
       61 lislmlwtlt iivtfkyvlf llradndgeg gtlsllallm kkapryttlm fmagilgaal
      121 figdamitpa lsvlsavegl klvtpafhdy vlpisvgimv llfavqsrgt gavsiffgpi
      181 tliwflvlga agvahigddl ailaafnpvn avtflwnagf vgfivlgavf ltvtgaealy
      241 adlghfgrgp iqaawfavvf paltlnylgq galvlshpea vsdpfflmfp nwallpvvll
      301 ataatiiasq avitgafslv rqainlgflp rfeicftset qtgqiylpfv nnallagviv
      361 lmfmfgsses lataygisvt gamvvttvla fefarhqwgw stltatavll pllvlelffl
      421 ganlfkihdg gyvpiliagt lmttmwtwrk gvsllrekta rqdiplsqfm amverkseha
      481 pvevpgtaif ltatpdttpa vllhnikhnh vlhqhnvilt iktarvpyvp ekdrytiekl
      541 sdrfsllelr fgfmddqnvs ralarcrkeg frfeimstsf ylgrrkliaa pqsglpqwqd
      601 klfiamadsa idpteyfhlp pnrvvelgeq vvi
//
LOCUS       WP_457663321             506 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663321
VERSION     WP_457663321.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ashikawa,Y., Fujimoto,Z., Noguchi,H., Habe,H., Omori,T., Yamane,H.
            and Nojiri,H.
  TITLE     Electron transfer complex formation between oxygenase and
            ferredoxin components in Rieske nonheme iron oxygenase system
  JOURNAL   Structure 14 (12), 1779-1789 (2006)
   PUBMED   17161368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..506
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54581
     Region          28..395
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          424..503
                     /region_name="Rieske_YhfW_C"
                     /note="YhfW family, C-terminal Rieske domain; YhfW is a
                     protein of unknown function with an N-terminal DadA-like
                     (glycine/D-amino acid dehydrogenase) domain and a
                     C-terminal Rieske domain. The Rieske domain is a [2Fe-2S]
                     cluster binding domain involved in...; cd03477"
                     /db_xref="CDD:239559"
     Site            order(462,464..465,480,483,485)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239559"
ORIGIN      
        1 mnvsaertvs lwaavevapd aapltrdeqv dvavigsgia glsvayelal agqkvavidr
       61 gpigsgmtar ttahltsicd dyfsklielr ghdlarlfye sqstaidrie aiqqtervac
      121 dfrrvdgflf pssatqeadl ereldaalqi gvaverttgl pfagfsaspa lryagqatfh
      181 plkylralav avrarggalf adtvvekvee tesgvrvatt sgfvvtgkwa ivatnspind
      241 rvalhtkqap yrtyamsfei argvvpdaly wdtedpyhyv rlqpgdgetd slivggedhk
      301 tgavddager farlgawvrs lvpdlgaeth rwsgqvmeti dytgfigltp gnnrvfvvtg
      361 dsgegmthgv vaslvirdlv lngdspwrea ynpsrktara frdylvenat aiknfaeyva
      421 pgeidavekl qpgegaivre gltkiaayrd edgtlykrsa scthvgchvh wnslercwdc
      481 pchgshfafd gtalngpavs plsdlk
//
LOCUS       WP_457663322             101 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663322
VERSION     WP_457663322.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..101
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10697
     Region          5..>66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mkaeaealei igdhfrrarl aagltqeqva dlagisrpry rdvetgaaaa rattlinitr
       61 alglemmlvp qamvpaiqal lspqgeddrp afspqaegdd e
//
LOCUS       WP_457663330             642 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663330
VERSION     WP_457663330.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 642)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 642)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 642)
  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   6  (residues 1 to 642)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 642)
  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 10170692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..642
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72135
     Region          54..618
                     /region_name="PBP2_NikA_DppA_OppA_like_4"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08500"
                     /db_xref="CDD:173865"
ORIGIN      
        1 mqefsrrafl lastaavllp vmpvialans akepamleal akagslpava drlplnpmvv
       61 tpldrvgthg gdwnsaivgg gslsmlfryq ayepllryap dwsgvvpnva ehyesnadat
      121 eftfrlrkgm kwsdgepftt edilfwyedi fnyeglndvg qnhlraggkk arfeavddvt
      181 fkvifaapng lfplrlawan ddqttrapkh ylkqfhikyn pnaeeeaktk gasgwiqlfq
      241 reaglvvdne ffqnsqrpvi hawkvaiapg qstdravaer npyywkvdte gnqlpyldwi
      301 vyqmvsdpqv lllkamqgei dlmdqyiatp anravlydsq eqgrfgfytl tstetnemvf
      361 qlnlnhpnev krklynnkdf raalsmaldr qaiidtvfig qgtisqpavr addplynerl
      421 atqytqydpd ranalldkil ptkdsegfrl deggkrvsii feidqaratf ldifqlalpm
      481 fravgldvqm rsmdrslwev rvrqgieyda tahrfggngg iaaildpryf ipnttealya
      541 kgwqlwyrds qsqgaveppq pvrnalalyd rvlasadpde qkklmaeile iaadqfyvfg
      601 iclpadsygv vkndmqnvpe ampnswgypt pgpanpetff kv
//
LOCUS       WP_457663332             241 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663332
VERSION     WP_457663332.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..241
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25644
     Region          5..238
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msvhktvvit galqgigagl vktfldkgws vvatsrrise atsfdragrl elidgdigdp
       61 ktaervsqva veqfgsidal vnnagvfftk pfleytiedf rrlsatnleg fvhftkhair
      121 qmlrqrsggs vvtitssltd hpiagvkasl pmitkgglna itkslalefa sdnirvnavs
      181 pgvvdtplha tgsrdylrsl spmgtitavq eivdgviylt easnitgevl hvdngahlgk
      241 w
//
LOCUS       WP_457663333             336 aa            linear   BCT 27-JAN-2026
DEFINITION  PAS domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663333
VERSION     WP_457663333.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Imamoto,Y. and Kataoka,M.
  TITLE     Structure and photoreaction of photoactive yellow protein, a
            structural prototype of the PAS domain superfamily
  JOURNAL   Photochem Photobiol 83 (1), 40-49 (2007)
   PUBMED   16939366
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..336
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=37191
     Region          155..>316
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mndilsvtal paawtggtvd gicsalldal rsildvdflv vnvagsgdqa evlkersrtn
       61 fvdagaviis dlvrtlgani avwpretnve hgeadlrvli eklgvngkvg vlvagstvss
      121 fpteedrill hvaacqaala iteairfrhd travaereln riadaipvma wstlpdgrad
      181 ffnehfltfl gitseqaagw gwaasihpdd sralqsvwme llasgmpget earlrrwdgh
      241 yrwflfranp vysdegavvr wygtntdidd rkrfeeemrr saalmaqaqr ltvtgsvwwr
      301 patndiywsd eaycwfprgt epvfpprsep plsmvf
//
LOCUS       WP_457663337             569 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663337
VERSION     WP_457663337.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 569)
  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 569)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 569)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 569)
  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 569)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..569
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63052
     Region          26..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
     Region          297..569
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mhsrpclttw lylsplhlll lamltvpsly vfwlslngss ygtgltwvgl enyravfddp
       61 yfwraalntf lvvngvvyve llfglalaal fvsgvpfrgv mfacilmpya isevvavlvw
      121 kmmmdpniga iartieelgl grvnwsasps tglvlvgvin iwthlpftfl miyaglltid
      181 gslyeaarid gasrwqrflr itlplliptl litlifrlif afrmfsevwl ltkggparls
      241 evlavylyqh gfrygdfgma aatgwlmvlg slllasvflf amqrgmkggr amsdafspie
      301 rfarglllgf iliwsvapil fivsssfkrq vdifvyppki vfiptfdnyl kltsqwqdff
      361 tsmgnsliaa igatvlagiv sffggyaysr yrsritawsa vymiavrvlp pivvtlplfp
      421 vadllglgdt hlllillyat fwvslntmim knffdqipye ldeaayvdga sewqlvsqil
      481 arltlqgmta gsifvfvfsw neylfamift tnqaktapli lselmgavdg tewgvlfagv
      541 slqllpvvll vtlarrylia gltagavkg
//
LOCUS       WP_457663341             324 aa            linear   BCT 27-JAN-2026
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Sinorhizobium medicae].
ACCESSION   WP_457663341
VERSION     WP_457663341.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Herrou,J., Bompard,C., Antoine,R., Leroy,A., Rucktooa,P., Hot,D.,
            Huvent,I., Locht,C., Villeret,V. and Jacob-Dubuisson,F.
  TITLE     Structure-based mechanism of ligand binding for periplasmic
            solute-binding protein of the Bug family
  JOURNAL   J Mol Biol 373 (4), 954-964 (2007)
   PUBMED   17870093
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33765
     Region          3..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkilfrvaal slalvaglaa paiaqtypdr tiqvivpyap ggqgditarl iaehlspalg
       61 qpvvvenrpg angsigstfv aradpdgytl evvvqshvlg kalmpnlpyd pvesfepvsl
      121 martqvglvv patlpvntla efvayvkerp gqlgfasagi gsnvhifsew fldlagldmv
      181 hapyagsaaa hpdlisgvat mafdtlpsvs alvregrlkl lavggtqrsp efpdiptvae
      241 fgyadynags wsamlapagt pqeiieklna evvnilkkpe vaerlsklga tvvasspaea
      301 ktaiqkegkv fgelisrlgi kvgq
//
LOCUS       WP_457663342             298 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663342
VERSION     WP_457663342.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..298
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32382
     Region          61..286
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mtavstrhrg sgaaaampts lprldiaeav rirrfrplrl llgalaiafa ifvfkafvda
       61 qidwsvvgey llaritivgl gftilmtvva mliglsvavl lavgfgshnp virwicktyv
      121 wlfrgtpqll qlllwynlal vfpvaglpgl gswqtvdlmg pfaaaaiglg lnagaymsei
      181 irsgllsvda gqyeaakaig mtrgkalrkv ifpqamrvii pplgnefigm tkntslasiv
      241 gfselifvmq siyfynfkvi emllvsafwy livtsilsvg qyqlekrfgr gfgrggrl
//
LOCUS       WP_457663343             885 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663343
VERSION     WP_457663343.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..885
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=96228
     Region          <1..883
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlldregplk allasarsaa lghgstvvve geagigkttl lrefeehsdh gcrvlwgwce
       61 alitpcplgp lqdmgqllda rvaallnqaa sperlfpavl nalqhasdpv ilifedvqwa
      121 dnatldliky lgrrisllpt vlvlsfrsde igadhpltrv lgdlpsasvs rltlqplspe
      181 avaalteqag rcaddlyqvt agnpffvtel lasktgpgri phsvrdavwa rlsrltager
      241 kalevisivp ggvepwlvra llgveadill dqcltrgllr rddqgavmfr helarqatvd
      301 rlppslqksl hskveaamsq hvttqapall arrvhhaaga gdgervlela pqaaahaarl
      361 gahreaashl atalryvaqa apeqaaqlye dwayeaglal lvyepvieah hrviaiwrel
      421 grtekigpnl crlsrlhwrr gegeaaedca aqavcemekl ppgpelamay strsqlrmlh
      481 yrfdeaiewg lralaladql geietrihal nnvgtallfa grpggrerle etlalalahg
      541 fhdhavrayt nfaecavvsk efglaerlla egiafatrhd ldtaahyllg rqaelrmeqg
      601 rfreaetiaq gvmnlerlpm vmhlpaltvl grvhmrlgep ggmallhnal qeglatgelq
      661 rivpvrsalt eaawlhedyg acqeqltala aidlncfraw dfgelavwwr rcgmamplpi
      721 pnaqiplpha aelyghplaa akewdrlglp ydaalalmqv rgvdagpala ravtifesle
      781 arpaaalart qaqrlgvagq lpkarrgpyg aarrhplglt rheqqvlali aagmsnkeaa
      841 qllsrsprti ehqvsavlsk fsaasrmevl lrlrgepwll atdst
//
LOCUS       WP_457663346             224 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663346
VERSION     WP_457663346.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25332
     Region          1..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msenifyklr ddiengivtg afepgerlde tqlatrfgvs rtpirealmq lsaiglveir
       61 prrgaivvdp apqrvyemfe vmaelegmag alaarrhtee dsaallaahe kcrkaavsed
      121 tdryyyenei fhraiyaasr sgfleeqctt lhrrlrpyrr lqlrvrnrmk vsfkehgeiv
      181 eavlsgdadr areglrshva vqgdrfgdlv anlsnrerrs grlg
//
LOCUS       WP_457663347             332 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Sinorhizobium medicae].
ACCESSION   WP_457663347
VERSION     WP_457663347.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..332
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35948
     Region          118..329
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 matsllfpvf vfllastsig gvmvaafypr vskasayrqr larmsapaen krsepteadg
       61 rdrrrsvekt lreieekrqa narkgkttlt arlrqsglhw spktyfvvca caalaswcam
      121 llldtgalvs agfaisggll lphvyvnikr narfakftae fpnavdvivr glkaglpmpd
      181 clrviateaq epvkgeflai vqdqtlgipv deavkrmser mplaeahffa iviaiqsrtg
      241 gslsealgnl skvlrerkkm kakikamsse akssagiiga lpfliagavy faspdymall
      301 fatvtgkivl vgcglwmgig ilvmrkminf df
//
LOCUS       WP_457663348             545 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Sinorhizobium medicae].
ACCESSION   WP_457663348
VERSION     WP_457663348.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..545
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58490
     Region          3..535
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mprlansvyg tlglamvlfv aasallvgss fialerlrsd laatsslgke rlayrmiyaa
       61 shleraqgpa rgaaadelrq lmdqnerfle rlgsdrerig lattsdpaaf aqlervreqw
      121 rddvrpales aiaevpltha aldaldpkvr afaeqledli npieqagiar lkrsqllqlg
      181 fsilslllli hilrvvrrla rrtraladla ervstgdlgq kaavegtdel avlgasfnam
      241 ttrlaamids ergsrerlea llatisetaq hlsssaaeil agatqqvegm reqssavaqt
      301 vtsvdevlqt seqaaqraqq vaasydnavk isnegrrald dtvrvmnavn arteaiaadi
      361 lslaenslei geivsvvaei adqtnllaln aaieasrage hgrgfnvvat eirtladqsk
      421 satarvrril meiqkstnsa vigaedgsks vsraletvse agetirqlea ivadsarsva
      481 qiaasagqqr agmkqiheam hyieqtssqn lsairqaeea akdlnelgsr lkemltdhgn
      541 dhdnt
//
LOCUS       WP_457663350             179 aa            linear   BCT 27-JAN-2026
DEFINITION  chemotaxis protein CheW [Sinorhizobium medicae].
ACCESSION   WP_457663350
VERSION     WP_457663350.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..179
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=19534
     Region          58..>154
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mttpsrpalr sldwtavrsr maeaieqtea hlkaaqqdad eqserraprp avdvstgrse
       61 eatvgavifm ladrrfalei ryvceivska risplpgmpa hacgvydlrg qllpvfdllg
      121 pldlprragv gddwaivcgq eqpeflilse aaprnphapp wrrsaqrspp qamhgngqp
//
LOCUS       WP_457663354             457 aa            linear   BCT 27-JAN-2026
DEFINITION  type VI secretion system Vgr family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663354
VERSION     WP_457663354.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..457
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=51137
     Region          20..>446
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvqhttenpl krnrfaavts aafqpndvtl rwlrgterlg qpfhyevkla ittpiqnfas
       61 vpgqsltagl klkgggtrff ngvitrfeyv glddtehlny laelrpwvfl lnyrtnsrif
      121 qnktsieiit aifqenkgnf knrtmgrfpr rifcvqhget dldfvsrlme qdgiyyyfeh
      181 gqdrhdlvlv dnlssheacm penvethhnl rpagnlhrdd vildwseivs lqpntvvlkd
      241 ydhekpaael tsvarvptvr iggippakda rqrlsgaprv asqtanagas sklhatfnyp
      301 gcykekwhgd fyatvraeel acstyrarie ttarqittgs tfkaanpyny gdvgarpkst
      361 qrfmaiandf tilgelgggp trsatghkae cflyhsavei ipastqyrpp rrtplpvikg
      421 pqtavvvgpr getiatdryg rikvqfflgp rgqqgrk
//
LOCUS       WP_457663357             288 aa            linear   BCT 27-JAN-2026
DEFINITION  TniQ family protein [Sinorhizobium medicae].
ACCESSION   WP_457663357
VERSION     WP_457663357.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=31264
     Region          11..128
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 misapsstql pvvprparde rlsswlnrla rfyampidaf lehcglnckd atvlewrlge
       61 eegailasrt gltiealrtm tfeeiaphar ltvargsryv crscssgihr kraafpwnfw
      121 crehdlrlda cggrklgewl pepalalldf sasdgaarlt dwahgrddgv psipqrldfl
      181 ttrhrrsspp slaeqpilsl aarranhdfl srpiarqall iivpeydrva pvlakpvraa
      241 lsadpvgyva svllasdgeg gggaaptasl agvaaritpa hlwtfptp
//
LOCUS       WP_457663359             595 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663359
VERSION     WP_457663359.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..595
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65887
     Region          122..526
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mlqalqddll asykaarldl yagewhrpai aagagfvaga amlitlatgk kkstdarfls
       61 tmearalglt rtggvfvgri ggslikvpgg ftqrgsgrrr ltkpklfggk klwidgddvg
      121 gfvigpprsg kgaslivpnc llwpdsivvl dmrgetyeat aghrskfsrv lrfspadeng
      181 dtecynpldf vainpdqrdi dinsiatall ptpkgdaywi sdaralfagv tswvlenpdi
      241 pdkdknlgtv lnvveggdqp lrewleevan pelraewiss ftyttiarfa vmagkqfdgv
      301 ygslaaavrp fknnrilrat arstfdiram rrenmslyld friqqvasig pifnvlmvqf
      361 mdymsrnmmt rgerrvlvll defqnlgkle naltvatvlg gygipcwffv qslrsidnvy
      421 tregrqtlvn saraqiflga qdpedqryvs qllgerkevt vdkavstgvt lfdrkgatms
      481 yrtamrplmr pdelgamnet rciiklrnqq pifglrnfyy addelmkraw lpiaatneqh
      541 rmtrtpevvv ehidpcpsnq aaqstvapge kfalkapprs rsgldqdakr tkpkk
//
LOCUS       WP_457663369             387 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663369
VERSION     WP_457663369.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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..387
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..387
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39016
     Region          42..296
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 milkgtnlsd tingalgnde lwgyagddhl dggdgndkif ggdgndfivg glgddyaegg
       61 agndrfnggl ghdtlkgglg ndifdggdgs dvldggdghd qilggrghdk ifggageeyi
      121 dagdgddiiy agsgddgfnn rvnpatgqvt qqavsggagh dkiygedgnd alkgqsgndw
      181 vyggigndiv dggdgnnyld ggegndvlds eggideahgg sgndkvvvga gddrvfgedg
      241 ddmlygeagn dtlsggnnyd rifggdgndt lrgdaghdvl vgeagsdilw ggtesdrfvf
      301 kgavalsgqd tvmdfqdgvd flvieklgik qysssgaagt vyaydatggd vlvkgydaag
      361 tafsilvddp ngtlsaanfs ssdflfa
//
LOCUS       WP_457663372             552 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457663372
VERSION     WP_457663372.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 552)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..552
                     /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=60890
     Region          343..549
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maitrndatl rayrpakefa gaarewllrt dperliclgr vitavfaila iyldptrpns
       61 mlyefrlvlg lylllavalv ffplrfsfvs pvhllihgvd aavvgwltfl tnelaspffs
      121 ilpfvilamt mrwglkgasl galialivql vvglpdlldg daelnifimr siyfvliaat
      181 lgyfgayrer srqrlaqlaq wpsgaigedr lswlsivlqh asgvlgdahl lviwreqefe
      241 sgcaafwtsg rlqladlrdp efwrrhdpdg cderhsrsge alnglfadlp qihanagrpn
      301 ckvvsaafss lryrgrvfvi syanstddmk dltqiiatrv gtelervali qaaraegrmr
      361 lardlhdsvl qnltaarlkl kligeafpdg arqklmevgs lileqqqcvr kfvdenrpge
      421 egnlarldqd lpefldllrm qwscsidvsi gspgmmvprw mlfeimqlis eavanavrhg
      481 ratvvrigfi gsaglleldi sdngtgiadg ltskkpfsls qriaelggsl aicrsspgig
      541 ltitlplkpg lr
//
LOCUS       WP_457663374             422 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Sinorhizobium medicae].
ACCESSION   WP_457663374
VERSION     WP_457663374.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..422
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45246
     Region          21..392
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 mgnvnscggr lrvaktgstt vsalvalvll agcgghakgv mapvalaqps atsqvdmlva
       61 ttrepsgdaa tlfsgerspt lsmtdvavsi ppdsrrkpgt vqwprklppn petdfavtrv
      121 rklasndear dwfqvhnegg hvllfvhgfn nryedavfrl aqivhdlgaq atpilftwps
      181 rarlfdynyd kestnysrta ledtlrtlas aprvkditil ahsmgtwltm eslrqmgird
      241 ggiapkienv ilaspdidld vfakqwvdmg karpkftifv sqddralavs rlisgdvsrl
      301 gaidptaepy rtqletagit aidltkvqtd dglhhgkfae speivqligq riikgqtltd
      361 sdislgegit avvagtaknv gtvaaatita pvtiieqrgt prkkvnleet ltssenagnt
      421 ar
//
LOCUS       WP_457663376            1050 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457663376
VERSION     WP_457663376.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1050
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114993
     Region          12..1015
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mqastedrkp fnlsrwaigh psiarfllal iiitgalgll rmgqredpef tfrvmvvqav
       61 wpgasiqeme dqvvnkierk lqetphldfv rsytragsai itvqiegdtn adevadafyq
      121 vrkkvgdian elpegvlgpy fndefgdtfi tlhsisgdgf sypelrrfai egrdmllttp
      181 gvekvvilgd qpekifidvs skalaerglt lndlrdaiag qnnvnhagsv dtgtrsvris
      241 veggvteaed irelrlragd rtirlgdiat vtsgledpys rkfrfnghds vqigvvmakg
      301 fnvtdvgnav eatydrfesa lpygvsvdqv snqpevvtea isefshalve aliivlvvsf
      361 lsigwrsglv iaiaiplvla atfaimyelg idlqrislga liialgllvd damivvemme
      421 rkleegleki daasfaysst afpmltgtli ttagfipvgf aqstageyvr slfyvvgial
      481 vvswfvavyf tpwlgymilk qrhhagthhd vfdtrfyrrl rstvgwavrh ritvllmtla
      541 ifmtslwgfq fipknffpqs srpeilvdlw lpegtsikev ekqakaleqr lmddkdkrfi
      601 atyigegapr fflpldqqlr npnfaqllvm akdeparerl igklrtvlae efpsirtkvd
      661 rlflgpptgw pvqmrvmgpd reevrriane vkakfrenpl lgaihddwle pvpamklvid
      721 qdraralgit sqrirqmlqa amsgvpldsf rdgeeavsiv arepggnrhl lsavqsvyvp
      781 tdfggfvpvs qvakvvpvme qgvewrrdrl ptitvratlp dgvqsndvam klfdelrglr
      841 dslppaykve iqggaedsae sqasiaakap imlvvivill mvqlqhfgka mlvlatgplg
      901 iigaaaalli sgapfgfvai lgviallgii irnsiilvdq idqdiaagme ryeaiigaav
      961 rrfrpitlta ltavlalipi srgvfwgpla yammggilva tvltivvlpa ayalffgkep
     1021 karktapgpa aaqgdadeds tpypaplaae
//
LOCUS       WP_457663378             103 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663378
VERSION     WP_457663378.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..103
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11475
     Region          1..>99
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmklyglgpt rslralwalr eldaefefvp vnilggearh pdflrlnpag klpvlvdgdf
       61 iltesaaivm ylaekygakg lmptdlkera qayrwtlfcg yra
//
LOCUS       WP_457663380             604 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663380
VERSION     WP_457663380.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 604)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 604)
  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 604)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..604
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65997
     Region          10..594
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 maftrftarn raflsvfrfs wahwkrqpvr laalltavlf stladvltpl ysgrlvdavv
       61 sgaasdeiaw naaiaafmml malslgaill rhvtfmgivs ltlkmmsdia aaafhhiqrf
      121 ssdwhansfa gstvrkvtrg mwaldllndt llvalfpsvv mlvgstalma wywpmmgvii
      181 glgsivfivv tvslslgyva pmaslanswd trlggalada vscntvvkaf gaegredarl
      241 akvlrkwenr trrtwsrgtl ngtaqgamll vlraavigfa lllwargqat agditfvlts
      301 ffilqgylre vgmhirnlqr sindmeelva ihdqslgved rpgakpirit eggiefrdvt
      361 fhygahrapl yqgfsvsiaa gervglvghs gsgkttfikl iqrlhdlnag eiridgqnia
      421 dftqaslrqq iaivqqepil fhrslaenia yarpgatqrd ieeaarlasa hdfitelpkg
      481 yatlvgergv klsggerqrv aiaraflada pilildeats sldsefevli qqamerlmtg
      541 rttlvvahrl stvraldrll vfdrgriaee gdhgalirvk ggiyrslfer qaleltkgli
      601 lseg
//
LOCUS       WP_457663382             295 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663382
VERSION     WP_457663382.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..295
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32906
     Region          1..245
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mhlsthnwmr aeplavtlkr ikkygyesie isgepaqydi kdtrallkeh gircwgavtl
       61 tlgernlaak desqraksvd yvksvitmvs elegeivtlv patvgklipd ateeeewtwv
      121 vdatkecfah aqkkgvrlav eplnrfetyl fnraaqalal adavspecgv cldafhlnie
      181 eediydaikl agnrlldfhv adnnrfaagl ghldwpkiva tlkeigydga ltnefvapvd
      241 rtpaakypdm vertpvdipp eqlkfiqdhg sslltekfyd dqmritaeti lplik
//
LOCUS       WP_457663383             341 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfate ABC transporter substrate-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663383
VERSION     WP_457663383.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 10004067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..341
                     /product="sulfate ABC transporter substrate-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36789
     Region          1..339
                     /region_name="Sbp"
                     /note="ABC-type sulfate transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1613"
                     /db_xref="CDD:441221"
ORIGIN      
        1 mgarvfvgim fgvisvgalq vgflgaavag ttivnvsyds trklykefna afaekwetet
       61 gekvtidmsh ggsgkqarlv idgleadvvt lalegdidai aqatgklppd wrtrlennsa
      121 pytstvvflv rkgnpggird wgdltkegiq vvtpnpktsg garwnflaaw awardanngd
      181 eakaqeyaaa lfkqvlvldt gawgamttfv hrglgdvlla weneaylald elgpdkfeiv
      241 tpsisiraep svalldgnvd skgtrnvaea ylgylysdvg qkivakhyyr pfkpeladpa
      301 dsarfadlkl vtigdfggwq eaqpkffddg gifdqiykpg r
//
LOCUS       WP_457663384             269 aa            linear   BCT 27-JAN-2026
DEFINITION  hydroxyacid dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457663384
VERSION     WP_457663384.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Matelska,D., Shabalin,I.G., Jablonska,J., Domagalski,M.J.,
            Kutner,J., Ginalski,K. and Minor,W.
  TITLE     Classification, substrate specificity and structural features of
            D-2-hydroxyacid dehydrogenases: 2HADH knowledgebase
  JOURNAL   BMC Evol Biol 18 (1), 199 (2018)
   PUBMED   30577795
  REMARK    Erratum:[BMC Psychiatry. 2019 Jul 16;19(1):221. doi:
            10.1186/s12888-019-2207-3. PMID: 31311510]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..269
                     /product="hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28569
     Region          2..245
                     /region_name="PGDH_4"
                     /note="Phosphoglycerate dehydrogenases, NAD-binding and
                     catalytic domains; cd12173"
                     /db_xref="CDD:240650"
     Site            order(14,16..17,41,173,221,224,230)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240650"
     Site            order(17,41,45,90,92..94,112..115,143..145,150,171..173,
                     197..198,221,223..224)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240650"
     Site            order(43..44,47..48,50..51,54..55,58,60..61,63..64,67..68,
                     70..72,74,77,78..82,84,101,104..105,199,202..204,210..214,
                     216..223,225..228,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240650"
ORIGIN      
        1 mmietapalr visrhgvgyn nvdiesatrr gvpvliadga ngksvaelav glalsvarki
       61 ttqdasirar qwnrsayglq fagktagiva fgaigrrvae ilramdmrii afdphardrs
      121 ttgvdwtetl dellqesdlv slhcpltpet rnmitaprla rmkpgailin targglidek
      181 alaeavlsgh lagagldtfa deplpadhpf lslpqivmtp hmggstdval dgvaisaarn
      241 vldvlidgkv drrllvnpav lehrtveak
//
LOCUS       WP_457663385             633 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Sinorhizobium medicae].
ACCESSION   WP_457663385
VERSION     WP_457663385.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 medicae"
                     /db_xref="taxon:110321"
     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=68782
     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 mtigaigvvy gdigtsplya frealrpfgp dgveraevvg
       61 lislmlwtlt iivtfkyvlf llradndgeg gtlsllallm kkapryttlm fmagilgaal
      121 figdamitpa lsvlsavegl klvtpafhdy vlpisvgimv llfavqsrgt gavsiffgpi
      181 tliwflvlga agvahigddl ailaafnpvn avtflwnagf vgfivlgavf ltvtgaealy
      241 adlghfgrgp iqaawfavvf paltlnylgq galvlshpea vsdpfflmfp nwallpvvll
      301 ataatiiasq avitgafslv rqainlgflp rfeicftset qtgqiylpfv nnallagviv
      361 lmfmfgsses lataygisvt gamvvttvla fefarhqwgw stltatavll pllvlelffl
      421 ganlfkihdg gyvpiliagt lmttmwtwrk gvsllrekta rqdiplsqfm amverkseha
      481 pvevpgtaif ltatpdttpa vllhnikhnh vlhqhnvilt iktarvpyvp ekdrytiekl
      541 sdrfsllelr fgfmddqnvs ralarcrkeg frfeimstsf ylgrrkliaa pqsglpqwqd
      601 klfiamadsa idpteyfhlp pnrvvelgeq vvi
//
LOCUS       WP_457663387             226 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiX family flavin prenyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663387
VERSION     WP_457663387.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  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..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /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=24005
     Region          31..206
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mgtracyagg scregrsild rtgpgrsami kerivvgvsg asgaalalrv verlaeipsv
       61 ethlivsaaa krtllhevgp halhqllaia drtyqvgdig aatasgsfrt agmivvpcsm
      121 rtlaaiaagv adnlivraad vhlkerrrlv lmtretplhl ghlrnmtavt emgavvlppv
      181 pafyhrpksi eeiidhlaar aiglfgepfa tewdpqshrp hcavar
//
LOCUS       WP_457663389             592 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Sinorhizobium medicae].
ACCESSION   WP_457663389
VERSION     WP_457663389.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..592
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65402
     Region          52..481
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,316..317)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,317)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mkpisesrlg ataaaiarsq gwkafalagt ilvssvvtts spasaqdapg kpnilvifgd
       61 dvgqfnlsty sfglmgyktp nidriadegm kftdyyaens ctagrssfit gqtpkrtgls
      121 kvgipgapvg lqdrditiaq alkplgyatg qfgknhlgdr deylptahgf deffgnlyhl
      181 naeeeperpy wpkddlayvk ansprgvihs yadgriedtg alnakrmeti ddettsaaie
      241 fmkkqveqkk pfftwmnttr mhvfthvrps mlgqsgmpgn eyadgmiehd ghvgkllkal
      301 ddmkiadnti viyttdngpn qfswpdaatt pfrsekdtnw egafrvpami rwpgkikpga
      361 vsnemfsgld wfptllaaag egdikekllk gtdvagkqfk vhldgynqlp yltgeteqga
      421 rqefayfndd gklvafrykd wkavfcemka pggfrvwyee fdclripklf nlrmdpmera
      481 dtvsdqyddw riknaymmgw mtfhaaqfle tfvdyppsqt pasftidqie adverrsaek
      541 aggeqivhga crlsstrpis ssgasplpar ssgsttrsnl qdgsslqthk np
//
LOCUS       WP_457663390             137 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663390
VERSION     WP_457663390.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..137
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14883
     Region          <48..117
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(67..69,79..80)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mlcsdrplrr lkpsatplra tamletcsag stssswsveg rnglgrpgrl rarqvrerat
       61 gvlyydlavd egyrrqgiat alirrlcdla aerggwvvyv qadlgdapai alyeklgvrq
      121 dvlhfdivid akrvgps
//
LOCUS       WP_457663394             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663394
VERSION     WP_457663394.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38828
     Region          2..354
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mskhfgegah altvirdlnl tigkgeffsl lgpsgcgktt alrmiggfeh psegdvlldg
       61 esitgvppyr rdvnmvfqsy slfphmdvye nieyglrrkk vprqerrkri advvalaqld
      121 dyvsrrpnql sggqqqrval aralvnqpkv llldeplaal daklrgtmqe elrriqrevg
      181 itfvfvthdq qeafalsdrv avmragrleq agtplelynk patrfvadfv gqsnfisgpv
      241 ctmarrllel gqegdrvflp aeapgtaati vvrpeqialh adqpelqges rsrlagfvse
      301 ntflgskhvl riktclpepi lveashgavs alapepgrsl wlswrsgdga llad
//
LOCUS       WP_457663396             392 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663396
VERSION     WP_457663396.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..392
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42105
     Region          <1..377
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mkagtqaglp lnhdfngmtq egvgrfqltt rngrrsssar aflgpatrrp nlhiltgisv
       61 drleldgrqv rgihcrrggd rlhllcrrei vltagaigst qilqlsgigd paqlvaagvr
      121 plhalpgvgr hlqdhlqsrl mlklnlpisl ndltrgpwrk lligmdyvfr rrgvlsfgas
      181 laggfgrtpl asdrpdvqfh fqplsldnyd gglhpfpgat isacqlrpqs egtifitspd
      241 psvhpeirpn ylateldrqt miegfrfarr iaaapalaev iagehrpgng vnsddeildy
      301 iratgssiyh psstcrmgpd pdlgdvvdar lkvhglaglr iadcsimprl vsgntnaaai
      361 migeraaaii redaaaamat dgtitnetek ta
//
LOCUS       WP_457663404             642 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663404
VERSION     WP_457663404.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 642)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 642)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 642)
  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   6  (residues 1 to 642)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 642)
  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 10170692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..642
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72107
     Region          54..618
                     /region_name="PBP2_NikA_DppA_OppA_like_4"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08500"
                     /db_xref="CDD:173865"
ORIGIN      
        1 mqefsrrafl lastaavllp vmpvialans akepamleal akagslpava drlplnpmvv
       61 tpldrvgthg gdwnsaivgg gslsmlfryq ayepllryap dwsgvvpnva ehyesnadat
      121 eftfrlrkgm kwsdgepftt edilfwyedi fnyeglndvg qnhlraggkk arfeavddvt
      181 fkvifaapng lfplrlawan ddqttrapkh ylkqfhikyn pnaeeeaktk gasgwiqlfq
      241 reaglvvdne ffqnsqrpvi hawkvaiapg qstdravaer npyywkvdte gnqlpyldwi
      301 vyqmvsdpqv lllkamqgei dlmdqyiatp anravlydsq eqgkfgfytl tstetnemvf
      361 qlnlnhpnev krklynnkdf raalsmaldr qaiidtvfig qgtisqpavr addplynerl
      421 atqytqydpd ranalldkil ptkdsegfrl deggkrvsii feidqaratf ldifqlalpm
      481 fravgldvqm rsmdrslwev rvrqgieyda tahrfggngg iaaildpryf ipnttealya
      541 kgwqlwyrds qsqgaveppq pvrnalalyd rvlasadpde qkklmaeile iaadqfyvfg
      601 iclpadsygv vkndmqnvpe ampnswgypt pgpanpetff kv
//
LOCUS       WP_457663410             473 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663410
VERSION     WP_457663410.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..473
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=49916
     Region          36..466
                     /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 mnedrvevsw vpalgrakgp fylaiadeia adiaagrlan gmrlppqrvl aaalgidftt
       61 vsraynearr rglvegrvgq gtyvrtrers sgrpsadrla aglvdmsmnl pplfddpals
      121 akmwadvgal ghggldqrsp ellmryqpvg gterdrsaga awlkprlggl qadrmvvctg
      181 aqgallasvg mlatkgdrvc aealaypglr slaaylgiel vsvgidrngi lpeafeeacv
      241 lhrpkalycn ptlhnpttat lpldrreaiv eiarrhgvai ieddaygalp aspvpplaal
      301 apdlvyhvag lakclspalr iaylvapdrs aairlegavr atagmtspls vaiatrwlee
      361 gtaqavldai rteagarqqi asrslegadl ssdregfhlw lklpsgwnrg eftaqlraag
      421 igvvasdafa isdppeavrl glgaartrdd lresldviag llarspaahn liv
//
LOCUS       WP_457663411             191 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663411
VERSION     WP_457663411.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..191
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21458
     Region          5..181
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 miiheterlk lrawleadrd lfaeinsdpk vveffpfrrn radadalfds nnrnihetgf
       61 gffalalren dapigfcgla rtdlkphlpd gtveigwrla arhwgkgyvt eaagalldyg
      121 feerklgeiv aiavatntrs iavmkrigmy cdpsrgfehs gvpdthpqlr phvlyaitad
      181 rrqrngetak r
//
LOCUS       WP_457663412            1246 aa            linear   BCT 27-JAN-2026
DEFINITION  AsmA family protein [Sinorhizobium medicae].
ACCESSION   WP_457663412
VERSION     WP_457663412.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1246)
  AUTHORS   Prieto,A.I., Hernandez,S.B., Cota,I., Pucciarelli,M.G., Orlov,Y.,
            Ramos-Morales,F., Garcia-del Portillo,F. and Casadesus,J.
  TITLE     Roles of the outer membrane protein AsmA of Salmonella enterica in
            the control of marRAB expression and invasion of epithelial cells
  JOURNAL   J Bacteriol 191 (11), 3615-3622 (2009)
   PUBMED   19346309
REFERENCE   2  (residues 1 to 1246)
  AUTHORS   Deng,M. and Misra,R.
  TITLE     Examination of AsmA and its effect on the assembly of Escherichia
            coli outer membrane proteins
  JOURNAL   Mol Microbiol 21 (3), 605-612 (1996)
   PUBMED   8866482
REFERENCE   3  (residues 1 to 1246)
  AUTHORS   Misra,R. and Miao,Y.
  TITLE     Molecular analysis of asmA, a locus identified as the suppressor of
            OmpF assembly mutants of Escherichia coli K-12
  JOURNAL   Mol Microbiol 16 (4), 779-788 (1995)
   PUBMED   7476172
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1246
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1246
                     /product="AsmA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=132170
     Region          1..434
                     /region_name="AsmA"
                     /note="Uncharacterized conserved protein AsmA involved in
                     outer membrane biogenesis [Cell wall/membrane/envelope
                     biogenesis]; COG2982"
                     /db_xref="CDD:442221"
     Region          <688..992
                     /region_name="AsmA"
                     /note="Uncharacterized conserved protein AsmA involved in
                     outer membrane biogenesis [Cell wall/membrane/envelope
                     biogenesis]; COG2982"
                     /db_xref="CDD:442221"
ORIGIN      
        1 mlarilvtlg gllvvalfaa liaplfidwt sfrndferea srimgkpvvv hgsvdarlip
       61 fptvtlndvr vgssdggppl iqvaqfsmsa elapflsgea lifdmrldrp karirlqpdg
      121 tldwargsrt aipahtvile kveiadgeie fvdeqtgrtr rvsdlsadls artlagpwra
      181 egraaldgev gsfsftsnav detgalslra rlvpderpfg veldgslkvv dfrpvyagrf
      241 tltenrpane vkadgalrin gefqltnesi rvpeyhfeig ppddpyivtg eatldtgkdq
      301 rflliadgqq idvsrignsg ssgktgrdpa islrqridam laiaadipip qvpgraslkl
      361 paivigdttv rdvrldvrpd gagwivdnav allpgrtlle akgrlnlkeh rsfrgdlvia
      421 snqpsgfanw lagsvdpair tlktagfsat vnltdtlqqf eslevaagpa tlrgrierqs
      481 fadqppalsm qlkgnhidle alqalaglva gdastgtllq hsiaadlsae tfsafgeear
      541 dvqavltlkn gqlqaervai ralagaqlaf sgrmsgglek pvvsakmkla aeeltpflem
      601 igrhstahpa ltrlikagsy ysdaaldltl tagnkegnap vtfgvigtas ggriagsyqa
      661 pdvaqalsgq gmlleatlen prtavllgqa gldplpfead angilaiklq stegskanga
      721 lsfttertsl aangvfdlsr ahylegqgkl tlksedlepy lllqgiglpq mgsglpltvs
      781 aefstdpdki aitaiegrad rngfagalai drkvpgkaeg elaldtldla wlaegilgqv
      841 hdtstgglal apvakpawtg ldmavninak rfwpgvydpv snfagrlewk gdelalsdat
      901 gdwlggkleg rmhfgnangs gylrsqldlk gadlaeagwv rangpvatgr fdlavameat
      961 gatpeamaqs lsgsgtasfn gltlngvnta alpqlmaaad amktdispes irraaenllf
     1021 sgqsvvgtvk vpfgiaggtv rvqnvaagdg naafsgeasf dlpegrmagt idltfrpgee
     1081 alagadprvr fgyagllssp gvtvdvtels nflslrafer errrveilqa nvlekqrlrr
     1141 evalyraraa ereqqrlrti aeerrrqaaa aeaarmraea qaraaaarra edeerlrmrq
     1201 lparsigrqq apvtppqdag trqrqnagpp agqglnfdll pditvr
//
LOCUS       WP_457663416             316 aa            linear   BCT 27-JAN-2026
DEFINITION  RecT family recombinase [Sinorhizobium medicae].
ACCESSION   WP_457663416
VERSION     WP_457663416.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Caldwell,B.J., Norris,A.S., Karbowski,C.F., Wiegand,A.M.,
            Wysocki,V.H. and Bell,C.E.
  TITLE     Structure of a RecT/Redbeta family recombinase in complex with a
            duplex intermediate of DNA annealing
  JOURNAL   Nat Commun 13 (1), 7855 (2022)
   PUBMED   36543802
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Muyrers,J.P., Zhang,Y., Buchholz,F. and Stewart,A.F.
  TITLE     RecE/RecT and Redalpha/Redbeta initiate double-stranded break
            repair by specifically interacting with their respective partners
  JOURNAL   Genes Dev 14 (15), 1971-1982 (2000)
   PUBMED   10921910
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..316
                     /product="RecT family recombinase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=35324
     Region          43..189
                     /region_name="RecT"
                     /note="RecT family; pfam03837"
                     /db_xref="CDD:397770"
ORIGIN      
        1 mnqlakaprr svlvdmaghf gmeadafemt vraqcsptpk kgeqfrpltr eefaafllva
       61 kkydlnpltr eifaypkrgg gvvpivsidg winlvnshpa cdgfqftwer dangdpisct
      121 cimhrkdrsh ptavteylae cwrdtepwkm khrmlrhkal mqcaryafgf agiydedegr
      181 riaedqnial lppaprapri gqqspageki qtaqgdatev esgtgqppvd sasplddepd
      241 pdreemggvd adstpdaeff delrdrlaea kdaasveeiw teldpmarfe gsdldqeicq
      301 kikarrlrdl ekedgk
//
LOCUS       WP_457663426             281 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663426
VERSION     WP_457663426.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..281
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31651
     Region          <37..>265
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 maipnaiirs tssrsipisa iststrsrrr ccrrrrgday wisdaralfa gvtswvlenp
       61 dildkdknlg tvlnvveggd qplrewleev anpelraawi ssftfttlar favmaskqfd
      121 gvygslaaav rpfknnrvlr atarstfdir amrrenmsly ldfriqqias igpifnvlmv
      181 qfmdhmsrnm mkrgerrvlv lldefqnlgk lenaltvatv lggygipcwf fvqslrsidn
      241 vytregrqtl vnsaraqifl gaqdpalprl ncslrmgycl i
//
LOCUS       WP_457663436              71 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Sinorhizobium medicae].
ACCESSION   WP_457663436
VERSION     WP_457663436.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     New connections in the prokaryotic toxin-antitoxin network:
            relationship with the eukaryotic nonsense-mediated RNA decay system
  JOURNAL   Genome Biol 4 (12), R81 (2003)
   PUBMED   14659018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..71
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0097351 - toxin sequestering activity
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045927 - positive regulation of growth
                     [Evidence IEA]"
                     /calculated_mol_wt=7892
     Region          4..62
                     /region_name="PhdYeFM_antitox"
                     /note="Antitoxin Phd_YefM, type II toxin-antitoxin system;
                     pfam02604"
                     /db_xref="CDD:460615"
ORIGIN      
        1 mtstvtaaav sknfgayqda avrepviitk ngrprtvlla yedylrlsrr drrveatadl
       61 apvhywdadi r
//
LOCUS       WP_457663438             119 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Sinorhizobium medicae].
ACCESSION   WP_457663438
VERSION     WP_457663438.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..119
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=12540
     Region          <1..118
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mgvsnwfass srgdssklsg gtfssglrmg tlveltnpkg iafflglyav sippdaaisv
       61 kltvlaggfi lemlwysfvt vlmssppaqa vyrtsgawid rfvgtlligf gikllserl
//
LOCUS       WP_457663457             550 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663457
VERSION     WP_457663457.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..550
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=61428
     Region          18..423
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mkalsktlld gtprqdlraa lylrvstgrq vdndlsipdq rrqaaefcaa rgwtvavefv
       61 daglsgtddk rpelqrllel atdggspfdv vvvhsfsrfa rdhfalehav rrlrkhgvrl
      121 vsitqdlgdd pmsvmvrqvf alfdeyqske nakhvlramk enarqgfwng aqspygyaiv
      181 aaeqrgaktk krlaidpvea evirlmfrlv tegaensgpl gvkaatswln erdyrtrkga
      241 rwgigqlhkl ltsptykgey lfnrkvwktk edkpetervm vpveaiiepa qfeavqarlk
      301 srspramppr tvtgpilltg latcagcggg mtlrtgksgr yryytcataa qqgksackgr
      361 svpmerldni vtarlaetlf tpdrvraivg gllerqaars edhttriavl qnkvadsetr
      421 lsrlyqaien giadasdptl kerldnlkse rdqakaarer afaelrpetr lteekisafa
      481 tlmrenvtng pvpfrraylr svidqievdd dqirihgrrd vlerlvttgv aaagvpsfvr
      541 kwrtrrdsns
//
LOCUS       WP_457663460             194 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663460
VERSION     WP_457663460.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..194
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20895
     Region          <6..162
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 msvgtglslg iifglligls gfwsrllgsi irffyaivev awiplleiwi gygfptilia
       61 isyvvffpvl yntltgvqti qpvlinavrt lgasrfqvlt svilpaalpn imtglrvgag
      121 fafrglifae miaagsglgf lifdgastrq tdrvvvgmim mgllwllmdr lllrpierat
      181 iercglvraq gges
//
LOCUS       WP_457663472             322 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663472
VERSION     WP_457663472.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35505
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,224,241,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpwidrrrwr cfsplsrrgd fsaaarrlrm tpsavskivg rlesrlgvrl lqrstrsisl
       61 taegnsyses vrrilgdmee aelaiqpgae prgrlrvslp safghrlivp mlpafigryp
      121 aieleldftd aivdlvngda dvavrvaaqg dstlvtrrla pnrrvicgap dyferhgvpm
      181 rpddllkhic lgissrggln lwefdeaggr rsmrirssie anstealrrl alagmgivrl
      241 semlvgqdir agrlkpvltd cnhaeaepis vvyphrrfls prvrvfvdfl aeqfaksiae
      301 ggdaarvirg tsgglpesda mr
//
LOCUS       WP_457663489             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663489
VERSION     WP_457663489.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35482
     Region          1..323
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtaapvlsvs glaidyelss gglfrkrrsv savsdvsfel apgetlglvg esgsgkttvg
       61 rallrripaa kgrivfdged itnlqgealr rlrarmqivl qdpytslnpr mkvssivaep
      121 livhglaasa eeartavael lervglpgda adryphsfsg gqrqrigiar alalkpaliv
      181 adepvsaldv svraqvvnlm qdlqrdlgis ylfiahdlai vrhishrvai myagriveia
      241 prqaiyerpi hpyteallsa vpvanpklqr arrrivppge svditnppkg crfhprcpla
      301 snrcrkeepq llrksgdhfa acwnrda
//
LOCUS       WP_457663490             371 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663490
VERSION     WP_457663490.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11438329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40681
     Region          1..300
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
     Region          256..366
                     /region_name="CBS_pair_SF"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains superfamily; cl15354"
                     /db_xref="CDD:449531"
     Site            order(258,260..262,285..287,342,355,357,359..360,363)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341359"
     Region          258..315
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341359"
     Site            order(285,297,302..303,306,320,342..344,359)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341359"
     Region          320..363
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341359"
ORIGIN      
        1 mirlenltkh ygpahdplia vdnvsldlpt geicvllgps gcgktttmkm inrliqptrg
       61 kvfingkdts tvdpielrrs igyviqqigl fpnktieeni cvvpdllgwd rrksrdcake
      121 llelvglqpd lflkrypkel sggqqqrvgv lralaadppv mlmdepfgai dpinreviqe
      181 eflkmqreir ktiifvshdl deavkmadki aifrsgkleq yaapddllar pansfiedfl
      241 gsdralkrlr lvsvgdamet dfitvletds vehararirs srsaaafvld aegaprsvls
      301 eqvaeacsgt vgehaepvks tvpttgdlrq avsvmfahdm pllpcideag rlagvmsyrs
      361 ivhhlghggk a
//
LOCUS       WP_457663492             594 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457663492
VERSION     WP_457663492.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 594)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..594
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=64582
     Region          3..589
                     /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 mplvaklqer laagdeagts dqvlsigesd lvriggrpai vsakpivsdt gdivqepgre
       61 flhlairfld ddfltglgad ygfedlrfsv spdlgrnrsy apivrssgep igyfswlpfr
      121 pgaavmkata pvllisglll ftltsglsvv lrrrsrrlqe sqaelnhlar hdpltglanr
      181 asfnqslaqa vassaadqan allyldldrf kqvndtlghp vgdrlmvava krlmetasag
      241 visriggdef tivvertrqe eveklcdsli aairqpfeid gqpiliglsi gvavatgnda
      301 dpveitrkad ialyhaksag rnryavfghh mdelirtkrd leqdlraald agnqlevfyq
      361 pvysaqsrei sslealvrwr hpskgaiapd vfvplaetag lidrlgafvl keacstaref
      421 psldiavnvs aielgqrhya aqvfsllrqf svepwrlele itetalldea gvceknital
      481 rdfgvkfald dfgtgfssfg rlqrlevdri kidrsfvhaf drpgggvavv qsivgvahak
      541 glritaegve teeqseilrn lgcdelqgfh lskpvpkssl rqllgaetak rtss
//
LOCUS       WP_457663497             100 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Sinorhizobium medicae].
ACCESSION   WP_457663497
VERSION     WP_457663497.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..100
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11442
     Region          7..94
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 maelsnmayf takpgrskkl gdellrlvap srkeagclry eihqsndvpd vwmvlenwry
       61 asdfklhmst dyvrafmvkv pdlcvedvei cgyrqrspqa
//
LOCUS       WP_457663498             198 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent F420 reductase [Sinorhizobium medicae].
ACCESSION   WP_457663498
VERSION     WP_457663498.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..198
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20621
     Region          4..187
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mityaiigsg aigsalaerf haagvdavia ntrgpaslqp itdrfgsavn aveleqalrs
       61 dvlilavpyd avpeiaerka dwngrtivda tnaidfpafk prdlggrlss eivadlfpga
      121 qlvkafntlp aavlaaepvk asgkrvlfls gnypeaskkv adliarlgfa psdlgsfkas
      181 gslqhfgqpl valnllrd
//
LOCUS       WP_457663502             133 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457663502
VERSION     WP_457663502.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 133)
  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 133)
  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
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..133
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=14285
     Region          2..126
                     /region_name="PIN_MtVapC28-VapC30-like"
                     /note="VapC-like PIN domain of Mycobacterium tuberculosis
                     VapC28 and 30 and related proteins; cd09871"
                     /db_xref="CDD:350219"
     Site            order(12..15,19,23,26,31,44,50,52..53,56,59..60,63)
                     /site_type="other"
                     /note="toxin/antitoxin interface [polypeptide binding]"
                     /db_xref="CDD:350219"
     Site            order(35..36,38..40,42..43,46,51,54,58,70..71,76..77,
                     79..80,83..84,97..98,100..101)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:350219"
ORIGIN      
        1 miavdtsvil tmalaepeae rftalvgres iaigwptlle vrivltgkgf pnssdivdql
       61 vqlpnvaaia fdeahyreae rafdrfgkgr hpatlnmgdc fsyavariak apllfkgndf
      121 gqtdlkihpa ssg
//
LOCUS       WP_457663503             394 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663503
VERSION     WP_457663503.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  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 10009251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43299
     Region          1..334
                     /region_name="COG5397"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444156"
ORIGIN      
        1 mlktvdliyq tmlaeigqra mddawtldfp pigrfvkvkv kereywyfdq sdgeggqkrk
       61 yvgpaedpei skrvedfsrt ksdyrirrrl vssltrdggl laadrtsgli vetlaaaglf
      121 rlrtvlvgtl afgtysgllg vrmpsaaimt gdadfaqdya isaevmdslp pilellqsad
      181 ptfravptfd ggattafvng egyrvefltt nrgkdeyldk padmpalgga saqplrfmdf
      241 lirepvravl lygagvsvlv pdparyavhk liiasrrhah salkrdkdlv qaailveall
      301 qtkrspdlam ayveawergp awqeaieiga amlsvehkdr lrecleagga gnrregdiav
      361 lrshgsskmv irsfftpevk vgsssrpqri tktn
//
LOCUS       WP_457663510             791 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663510
VERSION     WP_457663510.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..791
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88370
     Region          2..787
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mtdtlspell ermdaywraa nylsvgqiyl rdnpllkqkl tlahvkprll ghwgttpgln
       61 flyvhlnrli qahdlnmiyv tgpghggpgl vantylegty selypkvsqd eagikrlftq
      121 fsypggipsh vaaevpgsin eggelgyclm haygavfdnp dliaacvigd geaetgalat
      181 swhsnkflnp ardgavlpil hlngykianp tvlarishde laalfrgygy eplfvegadp
      241 rqmhqlmasa ldkahskiae iqrqarskgf srrpawpmii frslkgwtgp revdgkkaeg
      301 twrshqvpla klaevpehlg ilegwlksyr pwelfdesgs lrpelgelap kaerrmganp
      361 hangglllkn lnlpdfrqfa vdistpgtlm aestrivglf lrdvmklsak ernfrifgpd
      421 etesnrlspv feetdrvftg qilasdtqls pdgrvmevls ehlcqgwleg ylltgrhgff
      481 scyeafihiv dsmfnqhakw lkvcreipwr kpiasltyll tshvwrqdhn gfshqdpgfi
      541 dhvankkadi irvylppdan tllsvvdhcv rsrdyinviv agkqpqlqwl dmdaavahcr
      601 aglgvwewas ndegdpdavv acagdvptme alaavmilre afpslrlriv nvvdlmalqa
      661 psqhphgiad dafdrmfttd kpvifayhgy palihrltyr rvnhanfhvh gyqeegtttt
      721 pfdmavlnkl drfhlakavv ervpslaatk egfahfvenk laehdayire ngedlpdirn
      781 wrwlapavda q
//
LOCUS       WP_457663514             699 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663514
VERSION     WP_457663514.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..699
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74799
     Region          372..666
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mdigglvhas illffqfvfg laaplaaqev atqappakvq qliellddpd vrqwlaakqt
       61 tataavippa gyasrlvtgi rrhligmgqa iprlvpewia areriahelq ngattaivwg
      121 lslvliagna aeflvryalr rsarrsaaep gpglaaltgi aplvvfaiaa vaafahtgwp
      181 srleaavapl lvawigarll savasavmep rytgsgaaqg ragapgpevm lfwykrsvpf
      241 iyamaftwav vdmmqalalp advrdltaav lglvvlgmai davvrrplve mtagrrilrd
      301 aliigllall wllwaagmkv lfwvgvfali lppllrfttv atrsmldtea adyipmmrnv
      361 lidrgirlli valaaawlai vfklhgspvi qgdvakhifr gvlagviill vadfvwqlmk
      421 efinlhlkra tmesgdsaqi arnmrvrtll pilrnflavf iaivagmmil sslgvhigpl
      481 iagagvfgva igfgsqslvk diisgifymm ddafrvgeyi qsgsymgtve sfsirsvrlr
      541 hhrgpvftvp fgslgavqnm srdwvidkft invaydsdva kvkkvvkgvg aalledpelg
      601 pliietvkmk gveqfgdygi tlgfamttkp ghqtqvrrra qalikdafkt hgihfasptv
      661 qvagdeaqss maaaamtrdt iakknaalaa qqggeaaae
//
LOCUS       WP_457663519              81 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663519
VERSION     WP_457663519.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   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..81
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..81
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8636
     Region          11..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 mkgilnemag mvafvrtvet gsfsaaaksl gltpsaasks vsrlelllga klfrrstrtl
       61 srgrcvlwar daldapnrkr d
//
LOCUS       WP_457663520              75 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457663520
VERSION     WP_457663520.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..75
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=7855
     Region          <1..74
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mygnigskrr ldftvigpav nlasrleglt ndlkrpvlvs gdfvtaagcs aktdclglhs
       61 ikgfddalev halrl
//
LOCUS       WP_457663521             253 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663521
VERSION     WP_457663521.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..253
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26723
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggtg ligsklvkrl qakghevvaa spasgvntat gegladvlig aqivvdvans
       61 psfedkavme ffqksgqnll aaeaaagvkh hvalsvvgtd rlqdsgyfra klaqeklikd
      121 akipytlvhs tqffefmfgi aqsgaqgekv hlspammqpi fsddvadlla dlvlgqpvng
      181 vaeiagpepi riadavtkyl rqigdgrevv vgektpyfga llddktlmps ksvrlgktky
      241 sewvktatpp par
//
LOCUS       WP_457663525             194 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663525
VERSION     WP_457663525.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20850
     Region          3..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrkakeltr ndwvlaglaa laeggidsvr verlakslnv skgsfywhfs drsdllsall
       61 dlwekdftaq vianvasqpt prarllalae ealdasmdgv dvaqaegafs awavldpaaa
      121 vrvraieaqr igylvrelsl mgadtaqael lakgiylall gvfaarrynp alaedavfrr
      181 ivalaldavg grrr
//
LOCUS       WP_457663526             328 aa            linear   BCT 27-JAN-2026
DEFINITION  hydroxyacid dehydrogenase [Sinorhizobium medicae].
ACCESSION   WP_457663526
VERSION     WP_457663526.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Matelska,D., Shabalin,I.G., Jablonska,J., Domagalski,M.J.,
            Kutner,J., Ginalski,K. and Minor,W.
  TITLE     Classification, substrate specificity and structural features of
            D-2-hydroxyacid dehydrogenases: 2HADH knowledgebase
  JOURNAL   BMC Evol Biol 18 (1), 199 (2018)
   PUBMED   30577795
  REMARK    Erratum:[BMC Psychiatry. 2019 Jul 16;19(1):221. doi:
            10.1186/s12888-019-2207-3. PMID: 31311510]
            Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10187407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=34669
     Region          4..304
                     /region_name="PGDH_4"
                     /note="Phosphoglycerate dehydrogenases, NAD-binding and
                     catalytic domains; cd12173"
                     /db_xref="CDD:240650"
     Site            order(53..54,73,75..76,100,232,280,283,289)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240650"
     Site            order(76,100,104,149,151..153,171..174,202..204,209,
                     230..232,256..257,280,282..283)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240650"
     Site            order(102..103,106..107,109..110,113..114,117,119..120,
                     122..123,126..127,129..131,133,136,137..141,143,160,
                     163..164,258,261..263,269..273,275..282,284..287,291)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240650"
ORIGIN      
        1 mgpkvlmtak tlatpglall eqtgcavsfl kegteaelae slrstpfdav isrtlalpam
       61 mietapalrv isrhgvgynn vdiesatrrg vpvliadgan gksvaelavg lalsvarkit
      121 tqdasirarq wnrsayglqf agktagivaf gaigrrvaei lramdmriia fdphardrst
      181 tgvdwtetld ellqesdlvs lhcpltpetr nmitaprlar mkpgailint argglideka
      241 laeavlsghl agagldtfad eplpadhpfl slpqivmtph mggstdvald gvaisaarnv
      301 ldvlidgkvd rrllvnpavl ehrtveak
//
LOCUS       WP_457663474             155 aa            linear   BCT 27-JAN-2026
DEFINITION  transcription termination/antitermination protein NusG
            [Sinorhizobium medicae].
ACCESSION   WP_457663474
VERSION     WP_457663474.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 155)
  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 155)
  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 155)
  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..155
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     gene            1..155
                     /gene="nusG"
     Protein         1..155
                     /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=16883
     Region          7..155
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 meksldamgv rslvpmrkgp dlrrrgrvie gqmmpvihgy vlvqmmalse ylagllgveh
       61 vidvlggcer pmrlsdkevs rfnglarkgn fdwerpvhlv vragdpvwit agpfcdrkat
      121 vvtpgkkgrg dvvvsidlmg gevpvtvpla llkkl
//
LOCUS       WP_457663529             450 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457663529
VERSION     WP_457663529.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 450)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 450)
  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 450)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..450
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48826
     Region          123..446
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrletrslag rlvlslslll avfwtiavgl sihvmraefd evfdsalqet terlaslvvd
       61 dyfrrdaatg pnqvaaldpg atdeyltyqv rdaygrvllh shnigtepyp aplkpgfwsg
      121 nerriftiat vsdtlfvqva dslahrreat lesaltlllp illllplgmf avrwvvvrat
      181 rpvnelrdai strdgsnlep ivlqglptei aaipgsvntl lgrlklalqa erdlaansah
      241 elrtplagal aqmelladql tapddrsrsd rvlealrrls lmlekllqls radagigvss
      301 tpvdllalvk llvesfqrsh qtstiqlrtp pgpatllrav dpdafaiafn nllenaacyg
      361 tagqpitvai sadgrftvtn pvsvlldpdl dvyrarfrrg qtskpgsglg laivdklmaq
      421 mdgtmilrtv klsgertgfe celslpptnq
//
LOCUS       WP_457663540             626 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663540
VERSION     WP_457663540.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..626
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=70715
     Region          14..427
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 msntdlipta llarkaivyv rqssqsqvmt nlesqrrqyd lvdvarqhgf sdietidddl
       61 grsasgtvar pgfdrlvall cagqvgavlc fdasrlarng rdwhhllelc glvearvidh
      121 dgvynpcrpn drlllgmkgs isefelgvlr armlddarsk arrgelrlsv pfgyiwhrea
      181 glgldpdlrl qdvirsifar frelgsarqv llsmtrdnih fprpsdegrm tsfvwtpvry
      241 rnvigilknp fyagvyvygk sekrtaivdg rtrrsyghgk pagtwevmir dhhegyiswe
      301 eyernqqqla lnnygrsggt ksgrggksll sglltcgrcg rrlsvaytgn pqnpvyrcyk
      361 qnlmmglpgc mtfggskvda avarellrav eplaieatfe aermhrerqe eqrhihdlel
      421 rqaryeasla erryaacdpd nrliaaqlek nwetalrrvr dlevrkpads pstievdtgt
      481 fanladnlqa awespdvtmr vrqqllrtli adivvdvede vrdvvltihw tggqhselrv
      541 rkpqsgehgc attedalavm rsmagrwpde hiaaslnrmg mptgqgktwt ahrvvrfcsr
      601 nrgrarrqsr plsaprqdlp qlrrri
//
LOCUS       WP_457663543             387 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663543
VERSION     WP_457663543.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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..387
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..387
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38918
     Region          5..264
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <255..>320
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 milkgtnlad tirgfladda iwgyegddyl ygdagndrif ggsgndfina glgndsaegg
       61 dgndrleggl gddtldgglg ndtfdggngn divkggdghd qilggrghdt iyggageeyi
      121 dagdgddviy agsgndgfnn rinpatgklt qqavgggagn dtiygeegnd alkgqagndk
      181 vyggigddiv dggngdnfld ggdgndvlds eggidvaygg vgkdkiavga gndlaygddg
      241 ddilsgeaga dvlhggtgnd liyggngndi vrgdvgkdtl vgeagsdilw ggadsdrfvf
      301 kgtptlsgqd svmdfqdgfd ilvienlgvt rysssgangt vfaydttggd vlikgndsvg
      361 rvfsilvddp igtlsaaqfs kadflfa
//
LOCUS       WP_457663544             164 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663544
VERSION     WP_457663544.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..164
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17995
     Region          1..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldaidlri leaiqadgri tklalaekag lsptpcwmrl rklektgivt gyharvalrr
       61 vapvasvmme itlgnhrqad fdrferaiaa ipeivacwsv gggvdyilki mtadidayqr
      121 lvdgllerel gidryftyiv tktvkdetvl plgsllpqas agqd
//
LOCUS       WP_457663545             456 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Sinorhizobium medicae].
ACCESSION   WP_457663545
VERSION     WP_457663545.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..456
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47743
     Region          <88..123
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 mtiaaprlyr llavlfcwls tqgpalsadp laraalqsqg tlyagqqilv dvdvlvpnyf
       61 lqspqfpaid ipgaivtldd gralnlneti dgtpysgirr tyiivpqaag dftlppvpit
      121 fgyaavppqa trgevtfppl rftvrsapgt agdspgivaa kvsvsqeldq dpaqlkagdt
      181 mvrtvtvrae glrammipep dftapqgvrl yrqdpslsee tdrngqsiag lrkdvasylf
      241 qdagnyvlpa vtvswfdpas aktqsatapa vsvtvsaaaa lspalappra gaatrclrla
      301 apgsdrgdra shrllalgcr qrivpagslv arapleraav gagffpasga gvqkrprrrd
      361 rararrlvaq sgsdaartla walrgcrdqa glpglaenal rfsasipavr srlasarpee
      421 gsgslvdagn gsarpqagla spqpdyavtr rmkadl
//
LOCUS       WP_457663546             552 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457663546
VERSION     WP_457663546.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 552)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..552
                     /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=60816
     Region          343..549
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maitrndatl rayrpakefa gaarewllrt dperliclgr vitavfaila iyldptrpns
       61 mlyesrlvlg lylllavalv ffplrfsfvs pvhllihgvd aavvgwltfl tnelaspffs
      121 ilpfvilamt mrwglkgasl galialivql vvglpdlldg daelnifimr siyfvliaat
      181 lgyfgayrer srqrlaqlaq wpsgaigedr lswlsivlqh asgvlgdahl lviwreqefe
      241 sgcaafwtsg rlqladlrdp efwrrhdpdg cderhsrsge alnglfadlp qihanagrpn
      301 ckvvsaafss lryrgrvfvi syanstddmk dltqiiatrv gtelervali qaaraegrmr
      361 lardlhdsvl qnltaarlkl kligeafpdg arqklmevgs lileqqqcvr kfvdenrpge
      421 egnlarldqd lpefldllrm qwscsidvsi gspgmmvprw mlfeimqlis eavanavrhg
      481 rasvvrigfi gsaglleldi sdngtgiadg ltskkpfsls qriaelggsl aicrsspgig
      541 ltitlplkpg lr
//
LOCUS       WP_457663552             537 aa            linear   BCT 27-JAN-2026
DEFINITION  GumC family protein [Sinorhizobium medicae].
ACCESSION   WP_457663552
VERSION     WP_457663552.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Grangeasse,C., Nessler,S. and Mijakovic,I.
  TITLE     Bacterial tyrosine kinases: evolution, biological function and
            structural insights
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1602), 2640-2655 (2012)
   PUBMED   22889913
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Grangeasse,C., Doublet,P., Vaganay,E., Vincent,C., Deleage,G.,
            Duclos,B. and Cozzone,A.J.
  TITLE     Characterization of a bacterial gene encoding an
            autophosphorylating protein tyrosine kinase
  JOURNAL   Gene 204 (1-2), 259-265 (1997)
   PUBMED   9434192
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Stingele,F., Neeser,J.R. and Mollet,B.
  TITLE     Identification and characterization of the eps (Exopolysaccharide)
            gene cluster from Streptococcus thermophilus Sfi6
  JOURNAL   J Bacteriol 178 (6), 1680-1690 (1996)
   PUBMED   8626297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..537
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59652
     Region          87..>527
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 myrrsepegq glrhgrpsqr lrpaggslld fvpasaeeta ppeeartlek vgasvrvvdl
       61 papshnarap eepasaadff pqlhllgsig indiivwlrd girwiviall lsgaaafaya
      121 vtatprytvy tdlvvdpsnl nvvsddvftt npqrdaqlle vesklrilts rnvlqrvide
      181 lrlsedpefv kptlldwlka llaprdgktd kelaamrvls ervearreer sfvvvlkvws
      241 eepakaials daiveafeae lfqssaesag rvaqnlnarl delrrnvtea errvedfrrq
      301 nglqstngel vsnqlsseln tqvldgqqrf iqaetryrqm ssavaggrta sasvfelanm
      361 tdlrqqynal qqqigsmqlt ygerhprlva arseratlet amkdearril erakadfdre
      421 rkalatlrgk adneksnvft dnqaqvqlrd lerdarskaa iyethlaraq qiterqqidt
      481 tnvrvisral ppnarswppr tlvlliggaf lglalgiata lalglwrflr gktraaa
//
LOCUS       WP_457663554             365 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457663554
VERSION     WP_457663554.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..365
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40033
     Region          2..357
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mkiafhaplk spdhpvpsgd rqmarmliea lrlaghdvav vsqlrsflre ashsafsalr
       61 desqreidri rrlrrsegpp dvwfcyhpyy kapdligpsl stefsipyvt aessysyrrn
      121 igawklaqde vaagarraav nvcftqrdrh gldeaipgar tallapfidv spfrdlrrtk
      181 qgetrllava mmragdkmds frmlarslal vadlpwkltv igdgparaev letfaafpse
      241 rlewlgekap qavpallaag dlyiwpgcge ayglayleaq aaglpvvaqr tagvpevvrd
      301 getgclttpg niepfaaavr qllvdeasrk qmaerarqfv feqrslpaaa arlsgifaef
      361 vecak
//
LOCUS       WP_457663555             132 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter small permease [Sinorhizobium medicae].
ACCESSION   WP_457663555
VERSION     WP_457663555.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..132
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14684
     Region          <2..115
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mvsryvfpqp aawtyelamm afaylvffga vagvrlgtha aidvlvaalp dgwqkavawf
       61 nylllalffi vmtilfawqa wtsrhvhtia ldlsralsya plalasagml lqhliaerpw
      121 svrlhrnpes li
//
LOCUS       WP_457663556             256 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663556
VERSION     WP_457663556.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 256)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..256
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28020
     Region          4..253
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mgyltshfrv vgallvrema arfgskpggy vwalldpaah illmtvifha iarapalgts
       61 falffatgyi afqfyhaisg ylnaavkank allsypnvap idtivarfvl qmgttslvaf
      121 ivlgtivatm rvdtdihwps iieavglacl fglgvamvnc vlflkyplye qvfsivnrpl
      181 flisgvfflp nsipasyrdl vlinplvhii mgfrqgfypd ygaigldmdy lygiafltlf
      241 agmlvftlsr ktlrne
//
LOCUS       WP_457663559             477 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457663559
VERSION     WP_457663559.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 477)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..477
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51373
     Region          3..461
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 mriavggiht ecstyspvlm tvedfrvlrg edllnsdyfg flsaegidhl pllharavpg
       61 apvsrpayda lkseflerlk aalpldglyl amhgaikvdg mddaegdwis aaraivgasc
      121 plavsydlhg nvsqriidqi difaayrtap hidtretmmr swsmlvealr sgtrpgvawa
      181 rvplllpger tstedepaag lyrgladinr rpgildanlm vgyvwadepr atacavvtga
      241 dkeaatkave eiaasywfnr eefrfgsisg slaqmlgiae saktapvila dsgdnptggg
      301 vgdradvlia liergwrdal iagiadrpav dacfaagtgg ilkfrvggsl dtsspsaeie
      361 akvvrlddpg paterqavve aagieivlsa rrrpyhnied ftrlgldprg vrllivksgy
      421 lspelapian pslmaltdgv vnqeieklas lrrerpifpf drdfefrpsa rlsarwi
//
LOCUS       WP_457663562             644 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663562
VERSION     WP_457663562.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..644
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=73414
     Region          18..431
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mstdnamkis adhlrrdafl yvrqsslrqv fentestkrq yalrdraval gwpiervhvi
       61 dndlglsgaq sqdrdgfqrl vtevamghag ivlglevsrl arnnadwhrl lelaamsrtl
      121 imdedgvyda asfndrmllg lkgtmseael hilksrlqgg ilnkarrgel elplpiglvy
      181 tpdmrvvldp drqiqdtvrm lfdtfrevgs acavvrrlrs ekilfprrir rgigkgdvlw
      241 seidhsrviq ilhnpryaga faygrtrtiy naklksvqqk mprsdwqvli pqahegyisw
      301 defernlrpy yicneavvrr agkacqwarg paideavsal lleamaptai evalavqeei
      361 sqrveqaasl rdkqlqrary eaelarrryl kvdpdnrlva daleadwngk lrdldtlqre
      421 herqnetdqs lldgamqeri ralaadfpri wnnertspae rkrmlgllie dvtllvneki
      481 nmyirwrggr tqslavarpr pmavirktpe avvalinell etdndqqias rlnalghrnw
      541 rgeaftlkkv mlvrrayglk trferlresg mltgeevarr fgvsattvhq lgrdgvlkrh
      601 ryatnhryly eppgnvrlak gvggrygsrq prlidaqqiq qgas
//
LOCUS       WP_457663564             391 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663564
VERSION     WP_457663564.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..391
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42360
     Region          2..391
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mrperskssg siindpqvrg ifyqaitiii laaliywivd ntvdnlrran iasgydfvrs
       61 ragfdvgqsl isftsdstyg rallvgfint llvaitgiit atiigfivgi grlshnwiia
      121 klslayvevf rnippllvif fwysgvlsil pqardalalp fdiflsnrgv afprpiaeeg
      181 aeytllafvi avaasvffar yarkrqlatg erlpvlwtvl gliiglplvt flvtgapitf
      241 dipvagkfnl tggsvvgpef mslflalsfy taafiaeivr agirgvskgq teaahalgir
      301 palttrlvvv pqamriiipp ltsqylnltk nsslavaigy adlvavggti lnqtgqsiei
      361 vsiwlivyls lslatslfmn wynarmalve r
//
LOCUS       WP_457663565             384 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663565
VERSION     WP_457663565.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..384
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41667
     Region          172..383
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mstnqasfvr asmieaspap slesgavswl rknlfatpkd taltiislli lawlvppaiq
       61 wlfidaawsg ggrgvcatls qggsqpegws gacwafvnak faqflfgryp lderwrpalv
      121 gilfvlllvp mlipripykg lnallllval pilsaillpg gwfgltyvet plwgglmvtl
      181 vlsfvgiavs lplgillalg rrsnmpvikm lctvfievir gvplitvlfm asvmlplflp
      241 qgvtfdkflr aligvslfas aymaevvrgg lqaipkgqye gadslglsfw qkmgfivlpq
      301 alklvipgiv ntliglfkdt slvsiigmfd llgivrlnfs dtnwatavtp ltglifagfv
      361 fwlfcfgmsr ysgfmerlld rsqr
//
LOCUS       WP_457663572             275 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663572
VERSION     WP_457663572.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 275)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..275
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29875
     Region          9..275
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mglstpsaiv cqalllctsa iillpfvwmg slsikppgei frvsfallpe hfygienysq
       61 altaapltry mvngllvcsa iltlqvlvca pcayalaklq frgrdmlfgl vliglliphq
      121 vlalplfifg yqigilntya alilpfivsp fgiflfrqff kaipddvvha arldglsefa
      181 ivwriilpma lpaviafsif svvghwndlf wpliavrdqd lmppsigivt frdaesgsdy
      241 gplmaasviv iapllicfla aqryfieglt aggvk
//
LOCUS       WP_457663566             258 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663566
VERSION     WP_457663566.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..258
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29214
     Region          19..256
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mantatapkl avsttdvaie itnmnkwygd fhvlrdinlr vmrgerivva gpsgsgkstm
       61 ircinrleeh qkgkivvdgi eftndlkkid evrrevgmvf qhfnlfphlt ilenctlapi
      121 wvrkmpkkea eqvamhfler vkipeqakky pgqlsggqqq rvaiarslcm rpkillfdep
      181 tsaldpemvk evldtmvsla eegmtmicvt hemgfarqva nrvifmdqgq iveqnspaef
      241 fdnpqhertk lflsqilh
//
LOCUS       WP_457663577             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663577
VERSION     WP_457663577.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28164
     Region          2..253
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mtnllpvlan vactislplv lllawglssr fgwlpeqilp apevvwatia elwrdgslie
       61 htlvslrrva igfsigalsg llagaalgll pvvrsfvwpv ftavaqvntl awlpllvlfv
      121 gideelkyvc iawstavpvt lattrsiadv ssnlvelgrv fdftplqrvs aivlpaalps
      181 lftgvregla aawqslvive lfasfdglgy lmtwgrqlfq lelviaamlv iaaiglslna
      241 vleylehfvq pwkmearhdr
//
LOCUS       WP_457663573             228 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663573
VERSION     WP_457663573.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..228
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25202
     Region          8..>169
                     /region_name="Csa3"
                     /note="CRISPR-associated protein Csa3, CARF domain
                     [Defense mechanisms]; COG3415"
                     /db_xref="CDD:442641"
ORIGIN      
        1 mgsaislrtd fdgarlrlla rqakdanqar rllalasiyd ggsrsdaarl gsvtlqivrd
       61 wvvrfnargp dglingkapg kssllndtqr aalaqaierg ptpyldgvvr wrlcdlgqwl
      121 weefrvsvse qtlgrelrsm gyrklsarpr hhaqeadaae tfkknfpaav velgagdlrv
      181 sqvlqgsflp qpvlstasrs plhfllrnhl lgddgdrtlq irrridrq
//
LOCUS       WP_457663581             269 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663581
VERSION     WP_457663581.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..269
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30037
     Region          25..236
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mhpekirltg aretllitlq akaaesampd sllrdrfaad alhrldpdgr hlaighdmti
       61 gialraymld rwteaflqrc peatvlhlgc gldsrifrid pgpgvrwfel dvpdvislre
      121 wiypdragca tiacsiverg wierlpadrp tliiaegvlp yleddqvpqv lrriaghfps
      181 geiafdayss iairllrfnp airatgarlq wavddpaele rqvpglelie drsgwdvgqv
      241 armspaaqia lqlfstipyr mghllrygf
//
LOCUS       WP_457663591             389 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 aminoacylase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663591
VERSION     WP_457663591.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 10145370
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..389
                     /product="M20 aminoacylase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /calculated_mol_wt=41678
     Region          13..384
                     /region_name="M20_Acy1-like"
                     /note="M20 Peptidase aminoacylase 1 subfamily; cd05666"
                     /db_xref="CDD:349916"
     Site            order(105,107,140,166,361)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:349916"
     Site            order(189,211..212,216,219,222,239..245,249..250,252,
                     258..260)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:349916"
ORIGIN      
        1 mlntvdvrel hrevtewrry lhqhpeldyq lhntarfvce klasfginhi etgiaetgiv
       61 aliqggggdg dgptiglrad mdalpiieas nqpwsstipg kmhacghdgh tamllgaaky
      121 lastrnfkgt valifqpaee galgglrmvq egimdrfsis qvfgmhnepg ievgkfaicd
      181 gpilaaldef dlvvkgkggh aaaphetidp vviaaqiilg lqtlvsrstd plealvvsvt
      241 mlkgaeafni ipdqvemtgt vrtlvpslrd faesrilaca qgtargygad velryrrhdp
      301 vtfnsaaetk lavkaacrlv gtgsvdqkvk pqmgsedfay mlearpgafi llgngatasl
      361 hnpaydfnde allygigywv hlvesvlap
//
LOCUS       WP_457663593             367 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663593
VERSION     WP_457663593.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..367
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40849
     Region          36..308
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(43,178,244,268,270)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 msilinrrrf mqassaiavg alaspaikas aqpsgelrvl tyggqvgkfv idgyvkpfea
       61 etnikvipit qdfelaqlel mqrsnsitvd vgpmgdgaar qaaekgylek idyslfakdd
      121 leaflpnvkq dfglgfyfys lnlvyntkky pagkprpdnw adfwdvekfp gvrymvsgqy
      181 gsegpweeal ladgvspdki ypmdidrifs sldkikphvr kwwtsgseiq qimlsgsgdl
      241 mqsydgraay siaqgaqiem srkiakmtcd ywvipknspn aqsaqkfief vsraenqaaf
      301 akllpegpin knafkllsde vgrtlpshpt nmeqaflqsg awynevgsdg lsnmqrlsqr
      361 wsewvll
//
LOCUS       WP_457663597             378 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457663597
VERSION     WP_457663597.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..378
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=41770
     Region          195..371
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(229,323,326..327,358)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mltqraymcc iahfahwmtq egygleaigq aavirflseh lpacvcpdpv rrirhdlqaa
       61 lghllevlka ggvvpqypar nsaieqeltr fdihmrdvcg ladrtrrrrc kvveeflveh
      121 vgeqpismat vkattvrhfn lgeqgrgpaa iaaigvtisc ylrfrsisgd rvselktaip
      181 rvarwrlasl pevltdteid qllssfdqsf psrlrayamv rclidlglrs gevvklqlnd
      241 inwsngtinl vgtksrradt lplpvstgaa laaylreerp ttsnravfvr hvapydkpit
      301 tksvvravla gyrrcgwtrt gvhilrhsaa srllragapm keiadilrhr sldtsaiyak
      361 vdlnnlsava lpwpgsaq
//
LOCUS       WP_457663592             389 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457663592
VERSION     WP_457663592.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
REFERENCE   3  (residues 1 to 389)
  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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..389
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42034
     Region          20..389
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mampqgpqaf prseylrrla avkqemerrd vgalvvvlpa nityltgyta ksgyvpqgli
       61 valneeeptf itrrmdapaa vhqmfvdrgr vigyaeslia npdkdgwdai idhlmeagfg
      121 tgnigieeqt lssqtvkkfh ararpasvvg fgntvcwirg iksdleialm reaaaiadag
      181 mlrakevmrp gmseadaaae iiaqlvrgag gkqgtdvadf tlcasprtst ahitwaedef
      241 rngsqiniel agvrhgytsa lmrtfsigkp sdvlqrlheg evagleaala vvkpgatcge
      301 vatafndtlk kfgfekesrc gyaigidwte ptasfkigdp tilkpnmtfh lmlgnwided
      361 lgyaisetlr vtdvgaetfs tlpreiiqi
//
LOCUS       WP_457663599             602 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663599
VERSION     WP_457663599.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..602
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=66897
     Region          13..412
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mmhekigahh lerkailyvr qssahqvlhn ressalqyam rdrlaalgws hietvdddlg
       61 rsaaggvara gfdrmvaevc lgkvgavaar evsrfarnsr dwqqliemcr vvdtvlidqe
      121 avyaprqgnd rlllglkgsl neyeldllrq rslsaryeka rrgelvvtvp igflkagdri
      181 ekdpdrriqe aialvfdkva elgsarqall wfleqgldlp vryangdvtw rrpnyatihr
      241 mianpiygga yaygksrsvp gydgrsgirr kardewlali pdahegyvsw eraeeirkmv
      301 sdnvptsrhh gapkhgdall aglfrckrcg rkltvrytgs nhnipryscw rglldngepr
      361 ciafgglrvd daieeallgv vepgaiaaav eadrnmasqr dqvqdallrd leaaryaadr
      421 afrqydaadp enrlvtsele arwnkalarv geieakiakh wtvapqpipm sasqlvalag
      481 nlravwtaps tdarlkkriv rtlihevvad lddvaseivl vihwvggvht elrlpkrrrg
      541 qrnatpddiv eavrqlvlia nddviagvln rnglttghss targsmdlqp fktrvprsas
      601 dp
//
LOCUS       WP_457663602             153 aa            linear   BCT 27-JAN-2026
DEFINITION  Fic/DOC family protein, partial [Sinorhizobium medicae].
ACCESSION   WP_457663602
VERSION     WP_457663602.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Veyron,S., Oliva,G., Rolando,M., Buchrieser,C., Peyroche,G. and
            Cherfils,J.
  TITLE     A Ca2+-regulated deAMPylation switch in human and bacterial FIC
            proteins
  JOURNAL   Nat Commun 10 (1), 1142 (2019)
   PUBMED   30850593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Kinch,L.N., Yarbrough,M.L., Orth,K. and Grishin,N.V.
  TITLE     Fido, a novel AMPylation domain common to fic, doc, and AvrB
  JOURNAL   PLoS One 4 (6), e5818 (2009)
   PUBMED   19503829
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..>153
                     /product="Fic/DOC family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /GO_process="GO:0018117 - protein adenylylation [Evidence
                     IEA]"
     Region          8..>153
                     /region_name="FIDO"
                     /note="Fido, protein-threonine AMPylation domain [Signal
                     transduction mechanisms]; COG2184"
                     /db_xref="CDD:441787"
ORIGIN      
        1 madqhpkdsy typntsddpd rtnvlknrwr iethselrvk eyratavrmq eiaegdgpqg
       61 nfdkahlkai hgyifqdvye waghtrnesp vvegqrvepi gglskggtsf lpgsriemgl
      121 dealtpirdp qalrnatpee faeragkvls eln
//
LOCUS       WP_457663612             342 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Sinorhizobium medicae].
ACCESSION   WP_457663612
VERSION     WP_457663612.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..342
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37136
     Region          9..331
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mdapvntnll elyrtmrrir tfeervgelf vrgqsagsml hlsigeelsa agvcaamkpq
       61 dtftthhrgh giflargadp krmmaeiggk etgycrgkgg smhiadmalg hlganaivgg
      121 gipavigagl ssrhlkqdsv siaffgdgam qqgilyesmn maslwnlpvl fvcinnqygm
      181 gtridqatrn tafdqrakaf glngavvdgl dveevqaaar wlvdearagk pgflsvevyr
      241 ffgharmdks pyreeaeele grkkdpvlfa rnklidtgie eerildeldk aiaaemdati
      301 dfaveskapp lgsmfkdvya agepepesvr aridrvlard da
//
LOCUS       WP_457663613             502 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457663613
VERSION     WP_457663613.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..502
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=53581
     Region          3..492
                     /region_name="ASKHA_NBD_FGGY_L-RBK"
                     /note="nucleotide-binding domain (NBD) of ribulokinase
                     (RBK) and similar proteins; cd07781"
                     /db_xref="CDD:466799"
ORIGIN      
        1 mgyfltadgg teslrarlyd ltgnclgsaa vpyetrfsag araeqnpedw wrafveasrr
       61 tiseadvepa aieaitlatt sctvvaldre gkalrpaiiw mdvrtsdead avlatgdeal
      121 isngagrgpv saewmipkal wiarnepeif eeahticeyq dfmtlrltge raaslnnvtl
      181 rwhyqtdrgg wartlveklg lsalldkwpq rvvapgevvg tlspaaaqel glstrvklvq
      241 ggadaligmi glgvakpgql alitgsshlq fgvtesavha pgvwgtyrdc vypnryiveg
      301 gqtstgsiia wlgrlmngtm dldelnrkaa alepgcdgll vqdhfqgnrt pytdalsrga
      361 ivgltlahep hhifraimeg igfgtraild amaeagyrgs eitvgggaga selwlqihad
      421 taglpvcvpa srdapsvgaa vlaahgagyf asidegisam vrpgkriepr preaalydgi
      481 yqqyralypa lkslrdrgge pr
//
LOCUS       WP_457663604             161 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663604
VERSION     WP_457663604.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   2  (residues 1 to 161)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..161
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18018
     Region          36..102
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mslmstrglv eitdpefdrp vfrqpgfdgt ltakemdeki sawlkktrea kgisradlah
       61 llglsvsvyg ryergsearl siprlihlce imgfmpldvi fdaaphlwgn tveeaedrmt
      121 lmrlveqlpq dtmrdlirll rrmipgesaa davatsmseg r
//
LOCUS       WP_457663622             196 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663622
VERSION     WP_457663622.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..196
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20906
     Region          19..168
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 maavvdslra ffapttfvid setpgdvvar enlldramgp grrrkssekl rrgrvpaegl
       61 alvardtdgh vigtvrlwnv eagvnregqa vpalllgpla vdpahegkgi ggmlmraaiq
      121 eaknrghgav llvgdaayye qfgffahraq hlvmpgpfer nrflalelkd gwldgaagml
      181 vasgrklalp plrraa
//
LOCUS       WP_457663617             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663617
VERSION     WP_457663617.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38255
     Region          1..352
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mlemkniskv vggemhihpt dlvlergsln vllgptlsgk tslmrlmagl dkpasgsihl
       61 dnadvtgvpv qkrsvamvyq qfinypamtv yeniaspmri kgadaatidr evrkaaellk
      121 ltpyldrtpl nlsggqqqrt alaraivkna dlvlldepla nldyklreel reelpkifsa
      181 sgaifvyatt epsealllgg ntatmsegri tqfgrtidvy rqpvdivtar tfadpplnti
      241 dllksgshfa legkpvlpvp vhlgavadgp ctvafqphhl sfdppngsdq plavktaise
      301 itgsesfihv afagarwvml apgiheiepd atlkvfvdtr hlmafgpdgr avggra
//
LOCUS       WP_457663624             295 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Sinorhizobium medicae].
ACCESSION   WP_457663624
VERSION     WP_457663624.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 11419012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..295
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32024
     Region          71..291
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          78..106
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          112..140
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(113,116..117,120..121,123,147,150..151,154..155,
                     157..158,181,184..185,188..189,192)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          145..175
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          180..208
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          248..276
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtlaamtadv sglateeanr rrqrkpklaa ffvlgsallv agcqtdkpes mfrveraqgs
       61 egniaslssv iasnpgdpeg ynvrgsaygr agefrravad fdqaiqlnpr fyqayanral
      121 vqrnlgnqqa aladynaalq inpnydvayi grgnlyrqan qldaafndfn kaieldtadp
      181 rayhnrgliy qarnqhvqai edfskaisls psspepyngr gisyvaqgdd dnafsdfnta
      241 inlngklaes wanqalvyel rgdkakaaks yshalsldpk yeparaglar akams
//
LOCUS       WP_457663633             515 aa            linear   BCT 27-JAN-2026
DEFINITION  xylulokinase [Sinorhizobium medicae].
ACCESSION   WP_457663633
VERSION     WP_457663633.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..515
                     /product="xylulokinase"
                     /EC_number="2.7.1.17"
                     /GO_function="GO:0004856 - D-xylulokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005998 - xylulose catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0042732 - D-xylose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54623
     Region          5..487
                     /region_name="ASKHA_NBD_FGGY_CvXK-like"
                     /note="nucleotide-binding domain (NBD) of Chromobacterium
                     violaceum xylulose kinase (CvXK) and similar proteins;
                     cd07805"
                     /db_xref="CDD:466807"
ORIGIN      
        1 mgdtvaafdl gtggvkaaif rpdgvclaee vvsyrtfyps ssyheqrped wwdavcaslr
       61 tllgnpavla deiravaisg hslgclplde dgvllqesvp iwsdgravae sedfftrvdp
      121 dgwyrktgng fpaplytvfk amwlrrnapd ifvrtrtiig tkdyinlwlt griatdpsya
      181 sgtgvydlra gsyapdliea aglsaglfap ivastdiige ilpeiadslg lprrvkvvag
      241 gvdnscmalg grtflegday asmgssswit vsasqplldd rvrpfvfahv apgkfisats
      301 ifssgtsvnw vadtllpdvk qaarasgldv hdalfqlage apagarglmf vptlgggtsf
      361 eggpavrggf vgldlqhgra difratlegv alglrvalde lrrmtpigpe miivgggars
      421 pfwrqvfadv fdctivktgi dqqaaalgaa alafvgmglw qdflpirvlh vaegrnepap
      481 earavyraal aayriaaeqq relsgalvtl reaat
//
LOCUS       WP_457663636             322 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663636
VERSION     WP_457663636.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35501
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,224,241,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpwidrrrwr cfsplsrrgd fsaaarrlrm tpsavskivg rlesrlgvrl lqrstrsisl
       61 taegnsyses vrrilgdmee aelaiqpgae prgrlrvslp safghrlivp mlpafigrhp
      121 aieleldftd aivdlvngda hvavrvaaqg dstlvtrrla pnrrvicgap dyferhgvpm
      181 rpddllkhic lgissrggln lwefdeaggr rsmrirssie anstealrrl alagmgivrl
      241 semlvgqdir agrlkpvltd cnhaeaepis vvyphrrfls prvrvfvdfl aeqfaksiae
      301 ggdaarvirg tsgglpesda mr
//
LOCUS       WP_457663637             288 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457663637
VERSION     WP_457663637.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30129
     Region          1..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mssisilglg amgtalaqtl lknghtvtiw nrtgrraepl aeagakiaes paeaiaasel
       61 tilcvvdypa aravltqaeg vlagrdllnl tngtpgdare fgawlaakga tyldggimai
      121 ppmigeagal ilysgsptlf erhrktldal aesrhlgdev slaslydlal lsgmyglfsg
      181 flhasafvts aggkaadflp llqpwiqams gtlpdladkv dsdmhgrnvv sniamqkval
      241 enivrasaeq gvapdfiepm lrlaggridk gghdedisav ieeirqrk
//
LOCUS       WP_457663640             376 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663640
VERSION     WP_457663640.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..376
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41202
     Region          180..374
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 miarflkwsr hnlfgkpfdi llsltvipgf lwlayqvaaw tvttarweii peslrilmig
       61 ifpaeqawra wvaimiiaal lgaalgcvfa frkrhaagll lvlaavialt gskdltnall
      121 tastiaifas gcaaislipl lrrallpagf ialiaifavm sppgaglwgg lllsilltlv
      181 tsivslpvgi llafgrrsrf ssmrwicmgy ievmrsvpli mvvywiwilm pvlapqfgla
      241 dvvrgmigft lfysayvaey vrsglqavpr eqteaarslg msefdinrsi vlpqalrvav
      301 pplvgnvldi fntaplvfii gptdflragq milanpqygd rtyevyaflf ltyflvgsli
      361 tfvarrleth largnr
//
LOCUS       WP_457663642            1044 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Sinorhizobium medicae].
ACCESSION   WP_457663642
VERSION     WP_457663642.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1044
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110927
     Region          20..1023
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnigmgghhp gggqggktgf talfirrpif alvvntlivv aglaawngve irelpqvdqp
       61 vvsvttefdg aspetidrev tsvvegavsr vqgikdisst ssfgrsrvtl efsdttdigq
      121 aandvrdalg ritgqlpdda deprivkads dsqpimrlal tsdtmsmddm tllveneisd
      181 rlaavegvad vtvygdqeki fridvnqakl agrgvtvanl realanasyd vpagsltsan
      241 qdisvratad lqtpeqfenl mlgnnvrlrd vatvtlgpdt gtsalrsngr egiglgiirq
      301 aqsntvdisq gvrsvvnais sdilppgtel kvtsddavfi ngaiheveia lfvavfivtl
      361 viylflldwr atliptitmp ialigtvaai ylagfsinil tllaivlatg lvvddaivvl
      421 enivrrraeg lgpraaavhg tlevffavla ttatlaavfv plsflpgqtg glfrefgfvl
      481 afsillssfi sltlcpmlas rmltkerqeh qgvmqrfgqr asafyrvtlg aclnaplivf
      541 avaafftaag algfltlkse ltpnedrsqv mlrinapqgv sleytqaqir rieeglqpll
      601 ksgeisnvfs isgqggsans gfmvltlaqw eerdrtqsqi vadinrmtak ipslraftiq
      661 anslgirgag sglqvalvgn dytklgdaaa kllramedsg rfenvrlnye anqaqlsvti
      721 drertsdlgv digglswalq amldgssvvd ifvegeaypv kllsstepln dptdlqnifi
      781 kagdgrivpm ssiatieeka aapqlsresq lravslsagl ksdlalgeal smveemaepi
      841 lppgsrimpl aeaatldena nglfvtfgfa iviiflvlaa qfesfvsgli imstvplgla
      901 caifamiltg ntlniysqig lvmlvgimak ngilivefan qlrdrgqdvr saienaanir
      961 lrpvmmtmia tvvgavplvl asgagaeari algwvlvggl glavivtlyl tpvaylviag
     1021 ftkphadeer kleeemkaae vlki
//
LOCUS       WP_457663650             344 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457663650
VERSION     WP_457663650.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..344
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37773
     Region          87..331
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgdmprkpfl shektrhgri vwyfkrngkr irlpdeygsd efnaayekal tgastaaepp
       61 ksktgsfkwl vgqykrsaaf aalapatrra rdnilkqlla dpknadgqfg ditkahvkka
      121 idkraatpna annllktfsh lfkwaveaeh mevnpvigvs kvsvksdgfh twtvdqveky
      181 rahhpigtkp rlaidillfl glrrsdavvv grqhlkdgvi slrtgktgaw vylpvfkqll
      241 esieatptgd laflttstgk pfssgasfgn wfakqcqaag lpdecrahgl rkagatiaad
      301 egatahelma mygwtrlama evytkeadkk rlakgaserl anrm
//
LOCUS       WP_457663657             118 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Sinorhizobium medicae].
ACCESSION   WP_457663657
VERSION     WP_457663657.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..118
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13573
     Region          15..75
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mrsvpewvgk tddekvpprv rlrvfekygg icqlsnrkim agdawdldhi kalwrggehr
       61 esnlhpvlkq phreksaeeq seqakcdrir kkhlglwpqs kakiksrgfa strndhae
//
LOCUS       WP_457663634             385 aa            linear   BCT 27-JAN-2026
DEFINITION  pepsin-like aspartic protease [Sinorhizobium medicae].
ACCESSION   WP_457663634
VERSION     WP_457663634.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Dunn,B.M.
  TITLE     Structure and mechanism of the pepsin-like family of aspartic
            peptidases
  JOURNAL   Chem Rev 102 (12), 4431-4458 (2002)
   PUBMED   12475196
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of aspartic peptidases, and those of unknown catalytic
            mechanism
  JOURNAL   Methods Enzymol 248, 105-120 (1995)
   PUBMED   7674916
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Davies,D.R.
  TITLE     The structure and function of the aspartic proteinases
  JOURNAL   Annu Rev Biophys Biophys Chem 19, 189-215 (1990)
   PUBMED   2194475
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10144329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..385
                     /product="pepsin-like aspartic protease"
                     /EC_number="3.4.23.-"
                     /GO_function="GO:0004190 - aspartic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42217
     Region          50..305
                     /region_name="pepsin_like"
                     /note="Pepsin-like aspartic proteases, bilobal enzymes
                     that cleave bonds in peptides at acidic pH; cd05471"
                     /db_xref="CDD:133138"
     Site            order(70,114,161,260,262,264)
                     /site_type="active"
                     /note="inhibitor binding site [active]"
                     /db_xref="CDD:133138"
     Site            order(70..73,260..263)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:133138"
     Site            order(70,260)
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:133138"
     Site            order(110,112..114,119..122)
                     /site_type="active"
                     /note="Active site flap [active]"
                     /db_xref="CDD:133138"
ORIGIN      
        1 mkknelilsq revyrtkmrk ggvrstveae ntlvfelrrg aitnngatpw wvsatvgtst
       61 vpqtfkfmmd tgttntwvta kscstsectq hdsfdetass tfvwqdqslt pidfsgwgnm
      121 dvnlgndvwv lsdknaidqd vtvdfwlsqs ysgarfgeli qdgfiacgpy gdnsrsnlif
      181 dalwysgala spwmsywvdy tidgaavdsg emifggsnad kydpdtvisl divpgiwthm
      241 gdsivvdgae iftspallid tgaseikgeq aeidkliaav tldgqlplsp dnpdhyaypd
      301 lvfnlgktsd gstgqlvfpp rayfnyieag tdqgkwqiam tvledlgens lifgrnlldr
      361 lyseweydts gtsvagktir laqrv
//
LOCUS       WP_457663665             127 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663665
VERSION     WP_457663665.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..127
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14564
     Region          27..82
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(29,33,58)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mekhifawdn vimapikkpk qqlqrtflke wreyhnlsqe aaasrlnvsr tllskienak
       61 spytqqfmen aavaygcevp dlimrnpldr davwslqeql kkapperrnd iltvveamlr
      121 pktgtdg
//
LOCUS       WP_457663697             118 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663697
VERSION     WP_457663697.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..118
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12611
     Region          <25..115
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 maefvgqkig vtfsppltcl giekdgeivg gfvfnsyega dihvsaagrg atkgflaevg
       61 hyvydvlgce rmtvitekas vvrsaerlgg qveglmrnhf gkgrdaflvg ilkedwkf
//
LOCUS       WP_457663713             284 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663713
VERSION     WP_457663713.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..284
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=29916
     Region          185..231
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mhigkyfgls aafivggcat setmvlkpyr lengvvlqdv vtvggngkgt apvvtavktf
       61 elagnktrlv hsasgsegsm gsavaravas gvaagvpaav aqvianradg eritvsnsns
      121 sspvntntnt ptntnnptnt ntnnptntnt nnptntntnt smptntntnt ntndnapepd
      181 aneasdrrlk rdiarlaela nglgvyrfry lwsdevfvgv maqevlevmp eavvigsdgy
      241 mrvnykklgi emlsleqwts rlvagvpssr alrmdhrsla lasr
//
LOCUS       WP_457663714             330 aa            linear   BCT 27-JAN-2026
DEFINITION  RluA family pseudouridine synthase [Sinorhizobium medicae].
ACCESSION   WP_457663714
VERSION     WP_457663714.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..330
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=36964
     Region          97..317
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 magiehrqvd sdeagmrldr wfkvhfpglg fgplqkllrs gqirvdgara ksdtriqpgq
       61 tiripplgvd pkekktgpig grdlrqspdg ellsrmvlhe dakvivlnkp pglavqggsg
      121 vnrhidkmle awtsqkgekp rlvhrldrdt sgvlviartr gaaqqltaaf rerdtkktyw
      181 alvrgvprkr edkistwvvk eqtpdgdrvr iakhgedgad yaisfyrive qagqnlawle
      241 mepytgrthq lrvhaahigh piigdpkyfe advnwtfpgg mqnrlhlhar hidiphpngg
      301 rlkvtaplpq hmmqswnllg feenaadeee
//
LOCUS       WP_457663715             291 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663715
VERSION     WP_457663715.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..291
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31392
     Region          35..276
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mskdktgdks ardthyanlr rahrdgrrer geiptprqdk rgkpsadwkp palapdqvll
       61 yglhtvraal dnperriirl svtqnaaarl dlgdsaalpf pvetvtpqel drilgpdaih
      121 qgvmletrpl phrklealrd cplilvldqv tdphnvgaim rsavafdaga littmrhspt
      181 elgvlaksas galelipyiq isnladtide lhalgfmtig ldsegpqple gtfagdkial
      241 vlgsegkglr qktrqtvkal arldmpgaik slnvsnaaai amyaarhhlk g
//
LOCUS       WP_457663721            1153 aa            linear   BCT 27-JAN-2026
DEFINITION  chromosome segregation SMC family protein [Sinorhizobium medicae].
ACCESSION   WP_457663721
VERSION     WP_457663721.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1153)
  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 1153)
  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 1153)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1153
                     /product="chromosome segregation SMC family protein"
                     /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=127539
     Region          1..1152
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mkftklrllg fksfveptef iiergltgvv gpngcgksnl vealrwvmge nsyknmrasg
       61 mddvifsgsg nrparntaev glyldnsdrt apaafndsde iqvtrriere qgsvyringk
      121 earakdvqll fadastgars psmvgqgrig eliaakpqar rqlleeaagi sglhsrrhea
      181 elrlkaaetn lerlddvtsq lesqieslkr qsrqanrfkm lsaeirrhea ilfhirwiqa
      241 keaeaeatsq lnqvtalvae taqsqmeaak aqaitslklp elrqneakla aalqrlqiar
      301 aqleedagri lrrreelqrr laqlsediar eerlvadnag ilarldqeee elrdalaead
      361 drslearerl eeaneklaas egalarvtae raeaqaarnq ieralrdlse rqarlarqla
      421 dqarelddld grmaslpdpd ekreqvehae asmeeaeaav saveeslaea raaetatrpp
      481 vdqararlng ieteartirr mleaagastf pavveslkve rgfeaalgaa lgddldssle
      541 qaapahwrmp gddaddpalp sgvlplidfv qgpdalrrtl rqiglvqsed eaeqllpflr
      601 agqrlvtrqg avwrwdghva gseapsaaal rlaqknrlfe legeaeaasg alskaeadla
      661 aagarirged erlrlsreaq rmrarqlaea rdalaiaera sgdlarrrav laetklqieg
      721 qaeeiaeqie vaneafadqp dpaeldrhls drtaevatdr aaaaearaah dglarenner
      781 hrrlmaiage retwgaraas aenhiatlre reaeaqeeve elleapdafd ekrralmnel
      841 qkaeasrrea adnlaeaesr qresdrqaat alselaeare krgraeerlv sarerrleie
      901 arilealsca phevmrltgl aanealpdmr svereverlk iererlgavn lradeeqkel
      961 serlaallke rddvieairr lrsaiqnlnr egrerliaaf dvvnvqfqrl fthlfgggta
     1021 elqliesddp leagleilar ppgkkpqtmt llsggeqalt amalifavfl tnpapicvld
     1081 evdaplddhn verycnlmde malstetrfv iithnpitma rmnrlfgvtm aeqgvsqlvs
     1141 vdlqtaermr eav
//
LOCUS       WP_457663728             561 aa            linear   BCT 27-JAN-2026
DEFINITION  heparinase II/III family protein [Sinorhizobium medicae].
ACCESSION   WP_457663728
VERSION     WP_457663728.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..561
                     /product="heparinase II/III family protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=62122
     Region          8..561
                     /region_name="COG5360"
                     /note="Uncharacterized conserved protein, heparinase
                     superfamily [General function prediction only]"
                     /db_xref="CDD:444135"
ORIGIN      
        1 mplsnkprfl ylylregtrr lerrlslgrt aaqryagstp vrlivaptdl raidpfvaee
       61 ilagrfplag rvldtegesa feidlpsyef airlhsfgwl rhmravqdea gsarlrqivd
      121 dwmgshgrti geiswdadvv aqrviawlsh spvvlrnaeh gfyrqflksl alqvrhlrhv
      181 agtvpdgear lrvrlalama svsmpatasa irrasrnldl elerqilpdg ahfsrnprag
      241 lellldllpl rqtyvnlghd vpskliscid rmypalrffr hqsgelalfn satsvaahel
      301 asvlrydeta gepfrslpha qyerlslget vvivdtgrpl svdlsrsaha gclsfemssg
      361 rnrfvinsga pkfagdrfrq marttaahst vtlndrsscr fsqsrflgpi vaggpsrvav
      421 erkdepgrme tvkashdgyv apfgllherd igilnggrli rgrdrllled ggdpdpedgs
      481 iaiarfhihp aigmrrhses eiyltapdge awlfacrdgk laveediffa dpsgvrassq
      541 itvtfaagdq peiqwtftra a
//
LOCUS       WP_457663729             704 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family metallopeptidase [Sinorhizobium medicae].
ACCESSION   WP_457663729
VERSION     WP_457663729.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..704
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=77756
     Region          8..684
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mndiaslnpa lvnwtghegl prfeavrded fgpafdaala aheaeidaia rnaeppsfgn
       61 tvvaleiagd elsrvsalfw skagahtnet iqalereiap kmsrhyskig tnpalfsrid
      121 alwerredlg ldveamrvle rhwksfvksg akldkadqdr laaineklas lgarfgqnvl
      181 adekawalll sseeelagip dflrdamaaa arergeedky avtlsrsiie pfltfseire
      241 lreqafrawa argenggetd nrgiigetls lraekaellg yenyaalkld ntmaktpdav
      301 ngllmqvwek avarareeea dlarliaeeg rnhevmpwdw rhyaeklraq rfsfseselk
      361 pylqlekiid acfaigkrlf gltavekkgi payhpdvrvy eirdasgklt alflgdyfar
      421 pskrsgawms sfqsqhrlal kngetgeipi vynvcnfakp aegkpallsi ddartlfhef
      481 ghalhgmlsn vtypsvsgtg vardfvelps qlyehwltvp evlrtyavhy rtgepmpqal
      541 ldkvlaartf nsgfatveft asalvdmayh ttegvgdpma lekatldkig lpksivmrhr
      601 sphflhvfsg dgysagyysy mwsevldada faafeetgdp fdpataarlk dniysvggsv
      661 dpedaykafr gklpspeaml gkrgacgleg tratpvrpey tagv
//
LOCUS       WP_457663698             324 aa            linear   BCT 27-JAN-2026
DEFINITION  tail fiber domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663698
VERSION     WP_457663698.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schwarzer,D., Stummeyer,K., Gerardy-Schahn,R. and Muhlenhoff,M.
  TITLE     Characterization of a novel intramolecular chaperone domain
            conserved in endosialidases and other bacteriophage tail spike and
            fiber proteins
  JOURNAL   J Biol Chem 282 (5), 2821-2831 (2007)
   PUBMED   17158460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10620719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..324
                     /product="tail fiber domain-containing protein"
                     /GO_component="GO:0098024 - virus tail, fiber [Evidence
                     IEA]"
                     /GO_process="GO:0019062 - virion attachment to host cell
                     [Evidence IEA]"
                     /GO_process="GO:0046718 - symbiont entry into host cell
                     [Evidence IEA]"
                     /calculated_mol_wt=34694
     Region          259..303
                     /region_name="Peptidase_S74"
                     /note="Chaperone of endosialidase; pfam13884"
                     /db_xref="CDD:404724"
ORIGIN      
        1 mvstpkapdp qataqaqagm nrdtaitqsq lnmvnqqgpy gsltynqtgt skfkdsngnw
       61 ietptytatt slspeqqail dqtqkanlnl gtianersaf lkdylaqpfd vnasteakin
      121 elgssrldpr fareqealrt qlinsgirpg saaysaamnd fgqtkndayn qlaltgrqqa
      181 fqeasyeraq plneisalls gaqvtqpqfv stpqsnvagv dytglvnnqy nqqvassnaa
      241 mgglfgllgt gltagikysd rrlkssitrv gmldnglpvy lyeingtiel gvmadeveav
      301 ipnavhiaen gfkmvdynaa traa
//
LOCUS       WP_457663730             269 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663730
VERSION     WP_457663730.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29269
     Region          46..237
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mpsisdrapf gfpgrsgaer lvfwrccccg rypsgssifr pisilpprdv laafgelirn
       61 gilieylads swryavsvgt glslgiifgl liglsgfwsr llgsiirffy aivevawipl
      121 lviwigygfp tiliaisyvv ffpvlyntlt gvqtiqpvli navrtlgasr fqvltsvilp
      181 aalpnimtgl rvgagfafrg lifaemiaag sglgflifdg astrqtdrvv vgmimmgllw
      241 llmdrlllrp ieratierwg lvraqgges
//
LOCUS       WP_457663731             253 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663731
VERSION     WP_457663731.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..253
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27438
     Region          1..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mielshivkr fgtntvlndi svslaegsvt alvgpsgggk stllrcvnll eiptagairl
       61 gddrlefaeg rkvgwqaiqr lrrqtgmvfq nfqlfphqta ignvmeglvt vlkwppdrar
      121 tralellekv gmahkadawp atlsggqqqr vaiaralaps prvllcdept saldpelaee
      181 vvevlsrlar dgttmimath dlrlasrvad hvvfldggvv vesgpprkif stpererter
      241 fiaslsapms ydi
//
LOCUS       WP_457663733             316 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar-binding transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663733
VERSION     WP_457663733.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..316
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34303
     Region          12..314
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mgrlnelrli arvaqmyhie skrqaeiaei mhmsqatvsr mlkraeqedi vrttvippag
       61 tfadletalr eryglteaiv idcsedrdga imarigeaaa hflevtlqqd eivgvsswsq
      121 tilrmvdnih plknakakyi vqilggmgda svqthatqlt arlarltgge prlllvqgit
      181 ssreaklvml adpvvretmd lfgrlslaii gigavepsel larsgntfsr qemamlheag
      241 avgeisyrfy dkggkpvetp lndrvigisl edlrktgrvm alaggesktq aitgalrlgv
      301 idvlvtdkft aarlta
//
LOCUS       WP_457663732             226 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663732
VERSION     WP_457663732.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24500
     Region          5..218
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mphwlqlmtd slpallwagl iftipltlls ftlglalglv tavvrlfapa pfavvarfyv
       61 wvirgtpllv qlfvifyglp smgilldafp aaligftlni gaysseiira vissvprgqw
      121 eaaysiglsw sqamrrtilp qagrvavppl sntfislvkd tslaaaitvp elfqtaqriv
      181 atsyeplily ieaaliylvm ssvlsalqgk leqrfarygg fleara
//
LOCUS       WP_457663735             367 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457663735
VERSION     WP_457663735.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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 367)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..367
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41431
     Region          3..361
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mkkldkitiq gfrsireqtv llgdinvlig gngsgksnfi eafrmlreis egrlkqyvlt
       61 sgeadriahf gvkvtnkvrf kayfndsvdq yeisltptel gslvpseeya yywnkglypq
      121 pyqktlpslg aeaaishskv dgvsayvkaa lsswriyhfh dtsrsspmka isdiddnrfl
      181 rpdgsnlasf lyvlkqrfen eyemirgtiq riapffedfv leprsldntk irlewkhvns
      241 dsyfdvssfs dgtlrfials vlllqprmyk psiilvdepe lglhpaaitl lgalirqasa
      301 htqvilstqs pflldhfdie dvvvaetsdg asvfrrldkd klskwldeys lgelweknel
      361 ggrpgsi
//
LOCUS       WP_457663737              88 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457663737
VERSION     WP_457663737.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9809
     Region          15..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mlvlelalpl sslrsdlylr miellvqark dagitqvelg rrigqrqtfv skfelgerrl
       61 daaefitvcr algadphali kmaeknpf
//
LOCUS       WP_457663742             418 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Sinorhizobium medicae].
ACCESSION   WP_457663742
VERSION     WP_457663742.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..418
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46992
     Region          75..394
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkefnvsits atrrrklkdg tiaeypqyyc eyrepltqkr rrrafdrkkd aeafrnslll
       61 kvaennyvde rkvptvgkav dhwlsdkesk vkastlkgyk vvangairgp lligtkqera
      121 dytesgvapk sarfiklldd vkltdlttam irvwhktvve qcgnytanra kshlksvlal
      181 aeedfsirap smptglarar hkqkkailts ediarliava kmdaehgiyy afpfltgtrp
      241 seqlgllwse vdfdknviri rriqerdgsl temtktaagt reipmgatlr emllewrlrc
      301 prkgkelhrv fpgpgrlqew pklriggggp llyqnfrkry wqpafkklrl syvtphsarh
      361 sfistlqaqg ievglvaqia ghanptvtlg hytqavrgga aaldaleray tsvsnats
//
LOCUS       WP_457663756             275 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Sinorhizobium medicae].
ACCESSION   WP_457663756
VERSION     WP_457663756.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..275
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=30380
     Region          80..206
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgctlilanl ciiissitle irlpyylptw gvvqkhaitg kelsvfnpte lkklrgrids
       61 lserpiripv fphlnpsngl visiydrrly atiegksdsf pisiglpshp tpvgvypivr
      121 kasdpvwypp psailhndkl phsippgpdn pmgaaalyls lpryaihgtn deysigdvnt
      181 lgcirlrnsd atyllknvpl gelvhitddl vlswthdeqh fariatfasf eealgtpvtv
      241 fgetfklgei qevmhlsele mrsalfvfkr pvpkg
//
LOCUS       WP_457663768             461 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663768
VERSION     WP_457663768.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Solano,F.
  TITLE     On the Metal Cofactor in the Tyrosinase Family
  JOURNAL   Int J Mol Sci 19 (2) (2018)
   PUBMED   29473882
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Xu,Y., Bartido,S., Setaluri,V., Qin,J., Yang,G. and Houghton,A.N.
  TITLE     Diverse roles of conserved asparagine-linked glycan sites on
            tyrosinase family glycoproteins
  JOURNAL   Exp Cell Res 267 (1), 115-125 (2001)
   PUBMED   11412044
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447028
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..461
                     /product="tyrosinase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49505
     Region          96..247
                     /region_name="Tyrosinase"
                     /note="Common central domain of tyrosinase; pfam00264"
                     /db_xref="CDD:425566"
ORIGIN      
        1 mgvvaamsla pvpartagqr vrfgattpdg krmleayakg vagmkalsga dpkswtfqwy
       61 thwvrgdsdk lielanffgd tnnpakdlan lmwsscqphg sgmnpynflp whracllyfe
      121 eivrrvsgvd eftlpywdyt vdgvlpeefr kpgdpvwgvl yvderrgsvn sgasittaav
      181 nlnalrnpsy ydsairqgfn nqvdggvhga vhvnvgttqn mgsvdfagrd pifwlhhcni
      241 driwaawnka granptdsgw tdikhvfadk dgnriettng dvsslsnvgy sydtlppaps
      301 aqaaelivla qaveplarna etvslaqdva taslaplspa stamlgalgn arlllvidgi
      361 tasaqpgtvf dvygkvgnna pdkgvylgsv nffdavplgq qgarpkrlvf dvtdalrqan
      421 valtqidvft yyfvpvdpva agsdpviqrv elvretapsg g
//
LOCUS       WP_457663763             525 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Sinorhizobium medicae].
ACCESSION   WP_457663763
VERSION     WP_457663763.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 525)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 525)
  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 525)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..525
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55812
     Region          148..463
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 magkwlslvd daaapwlprs vlapaivrhd frrlrtvaav sltalpiipl altlalpvsa
       61 alpagaalwa sasllaaaaa isggraepiv aevevapapg lpdldtaydl faglvtvhdi
      121 rghvrsvhgr dareylklmr dpqgrgfieq ihvsdriafl raidslrlds ertavdirle
      181 rtsadgpqfa hfycemtplr daegnllaiv aqssdvsega rlqaeaaara ahaesandak
      241 trflaavshe lrtplnailg fsdvlageyf gklendrqre yvslihqsgt hllsvvntml
      301 dmskieagry ellrepfrva eaiaaceaml shqarekgvr lasrvtrsvg einadqravq
      361 qilinlvgna ikftdrgglv tvdaaregal lkltvsdtgi giaadklkml gqpfvqiqnd
      421 ytrryegtgl glslvkglae lhggdvsirs aegegtevvv sipcdvssia gaecarvpvt
      481 vefpprltlr gdgksdvgep avvealrkge mgregghgta qakta
//
LOCUS       WP_457663770             139 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system VapC family toxin [Sinorhizobium
            medicae].
ACCESSION   WP_457663770
VERSION     WP_457663770.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Clissold,P.M. and Ponting,C.P.
  TITLE     PIN domains in nonsense-mediated mRNA decay and RNAi
  JOURNAL   Curr Biol 10 (24), R888-R890 (2000)
   PUBMED   11137022
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..139
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=14638
     Region          5..131
                     /region_name="PIN_Pae0151-like"
                     /note="VapC-like PIN domain of the Pyrobaculum aerophilum
                     Pae0151 and Pae2754 proteins and homologs; cd09873"
                     /db_xref="CDD:350221"
     Site            order(9,38..40,42..47,49..51,67..68,70..71,84,87..88,
                     90..91,95..99,101,116..119,123)
                     /site_type="other"
                     /note="homotetrameric interface [polypeptide binding]"
                     /db_xref="CDD:350221"
ORIGIN      
        1 msvfvldast aaawllpeeh seiaeqliag isgqcpvpgl fwhearsilv taerrqriaa
       61 gqaltamtrl rrlpledaga gqdgsviela tvqglsayda aylelaiars lplatldrkl
      121 aaaaraekvp vlgpfgneh
//
LOCUS       WP_457663782             536 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663782
VERSION     WP_457663782.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Solano,F.
  TITLE     On the Metal Cofactor in the Tyrosinase Family
  JOURNAL   Int J Mol Sci 19 (2) (2018)
   PUBMED   29473882
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Xu,Y., Bartido,S., Setaluri,V., Qin,J., Yang,G. and Houghton,A.N.
  TITLE     Diverse roles of conserved asparagine-linked glycan sites on
            tyrosinase family glycoproteins
  JOURNAL   Exp Cell Res 267 (1), 115-125 (2001)
   PUBMED   11412044
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447028
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..536
                     /product="tyrosinase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58387
     Region          70..311
                     /region_name="Tyrosinase"
                     /note="Common central domain of tyrosinase; pfam00264"
                     /db_xref="CDD:425566"
ORIGIN      
        1 mtrtrfltvs rrsfvkgata aagtalfaps ilraatkhrr knmtsadgqk dlqsymdavt
       61 amlklppsdr rnwyrngfih lmdcphgdww ftswhrgylg yfeetcrels gnpdfalpyw
      121 dwtanpevlp plfgtildpv nssayipdhn rfqdimqepi kacwdslssa qlqqqnlrgy
      181 pdfdalwsda masfanqpna rfltaqnpkl npatqtavdi dtikaslapt tfandagapg
      241 lafnspvsss hqvapvgfsi legqphnrvh msvggqsapy glmsqnlspl dpifflhhcn
      301 idrlwdvwtr kqqamglpvg ptadqqtqyd pepylfyvna dgspvsdktr aadylaigaf
      361 dydyepgsgd evipvatagr sapipaleaa vpasaavain kpatakltvs qelvdvaakp
      421 seqsrqfakv siappmdvgg lnflvfispe gttpdlnpdg pdfagsfeff gvrhhhtdtv
      481 sftipidkal drliedgrlk agepidfavv vaqagkrieg smpakaqltd iqvgsf
//
LOCUS       WP_457663784             247 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663784
VERSION     WP_457663784.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 247)
  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 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..247
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=27828
     Region          17..186
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 msmagdldpw qvsselrvdi flsqpreasv rlwnaarnvl neeerqrarr fvfdrdrdmy
       61 vfshgllrll larymvadpr eltfasapgg rpelvspssa pirfnlshtd glvgciltqe
      121 adcgldveqi grvdyrhlmp tvlapeersa llglaeadrp drfceiwtlk eaylkgrglg
      181 isypirnisf sgfdgdrrcr vvgderddgs twhfwsrpfa gaysaaaavr tqrddvkfsa
      241 tfiedlp
//
LOCUS       WP_457663794             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663794
VERSION     WP_457663794.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21848
     Region          13..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnigstsprp vgrprefdmn qaldaairif sekgyhgtsi aelkaemglt agsiykafrd
       61 krdvfvaayd rykqiradll dqalssastg rekiarvvqf yamsacgetg rrgclaigaa
      121 velvlsdtvi adkvgghnrk laarlegfvr dgqldgsirq dvdpaptala lfsylqgvri
      181 agktgelenq mlpsaeallr ild
//
LOCUS       WP_457663797             114 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663797
VERSION     WP_457663797.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..114
                     /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=12784
     Region          6..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpsvserpvk rsirrnelre ivpladstiy emeqrgefpr rfglsprcvv wdlaeveacl
       61 esrrtrsipr akhpdvtqrk frpvkgqgra qalgmvgggg gsrvtgdlmr vklr
//
LOCUS       WP_457663795             324 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663795
VERSION     WP_457663795.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35172
     Region          2..184
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          216..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplsdvlsl lkprshissg fdaggdwliq fsdlherikc yavvsggcwl svegvadpvr
       61 leagdcfvlp sgrpfrlgsd mglspvdagt ifpparaggv vrvngggdff lvgsrftvsg
      121 hcahavlrtl ppivhikkes eqaalrwave rmmlelrepq pggflvaqhl ahmmllqslr
      181 lhladgvgnq vgwfsaladr qicaaitamh aepayrwtlq elaeraamsr safamkfkat
      241 vgetpmdylt rwrmtlaadk lensgdpvsa iafslgyese ssfsaafkrv mgcsprqysr
      301 nqirlplalr aeakpgrqta mvsn
//
LOCUS       WP_457663808             401 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein, partial [Sinorhizobium
            medicae].
ACCESSION   WP_457663808
VERSION     WP_457663808.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..>401
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
     Region          35..397
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mvssaavdlr qseapgvsvg ghqavvcfpf igdlvggshm sslglirnlp rdrfvplvvl
       61 hhtdgpvael frregigfve apvlnrlera aprngaavvn vvrtvpglvk flrarnasiv
      121 htndgrthli wglaariags khlwhhrgda tsfglrhvap wlpnrlvavs kfasprpgff
      181 saagkcsvvh spfdvmkmdg fdrvearnnv laaigcspdt kllgyvgtlv arkrpiifve
      241 aiaalkrlsp etkvaglffg dalngldeta rsraealgva dcihfmgfry pgeawiagld
      301 allvtavnep lgrtlveaml lrtpviaads ggnpevvedg rtgmlvpadd pdefakacla
      361 lfnnsglrdh lvetargevr srfsferhvh aitsvyekli g
//
LOCUS       WP_457663809             393 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457663809
VERSION     WP_457663809.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..393
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41440
     Region          <22..393
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 mfklenpnst laatgedsit qgayayalrk ggggdwylqs ellagpvdpv dpvptfnqga
       61 gvyetyaqdl laftrlpslr qragnrswam paapvcfadg qgrenagnap acieegglwa
      121 rsegetadiv pqvssagvsg ydrdigriea gidgllhesg qgkliggvsa hygsggssva
      181 sfhgggeids raygmggtlt wygqngfyad vqgrlnwfss dlasallgnl asgndgfgyg
      241 lsleagqrfa igdnwaltpq aqlsyasvdf dgftdpfaar vsledgdslr ariglsidye
      301 niwqgqqgdt rrmqvygian vihdmsgrtr armsdvtlds rpdswtgevg lggsynwgdd
      361 kyalygelra atgltdfgds halggtvglr vkf
//
LOCUS       WP_457663815             440 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Sinorhizobium medicae].
ACCESSION   WP_457663815
VERSION     WP_457663815.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..440
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47417
     Region          <81..116
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 myrllavlfc wlstqgpals adplaraalq sqgtlyagqq ilvdvdvlvp nyflqspqfp
       61 aidipgaivt lddgralnln etidgtpysg irrtyiivpq aagdftlppv pitfgyaavp
      121 pqatrgevtl pplrftvrsa pgtagdspgi vaakvsvsqe ldqdpaqlka gdtlvrtvtv
      181 raeglrammi peadftapqg vrlyrqdpsl seetdrngqs iaglrkdvas ylfqdagnya
      241 lpavtvswfd pasaktqsat apavsvtvsa aaalppalap papkpqrdaf dwlhlaligg
      301 ivlltasllw vaanglsrle awwqerrsre rqsepaffrq veqacksgrd daiaraldaw
      361 srkagample twlgrfadve tkqvyqawqr tryasqetsq pfraglllpg lkkareawlt
      421 qgqeapgrkp allplnptmp
//
LOCUS       WP_457663812             597 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663812
VERSION     WP_457663812.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 597)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 597)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 597)
  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 597)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..597
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64292
     Region          1..572
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mrrfllpgle vlrgalgrqm rllpavvilg ltsaalegag igliipmlsi iagdeqatgl
       61 sgisayfqgm geglddgerl laisvavlal illknvlsfa ntllttfiyg kashsvrsal
      121 sdqllrigyp ffmqhnpgrl lniisneswr asdaiqtvla aivhgsaali llaflllmsw
      181 qmtlfvalgl vlvqlahaal satlkgpsrh vtsfnselsa rmlhlvhagr lirvfgqepr
      241 ekqafnsasd avrragfvlq srqgalpplt evlhsalfla vvvsawsvgv sfpvivafvv
      301 llyrlqphvr alqmswsqiq gwsgsleevr wlldssgkpk ppegktpvdg lheilvfdrv
      361 tfrypgsevr pvvlrsasfe irsgrstaii grsgagktti vnllcrfvep degcilvdgv
      421 plseidpiqw rrqiavasqd lelvdgsile nitygqsatf veaeraakla eahgfieqlp
      481 qgyqtvvgyr gaslsagqrq rialaralvr dpailildea tnavdglsea aivetlrlra
      541 grrttivish hrstisfcdd vvvlgsghvk gqaaladvas lsmdqlyehe tradsat
//
LOCUS       WP_457663816             338 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663816
VERSION     WP_457663816.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 338)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..338
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35262
     Region          26..329
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mrtvaqpaaa valalacgaa llafngydar avidvmvlgv fqdtrsiaei llkatplili
       61 gvglcvafrc siwnigaegq fyagaaaata igvsfnglga wlyvplvmla galagaawaa
      121 iagllkiyfr aseivttiml nyialimtsy lvtgplrdaa aaypqsarlv qeawmprilp
      181 ptrlhigilv alvlavvmyv flfrsargya lrvvgispda aryagisvpr nimisislsg
      241 smaglagafe iagvtrrlfq sispgygfeg iavallannn pigaifsgll favlrsgsel
      301 mqitaqipqv lvlviqgivi lsvvgfavlr ipslrpse
//
LOCUS       WP_457663818             360 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457663818
VERSION     WP_457663818.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133532
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..360
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38701
     Region          1..359
                     /region_name="GT4_WbnK-like"
                     /note="Shigella dysenteriae WbnK and similar proteins;
                     cd03807"
                     /db_xref="CDD:340836"
     Site            order(14,190..192,255,277)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340836"
ORIGIN      
        1 mimhvitnft asagaetmla rllhgsmder iivvsligvs drnrrladnp rvsyvslaaa
       61 sltalpgail llatlirker pdvilcwmyh amvagslaag larhgapvfw nvrqslddpa
      121 sltrssriai aaakllsrrp tgiiynsara ldlhraygya nqntvvipng felpelaape
      181 praarrigiv grfhpqkdhg tffkaaaqvl kthpqavfsa agnglvcdnp qvmeliakad
      241 lpahavdlrg evsdmpafyr sidllvlssr tegfpnviae amsygkpivt tdvgdaavva
      301 gragiavppr npqalaeamr afldlpeaey aryartarer ieneyalaav sakysnflma
//
LOCUS       WP_457663819             332 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663819
VERSION     WP_457663819.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..332
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35273
     Region          2..319
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mltggtwcad ynrtvshwpg edglaelfee erhgggsgcn laldikhldp aipvetiglv
       61 gddddgrylr ataaaagidt sqmmvtaaaa tqfcdayvsl sshrrthifh agsgalltpd
      121 hfdfsstrmr ylhlglpgvh rildapwhde angwvvvlkk araagletnl elasvdralm
      181 arlvapclph ldflivndle igaiagveti vrdapdqaac mraaravler galklvavhc
      241 pafaiavtrw gegvvlpsva ipeqeikgan gagdafaagm lygihegwsv gqslrlahat
      301 aaaslrsist tgavlpwrdc laladkwdsr dy
//
LOCUS       WP_457663825             300 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Sinorhizobium medicae].
ACCESSION   WP_457663825
VERSION     WP_457663825.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 300)
  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 300)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..300
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=32211
     Region          10..299
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mftrrgfvkl lgggfsgama lggyafgvep larlsvaryl ltpprwpsgl klrivaladi
       61 hacepwmstr ritsiceran alggdvtvll gdyaagmnlv tryvhsnews kalatlkapl
      121 gvhaimgnhd wwedrtaqkn gggetfghra laeagievys nravriekdg sgfwlagled
      181 qlallpgrkw krasmggldd ldgtlaqvtd eapvillahe pdifpkvppr valtlsghth
      241 ggqvrfaghs pvvpsrfgdr yayghiveyd rnlivsgglg csiapirfgv ppeivvvdig
//
LOCUS       WP_457663828             232 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457663828
VERSION     WP_457663828.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..232
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26425
     Region          16..192
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrdlahwkgc papepvrmeg ryvllepydr aghlsalwnd afggmainpl lkyfsqddfs
       61 giedfdtwls tvqrksgwvt evfrdkatgk vvgmanymra daangvvevg gvahgsamar
      121 splstevhyl makhvfedlg yrryewkchs enqasrttaa rlgftfegif rqhivskggn
      181 rdtawfsiid rewplirsaf erwlspenfd hggrqkrrle eiraelaqee pr
//
LOCUS       WP_457663829             286 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663829
VERSION     WP_457663829.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..286
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31502
     Region          20..284
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrgrlpvlil flppalllft vfvilpmgea awyslyrwng ygtptqfvgl rnfevlfnna
       61 afsralinng iiifvsvllq iplalwlamm laqriagvva frlifflpyv ladvaagliw
      121 rfvydgdygl vaavagffgv atpyvladrs laiyavlavi iwkyfgfhmm lfiaglqavd
      181 rsvleaaeid gatgwqkfry vtlpllgstv rlsiffavig slqlfdlvmp ltgggpsnst
      241 qtmvtflyty gvtrmqvglg savgvvlfvi cvtlafgykr ifmrhd
//
LOCUS       WP_457663830             549 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Sinorhizobium medicae].
ACCESSION   WP_457663830
VERSION     WP_457663830.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 549)
  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 549)
  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 549)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..549
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62416
     Region          78..403
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 mtsrigreir rqtkrklnla paaigsaiar lsrdgdaypi ifsaieevrr qdenrglphs
       61 vaieeklpkp eidlnqprik hvrihnfksl esidfsmkaq mpevavamsv pnefsdvpda
      121 pcllilgena tgkssileai altciptqlr nqlqespadl lldpeymgsa ghapinrgsi
      181 evefhndtpt lklvldreng ifsdnsdahh plifaygahr lfdreqrddv vrhidtlfrr
      241 dqvisnpepw lielskrspe slnevvsalr hiiqidghfr nievgrdqdg keycainier
      301 knpdgllrqr lsvvssgyra vlavvcdifs rllelsnydp raarhgraii lideieahlh
      361 prwkmqivsg lrralprstf iltshdplcl rgmfagevmm lnryrnrdqt adsssmnevv
      421 eqisdfanie nltidqllts difqlfstdd rrieatfaev pailkkeeef lrtreerwrl
      481 sereqtilrs frdeisnglp ygktevsrlv qeavaeyvag rrvrdkssne ekreraknai
      541 ksylgdllg
//
LOCUS       WP_457663835             366 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457663835
VERSION     WP_457663835.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 366)
  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   2  (residues 1 to 366)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..366
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39888
     Region          60..343
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mnhrvlrktr lplvealpwh tyafsllrqe kggsastnll withhdlntn trhseakvgs
       61 rvrlsdvakr agvgvgtvsr vlnrsakvsa itrkkvldai aelgyrpnlv arslaanrtg
      121 liaaiipeig ytqhseiilg mtdvlhanem nlmigtcgys degelkviea llsrrpdaiy
      181 vtgvrhteav rtalersgip vvegtnltdh pidtvvgysn fnasadltrl lidhgyrhiw
      241 hvtvnkdfsc rsddrlkgfq watsteagle vnvircensf dggaeavrlv tapgvkveal
      301 tfttdvmavg gllecqrrgi avperlaiag fddltiarsi npppyngesr pgrsraegcg
      361 nyrqpp
//
LOCUS       WP_457663839             324 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663839
VERSION     WP_457663839.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..324
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35561
     Region          105..322
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mlyqdtvese vlvhrpwfva sifavvfaaf lavnltgtsf gevmrpiigd plqsgaygrf
       61 aialvlaiif svnivligfa plkvqigivw aellllflaf fesfdlsipf iwenlpylit
      121 qgvvttiyvs avslifasil aiiaavakls sngfayaiaa fytsffrglp llmqiyliyl
      181 glpqlgivln avpsgilals lcvgaymtei fragiqsidr gqweasrsmg fgfgltmrri
      241 ilpqalpvii ppmgntfism lkdsslvsvl gvweltflar tigqptfhhm emliaasmiy
      301 wimsaclevg qsrleryfgr skvr
//
LOCUS       WP_457663848             298 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663848
VERSION     WP_457663848.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31217
     Region          15..292
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtnahtgadr ealstrmgag skrylshgsf tlggflvlfv vamailapll apydpyaqsl
       61 agrftppvwm ngggwahplg tdqlgrdyls ritygaqisl migigtails giigtslgvc
      121 agyfggkids vimfiitarl ampvilvala vvalagaslt ivtltlglll wdrfalvsra
      181 ttmqirnsdf vtaaelqgas vaqiviheil pnlvnnlivv atleiaqaiv leaalsflgl
      241 gvpaplpswg lmisegkssi lfepwlitip giflfslvlg tnllgdglrd mlspdgrn
//
LOCUS       WP_457663849             535 aa            linear   BCT 27-JAN-2026
DEFINITION  5-oxoprolinase subunit B/C family protein [Sinorhizobium medicae].
ACCESSION   WP_457663849
VERSION     WP_457663849.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..535
                     /product="5-oxoprolinase subunit B/C family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56470
     Region          1..216
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
     Region          233..522
                     /region_name="PxpC"
                     /note="5-oxoprolinase subunit C/Allophanate hydrolase
                     subunit 2 [Amino acid transport and metabolism]; COG1984"
                     /db_xref="CDD:441587"
ORIGIN      
        1 maeplrflpv gdygllveld dlhttltlld alqadrpdgv velipaartl mvrfdthvtn
       61 raslvetiah idlsakssrl gevfeipvsy ggedlndvae llglsveeli rrhteatytv
      121 aftgfapgfa ymtsddpvfd vprrksprvr ipagsvalgg kfggiypsds pggwqllgrt
      181 elrmwdtnrs raaflapgdr vhfcdiakga svpvsampav skaciqapkn sdgllvtrad
      241 rpaffqdlgr sghagqgvse sgaldrrslv eanlcvgnpr gsaaveiayg gfamradrpm
      301 tlavtgapsq ttirtsdgrs ltvrigkpfa lnagdelile fpgegthsyv avrggftvek
      361 vlgsaatdtl akvgpapiva gdilmpanea isavapdlpc agklprvadt vtlditlgpr
      421 adwftshslt tlltqewqvt pessrigirl agavplqrad atelpsegtl lgaiqvphng
      481 qpvlfladhp ltggypvigv vasyhhnlag qipigakirf navagfepls rgmtr
//
LOCUS       WP_457663852             452 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663852
VERSION     WP_457663852.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..452
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50565
     Region          1..433
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 mpsqaaafvt yqyanwlvtr tpsgelkgel teswessgdg krwafklkqg ikfhngkeft
       61 sadviysldr hrapgskspi anlmkgidnv kadgpyqfsi vlkepdaglp ylltqiylvm
      121 qpkdessdrg igtgpyvlek aepgkrftfr rntdyfdpds vwfeeleili inddtarisa
      181 llsgsahlit eippnlvarl ktasslnivs tpetklyyfv mqidkppydn pdlrlalkys
      241 vdrdmilkgi aagygeignd hplnsvyplh pkdipqhsyd vekaryhynk sghsgpivlh
      301 vaeifpgavd msvmfqqsaa kagitielkr epvdgwwdnv ylkapfqvsy wgslttedha
      361 lslpyasdas wndshfrrpe fdkllaqara qldpklredl ykqaatmihd dgghivvmfp
      421 hniegmsskl qgyvqdpfgg aakatqrcwf as
//
LOCUS       WP_457663863             330 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457663863
VERSION     WP_457663863.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Bondos,S.E., Swint-Kruse,L. and Matthews,K.S.
  TITLE     Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox
            Proteins
  JOURNAL   J Biol Chem 290 (41), 24669-24677 (2015)
   PUBMED   26342073
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Ravcheev,D.A., Khoroshkin,M.S., Laikova,O.N., Tsoy,O.V.,
            Sernova,N.V., Petrova,S.A., Rakhmaninova,A.B., Novichkov,P.S.,
            Gelfand,M.S. and Rodionov,D.A.
  TITLE     Comparative genomics and evolution of regulons of the LacI-family
            transcription factors
  JOURNAL   Front Microbiol 5, 294 (2014)
   PUBMED   24966856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Swint-Kruse,L. and Matthews,K.S.
  TITLE     Allostery in the LacI/GalR family: variations on a theme
  JOURNAL   Curr Opin Microbiol 12 (2), 129-137 (2009)
   PUBMED   19269243
REFERENCE   4  (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   5  (residues 1 to 330)
  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   6  (residues 1 to 330)
  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 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   8  (residues 1 to 330)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   9  (residues 1 to 330)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
REFERENCE   11 (residues 1 to 330)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
REFERENCE   12 (residues 1 to 330)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..330
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35960
     Region          7..52
                     /region_name="HTH_LacI"
                     /note="Helix-turn-helix (HTH) DNA binding domain of the
                     LacI family of transcriptional regulators; cd01392"
                     /db_xref="CDD:143331"
     Site            order(14..18,20..21,24,29..30,33,47..48,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143331"
     Region          59..327
                     /region_name="PBP1_sugar_binding"
                     /note="periplasmic sugar-binding domain of uncharacterized
                     transport systems; cd06307"
                     /db_xref="CDD:380530"
     Site            order(71,145,196,271,291)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380530"
ORIGIN      
        1 mkvkltdiar ragvghatvd rvlnerggvk pdtakrvlda arelglartl aklyrnglrf
       61 evllgrrdnp lcarindafr rfihlmddni vlertfvdet kpdlvaaair nsrcnaiivy
      121 gqehemiiea iaevtsigkp vitlvsdvpt aprlnyvgin hynagraaaf flskmtnegr
      181 vvllcgslhy rahaerisgf rdgiadysgr laivdliear gddaaaeyml ckaltegeva
      241 giynagasda averaistmn rqlapvlvgh dltenaarml qngvmavvid qnpdlqaqka
      301 lrilaarfgi sneaqespiv pftihvkdni
//
LOCUS       WP_457663865            1025 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Sinorhizobium medicae].
ACCESSION   WP_457663865
VERSION     WP_457663865.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..1025
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=112430
     Region          2..475
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mlggelsrta lalwphqhaa ldtveayfvs asaraclvnm ptgtgktgvm atiarqraqv
       61 rpvlvvcpsa alveqliaqf edrfwdkiga spvwkpdrvw nvlpsdiesl tkrldghgge
      121 rvivvgtvqa iqqidadgki dqlhgrigti lfdeghrepa pswarvvrgf avptvlfsat
      181 pfrgdlkifd vdddhihflg fadavdqgli rgveideqpl plspddyala liarvdalva
      241 egrftaankv ivrcdseelv temhqaltag lagraagvla ihhnfrerpd dgifdavprd
      301 laaraerfli hqfmliegid dprctmlaly epftntrmlv qqigrlirhp gpigdaapaa
      361 yvlapkgrdi anewnsflaf daaskangnk pfvrndatil enliaalptl dyvmgrfrer
      421 pdlddpglhd dlrfpsaava ftiepdldld elqkaikael iredrhealt grtadgncry
      481 hitlrltpsp flsgslfqap sleatiyakk nkrlfffdsa glwineldgi gprvnaktlr
      541 allpdgydns isfmsvkntd lgplalrsrs lsarsldrsg vfmgehlnvv tratgyihpk
      601 aaedgirrav gfsrsrvrdg kgndltaqqy adwcvtvdaq ldaaartasv ftrfavpdtv
      661 padtmplnil vdmvemadqf vakgqtaavr iedlcvavee dtdpkapalf rfllhvdgee
      721 hpvwidwnak kakywlvspg lsriktkdnp kisltrrlnq lqpfriitrd lahtyvggdf
      781 yrldldltdp kgaaslvldl itaipglgav tsekgvlvdg hvdywadgsl fefldkalrp
      841 drgpalfgrs fpdlvcddlq devgdflgld etsasqaava vagkwksgnp gvsasafydv
      901 caqglknlay mksdgvvlpg sqtrfdgrwr lskrnspitq tvdrkrhgrg stafrgafqr
      961 lraapttdra iwlvcsggml slaklkaefa kpqpephvlq fyhlvlstys acqsvgvqlr
     1021 ifcae
//
LOCUS       WP_457663868             214 aa            linear   BCT 27-JAN-2026
DEFINITION  transcription termination/antitermination protein NusG
            [Sinorhizobium medicae].
ACCESSION   WP_457663868
VERSION     WP_457663868.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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..214
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     gene            1..214
                     /gene="nusG"
     Protein         1..214
                     /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=24088
     Region          42..214
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mimqrrisgs pialqgrerf sdrirritaa nlkaasmkvt emnpenarwy clhvksgkef
       61 dvenaltkan veafmprerv vlvrhgrkie sdrpffpsyl lvrlvptpea fhglryqkdv
      121 ldfvggpagy hvindadvvv fkrlsdgvea prvatdksfr dgdqadivlg pfagfrcvvt
      181 avkwcrqaka svridvqgrp fdiesmplaf lrkl
//
LOCUS       WP_457663877             314 aa            linear   BCT 27-JAN-2026
DEFINITION  acetamidase/formamidase family protein [Sinorhizobium medicae].
ACCESSION   WP_457663877
VERSION     WP_457663877.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wyborn,N.R., Mills,J., Williams,S.G. and Jones,C.W.
  TITLE     Molecular characterisation of formamidase from Methylophilus
            methylotrophus
  JOURNAL   Eur J Biochem 240 (2), 314-322 (1996)
   PUBMED   8841393
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Mahenthiralingam,E., Draper,P., Davis,E.O. and Colston,M.J.
  TITLE     Cloning and sequencing of the gene which encodes the highly
            inducible acetamidase of Mycobacterium smegmatis
  JOURNAL   J Gen Microbiol 139 (3), 575-583 (1993)
   PUBMED   8473863
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..314
                     /product="acetamidase/formamidase family protein"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=33231
     Region          5..313
                     /region_name="FmdA"
                     /note="Acetamidase/formamidase [Energy production and
                     conversion]; COG2421"
                     /db_xref="CDD:441971"
ORIGIN      
        1 mcsncdytih grhhhygwdr sippaetvas gsrlefncld lgsghftags tvadvstvdf
       61 tkvnpvtgpi yvdgampgda lkvtiehfkp sgfgwtanip gfglladqfe epalalwkyd
      121 pdtlapaafg efgrvplkpf agtiglapae pglhsvvppr rvggnldird laagttlylp
      181 vevegalfsi gdthaaqgdg evcgtaiesa mdvvvkldvv kganlhmprf ttpgpvtrhl
      241 daegyevttg igsdlmegar aavsgmidll cathgmkped aymlcsvcgd lriseivdqp
      301 nwvvsfyfpr vvfa
//
LOCUS       WP_457663882             308 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanine--D-alanine ligase [Sinorhizobium medicae].
ACCESSION   WP_457663882
VERSION     WP_457663882.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..308
                     /product="D-alanine--D-alanine ligase"
                     /EC_number="6.3.2.4"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008716 - D-alanine-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          1..308
                     /region_name="ddl"
                     /note="D-alanine--D-alanine ligase; Reviewed; PRK01372"
                     /db_xref="CDD:234948"
ORIGIN      
        1 msskhvavll ggfsserpvs lssgtacada legegyrvtr vdvghdvaav lqelrpdvvf
       61 nalhgpfged gtiqgileyl eipythsgvl asalamdkaq akhvaeaagi pvaeavvmdr
      121 rsfgnqhpmk ppyvvkpvre gssfgvvivk edqshppqvi tssdwrygdr imveryvagr
      181 eftcgvmgdv algvteiipq ghafydydsk yvkggskhvi paqvspniyq kiqtlalkah
      241 qaigcrgvsr sdfrfddrgd gegeliwlei ntqpgmtpts lvpemaqhag lrfgeflrwm
      301 vedasclr
//
LOCUS       WP_457663883             307 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457663883
VERSION     WP_457663883.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..307
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34549
     Region          1..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 masvthssar rsrfriskrv lpyvlslpal lvcigilipf ftaviysfqr yrlsqpwarq
       61 fnwgdnylnf ftdpgfwntl kisllyagvt vtlelllglg ialllqrrst vnnftsimll
      121 lplmtapala almwklmtnp gfgilsylas liglenfrwa sspdtalltv vlvdiwvytp
      181 fimilllagl rslptqpfea aaldgvprsf vffritlpml tpyiltatlf rlldsiqqfd
      241 iiyamtqggp gdtltvfqve aylnffqstn vgrsaallii lwaityilsn ifiknwlrlr
      301 erargea
//
LOCUS       WP_457663887             335 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 172 protein [Sinorhizobium medicae].
ACCESSION   WP_457663887
VERSION     WP_457663887.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Kashima,T., Okumura,K., Ishiwata,A., Kaieda,M., Terada,T.,
            Arakawa,T., Yamada,C., Shimizu,K., Tanaka,K., Kitaoka,M., Ito,Y.,
            Fujita,K. and Fushinobu,S.
  TITLE     Identification of difructose dianhydride I synthase/hydrolase from
            an oral bacterium establishes a novel glycoside hydrolase family
  JOURNAL   J Biol Chem 297 (5), 101324 (2021)
   PUBMED   34688653
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10567709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..335
                     /product="glycoside hydrolase family 172 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37244
     Region          72..>309
                     /region_name="DUF2961"
                     /note="Protein of unknown function (DUF2961); pfam11175"
                     /db_xref="CDD:463235"
ORIGIN      
        1 mnnaglsplr glaklrdakt rrfssydrtg gnddrlhiep gqtvtiaeya gagivthiwv
       61 tiqcesesyl rkavlrawwd gegapsieap igdffgmgna rtgnyaslpm qaspedgkaf
      121 ncyfpmpfgs gmkftitnea ehdllfyyyi dlelhdelee dlgrfhaqyr qerpenfdea
      181 gltneqvlfg genvdgkgny vildaaghgh yvgvlysvys rrrsevwdwy gegddmiyvd
      241 gepgisvpdg irkpdprigp kaaliedrpe sapgandawp ptlhgtgted yfntawcptq
      301 dydaplprhh lrrrseldra gdplslahrg pgdfp
//
LOCUS       WP_457663889             176 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase, partial [Sinorhizobium medicae].
ACCESSION   WP_457663889
VERSION     WP_457663889.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         <1..176
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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          <1..167
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(1,38,53,55,63..66,115,140..142,144,147)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(13,79,81..85,113,117)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            38
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 evdsyggevt gafdcaeqif elsqlkptia vltdhacsag yllaspcrql vipqtgicgs
       61 igvismhvdm sawlakeglk vtilkagehk adfnpyeaip ddvlqqelae leelrvefaa
      121 tvaryragrl tqqsalatea rvyrgqkavd agladavarp sqvleafeae lsrtag
//
LOCUS       WP_457663891             300 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457663891
VERSION     WP_457663891.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..300
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33063
     Region          3..294
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mskgetlciv gesgcgksit alslmgllpk aarpsaeell fdgidlqkin skdlralrgn
       61 rismifqepm tslnplhtig rqlsdvyrah rqatrkeaea ravhllqevg isnaaqrllq
      121 yphelsgglr qriviamalm cepdlviade pttaldvtiq aellrllkdl qkrfgmgiim
      181 ithdlglvsr iadrvivmya gqvvesapar qlfdrpahpy trallgsvpd psharmqplp
      241 sipgnvpsll tpmdgchfyd rcsyaseacr rqinlrevsd qhqarcimvd etsaplrvmk
//
LOCUS       WP_457663894             285 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Sinorhizobium medicae].
ACCESSION   WP_457663894
VERSION     WP_457663894.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..285
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29977
     Region          23..263
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtglgglals fdiplirsad gevwsilavr slstflaala twvvinhllg rrvalipgka
       61 gliagllygi nsftfllavf ntstanvvfi laftsmfaai lswiflkerp snatfltmgv
      121 ilvgvgvivs dglesghlfg damaacsafl laaaitisra sgrdmslvpl ttaifpaiag
      181 fmllpagglt iaepayilfn glvmiplaff clatgpryls apevgmfyll etilapiwvw
      241 ivfsetpssp tllggtilil alvghslwqi rmraararla cevag
//
LOCUS       WP_457663929             641 aa            linear   BCT 27-JAN-2026
DEFINITION  type VI secretion system Vgr family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663929
VERSION     WP_457663929.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..641
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=70936
     Region          20..>572
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvqhttenpl krnrfaavts aafqpndvtl rwlrgterlg qpfhyevkla ittpiqnfan
       61 vpgqsltagl klkgggtrff ngviarfeyv glddtehlny laelrpwvfl lnyrtnsrif
      121 qnktsieiit aifqenkgnf knrtmgrfpr rifcvqhget dldfvsrlme qdgiyyyfeh
      181 gpdrhdlvlv dnlssheacm penvethhnl rpagnlhrdd vildwseias lqpntvvlkd
      241 ydhekpaael tsvarvptvr iggippakda kqrlsgaprv asqtanagas sklhatfnyp
      301 gcykekshgd fyatvraeel acstyrarie ttarqittgs tfkaanpyny gdvgarpkst
      361 qrfmaiandf tilgelgggp trsatghkae cflyhsavei ipastqyrpp rrtplpvikg
      421 pqtavvvgpr getiatdryg rikvqffwdr egnkdenssc wirvaqnwag kgfgcllipr
      481 igqevvvdfv hgdpdrplii glvyngsnlp pevlpanktr stfrthtdgg tiaeynelrf
      541 edrpgceevf lkaqkdhnve vgnnyaidvk kqylltsasa aasrssievt pdkirlsvkg
      601 atglqaieis eagitlingq gasiqmsgls vmindealvv t
//
LOCUS       WP_457663908             607 aa            linear   BCT 27-JAN-2026
DEFINITION  phage terminase large subunit family protein, partial
            [Sinorhizobium medicae].
ACCESSION   WP_457663908
VERSION     WP_457663908.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         <1..607
                     /product="phage terminase large subunit family protein"
                     /EC_number="3.1.21.4"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          1..584
                     /region_name="gpA1"
                     /note="Phage terminase, large subunit GpA [Mobilome:
                     prophages, transposons]; COG5525"
                     /db_xref="CDD:444276"
ORIGIN      
        1 laksaqiggt icaniftlgs ldmapgdfly vhpteenaar wsktklmplv rempavaklf
       61 sqnsrdasns vlykeridgr gaiqaagans paglsmispr kqvqddlakw qmneagdpev
      121 qadsrskaff ngkifkistp mvspgckits nyqegtqety hvpcphchel qelrwenmrd
      181 hidpehpeqa hfvcihcgce ihehhrewmv kpengakwva kypergrrhr sfriwmaysp
      241 ferwenlare wltvqaggpe nrekgsgaeq tfwndwlgla feadnkaidw evlrdraedh
      301 gfqrgvipae alalvlgmdv qgdrvewllv gygrnryrav idhgvvdhra gshladakeh
      361 sghisepevr aaldrllqre wlddagrkrt adrvaidgna ytddvwnwvr khpksrvimv
      421 rggnteaapp ivqtkeydrr gkpkkqkwls rfftfnasaf kirlyrdykk ddpeqagyir
      481 fargfgddfy qqatsearvp ektrsghtry vwklaegkrn eiidmlnqsl ggayrwgvpy
      541 wtdeewdaia drlgrleapq qgdledrlnq iavktepaag esaaaeqqsp lvaaalaraa
      601 raaqrnr
//
LOCUS       WP_457663949             266 aa            linear   BCT 27-JAN-2026
DEFINITION  outer membrane protein [Sinorhizobium medicae].
ACCESSION   WP_457663949
VERSION     WP_457663949.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..266
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=27954
     Region          85..263
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mdwrrglcsv afcaglsapf faqaadedfl dapeitisse eaaggglylr gdigyaawld
       61 egdpyyrspg sgnvafdnar feepasatig lgyqftdvir adltaeyfeg rfdgtslsap
      121 ppcagegagt gcafshranf salglmangy vdlatlagft pylgagigat ridwktahet
      181 sscvgpggac sgnaggasyg grdswrftya lmagvsydvt drlkfdagyr ysqisdgdmf
      241 gsgdaqgydd glsrhefrvg lrfalw
//
LOCUS       WP_457663952             251 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Sinorhizobium
            medicae].
ACCESSION   WP_457663952
VERSION     WP_457663952.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..251
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27988
     Region          12..249
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mptsidtasl eitlsgvhkw ygqyhalddi nlsiaprekv vicgpsgsgk stlircvnrl
       61 eahqqgrivv ggvevgeder kvdairrevg mvfqqfnlfp hltilencil apmwvkripr
      121 aqateiamdy lnrvripeqa nkypsqlsgg qqqrvaiara lcmnpkvmlf deptsaldpe
      181 mvkevldtmv slanegmtmv cvthemgfar qvadrvifmd qgriveegep deffahpktd
      241 raslflsqll h
//
LOCUS       WP_457663953             421 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457663953
VERSION     WP_457663953.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..421
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=47497
     Region          <277..398
                     /region_name="DNA_BRE_C"
                     /note="DNA breaking-rejoining enzymes, C-terminal
                     catalytic domain; cl00213"
                     /db_xref="CDD:469662"
     Site            order(359,362,385,394)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mvsapglkvr rradgvayyw vakssspkak eyhtktkrlh gtedeiaaqc rvlqaefkew
       61 lsghgadgkr gydgtlrsli rlyqqtpesp yntkirsntk amydeslgll ektvgtrrle
      121 kltgldfirw yanfkepavd nekkakrrae laakgiilpp ngervrrayk amqllrivig
      181 fgvvlnitec frlaailgem efsspkarta sitfeqaqai cnkavekgll sialaqalqf
      241 eltlrqidvi grwekvtdan aggivdrdqr wrdgllwsdi dengillktt skvddvvaeh
      301 dtmaypflre midkvppekr vgpmikceat gmpyryrffs kkwreiatea gvptnvwnrd
      361 sraggvtegs dagadlehlr hhanhknaqt tqrynrktle ktqkvaelrv ahrgqknvpq
      421 t
//
LOCUS       WP_457663972             146 aa            linear   BCT 27-JAN-2026
DEFINITION  RusA family crossover junction endodeoxyribonuclease [Sinorhizobium
            medicae].
ACCESSION   WP_457663972
VERSION     WP_457663972.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Macmaster,R., Sedelnikova,S., Baker,P.J., Bolt,E.L., Lloyd,R.G. and
            Rafferty,J.B.
  TITLE     RusA Holliday junction resolvase: DNA complex structure--insights
            into selectivity and specificity
  JOURNAL   Nucleic Acids Res 34 (19), 5577-5584 (2006)
   PUBMED   17028102
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Sharples,G.J., Ingleston,S.M. and Lloyd,R.G.
  TITLE     Holliday junction processing in bacteria: insights from the
            evolutionary conservation of RuvABC, RecG, and RusA
  JOURNAL   J Bacteriol 181 (18), 5543-5550 (1999)
   PUBMED   10482492
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Sharples,G.J., Chan,S.N., Mahdi,A.A., Whitby,M.C. and Lloyd,R.G.
  TITLE     Processing of intermediates in recombination and DNA repair:
            identification of a new endonuclease that specifically cleaves
            Holliday junctions
  JOURNAL   EMBO J 13 (24), 6133-6142 (1994)
   PUBMED   7813450
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10531192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..146
                     /product="RusA family crossover junction
                     endodeoxyribonuclease"
                     /EC_number="3.1.21.10"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0000400 - four-way junction DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008821 - crossover junction DNA
                     endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=15730
     Region          16..133
                     /region_name="RusA"
                     /note="Endodeoxyribonuclease RusA; pfam05866"
                     /db_xref="CDD:428654"
ORIGIN      
        1 mtarirftip gdvvpwarag ggktvvkftp krqrdymgmi raeahrqmka fpgpltgplq
       61 lkiaavylwp ksttkariaa adgawkttkp dsdnitkiik dalntiayvd daqisfstcw
      121 kllgpkaglv vevislegvp apainl
//
LOCUS       WP_457663978             168 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457663978
VERSION     WP_457663978.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..168
                     /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=19091
     Region          10..59
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mrhlvnlkks eiyvsardvm drydisratl drwikkrgfp aprvivgkrh fllsqvdawd
       61 veqsgveaep qgeiafgmpi vsgliqnydd lvtamverrk elgiscield alsgmqegya
      121 nklenwrkqy grgmgpdtfp lwlgglrlgl vlvelprrpr kkrpqvse
//
LOCUS       WP_457663944             320 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase domain-containing protein, partial [Sinorhizobium
            medicae].
ACCESSION   WP_457663944
VERSION     WP_457663944.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Schneider,A. and Marahiel,M.A.
  TITLE     Genetic evidence for a role of thioesterase domains, integrated in
            or associated with peptide synthetases, in non-ribosomal peptide
            biosynthesis in Bacillus subtilis
  JOURNAL   Arch Microbiol 169 (5), 404-410 (1998)
   PUBMED   9560421
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         <1..320
                     /product="thioesterase domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
     Region          <20..306
                     /region_name="EntF2"
                     /note="Thioesterase domain of type I polyketide synthase
                     or non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG3319"
                     /db_xref="CDD:442548"
ORIGIN      
        1 vlvqalalgm kvsasnifda pilkdlapki eldsshytpg vlpvrtigsq apvffvptgy
       61 gdcsyvfrlv remdidcpvy alpwppfeea rrasleeiat kvahavrkvq prgpyrfagy
      121 ssgavlayal aerllyleet vsfmafidvp ipamspamtd teialqmife pleslgdegf
      181 evlrqsagqs sveqlfekar qigavvgrpd lyydairyaq fhqavhsyem pslpvsvhqf
      241 yalehslsrg arlpagpdan spmrgwdril gaefiqavpv pgdhvtmmav penrrvlarq
      301 lsaalnnspt thpnrkldvk
//
LOCUS       WP_457664005             255 aa            linear   BCT 27-JAN-2026
DEFINITION  CatB-related O-acetyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457664005
VERSION     WP_457664005.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..255
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=28104
     Region          47..203
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(50,52,71,83..84,89,91,93,138,140,143,162,178,186)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(52,54,82..83,85,94,100,140,143,160..161,166,174,
                     176..177,179,183)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(52,54,82,94,100)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100040"
     Site            order(83,85,130,140,143,148,160..161,166,174,176..177,179,
                     183)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 msiavkppes spsvrivgdv rlrfgcsrie veepvelrag lydverigaf tflggegsvi
       61 rhvesigrfc migpsaqfgl vehpgahisa hvlfehdvtr qfptqetrdf fdrnrslina
      121 areswsrrsg sririgndvw igqgvtisrg ctigdgaiia sravitkdve pysivggvpg
      181 kpikwrfpee irkklldlqw wqygllamdg vdvtdisgav rrieenirsl phvnstsslt
      241 ldealinarr gttsn
//
LOCUS       WP_457664007             273 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 108 protein [Sinorhizobium medicae].
ACCESSION   WP_457664007
VERSION     WP_457664007.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..273
                     /product="glycoside hydrolase family 108 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /calculated_mol_wt=28942
     Region          9..165
                     /region_name="ZliS"
                     /note="Lysozyme family protein [General function
                     prediction only]; COG3926"
                     /db_xref="CDD:443130"
ORIGIN      
        1 mrdnlptsld lmfgheggys nvktdrggpt kygithttla ahrgvksvta dqvramslqe
       61 aediyrrsyw sqsggdtlps gidyavfdfg vnsgparavk tlqrvlgire dghvgeqtla
      121 avrkypggis tlirdycdar mrflrsltna ktgfpvngrg wtirvtgkdp qgkwgdqpgv
      181 lgnalrlaad asgrtvekvd appeagakad srdtglgevl kkpeawgplg gllsaggalf
      241 agngpvqwal aaamvgavgv glwyfvrrvr ead
//
LOCUS       WP_457664019             470 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664019
VERSION     WP_457664019.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 470)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 470)
  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 470)
  AUTHORS   ter Beek,J., 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 470)
  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   6  (residues 1 to 470)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   8  (residues 1 to 470)
  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 10170708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..470
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52397
     Region          1..453
                     /region_name="PBP2_NikA_DppA_OppA_like_16"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08502"
                     /db_xref="CDD:173867"
ORIGIN      
        1 miydklfefd esgvplpqla ekvdisadnk sftiklrdgl kfsdgtpits ddviqsltrw
       61 asrdqtgqll rartkdlvki ddntlridlt esfdvpsala gitgnpafim pkrvaslppt
      121 ealtdtvgsg pyqfdfstwk pgqmrvytkn syyiprdeaa sfyagrkeav mdriefsyvp
      181 dpntamasml tgkqdiwldp pmanavalrn npnlkvvkgy slqglfvinh vvppfdnvka
      241 kqaltylidq keinaiavgd pefwhacyaf ltcsgtygne svydghrgpa nvekakelfn
      301 eagydgqpvv ildptdwpea haralylaqq lreigvkvdl qamdwgtlts rrtskepadk
      361 ggwnlfpnvm egqpassplt hlmlasscek awfgwpcdkq iedlrasfir tvdidekkki
      421 adelqarasa ylpfvmtgey nvvmsyglni egfipsapep ffwnvrrksq
//
LOCUS       WP_457664024             227 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457664024
VERSION     WP_457664024.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 227)
  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 227)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..227
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24904
     Region          <26..227
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mpfihkgeet hayrnvaaig lnglihcsgt ligrrtvlta ahcvenyqny itagrmtvsf
       61 gslffrpekn yvvtgfdfpr dpaagfffnp qtyeddiavl yvdedvdsay ppsslhvgdr
      121 ptwaeikdkp iaiiivgfgf nvvrndavga gikreaaiha dgytnrsfff qrsnpntckg
      181 dsggpsfliv nddfvligvt stgdagcnqg nnlrvdsylp wltrrir
//
LOCUS       WP_457664027             689 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664027
VERSION     WP_457664027.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Solano,F.
  TITLE     On the Metal Cofactor in the Tyrosinase Family
  JOURNAL   Int J Mol Sci 19 (2) (2018)
   PUBMED   29473882
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Xu,Y., Bartido,S., Setaluri,V., Qin,J., Yang,G. and Houghton,A.N.
  TITLE     Diverse roles of conserved asparagine-linked glycan sites on
            tyrosinase family glycoproteins
  JOURNAL   Exp Cell Res 267 (1), 115-125 (2001)
   PUBMED   11412044
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447028
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..689
                     /product="tyrosinase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75329
     Region          132..274
                     /region_name="Tyrosinase"
                     /note="Common central domain of tyrosinase; pfam00264"
                     /db_xref="CDD:425566"
ORIGIN      
        1 mhinrrtaig alvssallpw lhhvknaraq apkvqhgart aqgkaailky reavsllksr
       61 qrhdpaswhf qanthwyprt enleeifstv gaspaeaqki eafralalgg smdgqnvegv
      121 wrtcphssss inydflpwhr ayllcietli esaigepfam pywdytvapl lptefrqpsn
      181 ntnalyheqr llnddpalpi gaadasssls qeqfgffdvt algfsldles nlhgtihvft
      241 gtaggmadps yaardpifyl hhsaidrlwe swrrnitdpd psdsawlart hrfigvdgap
      301 mtwstqqild iqslgyeydt yeevlvasne lrpfglgatl eiansrgqvg gvlvvsapve
      361 vplsaaelpf dakrvteqgr fvltlenvsa qtnpgvgyrv yfniksdapp eekaarfagf
      421 fnlfglvegh gehgaggktv tidvtplvgr gvieppttqe efdkfanavs dkaaftaalq
      481 lidfsnnqll sarfmapkiv dvtgkppyds gwrkilriqa ragsaaktag igsgfilfny
      541 lrpqtdpapf paqgsnpdqa sknnqvmlia epgapnlkds aywavydske ngyrsayfla
      601 avfdlpdnpq tdgkyyvpra cadchghvdg gvvtpggvqy pnaklqlpgy rslggprgge
      661 rlfshcrdsc rnsvrrwygq gvtrvcsci
//
LOCUS       WP_457664034             529 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457664034
VERSION     WP_457664034.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..529
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58813
     Region          390..447
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 milvrssqci frvastaclt gllcvanlar addipnskai iqldnayddi signgriyaw
       61 nlssgeidev ayepevrvnn itqnaapygr iesvsteres gdiyflsrgr kdskgspllv
      121 griekgagva apllnleest grpqiyaykr dadtvlvvyd elsslltvir npdlwrnetv
      181 rraqfkneni flgrgsieri vtsedgqylv ayhsddqtqt fsfvdldeps vvfkhvplfs
      241 grikepallq fkvsdgdafv lysvagrflq ivsldrnfnr lieksfwqls glpnslvdks
      301 avtrtsssls vivsgsanst elaimsllrn drfssnilmg pylvkrlpei rafavsedgs
      361 rmailydrgs kvaivenpie wakgldgrpr sdevedvqvl ltelfetvpa dgikgpqtdq
      421 alrrvknlmg lpnlseidqv tlnalrqvks erdpeypnqe fteserceyn gqlttfcitn
      481 kdkykpiqvd yylsnssgek iyqasqlhsc afikasfpgs ntckisdve
//
LOCUS       WP_457664038             213 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Sinorhizobium medicae].
ACCESSION   WP_457664038
VERSION     WP_457664038.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22488
     Region          23..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdfvpslptl lafaaaslll aatpgpdmtl sisralaqgk kaalpvvlgt glgivvhtll
       61 vafgisalit asptaflalk tggaayllwl aiqairygss lsvtkmtdak gsgfsnvatg
      121 fsvnilnpkv viffmtflpq fvrvddpavt gkllflgfff ivigmpvnal vvlaadwlaa
      181 wlqrnrrvmr aidygfagvf sifaikifft qar
//
LOCUS       WP_457664039             489 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457664039
VERSION     WP_457664039.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..489
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51442
     Region          1..479
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mttailaidq gttnskavlv sttgeilsrg aspvgiehpq pgwveqnplr iwesvqeaia
       61 aclqkgprsd ilgiaisnqr esvtawdaat gkplgpvvsw qcrrsapaca elsaaghaer
      121 vraltglpid pmfpgpkmkw lldrippghe vrlgtidawl ihcftagaih acdagnaars
      181 qlydlnrraw sdelcdlfgv pksalpevcd saarfgvtkn vpglkdgipi asaigdshaa
      241 lfghgafkpg dgkvtfgtgs simttlprfi apeqgittti awsiagrpty afegnilvsa
      301 aalpwmaeml glshvedlid laataeprgp gfvpafvglg apywhadara lfsgitfntt
      361 raqmaravtd smafqvhdvf kamsaqsptp lgqlyadggp skntflmqcv adtlnhvitq
      421 cdapeasalg aaylaglslg vwpdlaavas lpragkpvlp rpcdaadrlm vwqdaiyrst
      481 vpgpsimse
//
LOCUS       WP_457664040             227 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664040
VERSION     WP_457664040.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 227)
  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 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..227
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24278
     Region          <11..223
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 msnpptkahs dwlrseagni dgvigivgwl difaadcrve medlisdplv cgirimlnrm
       61 aspetlinpa sltrigelad sglaiecltp pehldvvarl ateverariv vdhcglppvs
      121 ngfaewkvdi aslaglpnvt tkfsgltepf gpdvrladia eradwilglf gparlmaasn
      181 fpvcelgggv arwselleei lstaglspee yqaircgsas rvytrgr
//
LOCUS       WP_457664044             344 aa            linear   BCT 27-JAN-2026
DEFINITION  heme-dependent oxidative N-demethylase family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457664044
VERSION     WP_457664044.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Ortmayer,M., Lafite,P., Menon,B.R., Tralau,T., Fisher,K.,
            Denkhaus,L., Scrutton,N.S., Rigby,S.E., Munro,A.W., Hay,S. and
            Leys,D.
  TITLE     An oxidative N-demethylase reveals PAS transition from ubiquitous
            sensor to enzyme
  JOURNAL   Nature 539 (7630), 593-597 (2016)
   PUBMED   27851736
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..344
                     /product="heme-dependent oxidative N-demethylase family
                     protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=40266
     Region          53..284
                     /region_name="DUF3445"
                     /note="Protein of unknown function (DUF3445); pfam11927"
                     /db_xref="CDD:463399"
ORIGIN      
        1 maiafkqetf rddfsyrnsa enirrfpfpf drdeymyavn mephvkgqkg tafenlidid
       61 ehyvaemrdr alvlkedplr yqalphmmaa qwdtlellme eqavgfpehf tlarngdqwr
      121 winrplgidd tftfgdrstl pcepleyitr qgdfcivdqr dgnlwmdagm vttqadwsld
      181 fdigmnfmew hgpvplahqm gvfdralkfl lnlqqgkptr rfnwtmtinp rldtspenyh
      241 kwgpdratvt tgnvgdkvhl rvevqslwrl prsnailfvi rcylmnmnel vtvpkwarrf
      301 prvlrtlppe lidykgltry rqttidwlsk fddgeptspg tfpd
//
LOCUS       WP_457664055             463 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457664055
VERSION     WP_457664055.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..463
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49576
     Region          6..423
                     /region_name="ASKHA_NBD_FGGY_NaCK-like"
                     /note="nucleotide-binding domain (NBD) of Novosphingobium
                     aromaticivorans carbohydrate kinase and similar proteins;
                     cd07772"
                     /db_xref="CDD:466792"
ORIGIN      
        1 mtmktvavid igktnakial velerfeeia vrkagngvkd dgpyphfdte rlwrfildsl
       61 aalnrehpid aisvtthgat avlldssgal alpvldyefa gpdaladeyd kvrprfsetg
      121 sarlpmglnv gaqlfwqqrm fpdhfarvat iltyaqywsy rltgiranel tslgchtdlw
      181 npatadfssm vdqqgwrpvf apvrragdvl gpvlrqvade tglppetpvh cgihdsnasl
      241 lphlitrqap fsvastgpwi vmlavgarpv klderrdtli nvnalgdpvp sarfmggraf
      301 slliggdppp aspeaeasvl enghmllpsl pggsgpfpts sprwttdedr ltpaerlaav
      361 sfhlalmtat cldligarge ilvegpfasn eaylrmlaaa tgrpvlanrl nstgtslgaa
      421 clvagahvrt gaepvalqmp vayagyadlw rrltaahvqa gsq
//
LOCUS       WP_457664056             759 aa            linear   BCT 27-JAN-2026
DEFINITION  chemotaxis protein CheA [Sinorhizobium medicae].
ACCESSION   WP_457664056
VERSION     WP_457664056.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=81315
     Region          1..751
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmneikeif fqeceeqlae letgllklnd gdrdpetvna vfravhsikg gagafglddl
       61 vsfahvfett ldcvrsnrle ptqdvlkvml rsadvladlt naardggsvd ggrsrqlike
      121 lealangelp qaatepvpka vpsaaapvap vvneegfqpv afsfddfeag deltiepvay
      181 eivfkpksdl yakgndatll lrdlsrlgem sihcdmdglp pldrlnpeea yfswkislst
      241 dkgeeairsv fefaewdcdl evavagglig mdeelpmqpv pfdlsildee aqmpageedr
      301 ayphegeaqn atipaaetas nvlqmaqsaa rvspenvrnp tsastaqnia aqqaasaatp
      361 tirvdldrvd rlinlvgelv inqamlsqsv iendtngtss inmgleelqq ltreiqdsvm
      421 airaqpvkpv fqrmsrivre iadmtgksvr litegentev dktvidklae plthmirnav
      481 dhgletpdkr iaagkspegt vrltakhrsg rivieladdg aginrekvrq kaidndliaa
      541 danlsdeeid nlifhagfst adkisdisgr gvgmdvvkrs iqalggrini ssrpgqgsif
      601 tmslpltlav ldgmvvtvan qtlvvpltai vetlqpeasa ihsfgasqrl iairnsfcpl
      661 vdvgrilnfr gaqanpvegv allveseggg qralmvdaiq gqrqvviksl eanythvpgi
      721 aaatilgdgr valildvdai vaasrgqslr pemplaaag
//
LOCUS       WP_457664058             293 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664058
VERSION     WP_457664058.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32437
     Region          1..287
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mnwddvrvfl avartgqila askrlgvnha tlsrrvtale atlktrllvr rpsgceltae
       61 gevffaaaer metemlaaqs qvgridtaia gtvrigapdg fgvsflaprl gqlmarypel
      121 klqlvpvprs fslsqreadi aitierpeqg rlvsskltdy tlglyasady laghgtprtv
      181 ddlkkhrrig yvedliftps lnfsaevmrs wdasfeissa tgqteavrss agigilhnyi
      241 arqypelirl lpetairray wttyhesard lvrvrtavsf lqelvteehs ifv
//
LOCUS       WP_457664067             112 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Sinorhizobium
            medicae].
ACCESSION   WP_457664067
VERSION     WP_457664067.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..112
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12014
     Region          51..102
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(72..74,76,89..90,94..95,98,102)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mprktprica cgrvvpagqq cqcakarkaa sdaarpaaad rgydadwraa rakhlarfpd
       61 cvecgdratl vdhvisirka phrrldptnf asmcptchgr ktaavdgsfg rk
//
LOCUS       WP_457664073             561 aa            linear   BCT 27-JAN-2026
DEFINITION  terminase large subunit [Sinorhizobium medicae].
ACCESSION   WP_457664073
VERSION     WP_457664073.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..561
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61633
     Region          42..554
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mttlrsrsrl hrpandntpa lvskafphwi hddspiadpf gygeravefl rrlkhpkstl
       61 pgsqfvlnpw qerivrriyg prdehgrriv rtvflmlprg arktslsaal sllqtigpeh
      121 tpagesvfaa sdrtqagiaf reaadiirad krlvaatkin dafnapkqiv lkrdnatlkt
      181 vssdggaqhg gtprfvlade vhiwkgsdlw ealrtglskt pgsllviatt agrgqenlaf
      241 dtydyarkva rgdiidpsfl piifepapda dwrdeavwha vnpglalgyp dlaglramar
      301 eaearpaere afrqyhlnvw ldhsaapfvd mdvydegaea idldelrgqp cwlgcdlsss
      361 tdlsvivaaw qdgdggyvvm pwffcprdnl rerqeasgap yvqwakdgli tategnvvdf
      421 raveqrirdl adefdvqeia fdpalarvil nnlmddglpa iefrqgslsm mpaiaelera
      481 vvgrklqhgg hsilrfcman aevetnshgh kvrlkkskkw lsidgavaaa matmraslgg
      541 sagvgsvyds ddweealaaf g
//
LOCUS       WP_457664079             286 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664079
VERSION     WP_457664079.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..286
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31691
     Region          14..265
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrmkrtkegs mgrdtegtgt lgkamavlev vamaerpqrf tdivmalrqp rgtlhrllgh
       61 lveegllvqr pdlsyepglr llkfayrsws gnrfreiaap yllklhqltg etvhlgvlre
      121 teiiyvdkve sqqtvrmssq igkaspayct gigkaalsvl psselqrisa rmefrpftpk
      181 thrsaetlya eiaeirhdgh afdreeheae iccvaapisv pdhdliggis vtgpsyrvsl
      241 aqltawaqdv rkaaadieee lrirsgpgre tggetprvrs daqrpr
//
LOCUS       WP_457664081             122 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457664081
VERSION     WP_457664081.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=13834
     Region          17..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mphadvspea rdnarrmrsa mteaevklwn elrahrlmgl dfrrqvpiag yivdfacaeh
       61 rlivgidgsq hagaeeadcd rrrtqrlear gwtvlrfwnd dvlrdvndvc ehivrvigkg
      121 gd
//
LOCUS       WP_457664082             192 aa            linear   BCT 27-JAN-2026
DEFINITION  LabA-like NYN domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457664082
VERSION     WP_457664082.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Taniguchi,Y., Katayama,M., Ito,R., Takai,N., Kondo,T. and Oyama,T.
  TITLE     labA: a novel gene required for negative feedback regulation of the
            cyanobacterial circadian clock protein KaiC
  JOURNAL   Genes Dev 21 (1), 60-70 (2007)
   PUBMED   17210789
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180866
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..192
                     /product="LabA-like NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21796
     Region          6..164
                     /region_name="PIN_LabA"
                     /note="PIN domain of Synechococcus elongatus LabA
                     (low-amplitude and bright) and related proteins; cd10911"
                     /db_xref="CDD:350235"
ORIGIN      
        1 mfdprekial fidganlyaa skslgfdidy rkllkafqkr gyllrayyyt aliedqeyss
       61 irplidwldy ngykvvtkpa keftdslgrr kikgnmdiel aidameqsel vdhlvifsgd
      121 gdfttlveal qrkgrkvsvv stmatqppmi addlrrqadh fidlaslrae igrepservq
      181 rpvepvsddv el
//
LOCUS       WP_457664084             218 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457664084
VERSION     WP_457664084.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..218
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23081
     Region          24..218
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 msripalaaa faphaelage llphafaaed gshdashlir vwknalriqa eeggdirqla
       61 aavllhdcvs veknsplrae asrlaaekas avlgdlgwsp adissvahai lthsfsanla
      121 petlgagilq dadrldaigm vgaarcfyia grmgsglydp ldplaeerpp ddkafaidhf
      181 etklfrlsgg fqtgagrrla lerearlrsv lammldei
//
LOCUS       WP_457664085             322 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664085
VERSION     WP_457664085.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..322
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34201
     Region          7..312
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mvtsagplpv tviggflgag kttlvnhilg gdhglkiavl vndfgainid talitsmegg
       61 lynlsngcvc cglnqglveq leallterpd vdhilieasg vadpgrimdt vlyarfcgrl
      121 rgdavlvlad aagfddaiai apglaeaqvg sadllilnkt dlatrdalda wrkrwsfads
      181 rivetenarv pfsilfaget lardpasafa atsvheqaes vtwrhhepid akrlhavlat
      241 lptgiyrakg fvtasdgrcf tvhvvgtrvt fqplarlpeg lgvenllvli gfgqglefer
      301 ilaqldgcag rpplhrkrrs lr
//
LOCUS       WP_457664089             129 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Sinorhizobium medicae].
ACCESSION   WP_457664089
VERSION     WP_457664089.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..129
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=14231
     Region          31..114
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mglkslliva aliiaplavq pvaaqeakgp viriaeleid paqmaaysaa vkeemeesir
       61 vepgvlalya vsikgqpnhl kffemyadqa ayeahresph frkyvettkn mitsrklfet
      121 dnfqlsakr
//
LOCUS       WP_457664090             259 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457664090
VERSION     WP_457664090.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..259
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28135
     Region          27..133
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
     Region          162..259
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mkrliaplig vmmmtasnag aqqpnvegrr fspdqvrsva paleqytqqr lygdvwqrpg
       61 lnrrdrslvt iaaliargea paltyyadqa lengvrpsei setithlayy sgwgkamati
      121 gpvseafakr gisqdqlaav estplpldee aetqrattvg nqfgsvapgl vqyttdylfr
      181 dlwlrpglap rdrslvtvaa lisvgqveqi tlhlnkaldn glteeqaaev ithlafyagw
      241 pnamsalpva kavfekrrg
//
LOCUS       WP_457664094             555 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease J [Sinorhizobium medicae].
ACCESSION   WP_457664094
VERSION     WP_457664094.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..555
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60239
     Region          3..555
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 maqneelvfl plggvgeigm nlglygygrp gsrqwimvdc gvtfpgpdlp gvdlvlpdia
       61 flaeerrnlk aiiithahed hygalndlwp glnvpvyasp ftagmleakr afeksrseip
      121 itifkqgdri nvgpfsveav gvnhsipepm aliirtqlgt vvhtgdwkid lepslgpltd
      181 ekrlrqigee gvlalicnst nalregvsps erqvseslsk iiadaegrvg ittfssnvgr
      241 irsvaqaaea agrevlllgs smkrvvdvar dvglmeglrp flaedefgyi prdkvvvilt
      301 gsqgepraal akiardemrn vafsagdtiv fssrtipgne kaindikngl ieqgihiitd
      361 sealvhvsgh prrnelqqmy qwvkpqivvp vhgeaahlta haelalqsgi psvprlrnge
      421 mlrlapgpae vvdqaphgri ykdgtligdf eemgigerrk lsfaghvsvs vvldnrydfl
      481 gdpdvvpigl peyddegesm edtlydavlg avesiprakr kdlamlqeav rravrstanq
      541 vwgkkpvvtv fvtkv
//
LOCUS       WP_457664099             267 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664099
VERSION     WP_457664099.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29654
     Region          9..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 miekpvqdad sgpkisfqnv trrfgegeas flaldrlnld vgdgefvtvv gpsgcgksta
       61 mniaagltdv sdgrvlvdgk pvdgpgperg vifqqyalfp wstvrqnvef glrikrmpaa
      121 errriadhfi slvglkdfad alpktlsggm kqrcaiaray avnptillmd epfgaldalt
      181 rvnmqdqlld twnrerrtvi fithdvdeav ylanrvivma arpgrlhkii pvnlpyprte
      241 emrlspefae irnqvwhavy hqntrtn
//
LOCUS       WP_457664110             276 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457664110
VERSION     WP_457664110.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Somme,J., Van Laer,B., Roovers,M., Steyaert,J., Versees,W. and
            Droogmans,L.
  TITLE     Characterization of two homologous 2'-O-methyltransferases showing
            different specificities for their tRNA substrates
  JOURNAL   RNA 20 (8), 1257-1271 (2014)
   PUBMED   24951554
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..276
                     /product="RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=30279
     Region          13..253
                     /region_name="TrmJ"
                     /note="tRNA C32,U32 (ribose-2'-O)-methylase TrmJ or a
                     related methyltransferase [Translation, ribosomal
                     structure and biogenesis]; COG0565"
                     /db_xref="CDD:440331"
ORIGIN      
        1 magtnserel stegpaiila fpqlgenigm varamanfgl selrlvsprd gwpsekarsa
       61 asradhvidg aklyetleea ladlnfvyat tardrdgfkp vrspivaare lrqrfsvgqk
      121 vgiifgrert gltnaevala deivtfpvnp afaslnlaqa vllmsyewlk tgmasedetf
      181 fqpseqrpat keqlhglceh leealdarny frsadkkpkl venlravltr psfteseiqv
      241 lrgvissldr ftresprgsa appgysrkeh sggdkd
//
LOCUS       WP_457664119             301 aa            linear   BCT 27-JAN-2026
DEFINITION  S49 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457664119
VERSION     WP_457664119.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ekici,O.D., Paetzel,M. and Dalbey,R.E.
  TITLE     Unconventional serine proteases: variations on the catalytic
            Ser/His/Asp triad configuration
  JOURNAL   Protein Sci 17 (12), 2023-2037 (2008)
   PUBMED   18824507
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wang,P., Shim,E., Cravatt,B., Jacobsen,R., Schoeniger,J., Kim,A.C.,
            Paetzel,M. and Dalbey,R.E.
  TITLE     Escherichia coli signal peptide peptidase A is a serine-lysine
            protease with a lysine recruited to the nonconserved amino-terminal
            domain in the S49 protease family
  JOURNAL   Biochemistry 47 (24), 6361-6369 (2008)
   PUBMED   18476724
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Paetzel,M., Dalbey,R.E. and Strynadka,N.C.
  TITLE     Crystal structure of a bacterial signal peptidase apoenzyme:
            implications for signal peptide binding and the Ser-Lys dyad
            mechanism
  JOURNAL   J Biol Chem 277 (11), 9512-9519 (2002)
   PUBMED   11741964
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="S49 family peptidase"
                     /EC_number="3.4.21.-"
                     /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=32132
     Region          78..292
                     /region_name="S49_Sppa_36K_type"
                     /note="Signal peptide peptidase A (SppA) 36K type, a
                     serine protease, has catalytic Ser-Lys dyad; cd07022"
                     /db_xref="CDD:132933"
     Site            order(85,126,163,178,180,188..191,240,265..267,269,272)
                     /site_type="other"
                     /note="tandem repeat interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            order(105,112,138,204,206..210,238,242)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132933"
     Site            163
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132933"
ORIGIN      
        1 mrnypeiasr mfgtplmlhp skgdiiaraf gprvlgspda paqvaggeem gllgeklrda
       61 tdywgdavyk gpeliapgia lieiegslvn kgkwigkscg mtsyegisaq vrdcierddi
      121 kavvfevdsy ggevtgafdc aeqifelsqa kptiavltdh acsagyllas pcrqlvipqt
      181 gicgsigvis mhvdmsawla keglkvtilk agehkadfnp yeaipddvlq qelaeleelr
      241 vefaatvary ragrltqqsa latearvyrg qkavdaglad avarpsqvle afeaelsrta
      301 g
//
LOCUS       WP_457664120             176 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma carbonic anhydrase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664120
VERSION     WP_457664120.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..176
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18507
     Region          1..172
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mplyalgplr pqtptegsyw vapdaniigq veigedvgiw fgatlrgdne pirigartni
       61 qesvvvhvdp glpvtigegc tighraiihg ctigdnslig mgatvlngak igrnclvgan
      121 alvtegkefs dnslivgapa kvvrtlddaa veglkrsaeh yvknwqryaa qltlld
//
LOCUS       WP_457664121             300 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664121
VERSION     WP_457664121.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..300
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33158
     Region          4..300
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 magrsvtdlp apsltrhrkw wgllfvapav lffavfaifp igfgvylsft rydlltpphw
       61 iglgnytglf rdraflvaig ntmlfvfgat vpvwvlslwl alrfdrcfas rniwkslffs
      121 pvlpplvvva viwkvllhpn glvtglvgpi fgvteirwlt dpvlsrlvmi vvndwtmipf
      181 fsmiwlagla gvpddlrrag eldgasdkqi fflitlpllk ptavlvaals tinafqafvl
      241 qyemtpdrgg padanltlgl lilkygfqyf rmgeaaaasv llfavillvt aaqlwlgrqk
//
LOCUS       WP_457664128             250 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphodiester glycosidase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664128
VERSION     WP_457664128.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Gorelik,A., Illes,K. and Nagar,B.
  TITLE     Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme
  JOURNAL   Structure 28 (4), 426-436 (2020)
   PUBMED   32109365
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Das,D., Lee,W.S., Grant,J.C., Chiu,H.J., Farr,C.L., Vance,J.,
            Klock,H.E., Knuth,M.W., Miller,M.D., Elsliger,M.A., Deacon,A.M.,
            Godzik,A., Lesley,S.A., Kornfeld,S. and Wilson,I.A.
  TITLE     Structure and function of the DUF2233 domain in bacteria and in the
            human mannose 6-phosphate uncovering enzyme
  JOURNAL   J Biol Chem 288 (23), 16789-16799 (2013)
   PUBMED   23572527
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007847
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..250
                     /product="phosphodiester glycosidase family protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26936
     Region          9..249
                     /region_name="YigE"
                     /note="Uncharacterized conserved protein YigE, DUF2233
                     family [Function unknown]; COG3698"
                     /db_xref="CDD:442913"
ORIGIN      
        1 mplfsrafia gaallsagia apasaacrdv rhlgeayiac sfdpqtndlr iynkdragvp
       61 fssfralsle lrrrgqylif amnggmyqed lspvglhvee gteqtplntn pgwgnfhmlp
      121 ngvfhvdggk agviaaeayr lagikprfat qsgpmlvvdg alhprflpds dslrtrngvg
      181 vatngkvvfa askrpvrfhv fatlfrdald cpnalfldgt isslyapein rhdrlfplgp
      241 iiavvadfpr
//
LOCUS       WP_457664130             850 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Sinorhizobium medicae].
ACCESSION   WP_457664130
VERSION     WP_457664130.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..850
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95387
     Region          41..798
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mskgfddipf fdeepaprqa aaatggiaar amaardkaqr pdylsglnpe qreavealeg
       61 pvlvlagagt gktrvlttri ahilstgraf psqilavtft nkaaremker igvlvghave
      121 gipwlgtfhs igvkllrrha elvglrsdft ildtddvvrl ikqliqaegl ddkrwpakqf
      181 agmidtwknk gldpsqipeg darafangkg relyaayqnr lltlnacdfg dlllhpirmf
      241 ranpdvlkey hgkfryilvd eyqdtntaqy mwlrllaqrp rpsersasag pgdarqgqva
      301 aapdrapprs gdsvsaskqq qiniccvgdd dqsiygwrga evdnilrfek dfpgakvikl
      361 ernyrstehi lgaaahliah negrlgktlf tertnpedek vhvhaawdse eearavgeei
      421 eqlqrknhkl ndiailvras fqmrefedrf vtlglnyrvi ggprfyerme irdamayfrl
      481 vcqpaddlaf erivntpkrg lgdttvrtlh dyarardipm laaaseiiet delkakarks
      541 lfdvvadfrr wqtllettph telaeqilee sgytamwqad ksaeapgrle nlkelirsme
      601 afesmrgfle hvalvmdaeq nenmdavsim tlhsakglef stvflpgwee glfphqrald
      661 eggrsgleee rrlayvgitr akhrchiwfv snrrihglwq stlpsrflde lpiahvevae
      721 qeasyggysr gygqsrfdka dpfensyqtp gwkraqqhrs eatrdnwgtr sghsverigy
      781 gelgprtrti egelvakstt aepsrfnvgd rvfhikfgng niaaiegnkl tidfdragqk
      841 rvldgfvera
//
LOCUS       WP_457664132             288 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664132
VERSION     WP_457664132.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 288)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..288
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31489
     Region          31..288
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mrklttlhgr paserlgdaa lllislllai fflmpivwsv ansfkpaaea lanpvalfsk
       61 afslenyrrl edvgagwyvy aansvlialg tivltvliav pagygfakfr fpgqslifvv
      121 vmatmmipfq siltplflil kflglqnnlf glvlvyttfq lpfsifmmrn sfdaipsali
      181 eaaridgasq wallrrimmp lalpgvatva mfaflnswne flaaliflsd qnkftlpiml
      241 vnvssgiygi inwgalqagi tvtmfpcivl flalqryyvr gltagavk
//
LOCUS       WP_457664133             358 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664133
VERSION     WP_457664133.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..358
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39014
     Region          77..353
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mgsarssngp tpessrgras gapraprpat awlpirtaar rptsqlaegp rtlvstpkre
       61 qaraaraeaa drephgwlgl vfiapsmvfi gglfviplvm tawmsfyhwp llgrrkfigl
      121 dnyadtqlwq algftllytv lvtaailvva fplallvdrp lrntgifrti yfmpvvigfg
      181 aastlwmwll npdsgvfsrl llglgivdaa prplesfwpa lavvilmvvw ktagftmvil
      241 ltglqsipqe iaeaakidga nafsrfrrit lplmrnalll alvlnitssm lafdqffiit
      301 qggpenstis avfsiylasf ssyrlgygsa lsfallvvlv aissiqlsfm rqrpeegr
//
LOCUS       WP_457664122             824 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-mannosidase [Sinorhizobium medicae].
ACCESSION   WP_457664122
VERSION     WP_457664122.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Nascimento,A.S., Muniz,J.R., Aparicio,R., Golubev,A.M. and
            Polikarpov,I.
  TITLE     Insights into the structure and function of fungal
            beta-mannosidases from glycoside hydrolase family 2 based on
            multiple crystal structures of the Trichoderma harzianum enzyme
  JOURNAL   FEBS J 281 (18), 4165-4178 (2014)
   PUBMED   24975648
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..824
                     /product="beta-mannosidase"
                     /EC_number="3.2.1.25"
                     /GO_function="GO:0004567 - beta-mannosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005537 - D-mannose binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=92087
     Region          17..>646
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          751..811
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mssdtpnrda lridlsgdwl lasadnshal tialpgdvhs alqragiiad pyhgrneaei
       61 qwvarkewvl ertvvigadd lnggwyldfe sidtvasvfv neqlvltaen cfrryrpdvs
      121 daivagenri riilhsaiae gerrqaaqpf yvpyhdgnsp iangnmlrkp qchfgwdwni
      181 aiaplgvygs lalcrletar iehlttrqlw ledgsvdlqv tvqlfardpg ivpvyftldg
      241 vrerldcavg pgetrvthvf tieeprrwwp agsgdqafst lkvevpgetv trqigfrtik
      301 lvtdsdeags rfafkvngre vfcrganwip adalrsrvtp eavedllrsa vdanmnmirv
      361 wgggfyepdw fydlcdrlgl lvwqdfmfac nlypstpdfl envadevdyq vrrlsthpsi
      421 alwcgdnelv galtwfeesr kdrdrylvsy drlnrtveta mrracpeaiw wpsspsagyl
      481 dfgdawhadg agdmhywsvw henksfdnyr tvrprfcsef gfqsytsmpv irqfagerdl
      541 niaspvmeah qknaggneri agtmfryfrf pkdfpsfvyl sqiqqglair tavdywrslk
      601 phcmgtlywq lndtwpvtsw ssldfggqwk amhymarrff qpvavaaips aegsevaism
      661 vndtaepvtv elqaflvsld gerqpllava gtcspdraat lvaiaakdip sdmllfwsfe
      721 asngstgegh yvngtykald lapsgltvea vprpdgsfdv svkaaglalh vmieadiegr
      781 ysdnafdlta getksirfrp rvpvdagasp rfsaydletc qgkg
//
LOCUS       WP_457664135             302 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664135
VERSION     WP_457664135.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444039
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32940
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..293
                     /region_name="PBP2_PAO1_like"
                     /note="The C-terminal substrate-binding domain of putative
                     LysR-type transcriptional regulator PAO1-like, a member of
                     the type 2 periplasmic binding fold protein superfamily;
                     cd08412"
                     /db_xref="CDD:176104"
     Site            order(102,106,149,169,203,227,244)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176104"
     Site            order(104..106,109..110,112..113,126,128,136,139,215..216,
                     222..224,226..228,232..233,236..237,247,254..255)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176104"
ORIGIN      
        1 maftlrqlqy fvavaeqgsv traaqnlsis qssiteavke lesdlgvelf drhprglsit
       61 hnghqflrha tkiladvsda rrsfsdsrev rsgrlnlgvt slvagyvlsd llaryrracp
      121 gvevsaiedn gsylehllig geldvavmvi snlrdrmalq aeiletspyr lwlpighplv
      181 sadiisvedi areplimltv deieentgkl ltalgarphv afrtrsveav rslvatgagi
      241 allpdlvyrp wslegdries rdvsgalpvv qvgmvwrkgs slpqsardfv giaealrsar
      301 pr
//
LOCUS       WP_457664145             229 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664145
VERSION     WP_457664145.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..229
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25071
     Region          8..>214
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstsvrpktk frhsrlsarn rewiagylfv lpdalgllvf lglpmllslv lglydvdgfg
       61 ayrfvgmany tkmmrdplfw qsakvtalya lmlvpllyvc glslallvqk tnrfngvirs
      121 mffaphmvsl ivvalvwqfl vvdkigvlsr ltpalglggi sflgdpdyal ftvvavsvwf
      181 lmgyymlifl gglqdipamy yeaatmdgag piaksgtspc rclsprass
//
LOCUS       WP_457664146             530 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Sinorhizobium medicae].
ACCESSION   WP_457664146
VERSION     WP_457664146.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..530
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=57895
     Region          4..523
                     /region_name="ASKHA_NBD_FGGY_D-RBK"
                     /note="nucleotide-binding domain (NBD) of D-ribulokinase
                     FGGY and similar proteins; cd07782"
                     /db_xref="CDD:466800"
ORIGIN      
        1 mreyvvavdi gtgsaragvf dgrgrllara dqpiamnrpe enhaehdsed iwaavcgavr
       61 sarekaavpa esvaaigfda tcslvvrdrd gaplsvnrqg earwdtivwl dhralaeadf
      121 ctatrhqvld hsgkvmspem empklmwlkr nlphqwekag yffdladyms wratgspars
      181 rctltakwny lahekrgwqq dyleqigled llargglpee tlpveravgr lnasaaeelg
      241 ldaecrvapg lidayagalg vlggfagdka klerqlalig gtsscivafs kdmkpgfgmw
      301 gpyfeavlpg lwlieggqsa tgalldhivr lhggglpptt ethakiierv qelralhggp
      361 gfadrlhvlp dfhgnrspla dphalgvisg laldssfdal crlywrtcva ialgirhile
      421 mmkevgyeld tlhvtgghvr nsllmelycd vtgcrvvape tpdavllgta mtaavagkly
      481 pdlasagpam ssagkerlpd atrrrdydrd yrrflalyrh reelefdrit
//
LOCUS       WP_457664148             277 aa            linear   BCT 27-JAN-2026
DEFINITION  urease accessory protein UreD [Sinorhizobium medicae].
ACCESSION   WP_457664148
VERSION     WP_457664148.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Farrugia,M.A., Wang,B., Feig,M. and Hausinger,R.P.
  TITLE     Mutational and Computational Evidence That a Nickel-Transfer Tunnel
            in UreD Is Used for Activation of Klebsiella aerogenes Urease
  JOURNAL   Biochemistry 54 (41), 6392-6401 (2015)
   PUBMED   26401965
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Farrugia,M.A., Macomber,L. and Hausinger,R.P.
  TITLE     Biosynthesis of the urease metallocenter
  JOURNAL   J Biol Chem 288 (19), 13178-13185 (2013)
   PUBMED   23539618
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Characterization of UreG, identification of a UreD-UreF-UreG
            complex, and evidence suggesting that a nucleotide-binding site in
            UreG is required for in vivo metallocenter assembly of Klebsiella
            aerogenes urease
  JOURNAL   J Bacteriol 179 (13), 4081-4086 (1997)
   PUBMED   9209019
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Neyrolles,O., Ferris,S., Behbahani,N., Montagnier,L. and
            Blanchard,A.
  TITLE     Organization of Ureaplasma urealyticum urease gene cluster and
            expression in a suppressor strain of Escherichia coli
  JOURNAL   J Bacteriol 178 (3), 647-655 (1996)
   PUBMED   8550495
  REMARK    Erratum:[J Bacteriol. 1996 May;178(9):2725. doi:
            10.1128/jb.178.9.2725-2725.1996. PMID: 8626347]
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Park,I.S., Carr,M.B. and Hausinger,R.P.
  TITLE     In vitro activation of urease apoprotein and role of UreD as a
            chaperone required for nickel metallocenter assembly
  JOURNAL   Proc Natl Acad Sci U S A 91 (8), 3233-3237 (1994)
   PUBMED   7909161
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..277
                     /product="urease accessory protein UreD"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=29303
     Region          9..275
                     /region_name="UreH"
                     /note="Urease accessory protein UreH [Posttranslational
                     modification, protein turnover, chaperones]; COG0829"
                     /db_xref="CDD:440591"
ORIGIN      
        1 meaaaaiapq rawgkgrlva ktggartria glyqegcaki rlprtfdasm eavlinssgg
       61 vtggdrlawe feagegtnlt lttqacekvy kasvdtavva trisvaargh vdwlpqesil
      121 fdrsalsrsl evdlapdasf laleavligr kamgetvrsg lfrdhwrirs ggalvhaenl
      181 alagdiaalg srravldgav afatlvyvap dceallprlr tslaehalsg vshfavngrd
      241 kivarvvaad gfalrkilip lishlrkgas vprvwtf
//
LOCUS       WP_457664149             268 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664149
VERSION     WP_457664149.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..268
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29204
     Region          9..262
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mpeqlalpil etraasigyg arlilrdldl svpeasftvl lgpngcgkst llralaglir
       61 pqqgtvling ysismfprke laqrigllsq nqsapegmtv mdlvrqgryp hrtlfgrwtk
      121 eddeackeal avtdtadlag ekfdtlsggq rqrawiamtl aqrtsvllld epttfldlsh
      181 qidtlrlark lvrergvtiv avlhdlnqaa ryadnlvllk hgaivsegsp advltsdivk
      241 rvfdvdvtii teprtqapic vpvedadl
//
LOCUS       WP_457664150             328 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Sinorhizobium medicae].
ACCESSION   WP_457664150
VERSION     WP_457664150.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   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 328)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36262
     Region          9..307
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(17..19,51,56,81,123..124,153..154,173,201..207,258,
                     275..280,283,286..287)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(51,56,81,123)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mgvrklgsle vsaiglgcld mvgyygggpr drksmvslir aafeqgvtff dtaevygpyi
       61 seeyvaeala pvrdqvviat kfgfgveegq ptalnsqpdh lrravdgslk rlktdhidll
      121 yqhrpdpnvp iedvaeavkd liqagkvkrw glseasagti rrahavhpvs avqseyamww
      181 repetrifpt leelgigfvp ycplgrsfla gavnpsqrfe rtdrrhnlpr ftpealaanm
      241 alfdyvrdwa qrkkttpaqf alawilaqrp wiapipgttq yphlaenlga tgvqltadel
      301 reidaglari klqggradpf tesqfdys
//
LOCUS       WP_457664151             380 aa            linear   BCT 27-JAN-2026
DEFINITION  pectate lyase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664151
VERSION     WP_457664151.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wu,P., Yang,S., Zhan,Z. and Zhang,G.
  TITLE     Origins and features of pectate lyases and their applications in
            industry
  JOURNAL   Appl Microbiol Biotechnol 104 (17), 7247-7260 (2020)
   PUBMED   32666183
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Hugouvieux-Cotte-Pattat,N., Condemine,G. and Shevchik,V.E.
  TITLE     Bacterial pectate lyases, structural and functional diversity
  JOURNAL   Environ Microbiol Rep 6 (5), 427-440 (2014)
   PUBMED   25646533
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Marin-Rodriguez,M.C., Orchard,J. and Seymour,G.B.
  TITLE     Pectate lyases, cell wall degradation and fruit softening
  JOURNAL   J Exp Bot 53 (377), 2115-2119 (2002)
   PUBMED   12324535
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Yoder,M.D., Keen,N.T. and Jurnak,F.
  TITLE     New domain motif: the structure of pectate lyase C, a secreted
            plant virulence factor
  JOURNAL   Science 260 (5113), 1503-1507 (1993)
   PUBMED   8502994
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Linhardt,R.J., Galliher,P.M. and Cooney,C.L.
  TITLE     Polysaccharide lyases
  JOURNAL   Appl Biochem Biotechnol 12 (2), 135-176 (1986)
   PUBMED   3521491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..380
                     /product="pectate lyase family protein"
                     /EC_number="4.2.2.-"
                     /GO_function="GO:0016837 - carbon-oxygen lyase activity,
                     acting on polysaccharides [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41188
     Region          22..380
                     /region_name="PelB"
                     /note="Pectate lyase [Carbohydrate transport and
                     metabolism]; COG3866"
                     /db_xref="CDD:443075"
ORIGIN      
        1 mnsidrtsvl gaglllalgc mplpvaaqsd psretattgw atqnggtrgg ahaaasdvft
       61 vrnarelkna lttrvgqggr ivrvtglidv sqgrayktsa emesrakivl pprttligvg
      121 traelqeayv vvnsndviir nlrienpwdp qpawnpndge ngnwnsrfda vtidgawnvw
      181 vdhvtftdgr rtddqngmqn grpkqhhdga ldvrnganfv tisysifrdh eknnligssd
      241 gadgedsgrl kvtiyntlfq nisaraprvr fgqvhlynny htgsmanrvy pfshahgvgk
      301 esrifseanv fridgvkgcd kiagnyggrv yrddgsllng atlvcswnrq igwrppysyt
      361 plnaaevpan vlakagagnl
//
LOCUS       WP_457664155             396 aa            linear   BCT 27-JAN-2026
DEFINITION  calcium-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664155
VERSION     WP_457664155.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 396)
  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 396)
  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 396)
  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..396
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..396
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39397
     Region          <2..149
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          113..360
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mningtsvan kligtnladt lrgydgndvi wgdagddyld gglgndtlyg glgndfvkvg
       61 agddyaeggd gndsfdggag adtligglgn dtfsgedgnd iidggdghdh ilggpgndei
      121 hggageeyid aglgddiiya gsgndgfnnr idpatgkltq qavgggagnd tiygeegsda
      181 lkgqsghdrv yggigddivd ggdgnnyldg gdgndvldse ggidearggi gndriavggg
      241 ndlaygdagd dilsgaagdd ildgglgndl vtagdgndtl rgdagkdtll aeagsdilwg
      301 gadadrfvfk gagslvgrds vmdfqngvdl fvlenlgikq ysssgaagti yayndasgdv
      361 mlkgydsagn avtihvddpa nslaashfss adflfa
//
LOCUS       WP_457664156             252 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457664156
VERSION     WP_457664156.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..252
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25350
     Region          6..251
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtdaprilvt gagsgigaai arriaapgmr lllhtganve glrkvteeag akgaevatel
       61 gdlsdpavpg rlveaaraaf ggldqivsna graqrsafgq ltdadlqaaf dmmpmaffrl
      121 vdaalpdlrs saqarvvavs sfvahgfgtn gmhfpasgaa kaalealaks laaqlapegv
      181 tvncvapgft rkdngghaat ssaamesara vtpngrlgep vdvaelvafl lspgarhitg
      241 qvmhvdggll lp
//
LOCUS       WP_457664157             545 aa            linear   BCT 27-JAN-2026
DEFINITION  methyl-accepting chemotaxis protein [Sinorhizobium medicae].
ACCESSION   WP_457664157
VERSION     WP_457664157.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..545
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58462
     Region          3..535
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mprlansvyg tlglamvlfv aasallvgss fialerlrsd laatsslgke rlayrmiyaa
       61 shleraqgpa rgaaadelrq lmdqnerfle rlgsdrerig lattsdpaaf aqlervreqw
      121 rddvrpales aiaevpltha aldaldpkvr afaeqledli npieqagiar lkrsqllqlg
      181 fsilslllli hilrvvrrla rrtrtlagla ervstgdlgq kaavegtdel avlgasfnam
      241 ttrlaamids ergsrerlea llatisetaq hlsssaaeil agatqqvegm reqssavaqt
      301 vtsvdevlqt seqaaqraqq vaasydnavk isnegrrald dtvrvmnavn arteaiaadi
      361 lslaenslei geivsvvaei adqtnllaln aaieasrage hgrgfnvvat eirtladqsk
      421 satarvrril meiqkstnsa vigaedgsks vsraletvse agetirqlea ivadsarsva
      481 qiaasagqqr agmkqiheam hyieqtssqn lsairqaeea akdlnelgsr lkemltdhgn
      541 dhdnt
//
LOCUS       WP_457664160             592 aa            linear   BCT 27-JAN-2026
DEFINITION  arylsulfatase [Sinorhizobium medicae].
ACCESSION   WP_457664160
VERSION     WP_457664160.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..592
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65390
     Region          52..481
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,316..317)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(60..61,101,154,156,262,317)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 mkpisesrlg ataaaiarsq gwkafalagt ilvssvvtts spasaqdapg kpnilvifgd
       61 dvgqfnlsty sfglmgyktt nidriadegm kftdyyaens ctagrssfit gqtpkrtgls
      121 kvgipgapvg lqdrditiaq alkplgyatg qfgknhlgdr deylptahgf deffgnlyhl
      181 naeeeperpy wpkddlayvk ansprgvihs yadgriedtg alnakrmeti ddettsaaie
      241 fmkkqveqkk pfftwmnttr mhvfthvrps mlgqsgmpgn eyadgmiehd ghvgkllkal
      301 ddmkiadnti viyttdngpn qfswpdaatt pfrsekdtnw egafrvpami rwpgkikpga
      361 vsnemfsgld wfptllaaag egdikekllk gtdvagkqfk vhldgynqlp yltgeteqga
      421 rqefayfndd gklvafrykd wkavfcemka pggfrvwyee fdclripklf nlrmdpmera
      481 dtvsdqyddw riknaymmgw mtfhaaqfle tfvdyppsqt pasftidqie adverrsaek
      541 aggeqivhga crlsstrpis ssgasplpar ssgsttrsnl qdgsspqthk np
//
LOCUS       WP_457664161             353 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457664161
VERSION     WP_457664161.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..353
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39812
     Region          4..340
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 mtlkrlsigt fnlynlnepg lsiytdktgw sqeeydrkie wtsrtirllq pdifgfqelw
       61 hsasieralt qsgiagdydl ivpenadgkr ivcaaivrkg lmisepqwik rfpekftlks
      121 sgddpqtpai tvsipsfsrp vlhfsvrpre dhepihvyvc hfkskgptkv fqedwfeadg
      181 alykkhatsi gaaistirrt aeaaalrfil teqmkgtrtp vivlgdindg qhsntanilt
      241 eqprylvgds lgggdvslyt aqtlqeyrst rdvyythvhq dimesldhil vseefydnsr
      301 rrvwmfdgmt vnndhlnsdd hkeagtsdhg vicatfkyrp ikaeaqeian gta
//
LOCUS       WP_457664162             334 aa            linear   BCT 27-JAN-2026
DEFINITION  Ldh family oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457664162
VERSION     WP_457664162.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Cendrin,F., Chroboczek,J., Zaccai,G., Eisenberg,H. and Mevarech,M.
  TITLE     Cloning, sequencing, and expression in Escherichia coli of the gene
            coding for malate dehydrogenase of the extremely halophilic
            archaebacterium Haloarcula marismortui
  JOURNAL   Biochemistry 32 (16), 4308-4313 (1993)
   PUBMED   8476859
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Honka,E., Fabry,S., Niermann,T., Palm,P. and Hensel,R.
  TITLE     Properties and primary structure of the L-malate dehydrogenase from
            the extremely thermophilic archaebacterium Methanothermus fervidus
  JOURNAL   Eur J Biochem 188 (3), 623-632 (1990)
   PUBMED   2110059
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..334
                     /product="Ldh family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34664
     Region          8..329
                     /region_name="Ldh_2"
                     /note="Malate/L-lactate dehydrogenase; pfam02615"
                     /db_xref="CDD:460620"
ORIGIN      
        1 mklqptglre lavtllerrn aptesarlqa dllieaelrg lpshglqrlp lilsrldkgl
       61 adarargsgi wrrqaflsmd gerglgpvvv lnamrimrsi lgetgiagaa irnanhigml
      121 ayyaeaaard gligivmsts ealvhpfggt eamlgtnpla igipsgdrpf vldlatsvvs
      181 mgkinnhamr dmpipegwav dgegrpttdp haakagaiap fggakgyglg laiellvaal
      241 agsdfapdvh gtlddthpan kgdllvlidp agasgtlgpl aayldrlrls rpvnpaspvt
      301 vpgdgararr aataeagidl pqplyehlma leaa
//
LOCUS       WP_457664165             885 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664165
VERSION     WP_457664165.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..885
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=96174
     Region          <1..883
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlldregplk allasarsaa lghgstvvve geagigkttl lrefaehsdh gcrvlwgwce
       61 alitpcplgp lqdmgqllda rvaallnqaa sperlfpavl nalqhasdpv ilifedvqwa
      121 dnatldliky lgrrisllpt vlvlsfrsde igadhpltrv lgdlpsasvs rltlqplspe
      181 avaalteqag rcaddlyqvt agnpffvtel lasktgpgri phsvrdavwa rlsrltager
      241 kalevisivp ggvepwlvra llgveadill dqcltrgllr rddqgavmfr helarqatvd
      301 rlppslqksl hskveaamsq hvttqapall arrvhhaaga gdgervlela pqaaahaarl
      361 sahreaashl atalryvaqa apeqaaqlye dwayeaglal lvyepvieah hrviaiwrel
      421 grtekigpnl crlsrlhwrr gegeaaedca aqavcemekl ppgpelamay strsqlrmlh
      481 yrfdeaiewg lralaladql geietrihal nnvgtallfa grpggrerle etlalalahg
      541 fhdhavrayt nfaecavvsk efglaerlla egiafatrhd ldtaahyllg rqaelrmeqg
      601 rfreaetiaq gvmnlerlpm vmhlpaltvl grvhmrlgep ggmallhnal qeglatgelq
      661 rivpvrsalt eaawlhedyg acqeqltala aidlncfraw dfgelavwwr rcgmamplpi
      721 pnaqiplpha aelhghplaa akewdrlglp ydaalalmqv rgvdagpala ravtifesle
      781 arpaaalart qaqrlgvagq lpkarrgpyg aarrhplglt rheqqvlali aagmsnkeaa
      841 qllsrsprti ehqvsavlsk fsaasrmevl lrlrgepwll atdst
//
LOCUS       WP_457664167             257 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Sinorhizobium medicae].
ACCESSION   WP_457664167
VERSION     WP_457664167.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..257
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26675
     Region          1..249
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 meefllfalv gflaqaidga lgmaygviss tvllalgvpp aqasasahaa elfttaasgs
       61 ahlyhrnidw klfwrlvpfg vvggmlgafv vtsfdgdqvk pfvtaylavi gawllyrsfh
      121 riptkpvklr ivaplgavag fldaaggggw gpvattgllg aggqprfvig tvsaseflia
      181 lsvslsflat iltghweqag efrdylasig gliigavmaa plagwavkal rektllrlvg
      241 smivllagyq tleltgf
//
LOCUS       WP_457664170             412 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Sinorhizobium medicae].
ACCESSION   WP_457664170
VERSION     WP_457664170.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44989
     Region          1..402
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mndrftlalt gqslikhdir dirtpafqdi qsllrqadls ftnfegtilg thggwplkgs
       61 ffgcsdpavl dalgaigfqa lslsnnhafd lgpsgvlstl eevekrgffh aglgrnarev
      121 srasiatinq rrialvamdg gpgpdfmyaa dadenrperp gvnrlrlsql levddlafeq
      181 iravrdkigy taidlandsq pddpprldpq aevaiarsvf krsdrygrgv ridevdmarn
      241 laaiasaard salviaylhh hhwasdwyql pewvsgvakr cidagasmfv shgapvlqpv
      301 eiyrgrpify slgnfifhvr sekstwtaae vwesvvgvcs fasdnslidi sfhpvvigge
      361 dgledgvler rlvpqlvtgd savrilgrlq eqsarlgahi eisgnvgrlq ar
//
LOCUS       WP_457664172             239 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664172
VERSION     WP_457664172.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25915
     Region          <16..226
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mspspcervk rllswgesgs gkstlsrill glsplsegrv lcfgkdigsl srreraarmq
       61 pvfqdpyssl nprhtlaeiv aapllargea rasalnratg fleevglgsa yarrrpsals
      121 ggqrqraaia ralianpeil vcdeptsald vsvqaqilnl lqqqrrerkl svllithnig
      181 vvahmadrva vmrhgeivet gsvrdvllep redytrllis svpdlhgglh serpwdaap
//
LOCUS       WP_457664173             394 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664173
VERSION     WP_457664173.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 394)
  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 10009251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..394
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43239
     Region          1..334
                     /region_name="COG5397"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444156"
ORIGIN      
        1 mlktvdliyq tmlaeigqra mddawtldfp pigrfvkvtv kereywyfdq sdgeggqkrk
       61 yvgpaedpei skrvedfsrt ksdyrirrrl vssltrdggl laadrtsgli vetlaaaglf
      121 rlrtvlvgtl afgtysgllg vrmpsaaimt gdadfaqyya isaevmdslp pilellqsad
      181 ptfravptfd ggattafvng egyrvefltt nrgkdeyldk padmpalgga saqplrfmdf
      241 lirepvravl lygagvsvlv pdparyavhk liiasrrhar salkrdkdlv qaailveall
      301 qtkrspdlam ayveawkrgp asqeaieiga amlsvehkdr lrecleagga gnrregdfav
      361 lrshgsskmv irsfitpevk vgsssrpqri tktn
//
LOCUS       WP_457664182             350 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Sinorhizobium medicae].
ACCESSION   WP_457664182
VERSION     WP_457664182.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..350
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36676
     Region          7..330
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msedavdlvi igsgpagmaa aceagscgls vvlldeqtei ggqiyrrves apqkllgilg
       61 qdyaagqlla sdfrnsgary fggatvwnvt tegvvdyvan grageitgkf vllasgamer
      121 pfpiegwtlp gvmgagagqi mlkgsgalps epvvlagcgp llyllawqyl ragaeiaaiv
      181 ettqrsayfr alrqtvgalm gwrdlakglk lvsairrtgv pvysgardla iegtthaegl
      241 rftvngkamh vaaslvllhq gvvpntqlsw stgtdhrwde eqlcwkpvtd etgrmgdtql
      301 yvagdsrgiv ganasavqgr laalaiaeql glkrspppdh epesrpstph
//
LOCUS       WP_457664183             324 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664183
VERSION     WP_457664183.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..324
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34836
     Region          5..275
                     /region_name="PBP2_polyamine_RpCGA009"
                     /note="The periplasmic-binding component of an
                     uncharacterized ABC transport system from Rhodopseudomonas
                     palustris CGA009 and related proteins; contains the type 2
                     periplasmic-binding fold; cd13589"
                     /db_xref="CDD:270307"
     Site            order(12,151,210,236,238)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270307"
ORIGIN      
        1 mtqdtmyvgg ysgdfqtmfe keiapgfeak nnvkivyvag nssetiaklq aqkgnqeinv
       61 alvddgpmhq avqfglcdal aeapvyndiy dvakvsvfgg kavgvglvat gitynkklfd
      121 engwpaptsw ndltdekfaq rvtsnpisgt fglntlvmfa rmngggekni epgfdairdk
      181 lapnvlswss snaqlaqmfq ngdidlgvwg snravalkkt gfpvefvyps egapaivasa
      241 csvagnrlpe ksqallqyla spevqakfas qgfgptnska klegalaeev pygaeklskl
      301 vnvdwdtinq nraewtkqwt rtve
//
LOCUS       WP_457664194             105 aa            linear   BCT 27-JAN-2026
DEFINITION  c-type cytochrome [Sinorhizobium medicae].
ACCESSION   WP_457664194
VERSION     WP_457664194.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007442
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..105
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11399
     Region          27..103
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mkricglrca atvalllmvt resaavdqlr gralahrwcs echvvapgqs hgsdtvptfa
       61 qigeserfde rslsaflatp hhsrmpnlsl traeiadlva yikar
//
LOCUS       WP_457664196             225 aa            linear   BCT 27-JAN-2026
DEFINITION  BON domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457664196
VERSION     WP_457664196.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..225
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=24658
     Region          3..145
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          79..216
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mdndvplrqd ildelqyeps idaanigvav engiatltgh vrsyaekhaa eriaervkgv
       61 raiaeeievr lpehkktadd eiagrvlkil awgaaisdpe diyvkvekgf vtlegavdwh
      121 fqrsaaensv reltgvtgid nqlrirprmn vvdvrhgire alkrnaetea enidvevsgs
      181 hvilhgkvqs lrarvmaera awsapgvtav edrlriedar valga
//
LOCUS       WP_457664198             399 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Sinorhizobium
            medicae].
ACCESSION   WP_457664198
VERSION     WP_457664198.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..399
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43686
     Region          38..396
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 msvvkrrlai wggliallaa giayalrpqp iqvdlavaei gvlrvtldee getrvrdvyt
       61 lhaplrgqlq risaevgddv kagetqlaqi epalpafldv rieaelqaav eaaraahnla
      121 aaelnkakad ltfaegerar arqlierrti sqrtledaer synvaqanla taeaalkvre
      181 helhqarsrl lsrqeirslr edcecmpvta pvsgvvlqvl rrsegvveag tplldigdpa
      241 dleivvnfls edavritpgq raiitgwgge dltavvrrie pfgqtevsal gieeqrvdii
      301 ldfadppkrw rslghgyrvd vrvilfegkv ltlplgalfr qgeewavfva aegrarlrpv
      361 avgqrnslev eireglvpge pvilypsdri kdeaaiver
//
LOCUS       WP_457664199             787 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664199
VERSION     WP_457664199.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 787)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..787
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85564
     Region          131..368
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          543..786
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mssldrklvr elwrlkaqvl aialviasga allimaltti ealeettaay yertrfadvf
       61 aqakrapehl grdiaeipgv rlvetriveg aildmpgfae pvvaqllslp ergpellnal
      121 virsgrltdp arpnevvvse pfaeahdlkp gdsfsavlrg rkrtlqvvgt alspefvyai
      181 apgglmpdde rfgvmwmghd avtaafdlka sfnsvtlgll pgadekdvir rldgllapfg
      241 gigaygradq tsnwflesei aqqknmsrim ptiflavaaf ltnmviarli eterheigll
      301 kafgysnlai gwhyakmvlv igtigiligs llgawlghwn telytkfyrf pfllyrpgpa
      361 gfviagaisl gaalagslaa vrraarlapa eamlppsppi yrrswasrta lagaldepsr
      421 miirriirwp vraflaslgl amsiavlima lqwvdaidal aetafergqh qdatvafndl
      481 lpihtagdyk hlpgvlaaep yrhasarish ghlverqgii gvppgailsp vfdvergrid
      541 vppgglvlsr klaellqvsa gdsvgvelle grqarlslpv aqvfetylgt paymdmeeln
      601 rlsgdgrvas glhilvdaps rtsllaklkd ipnvaavlfr qaaidtfyqt mgetififvg
      661 ffvafsmtls vgvtynsiri alserarela tlrvlgfsrw etsyillgev giltwiaipf
      721 gaivgyglaw ymtsafetel yrvplvlrda tygkaalial aatlvcaafv rrrldrldli
      781 avlktre
//
LOCUS       WP_457664203             633 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium transporter Kup [Sinorhizobium medicae].
ACCESSION   WP_457664203
VERSION     WP_457664203.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 medicae"
                     /db_xref="taxon:110321"
     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=68524
     Region          1..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 madsldhapa qanslpqfla ltigaigvvy gdigtsplya frealrpfgp ggvgrdevig
       61 lvslvlwtlt aivtikyvlf llradndgeg gtlsllalll kkgtkypvlm ffagilgaal
      121 figdamitpa lsvlsavegl klvapalddy vlpisvviil llfavqsrgt gavsvffgpi
      181 tlvwflvmaa agvshigddl ailsafnpln aigflwnagl tgfivlgaif ltvtgaealy
      241 adlghfgrlp iqvawfavvf palalnylgq galvlshpda lsnpfflmfp twallpmvil
      301 ataatiiasq svitgafsli rqaihlgflp rfeicytset qtgqiylplv ntillagvla
      361 lmlmfgssea lapaygvsit gamvidtila fefvrrqwgw paltaiavll plfslelvfl
      421 ganllkvhhg gyvpiliagt litmmwtwrk gvsllrekta rqdiplsqfm amverkseha
      481 pvdvpgtaif ltatpdttpa vllhnikhnh vlhqhnvimt iktarvpyvp ekdrytitkl
      541 sdrfsllelr fgfmddqnvs ralarcrkqg fkfeimstsf ylgrrkliad pqsglpqwqd
      601 klfiamansa idpteyfhlp anrvvelgeq vii
//
LOCUS       WP_457664204             201 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457664204
VERSION     WP_457664204.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Perraud,A.L., Weiss,V. and Gross,R.
  TITLE     Signalling pathways in two-component phosphorelay systems
  JOURNAL   Trends Microbiol 7 (3), 115-120 (1999)
   PUBMED   10203840
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..201
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0140299 - molecular sensor activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22301
     Region          <2..139
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
ORIGIN      
        1 mggahypvas ygfsqefgdy lrnlplepgr gtivgrtlle vgpvqvadvl gdpeytmseg
       61 qrlggfrtvl gvpllregsp igvlaltrst vrpftekqve lastfadqav iaienvrlfq
      121 evqarteels rslkdlrtaq drliqaeklq lsykaagddr rfyfekccrk rvltsnskte
      181 ktsptpdqtq wlnthngerp d
//
LOCUS       WP_457664206             394 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate/propionate family kinase [Sinorhizobium medicae].
ACCESSION   WP_457664206
VERSION     WP_457664206.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     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=41853
     Region          6..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdalpvvnag ssslkfqvfg ivgmdltrqi rgkvdgigtr prlqataadg tqlidqtyda
       61 kavrdlpaai tearrwlltl egfelqavgh rvvhggpdyt rpvlidatvl dhlagyqdla
      121 plhqpnnlap irlameinpd vpqvacfdta fhrghakhtd cyalprsfyd egvrrygfhg
      181 lsyeyiaerl revssraakg rvvvahlgsg asmcglrdgr siestmgfta ldglpmgtrp
      241 gqldpgvvly lilqkgmkaq avsdllyhda glkglsglsn dmrdllasdg phaalsvahf
      301 vyrcvlnggm laaalggida fvftagvgen sppirarive glawlgaeld paaneagaal
      361 istatsrvav hvlptdeelm iarhtlalis apna
//
LOCUS       WP_457664207             506 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457664207
VERSION     WP_457664207.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 506)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..506
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=55070
     Region          <3..490
                     /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 mkpahrtefl tvpgmaayri tpltsnftev dpaaalalgl aiaivalivv gagmasylid
       61 tdvrahsqqq lcymaahdal tglpnrisft drlidvlhea rgsgrkfavi gidlnrfkei
      121 ndtlghsagd ealrivsrrm aqsldsdefv arlggdefaa vktcgtkkev safadrlaei
      181 fdrpirvgni evtvgasmga aiwpddaeap delvnnadla myhakhtfld vpcfydsgig
      241 asvrkrrqlg ealrhaleqd elaihyqvqk slstgevqgy eallrwthpq lgpispsefi
      301 piaeenglvr slgvwvlrra cmdavtwdkp crvavnvsav qfmdanlprl vhevlietgl
      361 ppqrlelelt etalikdkgr slhiigqika lgvglalddf gsgyssletl rsfpfdkikl
      421 drafvdgies drqskaivra vlalgksldi pvlaegietd eqmsvlrleg cdegqgyllg
      481 rpspigdlaq nrqpaqsdtp rhqrva
//
LOCUS       WP_457664211             195 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664211
VERSION     WP_457664211.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..195
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21693
     Region          2..172
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mytpgeliva hgesgrdvff ilegrarvtl fsengreify gdrgpgdiig evsaidgkar
       61 sasvvalept raarlpapaf rrlvtdhpdf swallehlss girhmtdrvy efstlvvrrr
      121 lilellrrad drdestsrvf idpapthfel aasisthrea vsremsvlak ggphremrtq
      181 apavrpycsg iarrr
//
LOCUS       WP_457664208             243 aa            linear   BCT 27-JAN-2026
DEFINITION  MHYT domain-containing protein [Sinorhizobium medicae].
ACCESSION   WP_457664208
VERSION     WP_457664208.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Galperin,M.Y., Gaidenko,T.A., Mulkidjanian,A.Y., Nakano,M. and
            Price,C.W.
  TITLE     MHYT, a new integral membrane sensor domain
  JOURNAL   FEMS Microbiol Lett 205 (1), 17-23 (2001)
   PUBMED   11728710
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..243
                     /product="MHYT domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=26145
     Region          6..>195
                     /region_name="MHYT"
                     /note="MHYT domain, NO-binding membrane sensor [Signal
                     transduction mechanisms]; COG3300"
                     /db_xref="CDD:442529"
ORIGIN      
        1 mmtvmscitn ehnlllvsva alvclfgsai tlrllnravs asggqrfgwq flaavagggg
       61 vwtthfvavl ayepsapvsf dpvltllslv iamgglvasf svsgiranrm faplggavvg
      121 lsysamhytg mfaysvmglv ewqlgyvvas illpvlcsav avalvsrpdl raqrfwmavt
      181 lfvmgivglh ftgmgdcqef cavghddeke riitwlsrkn fwtsswldvi hprfsartvc
      241 wti
//
LOCUS       WP_457664212             252 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Sinorhizobium
            medicae].
ACCESSION   WP_457664212
VERSION     WP_457664212.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..252
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28472
     Region          2..243
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mmqtgifsgy fpygleetar kiraldfntv qldmhfkdme lsagqitkek cirireafrd
       61 nnlpiscisg ytniihpdka ererrvgylk eiishaqylg tpyvnnvvgs veetvkmfaq
      121 vdhpglgllm dptnyfethn idrmddilnq vfdtlsdkik iahakdvkrs gddktekhad
      181 igdedalesh tfrgvgeiel papglgslny dlylrrlakk hpnvpmiieh ldesdvprak
      241 kfldgklral gl
//
LOCUS       WP_457664218             356 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457664218
VERSION     WP_457664218.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10116212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..356
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=39936
     Region          108..213
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cd02440"
                     /db_xref="CDD:100107"
     Site            order(108..114,131..132,156..158,185)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mvdrltiehw rnaprltcla affettasgq ggapdlaqpq ldmslldfdl evsvfsdthr
       61 rlwgpfdshy fasipyrlee ecrlgaails fasrawarsa spttiytlgt gtgclartla
      121 tlgngrieal ccsptaanrt sffakraseh ahffhgpffe ldderyatdd dllpfrggfd
      181 vlledttfqm ydrdrlkqle fvvprirpgg llvqvqklah edrdiyeere rqkdevfksr
      241 ffstghiskk kdevlntmtd lqvdlattva alraffrysv ltwnsgnfyt ivssnsrssv
      301 lelislmvkp aippgycher lpativdtev ealaadltwr santmvplap klgimk
//
LOCUS       WP_457664216             511 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Sinorhizobium medicae].
ACCESSION   WP_457664216
VERSION     WP_457664216.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..511
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53985
     Region          107..>498
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mgplfrnsgf plyheamlfv rmrpqqrqas featftaars plssglqala fyeraglvkr
       61 itplseeaph yasrmlvrsa rnarvkpell gapgngaegw sasalnlsaa vdertpggaa
      121 slvelasdad lrelqlalag dpsvasvsrv prryltakms rksskpsaag rertatappp
      181 ahtmwnlrki nwqeardlng fndaseikva vldtgidagh pdlkdqiagy iyehpdlpga
      241 ssdqdlighg thvagtigat inndvgingi sqarihawki fddrpdllth pdgtaefayf
      301 vdpvmylral ldcvdagidv inlsigggga pdptesaafe allaggtsii aamgnerreg
      361 spisypaamp gviavgatnl qdritsfsnr gnhvaiaapg daiwstlpty pgqtawraek
      421 gpdghwwqgk aairetdyda wpgtsmaaph vaaaaalfia nggdrdpaai rdalvasadk
      481 vpamggqdft pdfgygrlnl krliagigtn d
//
LOCUS       WP_457664220             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664220
VERSION     WP_457664220.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35971
     Region          6..325
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtkplqktpa ltvdhlvktf dvsapwlnrv verkprqylq avndisftvp aggclsivge
       61 sgcgkstvar lvtglhrpts gamrfapgks gaalsaqmif qdpyaslnpr wrvknivaep
      121 lremklrkta aevterveel lhtvglspsd gekfphefsg gqrqrisiar elasepeflv
      181 cdeptsaldv svqaqvlnlm rrlqdelglt ylfishdmsv vrqmsdriav mylgriveeg
      241 dteqlfaepr hpytqlllqt ipniaapnrn repasgevps plkppsgcaf hprcpvaigr
      301 cskevpevrv lpngtrvach lvedglak
//
LOCUS       WP_457664224             491 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664224
VERSION     WP_457664224.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..491
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53901
     Region          4..435
                     /region_name="SsnA"
                     /note="Cytosine/adenosine deaminase or related
                     metal-dependent hydrolase [Nucleotide transport and
                     metabolism, General function prediction only]; COG0402"
                     /db_xref="CDD:440171"
ORIGIN      
        1 megllllhgm ivtvddkrqi iedgalaven dkivdigtsq alaprhagkk midcrgkmii
       61 pglidahgha ghalirsiga dtnslwmriv tptyyhyvtr dywyadglvs glerlragvt
      121 tsasivtsmp rsddpvfain harayselgl reiicvgpag lpwpqsvtrw esgkperrsv
      181 sfeamiegae avieslngts egrikvfltp ftivpsveps nastpdfavn lteddrmqar
      241 riretackwg vrihsdafag qirmawqdre nallgpdvhl qhcwgishee idilaetgth
      301 vthappgrst pvmqmmargv svaitsdgaa psrhfdmlqi artaqatqhi lhnhdryilp
      361 pgkifemiti daaraigmdh eigslevgkk adiavidmlk phltpnwmpv hrlihqvlgs
      421 dvdtvivdgr iimeegkvlt admyealafg eaeakalver aglqahmhdp gwgqlhrtfe
      481 rpvplptppd c
//
LOCUS       WP_457664225             203 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457664225
VERSION     WP_457664225.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..203
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22645
     Region          35..146
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mgiysdvilp klcdlsmrnv rlhpyrkrvv gaaegrvlei gsgsglnlpf yrrdvreila
       61 lepdpallam arrvphteip vnfmeasaea iplddnsidt vvttwtlcti pgaaaaltem
      121 rrvlrpqgkl lfvehglspd rgvrwwqdrl tpiwgrisgg chlnrpirsi ienggfridr
      181 ietgymqgpk pmtfmyegsa rpe
//
LOCUS       WP_457664233             326 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664233
VERSION     WP_457664233.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34301
     Region          36..319
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mkrflkiyld kpelaglall ivlvlvfqak sngillsfen irgvmgllpe ialvaigvtl
       61 lmicgefdls vgsvfalmpm smavilnsgv pftaavllgl micgavgfin gyvtlqfsip
      121 sfittlgmlf iarsltivis ggfppllppd lptwlftdyi ggspfrmsfl wfvviaalva
      181 allsltnfgn wiratggfne aaasmgipvk rvkiacfmlc svlagfagll qvlrlgsplp
      241 sigeglelqa vaaaviggta laggigtvfg aivgtllirt idnglvlsrv danwfkfaig
      301 vltmfavian awmgkmsrki kveahk
//
LOCUS       WP_457664230             305 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664230
VERSION     WP_457664230.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..305
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33692
     Region          9..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtlvlennaa rprskrtkrp glwlmlpaaa amllafgapl ifsawysftr wslvrpasks
       61 efvglsnytr vltdhecwqa igvtltyaas avtiecilgi alalllnkqm fgrgifrslm
      121 lipmvmtpav vglfwklffe esdglfnyfl taaglpalpw lgvsmalvsi vildvwqatp
      181 ffmlimlagl qsmdrnivea aeidgasrlq vfryitlphl vpyimvaaaf riigaladfd
      241 kiylltfggp gnvtttvsly aynrgfkifd igqttaiswl fiilvltita pliwhllrgs
      301 starh
//
LOCUS       WP_457664235             230 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664235
VERSION     WP_457664235.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..230
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25605
     Region          25..226
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mkesnllsdl aahlfssssg ngrtpserel aehftvsrgq vrealailea mriverraks
       61 giylttteas veaialfara gvpldpiviy etvelrkihe ikaaelasar ateenyerlr
      121 eilaaserki aageglared rdfhleivra tknsvfhrvc svyytmgekr lpiyfadldr
      181 srrshdehir iyeallardg nlaqalmnah lqgaesywkg lisgpatvve
//
LOCUS       WP_457664237             226 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664237
VERSION     WP_457664237.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25056
     Region          20..226
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 metlqltssd wttllgsrff vrlprstvea ileetrlsty eehdvlfhqg dsigdvffvl
       61 sglirlyrvg kdrreadvtv lskgemfaen aiylgratas aeaaeasvia ridssklrki
      121 aaadpdvaqa fiehlchrgk mtedmlaqdr lltatqrvas yilshcpngt ntsfsfrlpf
      181 qknilagklg vapealsraf stlrqsgviv kgrmieihdr halerf
//
LOCUS       WP_457664239             226 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664239
VERSION     WP_457664239.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23628
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar paedrfaavd warapngcpi faqvaawfec
      121 sihnvieagd hvmmvgrvta fessglnglg yarggyftpg anssaaggei gavavlerha
      181 alfplgdqnl vlpsysagsg dpaktlasql ersglsvhdw fslldl
//
LOCUS       WP_457664241             229 aa            linear   BCT 27-JAN-2026
DEFINITION  mandelate racemase/muconate lactonizing enzyme family protein
            [Sinorhizobium medicae].
ACCESSION   WP_457664241
VERSION     WP_457664241.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Gerlt,J.A., Babbitt,P.C. and Rayment,I.
  TITLE     Divergent evolution in the enolase superfamily: the interplay of
            mechanism and specificity
  JOURNAL   Arch Biochem Biophys 433 (1), 59-70 (2005)
   PUBMED   15581566
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Babbitt,P.C., Hasson,M.S., Wedekind,J.E., Palmer,D.R.,
            Barrett,W.C., Reed,G.H., Rayment,I., Ringe,D., Kenyon,G.L. and
            Gerlt,J.A.
  TITLE     The enolase superfamily: a general strategy for enzyme-catalyzed
            abstraction of the alpha-protons of carboxylic acids
  JOURNAL   Biochemistry 35 (51), 16489-16501 (1996)
   PUBMED   8987982
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..229
                     /product="mandelate racemase/muconate lactonizing enzyme
                     family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24965
     Region          <2..224
                     /region_name="MR_like"
                     /note="Mandelate racemase (MR)-like subfamily of the
                     enolase superfamily. Enzymes of this subgroup share three
                     conserved carboxylate ligands for the essential divalent
                     metal ion (usually Mg2+), two aspartates and a glutamate,
                     and conserved catalytic residues; cd03316"
                     /db_xref="CDD:239432"
     Site            order(38,53,87,113,139,162,189,214)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239432"
ORIGIN      
        1 mrgdvklyan gwnhehddvv nwakaaarpl adgyralkay pfayelpdgt frhvsarmld
       61 dgrfrqaier vkalraevgp dielmldlsg glcddqllrf ldvcrdldit wieepldpfn
      121 ltglsrvaar sgipialger vygrggfrnv ldtgavsivm pdiancggml eavqiagmae
      181 tynvrvsphn casslctaas lslcvaipna mnlevypyfa elehlrpga
//
LOCUS       WP_457664242             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664242
VERSION     WP_457664242.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36200
     Region          1..329
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mstppliear titqrfgarp dlaakialgl klakpapvvh aldgvslsir ngevvglvge
       61 sgcgkstlgr viagiatptg gsvfwkgvdr ntmsaaeqke aglatqmifq npmaalnprm
      121 tieeliweap kthgmatate rasyvdnylt lagfdpsmkt ryphqfsggq rqrvniaral
      181 avqpkflvcd esvaaldvsi qaqvinlfmd lrerldltyl fvshdlgvve hisdrvaimy
      241 lgriveqapv edvfrrpnhp ytrallaevp rietgkrrfk avegelpspl dppkgchfhp
      301 rcpfamercr vevpvrkeia pkhlsachln g
//
LOCUS       WP_457664244             377 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664244
VERSION     WP_457664244.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..377
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40930
     Region          17..373
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mpsaplnsgg kvvtleaagq wtlirqrflr hkiaafaagi ilvlyligaf aeflapglpn
       61 asrpqytfap pqrislftht dnagtrflph vkgykieiep kalrrsfvvd eakiipigff
      121 vkgapyklwg vipmethlvg pldarepmyl lgsdrlgrdl msrliygtrv smsiglvgva
      181 isltlgvvmg avsgyyggwv dtliqriiei vsamptiplw lglaaaipls wsplsvyfmv
      241 tlivsllswt glarevrgrf falrgddfvt aarldgager riifrhilps ltshilavvt
      301 laiptmivae tslsflgvgl kppvvswgvl lqdaqnvrtv atapwlliwp slavvlavls
      361 fnffgdglrd aadpydt
//
LOCUS       WP_457664249             155 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457664249
VERSION     WP_457664249.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..155
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=16201
     Region          1..150
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(2,4..9,44,46..48,51,93..95,99..100,103..104,140)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(4,48)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(9,21,24..25,28,32,44..45,94..97,100,140)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 mftdivgsts vaaelgdrgw qelvhrhdea vraelgrfgg seiktmgdgf laifhgpska
       61 ihcacairrr aadiglsvra alhtgecakr rndisgiavh lasrlldhag agdvivsstv
      121 kdlvvgsgvt fkargeailr dvpgswqiya ateag
//
LOCUS       WP_457664250             105 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Sinorhizobium medicae].
ACCESSION   WP_457664250
VERSION     WP_457664250.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..105
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11783
     Region          10..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maydyrqmva ladptrrrvf eliaqrprsv aelthslpvs qpavsqhlkv lryanlvqae
       61 argasnvyhi dpqglgemra wldsmwtdal gsfreaisks ketke
//
LOCUS       WP_457664259             564 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sinorhizobium medicae].
ACCESSION   WP_457664259
VERSION     WP_457664259.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 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
REFERENCE   4  (residues 1 to 564)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..564
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=62239
     Region          <41..555
                     /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 mpdgdttlpg spsvdfgffa dfdevvslyd enfqliectp rhreayvves lietslwhiy
       61 pellapgaks avefvvatgl prtveiahas agprrtllif rsrsgvgvve aessamyret
      121 frqsesdral llhqathdvl tglpnrrqfs dqlrgalpvp ngaqvalmqi dlddfkpind
      181 tlghgagdav lkmaadrirs ilrdrefayr lagdefaviq wrsdqpseae rladalinaf
      241 kepfmvegin vfvgasvgia vapedgneve qlmkaadial yaakkdgrgr sstftrsmlv
      301 vleqremlrr slrtalqegq ffleyqplvk psssvagfea llrwrhplvg tippnvfipm
      361 aeadglmsdi grwlleracr tamdwpshft lavnlspaef lhegltdrva qtldlvgmra
      421 drleleites vllertinnl dtlntlnvlg vqislddfgt yysslsylkn fpfdtikidq
      481 yfikdlerne kgqtivrsii alahglgmnv taegvetagq aawlqkegcd rlqgyflgap
      541 maadaigdfl rkasatpatg lqri
//
LOCUS       WP_457664260             730 aa            linear   BCT 27-JAN-2026
DEFINITION  hydantoinase B/oxoprolinase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664260
VERSION     WP_457664260.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Watabe,K., Ishikawa,T., Mukohara,Y. and Nakamura,H.
  TITLE     Cloning and sequencing of the genes involved in the conversion of
            5-substituted hydantoins to the corresponding L-amino acids from
            the native plasmid of Pseudomonas sp. strain NS671
  JOURNAL   J Bacteriol 174 (3), 962-969 (1992)
   PUBMED   1732229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..730
                     /product="hydantoinase B/oxoprolinase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=81493
     Region          38..648
                     /region_name="HyuB"
                     /note="N-methylhydantoinase B/oxoprolinase/acetone
                     carboxylase, alpha subunit [Amino acid transport and
                     metabolism, Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0146"
                     /db_xref="CDD:439916"
ORIGIN      
        1 mldktanplq rrlleserlm eetgcydgit elrlrgqdpl kfetlhtklr aycvsarema
       61 rrisaspgvr evgemvvaiy tpegdaials ngimvhvhtm srfikwmirn gyeqnpcird
      121 gdifanndaf igtvqgpdvm dvvpifhegt lvgwagavch eleaggitpg gdvclaqerf
      181 teglfvcaek igendeirrd yvircernlr mpiywvldek akvaacidmr envkqlieei
      241 gleywqrlsk efieegrraq lartrqltvp giyrghtfyg hvtegkpgfq pladpnwlyn
      301 ipiemeitse gkirldfdgt qpwgyhsmnc tpagmdggmf vtltqhmnfe glvndgawla
      361 teiniphgtw tnpdnemaat atswalllpa ygvfqrllsr gfiargfvee acvgqvnspm
      421 iemggtsqyg tgfgmahfec aaagsgalai kdgldtayvg wnpesdmgni eiweqnmpmv
      481 yigrsivpns ggagkyrggc afistwlink tdhlrlvtse hssrvfdngg lcggypaptc
      541 ekhhavrnsd iheraerrep lahtpgtdpl vsdferiykg eqvweegpyi trphkagdif
      601 shaynggggf gdvlerdpik tawdvengfl treaaekvfg iilkedaegy pqadidatva
      661 rraeirrerm rkaipvsewm vreqlrvkas dfapevakmy rsamklsprf skdfrefwgl
      721 asdftiagen
//
LOCUS       WP_457664262             239 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664262
VERSION     WP_457664262.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..239
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25246
     Region          4..224
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msvrplssvl ktlatfecig aaaeplrlad varqlgearg avhqrlvtlv eagwieqttd
       61 gryrltlriv ghaamaleqs nlgarfagvl eemvtqsget aslaildgks avivrrvesr
      121 gilradlrig tqlrldrtaf grvlvsfars eiidrlraeg velpgdeiia evrkcgyais
      181 evegprtvsa vaapiidaqg ecigalalsg pftgfdtdkc arivvaaaaa saarlrgeq
//
LOCUS       WP_457664263             349 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664263
VERSION     WP_457664263.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..349
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38502
     Region          1..349
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnarsltlsn itktydgrhm aaddvsldik agefvsflgp sgsgktttlm miagfqhpts
       61 geirlgerai dnlpphkrni gmvfqnyalf phmtvadnvg fplrmrgvak qdkerrsrea
      121 lakvglqgfe krvpselsgg qqqrvalara lvfepdiill deplgaldka lrehmqvelk
      181 rihkdlgvtm vyvthdqsea mtmsdriavf nqgrieqvgt pneiyrapkt rfvacfigds
      241 nliegsalgd grfdtpvgiv earsrqtdrn rradlllrpe miriaetsqg grqplkidst
      301 inygdnllvi gklgsqairm rvpgadarrl egvsechvtw haedvhvia
//
LOCUS       WP_457664264             461 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate aminotransferase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664264
VERSION     WP_457664264.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..461
                     /product="aspartate aminotransferase family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50335
     Region          1..460
                     /region_name="PRK06105"
                     /note="aminotransferase; Provisional"
                     /db_xref="CDD:180401"
     Site            order(117..119,151..152,154,225,258,260..261,287)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(118..119,151..152,225,258,261,287)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            287
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mndrpnslha ldkqslvhpy tnlalhqetg phvitggdgi yvvddqgkry ieglaglfca
       61 glgfseqrlv eaatrqlktm pfyhsfahks tepgirlaek llsiapvpms kvffagsgse
      121 andtaikliw yynnalgrpd kkkiisrrka yhgvtvatas ltglpfnhrd fdlpianilh
      181 tdcphywrfa etgeteedfa trmadnleat ileagpetia affaepvmvs grvitppkty
      241 fekvqavlrk ydillvadev icgfgrtgnm fgletyglkp dmiscakqls aaympisalm
      301 inqriadalv dqsrkigtfs hgftygghpv aaavalealt iyeeidivgh vrsvapvfqd
      361 rvrklgehpl igeargvglv agfefvkdka trenfppawq vanqagkfat argvltrglg
      421 dmvslcpami idegqiddlm trmglalddt lawartqghv a
//
LOCUS       WP_457664267             456 aa            linear   BCT 27-JAN-2026
DEFINITION  BatD family protein [Sinorhizobium medicae].
ACCESSION   WP_457664267
VERSION     WP_457664267.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Tang,Y.P., Dallas,M.M. and Malamy,M.H.
  TITLE     Characterization of the Batl (Bacteroides aerotolerance) operon in
            Bacteroides fragilis: isolation of a B. fragilis mutant with
            reduced aerotolerance and impaired growth in in vivo model systems
  JOURNAL   Mol Microbiol 32 (1), 139-149 (1999)
   PUBMED   10216867
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..456
                     /product="BatD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48887
     Region          <88..123
                     /region_name="BatD"
                     /note="BatD DUF11 like domain; pfam13584"
                     /db_xref="CDD:463927"
ORIGIN      
        1 mtiaaprlyr llavlfcwls tqgpalsadp laraalqsqe tlyagqqilv dvdvlvpnyf
       61 lqspqfpaid ipgaivtldd gralnlneti dgtpysgirr tyiivpqaag dftlppvpit
      121 fgyaavppqa trgevtlppl rftvrsapgt agdspgvvaa kvsvsqeldq dpaqlkagdt
      181 lvrtvtvrae glrammipep dftapqgirl yrqdpslsee tdrngqsiag lrkdvasylf
      241 qdagnyvlpa vtvswfdpas aktqsatapa vsvtvsaaaa lspalappap epqrdafdwl
      301 hlaliggivl ltasalwvaa sglsrleaww qerrskerqs epaffrqveq acksgrddai
      361 araldawsrk agamplefwl grfadaetkq gyqawqrtry asqeasqplg aglllpglkk
      421 areawltqgg gsarpqtgla spqpdyavtr rmkadl
//
LOCUS       WP_457664270             837 aa            linear   BCT 27-JAN-2026
DEFINITION  TRAP transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664270
VERSION     WP_457664270.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 837)
  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 837)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..837
                     /product="TRAP transporter permease"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89025
     Region          3..693
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
     Region          645..822
                     /region_name="DUF3394"
                     /note="Domain of unknown function (DUF3394); pfam11874"
                     /db_xref="CDD:432151"
ORIGIN      
        1 mtglillcta vawslfqlwy asplpfvfgf gilndteara ihlgfalflt flaypalrss
       61 prdrvpladw vlaalgafag aylfifygdl agrpgqpstl dlvtgtigil llleatrral
      121 glpmvivagv fifytfggqy mpdviqhrga slvkfinhqw lttegvfgia lgvstsfvfl
      181 fvlfgtllek agagnwmmqi siallghlrg gpakvavvss alngvvsgss vsnvvsggif
      241 tiplmkrtgl sgvkagaiea tasingqimp pvmgaaaflm veyvgipyse ivkhallpav
      301 fsyiallymv hlesvkldmq pipqrptpar erwirmglgl tgsvlavcll yygilgiraa
      361 fganapllla iggaalyiat iwyssrypdl elddpnapil elprawdvtr tgldflipia
      421 vllwclmveq lspglsafwa tvtilaivat rkplmaifrk edfassvgaa aydlvdglal
      481 garnmigiav atatagivvg titltglglm mtelvefisg gnvimmlili aaislvlgmg
      541 ipttanyilv atlmapvvve lgsqaglaip liavhlfvfy fgimaditpp vglasfaaaa
      601 iskedpiatg fqgalyslrt ailpfvfifn pailligvdt wahtiwvaai slaailifsa
      661 atmnwfvtks rlwesavlll acftlfrpdw wvnqisppye elpsseflrt veeapakari
      721 nfvvqgidlm gddvrktvnv plgepgeplq rlravgltvt pagdslmisn vafgsyakri
      781 gldvgydvva vlkkadqpst aipvsialil tagiaglqfa rkradrsgas lrgtark
//
LOCUS       WP_457664274             259 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664274
VERSION     WP_457664274.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28488
     Region          38..257
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mdcsctlskt lqhpalvral slglllllwi aaaaltadts vlpqpwalwt pflqalgsga
       61 lpyhlgmtlw rvvcafvpam iigvavgflm grfasvdrwl dpwlvvflnl palvlivlcy
      121 iwiglnetaa itavvlnkip nvatllregt raldpnldsm aavyrmrpla rlrhvimpql
      181 apfiaasara giaviwkivl vveflgrssg vgfqihfyfq lfnvamvlvy alsfigvmll
      241 vealflqpae rrvrrwrta
//
LOCUS       WP_457664275             547 aa            linear   BCT 27-JAN-2026
DEFINITION  Na/Pi cotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457664275
VERSION     WP_457664275.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Tenenhouse,H.S.
  TITLE     Recent advances in epithelial sodium-coupled phosphate transport
  JOURNAL   Curr Opin Nephrol Hypertens 8 (4), 407-414 (1999)
   PUBMED   10491734
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Takeda,E., Taketani,Y., Morita,K. and Miyamoto,K.
  TITLE     Sodium-dependent phosphate co-transporters
  JOURNAL   Int J Biochem Cell Biol 31 (3-4), 377-381 (1999)
   PUBMED   10224663
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Werner,A., Dehmelt,L. and Nalbant,P.
  TITLE     Na+-dependent phosphate cotransporters: the NaPi protein families
  JOURNAL   J Exp Biol 201 (Pt 23), 3135-3142 (1998)
   PUBMED   9808829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..547
                     /product="Na/Pi cotransporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005436 - sodium:phosphate symporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0044341 - sodium-dependent phosphate
                     transport [Evidence IEA]"
                     /calculated_mol_wt=57456
     Region          1..539
                     /region_name="NptA"
                     /note="Na+/phosphate symporter [Inorganic ion transport
                     and metabolism]; COG1283"
                     /db_xref="CDD:440894"
ORIGIN      
        1 mesvivganl fgavalllyg lgqvkdgmsr awgarlrtgl aagtrggars faagfvatia
       61 lqsstatalm vasfvekeli apamaqvvll ganvgtaata wivalglgwl spllivagva
      121 lsrtrssarr gagsaivgig lmllslhlla natdplrqsp alsaflamle nawpvalffa
      181 aglavlasss laivvlilsl satgglstal vivlvlganl ggavppvlat lgasasarrv
      241 tignlivraa gcaialplag ygaylmelar lspqklavda hllfnlaval aafplsplly
      301 rltaslipee aesengpryl dmealarpva alagagrevm svgdliesml vralealrgn
      361 dlsrladisl lecrvdriqh eiklyvskvg kdgmtdedhr rarqivdyai nlehigdiie
      421 kglhpeiakk islglrfsed gqgelgrlfa itldnlrmaq avfatgdael arrlvevkee
      481 vrrlekqsae chlqrlregr ldsiqtsslh ldmlrdlkri nahvasvahp ildgsgllid
      541 srirqav
//
LOCUS       WP_457664276             273 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664276
VERSION     WP_457664276.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10452004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..273
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29679
     Region          84..126
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          153..269
                     /region_name="TetR_C_7"
                     /note="AefR-like transcriptional repressor, C-terminal
                     domain; pfam14246"
                     /db_xref="CDD:433807"
ORIGIN      
        1 mgslpvrpag frlkqskrqf apedsdawyr rcsatqrile plqdlrstep enwmgeeefa
       61 ededdqeaas grsgkrdarr eeflraatev flssgfsgas vdsiiakagg skrtiysyfg
      121 kkdqlfttvi keitgrvmgp fpaaniagad ldtvlyrsgs hyldavmspe alqlyrivvg
      181 egarfpgvar affengpgra saalasilee gaddwgipkr saaklaehfi gmirddlhlk
      241 vvlglcdppt paearssvrd avdvfvygig rps
//
LOCUS       WP_457664278             366 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457664278
VERSION     WP_457664278.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..366
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40888
     Region          2..340
                     /region_name="GT4_AviGT4-like"
                     /note="UDP-Glc:tetrahydrobiopterin
                     alpha-glucosyltransferase and similar proteins; cd03802"
                     /db_xref="CDD:340832"
     Site            order(20,178..180,240,263)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340832"
ORIGIN      
        1 mkiaqiaplf ervppklygg tervvhhlte elvrqghevt lfasgdsmts arlvpcsqma
       61 lrlnpaiqdp ipyhmmllee vrrqaaafdi lhfhidllhf plvrdlagkt vttlhgrldl
      121 pdlqpfyaaf pdvplvsish dqrrpmppvn wiatvhhgla pdvlpftshp kgdylaflgr
      181 ispekrpdra ieiaaragmp vkmaakvdrv depywlseie plirrypnve figeinehqk
      241 adflgnaral lfpidwpepf glvmieamac gtpviafrrg svpeivdhgv sgfivdstee
      301 alkavheldr vdrhmvratf drrftaqrma ndyldiyral asgsqrvmpi haanesnvgp
      361 gsarva
//
LOCUS       WP_457664284             301 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664284
VERSION     WP_457664284.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32473
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdrwqamrif vqvvesggfa paakvlhmsp psvtravvql egligtrlli rttrslkmta
       61 agegyladcr rilaeiaeae anaagsftap aglltitapv lfgrihvlpv ildfldgypa
      121 mqvktvfvdr vtnlvdegld vairiaslpa sglvarrigs vrqvlcgspd yfarfgepgs
      181 phelaghrii greglfghse wlfgrdssir ipisprlicn tndavlsaav agwglsrfqs
      241 yqveadirag rlkvaladye repvpihivh aegrmvsarv rafvdfaagr flrhaglste
      301 l
//
LOCUS       WP_457664286             754 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 2 protein [Sinorhizobium medicae].
ACCESSION   WP_457664286
VERSION     WP_457664286.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..754
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83832
     Region          9..>547
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          654..743
                     /region_name="Glyco_hydro2_C5"
                     /note="Glycoside hydrolase family 2 C-terminal domain 5;
                     pfam18565"
                     /db_xref="CDD:436582"
ORIGIN      
        1 mrsvtsfnds wvfsagftaa dagtlqagqp islphnaiel pfnyfdetcy qraftyqkvl
       61 awrpdfsgre vslvfdaama davvylngee ivahkdgytp iearltgrlr egdnlitvki
      121 dgsenpeipp fggridyltf agiyrdvwlk itdpvsiani kietrdvlsd artvsvrcdl
      181 anpqglsftg avsallkdaa gdvlaevage tagggvtvqm dglkglslwd iddpvlyeve
      241 velrtgrgsd rvaahfgfrt aeftnegfrl ngrllkirgl nrhqsfpyvg yamgrtaqer
      301 daeimkhtlh cnlvrtshyp qskwfldhcd rigllvfeei pgwqhiggea wkeeailnva
      361 rmierdwnhp siviwgvrin elqdshdfya ktnrlareld ptrqtggvry itdsefledv
      421 ytmndfilgn eelpgsnrpr talrpqqect glsrkvpyli tefgghmypt kiydqeqrqa
      481 ehvrrhlevl naaygdpsis gaigwcmfdy nthkdfgsgd ricyhgvmdm frepkfaayv
      541 yasqcdpsee vvmkpvtfwa rgerniggvl plivltncde velkygslvk rigpdrenyp
      601 hlphppvvid hrhftkdelg vwgmkwesae ftgfidgkpv agrrmvadpv pttleieadg
      661 ktlraggrds irimlraldq agnvlpflnd avaievhgpa rvvgptrlvf qggstgfwle
      721 stgaagaivv tavssrlggv klelvamaeg ewna
//
LOCUS       WP_457664293             779 aa            linear   BCT 27-JAN-2026
DEFINITION  autotransporter family protein [Sinorhizobium medicae].
ACCESSION   WP_457664293
VERSION     WP_457664293.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Grijpstra,J., Arenas,J., Rutten,L. and Tommassen,J.
  TITLE     Autotransporter secretion: varying on a theme
  JOURNAL   Res Microbiol 164 (6), 562-582 (2013)
   PUBMED   23567321
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Benz,I. and Schmidt,M.A.
  TITLE     Structures and functions of autotransporter proteins in microbial
            pathogens
  JOURNAL   Int J Med Microbiol 301 (6), 461-468 (2011)
   PUBMED   21616712
REFERENCE   3  (residues 1 to 779)
  AUTHORS   Wells,T.J., Tree,J.J., Ulett,G.C. and Schembri,M.A.
  TITLE     Autotransporter proteins: novel targets at the bacterial cell
            surface
  JOURNAL   FEMS Microbiol Lett 274 (2), 163-172 (2007)
   PUBMED   17610513
REFERENCE   4  (residues 1 to 779)
  AUTHORS   Henderson,I.R. and Nataro,J.P.
  TITLE     Virulence functions of autotransporter proteins
  JOURNAL   Infect Immun 69 (3), 1231-1243 (2001)
   PUBMED   11179284
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..779
                     /product="autotransporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015474 - autotransporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81833
     Region          8..779
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 msftsdvsit gpgtstlnnn gtltnslrat dndrftlnnr glidgtiflg gsganviiny
       61 aggdvqngvt stgdshdtvi nrgffagsiv lgdgndvlgl iegtvqtsvd mgagddqftw
      121 lvgniaatvq mgegddravf gsltqqnlsa gkrvdgglgi dtlvwenttn ddgggsgdhp
      181 enivnweeie lrngwemtfi ystgnltlgd svsgtgtlsi detsavragn sfgygvrafd
      241 psqlvtvyna giidmtndtv nvgdllhdtf tvygnyvgqq gglqlhtvle sddapsdklv
      301 isgtgasasg gtsilitnvg gqgaltladg irvvdataga ttegtaftlg apvaagifey
      361 qlyrgglted pdndddwflr sggvsppppp pppppppppp pppppppppp pppppppppp
      421 pppppppppp pppppppppp pppppppppg pspitpsvrp eipgyilkpa lmqkmgvaai
      481 gtfherqgdq fllnsngylp gawgrlfges fdqswsskis rfefevspsf sgelwglqag
      541 qdligalhdd gsqdrvgvff aytgtsgsng gntlgrlqve sgsidlhans igaywthiga
      601 dgwyvdsigm yswldggsss drgigvdtsg nstalsieag ypfrfdngwv lepqgqliwq
      661 hvdlddandr ftgidyesfg twtgrlgvrl eanttmndvp vqpfasvnlw hdfdqdykvs
      721 fnrvpvvtel eqtllelnvg fsaqmsetvs vygglqfatg lndddnrgyg gniglrikw
//
LOCUS       WP_457664295             508 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664295
VERSION     WP_457664295.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..508
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55594
     Region          9..506
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mdretvdaar vvlearrisk sfsgvqvlfs vnfelragei halmgengag kstlvkifsg
       61 feqpssgevl ldgqpvtlpa ngaaealgiv iihqefnlae hltvaeslfl grevtrfgml
      121 drkymraetr rvldllgcnv danaligsls iaekqmveia kaisrdariv fmdeptavls
      181 reetsflfrq vrklrdrgts fvfvshklde vieltdrvtv lrdgqwvkta ptsmldgesi
      241 aqlmvgrems slypaknepd vdeevvlrvd alstdyvkda sfevrkgeil gfsgmigsgr
      301 telmeavagl rhrlsgdvai rgesvpsgdv haanrcglay mtkdrkakgl llnsgmtanl
      361 tlqslgrhar igylspasea salerarrrf dirvrdgnvv arrmsggnqq klllakvmet
      421 epdiiiidep trgidvgtkq qiyhfisala rdgrsiivvs sempeviglc trvavmregr
      481 ivgmlegdei seqeimryaa glkkmaaa
//
LOCUS       WP_457664296             343 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457664296
VERSION     WP_457664296.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 343)
  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   2  (residues 1 to 343)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..343
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37052
     Region          4..337
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msdstpatie dvariaevsi atvsraihtp ekvakstrlk vnqaiaitgy ttnamarslr
       61 lgrsnmilvv apdigdpnfs silvglenea rshgygvlig htqndaqrav eylkflnsnq
      121 aaglilftgi lpfghetiaa rlppsvgife pvfnggipyv gvddeegark vvdlllaegh
      181 rkiafignsr trlaykrrra gydaglnsaa vpaelrlvqe gdgtlesgra averlfvrdt
      241 lptafmcvnd qtalgvmigl kargydiprd fsvtgfddvp qatfmtpalt tirqprtlig
      301 khamalllel lsnglpaeme illrpdlvvr nsvstpsprw rer
//
LOCUS       WP_457664301             338 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457664301
VERSION     WP_457664301.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 338)
  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   2  (residues 1 to 338)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..338
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36270
     Region          1..331
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mldvakvagv svatvsavin ssapvspelr srieqaigqi gykrnaiars lklgttrtvg
       61 llvaditnpf ftdvvaviqe vlhragyavm lccsdedvil qdeqiallid rsvdgliiap
      121 agddetlkrm iaaaslptvl idrlcdgidt davvldnrra vqdatrymlg lghrrigyis
      181 galdtstgre rlsgyraale aaglpfeesl irignfrekd aytaaiqllt sperptgifs
      241 annlmvigvm kairdiglrc pddvsvasfd dfpwadvfqp hlttiaqpvq aigeqaaqlv
      301 ldrlsgaspe tprrlvlqgr lvirdscrpv slaqraia
//
LOCUS       WP_457664298             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664298
VERSION     WP_457664298.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38960
     Region          1..348
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maeirlknvs krwhnfvgvd nfdldiadre flvllgpsgc gktttmrmia glddisegei
       61 wlgdrmvnnl epkdrdismv fqsyglypnm tvyenirfpl rvrkvpkelh hekvmqaarm
      121 velvdflerr paalsggqrq rvalgraivr qpaaflmdep lsnldaklrv straqiknlq
      181 htlkvttiyv thdqieamtl adrvvvmnkg viqqvgtptd iydnpantfv ssfigspamn
      241 lvfgdiengt frgpgitigg lqtnvkgpvt lgfraedasl vfeggelgae iysmellgea
      301 tmasfrvgdq lvsiksgkey raeigdvvha aipasichlf dartgvriar tpgn
//
LOCUS       WP_457664302             528 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664302
VERSION     WP_457664302.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..528
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=56535
     Region          18..518
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mrdavptllg dsvtteparp ilaaeavsks fggvaalkdv rfdlrsgeih almgengagk
       61 stlmkvlsgv yadyegtvrv dgeiarfssv rdaeaagiai ihqelnlvpe lgvadniflg
      121 rervvaglfv drkasleaar gllnrlgiel dpearvgqlr vgeqqlveia kalsvearil
      181 imdeptsals sgecrrlfki vrqlaadgvg ivyishride vmqlsdrvtv frdgrhvwtr
      241 pmagldedti iaamvgrnll dahpvnrpkg aepvlsvsgl slavagrhgw rdvlkgvsfd
      301 vhageilgig gllgagrtei letvfasndg vrggeirldg iavdirsprd arrlgfalvt
      361 edrkakglhl qelirdnval plvgrlarfg lrsfereral asravealgv rcagtdqtag
      421 tlsggnqqkv vigkwlatgp rvllldeptr gidvgakrei ydlvfklaad glaivvvsse
      481 lpelllladr ilvmaegrqt glisreease erimqlaapr stfgrsva
//
LOCUS       WP_457664303             260 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664303
VERSION     WP_457664303.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..260
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28480
     Region          15..246
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 migspiltqm pkvgrslerr tareliadkl mvlvatnmlr pgdvlpgere lanvlhvsre
       61 tvrgaiqtla argvvevsqg srtrvgnidl shltvtiasp saidsynied vhaarlhiel
      121 kvvgdaaeii deetlgklga lldaqklcsd damrflicdr efhvaiyrac gnpllsdfvt
      181 dlytymmdhr rsamsrpgai dasykdhsdi vaalrrrdra avvaafhhhl iriyettktl
      241 laneeasgrk pkqkapagqv
//
LOCUS       WP_457664311             253 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664311
VERSION     WP_457664311.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26557
     Region          4..245
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mvslalkdvg atygrrvvls dintgvlkgg qltavigpna agkstlfkri aglaagpglv
       61 hlsdtakgse aicymppdtg anavltvyel vllsakqgsg wkvkdgelqe idrvlaalki
      121 nelafrglge lsggqrqlvs iaqalvrkpe vllmdeptsa ldlfrqievl gfmkrlatqs
      181 gmavlialhd lnhalryced tivisdgsvv asgpthavvt admlksvyrv earveacsrg
      241 rpviivddsi alg
//
LOCUS       WP_457664312             297 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Sinorhizobium medicae].
ACCESSION   WP_457664312
VERSION     WP_457664312.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33625
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqredmkdll wflevareqs ftkaaaalgt sqstlsytik qlearlgvrl ltrttrsvat
       61 teagerlfqs laprfqqiea dlaalvafre kpsgtvrltl sdhalqttvw pklsrvlsdy
      121 pdirlelysd ngmrniveer fdagvrlges vdkdmiavri spdwrlrava speyftkhgi
      181 pttpqdlvgh lcinmrqatw ggfyswefek dgrelrvrvd gqlsfnssit qveaalegyg
      241 iayvpenlve ehlavgrlra vlddwsqpft gyhlyypsrr qmspamtviv ealrhrs
//
LOCUS       WP_457664317             629 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Sinorhizobium medicae].
ACCESSION   WP_457664317
VERSION     WP_457664317.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 629)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..629
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67934
     Region          7..571
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtsgadllrv eglritfsvl gggveavrga sfrilpgrvt alvgesgsgk saisqaimgi
       61 lpsvasvtgr vvfndptgnk pvdllsldsg greiqdirga riskifqepm tslsplhtig
      121 nqisevlkiy tdidkagrre rteqllgyvg fsdpkraydm ypfelsggmr qramiamali
      181 cspalliade pttaldvtvq aqilqllrgl qsklnmamll ithdlgvvan madevvviyh
      241 geiveagpvd aifrnpqhpy lkglmaavph fnmkpgerlk alrevpvqag aiigdrdvrk
      301 aggpnvlvsv rnlsktfstr ssgwfgsgsa frhravdnvs fdirrgeclg lvgesgcgkt
      361 tiskilmrav tpdkgtitfd dgegaldvlk ldgaelkalr akiqmvfqdp vsslsprmtv
      421 knilseplei hgrgtpksrv etvrsllqav gldqrfinry phsfsggqrq rigiaralal
      481 vpqllicdep vsaldvsvqa qilnllkdlq kelgltmlfi shnlavvdym adriavmyag
      541 rivelaprev lmsdpihpyt ksllaavpyp dldrkldfdl lqvsggsdqq rwgvqfadgg
      601 ddealvpadl ggghfvlark svdarelrp
//
LOCUS       WP_457664320             343 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Sinorhizobium medicae].
ACCESSION   WP_457664320
VERSION     WP_457664320.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12124374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..343
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37310
     Region          <1..37
                     /region_name="OppC_N"
                     /note="N-terminal TM domain of oligopeptide transport
                     permease C; pfam12911"
                     /db_xref="CDD:463747"
     Region          <122..339
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 magcvmlvli glfsfvgplf sphsydqvfp syvtigpsle prpdsstlqd vmegvasrar
       61 vrltefaved qsftatvtsd apidpratry fdranefent kvvategdgr tlkvegdvar
      121 eyfpfgtdsn grdllvrvml ggqisiavgl laslvslgig vlygatsgyi ggrvdnvmmr
      181 lveilyslpf vflvvvlvvf fgrsfilifl vigavewldm arivrgqtla lkrrefvgaa
      241 qalgltdwqi irrhiipnti gpvivfvtvv vpkvillesf lsflglgvqa pltswgalis
      301 eganniqsap wllifpaiff vltlfslnfv gdglrdaldp kdr
//
LOCUS       WP_457664322             232 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Sinorhizobium
            medicae].
ACCESSION   WP_457664322
VERSION     WP_457664322.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bondos,S.E., Swint-Kruse,L. and Matthews,K.S.
  TITLE     Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox
            Proteins
  JOURNAL   J Biol Chem 290 (41), 24669-24677 (2015)
   PUBMED   26342073
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Ravcheev,D.A., Khoroshkin,M.S., Laikova,O.N., Tsoy,O.V.,
            Sernova,N.V., Petrova,S.A., Rakhmaninova,A.B., Novichkov,P.S.,
            Gelfand,M.S. and Rodionov,D.A.
  TITLE     Comparative genomics and evolution of regulons of the LacI-family
            transcription factors
  JOURNAL   Front Microbiol 5, 294 (2014)
   PUBMED   24966856
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Swint-Kruse,L. and Matthews,K.S.
  TITLE     Allostery in the LacI/GalR family: variations on a theme
  JOURNAL   Curr Opin Microbiol 12 (2), 129-137 (2009)
   PUBMED   19269243
REFERENCE   4  (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   5  (residues 1 to 232)
  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   6  (residues 1 to 232)
  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 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   8  (residues 1 to 232)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   9  (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
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
REFERENCE   11 (residues 1 to 232)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
REFERENCE   12 (residues 1 to 232)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10105145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..232
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24992
     Region          23..68
                     /region_name="HTH_LacI"
                     /note="Helix-turn-helix (HTH) DNA binding domain of the
                     LacI family of transcriptional regulators; cd01392"
                     /db_xref="CDD:143331"
     Region          83..>181
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mgkgnggngs pkdagggrpt mtdvariagv sqssvslvln emsgarisae trarvrdaar
       61 kigyrlpntr qdldhapaie kdtiafivde istsphpvvs ldgirdyafe qgllvsahat
      121 rsnpdlesav lrsvlrdpai agviyatift rkvsvprele nvptillncy aeprqhmaiv
      181 pgggcgglrg drasnvsrap ahrlhqrrtl dgrryrpaqr lqaslgdrry rl
//
LOCUS       WP_457664323             330 aa            linear   BCT 27-JAN-2026
DEFINITION  YihY/virulence factor BrkB family protein [Sinorhizobium medicae].
ACCESSION   WP_457664323
VERSION     WP_457664323.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..330
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35846
     Region          30..311
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mgtnevelve rldaaepgrg raasapgeip vkgmrdvfwr vvseiaeerv vliaagvsfy
       61 lllslfpalg alvsiyglva dpseigthmg ilqallpqds yglimdqlkt lttqkpstlg
      121 mgffislsis lwlaangiaa lfdamnvayg erekrgflfr tvlciaftfa allfavaliv
      181 aigvvpavla hlwvdrwvel vtwvarwpal lllvtfgtvl icrfgpsrer aklrwlnwga
      241 vfstlfwfaa swlfsyyleh fanynatyga lgalaglmtw vwisvmilii galinaeleh
      301 qtavdsttge plplgergah vadtigkaan
//
LOCUS       WP_457664331             407 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Sinorhizobium medicae].
ACCESSION   WP_457664331
VERSION     WP_457664331.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..407
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=44816
     Region          <141..398
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mqdeeidilr wlanaglrgd epnemfrafc ercsragipi syamglmdtl hpefeghafe
       61 wraqdngprp lqtysssdsg nvretwessa fnhlrqtges elrreigkga pvdfyrlpel
      121 reegctdvif hierftrkgs igamdafysv wgtdepdgft edqlallrrl lptlalalks
      181 vgsirivktl arvylgqdaa srvidgqvar gqaetidaii wlsdlkdyta imdaarpeqi
      241 ipllndyssv vigalhrngg nvlkligdgv laifkgpdlt aaasralqte rdlrrdldhl
      301 nrrrgargep stglyvslhl gtvfygnigs rnrldftvvg pavnevsric tickttnnda
      361 lvsadfvnvc rpasreglsp lgefslrgvs epmvlytvnr gsvsvvv
//
LOCUS       WP_457664342             144 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664342
VERSION     WP_457664342.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 144)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..144
                     /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=15604
     Region          5..>117
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mlpkvrllqi gdihlvsnag nkafvddkdt tfplnlknii srspiktvfr rifeiikeqd
       61 idavlfmgdl tdygkldgye acskyiasal qigskglyrd ipvgivpgnh dinrtlalkp
      121 gtstkftplv ealtgaglpp larp
//
LOCUS       WP_457664344             225 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Sinorhizobium medicae].
ACCESSION   WP_457664344
VERSION     WP_457664344.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..225
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=23692
     Region          15..156
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mkadvfdpra lreafgafpt avtvitasdp agrpvgftan sftsvsldpp lllvcvakta
       61 rdypamtaae hfainilsea qkdvsikfar pledrfaavd wargpngcpi feqvaawfec
      121 smhdvieagd hvmmvgrvta fessglnglg yarggyftpg anssaaggei gavavlerhg
      181 alfplddqnl alpsysagsg dpktlasqle qlglsvhdwf clldl
//
LOCUS       WP_457664321             893 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Sinorhizobium medicae].
ACCESSION   WP_457664321
VERSION     WP_457664321.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 893)
  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 893)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 893)
  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 11421621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..893
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=98640
     Region          10..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          486..853
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 msgnredtdl ivvamplygh aalvleaies vlasklsgcs vavvvsvdgd prqetfdqll
       61 lyaaahpavh vlfganagpg garnraieyv lanlpeaeav yfldadnrvl pgtietlyrq
      121 lrtsgcgwiy tnidtfsvsw rahygnrysr llhcitdnic dtgsmisldv fragvrfdad
      181 rqngfedwef wlsciehgfv gepchdttfe yrlraesrfk eanrdraasv sflrkrhral
      241 fqrpmlvdfe heecprylfa rtedaaisyf tdptkapkrl rlddiipafw asvgepdnvh
      301 fppfliagsg atldlllrsr mlpnvlshle rlsekanvvf vqlgndaaqr kiepvfleag
      361 aqhnaspdli flstslvrdv iqnkaldwfa signqqvwpt sailkvrfpf prslprrlli
      421 tpqqvmincv naiatsplrr tagkrwtwrp arlvpysdlh kalrqevggs pilplghseg
      481 grktaallvp nasfggaekv vyaasrelka agyethlfvl gtsrmdvide fdqsfdyihf
      541 wdqgipawgg sgsflghdfi aeghdvdwaa lkgqlsgfdl vinnhvmavh pliarlrseg
      601 trtacylhvv dntafkrpag qpfaaiaheh cydafltcse qlklylhsfg vphekifavp
      661 ngasfsvppk vlsevlsvrr ierkddrlrv lymgrldqqk gidrlaaaia elrasrvpfd
      721 aravggeila datiswmdrl rdlgvevrsp vfaskdlika lgwadvllmp srwegaplmi
      781 aeaqqlgcvp iatavgavde litdgedgil ieaaadpqvv rdmakaieev alnrkqlapl
      841 megclrtaar rswgssfsef lgwcdrsvhn sslsratvir greasnpgva avg
//
LOCUS       WP_457664348             412 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Sinorhizobium medicae].
ACCESSION   WP_457664348
VERSION     WP_457664348.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10315023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..412
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=45921
     Region          116..200
                     /region_name="Phage_int_SAM_1"
                     /note="Phage integrase, N-terminal SAM-like domain;
                     cl12235"
                     /db_xref="CDD:472283"
     Region          227..405
                     /region_name="INT_RitA_C_like"
                     /note="C-terminal catalytic domain of recombinase RitA, a
                     component of the recombinase trio; cd01188"
                     /db_xref="CDD:271188"
     Site            order(260,357,360..361,392)
                     /site_type="active"
                     /db_xref="CDD:271188"
ORIGIN      
        1 mlefyfsygg vlkrlrsgal ggemdrlaeh ffrlgykras akiylsriar fsrfagtrcg
       61 pmpihqdvvd sylrtfptdt prigamsalg harrvaperf iisvpseedd pdapllasfs
      121 dylrrvrgle pksregvllg grrfldwcrh hhpgqdieal takqvlaave yrlslsttsg
      181 srtaatshir tflrflywag rhhqdlariv prkpswrlah lpprlawndv rhaidaigat
      241 tpvgirdrav llllattgir ngelrairlr didwrtgevf vrrtkgkrdr vvplleetga
      301 aladyilrar prvdspylfl sftppvgpfk caapvsrivr krlrhggvel grvagahllr
      361 hslatqlvgq rrpinevadl lghrsintta lyvkvaasql aevalpfpgg va
//
LOCUS       WP_457664316             382 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Sinorhizobium medicae].
ACCESSION   WP_457664316
VERSION     WP_457664316.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   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 382)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..382
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42026
     Region          5..357
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(17,193..195,255,277)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 msgarvtiil pslgaggteh vvklvanhwa qlgckvtlit lelpharpyy efdpriaier
       61 lglppqqggk iragllvlrr iyrlrsairh sqpdfvlsfl trtnvltlla tiglpvpvvv
      121 sernnpalqp fgvfwkwiqr rlyprafglv tmtrgaldyf pekmrsrgwv ianavdlpge
      181 wqkrrgnnil tavgrltrqk gfdllieafa riasrhpewk lviwgegddr kslealrdal
      241 dmtdrvempg vtqrpgvwve tadvfvlssr yegwgivlle amaaglpvvs facewgpsdm
      301 vehgedgllv psndvdalae alsrvladge lrsrlaanae asakrylpdr ilsqwdaval
      361 salkhtardh aatasvvgag sa
//
LOCUS       WP_457664315             226 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Sinorhizobium medicae].
ACCESSION   WP_457664315
VERSION     WP_457664315.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..226
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24582
     Region          <7..201
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mktfrepaav slglpaslgy yclkrlldcl lagtvfvlcl plmaatavvv waalglplff
       61 sqaragaemr vftvakfrtm tdarapdgtl lpddmrqtas tallrrlrfd elpqliavlc
      121 ghmsmvgprp lplatvagfg elgrmrcrva pgmtgwaqvn gntrlsddek ialdlwyvah
      181 anlwldaril lltvktlvtg ervhaghlqe areflsrrlg aeppka
//
LOCUS       WP_457664443             200 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Streptomyces albidoflavus].
ACCESSION   WP_457664443
VERSION     WP_457664443.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  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
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Identification of a PD-(D/E)XK-like domain with a novel
            configuration of the endonuclease active site in the
            methyl-directed restriction enzyme Mrr and its homologs
  JOURNAL   Gene 267 (2), 183-191 (2001)
   PUBMED   11313145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..200
                     /product="restriction endonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21629
     Region          44..164
                     /region_name="Mrr"
                     /note="Restriction endonuclease Mrr [Defense mechanisms];
                     COG1715"
                     /db_xref="CDD:441321"
ORIGIN      
        1 mtwstiwpyv lvaaatgasa talwwlhhtd rlprrgeprp hepaalraas laeidaltwq
       61 efehhvaalc rrdgcrdvvv tggagdlgad vtatlpdgrr lviqckhyap hryvpsgdmq
      121 kflgtawlhh radvavfaat cpfgkaalal aaehritavh rdllglwnsg tpltallavg
      181 gagqgdaahr rrwretygrg
//
LOCUS       WP_457664470             362 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces caniscabiei].
ACCESSION   WP_457664470
VERSION     WP_457664470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caniscabiei
  ORGANISM  Streptomyces caniscabiei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 999995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces caniscabiei"
                     /db_xref="taxon:2746961"
     Protein         1..362
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35255
     Region          1..333
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(1..2,5,37,87..88,90..92,95,114,117..118,121,196,
                     199..200,203..205,208,235,239,288..289,293,297,309,
                     312..313,316..317,320)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mavwgarmpa vqqaadlsta glalvllaaa vgmviglhvg grlaaparep llltsgavgl
       61 aaalavigac rtpltlapga fvfgiahgvl dvalnaaavr cqdrlgrfim sslhaayslg
      121 alggaglaal sahtshtwlf avtglavasa avamapvart lgmlepttpa tsrrspdpkd
      181 spglprarlw llgalaaacl lgegaaadwa avhlhsldas tavsaaafal ysafmaagrl
      241 agdrlttrfg apivvrtgav laaagltagl alatvpaala gwaalglgls vtipslitaa
      301 grggpravat vsvtgyagll agpaligala tltalpqall lpallaaava alsrkalenp
      361 tp
//
LOCUS       WP_457664518             521 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Vibrio campbellii].
ACCESSION   WP_457664518
VERSION     WP_457664518.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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 11459492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..521
                     /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=60236
     Region          4..518
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 miarflmita llvpfcsfst vvsldasaqt eqegavekls vekmihypev idqlyqstny
       61 rlnweneddv aqlifqmelv tladvtqefd nqlrrieqvr eqgdqldfdl vmtdsllmyl
      121 syleqvpeeg inwlfankvh vkfpapsiet lsllsneitv gkldqfltdl rsplqmdesf
      181 ntafsslsty akfefplyqq dqrlarvgde lfdkssliar mqivgvevgh ldtettlyde
      241 nlelavmefq rihglkqdgi igpntlrwin fspqlrlhsl alnaersriw skerdnvvfv
      301 nvpgyevtyw hdgqplfesk vvvgkasrkt pimtgtmdsv ilnptwnvpw kimvkdiipk
      361 vkrnpmylme hniqiirswt sreiidptti nwatvnprtf pyrmrqssgs hnalglykfn
      421 mpnpqaiylh dtpsknlfnq drrafssgcv rvehadqlae llfktqglee rlakkrqsgr
      481 rsntsvplte riqvhiiyqt awleegtlyy rddiyqydhq g
//
LOCUS       WP_457664519             234 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Vibrio campbellii].
ACCESSION   WP_457664519
VERSION     WP_457664519.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..234
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=26377
     Region          46..170
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(51,53,108..109,112)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            53
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(107,151..152,154..155,159)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(113,118..119,147,150..151,154..155,158,161)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(136..138,147..148,151..152,155,159,162,166)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(136,152,155,159,162,166)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(160,166..167)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          182..225
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(183..185,219..220,222..224)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 meqsqiylis lyqkklscfn tylknkvsip sytdefwyil rmnfvligya rvstqsqsld
       61 lqisalkkag cekiftdias gaktarpglk daemvlrkgd alvvwkldrl grsiqhlies
      121 inhlkgkgig frslqesidt qtsggklvfh ifsalaefer dlirertnag levarargkk
      181 ggrpkslsqs kniallkqmy adpnysiddi ckmlsisrst fyrylksdnn esdd
//
LOCUS       WP_457665138              92 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Thiolapillus
            sp.].
ACCESSION   WP_457665138
VERSION     WP_457665138.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..92
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10276
     Region          <8..75
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mltkkqkaly dafyesthan shldekteil iglsaaiamn cnpctsyylr lakqrsvsrg
       61 eisetlakvm avaagqkrlq fqevideyei df
//
LOCUS       WP_457665860             186 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Thiolapillus
            sp.].
ACCESSION   WP_457665860
VERSION     WP_457665860.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..186
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20786
     Region          <21..92
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
     Region          74..186
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mestasfmqa lkharsygig efleiigels qestkkglls rktkelitfg ialhkhcerc
       61 inihaedakk lgakekelel vrkislfmrs tpekdehlws twksswkqfv lgkgpirnrd
      121 relialamsi imqhkkhisl hvkeaiklgh sgaeivevlp iallmdgapa lsqiptlmka
      181 ieknsa
//
LOCUS       WP_457665943              93 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Thiolapillus
            sp.].
ACCESSION   WP_457665943
VERSION     WP_457665943.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..93
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10020
     Region          <4..87
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 metdaflgfl qkaesgkalg ikekelinva lavaaqcewc iafhveqavr agatrdeive
       61 sgfmavimhg gpaymymtpl leaideflpk dsd
//
LOCUS       WP_457666340             422 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105245].
ACCESSION   WP_457666340
VERSION     WP_457666340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (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   4  (residues 1 to 422)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19835644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..422
                     /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=44846
     Region          9..374
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          212..420
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mavtgfrkrv valtvliata vvavlvvvsh vllsrvtdad ahdlahtrae avaanvtarg
       61 grvvltengs ealdevawvy adgrlidgnv ppslvhrvee lagsgrsqtv svgdyllyar
      121 qipihghhvm vivrvdltpy etseqrsltl slilggltil laggvahlvv rralrvvhem
      181 aaladdwgrh epgrrfnlgv prdefgelgr tldhllervd saladerrlt deiahelrtp
      241 ltvlraeaql aqlsgepvpt eavlsevdrl dtaittllra arartdegtr cdlrsaarqa
      301 iagravevaf paevdvavap evavsllspl ldnglrhaks rvwitarnqd eaivvdvldd
      361 gpgfdpadvd rvfeagvtgg ggyglglpvv rriaasagve vraiadgrgh vemtlpaara
      421 aa
//
LOCUS       WP_457666381             219 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces sp. 900105245].
ACCESSION   WP_457666381
VERSION     WP_457666381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13585897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..219
                     /product="potassium channel family protein"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24092
     Region          54..185
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          <148..205
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mdvdsraarw eqrteiplfv aslvfmaaya trvlavglah wrdlclwvml alwavfaady
       61 lvrwrlggqr flrfvsthfl htvvvvlpll rplrivplyd viqrrqgepr lslyarvisy
      121 aslstlllgf agalavfqqe rgapgatmtt fgdavwwaas tlstvgygdi tpvtrlgrti
      181 aigmmacgig llgavtgsfs swlmqtftre sdrkgplgp
//
LOCUS       WP_457666405             145 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces sp.
            900105245].
ACCESSION   WP_457666405
VERSION     WP_457666405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..145
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15396
     Region          16..129
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msesttreer fahglevlna vdgeagrrvi dsladvspel ghqivswgfg eiyarpqlap
       61 rdrqlvtlgm ltalggcepq levhvnaaln vgltpeqive allhsagycg fpkalnatfv
      121 arkvfaergl lpleqpaeep paasa
//
LOCUS       WP_457666868             657 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Thiolapillus sp.].
ACCESSION   WP_457666868
VERSION     WP_457666868.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 657)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..657
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74998
     Region          25..327
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          294..470
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          584..639
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 midmllqkpl srpllwlsgl llllaaiphf ghinllisgs ftgliilrfl fwptpdkpap
       61 gwlllillpa alalvfylan wtegrqfgva llvlmagmkl lemktrrdly iavfmgyfil
      121 vtlflfyqdp litlyvflvs tgltglliat nlaedalpwq lilkrsatmm lgsipvmill
      181 fvlfprldgp lwslnlggns gltgmsdnih mgsisnlsqs reiafrvrfr ndpppaaqry
      241 wrgmvlwysd grnwerdkte kriarfvpqs qpydyeitme asgqpwlfpl dhvlaapqrl
      301 ilntygelys srdidtrhty rldsslqiry parnnrqlrm glqlprdisp rtrqlaqklr
      361 gqgrsdeqvi raalqffheq pfvytlqppl lyndpvdefl fdtrkgfceh yatsfvtlmr
      421 lagiparvii gyqggelnpi gghlvvrqsd ahawaevwle krgwvrvdpt aavapdrieh
      481 siaptpysvg aparfnlrnp paflsrlvrn lkwmgdnlql nwhywvvgfn sdrqqsllqk
      541 mglsrlrgyq lgiaaamgai ltgslvfllg mrhrrhrqdp vrqaytlfqr klektglnid
      601 patgpqdlln iasahcpeks adiqvimqqy malrygrhpr kdlisafrkr vrkfrcs
//
LOCUS       WP_457666870             314 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF58 domain-containing protein [Thiolapillus sp.].
ACCESSION   WP_457666870
VERSION     WP_457666870.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1001782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..314
                     /product="DUF58 domain-containing protein"
                     /calculated_mol_wt=34886
     Region          145..>308
                     /region_name="YeaD2"
                     /note="Uncharacterized conserved protein, DUF58 family,
                     contains vWF domain [Function unknown]; COG1721"
                     /db_xref="CDD:441327"
ORIGIN      
        1 mgnpllkllr vvrpdtgapa rvtgrkiyil ptryglvfgv llitlliasi nyannpafil
       61 tflltglfiq aifqtwrnll dlsvqwkqtd pvfagetaff qyrvwddkgr ahyalqlafa
      121 gndgiitdcp anekplvrlp crsrrrgvld pgrltletrf plgllrawcy ldtgargivy
      181 paplkghlnl aspswgmale gdrgvgaddf vghrsyhpgd qlghiywkal agekgllvkq
      241 fggdrvnryw ldfdaidsad tetrlrilag avqtlsrdaa hyglrlpdqe ipmdsgeshr
      301 qrclqalaly gvqt
//
LOCUS       WP_457666996             345 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces sp. 900105245].
ACCESSION   WP_457666996
VERSION     WP_457666996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13933993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..345
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37186
     Region          3..>189
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          96..289
                     /region_name="LysR_substrate"
                     /note="LysR substrate binding domain; pfam03466"
                     /db_xref="CDD:460931"
ORIGIN      
        1 melevrhlrv lcaiadtgsl hkaarqlgla qpslstqlrr iehalgaplf vrartgcrpt
       61 plglavlsra rplvaefaai vtetraaaar aaggfqlrig atasraipgw lrllrarvpr
      121 ieptlqmnvs anfllgmvaa grldiafvhe vegsplripp glslrvlver epqfvtlaad
      181 hpaaarrqvp lsdlagdrwm vdstvdgewd alcralraag lesemlhgdy ltayslaatg
      241 evvtvsqpta hprpdlairp legdpigvrl llaarteael ddvyqalaes ywtvardapa
      301 yrewlerarv plvpldraae pplgrrrpgc paqasarpaa psthr
//
LOCUS       WP_457667003             296 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Thiolapillus sp.].
ACCESSION   WP_457667003
VERSION     WP_457667003.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14206253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..296
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=31820
     Region          35..251
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK00059"
                     /db_xref="CDD:234605"
     Region          149..275
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mnsklkilat slllsgalqs gaqaedskaa qttapqatgp qtlvtingqa vtdievlafn
       61 alqggqnkld sqqaqvqlln qlvnttllaq eakkngidkl pqvaaalkma diqvlaeaev
      121 ntyfekhpvt daeikaaydk kftpenlqey kvrhilvkee keandiidal akgedfvela
      181 kkhsldsskd aggelgwvgr nqvvkpfgda mtglkkgehs skpvktqfgw hvidvediri
      241 qepppleqvk eqiklqiqqq klaqmvselr nnakvevagg aaqpeaapaa tpaakk
//
LOCUS       WP_457667140             584 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Thiolapillus sp.].
ACCESSION   WP_457667140
VERSION     WP_457667140.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..584
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62201
     Region          28..437
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mnlsrkihgw fsrqlestrl hlarpdaliq lavmglitgl lagavivcfr ylieaaqnla
       61 lsgngpdafe slspwmrfaf plagaialal mfrwfakgly vlgvarvler mayhqghltl
      121 rgfllqffgv aialisghsv gregahiflg attgsllgqk lelpnnavrt lvgcgtaagi
      181 aasfntplag vifslevimm dyqlasfipv ilsavtatvv snaflgnaav fsvpimelgs
      241 laeiplvvil gllsgtlaag fivmvkkiag sgkawaiewq mmaagisial lgmwlpevmg
      301 igydtinial vggysagvll lmaaakmvat sicsalnvpg gmigpsffig atlgagfghl
      361 miawlpdigi qpglyamlgm sammgaslqa plaaltalle ltdnpqiimp gmlvvviagl
      421 taselfgqes lfitmlkakg ldykqhpvlv alrrlgvasi mskdfvrstr nisleqahkl
      481 leskpkwivi tedkkpkail pgialagfle aeheeppeei dlmaipgkrl elapihlhet
      541 lqealeklnk gegealyvrr msapgiwriy giltreqies syql
//
LOCUS       WP_457667150             475 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Thiolapillus sp.].
ACCESSION   WP_457667150
VERSION     WP_457667150.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..475
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50766
     Region          66..452
                     /region_name="EriC_like"
                     /note="ClC chloride channel family. These protein
                     sequences, closely related to the ClC Eric family, are
                     putative halogen ion (Cl-, Br- and I-) transport proteins
                     found in eubacteria. They belong to the ClC superfamily of
                     chloride ion channels, which share a...; cd01034"
                     /db_xref="CDD:238506"
     Site            order(118..122,164..168,367..371,451)
                     /site_type="active"
                     /note="putative ion selectivity filter [active]"
                     /db_xref="CDD:238506"
     Site            166
                     /site_type="active"
                     /note="putative pore gating glutamate residue [active]"
                     /db_xref="CDD:238506"
     Site            221
                     /site_type="active"
                     /note="putative H+/Cl- coupling transport residue
                     [active]"
                     /db_xref="CDD:238506"
ORIGIN      
        1 mnalpvaqle qshclscskd hnshpfsrwh lpgmyrkrlr qsgkqlmsrr vwrtravflv
       61 gailvgiaas llamgsdwas etflhvidnr pwlpfiitpl glmliiwmtr nlfvgaegsg
      121 ipqaiaalhi krhkhlrhkl lslsiafgkg imiimgllcg asigregpti hiaasisfal
      181 trfarfphhd isrglilagg aaglaaafnt plagvmfaie emaknfeekt ngtvftavii
      241 agitalaing nyayfgtvfa kaefpgifsa vvicgvaggl lggsfsaflv yggrylrpwr
      301 sghpyllalv iglllacigl vsggqtwgtg yteaktalmg igldsegypa fkylatllsy
      361 wsgipggifa pslsigaglg aelsqwlpni svatvallgm aayftgvvqt pltaiiiime
      421 mtdnqgillp vmavaliadg iskiinpqpi yralaedfir dlspshsekq qgrer
//
LOCUS       WP_457667418             430 aa            linear   BCT 27-JAN-2026
DEFINITION  cyanophycinase [Streptomyces sp. 900105245].
ACCESSION   WP_457667418
VERSION     WP_457667418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Law,A.M., Lai,S.W., Tavares,J. and Kimber,M.S.
  TITLE     The structural basis of beta-peptide-specific cleavage by the
            serine protease cyanophycinase
  JOURNAL   J Mol Biol 392 (2), 393-404 (2009)
   PUBMED   19591842
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Obst,M., Sallam,A., Luftmann,H. and Steinbuchel,A.
  TITLE     Isolation and characterization of gram-positive
            cyanophycin-degrading bacteria-kinetic studies on cyanophycin
            depolymerase activity in aerobic bacteria
  JOURNAL   Biomacromolecules 5 (1), 153-161 (2004)
   PUBMED   14715021
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790602
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..430
                     /product="cyanophycinase"
                     /EC_number="3.4.15.6"
                     /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]"
                     /GO_process="GO:0043170 - macromolecule metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45310
     Region          31..339
                     /region_name="CphB"
                     /note="Cyanophycinase and related exopeptidases [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG4242"
                     /db_xref="CDD:443384"
ORIGIN      
        1 mnaralprrt vvlgtaaalv avltgvpaah aahsrqpatg slvlvggala sdnteiygei
       61 ikraggskar igvltaasip esqdpdsadp drcsnsacng ayyaslfkkh gaadaqwipi
      121 dldhidnads dtiadqvrsm tgfffgggdq yryvttllhg hqhtdskvla airdrlahga
      181 viagssagaq iaagpdmvtg gdsypalrdg sspgyfddps rlgylpdggf gflgsglidt
      241 htgaegregr alrlasdtgh drvyaldent alvvdapgtq reaitvlgan gvgvfdlrra
      301 rtrhdrlgws lrnarytylt dgdrydprrw laspaqgkhr ltpiddtavp anddvfysla
      361 dpagtpysfr gtaralaats aqrsatatty etgprfrvtl tktrafsawa eeadsapqsl
      421 idmriavape
//
LOCUS       WP_457667571             577 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Thiolapillus sp.].
ACCESSION   WP_457667571
VERSION     WP_457667571.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 577)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 577)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..577
                     /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=61780
     Region          7..568
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,393,396..397)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mdlqtltyiv vgatfalyig iaiwarakst sdfyvagkgv npvlngmata adwmsaasfi
       61 smagliafyg yggsvflmgw tggyvllaml lapylrkygk ftvpefigdr yygksarila
      121 vicliiasit yvigqmkgig vafsrfletd ydtglyigmg ivfiyavmgg mkgitytqia
      181 qycvlifayt vpavfismhl tgnpipqigl gskmadgsgm flldkldatl kglgfteytt
      241 ntrlstlnmf vytmslmigt aglphvimrf ftvpkvrdar atagwalvfi allytvapav
      301 gamarmnlmd tiqpapgksi syeqrpqwfk nwektgllkf edkngdgkiq yvadkaknem
      361 vkvdrdimvl anpeiaklpn wvvalvvagg laaalstaag lllaiassis hdllkgvfap
      421 disekselma srvamagaia aagylglhpp dfaagtvala fglaassifp almmgifskk
      481 mnkqgamagm lvgigitlfy vfqhkgiffv adwkylqswg snwfmgiepn afgaigavfn
      541 fatafivakv tapppehiqh mvedirvpvg agaatgh
//
LOCUS       WP_457667993             160 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 900105245].
ACCESSION   WP_457667993
VERSION     WP_457667993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17060
     Region          5..131
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          74..149
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mdvrveiare agqelvdafg rllpqlssra epldheaver mvtsdattvl vartvdgiag
       61 tltlallplp sglrgriedv vvdsaargqg iaglliqeal riaeeagart vdltsrpdre
      121 aanrlyerlg fharrstvyr vegfpadpag kpptaldanr
//
LOCUS       WP_457668171             199 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase [Streptomyces sp. 900105245].
ACCESSION   WP_457668171
VERSION     WP_457668171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..199
                     /product="acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20850
     Region          4..>61
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     Region          35..160
                     /region_name="LbH_WxcM_N_like"
                     /note="WcxM-like, Left-handed parallel beta-Helix (LbH)
                     N-terminal domain: This group is composed of Xanthomonas
                     campestris WcxM and proteins with similarity to the WcxM
                     N-terminal domain. WcxM is thought to be bifunctional,
                     catalyzing both the isomerization...; cd03358"
                     /db_xref="CDD:100048"
     Site            order(56,58,66,74,76,82,88..90,114,116,119,138,154)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100048"
     Site            order(58,60,88,90,116,118..119,124,136..137,142..143,
                     152..153,155)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100048"
     Site            order(58,60,88)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:100048"
     Site            order(88,90,116,118..119,124,134,136..137,142..143,150,
                     152..153,155,159)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100048"
ORIGIN      
        1 msnriqptaq vderatvgdg ttvwdlaqir egarlgtgci vgrgayvgpg vrigdnvklq
       61 nyalvyepav lgdgafvgpa avltndyfpr svdpqgrlkr gddweavavv vgegaslgar
      121 svcvapvrvg rwalvaagav vtrdvpdfal vagvparrig wvgragvrlv eredvpggwe
      181 cpetgalyee kdgelvera
//
LOCUS       WP_457668447             233 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Thiolapillus sp.].
ACCESSION   WP_457668447
VERSION     WP_457668447.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 233)
  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 233)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13412423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..233
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27321
     Region          29..219
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          65..157
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mkknermrpa veegeldfsg kyslerarey yhkhqkgslg rrisnrweqh maskalklag
       61 npgsvldlpc gtgrfwella sdpdrellaa dyseamlvva qeerppeivq rfrvfqssaf
      121 diqlpddave nifcmrllhh igesedrlri lkefhrvard svcismwvdg nykawkrqra
      181 vqnrpkrkrf dnrflhtrqq vesefaeagf sirgkvdflp ryamwrtyvl ece
//
LOCUS       WP_457668857             261 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Thiolapillus sp.].
ACCESSION   WP_457668857
VERSION     WP_457668857.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..261
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27629
     Region          4..261
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msdkdtfsva grefssrllv gtgkyrdmee traaidasga eivtiavrrt nigqnsdepn
       61 ildvlppekf tilpntagcy dqktavrtcr larelldghn lvklevlgde ktlfpdvmat
      121 lkaaeelikd gfdimvytnd dpiiareled mgcaavmpla apigsglgvr nplnirtive
      181 nakvpilvda gvgtasdaav amelgcdgvl mntaiaaaqd pvlmasamkk aiqagreafl
      241 agrmpakrfa sasspvdglf f
//
LOCUS       WP_457669318             344 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces sp.
            900105245].
ACCESSION   WP_457669318
VERSION     WP_457669318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   di Salvo,M.L., Safo,M.K., Musayev,F.N., Bossa,F. and Schirch,V.
  TITLE     Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate
            oxidase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 76-82 (2003)
   PUBMED   12686112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1562906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..344
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37309
     Region          30..134
                     /region_name="YzzA"
                     /note="General stress protein 26 (function unknown)
                     [Function unknown]; COG3871"
                     /db_xref="CDD:443080"
ORIGIN      
        1 mslsstsqdr pghdkvaahr asppeaacgl hdvldayrtc efvtlgrdgt plawptavar
       61 redgtllvtt clafaqkasn vrrdgrvall fsdptgsglg hapqvfvsgr aecpetimag
      121 pqgaedywrr lferqphsrs ylthpmrplm swyylrllit vepehvdlrp pleelvhhga
      181 pvsvagtppl pgaaqlgrap savlaarnas gapvlartlp rptpsgylve vsadcpvedg
      241 pagllvhrhd erlnhmynaf vrgtlqrtga gwllvpsrvi epmgsgrakd alrvlrrtkr
      301 stdrylarrg ltrpkvewds fralvqpapv lpaapspvkg sphh
//
LOCUS       WP_457669546             526 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces sp.
            900105245].
ACCESSION   WP_457669546
VERSION     WP_457669546.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 526)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 526)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..526
                     /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=56112
     Region          4..490
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(51,54,330,333..334)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mngldwavli gyfgvmvaig vwshkrvdnv sdfftaggkm pwwlsgishh msgysavmft
       61 gyagiaytyg vtsfitwsfp ialgiaigsk lfaprinrlr srlhvasple ylknrydlpt
      121 qqalawsgml lkivdvgakw aaiatllsvf tgvslnqgiv itgaitavyc tigglwadal
      181 telgqfviql lagvsmfvav vlklsdqhig flgawdepal hghgkplvgp ygtvfllafl
      241 fiklfeyngg mlnqaqryma tgsahqaers arlsailwlv wpvvlffpmw mspllvhaqk
      301 pdgsdsyalm teqllphgll glvivgffsh tmamcssdan aiaavftrdv apvlsararg
      361 wgersglvaa rvttvvflal smavatqvns pafkdiitvv ikwvaglmgp iaipmmlgll
      421 rafrrsgpta altswaagll afwlvnypvn wnvdggvplq yqvsvplavs lvlyvligyl
      481 kpedtperla vietvntdgg aalavpvssg agddaaaats sggdvs
//
LOCUS       WP_457669743             794 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Streptomyces sp. 900105245].
ACCESSION   WP_457669743
VERSION     WP_457669743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..794
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=80903
     Region          205..726
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
     Region          525..780
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC C-terminal domain,
                     metallo-beta-lactamase superfamily [Intracellular
                     trafficking, secretion, and vesicular transport]; COG2333"
                     /db_xref="CDD:441904"
ORIGIN      
        1 mpelarrfat vtaevelsgd pwlsrprvrg drtaseavli raevrrveds dgtgartrtp
       61 vllvvdadvp apdggarpgp gapgppatag elpggdaehg hdararpaga vtgaggsagv
      121 psagvregvp ggraawlgll pstrlrvggr lapaltegdr taavlrvrgr pgprivagps
      181 gpqrlagrlr aglrqatdgl pqdarallpg lvvgdtarit peldgafket dlahtlavsg
      241 snltvllall igppglaqla errglaprlg lslratalsa galtlafvvv crpdpsvlra
      301 aacgaaalla latgrrrsll palaavvlll vlydpwlsrs ygfllsvlat gallvlapgw
      361 sealrrrrvp prlaealgat aaaqavcapv vavlsarvsl vavpcnllae aavapatvlg
      421 faalasaqva mpaakafawl aswpagwiag vartgaalpg agvdwpgswa galllaavtv
      481 avvltgrrll rrpwwcallg lllllavvrp apltrvitgw pppgwrfamc dvgqgdatvl
      541 aagegagvvv dagpdpapvd qclrhlgitr vpllvlthfh adhvaglpgv lrgrsvaeie
      601 ttgfeepagq aafvrreaaa rhipvtrava geerrsgpla wrvlwppptv rpppgapapp
      661 pwpgappepd gpndasvall vrtgglrlll lgdleppaqq allrspaaad vagvdvlkva
      721 hhgsayqepe lmrlaaprva lvsagadnpy ghpapstlaa lraggavvlr tdrdgalavt
      781 rapgaggevr vtre
//
LOCUS       WP_457669754             422 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105245].
ACCESSION   WP_457669754
VERSION     WP_457669754.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (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   4  (residues 1 to 422)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19835644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..422
                     /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=44844
     Region          9..374
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          212..420
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mavtgfrkrv valtvliata vvailvvvsh vllsrvtdad ahdlahtrae avaanvtarg
       61 grvvltengs ealdevawvy adgrlidgnv ppslvdrvee lagsgrsqtv svgdyllyar
      121 qipihghhvm vivrvdltpy etseqrsltl slilggltil laggvahlvv rralrvvhem
      181 aaladdwgrh epgrrfnlgv prdefgelgr tldhllervd saladerrlt deiahelrtp
      241 ltvlraeaql aqlsgepvpa eavlsevdrl dtaittllha arartekgtr cdlrsaarqa
      301 iagravevaf paevevavap evavsllspl ldnglrhaks rvwitarnqd eaivvdvldd
      361 gpgfdpadvd rvfevgvtgg ggyglglpvv rriaasagve vraiadgrgh vemtlpaara
      421 aa
//
LOCUS       WP_457669966             314 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF58 domain-containing protein [Thiolapillus sp.].
ACCESSION   WP_457669966
VERSION     WP_457669966.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1001782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..314
                     /product="DUF58 domain-containing protein"
                     /calculated_mol_wt=35056
     Region          144..>311
                     /region_name="YeaD2"
                     /note="Uncharacterized conserved protein, DUF58 family,
                     contains vWF domain [Function unknown]; COG1721"
                     /db_xref="CDD:441327"
ORIGIN      
        1 mdnpllrfqr vvrpradgqs rvsgrkiyil ptrygmvfgv llvtlliasi nyannpafil
       61 tflltglfiq gifhtwrnll nlhlqwrhad pvfagetaff hfqlgdekgr ahyaiqlsfa
      121 asdsiitdcp anekvqirlp castrrglle pgritmetrf plgllrawcy vetsaqaviy
      181 prplqenpgv aspswgaave gnkgvgtddf vghrnyhpgd plghiywkal agekgllvkq
      241 fggdrvnrfw ldfdalenad tekrlcilsg avqtlaqdas yyglrlpdee ipiatgeahr
      301 hrclqalaly qvek
//
LOCUS       WP_457669967             658 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Thiolapillus sp.].
ACCESSION   WP_457669967
VERSION     WP_457669967.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 658)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 658)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..658
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74043
     Region          27..321
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          293..471
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          585..>637
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 mkdllilkpl srpllwltaa llvlaaiphw wnmsplvsas lpllvamrll lwpapekpap
       61 rpvmlallla slvlvlyqad ltegrqfgva llvvmagmkv lemktrrdly vsvflgyfil
      121 itlflfyqsp lltfyvllms tgftgllvaa nqtrdslpwk lllskalvmv lasipvmill
      181 fvlfprldgp lwtlnlgsgs gvtgmsdnir mgsisnlsqs tevafrvrfk geippppqry
      241 wrgmvlwltd grnwereess ppsrgfaplg qaveyeitme psgqpwlfpl dhilgspvtg
      301 lslnqdgels tikpihtrkt ypafsapgir prklqvrewq lglqlpedit prtrrlaaql
      361 rgqgatdrev vqaalrfynq eafiytlqpp llknnpvdef lfstrkgfce hyatsfvvlm
      421 rladipsrvv igyqggernp mgghlvvrqs dahawaevwl edqgwvrvdp taavaperie
      481 hsitasdyat gapvtfhlgd speffarmak nmkwlrdnlq lnwhywvvgf nssrqqtllq
      541 klglddlygy rlgvaaalga milgavtfll gmrrrshgkd rvhqaylrfq rklrksglei
      601 spttgprdll kiavrrcpqq sadiqaivgq ymalrygkkp rkdmvssfck rvrkfrcs
//
LOCUS       WP_457670118             135 aa            linear   BCT 27-JAN-2026
DEFINITION  Asp23/Gls24 family envelope stress response protein [Streptomyces
            sp. 900105245].
ACCESSION   WP_457670118
VERSION     WP_457670118.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Muller,M., Reiss,S., Schluter,R., Mader,U., Beyer,A., Reiss,W.,
            Marles-Wright,J., Lewis,R.J., Pfortner,H., Volker,U., Riedel,K.,
            Hecker,M., Engelmann,S. and Pane-Farre,J.
  TITLE     Deletion of membrane-associated Asp23 leads to upregulation of cell
            wall stress genes in Staphylococcus aureus
  JOURNAL   Mol Microbiol 93 (6), 1259-1268 (2014)
   PUBMED   25074408
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Stoyanov,J.V., Mancini,S., Lu,Z.H., Mourlane,F., Poulsen,K.R.,
            Wimmer,R. and Solioz,M.
  TITLE     The stress response protein Gls24 is induced by copper and
            interacts with the CopZ copper chaperone of Enterococcus hirae
  JOURNAL   FEMS Microbiol Lett 302 (1), 69-75 (2010)
   PUBMED   19903200
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..135
                     /product="Asp23/Gls24 family envelope stress response
                     protein"
                     /calculated_mol_wt=13985
     Region          <75..128
                     /region_name="Asp23"
                     /note="Asp23 family, cell envelope-related function;
                     cl00574"
                     /db_xref="CDD:469828"
ORIGIN      
        1 mktrpgspge gsgppapaag lpppaergat vipdwvvari aaqaaraaqa rraavppdrg
       61 gpaaphasaa vrtgsvrlhl tmdlpyptdi prvceriqrd vaervaqltg lrvgevlltv
      121 rrlvtatdss rgrvr
//
LOCUS       WP_457670854             261 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces sp.
            900105245].
ACCESSION   WP_457670854
VERSION     WP_457670854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  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 261)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1008156
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..261
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28442
     Region          37..142
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mgtvtrgttn pnrlrrmdrw iaavhgaelr rasapvavdl gygaapwtav ellarlraaa
       61 prtrvvgvei epdrvaaarp yereglafrh ggfevpvpgr paliraanvl rqydeaqvaa
      121 vwerlcarla pagdgsrggl lvegtcdeig rrhvwvalgp egprtvtfat rlgslerpad
      181 laerlpkali hrnvpgepvh aflrdfdraw aaaapyasyg arqrwlravg dltadwpvtd
      241 rparwrqgev tvawealapr g
//
LOCUS       WP_457671012             430 aa            linear   BCT 27-JAN-2026
DEFINITION  cyanophycinase [Streptomyces sp. 900105245].
ACCESSION   WP_457671012
VERSION     WP_457671012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Law,A.M., Lai,S.W., Tavares,J. and Kimber,M.S.
  TITLE     The structural basis of beta-peptide-specific cleavage by the
            serine protease cyanophycinase
  JOURNAL   J Mol Biol 392 (2), 393-404 (2009)
   PUBMED   19591842
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Obst,M., Sallam,A., Luftmann,H. and Steinbuchel,A.
  TITLE     Isolation and characterization of gram-positive
            cyanophycin-degrading bacteria-kinetic studies on cyanophycin
            depolymerase activity in aerobic bacteria
  JOURNAL   Biomacromolecules 5 (1), 153-161 (2004)
   PUBMED   14715021
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790602
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..430
                     /product="cyanophycinase"
                     /EC_number="3.4.15.6"
                     /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]"
                     /GO_process="GO:0043170 - macromolecule metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45158
     Region          31..339
                     /region_name="CphB"
                     /note="Cyanophycinase and related exopeptidases [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG4242"
                     /db_xref="CDD:443384"
ORIGIN      
        1 mnaralprrt vvlgtaaalv avltgvpaah aahsrqpatg slvlvggala sdnteiygei
       61 ikraggskar igvltaasip esqdpdsadp drcsnsacng ayyaslfkkh gaadaqwipi
      121 dldhidnads dtiadqvrsm tgfffgggdq yryvttllhg hqhtdskvla airdrlahga
      181 viagssagaq iaagpdmvtg gdsypalrdg sspgyfddps rlgylpdggf gflgsglidt
      241 htgaegregr alrlasdtgh drvyaldent alvvdapgtq reaitvlgan gvgvfdlrra
      301 rtrhdrlgws lrnarytylt dgdhydprrw laspaqgkhr ltpiddtavp anadvfysla
      361 dpagtpysfr gtaralaats aqrsataaty etgprfrvtl tktpafsawa eeadsapqsl
      421 idmriavape
//
LOCUS       WP_457671020             137 aa            linear   BCT 27-JAN-2026
DEFINITION  Asp23/Gls24 family envelope stress response protein [Streptomyces
            sp. 900105245].
ACCESSION   WP_457671020
VERSION     WP_457671020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Muller,M., Reiss,S., Schluter,R., Mader,U., Beyer,A., Reiss,W.,
            Marles-Wright,J., Lewis,R.J., Pfortner,H., Volker,U., Riedel,K.,
            Hecker,M., Engelmann,S. and Pane-Farre,J.
  TITLE     Deletion of membrane-associated Asp23 leads to upregulation of cell
            wall stress genes in Staphylococcus aureus
  JOURNAL   Mol Microbiol 93 (6), 1259-1268 (2014)
   PUBMED   25074408
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Stoyanov,J.V., Mancini,S., Lu,Z.H., Mourlane,F., Poulsen,K.R.,
            Wimmer,R. and Solioz,M.
  TITLE     The stress response protein Gls24 is induced by copper and
            interacts with the CopZ copper chaperone of Enterococcus hirae
  JOURNAL   FEMS Microbiol Lett 302 (1), 69-75 (2010)
   PUBMED   19903200
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..137
                     /product="Asp23/Gls24 family envelope stress response
                     protein"
                     /calculated_mol_wt=14411
     Region          28..122
                     /region_name="Asp23"
                     /note="Asp23 family, cell envelope-related function;
                     cl00574"
                     /db_xref="CDD:469828"
ORIGIN      
        1 mntlpepvvp tgdragrhpa salpppaerg atiipdkvvg riaaeagrva qrnraavpqd
       61 rdpgaapsas vvsqagavrl rlavdlpypt dlarvceqiq hdvgdrvaql tgmrvdevtl
      121 tirrlltapg pgrrrvr
//
LOCUS       WP_457671276             582 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Thiolapillus sp.].
ACCESSION   WP_457671276
VERSION     WP_457671276.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..582
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62006
     Region          28..437
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mnpyrkihaw fstqlentrl hlarpdamiq laiiglltga laglvivafr llveqtqtwl
       61 lpgdspeaye llphwailal plagaillal mfrwlakgly vlgvarvler mayhqghlgl
      121 refllqffga aiaiisghsv gregphvylg aaagsllgqw ltlpnnairt lvgcgtaagi
      181 aasfntplag vifalevvml dyhlasfipv ilaavtatmv snamlgseaa ftmpamalgg
      241 lseiplviil gliagavsas fthlvqvvas nsrnlaiwwk vllagvitgl lglavpeimg
      301 igydtvnatl lgsygaafll llmgakliat sacvglgvpg gmigpalfig atlgasmgql
      361 aqlwmphldt qvgffamlgm galmgaslqa plaaltalle ltnnpqiimp gmlvviiagl
      421 tasqvfgqes lfitmlkarg ldyqqnpvla vlrrmgvasi mdkqfvrspr ainpetawel
      481 lkskpkwivv tkdntpafil sgislagyle veqeqeeidl meipgtrlql apvhlhetlq
      541 ealekldkge gealyvrhms apgiwrvygi ltreqiesay ql
//
LOCUS       WP_457671344             360 aa            linear   BCT 27-JAN-2026
DEFINITION  protein kinase family protein [Streptomyces sp. 900105245].
ACCESSION   WP_457671344
VERSION     WP_457671344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 229378
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..360
                     /product="protein kinase family protein"
                     /calculated_mol_wt=39450
     Region          <167..>255
                     /region_name="PKc_like"
                     /note="Protein Kinases, catalytic domain; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 mhhpdpryaa rlatygtvat rlsllsdrrl gevvaaaapl gsgiggrsae ldidgtqvfv
       61 krvpltdtel rpenarstan lfglpmfyqy gvgsagfgaw relavhvmtt nwvlgneyeg
      121 fplmyhwril pdsppegfad efggiegava hwegssavre rleaigrsss slvlflehvp
      181 qtlgdwlndh rtaapeggag saylwveeal srgtafmssh glvhfdahfa nvltdgrlly
      241 fadfglalss gfelsaaeae flsdhlsydr chtashllrh hlpdgvrggm eheaflrewi
      301 aghrpdgvpr efaaiidrhs raavifgefa rrllteskrt pfptaeierv wrttavaaph
//
LOCUS       WP_457671833             706 aa            linear   BCT 27-JAN-2026
DEFINITION  nitric oxide reductase activation protein NorD [Thiolapillus sp.].
ACCESSION   WP_457671833
VERSION     WP_457671833.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Edwards,Y.J. and Perkins,S.J.
  TITLE     The protein fold of the von Willebrand factor type A domain is
            predicted to be similar to the open twisted beta-sheet flanked by
            alpha-helices found in human ras-p21
  JOURNAL   FEBS Lett 358 (3), 283-286 (1995)
   PUBMED   7843416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..706
                     /product="nitric oxide reductase activation protein NorD"
                     /calculated_mol_wt=80958
     Region          273..706
                     /region_name="NorD"
                     /note="Nitric oxide reductase activation protein
                     [Inorganic ion transport and metabolism]; COG4548"
                     /db_xref="CDD:443612"
ORIGIN      
        1 mpspdsmprd varinallee ilevefsflh tgtiaaalsr lprdsrkfil qwtrrvsstn
       61 iqlafefasr agqalaamde emisawclha mdtydsaglh pamkvikdlq gfvetghlra
      121 raalweqvrp vlgpfiqgls grmlhmeegg sawtdgdtly lpgmlayfae eeqnfqlyka
      181 lathlwahtr ygtlnidpel llapwenrqr aihwfhvlet lrldcrlqqd lpglyrqmrr
      241 lqqrldggrw pdvpaevlss lqessstpyd svrllrklya sspprlpcya gelkleeawv
      301 areqrllrdq arfrhalrvi addistdaqq sppfslrekr qdagfaelpe melmiadqvv
      361 pvpesmkqli tsirldlaai peeylvpage geydpslled esldpddvwg gtyheegaff
      421 ydewdfgrqh yrknwcvlre lepqpgdssf ydqtrekyrg lihslhrtfe vlrgedrvlr
      481 rqpvgedidi dafvealadm rsgmemsdqv yarmrrdern iavlfmvdms gstkgwinea
      541 ereslvllte slqilgdrya iygfsgwark rcevfriktf adplddavka niaaieakdy
      601 trmgapirhf trmleavear tkllitlsdg kpddydhyyr geygiedtrq alfearmagi
      661 hpfcitidre gadylphmyg kanyvvldev aklplkvsdi yrrits
//
LOCUS       WP_457671888             262 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Thiolapillus sp.].
ACCESSION   WP_457671888
VERSION     WP_457671888.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..262
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27795
     Region          4..262
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msdskdtfrv agrefssrll vgtgkykdmd etraaieasg aeiitiavrr tnigqhadep
       61 nvldvlppdr ftilpntagc ydqktavrtc rlarelldgh nlvklevlgd ektlfpdvma
      121 tlkaaeelik dgfdvmvytn ddpivarele amgcvavmpl aapigsglgv rnplnirtiv
      181 enakvpilvd agvgtasdaa vamelgcdgv lmntaiaaaq npvlmasamk kaiqagreay
      241 lagrmpakrf asasspmegl ff
//
LOCUS       WP_457671937             164 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase, partial [Streptomyces sp. 900105245].
ACCESSION   WP_457671937
VERSION     WP_457671937.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..>164
                     /product="acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
     Region          4..>61
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     Region          35..160
                     /region_name="LbH_WxcM_N_like"
                     /note="WcxM-like, Left-handed parallel beta-Helix (LbH)
                     N-terminal domain: This group is composed of Xanthomonas
                     campestris WcxM and proteins with similarity to the WcxM
                     N-terminal domain. WcxM is thought to be bifunctional,
                     catalyzing both the isomerization...; cd03358"
                     /db_xref="CDD:100048"
     Site            order(56,58,66,74,76,82,88..90,114,116,119,138,154)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100048"
     Site            order(58,60,88,90,116,118..119,124,136..137,142..143,
                     152..153,155)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100048"
     Site            order(58,60,88)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:100048"
     Site            order(88,90,116,118..119,124,134,136..137,142..143,150,
                     152..153,155,159)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100048"
ORIGIN      
        1 msnriqptaq vderatvgdg ttvwdlaqir eearlgtgci vgrgayvgpg vrigdnvklq
       61 nyalvyepav lgdgafvgpa avltndyfpr svdpqgrlkr gddweavavv vgegaslgar
      121 svcvapvrvg rwalvaagav vtrdvpdfal vagvparrig wvgr
//
LOCUS       WP_457672025             328 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces sp.
            900105245].
ACCESSION   WP_457672025
VERSION     WP_457672025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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 328)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1000387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..328
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34580
     Region          <69..>161
                     /region_name="HemK"
                     /note="Methylase of polypeptide chain release factors
                     [Translation, ribosomal structure and biogenesis];
                     COG2890"
                     /db_xref="CDD:442135"
ORIGIN      
        1 mstqiahael vlspgeffei edparirssl glrlsdhsyl pkadepradw vasvavpafk
       61 tlaemgflap rfctigtgag ldvlaaveil karhvgftdl hedvvacara nieanllard
      121 velvagagdl laplagklsq ldvvyenlpn ipmarsadld dgqtsstfia erdeeipgfa
      181 eknlvtlhyl alqqahpalr vggwvlssig ariplseila lsgaagyngs iltytwkvqs
      241 epdevvggfa rwegeglgpf hfypvpvlrd afaglspaga garalgieqe laphaitaad
      301 alrlveqgek vghtvailds vkipgsal
//
LOCUS       WP_457672170             410 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces sp. 900105245].
ACCESSION   WP_457672170
VERSION     WP_457672170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 999995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41241
     Region          13..381
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(23..24,27..28,31,63,114..115,117..119,122,142,
                     145..146,149,223,226..227,230..232,235,252,256,309..310,
                     314,318,333,336..337,340..341,344)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
ORIGIN      
        1 mpsyrslvrt peftplllgs aaqtaaqtvg glalgtlvyr atgspllsav smfgpslaqv
       61 lgatvllsga drlpprtals aialafaagt avqavpglpv gavfavllal glaaslgggv
      121 rwgllheiip kdgylpgrsl fhmmngllqv agfatggall aalspracll lsaalqltaa
      181 lvlrlglsar rprttgrpsp satwranall wssrprrlty lglwvpgglv vgceslyvsy
      241 aphaagalfa cgalgmfagd vtvgrllrpg vrrrlatpll lllavpflvf carppllvaa
      301 vcvtvasagf gaslvqqerl meltpgelag qalglhsagm ltlqglgaal agavaqftsp
      361 aaamsataag svcvtlalat aarrtparrs pappagalpp svsarepsps
//
LOCUS       WP_457672350             722 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Streptomyces sp. 900105245].
ACCESSION   WP_457672350
VERSION     WP_457672350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105245
  ORGANISM  Streptomyces sp. 900105245
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Streptomyces sp. 900105245"
                     /db_xref="taxon:3154379"
     Protein         1..722
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75773
     Region          21..401
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          371..547
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          667..>718
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 msgrarlalc aaaatlmasc allplvaept wllqlvplva vqtgvgaaar rvplgrpltv
       61 aaqalvtlml ltlvfareha laglvpgpdt frylaellqq gaddvsqyai papltdgikl
      121 mliggvllig llvdtiavtf rsaapaglpl lalysvaagl sdgaadwlwf lvaaagylml
      181 llaegrdrla qwgrvfggap rtpgspdpgv aapvrtgrri gavalgvall vpaalpamqg
      241 glldaagtgv gagngnggti savnplvslr dslntdndrr vlslrtstsd isdlylrivs
      301 ldefdgttwt parrhvvgvp delptpvglg tdvkrgkvrt tvtaadwyaq nwlpmpypps
      361 evkvagrwry epvgmtvvgd hgqstrgqty qvtslnvrpt aeqladapep paaleraytr
      421 vpsslpkevs rtakeiasga kshyeeavrl qdyfavnggf qydtsvkvgr gpnaivnfle
      481 qkegfcvhfs famaamartl giparvavgf apgtpqadgt vsvserdaha wpelyfegig
      541 wtrfeptptr gttpsytqsd tpgdalpdpa lpsknassqp saaaspsesc anelrrlqac
      601 dspsaaaaph pgnggpspww lllvpgvlva laiplspllw rertrsrrlg ghprtpegaa
      661 ahtlavwqel tdsawdhgip pdesltprga aarlvrlghl dpadgasvhr vadaveqvss
      721 ir
//
LOCUS       WP_457673069              74 aa            linear   BCT 27-JAN-2026
DEFINITION  AbrB/MazE/SpoVT family DNA-binding domain-containing protein
            [Thiolapillus sp.].
ACCESSION   WP_457673069
VERSION     WP_457673069.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..74
                     /product="AbrB/MazE/SpoVT family DNA-binding
                     domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8633
     Region          5..74
                     /region_name="MazE_antitoxin"
                     /note="Antidote-toxin recognition MazE, bacterial
                     antitoxin; cl00877"
                     /db_xref="CDD:469969"
ORIGIN      
        1 mlkvkvirig nstgiewprm alrrfdvteg delylvekrd glilipcerh ldeqlqaaeq
       61 vlkryrdtlr rlak
//
LOCUS       WP_457673120             581 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Thiolapillus sp.].
ACCESSION   WP_457673120
VERSION     WP_457673120.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 581)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 581)
  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 10799491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..581
                     /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=62343
     Region          7..572
                     /region_name="Na_symport_lg"
                     /note="probable sodium:solute symporter, VC_2705
                     subfamily; TIGR03648"
                     /db_xref="CDD:274698"
     Site            order(51,54,397,400..401)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271374"
ORIGIN      
        1 mdlqtltyiv vgatfalyig iaiwaraktt gdfyvagkgv ppvlngmata adwmsaasfi
       61 smagliafyg yggsvflmgw tggyvllaml lapylrkygk ftvpefigdr yygksarila
      121 vicliiasvt yvigqmkgig vafsrfletd ydtglyigmg ivfiyavmgg mkgitytqia
      181 qycvlifayt vpavfismhl tgnpipqlgl gstmsdgsgm ylldkldatm kdlgfgtytd
      241 kvrlstfnmf vytmslmigt aglphvimrf ftvprvrdar asagwalvfi allytvapav
      301 gamarlnlme tihptsgpna gqwlevdqrp qwfknwektg llkfedkngd griqyvadke
      361 knemvkvdrd imvlanpeia klpnwvvalv vagglaaals taaglllaia ssishdllkg
      421 vfapniseks elmasriama gaiaaagylg lhppdfaagt valafglaas sifpalmmgi
      481 fsktmnkqga magmlvgigi tlfyvfqhkg iffiadwkyl qswgsnwfmg vepnafgaig
      541 avfnfitafi vakitapppe hiqhmvenir vpagagaatg h
//
LOCUS       WP_457673257             377 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein, partial [Thiolapillus sp.].
ACCESSION   WP_457673257
VERSION     WP_457673257.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..>377
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          33..377
                     /region_name="EriC_like"
                     /note="ClC chloride channel family. These protein
                     sequences, closely related to the ClC Eric family, are
                     putative halogen ion (Cl-, Br- and I-) transport proteins
                     found in eubacteria. They belong to the ClC superfamily of
                     chloride ion channels, which share a...; cd01034"
                     /db_xref="CDD:238506"
     Site            order(85..89,131..135,334..338)
                     /site_type="active"
                     /note="putative ion selectivity filter [active]"
                     /db_xref="CDD:238506"
     Site            133
                     /site_type="active"
                     /note="putative pore gating glutamate residue [active]"
                     /db_xref="CDD:238506"
     Site            188
                     /site_type="active"
                     /note="putative H+/Cl- coupling transport residue
                     [active]"
                     /db_xref="CDD:238506"
ORIGIN      
        1 myrkrlrqsg rqlisrrvwr travflmgai lvgiaatmla wgsdwasetf lhvtrdrpwl
       61 pflitplglm liiwmtrnlf vgaegsgipq aiaalhlkrh khlrhrllsl piafgkgimi
      121 vlgllcgasi gregptihia asisfaltrf arfphhdisr glilaggaag laaafntpla
      181 gvmfaieema knfeektngt vftaviiagi talaingnya yfgtvfatvd fpeifsavvv
      241 cgvvgglagg sfsaflvygg ryirpwrnkh pyllalaigl llagiglmsg gqtwgtgyse
      301 aktalmgigv dfqgypayky latllsywsg ipggifapsl sigaglgael sqwlpdvsva
      361 tvallgmaay ftgvvqt
//
LOCUS       WP_457673800             423 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105755].
ACCESSION   WP_457673800
VERSION     WP_457673800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  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 423)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..423
                     /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=45047
     Region          77..>152
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          106..129
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          193..419
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstvsgdisi rtfegrrwlf psaviheldp dagpagrrpr rtardwlvdf scfllavllg
       61 vaaantmrqd phvphglava dqligglsca avwlrrrwpt glaiamipvs fasdaaggas
      121 mvalftlavh rpfrhvawit aanlvlvplf ywlrpdpdlp ylavvilvvl ltllvvslgm
      181 fvrskrqlmv slrdrarrae teaglraera qrlareaiar emhdvlahrl tllsvhagal
      241 efrpdapree iaraagvire sahealqdlr eiigvlraad gdeaggrpqp tlaaldslva
      301 evrgagmkvv ldnhvgdpaa vpasvgrtay riaqegltna rkhapgaevt vrvtgapgdg
      361 lditvhnpap ateaphvpgs gqgliglter atlaggrleh ravgdggfev rawlpwaaas
      421 paa
//
LOCUS       WP_457674484             862 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Streptomyces sp. 900105755].
ACCESSION   WP_457674484
VERSION     WP_457674484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..862
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=87731
     Region          286..842
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
     Region          606..845
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC C-terminal domain,
                     metallo-beta-lactamase superfamily [Intracellular
                     trafficking, secretion, and vesicular transport]; COG2333"
                     /db_xref="CDD:441904"
ORIGIN      
        1 msratdgaap gpaavgrsvr agpgprtgta parqdaradl rlvppalavw ataalaldap
       61 pawtaaiavv clgagavllg lgrartrpgt gpgtgtadat sagprawrra sggalllcva
      121 gaaasaglhg advrrgpvpg larayatvta eveltgdpwt arprvrgdha tpaavlvrge
      181 vrrleqgdgt vvttrspvlm avdtgvpapg gggrarwlgl lpstrlrvsg rlapataggd
      241 rvaallrvre rpapavvgep sgpqrlagrl raglreatdg lpedarallp glvvgdtsri
      301 tpeldeafea tdlahtlavs gsnltillal ligppglaqq terrglaprl glslratalf
      361 asaltlgfvv vcrpdpsvlr aaacgavall alatgrrrsl vpalatavll lvlydpwlar
      421 sygfllsvla tgsllllapg wsealrrrgv perlaeglaa aaaaqavcgp vvavlsarvs
      481 lvavpcnlla eiavapatvl gfgalaaapv ampaakvlaw cagwpagwia giartgaglp
      541 gagvdwpgsw agalllagvt vavvalgrrl lrhpwwcgvl gvllvllvvr paplarvvtg
      601 wpppgwrlam cdvgqgdatv laagagtgvv vdagpdpalv dhclrelgit riplvvlthf
      661 hadhvaglpg vlrgrevaqi ettgfeepad qvefvrrqaa ehrvpltrav agerrrtgpl
      721 dwrvlwpppd paplpdgpnd asvallvrsa glrmlllgdl eppaqqellr spaaaemghv
      781 dvlkvahhgs ayqdpqllrl vaprvalisc gadnpyghpa pgtvaglrav gamvlrtdrd
      841 galavtgggt ggeagelrva rd
//
LOCUS       WP_457674782             270 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces sp. 900105755].
ACCESSION   WP_457674782
VERSION     WP_457674782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            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 229399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..270
                     /product="HAD family hydrolase"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29373
     Region          4..>105
                     /region_name="HAD_like"
                     /note="Haloacid Dehalogenase-like Hydrolases; cl21460"
                     /db_xref="CDD:473868"
ORIGIN      
        1 mavlvasdld rtliysagal altmpdarap rllcvevhen rplsylteta aqlltelgda
       61 svfvptttrt rkqyerinlp gpapryaica ngghllvdgv sdadwhgrvl trladecapl
      121 devraylteh adpvwlrkqr vaedlfaylv verallpedw vkslavwaen rgwtvslqgr
      181 kiyavpkplt ksaavrevar rtgaeltlaa gdslldadll laadrgwrpg hgeladagwd
      241 gpaitalper gvlagerilr eflkaarkgs
//
LOCUS       WP_457674847             295 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Thiolapillus sp.].
ACCESSION   WP_457674847
VERSION     WP_457674847.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14206253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..295
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=32409
     Region          6..274
                     /region_name="prsA"
                     /note="peptidylprolyl isomerase; Provisional; PRK00059"
                     /db_xref="CDD:234605"
     Region          146..272
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mnhrfktlva avamtammpl ssqaedkpaa ekkplepqti vtingdaitd levlafnalq
       61 ggqnkldsqq aqvqllnqlv nttllaqaae kdgvdklpqv vaalkmariq vlaeakvndy
      121 farhpvtdee ikaaydkkft realqeykvs hilvkeekea rdiiaalekg edfdklareh
      181 sldsskdagg elgwvgrnqv vkpfgdamst lekgsfsktp vksqfgwhvi lvediraqqp
      241 ppldqvkeqf raqlqqqqla klvtemrnqa tvkvagaena pqtapvqdek papek
//
LOCUS       WP_457675139             315 aa            linear   BCT 27-JAN-2026
DEFINITION  DUF58 domain-containing protein [Thiolapillus sp.].
ACCESSION   WP_457675139
VERSION     WP_457675139.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1001782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..315
                     /product="DUF58 domain-containing protein"
                     /calculated_mol_wt=35022
     Region          144..>309
                     /region_name="YeaD2"
                     /note="Uncharacterized conserved protein, DUF58 family,
                     contains vWF domain [Function unknown]; COG1721"
                     /db_xref="CDD:441327"
ORIGIN      
        1 maqarlkqlv rivrpssqge avvdgrriyi lptrygmvfg vllvtllias inyannpafi
       61 ltflltgifv qaifhtwrnl lhlhlrplya drvfagettf fhfrlrgagd rahyslqfgf
      121 reqapvladc pasgeteiqv pfqtrhrgll hpgrlivetr fplgllrawc yvetdmeaii
      181 wprfldapae qgeaanagsa dgdrgrgtdd ftgyrgyhpg dslahvcwka lagekgllvk
      241 qfggdrvkqi wldfdaldet saeirlgrla gairalasqp vhyglrlger eippdkgedh
      301 yrkcldalal yggsp
//
LOCUS       WP_457675623             599 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Thiolapillus sp.].
ACCESSION   WP_457675623
VERSION     WP_457675623.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..599
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=64019
     Region          45..418
                     /region_name="Voltage_gated_ClC"
                     /note="CLC voltage-gated chloride channel. The ClC
                     chloride channels catalyse the selective flow of Cl- ions
                     across cell membranes, thereby regulating electrical
                     excitation in skeletal muscle and the flow of salt and
                     water across epithelial barriers. This...; cd00400"
                     /db_xref="CDD:238233"
     Site            order(106..110,141..145,341..345)
                     /site_type="active"
                     /note="Cl- selectivity filter [active]"
                     /db_xref="CDD:238233"
     Site            order(107,109,143..144,341..343)
                     /site_type="other"
                     /note="Cl- binding residues [ion binding]"
                     /db_xref="CDD:238233"
     Site            143
                     /site_type="active"
                     /note="pore gating glutamate residue [active]"
                     /db_xref="CDD:238233"
     Site            order(188,197,212,219,389,392,400,408,415..416)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238233"
ORIGIN      
        1 mnlyqktrdw lgaqledmrl hlarpdallq lallglltgl laggvivlfr vlvesiqnla
       61 lhgrgpdafe alslaerfay pllgaillal mfrwfargly vlgvarvler mayhqghltl
      121 rgfllqffgv aialvgghsv gregahiflg actgsllgqk lelpnnavrt lvgcgtaagi
      181 aasfntplag vifalevimm dyqlasfipv ilsavtatvv snaalgnaav fsvpvmelss
      241 lkeiplvill glfsgalaag firlvraias rgkswsiewq mlaaglstal lgmwipeimg
      301 igydtinltl vggygagill lmaaakliat sicsalnvpg gmigpsffig atlgggfghv
      361 lahwlpgldi qpgiyamlgm savmgaslqa plaaltalle ltdnpqiimp gmlvvviagl
      421 taselfgqes lfitmlkakg ldyrqhpvia alrrvgvasv mdkrfvrsqr lvspeeawkl
      481 lenkprwivi vedktprail sgialagyle aqydgvaadi gdteeerget gealidlmki
      541 pgkrlelapi qlhetlqeal ekldrgegea lyvrrmsapg iwriygiltr eqiessyrl
//
LOCUS       WP_457676048             331 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Thiolapillus sp.].
ACCESSION   WP_457676048
VERSION     WP_457676048.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..331
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35648
     Region          26..271
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          26..52
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(54,56,60..61,64..66,68..69,73,76,85,87,89,93..94,
                     100..102,104..105,109,112,121,123,125,146..147,176..178,
                     180..181,185,188,197)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          54..85
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          87..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          238..>306
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Region          268..303
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mknmmkgfvc lllmliwlpv sassvlpdag mfgkirvler aikngesled rdedgstaln
       61 navtfgqiet vrwllehgad vnardndgst plhnlvllks snalevgkll ldhgadlhar
      121 ntdgvtpldi aafmgrqslv klyiehatqq ggkqeaqrlv nvtdndgasv ldtavslgrl
      181 evvklllesg advnardneg svplsalvdi ptrndvelgr mllekgadlg lvdnegdtpl
      241 hnavlyerpd lvalflekga dvsarnadgm tpvfwiceae klsearkild lllknganin
      301 akdkegdgla vytkcaenqa lmdllrakgl h
//
LOCUS       WP_457676171             275 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Thiolapillus sp.].
ACCESSION   WP_457676171
VERSION     WP_457676171.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1008156
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..275
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31819
     Region          53..154
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mkrkakpsla eqadrhelye lsvqcseaev dfvsdtyqel rgkparllre dfcgtanvcc
       61 ewvrrdpanr avgvdldqdv ldwgrvnnls rltgeqqsri slinddvltv kteqpdilsa
      121 mnfsywlfkd rktlgqyfsr vhqalkddgi ffldiyggye sfreceeere ietpqgdvty
      181 vweqasfnpi nhdltchihf hfeddsrleq afsyhwrlwt lpeirelled agfrvtvywq
      241 gwdedgepdg eflpatdgda dagwiayiva ekmpg
//
LOCUS       WP_457676524             262 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Thiolapillus sp.].
ACCESSION   WP_457676524
VERSION     WP_457676524.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..262
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27866
     Region          4..262
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 msentdtfsv agrefssrll vgtgkyrdmd etraaieasg aeivtiavrr tnmgqnsdep
       61 nildvlppdr ytilpntagc ydqktavrtc klarelldgh nlvklevlgd ektlfpdvma
      121 tlkaaeelir dgfdvmvytn ddpiiarele dmgcaavmpl aapigsglgi rnplnirtiv
      181 enakvpilvd agvgtasdaa vamelgcdgv lmntaiaaaq kpvlmasamk kaiqagreay
      241 lagrmqakrf asassplegl ff
//
LOCUS       WP_457676610             192 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Thiolapillus
            sp.].
ACCESSION   WP_457676610
VERSION     WP_457676610.1
KEYWORDS    RefSeq.
SOURCE      Thiolapillus sp.
  ORGANISM  Thiolapillus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Thiolapillus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Thiolapillus sp."
                     /db_xref="taxon:2017437"
     Protein         1..192
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21156
     Region          <21..92
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
     Region          75..187
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mkstssfvqa lgkargygig efleiigels qestrkgklg rktkelvtfg ialhkqcerc
       61 icihaddakr vgaseaeleq vrrialfmrs tpgkdehlwk swkqswkqfv largaikhrh
      121 relvalgisi vmqhkkhirl hvrsalglgh epaaivevmp iallmdgapa lsqipslmka
      181 lekaekhgvg sd
//
LOCUS       WP_457677446             144 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457677446
VERSION     WP_457677446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..144
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15314
     Region          27..129
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 msesttreer farglevlgq idggagqrvl dtladispel shqvvawgfg eiysrpqlvp
       61 rdrqlvtlgm ltalggcepq levhinnaln vgltpeeive allhsagycg fpralnatlv
      121 akkvfaergl lpvgrqpapd assd
//
LOCUS       WP_457677738             186 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 900105755].
ACCESSION   WP_457677738
VERSION     WP_457677738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..186
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20601
     Region          8..185
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          96..167
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mspmtsgdyv irairpdewe avkrlrlval rdpvadiafl etyddalkrp dsfyreraas
       61 saqepsgarq fiaetadgew vgtvtvliee agstdwagfp verrqghvvg vfvrpehrgs
      121 gllkalfdag vawareqgaq rvrllvhedn prargayrka gfvpsgvsvq lethagkref
      181 elvlew
//
LOCUS       WP_457677821             422 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Thermovibrio sp.].
ACCESSION   WP_457677821
VERSION     WP_457677821.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     Protein         1..422
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45883
     Region          2..406
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 mkwkvklftl siltglftgi aivfyyllte gisyllylge pfrtipklpw wyvvfittss
       61 ilivnliilh ndaareygvr eiakaleenr ltftmkdlal kivasslsig sgfavgnegp
      121 saaigtmiay rlsrllslpk ellkvaigig assgiaavfv spitgilfav envayslikd
      181 figfmvlgsf saflislsyl epilfkyssg kaiqsdyils illfiplvai giyfyltlrd
      241 kvlfyltsmi skrlspfqrt llisaiggit vgtllkvspy agfsghsvvs alinsklhlp
      301 lsvifslivl riitnavsly snavgglfit lmsigsligy gfgealrsfn fsvepfyfaa
      361 igaavfvgvv mkipftavvl alemtydynv vvptglivsv vglmasiafe lrkgflrrrn
      421 fs
//
LOCUS       WP_457677836             868 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457677836
VERSION     WP_457677836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 868)
  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 868)
  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 868)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 868)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..868
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87800
     Region          126..215
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
     Region          <252..571
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          <698..>860
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
ORIGIN      
        1 mdpnthrgpe eygeqgspae ppapafggaq sgstglarvv rlvsgpylvt vnpvdgseie
       61 pcppgerpaa pgrldpeera aaaraaappl ppgpsgfagh etaleerted terlvrllsr
      121 grsvrvtgps gsgrtrllda vatacadlap dgvvrlsgyh htstdllyal faavyrapqh
      181 rperaemlrm vaeigaivvl ddlefggaal delldatpec afliaatpdv aapsagshle
      241 evflggigrg acgrllerav drpltddees waadlwfese glplrfvqaa allrqydrlr
      301 aapgalddgy glfpeagqat adpaaedaep aeqpevplps lgeaaapapl lasrlteaar
      361 etlrfavalg gelphqahlp altqdthada algellacgl itpagshyrl aatvqdqlta
      421 agyadgapar ahtvaqhyaw waghpsvtpe raaaesdval aamgvltgsr esghasaavl
      481 lartaapafa aalhwsawer slrhgqeaar lagevaeeay fhhelgvlal ctgsldrara
      541 eleasiglrg vlsdrngava grralalvtd rtradsaaaa ttalpqaaga asasrraapk
      601 epaanpfdaa sapklrksrt eqtaetliar gassttattg vpaatdsgag agkgvrrvfg
      661 garrnvvaag agallaavlg tvvtigatgg ddtpndkvnt eqttddsdgt dlpaeqpatd
      721 sslpptgpgt srpgtagqsd rpspspsgta psgspsapgt gsadptagpt epterptspt
      781 grptrpthpp tdeptgtpse eptepspsgt tptedptdkp stqspsqsas gpsagspsas
      841 gtsgttpsgg tpsdatatss gtesapvt
//
LOCUS       WP_457677844             374 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457677844
VERSION     WP_457677844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=39691
     Region          87..358
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 madssgtakt aesrargira tgrrrkgptr rrravtitlc tltsavllgg aglgyvyfkl
       61 ngnlkgvdin aalghdrpkn iddgsmnilv mgsdsragkn geygkdegga rsdtamivhv
      121 ykghkkasvv svprdtmikr pdctkdgkdv pgaqramfnt afevggpaca vktvesisdv
      181 rmdhfvevdf tgfkklidal ggvdittska idddhshlhl qpgkhtlnge qslglvrtrh
      241 gvpggdgsdl griqlqqafi kalmnqvknv gvltnptkly diadtatkai ttdtelnsvs
      301 eltglakglg nigsenidmv tlpvtydpan pdrvvpltkk sdqvwdalrv dkeipksaik
      361 gsagdqggtd kyvk
//
LOCUS       WP_457677859             368 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457677859
VERSION     WP_457677859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 368)
  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 368)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..368
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42260
     Region          100..230
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(109,139,142,189,219,222)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mstrdlyvqd pgdpvwkvpa sgaarfswdy ddgrerllal yqkgkdkqwd anlridwdle
       61 vdpqdplgtp desmslygtk ywdkmtekdr gelrqhytsw qfsqflhgeq gamvcaariv
      121 esvpdldakf ysatqtmdea rhaeiysrfl qekigmlypv ndnlqallsd tlkdsrwdmp
      181 ylgmqvlieg lalaafgmir dtttkplpkq ilayvmqdea rhvafgrmal rdyykqltda
      241 elrereefvi egcylmrdrl rglevlenfg ipheeaaeft erseflhlfr kllfsrivpc
      301 vkdiglwger lqrayvdmgv femgdsnldl lmaqdeelae kldaerfvae eeartaevaa
      361 aiaegaeg
//
LOCUS       WP_457677881             351 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457677881
VERSION     WP_457677881.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  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 351)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38388
     Region          67..>321
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msdwliyrga gaphdgiehl pppppwrdfd ggplvappaa ldpsserrlg vqhreashhr
       61 pgeterelvn aalylrrpll vtgapgsgks tlahsvayel glgrvlgwpv vsrstlrdgl
      121 ydydaigrlq dlqiaraapa aaesgaapgp dptdepgggi gryirlgplg tallpaarpr
      181 vllvdeldks didlpndlln vleegefrip elerlagsap evevlsddga rvtvrdgrvr
      241 crafpfivlt sngerdfpap llrrcihlhi pvpdkerlaa mvrahfgega aeryaavidr
      301 fldrepgdvr avdqlfnaih ltqragwtde deeetrrrlt aelmrpldrt r
//
LOCUS       WP_457677896             430 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Streptomyces nigrescens].
ACCESSION   WP_457677896
VERSION     WP_457677896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43610
     Region          59..>396
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdgtlslvll llflwclcsr rmerfeltap aafvllglll gegtgvldla lphetvktla
       61 eitlvwvlft daarlsfral rpelgiyvrl laiglplcvg lgallasall pgvsgwsaly
      121 vgaalaptda algatmmvnp vvpakirrvi nvesglndgi vtplvvlala gvsaaehtag
      181 pdatgqalvq laigtaygav iglaagwllr tslrngwaae dfagagvlal sllgytsala
      241 iggngfvaaf vaglafgtah gapprvllyv eqsgallsvl vwlvfgavll pevfahvtwq
      301 avvyavlslt virmvpvalc lagsgldart vgfigwfgpr glasiifgll aveeltpaga
      361 rpvlpaiact vllsvlahgl tsaplanryg raaaakgigp agpaaeelpv rgmaagglhh
      421 ghgrggpaps
//
LOCUS       WP_457677899             431 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457677899
VERSION     WP_457677899.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46620
     Region          10..424
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mpvtaedttd eahraieavf riesarliag ltrvvrdvgl aeelsqdalv aalerwpetg
       61 vpdnpgawlm atarnraidl lrrqerlark vetlgrdaer epgpseaafd rvldragied
      121 dllrlvflac hpvlstqarv altlrlvggl rtdeiarafl tseatvqqri vrakkrlaea
      181 gvpfevpara ewgerlssvl eviylvfneg yaatvgddwm rpalcedalr lgrmaagllp
      241 eepevhglva lmeiqasrsa artgpkgepv llleqnrsrw drllirrgla alaraeelgg
      301 tvgpyalqaa iaacharart aqetdwpria vlygalaqva pspvvelnra vavgmafgae
      361 qglavvdgla aepalagyhl lpsvrgdlla rlgraaeare eflraaaltr ntreqallee
      421 raaeqgedgr a
//
LOCUS       WP_457677902             288 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457677902
VERSION     WP_457677902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=31058
     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 mrygqalrde iaaegttpli gvhdmyaasv aaghyngffv sgfgfaasyy glpdigfiaw
       61 pdmaafverl rgafphhhll vdiddgyvdp evachvvrrl ertgasgvil edqkrprrcg
      121 hadgklvlpl eeylekldlv lasrtdllvv artdateede ilrraaalag teadvvlvdg
      181 vrsvdgirri revvgdkpll fnqiaggksp rlslteltal gvdvaiystp clfaahrame
      241 talaelkyad grlpatgeag geigvreate llarnlsrhh pgrravpv
//
LOCUS       WP_457677907             516 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457677907
VERSION     WP_457677907.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..516
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53281
     Region          30..485
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(37..38,41..42,45,77,127..128,130..132,135,155,
                     158..159,162,230,295..296,299..301,304,333,337,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtttvpaahe aavpapaaag rrrwialavl ltasfmdlvd ativniaips iqrdtgagfs
       61 avqwvtagya lafalglitg grlgdiygrk klfllgmggf tlasalcgva tdpgmlvgar
      121 vlqgamaalm vpqvlsiihv sfpanergkv fgmfgavigl gavcgpliga lltegnllgl
      181 ewrpiflinl pvgiigillg rrfltesrst qalrvdligt alatvgllml lypltqgres
      241 gwplwgfvsm aasplvlavf vryerirark dgsplvelsl fsvrtfaaga gvqltfgvvs
      301 glfflvwtlh mqlglgwgpl hagltglpfs lacstaagms vqklvprfgr avlqagalim
      361 lsgallylwe aghygtalqs wqmapamllm gagmglivap itdaaisevp aehsgsasgi
      421 fnttgqlgma lglglssvaf fgvvggtgep ggaaaaaglg pafvdattha lwwisgglvl
      481 ifgllflmpr rvsapeaper tdrdgaeaeq qpvlvs
//
LOCUS       WP_457677916             209 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457677916
VERSION     WP_457677916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22313
     Region          11..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matketkqrg rprsfdreta leqavrsfwe rgyeatsisd ltramgisap slyaafgdkr
       61 alfdevvvey grlyggflsr avaeeptarr gveralreaa aeytlpgrpr gclvisaaln
      121 ispasaevad slremrlanv raiaaairvd iasgelppdt dagalaaftg aviqgmsqqa
      181 rdgaertele aiaelalkaw prkasgasr
//
LOCUS       WP_457677918             520 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces nigrescens].
ACCESSION   WP_457677918
VERSION     WP_457677918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53191
     Region          55..491
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mtplvrsvrs adtltrdala vlqpgftgtt apdwllrrlg eglvsvglfg rnvadpaqla
       61 altgrlraer eelivaidee ggdvtrlevr ggssfpgnha lgavddtalt ravarelgrr
      121 ladcginlnw apsadvnsnp gnpvigvrsf gadpqlvarh taayveglqs agvaactkhf
      181 pghgdtavds hhdlpriaad lptlqerelv pfraavaagt ravmsahill paldgehpat
      241 lspaalhgll rapategglg fdglivtdgm emqaisatyg iergsvlala agadaicvgg
      301 gladedivlr lrdalvravr dgelpeqrla daaarvrala grtrsadvge geqegaapap
      361 gigltaarra lrltaagpya plaepayvaa ftplaniavg detpwgvaae larllpgtet
      421 atctaeaaaa agtaalvdgl ltaaagrrvv avvrdvhrhp wmaealstll aarpdtavve
      481 mgvpqappqg alhlathgaa rvcaqaaaea ltdqrlspde
//
LOCUS       WP_457677921             330 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457677921
VERSION     WP_457677921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36711
     Region          55..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavqldgvvd rtaprtgkgg apptrrgggs rraargapyl lllpallata vllgwpmvrn
       61 illsfqnlnm keliqhltdw rgfgnyqeil gseqfwrvtl rtlvftavnv vlimvlgvli
      121 glllarlgkk mrltlslalv ltwampviaa ttvfqwlfds rygvvnwlld rlgahsmahy
      181 dwvgsqlstf fvitvlivwq slpfvalnly aatttipnel yeaarmdgag twkvftsvtf
      241 pflrpfflat tfleiiwvfk afpqifaine ggpdrltetl piyaftegvg nlhfgmgaai
      301 slltivvllv mtayylrltv kqeqqeenel
//
LOCUS       WP_457677928             296 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457677928
VERSION     WP_457677928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31936
     Region          67..286
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mtsalprpgh eddrpaaadr llvrrpgpre lrpgrthrrr rtleislava vplllvllwq
       61 laadrawldd rvypapstil adgwdralag elwpdvwatl rrvlagyavg tvtgyllgll
      121 mgslslvraa leplldalyv vpklallpvf lnmfglgegp qvalvattvf ffvwistmaa
      181 vmaipsghrd agqvfgagpw qmfrhvllpa slpavlvgar iaagvavlvi vaseqiaatd
      241 glghlifdsr alfqndvmfv givcvavlgv lfselvrlag rfltpwaprd rgrprs
//
LOCUS       WP_457677931             376 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457677931
VERSION     WP_457677931.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..376
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39873
     Region          76..354
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mrirtttaal iaalalgagc aapetapsta rprtvkpvac cgtaswtdpa dlapdrapar
       61 cdkgtpaprr lterrtltva tgtlsaeyva plrlalarge fekegldvrl kvlptpealp
      121 llakgeldal waapeaavvn gvhggfdirw vagnfspdpr srsglwvrlk sgesaasvsl
      181 egaklgtmig kgsvimypma rtfaghgarl dsvafqqlgs sdvltaltgg gvdsawlldp
      241 vwrrvdgdsr yaflggqprg eplggalygp nllqqdpdag vaflraylrt vntyfagdyk
      301 adkafaaela klldvdgkil tsvpslrmdw evrkgttdrl qkayrdagvt kgaplpedrl
      361 vdrslyaeav ghrlrk
//
LOCUS       WP_457677934             176 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457677934
VERSION     WP_457677934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 176)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..176
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19211
     Region          47..171
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mslhedaarv lkewpapspe qeqlrltyld hlaahqdgmw kpckdghlta salvidpagg
       61 rvlltlhrkl emwlqmgghc epedaslada alreareesg iahgltllpg gpvrldrhht
      121 pcawhldvqy aalapagava eisdesldlr wfaydevpgv adasvlrlve rtrall
//
LOCUS       WP_457677941             208 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457677941
VERSION     WP_457677941.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 208)
  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 11574951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="M48 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23016
     Region          97..191
                     /region_name="M48_yhfN_like"
                     /note="Peptidase M48 YhfN-like, a novel minigluzincin;
                     cd07344"
                     /db_xref="CDD:320703"
     Site            order(159..160,163,169)
                     /site_type="active"
                     /db_xref="CDD:320703"
     Site            order(159,163,169)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320703"
ORIGIN      
        1 mpadpsahgp getplrraad tsrgaapspv aggpvtsave vrrssrrrrt vsayregdrt
       61 vvliparmse aeerrwvtvm ldklaaqesk rmlgdgelae rarrlsgqyl dgrarpasvr
      121 wvtnqntrwg sctpaegsir lshrlqgmpe yvidyvllhe lahllvpghg prfwrllesy
      181 prterargyl egvvaadrlp hlpvarse
//
LOCUS       WP_457677944             475 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC1 kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457677944
VERSION     WP_457677944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51370
     Region          1..458
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 msdlprkavt rtaklaalpl gfagratwgl gkriggrsae ivgrelrqrt aeqlfkvlge
       61 lkggamkfgq alsvfesalp eevagpyraa ltklqeaapp mptstvhavl aeqlgedwqe
      121 lfeefedkpa aaasigqvhr gvwhdgreva vkvqypgagq allsdlsqls rfarllgpli
      181 pgmdikplit elrdrvseel dysleaeaqr ahaeefaddp dvvvpavvhq cdqvlvtewm
      241 agvplsevia dgtdeqrdra gqllarflfs gpartgllha dphpgnfrll agdfpdgpve
      301 ewrlgvldfg tvdrlpeglp ptigaslrmt ldgeadavyq llceegfvke sieldpdavl
      361 eyllpiiepa qvdeftftrg wmrhqaarvg dprspahqlg kqlnlppayl lihrvtlsti
      421 gvlcqlgatv rlrdeleawm pgfvpeeepa gsdladfgtv vgadigeeav egsta
//
LOCUS       WP_457677957            1221 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Streptomyces nigrescens].
ACCESSION   WP_457677957
VERSION     WP_457677957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1221)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1221)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1221)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1221
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=129887
     Region          40..936
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          956..1216
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 msssfsaapp tqqphraarr aaagayrlvr tppgrvdppd ldaaqravvd hrhgpllvla
       61 gpgtgktttl vesvarrvra gddperilvl tfsrkaavel rdrlaarlaa legqpdgrpg
      121 tavggrragi pqattfhsfc yalvrahqda dlfadplrll sgpeqdlvvr ellegqaela
      181 gagralvswp delraclttr gfadevravl arsrelglgp ealgafarrt grpdwsaaaa
      241 flaeyldvld aqgvldyael vhravllaeh tdvaaqlars ydavyvdeyq dtdvaqvrll
      301 ralagnhgat gtpgspgrtl iafgdpdqsi yafrgading ildfpetfrr gdgtpapvav
      361 lgtsrrsgat llaatrlltr rmpltrlpaq kvrahrepap vrdggrvevy typtpgaeld
      421 niadilrrah ledgvpwrem avlvraggrs lpavrralts agvpldidgd dlplrhepav
      481 aplltalraa araalrqepg gaadgepada vdgeladaad ggagagsgea ggdeagggas
      541 vvdasrvgvp agdeagpggs dadeagpgdp dvnepvpdap gagastgvtp tpatprwlda
      601 etaldllasp lggmdsadlr rlgralreee raagqplprp sdeliarala epqrlvahdp
      661 ayargaqrlg lllrkarell agggtaeqal welwdgtpwp qrleraahrg gaagrnadrd
      721 ldavvalfet aaraeertgg rgalnfleel daqdiaadtl trravrpdav rlmtahrakg
      781 lewrlvvvag vqeglwpdlr rrgslleadr igrdglaepl tpgallaeer rlfyvattra
      841 rerlvvtavk aaaddgdqps rfltelgvtp qditgrprrp lsvaalvael rattvdpaat
      901 palreaaaqr laklaalhdd dhhplvpaah pdnwwglhep thssvplrdr drpvvlsgsa
      961 ldqlahtcsl qwflgrevka dtpataaqgf gnvvhvlade vasgrtpadl tvlmerldsv
     1021 wdalafdapw ksrqekdhar aalerflrwh vmeretrgrd tvatehgfdl tlragayevr
     1081 irgsmdhvsq dtqgrayvvd fktgkqkptg pevarhpqla vyqlavrega vddafdgrtp
     1141 epggaelvhl rlgapqkegg dalpavqaqq pldgewvgel lataagrvle erftpttgsh
     1201 cthcsfrasc saqpegrhiv e
//
LOCUS       WP_457677973             803 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457677973
VERSION     WP_457677973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..803
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84760
     Region          45..423
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mperwqwsrp tgrlrpartn pyegavrpps pphaashrrg kilstfrdlg ifpetaeale
       61 avgiispfpi qeltlpvals gndvigqakt gtgktlgfgl pllervrvpa dveagrarpe
      121 elteapqalv vvptrelcqq vtndlltagk vrnvrvlaiy ggrayepqve alkkgvdvvv
      181 gtpgrlldla gqkklnlsqv kslvldeade mldlgflpdv ekiiqllpak rqtmlfsatm
      241 pgqvislarr ymsqpthira tapddegqtv rnttqhvfra hsmdkpemva rilqaegrgl
      301 amvfcrtkrt aadiadqlar rgfasgavhg dlgqgareqa lrafrngkvd vlvctdvaar
      361 gidvegvthv inyqspedek tylhrigrtg ragakgtavt lvdwddiprw klinkaldla
      421 fdepeetyst sahlyaqlni pegtkgvlpr aertraglaa eevedlgetg grgrgprkga
      481 vveeerpart rtprqrrrtr ggtaldgpag seaqttgspa aaessegtea agprqprrrr
      541 rtrsgqsgaa apapvaeaap taavvteaat vvtesaavva eapaepakpr rrrarvarpv
      601 dtesfqtvev aaralaaega aiaaesvavp epaeapakpr rrsrsaakaa vetapavvte
      661 svaeaadtvv eapakpkrtr ktaaakaaea aadtaegave apakpkrtrk taaakaaeaa
      721 adtaegavea pakpkrtrkt aaakaaeatv dapaaedapa kpkrtrksav akpaadapea
      781 aeakpvrrrt rataavaeaa pes
//
LOCUS       WP_457677992             539 aa            linear   BCT 27-JAN-2026
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457677992
VERSION     WP_457677992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 539)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 539)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 539)
  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..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /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=58750
     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 mrratcaqwg acavavalva tgcgggsgas rsgvvsaswg dpqnplepan tnevqggkvl
       61 emlfrglkry npktgaaenv iadrietkds qnftvtlkgg wtfsngekvt aksfvdawny
      121 gallsnkqkn apffqyidgf aqvhpdggsp qaktlsglvv kddrtftvkl nqkfsswpdt
      181 lgysafmplp qvffrdhdaw irkpvgngpy tvdsyekgsv lrmrkwgayp gndparnggi
      241 dlrvytdnnt aytdlqagnl dlvddvpaaq lknvqadlgg ryinqpagii qtltfpmydk
      301 rwsrpgtdkv rrglsmaidr dqitreifrk trtpatdwts pvlgkeggyk aglcgeacef
      361 npakakqlik eggglpggri altynadtgs hkdwidalcn sinkslgddq acvgdpvgtf
      421 adfrnkitak rmsgpfragw qmdypliqnf lqplyytnas sndgkfsnas fdklvneana
      481 dtdpqkavrt fqdaekilas qmpaiplwyq ngsggysdri snvslnpfsv pvyneikvn
//
LOCUS       WP_457677995             799 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter family substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457677995
VERSION     WP_457677995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Lewis,K.M., Greene,C.L., Sattler,S.A., Youn,B., Xun,L. and Kang,C.
  TITLE     The Structural Basis of the Binding of Various
            Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA
            from Chelativorans sp. BNC1
  JOURNAL   Int J Mol Sci 21 (11) (2020)
   PUBMED   32486296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Marland,Z., Beddoe,T., Zaker-Tabrizi,L., Lucet,I.S.,
            Brammananth,R., Whisstock,J.C., Wilce,M.C., Coppel,R.L.,
            Crellin,P.K. and Rossjohn,J.
  TITLE     Hijacking of a substrate-binding protein scaffold for use in
            mycobacterial cell wall biosynthesis
  JOURNAL   J Mol Biol 359 (4), 983-997 (2006)
   PUBMED   16698034
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..799
                     /product="ABC transporter family substrate-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84094
     Region          65..782
                     /region_name="PBP2_Lpqw"
                     /note="The substrate-binding domain of mycobacterial
                     lipoprotein Lpqw contains type 2 periplasmic binding fold;
                     cd08501"
                     /db_xref="CDD:173866"
ORIGIN      
        1 mtdhdhpagr ravchrrrca aliaagvllp lpalagcsed areasvaasq diapaprsal
       61 knggtlrwav dampgtlnaf qsdadattar iagavlpsmf tidasgrpqr nadyldaadi
      121 strdpkqvvt ykinpkarws ngtavtaadf iaqwtalrgk dnaywtarna gydrigkveq
      181 ganahevkvt farpyadwrs lftplysksv mgspnafneg areqlkvgag pflvqkrdte
      241 egrvilvrna rwwgepaklk rivlqslpgd kraaalaegs vdvaavdqia akrvasarrp
      301 assgsprtpa egnagpqsng nragakaaaa ensvlrgyti rkalepaytq lalngssgpl
      361 addrvrrava raldrqalad tvlkpldlps kplgshllma gqygyadhsd algeqdagaa
      421 kalladagwk sdgadhqqag ekagapapdg ypdedgdeps deryagdryd esdesdesde
      481 drpdgdsddr nparagrgha gapgrgdrpa aaeaplsftg avgsevqqsa llrqsasfyk
      541 qaaasekada dgdtgsaaya kykrykmraa ealgaaelie tgqgpqlpgs gghpgarhaa
      601 veraadaaaa prpadgktsr iaavkkngkp ltlrfvlpdg agseqlrtvg rriasmlgki
      661 gvqtslqrvs dasyfqdhia ggdydlalys wpgtaypatd arpiyakpqp apdgsltveq
      721 nytrvgtdhi dqlfdqaase ldegaahtlv aqadariwaa agsiplyqrp elvatkksla
      781 nvgafgfatp rfqdigyqk
//
LOCUS       WP_457677998             567 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457677998
VERSION     WP_457677998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60067
     Region          10..461
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msttktpsae qgshsnyrrs lgtialtatg lgsiigsgwl fgaeraaaia gpaailawvi
       61 gavvaltial tytelgsmfp kaggmvrygq yshgslagyl aawanwiaiv svipgeatas
      121 vqymsswdfg waqalydgke ltgtgvglas vllifyffln wfaislfakt ntaitvfkvv
      181 vpamtagalm mahfdtdniv hhggftpngw ssvftavavs givwayngfq splnlaaear
      241 npgkslpkav vwsivialvi yvalqvaflm avpgdklaag ggwaglgfns pladlaiawg
      301 lnwlalllya dafvspsgtg miyaattsrm ihgvqenghl pgifgkvdkk tgvprpalll
      361 nlviaflfla vfrgwgslae ivsvatvisy itgpvavmsl rrvspdlkrp vklkampvia
      421 piamifgslv lywgrwpltg kvilimavgl pvwawyeigk pltqgrkpwa alrphlkaga
      481 wmvayllvma svsymggkef ggkgylpegw dialvaaigl afyywgvrss wrnpslvqae
      541 aemraedear eadeageaeg vkapvga
//
LOCUS       WP_457678007             513 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457678007
VERSION     WP_457678007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..513
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51165
     Region          29..422
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpvtggsgee gaadgaaggg ggsaatgalr rtltfrdllv ygllfiapma pvgifgalqa
       61 tshgavtlvy lvatvamaft afsyaqmvrv apragsvyty arvglgegag fvagwmamld
      121 yllipavayl fsgialhalv psvhpwvwta lavavttlln lsgvrtaara gfavlameiv
      181 vlavfvvsav veliahgapr gwaepltgeg gfsagavlaa vsvavlsylg fdaiasfaee
      241 agggedgrgp ggpdrvarav lsclvvagvl favqtylaal lmpvsaaela arpaeqgaaf
      301 yatadsavgr wlqdlvavsk avgaafaala gqaaagrllf amardrrlpg amskvdagsg
      361 vprrallgaa lvtlvaavga arrddglaql ssivnvgalt afgllhasvi gwfwvrgrrg
      421 rpplgrsggl vgrtgelggr sgelvgrtge lgggppsvlr havvpllgla vvvavvveas
      481 ataqlvggvw lvaglvvlav qhggraragg mrg
//
LOCUS       WP_457678019             443 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 27 protein [Streptomyces nigrescens].
ACCESSION   WP_457678019
VERSION     WP_457678019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Naumov,D.G.
  TITLE     [Phylogenetic analysis of alpha-galactosidases of the GH27 family]
  JOURNAL   Mol Biol (Mosk) 38 (3), 463-476 (2004)
   PUBMED   15285616
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14423446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47492
     Region          39..334
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(46,81..82,123,157,159,200,222,226)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          346..423
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
ORIGIN      
        1 mrvlscllft lsllppllgv plltagpaqa ldndlartpp mgwnswntfg cnateqivkd
       61 tadfmvssgm rdagyqylti ddcwmersrd segrlvpdaa kyphglaela ayvhgkglkf
      121 gvyesptyht cqgfpgslgh eqkdadtfas wgvdflkydn ctasdpdqrp gdeklpletr
      181 dgtmrdaler tgrpivfsls lqpaaqgesp wewgksvanm wridgdrdas fdglrrliht
      241 dldkakwagp ggwndidmlg tgnyafasgs ndpnkrltyd qekselsvaa vlaaplisga
      301 dlrtpaaagg sgfpisdqdr svylnkdvia vnqdsrgeqg tavttengln vlrrplangd
      361 vavalfness sqavisttaa avglpanstg yhlndlwahs shvstdgtis atvpaggtvl
      421 yrvsprppar svwwpvtgsi rtg
//
LOCUS       WP_457678040             283 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678040
VERSION     WP_457678040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31411
     Region          15..62
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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 mptrttptvr qqrlgaelrk mrlaagatte yaagllgidr trisnmeggi rpvsldrvrt
       61 lacnyacpde syvdalvdma anrergwwer yrgtlaagll diaelewhaa risttqtvhv
      121 pgllqtedya ravftavlpp ptrleielrv ahrmerqqvf erpepptyva yvheaalcmr
      181 fggadvmrhq lkhlchvser egvdvrvlpv evgafpgagh allyaggvvp qldtvqldsa
      241 hgpefthaea qlakyrahld wmdnaslsvp asrdfirnve rsl
//
LOCUS       WP_457678052             371 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces nigrescens].
ACCESSION   WP_457678052
VERSION     WP_457678052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39697
     Region          1..325
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(24..25,28,80,96,98,127,159,285,288,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(214,219,276,285..287,290,312,316)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mvtflprlpg rladvpsfdr aiggaesnva ctlartghtt rwisrvgtdg fgdhlltaia
       61 dcgvdvahvr rdplrptgvy frtagdratd thevayyrag saasamtadg ldaaalragr
      121 ilhlsgitaa lsadclgllr eltarrpgrp llsfdvnyrp glwrdtarar vlldlargad
      181 lvfvgddear dawglhgpra isralpepql lvvkqgraga tvfrrtggpd frrtgetdfr
      241 rtgepdlrrt getdlrrtge ldgrrddata tfvpalnvdl vaatgagdaf aagflsatlr
      301 glpdrdrlrh ghlwaaaalt vpgdlatpps rpqadrlaal ddtawerlhl gpgwtdadvs
      361 grradeevpt q
//
LOCUS       WP_457678065             382 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678065
VERSION     WP_457678065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39736
     Region          53..270
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttddeggrg rltgpagpde ephtpaapap dapgpnaplp dapgpnapvp davtcralry
       61 afgetkavdg vdlsvrtgev fgllgpngag kttaircitt llpvpagmvr vfghdaaker
      121 mavrrllgyv pqqlsadagl tgrenvalfa rvfdvsrrer aarvtqalaa vgltdaagrl
      181 aktysggmir rlelaqalvs aprllmldep tigldpiart svwehinavr aatgmtvlvt
      241 thymdeadqh cdrlalmhqg riralgtpde lrsalrarrr atrtpaaahp apltpgtptp
      301 aaapdtsatt apvsapdtpa ttapasappt tpssppsaps rpsdteptle dvfrdvagsg
      361 ldeqsgdfrd vrstrrtanr vg
//
LOCUS       WP_457678123             100 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678123
VERSION     WP_457678123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..100
                     /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=11033
     Region          21..75
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mparplrapt aspgalhtas ltvkdaaeyl glsphtlyvw rhrrqgppsf rmgprgrvmy
       61 rlevldawvr eqeqadsrsn aalnplnapc qerstrltsa
//
LOCUS       WP_457678121             183 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678121
VERSION     WP_457678121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20462
     Region          <45..170
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mdrhrhlrtr plprrsgrdv lalgtrphpp rrlrpsgtrv prsthrrhdp ptprrdirft
       61 iyrlesgepv pagvatllpd havrtaeyii mlapeargrg lgtqatrltl dyafhianlr
      121 mvwlkvlapn qagirayeka gfrtvgslre agywlgqtcd evimdavage fegpsivkpl
      181 ltn
//
LOCUS       WP_457678133             439 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678133
VERSION     WP_457678133.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44612
     Region          33..412
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(43..44,47..48,51,84,139..140,142..144,147,167,
                     170..171,174,247,250..251,254..256,259,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtatpepapa cpsppaatap psadpplwrd rrfvllaaar iisvlgngfa rvalsfavla
       61 lpgagpgqls lvlacqavpq lvfilaggvm adrmsrsrlm ivtdlvgaaa yaglaamvlt
      121 ghaplmalca laalagtata lfspamdgvi pllvpagrlq rangllrvgm nssmllglal
      181 sgvavavvga gwalalnaas fvvsallvrg lrlparartg ssgwadlrdg wrefagrqwl
      241 wvvvaqysvv vaalnanagv lgplvaenel ggarswsliv aaqalgtitg aglaarirvr
      301 rpvliavlat fplalpiall avrapvpwia lamfgsgiaa difgvlwatt iqrevpeaal
      361 srvssydwfg slafaplgll iagpvaartg vgpalagcaa livlasaaal lspqvrgvra
      421 prpaptgeer deceaerpr
//
LOCUS       WP_457678126             390 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457678126
VERSION     WP_457678126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43331
     Region          69..376
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mygkctryrv kgipgvkdrs fdalqdaktw laqaqtdarr gefvdprdga islkdyiath
       61 wwptqsgdps tlerieqrvr rhivphlgal plngvgtevl rswkkrlekd lgptsirlvw
      121 atlsgvlqaa vedlrlarnp crastvrppa aapgrveawl pervlavraa ipdryrvlve
      181 igaglglrqg eafglsmedi dfdseivhvr rqvkmvrtkl cfalpkgrkv rdvplpssva
      241 kalrqhvefl apvpvtmpwd dprppqtpve aklrrprtyk llvtgrehka inrnylnsyv
      301 wkpalaevgv iaaleesapd gsrawepsre hgyhalrhfh aseqlkages vvslaswlgh
      361 sdpgftlrky ahflpragar ggaaidavfa
//
LOCUS       WP_457678136             312 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678136
VERSION     WP_457678136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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
REFERENCE   2  (residues 1 to 312)
  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 10144160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33801
     Region          56..>116
                     /region_name="NT_KNTase_like"
                     /note="Nucleotidyltransferase (NT) domain of
                     Staphylococcus aureus kanamycin nucleotidyltransferase,
                     and similar proteins; cd05403"
                     /db_xref="CDD:143393"
     Site            order(76..78,81,89..90,92)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143393"
ORIGIN      
        1 mtstpgpapl pepappgaaa eatgernpad ratpdgvppd rvtpvrpatd ratahlldrf
       61 laalrprlpl ralwahgsla ggdyqqgrsd ldliaivdrp ctpeeerqlg elhatldrtd
      121 plaaklhcsy laadetadpa hihltwahre lkrrtvtpvt rrelhtfgrv lygdaptall
      181 ppvtdaelat firtdlwefw rpaldepeew lqdiwvdlgm ltlaratvtl rdgtliskge
      241 alavlgelga pdeviadirh rrygpaappp ppgparpsdr varradltra flgpaidrtl
      301 atyghtfpap pg
//
LOCUS       WP_457678145             117 aa            linear   BCT 27-JAN-2026
DEFINITION  RidA family protein [Streptomyces nigrescens].
ACCESSION   WP_457678145
VERSION     WP_457678145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..117
                     /product="RidA family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12245
     Region          4..106
                     /region_name="YjgF_YER057c_UK114_family"
                     /note="YjgF, YER057c, and UK114 belong to a large family
                     of proteins present in bacteria, archaea, and eukaryotes
                     with no definitive function. The conserved domain is
                     similar in structure to chorismate mutase but there is no
                     sequence similarity and no...; cd00448"
                     /db_xref="CDD:100004"
     Site            order(4,7,9,11..12,52,54..55,57,59,70,73,83..90,101,103,
                     105)
                     /site_type="other"
                     /note="homotrimer interaction site [polypeptide binding]"
                     /db_xref="CDD:100004"
     Site            order(66,70,85,101)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100004"
ORIGIN      
        1 maftgttaav sgqvpvdgeg rlvgegdaea qvrqvyanla taleaasctl ddvvkltvyl
       61 tdladlpafr rvrdehqdar rppacslvqv aglvqpgfrv eiealavrpa paesndq
//
LOCUS       WP_457678151            1135 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457678151
VERSION     WP_457678151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1135
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=122292
     Region          244..1015
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mrlrhrhspl rgiarpaala aaallvitvp gpaqaappqp pqgatefrss fesgepqpdw
       61 tdtvdtgadg kprtsgvtpe tapaapgmnt gtdtgprdsp takahagftg ghalryagth
      121 tapgrgysyn kifdvnvpvt aatslsykif pemaksdpay pathaavdla ftdgtylsel
      181 savdqhgapl tprgqaaskt lyvnqwnnre arigavaagk tvdrilvgyd apeaprtaaa
      241 frgwvddltl apkapdkpld rlsdyavttr gtlssgsfsr gntfpatavp ngfnfwtpvt
      301 nagsadwlye yarknnadnl ptlqafsash epspwmgdrq tfqvmpsvaa gtpdasrtgr
      361 alpfhhanet akphyygvtf dnglkteitp tdhaalmrft fpgdraslif dnvnnkggls
      421 ldtgrgvvtg fsdvksglsv gatrlfvygv fdapvtgggr ldggggkdvt gylrfrpgad
      481 rtvtmriats lvsvdqakan ldreipdgat fagvkeraqs qwddllgrie vegasrdqlt
      541 tlysnlyrly lypnsgfeqv gsrsryaspf spqvgqdtpt htgskivdge vyvnngfwdt
      601 yrttwpaysl ltpkragkmv dgfvqqykdg gwisrwsspg yadlmtgtss dvafadayak
      661 gvefdaeaay aaavknatva ppqpgvgrkg matapflgyt stdtregmsw alegylndfg
      721 iarmgkalye ktkkprykee sayflsraqn yvklfdrkvg ffqgkdsqgn wrlppgafdp
      781 rvwghdytet nawtfaftap qdtrglanly ggraalakkl dayfstpeta skefagsyge
      841 vihemteard trmgmyghsn qpshhiayvy daagrpwkaq ekvreamsrl ylgseigqgy
      901 pgdedngems awyvfsslgf yplvmgqgey avgsplftka tvhlengrdl tvnaprnnar
      961 nvyvqglrvn gkpwnstalp hrllarggtl dftmgdrpsa wgtgehaapt sltkddkvpt
     1021 ppadvtdpat gplfdntsgs saaltgapvd larparvtsy tltsadrata pagwtlegsp
     1081 dgqrwtrldh rdgesftwdh qtrvfgisdp gsyrhyrlvp dgpgtlaeie llgap
//
LOCUS       WP_457678157             406 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678157
VERSION     WP_457678157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 406)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43098
     Region          6..399
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mprtardvvf vdgvrtpfgk agpkgiyhet raddlvvkai rellrrnpal dpakidevai
       61 aattqigdqg ltigrtagil aglpqsvpgy sidrmcagal tavtatagsi afgaydavia
      121 ggvehmgrhp mgegvdpnpr fvseklvdqs alfmgmtaen lhdrypqitk qradeyavrs
      181 qekaakayan gkiqqdlvpi svrntnaeig etgwglvtad epmrpgttle nlaglktpfr
      241 thgrvtagna aglndgatas iiasedfare hdlpvkmrlv syafagvepe vmgygpipat
      301 ekalakaglg iedidlfevn eafavqvlaf ldhygiaddd arvnqyggai afghplassg
      361 vrlmtqlarq feeqpqvryg lttmcvgfgm gatviwenpn fdggsk
//
LOCUS       WP_457678171             646 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Thermovibrio sp.].
ACCESSION   WP_457678171
VERSION     WP_457678171.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 18640031
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     Protein         1..646
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=76237
     Site            order(25,28..29,32..33,35,59,63..64,67..68,70..71,104,
                     107..108,111..112,115)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          25..52
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          28..>289
                     /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          57..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          103..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(179,182..183,186..187,189,217,220..221,224..225,
                     227..228,254,257..258,261..262,265)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          179..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          188..293
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
     Region          215..245
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          250..281
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mralltilll lfltlpsfge vngdevlykr glyqykvgsy staldyflrl lkpnskyydk
       61 allmlsktyy aigkktglkr ylwqalnylq lyfievssre lpweyyytka qiyeslsfye
      121 qafalyrvaf lkaktqrqkv dttigiirta vwirrpevve eyfilvstqk nlteyekrel
      181 afvrglylft kgkykealpy fyklykeyeg ylidnptyyy liaediyrlg klnlaehlfr
      241 riasltgdre vvrratlrlg dielrrknyk lafvyyysvi rdypdsleak varlkvipmm
      301 dnpevryral ltkdgafrep iryisrllvn yrttyvgiya ladlgylvfk lgspekvfkr
      361 ltwevslvfp eeikyeqref irylwkpylf klppkkacfl yrsnprffee lfgrglllkf
      421 akdlklcnmr ilryrllsfm lkrwrddetk llmaqalfes rdfkeafkvl skvknkncry
      481 wvvlgklslf lpevnftlsd lnssckkpsv dtvslsiyyl aksgmiesaf nlflkfeedl
      541 tkdyrkelvv kaalnqller atlegnyqis ygvskalfng wsrdclvgsy llisssrlkr
      601 lkeakeayea vrgcidsfsf iaktvyeglr leeevdsgsl stvdsh
//
LOCUS       WP_457678176             228 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678176
VERSION     WP_457678176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24048
     Region          3..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msleltdvtl typdgdarlt aldrvsltvp agcltavigp sgsgksslla vaatligpdr
       61 grvvidgtdt aglgrseltt lrrttigtvf qqpnllpslt aaeqlevmar ldgrpsstar
      121 vrarellaav glaelagrrp hqlsggqrqr iniaralmne pavllvdept saldhergaa
      181 vltllrtltq eratatvlvt hdrahldaad evaevldgrl rphrgarr
//
LOCUS       WP_457678179             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457678179
VERSION     WP_457678179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36975
     Region          18..180
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          125..370
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvawrdlrf akgrfalmgt vivlitalvg llsgltaglg rentsaitgl padhlvfaap
       61 idgskltftd srlpertvra wsrvpgvrha eplgiatara eaggrtaavs afgvrpgsrp
      121 apgrvgdgav vlsekaaasl gvraggrltl ggrsfevaav sgaamyshtp vvwtslddwq
      181 glaggsgpag agpgsgrsgp drgsvgatvl alsttgtsgl paadkelgtk tvttddavra
      241 igsftaengs lqlmrgflfv isalvigaff tvwtvqrsgd vavlkalgas tgsllrdalg
      301 qavvllvagt algtavvaav gaaiggtvpf vldpptvlvp alimialgaa gaalairrit
      361 svdpltalgs ar
//
LOCUS       WP_457678183             378 aa            linear   BCT 27-JAN-2026
DEFINITION  flagellar biosynthesis protein FlhF [Thermovibrio sp.].
ACCESSION   WP_457678183
VERSION     WP_457678183.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     Protein         1..378
                     /product="flagellar biosynthesis protein FlhF"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005047 - signal recognition particle
                     binding [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0044781 - bacterial-type flagellum
                     organization [Evidence IEA]"
                     /calculated_mol_wt=42789
     Region          1..377
                     /region_name="FlhF"
                     /note="Flagellar biosynthesis GTPase FlhF [Cell motility];
                     COG1419"
                     /db_xref="CDD:441029"
ORIGIN      
        1 msvkvfeged ltsliekakk elgeveilyy evekkglfpf lkkkwyrlfv mekeeerere
       61 evrellklek eveelkellk evksvatspp sppvppyvee rlpcgeveef keftgdalel
      121 idllvkkgve kevaravvke acgldiesek ldlntatfre allkgisstv sftgefkver
      181 gqkkafvflg ptgvgkttnl fkiaskfvie relkvgvitt dtfkvggtaq artyasilnv
      241 pffvatdhkk lkeivnglke ldvilvdtvg rshydywrlg evkavlqgle vptemlllls
      301 cnysfkeale vvnryrsffp itslfftkid etsrpgllls vpyyagfpvs yistgqrvpe
      361 dirlltpevi tnyllger
//
LOCUS       WP_457678182             413 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457678182
VERSION     WP_457678182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 413)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /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=42273
     Region          162..403
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mteeavtsps ltpvqralrs clhlmvatll alaavravad rtpdapavla aavalcalyv
       61 tghrlprlrt stgaaalwla alalvwlvll altpdgvwva fplffvqlhl lplrgalpav
      121 aattlaavag fgrhthtlsv gtvlgpvlga avavavvlgy ealyreseqr rrlieeltat
      181 rgeladaeha agvlaererl areihdtlaq glssiqlllr aaeralperp gtalghvrqa
      241 rtaavdnlae arrfvralsp pdlaagslpa alerlcatta aasglavhcq vsgaptalpt
      301 phevallria qsalantvrh aaadrveltl symdtevald ivddgtgfvp aevpapgsaa
      361 vpgtgfglaa mrararalqg tlavesapge gtavaatlpc patapvaape aas
//
LOCUS       WP_457678193             314 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457678193
VERSION     WP_457678193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33899
     Region          1..>181
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          92..300
                     /region_name="PBP2_LTTR_substrate"
                     /note="The substrate binding domain of LysR-type
                     transcriptional regulators (LTTRs), a member of the type 2
                     periplasmic binding fold protein superfamily; cd05466"
                     /db_xref="CDD:176102"
     Site            order(107..108,110..111,114,118,120..126,236..241,
                     247..248,250..251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mslrqmeylv evveqesftr aaealhvtqs alshqikale rtvggpller mtrgvrltvm
       61 grayfphaql avrsarqarr aalaaggaes gelhiatvhs qavgvlpevc arwatarpgv
      121 rlvlheyatt eeldeqmarg vadlalgprp kdwpgpvtvv gqermvlvvp hgdplaares
      181 vrlaeladrp wvrcslepvv dsasdgqeqg rggaqrsgrr wldrecervg ftprtavrtq
      241 hsstavrmaa agvgvlltaa helrgldcaa vptdppwhre itvfsrvept gaaaeftell
      301 rtvgsaelsq dapm
//
LOCUS       WP_457678199            1157 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678199
VERSION     WP_457678199.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1157)
  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 1157)
  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   3  (residues 1 to 1157)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1157)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1157
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=122700
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          183..1135
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhfrvlapld vrsadgrpap vpetkvrall aallahhgrp vstarlvahl wgprsparpt
       61 aslqskvsql rraldtaepg arklvtatpp gyrldiaada ldagrftalt araraaatpr
      121 qragllgeal elwhgpafag fadsdlvrpv aesleeqrlt aleeraaarl elgehaplta
      181 elaglaarhp lrerlralql talyragrqs dalaaydeir arladelgvd pgpeltavhr
      241 ailrqepwrp hdggawqdgg awhdggawqg qgaqrddgtr hdhgarhdgg srhdggtrhd
      301 ggtrhdggat rpadrpepdl atappagprp rtnlptplta llgrrdavrr ieallaanrl
      361 vtltgpggvg ktrlaletag rlagsfpdgv wlvelaalsr pdaperagsk ctaaqvaeav
      421 lavlgirega sagpvaerli gavrgkrlll vldncehlve aaaevtaell gaapdlrvlv
      481 tgqeslgltg etlwpvpple pagavelfta rasaadpdfv ldadataava eicrrldgip
      541 lalelaatrv ralgvrelsa rlddrfrlla sgrrgvpprq qtlramidws wellpaaert
      601 vlrrlavhad gctleaaetv cagdgvrrde vldllarlvd rslvtvartp ygpryrllet
      661 vaayclerlr eageltavrr rhhrhytela eraapllygp dqrkwlerld qetanlrdal
      721 daavregaad halrlvdala wywflrgrla eagrsltaal aayeaarata adagdpaaeg
      781 rrlraatwqv gmaslagddt dpveratavl rqygthddpg arawaqwflg faqvglgepa
      841 varervadsl aafralgdrw giaaalssra qgsvggdlra rlrdaeesaa lfrelgdrwg
      901 qlqaadalga laeitgdygs aarlhrdglr iaeelglwiq asyklsglgr ialltgdlaa
      961 ardfhergmr laaeqshlrg emfaecglal garregrldd aeahllpwle wclgrdgdpg
     1021 tafvlselgf laelrgdaet arrrhldgfv aaratadpra valaleglag avaltgrcav
     1081 aarllgcaaa aratagapqp aaergdvars tatarrglgd aayeaayasg agvapevlvk
     1141 eatgsagarg arttasp
//
LOCUS       WP_457678202             296 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678202
VERSION     WP_457678202.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /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=31727
     Region          37..245
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtepspaaft earardvlaa aghpeaaada sllslgenav falgdngpvv rvgrsaelle
       61 raerelgvaq wlaaegvpav raaepvatla dghpvtywqr lpeavrpagp ddlaallklv
      121 halpeppfal prrellggve rwlrlagdav sapdaeylrg rrdafaaaat alephlprgp
      181 ihgdalarnv hvgpdgpvlv dletcssdlr ehdlvvmals rdryglapda ydtfvsvygw
      241 dvrdwegcav lrgsretasc awvsqhapgn paalrefqrr iaslrdkdat vrwypf
//
LOCUS       WP_457678205             328 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457678205
VERSION     WP_457678205.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 328)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35007
     Region          63..327
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtatestggs erssaprgag sapvprgtpr rtstarrtst srrtstsrrr atprrtatra
       61 gqyaallgyl aflafpflwl lstafkppre lssmhptwip eaptlenfrq afaqqpllaa
      121 agnsllaaav sallaillat pmayvlarfr nrlsraatgw vvisqafplv lviiplflil
      181 kglhlvdsri glimvyvvws lpfalwmltg yvraiprele eaaavdgagr lrtlvsvtap
      241 llapglvata lfafitawne fffalvllks pekqtlpvvl thflgaegva dlgplaaaal
      301 latlpslllf aaiqrritgg mlagavkn
//
LOCUS       WP_457678208             441 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678208
VERSION     WP_457678208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..441
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48628
     Region          33..379
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrhdrapgrp prftrrgllt taaalpaaal lpgcsdgrrr taggritlrf qslawqqdsl
       61 kankqlvaew nrqhpdvrvq yvqgswttvh dqlltsfegg eapdiihdas ddladfaygg
      121 dladltallp prlkrdipqr swetgtfagr ihgvpflqep rvlianrakl drsgvrvptp
      181 ehpwtwpefe eaaqrltrgt tygvawplke pvsatlnlal stggrifhrr rdgkvevrfd
      241 avdqqvprti hdqvnvdrsa srttlgmggs dtlpgffagr yamvplgfsy rqqiaqqapk
      301 gfdwtvlpap kgtaldqgvs pqtlsiaedc phkeeamafi dfllsppnmv rlalgdwllp
      361 tgqealkdpa lraaeydwat gtalapslhs apaqsvrgyp ewkdkiatpg lqeyysgaig
      421 ldtlrkrlve dgnlvlaryq r
//
LOCUS       WP_457678210             508 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678210
VERSION     WP_457678210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51113
     Region          17..459
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtarrrqrlv ltgsitgavi valdgtvltv aqpalqrdlh asfgqvqwts tgyliavasl
       61 lvfagrlgdr yghqqifalg ilgfgaasag iglapgvgwv iglrvaqgvf gallqpatlg
      121 mlratypsdr lgmplalrts aiglaaaagp vlggalvahw gwravfflnv vpagliglla
      181 lavrvptpad retagattta ggtrapaprl dlpgacllal alvclvhtlv tlpetgwtta
      241 ttlggaaaal acgafirher rtasplvpls vlrsttvasa lavllsasaa lfgalfvsty
      301 flqdvlamdp lqcglrvlpl avmmvlsapa savlqrrygp rrttvaamtl ltlgilalsq
      361 ldrtstapai sggflllgag fgtvmvtata vivrqvsadh agvagglqrt amnigpalgv
      421 atatmlvtlt aptaagnrpt ggphwtgeaf lsamgptllt laavaatgal aaaklprrta
      481 ggdspqspai tgrdrdpaaa tkavtsgd
//
LOCUS       WP_457678216             460 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678216
VERSION     WP_457678216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46162
     Region          10..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,135,
                     138..139,142,265,268..269,272..274,277,305,309,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mhkwlplvat csgtfmllvy stivtvalpg vaddlhasfs slqwiidvyt lalaglllgm
       61 gslgdnlgrk rlyltgltvf alatlacgla pdvmtliaar avqglagaam fstllpligl
      121 tytgrdrgva favwgavaga aagignvagg iltqflswqw ifhvgvpvcl atlalsaavl
      181 tddartptri dylgivtftp aalgitfgii nggeqgwtsg pavlgfavga vmlalfllae
      241 rtgsnpmiap alfrkrefng tlvaamgyyl agfgalpvis lwlqdgagls alstalvitv
      301 qpvaffatsa vagsmlhrlp ahrtlgggal avgagnvlml aigagsswta lipglvvtgv
      361 gagivspvlp saamsaapps qsgvasaaan carqlglalg iavlgsvfhr fsttsggtgl
      421 haayahglta vfavaaaigl gsgilalrll kpprpatqpa
//
LOCUS       WP_457678219             335 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678219
VERSION     WP_457678219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /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=35415
     Region          <81..>123
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          143..309
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdgvdhierm dgvdgvddri egggegggai esaeraggvd gvgdarralg gflrarrgrv
       61 apehvglagg rrrrvrglrr eelaqlagis vdyyvrleqg ratqpstevl dalagalgld
      121 aaerrhlatl agarrdpapr arvspllqrl ldsmahfpaf atnhrldvva wnglgaelig
      181 gvadpgrrdr nnarylfldp asrtvhpdwe drageavgql rvsagrypdd aeltalvgel
      241 sarsaefrri watgevvmca agrkrlrhpe aglltldyet lhvpaapget glvvhvfsae
      301 edseaavalg rlamtvmgsa qrsagadsae gggpr
//
LOCUS       WP_457678191             491 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457678191
VERSION     WP_457678191.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Perham,R.N.
  TITLE     Swinging arms and swinging domains in multifunctional enzymes:
            catalytic machines for multistep reactions
  JOURNAL   Annu Rev Biochem 69, 961-1004 (2000)
   PUBMED   10966480
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Mande,S.S., Sarfaty,S., Allen,M.D., Perham,R.N. and Hol,W.G.
  TITLE     Protein-protein interactions in the pyruvate dehydrogenase
            multienzyme complex: dihydrolipoamide dehydrogenase complexed with
            the binding domain of dihydrolipoamide acetyltransferase
  JOURNAL   Structure 4 (3), 277-286 (1996)
   PUBMED   8805537
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11482251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..491
                     /product="dihydrolipoyl dehydrogenase"
                     /EC_number="1.8.1.4"
                     /GO_function="GO:0004148 - dihydrolipoyl dehydrogenase
                     (NADH) activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=50330
     Region          6..489
                     /region_name="PRK06416"
                     /note="dihydrolipoamide dehydrogenase; Reviewed"
                     /db_xref="CDD:235798"
ORIGIN      
        1 msetdpnttd vlvigggtgg ystalraasl glrvvlaerd liggtclhrg cipskamlha
       61 aelvdgiaea rerwgvkatv dsldwpalva trdgivernh qgvaghlrta gvrvvkgtar
      121 ltgprtvhve gageftarrg ivlatgsrpr llpglaadgr rvvtsddalf aaglpasvlv
      181 lgggaigvey asfhrsmgae vtlveaagrl lplededvgr hlarglkkrg itvrtgstlt
      241 gtelladgvr atvrtpkgee lvigaerllv avgrapvtdg ldlaaaglaa dergfvapad
      301 wsrletsvpg ihvvgdllpp pslglahasf aegllvaetl aglpsravdy aavprvtyss
      361 pqtasvglte aearargldi kvntmplaat akgmvhgqgg mvkviaaadg aggdrglpws
      421 ndveslgktg avlgvhlvgp qvsemiaesq livgwdaepa dvaqhihahp tlseavgetf
      481 ltlagrglhq h
//
LOCUS       WP_457678222             264 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457678222
VERSION     WP_457678222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=28795
     Region          11..223
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mneatprqpk kilvvsahpe prslnaaltt favehlraag hevrvsdlya mkwkaavdad
       61 dfpdhpadrq lgvmaasers tlagrlapdi aaeqekvrws dalilqfpmw wfsvpailkg
      121 widrvftsgf gygpevpppy segalagrra llsatmgare safsdrgihg rladvlhpvq
      181 hglfwftgma plepfavyda nelpqdrfta akqaygqrld glftdepvpf rslvggdygr
      241 dmrllpgaes pgtagldlhv rpqa
//
LOCUS       WP_457678231             394 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678231
VERSION     WP_457678231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42363
     Region          1..394
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtelplsgit vvsveqavaa pfatrqladl garvikverp dggdfarryd ttvqgqssyf
       61 vwlnrskesl tldlkstrgr eileellvga dvfvqnlapg aaarleldaa slagrhttli
      121 pctisgygtt gpwadrkayd lliqcqtglv sltgtaeesa ragvsvadia agmyaysgil
      181 tslytravsg varavevslf ealaewmhqp ayytrfggtq pprlgtqhat vapygaytaa
      241 dgqevlfsiq nerewaalce rflerpdlvd dprfatgpdr vthrdalnai vaerfrrsds
      301 revtklldsa gianagvnsv eqfldhpvlr ergrwrdvgi pggtvpallp padlagtapr
      361 mdvvpavgeh terilaelgh gtaeieslra dhvi
//
LOCUS       WP_457678234             555 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces nigrescens].
ACCESSION   WP_457678234
VERSION     WP_457678234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 555)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61661
     Region          14..493
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(70,73,110,113,158,176,180,212,276,336..337)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(212,276,337)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          474..551
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 mtaqhldpar dttdwwrqav vyqvyprsfa dsdgdgigdl pgvtsrlpyl aslgvdavwl
       61 spfypselad ggydvadyrd vdprlgtldd fdamvteahr lglkvmvdiv pnhsshqhvw
      121 fqealraepg saardryvfr egkgehgelp ptdwiscfgg pawtrlpdgw wylhlfapeq
      181 pdfnwdnpev radfrttlrf wsdrgvdgfr vdvahglakd laaplrdigt vegytpgdlp
      241 edgshpfwdr devhdifrew rkvfneydpp rvavaeawvr ssrrtayatp qelgqafnfd
      301 flkasldaae lrasidtala daraagatat wvlsnhdvir hasryglpag rdeeawllsd
      361 gqepaldref glrralaatl lmlalpgsay vyqgeelglp evadltrdsl qdpvwtrsgg
      421 alkgrdgcrv plpwrregss ygfgsggswl pqppgwgals veaqqdeasa plelyrtala
      481 trrwlvpdea lewaddtsat argilhfrrs ggwecvsnlt deprplpage lllssapvtg
      541 dqlppwttvw lrttr
//
LOCUS       WP_457678237             451 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfate adenylyltransferase subunit 1 [Streptomyces nigrescens].
ACCESSION   WP_457678237
VERSION     WP_457678237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11458414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..451
                     /product="sulfate adenylyltransferase subunit 1"
                     /EC_number="2.7.7.4"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0004781 - sulfate adenylyltransferase
                     (ATP) activity [Evidence IEA]"
                     /GO_process="GO:0006790 - sulfur compound metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47364
     Region          1..426
                     /region_name="CysN"
                     /note="Sulfate adenylyltransferase subunit 1, EFTu-like
                     GTPase family [Inorganic ion transport and metabolism];
                     COG2895"
                     /db_xref="CDD:442140"
ORIGIN      
        1 mstttsaida vdagatsllr fatagsvddg kstlvgrllh dsksvladql eavehasrsr
       61 gqeapdlall tdglraereq gitidvayry fatprrrfil adtpghvqyt rnmvtgasta
      121 elavvlvdar ngvveqtrrh aavaallrvp hvvlavnkmd lvdyaepvfa aiaeefttya
      181 aslgvpeita ipisalagdn vvtpsatmdw yggptvlehl etvavvadps ddpgrfpvqy
      241 virpqtaehp dyrgyagqia sgvlrvgdav tvlpsgrtst ieaidalgqa vdvawapqsv
      301 tvrlsddldi srgdliapta gapgvsqdie atvchvadrp ltvgqrvllk httrtvkaiv
      361 kdipsrltld dlsqhpapge lvandigriv lrtaeplald ayadsrrtgs fllidpadgt
      421 tltagmagta faeaaeeaap aaaaddegwd f
//
LOCUS       WP_457678240             203 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678240
VERSION     WP_457678240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22131
     Region          52..186
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 msisvttwhl eqtspadlsp aqappaeqdv rivrsevpsp efsrflytav ggdiawtdrl
       61 twpyaqwaef lgrpgvetwv ayergtpagf ielageadgs veityfglvp afrgrriggh
      121 llaygieraw dlaerwpgra ptkrvwlhtc skdgphaman yqrrgfrlyd tkvaeedgip
      181 apgpwpgagp itgpittgtp age
//
LOCUS       WP_457678249             558 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457678249
VERSION     WP_457678249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..558
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60352
     Region          50..554
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mtphthdvvp rsgwaapsgk pplasrmmra twrglptkrh dvgwepglvv paadgsplrt
       61 dhyfprtkgd fptllvrspy grgvpwsply gilfaeqgfh mvlqscrgtg gsggrfdlsr
      121 neaadgqaav swlreqpwft gtlgtigpsy lgyvqwalal dpppelkamv vqvglddpha
      181 lfyeggalll enalavgagm tyqhrglmpf vrstlrlqrr lreitgarpl rgayvsalge
      241 vpwldevmth pdaddpywng asvaaaaera avptsvitgw hdvladqnlr qfarlrragg
      301 essllvgpwt htsalqqgwp evfseslawl rahlcgdrtg lrptpvrvhv ggedvwrdld
      361 dwppapatta wfpaengtls rqdpvesgpl vsfrhdpadp apsvggplls rsagprdnsa
      421 rearedvltf tgppltepvd ilgpvsarlr istdtghadv farlcdvdpe nrstnlcdgl
      481 vrlrttgqap sevtvamrat ahrfaaghri rlqvsagahp ryarnpgtge psaeatrflp
      541 vhltlhsgsa lmlpqetp
//
LOCUS       WP_457678262             183 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457678262
VERSION     WP_457678262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18678
     Region          26..164
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mghdahrvpr pagaagaags gddaldheve eviaavltas rmlvgvsara lgrtapsltl
       61 pqlralvvld grgpvklaal advlgvnpst alrmvdrlea agsvtrqanp gnrrevvlsl
      121 tdrgrglvaq vladrhaeia tivsrlpadr raglvealra ltdaadeppv aprpapppep
      181 sap
//
LOCUS       WP_457678265             397 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678265
VERSION     WP_457678265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42113
     Region          17..390
                     /region_name="Beta-lactamase"
                     /note="pfam00144"
                     /db_xref="CDD:395092"
ORIGIN      
        1 mepatvnghc apeftgvrda fernfsehge vgaavtvtvd geavvdlwgg hadaagtrlw
       61 erdslvnvys tskgmtalca hllvdrgeld ldapvtrywp efgqagkqdi pvrwllshra
      121 gliapreplp aghaydwerv cavlaatppw wepgtaqgyh avtfgylvge vvrritgqsl
      181 gaflrseitg plgarvfigt paeeharcad mvgqldeari aeqfpgvpkp pfrsladhpl
      241 aivmlaltyi ptgdvnsaay rsaeipagna hagahglatv ygalaggtlv gpgtleamrr
      301 sqslpgerdl tidalapagy ehrwglgfml nhqghagpnp rafghggagg sfafadpenr
      361 lsyaytmnky gggttgqdpr nagliravyq alaqhrs
//
LOCUS       WP_457678268             188 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678268
VERSION     WP_457678268.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19613
     Region          25..187
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mestqhpadt ggapsadgqs sslvlhingv tqtltvdhrt tvldllherl gltgakkgcd
       61 hgqcgactvl vdgrranscl lpavaqdgre ittveglaeg erlhplqqaf lerdalqcgy
      121 ctpgqicsav gmlaetadgf pshvtpptad paapveltdd eirermsgnl crcgaypriv
      181 eavreaas
//
LOCUS       WP_457678271             331 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457678271
VERSION     WP_457678271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34893
     Region          1..315
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpfgylrat sveeavraaa gqpgarflgg gtnlvdlmkl gvetpellid vtrlpldrie
       61 elpdgglrig amvrnsdlaa avpvrdrypa lsqallagas gqlrniattg gnllqrtrcl
      121 yfqditkpcn krapgtgcpa regvhrdlav lghsahcvat qpsdmavala aldaevhlhg
      181 pdgertvpvt dfhrlpgdsp erdteirpge litavrlppp apgarsryrk ardrasfafa
      241 lvsvaavlev rdgavqraal afgglahrpw raraaeevlh gspatedtfa raadaelaaa
      301 rplrdngfkv tlarnlavgv laalaapadd h
//
LOCUS       WP_457678287             266 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457678287
VERSION     WP_457678287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28728
     Region          24..240
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mnsshpagra avgpavhrva vatetaafva aldgadlsvp vpgcpewtlr dlvrhtgsvq
       61 rlfsvllrrl vqepprsrev eldlptaedg wadwlsasaa eaadafaatd pdapmwawgv
      121 dqharfwmrr mlfetlvhrt daeravgrrp vidpalatdg vdeflanlpf atsfaphvar
      181 lrgkdetlrf gctdtdgdwl vrlrpdgfga eprtgdaaae sadagvrgta adllllvygr
      241 ldrgadtvet tgdeelltrw ftnsaf
//
LOCUS       WP_457678296             507 aa            linear   BCT 27-JAN-2026
DEFINITION  long-chain-fatty-acid--CoA ligase [Streptomyces nigrescens].
ACCESSION   WP_457678296
VERSION     WP_457678296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..507
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54820
     Region          5..505
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(167,170..175,177..178)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(170,284..285,307..312,392,404,407,418,498)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(170,210..211,258,260..261,264,284..285,307..312,392,
                     404,407,415..418,479)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(210,260..261,264,284,415..417,473,479)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mtfnlatalr esrrshpdkp lchladrtat yaqadeasgr iaatlrglgl rpgakvavhl
       61 pnvpqflfty ygilkaglvm vplnpllkap eiayhlqdse srllitfeef aaeavkgael
      121 aggvgtyvvh ppgsdrriag trhhdelyaa ddtgeiapts addtavllyt sgttgrpkga
      181 elthfqlhmn ctvsgelfgf rpddialavl plfhvfglss vlnmavrhgg tlalvprfgt
      241 davlevlerh rctvfagvpt myaallqadt vkrdlgalrv gvsggaampg evirafeekf
      301 pgvvilegyg lsetastatf nisaeqrkvl sigkpiwgve vrivdpsgae lppgpehvge
      361 ilvrghnvmk gyhrrpeeta ealrdgwlht gdlghrdedg yffvvdrkkd lvirggynvy
      421 preveevlht hpavaeaavi grpddrlgee viavvslkrd ttataedlta hckerlaayk
      481 ypreirivde lpkgptgkil kkalrag
//
LOCUS       WP_457678309             285 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678309
VERSION     WP_457678309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30936
     Region          29..269
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 madeqsqvpd gtavrvalwr amhvqvdspp hviedeiglq laapeegwrr rpdmdprgts
       61 pfraaivara rfiedlvveq aghgvaqhvv lgagldtfaq rrpdiaarlr vfeidqpatq
      121 awkrqrliel gygipdwlrl vpvdfeaggd wweqlsdagf dpgrpavvvc agvtmyltkd
      181 anaatlrrla glspgstltm tfmlptdlvd dadrpaleat kpqaqaagtp fisfytpqem
      241 lalardagfk dahhvpgaal avryfaerpd glrpssgedl lvatt
//
LOCUS       WP_457678318             461 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678318
VERSION     WP_457678318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46278
     Region          10..441
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,135,
                     138..139,142,261,264..265,272..274,277,305,309,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrkwwplvav clgtflflld ttvlsvvlpg tgeeldasls alqwvaniyt lvlavlmltm
       61 galvdrlgar tvyvvgltvf giaslvcgla pdagvliaar gvqgiggaam avttfaligs
      121 vyrgpdmgra mgifgavtgl aaavgpmlgg vltqylswra vfflnlplva vtvalslrvl
      181 aagrpgtgrr idlpgmaafa acagsltyal tlaadegwas paalglltla tlslvvftri
      241 elrsgaplld vrlfsrasfs gvmmcvaast aafaalvyts vwlqsglglg pvraglalmp
      301 lalasfatsl isgrrlhgrs prailatgll lsgigcalqa gldadssags laaglaltgi
      361 gvglmgpamg aavfaalppe rggmaagamt tfrqlgqtlg vaafgllfqh hggamsegln
      421 rvliaaaatg iigsalacaf vpkpaaakat gtrprnltgs r
//
LOCUS       WP_457678321             793 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces nigrescens].
ACCESSION   WP_457678321
VERSION     WP_457678321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..793
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=84070
     Region          15..790
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mgttgtptki tqgsqtkggi gestlrpdgt lkvtgefays sdmwhedmlw gftlrstvah
       61 aeivsidtse alaqsgvyav ltyddlptsi knygleiqdt pvlahgkvrh hgepvalvaa
      121 dhpetarraa akikidykel pvvtdeasat aadapllheg rddhhaghva hpnivhrqpi
      181 vrgdagaaak kadvivsgey vfgmqdqafl gpesglavpa edggvdlyia tqwlhsdlrq
      241 iapvlglpee kvrmtlsgvg gafggredls mqihacllal rtnkpvkivy nrfesffghv
      301 hrhpaklwye hgatkdgkit hmkcrivldg gayasaspav vgnaaslavg pyviddvdie
      361 avalytnnpp cgamrgfgav qacfayeaqm dklaaklgld pvelrqlnam eqgtimptgq
      421 pvdspapvae ilrrvkarpl pperqwesse gadvrqlpgg lsntthgegv vrgvgyavgi
      481 knvgfsegfd dystakvrme viggepvatv htamaevgqg gvtvhaqiar telgvtqvti
      541 hpadtqvgsa gstsasrqty vtggavkhsc elvrekvlem grrkmgtyhp awataellle
      601 ggkvvtdgge vladlvdvle geaveieaew rhrpteafdl vtgqghghvq ysfaahravv
      661 evdtelglvk vielacaqdv gkalnplsvv gqiqggttqg lgvavmeeil vdpktakvrn
      721 psftdylipt ildtptipvd vleladehap yglrgigeap tlsstpavla airnatglel
      781 nktpvrpehl tgt
//
LOCUS       WP_457678327             191 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678327
VERSION     WP_457678327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..191
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20619
     Region          11..180
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 midatalaek pvltgsrirl vplairhaaa fhaacqdpet rrltgthhdf tlaeleawca
       61 gsaeradrld laiedresgd flgelalsqi dppnahgsfr ialvpeatgr gvgseatrll
      121 lgyafdrvgl hrvqlevydy nprarrayek cgfevegrmr ealfwdgawh dvlvmavlrt
      181 grgggagaga g
//
LOCUS       WP_457678340             127 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase TusA family protein [Streptomyces nigrescens].
ACCESSION   WP_457678340
VERSION     WP_457678340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Tanabe,T.S., Leimkuhler,S. and Dahl,C.
  TITLE     The functional diversity of the prokaryotic sulfur carrier protein
            TusA
  JOURNAL   Adv Microb Physiol 75, 233-277 (2019)
   PUBMED   31655739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..127
                     /product="sulfurtransferase TusA family protein"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13140
     Region          <43..89
                     /region_name="TusA"
                     /note="Sulfur carrier protein TusA (tRNA thiolation,
                     molybdenum cofactor biosynthesis) [Translation, ribosomal
                     structure and biogenesis, Coenzyme transport and
                     metabolism, Posttranslational modification, protein
                     turnover, chaperones]; COG0425"
                     /db_xref="CDD:440194"
ORIGIN      
        1 msrrrdtprv tatspaapgp apeadltvdg tgllcvalll rlraaiaeag pgtvvhiitt
       61 dpaapldlpa wchmtghhyl gpvlddedgs vddedssvya lrlaadarpt radapwrtar
      121 psgdtgp
//
LOCUS       WP_457678346             415 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678346
VERSION     WP_457678346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41867
     Region          23..381
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,150,
                     153..154,157,238,241..242,245..247,250,278,282,331..332,
                     336,340,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mnqltdtgrr alatapphma rlrraislff aldgfvfagw vvripaikeq ihasagalgl
       61 allgvsvgsv atmlltgklc rrygnhpvtv vtaallslsv alpplthsal hlglvlllfg
      121 aaygglnvaf naaavdlaea vrrpilpsfh aafsagglvg aglggllapr lsplchllll
      181 tatglvvtay agrvllrtpg ppatgqrarr dgtdavpgrg raavgrtrlf vtayglitlc
      241 taygegalad wgslhlsadl htgpgaaaag yavfallmtv srmsgtwlle rlgdtpvlva
      301 ggllaavgml vgalapqlwl vylgyaltgl glanvfpvav ggagalagph gvavastlgy
      361 sgillgppsi gflaeayglp galttiaala alaallgrvv grgrvgrrgr rrapc
//
LOCUS       WP_457678352             549 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457678352
VERSION     WP_457678352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..549
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59525
     Region          79..>261
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          443..522
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mvtalatapa ggatgaaaap papvahrief grcaavehlp ssvecgrlav pldyarpdgk
       61 eihltvsrir atargerqga lvfnpggpga ssmefplygs lpkwsklara ydfvgyaprg
      121 vgrsaplscq dpkefakaps dsrmhpdaaf krqkrteare yargcvrrag adlpyynsin
      181 nardldmlra algekkltfm gasygtyfga vyatlfpghv rrmifdsvvn psprkiwyrn
      241 nldqdiafer rwgdwlgwva rhdkqyhlgt tkkavqhsyd kaayklrrkp lngkigagql
      301 qsaflktgyn dafwpmraea lsgylhgdpk pllaqalpra agaaadensn avytavecnd
      361 apwprdwgtw drdnteiarv apfetwdnaw mnlpcaywpd rsasaaaeld aavrradhpa
      421 agqdlvdvag haartqvdda lhgrrgpldv htepgalppv lllaaerdaa tpypgalelq
      481 rrlpgsslvt engagthgva fndnacvnky aeayllhgki pahkvycgpr aepvpgqqat
      541 raqhalpgk
//
LOCUS       WP_457678360             485 aa            linear   BCT 27-JAN-2026
DEFINITION  catalase [Streptomyces nigrescens].
ACCESSION   WP_457678360
VERSION     WP_457678360.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..485
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54160
     Region          2..480
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mtarflttea gapvadnqns atagvggpiv lqdqhllekl arfnreripe rvvhargsga
       61 ygyfevtddv tgfthadfld tvgkrtetfi rfstvadnlg gpdaardprg falkfyteeg
      121 nydlvgnntp vffikdpikf pdfihsqkrd pftgkqepdn vwdfwahape athqitwlmg
      181 drgipasyrh mngygshtyq wtnaegeaff vkyhfktnqg ircldaeqga elsgkdpnsh
      241 qtdllqsier gvypswtlyv qimpaaeaad yrfnpfdltk vwphsdyplq rvgrlvldrn
      301 pdnvfaeveq safspnnfvp gigpspdkml qgrlfayada hryrlgvnht qlpvnapkat
      361 taanhgrdgl matngydrya knyepnsysg pvqtgrplsa plavnghvgt heapahtkdd
      421 dffqagelyr lmsqeekkrl vnniagglsq vsrddviekn lahfhaadpd ygkrvearvr
      481 elred
//
LOCUS       WP_457678369             165 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678369
VERSION     WP_457678369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17874
     Region          <43..154
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrfvelsstt mvalleddla rasaeagval teyfvtdrak wvwqyrvnql tsdpgcagwv
       61 tqmvvaepeg vvvgyagfhg ppdeagmvel gysvipvhrr qgyarailta lvrravaear
      121 vrtvrvtisp dntaslatis gfgfveageq wdeedgleli fevpv
//
LOCUS       WP_457678383             567 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457678383
VERSION     WP_457678383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59353
     Region          2..564
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mdtyadlvfl ggrvvtvdae fsvasalavt ggiisavggq ddvaplvgpg trvvdlrgat
       61 llpgindshl hgcafgmatp plsldlghpa acsladvaea vceavgrvpd gqwitghgwd
      121 tgyldecvsd psrlpsrhdl davspdhpvv lysfsghatw vnskalelig idrhtvappg
      181 gaivadeage ptgllhegaq alvqnalppl srqertdair stlatlarlg vtsytepglg
      241 pggdgimrga lgaetldiyr rlladgelta rlgvlllptg mastaeefar tltalgecgd
      301 adprrlaihg vkifadgivp nktawmhepy vgggcgslcv ggatdaeria eidamirhah
      361 aaghqlgvhv tgdraidtva dafaaamaeh prldarhyvi hgdfltahsm kvlaahgfgv
      421 nmnptikwtv admeeefvgv graayawpyr daidagvrva sgsdapvtyp dwrqgvatmm
      481 lreskaagrv sgpeqrigla eairtytida awqdfaddwk gslepgkvad lcvldgdllt
      541 adphdipelp vvltvmdgqv vhnalrd
//
LOCUS       WP_457678390             391 aa            linear   BCT 27-JAN-2026
DEFINITION  ice-binding family protein, partial [Streptomyces nigrescens].
ACCESSION   WP_457678390
VERSION     WP_457678390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Vance,T.D.R., Bayer-Giraldi,M., Davies,P.L. and Mangiagalli,M.
  TITLE     Ice-binding proteins and the 'domain of unknown function' 3494
            family
  JOURNAL   FEBS J 286 (5), 855-873 (2019)
   PUBMED   30680879
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10572153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..>391
                     /product="ice-binding family protein"
                     /GO_function="GO:0050825 - ice binding [Evidence IEA]"
     Region          17..203
                     /region_name="Ice_binding"
                     /note="Ice-binding-like; pfam11999"
                     /db_xref="CDD:432251"
ORIGIN      
        1 matlvplgsa atfgvlanta vtntgptvvt gdlgvspaga vtgfnppgtv tgtihvndaa
       61 aaqaqadlli gygnallqpa tatvatelgg ttltpgvyns lsgtfslngp ltldaqgdpn
      121 avfifktntt litgaagtvn laglaqsshv fwqvgssatl gvgttirgsi lantsitant
      181 gaivdgrlla lgaavtldtn avtvpalatc qvvvqpvvgp vvvgqptpvs avvtcnglpv
      241 sgasvtfngg avpvtvttna agvatgsltf ntagaatvta tvtaagtacs ctgvvsaplt
      301 itvtpqqscq vvvqpvvgpv vvgqptsvsa vvtcnglpvs gasvtfngga vpvtvttnla
      361 gvatgsltfn tagaatvtat vtaagtacsc t
//
LOCUS       WP_457678405             629 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678405
VERSION     WP_457678405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 629)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 629)
  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 629)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..629
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66275
     Region          11..606
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtaattktpd rstwgavttm yrlttghras vvvatvltla gsalglsqpl laknivdasr
       61 hgrtfwplla llatlfvtea atgavgrfvl ermgegvvrg lrhgliarll rlemnqyhrh
      121 rtgdlisrvt tdttllrdvv sqalvdlvtg alaaagavvl mawidpllll lvaltvataa
      181 vvvasllkgi raasarmqgs vgavaaeler algalpmvrv hraeereaar igtrvnaayd
      241 agvrtaklas vmspavelav qgsfllvlvi gglrvnghan slgdlvafll yasylvlpls
      301 svfravglmq rgmgayqria qalampaepe evveraeave avertgpggc vvrvtprrae
      361 rtgkgeapal alhdvrfgyv pdrpvlngvs ftvphhgqva lvgrsgagks tifalvarfh
      421 epdsgtllfd grpaaelsrg acrariavvd qnthvvhgsl rdnityaapd agdaevrrvv
      481 elarldgvvr rlpgglsgvl gergntlsag erqrvalara llarpallll deptshldai
      541 netalttlmk eaaqecallv iahrlstvrh adriivleeg rtvasgshee llttspsyra
      601 laagqmlrpa hgtsgadaat aaherprtp
//
LOCUS       WP_457678411             330 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457678411
VERSION     WP_457678411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  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 330)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36125
     Region          9..309
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(18..20,51,56,81,126..127,156..157,176,204..210,261,
                     278..283,286,289..290)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(51,56,81,126)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mqqrklgqdl evsalglgcm gmsffygqpq dtaemtkllr aavdhgvtff dtaevygpft
       61 nedlvgqala pvrdqvviat kfgikhgeng ptpmsgvdsr peqirqvaea slkrlqtesi
      121 dllyqhrvdp nvpiedvagt vkeliaegkv khfglseaga atirrahavq pvtalqseys
      181 lwmrehetei iptleelgig lvpysplgkg fltgkidsst sladndlrrl lprfspearq
      241 anqvlvdllq qiaddkgatp aqialawvla qkpwfvpipg ttklhrleen lgaldveltt
      301 gdlhrieeaa aniriqgerl peqlqsrfgr
//
LOCUS       WP_457678465             445 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Thermovibrio sp.].
ACCESSION   WP_457678465
VERSION     WP_457678465.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000486
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     Protein         1..445
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48139
     Region          35..427
                     /region_name="ClcA"
                     /note="H+/Cl- antiporter ClcA [Inorganic ion transport and
                     metabolism]; COG0038"
                     /db_xref="CDD:439808"
ORIGIN      
        1 msrkerwdff lsfvkgcakt nlkhrfdlss islffgrwip fafavgittg aiaslmdvli
       61 ieinkllikn ppililypll vavitglala kdpaiggpgi gyailhlktr vyiplssvim
      121 klitstfals ggfiagregp sffigvaige wlgkayglgk ryksllglig ggaftgallk
      181 aplgsaifam eleemynldy rpfvpmiias iisyltfsff rgenafihlt kmphwdlkti
      241 pyivvmglai slviyaytfi fhtcnctgkf fdpkvrplvg tavaipilla lylvthdtdf
      301 lsapahmgvv sklaqvqfpi widlvvivsv ilatsftlaf gipgglvlpn lligaavgnm
      361 fghlfpneiv tftlagmgaa laagaktpla aivmitemth advvipmtaa iitsyttsfg
      421 fslylgqeir lrpmmgrdrr dgtkr
//
LOCUS       WP_457678475             444 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678475
VERSION     WP_457678475.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 444)
  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 444)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 444)
  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 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46703
     Region          144..412
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 msaespliks mrtavaaspd dvplrlhlae lllgaghgda avgevaaalq hapgdvqare
       61 lmvralahtp astpgeaalp pppqapvpar ppapagvppq dsvlgpppap asspgfdwka
      121 aqdqvgdavp prfveaplav dgggdpgdaa awdverpgpv rladvggmqe vkerleaafl
      181 aplrnpelrr lygkslrggl llygppgcgk tfiaravage lganflsvsv ndvldmwign
      241 sernmhelfq tarrqapcvi fldeldalgg krsrtqssgm rntvnqllte ldgveaaane
      301 gvfvlaatnv pwdvdialrr pgrldrtllv lppdgparea ilryhlrerp ienvdlgklv
      361 katdslsgad lahvceaaae halldsartg tvrligmkdl laaagqiaps tepwfasarn
      421 vamyandggm yddlvaylkk krkl
//
LOCUS       WP_457678478             375 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces nigrescens].
ACCESSION   WP_457678478
VERSION     WP_457678478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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 375)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18770923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42028
     Region          9..255
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          9..117
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(9,12..13,15,39,42..43,46..47,49..50,73,76..77,
                     80..81,84)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          9..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          37..67
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..102
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mttlhpaveq aqalidfery dqarallsqh lvedpgdtra wielgychlk mqqpeqalea
       61 adealkiape dfyvlilrak altsgpnssw raaepvlrea vradpqhwyg ytmladavcr
      121 msmvrffqan gsrkpephev dlvyreaadl asealrlgpe evyaheiahq iatfsgnitr
      181 adqlerailr ldpthaeala aqtrkaaeap gvkapqaadl yatglasapn stelqrgldq
      241 atyrmlrgvr wlallcvcls gagmdlfave gevqrelplp lgqrlwdlvp mtaiwlvgal
      301 lryrrrragv rlnvqslirr rrwarivvaq avwamlcall itqvpweert lpqvllwagi
      361 aptfatiwfd rnktr
//
LOCUS       WP_457678481             414 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678481
VERSION     WP_457678481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 414)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Domain dislocation: a change of core structure in periplasmic
            binding proteins in their evolutionary history
  JOURNAL   J Mol Biol 286 (1), 279-290 (1999)
   PUBMED   9931266
REFERENCE   6  (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   7  (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 11450659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="sugar 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=43110
     Region          11..414
                     /region_name="MalE"
                     /note="Maltose-binding periplasmic protein MalE
                     [Carbohydrate transport and metabolism]; COG2182"
                     /db_xref="CDD:441785"
ORIGIN      
        1 mrtsvecrri rligtlaatv taaglllisc ggdgsrprpt esgkitltem dyyssepgrs
       61 alakqltrcg kpagvtikrq ivpdlrtkvl qlansralpd lilldnpdlq qlaatgalad
      121 lgaagvktdg mypnivaagk yqgkqygvap gvnqlalyyn tsmlekagvk ppatwdelri
      181 aakkltqgdk vhgigfavpa teegsfqfes fffsagaslk kldspdavsa lsllkdlvas
      241 gsapkdvlsw nqmnvgeqfa ngslamming pwelpllrka gmkdfgivpv papaggtssg
      301 alggevwaag sggdksrkaa evikcmvskg nslewakltn yvpsdpevaa efsaavpamk
      361 tfvetigsak srtaevgpdy ptysqalwta vqaalsgsks pgaaltdaqk qatq
//
LOCUS       WP_457678484             299 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457678484
VERSION     WP_457678484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32555
     Region          27..292
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mapaargrrl girfivpvvv fvavfylypl arnvvlsfqd ydinslysgn apfiglgnyr
       61 rllstptfat avvntvvfva gslffqftig lglaeffrrs fplspllrsl mllpwllplv
      121 vggtlfrwll dtsngvvnqi lltlhlvqdp vpwlntpnta masvlicniw igvpfnmvil
      181 hsgllaipte lyeaasldga ghwqqfryvt lpqirpvigi vvtlgliytl kvfdviwvmt
      241 kggpanatht ittyayqlsf gglsefglga aagdlliiva avfallylra lradpgara
//
LOCUS       WP_457678487             688 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 31 protein [Streptomyces nigrescens].
ACCESSION   WP_457678487
VERSION     WP_457678487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..688
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76261
     Region          142..245
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            180
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          245..577
                     /region_name="GH31_xylosidase_XylS"
                     /note="xylosidase XylS-like; cd06591"
                     /db_xref="CDD:269877"
     Site            order(262,290..291,329,404,406,459,473,476,509,539)
                     /site_type="active"
                     /db_xref="CDD:269877"
ORIGIN      
        1 msppdgtrpa psastsdaag tssrppassr pavclefgda ehvlrvepwg adsvrvrsar
       61 hrvrddlpga lsvppaaaaa elgvgphgsr iltvgrlqve lsprghlrfa rtpdgtellr
      121 esvghfawpg prqftpvgeg ryqleqrfaa ydgeqffglg qhshgrldhk hmvidlvqrn
      181 gevtipftls srgygllwnl pavgrvelaa hqtrwvadaa dqidywittg ptpagimany
      241 adatghapal pewalglwqs rlryrtqeel lgvareyqrr glplsviavd ffhwphlgdw
      301 rfdaadwpdp agmvaelasm gvrplvsvwp svsvvsenyp hmrderlllg tehgqpfqhv
      361 fpdsqvddks lpvvfydptd erardyiwsr ikrnyydlgf rlwwldacep emypeqfgnl
      421 ryaagpgrav anlyprehvr gffehmraeg edvpvslvrs awsgsqayga alwsgdipat
      481 fealaaqvra glsaglsgip wwttdiggfh ggdpddpdyr ellirwfqfa vfcpllrmhg
      541 hreprdafaa grtggpnelw sygqdayril trqlrlrqdl raylhrqmvs aadcgapvir
      601 plffgfpddp aawtvedqfl cgpdllispv trlgerhrqv ylpagadwka aatgtvqdgg
      661 qtttadaple cipvfvrhgs tldvrfpg
//
LOCUS       WP_457678493             273 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678493
VERSION     WP_457678493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29570
     Region          24..162
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mptlpreqpe paqshqarrt aesfgadaqr ydqarpgypd glvarivags pgpdvldvgc
       61 gtgiaarqfq aagcavlgie pdarmadlaq arglqvevat feawepvgrv fdaliaaqsw
      121 hwvdpvagav kaaqvlrpng rlaifghvfe ppaevaepfa aayrrvapds pfgnqparrs
      181 lemyqagyak iadkireteq fnepeqwrfd weqsytrdqw lellpttggl trlrpdqlae
      241 ilgavghaid alggrftmhy ttlattavra gtp
//
LOCUS       WP_457678496             200 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678496
VERSION     WP_457678496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21156
     Region          8..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptgvhlrda rqqlfdaaer vllrdgpngl tsravtdeaa cakgvlhrhf tdfdafltel
       61 vldraaqlet qahelretvg tgtvadnlts alttlfgpvp vaiiplitfr delrtrlrqa
      121 tpgggiaila qvttavsayl aderamgris adadidsltl slvggghllf adrdpdpptt
      181 atvnklvttv lagvvqrrpg
//
LOCUS       WP_457678503             734 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457678503
VERSION     WP_457678503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..734
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77096
     Region          28..708
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdvvvrsva ggrarltvpw vrarpgsagl vderlmgvrg fralrifprt gsvviwmapd
       61 llhidrlvaa ldeappastp akasrsvpds stgelarlvv ggavpafval rrllrrprit
      121 agssgllgai tlftglpffr galrslrgrs hpgtdtlvta atvislvlre nvvaltvlwl
      181 lnigeflqtl tlrrtrraie elltireerv wlvrdegadg agrveteval devtpgdvva
      241 vyehhripvd ghvatgealv dqaaitgeal pvyaragaev yagtivtsgs ltvratavga
      301 dttvgriisr veeaqsdrap iqtvatrftq rfvpvsfala altyvvtrda rramtillia
      361 cpcaaglatp taisaaigng arrgtlikgg phlegigrvs avvfdktgtl tfgrplvtsi
      421 vtlsdrhtan evlslaasge lharhplaqa ivahteeqhl raplhqacev vlgmgmrael
      481 dgtrllvgsp allrqhgvel tqqaqgwteq lrgsgetvic iahddeligl lgvsdavrsg
      541 agsviqqltd lgvsrlillt gdapetaqvv adtlgitevh ahalpegklq lirdlqtegh
      601 tvamvgdgtn dapalaladv gismgahssh valetadial pgddlrqvpa vvelsrhtlr
      661 vvrqnyglai gvnllglvag aggsnnpvla allhntssia vvansarlvn htphlpqtad
      721 dmltaapled rrvr
//
LOCUS       WP_457678517             317 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678517
VERSION     WP_457678517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34221
     Region          16..273
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtnhdeaaav rpltlawvsr hlevgerivr tealqggita emrrltigrp dggtrdlvlr
       61 tfvnvehaed wlnreagalt lltgtgvpap glvavdpaaa hceypsllmt hlagrtvldd
      121 egletrvpll arqlvaihal rpaerpreyv awttadtvvt pkgadaaawa aaidvirrpa
      181 pryegrflhr dfqpgnvlfd vsppesagar itgvvdwaat swgpadldva hcstnlallh
      241 gpawglrfae ayeeaggvla aaaserlywq vrdglafsee vqlvaqpwre agraelttra
      301 veerldayvt almdalg
//
LOCUS       WP_457678526             205 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457678526
VERSION     WP_457678526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 205)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22601
     Region          1..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msdgnrrvea aealqdrarr llpdhpvria lldliaetgt ltsteaaarl ghssglcsfh
       61 lrqlarygli eeaphhggra rpwrlrwdtp qhtgeeesee ftalargled esyqhwlahr
      121 dqapagwqqd esfstvlhlt paetaelats irrllagyrn rgdhpatrsp navavaavtr
      181 lfplltehql psqstpsrve gstds
//
LOCUS       WP_457678529             191 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678529
VERSION     WP_457678529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20848
     Region          9..>126
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtepsgrrer kkaatrqkia daalrlfler gydavgirdv aaeadvavtt vfahfaskea
       61 lvferdqdfe qrlaravtdr ppheplipal hrevqalvrh ctaegsapvr rmieespalr
      121 eyeesmslrh aqalaaalaa dphlsrsata cratarfaid ayalacradd pgatvdevfr
      181 mitaaweata p
//
LOCUS       WP_457678532             214 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457678532
VERSION     WP_457678532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  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 10172259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=23200
     Region          57..207
                     /region_name="SRPBCC_Smu440-like"
                     /note="Ligand-binding SRPBCC domain of Streptococcus
                     mutans Smu.440 and related proteins; cd08862"
                     /db_xref="CDD:176871"
     Site            order(59,61,63,72..74,76..77,92,104,106,108,110,127,129,
                     138,140,154..155,157,159,168,170,172,174,186..190,
                     192..194,196..198,201)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176871"
ORIGIN      
        1 msgirstgvr aalftaplll gllgtaaapa ravgshtshp dksltcrgkg vdpdalvrhr
       61 teivinaplr tvwklqadve rwpswqtpve tverldhgpf rkgsafrwtt pippnpstpa
      121 tslditstvq qikrnscirw tgpaigeglr iegvhvwnft kvkggvrvst eethtgaqve
      181 advptatkll regleawlrd lksaaearah nrph
//
LOCUS       WP_457678538             520 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457678538
VERSION     WP_457678538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56519
     Region          5..510
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 maiqrrqllr sglflgagaa lptalasagp alaapalvrs grpalthgvq tgdvtahggv
       61 vwtradrpar mavevstrpd farsvtipgp vltaetdftg kvklsglpag sdvhyrvrla
      121 dpgdaslvge patgrlrtap tvrddvrfvw sadlagqgwg inpdaggyri framaerdpd
      181 fflcsgdfwy adgvipetrt lpdgsvwrnl vtpekskvae tlaefrgqhk ynlmdenlra
      241 faaavpqinq wddhevlnnw ypgevltdtr yterrvdvla ararqalfey lpietgpsgd
      301 grvhrvmryg plldvfvldm rsyrdansan tgpatdsgil gtkqvawler elaasratwk
      361 viaadmplgl vvpdgtaqea iaqgdggapl gregeiarvl sfihrrhian tvwltadvhy
      421 taahyydpdk aafqdftpfw efvsgplnai vanepnkldg tfgpqvrfqa lapdaehnnp
      481 afghqyfgev didgsskvmt vrlrdidgka lysvaidpqr
//
LOCUS       WP_457678541             527 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457678541
VERSION     WP_457678541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..527
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57008
     Region          92..>272
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          399..492
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrsrriapvl aasavaaalv ptltpatasa aenplpqhle qrpawhrcss atpasfqcat
       61 ikvpldysrp ggkkidlais rikasssaer rgvllvnpgg pggqgldmpq vlsaelpksv
      121 trkydligfd prgvgqsspl scgltaeeen wqrpykaatf akdvkwartv aekcnakqgd
      181 klrhittrnt ardmdvirav lgekkisylg ysygtylgav ytqlfpkrsd rivldsaidp
      241 ariwrgmiqv waegseptft rwsewtaqrn atyklgntpd kvrktfwglv aradrkpief
      301 kgamvsgddi ragramffsv rdaaeeivel kkaadgrapd snpdtgtper pappsfgrav
      361 psdnasaafw avacadtraw prdpeqyrrd airdkakypl ygdfashikp cafwkkngse
      421 pattidnkvg vltlqnewds qtplssglgm hrvmkgsrmv tvaggaghgi ygskscadkt
      481 ataylttgkl pakdvtcqap aaarerssat klplppppgi pgmpgrf
//
LOCUS       WP_457678545             304 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678545
VERSION     WP_457678545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  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 304)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10015415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32858
     Region          19..279
                     /region_name="mthyl_TIGR00027"
                     /note="methyltransferase, TIGR00027 family"
                     /db_xref="CDD:272862"
ORIGIN      
        1 mvgtahrntg vedveggvgl tallvaaara iethrhdsla rdvyaehfvl atpacagwpv
       61 lvqqvpdgda nplwgrfary fglrtrvldd fllrsmhaga rqvvllgagl dsrafrldwp
      121 pgcvifeidr egvlafkhkv lgglsatpka arvpipidlr adwvgaltda gfdtaapsvw
      181 laegllfylp naaetylida vdrlstegsa lafevklekd llayrdsply tstkhqigid
      241 lltlfdrepr pdsagnlaak gwstsvhtpf dftrrhgrgp lpeqndalag nrwvfankpc
      301 aagt
//
LOCUS       WP_457678557             489 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678557
VERSION     WP_457678557.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50754
     Region          23..469
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,282,285..286,289..291,294,322,326,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 msaviqerpa vqagriptvv rllvlatfvv ilnetilina iprlmeslhv tqqsaqwvst
       61 afmltmaaii pvtgwflqrv ttrqayaiam gvflagtals avapsfevll lgrivqaagt
      121 avmmpllmtt lmivvpeqdr grvmgnvtla isvapalgpa vsglilqvgs wrmlfvvvlp
      181 iaalvtlfgl rkvdnisepq vssidwlsvs vaalgfgglv yglsllgetd ggvglgigiv
      241 iagvaaiavf virqlklqrn gvplmdlrtl ghrtyglsla lisvgflaml gsmillplyl
      301 qnmrglsple tgllvmpggl amgllgptvg klfdrfgsrp lvlpgsigmv lalggftqvs
      361 mtmpywqvlg lhallmvsla atftpvftlg mgalpphlys hgssmlgtlq qvaaafgtal
      421 vvtvmtarag hlvddgvaaa paelsgmkla fgvaavlslv tivvaaklpr riaaadaqeg
      481 stadqptas
//
LOCUS       WP_457678569             289 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase [Streptomyces nigrescens].
ACCESSION   WP_457678569
VERSION     WP_457678569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29727
     Region          19..279
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mngpspgalp gplvgtdwva prlgtpglvv ldasigghrd ageripgarp fdidgalsdh
       61 sgplphtmpg gghftremra lgvddgdtvv vydgaglyst arawwmlram ghdrvavldg
      121 glpawraagl pletgaptpa arpgdftarp rpglivgsde vsaaltdpas avldarardr
      181 fagavaeprp glrpghmpga lnlpfgelqr dgrmrpasql rdafaplagd rrrlffscgs
      241 gvtacilalg aelagyddla vydgswsewg lpdadrpvvt gpqsggpsa
//
LOCUS       WP_457678587             405 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678587
VERSION     WP_457678587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43786
     Region          14..405
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 msnehrdtgg hgqlhglkvv efahvvagpl agsmladqga dvvhveppgs gdaaramgpk
       61 kdghplwfkv agrnkrsvtl dlhhedgral ahrllawadv vivtlragrl rswgldweav
      121 hrinpkavll qvsgfgatss qadapgfgkm gearsgavhl tgfpdgppvh tgfshgdavt
      181 glmgayaila alhrrdhdpd fdgewidlal feplfrlvew qvivhdqlgt vperagnqla
      241 vapaavinty ssrdgewitv tsatlrsvcn iarllglpee efataeqqha grrrldeglr
      301 awvaerttae cleeftrnev vasrvfsaad iaadpiyaer edivtvddad lgpvrmqavi
      361 phfrqnpgqv wrtgpalgqd nhlvysewlg lgeqeladle kngvv
//
LOCUS       WP_457678590             245 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457678590
VERSION     WP_457678590.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26625
     Region          7..120
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          134..242
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtlqlvqvnf karddsalgr fwaealgwgv ssegpgvtnl epagfdwpdp savcidlvrv
       61 pdpetvkcrv hielattsda hqaelvarlk elgatpadmg qgdvpwtvma dpegnvfsvl
      121 eprelyrdtg piaavvvdca dpramvrfwg eaidwtvhel tddrallrsv kgvgpylefr
      181 rtpddevvwn rihldvmsdp vedqakevar leglgairad vgqgdvswvv ladpagnefc
      241 vlgrg
//
LOCUS       WP_457678593             353 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457678593
VERSION     WP_457678593.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=37202
     Region          <13..341
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mdlltptsvs sapllavapv tavslfgpvg ivgvgltama vqaglafvag sydwqgdaav
       61 qitlasvtal avglnrslrm qhasasrary aaevaqravl psppsrlgdl riaaryvpae
      121 dmaliggdly vmqetpfgvr amvgdvrgkg lsavtavsvd igvfryaadh epdlpalvgc
      181 meealwresq rregldateg fttalivqfa ddlsqvhivn rghpapvllh adgrarvlep
      241 eeaapplgit glgdwsspve typfppgaml lcftdgvtea rdpagvfydp adrvphmvqs
      301 ylrqtshfpd pstvldllar dvsrhsggap qddqallalh rplpqqdlla rpg
//
LOCUS       WP_457678599             198 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678599
VERSION     WP_457678599.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21244
     Region          17..165
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mttddtgavp rsaealirre hrddhpvvra lhlaafegde hvpaladalr caeaplapms
       61 fvatvegqva ghvllsagrl daprrivdvl vlsplgvlpq fqnqgigtrl iehalaaada
      121 qhaplvfleg spryyakrgf eradtigfrs pslripppaf qvarlaahep wmtgtlvysd
      181 tfwaldcvgl rdteastg
//
LOCUS       WP_457678615             141 aa            linear   BCT 27-JAN-2026
DEFINITION  sterol desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678615
VERSION     WP_457678615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..141
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15229
     Region          <12..102
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mpaslltava dvplaligip awmivlahsi vllfqypihp eridrlpwqv efvfntpshh
       61 cvhhgannpy ldknyggili vwdrmsgsya aetepvrygl ttlgprsgpg rthraatadg
      121 pftdrtgppr gacssashrp s
//
LOCUS       WP_457678612             354 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457678612
VERSION     WP_457678612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38156
     Region          14..319
                     /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 mvvaedigvp swdlyelsip ctvfgkpqpd ladpwydlrl cstgereqds saagaglsmr
       61 tryglddlag adtvivpsvp dacvedgrpl ppalitalrh aydagarmvs lctgafalae
      121 aglldgrrat ahwmhtaqla erypkvdvdd svlyvddgdv ltsagltagl dlclhlvrrd
      181 lgahvanqla rrmvvpahrp ggqaqfidls vpttddgslg pvldwarrhl dqpltvedla
      241 qraamsprtl hrrlqaatgt tplqwllnqr lgraqnlles tdlpiekige lsglgtannl
      301 rhhflkqigv spsnyrrafp rtmpdsephp slpesrpgpe rgdggptaah pmpr
//
LOCUS       WP_457678617             401 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457678617
VERSION     WP_457678617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42384
     Region          6..382
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtrpgkvviv ggssaglata ealrrqgyeg rltlldaerh lpydrpplsk qvltgaweps
       61 rtqlrsqehl asleaefira eptvmcdave ravttatgrv vrgdalviat glrprilpdq
      121 eelagvhvmr tlddalalrc dlaagrrlvv vgegvlgaei aasaramgve vtlagfgsvl
      181 lgsqvggrvg gfltrlhter gadlrlgvav ealagsggrv cgvrlasgev lradtvvvai
      241 garpatewle gsglalgdgv ecdaychaap gvyavgdaas whhegldrrl rlenrtnate
      301 qaqavaanll gaerpytptp yfwtdqydak lqvhglptpa aethiaegdp aqghfvavyr
      361 engevtgvlg wnmpkqsrll rqkhlvaprn gelpttvrsa p
//
LOCUS       WP_457678635            1843 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Streptomyces nigrescens].
ACCESSION   WP_457678635
VERSION     WP_457678635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1843)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1843)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1843)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1843)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1843
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1843
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=193962
     Region          3..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          31..1378
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1211..1656
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1409..1410,1412,1433..1436,1461..1464,1488..1490,
                     1511..1512,1534..1535,1549,1576..1577)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1512,1536,1549,1553)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1672..1755
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 meneaklrdy lkratadlrr trqrlrevee kqhepiaiig macrypggvs speelwqlva
       61 dgrdavttfp ddrgwdlesl hdpdsgrpyt syvreggflh dalefdpemf gispheasam
      121 dpqqrlllea sweafehagi dpmalrgspt gvfaglmyhe yasrlnnvap eaagflgtgs
      181 igsvlsgris ysfglegpav tvdtacsssl vtlhlavqal rtgecslala ggvtvmstpd
      241 tfidfsrqqn larngrckaf asgadgttla egagmllver lsdaernghp vlavvrgsav
      301 nqdgasnglt apngpsqqrv veqalanarl sadqvdavea hgtgtalgdp ieaqallaty
      361 gqgrqedrpl wlgsvksnlg htqaaagvag vmkmvlamrh gvlpktlhvd epsshvnwsa
      421 gavelltear dwpesdqprr agvssfgisg tnahvvleqa ppvpapeale taddepveaa
      481 aragvvpwvl sarseqalaa qaerlasfva enpeldatdl gfsllstrag leyrsvvlga
      541 dreeslsgvr glaggldpag vvrgstgtga gsrvalvfpg qgsqwlgmad elqanspvfa
      601 grmadcaeal sefvswklde vlsdedmlar vdvvqpvlwa vmvslaavwe dcgvvlaavv
      661 ghsqgeiaaa cvagilslrd garvvalrsq aigrvlagrg gmvsvagsre avkdriakwg
      721 erisiaaing ptstvvsgep ealqellaec aeqevrarqi pvdyashgaq veelreelat
      781 vlaevrpgqg ripfysavna alisgeelda gywfenlrnt vrfeeaiqal ladghgvfve
      841 csahpvltpg iedtaqeags pvvvtgslrr deggwsrfaq slaqlwahgv pvdwstllpt
      901 grriglptya fqrqrywled tgtvgdvtaa glssaehpll gaavsmpgtq vltgrlslat
      961 hpwlaermvl nttvvpetaw vdlalragdq vgcdlvrelt vhtplvlpdr gavllrvlva
     1021 epgaddarel tfysrsedap deqawtrhat gvltrgaepa afdartwppa eaerveledf
     1081 yreradlglg ygpvfqglra vwrrggelfa evalpegdtg dtggfglhpa lldaalqfag
     1141 pagahlplaw agvslhavga talrvaltpa gdgysvrlad tegdpvasia avawdevpae
     1201 rlaeaagrre slygvdwvaa starvdpegs alvvlgdddg lgvgaalgad vmdldavkal
     1261 dptpevvvlp vpdsgvvgvs ggvrevaygv letlrawlae erfagsrlvv ltrsavsvtg
     1321 eevdlvtapv wglvrsaqse npdhfllvds delqasrsvl saavalgepq vairngelsv
     1381 prlttlepse kdggpvwkpe gtvlitggtg tlgtlvarhl vtehgvrnll ltsrrgpdae
     1441 gaaglrdelt algarvtlag cdtadrdala gllagipaea pltgvvhtag vlddgvlgsl
     1501 tpdridavlr pkvdaawnlh eltkdldlsa fvlfssaagv fgapgqgnya tanafldala
     1561 ayrrahtlpa eslawglwee ssgltgtlse adrqrkardg lrpmssaeal alfdasvagg
     1621 raltvpvrld ltalgaglrt devppllrnl vrgtrrsaaa gqggadglpe rlrtaspaqr
     1681 arlllnlvrg hvvavlgyad adaveagraf kdlgfdslta velrnrlnrd tglklpatti
     1741 fdypnsrvla eylgthfapy gdtgtgaadd eetirrmlts iplnrlaeag lmssllelag
     1801 iteeasette dddresldtm dmeamiqlal dgsgaeddmt rgl
//
LOCUS       WP_457678643            1031 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457678643
VERSION     WP_457678643.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1031)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1031
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=110739
     Region          3..>1029
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mqpmstplsr asqkeealwl ldklvpdsgv nnipaaiqva grlrttalre aavrllrkhe
       61 vlrtvfhdeg aglrkailap edapvdievs rstadgladd ltalaarpfk fngrpmlric
      121 qveapegdvl cvvahhlvfd vasaqivmge ltrlydavla gedlsgeavv pvaavaadep
      181 rpesfrfwrd hlsgfdagsl dlwmdrqgsa ettlkgstva hdlsdeardv vrrlrrelra
      241 sepvillaay ylllaqhgag pdivigspad irgqqaagai gyyvnilalr vrtdpaqsfr
      301 alvrqardvf leavshvdvh vdlllpeipr vnsawsttlf rhmfnylpgg lsaettiggl
      361 paralmvrng ysrmnlefdi lsekdritve alygleshrr ddvalllqry dallvavgae
      421 pdrpvgelss wserdrtvia aanrtatdtp apsvlrtvae raaaapdava ladgdrktty
      481 aelwqaasdt rellcasgvt agdvvavaar rgpelaaaal gvwlagcayl pvdpdhpadr
      541 isyqladsga ravlagdtvt lpegtprlem aglravrggt aelpadpdpa scayliytsg
      601 stgrpkgtrv shgnlanlvr hffdelkpgp gqvtlwmttf afdisalelf lplasggtla
      661 vapdearvng tllrellvrh dvgivqatpt twrtvieqvg dqlagrrvlc ggealpadla
      721 erlletaaev rnvygptett iwstvgklda adgavhagtp lrnttafvld pagrelplgv
      781 hgelciagag vaigyhnrpe ltaerfgehp eygrfyrtgd larwrdngtl evlgrvdrqi
      841 klrgnrlela eieavlrehp evtgaavvtv gdlsadavlv afvvahpteg iverlwehar
      901 aklpssavph dfvltdelpt nanekvdyph ltrlatarra aaghgaaaeh hedplvdall
      961 smfrellgre dvtadanffv lgghsllaal lvqriqesfg aemrlaeffa lptplglaaf
     1021 lrsrgvepgt g
//
LOCUS       WP_457678646             252 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457678646
VERSION     WP_457678646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26372
     Region          5..251
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtgqrldgkv alitgatggi gaatarlfar egarlvvtdv rpeplaalte eleetgtevv
       61 sacldvssar qwdgvittvr erfgtldvlv nvagildwpg iedtredmwn rvidvnqkgt
      121 wlgmkaalpl lrssgnasvi ntssvlglvg sgaaaayqas kgavrllskt aaveyarqgv
      181 rvnsvhpgvi atpmiqelld eqgdqqpdiv rtpmrraghp devasamlfl agdessfvtg
      241 tevvvdgglt ah
//
LOCUS       WP_457678654             361 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457678654
VERSION     WP_457678654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36677
     Region          48..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msitkgdrpk aervrprsrs pfrsrtavwa aaglvavllg fvllslligt gsssaarawe
       61 ylrgdpsara daqlrlavle vrlprtlaav lvgvclgtag cllqaatrnp laetgllgvn
      121 sgaafavvlg ltffgatsss alllwalvgg maasavvllf aasgrtagsp lrlvlagsal
      181 gatfhgmtsy vllgtqstyd tyrywtigsl agvetsdllp llpvvavgll ialgcarpls
      241 alglgddsar slghrpgrvr llvaaavsll agcavavagp iaflgllapy aaralagarm
      301 aaqlvlsali aadvmiladi larivirpwe tpvsvllafv ggpllvwiar ssrlstagaa
      361 v
//
LOCUS       WP_457678670             514 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678670
VERSION     WP_457678670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 514)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..514
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54975
     Region          39..496
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 mnrrqvlwag galgatalla acsgsggtst kpaatggkpk rggtlrvgal grasavtrdp
       61 hgtqtnesdy livalvhdtl ttpgaktntv prlasrwqas ddlktwrfti akgakfhdgs
      121 pvtagdvaws lrrlratpng asrlpgikae niraegtgtv vlvsdypnae lpqltrlttf
      181 vlkkgtkdke agtapgsgpf kldwfrsgna rlvcnedwyg gevlldaiev kifespqama
      241 nallggqidv asnvgavaar taeqrkdvqi irrpddmamp ivmrttggpf adakvrealr
      301 lavdreamvk qvlsgygava ndilgtgdpa yatsipqrtr dlgraksllk aagfdtskty
      361 kllttedvsg ltesatlfat qvreagvkid vvkqesatfw dktwlqgdly ttywgtndsl
      421 vffasktmfs esatnetgwk naefdavyrk aigardaakr atalkelqri eheasgyllw
      481 gmadgidlaa apvrglptlp gygrvqlera wlar
//
LOCUS       WP_457678676             508 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678676
VERSION     WP_457678676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53388
     Region          17..507
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mnhmpgrype dpapsaepav tvtdltiaap dgrllldggs levrpgrita ltgpsgsgkt
       61 illravagvl ppgtrltagr ievlgrdvpa ldatalrtlr rhrlayvgqd pgsglnprmt
      121 vrrlltevaa drspqalrdl iaevqlpteg gllgrrpgal sggqqrrval aralarrpaa
      181 llldeptagl dpelrheiae llrhladrhq laialschda dlvsrladdv vdlsrgapap
      241 pplphttdrp lptgaptltv sglyaafgrr grrtpvlhdi glavpagsst givgasgsgk
      301 ttlvravvgl hrptsgsvtl dgvrlaptaq grtreqrrrl qlvpqdplgt lnpsrtvgat
      361 lgrplrlhrr atpdqaptrv lelleqvglp arfadryphe lsggqrqrvs iaralaadpd
      421 vlvcdevtsa ldavtassim dllddlrdrr glvlvlishd lrlmasrtds llvlsagrav
      481 esgptpqift spahpvtaal vagaaqpa
//
LOCUS       WP_457678688             647 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678688
VERSION     WP_457678688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 647)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 647)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 647)
  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 647)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..647
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69576
     Region          22..620
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mdmevtawha lhssmtaqqg rrrfsrgtlr ritafarphr rhlvwflvls tvtamlavat
       61 pllagrvvda ivggdspsiv vglsvliavi avaeaglgll trwlsasige glildlrttv
      121 ydhvqrmpia fftrtrtgal vsrlnndvig aqrafsdtls gvvsnivtll ltlgvmltls
      181 wqitlialvl lpvfvlparr vgrrladlrr egadhnaemg tqmterfsap gatlvklmgr
      241 paresaefat rarrvrdigv rsamvqtyfv taltlvsala lavvyglggf lalrgqleag
      301 aivslalllt rlyapltals gahievmsal vsfervfevl dlkplitekp dartvpegpv
      361 svefdsvrfg ypsadkvsla sleevatldt rggeevlhgi sfraepgqmv alvgssgagk
      421 stvaqllprl ydtdagavrl sgvdvrdlta aslrdvlgmv tqdghlfhds irenlllakp
      481 eateaelwda lrrsrleeli aglpdgldtv vgergyrlsg gerqrltiar lllahprvvi
      541 ldeatahldn tseaavqeal tealdgrtal viahrlstvr aadqilvveg grivergthe
      601 tllaaegrya elyrtqftds edrpaaavet grpdsgpdll pesalvn
//
LOCUS       WP_457678699             287 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457678699
VERSION     WP_457678699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31317
     Region          1..264
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtavpvaliq vtdvrritpr mvrvtfagdg lddfptwpdq qlkllfprpg hraprlpdta
       61 adgdgmrwyq aflalpeder pwmrsytvrs ydpvrhriti dfvlhgttat agpatrwaas
      121 aavgdllary gpaaqyakpl pldradwlll agdatalpai gslvealpag tralacveva
      181 gaaeeqhftt radltvqwvh adgrqdalpa avraltfppg avfawlagea gavralrryl
      241 veergigkrq idfsgywrrt ltqddaptee dlaeaherla aarppqd
//
LOCUS       WP_457678702             367 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces nigrescens].
ACCESSION   WP_457678702
VERSION     WP_457678702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37187
     Region          35..306
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkrsgwmawl rllaglgilv alvwhlgsqa flaglrridt atllaalgig vlttvcsawr
       61 wclvarglgl rlplgravad yyralflnaa lpggvlgdvh ravhhgrssg dlgrgvrava
      121 lertagqvvl lvtgavvllv rpspvlapvv rflaspaval svaaagllvl avavrlrrrr
      181 gasrgeralr tvvaearqgl largvwpgva lssaavlagy lgmfvlaarv agataptael
      241 vplvvlalla malplnvggw gpregvaawa fgaaglgaaq glttaviygv lafvaslpga
      301 avllarvspl starpatsga vprqaerppl aaatgmirqr aaevpsavag gvrsqtsqaa
      361 aargdts
//
LOCUS       WP_457678705             284 aa            linear   BCT 27-JAN-2026
DEFINITION  RibD family protein [Streptomyces nigrescens].
ACCESSION   WP_457678705
VERSION     WP_457678705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Stenmark,P., Moche,M., Gurmu,D. and Nordlund,P.
  TITLE     The crystal structure of the bifunctional deaminase/reductase RibD
            of the riboflavin biosynthetic pathway in Escherichia coli:
            implications for the reductive mechanism
  JOURNAL   J Mol Biol 373 (1), 48-64 (2007)
   PUBMED   17765262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="RibD family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29535
     Region          61..267
                     /region_name="RibD"
                     /note="Pyrimidine reductase, riboflavin biosynthesis
                     [Coenzyme transport and metabolism]; COG1985"
                     /db_xref="CDD:441588"
ORIGIN      
        1 mtelldaaaa wdrlrrirtt dealaagmva dgdgglrwqq patpealela grylplclag
       61 prvavaqlgq sldgfiatrt gdadyvtgee drchlhrlra lsdavvvgag tavaddprlt
      121 vracagdnpv rvvldprgrv prgsgvftdg aaptlwvvgp evtptapgtg tevlvlpdaa
      181 afaperllta larrglgrvl iegggvtvsr flqeralhrl yvtvapvllg dgipglrfpg
      241 tpvmrealrp plrrtllged tlfelelrpg ggpsggtgsg grag
//
LOCUS       WP_457678711             346 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678711
VERSION     WP_457678711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36996
     Region          9..343
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mspdrpgpal adrladavtl idapdivlav trrgrrtvmt ggsamapptp rhalryelgs
       61 lsktftvlll aelartgvls lddplaahlp dlplphpasr rialrhlath tsglpripad
      121 liagalvhpy angyarydte rllhtfartr prnepgtrwr ysnfglallg pamsraagag
      181 ypalltdrvl splkltdttl gpgttgtdai ghrtngvtpv rsadmgafia agsvratpgd
      241 lltyleahls pgetplagpl rdvqvpqlrr gwrkrdthtl twyqhpaarg pllfhvgatf
      301 gqqaflgyhp ashtglvala trrgrtchvi ntayellytl aadpsp
//
LOCUS       WP_457678724             175 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678724
VERSION     WP_457678724.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 175)
  AUTHORS   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 175)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 175)
  AUTHORS   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..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /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=19197
     Region          85..170
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(104,123..124,141,144,152..153,163,168)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mnssttplal rpdadfgrpp tagpgegppl avdrlpdgtw qltlhalepi svhrlpsdev
       61 hiilappree pageatagrs rpepiridta artvfirgrq ldltrlefdl lahlvlhprr
      121 aftreqlmaa vwpscqssnr tvdvhiarlr rrlgpglrds istvfgigyk yqpta
//
LOCUS       WP_457678713             489 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457678713
VERSION     WP_457678713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50373
     Region          14..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstpkvtsaa psprtakalg rnaigtgdlv ffvvaaaapl tvmagaapva igmagqaapl
       61 gyllsgllmi vfaagftams rhvrnagafy ayigrglgra tgvgaayvav lsynaieval
      121 lavfgwfses gfqdltgvrv pwwvwamagl iaigvlgclk vtlsakvlav alalevlill
      181 vfeaavyahg ggpdgpgfga lspahlgtag aggmfvlsvg afigfeatav yaeearrper
      241 svpratylav gflalfytft vwtvlnayga dragtvanga agtdmvfaat arfagawaad
      301 amrllivtsa faatlafhng atryfyalgr erllprrlgt vtarhrspaa avvlqsaial
      361 vvvlatlvsg qdpyavtflw sngtgivgim llqtlaalav ygffrrdrrg lpawrvvaap
      421 ltacaglavl ivlvcrnfgl lteastgvnl allaslplvf vlgvgvalri rrrapraysg
      481 lttvdvesg
//
LOCUS       WP_457678775             427 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457678775
VERSION     WP_457678775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..427
                     /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=44768
     Region          195..398
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mgirgriala iscmtalavv vlgfavhhia daerersara yqddrlssal qiyerdgtla
       61 lgaqlddatl pvplrdavfq nqsgtyvsgg edprvwaatg vgggdgrapt rslsvsaayp
      121 dddpaqvtld ralliagcgt vtlmagvswf vaqrlsrrlr msaaaarria agaapdadal
      181 asngrdevae lgrsvhhmat slaarveaer eftadvahel rtpvaglvaa aellpqprav
      241 elvrdraqam rrlvedllev srldagvera dvdacelpsl vrgivqraar qrgvdeadev
      301 svtvegepri vetdrrrver vlvnllanaa khgkppievv vagsrivvrd hgpgypaelc
      361 aegprrfrta apergtghgl gltiaagqae vlgarldfga aaeggaeavl elpdqavpdl
      421 avtapgp
//
LOCUS       WP_457678772             225 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457678772
VERSION     WP_457678772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..225
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25277
     Region          139..205
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msggvrysre vlqeaaeact diddvvaflg trpygqlhry lfkrfahfgi dvshirrrsp
       61 hqacpspphs elrkavaest siadtlrrlg lpdnartrsq frqwltesgi stahflgqah
      121 rrgrpgttpa kppeqilvkh rgarrtrsvq lrralrqigi percaecgta pvwhgkpmtl
      181 evdhingdws ddraenlrll cpnchatttt wcrggrpdrn grrgr
//
LOCUS       WP_457678781             383 aa            linear   BCT 27-JAN-2026
DEFINITION  YidC/Oxa1 family membrane protein insertase [Streptomyces
            nigrescens].
ACCESSION   WP_457678781
VERSION     WP_457678781.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Hennon,S.W., Soman,R., Zhu,L. and Dalbey,R.E.
  TITLE     YidC/Alb3/Oxa1 Family of Insertases
  JOURNAL   J Biol Chem 290 (24), 14866-14874 (2015)
   PUBMED   25947384
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Keil,M., Bareth,B., Woellhaf,M.W., Peleh,V., Prestele,M.,
            Rehling,P. and Herrmann,J.M.
  TITLE     Oxa1-ribosome complexes coordinate the assembly of cytochrome C
            oxidase in mitochondria
  JOURNAL   J Biol Chem 287 (41), 34484-34493 (2012)
   PUBMED   22904327
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Funes,S., Kauff,F., van der Sluis,E.O., Ott,M. and Herrmann,J.M.
  TITLE     Evolution of YidC/Oxa1/Alb3 insertases: three independent gene
            duplications followed by functional specialization in bacteria,
            mitochondria and chloroplasts
  JOURNAL   Biol Chem 392 (1-2), 13-19 (2011)
   PUBMED   21194367
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Ravaud,S., Stjepanovic,G., Wild,K. and Sinning,I.
  TITLE     The crystal structure of the periplasmic domain of the Escherichia
            coli membrane protein insertase YidC contains a substrate binding
            cleft
  JOURNAL   J Biol Chem 283 (14), 9350-9358 (2008)
   PUBMED   18234665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="YidC/Oxa1 family membrane protein insertase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0032977 - membrane insertase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38593
     Region          3..234
                     /region_name="YidC"
                     /note="Membrane protein insertase Oxa1/YidC/SpoIIIJ [Cell
                     wall/membrane/envelope biogenesis]; COG0706"
                     /db_xref="CDD:440470"
ORIGIN      
        1 msmfgflgea lahgaqaiap lfgtaamaaa ivlftlgvra alhplaraaa rgekartala
       61 pqlaelqrkh kgnperlqka tadlyaktgs splagclptl lqlpvffvmy hlfstgsggl
      121 ldhtllgapl gghwtgalad gglfgpqglv ylglfaliaa vatwnfrrar atmakapqpa
      181 agnaalpgma smakvmplls fgtlitvavv plaadlymvt tttwtacera llhrdraarg
      241 aqetgiegav aakgktasak gkvtpapkgk aapageqtsp agapaaaaad gasggraprq
      301 gpaqqragrr tpksraarqr aararansqa nsqgsaharv aapvgsrans rteadsrngs
      361 rpageagsqs gggapghivt tpq
//
LOCUS       WP_457678792             185 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457678792
VERSION     WP_457678792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  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 185)
  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 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19842
     Region          <30..183
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpedavnsae wvttsvpyla prepgqrdaw saetaargrr gsqrivqage vaapgeiael
       61 lgvepgglvv grrrvmyldg rpceltdtyy plgiargtrl agtakiagga vtllaelghv
      121 gvrahedvsa rlpsdeeata leaepsqpvl qllrltldar drpvqadrmv mparlqrlry
      181 dvrig
//
LOCUS       WP_457678802             667 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457678802
VERSION     WP_457678802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 667)
  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 667)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 667)
  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 10157530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..667
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73715
     Region          166..404
                     /region_name="CESA_CelA_like"
                     /note="CESA_CelA_like are involved in the elongation of
                     the glucan chain of cellulose; cd06421"
                     /db_xref="CDD:133043"
     Site            259..261
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133043"
ORIGIN      
        1 mtsppegarp qhsydssata rlrlprqqrq rraqrkplpr ydyehysrla gpltqpdpdk
       61 pykvryrsll adephriraa lllgaaplls fgllvwlmqp snwterdypa yeflpvldtv
      121 mlvaiglief frcmnvlsna hatfvardpi pvipesgtrv afltsfvpgk eplemvtktl
      181 eaavkirhrg llhiwlldeg ddpevkevcr rlgvhhftrk gipewnrpkg phraktkhgn
      241 ynawlaehgd dydyfasvdt dhvplpnyle rmlgffrdpd vgfvigpqvy gnydtfvtka
      301 aesqqflfha liqragnryg apmfvgtsna vrisalkqig glydsitedm atgfeihrhr
      361 npqtgkkwrs vytpdvlavg egptawtdff tqqlrwsrgt yetilkqfwk apftlpfgrl
      421 vnytmmvify pmsalnwila alscalflgm gasgveidpa vwmmlygnas alqiglyiwn
      481 rrhnvsphep egsggvagmv msalsapiya rslfdaalrr kskfvvtpkg dssspdtlfg
      541 tfrvhlffll vfggsliasf vlghshpamv iwavlamlit aapivawrlt vrdekqkrsa
      601 aaatsdatgs sapdggsppe padggdppat gadeaaapag dragdragdp aatteqtmqi
      661 alggrht
//
LOCUS       WP_457678818             507 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces nigrescens].
ACCESSION   WP_457678818
VERSION     WP_457678818.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..507
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53455
     Region          <174..506
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mttesadahr sarvpppsav prpaaavrpp rgpgretlpp prpgrgvrrr tvapllavda
       61 lataatallv lgpgtapaal glllagllll hshaglyrpg paprtlndlp tllgrsavcw
      121 caaaavlaav rpgqalppal lvgavavhta lgcggraavh rarraaarrr pratlivgtg
      181 paarqlaavl hthpeygmrp vgvvtppslp pagsdatgts gsgtppgtag pplprlgsaq
      241 ditraviqht vrdvvftlpp ygdphttall rrfiaqgsav wlagaaaare grtphadtdh
      301 lrgfacrlld tapprhgggs krlldltlaa sglvvtapvl lgcalavrla vgpgvlfrqe
      361 rigrggrrft llkfrtwqpc deheaatrws ladesrmsrv grllrrtsld elpqlwnvlr
      421 gemslvgprp erpffverfl gtcpdygarl rmpagmtgla qvhglrgdts vedrvrfdnl
      481 yidswslrqd llillrtvas vvrlegr
//
LOCUS       WP_457678816             419 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678816
VERSION     WP_457678816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 419)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11660203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44391
     Region          2..320
                     /region_name="Glycosyltransferase_GTB-type"
                     /note="glycosyltransferase family 1 and related proteins
                     with GTB topology; cl10013"
                     /db_xref="CDD:471961"
     Region          274..375
                     /region_name="RfaB"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0438"
                     /db_xref="CDD:440207"
ORIGIN      
        1 mkvlhvitdl dvggaeqqlr lllrrlpahc evltltgpgp vaegieadgt pvrhlgmtgn
       61 rdltalprla glirdggydl vhthlyracv ygrvaarlag vravvatehs lgdaviegrr
      121 ltrgvrtlyr aterlgtatv avsdtvaarl rrwgvpeqri hvvpngieah rfgfdpaara
      181 lvrtrlglpl dafvvggagr lvpgkrfdvl vravtqlpgv hlllagagpe remlrrmaeq
      241 fgsgdrihll gerdgavdta aagrgaaepd ipgllsaidv fvspspdeaf glavlealas
      301 glhvlygscp avdelpadra pgarhfglnv helgtalrdl rrqgpgrlpv ppvvrrydis
      361 rsaealmsvy eqavavtsar rrtpavvppp qgraavlpaa svslpdpsrs pdpsplpnr
//
LOCUS       WP_457678823             303 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678823
VERSION     WP_457678823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /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]"
                     /calculated_mol_wt=32488
     Region          55..299
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvrkrqegge pvpeirevaf sapagrpagv evltlaelra radacqlatp hrpgfhhlll
       61 ldrgrlvhsv dfrehlmapg dllwsrpgqv qhfgdltgae grlvlfeagf ldpataaaar
      121 iedwygppvr hpegaaargv aealrqlhte fgalgglple ihldvlrhll avlvlraahp
      181 ggaaggerdg acaasatylr frdavergft rsrrvadyar slgyaprtls rateaaagvg
      241 akefidrrvv leakrllahg dqsaariadr lgfadatnfs kffqrqtgtt piafrmavrg
      301 gag
//
LOCUS       WP_457678829             394 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678829
VERSION     WP_457678829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43256
     Region          10..>67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpslhddhtg ariahtrkvr rltqreladl ahvsystltk veqgvlpasp svlgalarsl
       61 svpvteltgq pyleelrqdq ldglinpire alniydlgpd pevlprtvee laahadrlca
      121 mvratnikqv aaelpglihe atttahlhpt drnwrllast yrtaydvaak lgfsdlgmva
      181 ldrmgwsaer asdavlsgvr qymrgvaylr agdyrtgkrl vwlgltdldq aapgrvldav
      241 tgqlhlgaav lagrdkdrdt aeghlgeaqr iaertgpaek vhwlsfgptn vgvhrvsvla
      301 eldlypeavq caqeiaipdg wppsrlahhh aevaralmwt grtdaafksl lnarkvapqq
      361 tryhptvret yagldsarrr mpetfgnygs wlrm
//
LOCUS       WP_457678844             225 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678844
VERSION     WP_457678844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23892
     Region          23..185
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msvptvrrgg agdgtapgta pgprrsstrr rifdaavili aeqgfsattv deiadragva
       61 kgtvyynfas knvlyeellr dgidlladsl rraadataer ggtrvdalda miragldfia
      121 cspaliqlyv aelwrtnrtw ratltsvrgr aqavvedvlr davrngelsd eldipltasa
      181 llgmvlvaal dwqsfqpdrs vedvhaalsr llqgrvgagg dpsea
//
LOCUS       WP_457678853             383 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457678853
VERSION     WP_457678853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42405
     Region          4..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mthttvriam ngvtgrmghr qhlvrsvlal rdqgglvlad gtrirpepvl vgrsahklra
       61 laerhgvehw scdldavlgd gtigiyfdaq itaareeavr kaiaagkhly vekptagsld
      121 galelarlaq eagvkngvvq dklflpglrk lrrlvesgff grilsvrgef gywvfegdlq
      181 qaqrpswnyr aedgggiaad mfphweyvlh elfgpvrsvq ahlathiprr wdesgtpyda
      241 taddaaygif elaggivaqi nsswavrvhr delvefqvdg tegsavaglr hcriqhragt
      301 prpvwnpdvp asepfraqwq evpdnaafdn gfkaqwelfl rhvvrdepwr wdlaagargv
      361 qlaelarrss aegrrldvpe pir
//
LOCUS       WP_457678850            1308 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678850
VERSION     WP_457678850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1308)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 1308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 1308)
  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 1308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1308
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=140089
     Region          19..601
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
     Region          735..1303
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mggrhrvagt dteragwarr ltrdcwqyrk dvllalgssl agmavlalvp lvpkliidev
       61 ivrheralgp waallvaaav vvyvltyirr fyggrlaldv qhdlrtrmfg aiarldsrrq
      121 delstgqvvg ratsdlqliq sllfmlpmmi gnvllfvisl vvmavlspll tvvalaaapa
      181 lwfiaqrsra rlfpatwyaq gqaaavagvv dgavsgvrvv kgfgqeeqet gklrevsrrl
      241 fagrlrtvrl narytpalqa vpalgqvaml alggwmatqg qvtlgtfvaf stylaqlvgp
      301 vrmlammltv gqqaragver vyelidteps iaerpdahel padapatvef drvtfgyapl
      361 hegageaade dagpareapp avrpvledfs lrieagetva vvgtsgsgks tvslllprfy
      421 dvsagrvlvg ghdvreltle slraaiglvp essflfsdsv rdniayghpd atdaqvraaa
      481 raaqadgfis elpegydtkv geqgltlsgg qrqrvalara iltdprllvl ddatsavdar
      541 veheihealr gvmagrttll iahrastlal adrvavldgg rlvdlgtqee leercplyrr
      601 lltdpeelgg verdpagala gafdgefaag gllerdpaad tdgpdgvrdd aaartgadgt
      661 itpelwvrre qeaeaggagm aaraavaagp gmgaamaglp atpellaqva alppatdnpd
      721 vdedqavrpe rsyglrrllh gfggplafal alvavdalag lllpvlirqg idegvrrgal
      781 igvwtaaaia lvvvlaqwaa qiggnrmtgr igervlyslr lkifaqlqrl gldyyerelt
      841 gkimtrmttd vdalstflqt glvtalvsml tffgilvall aidlqlalvv fatlpplivg
      901 tyffrkqsvk ayelareris vvngdlqesv sglrivqafr rerqgaerfa arsddyrrar
      961 vrgqflisvy fpfvqllssv aaalvlivga grvgsetlta galvayllyi dlffapvqql
     1021 sqvfdgyqqa svslgriqel lreptttpav erprevpalr gditfddvhf hygededpal
     1081 agialtipag qtvafvgetg agkstlvklv aryydpssga vrvdgadlre ldltgyrrrl
     1141 gvvpqesylf tgtvrdaiay grpdatdaev eaaaravgah amiatldggy lhevaergrn
     1201 lsagqrqlla laraelvdpd vllldeatas ldlateavvn qatdrlvgrr ttlvvahrlt
     1261 taaradrvvv ldrgrivedg shaqllardg ryaelwrtft geeeelaa
//
LOCUS       WP_457678856             216 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457678856
VERSION     WP_457678856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22457
     Region          23..186
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdvlafygll vlttlpplvp nsallvsagv lasrgelflp lilltvagsa ltgdllmyla
       61 arrfggpvra wmrrkprrra llewtsgriq ryglpfviav rflpsgriag alasgvlryp
      121 lrkyvlgagi aeatwatysv glgylgsatt grplhaaaig fgvscavati gaaiqwaarr
      181 ralrepsedg gegesggprk gdgedpggra ssvaat
//
LOCUS       WP_457678863             473 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar porter family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678863
VERSION     WP_457678863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49597
     Region          40..449
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(40,158,161,165,275..276,280..281,284..285,373,
                     377..378,382,405..406,409)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 maaptgqmas agpregardr narrfivgia aiaalggalf gydtgvisga lpfmeghfgl
       61 tsldegiits alligaafgs liggrmsdal grrnsllwag avfiggalav alapdvpfmt
      121 varfvlglav gsasvitply lsevapphir grlvsfnslm ivsgqllayl inaflaqwaa
      181 wrwmlglaal pavalfvglf flpdtprwyi skgrqdeaar vlrrtlpade vpaelaridh
      241 arsleadarq ggwqqlrtpw irrlllvgig laavqqitgv navvyfapki lastglgtga
      301 sitatiaigv isvlatalgm slidrvgrrp mlltglagmt vslallgasf hlphspgvst
      361 lvlglmvlym afmqgtlntg vwlllaemfp lkvrglamga avfvmwlvnf gvalvfplll
      421 davgagttfw ffgamcvlsl vfckryapet kglaledled elrkatgaap aaa
//
LOCUS       WP_457678883             254 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457678883
VERSION     WP_457678883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27200
     Region          1..254
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mwvraalayr tsfvmmtigs faangldfva immmfsqiea lggftlpeva flygtsgial
       61 gladlllgsi eglgrrirdg tldtlllrpv pvfaqiaadr falrrvgrvt qallvlgwal
      121 prievdwtvg rvlmvplmav cgtaifaavf tagaafqfwa qdaaqvqnsf tyggnallqy
      181 pptvfakelv rgvtylvpla fvnwlpalrl lghpdplglp gwvdflgpmv aalmctgagl
      241 awrvglrgyr stgs
//
LOCUS       WP_457678894             484 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678894
VERSION     WP_457678894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51428
     Region          27..372
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mseylkqeaa kagsplrgag vdvpafdsar wqarldella ahhvpgaala vvsdgavhel
       61 asgvlhtgtr vavtpdsvfq igsiskgyta tlvvllahag kldldapvtd llpdfavada
      121 eatktvtprq llnhtsgieg dfvsdtgrgd dclaryvegv rdvgltnppg atmsysstay
      181 nilgrivevv tgrtwdealk emlcvplgla htmtlpeevl rfraamghmg epgedpvptp
      241 lwnmlprsag pyggicatag dvarfarlfv dggrtpdgsq vlaaeaveam lrrevempdq
      301 wylgahwglg wglfewdgvr gfghdgstfg qlaylralpe agiavalltn ggaaapkvfe
      361 tlcreltael agvgmpefgp ateepamdpa lfvgsyrreg flmtvtdrpa gegvlrmkye
      421 gadglkdtfe plfwnlvpvs dtpsktvfag rrndkdgwip vvfyaladgs ryvhfgvrat
      481 akss
//
LOCUS       WP_457678886             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457678886
VERSION     WP_457678886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=37139
     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..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 mgstgatgnp gvnlpalrgh naalvlgllr aageqgvsrl elaahtgltp qavskitarl
       61 rteglaaeag rrastggkpa tvlrlvpgar havglhldrd eliavladlt gapvaerrap
      121 lafeagagrv ldtagrevaa lraeaggppv lgagvacpgp ldhtagvlhr vtgapqwdgf
      181 plrdalterl glpvvldkdt naaalglaqg mpsgagsfgy lhlgtglgag lvlggslyrg
      241 prtgagefgh qtvqwdgprc scgrrgciea lclaavargd ltgaaqvlgt gaanlvelld
      301 idrvllggrt vlenpdgfrt gvaaaldaqa rargrvavpv alarggarvv adgaaelvla
      361 plfgtrqpal va
//
LOCUS       WP_457678899             440 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678899
VERSION     WP_457678899.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45592
     Region          1..383
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdftptpeqt aarelaaeif gdlstperla aggsgtdagl wkalcaaglp gaaeetgllg
       61 lvlmleeqgr ttaqvpfaat cvygllavga hgsaaqrarl lpalrageav atgafparrg
      121 gvraeeaadg tgrltgvvpv vpwlraathv lvpdgdtrtl wlvrpddaga rrdpvettap
      181 wsagrltldg apaerlghda eapahdaeap ahdaqplard aqalandaqa paqhaqapar
      241 ttqtpapahp dpytdiltla rtafaglqag vcagslarav shtttreqfg rplstnqgvl
      301 lraadahmdi eairltayea awrrdaglda gphaltaaww aseagtrvvh tgqhlhggig
      361 advdhpvhrh flwgrqlagy lgsgaealee lgelltgers tpaarpdepp rarrpgpadp
      421 dhppgpaapd qptrtrteap
//
LOCUS       WP_457678902             433 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional MaoC family dehydratase N-terminal/OB-fold nucleic
            acid binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457678902
VERSION     WP_457678902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Krishna,S.S., Aravind,L., Bakolitsa,C., Caruthers,J., Carlton,D.,
            Miller,M.D., Abdubek,P., Astakhova,T., Axelrod,H.L., Chiu,H.J.,
            Clayton,T., Deller,M.C., Duan,L., Feuerhelm,J., Grant,J.C.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kumar,A., Marciano,D., McMullan,D., Morse,A.T., Nigoghossian,E.,
            Okach,L., Reyes,R., Rife,C.L., van den Bedem,H., Weekes,D., Xu,Q.,
            Hodgson,K.O., Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A.,
            Lesley,S.A. and Wilson,I.A.
  TITLE     The structure of SSO2064, the first representative of Pfam family
            PF01796, reveals a novel two-domain zinc-ribbon OB-fold
            architecture with a potential acyl-CoA-binding role
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1160-1166 (2010)
   PUBMED   20944206
REFERENCE   2  (residues 1 to 433)
  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
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11629928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="bifunctional MaoC family dehydratase
                     N-terminal/OB-fold nucleic acid binding domain-containing
                     protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45655
     Region          58..185
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Site            order(91..92,137..140)
                     /site_type="active"
                     /note="active site 2 [active]"
                     /db_xref="CDD:239524"
     Site            order(97,100..101,104,124..126)
                     /site_type="active"
                     /note="active site 1 [active]"
                     /db_xref="CDD:239524"
     Region          278..426
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 msgvvgasga vgasgvsgar gaspegataa grpgdgpppd ltherlkaye grptaaagvg
       61 kdmvnepmir hwceavgdth payrgpdaia pptmlqawtm gglsghadrs gaydelsrll
      121 dsagytsiva tdceqeylrp lrpgdritfd sviesvserk ttklgtghfi ttrmdiradg
      181 epagthrfrv lkyapaarlp ktaerpqate psraverpqa teptraaeqr taaeqrmsaa
      241 aeqstaaers avpeqrktpe rrtprrprpv inrdnagfwe gvrghrlliq rctgcrtlrf
      301 pwlpgcnacg spdwdtveas gagtvfsyvv mhhppfpaft vpdqpadgag pdaaavpgaa
      361 gsdaagpdaa dpgaaspyav glielaegvr mvsnivgipy dkvrigmpvr leflcadeel
      421 elpvfrvaeg geg
//
LOCUS       WP_457678911             447 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678911
VERSION     WP_457678911.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..447
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=46684
     Region          238..444
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(245,284,322,426,429)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(245,426,429)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(245,284,322)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mgffqfvpar rvvplvgmam vmalvgagga agggggaatd adavadahaa gpraarwtea
       61 wgaavqqpve gdvddvpnws gkgfrqqsvr qvvrvsagga rvrirlsnrf gkaplrvdga
      121 viarsgggaq awpgttrkvt frhsgrhsas tvipaggeai gdavrlstsp lenlvvtlyf
      181 agatgpatfh rvglttsyra agnhlndvla kayrqssess yflsgvdvsg pfrerrntvv
      241 algdsatdgv gstpeahggf tdglaerlva arrnvgvvna giagnmllts sscfgekgvt
      301 rfrrdvldrp gvrtvivelg andvganwat gpcfppshkp vsarritegy raliraahgr
      361 gikvigatmv plkgypgysa kverlraqvn hwirtsgayd avvdfdkala dpahpdrprp
      421 gyvyedglhp ndagyqaian afdlgel
//
LOCUS       WP_457678920             539 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457678920
VERSION     WP_457678920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=56505
     Region          80..476
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 magiepalpa pthtvdprpg ktpadppsdt psgtppdapr dtapdaasdd apdfsvvdql
       61 aavqdrlagw isdlstlhdl teqlartrtl edalhellra gaslvgarrg lvvlapadgf
      121 gpettvglgl ghaeigtiet iprralsyar ildglpepga tgdgprtgpl hdprheardt
      181 grppgprgaa aagpcteise pdipgekdld prlrevaarl gyaasyavpl aadpigrtga
      241 avwlydepae pterqrhlig lyrahaaehl arllelhrsr qavrtlreel lphrlpripg
      301 vrlavrhhsg prgggdwyda lplpdgalgl aigsvtgsgp savaamgrlr aslrayavme
      361 gedpvavlsd lelllrltep arsatalfaf tepppgspgg ppappmpggi tdpfarkivl
      421 agaghcppli lgdlrteyve tslsaplgml acweapsvei epaggetlll ysdgllhrtg
      481 epmdrafarl haaaagvpqa arhdpeavvd hivrtmlpqg lddpsseedv vllaayfee
//
LOCUS       WP_457678925             262 aa            linear   BCT 27-JAN-2026
DEFINITION  YcnI family copper-binding membrane protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678925
VERSION     WP_457678925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   de Oliveira Silva,Y.R., Zheng,D., Peters,S.C. and Fisher,O.S.
  TITLE     Stabilization of a Cu-binding site by a highly conserved tryptophan
            residue
  JOURNAL   J Inorg Biochem 253, 112501 (2024)
   PUBMED   38342077
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Chillappagari,S., Miethke,M., Trip,H., Kuipers,O.P. and
            Marahiel,M.A.
  TITLE     Copper acquisition is mediated by YcnJ and regulated by YcnK and
            CsoR in Bacillus subtilis
  JOURNAL   J Bacteriol 191 (7), 2362-2370 (2009)
   PUBMED   19168619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="YcnI family copper-binding membrane protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=27465
     Region          21..203
                     /region_name="YcnI"
                     /note="Uncharacterized conserved protein YcnI, contains
                     cohesin/reeler-like domain [Function unknown]; COG4549"
                     /db_xref="CDD:443613"
ORIGIN      
        1 mskiskmtqm pqqqpdlsrt rrlarllplv gaaavgsvvl laapafahvs vqpagaapkg
       61 gyatvnfkvp nerddastvk levtlptdqp lasvmpqpvp gwkvdvkksk lakpiemhge
      121 kineapskit wtaedkgvep gqfqqfpvsv gmlpedadqv vfkalqtydd kevvrwiept
      181 kdggpepenp apvlkltape edghgataag dksggkdhlk naaaaedast sdntarvlga
      241 igivvgiigv gfgvfagrrr sa
//
LOCUS       WP_457678923             486 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces nigrescens].
ACCESSION   WP_457678923
VERSION     WP_457678923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Singh,R., Goyal,V.D., Kumar,A., Sabharwal,N.S. and Makde,R.D.
  TITLE     Crystal structures and biochemical analyses of intermediate
            cleavage peptidase: role of dynamics in enzymatic function
  JOURNAL   FEBS Lett 593 (4), 443-454 (2019)
   PUBMED   30582634
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wilk,P., Uehlein,M., Piwowarczyk,R., Dobbek,H., Mueller,U. and
            Weiss,M.S.
  TITLE     Structural basis for prolidase deficiency disease mechanisms
  JOURNAL   FEBS J 285 (18), 3422-3441 (2018)
   PUBMED   30066404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..486
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53709
     Region          68..191
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          222..467
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(285,302,314,397,428,452)
                     /site_type="active"
                     /db_xref="CDD:238520"
ORIGIN      
        1 mtdeltpetp dedeqpikqr knglypgvsd elaenmksgw adtelrdlqp veqapnaarr
       61 raalsarfpg erlvipagnl ktrsndteyq frasteyvyl tgeqtddsvl vlepkgdshe
      121 atihrlprsn rengefwlng mgelwvgrrh slseseallg vpckdvrela dalkeatgpv
      181 rvvrghdagi eaaltdkvta erdeelrvfl searavkdef eigelqkavd stvrgfedvv
      241 kvldkaeats eryiegtffl rarvegndig ygsicaagph attlhwvrnn gevrsgdlll
      301 ldagvethtl ytaditrtlp ingrysdlqr kiydavyeaq eagiaavkpg aayrdfhdaa
      361 qrvlaeklve wglvegpver vldlglqrrw tlhgtghmlg ldvhdcaaar tehyvngtle
      421 pgmvltvepg lyfqaddltv peeyrgigvr ieddilvtdd gnrnlsaglp rrsdeveawm
      481 agllgk
//
LOCUS       WP_457678935             352 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678935
VERSION     WP_457678935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37326
     Region          26..155
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          197..329
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mksdrkpeaa drangtgdpg gptgfdaldh rlihalqldg rapfsriaav lgvsdqtvar
       61 rytrhrthgt lkvlglpnaq algevqwlvr vqctpdaava vaealarrpd tswvslmsgg
      121 teisavcrav ssdhsdvlll qklprtpsvi gvtahcqlhq fyggpqglis ksgaltdeqi
      181 aalsppppdp aaapvaltda drrlfdvlar dgrtplaela aatgwspttv rrrfaelran
      241 gvlyydvdyd lrqfgygvmv alwlsvepar laaageamaa hpevayacat tgpnnlfasv
      301 lcrdvgavyt ylttrvaalp gvrsmesapr irhikgpgpl flaghaapgr rr
//
LOCUS       WP_457678938             524 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678938
VERSION     WP_457678938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..524
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51982
     Region          36..493
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,242,245..246,249,312..313,316,344,348,
                     401..402,406,410,426,429..430,433..434,437)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrstpergta aggrtpgagg epgggpagkw wplvaialgn flllvdvtiv ntalpriadg
       61 lgatltslqw vldiyalala allmvagsaa dlfgrrrlyv agltlfalas lvcglapdag
      121 vlvaaraaqg agaaamvatn apllmaayqg rdrgvafgvw ggtngaaaai gpvlggllte
      181 yvdwraiflv nlplaavavw itvrrvpesh gtlprprsds agkapltrid wpgtasftac
      241 agaltyglmr ggdqgwteag tltalggaal allvfvvver rvqrplldlg llrrpsfaal
      301 laaalllqaa afpyltfvgl wvqnilglsp vqaglavtpm alvsllvgal ggrllqrmap
      361 qlpvgiglll vgagvlleya llddgagwaa llpglaisgl gigaampvlv saalgaappq
      421 ragmasgavn tsqqlgyavg iaalgtvfag alhdvrpgas rtavaaahvs gltdillisg
      481 tvalaggvlv lavvrrgagg dgtadrpaar aaaaparaga pgga
//
LOCUS       WP_457678944             423 aa            linear   BCT 27-JAN-2026
DEFINITION  CynX/NimT family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457678944
VERSION     WP_457678944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42960
     Region          38..418
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(48..49,52..53,56,88,137..138,140..142,145,164,
                     167..168,171,249,252..253,256..258,261,288,292,341..342,
                     346,350,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 magpraeapl ieaeedlvat ppvavarrrl rahpalvmtg ivlaalnmra alagvspllg
       61 eigahfrlta tasslvttip lvfmglgsia apklarrwgt etalcaalva lcggivlria
      121 ppvvalfagc avvgssiall nvlmpglikr dfpdraagmt alystamilg atvsaasavp
      181 mehalggwqg alvswallaa vaavvwipqt lmarrgtrhg aaaatpahlt edgprlsrsp
      241 lawqvtlfmg sqsliayvai awmptiftdh gmgkgeaglv fafstlvqma gsfvvpmlag
      301 rmrqqrllav avtglmacgi tgllvapvag awlwaallgi gqggalglal tmmvlrsgda
      361 htaarlsgma qtggyllaaa gplvlgavhq atggwtvplv llltvcagla llgmgagrdr
      421 rig
//
LOCUS       WP_457678947             303 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678947
VERSION     WP_457678947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33159
     Region          4..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttlhidhvs rwfgnvvavn ditmtigpgv tgllgpngag kstlinmmgg flapsngsvt
       61 ldgttiwrna giyrhigivp ereamydflt grefvlanae lhglgraeaa ralatvemey
      121 aqdrkistys kgmrqrvkma salvhdpsvl lldepfngmd prqrmqlmel lrrmgaegrt
      181 vlfsshilee veqlaahiev vvagrhaasg dfrkirrlmt drphrylvrs dndralagal
      241 iadrstagie vdlaegalri qavdfgrfte llprvardhg irlltvspsd eslesvfsyl
      301 vaa
//
LOCUS       WP_457678953             449 aa            linear   BCT 27-JAN-2026
DEFINITION  carotenoid oxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457678953
VERSION     WP_457678953.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..449
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48998
     Region          10..443
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtptspttas ashapaphma gnfapvadel taydlpvtga ippelsgwfl rngpnprdaa
       61 tphwffgdgm vhglrleggr avsyrnrwvr tttftegarp vdaqgrrnlt agvanthivr
      121 hagrtlalve ssfpyeidcr pgheletvga hdfggrltta mtahpktcpt tgelhffgyg
      181 gptppyltyh radaagelvi srpidvpght mmhdfhltag hvifmdlpvv fdrsrpgmpy
      241 hwnpeygarl gvlrrddpyg evrwlpidpc yvfhalnahd egdqrivlhv aryadyggqa
      301 pahlwrwtid latgtvaeeq lddqfcefpr vddrlagqpa rfghatigel pgtgpipgal
      361 irydlqtgea vrhdfgpgrt pgeavfapad drpggpgwll tyvydastdt sdlvvldsed
      421 isadpvatvh lpqrvpygfh gnwlpdpar
//
LOCUS       WP_457678971             149 aa            linear   BCT 27-JAN-2026
DEFINITION  GlcG/HbpS family heme-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457678971
VERSION     WP_457678971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=15231
     Region          17..144
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mstatvtptv tptvrplttr eadalieaav raadglgvrg svtvldaggq llgfrrddta
       61 vlisgetstr kaytalqlda ptadlvdlvr pdglfhtlpt aldrpllfia ggvplhrdgr
      121 ligalgfggg apdqdhrivt aaiaeadlg
//
LOCUS       WP_457678974             292 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457678974
VERSION     WP_457678974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31004
     Region          54..205
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdpatattkp ltimlepshr igmtdpvrip arrpgvnrfs ggpavtdggv tpsradarrn
       61 ralvlqaarf afeeqglgvp lgeiarragv gagtvyrhfp skealfrati vdrielftdt
      121 ardlaevpdp gavffrflss vvrlavrnka lcdaleaaga grfepspgvg qdfddalevl
      181 lrraqeagav rqdvgiadlr allvgclsme ravpgsgseg gapgrmtalm cdalrperav
      241 teleiepvkr nesrcgvcga aiaaahtgrp arycggacrq kahrarertr qt
//
LOCUS       WP_457678976             482 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457678976
VERSION     WP_457678976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51621
     Region          29..363
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtiaqstefp rpepvghgpg avgtpdefae llpqtrrall hrlavgqaeg rapsmtgavv
       61 rdgravwtga rgavageaph gdvqyrigsl tktfvavlvl rlrdegllrl edpvgrhleg
      121 tpvpdatiaq llshssglaa eprgpwwert agalrpepad lfderpqrlp agrrhhysnv
      181 gyallgalve qlrdgvpwge vlrrevlepl gmdrttlrpe kpyasgwavh pwadallpep
      241 aedtglmgpa gqlwstlqdl crwaafllrg darvlgaasl aemrtpavpp esgawdagsg
      301 lgvqllrrdg rllvghqgsm pgflaalwad teedvagvvl tnctsgpaag alaadltgiv
      361 lahepripep wrplpgpldp ellaltgpwy wganphalrl raergleltp lsgagrssrf
      421 raeedgtwtg ldgyyagetl rvrrdrdgav shldlgtfvf trgpyepsap vpggvdpegw
      481 rv
//
LOCUS       WP_457678981             321 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457678981
VERSION     WP_457678981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33458
     Region          9..317
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(48..50,53,135,139,161..166,185..186,188,202,
                     221..222,243,246,265..267)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 msetgtpqmr avsqdtaggp evlkvittdr pvpgpteilv rvhaagvnpa dwktrtagrf
       61 hngseppftl gfdvsgvvea vglgvtlfap gdkvfgmprf phpagayaey vtaparhfah
      121 lptgldhiqg aalplaslta wqalvdtaqi qpgarvliha aaggvghlav qiaksrgayv
      181 igtarrakhd flrglgadev idyteqdfat avrdvdlvld tiagdygars lrtlrpggsl
      241 isilplddtf padrareagv raafvlvepd raglqavael vstgklqvnv dtvfpledaa
      301 kahalgetgr ttgkivltva p
//
LOCUS       WP_457678984             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457678984
VERSION     WP_457678984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20126
     Region          18..153
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
     Site            order(99..100,110..111)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 msslpamnsw parirtarll lrpaesadvk eftrlwtdpe vrrflggpve eqklalyqeh
       61 fasrphlfsv ttrdeapvig svsvdprsrf dgrrevsylf lpeywgrgya reavaalvdw
      121 aletvssdsp sviavtqean vrscrlleai gmrhidsfte fdapqamysv erqglrlgl
//
LOCUS       WP_457678987             445 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Streptomyces nigrescens].
ACCESSION   WP_457678987
VERSION     WP_457678987.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..445
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45442
     Region          15..435
                     /region_name="MATE_DinF_like"
                     /note="DinF and similar proteins, a subfamily of the
                     multidrug and toxic compound extrusion (MATE)-like
                     proteins; cd13136"
                     /db_xref="CDD:240541"
ORIGIN      
        1 mtlapatprr tgrrhdreii alalpafgsl vaeplfvmvd savighlgtp qlaglgvaaa
       61 llttavsvfv flayattaav arrvgagdlp aairqgmdgi wlalllgaav iatvlptapw
      121 lveafgasgt aapyattylr isalgipaml vvlaatgvlr glqdtktply valggfsana
      181 alniglvyga glgiagsawg tviaqcgmaa vylavvvrga rrhgaslrpd aagirasaqa
      241 gvpllvrtls lravlmiata vaarlgdaei aahqivltlw sllafaldai aiagqaiigr
      301 ylgagdrdga raacrrmiqw givsglvlgv lvalarplfi plftadpavq gpllatllvv
      361 avtqpvsgiv fildgvlmga gdgpylawam vatlalfapv alavpllggg lvalwwamtl
      421 mmtvrmltlw lrtrsgrwiv tgasr
//
LOCUS       WP_457678998             492 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457678998
VERSION     WP_457678998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..492
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=50672
     Region          8..257
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,67..70,82)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,65,81..84,88,90,127,129,
                     131..132,134,148..149,152,169..172)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,65,81..84,88,129,131..132,
                     134,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,88,90,127,129,131,152,169..172)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(148..156,165..172)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgeifagrye lidpigrggv gavwrawdar rrryvaakvl qqsdahtllr fvreqalrid
       61 hphvlapasw aadddkvlft mdlvnggsla hligdygplp prfvctlldq llagltavha
      121 egvvhrdikp anilleatgt grphlrlsdf giamrkgepr ltetnyvvgt pgyfapeqll
      181 gaepdfpadl favglvalyl itgtkpdgea msrhfsehgi pnapegvpep lwqvlaslvh
      241 pdpearfkta tgarkamlsa vellpdatie eeivevfdhi gplpadfgpd gplrprntag
      301 patagatagt gatgqvsmsd tgsfqlappe pstpatpapt ptptpmpgav pgststghgs
      361 tptghgapst ghgasltghg gafphhggtp tghgipagpp assgipttpp pppapayept
      421 aaahpersat rpytagplpv pgqppagisv tvpamaypap rrkpgpppkv avpvlivall
      481 ciavgvwalt aa
//
LOCUS       WP_457679010             381 aa            linear   BCT 27-JAN-2026
DEFINITION  J domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457679010
VERSION     WP_457679010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10154716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=40653
     Region          <247..285
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(261..263,272,277,279,282..283)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtnshaenaq dgqhrpdvpg tpdaqadpqa pdardggqsd qlghddgped qvagsegsdl
       61 grgahtdppv gqaaagpdqg vdragagsda gvgqagagse pgvgqaeaap epggvpdeqa
      121 taaqdeatrr lakavlaaeq aliefeiave tfrvevenfs rlhhqrlgpm yarldeldaq
      181 iaeavaartg dpadlrkare arasvlpmpe veelfhgwmg adglfpeaqa mlteqsvqpp
      241 qkvrpseear kvyrdlvrka hpdlarddae rarrdafiar vnmayaqgde tvlrelarew
      301 eagpapveer lseseelyar lewlaerkel laamaaelee saigamikma pedpdallde
      361 iaeklladva eretylaqlv g
//
LOCUS       WP_457679044             424 aa            linear   BCT 27-JAN-2026
DEFINITION  SagB/ThcOx family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457679044
VERSION     WP_457679044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 424)
  AUTHORS   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="SagB/ThcOx family dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46491
     Site            order(207,230,233,272..274,345..346,349,357..358,361..362,
                     365..366,368..370,372..374,386,388..390,405..409)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380318"
     Site            order(207,209,211,274..276,278,359,362..363,368,372,
                     383..386)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380318"
     Region          242..414
                     /region_name="antibiot_sagB"
                     /note="SagB-type dehydrogenase domain; TIGR03605"
                     /db_xref="CDD:188352"
ORIGIN      
        1 mgrltaeqrs llqvlstdrs veeltrrcpr dqaerllaml ssggwlittv vcgdrplfss
       61 rplvphwkpl ppveprrlsr fasvrrdgde ivvespaaga qvrlydrrlv epvltpgaeq
      121 ersdlpleav rllageladr gflataaedh slsslqwsph elafhhgsrl radhrmgqdf
      181 ggsywakgrf dappgkhprw peaaielprp dlaglrakdp alaevmeerr slrsydedtp
      241 ltveelgefl frtarvratg rdtegldvss rpypgggaay elevyplvrn vrgldaglyh
      301 yaphghrlhp vpasatvlrr lmkasaagmt gdatpqvllv iatrfgrlaw kyqamgyalt
      361 lkhvgvlyqs mylaatamrl apcalgvgds dafaeatgld yfeetsvgef algslpaarr
      421 estg
//
LOCUS       WP_457679056             471 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457679056
VERSION     WP_457679056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50065
     Region          29..457
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnhpdrlgas hgslarsapl tsmvspvasf adlelpaavl rtltehgvre pfpiqaatlp
       61 halagrdvlg rgrtgsgktl afglpllvrt agrraepkqp laliltptre laqqvteala
      121 pyaealrlrm atvvggmsig rqaaalrdga evvvatpgrl hdlierracr lgrvritvld
      181 eadqmcdmgf lpqvtevldq vhpdgqrmlf satldrdvdh lvrrylhdpv vhsvdpsaga
      241 vttmdhhvlv vhgpdryavt teiaardgrv llfldtkhav dqltrhlras gvhaaalhsg
      301 ksqpqrtrtl aqfkngqitv lvatnvaarg lhiddldlvv nvdpptdpkd ylhragrtar
      361 agesgsvvtl vlsgqrrems rlmagagiea titkvrsgea elsritgaka psgtpldggp
      421 aaprakntna pfrglgtskd asrgsggksr kagearklae arkaarvrrg n
//
LOCUS       WP_457679061             618 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679061
VERSION     WP_457679061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..618
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=66338
     Region          6..421
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mirtgagala elpagarvvi rlpngsalad vllacfdrrl vavplhprat dravagiaer
       61 vsaaalvdvh glhrtalpdv htvpddlafi mftsgstgpq kgvmlsrrav lgnaaktaal
      121 hglsperphg tclplyhcna lvmsllgthl tgtpltqqaa fdpagyfaal gaagartasi
      181 vpalladlle vgpdwpdgle ylitaaaplt sdlarrfhrr ygprlrqgyg lteavnfsft
      241 mprlddaefr dqylehvppv gaplpdtelr lesgevwirt pdlmtgywqd srttaatvtd
      301 dgwlrtgdlg elrdgllvlr gragecinrg gekhypldie hgwrqaglsg rfaavavdep
      361 slgqdiglia teqpvsavrd lyeraqlrpa alqfgglltt stgkpqrkam srglaarrla
      421 paryerllry aaatahdllh sgadhpglra latqagdrph pdeetifgaf dflrehwhhe
      481 dnaelsraka hwrttlrtew plavhaelaa evaarhgfeg ppvpfgteal fgdgalqvlp
      541 hgpaadgpvw plgpllsfld gplggcerdr wtrlarlrdr gflttgcsvl ragrhdlggv
      601 lwarqpdsgp nehagatg
//
LOCUS       WP_457679070             609 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679070
VERSION     WP_457679070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 609)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 609)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 609)
  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 609)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..609
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65034
     Region          16..581
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtdrqsvprn aavprlrilw sfarphkgal iralllalva salglatpmv tkwvldalgd
       61 asplkgplaa llvllvvgva vrfwqwtllg avgervvlea resmvrrflr atvpaitrrp
      121 tgelvtrvts dtvllreaat dalvglingt vmllgtlvlm gvldvvllgt tlasvalvgv
      181 lfavlmpgia taqqraqehl grlggalegt lrairtvkvs raeertaeri aadarasaey
      241 giravrreal awtvswsgie laiivilgvg awrvgegqme vssliaflly afglmdpite
      301 lssnvtalqa gmaaaerire tddlqtesta ahpaprtgpd hrhdvpvlal rqvtaaygpd
      361 aepavrgidl avprrghtai vgpsgagktt lfslvlrfle ptqgellldg rpyrdlthde
      421 irarlayveq dtpivpgtir dnlllsrpda tdeelrrvlr dvrlaekina lddgldttls
      481 tttvsggerq rialarallr tpdvllldea taqldgitea avhdcirsra aagavvtiah
      541 rlstvidaht ivvmeagrir vqgsheelle tdllyrelve aldisaspap apeaeavsvt
      601 sggsrprat
//
LOCUS       WP_457679072             616 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 35 protein [Streptomyces nigrescens].
ACCESSION   WP_457679072
VERSION     WP_457679072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..616
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68513
     Region          46..360
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtqfsrrrfl saaivtgasv gvalgsgrta faqadnprgl tirgdeflld gepfrilaga
       61 fhyfrthpkd wrdrllrmra mglntvetyv awnfhqpyee kadftgwrdv aafvrtadea
      121 glkvivrpgp yicaewdfgg lpawllkdkd aplrrsdpay eravddwfae llprlvdlqa
      181 trggpiiamq veneygsydd dhahlehlrd tmraqgvdsl lfcsngatqe alragslpdl
      241 lstvnfagdp tgpfaelrkf qpdkplfcte fwdgwfdhwg erhhttdpaq taadvaklle
      301 agasinfyma vggtnfgwsa ganltgsayq ptvtsydyds pisesgelte kfhkvrevla
      361 kyttlpdtpl patprrmppq rvavresvpl mdtldalstp vrhtapvhme algqpyglih
      421 yrtrvrapqg tkalritglg dralvfgdgk rigtfdrnqp dhtvdftvad tsstldllvd
      481 ptgrinfghn fndtkgisgk vllddqelsd weirrlpldn lsalkfasgn tptgpafhrt
      541 rihvdtpadg flafpgwdkg mvwlngfalg rywslgpqvt lyapshlwrr grnelvvlem
      601 ertgdrievr sepdig
//
LOCUS       WP_457679101             412 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679101
VERSION     WP_457679101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45482
     Region          45..399
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrihrvvtta valalsltig vgvaasatap sdsrpsaahd avrfelpept grkpvgntel
       61 hlvdherpdp wadgrdrelm vsvwfparst reyprqpylq pgtarfvdes dpfrltrpge
      121 vdwaairtda aatapadhhg rrpvvlyspg lqsfralgts tavelasrgy vvvtidhtye
      181 apavefpggr velqkpmrgv eglkkaidtr vrdtrfvldq levlreggnp daegrrlpng
      241 lgraldldri gmfghsggga taaetmradr ridaginmdg tlqysktefl pvareglnrp
      301 fmlmgkadqt hlnkpswqsf wdrstgwkrd lslergshfs ytdaqsfvpa ldeyldipaq
      361 treqyigtvd pgrstaaqra yvtaffdqhl lgrprrlldg sspshpevrf vr
//
LOCUS       WP_457679104             561 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679104
VERSION     WP_457679104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 561)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 561)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 561)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..561
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59063
     Region          71..545
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mkrtsrptap lltaavatla lgtagcsgat ntlgggkaln aadlrltptt aeatgrldtv
       61 nwlledepds ldldtqgtsa gravltnvce rlyqlqpdms vrpflarkat rpdpttlvls
      121 lrddvtfhdg akmtaddvlw slkrhadpdm eqadefgnvk kmaktgphei titfkepdal
      181 ftkalagdag lvyhrsqvqa agaefgtpgp gdacsgpyel tswksgdslt irrsesywgs
      241 epltrqivfr wasdsafvna lttgaadggy aespntaaal agrkgltehy gpstaslali
      301 ptergglkdp airralslal dragiaasgy gglvqpwatp vgsgswgyak pafataqrkl
      361 naaaparpda aalarakklv qsagapaepi vigtdasqgr tvianavraa lqsiglvgqi
      421 ktvptaqfee fyssqqarse idvlvgdwyi sksdpmgfyd nalsdspnnw vgfksrtyds
      481 tvhqalrtld dgararlavr vqkefadaav wvpvaqvpsv lvlkdgltgp pasqahlyyp
      541 waaelgtapg aapahqpqek d
//
LOCUS       WP_457679111             257 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679111
VERSION     WP_457679111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27275
     Region          12..231
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mppspppsll gvfahpddes lsaggvlaqh aaagartavv tttwapdspr aielthalri
       61 lgasaprmlg yadarnpesa pgrprfcdap lddviaelvg qlrefrpdiv vthdalgqlt
      121 ghpdhrhthr vavlaveaag lahlypvtgd pwqtsalyaa thpcsgvgal aplltgvgkt
      181 llsvpdeyvt aivdvtpwle rkwrailahe gevarerslp gllsrlpedi rhqiisteyf
      241 trlppgpapg dprqlts
//
LOCUS       WP_457679135             228 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679135
VERSION     WP_457679135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24325
     Region          28..170
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mshptpgrpl sqtdrtrhqr lreqgsldrn dldailkagf vchlgvtvds nllviptvyg
       61 tdgatlyfhg svasrslvas pdasvcvtvt hvdglvlars vfehgvnyrs amifgiprlv
      121 tdpeekwtgl rclteqaapg qwdyarqpsr kelaatslla lsldeasvki rtgapddgdt
      181 pdaglglwag vlplqahwgd lepdpalpah iktpphlanr qgvsafgs
//
LOCUS       WP_457679158             449 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679158
VERSION     WP_457679158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..449
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47026
     Region          122..414
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrvdrrwaar lalaagtaal lvllvfaglr sivlvgvgla glaataaglw wvlartgvir
       61 vlafllatat pvvvlvlyav agllwvvlvs lalwtlavft grtalvpqkt epapqperpv
      121 apprrpflim nprsgggkvg rfqladqara lgaevveldp aqpqdvaela rravddgadl
      181 lgvaggdgtq alvaavaaar dvpfvvicag trnhfamdlg ldredpsacl ealtdgvelr
      241 idlgfidvgq paaegrgrvf vnnasfgaya tvvqspayrd dkarttlqml pdllthhsgp
      301 rlqvrtgdvt vdapqavlvs nnpyrmgdpa glgyrerlds gvlgvlgvtv dnavqaasml
      361 rgshgpglts ltvqevvvda dapvipvgvd gealtvptpv rcwiepgalr vrlpsnrpgt
      421 prakppmnwr rvrrlaltvg rtaagrdtg
//
LOCUS       WP_457679171             241 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679171
VERSION     WP_457679171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 10004355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25736
     Region          17..89
                     /region_name="MJ0604"
                     /note="Predicted nucleotidyltransferase, MJ0604 family
                     [General function prediction only]; COG1708"
                     /db_xref="CDD:441314"
ORIGIN      
        1 mndpaaptal alglvtsrfp halgatlggs aaqgratpts dldvavllpd sdtsrrevvr
       61 hdgrlaelfl htladlpglf ardrarrrgt vlflydqgvp lmdpqgqvsr araqaravla
      121 agpppltpae wergryyltc fmddlvdtqp adryeqlala dstlgesahl ltahhgawtg
      181 igkwlprrll sadpergral ldghravaeh gdpaplaaaa eqvldlrggp lregytqpwg
      241 g
//
LOCUS       WP_457679163             567 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457679163
VERSION     WP_457679163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  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 567)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /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=59488
     Region          196..409
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mssstppvae nrptrsffag pgeqgrwllw raageallag alvllvhegv stidgrlegg
       61 apalgligia lvlvrrrfpv acvaglaalm gvvpavallt svaaytaarq trtprrrigv
      121 llgaaaltml tcaafapele mgsrlfglal gavfavttvv lpglagtagg qqdrllralr
      181 eraaaaeear rladsesrmr ersriaaemh dlvghrlslv slhagglema llkeapelrd
      241 eaavvrratr damqelreal gvlgplgsdt gtgaltdatg tradiealve esrsggipva
      301 fswegpdlda rpaqvrravh rvvresltnv hryaaeahvt vavrhtdqrv avrvrngvpp
      361 trpatvtglg sgrgltglre rvtllggsle agrtsgggfa vaaeipatpg pgaetadaap
      421 ddsgsasvde srsrlsvlqr rvagavigll glagvgvmml favllvdhsr yelayqspek
      481 prlgmtrgqv eravapddda sraaaagrep prpasatdcm ypyaggkrkg grmelvrycf
      541 rsdtlitidr ftvpivtepp hesrmhd
//
LOCUS       WP_457679180             467 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457679180
VERSION     WP_457679180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..467
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48397
     Region          13..420
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtpaavppgt trttnafswr fvtplftgsa inaintslia talvpiaaav hvsvgrtavl
       61 vsalylacai aqpmggklae efgprrvfla gilivlaggt vgglgqdlta lvvarvligv
      121 gssavypsam llirrraeat gldappggvl gglmiagaat salglpmggm lvdawgwrtt
      181 ffinlpfall alamayfwip sdppavgsra lrelaarldv agivgfagai aallvflrgl
      241 phpdwlvlvl aaaigaglvw welrtsrpff dvrllgknpa ltrtylrfav aslcvytvly
      301 gltqwlqagr nmsseaagll llpmsalsal larpisqrnl vrmplivaav sclaasagvl
      361 altastptvw ivvitlvfgi tlgttisanq talytqagsg eigtaaglfr tfgflgsias
      421 salisvvfht qvsdhrlhli alimvivsvl glilvitdrt vmtrara
//
LOCUS       WP_457679177             363 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional class I SAM-dependent methyltransferase/NUDIX
            hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457679177
VERSION     WP_457679177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 363)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
REFERENCE   4  (residues 1 to 363)
  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   5  (residues 1 to 363)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18603225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..363
                     /product="bifunctional class I SAM-dependent
                     methyltransferase/NUDIX hydrolase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38772
     Region          18..159
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          221..344
                     /region_name="NUDIX_MTH2_Nudt15"
                     /note="MutT homolog 2; cd04678"
                     /db_xref="CDD:467561"
ORIGIN      
        1 msgslktlkg siamgnvtre aqeawdthyg egrtfrplsd aeltflrelv pappggghal
       61 dvgcglgdla rhlaatgytv davdfaasal siaeqtppas gtvrfvqcdi erdpldglrs
      121 sydliafrls yafigdrtrv mhrlrerlrp ggavvvitpv vagvpadrra ialdeeeitl
      181 lsagwhtver rdaeglaflv lrdpapgpva yrgkgrpsph altgagvvvt deagrvllgr
      241 slrgtwelpg gkndggesfv eaavreleee tglrakaada rllailmdav hgmprvtaav
      301 rivdfcgkpa vrepdlihrw ewhdvadlpt laaalftpsa hvldvvwpgl lpglppvhrh
      361 plv
//
LOCUS       WP_457679183             144 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457679183
VERSION     WP_457679183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..144
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15582
     Region          3..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maddldvnav gsalqlslgl fvrrlrqplp geltlpevsv lsrleraest tselaraeqi
       61 tpqamgmtla gleerglvrr rpdpadgrrv vmsvtedgqr elrnrrsara eqlaealaag
      121 gftraeletl raaaplierl genl
//
LOCUS       WP_457679201             124 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457679201
VERSION     WP_457679201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..124
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12942
     Region          6..117
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mtgpvvrvdt tgpvppyeqi raqlaaliat gqlaegerlp tvrqlatdlg lapgtvaray
       61 reletaklih trrgagtrva alpsepqqpd paqlarlard fasaaralga dteailtavr
      121 kale
//
LOCUS       WP_457679207             440 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679207
VERSION     WP_457679207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46317
     Region          35..431
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mdwdglrrrm tgallrpgda gfetarklfn plnddlvpaa vaqcatvgdv reavlaaanr
       61 vplaarsggh syvgysaphg gltldlrrls tvrahpdgta tigagatlqa vytalgqanr
      121 clpggscftv giagvalggg igvlqrkfgl tcdhlvsaev vtadgrtlta satqnpnlfw
      181 alrgggggnf gvvtqftfat dpapaltvfr ldfpagsvtk mltawqpwit aaprelwanl
      241 nvsggaiprc kvagcfvgps sacnpllndl vtradvrpdl rrvedrdyfk amrffsgspd
      301 rqsfvassrv ltshaanpga vvsllkdrlg mdlildplgg avadvdvqqt afphrkafat
      361 aqiyasataa seaavtrsvg qvvagladqg ikdgyinyid palpdwakay ygpnlerlrt
      421 vayeydpdrv fdfpqavtht
//
LOCUS       WP_457679213             512 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679213
VERSION     WP_457679213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..512
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=54257
     Region          16..511
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mhdapdripp phhgleplvr irglskrfgg tlaldavdld ihsgsilall gpngagkstl
       61 ikvlagvhha degevtvagh plgteaaart msfihqdlgl vewmtvaeni algtgyprra
      121 gllswrltre rcaealsiva ahldprtvla dlpraerslv aiaralstra elivldepta
      181 slpaadcarl fevlhtlrdq ghalvyvthr ldevykvaev favlrdgrli sqgplaghsp
      241 arlvhdivgh epvgfrrapa agsvvlsldg vrtentapvs lelrtgeilg mvgltgaghm
      301 elgralagar pvvggrvrln grpytpgtvt aavgsgvgfv tsnrqeegca aeltvrenfl
      361 anpradglra fhwisprrer agatalaerf svfprdseap iatlsggnqq kvmvgrwlri
      421 hrsllileep tagvdigakt avyrllqeal aeglavllis tdfeevaqvc hralvfvrga
      481 vteelsgkal tvaglahass amaaltgetr rp
//
LOCUS       WP_457679226             370 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679226
VERSION     WP_457679226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  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 370)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..370
                     /product="glycosyltransferase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39943
     Region          92..355
                     /region_name="YjiC"
                     /note="UDP:flavonoid glycosyltransferase YjiC, YdhE family
                     [Carbohydrate transport and metabolism]; COG1819"
                     /db_xref="CDD:441424"
ORIGIN      
        1 msaldyvtcp aheqghqvtl haplifrsea rrrgvefsga gtnwtcdplv qqaasevwqr
       61 hgnasfnryv fghlwpgqae akahdlltaw tqerpdlvia ecsdlgahla aralqlplla
      121 adnglgpvll dlwdthiapv llplykqheq dtptlppmlt papvhwfyet pppsaravrr
      181 tvadfrtalp ewldrapslr psrplvyvsl gtlttamsgl rtavgnvyre imaalraidc
      241 daivsagdla qhlpsasphi kvvkhapqpa llhradlfvt hggrasllda vqgttpvlgl
      301 gvladqpdna aaftrsglgr sldltarhde iadaltelld aprygaamse acaelsqlpp
      361 lnlteirdsl
//
LOCUS       WP_457679232             405 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457679232
VERSION     WP_457679232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 405)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45809
     Region          20..404
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(69,94,96..97,180..181,190..191,194,197..198,201,234,
                     237..238,241..243,246,289,291..294,318,394)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(95..96,103,107,114,159,162,238..239,242..243,
                     246..247,250,288..289,292..293,295,318,345..347,350..351,
                     353..355,358..359)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mvhepkapvi pykrtcpfdp aaeyarlree dpispvtfel aprekngwlv trhdhirqim
       61 tdprfshrse llalvhsppf pvehyspeps apgnfvrmda pehtryrrll tgfftvrkiq
      121 qyeptlvrii dgvldemaam eppvdlvkvf aeqisarstc simgvaesdl aalaqhfsvi
      181 mginytldef ihhnselnat lermmaerfa gdptddllgr liatgelteq emfniawiai
      241 ggaldttpnm falgtfalle hpeqlakvre rpelmestve ellryltish fgasrvaled
      301 veidgrtika gqtvvlslps anrdpryfen adefdinrps rrhlafgfgi hqclgqhlar
      361 aslrigfqkl fdrfpdlrla mpaeqvplre tamhygvyel pvtwg
//
LOCUS       WP_457679235             360 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457679235
VERSION     WP_457679235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..360
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37651
     Region          30..275
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mptrrstppq plsahsgpvp dreavdtaaa rpvrfgalgt ssfggrrvlp amtacpqtel
       61 vavggrsper sqrfadrfgc agssmaalle rddidavyis lppslhgewa aralhagkhv
      121 lvekpiatta aearavvrla edrdlvlren fmflhhpqhd avaaliaegr lgglrsfrga
      181 fcfpplpted iryvpglggg alldagvypl raaamllgpg lrvagatarv rqsdgldlsg
      241 qallvspsgv lasvefgfeh aygssyslwg egakltvgra ftppaayqpv lvleeqdhve
      301 kftlpaadql taslagfaaa vtaggaaasp rearwlqdav ammelvdavr aqavrvtveg
//
LOCUS       WP_457679247             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679247
VERSION     WP_457679247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27664
     Region          6..250
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttpiidakg lartfttkkg pveavrgidl tvsageilgf lgpngagktt mmrmlttllp
       61 ptggsatvag hdlacdpvgv rrrigyvaqa sgvdpavsvr eelvtqgrly rlgkteaknr
      121 arelaedldl adlldrptrs lsggqrrrld ialglthrpq llfldepttg ldpgsrsdvw
      181 dlvqrirteg ttvfltthyl deadvlsdrl vvvdgglvaa egtpqdlklr ytgseaaslr
      241 eaflaitghh plapdvpvai
//
LOCUS       WP_457679257             678 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679257
VERSION     WP_457679257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 678)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 678)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 678)
  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 678)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..678
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72977
     Region          56..652
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtsagprrda hqgarstaaa dgisnaerel yggrlrwdqt fvryegaltr lkfgqmaaal
       61 prmvgmvlrt gwevdrralt gvvtaqvgqg vtaawglvav nrvltqlfad gptadklrqa
      121 lpslvvlavv svgsallaaw stamsgrlep qvervvsary yaavtrveve aterpevqrv
      181 leagrfgtds arsmlrlsvg vgsvligmva aavvlvslhw illpmllaia fpkgwgavrs
      241 arreytsrln wvdhrraiss llayltrpha ageirvhaag etllrgyeem srqteaeqrr
      301 laraqahtdl vaggfaglas lacygllwwl laagglplav ggtaviairn sterltslvq
      361 qvnrlyeell fltdtkhate laaehaiprr gtplpcptra vhmenvsfty pgadspalkg
      421 vslsvrrgtv talvgangsg kttltkilag lllptdgsvw wegepgrrve lreadrtevf
      481 gmvgllgqdf phwemtaatn iaigagarpr dmdrvkeaaq aadvhaliag lphgydsivf
      541 kgyergvqls ggqwqklgaa rsryrnapff lvdeptsald phaeiaafeg lwalaerdha
      601 vvlvthrlaa takadhiyvl dhgrvveegt hdqlmsaddg lyrgmfaaqa aqygliqapg
      661 dvvpaprrgs aprreetl
//
LOCUS       WP_457679272             183 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457679272
VERSION     WP_457679272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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 183)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20411
     Region          11..176
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(25,40,79,105..106,119)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mtelspdalf eqlqrlpape gykveivega vymtpqcdvh wqtirrivra ledhfgmdvl
       61 vtsdvrinfp gerngfapdv akisdgaekd esgrwrhqdv efiaeviskg tapndygpkk
      121 kayalaevpv ymiadpylgr crvftdpqdg dykidstiay gtpvdlthtv vgitfsteef
      181 prd
//
LOCUS       WP_457679278             245 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679278
VERSION     WP_457679278.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /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=25028
     Region          6..221
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtaaalralh qgpdlplvlp gpwdavsakv fadagfpala tpsagvaasl gyedgrtpad
       61 emfaaisrit havdipvsad veagyglpak elvarltdag avgcnledtd httgalrdar
      121 eqadwlaqvr aeagdalvin aridtylhga qdleesvrrg rlyaeagadc vypilapppl
      181 ladlstgigl pvnavvtpdg psprelgalg aarvtfgpgl qhramaavae maerlreelg
      241 agsgg
//
LOCUS       WP_457679285             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679285
VERSION     WP_457679285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18662006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19960
     Region          17..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          79..>147
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mteharvleq lpghlalrhp apadhprlqq alvgwwdglg geagalqrql lvprlflqhf
       61 adtsfwverp dhtlhaflig flsqtdprva yihfvgvcpe grregigsal ydrffttara
      121 agrtqvrcit spnnrnsiay htrmgfqlep gdridddgvp lqgdydgpgl drvsfvrkl
//
LOCUS       WP_457679294             437 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457679294
VERSION     WP_457679294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 437)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46111
     Region          53..435
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(82,89,117..118,125,129,136,267..268,271,275..276,
                     279,312,317..318,321..322,324,347,376..378,381..382,
                     384..386,390)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(89,111,113,116,118..119,205..206,215,266..267,
                     270..271,275,318,321..323,425)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtdgqpisdd drrtapaplp ppgatcpvrp gggaphrlap ggagraaada llreagavvp
       61 vllpgevpav avthhavlre vlahpevakn achfaalhdg tvppgwpltt fatvdgmtta
      121 dgadhrrlrg lvtkvftprr vaalrprvve ltaglldglp gaaaadstvd lrrhfayplp
      181 msvicellgv daalrdrlhe lsnlivgttg tadevqaanr eitavlgeva earradpgdd
      241 ltsallaaqe edgdrlsare lvgtlllmii aghettlnli tnavralctg reqlelvrag
      301 ratwddvvee tlrhdspvah fpfrypvrdl elggtvvprg tpmlasysaa grdpeaygpd
      361 adrfdvtrrp atrhlsfghg phyclgapla rleatvalea lftrypaldl avpdaelpph
      421 qsfignsthv lpvrltg
//
LOCUS       WP_457679300             448 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Streptomyces nigrescens].
ACCESSION   WP_457679300
VERSION     WP_457679300.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 448)
  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 448)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..448
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=47787
     Region          197..443
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mifalivvpv lglffgvhry lwcrlvrdtt tpgsrprrtg tvaafvlplt tlaaflsgra
       61 gapfplqqal awpgylwlal vlyltlalla gevvravclr avrtrerteq vpssstdhgh
      121 kpraqtpppt peptpdpspa phptqppsps pspspssapt llpphtpalp platpprrlf
      181 laravaagas laataavgyg tattlrgpvv krvtiplakl praahgfria vvsdihlgpv
      241 lgrahtrrvv etinrtrpdl vaivgdlvdg nvadlapaae plrelqsrfg syfvtgnhey
      301 ysgadqwvdh vrelgihyle nartelpgfd lagvndvagq tenagpdydq alsdrdpara
      361 vvlmahqpvt ihdsvrygvd lqlsghthgg qmwpftyiad atnptiagle rygdtqlyvs
      421 rgagtwgppv rlgappdvtv velaslra
//
LOCUS       WP_457679308             572 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457679308
VERSION     WP_457679308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..572
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.52"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61490
     Region          80..212
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          217..555
                     /region_name="GH20_DspB_LnbB-like"
                     /note="Glycosyl hydrolase family 20 (GH20) catalytic
                     domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and
                     related proteins. Dispersin B is a soluble
                     beta-N-acetylglucosamidase found in bacteria that
                     hydrolyzes the beta-1,6-linkages of PGA
                     (poly-beta-(1,6)...; cd06564"
                     /db_xref="CDD:119334"
     Site            order(227,256,304,366..367,423,444,473,525,527)
                     /site_type="active"
                     /db_xref="CDD:119334"
ORIGIN      
        1 msnpmrppra prpsasprpt rpmtgkgpaa rsalpaaala galllagcsd aadteppgst
       61 sakmnptsva tptwapvtgt pqvipavrdf rradgrgwrp skgarvvvpa geksnvadea
      121 qrmardlggl avvygdqtvq pgdievkltg ngadqannvp vqgaadeayt ltaegtrltl
      181 taptdagify gtrtvkqavr aagglpegti qdrpgrpqrg msldnarkpf tqdwiearlr
      241 eiadlklnqf qlhfsddqgf riqsdthpei vsadhltkaq irqiialars lhisvipeld
      301 spghlgavlk hypdlllrra sgsvvpgaid isnpkaapli dsllkemsel ftnpkgapay
      361 whlggdeyqa llsstpatty pqltraarqk ygpngtiadl atgwlndrqk tveakgknri
      421 eawndgffss prasadknrm vdywtgkeag hrdpsaflre grnvmnfnde ylyyvlgepn
      481 qfvyptgqri yeswtplvir gtgavavpas mtgpdripga rfaiwcdraq aqtapqvaag
      541 irlplaalaq ktwdprtpal swtgfkalan rv
//
LOCUS       WP_457679315             303 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679315
VERSION     WP_457679315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=32693
     Region          93..161
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          191..302
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 magraaeirg lrmqrsrgrr tapavaavlv vaalavgcrp vtvtgagspd skgtryaptt
       61 pappplghhp ppaharhtak phpprtahht paaprplmap gsrgaqvrel qarlaqlglf
      121 draptgyyas vtatavrafq rrqglprtgt vqpaawralr sqtrrpshae lyppttrpvg
      181 tpdprcmrgr viciskrsnt ltwvvngriv samdvrfgsq ytptregtfh itfksrhhvs
      241 tlyhtampya mffsggqavh ysadfaahgy rgashgcvnv rdkqkiaalf htvkggtkvv
      301 vyh
//
LOCUS       WP_457679317             162 aa            linear   BCT 27-JAN-2026
DEFINITION  ribosome maturation factor RimP [Thermovibrio sp.].
ACCESSION   WP_457679317
VERSION     WP_457679317.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Nord,S., Bylund,G.O., Lovgren,J.M. and Wikstrom,P.M.
  TITLE     The RimP protein is important for maturation of the 30S ribosomal
            subunit
  JOURNAL   J Mol Biol 386 (3), 742-753 (2009)
   PUBMED   19150615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     gene            1..162
                     /gene="rimP"
     Protein         1..162
                     /product="ribosome maturation factor RimP"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /GO_process="GO:0042274 - ribosomal small subunit
                     biogenesis [Evidence IEA]"
                     /calculated_mol_wt=18380
     Region          6..157
                     /region_name="RimP"
                     /note="Ribosome maturation factor RimP [Translation,
                     ribosomal structure and biogenesis]; COG0779"
                     /db_xref="CDD:440542"
ORIGIN      
        1 meeraqeive rvkkllqpil eeggfelvdv efvrepvgwv lriyadrpqg gitisdcqwi
       61 serigtvldv edliphaynl evsspgldrp lksqkdferh kgivvkiktt epldnqrnfk
      121 gevistsekg vkvhdvsrna eveipyekik sarvdidslf dk
//
LOCUS       WP_457679318             532 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA mutase large subunit family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679318
VERSION     WP_457679318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Banerjee,R. and Vlasie,M.
  TITLE     Controlling the reactivity of radical intermediates by coenzyme
            B(12)-dependent methylmalonyl-CoA mutase
  JOURNAL   Biochem Soc Trans 30 (4), 621-624 (2002)
   PUBMED   12196149
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Marsh,E.N.
  TITLE     Coenzyme B12 (cobalamin)-dependent enzymes
  JOURNAL   Essays Biochem 34, 139-154 (1999)
   PUBMED   10730193
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..532
                     /product="acyl-CoA mutase large subunit family protein"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0016866 - intramolecular transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_process="GO:0006637 - acyl-CoA metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58011
     Region          4..529
                     /region_name="Sbm"
                     /note="Methylmalonyl-CoA mutase, N-terminal domain/subunit
                     [Lipid transport and metabolism]; COG1884"
                     /db_xref="CDD:441488"
ORIGIN      
        1 mahesgsvry nesglpiepv ygpealdgwd perrlgapgg ypftrgvyps mytgrpwtmr
       61 qyagfgtare snaryrqlia hgttglsvaf dlptqmghds dtpiasgevg kvgvaidsve
      121 dmrvllggip ldkvstsmti napaalllll yqlvgeeegv aagqlngtiq ndvlkeyiar
      181 gtyifppqps lrltadifqy craeiprwnt isisgyhmae agaspaqeia ftlangityv
      241 rtavaagmdv ddfaprlsff fvsrttllee vakfraarri warvmreefg aknpksmmlr
      301 fhtqtagvql taqqpevnla rvtvqglaav lggtqslhtn sfdeaialpt dksarlalrt
      361 qqvlayetdv tatvdpfags yavesmtddv aeaavalmrr vedmggavaa iergfqkeei
      421 ernayriare tdagervvvg vnrfqldeee pyeplrvdpa ieaqqverla tlrarrnqrt
      481 vstalgdlek aaegtdnvly pmrealrara tvgevcdalr gvwgtyvptd af
//
LOCUS       WP_457679321             384 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679321
VERSION     WP_457679321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41763
     Region          30..384
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtttqlttsa ppaapdlvtp apqpairgrs ragasrlral dglrllaalm vaayhyggrd
       61 geiaqawggs paeqfptaap lfaygclgvq iffvisgfvi clsgwgrtlr afiasrvsrl
      121 fpaywvaill vtavfalpwv aykalspsdv ltnltmlqqp lgvdrvlgvc wtlwaemrfy
      181 alfalcvvlp gatrgrvvlf cagwtlaaal aqaaheplld tilmpeyapy figgiglyll
      241 hrygardpia waivlvswli gqhyaiarlw hapsadgfsy rssagiiavv tlgfalvaav
      301 algklrwanw rwltvagalt ypfylvhehl gwvvvralhh gvglpsyatl lltvglmlll
      361 awvlhrfier pltpvlkrsi dprr
//
LOCUS       WP_457679340              98 aa            linear   BCT 27-JAN-2026
DEFINITION  divalent-cation tolerance protein CutA [Streptomyces nigrescens].
ACCESSION   WP_457679340
VERSION     WP_457679340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003543
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..98
                     /gene="cutA"
     Protein         1..98
                     /product="divalent-cation tolerance protein CutA"
                     /GO_process="GO:0010038 - response to metal ion [Evidence
                     IEA]"
                     /calculated_mol_wt=10637
     Region          2..98
                     /region_name="CutA1"
                     /note="Divalent cation tolerance protein CutA [Inorganic
                     ion transport and metabolism]; COG1324"
                     /db_xref="CDD:440935"
ORIGIN      
        1 mtdflqvsta tetreaavkl aqsvvsarla aeaqivgpvg svfwhkgefg sgeewqlvlk
       61 vradrydeve ahllkhhpwq npevsavpiv agadaylr
//
LOCUS       WP_457679334             386 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457679334
VERSION     WP_457679334.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40718
     Region          19..366
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mststknpav daiaksatrd kvilaiaapv laivaaivis slvflasgen pfraygimad
       61 yghysdsqvw iinkavpyyl salavaigfr mnlfnigvdg qyrlaafaaa avggaialpg
      121 aiqiillivi amlvgaiwsg iagllkttrg vsevittiml naiaasiigy flqdgrlaik
      181 dgnllhtkfl pesshffsfp thpkpvygfv viailagaly wfginrtrfg fdlravgase
      241 paaeasgvsv krmvissmll sgaaaglvgm ptllgesfqy gtdfpagigf tgiaiallgr
      301 nhpigmafga llwafldrtg srlefegyaq eivgviqgvi vlcvviayei vrryglnlqq
      361 rkvgeelail srttnsdksd kpevsa
//
LOCUS       WP_457679343             184 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679343
VERSION     WP_457679343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20336
     Region          15..184
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          99..166
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtapeaitve sldgpaaars epafrlvyae vfaeepyeet pesvaatfrr frsqvrkstf
       61 raalartacg epvgiayghp lsaaadwwdr lvtpvpadlr redgqrtfgl mefavrkhwr
      121 glgvgrrlhe allaegneer vmlnalpdae aahtayrswg yrkvgeahpg esavlydvmv
      181 lqlr
//
LOCUS       WP_457679358             560 aa            linear   BCT 27-JAN-2026
DEFINITION  phospho-sugar mutase [Streptomyces nigrescens].
ACCESSION   WP_457679358
VERSION     WP_457679358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Shackelford,G.S., Regni,C.A. and Beamer,L.J.
  TITLE     Evolutionary trace analysis of the alpha-D-phosphohexomutase
            superfamily
  JOURNAL   Protein Sci 13 (8), 2130-2138 (2004)
   PUBMED   15238632
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..560
                     /product="phospho-sugar mutase"
                     /EC_number="5.4.2.-"
                     /GO_function="GO:0016868 - intramolecular
                     phosphotransferase activity [Evidence IEA]"
                     /calculated_mol_wt=58679
     Region          47..552
                     /region_name="PGM2"
                     /note="This CD includes PGM2 (phosphoglucomutase 2) and
                     PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2
                     is thought to be a phosphopentomutase that catalyzes the
                     conversion of the nucleoside breakdown products,
                     ribose-1-phosphate and...; cd05799"
                     /db_xref="CDD:100092"
     Site            order(51,53,56,150..152,160,300,302,304..305,349,370..372,
                     386,388,390,512,514..516,521)
                     /site_type="active"
                     /db_xref="CDD:100092"
     Site            order(53,150,305,349,370,372,386,388,390,512,514..516,521)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100092"
     Site            order(150,300,302,304)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100092"
ORIGIN      
        1 matdpaelih raqawlaedp dpetrdelsk lieaedtdel aarfagtlqf gtaglrgelg
       61 agpmrmnrsv viraaaglat ylkaqgdgsg lvvigydarh ksadfardta avmvgaglra
      121 avlprplptp vlafairhlg avagvevtas hnpprdngyk vylgdgsqiv ppadgeiaae
      181 iaavrsladv prpeagwetl detvldayla rtdavltpgs prdtkvvytp mhgvgrdtlv
      241 aafaragfpa ptvvaeqaep dpdfptvafp npeepgamdl afatardrga agvdiviand
      301 pdadrcavav papgtpdgwr mlrgdevgal laahlvskra sgtfattivs sqlmsriaag
      361 aslpyeetlt gfkwlarvdg lryafeealg ycvdpegvrd kdgitaalli telaaelkqs
      421 grtltdlldd lalefglhat dqlsvrvedl sliadamhrl raqpptalag lsvtraddln
      481 rgtetlpptd glryylsgsp eagieaarvv vrpsgtepkl kcylevvvpv psaealpear
      541 tkadatlasi kadlseaagi
//
LOCUS       WP_457679370             494 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679370
VERSION     WP_457679370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..494
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=52479
     Region          <74..494
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnrplrhiav fcgvlvlall vrvtwvqfvq geelsndpnn rrvkieafsy prgniivggk
       61 pvtgsvatsg dfkykrtykn gpmyapvtgf asqaqgtsfl egiynkvlsg kddrlalkna
      121 kdiltgekpr ggdvittidp raqkaaykgl tdlnakgavv aldprdgrvl alastpsydp
      181 slftgisnae grkfkeldad kskplsnral retyapgstf kiltaaaale hgvvsdinas
      241 sgapapyqlp qsttkvgndv agapcdkasl ktgmqwscnn vfldaalkvg kdkmretaek
      301 fgfndnvyde dlgdllatks lypakldkpq taltgmgqgs ltstpmqmam vaaglandgk
      361 vmmphlvdev rgsdlstiek tepkmmsqav sadtakkvqe mmeytvnegt aekaaidgvt
      421 vggktgtaqh ganvnderpy awfvsyakqs dgsspvavav fvdpkdmnip reeiaggklg
      481 gpiaksvmea vlkk
//
LOCUS       WP_457679378             443 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457679378
VERSION     WP_457679378.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  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 443)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /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=46735
     Region          142..415
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtrearrape arvrwfglwd syfvicylvt tglvftsavp qtarliaiga ltlivpwyag
       61 igrplmlrhe sdrrngffvg glfvlfglat avdltsafal faivpmlmms lavrpavvaa
      121 vlgnllpvtm lwlqggatap lmlfvllasl lgialsvllg lwikrvvrqn rehaelieel
      181 rrnreqvarl shqagisaer erlareihdt laqsltsiis lvqaadaeve gapavarkhl
      241 alvgrmates laearafvad rtpaslress laqalrrqad glaaqtglla rfavegderp
      301 lpmavnvvll raaqeagtnv rkhadaravd lvlrygegqv glrvtddgkg fdateaerga
      361 aaeagpdggg sgdedsgfgl rgmaarvaei ggvlsvvsrr gagtvvevkv pldgaaerps
      421 gpsaprpgta grlteaaddg glg
//
LOCUS       WP_457679388             245 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679388
VERSION     WP_457679388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25450
     Region          5..243
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msgiegkvva itgassgige aaalllaerg arlvlgarrs erlaalvari eeaggaavqi
       61 rtdvtrpddl halvalager fgrldvlvsn agvgtispld dlrveewdhm vdvnvkgvlh
      121 giaaalpvfr aqgtghfvtt astaafrvvp amavyagtkf avraiceglr qeagdslrvt
      181 tvspgvtatd faeasshsrv raeitkmrdd laispdaiar aiafaieqpa tvdvneivvr
      241 ptaqr
//
LOCUS       WP_457679401             335 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679401
VERSION     WP_457679401.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  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 335)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="MDR family NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35372
     Region          5..333
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(50,132,156..158,178..179,183,199,222..223,244..248,
                     250,277..279,322..323,325,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(51,250,280)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(54,58,238,243..246,249,267..268,271..278,281)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 mthrthrevr ltarpqgpvt ddlfeivevp vpepgpgqvl vrntvmgvaa vmrtlmdenn
       61 vvpvpafevg eplngpalge vvaapgtdlt pgdlvehrlg wreyalldad gvhrrapglm
      121 pdpaaylsqg ptawmgivrg aevrpgdtvf vtgaaggvgs lagqvarlrg aarvigstgs
      181 qekadrlike fgydavvirg agpieeqlra aapegidalf dnvggeqlra aiavantgar
      241 lalvgalssq lsedgkphtt eidtlsllar nitlrgvalh ahmdlvpewn qrfgeglrdg
      301 tltfphtrlh gieqapralr eltegrhlga vlvel
//
LOCUS       WP_457679417             544 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679417
VERSION     WP_457679417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..544
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58221
     Region          1..542
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdtvfrdvrv idgsggpsyr advalsggri aeihresdgg prpgaarvve gqglalspgf
       61 idmhahsdla llrdpgheak aaqgvtlevl gqdglsyapv ddrtlaevra qiagwnggap
      121 gdtsldfnwr tvggyldrld hgfdgrgiav naaylvpqgt vrmlavgwdd raatadelar
      181 mrqlvaegle qgavglssgl tytpgmyasd aeltelcrvv arydgyycph hrsygagalq
      241 ayeemvaltr eagcalhlah atmnfgvneg rapellalld raldagadlt ldtypytpgc
      301 ttlvamlpsw aseggpgvim arlrdeataa rirhvmeveg adgchgvpid wdtieisgvs
      361 dpaladhvgk tvarsaaera eepwqtarrl liedrlgsti lqhvghednv rrimrhqvht
      421 ggsdgilqgd kphpraygtf pqylgkyvre lgvlsleecv ahltarpaar lrlpdrglvr
      481 egyradlvlf dpetvaagst fdaprtlptg iphvlidgrf vmedgrrtdv lagravrrta
      541 sgrg
//
LOCUS       WP_457679420             440 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679420
VERSION     WP_457679420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45967
     Region          37..408
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mvwgtagraa adgrgrpvrq gtaeqgsvgq gaveqgavda evariqreli alrrdlhrhp
       61 empgqerrta gvvarelraa gltvatgvgg ghgvigilhg arrgrtvayr admdavppkd
      121 ivgggpaaah vcghdihttv algvarvlar lrrqlsgtvv flfqpaeetl sgaralidag
      181 vlertgvaei halhcgpfpv gtfavtpgyg lpgqdkaevt lsgpgapdaa rrlaaeigal
      241 atvappqtpa dierlladal tpdgplarfv avraraqeag vsvayrcwpq erygevradi
      301 rrlamswaga avrfpaepfp amvcperdar mlahhlrram greavtelha afppfsgedf
      361 alyldrvpgt ftflgvraph apitagyphy pdfapderav gvgvramagw iaerthrarg
      421 lpggsgpggp ttptgsrtsg
//
LOCUS       WP_457679423             558 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679423
VERSION     WP_457679423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 558)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..558
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59164
     Region          15..517
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 mnaastssgp avpdapavel rgitkrfpgv vanhdihltv rrgtvhalcg engagkstlm
       61 kilygmqkpd egtialggeq vtlhtpadai argigmvhqh fmladnltvl entvlgaekl
      121 hgigagarak ikkisdaygl nirpdvlved lgvadrqrve ilkvlyrgar tlildeptav
      181 lvpqevdalf dnlrelkseg ltvifishkl gevlsvaddi tvirrgttva svepsgttpk
      241 qlaelmvgse lpspetrest vtdeemlrvs dvhlsatdsd gvvrtvldgi sftihkgevl
      301 gvagvegngq aelveavmgt rrpdrgtitl dgtdlsgast rarreggigy ipedrhrhgl
      361 lleaplwenr ilghvterpn skgklldipg arrdtarive eydvrtpgie vtasslsggn
      421 qqklivgrem shqpklliaa hptrgvdvga qaqiweqire arreglavll isadldelig
      481 lsdtlrvmyr grlvadadpa vitpeelgsa mtgaarghls asedgapedg apekgapedg
      541 ashdgvspda geqegdeq
//
LOCUS       WP_457679433             443 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457679433
VERSION     WP_457679433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46681
     Region          29..426
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(39..40,43..44,47,82,129..130,132..134,137,161,
                     164..165,168,254,257..258,261..263,266,297,301,353..354,
                     358,362,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtqtpelplr tadpapapap rrrrphraws vaavtfltii gaagfaslpg llieplhaef
       61 hwsrgtigfa vsvnlalygl tapfaaalmd rfgirrvvav altviaagag ltvfmtaswq
      121 lvlswgvlvg lgsgsmalaf aatvtgrwft arrglvtgil taagasgqlv flpllswiid
      181 rhdwrpaavt valaalavvp lvwlllrdhp advgvapyga tefvpkpppq rgaarravra
      241 lvsaastgpf wllagtfaic gattnglvkt hfvpaehdhg mpmtaaasll avigifdiag
      301 tiasgwftdr fntrrllaty yglrglslmf lplllsdtvh ppmvffivfy gldwvatvpp
      361 tialcrehyg ddgaivfgwv laahqvgaal iaflgglard afgtynpvwy asgalcavaa
      421 lmalvirqrr egpgdarvva aqg
//
LOCUS       WP_457679438             286 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679438
VERSION     WP_457679438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29631
     Region          29..279
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtpspspgsv ppaepgepaa raepvdslvl httdngvswl tlnrpdamna ltpdqrerli
       61 grladasadp dvravvltat gkgfcagadl rgspsagerv agdvarlird gaqrlitavl
      121 dcekpviaav ngtaaglgah lalacdlvla aesarfievf vrrglapdgg gayllprlvg
      181 pqrakellff gdavpateae rlglvnrvvp dgelaktare waerlaagpt ralaltkqlv
      241 nasldtdrat afaaeataqe inmttadaqe gvasfvarrh pafrgr
//
LOCUS       WP_457679441             751 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate--CoA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679441
VERSION     WP_457679441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 751)
  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 751)
  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..751
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..751
                     /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=79607
     Region          61..747
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt thsrparvva cgeqpphtvh gmsephrdgg gqgacpvdrd vsgrplhapv
       61 pdldrffrpe svavigasdr egrpntgitr qliawaervg arlhpvnpgr tevfgrpcha
      121 gvadlpepvd lavllvgdpl pvieqlaeak vkfavafasg faetgergaa aqdrlaeava
      181 rsglrllgpn tnlnafekfr tdldgpaial itqsghqgrp vfslqelgir lshwaptgne
      241 adletadfls yfatrpevga iaayveglkd grsfllaadr aarnkvpvva vkvgrtetga
      301 rtaashtgkl tgadevvdaa mrqfgvirvd gldelqdtaa llararkpta egvavysisg
      361 gtgahfadla taaglrlptl gaakqaelhq wipdylhvan pvdngghpvg dwrgrkilda
      421 iladpsigil icpitgpfpp msdklaqdlv daaeqtdklv cvvwgspvgt edayrrtllg
      481 strvatfrtf ancitavray ldhhrfvdgy rspfddaprv lspsarkaha lmrpgqqlse
      541 haakqllray girvpreqlv tsaaaavraa slvgypvvmk asgpqlahkt elglvkvhlt
      601 sasqvrdayr eltdiaryed ipldgvlvcq miergvemvv gvtrdslfgp tvtvglggvl
      661 vevlqdvavg vppfgedqar amldelrgra lldgvrgapp adidalvevv lrvqrmalel
      721 gdelaeldin plvvlprgqg avaldalavc p
//
LOCUS       WP_457679444             142 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679444
VERSION     WP_457679444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15658
     Region          15..140
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mrfdlpevda ftrpywdaaa egrlllrrcr aegcgaahhy prefcpycws gdvgwepatg
       61 ratlytwsvv hrndlppfgd rvpyvaavvd laegprmmte iidcperelr igmplvvhfr
      121 gadegnagge gtavaipvfr pa
//
LOCUS       WP_457679457             472 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679457
VERSION     WP_457679457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47341
     Region          1..431
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdaafteeqh eirrtlrell lkrcgpdevk aavrtpagyd tqlwqqlagr lglpglalpt
       61 ayggvgcgpt elalaceetg ravlpsplma taalaaplil algserqrta llpalaagel
      121 tatlavpggr latalaltgp ndggwagggr aggiqarrap qegeavpskn ggrpagggwr
      181 lygeagqvln ghtaevlvva ahtggfakgr tllflvraaa gggearsgaa pgvpgllrtr
      241 qtaldetrpq arlelrhvpa ellgegdgde aavagalaat gmtaaaalaa eavgaadaal
      301 artvahvqqr eqfgrpigsf qavqhrladl yvrlqaarsa ayyaawsagr gpsapgggpy
      361 apggaagpyg aaepgvgala laqaleslra vaaeavqlhg gigftwehea hlyfkraacd
      421 elllgpvhrl raraaeeagl fpdgaeepgg agkpggsgep agapgraaav ev
//
LOCUS       WP_457679468             579 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679468
VERSION     WP_457679468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..579
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=62029
     Region          1..573
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mldhlikgat vvdgtgtpsy tadvgirdgr iavvvppgtv teearsseda tglvlapgfv
       61 dphthydaql fwdpyatpsl nhgvttvagg ncgftlapln parpadadyt rrmmskvegm
      121 slvaleegap wswssfgeyl dalegriavn agfmvghcal rryvmgedav ggqptpaqle
      181 rmlalfheam aagawglstt qsathsdgdg qpvasrhaap aellalsrav gehegtqiea
      241 ivagcldqfs daeiellvem saaagrplnw nvltidaavp ervprqliag erareaggri
      301 valtmpiltp mnmslgtfca lnlipgwgdv lglpvperie klrdpgvrae mlrragskea
      361 gvfrrlthfg ryvigdtysp anegltgrvv qdiaaergqe pfaclveica ndqlrtvlwp
      421 mptdndpdsw alraetwqhe dvllggsdag ahldrmcgap yttrflgdcl rgrklmgleq
      481 avkmltddpa qlfglrergr ieegwhadlv lfdperidag katlvhdlpg dsprldskai
      541 ginavwvngv etiredvvtg avpgtvlrsg rdtrtvstk
//
LOCUS       WP_457679498             333 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-70 family RNA polymerase sigma factor [Streptomyces
            nigrescens].
ACCESSION   WP_457679498
VERSION     WP_457679498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="sigma-70 family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36720
     Region          37..322
                     /region_name="RpoD"
                     /note="DNA-directed RNA polymerase, sigma subunit
                     (sigma70/sigma32) [Transcription]; COG0568"
                     /db_xref="CDD:440334"
ORIGIN      
        1 matravarrq esssgsdgan svraiggeia drdlvgmyld eiartpllda akevelsqti
       61 eagvyaqqil dgevadgnaa gagheelerl veegakakdi firsnlrlvv avarryprag
      121 lplldliqeg naglvravek fdyakgfkfs tyatwwirqa itrsiadqsr tirlpvhlve
      181 elgrirrvqr efnrengrdp epaevagelg stparvtdvl dwardpvsln msvdddgdtq
      241 fgdlledtsa aspeqsvltl lrseeledli drldhrtasi ikarygiedg rertltevgk
      301 qhgltrerir qiekhallel krmahdtgfd aaa
//
LOCUS       WP_457679500             711 aa            linear   BCT 27-JAN-2026
DEFINITION  PTS fructose transporter subunit IIABC [Streptomyces nigrescens].
ACCESSION   WP_457679500
VERSION     WP_457679500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 13938247
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..711
                     /product="PTS fructose transporter subunit IIABC"
                     /EC_number="2.7.1.202"
                     /GO_function="GO:0005351 - carbohydrate:proton symporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0022877 -
                     protein-N(PI)-phosphohistidine-fructose phosphotransferase
                     system transporter activity [Evidence IEA]"
                     /GO_function="GO:0090563 - protein-phosphocysteine-sugar
                     phosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=72169
     Region          1..147
                     /region_name="PtsN"
                     /note="Phosphotransferase system
                     mannitol/fructose-specific IIA domain (Ntr-type)
                     [Carbohydrate transport and metabolism, Signal
                     transduction mechanisms]; COG1762"
                     /db_xref="CDD:441368"
     Region          223..686
                     /region_name="FrwC"
                     /note="Phosphotransferase system, fructose-specific IIC
                     component [Carbohydrate transport and metabolism];
                     COG1299"
                     /db_xref="CDD:440910"
ORIGIN      
        1 mselitaelv dldlsaetkd aaarslaerm vtsgrvtdle gfladiaare aqmptgldgg
       61 igiphcrseh vteptlafgr sasgidfgap dgpadlifli aapaggdadh lsilstlarh
      121 lmdetftgal rsateperta alirgdepaa vpetavpepa vpepevagpa aepgperdae
      181 pqattdaapt tpaaaeapas gapseaatdt tpdatptpaa pfrivaitsc ptgiahtyma
      241 aeslekagqa agvevfvetq gsagfkrldp qlvadadgvi fahdvevrek erfagkptvd
      301 vgvkaginrp aeliaevrqk aahgeagapa raaapmdkga dagdgfatrl rkwlmtgvsy
      361 mvpfvaaggl lialafaigg ytinkapsva ehfiwtesas waallfqigg vafgflvpvl
      421 agfiaygmad rpglvpgfvg gaialtinag flggliagli agavvmaiqr vrippvlrgi
      481 mpvvviplis saivgflmfl vigkpiaalq kgltdwlsgl tganaiilgv ilglmmcfdl
      541 ggplnkvaya favgglanpn egslkvmaav maagmvppla malattvrsr lftkaereng
      601 kaawvlgasf itegaipfaa adplrvipsa maggavtgal smafgctlra phggifvvpl
      661 igqpllylla iaagtavsta lvillkglrk pspthpapsp addeaevtva a
//
LOCUS       WP_457679505             293 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679505
VERSION     WP_457679505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29855
     Region          5..290
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mttvkksvav lglgsmgaal adallvaghe vtvwnrtpgr aeglvargar ragsvaeavr
       61 ageivlvcil dygdigplle qqgggraalq grvvvnvtng speeacamae rvtalgasyl
      121 dggimavpei iaspeafvly sgsreafeah rgvldafars vylgedpgla plhdlallsg
      181 mygmfggflh aaalvrsagg svaeftttll qpwlaamagg lpamaaqids gdyavtgspl
      241 amqvahdsig evsraqgvsp elfaplfalm errvadghgs eglagvvelv hpr
//
LOCUS       WP_457679513             460 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679513
VERSION     WP_457679513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47567
     Region          53..448
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mpqphrpqpr ppadaapept gaeptdtepp gagtytappt daappgaapa raldgilvad
       61 fsrvlagpla aatladlgae vikverpgtg ddtrawgppf vadppsgeep psgeepaphe
      121 ggaprrgtaa yfdaanrskr glaldlgdpd daaaarelar radvlienfr pgslakygld
      181 htatraanpg lvhctitgfg sgagarlpgy dfvvqavggl msitgepggt plkagvalvd
      241 vltakdattg ilaalrhrdr tgqgqlvevn llssllgslv nqasghlatg rdpgpmgnrh
      301 psiapyetla crdgqllava vgndrqfrel aralgapela edarfarned rvqnrtdlvk
      361 alerrlasdt phdwterlta vsvpcgpvnt vsealelaqr lglapvtpvg egripqvtsp
      421 lrlsgtpvaq pfapprldeh gtalrtwlsg padhplpphv
//
LOCUS       WP_457679516             238 aa            linear   BCT 27-JAN-2026
DEFINITION  VIT1/CCC1 transporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457679516
VERSION     WP_457679516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10116192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="VIT1/CCC1 transporter family protein"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /calculated_mol_wt=24058
     Region          16..233
                     /region_name="Nodulin-21_like_1"
                     /note="Nodulin-21 and CCC1-related protein family;
                     cd02432"
                     /db_xref="CDD:153123"
ORIGIN      
        1 mtsqttdhde ahggglgsrl nwlraavlga ndgivstagl vvgvagatde rgtlltagla
       61 gllagslsma ageyvsvstq rdsekaalaq ekrelatepq aelvelteml egkgldeqla
      121 revaeqlteh dalrahaeve lgidpdeltn pwhaagasfl aftagallpl lamvlppaad
      181 rlwitvgavv valalcgwgs armgfapvgr amvrnvgggv vamgvtyaag svlgaagv
//
LOCUS       WP_457679522             383 aa            linear   BCT 27-JAN-2026
DEFINITION  Dyp-type peroxidase [Streptomyces nigrescens].
ACCESSION   WP_457679522
VERSION     WP_457679522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Sugano,Y. and Yoshida,T.
  TITLE     DyP-Type Peroxidases: Recent Advances and Perspectives
  JOURNAL   Int J Mol Sci 22 (11) (2021)
   PUBMED   34074047
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Colpa,D.I., Fraaije,M.W. and van Bloois,E.
  TITLE     DyP-type peroxidases: a promising and versatile class of enzymes
  JOURNAL   J Ind Microbiol Biotechnol 41 (1), 1-7 (2014)
   PUBMED   24212472
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Sugano,Y.
  TITLE     DyP-type peroxidases comprise a novel heme peroxidase family
  JOURNAL   Cell Mol Life Sci 66 (8), 1387-1403 (2009)
   PUBMED   19099183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="Dyp-type peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=40097
     Region          49..354
                     /region_name="EfeB"
                     /note="Periplasmic deferrochelatase/peroxidase EfeB
                     [Inorganic ion transport and metabolism]; COG2837"
                     /db_xref="CDD:442085"
ORIGIN      
        1 msraesrpsr rafigatgav aatgitagce spaprpsrps spasptrvap tgrhqagitl
       61 pqpaqpnlla vvadlcdava vgpllaelgq avhtltagtd prllglppgd ltvtigvgpr
      121 lvrmadpslp gaadlprfsr eqiapqargg dlllqicagd plllpvvasa lleqaghrir
      181 erwrqsgrrg pdipvdkgis aprnllgfid givgphttae hrrhlwlagp asvgggtiav
      241 vrrmeldlpr ftalsvadqe avfgrrratg vplsggtaaw dpdlgaktpd grylvpadah
      301 vrrasphvag vglmlrrsys tdaphpgllf isfqndlrtf tntlarmdds dallgftttt
      361 asatflilpg fdrqhplgak tfh
//
LOCUS       WP_457679508             197 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Streptomyces nigrescens].
ACCESSION   WP_457679508
VERSION     WP_457679508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21051
     Region          7..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mgsekrmqva vivgstrdgr fgptvaawva eriaqrgdma aevidlvetp aptvfpafgq
       61 ppapgttell aeisprlaaa damvivtpey nhsfpaplkn vidwhhtewh akpvgfvsyg
      121 glsgglrave qlrvvlaeln amtvrhtvsf hnygdkfdae grptdpaaeg aakvmldqls
      181 wwalalaeak avrpyaa
//
LOCUS       WP_457679529             550 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457679529
VERSION     WP_457679529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..550
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55810
     Region          21..433
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,269,272..273,276..278,281,309,313,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpksephphl dararwalaa vatgafcvql dsfalnlalp vvrdalhgsa tatpwvvsgy
       61 llaagslmpv agrlgdlygr rrmltaglal fgvtavlcal apslpllvta rvlqgaggal
      121 impaglallt hacppgrgrr amgralglag latvcgpflg gvlarsvswr avfwltvpla
      181 laaalcarra aesrdpeagq sldgvgaiaa tgvvaclarw lehaadwgwa vgaaligalf
      241 vraerrssap lvdlalfrnr pyvaltvaga vansatvall yvvpwtlqqa egwsvleagv
      301 vfvapagala vggplagrvr pgaavpvmal clasgavala attrgtgtla lltaataaaa
      361 algvagglal tgtqavvrre rageasgvtk avmtatagvg laltdagadg gagpslvlpa
      421 avclataval viacvlrlrl vrglvpvvgr vlglgralvl grvlglgral isvrslvsvr
      481 apvcvralrl vrvllpvgrr adrrrmdrcg vdrcgvdrrg agqrqadrrr saqcrsaqcr
      541 sarcrtdrce
//
LOCUS       WP_457679534             206 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457679534
VERSION     WP_457679534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22746
     Region          <29..170
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mttfrkstpl rrmlllaiap tamgcvltla asevavaapa gtwshptkar hrisspygvr
       61 gtwqaghhtg idlavrpgtk vrsvgsgtvv lakrsgaygk avtirmndgr ytlfghlsri
      121 tvrpgqkvra rtrlgysgat gratgphlhf evrtgrhygt dinpltylak hgirltprts
      181 aaprhrhhhr pkhhhrhhrh hhrhhh
//
LOCUS       WP_457679537             431 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679537
VERSION     WP_457679537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  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 431)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44842
     Region          3..429
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(13..14,16,166,169..170,180,211,268,333,335,337..338,
                     341)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(13,268,333,335,337..338)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            14
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            order(28,111,423..424,427)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mthilitaag shgdiapytg vgarlraagh evalathdsy aplvraagle frrlpadprt
       61 rradladatg pedateqarp papggtralm rqaaafvkel gggiadaard dtdllllsat
      121 taplghhlae argipslelp lvpaaptgdf apvvsggrsl grwgnraagr lslrvidrly
      181 adaaremrar lglpaatprt vrrraeaagr pvlygfsevl vprpsdwrtg ldvvgnwwpw
      241 hapddrlppv vedflaagpp pvfigfgsma ggegerlsal aaaalrrakv rgilqsgwag
      301 lttrhtsadd dlltigevph allfprmsav vhhcgagtaa agvrvgvptv pvpvtadqpf
      361 waarlaalgv atapipfkdl stdhavarlv haitqataap arrdhataaa hrlatedgag
      421 evlkaaerll a
//
LOCUS       WP_457679540             261 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457679540
VERSION     WP_457679540.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29170
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          132..251
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 msysvgqvsg fagitvrtlh hydkagllsp sdrspagyrl ysdtdlarlq qilfyrelgf
       61 pldeiatile dpqanaldhl rarhrllndq itklqrlvev aehamevqqt gveltpeerf
      121 evfgevafdl tyatqahlkw qhheghqrsm araaahsked wakimaesad wrvrllaafd
      181 agepadstpa mdlaeehrqh varwftpcpt dmhgriaddf atdprafall vppteqrpgl
      241 apylrtavha navrqspphg g
//
LOCUS       WP_457679542             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679542
VERSION     WP_457679542.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33281
     Region          9..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdpsswaie aeglgkqygr gwalrdcsfr lpaghicalv gpngagkstf lgtatrlvqp
       61 ttgtlklfgv pvsdpavlsr vsflaqdkpl yprftvaetl rlgrelnprw dqelaerivr
      121 sgkvplsari gtlsggqrtr vafalafgkr pelllldepm sdldplarhe msgllmaeaa
      181 ehgttvlmss hmlsemevmc dyllvlaegr lrmagqtddl ipahllvtgv aegddgvpee
      241 lrrqhtvves rvtgrqfsal irsggplsds wevlspsmee vllaylrspd aptliadesr
      301 vdgqrgaaa
//
LOCUS       WP_457679545             509 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457679545
VERSION     WP_457679545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55664
     Region          7..446
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mdgrerrhvr vavigsgfgg lgaavrlrrq gitdfviler adavggtwrd nsypgcacdv
       61 pshlysfsfa pnpewprnfs gqphirayle rvtdtfglrp hlrfnsevhs lrwngealhw
      121 evetasgplt advvvsatgp lsdpkvpdip gldtfpgkvs hsarwdhdyd lrgkrvamig
      181 tgasaiqivp aiqpdverlt lfqrtppwvl pradrkisaa ekwlhsklpa traarrgllw
      241 glremqvsaf tkrpnelgli eflarnhmkk aikdpglraa ltpdyrigck rillsntyyp
      301 alaqpnvdlv aagltevrgs tlvgsdgsev eadaivfgtg fhvtdmpiaq rvtgangttl
      361 aeewkdgmea lrgasaagfp nfltvigpnt glgnssmilm ieaqlnylad fmrqldvlgg
      421 kialdarpsa vqdwnrrvqq rmtrtvwntg gcdswyldan grnttvwpgt tsefkkvtrq
      481 vdlaeyevlr ppgtgpagrs tgeraevav
//
LOCUS       WP_457679560            1112 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457679560
VERSION     WP_457679560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 1112)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 1112)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 1112)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 1112)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1112
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=120341
     Region          12..1086
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mparpdppgg sylrfphlhg gllcfaaedd lwiapiapdg eepgrawrlt vdrtrvghpr
       61 fspdgqqiaf ttwrsldpev hlapveggpa rrltywgstd arvcgwtppd heghshilav
      121 sshgqpfsyy swayslptdg spggqlpwgp vsdiavadia gehrtlllsg kpphepaswk
      181 ryrggamgrm wlhgtrllpd lrghldsvmf vdgriaflsd hegianvysc lpdstdlrrh
      241 sdhgdfyarh astdgkriiy qcagelwlid dlapdavprk lavrlggpra grrsyqvpaa
      301 shvtalavdt tgrasavgvr gslywlthrd gpartihdvp gvrvrlpeml gasgriayvt
      361 daegadaiei tnlprasapg eprrlaagel grvhemtaap dgerlavaan dgrlllvdva
      421 rpeegaseee tasggvteli rstngpvrdl afspdsrwlt wshpgigrsl rqikmarlad
      481 rhivdvtngr fedeqpvftr dgrylaflsw rgfdpvydvh tgdlsfplgc rpylvplssa
      541 tpspfalspe grpaaggldp devpppageg pllvevegle nrvtpfpvaa skysslepvs
      601 ggglvwlrwp isgalgetfa npaetsgrpt lehfdltkar rteltssldg falsgdgsrl
      661 vvndegelra vpateqpdsd stvfldlrri lhdvdpvaew hqafeeagri trayfweprm
      721 cgidwdavla qyrplldrva spdefadllr evmgelgtsh ayvsgarrne gpphyqramg
      781 llganlvcrd grwvvtrilp gessdskars plagtgireg aalthvdgrp vdpvagpypl
      841 laaaggttve ltfsppedeg parrvavvpl iderplryqd wvakrravvr elssgrcgyl
      901 hipdmggsgw aqfnrdlrme vsrpalivdv rgnaggnise lviekltrti mgwdltrdae
      961 pvsytsnapr gpvvavadem tssdgdmita afklqglgpv vgmrtwggvv gmtgrhrlad
     1021 gtaitvpmna awfrlygwgv enhgvevdie alrsplhwae grhpqlgvai rtalellerh
     1081 paamppdlsd vpdlrrpplp prsggaaeaa ga
//
LOCUS       WP_457679573             270 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457679573
VERSION     WP_457679573.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29215
     Region          1..93
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(49,52,56..57,66,79,83,89,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrigelagli gvstravrhy hhlgllpepe rrangyrdyg lrdavalarv rrltelglgl
       61 devrdvladd agrelhevld eldadlarqe eelrarrarl aavrrqaeeh gglpaegpvs
      121 delaalfaem artsaarpgp esamaskere vlallesmgg eegnkrmvel igematapga
      181 iertyevygl ldalveagtd dprveeaara ladcipdavi aevdreqwer aagpgaevdg
      241 gflaayyghf apaqaravrr aiqlvaerar
//
LOCUS       WP_457679584             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679584
VERSION     WP_457679584.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33716
     Region          24..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 magttrpgst aerasdaaav gfsgvtrsyg avravdgldl eiaagetval lgrngagkst
       61 tlnillgllp pssgtvrlfg dapepavrag qvgamlqdgk aiprvtvrel itfvaatyph
      121 pmdvaealel agldgfggrr vdklsggqaq rvrfavalag npellvldep tsaldvearr
      181 tfwrsmraya rrghtilfst hyleeadeha drivvidrgr vvadgsgeai krraggsrvs
      241 fdlagaatdp lsglpgvsav eirgdrallr ttdsdatvla laelglvrgl qvtpasleda
      301 flaltsteat paapaltaga rtakesv
//
LOCUS       WP_457679587             759 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457679587
VERSION     WP_457679587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..759
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=79050
     Region          1..388
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
     Region          385..748
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(470,500,502,534,536,730..732,734,736)
                     /site_type="active"
                     /db_xref="CDD:173838"
ORIGIN      
        1 mgigitqdqr dlaeaaggwa aravppeavr klldtapart grpvywdqla aqgllglhlp
       61 eadgggggel ldlavvleel graafpgpcl pttlaaallh rggapalvra latgarigav
      121 algtgsltav espdgyvldg tappvlsgad adlivlaaev ageagltgea egaggakgaa
      181 dgavrdgggg rragetvwla vdagaltvrv qesadptrpt aevrahgvpv paerrlavds
      241 dlvrdlagvl waaescgtas walhtaaeha avreqfgrpi gqfqavkhlc admlvryeqa
      301 aalvwdaara lheppavrgl vaglatatal daavscakdc iqilggigft wehdahlhlr
      361 ratvarqllg sgdthrlraa ryaadgarrp lhlelpaeaa efraeartvi dgvrgldpaa
      421 vrrtlaptgy aaphlpapyg lgagpvqqla iqqelaaadv risdlgiatw vvpsliahgt
      481 peqqercllp slrgdllwcq lfsepeagsd laslrtraer tadggwring qkvwtsaaqw
      541 ashgillart dpdapkhkgl tfflvdmktp gidirplkei tgeslfnevy fddvllpada
      601 vvgevdngwk varttldner vhmadqltfd tgltalldra aeldgsvrar vgalaaeaha
      661 lgciglrttl qqvsglepga gasirklvqt phqqkvaela lellgpdgav regageralh
      721 gflmsrclti aggttqvqln vvaerllglp rdpeprpli
//
LOCUS       WP_457679598             435 aa            linear   BCT 27-JAN-2026
DEFINITION  prenyltransferase/squalene oxidase repeat-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457679598
VERSION     WP_457679598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="prenyltransferase/squalene oxidase
                     repeat-containing protein"
                     /EC_number="5.-.-.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43333
     Region          <72..>185
                     /region_name="ISOPREN_C2_like"
                     /note="This group contains class II terpene cyclases,
                     protein prenyltransferases beta subunit, two broadly
                     specific proteinase inhibitors alpha2-macroglobulin (alpha
                     (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and
                     C5 components of vertebrate...; cl08267"
                     /db_xref="CDD:415487"
ORIGIN      
        1 mapmasmahq aplthpaafl arraatalaa avvlgtaaap aayadspsas pkklpdglyg
       61 tkdpkydgvw rqslallaqd tvglrpaasa vrwlvgqqca dgaftafrae pgkpcdgktm
      121 rdtnqtaaav qalaalgghg dtvkkavgwl ksvqnedggw ssmagspsda nstsvvigal
      181 aaagekpqsv tskkggktpy dglltfqlgc dakegergaf tfqlkgaapn adataaaatg
      241 algkgfvvap tdqratapvk alnckdagge kagkgdpaqa aeggdaylva qldkngqhll
      301 sampgaekqp dvgntadavv alaagghgaa aakplkwlek naaewaeqsg paayaqlvla
      361 ahatgtdprs fggtdlvaal natgpkpaaa pkkdagdsdd sadggaisvw wvigvglaig
      421 agigfllssr kknql
//
LOCUS       WP_457679610             175 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679610
VERSION     WP_457679610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19105
     Region          45..172
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 msdaatlrlp wtvaaepags pdaeallrey ytevadryfs lhedrrstpe eieeglaeyp
       61 tadlappggv llvarhgeev agcagvrlld artaelkqmf vrparrglgg agallraaet
      121 aavrlgaerl rldtrldlve avalyrrhgf leidpyhddd pyaeiffekr ldgas
//
LOCUS       WP_457679617             583 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457679617
VERSION     WP_457679617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 583)
  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 583)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..583
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=63776
     Region          112..473
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(118,161,164,223..225,229..230,441,443)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(118,161,164,223..224,229..230,441,443)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 maglrlgpll ryvdadsatv wvetdrpcvv hvrcddgaag aqhtwqvagh hyalvpvtgl
       61 tpgtetpyqv llddepgapp sgsgekvwpl pdsrfpasti rtlpasahep lhfafgscrw
      121 satpsnaahd pvgpdaldtl aatlatgsgr qrpdvllllg dqvyadqtse ataqvlagrr
      181 dlteppwkqv adyeeytyly yeswldpevr wllstvpscm ifddhdvidd wntsaswlar
      241 mratpwwrer ilgglmsywv hqhlgnlspa elaadelyaq vqsvpdatel vrefaagada
      301 daaharwsyr rdfgrvrlvm idtratrvld esnramldkt egewlrqavl dgrgsydhll
      361 lgsslpwllp hlihagegwn aalcagergp rwarrserlr qradlehwsa fpgsftalte
      421 liaeagsgah apatvcvlsg dvhhayvaep hwrgagphpa srvlqltcsp vhnsipgslq
      481 agfrfgwsrs grwlgkllar hgrlprpavk wrrtggpwfg nqlmtltlag raarlaldqt
      541 rrekqggvrl vtvwraaltd arvggesgga ggpeagterp ksg
//
LOCUS       WP_457679623             153 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457679623
VERSION     WP_457679623.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15817
     Region          6..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 msplttflqr stphvlalfr ivigllfach gasslfgvlg gamgqggtvp tgswpgwyaa
       61 viqlaggllv mlglgtraaa fissgsmafa yftahqgsal wpiqnggeas amycwaflll
      121 ffagpgswal drvffgdrgq etapsaqrep saa
//
LOCUS       WP_457679626             217 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457679626
VERSION     WP_457679626.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22110
     Region          13..183
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mleslgslgg tpwvyvivsl sivldvfvpi lpsgvlviaa attaagagta adavggvevt
       61 atvhtgahla eiislvlcaa tasvlgdmva yrlarrggdr fdraigrsrr lstaqerlgt
      121 altrggggiv vlarfapagr svvslgagva hrtvreflpw salaglawas ysvslgyfgg
      181 hwlgtswmst alsvvalfaa gsaaaflirr pdrrtah
//
LOCUS       WP_457679629             190 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679629
VERSION     WP_457679629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19779
     Region          28..171
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtgthashgp hetgdsgsgd pavawrprpe ttadtaavrr ihlaafetag eadlvdalrr
       61 dpsawlpgls yvadapdgtp aahalltrch vdevpavala pcavlpgyqk cgagdavira
      121 lleaaraage rtaivlghpp yyprfgfvpa arfgilppqp wpddafmals lddstpprgt
      181 vryaeafgid
//
LOCUS       WP_457679634             192 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457679634
VERSION     WP_457679634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20045
     Region          17..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mapsstssst psrrpradae rnrtrvldaa relfrtrgde aqmpevaraa gvgigtvyrh
       61 fpsraaliaa vgeqrqaeiv efgrdrclps aaaadglaay lahigevlsa erglsasiea
      121 afgsteptge gragaetvag qllarakeeg tvradaevgd vvmivcglaa virndagdwr
      181 ryvrnacagl rp
//
LOCUS       WP_457679642             183 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457679642
VERSION     WP_457679642.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18256
     Region          41..158
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtsplgtlas sriaiptrpa pslhgydagl lllrlalglt maahgaqklf gwfggpgldg
       61 tgqfftmsgy pagrtmavva gltetlgglg laaglltpla gaavvgtmin alavkwgggf
      121 fapkgveyel lltavaaalt ltgpgrcaid rflpalraar pvhgvvalvl gvvmaagvll
      181 vrk
//
LOCUS       WP_457679648             408 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679648
VERSION     WP_457679648.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43376
     Region          15..406
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrttphprpw lvhdgaltgl kvldlsrils gpfctmvlad lgadvikved tvsgddtraw
       61 gppfqgedaa yfhsvnrnkr giavdlkdpd clrliqelat tadvivenfr pgtaarlglg
      121 yqevrdhnpa vvyasisgyg qtgpyrnepg ydaiaqavsg vmsvtgeptg ppvrfgvspa
      181 dlaagmwaai gilaalrnre htgtgewvdv slldgqvawl syvaggyfas gsvpqrygsa
      241 hpaivpyqaf ptadghlmva agndglwrrf ataiglaglv ddprfatnpd rvrhraellp
      301 lieralsarg akawavllte aeipvgpint vdealrhpqv vargmvtelq htgagtlrti
      361 aspiklsghp atvrtppprh gehtapvlta mgvdprqlae lrarkaak
//
LOCUS       WP_457679645             265 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679645
VERSION     WP_457679645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10158671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27328
     Region          15..199
                     /region_name="crotonase-like"
                     /note="Crotonase/Enoyl-Coenzyme A (CoA) hydratase
                     superfamily. This superfamily contains a diverse set of
                     enzymes including enoyl-CoA hydratase, napthoate synthase,
                     methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA
                     dehydratase, and dienoyl-CoA isomerase; cd06558"
                     /db_xref="CDD:119339"
     Site            order(30,32,64,68..72,111,113..115,137..138,141)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:119339"
     Site            order(70,115)
                     /site_type="active"
                     /note="oxyanion hole (OAH) forming residues [active]"
                     /db_xref="CDD:119339"
     Site            order(95,103,124..127,139..142,148,150..152,154..155,
                     160..161,163..164,166..167,170,181,184,199)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:119339"
ORIGIN      
        1 mtavpapdvi iatfrsgaaa eirigdgsrr nalpgeawar larqvrelga crslrvlvir
       61 ghgdtfcags dmtdwvdads ayveesfahm eeafsaiedc pvpvvaeirg vaagagcqla
      121 lacdlrlmad sarigmpiar lgilaspafa armvaltgps varellytgr lvdartavel
      181 gladhqvpea qltdrtgrlt aavaaqppaa ihaaklavga vlgpqrqata vnprpavars
      241 hfgqaiaafl gkqpaavppd pplap
//
LOCUS       WP_457679669             463 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457679669
VERSION     WP_457679669.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  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 463)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..463
                     /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=49227
     Region          190..439
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtgrsstpep epahgpvrep ahqralraar qalrvlavel gtpteagtpl ldsvrspwlr
       61 rvpyvvafaf avsllpttit vlshdygldg gmsgalataq tvplllavtr plqawwvifa
      121 advigalala gedgvvgraw pwppmeivgy lalmlalslr errrtltavw lttgvaglls
      181 evftpegsns twvlmfvltg vvlmmgatlr ergdaqrkli eqetiseaer arrtlleera
      241 riarelhdvv ahhmsvitvq aasapyrisg ipreaeeefg siaataresl aemrrllgvl
      301 rseeavrhdg pektpqpgia mlpklvegtv ragvpvelal peepvalepa vdlsayrivq
      361 ealanvvrha pgaptrvsvt paadgarltv lvvnsapsap stplettgtg hgligmrerv
      421 rlvdgsldtg plpdggfrva aqlplppppy passlsakds hpa
//
LOCUS       WP_457679672             414 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679672
VERSION     WP_457679672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /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=43696
     Region          31..>282
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msrllttarr grrtligaav avaertpadr draldglral allavptghw liggftldtg
       61 galhnasllt avgglapasw vlqllgiffl vgghasvlsf rratgrgesn wtwlrgrlvr
      121 lgrpvlgvta iwavllplly glgvpeatlr tgatlviqpl wfvgvyavit altpcclraa
      181 rwmgawaaap laaavaavdf lrygpyadam ppwlsllnll pgwmfayqlg vswgerrlgg
      241 raawslllgg aavfaalllf fhypasmvgv pgqdrtnshp psllvlalaa aqsgaavllr
      301 erlarllrrp vlwapvaivn lsaltilcwh qtamlslavp asflgqvpgl tvapdtlgwv
      361 larlawlpvf aaallligrt thrfeapwtg vdgvrraata llaagfgafa lgla
//
LOCUS       WP_457679674             313 aa            linear   BCT 27-JAN-2026
DEFINITION  ACP S-malonyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457679674
VERSION     WP_457679674.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32053
     Region          1..302
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mlvlvapgqg aqtpgfltpw ldlpgvegrl rawsaaidld lvhygtkade eeirdtavaq
       61 pllvasalls arqlfatadd vaaqtgavag hsvgelaaaa lagtltdeaa mtlvrrrgqa
      121 maeaaavtet gmaallggde avviphleql gltpanvnga gqivaagtae qiaalvenkp
      181 egtrrvvplk vagafhthhm apavsalesa taqlavadpr tryvsnkdga qvssgqelvq
      241 rlvgqvanpv rwdlcmetfk elgvttliea apggtltgla kralpgvrtl alktpddlda
      301 artliaeqsa pae
//
LOCUS       WP_457679681             296 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679681
VERSION     WP_457679681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30611
     Region          9..290
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 madntssdtl svavlgtgim gaamarnlar agldvrawnr traraeplaa dgvrvtgtpa
       61 eavdgaevvl tmlldgpavl dalrqaaaal tpgalwlqms tvgtdglapl arfadehrlr
      121 fvdapvlgtk apaekgeltv laagpqdvre ragrvfdvig nttrwvgedg asgpasrlkl
      181 vinswvltvi ngtgealala eglgvdprdf laavaggsld lpylrlksal iladnypasf
      241 tvsaarkdar liteaaqgag vrmdlvaada erfrraeeqg hgqkdavaay fasfdg
//
LOCUS       WP_457679683             348 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679683
VERSION     WP_457679683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36675
     Region          21..338
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
     Site            order(74,85,110,180,182,240,280,306)
                     /site_type="active"
                     /db_xref="CDD:185696"
     Site            order(180,306)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185696"
ORIGIN      
        1 mktqvgrepf gtledgtrvd rwtlesgpgg vrvrvltygg iiqtveapdr dgargqlalg
       61 fadlgsyvah ggsyfgavvg ryanriagas frldgrtwal tpndgrnslh ggsrnfsrvv
      121 wdarevdggv qlhrvspdge egfpgaldvr vtytlspgga lrivfwartd aptvvnltnh
      181 tylnlggdgs gsaaghelrl aasrytpcdd sgipvpgapa evtgtrfdfr tgravggafd
      241 hnfaldggvr haprkvaely dprsgralel attepglqly taghldgtlt gtsgvpygpa
      301 aglaletqhf pdspnrpdfp stvlrpggty rsetvygfsv rprsagnp
//
LOCUS       WP_457679690             433 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679690
VERSION     WP_457679690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45880
     Region          110..>262
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpteagtprg qrrvpralva gaalvlaalt tapalaapaa fttqraesge svhavaaprs
       61 gqgrgtllsl tplgrqslae vigqaqkqgl etgtarhgva ayrltyrtit pdgrpttasg
      121 llalptggds rhlppvvhth gtlayrgyap smadgpdrav svlyasagrv alapdylglg
      181 tspgrhpymd arssvsasld mlraahsaap klgatldrtv svtgfsqggq vamalgrelh
      241 rgadprfrlg mlapvggpyd lvgaelpgmf dgridprsav fylsffltaq nrlhplyndp
      301 aevfrapyad rvedlfdseh paediagklp erledlltdt wyrklrhpsg allealrvnd
      361 rtcdwkpgrg vritlysatg drdvpiantr scarqltghg vrakavdqga dadhyvsflr
      421 sqpsiartlp var
//
LOCUS       WP_457679685             296 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679685
VERSION     WP_457679685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30441
     Region          43..289
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maragqvggt ataprptlpa pssrggqstq tapaaqetqh dgatprqvav vtgagsgigr
       61 avahalnaag wtvvlagrra ealaetsrla gpldpdgpai mtvptdvtrp dqvdalfatv
      121 herfgqldll fnnagtfgra apleelsydd wravvdvnlt gsflcaqaaf ramkaqepqg
      181 griinngsvs ahaprphsva ytatkhamtg ltkslsldgr pygiacgqid ignaatemtg
      241 rmqtgilqan grtavepvmd aadvartvvh maalpltanv qfatvmatnm pyigrg
//
LOCUS       WP_457679693             417 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces nigrescens].
ACCESSION   WP_457679693
VERSION     WP_457679693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..417
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41346
     Region          36..395
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(65..66,69,121,135,137,167,200,356,359,395)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(327,332,347,356..358,361,383,387)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtgqpaaags edqrgaprag atpgrpllpg qpgrpdvftf getmvalrgs gplklggtmn
       61 vsiagaesnv aiglarlghd vrwagavged eagqlvlrtl raegvgvsga stdpgaptgl
      121 llfeprlpev trvhyyrags agsrigadvi qrafsaappr vlhltgitps lsptaraaag
      181 lvlqlsresg slvcldvnfr arlwtaeaaa evlrewipfv dvliasddel plclpgggdg
      241 ggegspggge gvkgttgvng dlgaegadgg larwasepee ataaggagac gdavplppqe
      301 vagdpaatva aqarllldhg vaevvvklga egatafthgg slhqpakpvr avdavgagda
      361 fvagylsall dgegpagrle ravttgafav aspgdwegap traelgmlga ppgtvvr
//
LOCUS       WP_457679706             794 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457679706
VERSION     WP_457679706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..794
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86352
     Region          10..783
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mpwlsrtrlr tagavlaaal igsalavpaa qaeppggplt glvnpfigsq ndgntypgaa
       61 vpfgmvqlsp dtghfagysy dderirgfsa vhlsgvgcgl ggdlpvlptt gditetdyak
      121 yasgyrhdde sarpgyyrvg ltsyggitae ltatartgkq rytfpatdka nvllnagqsl
      181 hktvstrvev ldsrtirtti tgrgfcqdtq pytvhtitrf drpftsygtw dgdkvtagsk
      241 gstaggrhga yarfdtrsdr tveattalsy vdaagaarnl raeggssfdr tkaaadaawe
      301 rrlglvkaqg gdrtlrrtfy sslyrsflap nigsdvdgry tgwdrkthra kgftyyqnws
      361 lwdtyrtqaq llallapges rdmalsvlri dkesgwlpkw gygtvetnim tgdpvtpflt
      421 nayqqgllrg heeeayaalk knadgvppdg spavgreana pylkdgfapy ikgrphpkpg
      481 dsdfdhgasa tleyalsdam laqmardlgh gkdadryaar aqnyrkifdg stgffrarda
      541 qgaftgpadp aksegfhegt swqyqwlvpq dlpgmlrlig grdkaderld affayrklle
      601 dpektarevw vngpydyyna dkynpqnepd liapytylst grpwkttdvv haaltlftdt
      661 ptgmtgnddl gtmsawmvls sigvfpvqpg tdswglstpv fdrvdltldr ryypsghftv
      721 tapgtsaahr yvrsvrldga dhdrtyltte dlrsgrelaf tvgtepsrwg tgehaapppv
      781 gtgsaaqqqs drqr
//
LOCUS       WP_457679717             474 aa            linear   BCT 27-JAN-2026
DEFINITION  lipase maturation factor family protein [Streptomyces nigrescens].
ACCESSION   WP_457679717
VERSION     WP_457679717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Doolittle,M.H. and Peterfy,M.
  TITLE     Mechanisms of lipase maturation
  JOURNAL   Clin Lipidol 5 (1), 71-85 (2010)
   PUBMED   20543905
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10535984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..474
                     /product="lipase maturation factor family protein"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=53665
     Region          121..463
                     /region_name="LMF1"
                     /note="Lipase maturation factor; pfam06762"
                     /db_xref="CDD:462004"
ORIGIN      
        1 mawfsdsgyw lgrlvfqrll avlyvvafla avrqfralig argmlpapay varvpfraap
       61 svfhwhysdr ffalwswggv llaaavaaga adavplwasm vmwavlwvqy lsivnvgqtw
      121 ygfgweslll eagslavflg naetappvti mwllrwllfr vefgaglikm rgdrcwrdlt
      181 clyyhhetqp mpgplswffh hlpkplhrve vaanhvaqla vpvllftpqp iagwaavamv
      241 vtqlwlvvsg nfawlnwvti alalsaaapl waqpsaplpa ppvwfevlvl latagvlals
      301 yrparnllar qqmmntsyes lhlvnsygaf gsitrvrrei vvegtadavt gpdttwlaye
      361 fhgkpgavrr mprqfapyhl rldwlmwfaa lspayarawf vpfvtrllen drdtlrllrg
      421 npfpdlppar irarvfryrf ttwrelrdtg awwhrteere flppvarsal hgrr
//
LOCUS       WP_457679712             393 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Streptomyces nigrescens].
ACCESSION   WP_457679712
VERSION     WP_457679712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=41536
     Region          51..355
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 msaytryaaa allaalavgc tsphpvprpa prptpeptpr ahagapvted agrqsftlva
       61 agsvlpsdpe vlatarrdap hdgydyrpil kgvrpvisaa dlalchldap lgplggpftg
      121 hpvlqappqi atalkatgyd scatashhal drgvpgvqrt lealdtvglr htgsardaae
      181 garpallrap ggarvaqlay tygtgggrrp ayapwtvnll dekriikdar aarrdgadvv
      241 vvspywgtey rtapdarqir laraltaset agrpdidliv gtrahtpqpy ekvngtwvvy
      301 glgdqlsgvt kkprgnwgti arfrfapphr agqrwrvtta eylpqlveqg krvrvrnlat
      361 sgrhdrirts vgtsvgtvvl srgaaadglt rgr
//
LOCUS       WP_457679723             469 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457679723
VERSION     WP_457679723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..469
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49705
     Region          12..463
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mstgtvrddg ttrdgapdap gglqqglkrr hmqlialggv igaglfvgsg vvirsagpaa
       61 vlsflaagvl tvlimrmlae mtvarpalgs fyahvretlg lragftvgwl ywyffvivva
      121 veavaggriv qlwlpgvplw avslvlmtll tatnmvsars ygefeywfss vkilaivvfl
      181 flgalfvlgl wpdspgglgn ltahggfape gvgavlaavv pcigfftgae ivtiaaaesa
      241 eperavadai rsivlrvvaf yvlsvflvvt vvpwtskaie vspyaavldr lavpaagtvm
      301 nalvliavls clnsalytss rmlfaltrng daprgftkvs asgvprrall agtsagylsv
      361 iaawispdvv fqflinsyga valfvylaia vaqvrmrrkl erteperltl kmwlfpwlsr
      421 ltialmavvi gamawlpdsr sqfwlslltv avvlagyelr rrkgpagag
//
LOCUS       WP_457679733             484 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 30 protein [Streptomyces nigrescens].
ACCESSION   WP_457679733
VERSION     WP_457679733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="glycoside hydrolase family 30 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004348 - glucosylceramidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006665 - sphingolipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52968
     Region          30..484
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mrassvrril tgaagavvaa lvvlwsvgpp asgpqqvqvy ltttagaggr qvvkglekqa
       61 pltfapgggg giavdegkky qrfegggasf tdtaawllns sgalsdrara atmkklfdpa
      121 dgiglsfvrn pmgasdlarf gytyddrpag rtdpglqhfs vahdladvlp ltawarrlnp
      181 avtvmaspws apawmkdnrk ldqgwlraky ygvyaryfvk ylqayrdrgv pvdyvsvqne
      241 ptccsgypsm rwngsglayf tkhdllpalr haglstkvlv ldwnwdtyre faaptvddpa
      301 vrrhpnfggv awhgysgevt rqtrlhhryp glaaydtehs ggrwvrnqqr edmrnlidyt
      361 rnwgrswvkw slavdqnggp hhggcgnctg lvtvhrgdgr hgtvdytvey ytmghltkfv
      421 rpgarrigst asaalpnvaw rnpdgsrali vyndtgrtrr tginwhgqhv tyalpagasa
      481 tftw
//
LOCUS       WP_457679739             302 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679739
VERSION     WP_457679739.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30644
     Region          4..300
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(41..43,46,122,126,147..152,171..172,174,187,
                     210..211,232..233,252..253)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mstaitysey ggpevltlsr valpepgpgq vrirvratav npidlrirag mmqgvfpvaf
       61 pavpgwdvag vvdkagegaa aavgdevfgv asaggysqya vldrpfakpa evsfetaaam
      121 itvgeaacra vehlgvrpgq tllihgaggs vggiavqvaa argitvigtt aerdiervng
      181 lgavavpyge gwvervmava pggvdcvfdt sgagvladsv alagdagkvi tiadpsfarh
      241 gvrftgmdpa drfhealpql agliatgkld vpvghvypla eaarahadie arrnqgkvvl
      301 lp
//
LOCUS       WP_457679742             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457679742
VERSION     WP_457679742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22261
     Region          16..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpqqplhrrq ptpgnprvqr trnrvltvar ellpqvgptg ltyallaera dvtrqtlyrh
       61 wpnraallfd lilegpdlgn yptpgsdvrt vatdwlkslr dgisepairt avlavtaqad
      121 hdadsaqalv rigqdrhaal nkllepsgvq iddaeftlly gpvlarlfld rshptdefid
      181 tvvtqwlttl eaqqrpgtpn as
//
LOCUS       WP_457679753             299 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457679753
VERSION     WP_457679753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31066
     Region          18..293
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtptaldaaa rtdttpagpg parrtlavfa rnklaltgal vllalcafcf lgplvhptdq
       61 ihtdlaqagr apgaghplgt tdlgydelgr lmyggrtsle vglaagllat lfgtvygava
      121 gyfggwadav mmrvtdaala ipplfllvvv aaivtpgkpl liliiasvaw lsparlvrge
      181 alalrsrdyi hamrlmgggg gravfrhilp nalgtvivna tfqvadaily vaylsflgls
      241 lpppaadwgs llsagltytq vghwwlifpp glaivltvaa fhcvgdglrd afdvrlkkp
//
LOCUS       WP_457679758             508 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457679758
VERSION     WP_457679758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 508)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53820
     Region          12..494
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 msstpsgsrl rigiggmaie ssqfcphrsg yddfritrer alldrytwtr pdgelsglve
       61 wvplvhavav pggpveravy drikeeltgr ieesgpldgl vydihgamsv vglddaeadl
      121 taavraatgp gtlisaamdl hgnvsrrfae hldlltahrt aphedawetr eraarklver
      181 lvhgrgrphr awvqipvllp gektstrlep arslygrlas vealdgvvda avwvgyawad
      241 earcraavvv taddpelala qagslarayw darrdfvfag ptgdadtcia ravasparpf
      301 lisdsgdnpt aggagdlaym lgrllaheel asgrvtalhp gitdpeavav craagvgaev
      361 tlgvggrfsa gtgphtapyv ltgtvtavde pagpgpgapr gnpaydgggr saavtcggvt
      421 vvlterrkpf htradfgsld playdlvvvk igylepelye maadwllalt pggvdqdllr
      481 lghhrvlrpl ypfddegfed pgltpvll
//
LOCUS       WP_457679766             302 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679766
VERSION     WP_457679766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31658
     Region          1..298
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mdtmrerfas vtsqllaedp rlalvladig aagfaeaekq hpdrvvnvgi reqlligvgg
       61 glaltglrpi mhtfasflve rpfeqvkldl ghqgvggvlv sagasydwps ggfthmapgd
      121 valldtldgw tvhvpghpde aeallrhaaa agddkvyvrl svqtnaapra vdgahfrtvr
      181 egrdgvviav gpmldpvlaa teglsvtvly attvrpfdaa tlraaagaag tsdvvivepy
      241 lagtstrpaa ealedrphrl lglgvgrqel rrygqldehl aahgldprgl reriagfvta
      301 gs
//
LOCUS       WP_457679761             407 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457679761
VERSION     WP_457679761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 407)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44274
     Region          22..407
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(59,66,89..90,97,101,108,241..242,245,249..250,253,
                     286,291..292,295..296,298,321,348..350,353..354,356..358,
                     362)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(66,83,85,88,90..91,173..174,183,240..241,244..245,
                     249,292,295..297,397)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mqnttetgpd apidvtplld dpyaacaalr dagpvhritg adghpawlvt ryddvrrala
       61 dprlsldkry aapggyrgfa lppaldanll nmdppdhtrv rrlvvkaftp grvealrapv
      121 rriadellda maergradli adyagplpia vicdllgiph rdrrdflaws dalitpdpsr
      181 pelmkqaiga mlefytglia akraepgddl lsdliavrdd aaagedgdrl tedeltslaf
      241 lilfagyent vhlignavla lldhpdqlrq lqrnpaelpt aveeflrfdg psplsirrfp
      301 kedmeiggvr ipagesvlls iasanrdpar fpapdtldrg rdlsghlamg hgihyclgap
      361 larleavtal dallgrfpel rlgvprgelr hrralrargl islpvtw
//
LOCUS       WP_457679775             394 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679775
VERSION     WP_457679775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41992
     Region          4..378
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mpttpapria vigagpggla carvlqrhgi gvtvydrdas adardqggtl dlhadsgqia
       61 lqeagllddf halarpegqa mrmltrhgev lvdyrptdae daapeidrgr lrtllanslt
      121 pgtvrwghtl tsvtphpagt hrltfdngvt rdvdlvigad gawsrvrplv saatpvhtgv
      181 tflearfdkv dtehpavael vgdgqvfatg dhkgliaqrn seqhvrayia lrddedryra
      241 agnglddtea vraallrafa gwderllvli tdndgpyvnr plfvlpapht wphtpgvtll
      301 gdaahlmtpl ggnganfalr dgcelalala rhdtldeavt ayertmlpra aaagdgaaal
      361 ksllgpgdrg radvpdfaee keryrqgaaa yrsr
//
LOCUS       WP_457679780             391 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457679780
VERSION     WP_457679780.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42741
     Region          93..340
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mtgsrprrtr lsalrpasfg ieptgerlar mrrspqfvdg qfrnpmptrq llhgsalpma
       61 rtqlsregrl rrapvgripv yrptaadwgq ppasglrltw mghssvlaei dgqrvlfdpv
      121 wgercspftw igpqrlhpvp laldeldpvd avvishdhyd hldmstvqgl agtgaafvvp
      181 lgigadlefw gvpadritel dwhestrvgg ltltatpaqh fcgrglrgpq htlwsswvva
      241 gpehrifhsg dtgyfsgfae iaaahgpfda tmiqigaysd fwpdihmtpe egvrshldlq
      301 ggeprgvllp ihwgtfnlap hpwadpaert laagrasrvt tahprpgepf epaepaavyp
      361 wwraiavppi hgwpawppav sptdvglaad r
//
LOCUS       WP_457679782             468 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679782
VERSION     WP_457679782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..468
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49293
     Region          16..357
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 maehsngght aiviggglag mlavtaltgh vdtvtvierd rypegrafrk gvpqarhlhi
       61 llrggslale ellpgtvaal geagarrlyl srdlltrtpt gwqrrfderr hltlsvtrpv
      121 ldsvvrervl raaagsatrv evleateatg ltgdagrvtg vrvrsrdgap ggrserelpa
      181 alvvdasgrg srapqwfaal grsapqeetv dagiayatrm yrpkdpatap dagvnvpgwp
      241 ecprgaayvp vedgkwlltl sgvrghhppt daaeftafsa tvgdpyvhel ldraeplsav
      301 hgfrdtcnrr rhferpgalp egflvlgdag ctfnpvygqg msvaalgala vrttladggg
      361 lrpgiaaeaq ravaravepa wlaavgadrp yaspgdtkag vgerlstwyi arlsarasid
      421 pvvgaafrdv fsltapparl vapqiflrtv flprrpglpg ppaaieal
//
LOCUS       WP_457679790             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457679790
VERSION     WP_457679790.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33997
     Region          44..306
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 msetthdsav amsappssde gltpaqraqk yglsqsgarp glpayvrqlw drrhfisafa
       61 sakmtaqysq aklgqvwqva tpllnalvyy lifglligtr ngvpdfvpfl vtgvfiftft
      121 qssvmagtks isgnlglvra lhfpraclpi sfclmqlqql vfsmgvllvi llgfgqlptw
      181 swllvipala lqfvfntgla mvmarlgskt pdlaqlmpfi mrtwmyasgv mfsidlilkd
      241 khvpafvewl lnanpaavyi dlmrfalids ftanklpphv wayaggwall mgvvgfvyfw
      301 kaeerygrg
//
LOCUS       WP_457679793             256 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679793
VERSION     WP_457679793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26401
     Region          5..248
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mepglkthvs dgtatvtisn tgkrnamtvq mwrdlpplle rladdravrs lvltgeggtf
       61 cagadigalr egaaesqgla vaaeealaaf pgptlaairg ycvgggaqla aacdlrfaee
      121 galfgvtpak lavaypasat rrlvrlvgls aakyllfsge lidcaralrt glvdevlaeg
      181 algkrvaefs avlasrsllt qtaakelang twdvppaeae ergaywaaqa rasgdtaega
      241 aaflerrapr ftwptg
//
LOCUS       WP_457679801             346 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679801
VERSION     WP_457679801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=36179
     Region          9..330
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mtsntesldi rvvgggvigl tsaialaedg hrvrvlsrda agdttsavag glcwpyriqp
       61 yeravewsvr sfqvlaalag rpeetgarmv tgtmtattgg grgasgkagd gaedglaawy
      121 davpglrrar aeelpeghas gwrartplvd mpshlryler rltaaggave rcevtsleea
      181 gaaadmvvnc sglgaralvp dpevhpvqgq lvivenpgie ewyvsadaga sdttyllpqp
      241 yglvlggtaq enawsrepdp avaeaivarc arrfpelara rvlahkvglr parpavrlaa
      301 erlsggvpcv hnyghggggv tvawgcadev lrmvravqee rgpvrg
//
LOCUS       WP_457679851             271 aa            linear   BCT 27-JAN-2026
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457679851
VERSION     WP_457679851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Edwin,R.K., Challa,N., Sharma,R., Satyamoorthy,K., Parsa,K. and
            Misra,P.
  TITLE     PIMT/TGS1: An evolving metabolic molecular switch with conserved
            methyl transferase activity
  JOURNAL   Drug Discov Today 27 (8), 2386-2393 (2022)
   PUBMED   35462043
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Furuchi,T., Sakurako,K., Katane,M., Sekine,M. and Homma,H.
  TITLE     The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase
            (PIMT) in intracellular signal transduction
  JOURNAL   Chem Biodivers 7 (6), 1337-1348 (2010)
   PUBMED   20564550
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="protein-L-isoaspartate O-methyltransferase
                     family protein"
                     /EC_number="2.1.1.77"
                     /GO_function="GO:0004719 - protein-L-isoaspartate
                     (D-aspartate) O-methyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0030091 - protein repair [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=28349
     Region          <12..147
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mstemdltas vleeldlrpg rrvldvgtga gvtaavachv cgdttvvtld rdpnvavaaq
       61 arigvlgfrp avvsgtgesg wpegapydri fvsfalpsap ealvdqlgsg gvllmhittd
      121 spswpalavv srgpdgriss hlravefahr aahgrkqvfl spafreriaa rrteggaevr
      181 rfrssevppl eeargfwlal dalhsglvqh rgvndlviga pncgswmags pdgsgawavm
      241 prwpaghldr gppdspalag rrragglpar s
//
LOCUS       WP_457679864             363 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679864
VERSION     WP_457679864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..363
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40471
     Region          <123..363
                     /region_name="COG2374"
                     /note="Predicted extracellular nuclease [General function
                     prediction only]"
                     /db_xref="CDD:441941"
ORIGIN      
        1 msiriatfnc enlfrrpivf grgndpirda vledfrklve ildhdtytan drtkiiellk
       61 khsvdvsqei stqtilmnep rgrarllqge grnievraea tgrsawvgwa elvkddlswd
      121 avkntarvia evnadilltv evedrltlhr fnkqvmagqf eaepypfnml idgndirgid
      181 vglfsrhpit svrshifdkk nsrdifsrdc pefeidvdge plwllgnhfk skrgggggdk
      241 rklqgervaq lyqaalersa hvvvagdlnd tpgspplmfl eatglkdamt hdsyegppgt
      301 hgkctnpsdk idylmfspel fakvdkveve rrgifefgtp fdtvtgpgdq asdhaaivae
      361 ldl
//
LOCUS       WP_457679866             358 aa            linear   BCT 27-JAN-2026
DEFINITION  LmeA family phospholipid-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679866
VERSION     WP_457679866.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Rahlwes,K.C., Osman,S.H. and Morita,Y.S.
  TITLE     Role of LmeA, a Mycobacterial Periplasmic Protein, in Maintaining
            the Mannosyltransferase MptA and Its Product Lipomannan under
            Stress
  JOURNAL   mSphere 5 (6) (2020)
   PUBMED   33148829
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Rahlwes,K.C., Ha,S.A., Motooka,D., Mayfield,J.A., Baumoel,L.R.,
            Strickland,J.N., Torres-Ocampo,A.P., Nakamura,S. and Morita,Y.S.
  TITLE     The cell envelope-associated phospholipid-binding protein LmeA is
            required for mannan polymerization in mycobacteria
  JOURNAL   J Biol Chem 292 (42), 17407-17417 (2017)
   PUBMED   28855252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10567863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="LmeA family phospholipid-binding protein"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38119
     Region          77..245
                     /region_name="LmeA"
                     /note="LmeA-like phospholipid-binding; pfam11209"
                     /db_xref="CDD:431728"
ORIGIN      
        1 mpsnepsads karvpasraa qddpagdtta anagtdntst vdekehprte rkprrivrrt
       61 akvvvalavv laflalgdrw avlyaenlaa qqvqkalklr aepevhidsf pligevlagn
      121 ighvevnvpd veagpvsvaq vkgtvddiri vgslpssvkg avlsrvrgdv lldfkdlnre
      181 vgasqihlmp gpekntvlag gdvpvgdkqa qirgraqlqr tgdrglrmtv qdtrvvvpgl
      241 ltyvpgkggg lqltapvadk mdkgelqrtt gkhvlpqqmm kghvldtlvd hpsllkptgi
      301 dpsliqglqk lrepkvaqkm efsaqlpdnl pgdirlrdis vtkngiraql tgkdvpvg
//
LOCUS       WP_457679897             380 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457679897
VERSION     WP_457679897.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39680
     Region          10..376
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnssqelprw pqlteddiea avaalrsnrl vglgnstiee feavlaagqg vehavavstg
       61 taavhlalha ldvgpgdevi vpthtfigsa spvvylgarp vfadvtpdth cldpvsvksl
      121 itqrtkaiva vhingiaadm aaltavaaea gvpvvedaaq algteiggrp vggfgdlacv
      181 slfeqkvits ggeggavltn npvhaervrr lrshgegpvs grpgmiwahe vgynyrltsv
      241 qaaigiaqhk rlgemvearr rnaahlsqql agaeglelpv eppgtthafw kyavrvapgg
      301 grrpaadvaa dlrsrgvpvl lrypfplhkq pafaehqgvs lpvaerlsqe llalpshpgl
      361 teghlnhiad evrravavta
//
LOCUS       WP_457679906             200 aa            linear   BCT 27-JAN-2026
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679906
VERSION     WP_457679906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="dTDP-4-dehydrorhamnose 3,5-epimerase family
                     protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /calculated_mol_wt=22026
     Region          2..174
                     /region_name="RfbC"
                     /note="dTDP-4-dehydrorhamnose 3,5-epimerase or related
                     enzyme [Cell wall/membrane/envelope biogenesis]; COG1898"
                     /db_xref="CDD:441502"
ORIGIN      
        1 mrplsvkgaw lsetrafadd rgefqelysg rslsaalgye pgvvqvnrsv srqgvlrgvh
       61 faqvppsqak yvtclsgavl dvvvdirtgs ptyrsweavr lddphrslyv eaglghsfma
      121 ltddavvvyl tsqgyasgre hgvhpldpdl aiawpehiep vlskkdqqap gikemerrgl
      181 lpsydecaaf hrslrerhmv
//
LOCUS       WP_457679887             261 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457679887
VERSION     WP_457679887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26415
     Region          16..260
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mpahvqtsgd gpqpgrlrdr valvtggasg igascaqrla aegavvvvad ldedgatrva
       61 rqitaaggta lprridvtdp dsvtrvvtet atlrdglqia vnsagingpl splaelppad
      121 fdtvmrvnly gvfhamrcql pamtatggvi vnlasiaahs gfrghaayaa akqgvlaltr
      181 taareyaghg irvvsvspgi vdtpmvtslp pgatdgllna vplrrtaqpa evaaliaflv
      241 sddasyvtgs dhvvdggyla k
//
LOCUS       WP_457679909             410 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS aminotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679909
VERSION     WP_457679909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089755
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="DegT/DnrJ/EryC1/StrS aminotransferase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43414
     Region          13..401
                     /region_name="AHBA_syn"
                     /note="3-amino-5-hydroxybenzoic acid synthase family
                     (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate
                     (PLP)-dependent aspartate aminotransferase superfamily
                     (fold I). The members of this CD are involved in various
                     biosynthetic pathways for secondary...; cd00616"
                     /db_xref="CDD:99740"
     Site            order(62..63,158,161,182,186..187,319)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99740"
     Site            order(62..63,87,158,161,182,187)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99740"
     Site            187
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99740"
ORIGIN      
        1 mpgpgyrffg deeranvmav ldrwyanrea fddpgegewv rrferaaaer fgaahclgvn
       61 sgtsalvaal vglgigpgde vivpgymfva siaavlhcga dvvlaevdes ltldpadvra
      121 ritprtraim pvhmlgapad mtalrdladk hglqlledca qsaggsyrgr plgtlgsaga
      181 fslnhykvit slqggfllsd aplvfqrays fhdqgwfpyr qdrgegdlll gmnlglgelh
      241 aavalaqlnk ldlilgrird vkrrlveaig elpgvrgrtl hdpagecgtv avyvfedagh
      301 aqevadrlgt rtlldspthy yaglpaltaf gcgdrstvpf rapggrpthp fepgalprtd
      361 svlarslala tgvsdgylgp gtgvhadssn aeidhaadtf rravkgealp
//
LOCUS       WP_457679914             214 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457679914
VERSION     WP_457679914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24108
     Region          2..191
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mirtlfvdag gvlynninee tdflervadr yganraeiar rveasapeye sgrrhvhqvl
       61 arlvadghrp padtptetrw ldhaylgsvr pyhdsfralr elrqerpevt vvltnneaeh
      121 wdrlkdetyg hfalfdmlcs swrvgrvkpa lsfftaalhg crataaetll iddratvlrv
      181 gaelgmhtlh vstpevfahr igrtvrgdvl psmp
//
LOCUS       WP_457679916             330 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679916
VERSION     WP_457679916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35707
     Region          38..231
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtgtttgrer aahaaqtaav aaeifrrhgv dfasarraag wtnatwlggg lavrvagsta
       61 aqdlvretrl arllppevgy ptvldsgttr gcewvvtqei patsldeawp tldgdqrvta
      121 trqlwerara vhrvdpasaa pvartrnpfy aqspdeaedg llrlhtagvl tdteherlsa
      181 aldrhwaals daapvlnhgd lspvnalwdg tdvvslldfe favlapvqld lnelvkmaya
      241 pvqadaqpta eehadrtllq eavadlarpl lstdadidll tgysiqletw glerelakpg
      301 sqaypqwepy rmlvawahtd ggcyapller
//
LOCUS       WP_457679919             555 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457679919
VERSION     WP_457679919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 555)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 555)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 555)
  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 555)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58419
     Region          15..538
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 msaaallgll wlgsqalvpv vvreaidqgl vpgemdavlv wsaallglgv vqaasgtirr
       61 rlsmhnalda gfrtvqlvvg hagrlgagle rcvddgelvs igtsdmttig nafdvvgraf
      121 gavvstllva vvlldqppsl glllivalpa iiltmgytlr plhrrqgayr dlqgeltsrl
      181 tdvvtglrvl rgvggetsfa rsyrersqrv rvagskvaga ealiratqvl lpgllvatvt
      241 wigaraalng svtpgelvaf yayaaflvep laiftdtadr farahvaarr aiavlslpaa
      301 spdtecgrtp lpagghdlvd qrtglvvtpg sflavvappa egvqladrlg gytdgpvrya
      361 glpltelrte qlrehilvvd nhsrlfrgpl rdsldphraa cdddvhaalr vaaaedivea
      421 lpngldteit adgarfsggq rqrlvlarav ladpgilvvv dptsavdaht edrvgrrlra
      481 arqgrttvlv ssspllldha eqvaflhggr vaatgshrdl latsahyrll iqretgedrt
      541 gdtpttsfvt rgpaq
//
LOCUS       WP_457679924             159 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679924
VERSION     WP_457679924.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..159
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17330
     Region          <42..101
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msgqegitpr qrltvaqkld hllnlhakpg ndgkpsyktm aaeiaaqsge tfsaaylwql
       61 hrgertnptl rhlsalaayf gvpvsyftdd dvarsvidee dlarreldrs maeagvsavy
      121 lrgdltalsp egkrmaadmi rqiraleqgt kkppsppra
//
LOCUS       WP_457679936             424 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457679936
VERSION     WP_457679936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43740
     Region          32..405
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(42..43,46..47,50,82,131..132,134..136,139,159,
                     162..163,166,241,244..245,248..250,253,281,285,335..336,
                     340,344,359,362..363,366..367,370)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mpgkseavtr rtearsgesg egsmfvlsrg vvmlfavacg aavanvyfsq pllvtmghdl
       61 gmspavvgsv vtlthvgygl glfflvplgd vadrrrliva qllllvmala vvaaahtaai
      121 llvgmaatgl lavvtqtlva faaslappag rgrvvglvts gvvigillar tasglmadla
      181 gwrsvylasa sltallalvl yrvlprhsda ppttlrygql lrstitlfar eqllrlralf
      241 gllvfaafst lwssvalpls eapyflphsa igalgligva galaataagr lndrglsrrt
      301 tgialtllav swlplafirs slwalvvgvi lldlavqavh vtnqtliyal hpdagsrlig
      361 gymvfysigs atgaiaatsl ytvagwgavc algatfsclg lvlwaftrhs tpdpaaevas
      421 rset
//
LOCUS       WP_457679948             315 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457679948
VERSION     WP_457679948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34030
     Region          1..296
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdliavrtfv tavdagqfqe aaanlsitpq avskriavle kdlgvqlfsr targarltid
       61 gqaflpyara llqaeeraaa svrpgrralr vdvigrrvsv agllrdfhra hpetdldvvt
      121 lfdsdtaiaa vrsgtidatf ravtmpgrql pdgieatpvy deplhlftgp ahefaaarai
      181 tptqlagrri wmpgnlpgte waayydelaa tfgltidavg pnfgieplld tiaasstlat
      241 fvseqtplvw paghdlrrip lhdptpvyph sliwrtdnph paltalrnhl tsaypsrpdn
      301 gtwtpdwaqg atqps
//
LOCUS       WP_457679954             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457679954
VERSION     WP_457679954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21808
     Region          10..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maetttgrre rkkaqtrqal tdaavrlfte rgfddvgvre vaeaadvsls tlfkhfpske
       61 alvfdldadi esaliaaird rapgqpvlha lrdhmvrtrt avrtddptfl lvestpalrd
      121 yarcmwsrhe kalaatlada tglaaedlav tglarfalev pslarasddp aravrdlfal
      181 lengwatttp larqedgpgq gg
//
LOCUS       WP_457679951             325 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457679951
VERSION     WP_457679951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422978
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..325
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34805
     Region          24..203
                     /region_name="GloB"
                     /note="Glyoxylase or a related metal-dependent hydrolase,
                     beta-lactamase superfamily II [General function prediction
                     only]; COG0491"
                     /db_xref="CDD:440257"
ORIGIN      
        1 msgqpslppw vtwrqrpfpd anllllhgrq palvdsgfvg haedtaawar ahageiglvv
       61 nthwhsdhvg gnallqarga aiaagapeae aisrrdpgcc aaeyldqpva pyavdmsldd
      121 gqvlrlgdtd wevvrtpght pghlalwqpd erllvagdal sdydvgwvnl aldgldaatt
      181 alaslkrmad laprvilpsh gpipadptaa fgtalrraqr lvddpdgavw ygarrifafa
      241 lmirggiasd evepylhara wltdaarlld ltpealatel vaamlrnral vlrdgrlhaa
      301 adhtpvaaes lrvpyprawp atelr
//
LOCUS       WP_457679957             389 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457679957
VERSION     WP_457679957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=42028
     Region          2..387
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 msttpriaia gaglgglvca rvlqqhglpa tvferetapd arsqggtldi hedtgqaalr
       61 taglfdefla lsrpesqewr lydrhatlir hdqadeddls rpeidrgqlr allldslvpg
      121 tvrwghsvra vtplphgtar lhhhnhtted fdlvigadga wsrvrpalsd aqpsyagvtl
      181 veahfddvdh rhpgiarlvg rgtmsakagr rslvlqrnsn ghvrayinfr gpqdwhagvd
      241 ladteavrar llaqyqgwde slldilrdne ggfinrpmfv lpvphtwrrv pgitllgdaa
      301 hlmppagvga nlalldgael aqsvighsti aealdayesv mlpraaenak taqqmlaglm
      361 pdtdsddaaf pdslwpaapl pdsrpahts
//
LOCUS       WP_457679963             210 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457679963
VERSION     WP_457679963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22261
     Region          17..194
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mtgssavgsa ptptsgrrss egfrlgneil afrfvatlge rradpverig tpeqlrawli
       61 anelgsadmp asesllrdar alreaihrag taiasggvpd padeellnrw tarhrarlvl
      121 tggrarwhlp etdsaraala vvaldavatl gghgdgvikr ceqrtcgglf vdtsrgrrrr
      181 wcsmatcgnk vkkanlkaar dgtepgltdg
//
LOCUS       WP_457679971             400 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces nigrescens].
ACCESSION   WP_457679971
VERSION     WP_457679971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42076
     Region          10..343
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(29,31,62,104,230,303,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(29,31,62,104,106,113,178,181,183,230,237,303,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(31,106,178,181,183,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            183
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mthtpaisrl feparlgalh lpnrlvmapl trnragvdgv pqpimttyya qrasagliia
       61 eaatpnavgq typhipaiyn erhvagwrhv teavraaggr mflqlqhggr vghpdnsglv
      121 pvapspvplp etihtpdgrq davvpremtl ddirstvadf ataarnalda gfagvevhaa
      181 nghllhqfms qgtnrrtday ggsvtgrirv avevtqavae aigpdrvglr ispgntingi
      241 degdtgniyp aliealsdsg laylhlvfad pdqplfhdlr kswpgtlian palgwgaplp
      301 adggmqager lltagadlia lgraflanpd lverlrigap lnpvrdqhmm yvggetgytd
      361 ypvlaavqhr aetqpgsepa yahahtpasn papapapagp
//
LOCUS       WP_457679967             806 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457679967
VERSION     WP_457679967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=88896
     Region          11..806
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mspppsrral lgtglagaav altgtlpagt asaqplrtqw kedegqrysv pglkkpvrvt
       61 vdvwgvphif adnvgdlfqa qgfnvarerl fqidtwrrrg lgrfsevlga syveqdraar
      121 lflyrgdmaa ewasygpear eaatrfvagi ngyidwlgdh pdalpaefqk lgyrparwsp
      181 edvvrirthg iggnlssqva rarlmsvggn kastyfhkle pdhmvqvpeg ldlslipadv
      241 lgvyslatsp mvfadgklrr mpdgrnvlre satgsnawav aatrtatgrp ilagdphred
      301 ytlpanryia hlsapglnii gagepwnpgi smghngmvaf gltnlpagqa dlyvyeldpd
      361 dhsryryrdr weklttvtek iavaggeprq aqlsftrhgp vvkideknhk ayavrtvwte
      421 pgtspylgsl nfqrvkdsre fveaisrwkt pganlvyadt kgdigwapga lipkrsgrgy
      481 dgllpvpgdg rfewdgfydn aqlptsrnpr sgffvsanef nfppgypipt ydwqpayrkd
      541 rihevlsqqr gtsiadtlal qndvksgvag qflpyvkklr stdpttakal rllssydgva
      601 skdsaaaalf etwmmrflyp awaqlllpkp aadylvgisi efdlrvmnds firpddwfga
      661 dgarkrdell lstlpkayte vasklgader awrwgamhih vflhplggpn vgpterggsf
      721 dtvsvsyfhh ldhpyaevvg atfkmaldvg awdnsrvina pgqsgdqrsk hykdlqdkws
      781 ageyfpllys eqaiernggt rillqp
//
LOCUS       WP_457679974             253 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457679974
VERSION     WP_457679974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27980
     Region          3..104
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,79,83,89,93,96..97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          150..247
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mawpiaevar msgvtartlr hydeigllpp arigsnghry yeerellrlq qilvlralgl
       61 glseigrvla aqvdelealr ghhrrllaer drldalagtv srtiteleqs rkdgrpmtsi
      121 nrpenlfegv epaqygeslr afpelagdie rrtsamseae ieaghrkrta qmirlaella
      181 agtpadavpa qaeidaqyra laelravsaq eyraigracv dneqwraaye tiapglaeyq
      241 rdaieayaat rls
//
LOCUS       WP_457679984             190 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Thermovibrio sp.].
ACCESSION   WP_457679984
VERSION     WP_457679984.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rosinski,J.A. 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 190)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13297907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     Protein         1..190
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21521
     Region          <61..181
                     /region_name="PRK10403"
                     /note="nitrate/nitrite response regulator protein NarP"
                     /db_xref="CDD:182431"
     Region          <127..180
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 meicvfvkly nrilevslvn flqklkveta lkpesssvav vdkvsllelp ysnlsaqgvk
       61 fllidlgede eelhflvkny pisgviypem epellkkcis tvakgekwfk rdflvslske
      121 gisvstfser evevigllik gktnkeiara lglteqtvky yinqllkktg lsnrvelvkl
      181 fskvykyvkr
//
LOCUS       WP_457680025             310 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680025
VERSION     WP_457680025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35247
     Region          40..101
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(45,49,74)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(48,73)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(55..56,67,70,74..75)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          125..302
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mdviqrasda eetgeggqka rdrvlflrde lapsapcmvl ggelrekreg lglhqqdvsk
       61 algwskskvs rieggrnavk eqdlecllsl yrvdekdqep lrelaligkr pmwwkpwsgi
      121 ttaylqavls feevaqrirs yeplylhglv qipeyaqali grgpdqghha alaelrqmrq
      181 akfaaahgke licvideasl rrpvgnaqim rrqlqhlmdl nedpryqlrl aelnrpnlpl
      241 evgsttifdf aeallptiay setfdgglvi qdeesvdrrv kkfdelrhms lnprkttqkl
      301 hdllrskyyr
//
LOCUS       WP_457680072             196 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680072
VERSION     WP_457680072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21721
     Region          17..85
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 mhhtknetpr tlgdltwhdd aacrstapqq vdpddffpep demdriraak alceqcpvln
       61 tcldaaleng dhdgirggmt eeeraplhrn frrrlsyarv navlaghdvh lthaerdavv
      121 caayldgipa eqlarilkit kqhaqkryre trrqirdraa dpkeqagnge ktptsepavl
      181 kasrtkpscd dlgtaa
//
LOCUS       WP_457680083             462 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680083
VERSION     WP_457680083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..462
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=51020
     Region          32..94
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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          114..276
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 maarrraesd dtaakkgtsr apvgvagqym gfggmlkrwr kaagvnqivl aralgigert
       61 yrniergatp rfsqpqcdal adllkldade rhalllynvg tylrastadg rpelgpalrl
      121 lidrqmpspt ylsdrnwnil aynkamaelw pwvmeprani irwalttpeg ratyhdwhkh
      181 aavfvrmlrf altthggdtd lqelisdvkk npeiqkiwda dadlvehrdg hvflasvptl
      241 gwktieivsh vaypaimpdc rfvvmtwvea epdaqrdalg gprnawaeet hntahersra
      301 qariaeadrl rdmdlhtarl vvdsaekaaa kagkdgiplp alsrlmgpts qltlspstrn
      361 vvwaveeapg ewgvsqvsps tliarvppaa ihgdaraelk rltrialpaa peaaadrvqq
      421 llseldqqqs llreiqrdle ghrsalrtpq giarevqael vs
//
LOCUS       WP_457680085             135 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457680085
VERSION     WP_457680085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..135
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15484
     Region          4..135
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mhqytyacpl rwsdadaygh vnnaqflrym eeartrmfqe vvatneeghr pnafvvsrti
       61 idyraplfyg pepvdvhvwv tkasaatfel ayairdaeql yveattkiva ynldtgaprr
      121 lseterafva rytkr
//
LOCUS       WP_457680101             241 aa            linear   BCT 27-JAN-2026
DEFINITION  2'-5' RNA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680101
VERSION     WP_457680101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26748
     Region          42..209
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 miarhewaal grvnemvnhw drpgwttstr ayywmitfpg aaaliqraqk cqqalrslvf
       61 ddipedglhl tlgrigpste islaqldslm asvqvavssf slqavpltas rgairfsvap
      121 wtplidlrim lakagasvgl plrkptsgfr phigisycnr lvpadsvrdv vrplraleta
      181 etevrqvhiv elrrepsayr wevvrtldlp taplrrnegt ragqardglh afehgdhrrl
      241 p
//
LOCUS       WP_457680104              85 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457680104
VERSION     WP_457680104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 85)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..85
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=8796
     Region          <3..46
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 miigdsledv rtglvggasv lgvtsgktsa qdlkeagakv vldslenvah rrpssgeqqs
       61 cqphtprvyt adhdaepcra gdlrl
//
LOCUS       WP_457680109             398 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457680109
VERSION     WP_457680109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  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 398)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43428
     Region          17..376
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mpgtvfvsld dftregftng lflqvrellq rvisrghpas lvciaqhtnp gierrtrtvq
       61 gctvhetlig apgqasvyrq alrdllkdld pdvillnsca vrlneahrav ldeclasgrh
      121 vavlvtdqly ptshdhpgde vrhyydlmrq asvhavsqti adafhsqtgv paqvlpnllp
      181 errvslapvg nagrfltlin hhpikgrrvw dalvrqrpgd aylvvetwpd vppyappspn
      241 vqvasfspdp ttiynrtril lvpslgpegl prvaleames gvpvvahrig slpelgsaak
      301 fvspppiagy elegnvlypl vspndvkraa rdfgqtidai dhdpalrarl vangkalvrd
      361 yrshseavig rlldvwcgwr dsgrsgardd lsaarnsr
//
LOCUS       WP_457680111             317 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680111
VERSION     WP_457680111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34693
     Region          19..257
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mkppteqeal kaasrclrqe avtarrismg rshfvftvel ksgesviari trrdraecfa
       61 gfaywrrqla rvgvpvphvl smdltatvlp wpimlleqaa gddlcnvyad ltaaekctva
      121 ddlldirdrv sglppgpgyg giasysdlrc hprwsdvlwe yvtgaidqlt psqrqrpaig
      181 eirrtirelr pefdridplp ylidathqnv lvgrgrvtai vdldelgfgd alyplgvara
      241 gllargpead ciehvaaplc vgpirqrvfd lysaiaslkm lspsplsvtg ppsadskiat
      301 rlwtlldffa aaaahke
//
LOCUS       WP_457680117             560 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457680117
VERSION     WP_457680117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 560)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..560
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=60784
     Region          31..432
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mttdcsgygd dfadwcnglf lrpdgdnadv lvelircald ealshqgagp vyprwdqedg
       61 rspvggghll edpvvsetvl sqlrrwlags vkvhhhmfak nvvpppsfvn laalcavslf
      121 mpngvtgeda aetltaelsc aqamarlagy dpdqagglft fggtatnlya invgiskaqp
      181 dhaergiepg mavvgswpah ysqksacawl gigtrnyisa aslpdqttdm esmeaacrgv
      241 larghrlaci mgaggttsnm avddfdeiaa mrdqlaaeyg ldytphvhad tvvgwaylcf
      301 idydlhrnpl gfsppvvakl srlverlrtv rhadsfgtdf hktgfapyts smiimrdgrd
      361 fsrlrrdggv mtplfhdkda ynpgtftlet srsaanmvat wvglqalgkq gmrkllghal
      421 etaealrrhv davaagdvta inkhsygpdv flrcyppddp aaseedfsdt ssvrrinqyt
      481 sdlfawlsrq rvpeaeqial sktsaafytp agepvvalrv yslnpyfsds harelvarll
      541 kgkrqfdaih pdtdvyegar
//
LOCUS       WP_457680120             216 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457680120
VERSION     WP_457680120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22975
     Region          6..211
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mqrlaifdld ntlvdrqgpl tdwvsafssq yalndhdrah llqvvharay psafetiraq
       61 yglapsaeal wrdycaymar svscpadvle glstlrrtgw kiavatngah eiqtekaams
      121 givdhvdavc aseaagvrkp evamfekaaa scgadialgg wmigdgvdtd irggraaglr
      181 tiwisggksw pgddaepdha ttdvcqaidl llttvs
//
LOCUS       WP_457680149             336 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457680149
VERSION     WP_457680149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37627
     Region          26..313
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdfatkmend krensyvdps agkvsvrrya adwlalkpma agteesyeri mrlhvlpqlg
       61 kktisqvtaa dveelyalwr rqgampntid srrialsgmf shavrhkrir enpvkqaekp
      121 anpimqvder alpsfgeisa lakeigprle pavwlmaccg lrigealgvf pedivdgtlr
      181 cqrqvvrikn ssgkyvalya plkhrkegew rdipapatle plaerlpirn qaggmiypdl
      241 frkswdralk rlglpdynph dlrhkwatvt lsngvpihev srwmghssik itvdryghlt
      301 ldgsdrcrqv ieatfgvhml sgfpaprvpg aelvla
//
LOCUS       WP_457680106             219 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457680106
VERSION     WP_457680106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23691
     Region          5..210
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtqspvelvi fdcdgvlvds ericvkvdam imaelgctft eeeiiekfvg sstevytaav
       61 eeqlgrrlek dwlqqyehly qaafdaelta vdgvaealss lttpvcvasn shhagirrnl
      121 eiaalsdhfe erifsaddvp rgkpapdlfl haarsmgvep ercaviedsa ygvqaaraag
      181 mrafgycggl tpatrlggpg ttlfddmrdl pkllaiarh
//
LOCUS       WP_457680162             187 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680162
VERSION     WP_457680162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19765
     Region          5..175
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mansallvmd iqqdivdivd dgsgylprlr taidgartag ipviyvvigl rpghpevgar
       61 nrvlnaavqa glfaegargt aihpavaprq ddivvtkrra safsgsdldv vlrargidsl
      121 vltglstsgv vlhtlcqand qdfgltvlad acldtdpevh rvlterlfpq wadvvavedw
      181 lkaiapq
//
LOCUS       WP_457680159             410 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680159
VERSION     WP_457680159.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40978
     Region          23..389
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,150,
                     153..154,157,225,228..229,232..234,237,265,269,318..319,
                     323,327,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 maangipddl tapiphpglr rarwsvavvf lihgsvtgnf atripwiqdh talspgqlgl
       61 alafpaigas lamplagris hrfgartalr gllalwtlsl vlpalspgly alcpallmyg
      121 aasgmsdvam nalgvetenr lgkpimsglh gmwsagallg saagtvaaha gwdarlhlag
      181 aalvltllga lacrgvldlr sapeehpppr falpprsalv igaigfcavf aegagldwsa
      241 vylrdelgtd aglaaastta factmtvarl agdkvvarfg avrtvraggv laaagglliv
      301 aarhpamamg gfglmglgia vvvplafaaa grsgpapsqa iagvatityt sgliapsaig
      361 glaqatslpv sfmlvttlac glvvgarvlr vpsrtasgsa pavtgdlers
//
LOCUS       WP_457680157             448 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680157
VERSION     WP_457680157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
REFERENCE   3  (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   4  (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   5  (residues 1 to 448)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..448
                     /product="ROK family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44005
     Region          22..97
                     /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(22..23,37..39,48..51,53..54,57..58,60..61,74..76,
                     81..83)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(37,40,90)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          86..430
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mhppraaaag rtaspttarl indrlalqll qsegpltagq lksltglsrp tvadlverlq
       61 eaglitvvge sgaqrrgpna rlygivadra hlvgldlrth svtvavadll grvraehtvl
      121 idpdgapdta vatalaavdk alaaagahap htiavgapgl vdpatgrfgg tdwipswhvg
      181 lvgalrartg vpvllenevn laaiaeqrdg aahdrdtfvl lwlgqgtgaa vvldgtlrrg
      241 asggtgeigf lpvpgtgalp sasgcdggfh slagsaaica laaehgmpyg aavdpkgada
      301 sspgtgvhel ssgtganepp sgtgapteas ptealpaesl vrsavaagda gaafldalaa
      361 rialgvaavc avldpgcvvl ggeigrggga aladrvaghl arlsplrtdv ragavggrav
      421 llgavlaard aaqnelfgaa gpgvsprp
//
LOCUS       WP_457680179             732 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457680179
VERSION     WP_457680179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..732
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=79448
     Region          2..710
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrrltrpgpl srpsperlra pgrpgnlpae lnrfigrdde laalarhles arlvtltglg
       61 gvgksrlagh gaailqdrfc dgvwlvelss lrephlldht vaealapadh sgrpvrtalc
      121 dhlagrelll ildgyehlvd acadltaell rrapglrvla agrrplgltg eqnvalapln
      181 tadatalftd raaavlggft vgaaneaavt elcerldgip lalelaagrl ralsvdqvlh
      241 rlddrfrllt gtargalprh qtlrtaigws helctpeerl lwarlsvfag qfdleaveyv
      301 csgpelpage lldviaelva qsvlvreeta agvryrmldt vraygagwla atpdgdrlrr
      361 rhrdwylgla twceldwfss rqaeiaarie aelpnlrval eqslecpadt hlgqylagtl
      421 wfywvgcgrl segrhwldra lelesdhdda rlkalwvagy vavlqgdtvg algalqecrd
      481 eaertgnata aayalhrtgc lalvcddmpr aeellrgalr ryreigelns nallgqvela
      541 mavafrgepa davrlcedvl evcedhgerw trayaqfvla yaswsrgdge rartlleesl
      601 avhhafhdll gvvlaiella mvtlgegdae eaavlqgaag riwpsvglpl fgsryfrrph
      661 alceeqarqr lgaehygral rtgerlglda tvarvlrpag pvpaphrtvr ivppdtnepa
      721 aspsasgget ag
//
LOCUS       WP_457680187             424 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680187
VERSION     WP_457680187.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45578
     Region          6..55
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(6,31)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(13..14,25,28,32..33)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mlslvrrlas lrqedmaqmt glsqsalsml engtrplthi dkitrlldgl avppelvrlp
       61 lartatalra vegdgsaapt leeippyewe spltvakrmn atltsntdpe tvkvlqrsve
      121 divaryearg phrmapeaed lrryvqelle grqpprqqea lfrlaaqasg llgymavnag
      181 rdslaeayca eaeklasaig aqdllmwiag trslnayylg dfataagwad agidlapghp
      241 qairllangr aralgktgdr kgveralaea eeltvrhplp ggltscisfa pyspartlan
      301 aatahlalgd tqrvlecagr iddlversds awsralvrld vatallngts pdvehamtig
      361 qqvlaagsgp pirsvvqrvg elnaltahwr dqpavrefae alqtwratpq nqlisnvcdd
      421 dtvv
//
LOCUS       WP_457680223             450 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457680223
VERSION     WP_457680223.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..450
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46322
     Region          6..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(6,30..31,59,64,69..72,84)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(13..14,16..19,21,34,36,67,83..86,90,92,128,130,
                     132..133,135,145..146,149,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(13..14,16..19,21,34,36,67,83..86,90,130,132..133,
                     135,145..146)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(17,90,92,128,130,132,149,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(145..153,164..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mliagryrlq dvvgrgavge vwrafdeslg rpvavklllp qgsdpsaasr frleaqtagc
       61 lnhphvvgvl dfgehedrlf lvmelvegds larlagsgpl laervaliaa qaaaglaaah
      121 rqnivhrdik panllldthg alkigdfgia rfvddpgaal tatgqivgts lylaperalg
      181 rpagpasdvy algcvlyqll tgrppfqadt alailhqhld aspvpprqlg aslppafesy
      241 llgllakqpe drptadqaad wfgrgawrga peplpqelpn qgrrpapsav rgphitgpgt
      301 avpgtpipgt avpapsvgsv ggvsvraaet ewkttvhraa phrprlpltr rsrlvallgg
      361 aalfsvalla gltwfspdtg taqvpqaeps alvnpslsps passgtapss sptpspsssa
      421 aqtadkktaa padpnkspka agkhggkgkh
//
LOCUS       WP_457680246             566 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680246
VERSION     WP_457680246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..566
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=61501
     Region          274..564
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mattsgttgr sprtswgreh lanlyslfvl smimndapde sdvltralta vgtlgpcrae
       61 aayltldngl trtpadwpda tphldaqvrr lggqggpvtv pdrewgwsla lrstadaigh
      121 lvvsapsrpt ddeyfllrvl aqqtaaaltq amarrterdr eqqlrqlsdd raatnarltt
      181 svselehqrs vhemltdasa nddgvqgiae alhrltgypv aiedrfgnlr awagpgrpdp
      241 ypkpeatphe ellqdaarrq rpvrvaeqvi alaqhrgevl gtvalidpea gageeerfal
      301 dyastalale lahlrnlaev elrlrrelvd dlitgtddas ayaraaavgh dlhgphylaa
      361 vqwtgrpadd tfvqavgrsa aglrmrslla rrsgmavlvl qgrpqakalh eavgrelgsp
      421 tgsigvggrc dtpseiprsf qealralevr qrsqsphgat tfdelglyri lgpgggyrev
      481 eqfvrewlgp lldydaahhs dlvqtlsqyf ecggnydata aalaihrstl ryrlqrirev
      541 sgsdlgdvds rlnlhvatrv wkvlgg
//
LOCUS       WP_457680257             219 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457680257
VERSION     WP_457680257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23927
     Region          1..213
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mriviaeddp llreglalll raesldvvat agapdealda idahrpdvai fdvrmpptht
       61 degivaavea rrrqhglavl vlsayveqtf atelltggvg glgyllkerv grveefldvl
      121 rrvaaggtai dpevitqlft rsrqdtrldr lsprerdvlv lmaeglgnna iaerlvvtds
      181 avhkhirsif aklglspthr ldrrvaavlh yledarrra
//
LOCUS       WP_457680254             453 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680254
VERSION     WP_457680254.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..453
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=50376
     Region          77..444
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(90,118,293..294,320)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 mvrhrkrisr rgllvtavia tgavlapvav qavqaapadt vggkqnpvra leqaahplrs
       61 tepgrstadl ralgsmigda kvvglgeath gshefftmke rvfrylveek gfttfalels
      121 wsaglqiddy lqtgkgdark vaeemltntp wdheefvsli ewmrdynrrh pgrtvhfmgd
      181 digapavsde ffgrvtgyvr qnhpealprl nelytglrpi ddvfaylgkp laqrqqlatk
      241 aqqaleliss qkgsggeafe waeqnarsia qtakfltmnp ddpgtlpsfq rfrdevmaqn
      301 vtwwqqrtgh killsaqndh vghvagysel ypktqgsflr dtmgknylpi gftfnqgsfl
      361 skdaalggdw kkftvdgaep grnehtldqv ryrdfyldvr napaparawl nvarptlgvg
      421 tqfpvkprdv aiaksfdvli hlhevreadk rmp
//
LOCUS       WP_457680282             605 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680282
VERSION     WP_457680282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=62160
     Region          392..597
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(399,440,486,579,582)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(399,579,582)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(399,440,486)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mrvrrwgtal tllltttalp atgpgtataa pagpaqsphr plplarhfdn ravsdnsapg
       61 aadfdgagrs lsaqdlaaag wspgsvltld gtrlglprta pgapdnvvad gqavavhgrg
      121 ealtflvagt ggtaagtgtv hyrdgsrssy eltapdwrsg plstkavalp hlntpggpsd
      181 esarlyavtv plpagrevas vvlptadgaa galhvfavav rdsgrrtgsw aastagyrav
      241 gpwtdrtlrl vvhsgaggpr arirlantfa atpvdigaas iavrgagaaa drapvpltfg
      301 rghtgtriaa gaeafsdpvd ftvpagadll vsihlpgtvt aapvhqeaaq lsylsaagsg
      361 drtadaggta ypetltvwpf ltgveveggp gsivalgdsi tdgvkstsgt nrrwpdvlar
      421 rfqtqqalpr ygvlnhgisa nrivtdryqg dgvstdtggv saqhrlerdv laqpsartvv
      481 vfegindvrw gtssdeviag lralarrahe rglrvvvati apcegyhdct pavearrqav
      541 nafvranaga vfdatldfda virdpqrpqr mlpaydsgdh lhpgdaglka lgesvdlrkl
      601 lpgrh
//
LOCUS       WP_457680276             145 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457680276
VERSION     WP_457680276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15719
     Region          2..117
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mernlsfnlh vltarldraa nrtlqaehnv sysrflalsl vrelgtptqr aladclgvte
       61 psvsrmtaal aaeglldaqp dpaggrrrrl sltekgvrlv tsaqqgfeer laalvarsgv
      121 pydeyaehta rllaafedle rggtm
//
LOCUS       WP_457680289             643 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457680289
VERSION     WP_457680289.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..643
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=68862
     Region          82..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msqffrpkrm mvgrpldsar lgetllpkrt alpifcsdpl ssvayateei llvvglggia
       61 llhltwyaaa aivlvlvvvv asyrqtcyay psgggayrvs aqnlgrsaal taasallvdy
      121 vltvavsvvs gvaaitsaip slgghdvals vgfvallalm nlrgvresgr vfavptygfv
      181 ffiylmfafa avrmatgahi raesadlplh avspytglal vllgmrafas gctaltgvea
      241 isngvpafrr pksrnaattl lvmgffsvtm fggitilaml ydvrvavqpt elglppgtpt
      301 stalaqiara tfgdldtlfy llqaftagvl ilaantafng fpmlasilae dgfvprqlhn
      361 rgdrlvfsng iillalaaig liilfdaelt rliqlyiigv fvsftlsqtg mvrhwrtvla
      421 apglpsrera rhrrsqaina vgavltgvvl iivlitkflh gawivviamp llflgmraih
      481 qhygrlerel avapgarpwe pagnhvrvlv nslhaptlka lgyaramrpt slealtvave
      541 pgdvrelraq wdahdidvpl qvlsspyrdf tgpvidyild vcarypggav tvvipeyvvg
      601 rwweqplhnq salrlkarll ftpgvtvvnv pyrlpsgkep gea
//
LOCUS       WP_457680303             355 aa            linear   BCT 27-JAN-2026
DEFINITION  lipoate--protein ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680303
VERSION     WP_457680303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kim,D.J., Kim,K.H., Lee,H.H., Lee,S.J., Ha,J.Y., Yoon,H.J. and
            Suh,S.W.
  TITLE     Crystal structure of lipoate-protein ligase A bound with the
            activated intermediate: insights into interaction with lipoyl
            domains
  JOURNAL   J Biol Chem 280 (45), 38081-38089 (2005)
   PUBMED   16141198
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Reche,P.A.
  TITLE     Lipoylating and biotinylating enzymes contain a homologous
            catalytic module
  JOURNAL   Protein Sci 9 (10), 1922-1929 (2000)
   PUBMED   11106165
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Morris,T.W., Reed,K.E. and Cronan,J.E. Jr.
  TITLE     Identification of the gene encoding lipoate-protein ligase A of
            Escherichia coli. Molecular cloning and characterization of the
            lplA gene and gene product
  JOURNAL   J Biol Chem 269 (23), 16091-16100 (1994)
   PUBMED   8206909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="lipoate--protein ligase family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="6.3.1.-"
                     /GO_process="GO:0009107 - lipoate biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /calculated_mol_wt=37739
     Region          106..354
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
ORIGIN      
        1 mqgrhhgeyk vpggklvvvd lavvggvlrg vrvagdffle pdealeaing alegapadaa
       61 ardlaarida alpagaalfg fsseavgiav rravadaaew tdfdwqiiha gpqppalhma
      121 ldevltseva agrrpptlrv wewdrpavii gsfqslrnev dergaerhgv tvvrrisggg
      181 amfvepgnti tyslsvpqsl vqglsvaesy aylddwvlaa lgdmgikawy eplndiatea
      241 gkvagaaqkr fasgagavlh hvtmsydida gkmtevlrig keklsdkgit sarkrvdplr
      301 rqtglpraev iermiasfra ryggsdgvvs daelaraqel aagkfssrew lgrvp
//
LOCUS       WP_457680327             381 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680327
VERSION     WP_457680327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39647
     Region          35..330
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mssrredppp agpavvpaal dplagvradg dpptdvyltg tvfldiiftg ldsapvrgte
       61 swargmgssp ggvanmatal arlglrtsla aafgddhyge ycwealeqge gidlalsrtv
      121 pgwhspvtvs mayegertmv shgheapppd fafdgkhapg cpppsracia slvpgrregw
      181 lgcaagrgsr ifadvgwdds grwdpadlad lehceaflpn aeeamrytrt dcpraaagkl
      241 adlvplavvt lgsegayavd grtgesaevp aiavealdpt gagdvfvagf vtgtladwpl
      301 adrlafaglc aalsvqefgg slsapgwaei aawwqqvrac eagapgvlrr qyafldevlp
      361 aayrpaplar avptigfrrp a
//
LOCUS       WP_457680332             490 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680332
VERSION     WP_457680332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..490
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49666
     Region          40..455
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(47..48,51..52,55,87,137..138,140..142,145,166,
                     169..170,173,297,300..301,304..306,309,337,341,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpitdtavap dtptaaatap avspagarma praklillll cgaqfiiald fsilnvalpv
       61 lgrdlgmgqa dlqwavtafa lpsggfllls griadlygrr rlfliglglf taasvltala
      121 wspavflagr alqglgaavi vptgmslltt tfaegpqrer algisgtvls mgftigmvlg
      181 gvmtdalgwr stmgllsvag vavlaaapll ltesrpperp ridvpgavtv tggllsliya
      241 lstaaeqgfg rpdvlvtlil gagllaafvr vesraeqplv slpmlrrrtv awgnlaglmt
      301 fammsavifl ltlylqevlr lsafhtglvf gvqgvvsaga glvapkvigr lgarrtlltg
      361 lllqagftaa llglgtgtgm wlaltgvtla slghlwaiia ygvtatsgvp daeqglatgl
      421 vtssqqvglt vgipllsava sahiaalrad gsgfaeatlg giklglglda alvavvallv
      481 aaglrtthrr
//
LOCUS       WP_457680342             342 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680342
VERSION     WP_457680342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=36224
     Region          44..338
                     /region_name="SEST_like"
                     /note="A family of secreted SGNH-hydrolases similar to
                     Streptomyces scabies esterase (SEST), a causal agent of
                     the potato scab disease, which hydrolyzes a specific ester
                     bond in suberin, a plant lipid. The tertiary fold of this
                     enzyme is substantially different...; cd01823"
                     /db_xref="CDD:238861"
     Site            order(50,92,144,300,322)
                     /site_type="active"
                     /db_xref="CDD:238861"
     Site            order(50,300,322)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238861"
     Site            order(50,92,144)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238861"
ORIGIN      
        1 msrygmpals rlavaavasl avvasafapa asgapardad rpeyvalgds ysagvfvrpw
       61 eehdgcgrsg rnyphqvagq lgfeltdvtc gaaevvdgvl apqpaskiyg pptipppggw
      121 sdlpaqvdal sqdtdyvtvg iggnslgfgp ivkkclelgv tkplqlrpct nhysnggage
      181 dwleerftql dtdlarmmtv ihrrapharv avvgypaivp dntgcnfwhw nqlgsvkkgd
      241 mpwldglelr lnallekhaa yhaasyvdty gpsaahgvce sgdakwmygi kdnltgeggq
      301 tdppneqcrs lpgageactf vhpnargldn qtrqvsralm ts
//
LOCUS       WP_457680338             416 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680338
VERSION     WP_457680338.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42530
     Region          61..409
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 msrpaapeal aepteragrg wtaslslang aiwvgwygpl qillalqaae lappgtakes
       61 vlawvtgaga avsmvanplf galsdrtasr fgrrapwvla gvlggaaalv llagagtvpa
      121 malgwclvql tlnaafaait aavpdrvpqr qrgavggwvg aaqilgvvag tglatvaggv
      181 vagylacagf vvlgalpyvl lhrdpalpaa rrpaltwrav lagfwisprr hpdlgwawlt
      241 rflinlgnal allyllyylr dvlhrpdpdg gvlvltavna vtllgtvvvg glwsdrvgrr
      301 qpfvlgagvi mtaatgllag wqtwpgalca aallgvgfgv ftsvdfalmt evlpaaahrg
      361 kdmglinian alpqvaapal aapivqhlgg yralycvaaa vgllgallvr rirgva
//
LOCUS       WP_457680345             408 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457680345
VERSION     WP_457680345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 408)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /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=43792
     Region          162..407
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtvpprlrra lirmrrdlaf vaagvplhlv pallfwwais lltdtvngvs seapveliap
       61 ltllviagyg fteaqrwrfr aicgvelprl rftegkrqlg ynwlvgpllg vlellllall
      121 ltalvaalvl vwvwlvppqw rrghpgytvp gayltvlglv alaavpglaa glvrleilvg
      181 ravlgvsrse elarrvedlt esragavdaa daerrrierd lhdgaqqrlv slalnlglak
      241 atltdlppea revidaahre akdaieelnh lvrglhpavl delgldaals glaaraplpv
      301 rlrvdlpael pqrtapavea vayfvvseal tnvtkharea traevtvtrl geilrvviad
      361 dgmggadpak gsglkglaqr vrsvdgtfrm sspvggptmm svelpcpm
//
LOCUS       WP_457680348             307 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680348
VERSION     WP_457680348.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33940
     Region          35..114
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          132..296
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtldpsppqp atghggaaap pygtaprdda arraelaafl rsrreritpe qvglprgarr
       61 rtpglrreev ahlgavgvtw ytwleqardi hvspqvldav aralmldrae rshlfalaga
      121 vdpmpgrect gvtrelrqll eqltpfpavv qnsrfdilay nrtygrllcd ldalpqedrn
      181 cmwlafthpe wrasmgdleg amrvmaakfr asmaehvaep awkalvarlt easpefreiw
      241 aqhevvrpvs svklfrhprv galeltatsl wtgpnpgpkl lfytpvdets rerleqlaae
      301 paalaav
//
LOCUS       WP_457680351             484 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680351
VERSION     WP_457680351.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50488
     Region          17..453
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpelsrrrrl lvlaiccmsl livsldntil nvalpsiqrd lhasvagmqw tidaytlvla
       61 allmlagsta drlgrrrifl iglvvfaags llcslapsle wlvvfrmvqa vggsmlnpva
      121 msiitntfte preraraiga wggvvgisma agpviggllv qsvgwrsifw invpigalal
      181 fltlryvpes rapkprrvdp vgqllvigll gsltyaiiea pdagwtspei lafvllalas
      241 lagligyerr rreplidlrf fhsapfsgat vvavcafaal agflfintly lqnirglsal
      301 daglymlpma gmtlifapvs grlvgsrgpr lslllagtam gasgllfaaf daqstnpllf
      361 sgyvlfgigf glvnapitnt avsgmpraqa gvaaavasts rqvgqslgva vigavlasga
      421 haaatadafl aagrpawwii agcgaavlll galttgrwar atadrtaalf edeapgyrpa
      481 darp
//
LOCUS       WP_457680354             504 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680354
VERSION     WP_457680354.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..504
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51065
     Region          47..501
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,310,313..314,317..319,322,350,354,405..406,
                     410,416,432,435..436,439..440,443)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mseltqdrvp epgrisaves adgvtrdapp aapkgkrpqh tgillvvlga vfmalldatv
       61 vnvatptmrt dldttgsalq livsgytisy aallitgarl garhgfrtvf ltglatftla
      121 slacglapsa gvliaarvvq glgaglmvpq iysliqltfe gpararalsl yatviavavv
      181 vgqvaggllv sadlfgtgwr paflinvpvg lallvaavrl lpvgtprsak gldlpglvtl
      241 taallllvip lvlgheqhwp lwttlclaaa apmfgvfvlv ergvarrgga plvpgrvlrs
      301 pdlvcgaaal ffgmagyagf lfsfsqhlqs glgesatrag lafaplalgv atgsltwqkl
      361 parwhlpmia aasalaaagy lgigctlrag gqgglvlpvl qllwglglgy ttsplltlal
      421 sridpadasd asgvlttvpq laqvvgvavy gsvflaladr pgtagaaaps avasaqalya
      481 talpvaagtl lgalailpll rkrr
//
LOCUS       WP_457680356             278 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457680356
VERSION     WP_457680356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 278)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30502
     Region          34..276
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mddaltrvgr alrvvllval allflvpffl lvrnglateq ditapdwtff prvlqwsnlt
       61 evfqdpnlpl grallnstli avsttagtvl laslagygla ripyrhanlv fyailgtlmv
      121 paavtfvpsf vlvsslgwis tlrglviptl fsafacfifr qyflgfprel edaarvdglg
      181 ywrtywrivv pnarpvfaav gtivfigawn aflwplvigq dqeawtvqva lstfttaqnl
      241 nlhelfvaaa vsiaplvvvf lllqryivag versgidd
//
LOCUS       WP_457680359             423 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680359
VERSION     WP_457680359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45317
     Region          24..321
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mteidrrrll aagggvalaa glatacgsnt grggggsgpe isqwyhqyge pgteravkry
       61 aaayrkanvs vqwrpgdydr qtaaalltds gpdvfevngp lldqiqggqv adltevvepv
      121 kddfnqavla pkiwqdkiwg ipqvvdtqvl yyrksllkea gvrppetlde lvdgakklsd
      181 rktkglflgn dggvgvlggt plfaaglsli sedgkvgfdd paaaralgki rqlyadksll
      241 lgaptdwsdp aafvqgltam qwsglwalpq ikkalgddfg vlpfpkdgsg gkpsvpvgay
      301 gsavsarsrr kaaatafakw lwvdrtdfqq dfalsygfhi parislakka eqlregpaad
      361 avrfatdhgy aepllwttad rtayqdalsr iikdganpes elktvvrkvn aelqrvkkkv
      421 kkq
//
LOCUS       WP_457680375             648 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457680375
VERSION     WP_457680375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..648
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67467
     Region          61..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 makvsqpdgr peeppdtapa tvtttaptat atgpagapva epdspaaepd arhrltalqg
       61 laalsldama svaygpesiv lvlaaagshg lgftlpvtla iavllavlva syrqviaafp
      121 ngggsyavar thlgrrtalf aaasllldyv lnvavsvtag vaaltsafpa lyddrvgicl
      181 avlalitaln lrgivdsaka flvptavfvg ailamvavgl frtapaatvt adghasvlad
      241 nattvgalll lkafaagcsa ltgveavana vpsfrapatr raqrtevalg vllgvmligl
      301 svligrfhlq pvegvtvlaq ladasfghha afyvvqfatm vllalaants fgglpvlmgl
      361 lardnylphv fglkadrqvh rhgvlalaav aaallifsgg dmntlvplfa lgvfvgftvc
      421 qigmvrhwrr ersprwrgka llngfgallt gvsavvvtat kfsegawlil valpllvltf
      481 eavhrayari gtrlglgrlp epprrapslv vvpvshlsrl taealnaavs lgdevvavtv
      541 thdtpedrpa tealrrdwel wspgvellel psatrslgrp iaayvtglaa rrpgtritvl
      601 ipeaepahlw qrllqnqrga vvahavrrdt davicrlrfr ltaparmw
//
LOCUS       WP_457680390             381 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457680390
VERSION     WP_457680390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41061
     Region          3..377
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdeallrslt psvltilvrr gadfaaaeda vqealveavr vwpaeqprdp kgwlvtvawr
       61 kfldgaradt arrrreglvd eepapgpapa vddtlqlyfl cahpsltpss avaltlravg
      121 glttrqiaqa ylvpeatmaq risrakrtvs gvrfdrpgdv atvlrvlylv fnegysgdvd
      181 laaeairltr qlaaqvdhpe vagllalmll hharraarta pdgslvplae qdrgrwetgs
      241 iaegvailqa alardrlgef qaqaaiaalh adaptaeetd wvqivewyde larltdspvv
      301 rlnravavge adgppaglaa laalddalpr htavaaylhe rdgdlttaar lyaeaarkap
      361 dlaerdhltr qaarlnarrs r
//
LOCUS       WP_457680396             146 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamylcyclotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680396
VERSION     WP_457680396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Oakley,A.J., Coggan,M. and Board,P.G.
  TITLE     Identification and characterization of gamma-glutamylamine
            cyclotransferase, an enzyme responsible for
            gamma-glutamyl-epsilon-lysine catabolism
  JOURNAL   J Biol Chem 285 (13), 9642-9648 (2010)
   PUBMED   20110353
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Oakley,A.J., Yamada,T., Liu,D., Coggan,M., Clark,A.G. and
            Board,P.G.
  TITLE     The identification and structural characterization of C7orf24 as
            gamma-glutamyl cyclotransferase. An essential enzyme in the
            gamma-glutamyl cycle
  JOURNAL   J Biol Chem 283 (32), 22031-22042 (2008)
   PUBMED   18515354
  REMARK    Erratum:[J Biol Chem. 2008 Nov 14;283(46):32152]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..146
                     /product="gamma-glutamylcyclotransferase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15494
     Region          10..138
                     /region_name="GGACT"
                     /note="Gamma-glutamyl cyclotransferase, AIG2-like;
                     pfam06094"
                     /db_xref="CDD:428763"
     Site            order(10,13,15..16,84..85,96)
                     /site_type="active"
                     /note="putative active site pocket [active]"
                     /db_xref="CDD:119400"
     Site            order(56..57,96..100,102,114)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119400"
     Site            85
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:119400"
ORIGIN      
        1 mtreperlpf fvygtlrpge anygrtlrgr taaeepahig gallydgpgy pyatagpada
       61 vvhgalvrpr dpdydevcav ldrlegytpg dprnlyerva teavcpdgrt vrawvylaaa
      121 plaarlratg tpieggdwpa sraaag
//
LOCUS       WP_457680399             421 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680399
VERSION     WP_457680399.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44623
     Region          22..419
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mvdahqtfvi vggglagaka aetlraegft grvilicder dhpyerppls kgyllgkeer
       61 dsvfvhepaw yaqaqielhl gqpavhldpg artvrlgdgt livydkllla tgaeprrldi
      121 pgtglagvhh lrrlahaerl rgvlaslgrd nghlviagag wiglevaaaa rsygaevtvv
      181 eaaptplhgi lgpelgglft dlhrehgvrf hfgarfteiv gqdgmvlavr tddgeehpah
      241 dvlaaigaap rtalaeqagl dlvdreaggg iavdaalrts dpyiyaagdv aaadhpllds
      301 rlrvehwana lnggpaaara mlgqdvsydr vpyffsdqyd vgmeysgyap pgsyaqvvcr
      361 gdvakrefia fwlgadgrll agmnvnvwdv aesiqqlirc gaslapeala dpevplasll
      421 p
//
LOCUS       WP_457680410             389 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457680410
VERSION     WP_457680410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  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 389)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41243
     Region          33..351
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mpqhlrpspp laapapapsa sgppgagppf prrivflarr dlgnpaaggs ellvdriadg
       61 laahghevtl lcggpqggvp argyrvvsag gdaghflrvp rqlarrvgdc dllvevcngm
      121 pylaplwhrg ptlclvnhvh tdlwrlrcpg paarigrrle hwalagahrr glmvavsgst
      181 asalhglgva pgrirlvyng vaepgplapk apeplflamg rlveykrvdl llrlwervrp
      241 vtggrlvivg dgperarlaa aagpgvtftg hvseerkhql lcsawlllhp slvegwglvv
      301 meaaarrtpa vgfdipglrd svedgttgll argesafaah wctlalsarr rdalgraaer
      361 raarfrwsht vqsfravaae avldplsgr
//
LOCUS       WP_457680419             495 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680419
VERSION     WP_457680419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50334
     Region          47..460
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,310,313..314,317..319,322,350,354,409..410,
                     414,418,434,437..438,441..442,445)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mplgapatap eaafpdapat peapaapgpa pqqqrptvlt plglltvllg aalpmidffi
       61 vnvalptidh dlhagpamle mvvagygvay amllvlggrl gdmigrrrlf lwglaafglt
      121 slacglapda wtlvaarvaq ggaaalllpq vlatiqattt gkrrakavsl yggtagvssa
      181 vgqvlggllv svdlagtgwr avflvnvpma aaawllaart vpetrsphpa rvdgpgtall
      241 atalialllp ltegraagwp lwswvllaaf pfaatafvlv erraerlgrt plvppsllri
      301 psvnsgllml vpftlgfggf mfvvavalqs glhfgpfaag lslvplcaaf flaslagprl
      361 vlrfgrrvvv agsliqgagl allaltvhag wpgisvagla psmavlgigq gmvmpvlmri
      421 vlselpmtqa gvgggamvtt qqsglalgva tlgtlflsll psvgirdall talltqlaiv
      481 agttllalrl prtvr
//
LOCUS       WP_457680421             429 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680421
VERSION     WP_457680421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Carrillo,N. and Ceccarelli,E.A.
  TITLE     Open questions in ferredoxin-NADP+ reductase catalytic mechanism
  JOURNAL   Eur J Biochem 270 (9), 1900-1915 (2003)
   PUBMED   12709048
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Dym,O. and Eisenberg,D.
  TITLE     Sequence-structure analysis of FAD-containing proteins
  JOURNAL   Protein Sci 10 (9), 1712-1728 (2001)
   PUBMED   11514662
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="ferredoxin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45929
     Region          2..429
                     /region_name="COG4097"
                     /note="Predicted ferric reductase [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:443273"
ORIGIN      
        1 mallrvlglg avvivalwla qaepsvrlda lfatlahltg llagygilvm lllmarvpai
       61 ehgvgadrla rwhalggrhv ltlclahtaf alcgyaahtg tdvlgatvdl mgypglaaaa
      121 vgtallaavg vtsartarrr vrhetwravh lltyvgaala fahqlagpdl aggpfavwlw
      181 tllhttvgtl lvwyrlvvpa rqalrhglrv tevrvegpdv vsvvmqglel dalraepgqf
      241 frwrflsrrl wrtalpfsls apvrddtlri tvkacgdhtr rirrlrpgvr vlatgpfgam
      301 tahrrtrrkv llvaggvgit pmralfetlp gepgeltlly ragnaaqlvl reelegiaaa
      361 rgaalhyllg psdgpfdpla pqalrnlvpd laqhdvylcg ppgmstaata aleragvpad
      421 rihseqftf
//
LOCUS       WP_457680433             329 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene/squalene synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680433
VERSION     WP_457680433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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 329)
  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 329)
  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..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /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=35542
     Region          16..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtareldaag vtdprlreay ahcrrlnarh gktyflatrl lpagrrpavh alygfarwad
       61 divddpatgh ttadrahala alqrclddgl rggvstepvv ravahtaavy gidhrhfadf
      121 mtsmrsdltv tdyptyadlr rymhgsaavm glqmlpvlgt vvpqeeavph aaalgiafql
      181 tnflrdvged ldrgrvylpa dllaahgvdr allrwsrdtg lpdpritaal aaaaeltrgv
      241 yreaapglam ldpvsrpcir tafvlygail davrddgyav lhrravvsrr rraatalggl
      301 arlaaaratv rppgvrrggv phyaqeetp
//
LOCUS       WP_457680436             413 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680436
VERSION     WP_457680436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42139
     Region          9..379
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,136,
                     139..140,143,214,217..218,221..223,226,254,258,307..308,
                     312,316,332,335..336,339..340,343)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 merslragrl atftffglng fvmgmwivhi psvehragig havlgwllll lgggafvgmq
       61 lvgrltdrfg arrvvpvsga lcslavtlpg latdgwtlga allvlgfgng cldvsmntha
      121 vqvergyrrp vmsafhavfs iggvfaalvg artlslgwsa aatlaatslf glvisafaap
      181 allppasara anpsaargaa prtppriwal aalammlmlc egvandwsvl dlrevldapp
      241 ataafaygaf stamtvgrll tdrvaarigp vavlrygasl aalgltavvl spwiplalcg
      301 wavfgaglsg cipqlfsaag hadqdaagan vsrvaglgyl gmlagptvig plthlvplnl
      361 tfllpvafca vaagtarlle prevtaagsa yvhprpeaga vprrglegda dgr
//
LOCUS       WP_457680439             273 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680439
VERSION     WP_457680439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30046
     Region          51..146
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtqqpattpy nsgllsndaq rerdrlesiq rsvdafttgv ldglpieasw nclelgagtg
       61 siaywlaerc pdgrvvavdl dtryldadra anleiqeadi trrdyapgsf dliharylfc
      121 hlpnrdemia raarwlspgg wlvieepyhl padtspsplv rrildayqrt yrkhgadmtw
      181 aralpsllar naltevaytg nlgcmggldk drwlplitqa apalladgli teadltefat
      241 llkdpafidi pqitisawgr rpkeipsgqs vat
//
LOCUS       WP_457680442             222 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457680442
VERSION     WP_457680442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23752
     Region          23..207
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtaclspcyp ravttsklss rpfdavlcdl dnvirfydtt elarlergag lmegttekva
       61 fapeidrpll lgaitkqqwv esiviglagq vpevqarelg talaeapfra ddvvvamllq
      121 vrahvplvlv tnatveledd laslgladfa dhvvssarvg vakpdrkiye iaaeqagvam
      181 drclfvddrl eniqaavglg mtgvhyrepa dlrgplglll sn
//
LOCUS       WP_457680447             324 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680447
VERSION     WP_457680447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..324
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35288
     Region          4..324
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msplrlgvla ypgcfasevf gvpdllamat hvaaaqgsaq payetsvisp rrrviasggs
       61 vldvsamrpv dvlivpgfel sptldldaal anlgpevasi rsqaasgnav vsicvgaflv
      121 aeaglldgre attswlfadr farryadvrl rqeslvvtdr gvtttaafsa mydfalqlir
      181 ehdgprvars tarialvdda rstqapyvdp eliptvgref slgvkrwldq nlstrydlpt
      241 laqefhvstr nmlrrfgdea getplaylqt vrvrrarhll ettdrtvasi atdvgyrdpg
      301 afsdifarht gqrpreyral fhrr
//
LOCUS       WP_457680450             284 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680450
VERSION     WP_457680450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30316
     Region          31..>165
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtmlrgqrdp lddffrrtvs vddvdktvhv agtgpavilm pempgispdv arfarwvrda
       61 gfsvylpslf gvdgayplae aretivrrac vsaefrafag ggtspvvtwl rglarlahae
      121 rggpgvgaig lcftgnfalt malepaviap vvnhpslpld dpggleisde daaavaerva
      181 rdglkvlayr fdndrwctrq rfaayrallg dafdgrvlka etantnpppf frdvvgcahs
      241 vvtahlvdqe ghptmqarne iiaflgraar daagmnfdar sgpg
//
LOCUS       WP_457680453             204 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680453
VERSION     WP_457680453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22460
     Region          14..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpshhparsr rsterkgdlr eraildtcea llahkgynam tvgdiaqgag itrgalyfyf
       61 gskqevvval vartvehlwe rsrttaqtde prqaiaeamq rtvelwnehg lvmrtaidls
      121 ltvpeigelw shtadlfita itavleragi qagtepeqas amaralcwmi ertfyhaaqe
      181 sretlqgasa tcehiwltsa gltt
//
LOCUS       WP_457680459             314 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680459
VERSION     WP_457680459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34332
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqlryfl tvaeelhfgr aaerlhivqs avsqqlrrle relgtelftr strvvrltea
       61 gnrllpyare mltlqarare avdelraeqa atvrlgtssg lgawldvvlt ayarhtghaq
      121 lelvtggtee rlaqvragdl daallrgert dpgleflplw qdalmaalpa ghelaaretv
      181 elarlaelpl rlsprsrnpa lhdlvmrscr aagyapvlgs eftndqdtla aighgkpswt
      241 vfyaphaeql pvpgvvfrpl sdpapvmrty lavrngppra alralieacy eavdggpgvr
      301 pgspltrdvr dvgr
//
LOCUS       WP_457680464             433 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457680464
VERSION     WP_457680464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46165
     Region          31..425
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtphtfhnlp glrravrelc eahrlpshhg arlllsvsrt ataafdaggp vrlevveqsv
       61 pdgekllavt lhtgqtaasl sltdlplrgq atpdgtiawh lplgegedsa rpaavaaphg
      121 avpaqshtre sdgavayeae iaalegdlga alsrvdtltt elhrlkdela etnsgvlaly
      181 iqleerderl rrahgqilre ledalrpppi tvsglefavh yapadtdapt ggdfydwlll
      241 pdgtvhitvv dalghgvrst rsalnvthav rtlaleghpl esivarthdi lapfdpeima
      301 tvllaridpe tgalrlangs hppalvvrad gtadylevrg rgigfplpgs esvledtlhe
      361 gdllvlytdg ltesrrdpie gearlvksaw aharrpvdev pgaiakdmht vilhpddtla
      421 lavrragnpq gsh
//
LOCUS       WP_457680470             546 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457680470
VERSION     WP_457680470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..546
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59639
     Region          15..494
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mhtaprppsp saapqldavi vgagfsglyq lyrlralglr trvleacddi ggtwyrnryp
       61 garcdvesta ysfsfspeld qewewserya tqpellrylh hvadrfdlrk ditlrtrvtg
      121 avydegghtw qvttdtgetv ttrfvvlatg cmsavkepdi pgagtfagra lhtadwphed
      181 vdltgrrvav igtgcsgiqa ipllaeqaae ltvfqrtpvy alparnrpls aaetaelkar
      241 ypefraaqrr skggtlfepp trsalevdea erratyeegw dsgvlsgllr tytdilvdra
      301 anetvaefvr skirsivtdp etaetlsprt fpfgtkrpcl dtgyyatynk phvsvvdltk
      361 tpiveitprg irtsdrehav dviafatgfd altgsqvamd ivgkggttlr ekwadgprnh
      421 lgllsagfpn lftvigplsp svlsnavvai eqhvewitdc iahlrrngit eidatpraea
      481 dwcahvadla aqtlypsvds wymganvpgk prvflaytgg leryraecda aaengyrafa
      541 lsggad
//
LOCUS       WP_457680475             386 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680475
VERSION     WP_457680475.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /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=40692
     Region          17..359
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrelirriaa atpadrdrgv dalralailg vmlghwlvta lvadsgtvrv vsplhqlpql
       61 tpaswlfqtl avfflvggqm aakswaaara rggtyrrwlg artvrlfrpv vavvvvwvvv
      121 agallvagag lqtvhtlgel alsplwfllv favltaatpl varlhplwpl avvlhidlir
      181 fgmggpvwlg wanvaagwlv pyclgaawar gglrgratgw vlllgggatt aglvlwagyp
      241 aamvgvpgag isnlnpptla avtfglaqcg aallllgplr rilrrpavwa avalmnlsam
      301 tlflwhqtam mavtavgllt ggflpglhtl pdgagwvlar lawlpvfala llvcwaafrt
      361 yehgrrggtk vvregrpaea ravrsa
//
LOCUS       WP_457680491             353 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680491
VERSION     WP_457680491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37995
     Region          22..341
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrspkdffrp lavgaptpvr evpfrpsrmi hffdpgnekm aakvpaiapt vdvllgnled
       61 avaadrkeaa rsglvkiaqa tdfgdtqlwt rinsldspwa lddlltlvge igdklnvimv
      121 pkvegaedih yvdrllaqle akarirrpil vhailetatg vanveeiaga sprmqgislg
      181 padlaasrrm kttrvggghp gylvredphg adgaapratf qqdlwhytla rmvdacaahg
      241 ilpyygpfgd ikdttacedq frnafllgcv gawslhpvqi aiakkvfspa padvawarrv
      301 ieamgdgtga vmidgkmqdd atykqcqvva eladalaard pelrdayaaa eke
//
LOCUS       WP_457680500             273 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680500
VERSION     WP_457680500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29277
     Region          47..145
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mrateagryg eglfrpeetg eagridlgal aydeasaarl aalgagpgwh cldvgagtgt
       61 varwllesag vtgvlavdrd trsldagrtp glstltadit apdfdpgrfq lvharfvlmh
      121 lrswrrmiak lgslvapggv lvlsdavdlt tagapatpyt tvmramwqgl resigtdisw
      181 mpdypyllre eglhrvaaei hvpplvpgsp lnrfwadtwd rargailatg qvdeaqiera
      241 rralssdect glspgmltaw gwrteeagrd qhh
//
LOCUS       WP_457680505             646 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457680505
VERSION     WP_457680505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10147902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..646
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=66800
     Region          56..541
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(195,198..203,205..206)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(198..199,313..314,330..335,361,429,441,444,535)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          570..629
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mtqpmtarta apttaagagg htpqsgtlsi ahgarpatdg aagvlarfee wvrrspeapa
       61 vidgahswty gqigsaadev aqalrarvrp gdlvgvcldr saalvvtava larigavylp
      121 lgprpgerrt davtedidvv cligdpgllp prhrtadrmd ltlpgegana tatvvaafaa
      181 pgpaahsapa gtfyavltsg stgrpkavav gepalgglld wyrattglgp gdrqslligv
      241 afdphllelw ggltsgaalv papdevrwds vvladwwrta gvsvsvaatp mveplldrpw
      301 pqdlrlrhlm tggdrmrrhp gaevtatvhn aygpaeatvi atthamhgtd gaagtdsapp
      361 igrpvpgvtv ivagqdgrpi ergtegelli ggsglalgyl dpeltarrft avpeglelpg
      421 vervyrtgdr vrmaadgqle flgrlddqvk isgvriepae veaafeqdpa vlsavvtapr
      481 sadgrarlva yvraaadsgl taeallpalr twlpeqavps dvrivgsfpl dangkvdrae
      541 ltrraaesaa prpggtapdd gapagtpger lvlsavrdll drpgtsladn fteaggtsvl
      601 aarlltviek esgvrlrape llrqpdlrav allvdqrcas rqpaga
//
LOCUS       WP_457680502            1064 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457680502
VERSION     WP_457680502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1064
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=113246
     Region          2..1064
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mlplsssqei vwlheqvqpg sraynftaal dlwgtldtea lrhglaatld rhaglrlelv
       61 avagampgqr vaeacaprlr tvdlsgaadp eaafqellrt eaetpldtye apllrwtlvr
      121 lgddrhrlih vehhlihdgh sfaillrdvf tvyrgrvlge pvelppapsy adhvrarsgd
      181 qataerqegl efwsgalrem sydmplpgla kpgarrrhhg gqlrqsigad laerlrahar
      241 trgltpfatl lglfaemlrr hsgrsemvig tavgnrprgf eetvgmfvnt iplplrldpa
      301 apaeesmdev tdtliralph qevpiqeltr alglhtsgad nplfgvmfsa hdaelpdidv
      361 pglditlfeg fntgttrfdl dvvllpddrr gvgprhgaag mtlvwdydad lfgedvakll
      421 agrfldllra yldapgtala dlapppappa lpaaapqapr hdpldpatah drslpallvg
      481 arritygdla drvaalaqrm qaagvtagqp vaavlprgad svvtllaclr travycplsp
      541 sdpparltll lerlnpalvl tsadtavtvp dglpsatvda svlpparaae avpgaaylih
      601 tsgstgipkp vavgraalen hltgvagrfg lgagdrvllf aqpsfdvale evlpslyaga
      661 clvaperevp tgtelaella aarvtvanlp tsyflatrqe mrpalrdghw aprllvlgge
      721 rlpadalraf ladtdstvln vygvteaais stvheitrdg ltdgaeiplg telpgervhv
      781 ldahhrplpd gavgelaiag aglaegyagn pevtearfrr iealggervy ltgdrgyrgr
      841 dgllyflgrl dhqvklrgyr ieleeveaaa saalggrsca vvldreapgg prlvgflesa
      901 dedgpwdeqa lhtelsrrlp salvpgrwar ldvmprlagg kpnrtaltrr aaalepaapa
      961 apaaepgdgq paepadpmta llvegwreal ghgrfdlssd ffrsgghsll aaqlaswlep
     1021 rlgqrpplrl lfqnpvltdq aaalaavgta tpvpaasttv tesr
//
LOCUS       WP_457680513             275 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680513
VERSION     WP_457680513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28383
     Region          30..272
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mrgtgetgqa atarqgavev gagdgrnpls gsvalvtgas sgigaatala laregcslvl
       61 varrtgrlee laeaigaqgg aslaltadla aadevrrtvd qtvdhfgrld vlvnnagfga
      121 rgavadsdpa dwdrmvdlnf kavlrmshaa lphllraahe gprgvadlvt vssvagrvpr
      181 kdnsvysatk havcsfseal rqevtgrqvr vglvepgmtt temtrggsqa asahglppes
      241 wlraediars vvfmvtqpph vavneitvrp taqer
//
LOCUS       WP_457680521             676 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457680521
VERSION     WP_457680521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..676
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74046
     Region          1..676
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mttsnpffep sdlpyelppf arirndhflp altrgmadql aevaaigaca gpptfentve
       61 alersgavlg rvcrvfsnka asdtdeeiqa leieitprla ahedllllds alfgrldalh
      121 eqreqlgldg eqlrllerhh tlrvragarl apeqqrrlre lnahiaalct efdqnlrvat
      181 adaalvldra eelaglpadq iaaaaenara lghpgkfvls lknfscqtel aaledpalre
      241 rllaaslgrg idsngpiavt larlraeraa llgypshaaw evadrtagtt daveellgrl
      301 vapavanaer egaalaeaag vaqiraadwq yyservrker ydldaaalrp yleletvlhd
      361 gvfhaaglvy gitftrrpdl vsyhpdahvy evhdadgspl glyigdfhar eskrggawmn
      421 slvvqshllg qrpvvvnnln vakppagepv lltwsevntl fhefghalhg lfsdvrypll
      481 sgtqvprdfv efpsqvnevw adwpevlahy arhhltgepm paelparlre aenfgagfrm
      541 vehqaaavld wawhtlsadg dvpgedevea feaaalerhg lamaaippry rtgyfahifn
      601 hgyaagyygy rwaevldadt vrwfrengrs iresgeifrr ellakggsvd plaafravvg
      661 rdaeigplla rhgltg
//
LOCUS       WP_457680524             903 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680524
VERSION     WP_457680524.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..903
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=93272
     Region          33..444
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(40..41,44..45,48,79,129..130,132..134,137,157,
                     160..161,164,227,255..256,259..261,264,335,339,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          <652..>882
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mstatsppga gteeisepgv lshrqiltil sglmlgmfla aldqtivsts irtisddlhg
       61 lsqqawatta ylitstiatp lygklsdlyg rkpyylaait ifvvgsvlct fstsmtglaa
      121 fravqglgag glmslalaii gdivpprera ryqgymlgtf atssvagpli ggalagqdql
      181 lgitgwrwvf lvnvpigiia lfvvakvlni phtrrdhrid wwgaltlsvg vvplllvaeq
      241 grewgwdssr siacyvigvv giiawifver wigddalipm rlfrngtfsk tsvlsvligm
      301 gmfggmlmip qylqivkgas ptssglqmlp lmagmfiasi asgqitaktg rykifpiigt
      361 almiaamllf hfrvqwdtpl wetmiymlvf glglggcmqt lvlavqnavp prdmgvatas
      421 stffrqmgat agtavflsvl fstvgdkisa afkdavster fqaalhdpav lhdpankpvl
      481 dmlkhpgnad ssgvlsdssf iqhldprlae pfkrgfadsm htvflmgaiv valafvlmwf
      541 ikevplrqis glqaraqada eaeadavaks aksaggavea vdgaaggaga aaagadgaav
      601 tpaqsessgs sessessgss dpagtpgadp vpalsgasap padrgfgttg peirgtvrdg
      661 dgrpvaraav tlisvdgrql grtstaadgg yalpttgagt yvligsagar qpqavtvvvs
      721 gepvsfdlal ggaaglsgev raekgdapvp galvvatdvt gevvasgvag pdggfafgel
      781 apgsytlavs aerhrpsalp vevtsgnrnw yevrltpgaq vrgtvrtahg spvddarvtl
      841 ldpagnvvgt atsgqdgeyv ftdldsgeyt liasgyppaa tplrleaagh gefdielghd
      901 pvr
//
LOCUS       WP_457680527             166 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680527
VERSION     WP_457680527.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18415
     Region          43..164
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mppymlrhap rercmstqrr ektgqapppp tgretlvhlp sellallrlp stcylatsmp
       61 dgspqltqtw vdtdgthvli nsvrghvktr nigrdprvav avsdpdnpsr ffqvrgrvve
      121 tttegavehv eklaqkylge pypwyggrde ervlfviape sissmg
//
LOCUS       WP_457680532             331 aa            linear   BCT 27-JAN-2026
DEFINITION  D-cysteine desulfhydrase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680532
VERSION     WP_457680532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10012093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="D-cysteine desulfhydrase family protein"
                     /EC_number="4.4.1.-"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32993
     Region          10..318
                     /region_name="PRK03910"
                     /note="D-cysteine desulfhydrase; Validated"
                     /db_xref="CDD:179673"
     Site            order(52..53,81,190..194,275,304..305)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107202"
     Site            53
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
ORIGIN      
        1 msadsgtprr aalatwptpl epaprlaral glgaedlwvk redltglggg gnkvrklewi
       61 cgaalaegat tlvttgaaqs nharltaaag arlgldvvlv lagaagssts gnlvldglfg
      121 atvvwagevg gtqlaaaaee vaqrlrerga vpaliplggs splgaygyae cgrellgqap
      181 dldtvvaalg sggtmaglvd tlgpgkvlgv dcgavpdpad tvtglvtals gtvhapetlr
      241 lrreqvgagy stlteesmda ltlagrtegi aldpvytgra laglraavrd gsvapgqrtv
      301 llhsgglpgl fghsdavarc qealtvlpvh e
//
LOCUS       WP_457680539             390 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680539
VERSION     WP_457680539.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42986
     Region          1..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfrytprqa dlkaraaayt ellfryeqqa eeaggplpad tvreltraai dagvyainmp
       61 ekwggpglsl ldqviveeef gkvtnclwdi pwrpanvlay gteaqrekyl lpvirgerfd
      121 afavtepgag sdpasgtsta trteggwlln gekwfvtcgd iadfllvqad agperaatlf
      181 fvdkqapgvr mtrvprfmhs avnghpeftf tevfvpdddv lggvgngyel tkewftderl
      241 miaarttgaa eralglardr sverkqfgsp iadfqlvqgm ladcavdiav nraythqvaw
      301 eadqpgtdrk alhakastak laaseaagrv idrcvqifgg rgydrsypve rlyrelrvdr
      361 iwegtseiqr liianelikr gtraldlplp
//
LOCUS       WP_457680537             389 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680537
VERSION     WP_457680537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43142
     Region          1..380
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfrltprqa dlkrtarelt etltayetdc eenngltaqd haairdavla sglqavnmpr
       61 ewggagltil eqaivqeelg qltgalwdtv wrpanalrfc tpaqreryle pvirgerrdc
      121 yavtepgags dpqnlattat rtadgwtldg ekwfvtvgdh adfmivlaaa gpdreatlfl
      181 vdmdtpgiem trvprfmhtf vyehpeftft evqvpedavl ggvgkgydit rswfteerlm
      241 iaarttgaae ralrlardwa verkqfgspi adfqlvqgml adcavdiavn rayahqvawe
      301 vdegtvdrkt lhakaaiakl aaseaagrvi drcvqifggr gydrsypver lyrelrvdri
      361 wegtseiqrl iiagelvkrg tgvlqmptp
//
LOCUS       WP_457680542             695 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate--CoA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680542
VERSION     WP_457680542.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 695)
  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 695)
  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..695
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..695
                     /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=69856
     Region          3..695
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mgrdlsalfd pesvavvgas ddpakyghav aaqalrapdr rpvhlvnrrg gtvlgrttat
       61 slagigepve lvvisvpgpg feaavddala cgaraivgit agfaetgplg larqqaiaer
      121 vraagavlvg pnclgiadnt telylasdrf apggiallsq sgnlalelhl rcaphglgfs
      181 rfvslgnqad vtlvdlieda arhdptraia vyaedfgdgr afaeaaaaag kpvvlltagr
      241 gtasarsaqs htgalttsad vvaaacrdag velvatphem tvvlaalngg rratghrtav
      301 ctdggghgai aadaaesagl avpelgpaaq qrlrtllweq savgnpvdla gmgeqnphsy
      361 gdtvgallal devdsvmltg yfggysaatg glggpaaesg tagggsalaa geletahqma
      421 vhaartakpl vvqsmfpdap scrtlveagi pvfastedaa ralaamtvdg aagppgvrpl
      481 ppsaaplsdp gyhgvrtlls aagvpfpear eitdeaella aadafegpyv lkalhllhks
      541 daggvalglp drsalvtafr emharlgaas ysveamadpt dgvelivgvn rdprfgpvam
      601 vglggvltea lhdvafalap vpaaraeqll tglrtaallr gvrgrpavdl aaaaavierl
      661 ttlaaahpei teievnpllv rpdgalalda ravla
//
LOCUS       WP_457680545             130 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457680545
VERSION     WP_457680545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..130
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13692
     Region          15..124
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mddhpshpaq rvcqpdsaad ardfvrafva llrpappagt iqnllllvse lvanalrhag
       61 avtalhlrad rerievlved pssahpqerr pdlsgsnggf gwlmvhslal dvvilpgscg
      121 gktvqaalar
//
LOCUS       WP_457680556             844 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680556
VERSION     WP_457680556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 844)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..844
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86323
     Region          66..456
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(66..67,70,101,151..152,154..156,159,179,182..183,
                     186,311,314..315,318..320,323,351,355,408..409,413,417,
                     433,436..437,440..441,444)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          <587..>828
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mapatavpia papaiapapt ptpapvasge peepghpgap aplgprrlrp vvaglmltll
       61 laalgqtiiv talpeiagel hgpgamswvv tsyllasvig lplygklgdl fgrkpvflfa
      121 llvftvgsal agwsrtmdel vvfravqgvg gggliigvqa iiadvvppra rgrytgllga
      181 vfglgfvagp liggfcadha swrwcfslnv plgvltflvi acvlklprpt rrakpdlaga
      241 lllaafsicl vllaswggtt yawdsrvvlg laagalgtal lflaveyfat epliplrlfr
      301 dsvfhvtglt gaavglalfg avsylpaflq radgatates gllmlpltgg lviaslvsgc
      361 lisrtgrhkv fpvlgcvpaa vgmwllsrwq qdtawevysl gtallglgig fvlpvlvlav
      421 rhsvrttdpg aaagathcvr qiggsvgaal failladrla rrlgdrlpgs arlpapeslt
      481 prlvralpaa lrdspvaaya dampriflfl vpvlvlglvl afflkgkplv shaspapqaa
      541 pspqmpygdp adpaavpqar aaadtnavns hgpgspytra hrhtttghta vmagvpvcgt
      601 vqhhdgsivp raaltlidva grqigrgatg edgryalstp gagsyvlias agghqpqavt
      661 vtvgerpvel dvvlggagrl agtvttadgt pvrdamvtlt dvrgevvatt rsgreggyvi
      721 gelvageytl assapafrpa alpvtvqasr etrqdielag gavlrgtvra gggrpvedar
      781 vtlldaagnv vdtattgpdg lfrfvdlsag eytviaagyp pvatvlqvag ggrterdlql
      841 ghed
//
LOCUS       WP_457680586             211 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457680586
VERSION     WP_457680586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22110
     Region          21..202
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mtlfgelvps vppestqqvv gypslfllvv lgslvpvvpt galvssaavv afhhtspfal
       61 lmvfvvassa aflgdvglys lgrrgshsph gsrwlarlrt raaperlaqa qhklrehgvl
      121 vlvlsrlvpa gripvmlacl laamplrrfv rgdvpaclaw aatyqligll sgslfrsawq
      181 gvamaialtv viaaapavwr rlgpargegg s
//
LOCUS       WP_457680579             257 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680579
VERSION     WP_457680579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 257)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28321
     Region          15..104
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          163..242
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpksrhaprm ttglrplpag tgvdahrhde hqivyagrgv lsvtteagsw iapatravwi
       61 pagtvhehha hgdtdlhlva lpvrdnplrl drpavlkvgp llrelilayt erpadrgaer
      121 rrlravlldq lrhsaeqplh vpaatdprlv avcallrddp adnrtlaqlg atagvsdrtl
      181 trlcraefgm sfpqwrtqlr lhhalrllae dtpvtvvahr cgwasssafi dvfrrafght
      241 pgahrahrah rahraqr
//
LOCUS       WP_457680589             349 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680589
VERSION     WP_457680589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..349
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38502
     Region          14..345
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mttsleffrs aggpaasags dfarlsrrvv aagllqrrpg yyavrltlvt mafaggwvaf
       61 falgdswwqm avaaflavvf aqvalvthdv ahrqvfrgrr psevggllfg nlgvgmsygw
      121 wmnkhtrhha npnheeldpd vapdilvwsr dqaraatglp rfigryqaql ffplltlegf
      181 nlrvssiral rsptmkhwgs eaalllthiv lylsalflvl spgralafll vhqalfgvyl
      241 gctfapnhkg mptltggarp dflrrqvlts rnvrggaltd fllgglnyqi ehhlfpsmpt
      301 phlrraqtiv raycaelgvp yhetglirsy aealrhlrra geplrgpra
//
LOCUS       WP_457680598             459 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680598
VERSION     WP_457680598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=50011
     Region          1..456
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mdvalclfss dlrlhdqpvl haalraapqv vplfvvdtgi agagfmvpnr aafladalad
       61 ldaglrergg rlvirtgdvv tetcrvaaet gagevhlaag vsgyalrrer rlgaelaaag
      121 rslvvhdavi taqppgavlp sgpgkdhfav ftpyfrrwqa agrrsvlpap rsvrvpaevr
      181 seklpsaqvl cpagepspal peggeragrr rfgawqrsgm adyqdrqddl pgdatsrlsp
      241 ylhfgclspv elvhkasgrs dagaeafvrq lawrdfhhqv laarpgaara dyrtkgdrwr
      301 ydgaevtawk egrtgypvvd agmrqllheg wlhnrarmlv asfltktlyv dwrvgarhfl
      361 dllvdgdvan nqlnwqwvag tgtdtrpnrv lnplvqarrf dpegayvrrw vpelaglagp
      421 avhqpwklsg peraaydypd pvvdladalv rfkrargle
//
LOCUS       WP_457680601             303 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680601
VERSION     WP_457680601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  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 303)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32212
     Region          63..167
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msnpdrpgpg hhhphdsahl dwevlgphle rgaelytply eqvadwlrep atgapgpgsv
       61 gvrrvldigs gpgvvsclla rafpdaevva vdatealler ardravrlgl gdrvhthpae
      121 lpdgldalgg adliwsskal hhigdqraav aalaghlrpg gllaiaeggl aprflprdlg
      181 igrpglqsrl daageewfte mraalpdaad etedwpafla daglrtprtr sflldlpapl
      241 sagarayvva nltqardmyg drfdeddlat larltdpeda agitrrpdaf flsaqtvhta
      301 raq
//
LOCUS       WP_457680606             358 aa            linear   BCT 27-JAN-2026
DEFINITION  bile acid:sodium symporter family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680606
VERSION     WP_457680606.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Claro da Silva,T., Polli,J.E. and Swaan,P.W.
  TITLE     The solute carrier family 10 (SLC10): beyond bile acid transport
  JOURNAL   Mol Aspects Med 34 (2-3), 252-269 (2013)
   PUBMED   23506869
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Doring,B., Lutteke,T., Geyer,J. and Petzinger,E.
  TITLE     The SLC10 carrier family: transport functions and molecular
            structure
  JOURNAL   Curr Top Membr 70, 105-168 (2012)
   PUBMED   23177985
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Hagenbuch,B., Stieger,B., Foguet,M., Lubbert,H. and Meier,P.J.
  TITLE     Functional expression cloning and characterization of the
            hepatocyte Na+/bile acid cotransport system
  JOURNAL   Proc Natl Acad Sci U S A 88 (23), 10629-10633 (1991)
   PUBMED   1961729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="bile acid:sodium symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=36875
     Region          16..323
                     /region_name="SBF_like"
                     /note="SBF-like CPA transporter family (DUF4137);
                     pfam13593"
                     /db_xref="CDD:433336"
ORIGIN      
        1 mrrpplpkll srlpvdgyil alvgtvalaa llpargpaat aaegastgav allfflygar
       61 lstreamdgl rhwrlhltvl actfvvfpvl glaarglvpq ilpptlytgl lflclvpstv
      121 qssiaftsia rgnvaaaica gsfsslvgiv vtpllaglvl hgggggfsag slvsivcqll
      181 lpflagqllr rwvgnwlirh kkalgyvdrg sillvvytaf sagmvqgiwh qvsalrllcl
      241 lgveavllav mlsatwygsk klgfhradri aitfagskks laaglpmasv lfgaqaglaa
      301 lplmvfhqmq lmvcavlakr faasaastap eaamagaaag stavteaagd vvasgerr
//
LOCUS       WP_457680614             147 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457680614
VERSION     WP_457680614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15784
     Region          18..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 madtpyapsr iralpswllg raaarghrlv adalaaegmr mmhhavlsav aelgpvsqae
       61 lgrtlaidpk dmvaivndlq kdglvtrtpd pndrrknave isadgrrrlr rtqqlgdean
      121 aeltaaltpa ereqliallt rialpeg
//
LOCUS       WP_457680611             314 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680611
VERSION     WP_457680611.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  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 314)
  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..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /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=32283
     Region          1..314
                     /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 mrrvrfhsyg gpdvlrveet aeepvpgpge llvrteaigv tlpcvrrvrg dgngggdplp
       61 smpggeiagt vvalgpdvtg fapgdrvtsl tftgsytela lapaflasri pdgasaveav
      121 alvrsghval aalstaaprg aesvlitgaa gatghlavql aklqgvprvv aavssaakae
      181 flrelgadev vtydqeswga padivldgvg gellpralaa lapggrliff nsgggtvpay
      241 ellagdktit gltmrrfstv qrelyeehra qlwelagsgr lraavhaelp ldeaakahet
      301 iearanlgkv vlrp
//
LOCUS       WP_457680627             520 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680627
VERSION     WP_457680627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56743
     Region          8..518
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mseeapvdef dyvvvgggta gavvaarlse dptvtvclle agpsdvgden vlrldrwmgl
       61 lesgydwdyp vepqengnsf mrharakvlg gcsshnscia fwapaedlde waamgctgws
      121 aadcfplyqr lenndaagdh hgrngpvvvr tipphdpcga alleacaaag ipttafntge
      181 tvirganwfq incrpdgirs sasvsylhpv mgtrknldvr tglqarrlnf dsarhctgvd
      241 ylapdlihtr tvnarretvv scgsidspkl lmlsgigpat hlratgiepi vdspgvgsyl
      301 qdhpegvimw dakkpmvrss tqwweigifa dtepgldrpd lmfhygqvpf dmntyrrgyp
      361 tsenafcltp nvtrarslgt vrlrtrdfrd kpkvdpryft dehdqrvmih glrlareiis
      421 qspmadwagt elapgpsars dtelldyirt thntvyhpac tvrmgaaddq atpldpqlrv
      481 kgvtglrvad gsvmpflpav npcittmmig ekcadmmrsg
//
LOCUS       WP_457680635             302 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680635
VERSION     WP_457680635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33479
     Region          30..90
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,39,64)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(38,63)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(45..46,57,60,64..65)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          116..296
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msaaqpssgp slrryldhpr ggptvlrivl gtqlrrlreg agitreaagd airgshakis
       61 rlelgrvsck erdvadlltl ynvtdeavra dflklarrts spgwwhqygd vlpgwfethi
      121 gleeaasvir tyevqfvpgl lqtpdyarav aqlghprssp eeierrvqlr vqrqelltip
      181 daprvwavid easlrrplgg pevmadqlrh llkvtklpnv tlqiapfslg glaaaggpit
      241 ilrflepdlp divyleqlts alyldkrddv dhylavmdrl saqsespres vailerllkq
      301 es
//
LOCUS       WP_457680643             254 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680643
VERSION     WP_457680643.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26854
     Region          2..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkkvdhear rqeisealwr iagsrgldgt slrdvaaeag islgrlqhyf rtrdemllfa
       61 lqhinrlaad rireriasla eeptprevlr aclsgmlpld eksrigllvg aayyaravhd
      121 ealraeakng ipplrtffad qlrlaadrge lpperatede amllismteg latyvllgvh
      181 dpedalllld lhlenlfgae qaagggadra agggadravg ggavraargg adraaevggg
      241 rgaeapassg rsap
//
LOCUS       WP_457680650             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680650
VERSION     WP_457680650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22827
     Region          14..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpaakkkttt asasperrre lltiaaevfa ahgynattvr riadeagmla gslyyhfdsk
       61 esmldeilss fltelwdgyd avlaaglgpr etiealvtes freidrhraa vaiyqkeskh
      121 laaqprfgyl adsqqkfkka wlgtlergva dgafradldi rltyrfvrdt vwvaaswyrp
      181 ggqhnpeeia rqylsmvldg iaira
//
LOCUS       WP_457680653             301 aa            linear   BCT 27-JAN-2026
DEFINITION  SIS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457680653
VERSION     WP_457680653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32101
     Region          8..296
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 msetsymeqe lcsqpetwrq aarigaaagp lpkagqrvav vgcgtswfma qsyaalreaa
       61 gqgvtdpfaa seaflggdrg ydavvaitrs gtttevlrvl davkgriptv tilgdpetpa
      121 valsdetvtl pfadeksvvq trfattaltl lrahlgedis ravtdaeeal aapmekewvd
      181 aeqfsflgsg wtfglaneaa lkmreasqsw tesypameyr hgpiaiaapg rvtwlfgqap
      241 dgleadvvrt garfahhard pladlvlvqr valerararg ldpdnprslt rsvmletpaa
      301 s
//
LOCUS       WP_457680661             400 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680661
VERSION     WP_457680661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41562
     Region          3..366
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 maepgngpls gvrvvelagi gpgpfaamll adlgadvvrv drpggaglgi dpayditnrn
       61 krsvlvdlks pdgvaqvlel veradvlveg yrpgvaerlg vgpeecltrn prlvygrmtg
      121 wgqegpladt aghdigyiai tgalgmigpp dgppavpanl vgdyaggsly lvigvlaalq
      181 harteggkgq vvdaaivdgt ahltamihgm laaggwqdrr ganlldggtp fygayetadg
      241 ghmavgalek rfygefirll gieeeapsrd dlaawdelrt viaarfktrt reewtavfqe
      301 sdacvapvls lreaprhrhl aargtfvehg gitqpapapr fshtpgavrr ppalpgadte
      361 eiardwqapg llaplpsass paapappagp srteqkdtag
//
LOCUS       WP_457680659             395 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680659
VERSION     WP_457680659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41752
     Region          7..395
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mprqdtsgra ydlvlygatg ftgaltaayl aahapkgcrw alagrstakl eqlrnrlaks
       61 dpscadlpll radssdpgsl rdlaaetrvl vttvgpyllh geplvaacaa agtdyvdlsg
      121 etefidrmyv rhdatarasg arlvhacgfd svpydlgvry tvgllpedvp vridgfvrtn
      181 asfsggtlss altaasrpva maraarerqr veprpagrtv hapfgppirs setrtwgvpl
      241 ptldpqiiar saaaldrygp dfryrhyagv rrlpiavggv lgagalcala qvpsarrwls
      301 grlepgdgps perrarswfk vrfvasggdt hlitevsggd pgydetakml aesalslafd
      361 dlpetagqvt tavamgaalt trlqeagikf gvvqe
//
LOCUS       WP_457680676             152 aa            linear   BCT 27-JAN-2026
DEFINITION  RrF2 family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680676
VERSION     WP_457680676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16167
     Region          2..141
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrisaradya vraalqlada rdaeplkaea iaqaqdiphk flegilndmr rgglvqsrrg
       61 gnggyrlakp aeaisiadvi rvvdgplvsv rgvrppelsy tgaarsllpl wialranvre
      121 ildgvsladv asaelppqva eltenpdswt np
//
LOCUS       WP_457680679             332 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457680679
VERSION     WP_457680679.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35222
     Region          1..322
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mraisytrat dvhsavaavt sdpgssflag gttevdllrl dvlrphrlvd inrlpltgve
       61 drsdggllig alarmsevae dravverfpm lsqalllgas aqlrhmasmg gnlmqrvrca
      121 yyrdpesacn krvpgsgcsa ldgvnrghav lgtsehciat hpsdlavalv aldamvhveg
      181 mdgtrtipvd dffllpgdtp erehpltpge litaievpal pmarsslylk vrdresyefa
      241 lasvaaaval edgvirevrl alggvatkpw rarraedllv gqradegtft raaaaeltpa
      301 vtrpmnafka elarrtlvra lrtaattggg ta
//
LOCUS       WP_457680681             749 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces nigrescens].
ACCESSION   WP_457680681
VERSION     WP_457680681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..749
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80097
     Region          1..749
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mttgatleav grpvdrvdgp akvtgrgrys aeitlpntay atlvgartas gritgirtda
       61 aeradgvlav lthqnlpkip grpsllpsla ghaapgesff plqddivhyf gqpvamviad
      121 sleraqfaar qlhvdydrsa svttldegrd qayepeaifa gflpartvrg dveagfkaat
      181 qrldatyhfa anhhnpieps attavwdgdr ltlydatqgi vatqstvaal lgippskvrv
      241 rasfvgggfg ckamiwphvt laalaarqvg rpvkltltre qmftscghre eqeqrielga
      301 tddgrltalr hhklsltspf dewaepslgm asqayacphy egvyrlirsn tmtptftrgp
      361 gettgmcale clmdelahqi gvdpvqlrlr nhaeadpntg hpwssdgaee cyrrgaarfd
      421 wqsrnpeprs erdgnwligk gmatagypvl fpmqpqrara rlyadgtavv qagtqefgtg
      481 vgtamtqvaa dglgvalrnm rfeygdtdlp nvaaavgsag agmisaavyt aattlrdqmi
      541 eqaiadpgsp lhhadpatvi vregrmqlrd rpetgetysa lmqrhfmtdl dalgswsppp
      601 qnlpyglatf gaqfaevavd pdlgmvrvrr mvgtfapgrv lnaktarsqa vggmlwglgq
      661 allegslvdt rdgrwanasl geylvpvnad apdvavefve vpdtvvnplg vkglgevgmv
      721 gaaaaianav fhatgyrare lpiriehll
//
LOCUS       WP_457680690             304 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680690
VERSION     WP_457680690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32435
     Region          1..301
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdtrllrtfv tlaragsfta aardlhlaqs tvtvqirtle kelgaplfdr mpsgtvptra
       61 gqrlleeaed vldavarlrt taavaagqcd teggtaegqv vvgagdslcs arlpgviaal
      121 rrahpqlevq lhavstaeav dglrtgrldl alllepevae ndllarrias eplayvaapg
      181 hplagraagw delaqecffv heegcsysdr lvrtllglpg arpritrfgs idaarscvaa
      241 glgltllprv tverhlregw ltmvegpeap pvpvqlvrhr rrwfapgari vaeemtrtfa
      301 aaea
//
LOCUS       WP_457680693             318 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680693
VERSION     WP_457680693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=33965
     Region          35..315
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mtsqttspts snplphtaes pdilqspdtl pspdsievlr ysaftadpag gnpagvvlda
       61 egldearmla vaaevgyset afvtahdtaa rryrlryfsp raevafcgha tiatavalas
      121 rtgtgellfe tpageirvgt slddglvrat ltsvpahshp ardtqvepvl ralrwsrddl
      181 dtglpphvaf agndhlvlav rsreqlaald ydfdalhalm rrhgwttvhl vhreaadrfd
      241 fhardpfpvg gvvedpatga aaaafggylr tlglvteplr vhirqgedmg rpsdlyvdvh
      301 pddprvrvtg qavplpap
//
LOCUS       WP_457680696             178 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680696
VERSION     WP_457680696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19197
     Region          <55..153
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtahlpsttp avirltrytr telseilgdg pdpfgvswag ltwldkdehf gvkldgrlva
       61 htglvtvpls igsletravg fggvavapdl rgqglarivm taaleharti gpqygllfcl
      121 prllplyerl gwrqlhgdvv veqpadtttv mpletmwtpl rdgaqwpagg vqlrslpm
//
LOCUS       WP_457680705             519 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457680705
VERSION     WP_457680705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55978
     Region          131..>315
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          406..501
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 msafrtprwp raalsgmaaa allsavlpta sparaadrsg ppvparyahq rlnwqpcaak
       61 pslecarmtv prdwhhpgtg adlsvavsrh raadparrrg vlmmaaggpg asgltrpadf
      121 aarspavgaa ydvvgfdqrg vgsstpvrcq tdaefqdfya hdfrdrspaa lrgvldrsrq
      181 lvagclrrsg dlipwltteq avrdmdlfra llgvrkisyy gpsyatwlga yyatefpqrv
      241 eravldsnld fsgtwqdveg gqprsfqrrf eqdflpwiar ydatyhygrt aaeakarwea
      301 rrralrdhpl tvgsltigpn qldnatlqni ynagqqfpql asalsaldhw psatpaertl
      361 agkvfgnyls pgfaaaffsv tcndtpwrrd lghwirrsae dtaahplaga relayaatca
      421 swpvpaaprv rvtgkglptt lmlnsvhdpa tyyegalaah ralrgsrlvt vtgggdhgqy
      481 qngnacvdgi vdaylldgaa pehdvacaag plpvppgrg
//
LOCUS       WP_457680714             300 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680714
VERSION     WP_457680714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32247
     Region          33..263
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(38,41..43,46,54,56,86,105..108,198,200,202..203,205,
                     215..216,219,234..235,238)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(38,42,46,54,56,86,105..108,198,202..203,205,
                     215..216)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(41..43,198,200,203,216,219,234..235,238)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 mcarkmhade adidvplvrr llaaqfprwa dlpvtavdsa gtsnamfrlg ddmvvrlprv
       61 egaaqdvake hrwlprlaps lpvavpgplg kgtpaedypw pwsvyrwldg etpavgrlaa
      121 prslaadlae fvtalhridp adgppsyrgr pletrdgttr atvaaldgii dtdaaiagwe
      181 aalqapawpg pavwihadlq pgnlltvrgr laavidfgcl glgdpavdmi vawyllpada
      241 rgvfrtavga ddatwargrg walsialdel ryyretnpvm aaiarhviee vrteqahtaa
//
LOCUS       WP_457680716             382 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457680716
VERSION     WP_457680716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39619
     Region          13..377
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtdalslvde wgpektvvvs hrrtgmkgvl vidntargig kggtrmspgv tveevsrlar
       61 vmtwkwaavd lfyggakagi vadpaardke avlrafaral snevpreyvm gldmgltesd
      121 aaiiqdelgd rgaavgtpeh lggvaydklg vtgygvaeaa daaarhqglp lagsrvalqg
      181 fgavgsaaaq rfaelgativ avstahgvry dpsgldvgal ltardehgdh fvtrhsagta
      241 lpsgaeltvd cdilvpaalq dvitrgtahe ikaklivega nlptsadars ilaergitvl
      301 pdfvanaggv vaaafamdar ysgfrpgtsg ifesvsarlr antvtvldea qqqditphaa
      361 grrlaeervr tamqskgrip rg
//
LOCUS       WP_457680722             304 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680722
VERSION     WP_457680722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32575
     Region          6..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mlkplhlltl kavvrsesfa laardlgyta saisqqisal eketglvlfe reahgirpta
       61 aahrlvdlst hvlaamddld hqvqelatga tgrlrlggfp tadvrlvpaa lsalvethpr
      121 aqiqleeaep eelitalshg dldvalvyey glsprqwpag ltrhhllred lvllrargsg
      181 lgaqlpqlss arwitsredt agarsfvrlc aaagfeaava frsnnyavvr elvsaglgva
      241 vvpalghlps egveatrltq rsahrqvmal hrsensnpll pavlsclrra vpsgepylhp
      301 arsd
//
LOCUS       WP_457680725             389 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680725
VERSION     WP_457680725.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41086
     Region          24..375
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msstsrtvpp tadvvivggg vmgtsiafhl aeagvhnivv vergelgsgs sgkpiggvra
       61 qfsdplnial gsrslrawqd fprrpgadir ldsvgylfll tsdqqatdfe tgvhiqnsfg
      121 vpsrmigpre arqlcpyvst eglvaaaysp tdgharpgla vqgyaraaar agvvfaphta
      181 vtgidttgdr vtavhtdhgr iscstaicaa gawsarigem agvhlpvrpv rrqlaftapl
      241 appapripft idfastayfh nsddgllfgl adpaqadgfd ttwtpdwlel fraaarrrap
      301 aladmethdg waglyevtpd hnaligrsgt lsnflyatgf sghgflqapa vgeimrdihl
      361 drtpfvdvtp lsadrfttga etrpeahvv
//
LOCUS       WP_457680728             305 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Streptomyces nigrescens].
ACCESSION   WP_457680728
VERSION     WP_457680728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31717
     Region          2..266
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 mprraasfqq ipvsdaaagp yaltagpdga lwctlvhagq iarltpegql dryaldsasc
       61 gpsvitsgpd galwftrsqd hrigritvtg evtsfplptp gsgpygmvsa pdgalwftql
      121 hgdrigritt dgrvtefplp lsgafpsaia agpddalwft lnqahaigri sfdgeitlha
      181 lptenaapvg itcggdgalw fveigagrig rittdgeide fplpdpasrp haivagpagd
      241 cwftewganr igsitpdgri eeydlpiaas ephglafgpd galyvaleig avvrlapqge
      301 rggrh
//
LOCUS       WP_457680731             252 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680731
VERSION     WP_457680731.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27109
     Region          6..249
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgngegptli tsvqrafrlm eavgahegga pakqlaretg lplattyhll rtlahdgyir
       61 klddggfvlg eklttlhagg qgqalltrvr palaalrdal saaayltfye dgeirvveii
      121 dgpraprvdl wvgfedagha talgkcvlre lddearddyl srhpltdltp rtitgraell
      181 rqldttplqp amtdmeeyal gtfcvavpvy sgetlgslgv slradrisri devrnrlipa
      241 agrvtrglsl ti
//
LOCUS       WP_457680738             254 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457680738
VERSION     WP_457680738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26625
     Region          5..205
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          6..35
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          37..73
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          78..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(80..81,84..86,88..89,93,96,105,107,111,115..116,
                     119..121,123..124,128,131,139,141,143,147..148,151..153,
                     155..156,160,163,172)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          107..139
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          141..172
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          174..205
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtetltprli savyanevdt vgellrqgas paapdagget plylaavsgq sdivrlllea
       61 gaspdtesrg qpgseglplc aaacwghdev vrallahgad pdlreddgts ytplmwaatn
      121 ghhrtaqlll egqadpdagh rdrtplmvaa ergsiavvra llhhgasprl tdaqgrtach
      181 lareesgkdi eselrrkaga apdarcevrr sprpegtelv eltvhapdgt ggaeyhqetg
      241 haaivallee ntpd
//
LOCUS       WP_457680740             359 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680740
VERSION     WP_457680740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38913
     Region          3..343
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mssltglrfa aavavlyths mlminphlak tlgpevwvgg savslffils gyvlthsarp
       61 gdtarafwrr raakifpnha ltwcivvgal acagattfse gsgiaaslss lflvhtwvps
      121 hlfvsagnpv swslaaevff yflfpfmlpr ikrlsprgll igaataiavv wlwpvfcalv
      181 vnpdgssfpe ywflymlpvt rlpefvlgml aariassglr iprigvipsa lgvisavimn
      241 saflpqgfly aastvaplvv lvyataeldl rdrtsllrtr plvllgemsy amylvhflvl
      301 gllylglkdh gwsnlsvvll gipfvlltsw llyagverpc vrrfstprar artraaaas
//
LOCUS       WP_457680743             359 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457680743
VERSION     WP_457680743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36613
     Region          105..156
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          172..355
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(204,229,264,267..271,273,281..285,288,292..295,297,
                     305,310..315,330..332,337,341)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(204,293,295,297,310..315,330..332)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mkhtrvptpr tvltgaalvv altaatltlr tadaapaknp dppsasaagq rakglsstlg
       61 adgagayyda ehhklivnvt teaaaakara agaeprivkh slasldaara tlkkqatipg
      121 tswgmdprtn kvvinadrtv qgdkleqlkr vatslgdrva lrqsadalrp liaggdaiwg
      181 tgarcslgfn vtkggqpyfl taghctnavr swsatqggte iavteagtfp gddfgivkyt
      241 aadilhpsav dlyngsmqti akagdpivgq kvqrsggsth vhegdviale vtanyqqgsv
      301 dgliqatvca eagdsggsly egdtalglts ggrgdcslgg vtyyqpvrea lektgaqig
//
LOCUS       WP_457680751             205 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680751
VERSION     WP_457680751.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22874
     Region          1..99
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mtatvkgspl gltvlvllhh rplhpygiqq llkrwgkvhv vnvgqragly rtierlqagg
       61 liavrqterd qlypertvye vtdegravtr dwleqmlavp kaefpvfpaa lsnmlmlspa
      121 evlpilerra arladrrael erqtadaevg lpritliene yllavlgaee rwlqgvmsdl
      181 rdgsltwsae mlaafqease ptsde
//
LOCUS       WP_457680757             181 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Streptomyces nigrescens].
ACCESSION   WP_457680757
VERSION     WP_457680757.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18639
     Region          49..165
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mpyltaavvf vgalsalnlv lalamvkrlr ehsglltgrr gapsaelevg triaefetvt
       61 eagepltras laddllvafl spgcapcvek lpafvahtrs lpggrrgvla vvvgepweaa
      121 afaaplgpva qvvieepnga lsrafgvhsy ptllrigpda egrpvvtsna vdlkrptama
      181 a
//
LOCUS       WP_457680769             187 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680769
VERSION     WP_457680769.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20720
     Region          13..178
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mfaislgddg aelrplepwh ageflahmdr greyigqyva lpdratdlas ataflqmyad
       61 kaaadsgrly giwsdgvlvg gvlfvtfdvt fgsceagcwl eesavgrgli trairviidw
      121 aveergmhrv ewiaasantp sinaakrlgm vregvqresy phrgvrhdme vwsvlapewr
      181 rqretar
//
LOCUS       WP_457680760             633 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457680760
VERSION     WP_457680760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 633)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 633)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 633)
  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 633)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..633
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66948
     Region          45..620
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mkpvpkpaap gpvphtppqs atdgaaplrl araactlvaa aapvlltgya vltlaagvlp
       61 vatawltklv ldaladgapl aqvarpamgl aaagvalvlt gevaqylraq lgrevavtaq
      121 erlyravdgf vglrrledpa fldrlrlaqq sggaspgqvl davltvagsv ftvtgflgsl
      181 fvlsplmtll vtaasvpvla aelwlsrlra rmawdlgpve rreffystll srmeaakevr
      241 lfgtgaflrg rmvadrravn earrgldlre arvqtalgll aalvsgggll wavaaardgr
      301 lsvgdvtifv aaiggvqgal aslatafart hqalllfghy tavvdagpdl pvppeprtlp
      361 alrhgielkd vwfryaddhp wvlrgidlfl phgtslalvg lngagkstvi klicrfydpt
      421 rgavlwdgvd lrdtdpaelr srlgavfqdy mnydmtaten ialgdisasp dhsrvaaaaa
      481 ragiapqlaa lphgydtlls riffagtdrd dpetgvvlsg gqwqrlalar aflrdrrdlm
      541 ildepssgld aeaeaeihss lkrhrsgrts llishrlgav readtiavlr dgriaelgsh
      601 dalmaaegay arlfalqaag yrdttaapng rqp
//
LOCUS       WP_457680778             307 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680778
VERSION     WP_457680778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31607
     Region          19..284
                     /region_name="F420_MSMEG_4879"
                     /note="F420-dependent oxidoreductase, MSMEG_4879 family;
                     TIGR03564"
                     /db_xref="CDD:274651"
ORIGIN      
        1 mtvgvalnat gadnqvdatv rlaeeaaaag lrsawfgqtf gadspqlsai vgravpglhv
       61 gtsaipvfgr hpllissqaq taqaathgry hlglalgtkl lteagfgiph erpiarlref
      121 ltalrqltet gtadfhgell tattpiparv pgaesgvpll vaamgpqalr vsgqladgil
      181 pylagprala ehivpavtaa aesagrpapr ivalvhgvvt ddvdavreka teqlafyeqf
      241 psyarvigls ggkraadvav igdegtvaae vrryrdagat evvfsgteia gdadrrrtwa
      301 llgelag
//
LOCUS       WP_457680784             503 aa            linear   BCT 27-JAN-2026
DEFINITION  PepSY-associated TM helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680784
VERSION     WP_457680784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=53387
     Region          33..449
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msteqrlsss dspgspdptr sgeertvrht gwaalrplvl rlhfyagvli apfllvaavt
       61 gllyacsfqa ekvayahelt apagteklpl sqqvadarka hpegeiaavr papqpgdttr
      121 vllsdvpgvs ddhqlavfvd pytgnvrgal etygstgalp lrtwldalhr dlhlgeggrl
      181 yselaaswlw vvaggglalw igrrrknrgl ralalpdrta tgrrrtlswh gavglwaavg
      241 liflsatglt wsayaganig dlrealgqat ptvstavtks daghdghgss sgmagmpdmp
      301 gmggtkenps sgsapsdvgi dkvlraaraq glsdpvevgl ptdegtayvv kqvqrswpek
      361 qdaiavdpat gkvtdvsrfa dhpvlakltr ygidlhtgtl fgianqiala alalalifli
      421 lwgyrmwwqr rptrdralsf grpmprgawr qvplpvlipl vlavgamgwl vpllgislva
      481 flavdialgt larrrrvstt agd
//
LOCUS       WP_457680781             578 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457680781
VERSION     WP_457680781.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
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,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 578)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19831406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..578
                     /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=61748
     Region          85..578
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
     Region          355..578
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mspevagpat apaplpdrap pgpgplfrlp glpswwrpwg attldvliam gcawfdaqfr
       61 tsfveeqlhs plpqgwavgl tvvgalllvl rrrfpaavta aitcglllgt gsvlatvvaf
      121 yslarhtprv rtvfvaapvg lllvlgvavl hlrqyaphhg tevtrepvli alvaltgvvv
      181 pvltglypra prqpwwwehr samlfdvllv llfplanpva lvsglngpdd dpllvpapvl
      241 vllvmvqgva liwrrrypda laavavilip lvlpsfsilp vslyalakyg asrrnlllgs
      301 gaaavvlvaw tvaatefeae qfipysiflv vpsvvvpvlf gmyrgakrsl mvtlqdradr
      361 lereqhllas qarmeertri aremhdvvsh rvslmvvhag aleagaggpg vatdtgrlig
      421 dmgrqalnel rqvlgvlrld dgeqqvplsp qptpedlatl veesraagmq iafdvigeps
      481 atdstvqptl yrviqegltn ahkhagnvpa rvevryrkdt vrviveneap agpvptllps
      541 gghglvglge rvtvlggtfe agalenggfr itatvplr
//
LOCUS       WP_457680792             384 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680792
VERSION     WP_457680792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39230
     Region          29..379
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mptrrtsdvi vvgagvvgaa cayyaaragl svtvldrgpv aggttgageg nllvsdkepg
       61 peldlallst glwrelaell ppqieyepkg glvvaageag mqalrdfaag qgkagvraee
      121 vqgdrlqele phltpglagg fhypqdaqvm palaaahllr aagdrvclrl geevtgllta
      181 adgsvrgvrt aagevhaphv vnaagtwgge farlagvglp vlprrgfvlv teplprvvrr
      241 kvyaadyvad vasgsaalqt savvegtaag pvligasrer vgfdrtlste vlrrlaaqat
      301 alfpvlagvr amrtyvgfrp ylpdhlpaig pdprvpgllh acghegagig lapatgllia
      361 rslgggelpl dpgpfnparf eata
//
LOCUS       WP_457680795             487 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680795
VERSION     WP_457680795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Blumer,C. and Haas,D.
  TITLE     Mechanism, regulation, and ecological role of bacterial cyanide
            biosynthesis
  JOURNAL   Arch Microbiol 173 (3), 170-177 (2000)
   PUBMED   10763748
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Castric,P.A.
  TITLE     Glycine metabolism by Pseudomonas aeruginosa: hydrogen cyanide
            biosynthesis
  JOURNAL   J Bacteriol 130 (2), 826-831 (1977)
   PUBMED   233722
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14289850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="FAD/NAD(P)-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50091
     Region          32..344
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     Region          394..435
                     /region_name="GlpA-like_Fer2_BFD-like"
                     /note="bacterioferritin-associated ferredoxin (BFD)-like
                     [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate
                     dehydrogenase subunit A, hydrogen cyanide synthase subunit
                     B, and similar proteins; cd19946"
                     /db_xref="CDD:381079"
ORIGIN      
        1 maasasdphd lavigagcag lagavaaagh glsvalldas pqtggqfyrh papalgaarp
       61 ealhhdwpaf aalrrrlers dvrqlsghhv wavtkedgdl wavhaatgad gaderpvrvr
      121 aravllatga yerqlpfpgw tlpgvvgagg aqamlksglv lpgrrivvag sgplllavas
      181 slaaagaqvp avieasgyqg yarhprvlaa nprklaeaav hgaallrhrv rlrtrsavte
      241 vhgtdrvsav tvtrldrdwr pvrgtgrria cdalavghgl vpqielatal gcatrttadg
      301 tlalaldglq etsvrglwaa getggvggae laraegelag laaavrlhgh pvhggrvrel
      361 rrrrdrmraf aeamavshap aagwtgwltd dtdvcrceev tagrireavt dlgardahtv
      421 klltragmgw cqgrmcgtaa aclaagggaa eppaerrpfa vpvplsalas pdestgsrpd
      481 aappvdd
//
LOCUS       WP_457680798             460 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680798
VERSION     WP_457680798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=46726
     Region          69..451
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mttavssvts rnpadpsdvl vsfpapgafa avaaverara aqpnwstgga aarssalgav
       61 aaaleaaade ltalavrevg kpltearaev artvaiwryy aqapyeplga vhetaagpgl
      121 lltrrrpygv aglltpwnfp faipswkaap alaagntvvl ksapeataca rrlaalveqa
      181 lpagvftvlp ggategnalv saadvvsftg stavgravvh tatargipvq aemgglnaal
      241 vlpdadieqa alhiaaaiag yagqkctats rviavgaald plrealpeal ravavgdpad
      301 astvcgplin epardrvgra wdglsvlagg tvpglpgwya aptlvekvpp dhpllreevf
      361 gpvaallpad dlahavritn svpyglvtsv hsagldpvlh gldrldtgmi rvnapstgvd
      421 fhlpfggake sghgpreqgr aalefytssr tytlspaetm
//
LOCUS       WP_457680810             637 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 5 protein [Streptomyces nigrescens].
ACCESSION   WP_457680810
VERSION     WP_457680810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Schroeder,H.R., Yeager,F.M., Boguslaski,R.C. and Vogelhut,P.O.
  TITLE     Immunoassay for serum thyroxine monitored by chemiluminescence
  JOURNAL   J Immunol Methods 25 (3), 275-282 (1979)
   PUBMED   762437
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..637
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=68711
     Region          101..425
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mclvltgvav pgataapaqp easaqgpsaa gkaaeawtap lstrgryivd adgrrfrlks
       61 anwdgaqgsw ngsgdindpa ahhsgqdshg iplgldrvgi aallkdfral glnsirlpfs
      121 nemihstarv pdaavaanpq lrgrtplqvf davvaaltag gfavilnnht nttrwccgld
      181 gnerwnsrqs trqwaddwvf marryqhnsr vvgadlynev rrdvlddpnw glgdrhdwqa
      241 aaqeaadril teanprlliv ieginwtglp vdglphgrpt lapvrtlsht lvtsgklvys
      301 ahfygytgph hsgatgvget sdpryqdltr dqlravlhdq afyvsaetgr hftaplwise
      361 fgtgseesgq aarawfgnlt dyladtdtdt dfaywplvgw stdgqgrpag dnwallrydn
      421 agrrtgvldg ddwrapawhr lmsapqktgp vpmtpawhll ttdhrdfvqs lsarslgdwd
      481 sgarkaacpd gerligisht rgrglctdap tardlrapgs vptvvrdery vpaggdwapg
      541 ysklqcpdgq fltgyslrge kvsaalctpa rtalgtngtt lwfdrgdnrp pgdpggdfah
      601 ghfkgqcpsh syaaglayts rlghqgrpda llcrslt
//
LOCUS       WP_457680825             402 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457680825
VERSION     WP_457680825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..402
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42530
     Region          147..392
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msqrsapppq asepgedire qvvrmaarle pginqlarlv verqraevpg fdrlpgdmqd
       61 leiasaarht irgflrsvqg ladtdaevlr eraiqraseg vhltgllrgy hvatevvtda
      121 lcaaarpgee aallwltrrl fttvnslveq ateayllgma gqqeakrela aallrgdapq
      181 evaarcglpl epgylvlsvr apvpqepvaa rrllhqvlvr lapaadgrvl slpneqgghi
      241 llplgtphad lvghlstgps rpviagaala atpgdvpaaa eqahriaaia rtpgvhrlqd
      301 vlldyhlags kdsaaelaaf ldpldghagl veavaafldc dldrrrtaqa lrvhpntvdn
      361 rlaraaqltg ldphtthgvq lfgaaltlrr laegsatgfl pg
//
LOCUS       WP_457680831             338 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680831
VERSION     WP_457680831.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34822
     Region          4..336
                     /region_name="CurA"
                     /note="NADPH-dependent curcumin reductase CurA [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG2130"
                     /db_xref="CDD:441733"
ORIGIN      
        1 mtvpstgtev rlaarpegwp ttgnfsvvra plpavgagqv lvrnlvmsvd pymrgrmnnt
       61 rsyvppfavg kvldggavgr vvvsksprhs vgdlvlhglg wreyavvgaa gavtvdpala
      121 ppgaylgvlg mpghaayagl lkaaefrpgd tvfvsgaaga vgslvgqiar lcgaqrvigs
      181 agsaekvayl teelgfdaaf dykagpvldq lakaapagid vyfdnvggdq ldaalalarm
      241 garfalcgtv sqinekdgpa gprnlvqaia kgitlrgflv snyaglkdef tarmggwlte
      301 grisyretvv kglenapaaf idmlrgantg kmlvriad
//
LOCUS       WP_457680854             109 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces sp. 900105755].
ACCESSION   WP_457680854
VERSION     WP_457680854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..109
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11904
     Region          22..97
                     /region_name="HTH_MerR-SF"
                     /note="Helix-Turn-Helix DNA binding domain of
                     transcription regulators from the MerR superfamily;
                     cl02600"
                     /db_xref="CDD:470628"
ORIGIN      
        1 mtaddtfsrl ddvyractmg raaemlgttq gflravggar litplrsrgg hrrcsryqlr
       61 iatrarvlvd egtpveavcr iialedqlee aqcinaerrr saalhtaat
//
LOCUS       WP_457680855             492 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457680855
VERSION     WP_457680855.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 492)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..492
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54174
     Region          12..480
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msenvgdwsp eelekngqll lsqlrehfst lgnqpvttqr saqeiralld eplpdapqpf
       61 teilsqtwdd vrpnltlwnh prfhayfsns ssgpailaem ftaalnvnvm lwdaapaaaa
      121 veltvldwla qmvgytvaqd svlvdgaslg tlyglaaare hlagldirqq glagrdvprl
      181 riytsdqths sidkaaitlg igldnvvrip adpdgrldpd alrerlerde rlgyramavv
      241 anvgttsvga idpveeiaei caahdtwlhv daayggfwrl apqvgpqlpd lsradslvan
      301 phkvlmcpme asalfcrhrd altntfrvvp eylrtrhedg svdfmnyslq lgrqfralkl
      361 wwliksfgvs gltdrlsaaa alaeglrdra rsdpdwvven dtpfplvclr yqphdqeldp
      421 rdvdelnrri hravnkaggs fvshtvvpsg yairvsigni htteadihal waelttaarr
      481 cavprtpegs tr
//
LOCUS       WP_457680860             331 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680860
VERSION     WP_457680860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37026
     Region          7..177
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mftlplgdha rlrplepwqa qeflahidra rtsvdpwipw atfstdldsa tatlqryadr
       61 laqdtgriyg iwldgtlvgg vmfthfdsas gvceigcwle qagegrglvt racrmlidwa
      121 fqergmsrve wwvaagntrs idvarrlgmt rdgvlrqrss yrgarqdsev wsvlaeewps
      181 pgeasgsrvq aeldrlmrvf tgaftntgds rpdlgvirdv fipqgriian vgdepviydl
      241 dafieprqkm ltdgtltefc ewevaertei sgsiahrfse yrksgfhhge wfegtghktt
      301 qfirtpsgwr msslawddap atatatatvt d
//
LOCUS       WP_457680863             182 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457680863
VERSION     WP_457680863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..182
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19807
     Region          13..166
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mtelgpvawp papirterlv lreseardra afielfaspe vgtyiggprt rdeldravpe
       61 vpgrrpgffv vdldgamigm itfdrrgaeh pghvhpeage pglgymflpe awgygyaaea
      121 caaaldwftg alpsepvvlc tqtaneramr laaklgftev erfeeygaeq wfgvwspvtp
      181 sg
//
LOCUS       WP_457680869             210 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680869
VERSION     WP_457680869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=21916
     Region          22..>185
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mptdthvrha vvmgagmagl aaarvladsf eavtvierdt lpsasaprag vpqghhvhgl
       61 lalgaevfeg yfpglraele qagapvwdwg eglcavlpng ippstpmgmp iqtfsrplle
      121 hvlrqrvtal gpvtlrdglt viglrtaapg kitgvrvrdg ggedeiaadl vvdasgrssh
      181 lpqwlaalgl phprtttvda heppdrhrpp
//
LOCUS       WP_457680872             287 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457680872
VERSION     WP_457680872.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=30377
     Region          33..284
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mtaeqlgtse satpesaise sgtsesataa etatyvyavs rrldpaalsg laglaegfpv
       61 rtlplgplta vvqhvpaaef tqdawqqrls draelercar ahhevvtaaa acgptvplpl
      121 atlyradera qqvlgadrar faaalarieg haewgvkvsl ptaapeppra gspgsgggps
      181 ggagrayldr krglhrareq hhdralqtae didaalsrla tatrrlrpht pemtgerhrl
      241 qvlnaaylvt tvrekellaa vetlrhrtga evevsgpwvp ysfvgev
//
LOCUS       WP_457680877             441 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457680877
VERSION     WP_457680877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45180
     Region          19..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(29..30,33..34,37,69,124..125,127..129,132,152,
                     155..156,159,232,235..236,239..241,244,268,272,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mgvkralvdv tplrrsapfr rlwlgqtlsr lggqmtlvav mfqvwqtths tvwtgavgla
       61 ravplivlgl fagslvdrvd rrtfylitts gqavcvslla lqgflgnfpt agvlllvavq
      121 scfvagsgpv srtflprllp kqqlaaglal nriafqgaml tgpvlgglil gglgaggvyl
      181 idaltfaaaf hgafglprmr pgdeparpgl rgvadglafl vrtpvirgal ltdlattvls
      241 mpislfplvn aerfgndprt lglflsavaa ggvlaslfag tftrlsrpgl vmlggsatwg
      301 aalalfglsa dpwtgpaflv lagaadtvav vsrstlvqlh tpdellgrvs aaeqivgqag
      361 pdlgnmrggl madatsgtaa lvsggllcig avalvgtttp glrfsrspsp spspspspsp
      421 spapspvpap crakwwslwa k
//
LOCUS       WP_457680880             518 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680880
VERSION     WP_457680880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56172
     Region          1..513
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mydyiivgag sagcvlaarl tenestrvll veagpvddaq eihvpaafsk lfqtkydwsy
       61 lsdcepgldg rrrflprgrm lggsssmnam iyirgnrrdy dawaaagaeq wgwddvlpyf
      121 lraedfrget spwhatggpl tvsegrsrhp lmaayvaasq eaghpytadf ngpeqdgvgy
      181 yhltqrdgmr cstavaylrp alerpnlevl tgaqctrvlf egsrasgvel erggdllqlr
      241 aerevvlsag aynspqllml sgigvadelt argitprvdl pvgenlqdhp higlsyltdt
      301 eslltaetpd nvrmletegr gplssnvgea ggfhrtregl dapdvqvhat pvmfheegis
      361 pvtdhafmfg avlltptsrg kvslrsaips akphilhnyl ttdedrttav ralrmlldia
      421 dqpslrkhrr adfrvpratd dagllefarr elqtlyhpas tcaigpvvds rlavhgvsgl
      481 rvvdasvmpt vvrgntnapt imiaekaadl irglpapa
//
LOCUS       WP_457680886             552 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457680886
VERSION     WP_457680886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57354
     Region          28..547
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mthrmhdlvp galrrtwaaq ghcpdldlya lfrahrmrdp lrtavidaqg easyaeldte
       61 arclaaglae agirpgdvvg vqlpnsraav atdlalaalg aialpfpvgr ggreavsllg
      121 rsgaraviaa ttyrgtehar elaerardlp alhtviaagp gpvpagcrsl adltgdertg
      181 ftperpdpds aarilvssgs eaepkmvays hnalaggrgn flasllvegt pprclflvpl
      241 asafgsngta vtlarhggtl vlldrftped alaalrthrp thvlgvptmv rmmvercate
      301 grtadgpkal ilggsaldaa theeaarvfg cpvvnlygsa dgvnchtgta qqpplpddgp
      361 givvgrpdpa vceiriappp gaasdgtgei largpmtplc yvgapelnmr yrtadgwvrt
      421 gdlgtlaadg tlrvvgrlkd ivirgganis paevegelss hpdvrdvicv gvpdplmger
      481 laacvvprag reitlqslca hldarglerr khpehllpvt galpltpagk pdraalrdrl
      541 aaglpdepar tg
//
LOCUS       WP_457680892             413 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680892
VERSION     WP_457680892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43213
     Region          25..404
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnagqqlsat dpplgsaglg qpgcppeida lrgrvmafvr ervmpcepvl daggaaarte
       61 lrglqaeakr eglwalplpe ewggqglalp lyshiaeaeg asdhgpaalg saplldvlml
      121 drhaddtvke rflrriadge vrtcyamtep etpgtdpglt atkavsdaag gwvlhgrkwf
      181 isgagdadll tvlaraddeg pgtdslslfl vpssaagftv vrelpvlgag gqweieldgv
      241 avppehavga pgqalriage rlvlgrvlrc lrwlgqaera fdlmclrars rsqsagplad
      301 rqlvqqmvfd sllairstrp lvheavarla aggdarletg lakvaaarml qqvadaaiqv
      361 hgaaglgpdt alpglfrtgr tarlldgpde lhitavarrv lrgypvtscp vts
//
LOCUS       WP_457680905             365 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457680905
VERSION     WP_457680905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37783
     Region          39..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matqkkdrip aalsaeahhd vvvvgggaag lsgalalara rrsvlvvdag eprnapadrv
       61 hnylgregtp psellaagra evaayggsvv sgrvvsarrr tgdggehegf dvaladgtrv
      121 rarrllvatg lvdelpevag laqrwgrell hcpychgwev rdqpigvlat gpngvdkall
      181 frqwsaevtl flhtapepse eqweqlaarg iavvdgkvtg veltddrltg lrldsgravp
      241 cravvvaprf aargavlarl gleadeqkgg eqvlgsavaa gpagatripg vwvagnvtdp
      301 yagviqaaaa gltaataing dlvkedtara vaahraripa prepfaarte aevcarvlgg
      361 rrhgl
//
LOCUS       WP_457680908             288 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457680908
VERSION     WP_457680908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29432
     Region          1..280
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 misgaaclsa samfvkladv tagtaaflrc alalavlvpl lvhevrrkgr larplqgyav
       61 vagiflgvdy vmwtmsildv gaavatvlin vqviafplla riidgtaisr rflftipvml
      121 agialssgal ehgegdgnpv rgavlgvaag iayaaylyln rvsgerspah vvtpicistg
      181 aaavaagvis lfttgislsm spmswgwvia lallgqvvaw llistgspkl apntsaalll
      241 lqpvmaigfg liilretpta gqlvgcvvvi aavwfsnrrp spsstsgs
//
LOCUS       WP_457680919             490 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680919
VERSION     WP_457680919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   McLeish,M.J., Kneen,M.M., Gopalakrishna,K.N., Koo,C.W.,
            Babbitt,P.C., Gerlt,J.A. and Kenyon,G.L.
  TITLE     Identification and characterization of a mandelamide hydrolase and
            an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas
            putida ATCC 12633
  JOURNAL   J Bacteriol 185 (8), 2451-2456 (2003)
   PUBMED   12670968
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Vasiliou,V., Pappa,A. and Petersen,D.R.
  TITLE     Role of aldehyde dehydrogenases in endogenous and xenobiotic
            metabolism
  JOURNAL   Chem Biol Interact 129 (1-2), 1-19 (2000)
   PUBMED   11154732
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..490
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_process="GO:0006081 - aldehyde metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53106
     Region          40..463
                     /region_name="ALDH_F3-13-14_CALDH-like"
                     /note="ALDH subfamily: Coniferyl aldehyde dehydrogenase,
                     ALDH families 3, 13, and 14, and other related proteins;
                     cd07087"
                     /db_xref="CDD:143406"
     Site            order(146..148,174,203,221,320,322..323,326,367,369)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143406"
     Site            order(148,243,274,277)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143406"
ORIGIN      
        1 mrnqlfaggi qdtadvheaa eandvadvne aaeandaart vgrlretfat grtrslawrr
       61 rqlkslrall teqtpalaea lrrdlgkspv etltsevrlv tneidhtlrh lhrwlrpqrv
      121 pvpaallpar artvreplgv vliispwnyp vqlslaplvg alaagncavl kpselapats
      181 aelarllpry ldqdavtvve ggvrqttqll eqrfdhlfyt gngtvgrivm taaarhltpv
      241 tlelggkcpv licpgddlat aarriawgkf lnagqsctap dhvlaigdta galerhlaea
      301 vramygpdpa rspdygriin drhfdrltal lghgrvvtgg ghdraaryia ptvladvepd
      361 apvmaeeifg pllpilrmpd ldtaltfina hdkplalyaf ttdrrtrrrl laetssgavg
      421 fglpnahltv pglpfggvge sglgryhgrh svetfsnaka vldkplfpdt vravyppftt
      481 akerlirrfm
//
LOCUS       WP_457680922             392 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457680922
VERSION     WP_457680922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..392
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=41832
     Region          184..390
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(191,230,268,371,374)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(191,371,374)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(191,230,268)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mndnttslfw nagwaaaiqr psegfhknwa qegfadqtvr qivrvtgsgt sariklshry
       61 gtaplelaga tialtgkgaa eragsvrplt fggarsvrvp ageeiysdaa evhvapfesl
      121 tvslyfarpt gpasfhaqay attyraegdq laaadpavfg ettvswyyla aveladggpa
      181 rddtvvvfgd sltdgfasti dgnrrysdal aerladqgtp rpvlnqgigg nlllndsawy
      241 gdragdrfrr dvldqpgvrs vvvlvglndi gfseielpty rpnpdqspae liagyrelir
      301 qaraagvrit gatimpfkga eyhtptaeak rrevnawirt sgefdavadf ataladpsdp
      361 dallpaydsg dhkhpndegy ramaaaidlt tp
//
LOCUS       WP_457680937             837 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457680937
VERSION     WP_457680937.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 837)
  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 837)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..837
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93060
     Region          10..832
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtlidhlpnd adpdalfeaf sgwaeqqgis lypaqeeali evvsganvil stptgsgksl
       61 vaagahftal andqvtfyta pikalvsekf fdlckmfgte nvgmltgdas vnadapvicc
      121 taevlasial rdgkdadigq vvmdefhfya epdrgwawqi pllelpqaqf ilmsatlgdm
      181 srfegdltrr tgkptsvvrs atrpvplsye yrttaltetl telletrqsp vyivhftqaa
      241 averaqalms inmctraekd eiaqlignfr fttkfgrnls ryvrhgigvh hagmlpkyrr
      301 lveklaqagl lkvicgtdtl gvgvnvpirt vlftaltkyd gsrvrtlrar efhqiagrag
      361 ragfdtagfv vaqapehvve nekalakagd dpkkrrkvvr kkapegfvnw gentfeklia
      421 sdpeplnsrf rvthamllsv iarpgnafva mrkllednhe prknqirhir raiaiyrslv
      481 dggiverlae pdtegrivrl tvdlqqdfal nqplstfala afdlldpesp syaldmvsvv
      541 estlddprqi laaqqnkarg eavaqmkadg veyeermerl mdveypkple ellfhaygly
      601 rkshpwvgdh plspksvird myeramtfte ftsfyelart egivlrylas afkaldhtvp
      661 ddlksedfqd iiawlgemvr qvdsslldew eqlanpevet aeqaaeradq vrpvtsnara
      721 frvlvrnamf rrvelaaldk veelgemdae sgwdvdawge amdsywdeyd elgtgpdarg
      781 pkllqiqeda ehglwkvrqt fadpngdhdw gisaevdlaa sdeegravvr vtdvgql
//
LOCUS       WP_457680943             851 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457680943
VERSION     WP_457680943.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 851)
  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 851)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..851
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90033
     Region          108..826
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mppyahaapl pdtdplqlpd perhvrafld avadglprsp gaalvtgapa favtapqhip
       61 eqrawaadva aghdagvris lrvevhgaea eepmafgeqr gevdgagspl rgdaagalss
      121 itfkavlqlh sltdptlvad aaevwagtst agqafgarar mdtlltlrra adawapltpl
      181 lsaavpdald ladeeiaell gpaagalaaa gvqvhwpkel trtlsaravv gppeagggdv
      241 segrgtglps llsadallsf swrfavgdqe vdraeldrla eagrplvrlh gqwvlidpta
      301 vraardrqer kvtpldalga altgsvedgd ggrvevaasg wlarlrdrla dpeggdttpv
      361 rqpaaltatl rdyqlrglgw lhrmtslglg acladdmglg ktitlislhl hrqtapasag
      421 ptlvvcptsl mgnwqreiek fapgtpvrrf hagrrslael adgefvltty gtmrvdagkl
      481 aevgwglvva deaqhiknpf sataralrtl pakarvaltg tpvennlsel waildwttpg
      541 llgplgrfrt hyaqaiegga aaspeagaaa erlarlvrpf llrrrksdpg iapelppkte
      601 tdravaltke qtglyeavvr eglaeiagtd gfarrglvvk lltslkqicn hpaqylkesg
      661 paedgraaga vriagrsgkv elldelldsi laegasvlvf tqyvqmarll eghlaargvp
      721 tqflhggtpv arreemvrrf qdgaapvfll slkaagtgln ltraahvvhf drwwnpavea
      781 qatdrayrig qtqpvqvhri itegtiedri admlarkqql adavlgsgea amteltdael
      841 adlvalrgne r
//
LOCUS       WP_457680982             502 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Streptomyces nigrescens].
ACCESSION   WP_457680982
VERSION     WP_457680982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..502
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52506
     Region          16..443
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 msdprhhgaa paldgiwlgl dlgtqsarcv avdgtgqvla taarpltgrr dgnrheqdpe
       61 ewwralgaac rkaldgldtr rirglavdgt sgtilladhr gtprtpglmy ddgraaapaa
      121 avnaagekvw qelgyrsmqp swalpklval leddpglrtg srllhqvdli twrlagrqla
      181 sdashalktg yhlveerwpq evmdglgvpe sllpevvrpg splgtvcapa aeatgipegt
      241 tivagmtdgc aaqigagala pgawnsvlgt tlvlkgssph lvrdpagvvy chrgpggtwl
      301 pggasssgag ilsqrfpgad ldaltaqaaa ldpdavaypl vagggerfpf rapgaapfll
      361 geaptraaef hacllgvacl erlcfdyldh lgapvdgplt ftgggarnay wcqlradvlg
      421 rpvrlpqqae galgmavlaa tssgtglqea aaamvrtare itprpdrtar ylpvhlrfid
      481 eltrrgwldr svadharrra ap
//
LOCUS       WP_457680984             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680984
VERSION     WP_457680984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31153
     Region          8..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          108..273
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdtstagelg dflrsrrari qpeevglpgh grrrvpglrr eevaqlagvs vdyyirleqg
       61 rspsasdavl daigrvlrld dterhylrtv arpaarrtsa agpadrkvrp glrllldame
      121 kvpafvlgrr mdvlawnalg davvgfsqmp peernmprqv flnpqarely pdwpavaaet
      181 vaylrldags hprdkqlatl vgelslgsed frrlwadhqv kektygakrm rhpvageltm
      241 pyetltvsge pdqmlvvytp epgsrtadrl allaswtasp av
//
LOCUS       WP_457680994             298 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457680994
VERSION     WP_457680994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33022
     Region          11..91
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(37,62)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(44..45,56,59,63..64)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..282
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdtpamdfpa elgnflrtrr arlqpedvgl vrygtrrrvp glrreelaql agvsvayytr
       61 leqgqshqas egvldalara lrltaderah lralarpgaa prrpavrhdk vrpgvrqlla
      121 avadvpalal gpryeilawn rlghaltagh ldfdspgrpq drpnaqrllf ldphtrelyp
      181 drdeetqrav salrvtagqr pddqqlaeli gelsmkssef sslwarhvvh nctfgtkrfh
      241 hplvgdleld femmqtpdgs gqgvlmytaa qdspseaalr llaaergpvv rvleperp
//
LOCUS       WP_457681002             374 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457681002
VERSION     WP_457681002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="trypsin-like serine 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=38021
     Region          141..348
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 metsergtvp adnadraagd agapapevcp gpggpactgr gregvplrvt lalgvltvvm
       61 ggtvlalgsp srdpflapgd tatgsytatr adgdqaaaav lagpyterpg ppvaarhsgv
      121 maapptasrp llavpaapsp aigalfspaa dgtpahhcta svvqspagdl ivtaahcvhd
      181 ggfrtrlvfa pgmhdgiapy glwvptrihv dprwirdrdp dhdvaflrmr ragraggria
      241 dltgaerirf dapagrpaql tgypedqdtp vscrhtadaq gpaqlrftcr gfpngtsggp
      301 mltdvnpatg tgaligvigg lneggdnlvs yssrfgedva alyrrataep gpwppqprar
      361 adasgvrppa aprs
//
LOCUS       WP_457681011             404 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphodiester glycosidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681011
VERSION     WP_457681011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gorelik,A., Illes,K. and Nagar,B.
  TITLE     Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme
  JOURNAL   Structure 28 (4), 426-436 (2020)
   PUBMED   32109365
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Das,D., Lee,W.S., Grant,J.C., Chiu,H.J., Farr,C.L., Vance,J.,
            Klock,H.E., Knuth,M.W., Miller,M.D., Elsliger,M.A., Deacon,A.M.,
            Godzik,A., Lesley,S.A., Kornfeld,S. and Wilson,I.A.
  TITLE     Structure and function of the DUF2233 domain in bacteria and in the
            human mannose 6-phosphate uncovering enzyme
  JOURNAL   J Biol Chem 288 (23), 16789-16799 (2013)
   PUBMED   23572527
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..404
                     /product="phosphodiester glycosidase family protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40354
     Region          <294..402
                     /region_name="NAGPA"
                     /note="Sugar-P-sugar glycosidase (uncovering enzyme, UCE),
                     NAGPA superfamily [Carbohydrate transport and metabolism];
                     COG4632"
                     /db_xref="CDD:443670"
ORIGIN      
        1 mravltvlma wgvlagggva agapataaga glhrsgaasv apgvaygefr mtlprgtvhg
       61 hlltvdladp rvsvdllypg avgarspvsq laaerravga vngdffnite tqhpgvqatg
      121 asvgpavasg rqlkgavpdg qrfgpvmppg attedvlgvg ydrrarldrl tlrgavltge
      181 galplrglnq yalpvggiga ytpqwgpasr vratcgtdtd raapcsaeta evtvrhgrvt
      241 avgdvpgagg vavgsvvlvg reegarrlrt lrigepvsvs sylvgrghgr lrcavggfpi
      301 vrdgapvagl dtiavavrts agigaggrll ylmaldgapg qtgltvrela dlmaqlgard
      361 amdldgggss tlvtgdayga tvrnhpsgga erpvpnalgv fsag
//
LOCUS       WP_457681019             351 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457681019
VERSION     WP_457681019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39295
     Region          15..327
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mvelrekwpi lgrheqaaaw lqvwqdlgra prtidayarg laeylelcer esvdaaqatr
       61 ahvalhvrel ssrpsrrgvn vvaldsgagl snatlqqrlv svrlfydflv eeglrqdnpv
      121 grgrytpgar gggqrglvrr lvklpwipsd eqwravlaia aaepvrtrlm lamaydaalr
      181 reelcslrtd dldpgrrlvr vraettksrr ervvpysaat gvllsqylvh ratvsrargg
      241 lflsesrrnf aqplslwtws kvvrriaves gverfsthtt rhlcltdlar mgwevhaiat
      301 faghlhtdst mryihlsgrd laeklargme hihtqrvall sagaegtgqp r
//
LOCUS       WP_457681022             784 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457681022
VERSION     WP_457681022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..784
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=87339
     Region          292..633
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mralalaagk tapewawple gaswdrdpql sadehavlvq agprlfhssr ltraersala
       61 rllgpleqvr sclripdkag hhrwvdyqvv gmllvhtaea gsawwswdqs vwtrvigada
      121 eewsrqwpaq asrscrprll ayayllgapv dealflgfer lrlartvfgs esvdrevdtv
      181 ysllrgwgyr ldttgnrsvr tliahamlln rsplladmda alverlreav cstgrasgdl
      241 hslqralaal grceppvarn ekllgelgaq rwtnvpapwa emvcrwfdts ilsrnvrlay
      301 rqdlartgrw laaehpqite paqwtraica awvatvdrmr igdyaertat rgvfgdpmsp
      361 stkdsaltas raffrdlqew ewiprrfdpg raletprsvr allgpnprvi adevwakllw
      421 aginltsedl ptsssgpryp lelsravalt wlfsgqrsde irrlrtgcvr wqhdgtavsp
      481 daadvlarda vclldvpthk tgtsftkpvd pllgqaievw qavrpeqpmm ldaktserve
      541 fmfahrakrv skdyinrtii palctkagvp dsdvrgkits hrarstiasq lynakepmtl
      601 felqawlghr spsstqfhak ispktlakay seagyfarnv rtievlvdrd avasgaaaag
      661 epwqyydlgh gwctytffeq cqhrlacarc dfytpkgssr aqlleakenl qhmlasiplt
      721 ederaavddg qtaiealldr ltdtptpagp tprelglpat atmlpivevr qvpddvvtrt
      781 arrv
//
LOCUS       WP_457681033             158 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE family toxin [Streptomyces
            nigrescens].
ACCESSION   WP_457681033
VERSION     WP_457681033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=17494
     Region          11..98
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 msraryafaa hpealadlrs vpediralal lelqhlvhgn ergaalhrel vgchkvyvdp
       61 etrwrlviqy rdapassqhk reiyllavge rqdqaayrta arrlererea saatqplgrr
      121 aeaararsph gssgsratth pqtpaapatq prgrrarc
//
LOCUS       WP_457681044             198 aa            linear   BCT 27-JAN-2026
DEFINITION  DnaB-like helicase N-terminal domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457681044
VERSION     WP_457681044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10466160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="DnaB-like helicase N-terminal domain-containing
                     protein"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=21257
     Region          <15..103
                     /region_name="DnaB"
                     /note="DnaB-like helicase N terminal domain; pfam00772"
                     /db_xref="CDD:395624"
ORIGIN      
        1 mrvlrswtrs wagstpadfa daghqqiyrs lgalhhrgep idqltmlwet qrrgaladrt
       61 ldagrvlric dpsafagsae yvgeqvvras lvrtaaasar qvriladdes lapgqligya
      121 lhtlgpleev rrrwriatgt qaepsraagl paadppaari eaarsrsrpd lsstapaaas
      181 taasrravld rphrrsps
//
LOCUS       WP_457681050             597 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457681050
VERSION     WP_457681050.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..597
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62930
     Region          169..566
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mssprtstps tttgtdllly lllavaglgm aggslawlfg nltnaiagsd pwaayhpekt
       61 llhpervwph lpqptlitgc yvlpalvlta tavvaakvwl ryrsspsgla trrdleplla
      121 kqtaakaidl rpslagkkpn dvapddrgvl lgtfkpgkde lrsswedvil aimaprsgkt
      181 sglaipatlr apgpvlltsn kaardaytat idaraevgtv wtldpqqiah apqtmwwdil
      241 adardlagar rlaghfvtas vdessagdfw staaantlta fflaaaharr pitdvltwla
      301 spadrtaidl lqdagfdava aqlqgtvaga vetrdgifet arqyasclld pgiaawvtpp
      361 khlekmrefk peafatskdt lyllskdggg sasaiiaaaa davmraaviq aeldggrlda
      421 pllaildeaa nvckiadlpd lyshlgsrgv ipmtilqsyq qgvrvwgqsg mdallsaati
      481 kvigsgmdda dfadkisrlg gehdvrtisv stgesgksts vsmrqervlp ldvlrampkg
      541 tavlmatgir laridlkpwy kgrnakklga asakataais eraaakalrq ddftpaa
//
LOCUS       WP_457681081             378 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457681081
VERSION     WP_457681081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38226
     Region          179..377
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrkvaaiagg vvlapmllia piavalagas naqaaacgea ggggavdaka vakqvesilk
       61 gggkgsvsvs gldnpkeqip naktilatgv amkvpprgqv valatalqes glrnldygdr
      121 dslglfqqrp sqgwdtaqqv rdpahastkf yegllevsgw qsmtiaqaaq avqasgfpda
      181 yakwealata lqkaiakdlp akggsgkdag kgaqpgfpsg gcgtggdgsg fgpipagsvp
      241 kgykipadap kavrtairwe lgqlgtayqw ggsctdphgq dpmgrcdcss lmqasykagg
      301 vsisrttytq vkegkavsvd alkpgdllft rgtaavpehv gmfigqglil qapktgdvvk
      361 istlaswrpg vlaarrvv
//
LOCUS       WP_457681095             321 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681095
VERSION     WP_457681095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /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=35574
     Region          14..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkasrllhll lllqtrqrit ttelakrlev srrtvlrdve alstagvpvy aergrnggiv
       61 llpgarlnas hleppeleal svagldsaql ermglsavqe saarkiaarq aaapespsll
      121 rladlvlvds nawladskpa vdvsdlasal rhrrrlriqy rrsaekqasa rvvdpygiva
      181 ksgrwyliad dhgtgrlfal erlsayeqld apavlrpeet lrtrwaalke rterpgrvsv
      241 tvrlrengld larrilgtri hdvsdtengw ctivvrypdi esvrqllqfg nhieiltpet
      301 arkrisqlak dlterhsapa s
//
LOCUS       WP_457681115             413 aa            linear   BCT 27-JAN-2026
DEFINITION  MinD/ParA family ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681115
VERSION     WP_457681115.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Lutkenhaus,J.
  TITLE     The ParA/MinD family puts things in their place
  JOURNAL   Trends Microbiol 20 (9), 411-418 (2012)
   PUBMED   22672910
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Szardenings,F., Guymer,D. and Gerdes,K.
  TITLE     ParA ATPases can move and position DNA and subcellular structures
  JOURNAL   Curr Opin Microbiol 14 (6), 712-718 (2011)
   PUBMED   21963112
REFERENCE   3  (residues 1 to 413)
  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   4  (residues 1 to 413)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Surtees,J.A. and Funnell,B.E.
  TITLE     Plasmid and chromosome traffic control: how ParA and ParB drive
            partition
  JOURNAL   Curr Top Dev Biol 56, 145-180 (2003)
   PUBMED   14584729
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418836
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="MinD/ParA family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43284
     Region          183..410
                     /region_name="FlhG"
                     /note="MinD-like ATPase FlhG/YlxH, activator of the
                     FlhF-type GTPase [Cell cycle control, cell division,
                     chromosome partitioning, Cell motility]; COG0455"
                     /db_xref="CDD:440223"
ORIGIN      
        1 mpsgdgwqgd vlrdlrggae qgaqgpggqa yrasapgral paqgtqalda ahgggappqa
       61 gyqyggqeqh aghpggwpqq agyqqqrqkq qapaargpep qpqsapgsrp vvdeglagtl
      121 rskprhgesf aaraaralrr tlsssaasev aeitrtaavl qqpvttgrqi avtsirggsg
      181 kstvaallgt ayahyrhdpv lfleadpalg slplrlgaea lrwttsdiad ivkadmslld
      241 vtgylvqlpn nawllpasqg qigvmldsra yeravvalrr yfgvmvidce tlptevarva
      301 laaahgrvlt tpatpegits tfsvlqwmqg lprhviagtv vvltelvahs gvdldeaaqr
      361 lrstgvsvqv lpydrhlaag grvqtellaq ptreaaaria advfqlslaq qrh
//
LOCUS       WP_457681166             505 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681166
VERSION     WP_457681166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..505
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53291
     Region          103..495
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mpervvahll gdegldpelc ggevellpag qraagdmgsa artddasfag rlaalagerp
       61 lavhlrerrp gtaaepvtdg lrraglpvlr yrpdghhgdg aglagallre arlrgaavvv
      121 gplperpgal aralaggdvp vvffgsepyd pdwapdsglf aldapddgaa adevwstelg
      181 svdegfdlaa avapyrlgaa qirraaraat alaafdgtpv taahiqhsar qqsaplldrh
      241 arrvrpavgf dglvlppepl sllhelvqra rhrekvlgtw rlrtgggrgr gvvalfages
      301 gtgktlsaev vagalgldly vvelssvvdk yigeteknle rifseadrtd avllfdeada
      361 vfgkrsevks shdryanles ayllqrleaf dgiavlttnl ranideaftr rldlvvdfpf
      421 pddgrrlalw rsclaatpca ddlgldvcak efelsggair saavtagyla agrggpvtaa
      481 dvragarrey rkmgrlvpda splwd
//
LOCUS       WP_457681160             977 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681160
VERSION     WP_457681160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 977)
  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 977)
  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   3  (residues 1 to 977)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 977)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..977
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=103098
     Region          34..282
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          208..938
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 maggqgqgse ravrggadvl kgaegvgspd rgdrlrfqll gpvrawrgdh plnpgppqqr
       61 avlavlllha grpvsvpqlv dalwgeqppp ravgtlrtyv srlrgllepd rrprqqahll
      121 vssgggyalr vpgealdasv feerlatarr lreaddtaga yeqlrgalal pagmalaglp
      181 gpyaqrqrnr ltelcvtaqe elfdcvvelg gqagaiaglr afaaehplre rtqallmral
      241 hragrqaeal avyaatrrtl daelgaepgr elralyeevc agsrgsgtgs rpgpgtgpvg
      301 dqarpdrdrt gdsrdhrphp prparstsri gppppvpaql ppdiadfagr aeavaqlapa
      361 lrgaagvrap vvatlsglgg vgktalavhv ahsvrahfpd gqlyvdlqgs glapedssav
      421 lthflhalgv aesavpdgpa qkaalyrsll adrevlvlld nardsaqvrp llpgapgcav
      481 lvtsrartla lpgadrvdve vmaegealrl lgaivgaerv aaepiaarel vavcdglpla
      541 vriaaarlts rpgwamaglv arlseerrld elrvgdlgve atfrvgyevl gpglahafra
      601 lalcgmpsfc rgaaaalldt tddeaeeave alvdaglvel hgedryryhd lvglfarrlg
      661 erhdspcera aaqhrffgyv latvltavrl tephrvlpgl lhhpdspgrt ladadaaraw
      721 lhdahprlya avewalgaap gllgsavdll tawsqvlggt arhsaleplv rravdtarrh
      781 gddtatahal rllgapdhgt apdhgtaphh gtetyawaer apgeslrsah asagppvsal
      841 aerelavvpv tmdreraapp lrtavldgse yrlrqiryra rcalrrdgpp rqaaapcrqa
      901 rrrcrlraac drarlgpges ergpplptpa pppgrgcgcg sanmgnaavg rppqpcrgaa
      961 rcrkdiplcp rlcpyar
//
LOCUS       WP_457681181             177 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457681181
VERSION     WP_457681181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19875
     Region          8..159
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mptseltfrt aldadvpglv gliesayrgd vsrsgwttea dllagrrtdp davtavvrhe
       61 tgrlliaerd geliaccqie hrgdhayfgm favrpelqgs glgkvilaea ertaqeiwda
      121 remrmtvirq rteliawyer rgyrrtgert pfpygderfg ipqrpdlefe llvkplg
//
LOCUS       WP_457681183             300 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457681183
VERSION     WP_457681183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32223
     Region          <124..294
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mtygegvvkt rtaqtgaddg yvpsprrier erfkrararr atavaalstl vtgavlflvi
       61 trspgwprtr etffsleyar malpkvldgl llnlrlllvc gaavlvlgll lavartlrgp
      121 vffplralaa aytdffrglp liicllmvvf gvpalrlqgm ttdpvllggs alvltysayv
      181 aevfragies vhpsqraaar slglsggqal rfvvlpqavr rvvppllndl vslqkdtglv
      241 siagavdavy aaqiiagkdf nftpyvvagl vfvaltipmt rctdwitarm drrraqgglv
//
LOCUS       WP_457681200              61 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681200
VERSION     WP_457681200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..61
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7078
     Region          5..54
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mdqimwtvpa lanflgkpts wvydnhekqa ipsfrvgqql rfwpneimtw leencreqgv
       61 a
//
LOCUS       WP_457681209             275 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681209
VERSION     WP_457681209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29536
     Region          79..249
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(84..87,137..142,175,177..178,199,205..206,229,231)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(86..87,137,141,177..179,199,229,231)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mpkpisaarr tsmaglltaa slalalsgca tydvtapada raeapvaevt kkdaalaagk
       61 eakaprgaag dgvdcrkakc valtfdagps entdrlldil kkekvrasff mlgknhvekr
      121 paevkridae ghelanhtws hqilteispd aakremsrlq eavrkitgka prlmrppqgr
      181 tdgsvseisk dlglaqvlws vtakdyqtnd salitkrvle qterdgiill hdiyrgtvpa
      241 vpgilkelkk rgytvvtvsq llspakpepg mvyrp
//
LOCUS       WP_457681211             235 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457681211
VERSION     WP_457681211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  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 235)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..235
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24844
     Region          1..205
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrvlvvedee cladmiaael rraaivvdia hdgraalagl rlgaydvlvl dgelpaphgd
       61 alrryvvehg latrvlllta sapddrvagp epaaddclak pfaheelltr vltlgrparr
      121 mepqvierag vtvdtahrla ardgrplals rtefgvlevl lraqgavvsg delieevwee
      181 htsyggnavr vtlgalrakl gdppvieavp gagyrmtdgp gtggepepga rreav
//
LOCUS       WP_457681226             422 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457681226
VERSION     WP_457681226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43078
     Region          41..409
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,244,247..248,251..253,256,285,289,338..339,
                     343,347,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mspatrtsga arsgstspgp savadattep arspwdgrla vlavmlgifs ivtteilpig
       61 lltaigadfg isdgtaglmm ttpgvlaala aptvtvatar idrrlmlcaf vlllalanfl
      121 aaaataywlv llsrimvgit iggfwsigag laerlvrpea vgratavifs avplgsvlgv
      181 pagtfigdla gwrtafvvmg avavgvfvlt avvtpalpar qltrprvlre vlrrtptrfa
      241 llmtflivla hfgaytyvtp fleqvthlas pglvtvfllt ygaagiagnf lggatvarlp
      301 ratfgtaaal laaatlllpl lgrgawgala llvvwgiayg avpvssqtwf vkaapdapea
      361 asvlftasfq atislgalag gvaldhtsps tvmtlggata vlvaltawlh fagrhdwqrg
      421 nd
//
LOCUS       WP_457681232             501 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681232
VERSION     WP_457681232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53314
     Region          91..>246
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          409..493
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mttyphrall ltlsvattlt aaapavrada pdapgatvpa lawrpcaepg gpagqecarl
       61 pvpldyrdpd gpqlslavtr vrserpaarr gtllvipggp ggsgvqrlaa kgpalrkama
      121 gaydlvgldp rgtggstras celdaadrhl vtlrswpgpd geidgnvars rriaeacrrh
      181 ggavlrsftt vneardidrl rralgeekls awaysygtyv gavyaqkypr htdrwvldss
      241 sdpdparvgr gwlantsagt ddrfpdfaaw aadpareseg lrlarrtrdv rplflalaak
      301 ldrepkestt pgvpltgnrl rqalqnalqs dalfagtarl iqqaqdpaae pvlpdtlagp
      361 lsdqdaaamt atvcndvrwp asvpahrrav aadrarhplt aglpvnitpc gfwqapaepp
      421 tritadgpsn ilmvqnrrdp yspyfgalrm rralgerarl ltlehgghga ylnngpacgd
      481 rtvtaflttg rrpqtdshcg g
//
LOCUS       WP_457681234             436 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457681234
VERSION     WP_457681234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 436)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..436
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46959
     Region          58..433
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(104,126,128..129,212..213,222..223,226,229..230,233,
                     264,267..268,271..273,276,319,321..323,347,423)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(127..128,135,139,146,191,194,268..269,272..273,
                     276..277,280,318..319,322..323,324,347,374..376,379..380,
                     382..384,387..388)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mqheqsapap aptpaptptp tptptptptt eqtahgtavh pepvtlpvtr tpgcpfdppa
       61 elaelreqqp lrpmrypdgh vgwlatghsv vraiaadprf ssryellryp lpggpsgslp
      121 paplgdltgi dapehtryrr llagkftvrr mrqltarveq itadhldame rqgpvadlvq
      181 afahpvpalm icellgvsps drarfqehta mlsspdaape eqmaamtala ecvrelvvak
      241 rahptddlls dlttsdltdd elagiggfll aagldttanm lalgtfalls hpeqaaalrg
      301 dpgladqave ellryltith tglraaledv eldgqlikag dtvavsvqaa nrdplkfpdp
      361 dtldlrrkat ghlafghgah qclgqqlarv emrvafpalf rrfptlrlav ppedvplrda
      421 mniygvhrlp vtwdke
//
LOCUS       WP_457681240             396 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457681240
VERSION     WP_457681240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 396)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43321
     Region          20..396
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(66,86,88..89,172..173,182..183,186,189..190,193,225,
                     228..229,232..234,237,280,282..285,309,386)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(87..88,95,99,106,151,154,229..230,233..234,237..238,
                     241,279..280,283..284,286,309,337..339,342..343,345..347,
                     350..351)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtntpplktq ptvrscpfdp peeyrtlreq epvapvtfpd gaagwlvtry ddvrtvlsdp
       61 rfsakrivlr pggggmedap ppppglfimm dapehtrfrr lltgqftvrr mrqlapavek
      121 ivaeqldama aaegpvdlvq afalpvpslv icellgvpya dreefqrnsa tivrlnsspe
      181 efqqaqaamr gfihqlvlsk rdnptddils elvqsgeltd eelagvgvll liaghettan
      241 mialgtmcll qnpeqlaalr adpslmdgav eellryltvv qfgvrrtale dvelhgqqik
      301 egsmvvasla sgnrdtehla ddpealdvgr shtahlafgh gihqclgqql araemkaals
      361 alldrfptlr lavpveevpm rddmlvygvh elpvtw
//
LOCUS       WP_457681246             244 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681246
VERSION     WP_457681246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26222
     Region          6..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maalveqdsa kaariltvaq elvlkrgvkg vtvaeiaeka hvgkgtvyly wgtkedllvg
       61 lfareflavv egsidalttd pdaarphrlc pqlihngler pfvralqtgd sdllgvltqh
      121 prstellgtl gpaalmytvl pvwrqhrlar tdwpleeqay alqalmagfl etttrahtlr
      181 evtvdapdkv iaasvtallg pgeatpddvr atadeglrll rekrelvlas lagdhdtgqe
      241 tgqg
//
LOCUS       WP_457681257             359 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces nigrescens].
ACCESSION   WP_457681257
VERSION     WP_457681257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37879
     Region          5..340
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,227,314,316..318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,101,108,175,178,180,227,234,314,
                     316..317)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,101,175,178,180,317)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            180
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mttafdpiel ggkrlanrma mapmtrsray gpgasatelm aayyaqrasa glvitegvqp
       61 svvgqgypdt pglhsaeqva awrqvtdavh reggvifaql mhtgrighps llpdglipvg
      121 psavaakgqv ythqgpqdfv tpkelehdei vrtiadfada arnaiaagfd gvelhgangy
      181 lihqflapna nqrtdawggd vagrvrfave vtaavaeaig ahrtgirisp gtpfndiaet
      241 dpadleetyt alvaglapld laylhvlegp dqsltgrlrk dwpgtfvlnp fthpeptghd
      301 slgliengaa dmlafgalfl anpdlprrla sggpynepdr atfyggderg ytdypalpa
//
LOCUS       WP_457681285             272 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681285
VERSION     WP_457681285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /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=29724
     Region          73..131
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          159..265
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(223..224,227,239..242,244)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkrtfsallv casllvvagp pavavtpspa aavtppsaay rlpdlvpgip ragretagsr
       61 hieyvprsev ahagtralrc sastgpyqrq aerylgrqvd grqstgdcra irrfqqahri
      121 apatgfagpv tgatvrlmra kkdpnraghc pdlpqrtacv dlnrqlmwvq qsgrvilepv
      181 virsgaptme trtgsyriyl rhrrhisnly gtrmpyaqff drgealhgvy edifsgpgsh
      241 gcvnltmtda rrawevlrkg dtvyvwgrkp gv
//
LOCUS       WP_457681291             147 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457681291
VERSION     WP_457681291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15905
     Region          3..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 menevgheia dalglllrrt trtqlhkqlt egmgeavdel typvlsalar tgprsaadla
       61 pdvgvdrsgv trrasrleaa glihreadpd drrahllvlt eqgqravael rarlaahima
      121 slsswppgea eafaqhlrrf tvegpft
//
LOCUS       WP_457681294             207 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681294
VERSION     WP_457681294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 207)
  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   5  (residues 1 to 207)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=21299
     Region          19..178
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 mtlaataagq gflsptgvei afvlvgiatl gaavitvttr qlvhaalwlv valggiavey
       61 llltaefiaw vqvliyvgsv vvlllfglml tkapigrspd adsgnrwaal avalasagcl
      121 vwvvvdafra twisfegaaq gsteasgrtl fqywvlpfea lsvlllaalv gaivlsrrtg
      181 egraaaadlk tgasrgpaap apreeqr
//
LOCUS       WP_457681297             203 aa            linear   BCT 27-JAN-2026
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681297
VERSION     WP_457681297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="NuoI/complex I 23 kDa subunit family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22329
     Region          1..157
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 msfpgsglak glavtlrtmt krsvtaqypd vqpdlpprtr gviglfeenc tvcmlcarec
       61 pdwciyidsh ketvppaapg grersrnvld rfaidfalcm ycgicievcp fdalfwspef
      121 eyaetdirdl therdklrew mwtvpeppal dpaaeepkel aaarkaadkl aaqqaaeaea
      181 qaqseaadrg gdqdrpeipg egq
//
LOCUS       WP_457681305             437 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457681305
VERSION     WP_457681305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 437)
  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 437)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46221
     Region          32..221
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          229..437
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdtayaahpr gprvpvglsa pfsgrtwref lylflslpms vlmfvyaitv islgagllvt
       61 flgipvlagg lagsralggl erararallg ldvadpepar askpglmgwv gavlksgvsw
      121 rhlvysvlhm pwavfsfvfs vtfwsvgwal layplwrwtf layldqpgiq mwgdgrgngi
      181 yldtpadigf tsglglllvl agpwvihglt qvdrvmvrgl lgpsslatrv sqlesdrgvv
      241 vdtaaadlrr ierdlhdgaq arlaalamdl glakeklaed peaaarmvde ahgevkialq
      301 elrdlargih pailtdrglg palsalsarc tvpvtvtvdl dhrpaaaieg iayftasell
      361 qnvsrharat satldvwrta drlmvlvadn ggggahtgsg tglaglaerl davdgllivd
      421 spvggptsit aelpwrg
//
LOCUS       WP_457681249             257 aa            linear   BCT 27-JAN-2026
DEFINITION  LamG domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457681249
VERSION     WP_457681249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Hohenester,E.
  TITLE     Structural biology of laminins
  JOURNAL   Essays Biochem 63 (3), 285-295 (2019)
   PUBMED   31092689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Sasaki,T., Fassler,R. and Hohenester,E.
  TITLE     Laminin: the crux of basement membrane assembly
  JOURNAL   J Cell Biol 164 (7), 959-963 (2004)
   PUBMED   15037599
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10597119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="LamG domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=27046
     Region          94..249
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
ORIGIN      
        1 mtrrwslita iavltvalaf vvtqlvrgqg sgesgkgqag aepaspgaga eslrgvgwwp
       61 lhrsgtakeg ehdavvsggt qwtdgpegga lrldgtsgfa dtgsridteg kdysvaarvr
      121 ltpedlngvh talsqdgdav stfflqysgq denfafsfpg artvaeetgq pqtgrwyhlt
      181 gtysqkdhrm riyvdgrlag srgasskvkp tgavvvgrgk fggkaadhwk gdiadvhvyd
      241 reltpgevks lssrepd
//
LOCUS       WP_457681322             217 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces nigrescens].
ACCESSION   WP_457681322
VERSION     WP_457681322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23773
     Region          21..204
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtgtpltlpe ellllalepe rgrflnhary lryglagaal adleeagrit vgsgdritvt
       61 nplplgdpvl dgalaalpgp dkrgrgikae rwvrragrpv qelcvrrlee rgalrretrr
      121 alglfpyarf pagavdlvgp arerfaaalg agfpdrrgrl maalasatdl drrllispgy
      181 rpvrremkrf arefwmthav qravrqdkea ashaasp
//
LOCUS       WP_457681330             656 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457681330
VERSION     WP_457681330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..656
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70213
     Region          56..656
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mshqesaptg pltaptptsa ptptsaptht saptltepqk tvvngtvrev yvpplappvr
       61 sgslgdlpfl nadeapadvv larkqpsgiw rdvtaaefaa evravakgli ahglrpgdrl
      121 aimarttyew tlvdfaawaa glvtvpiypt ssahqaqwil hdsgaracvv egvdetrlis
      181 glrtelpald hlwqfntgav sqlvsagrdv pdeavderra atgpyalatl iytsgttgrp
      241 kgcalthanf faeadnavel lhpvfksvse epaatllflp lshvfgrmva vgclrarvrl
      301 ghapsirtdd lladlagfrp tfllaipyvl ekvfntgrat aekmgraasf dravriarsy
      361 geaveakehg tgpgpgvalk garklyaplv yrriraalgg kvrhvlcggs plgrrlaafy
      421 tgagieifeg ygltettaat tvtpplrpri gtvgwplpgt avriaddgei lihgdhvfsg
      481 ywdaalgaar pvtdqgwfat gdlgaldpdg yltitgrkke iivttggknv apapledrlr
      541 shplvgqcmv igdnrpyita lltlepdgla hwrqmnkkqd lpperlvrda rlladlqrav
      601 ddanelvsra esirrfavlp vdfseetghl tpslklrraa vardfakeia dlyesr
//
LOCUS       WP_457681335            1009 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional acetate--CoA ligase family protein/GNAT family
            N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457681335
VERSION     WP_457681335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Sanchez,L.B., Morrison,H.G., Sogin,M.L. and Muller,M.
  TITLE     Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming)
            gene from the amitochondriate protist, Giardia lamblia
  JOURNAL   Gene 233 (1-2), 225-231 (1999)
   PUBMED   10375639
REFERENCE   4  (residues 1 to 1009)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
REFERENCE   5  (residues 1 to 1009)
  AUTHORS   Mai,X. and Adams,M.W.
  TITLE     Purification and characterization of two reversible and
            ADP-dependent acetyl coenzyme A synthetases from the
            hyperthermophilic archaeon Pyrococcus furiosus
  JOURNAL   J Bacteriol 178 (20), 5897-5903 (1996)
   PUBMED   8830684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18515002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1009
                     /product="bifunctional acetate--CoA ligase family
                     protein/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.2.1.13"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0046356 - acetyl-CoA catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=106699
     Region          26..175
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          203..1000
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mqtppehayp thweadvvlr dggtarirpi ttddaerlvs fyeqvsdesk yyrffapypr
       61 lsdrdvhrft hhdyvdrvgl aatiggefig tvrydrineq glpaknpedd qaevaflvqd
      121 ahqgrgvasa llehiaavar ergirrfaae vlpanskmik vftdagythk rtfedgvvrl
      181 efdlepteqs mavmrgreqr aearsvqrll apgsvavigt grtpggvgrt alrslldsgf
      241 tgrvhavnha fpedlqrldp edvpavrtlr eitdpvdlav iavpadsvpd virdcgehgv
      301 qgvlvlssgy aeagpdgrer qrallrqars ygmrligpna fglintapdv rlnaslapqm
      361 pgaghiglft qsgaigiall sglhargpgd ggiagisafv sagnradvsg ndllqywyed
      421 pdtdvvilyl esignprkfa rlarrtaavk pvvvakgarh ngtappghav ptvrvpdstv
      481 aalmrqagvi rvdtvtelid aglllasqpl pagpriailg nseslallay daclteglrp
      541 qrprvlasaa tpddfraala ealsadgcda vvvtaipwvg egaavspggs egaaladalr
      601 taaaahpekp vtvvhlamdd laqtlaapap apapsaessa papdqaarpe paartinpap
      661 apapapappp ppippapshf prppaptgpp ptlaarqatp areaeagipr rprreplrip
      721 aypaaeravr slaeavryaa wrreaadpgr vpeyddiqea aagadierll drlgpdvpts
      781 rsvpvppqda eallarygih tlpvlpapdp dtavraaarl gypvalktta phlrhrpdlg
      841 gvrldiagea elrrtyaelt dylgspeelr pvvqsmvprg vdtvvraaid paagavlsfg
      901 lagapsqllg diahrlipat drevaeqirs iraapllfgw rgsqpvdtaa laelllrvsr
      961 lvddhpevvg vdlepvvvaa qglsvlgatv rlarppattd lgprrlpvy
//
LOCUS       WP_457681345             534 aa            linear   BCT 27-JAN-2026
DEFINITION  solute symporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457681345
VERSION     WP_457681345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10008332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..534
                     /product="solute symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015123 - acetate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55128
     Region          2..534
                     /region_name="ActP"
                     /note="Na+(or H+)/acetate symporter ActP [Energy
                     production and conversion]; COG4147"
                     /db_xref="CDD:443318"
ORIGIN      
        1 mtgdhqtlal llfsvfiavt laittwvsrr rrgsteefya ggrlfspmen gfaiagdyms
       61 aasflgisgl ialfgydgll ysvgflvawl ivlflvaelv rncgrftlad vvaarmrerp
      121 vriaagaasv tvsvlylvaq mvgagslval lvgsagqqar twmvigvgal mvvyvafggm
      181 rattwiqvvk avllmggava ltvlvlarfh gdinellnta aersghgrdf lapglkygsd
      241 wtsrldfisl gialvlgtag lphilsrfyt vptaraarrs vvwsigligg fylmtivlgf
      301 gaaavlgsda vrasntagnt avpllaldlg ggagstggtv lfavvaavaf atilavvagi
      361 tlassasvah dlyaslrrpr gtaqdaqrae vavariaava vgavaiglal laqdlnvafl
      421 vglafavaas anlpvllytl fwrrfttrga vwsvygglip aislvvlspv vsgspeslfp
      481 gldfavfpld npgvvsiplg flmgwlgtvl speaadearh aetevraltg agaa
//
LOCUS       WP_457681359             539 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457681359
VERSION     WP_457681359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58444
     Region          7..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mptqislhdi tksygdrlll dgvslsvrpg erigivgeng agkstllril agaerpdegq
       61 vvlradggvg hlaqtpdlpp drtvqdaida aladlremer rlrslesrld ratpvgleey
      121 gdlltvfelr ggyeadarvd ralhalglar lghdrrlgsl sggeqarlgi acliaaapei
      181 mlldeptnhl dataldwleg allahrgtvl tvshdrlflq riatalvevd adrrglvryg
      241 ggygtfiaak daarrrweqd harwceqitq ltdfaggaar svaqgrpmkd gnkmaydrdk
      301 grvqasvssr vrnaqerlrr lrenpvprpp dplrfraapd vgeaegtlvr ldgvrvedrl
      361 avdslavaag erllihgang agkttllrvl aglttpdrgt vlrrgrigfl aqeipvsrpa
      421 epllsvfrrg lagdveelta lllsfglfre cdlhvpvgal sagqrrrlal arllarpadl
      481 llldeptnhl alglveelea alsawpgalv vvshdrllrr rfsgcsyeir dgrpvlsah
//
LOCUS       WP_457681363             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681363
VERSION     WP_457681363.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20805
     Region          2..193
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkqvdhesr rrqiaeavcq ladesglegv tlrdvaaraq vsmgavqrcf gtkeemlifa
       61 lghigervta rvsarlaasp aqsartalgh aatevsllqe ehraearvwl afvaqaavsp
      121 plarilrtny aglqtvfarl iaeasdtadp draartllal adgltthvli ghlspadald
      181 vldgqlnrlw darts
//
LOCUS       WP_457681369             229 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457681369
VERSION     WP_457681369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24294
     Region          66..211
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mpptdpglsl ssadplgrql ppecralsed grrppapasg plldnlagwg aadtpagpfa
       61 lvpvrpdrdl dritgwmndp avaafwelag ppettaahlr gqldgdgrsv pclgvlagvp
      121 msyweiyrad ldplarhyaa rpqdtglhll iggagdrgrg lgsallrata dlvldhrpqc
      181 trviaepdlr ntasvaafls agfryadeie lpgkraalmv rdrarrhll
//
LOCUS       WP_457681366             588 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457681366
VERSION     WP_457681366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..588
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65999
     Region          10..586
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mspepqpshr awkhaarrlf aktlaefaye evltpepdgt apdgtpqyrl pvtdtlvyrf
       61 rarrgayghw rvdpdsitpd tdpfhfltha hdtvlglsgd ttghlirelt atlaadtrld
      121 agalsaaela dldyaslegh qtghpwlvan kgrlgfsatd aatwtpeart arrlpwlaah
      181 hsiahyrgip tlatpdrlyg eelapatrhs fartisdqgl dpadylylpv hpwqwdetia
      241 plfapqladr siialptdnd lrlpqqsirt flnlsrpear tvklplsiln tlvwrglpte
      301 rtlaapavtr wvhglrdadp ylrdetrvil lgetasvtve hplydrlpgv pyqfkellgc
      361 iwrepvtghl dpgerartla allqtdprgr altaelvrrs glaprawlar lfaallppll
      421 hflyrygtvf sphgenaivv fdeqdvptrl avkdfvddvn tssrplpehd smpddvravl
      481 lteppafltq fihsglfvgv frylaplcad qlgvpeaefw slvraeilrh herfpslker
      541 hetfdlltpr ierlclnrnr lhvdgyrdrt drphavvhgt vpnplhmp
//
LOCUS       WP_457681365             290 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Thermovibrio sp.].
ACCESSION   WP_457681365
VERSION     WP_457681365.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio sp.
  ORGANISM  Thermovibrio sp.
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Griffin,M.E., Klupt,S., Espinosa,J. and Hang,H.C.
  TITLE     Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host
            interactions
  JOURNAL   Cell Chem Biol 30 (5), 436-456 (2023)
   PUBMED   36417916
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Kim,B., Espinosa,J. and Hang,H.C.
  TITLE     Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
  JOURNAL   Methods Enzymol 638, 109-127 (2020)
   PUBMED   32416909
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Squeglia,F., Moreira,M., Ruggiero,A. and Berisio,R.
  TITLE     The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial
            Cytokinesis: A Structural Perspective
  JOURNAL   Cells 8 (6) (2019)
   PUBMED   31216697
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Aramini,J.M., Rossi,P., Huang,Y.J., Zhao,L., Jiang,M., Maglaqui,M.,
            Xiao,R., Locke,J., Nair,R., Rost,B., Acton,T.B., Inouye,M. and
            Montelione,G.T.
  TITLE     Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr
            from Escherichia coli: structural evidence for a novel cysteine
            peptidase catalytic triad
  JOURNAL   Biochemistry 47 (37), 9715-9717 (2008)
   PUBMED   18715016
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13493202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Thermovibrio sp."
                     /db_xref="taxon:2231115"
     Protein         1..290
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33293
     Region          <19..243
                     /region_name="PRK13914"
                     /note="invasion associated endopeptidase"
                     /db_xref="CDD:237555"
     Region          <155..271
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrkvivsfil tlsfalpasa gvyrvkpgds lykiakrfht tvsklkrlng lrssrlrvgq
       61 rlivpgfrrf hsvswyrkfk pkrssetiaf lerkaeseld srivekeinp ltdvvykeae
      121 kinqflatpl nfkydnwsls ilndpeyrga lfkylaqifk alkgtpyvfg gnnpnfgldc
      181 ssftkyvyrk lgvnlprtar aqfnygipvs iknlkvgdlv ffrtyaryps hvgiyigngr
      241 fihfssvlhg laisslsspy frrrfigarr vlsekkvrkv iyavnnkvrr
//
LOCUS       WP_457681372             676 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457681372
VERSION     WP_457681372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..676
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73145
     Region          90..676
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnerpgpdgg qpaervpahq gagtiesvpr qqrrapdetc hqqpheapdr avphgapapg
       61 padrarggdh dpldhpdpav aadaagiehl lrcwlresgp hhpaegrlrl plqaaasali
      121 ipvrywsptg whrlgaptle gapagaapld avtlaallrr eaahgdrras dgcehrvadg
      181 eqrpepagvp qqapdgdgae lvgrvansvr nvavfltdrr arpaddhgal fleaeqslll
      241 ghplhptpks reglseaetr ayspelrgaf plhwmavhrs vlaadsawte rgkpvpaeql
      301 trglagggcr lpddtvplpl hpwqarelad rpdiaalrea gllhdlgvhg plwhptssvr
      361 tvyrpdadam lklslglrit nsrrenlrke largvevhrl lrtglakqwq tvhpgfdivr
      421 dpaylavdgf dgapvrgldv virhnpfstt ddavciaglt sprpwpgrsg vrsrledlvc
      481 tlsartgrpl gavatewflr yleavvrpvl wldgtagivl eahqqntvvl ldpdgwpvgg
      541 ryrdnqgyyf rtsrraeler rlpgigaasd tfvaddvtde rfayylginn vlgligafgs
      601 qrlvreeill aafrrflada aaappahrsp lpeqllaart lrckanlatr lhgldelvgp
      661 vetqsvyvtl psplap
//
LOCUS       WP_457681374             731 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Streptomyces nigrescens].
ACCESSION   WP_457681374
VERSION     WP_457681374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 731)
  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
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..731
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=77843
     Region          41..719
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msaeatnpgn pgaagrkrgr rrlelrglrr igraallgpa prdglphale hvakvhrghh
       61 pdadldtltk ayllaesshr gqlrksgepy ithplavtli laelgaettt ltasllhdtv
      121 edtevtldqv rdlfgdevcy lvdgvtklek vdygaaaepe tfrkmlvatg ndvrvmsikl
      181 adrlhnmrtl gvmrpekqar iakvtrdvli plaerlgvqa lkaeledlvf ailhpeeyat
      241 tralvmeyta rpdplaalar rvrsvfaeag idaevlvrpr hfvsvhrvrl arreltgadl
      301 grllvlvaed adcyavlgel htcftpvise fkdfiaapkf nlyqslhtav tgpsgevaet
      361 lirthqmhrv aeagvialgn pyaptdgvda pegeradptr pgwlsrllew qrttpdpdtf
      421 wtslrddlaq dreitvfctd appdgpsggt ggviglpaga scvdaayerh geaahcciga
      481 rvngrlatls tvlhdgdslq llmapdsatg pspewlehvr tpaarlaiar wlagpresca
      541 rpagpgegfg aappadrgaa gldrpgagpa apasvlavad lpgaavrlag cctpvppdav
      601 tgfavrggtv tvhralcpvv armaatgrpp vgvrwrgadq gghgfrvtll aeafsrphll
      661 adlteaiasq gaavvsaave ppqqqrvrht ytlhlpnaag lpslmramrq vpgvfdvlra
      721 grarqpaalr p
//
LOCUS       WP_457681387             269 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457681387
VERSION     WP_457681387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29589
     Region          2..260
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpegdtvwrl aqrlhdaltg gpltrcdlrv prlatvdltg rgvldvlprg khlltrfegg
       61 ltlhshlrmd gawkiyapae rwrggpahqi railgtadht avgyrlpvld llrtadesrv
      121 vgqlgpdllg pdwdpaealr rllatperpl gealldqrnl agignvykse lcfllgaspw
      181 lplgalprpe rvptlakkll eankrrpari ttpsarpdrr lwvygragrp clrcgtevrt
      241 adqdptaeer vtywcpacqp dppdghrag
//
LOCUS       WP_457681393             338 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457681393
VERSION     WP_457681393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35737
     Region          96..333
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mslasgsstr rrtpeelkap eeltttedlt tskdltttee lttpeelsap atgtssaste
       61 esaavlpaap srprlprppa lprilraalt gatksaaiva lllvwelapr fglvdrtflp
      121 pfsevaqaww elvangqlad naraslvrsf sgfgiavavs vplglligwy rpvadllnpl
      181 lqvflntaal allpvfvlll gigetskisi vvyacawpil fntisavrtv dptllrlaks
      241 mdlsaprlfq kvilpasvpt iftgirlaga vsivvlvaae migakaglgy linasqynfa
      301 ipqmyagivt isvigvafnq llvavekrls swrvpats
//
LOCUS       WP_457681396             452 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457681396
VERSION     WP_457681396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49593
     Region          11..430
                     /region_name="FMN_nitrolo"
                     /note="FMN-dependent oxidoreductase, nitrilotriacetate
                     monooxygenase family; TIGR03860"
                     /db_xref="CDD:274819"
     Site            order(14,18,75,128,150,223..224)
                     /site_type="active"
                     /db_xref="CDD:238528"
     Site            97..98
                     /site_type="active"
                     /note="non-prolyl cis peptide bond [active]"
                     /db_xref="CDD:238528"
ORIGIN      
        1 mpaagprrlh lnaflmnagh hdaawrhprt qperltdlry fqhlaqtaer gkldsiffad
       61 glalwgkvkh nalggfeplt llsalatvte rigliatvst tfnepfhtar kfasldhlsg
      121 gragwnivts gtvdearnfg qdehlehslr ydrarefvev atklwdswed davlldrvrg
      181 iyvdagkvqp ldhrgehfav qgplnvqrsp qgypllvqag ssedgkefaa qyaeavftaq
      241 qtladgqafy kdvknrlpry grsendlkil pgicpvigat eaearaleqe ltdlqvpeyg
      301 laqlsgmlgt dltgvpldgp lpalpeerdi ngnksrftlv aelarrdglt lreliarlgg
      361 grghrvfagt peqvadqlee wftqgaadgf nvmpphlpgg ledfvdhvvp ilqerglfrt
      421 eysgrtlreh yglprpagrl asavtategq pa
//
LOCUS       WP_457681411             282 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457681411
VERSION     WP_457681411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30227
     Region          1..273
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 metrelryfi avaeelhfgk aaqrlgiaqp plsraihqle rrlgsaller tsrtvtltea
       61 gsvllreara aldaveaaer rtrraalsat ghagvvlatk agaagellak lldayaaepd
      121 avtvdlllcg igeqervlrd gradvallhl pfdstagfdt eelrtegqvv ilparhpltv
      181 rphvqmaevt klpglpvprw pgrdgtypdg pgpqvrehaq llqlvalgra cwiapescra
      241 qlrddlaavp vldapmvttv iawpphsrsr avaglvqaat rl
//
LOCUS       WP_457681414             403 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681414
VERSION     WP_457681414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42444
     Region          50..296
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtivygasea tadattnstt dsttkpkpgd rasltsyelt pgllkitsrp pgnptqvhgv
       61 lgmpkgegph pvvvvmhglh hncafsdkpp yfprkpvkar wplvcaapge phnpnlgpdy
      121 lrhdvglshv vqaltrkgfa avsidvvspe hwwagetvpe kgytdlvnah lrllsdlnkg
      181 vnhgldipgv kgridtsrvg lvghsrgggy vlspkaaqra glfgvvalep avgaekvphk
      241 vpvlnlrggc dedvdpsagl eemkelaksg stkvaadvll agtghrmlnt nlpptdtkeg
      301 gvgdcpaskv aapaaaqaqa aqitasfldq arhksksyrl paledldpkg gnlrkggpav
      361 tfhrapqqtf tdpltihevt skqrllpaip kdlkvnkrpg ddi
//
LOCUS       WP_457681420             291 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681420
VERSION     WP_457681420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32110
     Region          44..291
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mgdlaldldq ltaidmhtha evskdghgal spellgasae yfkahghrqp tieemaghyr
       61 errmaavvft idaehatghp risneeiaes caahpdvlip fagidphkgr agvrearrlv
      121 eeygvrgfkf hpsiqafspn drlayplyea ieelgvpalf htgqtgigag vpgggirlky
      181 snpmlvddva vdfpqlriil ahpsfpwqde alavathkpy vyidlsgwsp kyfppqlvry
      241 antllkdkvl fgsdypvitp drwladfekl dikpevrpki lkenaarllg l
//
LOCUS       WP_457681417             303 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457681417
VERSION     WP_457681417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30783
     Region          1..252
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(12,14..15,17,36..38,89..91,140..142,155,159,185,
                     186..187)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(113,142,155,159)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 mdlhgkvavv tgsgrglglg yaqalaaaga avvvndvdqg avdaavamit aaggraagav
       61 aavgdsaaae elvdtavref grldvlvtna gilrdrvlwk mtdddfddvv rvhlrgtftc
      121 araaavrmre qgtggrlvli sspagqrgnf gqtnyaaaka givamartwa melgrsgitv
      181 navvpvaate mtktipafap vieeaertgv plpdwlrkde glgtvedvag lvtflasdas
      241 egvtgqaigi ggdrlalwah pkekavafad ggwsadaiaa qwpdgvgaep etygilapka
      301 pea
//
LOCUS       WP_457681422             514 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA synthetase [Streptomyces nigrescens].
ACCESSION   WP_457681422
VERSION     WP_457681422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..514
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54742
     Region          10..497
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(164,167..172,174..175)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(167,282..283,303..308,388,400,403,414,494)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(167,207..208,255,257..258,261,282..283,303..308,388,
                     400,403,411..414,475)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(207,257..258,261,282,411..413,469,475)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mlnqgigswp trrarktpdr vavihedraw tyrefhqrvl rlahglqdvg vvrgdriayl
       61 gpnhpsflet lfaagllgav fvplnnrlta pelaynlsds gstvlihape qacaaraaad
      121 eagvrhritl dgshegalgy eevlagggtd pldepvapdd pcmimytsgt tgrpkgavls
      181 hanivwnsvn vlvdtdlggd evtlvaaplf htaglnmtcl ptllkggrvv lltafdatrv
      241 letienlrvt ymfgvptmyd amaaqprwst tdlsslrtln cggapvpart iatylargla
      301 fsqgygmtea spgilfldke qtsakagsag vphfftdtrv vlpdgldagp gqrgemlvqg
      361 phvmtgywnr peeteavfad ggwlrtgdva rtdtdgyayi vdrakdmfvs ggenvypaev
      421 eeavlshpav aecavigvpd qtwgevgrav vvlgpgahad epgildhlhg klakykipks
      481 vvltdslprt atgkivksav rasyantpad ephr
//
LOCUS       WP_457681427             235 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase [Streptomyces nigrescens].
ACCESSION   WP_457681427
VERSION     WP_457681427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  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 235)
  AUTHORS   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..235
                     /product="nitroreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24945
     Region          16..231
                     /region_name="PnbA_NfnB-like"
                     /note="nitroreductase similar to Mycobacterium smegmatis
                     NfnB; cd02136"
                     /db_xref="CDD:380313"
     Site            order(16..18,20,37,40..42,44..47,49..53,55..61,143..144,
                     146..150,157..158,161..162,165..166,168..169,173..174,182,
                     185,187,203,222..225,227,230..231)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380313"
     Site            order(20..22,24,47..51,132,159,162,179..183,204,222,224)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380313"
ORIGIN      
        1 mslshptels gyaeklirgr ratrafrpdp vpeetlravf alagaapsss ntqpwqvevv
       61 sgslrdrlag alqaahaeqr ttvdfpyred mysiaqqrrr aafgtalyga lgigrndhaa
      121 raafdaeslr fygaphvafl ftagdagdag dagarlaadv giyaqtllla mtaygldscp
      181 qgllsfyadt vrgelgldrg kllvgisfgy adesapvnhi ttdraaldat ttfrc
//
LOCUS       WP_457681454             272 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457681454
VERSION     WP_457681454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=28536
     Region          62..270
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mstplpgfed fgepdgakgp grpvasgepg gpdgsggage sggsgglhsp tanrsrartg
       61 srqeiapgav hvpgwltmaq qrelvtacrd wargpapirh tklprggvms vqtvcigwhw
      121 qpyaytrtad dvngarvpef pdwmvelgrr alveayqdsa agdgytpdta linfydgqak
      181 lgmhqdkeer sgapvvslsi gdtcvfrfgn tetrtkpytd ielasgdlfv fggpsrfayh
      241 gvpkvrpgtg dpasglaggr lnitmrvtgl dg
//
LOCUS       WP_457681452             284 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681452
VERSION     WP_457681452.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31518
     Region          30..282
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(35,70,162,196,198,247,274..275)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(70,274)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(162,198,275)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 maaaavvagp vvavhgpgta yaadggralr vmtfnlryas dvrphswaer rpvmrsllrh
       61 eaphllgtqe glygqlrdva vdlgphydwv gtgrgggsrd efaavfydar rlvpveydhf
      121 wlsdtpylig satwgntvvr mvtwvrfrdm raggefyaln thldhanqys rersarline
      181 rlggldpslp rivmgdfnva ahknsvyeam ldggslvdsw dtaderskqy atfhgyrplv
      241 pdgdrvdwvl tspgvrtrra tintysahgq fpsdhlpvqa lldw
//
LOCUS       WP_457681445             244 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457681445
VERSION     WP_457681445.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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 244)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=25612
     Region          23..243
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mmrrvrvlll tvlllvtgsv mssapasavi ggskstygpw avrmlvdgkp actgtavarq
       61 wilsashcff eqaqpiadkr isfqvgsldv rkgttvhpvp ggrvgsahad mmlikvppmt
      121 vhtarlatar avpgqavrqy gwgatcdgde ntcqspvlkq selrvvrpdd prcagytapg
      181 gsdfcmekvs gipaggdsgg pvmsigprgt etllgvfdgs drekiaeage isqqlawihs
      241 itrq
//
LOCUS       WP_457681459             178 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457681459
VERSION     WP_457681459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19023
     Region          16..176
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mispetttvt tsyttfdspl gelllvgees atapggtalt slsmpqqrgv tvqphwrrdp
       61 gpfaeavrql rayfageltr felafrtagt efqervwral eaipygtttt ygrladvtgv
      121 prgdvralga aiganpllil rpchrvigad gtmrgyaagv erkiallthe galqptli
//
LOCUS       WP_457681461             415 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681461
VERSION     WP_457681461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44103
     Region          132..414
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkvleaaqgl aallraerfa emvelfappl raavsadalr lawaaelagr gkvreigepv
       61 saagegeavr vripvrcadg nftvvtsvgg dgllhglrld pdggvewqpp hyaeptrfie
      121 rdillgtgql avpgtlslpv gpgpwpavvl lsgggafdrd essgpnkplk dlawglasrh
      181 vavlrfdkit ftrpdrlpsd ftmtdeylph alaavrllrq qpevdadrih llghsmggkv
      241 aprvaaadps iaglvllaad aqpmheaavr varyltalap hpsadeavta lvrqaalvag
      301 peltpdtpse llplglsaay wldlraydpv atasglacpm lilqggrdyq vtvaddltrw
      361 rgaladrpdv airihpdanh lfftgrgrpt paeytrpghv dsavvdeiat wlarr
//
LOCUS       WP_457681464             126 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457681464
VERSION     WP_457681464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13917
     Region          12..124
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mmagrpqisl atvvldcpda haladfyrrl lgwevkcsep dwvllrcpdg gtglsfqsep
       61 gyqapvwper peeqqkmlhl dlrvddldda etyavaagat raafqpqddv rvlldpaghp
      121 fclflh
//
LOCUS       WP_457681471             232 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681471
VERSION     WP_457681471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24980
     Region          1..227
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mktigllggm swestaeyyr llnqltrerl gglhsarcvl ysvdfaeier lqvegrwdea
       61 gevladaara lesagadmll ictntmhkva dqvaaavtvp llhladttad avrasglrqi
      121 gllgtaftme qdfyrgrles hgldvlvpda tgrdtvhrvi yeelclgivh eesrqsfmav
      181 irdlitagae givlgcteie lligaehspv pvfpttrlha eaavtlalsd ap
//
LOCUS       WP_457681473             397 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457681473
VERSION     WP_457681473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 397)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43429
     Region          18..395
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,83..84,91,95,102,230..231,234,238..239,242,
                     275,280..281,284..285,287,310,337..339,342..343,345..347,
                     351)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,82,84..85,169..170,178,229..230,233..234,238,281,
                     284..286,385)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 madivdleay gkdftadpyp yyaklraqgp vhrvrlpyap eawlvvghqa vraalsdprl
       61 nknwraaglq sdageesalw tnmldadpph htrlrklvak eftarrveal rprvqqitde
      121 lldtmlaape gradlveala fplpmtvice llgvptmdre afrawsneiv aptseqaaqe
      181 avvamsgylv dlietmrnap gdgllsalir tsdedgdqls rdelvgtafl llvaghettv
      241 sllangvral lqhpaqlaal radyslldna veemlrydgp vetatwrfta epveiggtli
      301 pagktvaivl asasrdrehf aaaddfditr darghtafgh gihfclgapl arlearvalr
      361 sllercptla mdadfddltw rtgmlrgieq lpvrwng
//
LOCUS       WP_457681492             876 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681492
VERSION     WP_457681492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..876
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93204
     Region          2..846
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          618..646
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(619,622..623,626..627,629,653,662..663,666..667,
                     669..670,698,701..702,705..706,709)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          651..687
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          697..720
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpgrglppal dafvgrerel srlhtllrss rlltltgpgg vgktrlalel agrvrggrtg
       61 raqwvaldsl qdgellpqal aaalgvrerg gragieslvh algtrttliv ldncehlaea
      121 carlaatlla rcprlrllat sreplrvpge vvfrvgelsl spageehdta allrseavrl
      181 flarartsda afelgsgear tvaeicrrld glplaielaa grvgslslpg ilhglddqls
      241 lltdgsrtgp grhrelgaai dwshrlldpl ervvfrrlsv lgggfdaega aevcangggd
      301 dergrdpdrd wdwdrdwgrd qngdgdvrgd geravsgeir geggahgggt grgdgvrrwd
      361 gvhhgddvhc edgahreedv hrgehvgqep pilvrpeqvl rvvcaleaks livrvrgdep
      421 qgtaryrqls airaygmdrl aeagelsdtw nraldwlagk aagavtpgvf ldtvegplar
      481 eqenlaaava hsaahsdhrh vplavalarl qyqqeqltaa rtllsgvler vrgpedrnaa
      541 lalaarsacl qddhaaalaf aqeavaagrt grhpgrlana ldalaaarlc rgefsdavav
      601 faecldvvrt lgcpldlalc rhhlawallq agraaeaeql mqeclpelet nappgqvtaa
      661 lhtagairla lgdvdaaerr faevllkapp gesfhglypl eglaivaaer gdlqrslrly
      721 aaaaamrrri dtepeahwwg qveavvarvr ervhpsgvsa amaagrrlrg arlvayalrg
      781 tqvrsvrqes vqtagsgrvd avgqppltgr esavaelvae gmtnqqiash lglakstvag
      841 hldrvrdklg vrsrtqiavr vtgrvagpep glhtdv
//
LOCUS       WP_457681489             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457681489
VERSION     WP_457681489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19382
     Region          13..163
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 medlgpvawp pepirtdrlv lrepeprdra afiellaspe vhtylggprp rdeleremsg
       61 aperwpgsfv vdldgsmigq illrratgnr rpaaegkadl gylflpqawg fgyaaeacaa
      121 algwlagalp gepvvlttqt anvgsmrlaa klgfteverf eawgaeqwlg mwspvtpss
//
LOCUS       WP_457681498             114 aa            linear   BCT 27-JAN-2026
DEFINITION  MmcQ/YjbR family DNA-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681498
VERSION     WP_457681498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..114
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12967
     Region          1..112
                     /region_name="COG3801"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443014"
ORIGIN      
        1 midsadvrri alslpetvek eawemptfrv agkmfvtipd detsfavrcp iherkeliaa
       61 epekfwvpph easshwvrvr laeledmtel hdilvdswkq aaptrlvdtf pgnd
//
LOCUS       WP_457681501             326 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457681501
VERSION     WP_457681501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="trypsin-like serine 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=34956
     Region          102..305
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 msrpiavrgr lalllttlll glsftlapap pahaaktphg hghglrpaaa sddtywtpqr
       61 mrearpaaat ksaaarrpat datppshpfd glpqvgtffw tdgtntgrfc ggtvvrsphr
      121 dlvvsaahcl rspdpkrhls fvpqyhdglk phgiypverl yldqryydlg tdagarwdya
      181 vvrlgaredg aeveevtggf dllpypgyah rnvrligypg nkdtthpkpl dctssthryt
      241 stdpaapgdf leiscagyig gtsggpflvr dftgyaligv iggfhtggdf pdvsyssyft
      301 adtlalylha vhgdppatpr qgvstr
//
LOCUS       WP_457681503             439 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681503
VERSION     WP_457681503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47349
     Region          75..>342
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mfrksvdege raggssaler glegvpgggq magvnrravt ksaalaatml lagggiaqaq
       61 pgkartakdl tvrlpaptgp hrigvttlyl vdrarrdpwe plpvrevmvt vfypartvrg
      121 ypvapqmtrg aaerlpfiep lfheglpakg vnwaatrtha htgapaqtvr rpvllyspgg
      181 gdprtfgtal aeelasrgyv vvtidhpgdg sevefphara grrkvretvf rgdprsdpkm
      241 frtvigtria dtrfvlnqle alaagrnpda egrplperlg raldlrrvgi yghsaggtta
      301 aeamyedrrl haainlegfl dhppaspgqe gqlfpiaryg tdrpllllgt dgfrykkele
      361 rswsamlahq hgctsrrqld htahgvftdy aaivpqlqaa glmtaahrtq lvgaldpavs
      421 vplvrhhvls ffarhlpvc
//
LOCUS       WP_457681505             335 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457681505
VERSION     WP_457681505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 335)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36424
     Region          <261..311
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mirvhftaad farvrfaprp aplqelnval mkmcspddtl lfgrwrrrll qslpptvqpl
       61 sdlvpaevap hfldvfsdtl kegldtvras ppelvraeie rvyarqpipa plwlrdlyrg
      121 dggawrllrr aqhaafdtal rpvwplvqdl hraeftrhal tvaehgigaa ltellpgarl
      181 henvwefeap yerditldgr gvlllptfhw tgppliadlp grpvavtypa gpglplspgg
      241 avgsdealag vlgrtrfdtl lllgeehtts alarrlnvsn atasahtaal rgaglitstr
      301 agravlhrrt elgsllvqrp gqgtrpvtvs dqgsp
//
LOCUS       WP_457681521             432 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681521
VERSION     WP_457681521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45616
     Region          1..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mrfgaelrrr rieaglslge laslicfskg hlskiergvk apshdlaqlc dsalhaggql
       61 sslisapers ttvtpmtead vgtpwtlrmh aggesdfvaf dpaspggggl pstivswsla
      121 ppllesgemn salpyfrnvf defrrlgqlf gpsvvaqlci aatsalrgma hqaqpahrdv
      181 vlrlasrfae ytgwmaqeag sdaaslwwte qavqlaadgg ddelaayali rraelalytg
      241 dsvatvqlar raaqqarsvr irglaaqrea qghalvgdrd acrraldrga eltagaappd
      301 gadpvlgsih lpdltafvag wcmhdlgspg eavsllgdgl daippesrra rarygarlal
      361 alanvgeieq acaiaelvas hvalidsati radllrlsra lnrwpknptv rrtlphlaig
      421 lhtnrtgpgt pa
//
LOCUS       WP_457681530             143 aa            linear   BCT 27-JAN-2026
DEFINITION  HIT family protein [Streptomyces nigrescens].
ACCESSION   WP_457681530
VERSION     WP_457681530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15157
     Region          29..140
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mvsygefrev ageapdtgpq rprtprrpgc pfclivcgra patvlrewpe tiairprhgg
       61 vtaghvlvip rvhvadvaed pvvsaatmlr aaelaaevgd cnvitsrgps atqtvrhlhl
      121 hlvpraegdg lllpwtdirp agt
//
LOCUS       WP_457681542             366 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681542
VERSION     WP_457681542.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38318
     Region          13..314
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msgaqapdgt hrrvivlgat gafgrhvcaa vgaagedvlr varrpgtatg agrffpmdlv
       61 gggpdglarl idaerpyavv naagavwlcs peamrqanha lvdtvlaama aaswrprlvh
      121 vgsvheyapq ppgtsldert ptrpttlygr tklqgteavl tasaagqvea vvlrvsnaig
      181 agtspgsllg rvaaqlraae adreavvrvs plrasrdfvd ardaadavla aaalpvggel
      241 inigrgeavp vrtmverlit asgqrarive eaepgarpat dqdwmrvets rarrllhwtv
      301 chsidssard lweatapgae pspqdhpaat vpvpprpeta dhrprggstr ttrtwppqth
      361 pvqqpe
//
LOCUS       WP_457681566             940 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681566
VERSION     WP_457681566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 940)
  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 940)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Rosinski,J.A. 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 940)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..940
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=100765
     Region          <8..880
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          869..919
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlldreveld laatalgsgr galvlvtgpl gvgksalldg igalraarga lhlrvnaapm
       61 erdfplgaar qllepalrha speamarwta gsasharsal dacrpagavp aqpvldslta
      121 lienmardqp vlllvdelqw adlatlqwlr hlsgrlaglp vllvcavreg ddlaghpavq
      181 gviehathil rpgnlawqdt htlihryhge aadgvfaaac hratggnpli lnclladaah
      241 rdlqpvadna eaaaalrpaa lqhrlllrld aqaeqvrria ramavlgddm npellsklae
      301 vdstgrdhal rkltdlgltt geqhpryvha lvqeavaegi pleertamha laaellhrsg
      361 rppeqvarhl maltaptytw atevlraaar aaqgrgapev aarylrralm gsspdaerae
      421 llvdlatser sfapytsvrh iaqavllcdg pvrraqavvr lapsafsstl lpvhellqea
      481 adalgpedrl hgperelalr learirqstl pdpeklagsv arlvalgpep ktgtvaerel
      541 lapligaatf snalpaheva qlakrvlere palpahvhtt mplvvaslva adaveelssw
      601 ldavqqnavg rqtrveqali gteqalvsla rgrltvakkq alaafelaga kheevftlss
      661 mtlatcailt gdhqladrll aikyraeeep yvwsglamlk gqsaarkgdl dsalgyflda
      721 grrleqcgwh npallpwasa aaflrlhlge reqarelsal evewarawga pgplgralrv
      781 yshmvegpgs tdvlreavdv lqlsanrfel cqalldlger lgpaeahgra alrrayaeav
      841 ecdtpwlarr aeellaeapp dpesargqlt paerkvaela tsgmtnqkia nelnitcrav
      901 ekhltncyrk msipgrvhls aalreldqqp pnspgpaapy
//
LOCUS       WP_457681569             431 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681569
VERSION     WP_457681569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46609
     Region          15..431
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrisrrraaa ttaalvtsal altacgssee aggsdsasgk vegrvtfqtw nlkanfkkyf
       61 egviadfenk ypdaevrwvd qpaegypekl sadaaggtlp dvvnvspdla yplakaglal
      121 dlektagkyr geyldgawes hrmpgmtgvy afpwylntgp mfynkelftk agldperppt
      181 sydqlfkdav tmarksdrki amlagtpsie dfgrygvrlm nargteftfn epkgvellkh
      241 ykelytagal dsqaltaqae sagrkfqqqs vamnpgsald lenfkkeapg lyrhigitda
      301 vnntgkanmy vqglmvnaqs kvkpaavafa hfvtgkknqm afakkvtifp stkgslddpy
      361 ftkedgtdat rvrvasaksl ktavnytpvl lsdqmktvlr navakavqgk qspraaldga
      421 vaecnrllkt a
//
LOCUS       WP_457681572             429 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase 5 family protein [Streptomyces nigrescens].
ACCESSION   WP_457681572
VERSION     WP_457681572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47075
     Region          1..334
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mrfgvnytpt hgwfhhwldf dldsvradld siaglgldhi rvfplwplfq pnrtlirpra
       61 veqlvqltda aaergldvnv dglqghlssf dflpawtqtw hrrnlftdpe vrsgqeeylr
      121 tlaaaladrp nflgmtlgne inqfsdrphp dpdritdeqa aawlermlaa cergapgrmh
      181 lhaaydaawy qdghpftpah aarlgavtav hswvfngtaq rhgptgtate hhaayliels
      241 kawatdphrp vwlqevgapa phipedraar fteatvtaal dcpdlwgvtw wcshdvprsl
      301 adfpeleygl gllgndrtvk pagralaalv sewrgrthrp pvrstaltvd aggagpaprr
      361 svcapggpvf eawaeltaqg vrptlvlsel aadsahltsr gitevctpdd vgraprrpsp
      421 avphrrsss
//
LOCUS       WP_457681581             341 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681581
VERSION     WP_457681581.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36096
     Region          38..317
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mkrpyavala lalaasssll agcsdagkpv dfnaggkgdg aararpvddd tlmptgpksd
       61 fritrtlddg thiaratlrg qksgvtgsvw vwapkeygdp kyaksgfpvl ialpgglgsp
      121 kepggvtnyw vggdielqen ltqwtaegks lpfivvmpml npdtryhdas dipgsqkmgt
      181 wltedvvqlt ranfrtfksr dgwafmgsss ggfaglksvl khpdkfkaai asgpdmapds
      241 plwaghqaek dsndpeklaq rllqkggpdv ylafqagsse paavtapiqr frqaygkgpi
      301 htslqiipgg rhnawdyqkg maagsikfis drmkapvasg s
//
LOCUS       WP_457681583             404 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681583
VERSION     WP_457681583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..404
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42302
     Region          58..324
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mpgpaaadgp hgidnlraga haagpagpag pagpaepadf esrldrrgvq flprpdvpep
       61 pevsalswmv tdladgkvla akdahrplpp astlktlfal tvlpkfsqga vhtvsledla
      121 giesgsslag lkedmpyqva dlwhgvflss gsdavhtlas mnggwrktid dmqetarrlg
      181 ardtrvesad gfdtpgqvss aydlslfgqa gltdpdfahf astkraelpq dggpdaftlq
      241 ntnrllvgsr gvrpydglig vkngytthag ntliaaarrd grtllvtlmn prsggrnavy
      301 eetrdlldwg feaapraaav gvlptvepve rtgetqpvah rprpvplhka gvaaqpdgar
      361 ltrnwwflsa agavgiiava glgtvlwrrr rtvraspggg sesa
//
LOCUS       WP_457681586             410 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457681586
VERSION     WP_457681586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42132
     Region          5..367
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(15..16,19..20,23,55,105..106,108..110,113,133,
                     136..137,140,209,212..213,216..218,221,249,253,302..303,
                     307,311,325,328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mpravyvlam gifamvtsef vvaglmpqma vglgvsipqi gflitafava maaggpflav
       61 avlklrqkta lmalfgifla gnvlaalapd ygvmlmariv tgvasqaffg valslcvqla
      121 rpevrgraia lvmnglmlgt llglplstlv gehfgwrmaf wvisgitvla alatfagipr
      181 lgraeggggv rqelvvfrnp rlwlvlstst liigatfsaf syfhpiltev tgfaagtvpl
      241 llvgygaatv igntavgrla drytvgvqlv glslnflfla gfavfahlpv pavalmtgig
      301 lvgvtmnpam vtrvqrtgna rplvntvhss fitlgvivgs sggglainsf glrgplwlga
      361 alavigvgtl vpdllrrspt apepfasvtd hpepaisaas epkavcaars
//
LOCUS       WP_457681588             208 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457681588
VERSION     WP_457681588.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22507
     Region          5..128
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mphpdatphp ywnhnvhyhr lvldavpdgc graldigcgd gllvrklagr irevtgvdrs
       61 aamvrlarer saqvpnaafv eadfmtpdga psggfdflta vavvhhldft aavhrmagll
      121 apggrlvlvg larnrtpldw lvsgagvpaa rflarrhggk sgppempvqd pamawgevrr
      181 aargclpgsr frrhllwrys lvwdkprs
//
LOCUS       WP_457681603             554 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681603
VERSION     WP_457681603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..554
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57174
     Region          14..549
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 msertpdpvr qhpsgparpr tvllrggevh spadpfatam vvegdriawv geegaadsfa
       61 egvdevvpld galvtpaftd ahvhttatgl altgldlsga atlsdalari rgyaaaread
      121 rillghgwda sawpegrpps raeldaatgg rplyltrvdv hsavvttall dlvpgvrela
      181 gfradapltg dahhavrqaa yatvtpaqra eaqsaalara aslgigsvhe cagpdisged
      241 dftallalar egngprvvgy waelvasakd aerirelgai gaagdlfvdg slgshtahlh
      301 apyvdaghtg tahldaeava ahvaacteag lqagfhaigd aaltgvvdgv raaaerlgla
      361 riraarhrve haemltdhti agfadlalta svqpafdaaw ggedgmyaar lgvdrartln
      421 pyaallkagv plalgsdspv tpldpwgtvr aavfhrtrah gisaraafta htrggwraig
      481 rddagvlvpg apadyavwrt gellvqapde rverwstdpr sgtpglpdlt pgndlpvclr
      541 tvvggrtvfg ppne
//
LOCUS       WP_457681606             381 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681606
VERSION     WP_457681606.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42031
     Region          60..321
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(62..64,67,83,85,120,139..142,251,253,255..256,258,
                     268..269,272,287..288,291)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(62..64,251,253,256,269,272,287..288,291)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(63,67,83,85,120,139..142,251,255..256,258,268..269)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mtphpppaag pdgnhpggap agrrprtttr dpealtrrlt awlgtrlpga ravaatvpds
       61 ngmssetllf diehpeppvp scalrlaadp aaytvfpryd marqyrtmrl vadhtdlpvp
      121 rtlwleedpa hlgapflvma radgrvppdv mpytyegnwl hdatdaqrdh leaasvsvla
      181 rlhgqvppaa adflatpgtg galhrhveaq rayyswvidg rprsplierg farladrwps
      241 dpgetvltwg darignivyd gfepaavldw emaalgprel dlgwmvflhr ffqdltesgg
      301 kpglpdflsr drvesryaal tghpprdmdf htlyaalrha ivmlrvayrq vhfgeipvpa
      361 dadalilhrd tleamiegry w
//
LOCUS       WP_457681637             256 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681637
VERSION     WP_457681637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 256)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28575
     Region          60..199
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkldflllrd stfgeyclyc haetvtwivv dgrkrctcss cgreaeravv idpricwwtd
       61 sdgeywhesa gvfvrdrrar flffqrtafp ysltvpaghv ergeepkcaa arelweevgi
      121 rdahgglrlv adeylkgdvc rrgsdahrwh ayllevdehr eagaqgevtv neegeapvwl
      181 tldearsrqt tfaverimdl hsgkllpggt rtptgprapg vprapgglrt padprtpgdl
      241 rnpgetwqdp sdgsra
//
LOCUS       WP_457681634             434 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457681634
VERSION     WP_457681634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43204
     Region          9..391
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mhdrkrgsqr raltspwkya latwlagvla aiglgavspa gpalrsslgl sggalawats
       61 sitavsavlg ipagwwvrrf gaqralswgl lvmavaaavs atagswglll gsriaegvgy
      121 llvfvagpvv ltgmtqgavr saalalwgtc vpmglaiaaa tggalaswwt whqwlaltal
      181 gplimagvlt tvlprlprta vpcahreagt wngalrlgva ygslslvgva vvmvlppflt
      241 ehrqatpavt gtvvavvclg savgglvasw llrrgaalas lvplgalmpv aclpafsael
      301 plvisggaat lvlvvdglli savfaavpas vsrpehldva ngilnqlggv gilmgppvfg
      361 lviaaagwga vaaatlvfgg lgavllltta rtsgtgspsg vshspgapdg vgmregpepi
      421 gkaadvsnpd srrp
//
LOCUS       WP_457681646             145 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681646
VERSION     WP_457681646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16184
     Region          25..130
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maphrntspd pqhhhstpls ttrghesdee acrevlqilg lvgskwsili vgqlrdrtmr
       61 fgelhravkg isqrmltltl rqlerdgllt rtvhpsvppr vdyaltalga tlldsvvalg
      121 ewasahrhei snnrhrydat hptrt
//
LOCUS       WP_457681655             628 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-keto acid decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681655
VERSION     WP_457681655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..628
                     /product="alpha-keto acid decarboxylase family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68172
     Region          3..609
                     /region_name="PDC1"
                     /note="TPP-dependent 2-oxoacid decarboxylase, includes
                     indolepyruvate decarboxylase [Carbohydrate transport and
                     metabolism, Coenzyme transport and metabolism, General
                     function prediction only]; COG3961"
                     /db_xref="CDD:443161"
ORIGIN      
        1 mttsstctva eylarrleql githlfgvpg dhlgpflstl hektkvrwvg tpteggagqa
       61 adgyarvtsa daeialgeqg igavavtysv gafnllnaig gafaeyvpli ainaapsyeq
      121 wlnqqaigll tshmsqrpes nlevyrqvtv daqalsnpgl aptqidsait aclshrrpvy
      181 levmddlwga qcpapqgrlt rrerpvtvkn ermldravta cvelvrrhgn pilwageeid
      241 rfrlsdefek lvretripfc ttigaksvvs eytlgfsgvy ngkashpeva evfnnagcri
      301 glgswatskn lggersigdd wavaahdgvh vgasyfpdvq larflpalre rlvaefgdga
      361 faadyfarah edglqvadst aahlasqtgg pypetvtyds ffrhinafle eqtseppgar
      421 snpftvvcda afaligsmnl rmaerasyva qnswlsigys vgaatgvalg rshagkrpmv
      481 fvgdgsfqet cqemsthvrh glrpvvfvld neafygieqm lvhpcyyqdg tprsdgadfy
      541 nelhpwryek ladvfgsakh pmhgfavrrh deltdllkri aepsdavnqg pvvvrvqldr
      601 hdypealkyk vaencppsgg apsegkvg
//
LOCUS       WP_457681660            1653 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-glutamate dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457681660
VERSION     WP_457681660.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1653)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1653
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1653
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=183544
     Region          1..1649
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mqtkldeakt ellaraarvv esspaggkhp vrgldpdtls gylqryylht apedltdrdp
       61 vdvvgaalsh yrlaemrpqg tanvrvhtpt veengwtcsh svvevvtddm pflvdsvtne
      121 lsrqgrgihv vihpqvivrr dvtgklievf dsncdahgkt gkgkgtklph davteswihv
      181 emdretdred lhqitadllr vlsdvreave dwekmraaag riadelpaep vaddlgdqei
      241 eeaqellrwl sadhftflgy reyelttapc eggadedvlt avpgtglgil radpthreta
      301 dghpvspsfn rlpadaraka rehklliltk ansratvhrp syldyvgvkk fdaegnvvge
      361 rrflglfssa aytesvrrvp virrkvaevl egagfspdsh dgrdllqile typrdelfqt
      421 pvdelrsiat svlylqerrr lrlylrqdey gryysalvyl prdryttgvr lrlidilkee
      481 lggtsvdfta wntesilsrl hfvirvepga slpeltdada drlesrlvea arswadgfse
      541 alnaevgeer aaellrrygh afpegykadn sprsavadvq hlekltgepg rdfsvslyep
      601 vdagpgerrf kiyrrgepvs lsrvlpglnr lgvevvderp helrcadsti awvydfglrm
      661 pehikgddar erfqdaftav wtsaaesdgf ntlvlragln wrqamvlray akylrqagst
      721 fsqtymedtl snnvhttrll vslfearmsp drqragtelt dglleeldga ldqvaslded
      781 rilrsfltvi katlrtnhyq kdsqgrphsy lsikldpqai pdlpaprpay eiwvyspkve
      841 gvhlrfgkva rgglrwsdrr edfrteilgl vkaqmvkntv ivpvgakggf vgkqlpdpsq
      901 drdawlaegi acyrtfisgl lditdnlvgg evehpkdvvr hdeddtylvv aadkgtatfs
      961 dianevaesy gfwlgdafas ggsagydhkg mgitargawe svkrhfrelg vdtqsedftv
     1021 vgvgdmsgdv fgngmllseh irlvaafdhr hifldpnpda atsyaerrrl felprsswad
     1081 yntellsqgg gihprsaksi qinaqvraal gieagvkkmt padlmqailk apvdllwngg
     1141 igtyvkssae snadvgdksn dairvngedl rvkvvgeggn lgltqlgrie famaggkinn
     1201 daidnsagvd tsdhevniki llnsvvadgd mtvkqrnkll aemtdevgal vlrnnyaqnt
     1261 alalalaqss smlnaqqrfm rrlvrdgdld raleflptdr qirerlnagr gltqpetavl
     1321 laytkitvae aliqtglpdd pylqrllhay fpsalhdrfp eqvdghalrr eivttvlvnd
     1381 tvntggtsfl hrmreetgas leevvrahta araifrlgqv wddvealdnv vaadvqtrir
     1441 lhsrrlverg trwllnnrpq plelsetigf fadrvsqvws elpkllqggd lewfqailee
     1501 ltdagvpeql avqvsgfssv fpaldivava drldkepldv sevyydlgdr lrinqlldri
     1561 lelprndrwq smarasired lfaahaalts dvlsvgngss tpeqrfkawe qanaailsra
     1621 ratleeihgs egfdlanlsv amrtmrtllr trs
//
LOCUS       WP_457681665             790 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457681665
VERSION     WP_457681665.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..790
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=88407
     Region          10..222
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          365..726
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 msetgvdagp rfsiivpvfr vqgflrecmd svltqeftdf eliaiddcsp drsgaildey
       61 aahddrvrvl hlpenaglgp arnaglarar gdyllfldsd dtlvpgalga laerlaatgt
      121 peilifdyar tywdgssrrn alsalldesg apsfplaerp rlldllqivw nkayrrdfve
      181 ehgfafpegy yedapwtfct litaqriavl drvclhyrqr rqggnilrtt srkhfdvfdq
      241 yarvfdylda hpelscwrph mfrkmvdhyl tvldkpgrlp qhaqaeffhr aardyrlrlp
      301 agfvrpsgva ggkyallard aypalaglkv agkvqrtvrk hagkrvrqak rkamdlryqa
      361 llrqpldenl avysaywnrl pscnplavye kakelapdvh gvwvvkkqla dsvpagidhv
      421 vlnsprywev varakylvnn vnfadnvvkr egqihlqthh gtplksmgtd qkrypaaakg
      481 msfrkllara drwdfslsan rhtteqwerv ypcdfasvda gyprndvyyr ataqdvldir
      541 erlgiapgrt avlyaptmrd yqvgyvprld leklsrelgd tfvllvrthy fydrdpglqk
      601 lqergalidv sghsvveelc laadalvtdy ssimfdyanl drpiityadd wdtyvrsrgv
      661 tfdllsglpg dtpgviatte delieafrsg rwddeaatgl raafrarfcp wddghaaerv
      721 vrrvflgqea tpeplpqder tiapspraaa aatgllklpa prtaahddvt psgtsgtsgt
      781 sgtsdvemag
//
LOCUS       WP_457681662             265 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681662
VERSION     WP_457681662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28584
     Region          21..264
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 maevrteqng sqatgaript viaddlhivy rvygtgagkg tataalnriv rrkpssgvre
       61 vhavkgvsft ayrgesigli gsngsgkstl lkavagllpa ergkvythgq psllgvnaal
      121 mndltgernv ilgglamgms reqvreryeg ivdfsginek gdfislpmrt yssgmgsrlr
      181 fsiaaakdhd vlmidealat gdrsfqkrse arirelrkea gtvflvshnn ksirdtcdrv
      241 lwlehgellm dgptddvika yeahr
//
LOCUS       WP_457681668             651 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457681668
VERSION     WP_457681668.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..651
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70666
     Region          19..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msvpddlaaa aptgtdapap tvsvivpvhn trryldrslg svfaqtldrr hieviavddg
       61 stdgsaewla eqarrhpqlt vlrqeasggp gkprnaglah atgdyvffld sddrldpqal
      121 fwltrtaqry gsdivygria gadgraapvd lrttsahvsv fdspvywsla ayklfrrsfl
      181 arhqlrfveg rllgedlpfg stallraevv svfaertcyy lhgrednsna srqetdwcey
      241 lgyigtvldp vaaavppgan rdklmvrhfh geilmpfgap ylardpagrt amaaaarplv
      301 eryltdrvla alpprlrlra hsiragldde ltavvradte nrpdpphldd dgrvyagypy
      361 frdprralpd tcydltdrvv lrqrlirqrw aggvlhlrgt aalpwlggdt veillrrggt
      421 thriparaad gawraavdpa taadgaplad gvwglkiavt ahgpggatgp avrreawlvp
      481 ederddeddt gfaprivgrg pagpavaalf rsrphghlhl dldrdgvrrp lggdlrgtad
      541 ctrsgratlt arltlpgcpv daelrlilyd atrtvalrtt veraagdryt vrsllrsgpt
      601 gtwrvalrvt agplrrelpv rtagrgadgr tpltltvpgg spagllrrar r
//
LOCUS       WP_457681671            1215 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457681671
VERSION     WP_457681671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1215
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=131415
     Region          2..>192
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          839..1213
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mkprltvvvp vhriegsern veeclesvaa qtlteldvvl vdgppaagrd dagaaesapa
       61 alarrfaard prfrivhhsg dgpapgcgav rntgarhayp htdylaflda gedvllpray
      121 edlvglldrs gsdlatgnvy rlgaagrsqs ahhpagretv lrtrvgddlt llsdhvarnk
      181 vfrrsfwdrh gfafpegewc hdaavtlpaf flaeavdvlh ehvcyrrlpe gpdrhrrlda
      241 rgvrdrfaav agirrfladp ardrlsghrr dydraqlteg lldlveslpg aapecrtafl
      301 dcardflsgv dprlfptlpv elrmrwylir agrladllal lthearnpag ftvagpplrk
      361 ravlpltppl elppgvtrld radfpvvarv reavwrdgvl vlrgyaylrn ldaaarhryl
      421 rtavlscgrr rillplrava mpeataesgq elhcydwsgf emrldparlr rgghweegdw
      481 tvgvllasag vvgsgalqap dtgsgaapra hdvagggadd gvritpwyag grlrlsvhrr
      541 trrlaghraa aagdldltvt vpgpppaalr lthqgtgtvv sfpvetappe epepgkegpg
      601 eagevsggay gapssthtfr irldalaaar ptrdgaprai ppahtvswaa elvlpgggtd
      661 pvacapgltp vpyplphgre lvvaatpagh lvlddripqp yldrllwrtd gtlllsgglp
      721 aaaphatelv lkhgahaael afptthdegr fhgtlplgal pslagtlplr egrwtlhlre
      781 rgavgsplda pvrcapsvld glpasrtvrg kplaldrhrq dealvvagpa lpatdrgpyr
      841 rrmlreqhys lhrsrplrdt vlyssfggra ygdspravhe elvrrgmeve hlwavrdaqt
      901 avpetaravl vgsaewhgal ahsrwvvtnt hlprwftrrg gqriiqtwhg tplkrigadl
      961 agtlcaglah laprprvsrq wsvllspnah stpvlrsalg ysgrlletgl prtdalfapd
     1021 reltaaavre rlgiepgrkv vlyaptprdd laydaghhrl hlpldlelar relaedhvll
     1081 vrghpmvadr lpahhapfal dvsahpdate lllaadvlvt dysslaadfa ntgrpmlflt
     1141 pdlphyrdtl rgftldfear vpgpllsstg elvdalgdlt aiaaagaeay adfretfchr
     1201 ddggaagrva dlmer
//
LOCUS       WP_457681674             417 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457681674
VERSION     WP_457681674.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..417
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43991
     Region          2..393
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mfllpamlll galvvypivf svhrslfdas gdgfvgldny gamfsdegir talrnnvvwv
       61 vvaptvstal glifavlter irwgtafkli vfmpmaisml aagiifrlvy dqapergvan
      121 avwvgvhdtf adpapfpgak prpradlkps gggafttgsa vrsgspvllp lvavqpgdlr
      181 garsaaaarp qpgritgtaw ldftrggggr pnavdgseka laglrveavr ggrvvasatt
      241 aadgtfalpa gkaegarlrl paanfaeayr gvdwlgpalv tpaiigsyvw mwagfamvli
      301 aaglaavpre lleaarvdga gewqvfrrit vpllapvlvv vlvtlminvl kifdlvyiia
      361 pgssirsanv lalqlfqssf gtdvdeglgs aiavfllllv lpvmyvnlrr lrkerrr
//
LOCUS       WP_457681677             459 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681677
VERSION     WP_457681677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47733
     Region          57..400
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrrrldrtag rattvvaata vlglvlaacg ggsgggtkee gsgggkggst aptvqlpslk
       61 gqklqvtavw tgperenfgk vldefekrtg atvdfvpsgd dmagfigskv agggppdiam
      121 lqqvgvlnef arkgwlkplg asakaqlakn yakgwrdlga hkgtpygvyf kasnkslvwy
      181 naqafdnaga hepktwpdfv kaaeviaesg vepvsvggsd gwtltdwfen iylsqagpek
      241 ydqlaqhkik wtdptvkral ttlgqlfgrk dllaggnsga lqtdfptsvt qtfsggdtpk
      301 aamvssadfa aanitqtkak vgtdakvfpf pavgakspvv tggdvavalk dtkaaqalla
      361 flastdaaki waqaggfisp nkeldqaaya davmreiaka lvaagddfrf dmsdqapasf
      421 ggkpgqgewk dlqdflknpk diagtqaqle kdaaasfgh
//
LOCUS       WP_457681678             522 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457681678
VERSION     WP_457681678.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 522)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..522
                     /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=55919
     Region          4..490
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(51,54,330,333..334)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mngldwavli gyfgvmvaig vwshkrvdnv sdfftaggkm pwwlsgishh msgysavmft
       61 gyagiaytyg vtsfvtwsfp ialgiaigsk lfaprinrlr srlhvasple ylknrynlst
      121 qqalawsgml lkivdvaakw aaiatllsvf tgvtlnqgil itgaitavyc tigglwadal
      181 telgqfviql lagvsmfvav vlklndkgig ffdawnepal hghgkplvgp ygtvfllafl
      241 fiklfeyngg mlnqaqryma tagpkeaerg arlsaalwlv wpvvlffpmw mspllvhaqk
      301 pdgsdsyglm teqllphgll glvivgffsh tmamcssdan aiaavftrdv apvvsqrara
      361 wnersgliaa rvttvvflgl smtvatqins ptfkdiitvv ikwvaglmgp iaipmmlgll
      421 rpfrrsgpta altswaaglf afwlvnypin wnvdggvplq yqvsvplavs lvlyvligyl
      481 kpedtperla iiesvntdgd gataaavpag agagagegvp ap
//
LOCUS       WP_457681691             213 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681691
VERSION     WP_457681691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22450
     Region          2..177
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 msapcelrfd cgricldlaa tadgaaaerl agpdqlrawl tgaglvphgt pldgvdgrwv
       61 grfrglrell lrvvhdelrg gaaeadlall nsaaaagqpp avravrapdg tlaralpgpp
      121 ecagllaava rdaiglltda aaraqlrqce gesctlvyld tsrgrrrrwc ssevcgnrer
      181 varhrrrttv rreqsggava dpvtraenfs agr
//
LOCUS       WP_457681693             858 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces nigrescens].
ACCESSION   WP_457681693
VERSION     WP_457681693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..858
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92299
     Region          16..843
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 maahnathap dhasdsvrdr eieaeqthld rvyrrleeki heaeflmdda akrgqvgtpg
       61 alaerdaqvf qagvhlhrln seyedflfgr idlllgkdgk kgpdgaftsv epadgaiedg
      121 ratiaetlhi grlgvldady splvidwrap aaapfyratp vapgrvvrrr virskgrkvl
      181 gveddlmrpe vtatldgeel paigdgalma algrarshtm rdivasiqae qdkvirapaa
      241 svteveggpg tgktavalhr aayllyqdrr ryaggilivs ptpllvayte gvlpslgeeg
      301 qvairalgsl vdgaeatayd ppavsrikgs srmqkllrka argalelavp gaphtgreaa
      361 taaangsngg gapdgdaqls ledlfeasgd dserdaaang srrrrhrapr paqpaagppa
      421 hlrvvafggr ieldadelra irqsalggta pvnllrprar rlildalwtk sgaarrytdp
      481 elaaearegf dedittepdf qefldawwpe ltprgvlaam aderllgrwa rrllnprevr
      541 qlarslqrld rgghgplsvh dvalldelqm vlgapmrppr preadpldhl tgleelttha
      601 drmgggrsrr erleeertdy ahvivdeaqd ltpmqwrmvg rrgrhatwtv vgdpaqssws
      661 dpdeaavard ealgtrprrr ftltvnyrnp aeiaelaarv lalampgmas pkavrstgle
      721 prfalvadgn gtgtgngngr arsgddtala qatvaeaerl mgevdgtvgv vvamnrraqa
      781 rrwlaplgdr vvalgsleak gleydatlvv spaeiadesp aglrvlyval tratqqltvl
      841 saerdepdaa gvpdllrd
//
LOCUS       WP_457681701             551 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457681701
VERSION     WP_457681701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..551
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60515
     Region          4..530
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mpetdptpta pggglvpapl sidgpyrsav rlgedtvlaa epgtedtarw lratlgaafg
       61 lplppgsgka tdalalaldp slppegyrla adarwgvrit gggpagvfwg aqtlrqllgp
      121 qafrraplap eraavlpqqt vddgprfawr gmlldvarhf lpkdgvlryl dllaahklnv
      181 lhlhltddqg wrieirrypk ltevgawrkr tklghraspl wderphggyy tqddireiva
      241 yaaqrhitvv peidipghsq aaiaaypelg ntdvldttsl kvwdtwgvnp nvlaptdntl
      301 rfyehvleev lglfpspfvh iggdecpkdq wrasataqar iaelspaged elqswfirhf
      361 drwladrgrr ligwdeileg glaegaavss wrgyaggiaa aksghdvvmc peqqvyldhr
      421 qdpspdepvp igfvrtledv yrfepvppel tadqaahvlg tqanvwteam dsqqrldyqv
      481 fprlaafaev awsrlpapad rdyqdftrrm aahytrldal gvdyrppggp lpwqkrpgvl
      541 grpidgappn v
//
LOCUS       WP_457681706             509 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681706
VERSION     WP_457681706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 509)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 509)
  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 509)
  AUTHORS   ter Beek,J., 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 509)
  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   6  (residues 1 to 509)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (residues 1 to 509)
  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   8  (residues 1 to 509)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   9  (residues 1 to 509)
  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   10 (residues 1 to 509)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   11 (residues 1 to 509)
  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 10002138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54767
     Region          90..488
                     /region_name="LivK"
                     /note="ABC-type branched-chain amino acid transport
                     system, periplasmic component [Amino acid transport and
                     metabolism]; COG0683"
                     /db_xref="CDD:440447"
ORIGIN      
        1 mstrlfeppr pprrwglwii svlvaaavvv aavvqivetn grcgegvrev adgecvgvtd
       61 gayafgnmks lsdriraend evvksgersv aiayleamag gsadrgpeat rqaisgayla
      121 qralnaerst lpkirlllan tgrgdrhwrq vvdqliamkd kerlvavagf gqsndrtmra
      181 vqrlraaglp mvgatvaadg lssrtagfyr vsfpnrdqta aaagylkeqq rkhpgyrvqv
      241 irdgnekdny ntslyedfsr aarhagldvd deiipfrsge deaatagnal slvadkvcgd
      301 pkppdavyfa grgrelrrfi eaageggrhc rttvlsgssa lgiyfdtggd rhraelatla
      361 erwkdsqltv yytafthpai skevyggagn gpfddferay rtavggpttd lasgqamlgh
      421 datytigkaa rnavgvygtr qvtarmvlam leqtngrsrv rgisgyiafd pdtgepvdrp
      481 lalvelrrpt dtgeagdiyr fvtglsagr
//
LOCUS       WP_457681712            1069 aa            linear   BCT 27-JAN-2026
DEFINITION  efflux RND transporter permease subunit [Streptomyces nigrescens].
ACCESSION   WP_457681712
VERSION     WP_457681712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1069
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110199
     Region          3..1015
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mswlsrlslv qrglialmsi vaiafgaiai pqlkqqllps ielpmvsvla pyqgaspevv
       61 ekqviepled giqavdgvkt vtstssegsg vimaqfdygn dskrlvadvq qavnrarakl
      121 pkdvdpqvvn gstddiptvv lavsssgkdq qtladqldrs vvpdlknidg vsqvtvdgvq
      181 drivavtpdd kklaaaglns qslgqaleag gtsvpagsfa eggqsktvqv gagytsvrqi
      241 kdlriapsaa gggegagaga gagagagagq aaaepvrlgd vatvkeesat ptsltrtngk
      301 pslavmvtmd qdgsaveisd avkdqlpeir qdlgkgtdvt vvsdqgpavs ksiesltteg
      361 llglamaviv ilvfllslrs tlvtavsipl svvitlivlw tgdlslnmlt lgaltiaigr
      421 vvddsivvle nikrhlgyge erreailsav revsgaitss tlttvavflp igvvggmvga
      481 lfgsfsltvt vallasllvs ltvvpvlsfw flrapeipeg sdpeelrrka eekearsplq
      541 rlyvpvlrfa trrritsvvi avvillgtfg mgpllktnfl dqgdqgtltv kqelkpgtsl
      601 daaekqakkv ekllaanddi adyqvtvgss gfmaafgggt ganqasyqlk ltdaadsdkv
      661 tsdlrdgldk lgtsigettv tagggfgnqd lsvvvkaadg evlkkaseqv rktvaglddv
      721 tdvqndlsqs vprisvkpna kaaaagfnqt tlggavaqav rgttsgtavl ddterdivik
      781 sahpatteae lknlalptpa gpvklgtlat vrtvpgpvem tridgarsat vtakptgdnt
      841 gavstalqnk indlklpdga saeiggvsqd qtdafsslgl amlaaiaivf mllvgtfrsl
      901 iqplillvsi pfaatgaigl lvatgtplgv pamigmlmli givvtnaivl idlinqyraq
      961 gygvveavie ggrhrlrpil mtalatimal lpmalsitgd ggfisqplav vvigglitst
     1021 lltlllvptl yamielrker rakkkaakrs gpagpqtket dpapepagv
//
LOCUS       WP_457681750             312 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457681750
VERSION     WP_457681750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31765
     Region          57..292
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 migveaglgl ladggedtgi wheifnfnny gellalvqns lfagvllglv gglagvfvim
       61 rdlpfavhgi selsfagasa alllgvniva gsiagsliaa aaigvlgvra rdrnsvigii
      121 mpfglglgvl flslykgraa nkfgiltgqi iavgtpqmaw lvgtsvvvlv alavvwkplt
      181 fasvdpevae argvpvrtls lafmlvlgla valcvqivga llvlallvtp aaaaaritas
      241 pvllpvlsvv falcameggi llalgstipi spyvttlafv iylgcrlaes rrtqraprta
      301 lgspgtpvrt ht
//
LOCUS       WP_457681765             296 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457681765
VERSION     WP_457681765.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=31582
     Region          35..288
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mnshlqeeae taaaprqplr lpteqresgp lwssyvyaig ragtglgtaa prltglrdgr
       61 lrtvtagplt alvssvpada fstegmkaql enlteleeia rthhtvveaa htgttvlpmr
      121 latvyldddr vrsmlrerga efgallsrle ghaelgvkvy adprataaep ppapdgpdpa
      181 aspvspgray lqqrraqrrt qrdayraaga laddvrvrva alardrvvhr pqqgelasga
      241 genianeayl vptdrirefh ralagladgv pgvrvevtgp wapysfatpp aesrsa
//
LOCUS       WP_457681774             589 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681774
VERSION     WP_457681774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 589)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 589)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 589)
  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 589)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..589
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60506
     Region          30..579
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mprtpgpssp ppaarpgpdt gvrsvltgaf rhspvravav clfsvasaga avalpavlgh
       61 tldlvlgarp glhgalvlca vlltaevlld alvaltggvt tarstawlrr rgidhllsla
      121 phrvadrltp gdlvtrltgn aadagtapta aatglaalit pvgalialal tdiwlaavfl
      181 aglplltrll rafargssds vrryqrvqad iatrlvealg gartvaaagt agrerarvla
      241 plpelgaqgr qmwqiygrav vsssilvpll ttavlavggi rlaygslsvg ellaasryaa
      301 ltaglggvvg qlnalvrsra aahrtgellt lsppvhgttp lpadgrgrle lravtlvrgg
      361 aqalrgvdlv vpggttmavv ghsgagksll aavagrltdp dsgqvlldgv plheadpaql
      421 rreigyafer palfgatvga aigfgpyepp ahaiegasra agadtfvrll pdgyatpldr
      481 aplsggevqr lglarafaha grllvlddat ssldsvtelh vrralvhdvr tgsrlliahr
      541 vssaaradlv awmekgrlra vaphdrlwad pdyravfaht ddedtrtas
//
LOCUS       WP_457681777             369 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Streptomyces nigrescens].
ACCESSION   WP_457681777
VERSION     WP_457681777.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  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 369)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..369
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=39498
     Region          6..354
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mgsdlltlfl cgdvmlgrgv dqilphpgdp alregyvrda rayvelaaar ngpiprpagf
       61 swpwgdalev lddaapaarv lnletsitqy ggfapekeih yrmnpanlpc laaarpdvcv
      121 lannhvldfg rqglaetlgt lagaglrtag agadpcaarr pamvpvadgr rilvfsfgmp
      181 ssgiprdwaa agsrsgvdfv arptpaaage iigrvrqlkr pgdlavasvh wgpnwgyhvt
      241 rseagfahal leggvdvvhg hsshhprale ayrgklvihg cgdfiddyeg itgyeayrdd
      301 lrllflvtvd pdtgrlhdvr iiplqsrrmr lrhaspedsr wlrglldrig sgfgpcaaep
      361 egtltlrps
//
LOCUS       WP_457681782             290 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681782
VERSION     WP_457681782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31387
     Region          59..270
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mylasvthqg rdrlagrlap qdpwrlapps vslaeviggt lpwswnqlpt gadlvpvlpy
       61 rpgalygvgm nyrdaieerg gerpaeprlf pklsssvigs geavvidpel tqrvdwetel
      121 avvigtearq vsetdalryv fgytvandis ardlqerdgq wlrgkgldtf cpfgpvlvta
      181 deipdpqrlr irtrvngetv qdgstadmvf gvpaliayls rfftlrpgdv vltgtpagcg
      241 dfmrprrglr pgdlleseve gigrlanpvr ssvrdgager vtvpqepggk
//
LOCUS       WP_457681784             300 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681784
VERSION     WP_457681784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=30823
     Region          6..298
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 maagtpfalv dvftdqpleg nplalvpdad plpegllpri arefhqaett fllrpdrpga
       61 twrlrsftaa gvevfgaghn algawwwlaa agrlgpglgt grwsqqlgte vlpvgitade
      121 hglievtleq raaaygdelt draalaealg vdgrelgaaa glpvaqvvst gaahlmvglr
      181 drgvvdaarp daarlrallp evggqgvyly aldpaepgad vharfvnpva gitedpatgs
      241 aagplacllg rhgragnevt lvqghtlgrp shlrvtvvdg ipcltgraal aatgelhlpg
//
LOCUS       WP_457681804             254 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681804
VERSION     WP_457681804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26369
     Region          14..247
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtgapslaac lhslravifd tdgvitdsap vhaaawkgaf daclaavggq rpfdpvddyl
       61 ryvdgrarqd gaaaflrsrg ldlppgepdd apgtdtvcav aarkeelfse slrarpiatw
      121 pgtvrllhal rhhgvpcaav sasrhatell saaevyplfg avvdgneanr lrlpgkpdpa
      181 lfveaarrlg vpprdaavve dalagveagr rggfglvvgv drtagpysat alrrrgadvv
      241 vtdpgellrs gege
//
LOCUS       WP_457681802             574 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457681802
VERSION     WP_457681802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 574)
  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 574)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   3  (residues 1 to 574)
  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   4  (residues 1 to 574)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12187228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..574
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61487
     Region          54..201
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
     Region          221..361
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          349..574
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvgdhgsgrr dtarrrldal pdelqqrlda lrqgpgdpan llleavlsvg rgldlpqvlr
       61 riveaavvlv daeygalgvv segtrlsqfl pvgvteeqqe eigrlpeghg ilgelirhpr
      121 plrlpelsrh pssygfpphh ppmrsflgvp irvrdevfgn lyltekrggg afdaedetvl
      181 stlavaagia ienarlyeea ryrqrwqean gaivaslllp eaderaalgl ivdqareilt
      241 adlgviavpe pdgtalhval asgvdaeahr glllplqgsf mgaaldlrep listdverdp
      301 rittgpprwm glgpavavpm itggrprgvl lvarvrerap fteletgpll tfagqaalam
      361 eladqrrsae hltllqdrdr iardlhdlai qrlfatgmtl qsavrfvehp easerllrav
      421 ddldetikii rstifglrth tsgrashglr vrtvaaveqa aralgftpsl rmqglidtdv
      481 paelaehvva vlgealsnaa rhahatavev slavgggals lsitdngvgl prngrrsgls
      541 nlakraesvg gemtletpaq ggtrllwqap lpss
//
LOCUS       WP_457681821             351 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457681821
VERSION     WP_457681821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36278
     Region          10..343
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 metpltrlvg vrhplvqtgm gwvagprlvs aaanagalgi lasatmtveq lraavhevks
       61 rtdapfgvnl radagdaaer vrlvvaegvr vasfalapsr eliarlkdag vvvipsvgar
      121 rhaekvaawg adavvvqgge ggghtgsvat tvllpqvvda vdipviaagg ffdgrglvaa
      181 laygaagvam gtrflltsds tvppavqary laaavkditv ttkvdglphr mlrselvetl
      241 ersgrstall ravrhaasfr klsglswaqm vrdglamrhg kdlswsqvll aantpmllka
      301 smvegrtdlg vmasgqvagv iedlpscael vdrimaeara tlaalppdpp r
//
LOCUS       WP_457681823             319 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotriesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681823
VERSION     WP_457681823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chen-Goodspeed,M., Sogorb,M.A., Wu,F., Hong,S.B. and Raushel,F.M.
  TITLE     Structural determinants of the substrate and stereochemical
            specificity of phosphotriesterase
  JOURNAL   Biochemistry 40 (5), 1325-1331 (2001)
   PUBMED   11170459
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shim,H. and Raushel,F.M.
  TITLE     Self-assembly of the binuclear metal center of phosphotriesterase
  JOURNAL   Biochemistry 39 (25), 7357-7364 (2000)
   PUBMED   10858282
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kim,G.J. and Kim,H.S.
  TITLE     Identification of the structural similarity in the functionally
            related amidohydrolases acting on the cyclic amide ring
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 295-302 (1998)
   PUBMED   9537960
REFERENCE   4  (residues 1 to 319)
  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
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Tuovinen,K., Kaliste-Korhonen,E., Raushel,F.M. and Hanninen,O.
  TITLE     Phosphotriesterase--a promising candidate for use in detoxification
            of organophosphates
  JOURNAL   Fundam Appl Toxicol 23 (4), 578-584 (1994)
   PUBMED   7867909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004443
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..319
                     /product="phosphotriesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32857
     Region          14..309
                     /region_name="Php"
                     /note="Predicted metal-dependent hydrolase,
                     phosphotriesterase family [General function prediction
                     only]; COG1735"
                     /db_xref="CDD:441341"
ORIGIN      
        1 mnrapagrpa apavrtvlgd iapaalgvcd ahdhlflrsp qlpgqeldda eaaaaelsaf
       61 raaggaaviq wtpygmgrra aelprlares gvrivaatgl hqaahyspel larvrpdlag
      121 lfvaeltegi ggtgpragmi kvaggfhgld rharhtmaaa aeaqratgaa igvhlelgtg
      181 aldvldllcg tlavppdrvi lghlnrspdl vvhrtaaeag aylafdgpsr ahhatdwrlp
      241 ealaalaeag fgdrillggd tttagarsvn ggpgmpyllr rhrerleval gadlvaqflt
      301 anparafaad warapggsr
//
LOCUS       WP_457681826             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681826
VERSION     WP_457681826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21577
     Region          15..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstqeppgtq eppgtqerlv rstqellwer gyvgtspkai leragvgqgs myhhfsgksa
       61 lalaairrta eelkhaseec laapgtaydr vaayllrerq vlrgcpvgrm tqdrdvvqsa
      121 elrrpldemf dwlreritev ltegqrrgel aaaldpaata atvaavvqgg yvlaraaddt
      181 apfdaavqgv lallaaqvpt ag
//
LOCUS       WP_457681833             485 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457681833
VERSION     WP_457681833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..485
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..485
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=49064
     Region          11..485
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msmlkgsnvp vpapavrvel gwqaapgvpd vdasalllvs gkvrddadfv fynqaahasg
       61 avrhegkrpa ggamtdclav dlaavepavd kvvlaasadg gsfgsvpglh irvldaagga
      121 elarfdsqda gaetafvlge lyrrqgawkf ravgqgydtg laglatdfgi sveepaapqp
      181 papapapaap apaptapapa paapappppa mapappmapp ppapappvap paapapplpt
      241 gqpaasvppp pgqpapapap pavrltkvtl tkdapavslt kqggtsgamr vnlnwsagsa
      301 gkrlgkklgr kameamgarg allppsgeld ldlcalyqlt dgsagvihpl gnnfgalhap
      361 pyiqldgddr tgavaagenm tinldhqdri krilifvtvy agarsfegls atvtlqpqhg
      421 apvdftldac tvpsnvcala mitntgselv vqrearylvp dpgvspqrtv dqaygwgldw
      481 spark
//
LOCUS       WP_457681835             282 aa            linear   BCT 27-JAN-2026
DEFINITION  glutamate racemase [Streptomyces nigrescens].
ACCESSION   WP_457681835
VERSION     WP_457681835.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10002726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="glutamate racemase"
                     /EC_number="5.1.1.3"
                     /GO_function="GO:0008881 - glutamate racemase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28054
     Region          24..217
                     /region_name="MurI"
                     /note="Glutamate racemase [Cell wall/membrane/envelope
                     biogenesis]; COG0796"
                     /db_xref="CDD:440559"
ORIGIN      
        1 mkialmdsgt gllaaaaamr rlrpdadlvl ssdpdgmpwg prtpddvtah alavarsaaa
       61 hrpdalivac ntasvhalpa lraelepqip vigtvpaikp aaagggpvai watpattgsp
      121 yqrdlidrfg rgadvtgvpc pgladavqaa deaaidaaia aaahltprdv rtvvlgcthy
      181 elvaeriraa lqqpgapalv lhgsaeavaa qalrrigaep apaaaptgal svilsgrpag
      241 lpaealayae grllarsrtd lapgaavpaa paadgataaa rr
//
LOCUS       WP_457681838             168 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681838
VERSION     WP_457681838.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 168)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18390
     Region          4..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpdfirdl rnsigrqllw lpgvsavvfd gqgrvllgkr vdtggwsvig gipepgeqpa
       61 etavrevyee tavrvvpegi vlvetmppth ypngdvcqfm dvtlrcravg gearvnddes
      121 levgwfavda lpelkeyalt rikraleagp awfhgmeeer pgrhpeea
//
LOCUS       WP_457681840             473 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457681840
VERSION     WP_457681840.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49040
     Region          15..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,75,133..134,136..138,141,161,
                     164..165,168,259,262..263,266..268,271,299,303,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 maapatsppa sanlrrivaa sligttvewy dfflygsaaa lvfnklffpg sdalvgtlls
       61 fltyavgfaa rplgalvfgh ygdrlgrkkl lvlslllmgg atfaigllpt hatvgtaapv
      121 lltalrlvqg falggewgga vllvsehgda rrrgfwaswp qtgapagqll atgvlsvmta
      181 llsdaaftsw gwrvpfllsg vlvivglwvr lsvdespvfr aalaraearr aegaalekmp
      241 lvavlrhhwr dvliamgarm aenisyyvit afvlvyatsh tglsqqtaln avliasalhf
      301 avipawgals drigrrpvyl lgaagvgvwa fpffalvdsh hfgplllavs vglvfhgamy
      361 apqaaffaem fatrmrysga sigaqfssva agapapliat alladydspt pialyviaaa
      421 lltllavgva retrsrdlta vegnavegda vagegrtagp dggassavps gga
//
LOCUS       WP_457681842             268 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457681842
VERSION     WP_457681842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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 268)
  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 268)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28609
     Region          1..268
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 marhkylrwp vlagllvlvg agfavlpahp aqaviggqks staaapwtvt inlwrqtdty
       61 prsgqfcggt lvtprkvvta ahcvvdeapt dlgvvagrtd lrrhegrmrk vtkawihprf
      121 grhlendvav ltldkpmppq ytplpvataa dtgpyrpgtr arvhgwglld negreanvlr
      181 sanlrvladr tcqrlnpwgd idpkmhvcan dpvtgahhae gdsggplvag gkligivswl
      241 aggnattptt gvytrvaafs reigrqlg
//
LOCUS       WP_457681846             193 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681846
VERSION     WP_457681846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=20021
     Region          32..174
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mslsaadssl qsgtqqsgqa svtagllrrv aghyptgvvl vtgprpapgq pppamvvgtf
       61 tsvslrpalv gflpaksstt wpriraagrf cvnvlgadqq qvcrrfaaad phrwevphre
      121 tatgspvlld alawfdceva geaeagdhwf vtgtvrdlgt grpgpplvfl rggyghcaed
      181 tdaarsgrpa gpd
//
LOCUS       WP_457681857             465 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457681857
VERSION     WP_457681857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..465
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49110
     Region          38..460
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mrprgaavaa diegtlirrg dpgyedartg avwnevtprr fpdvlvraat eadvvhaltw
       61 araqglrvsl rsgghnwsga plrdggllld lsglrqcait pahgsgppta tvgpaatgqd
      121 lvaaltpqdl afpvghcptv avggfllsgg lgwnsrawga scadvreira vtadgrtvic
      181 sdteypelfw aargagpgfc aavtgfrlal hphpasimat gltfpldevs rvtewaepla
      241 rrlppyveta fvlassgppa asaprgprit vaatafaate rearqalepf adcpfgacav
      301 trqppapvsf aalhegaaai wppahryaad nlwspeshat qltriadava hapsgkslvl
      361 spvqpvsqep allrnmafap lgesylvcya iwddpagdqd narwlrdama aadprgdgcr
      421 yiaetdleag pararrsyap atwdrlqeik aqwdpenlfh sylap
//
LOCUS       WP_457681854             403 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681854
VERSION     WP_457681854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43631
     Region          88..403
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslsslsrra vvgaalsgav vaatagpara asrpapapss ggparrippa papvpplnvp
       61 alraalsdle hpqltaaqlr vtgsaghwyg nagvadratg rgvherdtfr igsitkvfva
      121 tvvlqlaaeh rlspelpvqr llpgllpskf ppitvlqlln htsglpdeqd ppydptspee
      181 iarhrydrwt peqlvarvth gpmkftpgtk qeyrsinyil lallierltg rrygeviarr
      241 ilrplglrht svpgndprih gphvhgymrm tdgslldite fdqsaawggg emishtgdld
      301 rfltalfsge llpphelerm ftlppdevrm vdggparyaa glqtvtmngi tlwgktgery
      361 gycsamvatr dqqrravfsf nptrrdasqi qasqriaeal tka
//
LOCUS       WP_457681852             528 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681852
VERSION     WP_457681852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..528
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=54775
     Region          2..476
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mphrvrvkts agtvlgrqda gvsvfwnipy aaapvgtgrf aapvapapws gvrdagepgp
       61 tapaalragf gpldmsallg sgwvtgedyl gvnvwtpsph rdrlpvmvyv hgggflngsg
      121 raelydgtgf ardgvvlvtl nyrlgvtgwl dvpgapanrg lldviaalgw vrdnisgfgg
      181 dpdqvtvfgq sagamivaal laapqaeglf rraisqsgsg lcafaprqae rvtravavrl
      241 giapsagafa gipddrlvsa vaglgpvdva gdghydtslg sspfkpvldg avlsqqpvda
      301 vaggsgsavd lligtnadea nlyvvpagra ariteaevsa aaarrhpdpv alvaahraqr
      361 pdaspgella hlvtdafteg srqladahaa rsaagthayl frwrpaafgg slgachcvel
      421 pfvfdrtelp glrgprallg dgdlppdlas rmhrawisfa atgdpgwqpy raegraegra
      481 edraedraed raeertedra edraedravq iidvrwtmsq vrgassga
//
LOCUS       WP_457681865             142 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457681865
VERSION     WP_457681865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15690
     Region          8..141
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mpsikqfqvt fdcaeperla rfwcevlgyv vppppegfat wgdfhrslpp edqgswsaci
       61 dpsgvgprly fqrvpegkvv knrlhldvrv gtglvgeerl aaleaectrl vplgavrvql
      121 lydgndsciv mqdiegnefc id
//
LOCUS       WP_457681866             219 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681866
VERSION     WP_457681866.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22571
     Region          9..191
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msslptrtea vvfdcdgllv dtepcwtiae talfaahght fgpeqkalvi grtveaaaea
       61 madyfgrpga gpelaaelle rvrkelahga aalpgatelv racraavpia vasnsprell
      121 dtalesagla pyithsfaad evrspkpapd lyltacealg aapkrsvafe dsatgisaar
      181 aaglyvavvp slpgtgldhd wlstslgdpe llgwarelg
//
LOCUS       WP_457681879             690 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681879
VERSION     WP_457681879.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 690)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 690)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 690)
  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 690)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..690
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73247
     Region          33..617
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mpdeaetgge elqfvdrtgs reragqqirl admarrlprl vrrsvalaws idrwaclgll
       61 vcqvasgamq algllavsgt iaallaggdi ygrllaawps lvmlagaaaa rallgitvaw
      121 lssrlgpqms reaelgllra vtevelsayd apgfnhrkea aergaevaqd lvtegqdlia
      181 slasliagag vltalhpall pllalasfpq avaqisaarv rylarlrsng dyrllsilrw
      241 hvgdryaadq iragtmssfl vgryrhitdr inradrraad tgarmsvlga lcggvasaav
      301 waavvwmlat grmsvghagt avfalqtvgm alrglvvgga rimrtglymd dwsaflreag
      361 gyrmnrgttv pgppqqitvq dlvfryeeaa ndavrgvsft lrrgevvalv gyngsgkttl
      421 akllsglylp ttgsvtwdgv ptgeldpqam wshvalvpqd yarwpltare nmtlgqptsg
      481 gdadihaaca rsgadevlte lrsgldtvla rdwlggqels ggqwqrialt rafyrpagll
      541 vldeptaald plgehrifag lrqlaatrav vlithrltnv acadrilvlh kgrivqqgtf
      601 pelvaepgpf rdlwayqhtr eaadpaadgr saddcapsah papgvpvpvp apqpaphgdt
      661 vprtrksteg ertsasaeae tdaeaeaeap
//
LOCUS       WP_457681884             539 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681884
VERSION     WP_457681884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57566
     Region          18..536
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mnqpteaqdq aaeardqaar vqdlrvdieg ralvdgvslr vppgritali gasgsgkttt
       61 glallneypp garvtgqvht pdtlvgyvpq hpatvlnpar pvaallqdia rthvshlprr
      121 arrseirhri lralaqaqlh dgetlldryp hqlsggqqqr vvlaqalltg artliadept
      181 tgqdavtkqq iadqlaavar egiavlllsh dlevvralah dvhvlragri vesgppeqlw
      241 sspqhswtre llttaapaep sdgplapstd agtpagetts gpaaaeavlq vrsltarhgr
      301 stvlqtpell lppgcsalvg rsgsgkttla rclaglhrsy dgevlldgva lprslrdrtp
      361 eqlaavqyvf qdaraafdeh rpvlgqvmrs airlrrvprp ealaeaertl stlglsgdlv
      421 rrrpgqlsgg elqraalara llarprvlic deitsgqdsv trrnlrtlla dlvrthpems
      481 lvlithdrdt atlatwiavl ddghlveqgp tsqlltaprh pltaallqpe pevsaaspq
//
LOCUS       WP_457681888             495 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681888
VERSION     WP_457681888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52458
     Region          <185..>269
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          398..482
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mipavrrtgl lcaltataal lpaapapaap pppalrfgac pdsvpappap ervecgrlsv
       61 pldrshpdgq hldiavsrvr asgpaserrg vllvnpggpg gsglpyavtk raklpekvrr
      121 sydvigfdpr gtgasapadc gpmgglfdsp gqdpvptgra aeqkyldglr rtaddcaqhv
      181 kdalphlstt etardmdair ealgerrigy lgvsygsylg aayaaqfpqr vgrmvldsvv
      241 gpeewydfdl lqsramvrqr avffawaarh ekrfglgadg tavrtayqrv rdglaerpvd
      301 gfgaaefdra vyralgrter wagladglqt ylrdgttgpl rpaepfdgpa srtyeaanrt
      361 vkcadgpaps parvvadirr mrrldpqpvl tgmeasvcay whhrpahgtp lgspdappvl
      421 liasehdpvt piegaralqr rlpgsrlvsl hddyshgvfa srgngcvdga aaayltdgtv
      481 pradvhctgp glptp
//
LOCUS       WP_457681900             262 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681900
VERSION     WP_457681900.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28577
     Region          14..261
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mastrsslae vdrrrqdvlt hvvehgevri ddlarhfgvs latmhrdldq laerrllrke
       61 rgraapfpsl tmetatrfri gvnhpvkeal caavadeirp gstvvlddst tvfpladria
      121 rteavtvvtn slgvarlfde tpgtdvtllg gryrgefgsc vgpdvlrglg riradlavms
      181 avsvlggrlf hpireyaeik eamlecaqrs lllvdhskfg ktathaygdi ghydrvvtdr
      241 gtpaeeltal rrkgvtvdva ev
//
LOCUS       WP_457681905             243 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457681905
VERSION     WP_457681905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26605
     Region          20..217
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          60..155
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mfapqgptfr elavqalssv ergydllapk fdhtpfrtpd rvltpvsral hglgpfdsgl
       61 dlccgtgagm dvlrqvcrer vtgvdisagm lsvgrtcerv saaaprvewv radaralpfg
      121 pvfdlavsfg afghflprer pglfaqvhsv lrpggrfvfp igapprpgsa gywtllafda
      181 vmrvrnalwr pdfvmyyrtf rlaevraeli qagfevqlqa lpelgrrpdg sprcrlvvat
      241 rar
//
LOCUS       WP_457681908             540 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457681908
VERSION     WP_457681908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..540
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56514
     Region          225..526
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpvmslqrll dsvgpavlsg vcapggtavp vgdvviaerd ggfdlrpgdv vlgvnltdra
       61 qalrllslca ersagalllk apaavdetvv taasaaglpl vqveqqagwa qvvsllravl
      121 dsegyvdsgs gtagaeagdl fgladaiaav idapvtiedr ssrvlaysar qergdearva
      181 timgrhvpde vnahfrrygv fhkiaqdpgp iyvpavvegt kprlvvpvha ggdvlgsiwa
      241 ivpgpvpaer aeafadtaat aalhllrrra gadverlvlt dmvatvlhgq egaadaarrl
      301 glttgpwrvi avgvrceddg eaerqrltvw ermsrfrgsr lrspaaivgg vvygivpaer
      361 vapgaddgpg wletlrgtag rpaplvavgg laasvpglar sreqaddtld llrtgliard
      421 qavhdevwat vvlrhvarsa aaariagvgp lqqlvdhdra hgtncvptly awleamgdpr
      481 aaaarlhihp ntlrhrmrrl qdvvalpldd pevrtalllq ltarqysteg gpddtvsasa
//
LOCUS       WP_457681912             157 aa            linear   BCT 27-JAN-2026
DEFINITION  lamin tail domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457681912
VERSION     WP_457681912.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Eldirany,S.A., Lomakin,I.B., Ho,M. and Bunick,C.G.
  TITLE     Recent insight into intermediate filament structure
  JOURNAL   Curr Opin Cell Biol 68, 132-143 (2021)
   PUBMED   33190098
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Dittmer,T.A. and Misteli,T.
  TITLE     The lamin protein family
  JOURNAL   Genome Biol 12 (5), 222 (2011)
   PUBMED   21639948
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Dhe-Paganon,S., Werner,E.D., Chi,Y.I. and Shoelson,S.E.
  TITLE     Structure of the globular tail of nuclear lamin
  JOURNAL   J Biol Chem 277 (20), 17381-17384 (2002)
   PUBMED   11901143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="lamin tail domain-containing protein"
                     /GO_component="GO:0005882 - intermediate filament
                     [Evidence IEA]"
                     /calculated_mol_wt=17854
     Region          41..148
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
ORIGIN      
        1 mfrnasrvam avlgsaalaa taalpasadg hhrhtpqrwr savvlgtiqy dspgrddrsn
       61 rslnaewvtv rntgrtpvni kgwslsdksg htyrfgnlrl aghsqirvht gyghdnrwdv
      121 yqdrrnyvwd nnrdtvtlrn dhrrvvdqer wghghrh
//
LOCUS       WP_457681920             529 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457681920
VERSION     WP_457681920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..529
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55815
     Region          124..365
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          427..522
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 matsrllras aavlaatall isgcssgsss pgseaspghr teagvqrpae aaslaplpas
       61 tpaslrpyyd qklswrpcsv agfecatmka pldyakpsad tdlklavark katgpgsrig
      121 slqvnpggpg gsaidylqqy apqpapvrar ydlvamdprg vdhsepvecl tdkqmdrytq
      181 tdvtpdspae vnklisayrs fakgcasrag kllshvstie aardmdvlra vlgdkkltyv
      241 gasygtflga tyaglypsrv grmvldgamd paldsrtvnl nqtagfntaf safaadcikh
      301 kdcplgttsv edagrqlsal fkkldahpva tgeerkltes lattgvvaam yderawpvlr
      361 eylaqakagn grglltlsds yyerdpngty anqmyanpav ncldlasafn gpdqvraalp
      421 sfrkaspvfg enfawaalnc aywpvkptgt ahrieakgaa pilvvgttrd patpytwaka
      481 laaqlssatl ltyegdghta ygrgsqcidt ainnyllkgt vppkgkrck
//
LOCUS       WP_457681932             475 aa            linear   BCT 27-JAN-2026
DEFINITION  SagB/ThcOx family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457681932
VERSION     WP_457681932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  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 475)
  AUTHORS   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="SagB/ThcOx family dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50540
     Site            order(258,260,283,286,328..330,401..402,405,413..414,
                     417..418,421..422,424..426,428..430,442,444..446,461..465)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380318"
     Site            order(260,262,264,330..332,334,415,418..419,424,428,
                     439..442)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380318"
     Region          294..470
                     /region_name="antibiot_sagB"
                     /note="SagB-type dehydrogenase domain; TIGR03605"
                     /db_xref="CDD:188352"
ORIGIN      
        1 mtvhllslhp gttlhdergl ltvrhrwgat ttgpytpqla aalrtladgp tsldglaeri
       61 rtaaraetpa epqlallrha vdrlghtllr hitadaqvla tavplapeat fgrepapdap
      121 vvlaraahlr pvgdslales prsrfrvrie dgraaaalaa larpltaael rcavrglpad
      181 svdalrsllh atgflhpadd gsraaaaelp agwsfhella hdgsraglrd rqygpvyplr
      241 dtepppppva parpgrtvrl hrpdlgrvar edrsftdvle nrasrrayge hplslaelga
      301 ylyraarvrt lldarpeegr hyavtgrpyp sagsahelel ylavhrcdgl drglyhydpl
      361 ghaltalpgg pgtvdrllhe saaatggapp pdvhltvvsr ikrlswkyaa hayaltlkns
      421 gvllqtlylv gtamglsvca lgggdsdtpv hafgldpyde ipvgafligs apkap
//
LOCUS       WP_457681934             421 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457681934
VERSION     WP_457681934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 421)
  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   4  (residues 1 to 421)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44955
     Region          64..324
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          335..400
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mrylvlnrtp ltgrpfpdwl gadheavllt daaavsaepd vrsaqlggya hveviddfhf
       61 nplvesralt lhrkggfdrv ialsefdilr aarlrelfgv pgqdvasata frdklvmkri
      121 lakagiplap fapvanlqdl lgfieqqgfp vvvkprrggg smdvhvlhdp qdvesllaah
      181 rdlgtddgaq llaekyiehe lvhvdgivta getrlmwpst qgdstcldik qgqalhscll
      241 daddplldpv reltgralaa lpvpdtfmfh aevfldadrr lvfnevasrm gggmiehvlq
      301 lgfgitlpev yvrslggnap aavpavperi aglslfppra gtlvaipdtc pvpgidtytr
      361 haapgtvlep arlsvekigs vlatgrtrge vetalaeala wferstvirp gtdgtgagsa
      421 s
//
LOCUS       WP_457681936             420 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457681936
VERSION     WP_457681936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..420
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45186
     Region          56..332
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          345..420
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 msilllhtrn lsrrkhlarv rdyarehger llmimkdatw essyvdcvvp adttsieetv
       61 aavrtliaae eepvrgivtf veqsvpaaaa vaaelglpsi gekaaylard kyamrsafge
      121 aglaqpgfql atdldaavkr aaelgyplvl kpligggsky vrrvdndael aehfaplqrg
      181 awtgfahdpl htrtraqyde allleayvpg seisveslvv dgetrivavh dkplpmegpf
      241 feevyyttpt rlpdglvrri taavgaahea lgittgatht efritadgep yiletaarlg
      301 ggpvyqsvll stgidmveaq ldlatgrapr ldvagpprpt gfylffaera gelvgvagld
      361 qvetddrvse imlygqpgdq vlvpphasaa hghvvfsaat aeaveeafhe frdaiavevr
//
LOCUS       WP_457681943             278 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457681943
VERSION     WP_457681943.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30912
     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          92..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnrndlnpda speaaygarl rslreargwt qedlaeraey ssvhvsaven grkpptlrfs
       61 rsvdrvfgfe gtaesferay reikhgslle gfpeyvgyeg raveirlyni giipgllqtp
      121 eyarvladsa vrrgaitpeq aderveflae rqavlerprp pmvfvtldes cirrpvggst
      181 vmdaqlarlv efadlpntll qvapydiger rtlnlpvniv tlpdrsliyy aesqaqgnld
      241 restsvvpvl tayhqlqaea lsqaasvdmi eqlrkgip
//
LOCUS       WP_457681947             331 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA family dioxygenase [Streptomyces nigrescens].
ACCESSION   WP_457681947
VERSION     WP_457681947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Islam,M.S., Leissing,T.M., Chowdhury,R., Hopkinson,R.J. and
            Schofield,C.J.
  TITLE     2-Oxoglutarate-Dependent Oxygenases
  JOURNAL   Annu Rev Biochem 87, 585-620 (2018)
   PUBMED   29494239
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schofield,C.J. and Zhang,Z.
  TITLE     Structural and mechanistic studies on 2-oxoglutarate-dependent
            oxygenases and related enzymes
  JOURNAL   Curr Opin Struct Biol 9 (6), 722-731 (1999)
   PUBMED   10607676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="TauD/TfdA family dioxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35490
     Region          40..311
                     /region_name="TauD"
                     /note="Taurine catabolism dioxygenase TauD, TfdA family;
                     pfam02668"
                     /db_xref="CDD:367137"
     Site            order(83..84,111,113,118,169,314,316)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238154"
     Site            order(108,110,135,301,310)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(108,110,301)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
ORIGIN      
        1 mtatfdgtav petlgdgael ilgegrtpvl gvtgpdlpge tvrallgryg allvrglgla
       61 apadlgraaq algvtpmter egftgrtdfg dgvygasewp adepmcmhhe rsygdevpgi
      121 alfgcltapr tggatavada rtvlaklpad iverfardgw rlartyrdig vswaesfgtq
      181 dtaevdaycr ahaldhewlp dgglrtvqhr aavvrhpatg erlwfnqiaf lneltmdpav
      241 reylvslygp gslpfttfhg dgepvpaqvv etinevytaa tvrepwqagd llvvdnlrma
      301 hsreayegdr eivalfgdpv rldghvrpsa d
//
LOCUS       WP_457681949             809 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457681949
VERSION     WP_457681949.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..809
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=87670
     Region          2..805
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mrrtaipagt aeallllser pglsegqgls pdtlllaayv rvlaavtgds svvtgylpee
       61 gpeksplplw aalsqgswad lvtevaqlad evgrhapqal delraetgrt eplfdtvlva
      121 grapgpedlt dgtvlaagls rtgdrlelvl shrpdaldge qadrfagyll aalrelaerp
      181 gadhqewspv perevaqqla efagprrelp drrvhelied qvrlrpddia avhgteswty
      241 relneranrv ahalrrgglh dedvvavvte rnlpwlvavl avfkaggvyl pvephfpadr
      301 isgmlvradc rrvlterdas pgltealagl pavradhldt llaedhpvtd pgipvaagqs
      361 ayiyftsgst gapkgavceh agflnhllak iddleitegr vvaqtapqcf dislwqlvaa
      421 lavggrtlii gqpdildtar fietldtggv evlqavpsyl evvltelers pralprlrhv
      481 satgealkke lverwfatfp dvalvnaygl tetsddtnhe vmrrvpeqas vplgkpvanv
      541 rihvvderlr lvplgspgei lfsgvcvgrg yvndeertra afmpdpllpg ermyrsgdfg
      601 rwlpdgrlef lgrrdaqvki rgfrieigev enqllrvdgv rdsavvvtge gesrqlvafh
      661 sgeelsdatl leslgaalps ymipsrfrrl dvlpltangk idrkaltrla gqeesagdgv
      721 elrtgterrl aelwsqvlkv pagrigrash ffdsggtsls mlrlaialdr vvtpvelqqh
      781 pvlaecaall drraaeapnp grqpvdshv
//
LOCUS       WP_457681951             192 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681951
VERSION     WP_457681951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20017
     Region          19..172
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 maslppppsa pdtatrpvpa ddfrslmgaf ptgvavitty gtddrprgmt csslssvtta
       61 pptlsvwltt rgetlgalre ygafavnllh drgqragevf ahpvadrfsq vgwrrspeag
      121 lpwladdafa vaecrvtklv evsdhtlvvg avtgvtqdag tpllygarrf aswpggeapa
      181 aplaldtplt sc
//
LOCUS       WP_457681955             431 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457681955
VERSION     WP_457681955.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /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=45477
     Region          51..322
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtdlelrpps pvrrpplptg plrplpprrt pwqalhtavl ridaatpter draidvlral
       61 aiagvvlghw lvsgvvlqag ghlvgdsplg hlpglapvtw llqplavffl vggrvsarsy
      121 atarargigy rpwlaqrlar llrpatafal twglvwlglv lagtahetih tlmwlayspl
      181 wflgvyalli aatplvhkag ariavvaclv vaaldasrvl fadsgwpdtl rllnipagwl
      241 vpyclgavwa aggftrrrpa lalllgggga maalilwggy pasmvgvpgs tlsnlspptl
      301 aavafglaqt gaalllrgpl rravtapapt apataprsra twgqflwaav allnlsavtv
      361 flwhqtamlt ttviplglgh tfpglhtspd slawiaarfg wiavfvvall vlatafrdre
      421 gargnraiin q
//
LOCUS       WP_457681953             989 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457681953
VERSION     WP_457681953.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 989)
  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 989)
  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   3  (residues 1 to 989)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 989)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..989
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=108316
     Region          10..257
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          139..989
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          807..835
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          847..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(848,851..852,855..856,858,888,891..892,895..896,
                     898..899,928,931..932,935..936,939)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          886..916
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          927..953
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpedrsipra ikysvlrpll vitgsgriig vhgprqrtil tmlilawgrv vsvdslvdav
       61 wgdeppatar tqvaicigal rksfkqagve gdviltthpg yrlettgsdl dalqftslva
      121 eaaahvkqgr heqgrvlyrq aldlwkgpal agvtgrpved eatrlderry aayeawseve
      181 lalghhqdii seltsianss plheqlrynl mlaqyraglr aeategfrmw rrnfvdelgl
      241 epsvaikelh asilqddpgl tlpvqvkpmv vpaqlppdvd lfqgraaelg eldrllgeka
      301 pgmglitgva gvgktglivh wahkvagefp dgqlyadlsq ydgkqpefva gallgrflra
      361 lgvpgdqips dpaelaslyr svladrksli vldnvrtmsq itallpgtgr scvlaasreq
      421 laadsgtvrv dlglmtahes qtlitkiage gratsekaav nelcrlcdgl plalriaaar
      481 lvakqhwsvq hlvdrlrdeh rrldelstgg levrasfals yrglteqtar myrllglldv
      541 pdfpawvgga lldvspaeae dmierlvdah lltpigsdat gtmryrfhdl lrlyarerae
      601 sdeaedkrra alhrvfrtyl tlaeqghire yggdfaiihg stprrhldap lvgrllgspl
      661 dwfeaerpsl vasilqactl rmeelawdla mssvvlfetr nyyddwravs ekaleanrna
      721 gnirgeaamc yelasvemfq qrfdsatplf trafqlfdsv revhgraltl rnmaitdrvq
      781 gglrsamsrl dearntfrvv gdasaeahtl nqmsqielew gnpdaavrls leavriatal
      841 getrgaaqal nrlaaayvkq grfdaakqsy dgvlrivrsk gdtrgeayal mgigetlvas
      901 gqydeaesil adaleiaerv ddlfllakvh lalgtcsqql nqltrasqhl liarntfhei
      961 gsvwgelqas adisrlsaet cggrtlpgr
//
LOCUS       WP_457681956             401 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457681956
VERSION     WP_457681956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /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=41539
     Region          141..399
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mkddvpvrrr rrrgwcgaaa aamllpalls ppgaclpavm aalslvvals vwpvgrvsla
       61 raaagtavls laadtvsfgk aglallwlpf eavallvlle rvvrhvpgsr vglvggltga
      121 aavllplrft lhapqtgike svflaalafv paagatgvgl ylrsldrrra havalarreq
      181 rlevardlhd fvahevtgiv leaqaaqldg dggpgehral lhrieqaglr aldsmdrtva
      241 tlreadgrtw eeppptrlhg ladlpeligr faamtaaevt lsledevaga lsreaedtay
      301 rvvlealtnv rrhapragrv evcaarsadg avelsvadda gpgastgalp ralreqggrp
      361 gggtglagla ervgavggal eagpyaegwr vscrlpvaav r
//
LOCUS       WP_457681960             239 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457681960
VERSION     WP_457681960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..239
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=26220
     Region          67..222
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgkrdgekgg gqeatsavtr rralwigggg avaagtaafa grdvlaqwww rlpgndkprk
       61 agavdhrgaq wvaaspenyr radrpadygi drvvihvvqg syataldvfq dpdheagahy
      121 vvrkdghvaq lireldvafh agnrgyners igiehegfvd rpesftdamy assarltagi
      181 crrygfpadr ehlvghvevp gtdhtdpgph wdwdrylrlv raelrkpvqt gespparkt
//
LOCUS       WP_457681968             468 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457681968
VERSION     WP_457681968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..468
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51101
     Region          52..458
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(164,166..167,298..302,317,320..321,324,339,343,398)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 malsrsarrt srwlalatav asaatlaaap gaypgapgvg dsyfpglgng gfdalhydlg
       61 vsyhpgsgrl dgrtkltara tqnlsafdld lqkltvdtvr vngrrahfgr sgdeitvrpd
      121 fplrrgkkft vtvayhgvpk plsgpivfgs dygwmktkdg vfvacepnaa stwfpssdhp
      181 ddkatydiri dapkgltgvs ngrlissgea hgrayahwre nrpmatylat atigkfdvrt
      241 gttpggtpiy vatdptlptg kvdvygitae atdywskvfg pypfevtgai vddmpqagfs
      301 levqskpvys avrsestivh elahqwfgds vsvkrwkniw lnegfatyaq wlwaehrgtr
      361 sardtlrqqy adipagndfw kvkiadpqra tmfagavyvr gamtlqvlre rigdkaffel
      421 lpawtarhry gnaetsqfia laekisgqql ddlfdawlkt dsrpalpq
//
LOCUS       WP_457681970             232 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatase PAP2 family protein [Streptomyces nigrescens].
ACCESSION   WP_457681970
VERSION     WP_457681970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=23377
     Region          43..209
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(125,132,149..151,193,199,203)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mtaagpepgp aqghgtrprp gtaalltfaa vcaalfaata ltvslrngtp faaeqaavrw
       61 sgahqgepsr smagaltatg sgpvpylmav lagllagera rgrlravcca vavlaagqai
      121 ryglmellar prppagdwtg sasgyafpsg hattsvlaag ilawgiarra rpalartwca
      181 vlglwaagvg ltriylgvhw pgdvlggwfl aagllalall lepfalgrpg rs
//
LOCUS       WP_457681976             412 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Streptomyces nigrescens].
ACCESSION   WP_457681976
VERSION     WP_457681976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=43433
     Region          70..251
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          257..384
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvqpnsgvp arrrrwrhqg ggplavllaa mlllvtgcgg ddgddkkagk agggkdasqa
       61 avtiapkdga ddvatsgalk vtaqkgrlks vkvkdgkgne vdgkisgdga vwkpsghlga
      121 stkytvdaia vdgqgreaae hsgfttlvpk ntfigqyspe ngqrvgvgmp vsirftrgit
      181 dpaavedaik vsaepsvpie ghwfgndrld frpekywapg tkvtlklnln gvegrpgvyg
      241 tqakevsftv grsqvstvda kskkmtvvrd gktvktipit agapgtetyn gkmvisekhl
      301 vtrmngdtvg fggeydikdv phamrlstsg tfihgnywsg raafgtrnas hgcvglfdqr
      361 gggdgstpaa wffrnsvigd vvvvknshde tiqpdngfsd wnlswekwka aq
//
LOCUS       WP_457681974             259 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Streptomyces nigrescens].
ACCESSION   WP_457681974
VERSION     WP_457681974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27423
     Region          89..246
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mpvsasptrk laavgavial vvaviaigva igtsvegdrd tgradapeaa asagpqedpa
       61 qqkmfddlak rtsrradgdp laigkkdapv vlveyadyqc sfcgrftret qpglikkfvd
      121 ngtlriefrn ftvfgadser aaraswaagq qgkfwqlhda lysktrkgaa laedklvdla
      181 rtsgvddldk fradlksada eralkkdqde gyqlgvqstp sflvngrpva gaqpyevfaq
      241 aveqaaerag hgpaakgtk
//
LOCUS       WP_457681980             619 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681980
VERSION     WP_457681980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 619)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 619)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 619)
  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 619)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..619
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65790
     Region          19..610
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 madtaqtttr tdptdlaqrs avrsllrlwp farpvrarlf taafvavlas cvslviplvl
       61 kwlvdgpvae rdpggawlgg ayllllglae allfglrrwl varplagvea amrealyrhv
      121 qrlpvsfhdr wssgqllsrg ttdlqllrmf lafpltfllv ngvtilvggv lllaqrwslg
      181 lvllapvlpl mvlcsvfeak ygraarrtqd qlgdlttvve esvlgiriik gfgrhrsqad
      241 afrkltralr tselrkarll awiwgcnttl pelaigaalv lgtlqvadga lsagtlvafl
      301 stalalrwpv esigfllams neaatatdry fevldepavd aparaaaaaa atdtpaqdaa
      361 avdaparaap appglvfsgv qfrypdappd sppllrditl hirpgetmal vgatgsgktt
      421 ltalvprlyd ptagrisldg rdlatlgree vralvavafe eptlfsataa envlmggedv
      481 qesdfrrale vaqadgfvda lpeggatqvg eqglslsggq rqrlalarav vgrprflild
      541 dplsaldvht ealveaalrq vlatttalvv ahrpstvlla drvallsggr itavgthhal
      601 lrdhpeyatl msgegegar
//
LOCUS       WP_457681982             630 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681982
VERSION     WP_457681982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 630)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 630)
  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 630)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..630
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66998
     Region          54..625
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttttgrps dgpedhpgar prpaphppes gdpapdafaq dalpapkgas rsllasllap
       61 hrrrvgavav llllqqaavq agpllvayal dravpalrag dhgpllavav agvlcavlsg
      121 glqfgfiela arvsqdvlld lrgrifrhgq alsldfhery tsgrlisrvt tdveslrell
      181 deglqeliti vlstvyitvt lvwldwglgt aalasagpla llvrsfrrrs hqvysaksta
      241 maavivkfte tlngirpvqa frrerpndaa farlnhrher ingdtllema ryvvasrlva
      301 niavaaivlw gayrvatggl algvlaaavl ylrrlydpid rlgmflnsye saaaslqkia
      361 gllarrpgvp epavsaalpp vaggrpgrev tfrdvrfayr tggevlprfd ltlaagttva
      421 vvgatgagks tlakllarfy dptegqvlld gvdlrelsta vlrrgvvmvt qeaflfsgtv
      481 adnialgrpd atraqiegaa kaigahdfit alpdgydtdv rkrggrisag qrqlvgfara
      541 lladpavlll deatssldip geravqramd tvlegrtalv iahrlstvnv adrvlimadg
      601 rivedgppde liarrgrfaq lhqawrdsvg
//
LOCUS       WP_457681984             594 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681984
VERSION     WP_457681984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 594)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 594)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 594)
  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 594)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..594
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62382
     Region          12..565
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttargpgi pdhrgpgryv wwlvtsqrgr vaagasygsl wmvglmlppy vlsraidegl
       61 vpgrmpvltg wvavllgvgv anawlavmrh rtmtrirmda tfrtvrvlva htlrlgaalp
      121 hkttagevvt igigdvavis qtltmtgpgv gavlaygvva vlllsvspll atvvllgvpl
      181 lavlvgpllg rlqgaetryr erqsglaarl tdlvgglrvl nglggkevfa dryrrdsral
      241 rsegyrvgsv tswvqalgvg lptlflaavt wlaarmaaqg titvgelvav ygyaaalvvp
      301 vsffieggyd ltrglvaarr vvrflrlepd aadgpgdpag dapeaasalr dpasgvevvp
      361 glltalaaar paesaavvdr lgrfadsaat wgavrldeia lsqvrdrivv adneaelfag
      421 tlrevvggrr drteeaidsa vrtalaediv rglpdgldsa veaqgrnlsg gqrqrlrlvr
      481 alladpevll aveptsavda hteagiaarl hharagrttv vtstspllld radrvyflvd
      541 gravdvgshr qlldeqpgyr rlvsrgedgd gaddgtgprp agaaeapvtq edar
//
LOCUS       WP_457681986             618 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457681986
VERSION     WP_457681986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 618)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 618)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 618)
  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 618)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..618
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64216
     Region          62..615
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtataarpgr pedappdgva lpvagpaatr raalqlirrd grafalmlal nalaagagla
       61 gpwllgrivd tvragggvrt vdrlalvila cglaqlllar yaryvghrfg ertvarvreq
      121 yvdralalpa avveragtgd ltargtsdvt svartlrdav pevcvaaata lfllgavvvl
      181 dpllglcglg vlsgvfvvrw ylrrahgayl aegaatsala ellaataaga rtvealglqe
      241 rrtaaseeav ercrrtrtrt lflrsvllpv vdvayvlpva gvllaggalh grggislgvv
      301 iaaalylrql sdplatilfw aeqlqssgaa farveglgqa praprtvpap llprpspeas
      361 papatpvddr idvtgvhyay gdggrspaah rdvlhgvdlt vrpgerlalv gpsgagkstl
      421 grllagidap rrgsvtvgrv piaaldpavl rrqvvlvtqe hhvflgtlrd nlqiaapeae
      481 daalyaalaa vgadwaaelp agldtelgag ghrpdgsqsq qlalarvvla dphtvildea
      541 talldprtar hteralaavl kgrtviaiah rlhtahdadr vavmeegrlt elgshdelva
      601 argayaalwh swhsqgps
//
LOCUS       WP_457681987             522 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457681987
VERSION     WP_457681987.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 522)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..522
                     /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=56486
     Region          <3..474
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          164..382
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtpwkrpdag qlyarapglv lwllvcgppa lafgslahth lwataaafpl lgvcvllrrr
       61 rpltalalpi apslvisldl ftvaycaala vfgylagirm prarpalwff savaagglpl
      121 savvgrtvwp wfsllltlll nvmlpwllgr yrrqyaelar tgwqlaerme reqqavadrt
      181 rlrerariag dmhdslghdl alialragal evdprldadr qaaagelraa agtaterlre
      241 iigvlrtdde saprvpades verlvdrara sgmtvtleea ddtgartlpa mtghalhrvv
      301 qesltnaakh apgaavrvri graagqvrvt vantarpdep aadpvsggsg lvgldervrl
      361 aggtlragpa peggftvsar lptadgtpae plerpeptaa ereldraqrq vqrrlrqtvi
      421 vplallaalv vltstfhlvs pswtvlereh ydalrlgadr srmdsllpff aldappdgtp
      481 ppphgwtcey ysvrpgsdta yelcftdgdr lvkksvvhrr dr
//
LOCUS       WP_457681997             306 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457681997
VERSION     WP_457681997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33277
     Region          10..306
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtgvlartaa rartpgapsv gfwtrllrws plvpatvlll lflvgpigyc vliaftdtql
       61 tgqesasfvg lanfrrafgd pafrnavvlt lvftvlsslv gqntlglala glmrrasrpv
      121 rsltgamvit awvlpeivag fllytfferr gtlnallewl qlpaqnwlft lpimavsfan
      181 vwrgtafsml iysaalagip qevtesaevd gagglrrlwh itlpmirrsi gtnlmlntlq
      241 tlsvfgliwv mtrggpgnrs qtlpvfmydq aflksligyg tavalllllv galfsviylr
      301 llreev
//
LOCUS       WP_457681998             283 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457681998
VERSION     WP_457681998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 283)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30608
     Region          22..267
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mplprhrhhr hhrhrhrlaa dagllvaava favplvwlvl asldaeatlr vrlpesptlh
       61 nfsavltdei tftpmlnsll icggatlltv vcaalaaypl srfrsrlarp ylltvlfstc
      121 lpvtavmvpv yglfvqidli dtrygtalfl aaaqlpfaiw lmknfmdgvp kvleeaawtd
      181 gaswpqtllr vilplmgpgv avvaiytfim mwgnffapfm lllspeqlpa svsiftffgn
      241 ygaiafgela afsilystpv valyilvsgr lgggfalgga vkg
//
LOCUS       WP_457682003             310 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682003
VERSION     WP_457682003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33370
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdltavrtvv avadagqfqe aaatllitqq avskriaale kdlgvrlftr targarltid
       61 gqaflphare llrveeraaa svrpgsralr idvigrrlgp avllrdfhra hpgialdvvt
      121 tlfdadaala avrsgtidas fravtlparq lpdgvesarv fdepiqlltg paheyaaara
      181 vtpaqlaghr iwmpgviagt ewaayydela aefgltieat gpdfgtepll dtiadsasla
      241 tfvgaqtrlv wpadqdlrrv pvhdptpvyp hsliwrsdnp hpalttlrty lgatrpahrd
      301 dgtwtpawar
//
LOCUS       WP_457682006             422 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457682006
VERSION     WP_457682006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 422)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46614
     Region          19..405
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,91..92,99,103,110,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,85,87,90,92..93,175..176,189,238..239,242..243,
                     247,290,293..295,395)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mspssepvel ygpeykrnpy plyaelrerg pvhrvrfpsg vcawlvtgyd aahqaltdpr
       61 lgkhhsrgna awrarasimp epqhsqlqvh llhqdpprht alrrlitdaf apqrvealrp
      121 rfqvmadall dglpdsggtd lvelfaarfp fqvlaevigl peefadrfdr dwgkvvqpvg
      181 pedpgrpaye arlrglqqyi adlvchkrae rgedllsrlv aardadrlgq eeldsmvfql
      241 lvagqepvtn qittalvall rhparlaela arpellprav eellrhdsaf elttwrffae
      301 dtelhgtrip agdsvivsls aanrdsrqfp dadalhfdrt pnphlafghg ihfcpgatla
      361 rielqialgt llrrlpdlrl avpedelewt pavlargvgr lpvsygscpy agsgangpda
      421 ac
//
LOCUS       WP_457682011             616 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682011
VERSION     WP_457682011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..616
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66494
     Region          1..588
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
ORIGIN      
        1 mnhrpvsvai vgagsrglgv ferlvahclt qpapltvhli dpqpfgagfh lpaqpdhlll
       61 ntvcaqltaf adphmvdgpv pisgpslhew crrrdlrlad dgytvrpgag reiqpndflp
      121 rrllseyltw aageitdaap enltlvrhrt tavdihpgtp dtetvvladg tridadavfv
      181 tvghhslyrp aapapdprlv trpyplpeal dsigpgerva vlgmgltamd viatltlgrg
      241 gahttdehgm rylpsgqepl ivltnrsgmp srsrprlhpg rmrfaplalt tehldeirtr
      301 radrridfaa evlplveaem elayyrvllg remgdttdag lemarrcara ghktlldelr
      361 arfgtspvpg ilsagladrq wteysayrdw ftaevaadla eareglgvsp lkealevlrd
      421 hrdvlravid ppgvddasla affggfastv nrqvigpqld rsaellslid agivrlgpgp
      481 qpkivapagq gpwrlestcl aeplrievdh vvqahvtepg adrapgtllg tlvaagrvrt
      541 lahrggtvhg ldvtrqgqgi drtgtpqprl fflgphtegs syynhyvpsp gapsrallda
      601 eralstalpe lmtrkr
//
LOCUS       WP_457682007             802 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457682007
VERSION     WP_457682007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..802
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82165
     Region          21..781
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtpepgpgtp spdlapapah sttltvggmt caacvgrvek klgrldgvaa tvnlatgrat
       61 vnhpatvsvt dlittveaag ftaqlpepap eadpdpedrl sptdrpdaps sqdsqgspas
      121 qdaqddgara erhrllvttl lslpvlvlsm vpgwqfrdwq wlcfvlaapv avwgaapfha
      181 ralrglrhga atmdtlvslg vaasflwsay alffggagvp gmtmpfsllp tagdgaahly
      241 leaavgvplf vlagrrmear arrgtgaalr alaelaakdv avrtpegerr ipvsrlhvgd
      301 hflvrpgerv atdgtvvegs saldlslisg esrpveagpg tavvggavns ggllevrada
      361 igadtqlari trlvedaqtg ktkvqrlada vaavfvpavm tvsvsvlgfw lgagaepqaa
      421 itaavavlvv acpcalglat ptallaatgr gaqlgilvrg pealerlrri dtvvldktgt
      481 lttgrmsvaa ltprtgglda taalrlaatv eqgsehplar avtahaeerq pgqplppvad
      541 fsatpghgvr gtadgrrvev trpgdvtglp aplpdavhta eaaghtavlv tvdgtpeavl
      601 avgdalrpds yravdrlrrl glrpvlatgd raataravag hlaiteihae arpedkaalv
      661 ttlkeqggrv avvgdgvnda aalaladlgi amgsgtdaai gaadvtlvre dlqaiadavh
      721 larrtlgtir gnlvwafgyn litvplaavg llspmvaaat msassllvvg nslrlrawrp
      781 rgagtsarrp hspraqarwe tr
//
LOCUS       WP_457682021             390 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            nigrescens].
ACCESSION   WP_457682021
VERSION     WP_457682021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43521
     Region          27..381
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtttptepsp tapttpatva atsliatlag hhytdaeifr qeqekiferm wfcavrgadl
       61 ekpgafrtvr igresvlitr nragelrafl nicrhrgaql cteesgevrr nlqcpyhawt
      121 ydldgrlvaa pnlqkmpdld rterglvtvp lrewlgyawv cladeppsfe dtvigaaver
      181 lgdaasldry rteglalgkr ltydvranwk liienfmecy hcatihpelt dvlpefadgf
      241 aaqyyvghga afadeatgft vdgtegfgrl pgiedtqdrr yyaitvrpqv fvnlvpdhvi
      301 vhrmfpmapd rtvvecdwly lpeivdsgad vsksvelfhr vnaqdfdace rtqpamssra
      361 yrdggvlvps ehhigafhqw vtdclegkgg
//
LOCUS       WP_457682024             212 aa            linear   BCT 27-JAN-2026
DEFINITION  LutC/YkgG family protein [Streptomyces nigrescens].
ACCESSION   WP_457682024
VERSION     WP_457682024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22176
     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 mtatardtvl rrvrdaltls dgpevtvpra yrtgralpde erlalfvdrl vdyraqvrtc
       61 tagttaavla evlrahgarr tgvppgldpa wlagydgetv tdsadvpapr ldaldgvvta
      121 savscaetgt ifldgaaadq grraltlvpd lhvcvvnlss vrtgvpeava qltpehpitl
      181 isgpsatsdi elervegvhg prtlvvvirt da
//
LOCUS       WP_457682029             389 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682029
VERSION     WP_457682029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40202
     Region          25..380
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgrrrspapa apprngppvv nqlpertdav vigggvigss iacrlaeagv gtvllergal
       61 gsgssgttag vvrtyfpgkp lisslavrsl aayhalaert gidlglqrig llvlftedhq
      121 vqdfrhtqaa qqaagvdvel vtaaeaarln plvdertila aawspeayac dpaaivrgya
      181 taaqqagail rtetpvtgid pdgrvhtpag siradtvvca agpwagtvaa madvrlpvst
      241 ypvdmlltdt pssapsdplp mtmhpsslri rswgdrilvg mgrpapdetr qawlqrvshh
      301 lgtafpalag ngletgwsgd ldvspdgmaf igrdparpfl yaagfsgqgl cqapaageii
      361 rdlvldkesw tdtsglstar clsgsaetg
//
LOCUS       WP_457682032             519 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457682032
VERSION     WP_457682032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54678
     Region          29..484
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mseqslrqae rqqqqgaaqd aaqrqpgghv dagdagyqks ltsrhinmia iggaigtglf
       61 lgaggrlada gpslavayal cglfaflvvr algelvlhrp ssgafvsyar eflgekgafv
      121 agwmyflnwa ttgiaditav atythywgmf sevpqwvial ialaivlavn lisvkifgel
      181 efwfaivkvg alvvfmligi fllatqhpva ghspgpslis dngglfptgt lamllviqgv
      241 vfayasvelv gvtagetaep ekimpkains imwrvavfyv gsvvllamll pwsaysages
      301 pfvtvlsnvg vpaaggvmnl vvltaamssl nsglystgri lrsmamsgsa prftgvmsrs
      361 qvpyggillt sgvcvlgvgl nyvvpseafe ivlnfaaigi lstwamimlc hllfwrkara
      421 geltrpsyrl pgspwteivt laflafvlvl mwadggagrt tvlslpviva alvggwflvr
      481 grvgtlrdaa aarasgehpd talptqrtdt hhstesten
//
LOCUS       WP_457682036             586 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682036
VERSION     WP_457682036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
REFERENCE   7  (residues 1 to 586)
  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   8  (residues 1 to 586)
  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   9  (residues 1 to 586)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20761992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..586
                     /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=62300
     Region          39..174
                     /region_name="sCache_3_2"
                     /note="Single cache domain 3; pfam17203"
                     /db_xref="CDD:435783"
     Region          197..537
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mrirwprrvf aqvltaqval ttgvmvlats lflaplstel ddqamrrals iaqttaadpd
       61 larklvttep dahgpvqaga erirtatgal yivvmdtrgv rwshthpaei grhvstdpgr
      121 alagrqvrqi dtgtlgrsar akvplrddrg rivgavsvgi aydsvqsgll gtipgllrya
      181 gaalavgvla aivlsrrlrr rthgvaftdi salldeream lhgiregvva fdrrgrirlv
      241 ndeagrllgl daqaagrpld evlppgrttd vlagrvagtd lltvsggrvl vanrmptqdg
      301 gavvtlrdrt elellgreld stqglldalr aqdhehanql htlrgllelg ryekavefvt
      361 evasaqrasa eeiaervpdp llsallvgka aiaaergvsl rvspstllpd tvvdprdlvt
      421 vlgnlidnal daaaerrrgd pfvevelrae hstavlrvsd tgpgvppelr drifaegwst
      481 kaarplpgeg sptgpvafhr grgiglalvr rlaeryggma rvtaraggga vftvvlpeal
      541 apedgspgrr htaageaavt gaprrperpe rtesrkrrpm gsgasq
//
LOCUS       WP_457682041             309 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682041
VERSION     WP_457682041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32328
     Region          2..269
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mkvlviggsg flgtelvrqa taagwetaat yhsrpgsvpg aswypldlra pghidellat
       61 vapdavinvt sgesdwavta dgsirvamaa trrgcrlvhv ssdavfsgsr vhydesclpd
      121 pvtpygaaka aaetavrlla paaavartsl iigdggsvhe rlvhalaagt rdgvlftddi
      181 rcpvhvadla salrelalsd rpgmchlaga dalsrhelga liarrdglda trlpagrrad
      241 srmpgaldvr ldsratqrhv rtrlrgaref lhvrysarrn edpnempctp ppadscgpgs
      301 sasqamage
//
LOCUS       WP_457682049             525 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682049
VERSION     WP_457682049.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..525
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=58795
     Region          6..421
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 maftpkragi ycrlsyapdg slekverqea dcrelatrld wpvsdqhvfp dnsrsawqrn
       61 rkrpqwdrml taieageida iiiyhgdrli rqpydlekli giaeskgiri aspsgtrdld
      121 spddrfilri eaaqacresd ntsrrvrral earaqrgltq vggkrpfgfg vqigtrmkid
      181 ratgetievp vydtsqhepr eakygasaad rllagqsqgg vlrwlaeegv tttegnpfts
      241 kslrnvllsp rfaglveyrg vlyeaawpav isretqealk miyrssaeah pypgrerkyl
      301 ltgsaecykc hiptveagtc qvgdgkcqap hatvqtkptg grnrkdsriy fcpvckgvgr
      361 nmehldayvs gavlrllndp rfleelhaqs ddnapsirae italerrkre treqlenlad
      421 lpevdptlva kslasfdrki telrnqlaat srqrllfrma gitreqwene pvdvrtstvr
      481 alfrvvilpt tkrgpgfdps svrmerrrlt dsldadagqg rahla
//
LOCUS       WP_457682054             101 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682054
VERSION     WP_457682054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..101
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10524
     Region          18..74
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mvdldpapry glvdadllrr lmartgtgcs lsvrqlaaas gvshgtienl lqgriktarp
       61 dvahkicrai gvdllilwap tgravppagy geasshlrla s
//
LOCUS       WP_457682055             353 aa            linear   BCT 27-JAN-2026
DEFINITION  YqaJ viral recombinase family nuclease [Streptomyces nigrescens].
ACCESSION   WP_457682055
VERSION     WP_457682055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Hao,Z., Lu,D., Li,X., Raheem,A., Zhao,G., Dawood,A.S., Chen,Y.,
            Chen,X., Hu,C., Chen,J., Zhang,L., Zhu,X. and Guo,A.
  TITLE     Novel Nuclease MbovP701 with a Yqaj Domain Is Interrelated with the
            Growth of Mycoplasma bovis
  JOURNAL   Microorganisms 12 (12) (2024)
   PUBMED   39770711
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Liu,Q., Li,R., Shi,H., Yang,R., Shen,Q., Cui,Q., Wang,X., Li,A.,
            Zhang,Y. and Fu,J.
  TITLE     A recombineering system for Bacillus subtilis based on the native
            phage recombinase pair YqaJ/YqaK
  JOURNAL   Eng Microbiol 3 (3), 100099 (2023)
   PUBMED   39628932
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="YqaJ viral recombinase family nuclease"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38451
     Region          24..350
                     /region_name="COG5377"
                     /note="Phage-related protein, predicted endonuclease
                     [Mobilome: prophages, transposons]"
                     /db_xref="CDD:444142"
ORIGIN      
        1 mtlaseppra aaptavlvap aglehtqwla arrqgiggsd iaavlgmsky tspielyldk
       61 vgelgdvprs pelveaafwg hqheptvaev faertglgvv egpgmlahid rrwmlanvdr
      121 yviepgertp sslleiktrs afqlaewllg vpdgpalqth wylavtgyah ahvaallggn
      181 rllihriehd dgliehlvel vgrfwqnvld ripppadgse atrellahly dvapesvtva
      241 dpatvlplle qraaikareq qvadelrlve nqlktaagea evvkaageta ftwkqngtfa
      301 akkfadahpg laakythqvd aldtkrlaae hpdlfrkfra rrlvvptnke nnv
//
LOCUS       WP_457682096             143 aa            linear   BCT 27-JAN-2026
DEFINITION  minor capsid protein [Streptomyces nigrescens].
ACCESSION   WP_457682096
VERSION     WP_457682096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10577426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="minor capsid protein"
                     /calculated_mol_wt=15342
     Region          14..135
                     /region_name="Minor_capsid_3"
                     /note="Bacteriophage minor capsid protein; pfam12691"
                     /db_xref="CDD:432722"
ORIGIN      
        1 maepldylda lasyldersl ltydptgvcg dtfvetlppa pdeavclsly gagavdarng
       61 wderslqvrv rgtadprpsr rraealysal hglarcelpg giwlvlavav atpapmgsda
      121 ngrhehvtny rltieaptsy rds
//
LOCUS       WP_457682101             787 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein [Streptomyces nigrescens].
ACCESSION   WP_457682101
VERSION     WP_457682101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Plisson,C., White,H.E., Auzat,I., Zafarani,A., Sao-Jose,C.,
            Lhuillier,S., Tavares,P. and Orlova,E.V.
  TITLE     Structure of bacteriophage SPP1 tail reveals trigger for DNA
            ejection
  JOURNAL   EMBO J 26 (15), 3720-3728 (2007)
   PUBMED   17611601
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..787
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=77966
     Region          86..713
                     /region_name="COG5412"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444167"
ORIGIN      
        1 malsigelvg tidldasgar qgvaqadral qglqrsadgr lrdvrgrfvs asaalgaavg
       61 ngiaagagqa aaaagelgna vadgvsagad qarasasglg aqignaiggg aerarsalsa
      121 lgpalgvlrt stlalsggal aaggalavip alfagigika asssqevkda fsglkdhvts
      181 qvqgmvgpik tqlvgiagda rstfdkiaps lksafaavap qirsvaqgvl glveklapal
      241 artasaatpv iqaisgglik lgsglagffd glaagaqgaa qgfsglfagi gqllpvlgkl
      301 lgqlaqaggp llstvattvs qlasqllsal gpaltalagp lrilvqtvgv alrpvlaalg
      361 pvlkqaavav gelvraaapl lvtagklaas llpaltpvlr vvgsifrqla pvvrqlastl
      421 qaalapvlaq lpglirpfat ilqslastvl silgqqikal spaltslgks fgqilvaaqp
      481 llgalaslin sglralmpil tpliglagkl aailakvlat qitlivipal kiltsllrgd
      541 fsgawrqtkt lvanvgaflr vlfiklgiwv aagiakavaw iktlpgrams algplagrlf
      601 taasnafqrm nlaiiakanq alawlrglpg rmvsalgdlg sllvsaggdv vrglwrgiqs
      661 mgawlrstlt swaknlipgp iakalgiasp srvmardvgr wipagvaagi tsgqgavega
      721 mrrlvpvpsi psmaapgtag apygraagss pygnrsgall hvenwhagsa tpdqtaaala
      781 wkmkarg
//
LOCUS       WP_457682124              92 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682124
VERSION     WP_457682124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 92)
  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 92)
  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 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..92
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=9812
     Region          12..>88
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 meygpddqve rdapaspfqq lagilrarvk rgdwkpnrai psenalagey glsrptvrra
       61 iaaladeglv yavsgrgtyv aeqktekpas ge
//
LOCUS       WP_457682129             242 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682129
VERSION     WP_457682129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25974
     Region          61..220
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mrsareqqyg keadagepas greatvtaeg lpewldpvaq vaatieppql srflppesgg
       61 rqsavlilfg hgprgpelll meragtlrsh agqpsfpgga ldpedgdpeg sgpvraalre
      121 aqeetgldps gvqvfavlpr lyipvsrfvv tpvlgwwrrp spvgavdqae tarvftvpva
      181 dltnpahrvt trhpsghigp aflvenalvw gftagvidri lhyagweipw drdkavpldw
      241 rs
//
LOCUS       WP_457682135             732 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682135
VERSION     WP_457682135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..732
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=77984
     Region          52..676
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mpkkrdgggl sktqqaakfl gvsvlagavl aglalpaaga lgltakgsve gfddipanlk
       61 tpplsqrtri ldakggeiak vysrdrtvvg lkdmspyirq aivaiedarf yehgaidlkg
      121 ilravnknaq sggvsegast ltqqyvknvf veeagdnadk vaqatqqtlg rkvkelkyai
      181 qvekelgkrk ilqnylnitf fgqqaygvea aaqryfskha kdlnleesal lagivqsptr
      241 ydpvnapqea tkrrntvlqr madlkdvtqa qadaaakkpi klavsrpkng citatdgagf
      301 fcdyirkvfl ndkhfgksrk vrlqrwdegg mtirttldpq sqksvqaslk dhvyeddpva
      361 gaativepgt gkilgmgqsr pygfrenqtv inlsvdhdmg ggagyqpgst fkpviaaaal
      421 eqgtnpeqey pspyrmpyps pvqtcdgewq gtdmtqnenk eevgpyamke ataksvntyf
      481 vqlisdigic pavkmaqkmg ieradgkplq qvpsmtlgvq emspltmaag yaafanggey
      541 cspvaiesit darsralkvp qtscrsamsk rtadtintll kgvvedgtgk eaglqgrdsa
      601 gktgtsdsry aawfvgytpn aagavwvgdp mhkrkmydis iggvphdkvy gadtpgpiwr
      661 damagaladr papelptvpi adpakdrghg deggkgrgkh kpgrghggdn kpgggwsipg
      721 fpdilgggng gw
//
LOCUS       WP_457682139             301 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682139
VERSION     WP_457682139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30661
     Region          87..296
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 malviallca gaalrsgggr pedvrrrara lfggrgeavp pggwraclrg eevrkwcagr
       61 lvegeagrrw svgrrwdvgr evwclpaglv lgvlggsvvp viasmgavyl vrrwlvtrga
      121 grvrdrraaa viglcaavag elragrqpaq allavgapgl gaegsavlaa aryggdvpra
      181 lrvaarqpga agltgmaacw qvaveggagl asgleriaag lrtqrdqrde lraqlagpra
      241 tvlmlallpa agllmgsalg adplrvllht pagwgclvvg gllewggvaw tarivaaaeg
      301 a
//
LOCUS       WP_457682142             484 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682142
VERSION     WP_457682142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48687
     Region          48..451
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(55..56,59..60,63,95,145..146,148..150,153,174,
                     177..178,181,304,307..308,311..313,316,344,348,401..402,
                     406,410,426,429..430,433..434,437)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mitekaapha taheagtatq gqgqgedqaq apasppgrsr ggvqllvlal gfvmasldtg
       61 imnvaandlr arlgltmsgl twvvdgyvla faallllags lakrfgarri ylvglavfta
      121 asllgavapn gavlvaarfv qgvgaalfmp sslsllmhaf peparrakil giwsaivsts
      181 vglaptvggl lvgtlgwrsi flvnlpigla gllltrrvia avpargsalg gsghvlglla
      241 lgalsyalie gpdrgwsapv vlgafavaav alagflvrer avrapilpvs lfadrsfaaa
      301 navgflfnfa fygalfvlgl flqtargasp vtaglqmlpa vlvlpfgnml yarfgprign
      361 rtaltaslal saagyvllfl ilapglpywa lavvlaltni gggvsspalt gvlmaaagre
      421 htdigsatln anrqigslvg iagmgavltg agdgyqgaaf afaltagala vaavvgrmgi
      481 rtra
//
LOCUS       WP_457682146             334 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457682146
VERSION     WP_457682146.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  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 334)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=36095
     Region          2..310
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(21,209..212,215,265,283..287,290,293..294)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(51,56,85,129)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mkvrqlgthg ptvsplglgc mgmstsygvp ddaeslrtld ravelgvtll dtadaygrga
       61 neeflgrwlr srtgaqrdel vlatkfglrh dtatgrvnev dtsaawvrea chaslrrlgt
      121 dhidlyymhr rdpavpieet vgamaglvad gavrhlglse ispqtlrrah avhpisavql
      181 eyslftrevv egemlatcre lgigivaysp lgrgmltgal aarddltaed arrrwprfae
      241 enidrnlrlv qavrttaesf gctpaqavla wllaqgediv pipgtkrrsy ldenaaaagi
      301 tltpeqtdql raavpadava geryplaale rlgh
//
LOCUS       WP_457682148             274 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682148
VERSION     WP_457682148.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30819
     Region          16..69
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          90..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mqpankpkri tswhvigaql shfrraarit qpalaervgl hedtigsieq grrplkldla
       61 etldelldtk galavavakv pereklpafv qdlveheeea ltllsyqnqv vpgllqtesy
      121 vratfdslyp pldeeqaeew vsgrisrqkl lerktprpml nfileeavlh rpigsqellr
      181 aqlrhlrsca elpflglqim ptarcthaal dgplvllekp dheylayiea qrisflvddp
      241 dqvsvyqqvy gmlrsqaltp eetksllddl lges
//
LOCUS       WP_457682150             141 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682150
VERSION     WP_457682150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..141
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15593
     Region          21..133
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mhkeiqtlca rtvryrrerr svplarefar haladwgleg raddvllcvs elatnallhg
       61 vppgreyrlc lslyedgllr aevhdsggge prvpvrgaae eecgrglllv saladkwgvg
      121 erhpgkvvwc ewwpefgggp r
//
LOCUS       WP_457682155             743 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682155
VERSION     WP_457682155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..743
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77784
     Region          8..712
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mtalarwclr rrivvivlwl aafagvavaa gvtgaaysnn yevpgtesgq asarmakafp
       61 ersgdsdtlv whtdsgtvrs aavkktmrht lekiaalpgv sevespygrh adgtgarqis
      121 kdghtayasv lfdrrtddld vdqvqkvvdt aqtasrpglq velggagial teapraqlpe
      181 iiglcaaavv lflafgslaa tflpiitala avgtasagit llshamtvad fapmlgmlig
      241 lgvgidyalf ivtrhrkglr eglpvdeaat ravavsgrav vfagatvcia llgmlilrls
      301 flngvalaas ltvvltvaaa vtllpallgl igmralsrre rrrlaehgpr perttgiaar
      361 wsgfverhpk llgtvaaavm lalalpafgl hlgtsdqgnn patsttrkay dllagdgrgs
      421 gfgpgfngpl tlvgtldgak driafdalpd rlrdtpgvar vsrpvfdggh stgvitvvpt
      481 sspqsrqtsd lverlrtevl peaggaatlr vqvggitasy ddfaslivgk lplfigvvia
      541 lgsvllllaf rsigiplkaa lmnvaavass fgivvavfqw gwgsellglg sagpiepflp
      601 vimvsvlfgl smdyqvflvs rmyeewqlth nnrravrvgl aetsrvinsa avimiavfga
      661 fvlsgdriia mfgiglaaav aldafvlrtl lvpalmhllg ganwwlpswl drwlprisie
      721 pppepgavrl pgpqdgekpl vra
//
LOCUS       WP_457682157            1051 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682157
VERSION     WP_457682157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1051)
  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 1051)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Rosinski,J.A. 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 1051)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1051
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=113331
     Region          <8..943
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          985..1045
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mlssvetrsv spvfvgraae lavlgdaldr iaasgepqal liggeagvgk trlieefgel
       61 arargalval ggcieigseg lpfapfsail htlnwhlrde laaavagqeg elsrilpelg
      121 etpgeahdee igrarlfelt arllerlaah rtlvlvvedl hwadrstrel layllkalhd
      181 anvllvatyr sddihrrhpl rpflaeidrm rtvrrvelar fnreevrsqi agingsepee
      241 dtvdrvykrs egnaffveel argladgclh glsdplrdll lvrvealped aqrvvrtaae
      301 ggstvehell aavcrmpedd liealraavg sntlvptqdg tgyrfrhala reavvddllp
      361 gertrlnrry aealeanpsl vrtevcaarl asywykahda akalpavlaa svqarrrhay
      421 aeqlrlldra lelwddapke vrqgvrpvdy aeaypacgcd dgdalrfldl laeiavaarl
      481 sgdnerafti tkralrslrd endpppssqh gssrgdplrk awflvqrsrl cqstgrgngw
      541 adlgaaqelv rglppssvha evmaavaswa vlhepgpdtl ataeravela qlvgdkeael
      601 nsrltlaglr vdsgeveegl adfrtsldra vcrgyfavia rghvnlpsal egvgrsreav
      661 evtergvelt tryglkdsts wvlgnraesl qslgrwkeag ravadarrla qshraialaa
      721 srridlalne gdlaeaerel avaqehygth dpqpqhaivm aqhalrvaar qgrlldarsi
      781 lqqaldagfp pgthryawpl lwaattaead arglpaaepg raailarird aakrlpqlsp
      841 vwsayglavd aelrraegre tpdawagava afeplerphe laracyrwae sllhgserat
      901 aglhgrtpre aavllltqah taavtmgarp ladelellaq rariplpglt padaagtagt
      961 pagngraaae apapsdtapa aslgltprer dvlrlvadgr snrqiadalf ispktasvhv
     1021 snilaklgvs grgeagavah rlrlfgeptp g
//
LOCUS       WP_457682165             211 aa            linear   BCT 27-JAN-2026
DEFINITION  PRC-barrel domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682165
VERSION     WP_457682165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  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..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /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=21952
     Region          11..>58
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnaplgdapq sltglhvvda dgakvgtvqq vyrddatnep ewitvrtglf gmketfipla
       61 garrtgdelh vphakatikn apridanghl dpseeeelyr hygmtrpgma apdaagptsr
      121 pgpratgdtg pptptggern kliegpmaga gagagtragp qagdtgdtar gkeqmpetga
      181 eerergrhpg erekgrddgt gggregpdrp r
//
LOCUS       WP_457682168             455 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682168
VERSION     WP_457682168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..455
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46926
     Region          <326..455
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrgdyqqlvd eisaalgapa tledrdfgli afgahegddd evmdpvrtrs ilqrrssaav
       61 rawfeafgia raktalripp dpaagvfkgr iclpvrhrgi vhgyvwlldd ghltdlelgs
      121 rgappdpria qametaarig alladearag selgdllrel laappdgqpa aaaalrdalr
      181 dslrftpgap ltlvavvpwd tsdtdaaplp slpgllaaca lpagggpadg paagadepep
      241 aarpgsgrng ragsavlphs aapvpalaal vrlrasgasa pahtvaehll rsprasagpa
      301 egraprggar ggsghppppr pgaagiglgt reltdlpatw realdaaraa haeprlgpit
      361 qwdaigpyrm ltalpgtapd paigpllapa haelartaev fldcagqasr tahalgihrq
      421 tlyyrlgrve kltgldlddg ehrlllhmal kaarl
//
LOCUS       WP_457682170             157 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457682170
VERSION     WP_457682170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  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 157)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16919
     Region          <2..146
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mhgqianrlr ravdrhldeg ewaayqdinv vhdrkvwipd cfiapedsea hvtddgigik
       61 asavhlivev lspghdgter drepkrraya gagipvyvli ddydghgtvt vlaaprpdea
      121 vytdvhrvay gidviipegp akgfvigeai tgparga
//
LOCUS       WP_457682182             388 aa            linear   BCT 27-JAN-2026
DEFINITION  LOG family protein [Streptomyces nigrescens].
ACCESSION   WP_457682182
VERSION     WP_457682182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41425
     Region          168..381
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mqsnsqpsas rrththhdhd drddreiesl eefdqvvasg slaghrvqsv dltdrtfall
       61 sadttesvfl gcvmepdaaa kiraggalvf ppvpglpfdp yrgglygpde lfdglagtgf
      121 datpdartyr wyqdtksdgd ifasmlrsih ddavsdalde hlagtqvvgv mgghalergs
      181 aayagaarlg rrltrdgltv atgggpgame aanlgayaap fedemldsal ellaktphft
      241 psvtdwaraa feirhsrpgg gasvgiptwf ygheppnafa shiakyfvna vredgllars
      301 tagvvflpga agtvqeifdn atpnyyqsrg eptpmvlvnr ahwteklptw pllqalaadr
      361 pmatrialvd svdeapdala rlrtqtps
//
LOCUS       WP_457682193             494 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457682193
VERSION     WP_457682193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..494
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51755
     Region          4..469
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mgttsstsap apegavetrg iepvpdnerq grvrelfptw vaanisvlll tmgaslvvnn
       61 glnfwqvllv aaiaaavafg mvgvlsvsgk wggapgamls raafgvrgny fpgailwvar
      121 fgwetinavt gayavltvlh lllgvesnnv lvvvtllafv avtylvsglg rkalnvcnky
      181 stylfglfsi mvlvylvatm dwdavfakka gttamviagi gtiaaggisw vptgpdfary
      241 lphsasgkki vgatvsgaal vllpmvlmgg vmavsspkla gqntdpmsfl gsilpswlav
      301 pylitalvgm vlinslsmys agftaqtmgv klpralavsi navislvggl fmmlvakdfi
      361 gqfiafltll avsfsawigv ygidmarrrk lavrydadsl mntdrtsryw yvggfcwqam
      421 tawgvalvag lcftkvqwft gplattwige nglgwaatia iaalvfavlp spkettpaag
      481 tdeaaevrqp vevg
//
LOCUS       WP_457682192             407 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682192
VERSION     WP_457682192.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=42242
     Region          1..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 midvlvlggg faglwsaaaa trllraqgsa rsvalltphp dlvlrprlyq adparmrvpl
       61 drvlgpagvr riaatatavd tarrrvtalt sdgsrtevay rslvlatgsa vvrpelpgaa
      121 llhdidtlpa avrleehlrg lpeapagpgr wtavvagagf tgleiatelv grlraqaapy
      181 gaadevrvvl veraavvgag lgaaarpvit raldtlgier rlgttvtgld arsvhladgs
      241 tvpartavwt agmrastlta qipaprdalg rlavdrglrv rgieglyaag dtaaalaeed
      301 hpvlqscqha iplgkvaghn aaaallglpp vdfapdpyrt cldlgeagav atagwnrtlr
      361 egpegfakdl krainetwis ppvddpqell rradhrvgtr qeaapsa
//
LOCUS       WP_457682195             327 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457682195
VERSION     WP_457682195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35537
     Region          33..326
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mmsvlrinlv dpaptpatls aryraavema afaddrgftm vqteehhatt ngwmpspltf
       61 agavfgatrr igvtvsalit plhdplrlae dlasldllgg grlvtvaglg yrpeeyaahg
      121 kdwrgrgplq devlqtllsa wtgepftyqg rtvqvtprpy tqphplllig gssraaarra
      181 arlglpffps ahlpaleayy heqraafgtd gwvmqppert allhlaedpd rawaeygghl
      241 lhearmyasw qsagsrsavr ssaqdvgalr eegvyrivtp declrlarrt gdggalilhp
      301 lcggipvdeg wrslhlfaeq vlprlkg
//
LOCUS       WP_457682197            1293 aa            linear   BCT 27-JAN-2026
DEFINITION  chromosome segregation SMC family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682197
VERSION     WP_457682197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1293)
  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 1293)
  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 1293)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1293
                     /product="chromosome segregation SMC family protein"
                     /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=137422
     Region          1..1292
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mhlksltlrg fksfasattl rfepgitcvv gpngsgksnv vdalswvmge qgakslrggk
       61 medvifagtt grlplgraev sltidnsdga lpieyaevtl trimfrnggs eyqingdtcr
      121 lldiqellsd sgigremhvi vgqgqldsvl hadpmgrraf ieeaagvlkh rkrkekalrk
      181 leamkanlar vqdltdelrr qlkplgrqaa varraaviqa dlrdarlrll addlvtlrra
      241 leaeiadeaa lkerkqaaed rlrtaqqrea aleeevrtlt prvqraqqtw yelsqlaerv
      301 rgtislaear vksataappe erhgrdpedm ereaarireq eaeltaalea asraledtve
      361 hraglerqla deerrlrdva raiadrregl arlsgqvtaa rgraasaqae igrlaearda
      421 arrradtaqe eyeqlkaevd gldaddeeia erheaarrel aetetaltaa realtaaere
      481 raataarhda lalglrrkdg tgallaaadr ltgllgpaae lltvtpgfei pvaaalgaaa
      541 davavtgpat aaeairllrk edagraamvl ggsggrsgtg rvpaparave ategggaeea
      601 vgaveaagvs agsevvgavr aagvsagsqa agavgavgaa gsqgagevcg tgggegfaga
      661 aegavvgvra gaagapgvpg paghrvpgpr aepvpaaelv rgpgdltaav arllrdvvvv
      721 gtledaeelv aarpelmavt gagdllgahf aqggsagaps llevqasvde aaaeleelaa
      781 rceelaqaqr aaaqrrtaga elveelaerr raadrekskv agdlgrlggq araaageaer
      841 cdaaaakaee allrateeae elaerlavaq eepgvgdeep dtsvrdrlaa dganarqtem
      901 earlqarthe ervkalagra dsldrgarae reararaerr rarlrheaav agavaagarq
      961 llahvevsav raeeergaae rakagreqal vaernqgrel kseldkltds mhrgevlgae
     1021 krlrieqlet kaleelgvep aglmaeygpd qlvppsppae gevlpddpeh prnqpvpyvr
     1081 adqekrlkaa erayqqlgkv nplaleefaa leerhqflse qledlkktra dlmqvvkevd
     1141 erveqvftea yhdtarefeg vfarlfpgge grlvltdpdd mlstgvdvea rppgkkvkrl
     1201 sllsggersl tavallvsif karpspfyvm deveaalddt nlqrlirime elqessqliv
     1261 ithqkrtmev adalygvsmq gdgvskvisq rlh
//
LOCUS       WP_457682201             550 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682201
VERSION     WP_457682201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 550)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..550
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58645
     Region          2..541
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mavplaffal ffaypvvaiv grglkdggqw qlsrfgavls dpdvvhvlwf tvwqaaastg
       61 ltllialpga yvfarfdfpg kqllravvav pfvlptvvvg saflalvgrg gllddlwgvr
      121 ldtsvwaill ahvffnyavv vrtvgglwgq ldprqeeaar vlgagrfeaw rrvtlpalgp
      181 avaaaalmvf lftftsfgvv qilggptfst leveiyrqta dfldlptaav ltmiqfaavl
      241 gvlalhawtv rrresalrlv dasqtarrpr grgqwallwg tfaviavlll gplvvlvers
      301 fagpdgygav fyaslasaas adstfavapl dtlwnslayg aaatvialvv gglaaaaltl
      361 prlrrgpsgr apvvsrfvrg fdvllmlplg vsavtvgfgf litldeppld lraswwlvpl
      421 aqalvgvpfv vrtmlpvlra vdsrlreaaa vlgaspwrvw revdlpmvrr alliaagfaf
      481 avslgefgat vfiarpdqpt lpvavarllg ragelnygqa malstilmvv caaallvler
      541 lrpidrsgef
//
LOCUS       WP_457682203             278 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682203
VERSION     WP_457682203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 278)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28410
     Region          <27..183
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mdrvagraag raagraagra agraagverg evagraegva pvvravppae grswpvggag
       61 girptvvrgw epppapwtag hrgvdlgapa davvraaapg rvayagtvag rgvltlevsr
      121 sgrpplrtty epvrstvrkg qrvtagqpva elqhggpfhc repclhwglr rgktyldpls
      181 llppsmlggg psrllpifgv pvpagghtlp pppepsepta qasspapttt alaeavglaa
      241 vtiwalgrls sarsalseeg trrrwrgwgw rllgrggg
//
LOCUS       WP_457682214             412 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457682214
VERSION     WP_457682214.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 412)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45272
     Region          36..412
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(82,103,105..106,189..190,199..200,203,206..207,210,
                     242,245..246,249..251,254,297,299..302,326,402)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(104..105,112,116,123,168,171,246..247,250..251,
                     254..255,258,296..297,300..301,303,326,353..355,358..359,
                     361..363,366..367)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mttaeriere qetgpgvgrt pvavpaarat gcpfdpapal erahreesmt ratlwdgssc
       61 wlvtrhqdvr evlgdprfsa datrpgfpfl tagarqfasg npsfirqddp eharlrrmlt
      121 adfmvkkvea mrpevqriad dlldrmtegr haadlvaefa lplpslvicl llgvpygdhe
      181 ffqkhssvll slrstveevd laqkelqdyl rglaeskrre pddgivsrlv argelddaai
      241 asmgrlllva ghettanmta lstltllrnp dqlarlraep slikgaveel lryltivhng
      301 lpriadedvt igghtirage gvlcvlnvan rdeevfpgga aldvgrdarr hvafgfgvhq
      361 clgqplarve lqialetllr rlpglrldip fedvpfrhdm giygvhalpv aw
//
LOCUS       WP_457682212             492 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682212
VERSION     WP_457682212.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..492
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49729
     Region          35..430
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(42..43,46..47,50,82,132..133,135..137,140,160,
                     163..164,167,298,301..302,305..307,310,338,342,396..397,
                     401,405,421,424..425,428..429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtqtsptgtt grhtapvpps arqagaapwr altvvlvgaf mavldtfivl vaapaiqadl
       61 hsspadvqli lagyqltyal alitgarlgd rygrkrlflt gmalftlasv gcalapgsgt
      121 liaarlvqgl gaagmfpqvf aviqvlipea erpkafgalg avigiatmsg qlvgglliaa
      181 dlfgsswrpv fwvnvpvgvv tlllagrfvp esraprarrl dlpgavvltv alsllvvplv
      241 egraygwplw awlglaasvp afalfglver rvgagggapl vrlrlfgerp favgmtlvvl
      301 tyaginsffl ilsltlqdgl gldalgaglv ytplavaffa asliagrlar fgrrvlqlga
      361 llggvgflgt lllaaragaa ltawelapal vlvgsgngll vtpllnavlg nvgpeevgma
      421 sgvlstgqqi ggavgvavvg ilyygalgga ahhaigaygq alaaavalnv alsaaisall
      481 pllpdpaaar ra
//
LOCUS       WP_457682210             301 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682210
VERSION     WP_457682210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33030
     Region          10..88
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          107..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madqqrrrnl aeflrsrrer lspreagila gprrrtpglr reevaqlsgv svtwytwleq
       61 arditvsgqv ltslaralml nsverrhlfa lagvplperp pgrgpgpalq rlvdalephp
      121 aylldanwdl vgwnraeagl igdpgelepa ernllwlvfm dpamrellad wdgqardlva
      181 qfradsrqrs gdprfeqltg glreaseefr awweahdiae fgssrrtfsh prvgaltfdy
      241 vklaaldapg iklfacmpad aatteklpal qrcaaggesp daeaaeaadp gtagevtvsp
      301 v
//
LOCUS       WP_457682223             873 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682223
VERSION     WP_457682223.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 873)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 873)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 873)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..873
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..873
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89309
     Region          40..438
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(47..48,51..52,55,87,137..138,140..142,145,165,
                     168..169,172,300,303..304,307..309,312,340,344,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          558..>856
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 matttpagvr gghakhgggq hasdgapmth rqimealsgl llgmfvails stivsnalpe
       61 iihdldggqs aytwvvtasl lamtattplw gklsdlfskk llvqfalviy vagsvvagls
      121 qntgmliacr vvqgigvggl salaqivmaa misprergry sgylgatfav atvggpllgg
      181 vitdtdwlgw rwcfyvgvpf avialivlqk tlklpvvkre gvkvdwagaf fisaavslll
      241 vwvtlagdky dwmswqtaam vggavvlgai fvfvetkake piiplrlfrn ktitlaslas
      301 lfvgiamfag tvffsqyfql argesptmsg vltipmiggl fisstvsgqv itktgrwkaw
      361 lvsggvlvta glgllgtiry dteywhiaiy malmglgigm mmqnlvlatq nqvapedlgs
      421 assvvtffrs lggavgvsal gavlanrvdh yvkdgladlg pkaakaaaha gnsgggipdl
      481 dslpaplrtv mesayghgvg dvflyaapca llaflftlfi kevalktrgg laqssqdaav
      541 aatpaatpsa tpsatlseas seavvpaqae erepalvgaa pvapddeaht pswarpavat
      601 atqplaayas agggddtpag savhgfvrna eghpvprsav tlislsgrql gravaqangs
      661 yvlsapgags yvliaaadgh qpqastvvig dqphaydill sgtsglggqv rsaatgapvd
      721 gamvvvtdvr gevlatgktg aeghfafdel apgtftvavn apdhrpaalp veiggqgttr
      781 ieiellsgar vqgvvragah rrplpdarvt lvdaagnvva tsttgedgay aftdldagdy
      841 tviasgyppv atglavdarg vdgydvelah pgd
//
LOCUS       WP_457682225             256 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682225
VERSION     WP_457682225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28274
     Region          36..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          99..250
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maatdgrtgk rpnsvwlter pppkrkadqp aglgldkiva atvrlldaeg lakfsmrrla
       61 aelgvtamsv ywyvdtkddl lelaldsvmg emrlpdeadt erdwrdhlrs ladeyrtllt
      121 ghawvarllg tyinigphsi afsnasmrvm kesglslqqi tgglsavfqf vygfatiegl
      181 fndrcaeagl pvdeyfhqvm tavesrpefa etlenttkvm earggttvre mrdrdfafal
      241 dlqiagieam rarpgd
//
LOCUS       WP_457682227             519 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682227
VERSION     WP_457682227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52468
     Region          28..492
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,284,287..288,291..293,296,324,330,381..382,
                     386,390,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mspvasdatt tlqppgrtaa rwlilavicl aqltvildnt vlnvaipslt edlgastadv
       61 qwminayslv qsgllltagn sadrygrkkm lavglvlfgv aslgaalaqs pgqliaarag
      121 mgvggallvt ttlavvmqif ddderpkaig iwssvnslgf aagpliggvl ldhfwwgslf
      181 lvnlpvavva laailtlvpe sksragerpd lvgallsmig mvgvvfaiis gpvtgwlsgr
      241 vlvsaaiglv glavfalwel rvpypmldmh ffrnrrfiga vsggilvafg mggsmflltq
      301 hlqlvlgygp ldaglrmapl avtvillnft glsarllprl gtpgmivsgm sllaaglaai
      361 sllggdsygg mltglimmgv gvalamptma naimsaippa kagvgagvng tlmefgqglg
      421 vavlgavlns rfvallplaa agagslpaal artrtdaert avhdafaagi gtsqlvgaaa
      481 vflgglvaav llrraertgq dteapatpsa aepaaasae
//
LOCUS       WP_457682215             538 aa            linear   BCT 27-JAN-2026
DEFINITION  apolipoprotein N-acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457682215
VERSION     WP_457682215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Bork,P. and Koonin,E.V.
  TITLE     A new family of carbon-nitrogen hydrolases
  JOURNAL   Protein Sci 3 (8), 1344-1346 (1994)
   PUBMED   7987228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..538
                     /product="apolipoprotein N-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016410 - N-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58269
     Region          54..519
                     /region_name="Lnt"
                     /note="Apolipoprotein N-acyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0815"
                     /db_xref="CDD:440577"
ORIGIN      
        1 mlgtrerrre gegkgeargr gpergertar arpagrwlwg agtvllvlav hgnwhlasaa
       61 wlfpvfllry srlrparrgl lrvgyalgla qlvwltstgm vfvpsvlavf avlavvqtlp
      121 fvadrlvaar sgsawstlvy pvvlvcgeyl ftqladfgdy gvlgftqhgf lplvqlasvt
      181 gvygvsfvva wtasvahwaw grgfrwreir rgalvwagvl alvlgaggvr lvccapttdt
      241 vrvagisagr aaerateral rtagqelwrp rnlvradprr vraalapvad dlvaatdrea
      301 ragarivvwp etqagvladg qqrllgrvse iarkrqvyvn tafalytprp pyvrnvaalv
      361 tpegkvawty dkthptpmep mtpgkgavpv tgspygrlat vicydadfpg lmrqaadrdt
      421 alimvpandw agfeslhaqr avfrsveygy amvrqsvhgv atavdhqgri rgmadyftad
      481 rqtlvsempv rprtdtlysr tgdlfallca ggtllvvalg vrgrraragv pgagddrp
//
LOCUS       WP_457682233             575 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682233
VERSION     WP_457682233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 575)
  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 575)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..575
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO: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=59018
     Region          <191..500
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mttptpaatp agpiptprrr wslrtrlvvs avaliavvga vigtvtaial hsymqrqldg
       61 kvhefvvraq lprphepspv qggldfvamg gqplgtvgar vgtggtveag akldnpsgpl
      121 pdrlaeltra qlaalnkvpr dgrshtaelp glgsyrvesa qngslvlglp ldsvqktvgt
      181 lilieacvtv aglvaagmag samvgialrp lrrvaatatr vselplhqge valhvrvpas
      241 esdgrtevgq vgaalnrmlg hvgsalaarq esetrvrqfv adashelrtp lasirgyael
      301 trrgreqpgp etrhalgrie seaermtglv edllllarld sgrplayart dlsplvidav
      361 sdarvagagh rwrlelpeep avvygdagrl hqilvnllan arthtpegtt vtarvraaad
      421 aaagrggvvq leveddgpgi paallphvfe rfargdasrs raagstglgl aivqavvaah
      481 ggtvvvgsvp grtvftvtlp taaanstaaa tsavwdaagr kspvpgrkpp vtgrkspvtg
      541 realsvggea psaggealsv greapsadqa apsad
//
LOCUS       WP_457682245             738 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682245
VERSION     WP_457682245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..738
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=78108
     Region          22..730
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mrpaesrpke krpvtvrlav wsarhpwral agwlafvvlc lgvglamgth katgedyrvg
       61 eagraetlaa earldrepve qvlisarsgp ltraaaepav rdvtarmrkl pevarvappv
      121 rsadgsslrv avimkgaead addhvaplaa qtvavqrshp elrvaetgsp svsvgvdtqr
      181 gddlalseai tlpvtlltll avfgsalmva vplllalssi aaaiglsmvv shlqpdagvg
      241 tniilligma vgvdytlfyl krereerara ggrlgpealv elaaatsgra ivvsglaviv
      301 statlylatd vvfsslatst vivvlaavls sltalpallv kiaqradrra arraqrtgrr
      361 peprerpdgp grlwrallrp asehpagtlc vsvllmlala apalgmqlrv lnkdshsrei
      421 palqtydrlt tafpelrvqh qivvrapaae aaevasalrk lseraqsdpl yakgvtplvk
      481 tsrdrrtttm elstphkvss peavasldrl rtdhlpdtvg avpgaefavs gdvahdtdyl
      541 ahqdgklplv vgalllltfl mttlvfrsvv igligvalnl lsaaaafglv viffqhglas
      601 tlfgfdtaat saigsrvplf lfvilfglsm dyqifvvsri reaalcgvpt reavldgvga
      661 sakvvtsaav vmvtvfasfm flhlaemkqi gfslavavll dafvirvvil psaltllgra
      721 swwpsrtmrr aqsavpvp
//
LOCUS       WP_457682251              62 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682251
VERSION     WP_457682251.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..62
                     /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=7003
     Region          1..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtantsqllt vpevmaqlkf grskvydlir skrlisiteg rarripenal qdyirdriee
       61 aa
//
LOCUS       WP_457682249             383 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457682249
VERSION     WP_457682249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43056
     Region          73..373
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msqqrkrnpn gagtitkrkd gryqcavyvl qpdgtrarkf aygktwaecd akrrellakv
       61 dsgvpvptrs aklaewlpyw ldnvikpnrk rstyskyamh vrlylvpllg tkrletlgpr
      121 hvrvfladva rksspatake ahrvlrtalt aatreelvtr nvaslveapk vvsrettpws
      181 ldetlaflee arrdplyaaf vlaiamglrr gevlglrwsd vnldgcviri snqvqrigge
      241 lyqdttktgk irpvplplic laalrwhrlr qaheaekrgt eldpaglvft trsgrpiepr
      301 nlnrsfsrlt asaglrtirl hdarhgcatl ltaagvaprv lmeilghsqi smpmdvythv
      361 aqdtqreais hmdrllkrrl drd
//
LOCUS       WP_457682266             155 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682266
VERSION     WP_457682266.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 155)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..155
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16679
     Region          15..122
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mllymsnsaa qaqstplhsv svagvvvred gklltirrad ngawelpggv leleeppeag
       61 vrrevweetg ihvevdeltg vykntargiv alvfrckpvg geertssest avtwltpdev
      121 aesmsevyav rfldaldgag phvrshdgkr ltpar
//
LOCUS       WP_457682264             259 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682264
VERSION     WP_457682264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 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   4  (residues 1 to 259)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27752
     Region          10..258
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mgtavgggka vprylqiadd ilqqiragal kpgemvpses elverygvsg gtirkamvev
       61 rasglvetrh gkgsivkdrp pvrhrssdrf rrshrqggka aylaesaqsg atakvsvlyi
      121 gpmeapedva grlgvepgtq vlarrrlyfr ngtpvetass ylpwdvvkdi pelfaenpgg
      181 ggiyarledh ghefaefvet lqarsaskae aselalspga pvvhlvreal ttegrvvevc
      241 dtlmaadqfv fsyripatd
//
LOCUS       WP_457682283             251 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682283
VERSION     WP_457682283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27155
     Region          1..248
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpeqppylrt adelrrrvae hewtpgdrlp sraqiaeecg vgenvirraq ellisqgvle
       61 gragsgtyva aprqrvrvvr ssareqpdgs pfradmkavg klgdwesrte akvpapaeia
      121 srlgiaegdl cvrtvyefla dgkpvqlsts wepydltagt vvvlpeggph agagvvnrma
      181 eigitishav eqpeprqana eeasllgiqk ggfvthirrt yysdqgrpve tadivvpaal
      241 ceivyeipis r
//
LOCUS       WP_457682281             246 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682281
VERSION     WP_457682281.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26290
     Region          11..228
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mrsvtsrrhv iaddirnkia tgrikagacl pseaqlasry gvstatlrsa lsvlqgeglv
       61 ekihgkgnfv rhplrrityv ggghtlrtec saesalhvsv rttnlqahgq lacllgvsas
      121 spltefrclt hegksphsla riyvprdlsp tdvpaeshcc ksveaklael rpplaevrer
      181 vsarpptpee aatlrisstl svlaitrvaa drtgrvveaa llvipgdrad afftthhmtd
      241 ertsgg
//
LOCUS       WP_457682287             101 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces sp. 900105755].
ACCESSION   WP_457682287
VERSION     WP_457682287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..101
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10616
     Region          16..86
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mtvqqealag gealevwidq dlctgdgica qyapevfeld idglayvkga ddellqakga
       61 tvgvplpllt dvvdsarecp gecihvrrva dqvevygpda e
//
LOCUS       WP_457682291             242 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457682291
VERSION     WP_457682291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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 242)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26467
     Region          19..228
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mlsasptsga plprgsgqrl lvvdddprma ellettlsla gyevatagcg gealrayade
       61 ppdllvldvl lpdldgftic rrlvetgarl pvlfltards vedrvtgfam gaddyltkpf
      121 slpellarvh allrragrsa epgpllcfad ltvdersrrv rrgdrlials pteykllryl
      181 linadqvmsk eqimdhvwqh hfgegvvekl vsrlrakvdv hapalihtmr gfgyslrlpe
      241 gg
//
LOCUS       WP_457682299             487 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces nigrescens].
ACCESSION   WP_457682299
VERSION     WP_457682299.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=52475
     Region          11..486
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 masersaapa gaevlvasnr gpvsyaleeg gtltakrggg glvsglsaig sdaeavwvca
       61 algdgdreav rrtgggldpg dtggqrvrml dipaevytaa yngiansalw fvhhmlyqtp
      121 lepvfdaefr aqwasyesyn rafaqalaee aaegaavlvq dyhlalvpgm lrtlrpdvri
      181 ahfshtpwap peyfrmlpdd iarqllegml gadqlgfltr rwaeafaacc aavvggtgdt
      241 rigvyglgad agflrersqq edvaerlstl reqigtgpdg avrktvvrvd rtelsknivr
      301 gllayrqlla ehpswrervv hvafaypsrq dlavyreyta evgrvaeain seygtadwqp
      361 vvlhvkddfa rslaayrlad valvnpirdg mnlvakeipv vsdqgcalvl sreagaheel
      421 gqdaltvnpy dvsgtaralh ealtmdager sertarlaaa atalppaqwf lkqlralkev
      481 tpradar
//
LOCUS       WP_457682314             351 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682314
VERSION     WP_457682314.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37540
     Region          7..311
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtsgsavvig asgqigraav ralardgwev raasrhggrd aswpgevrsv avdreddtal
       61 agligegcdv lldcvaygaa hakqltalad rigsavvvst cavyaddrgr sfatmdepdg
      121 spvyplpvpe tqptvppgde dygtrkvale rallaqgdrl pvtllracav hgpysplpre
      181 lyfvkrvldg rrvrvlaygg ssrfhpvhvd nlaelvrlaa rrpgsrvlna adpqaptvae
      241 isaavdaamg apesevvrvd gappssdvgd tpwsvphplv ydmtaaerel gyravttyee
      301 slpatvawla dqvkgrdwwe lfprmagfyp deklfgyaae drwlaewggk r
//
LOCUS       WP_457682319             493 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457682319
VERSION     WP_457682319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..493
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51164
     Region          2..458
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mthrhgaaqp davahhtvde vperarhgct rdlftlgfgt hiaplalvtg amavqvfhqp
       61 lwsgvlavlv gqllggvfma phrapgpqsg ppqlirsrar sgslgalpgv vlaaalyvtf
      121 faahlvlagk slhvltpglp vgagillgaa gsallcligh rlihalnkva avvlglglva
      181 glalavthgl pgdfftrggf tfagwlaivs lsalwqpala pyaadrsral pgtvrttttf
      241 watyggaclg sllpflagaa vapacpgpdt gagiggaags fgpvllvlfl fsvlhhnaln
      301 lyravqatlt igqtlrthwq prprvrgavs alvlacgpal alglagdfvt rfadlvlvll
      361 aalvpwaain lvdfsllrhg sqdpdelcdp ddapyrrfdp valgsyvlgi avqipflagd
      421 lytgppaahf ggadlswlvg pavtaplyfl warsrlrrce ggavlgmreq aarildplrp
      481 lypedvrgfa dtr
//
LOCUS       WP_457682321             207 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682321
VERSION     WP_457682321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22551
     Region          3..195
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mtprrgdgpd eptfterarr eqlidatvdv istrgypats lsaiaeragl skaavlyhfs
       61 skdkltraal eqvmeqfsay vterlaraag prdaivayvr amigyqqanr rqvrviteml
      121 lddeggtrlk tpgshdthgr wqgladllte gqkagvlref dpqtvalaig gaidgviahw
      181 lahpeldlda aaaeleeftl naierrs
//
LOCUS       WP_457682323             438 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682323
VERSION     WP_457682323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44250
     Region          35..398
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(45..46,49..50,53,86,139..140,142..144,147,167,
                     170..171,174,252,255..256,259..261,264,292,296,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 myladgrpap ppsvspggrr dgrgrrvraa vpstvlvlga vslitdisse mvtavlplyl
       61 vaelglsplg fgvldgvyng vsalvrlvgg rlsdggggrg hkavaavgyg lsalckplll
      121 mvhtlpliga vlavdrtgkg lrtaprdami slaaepaarg rafgvhramd tagalcgplv
      181 afvllraaae gydavftvsf cvavlgvvvl llfvpgralp aaedtagrgp agprtpvral
      241 lrrpqvrrlt acavllgltt vsdsflylal qrrldlpagw fpllplgtaa aylslavpmg
      301 aladrigrrr lflaghlall gayglllapf gggaglvcgv lllhgafyaa tdgvlaaata
      361 davpedargs glavvqtgqt aarfvcslaf gaawtawgdh tavlaaavgl alaaalsarl
      421 lrpaapapap nspsehtp
//
LOCUS       WP_457682325             412 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682325
VERSION     WP_457682325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /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=43637
     Region          197..410
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpfslsavlr plfravtytr wlhlliasva gmltgflynk pffaggwltw lwmavlplpl
       61 lllaalipvv rrveglqaql lltpgphgle araasgiatt psgswsdrgr talwlllrle
      121 vgvalsalta qlpvlagafa masagrpthl kglpaieaph wwygllaplp lvllaavalg
      181 agsltaaaar lllgpsaaer ltelearter mlehnrlaqe lhdaighalt vtvlqagaar
      241 tagspefter alaaiedtgr ealadleral rllredapgp agrpaltdte rllesaraag
      301 adlraelsgp lerlpgpvsr egyrmvqeal tnvlrhagpv pvsvriaada dalelevrnp
      361 lpaaspapgs ahrgrglrgi reraallgge aetgpdggew rvrarlplrq lr
//
LOCUS       WP_457682341             186 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457682341
VERSION     WP_457682341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..186
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19620
     Region          20..157
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mhviqdeerg pmggpggrri vagvsgslgs ltalhraaae arvtgaelwa vlaweppgge
       61 iahrggpcpa pmavwrrmad erllraleda fgsagpempl rcvvirgkpg aallavadra
      121 ddllvvgaga rgrlrravwp svarycvara ccpvltvpps plqhafeavh rrnawklpld
      181 arelad
//
LOCUS       WP_457682352             432 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682352
VERSION     WP_457682352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43729
     Region          26..391
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(36..37,40..41,44,76,126,128..130,133,153,156..157,
                     160,233,236..237,240..242,245,273,277,331..332,336,340,
                     355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 metehipepp ageapgtrpg lgrgtlllms vaaglsvagn yfaqplldli grdlhlsast
       61 aalvvtvaqv gyglgllllv plgdllerrr lavtltaata vfltvtasap haallltgta
      121 ltgltsvaaq vvvpyaatla apaqrgrtvg tvmtglllgi llartaagll aelggwrtvy
      181 wvnaalmllm avllrlrlpa lrttaglryp allrstlalf gqepvlrwrg algaltfagf
      241 svlwtalafl msgpsygwqe saigllglvg aagslaasvg grladrglah rvtgaaafll
      301 lgswgllalg gsggswslaa llagvivldl aaqavhvsnq nlvyavrpea rnrlnsaymt
      361 syfvggavgs altsvvwgaa gwggvcvlga glaavvvalw avermrrras gggrtgpgqt
      421 aaaeapapsf ts
//
LOCUS       WP_457682354             294 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682354
VERSION     WP_457682354.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001217 - DNA-binding transcription
                     repressor activity [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31326
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..283
                     /region_name="PBP2_LTTR_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08436"
                     /db_xref="CDD:176127"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176127"
ORIGIN      
        1 melqqmryvv avaetggftr aaerchvvqs alshqiarle kelgarlfdr tsrsvrltaa
       61 geafvpvarq aleaaerara evaaatgevr grlavgaist vaavdlarel gafrtrcpqv
      121 rislqtamsd qlleqvrqgv ldvafvglvp aartvgvrek elsrgelvav vppghplavr
      181 ewttlsrmar etfvdftags aarrqredaf raagltseva yevttvefla klvraglgvg
      241 mvpeaiasel agldivrvrp apertervvw sglgpspaav aflsglgvdp ndrp
//
LOCUS       WP_457682360             838 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682360
VERSION     WP_457682360.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 838)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..838
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86374
     Region          1..838
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mfktalrnvl ahkarllmtv lavmlgvafv sgtlvftetv sqasqaqsrq dlrdvdvalh
       61 apsgngsgap vidqklldks arvpgaasat glisgftgia dkngalignp nssnggnyfp
      121 gadgkdaryp mrdgaaphgp hefvldarta deagykvgdt vrlsangpvh eqkltgiftt
      181 ddgavaaggs lalfdtptaq kllgapggfq eirikadpgt sqtalksave salpkgsvea
      241 ttgkqladdl gkmnakrasd mqtyllvfag ialfvgifli antftmlvaq rtrelallra
      301 vgasrrqvtr svlteafvvg aiasvvgfaa gigvgaglra lmgsmsgnvp egplvvpmsa
      361 vltsllvgtl vtvlaawlpg rraskippia amnsvhatat tkslvlrnti galfagagva
      421 vvlygtggsa gknvnlvlag gatllmigvf vltpllsrpl ialaapvlri fgvagtlarq
      481 nsvrnprrta atasalmvgl tlitgltvva tsvqtaiekq avaslksdyv vsmagpvpls
      541 pdvakklrtl devtavsplr qsfadhtmlt gvtgkdfdkv arldftqgsl gtiqgnqvvv
      601 dsktaeekgl hpgsrfpvtf adgkkstltv sgvyegndli ngvildnatl aphektadds
      661 rvlvktkdga tdatkdalit algknpalsv adkqevteai agmvslmlnm lyallamavi
      721 vavlgvintl amsvfersqe igmlraigld rpgikrmvrl eslvislfgg vlgiglgvff
      781 gwaagpliss dmptyalvlp wgrlglffaa aaligvlaal wparraarln mltaikae
//
LOCUS       WP_457682364             423 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682364
VERSION     WP_457682364.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 423)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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 423)
  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..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /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=44386
     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 ypngttavdd lsldlpeggv tvlvgssgcg ktttlrmvnr mveptsgtis
       61 vggrdilead aaelrrgigy viqqsglfph rtildniatv plllgwgrrk araraaelle
      121 lvglpadagk ryphqlsggq qqrvgvaral aadppvllmd epfgavdpvv rtqlqnellr
      181 lqeelrktvv fvthdideav rlgdriavfr tggrlvqcap paellarpad dfvadflgae
      241 rglkllsltt ladvpyapgr eiradepvga isrdgdrwrl vtsprgeplg wldtdalpag
      301 gtageaplea vrplrdtdsl lsalneavss paaavarvta dgvltgltsr davhdragrs
      361 haeagraaat teptpepape ppvaedaedg kngkdgrnaq daddaaslkt asapepsape
      421 psa
//
LOCUS       WP_457682365             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682365
VERSION     WP_457682365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36133
     Region          29..246
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtttdhqpad pstatpapta spaprqpvir vrdlrmsygs ahvlhgidld ihrgeifall
       61 gpngagkttt veilegfrqr sageavvlgt dparggdawr ariglvlqsw rdhrrwrvae
      121 llthfatyyp rprdpaella lvglteqagq qvdrlsggqr rrldvalaiv grpellflde
      181 pttgfdpear rdfhdlverl ardegvtill tthdlaeaer ladriamlvn grirahgtps
      241 elarraaaqa evrwtapdgt srrertedps qlvwelhqet ggpvadlevr rptledtylh
      301 mvhrdtgdgs dagttdanea gpsdgekraa
//
LOCUS       WP_457682373             330 aa            linear   BCT 27-JAN-2026
DEFINITION  COG1470 family protein [Streptomyces nigrescens].
ACCESSION   WP_457682373
VERSION     WP_457682373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11444751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="COG1470 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32957
     Region          <60..>280
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mpfrprtavs gailataavl lcpaaaaarp aaapappgws aapapgdgat psaqdrpyfy
       61 legapgtvmn drlslrnptg ravtvrlrgs gawiafaake vtvpprtraa vpftvtvprd
      121 aapgdhpatl iataagpgrg aagrdtvpvh lrvsgpvlaa ltvenvsvrg rgeaaviryt
      181 lvnrgntvlt prlavradgf fgpvlrrgvr tlpgrlspgq saeltepwad ppgldavevr
      241 ltatadggah gsatasytal pwgvvagpaf llaagagglv ivrrrrraqg pggpqgggpv
      301 gsadggkqps grqaadpave lastgsgars
//
LOCUS       WP_457682380             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682380
VERSION     WP_457682380.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37164
     Region          26..269
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnigektigg vgrggagsag sgagvievtg lrrsygaagr rerggrsges sgpsgpsgps
       61 gprsfeavrg idfsvergel fallgtngag ktstlelleg lalptagqvr vlghdpfrer
      121 rkvrprvgvm lqeggfpsel tpaetvrmwa gctsgarpvd ealgsvgler rrdvrvkqls
      181 ggerrrldla lallgrpevl fldepttgld tearhatwel vrelrdsgtt ivltthylee
      241 aeeladrlai mhggriaaag hvadvvaahp shisfelptg fhlgdlpplg elgiighetd
      301 grtvrlrtde lqraatgvll waqdkgialg nldvrsasle eaflhiakgl ena
//
LOCUS       WP_457682356             435 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457682356
VERSION     WP_457682356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 435)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47773
     Region          34..430
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(71,78,107..108,115,119,126,259..260,263,267..268,
                     271,309,314..315,318..319,321,344,371..373,376..377,
                     379..381,385)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(78,101,103,106,108..109,191..192,202,258..259,
                     262..263,267,315,318..320,420)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mhdkphttaa dapagcpaag papalftwef asdpypayaw lrehapvhrt elpsgveawl
       61 vtrytearqa ladarlsknp vhhseaahgk gkvgipgers anlmthllni dppdhtrlrr
      121 lvskaftprr vaafaprvqe ltdhlidqfa akgeadlihe fafplpiyai cdllgvpred
      181 qddfrdwagm mirhgggprg gvarsvkkmr gylaelihrk reslgetaea dedlisalir
      241 asdhgehlte neaaamafil lfagfettvn ligngtyall rhpaqrellq ksiaagdtdl
      301 lttgieellr ydgpvelatw rfatqeltlg gqriaegdpv lvvlaaadrd parfdepdvl
      361 dltrrdnqhl gyghgihycl gaplarlegq salatlltrl pdirlatepd dlrwrgglim
      421 rglrslpvef tperp
//
LOCUS       WP_457682384             561 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682384
VERSION     WP_457682384.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 561)
  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 561)
  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..561
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..561
                     /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=58821
     Region          279..456
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 maraarsrtp hpdtpqsplh rllhtgldgv ralpaavrrg yrsrrtapta glaesphpla
       61 rslgliaatv vgawlgllli gsirvpvgpm dtsmalrpsl aggtridvap lgdlelsshh
      121 apvrldvdvd rldpvrsqal vdhperfagl qaevthdvtr galglalhsc vavvsgatal
      181 glavyrrprr alaagglalt llaasagtay atwnpqsvle pkfsglltsa psvvgnarni
      241 vsefhvyqke larlvtnvtk lydatstlpa yqpdpttirv lhvsdihlnp gawriiaslv
      301 kqyrinvivd tgdtmdhgsa aenhfldpas algapyvwvr gnhdsrgtqk yltgrrhvtv
      361 ldhgkvtqva gvriagvgdp qftpdrsvva agdpaertag grladalrtq rlagtpvdia
      421 lahnpaavte adglaplala ghvhhrentl lpqgtrlmve gstgggglra vqnkkpepvl
      481 asvlyldrtt krlqawdeit lgglglsrae vsrhlprenq pgatpspsgs ppsadppsgp
      541 psgpssgsss rparspseha r
//
LOCUS       WP_457682387             372 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457682387
VERSION     WP_457682387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38107
     Region          183..366
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 masnrpapes psayelddrg afpgpgaddg dgpweewnpt eestrsvrgk hrvakqrggg
       61 farsgtvlgv gviaavgasg masaedrppv pismpdiggm addlsenlpd akslpgigel
      121 isdedsetas aaaaeaapaa sgpltratqt sadtgggtga gealrsrilq qadaqqgaae
      181 qeardtaeqa avqqaateaa ahqksaekaa aakkaaemea krkaeeaarq kaeaerlakl
      241 aksfiapvss ytltasfgqa gdrwaadhtg qdfaaptgtp vkalhsgtit qagwagsygy
      301 rivltlddgt evwfchlssm vktsgkvntg dvigrvgatg nvtgphlhle vrpdagdpid
      361 pmpwlrdhgi nv
//
LOCUS       WP_457682391             394 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457682391
VERSION     WP_457682391.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=42904
     Region          6..353
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtrtestfts veicagaggq avglhkagfk hralieidas acttlrrnve gnpewdgcdv
       61 ieadltdfdp aslalepgel dllaggvpcp pfsvagkqlg qdderdlfpt mldlvdelrp
      121 kavmienvrg lldqkfvdyr envirkrleq agyvicywkv leacdygvpq lrprailvam
      181 rsdyaqhfvw tepeksklit taealapsml rrfresgedp rwkgaytgrw esayekwrnq
      241 aelgtvaptl vggskkhgga dlgptrakea wrklgvcglg vaneptelkd perdlyaerg
      301 pkltvsqaai iqgfpeewef pgrktatyrq vgnafpppva qavgeqiiaa lragqemgaa
      361 esgesglldv papsrslgtt ladhrsdles agvr
//
LOCUS       WP_457682389             243 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457682389
VERSION     WP_457682389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Nemeth,E., Kozisek,M., Schilli,G.K. and Gyurcsik,B.
  TITLE     Preorganization of the catalytic Zn(2+)-binding site in the HNH
            nuclease motif--A solution study
  JOURNAL   J Inorg Biochem 151, 143-149 (2015)
   PUBMED   25898772
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Veluchamy,A., Mary,S., Acharya,V., Mehta,P., Deva,T. and
            Krishnaswamy,S.
  TITLE     HNHDb: a database on pattern based classification of HNH domains
            reveals functional relevance of sequence patterns and domain
            associations
  JOURNAL   Bioinformation 4 (2), 80-83 (2009)
   PUBMED   20198175
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Mehta,P., Katta,K. and Krishnaswamy,S.
  TITLE     HNH family subclassification leads to identification of commonality
            in the His-Me endonuclease superfamily
  JOURNAL   Protein Sci 13 (1), 295-300 (2004)
   PUBMED   14691243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="HNH endonuclease"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27142
     Region          126..236
                     /region_name="COG3183"
                     /note="Predicted restriction endonuclease, HNH family
                     [Defense mechanisms]"
                     /db_xref="CDD:442416"
ORIGIN      
        1 mwdelllaca lvvengwrel regdsrvdel snllrslplh gdaargipkf rstgsvsrkt
       61 tdlatnhpay qgkatrcgrl dremiarfaa dpdimlkaar aieagigsge lvkipeqpde
      121 vaedgatale grlltrwsla rernpklrrr kidrarrigq plqcevcdfh fgrfygdlge
      181 dyievhhvlp lhasgpretk ledlallcsn chrmchrsha geswrtpgml rakiaeygal
      241 srt
//
LOCUS       WP_457682392             153 aa            linear   BCT 27-JAN-2026
DEFINITION  very short patch repair endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457682392
VERSION     WP_457682392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Tsutakawa,S.E. and Morikawa,K.
  TITLE     The structural basis of damaged DNA recognition and endonucleolytic
            cleavage for very short patch repair endonuclease
  JOURNAL   Nucleic Acids Res 29 (18), 3775-3783 (2001)
   PUBMED   11557809
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Tsutakawa,S.E., Jingami,H. and Morikawa,K.
  TITLE     Recognition of a TG mismatch: the crystal structure of very short
            patch repair endonuclease in complex with a DNA duplex
  JOURNAL   Cell 99 (6), 615-623 (1999)
   PUBMED   10612397
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Tsutakawa,S.E., Muto,T., Kawate,T., Jingami,H., Kunishima,N.,
            Ariyoshi,M., Kohda,D., Nakagawa,M. and Morikawa,K.
  TITLE     Crystallographic and functional studies of very short patch repair
            endonuclease
  JOURNAL   Mol Cell 3 (5), 621-628 (1999)
   PUBMED   10360178
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="very short patch repair endonuclease"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006298 - mismatch repair [Evidence IEA]"
                     /calculated_mol_wt=17371
     Region          16..150
                     /region_name="Vsr"
                     /note="G:T-mismatch repair DNA endonuclease Vsr, very
                     short patch repair protein [Replication, recombination and
                     repair]; COG3727"
                     /db_xref="CDD:442941"
ORIGIN      
        1 mhrspdeqws ppsgswassa arrknmqair srdteperli rrlvhaqglr yrvaakplpg
       61 lrrtadmvfr pakvavfidg cywhgcpehy vppktnpgyw sdkvagniar drdtdrrlre
      121 agwtilrfwe hespdacalq iaavvskrra kgt
//
LOCUS       WP_457682398             437 aa            linear   BCT 27-JAN-2026
DEFINITION  PrsW family intramembrane metalloprotease [Streptomyces
            nigrescens].
ACCESSION   WP_457682398
VERSION     WP_457682398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Ho,T.D. and Ellermeier,C.D.
  TITLE     PrsW is required for colonization, resistance to antimicrobial
            peptides, and expression of extracytoplasmic function sigma factors
            in Clostridium difficile
  JOURNAL   Infect Immun 79 (8), 3229-3238 (2011)
   PUBMED   21628514
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="PrsW family intramembrane metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47062
     Region          47..314
                     /region_name="PrsW"
                     /note="Membrane proteinase PrsW, cleaves anti-sigma factor
                     RsiW, M82 family [Signal transduction mechanisms];
                     COG2339"
                     /db_xref="CDD:441909"
ORIGIN      
        1 mypsqppshp phapapppyt phtyepsaas arrrtapwrs ktlravalvs llalsgviii
       61 gmvrhetgte gflvglglav fpvpllvaaf cwldrvepep wrnlafaftw gacaatlval
      121 langfatdwl aaniastsps eaeawgatvi apvveevvka aavlllyrfr rrefdgitdg
      181 iviagitatg faftenvlhl gnafgqdqsl ghsgldslta gtfflriivs pfahplftil
      241 tglafgiaat ryprrrpari alallgllta vllhaiwnga stlgdlgfli vyglfmvpil
      301 ialtwlaiwa rnqellslrg ylapyitagw ltpteptals slktralard larrtqgpaa
      361 aravteyttv atalsfhrrr ahlmgpspdf aireqhlleh lrehqawgra altsaldttc
      421 qphvsaripq hgspdsq
//
LOCUS       WP_457682400             282 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457682400
VERSION     WP_457682400.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  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 10172349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=30347
     Region          6..153
                     /region_name="SRPBCC_CalC_Aha1-like_6"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; cd08899"
                     /db_xref="CDD:176908"
     Site            order(17,19,21,30..32,34..35,40,48,56,58,60,62,69,71..72,
                     74,77,83,85..86,91..92,94,96,106,108,110,112,116..124,
                     126..128,131)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176908"
     Region          161..279
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
     Site            order(173,175,177,186..188,190..191,203,206,214,216,218,
                     225,227,234..235,237,239,249,251,253,255,261..265,267,
                     270..272,275)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mnphsdtltt adgrtalrme rrlahppakv wsaitdpahl gqwfpsevtv elrpggamtf
       61 ampgvsgiam tgtvtdaeep rlfaftwged hlrweitpdg dgsllvlvht fgdrfggasf
      121 asgwhlclta lsqlldgdst rverdagelh eayleqfdlg rgvveetaeg prvrferqlv
      181 rpaeavwaal tsgdepaaga papegftsrq apagpvtevt apsvlayrwh pegtvrwelg
      241 qgtghgprlv ltqtgpegfd tdaaldawhd rieqlaarll ad
//
LOCUS       WP_457682404             306 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682404
VERSION     WP_457682404.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33866
     Region          31..280
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrgftrlrrv glpyllllpa lllellvhlv pmvigivmsf keltqlhiah wgtapwkalg
       61 nyrvtvdfda pvgatllhsf vvtcafsllt vglcwllgta aaiflqenfr grgllravfl
      121 tpyalpvyaa vitwaflfqr dnglvnhvlh dqlqltgdrp fwllgdnsfl allvvsvwkt
      181 wpfaflvvma alqsipkdly eaaaldgagi vrqirritlp slrpinqvll lvlflwsfnd
      241 fntpyvlfgk aapeaadlls ihiyqssfvt wnfgtgsams vllllfllvv tagyllatsr
      301 grksdg
//
LOCUS       WP_457682405             438 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682405
VERSION     WP_457682405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46518
     Region          40..436
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(155,157,281,283,320..322,363)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrilraatvt atvtalaava agcgggtsfd dggsddsprt ltywasnqgp nveadkkilg
       61 pelrkferqt gikvklevip wpellnrila attsgqgpdv lnigntwsas lqatgallpw
      121 drknldaigg rdrflapale atgaagkdpa avplyslaya lyynkrmfqe agiskppatw
      181 delvadgkri skdgkwglga eggqltnnih qafalgkqhg adffdrtgkp tftsdgavaa
      241 vkqyidfmak dkiiapgnae ygqnqslrdf atgrtamvlw qaaattfaad gmkpgdwgva
      301 pvpvpsgtpg tgrqinsmla giniavfknt rnlqgarkfv kfmtsdteqr llnktygsip
      361 pvkaaqqdpa fnrkdtrvlr etlirsaapl pqiaeesqfe tsvgtavkdl fadaaaghpv
      421 ttasvkarla kaqqqmaq
//
LOCUS       WP_457682409             565 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682409
VERSION     WP_457682409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..565
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60386
     Region          19..563
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mdlsttpdar tpgspeggpa dlvflagpvh tvdsartras avavrgdril avgheeevra
       61 ligpatevvd lhgkllipgf qdahvhpvgg grelalcdls aavtaeayre lisayaaahp
      121 qtpwitgggw smeafpggmp trefldalvp drpvflvnrd hhggwansca leragltest
      181 pdpsdgrier dadgrptgml qegamqlvag lipdptvaeq tegllraqrl lhgygvtawq
      241 damlgyapgm pdvtpayvaa rrdgkltarv tgalwwdrar geeqipelia rraeltegrl
      301 ratsvkimqd giaenhtaam ltpyltacgc asdnsgisfi dpealrsyvt qldaegfqvh
      361 fhalgdravr ealdaveaar rthgmrdtrp hlahlqvvhp edvprfrrlg ataniqalwa
      421 ahepqmdelt ipflgprraa wqypfgdllr sgatlaagsd wpvsspdpia alhvavnrra
      481 pedppsapvf lpeqridlga alaaytagsa yanhldetgt iqpgkladlv vldrdpfdgp
      541 deeiaatrvl qtfvggqrvy aadda
//
LOCUS       WP_457682407             442 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682407
VERSION     WP_457682407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=45563
     Region          1..>50
                     /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..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 maertqrtvr dlrranrtav lqrlysdgpm srqelgpatg lssgsvsnvv aelveeglle
       61 eagvvgsdgg rprtllrvap gsgcligvdv getrvrvelf dlamgelara elplrhhgyd
      121 vdlivrhiad giatvlrese aspgrllgvg vgvpgildrs rpggavvhgq tigwdavple
      181 ellhhtvalp pgvgfflsng akalgqaemw fgggrgaena aivlfgsgvg aclvtdgvid
      241 ggardsagew ghltvsvggr rcrcgargcl eaytgseall qrwqeaggqp ppdadeetal
      301 aalvaaahpp aggpavdpva rsvldetaey lgagisdlin lfspervlig gwaglqlgph
      361 llpavrahat ayslahpagr vtidlgrlgp davtvgaatl pladffangg rrraapadep
      421 gervtapgwr taleerarag rg
//
LOCUS       WP_457682420             684 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682420
VERSION     WP_457682420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..684
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72163
     Region          2..665
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtarvdrrpl pgvvgraveh elvsgllgsa plvtltgpag vgksllahav leehtarhdg
       61 tilrvgcwdg paegglpatl lraaqsadsa rrdtatalvr rtapscvgep vcgrtgrtdt
      121 ptgpspsddt aiaalaahcr qsratvlldd cdplrdecaq lvrqllradp slrivatarg
      181 alglpeeriv eiaplpvtlg egiagpavel laartgaaap ellvavcqal egsplaiala
      241 aqqldrmslp qlaaqvgsdg plfwsgpaat vrhtslyaaq aagyalcspt drrvwarlsv
      301 lpgdfdpwla gcvctscdvp aaavegaler lltasvierv rdaggaqddt gaalppryrl
      361 praardfgrt qlreageesa alrrfrqaca alaaeaqiaw qgpnqqvavr lvedeqanld
      421 aaltrppqda edalgaleia vslwfhwaac gfrregrahl drllllsrdd talraralwl
      481 agylaaqeha pgaaealldq awtaavmhad sdglariaha hgvlalyrgd taaavaclee
      541 aarhrsrdpw fgpgpahswa llavalssld aeraraaarr awearhsdgd fwlystvlya
      601 caatervhge paaalracrt alaakeligd plfiagahhm laglrhevrg geplpdrdee
      661 dawwrpggpd vppqpffsrl ragp
//
LOCUS       WP_457682424             503 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457682424
VERSION     WP_457682424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54319
     Region          10..455
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpelldervg fvrriglfqa tainmsqmcg igpfvtiplm vaafggpqav tgflagavla
       61 ladgliwael gaslpgaggs yvylrqafqy rtgklmpflf vwtamlfipl gmstgvigfv
      121 qylgylwpdm tsgqgdlvgi gvtvgivvll wrrveniakl tvvlwtvmit svllvivaaf
      181 thfsperaft ypahafelts shfwtgfvag ltigiydylg yntiaymgae irqpgrtipr
      241 ailfailgim tiylllqigt lgivnwqeml dphstasssv asavlerawg kgaagtvtvl
      301 ilitavasvf tgllggsrvp ydaarervff rpygtlhprh rfpvlglltm gtvmaagfll
      361 grhtdlatii qllttvmviv qalaqvaavt vlrrrqpglh rpyrmwlypl psvvaligwl
      421 viygyadrna pgrhpiewsl awvgsgvvaf lvwaryekew pfgpkritee ylhgsdpdtg
      481 graggegrek gaggtavgat dpg
//
LOCUS       WP_457682430             272 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682430
VERSION     WP_457682430.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /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=29754
     Region          17..>231
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mdldptirtl tlltllqsgg ewtaadlaer lgtsvrtvrr daqrlrrlgy tvearpgpgs
       61 ayrlrpgvkv ppllftadei talvaglhli rawlpedava ssallkldqv lprplrrraa
      121 atdlatevlq qpgavvaaat vgviadavae dgrlrfrytd qhgrpstrlv epyrhflrag
      181 hwylvafdvd rddwrtfrld ritdispvag afqphafpdv sierwlttdf graparspgs
      241 saampdvaed gepggevrgd tgpsredhrh pp
//
LOCUS       WP_457682426             837 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682426
VERSION     WP_457682426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 837)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..837
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86704
     Region          2..837
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mlkamlrdll ahkgrvvmtl iaialgvtat vgswvvsdsi attlagqetr hdvgvsvqsp
       61 gkeslltsad rdrlartpgv graegvivgr agligrghkf vrtttvldra gtnwssdkrf
      121 tveagtaptg pgqvalhkad adsagiavgd taqvllsdgr sdtarvtalf tyhrlgprat
      181 tdaneasdav pvvaydtata tkllgprfhr velipasgas pgalkaaaqk gvsdeyhvet
      241 gsalaqaavq qsdseaqdlr mtmlpfaava llvgmfvian tftllvsrrt rqfallravg
      301 arkgqvragi vveagvlgla ggtlgtlagv algpsmiavm rpqddvdltv spfavllgyg
      361 vallvtvvaa yrsarraaav ppvaalrtae tvpretkrtr hftglgcivt gvvmvamtad
      421 pgtsnlgriv glmgavlgvi gmivlapffa eallrplmrl lgarsgpavr lglrnaasdp
      481 rrtsgtatal tvglalvcaf atlsasfsal iasttranvp ptttvlqsaa ggessltpae
      541 adkvrklpgv tqvagsrdvl vgltykggrt errisaieps glkcvltphl tagspdlrrg
      601 vvisqnqadm ldlgmndrit lhldartsvt qsvvgiydat elqasifldv skapgslrkq
      661 ittlyasgpd pdtardsira afrdrpdvsv gsretlveqg vdqqslaftl myamfgvail
      721 iavsgvvntl vlsvmertre igviravgat rllvrrtirv esivislfga llgvivgvpa
      781 gavmqhamfg qrlgdfslpa giiglslagi tlaavlaaiw parraartdm laaiage
//
LOCUS       WP_457682437             310 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457682437
VERSION     WP_457682437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   di Salvo,M.L., Safo,M.K., Musayev,F.N., Bossa,F. and Schirch,V.
  TITLE     Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate
            oxidase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 76-82 (2003)
   PUBMED   12686112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1562906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..310
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33481
     Region          9..112
                     /region_name="YzzA"
                     /note="General stress protein 26 (function unknown)
                     [Function unknown]; COG3871"
                     /db_xref="CDD:443080"
ORIGIN      
        1 malldsapld vldayrtcef atlgrdgtpl awptavrrrp dgtlllstsl afaqkalnir
       61 rdgrvallfs dptgsgleqp pqifvggrae cpdeimtgpq gaedywrmlf erqphsrsyv
      121 tapmrlvmdw yylrllitvt pqqvvvrspl ppsgtpaapp gelvgaaqla rfptavlaar
      181 dasgapvlar trpvpagegf avdvpadcpa tegpaallvh rhderlnhmh nalvrgelra
      241 agsgwvlvpg kvvepmgsgr vsdavsvlrs trqatdrylr rrglprprvr waefralaqd
      301 arrsgeppga
//
LOCUS       WP_457682438             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682438
VERSION     WP_457682438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43240
     Region          13..391
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,118..119,121..123,126,146,
                     149..150,153,228,231..232,235..237,240,264,268,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mvrtvppwag rnyllltgat vianlgssga liatafavla aggsatdvgl vaaartipli
       61 fflliggava drlprhrvmv aanalscvsq glfallvlag epqlwqmall aalggtgqaf
      121 fapasegmvl asvsgdqagr afavyrmgmn ganiggaalg galvaavgpg wvlavdsaaf
      181 alaaalrafl dvsgvperap gggmlhdlrd gwrevasrpw lwavvvqfsl vnavvsaaea
      241 vygplvaeqh lggpgpwgla laafgvgtvg gallmarvrp rrmlltgalc ifplalpsaa
      301 lavplpvagl taimfgtgia vevfavmwmt alhqeipeek fsrvssydwl gslamvppat
      361 alagpvqdli grtaalwgcs avivlltaav lcvpdvrrlt rrpktepaag apaspaaeta
      421 apdtagae
//
LOCUS       WP_457682446             385 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682446
VERSION     WP_457682446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..385
                     /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=39167
     Region          136..374
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtdflvival aalgaalagl laapavralr rrsvalslfa vaalavaama agtvavaqam
       61 flsghdlgvv mavvavsgvv slaaallfgr riaagsrela rsartvgseg gfvapaeppt
      121 aelaalsqal eetsgrlaea rereraldas rreliagish dlrtplaglr amaealedgv
      181 aedtaryhar mrievdrlaa mvddlfelsr iqagalaltl srvsvydlvd ealagagpla
      241 rasgvrlvdg gvvplpvrvd aqqmtrvlgn llvdairatp adgtvavsar haegrvvlav
      301 edgcggippe dlprvfdtgw rggaartpra dgkggaglgl aivrgiveah egratvrnag
      361 agcrfevelp aaeaqagpqa kppta
//
LOCUS       WP_457682452             347 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682452
VERSION     WP_457682452.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36151
     Region          58..261
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(117,119,121..122,195..196,214,251)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(117,119,121,195,214,251)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mddataphka artsatpsaa rstgpgatgp dateppgagt paagspvpep yltelaagvh
       61 afiqpdggwc lnnagfvtdg datlvvdtaa terrarllrr riaesgapap rtvvnthhhg
      121 dhtygngvfa peatvighas crrellaagh qlhavwpeve ygdihltppe vtytdeltlh
      181 vgeievrlih pgvahttgdt vvwlpreriv fagdlvfhgg tpfllmgsla gslravrtlr
      241 aldavtvvpg hgpvtgpevy dgierylrfv grlaqegraa grtpletaqe adlgpfaela
      301 eserlvanlh rayaelagaa pgvpldpmaa fadmavlngg vpmscha
//
LOCUS       WP_457682454             350 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682454
VERSION     WP_457682454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37732
     Region          40..290
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(45,48..50,53,64,66,98,117..120,218,220,222..223,225,
                     236..237,240,255..256,259)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(45,49,53,64,66,98,117..120,218,222..223,225,
                     236..237)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(48..50,218,220,223,237,240,255..256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mskgtpppqd rdredppgld larlrehldr erpglvggpl raqlieggrs nltyrvtdga
       61 aswvvrrppl ghvlatahdm qrehrvisal hetpvpvpea lllcadesvi gapfyvmelv
      121 egtpyrtagq laplgpertr avvlslvdtl velhavepea vglgdfgrpd gflerqlrrw
      181 gkqltasknr elpgidelhe algralpasp apavvhgdyr ldnvligadd tlkavldwem
      241 stlgdpltdl gllamystdl nlpgspvstt sgapghpapa elieryaars grdtsaiawy
      301 tafawfklav ilegihyrft lgqtvgagfd rigelvpvfi dsglttlkeg
//
LOCUS       WP_457682458             256 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682458
VERSION     WP_457682458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26488
     Region          24..210
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maavrdktvv vtgagggiga alarrfaaeg arvvvndlde akakrtadei gavavagdas
       61 tvvpaareal gggidvfcan agvgtgggpe apeedwalaw dvnvmahvra arelvpewle
      121 rgsgrfistv saaglltmva aapysvtkhg ayafaewlsl tyrhrgidvh aicpqgvrtd
      181 mlaatgtagd lvltptavep edvaealfaa maegrflvlp haevadyyta raaepdrwlg
      241 gmnhlqqkle qaegrs
//
LOCUS       WP_457682460             425 aa            linear   BCT 27-JAN-2026
DEFINITION  exo-beta-N-acetylmuramidase NamZ family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682460
VERSION     WP_457682460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Muller,M., Calvert,M., Hottmann,I., Kluj,R.M., Teufel,T.,
            Balbuchta,K., Engelbrecht,A., Selim,K.A., Xu,Q., Borisova,M.,
            Titz,A. and Mayer,C.
  TITLE     The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the
            founding member of a family of exo-lytic peptidoglycan
            hexosaminidases
  JOURNAL   J Biol Chem 296, 100519 (2021)
   PUBMED   33684445
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..425
                     /product="exo-beta-N-acetylmuramidase NamZ family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0033922 - peptidoglycan
                     beta-N-acetylmuramidase activity [Evidence IEA]"
                     /calculated_mol_wt=45542
     Region          41..425
                     /region_name="YbbC"
                     /note="Uncharacterized conserved protein YbbC, DUF1343
                     family [Function unknown]; COG3876"
                     /db_xref="CDD:443084"
ORIGIN      
        1 malsrrvllg qlaatgaaga alaagagpar aaqpahgggr rvhtgfdrla adgyrlltgr
       61 rvgivtnptg vtrelrhivd vmhaddrvrl tavfgpehgf rgtaqaggse gryddpatgl
      121 pvydtynksg taladiftas gvdtvvfdiq dvgarfytyi wtlydcmvaa vlagkrfmvl
      181 drpnpvtgrs atgpvldkay asfvgrepia qahgmtvael allfngefvp gaagrpvele
      241 tvrmtgwrrt dfydatglpw vppspnmptp dtalvysgtc lfegtnlseg rgttrpfell
      301 gadgidrrwa aaatelalpg vhfreayfap tfskfqgkti ggvqlhvher aafdpvrtgi
      361 gllvtakrvw pgftwrpdhg idrltgssav rtmidagagp deivaawqeg lkgfrtvrrr
      421 ylryp
//
LOCUS       WP_457682461             941 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682461
VERSION     WP_457682461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 941)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..941
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=101495
     Region          124..930
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mrrrtgrlrt aaaaalfalg atllapppta aaaaaphdan dycqgqcgdi lppgatgnat
       61 lveilgnklf gthpehsadq lapygalasg yqsltddtlg sffndasfgv padqagkvtt
      121 prndvtitrd kktgvphikg ttrygtefga gyaagqdrlw lmdlfrhigr geltsfagga
      181 lanqgleqqf wpqapytedd lqaqverird tngergklam qdaqayvdgi nayreqskng
      241 ryfpgeyvlt ghvdaitnag eikpfkltdl ialasvvggl fgnggggevp salallsaqq
      301 kygvekgtev wesfrerddp eaaktlhdgs sfpyavkpak akgvalpdrg svtpeplvfd
      361 rtgaatvksg tpprdpvkap kkykkleglf kdgvlpkgsf dptqhrgmsn allvsgkhta
      421 sghpvavfgp qtgyfapqll mlqeiqgpgi sargasfagv gmyvqlgrgq dyswsatsag
      481 qditdtfave lcnadgstpt kdstsyryrg acvpmekler tnswkptiad ptaagsyrmq
      541 vfrtkygtvt hratldgkpv aytaqrstyr headsiigfq mlndpsyvrd aksfqqaaeh
      601 igyafnwfya dsrdiayyns glnpvrnpdv dpslpvkadd ayewkdydpe tntteytpsa
      661 qhpqsvnqdy yiswnnkqak dydsagygng svhrgnlldd rvraltkdgg atrasltram
      721 seaavtdlrg edvlpellrv vnsepvtdpk lktavqqlea wrkdgaqrre taagshtyth
      781 pdavrlmdaw wplmteavfk pglggdlyda lranlgides psaghgptga hagsafqygw
      841 wsyadkdlra vlgdkvagpl srqycgngel sacrdtllat lqqasgktae qvypgddsck
      901 agdqwcadai ihrtvgglth atiswqnrpt yqqvvefpah r
//
LOCUS       WP_457682465             215 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682465
VERSION     WP_457682465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22857
     Region          5..128
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          74..205
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 marprkplls rerivstala lidseglpal strrlaaelg vsgpslynhf ttkdeildav
       61 adtviakvdv safetgadwr tglldwarsy raalaahphi vpflaqgpgr rpaglkmada
      121 afggmveagw ppaqatrvca mvryfvagsa lgsfargfvd dpsaydpady phlgqahlla
      181 ehqrqvdega fetglralvd glalqhpdlv ppegr
//
LOCUS       WP_457682467             459 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682467
VERSION     WP_457682467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47835
     Region          22..435
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,265,268..269,272..274,277,305,309,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mdtapsaphg ntgtppstrs rrrvataaal asavewydyf vfgiaaalvl gpaffpsgse
       61 aagvlasfat favgflarpv ggviagqlgd rhgrkpmlvl altvmglatt aigllpsydt
      121 iglaapillv vlrllqgiav gaqwggamlm ateyapegkr glygslvqlg vplgvitans
      181 afllagaltd ersfstwgwr lpflvgvlvl llaryihtrv eetpafraae eklataeqaa
      241 aarrsplrei lryhlrtvll aggsfavnta tfyilitgvl dyatreldmr rtsvlavsll
      301 vsltqlamip aaaalsdrig rlrvyaagav glllwavpmf llidtaslvw lavgtfvcsc
      361 flsimygpqa alfaelftae mrytgaslgy qisailgggl apfvmvllle asgtsmavsg
      421 yimalsvial vsiwllirra gttaapggga epgatkvqg
//
LOCUS       WP_457682474             298 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682474
VERSION     WP_457682474.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30355
     Region          8..288
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msnahdprtp vtvlglgamg salagafvga ghpttvwnrt pgkaedlvar gavradtvae
       61 avaasplviv cvvdyaaahe ilepagsrls grvlvnltsd tperarsaaa waaghgidyl
      121 dgsvmvpttd vgqpgatlly sgsrkafety ketlkvlggr aaylgddham aavydlalla
      181 ffysamaglv hafalagaeg vpaeefvpft gaiadilppl aagmaqdldr gvlrgdqdni
      241 vmeaagmahi ieasvdrgin tdvlaavkgl adrtiaaghg kagflsiige mrkpsakg
//
LOCUS       WP_457682476             469 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682476
VERSION     WP_457682476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46837
     Region          4..358
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtgtdtrrpg rgwllrlvlt fsfaqgavsm arpavsyral algaderaig vitavyallp
       61 llvavplgrr tdhgrcapll vtgvalisgg calsglagsl pamaawsgvm glghlcfvig
      121 aqsivarrsa pedrdrnfgh ftigaslgql igpaaaglvi sehdgrmapt satallvsga
      181 vaavsyaslw rleqrartap sgapapaagp pvpvrgilrt rgvpagifms lavlsatdil
      241 taylpviged raiapttigl llslraaati acrlvmtpmi rwlgrtalmv vscalagvlc
      301 gglvlpvpvw alaamllalg fclgvgqpls mttvvqaape rarstalalr ltgnrlgqva
      361 apagagllag vagtaapfvl lgalllasaa laartgperg ggttpgaggg papavkvtgp
      421 aaegeaapap eeeagqgrvg hgtggpqarp qarpqarpqa rpqarpkgp
//
LOCUS       WP_457682478             487 aa            linear   BCT 27-JAN-2026
DEFINITION  CitMHS family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682478
VERSION     WP_457682478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Korithoski,B., Krastel,K. and Cvitkovitch,D.G.
  TITLE     Transport and metabolism of citrate by Streptococcus mutans
  JOURNAL   J Bacteriol 187 (13), 4451-4456 (2005)
   PUBMED   15968054
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Krom,B.P., Warner,J.B., Konings,W.N. and Lolkema,J.S.
  TITLE     Complementary metal ion specificity of the metal-citrate
            transporters CitM and CitH of Bacillus subtilis
  JOURNAL   J Bacteriol 182 (22), 6374-6381 (2000)
   PUBMED   11053381
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Boorsma,A., van der Rest,M.E., Lolkema,J.S. and Konings,W.N.
  TITLE     Secondary transporters for citrate and the Mg(2+)-citrate complex
            in Bacillus subtilis are homologous proteins
  JOURNAL   J Bacteriol 178 (21), 6216-6222 (1996)
   PUBMED   8892821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="CitMHS family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0046942 - carboxylic acid transport
                     [Evidence IEA]"
                     /GO_process="GO:1905039 - carboxylic acid transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=50507
     Region          1..487
                     /region_name="CitM"
                     /note="Mg2+/citrate symporter [Energy production and
                     conversion]; COG2851"
                     /db_xref="CDD:442099"
ORIGIN      
        1 mltilgfvmi aaflvlimmk kmspmaalvl ipalfcvlvg qgahlgdyvl kgigdlapta
       61 amlmfaiiyf gvmidvglfd pivrgilkfc kadpvrvvvg tallaaivsl dgdgsttfmi
      121 tvsalyplyk rlkmslvvmt gvaatangvm ntlpwggpta raatalklda gdifvpmipa
      181 lavglvavfa layvlgrrer krlgvltldd tlgdtrpvtg tvpekeaeqv lvgagtgatg
      241 gtpagtrrtt ggagtgadda paagsgdqad eddglqvldp qratlrpkly wfnaaltlal
      301 ltllimqtlp ipvlfligaa laltvnfphm kdqkarvaah aenvlnvsgm vfaaavftgv
      361 ltgtgmvehm arwlvsgvpd algphmgivt gvlsipltyf msndgfyfgi vpilaeagaa
      421 hgvapieiar aslvgqalhm ssplvpavyv lvgmakvefg dhtkftvkwa altslvvlca
      481 gvlfgii
//
LOCUS       WP_457682489             299 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682489
VERSION     WP_457682489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32568
     Region          60..296
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mpltsdipve qaapqragpp gaddpaalkv vlvrhpwrwa aivvtavlia qfvhglvtnp
       61 awewavfaqf ftaetvlkav wvtlqltvyg talgfalgvv lafmrlsgsp flrwvafgyi
      121 wafrsipliv qllfwfnlay lykrlefgip fgpgffhvdt mglvgamgaa vlglalhqaa
      181 yaaeivrggv lavdggqlea aaalgiprlr qlrrivlpqa mrsilpnatn evislfkgts
      241 ivsvmaigel fyqvqviygr ngrvvpllmv atawyvlltt vlsvlqhyve rhfskgatr
//
LOCUS       WP_457682497            1201 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase III subunit alpha [Streptomyces nigrescens].
ACCESSION   WP_457682497
VERSION     WP_457682497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1201)
  AUTHORS   Kelman,Z. and O'Donnell,M.
  TITLE     DNA polymerase III holoenzyme: structure and function of a
            chromosomal replicating machine
  JOURNAL   Annu Rev Biochem 64, 171-200 (1995)
   PUBMED   7574479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1201
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1201
                     /product="DNA polymerase III subunit alpha"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=129179
     Region          2..1079
                     /region_name="DnaE"
                     /note="DNA polymerase III, alpha subunit [Replication,
                     recombination and repair]; COG0587"
                     /db_xref="CDD:440352"
ORIGIN      
        1 mpgfthlhta sgfslrygas hperlaeraa ergmdalalt drdglsgavr fakaaaeagv
       61 rplfgselav aeresaptpt arrrtpvrgg afldesaara vflardgaag waalcrlvsa
      121 ahtgqgeqpv lpwsalesat dgltvllgpd sevgralaag rpdraarlla pwrerygeal
      181 rlevvdhgqp gsgpgsprla artlgfavdq glravltnav ryadpgqgpv advldsarrl
      241 vpvdrhrpea rdsgerwlkd gatmshtaer vaeaagfrrg lahrllamte etageclvdp
      301 qddiglgrih fpeprlvgag hrtaarvlrs rcaagmvlrg ydhdrerwar lhdelrtier
      361 lgfpsyfltv aqvvddirem girvaargsg agslvnhllg iahadpvehg llmerflser
      421 raalpdidid vesarrlevy raifdrfgae rvatvsmpet yrvrhavrdv gaalgmdpar
      481 vdrlakafph irardaraal aelpelrgvr eaggeqlwpl vealdalprg iamhpcgvll
      541 sdatlldrtp vvptsgegfa msqfdkedve dlgllkldvl gvrmqsamah avaeigratg
      601 rridlddpaq vppgdpatyd lirstetlgc fqiespgqrd lvgrlqpatf hdlvvdislf
      661 rpgpvaadmv rpfiearhgr kavryphpdl eeplretygv vvfheqiiel lrimtgcgrd
      721 egdekrrals hpelqgrvra wfaqcaerrg yapeviartw eiveafgsyg fckahavafa
      781 vptyqsawlk ahhpaafyag llthdpgmyp krllladarr rgvpvlpldv nrsavahrie
      841 lvsgdgprgg gpgdrsavwg lrlalsdvhg mseaeaqrie tgqpyhslqd lwqrarpgrp
      901 vaerlarvga ldafganrrd lllylaelhr hgrrapggql tlpgraldga gaepvdpvep
      961 aglpdlsdve rlsaelgvlg mdasrhlmad hreflaelga lparllrgar hgetvlvaga
     1021 kaatqtppir sgrrvifttl ddstglvdca ffddshaaca htifhswlll vrgtvqrrgp
     1081 rslsvvgaaa wnlaelaelr reggleavaa rlaavpdtea aeagapaaep gvpaagpgqg
     1141 ageesgeesg tgrepepaaa pgrtirlstg yelhpwadlq ppgeraatgr klwhsspgsa
     1201 g
//
LOCUS       WP_457682499             371 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Streptomyces nigrescens].
ACCESSION   WP_457682499
VERSION     WP_457682499.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=38839
     Region          <41..300
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mtpaprppaa ppdppgaprq pgmlhvrfrt adgtpvsagc feqllgllaq ftpviealpp
       61 daaladvrga lryfdrdaag iaelvrlral awhgvrctig iganpllarm aaqgaapgei
      121 rgvpddagtv aafldrrpas alhgvgpata ralcayglds igriaaappa tlqrilgart
      181 grivyerarg idptpvtpna aarsmgaehr fahdeldpar rrrallslad dlgarmrasg
      241 qvahaltltv ryadrstttr trrldgptah gpalteaaya lhaalglqra rvrsvalrae
      301 dlcraeraar qltfdpsddr ahrieaavdr ararfgtgsv rpaatlgrtp pppgtkplgp
      361 gakgdrggdr p
//
LOCUS       WP_457682505             839 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457682505
VERSION     WP_457682505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 839)
  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   3  (residues 1 to 839)
  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   4  (residues 1 to 839)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..839
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=89067
     Region          14..255
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          249..680
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          691..804
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mcasqsgrls gdgvfdltrt avvmadragv aqgwtkgaer llgyavseav grplaelfag
       61 vapaasqdnr wesrlaaadg wsgleavrhk dghrldlefr vlpvldater sarlvlaaem
      121 tqtpwsgasq sflegilgms pigvamvnad lefvwlndal ermggtsreq rlgkrladiq
      181 pglavealea emrkvlstgt psvgyeylgr pqsdpereha ystsffrled eagqvlgvcy
      241 mvldvtesyr arqrmallnk agerigssld vwqtaqelad aavpdladfv tvdlldallc
      301 geeptpgpvd aadlvtmrra gqqsvregcp eavvavgeat ayppsapvvl slvegnsalf
      361 qtldlaaggw aaddpvraah lrelgfhslm vvplrargvf lgaatfarwq htgpfqpddl
      421 vlaeefvtra aisidnarry trehnaaltl qhsllphdlp eqcaveaayr ylpadslsgv
      481 ggdwfdvipl sgarvalvvg dvvghgvhaa atmgrlraav qaladldlsp eevlahlddm
      541 lnrvahdana ddgvigatcl yavydpvgcr ctlaraghpa pllisptgng rllelptgpp
      601 lglggmpfes velplpegsl lalytnglll gkaldldggi trlrtalaap qapledlcdt
      661 vigglpggrp vddvalllar tralapsqla tweipadpsa vgqarrsaag rlaewdleel
      721 efstelivse lvtnairhas gpislrmira ralicevsds sstsphlrha rttdeggrgl
      781 fliaryaerw gtrytpqgki iwaeqplrsa avagpandls alldglddpa apftgaegr
//
LOCUS       WP_457682501             290 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682501
VERSION     WP_457682501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30614
     Region          52..166
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mklrwsrtlp llpalalalg vtttpaaaee asrhssssav ssgwnnysck psaahprpvi
       61 lvhgtlgnsi dnwlglapyl vargycvfsl dygqlpgvpf fhglgavdas arqlaayvdr
      121 vlaatgtrka dlvghsqggm msrvylkfhg gadkvntlvg lapdnhgtdl ngltrlldhf
      181 pgakkylhel tpgladqiag sdilnrlneg gdtlpgvryt viatkydevv tpyrsafldg
      241 pdvrnvvlqd lcaidlsehv aiglidrvaf hetanaldpa hatattclsg
//
LOCUS       WP_457682511             604 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682511
VERSION     WP_457682511.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 604)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 604)
  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 604)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64882
     Region          36..599
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mftslrparr sdaldsddal dtepaeepee plrvglrdll rvtrghrkai avalvfslia
       61 aglglaqpml atktiqefsg grpyltlavl lgvlfvveav vagvasysle rsseglvlgl
      121 rlriidkllr lpmrryesqr lgdslsrtts dttmlrdsla ydlsevvvgl fvvvggvamm
      181 vwldaalfli vlaivgvigg ltllllagir kavedaqdsl ggmsadlera lsairtvrvm
      241 raedrereri gqlarqayqq nlqaakrdav igpmmtlamh gsmmvvlvig girvasgegs
      301 ladlvgflly ityisapian mfdvmatvqr glaalqriee vtqlpgeads tpatapaagp
      361 aavptaegtt pavefrevtf sydadrpvlr qvsftaprht hvalvgpsga gkstlfalla
      421 rfydadegqi lldgiditrq msidecrskm slveqtapvm hgtlrdnity acpeatdeqi
      481 qrvvelasln dlvrrlpegl dtavgehgdm lsggerqria iarallprps lllldeptsq
      541 ldaaneealt raiaqisrec tllviahras tiraadtvia ldngrvtdtg tpeeitarra
      601 fafd
//
LOCUS       WP_457682516            1229 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682516
VERSION     WP_457682516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1229)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1229)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1229
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=136231
     Region          311..1169
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 msepsgavad fcsvlrrlvr gcdvqqtela ralhrsnatv sellngrrat ppslddvlli
       61 vshcrarveg hpppglsldp awwrtrlael edtaearrqr pepraekprp rvesvafdfa
      121 gavdvliggr dgfdgladel leplqlngga avelrglmdg fgarvraghg ttrtallcaa
      181 dvvllvtafc davagsgigh stqlsqgagd ittevlqelg ridlgsarvr dtaelreeis
      241 aayssateiv hglgnahghp phdliqqakr ryeqllssat wdcpelrlts etydvdredg
      301 qprtgaggvg lhrlglllee fahgctapag rrerlrapia saegsgpaip tlaagyvnph
      361 frvaahpvdw elssdewwqr qplrddievf laahlltdra trapllvlgh pgagkslltk
      421 liearlpete ffclrvelrh vpadmdvqgq meealfratg rrtewpdavd pasgavrvvl
      481 ldgfdellqa gaerldmrrr wdylksierf qqretelgrp taivvtsrtv vadqvftpta
      541 stvirlepfd ddqiadwlei wavtnrrhfl aeglepltqd vvrphrelas qpllllmlal
      601 ydavgnplrr lggqgierve lyerllvefv rrqvvkhrgp lpraaeadav eqelhrlgvi
      661 aigmfnrrgq simareadad laalrgegss pllfgrfffv heaqavvteg elrsyeflha
      721 tfgeylvvrl igdelrrtlg egddqgwsqa ddgrlhalls cvpltdraev vriagerlsl
      781 ieteqraslt vllrelfrra hwgsdhrkdv pyrpvtrnrt erdavysanl lllavlaedg
      841 vnaseffeeg dpvdrwwrca qlwrsqfsea sweaftrtls lerrtldgrl drtwdlrigt
      901 revapgtsdl awslrmpswg ptayhdtkgv daadlirrms flcetdgqql lhalspllhr
      961 lpdsmrtyri hddqsglsaa halvslmcrd pghpddwdrr yhdvlsvlpy lpfedcapvv
     1021 dvlarhlvhd aarlpgdtvv qilhgltqpr fadtsqvpaq twiallgcvq dqvgraavpq
     1081 delgklagrl gtctvfalen eeapqlrlls llreagsthi whrtghapgr ealddgfavl
     1141 eripvaersp evvigllrla relgrddwla ehaepmllsl gieglgrlra tdvdslrdrv
     1201 rdtalrtalg siervwrgvs edgrppssg
//
LOCUS       WP_457682517             458 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682517
VERSION     WP_457682517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50094
     Region          1..346
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtldiprira rvagllaeya ipsaaigvlh dgeltefavg vrnvetrepv ttdtvyqcgs
       61 mtktwtalaf mqlvdegkvg ldepvrtylp gfavadpeas aqvtprhlln htngieeayg
      121 dpgededvya rmveniadap qvfppghthg ysaalgyail arilevhdga hwddimrhrl
      181 fdpmgltstn swheqvdear aatghlirsl eegplvtpvr hlprafgpgg nltstsrevl
      241 amahvflnkg tapngkrivs aesiqemlns rvpvpdpymf gpawalgliv cdwqgetvya
      301 tdgstvgqna rlrilpdsnt alalltnggp resfshavfn eiltdlgmvt vpdlpapdtt
      361 lnldlsryeg vygrpgarye vaaddgklyl tlfldpmqaa flhkpdriry ellpvsethf
      421 lmppadpled tqtvalydft ngsaqylhtn crvhprqr
//
LOCUS       WP_457682543             310 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682543
VERSION     WP_457682543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33270
     Region          100..202
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mqalpflsap lliarlvatp lrcvrllptr asslplrstv vdlavlaghl llyptgisqe
       61 rplprpaphp aaeppegftt peapqpapga ptmlptegra hppvlllhgf idnrsvflll
      121 rrslhrhgwr hvealnyspl tcdlrkaael lsrhveevca rtghrrvdlv ghslggliar
      181 yyvqrlggdt rvrtvitlgt phagtriapl msahplvrqm rpdseviael srpapncrtq
      241 fvafwseedq vmvpattari shpdliaynv hvagvghlal pvngavaagi realtsaeta
      301 egaadaisva
//
LOCUS       WP_457682547             276 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457682547
VERSION     WP_457682547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27693
     Region          <215..270
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mthtaaapdt slrsavhawv dgwarargte apqavpggfr ievrrpghla rhvlseaepa
       61 vlrdlvdtlt tpglwikaca prevvepllt adweisepqy lmttdrlaas rsgaglpsgy
      121 rleivdegge vfearvhavg gpgagagags ccgaeagags csgsgtgsgs gtgsgsggae
      181 grgpvlaasg raalttgapg sspapyapsv vfdmigtepa hqrrglgrav maalagrave
      241 rgarqgvlva spdgralyea mgwrlrspvt aagrmg
//
LOCUS       WP_457682549             478 aa            linear   BCT 27-JAN-2026
DEFINITION  PspC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682549
VERSION     WP_457682549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Joly,N., Engl,C., Jovanovic,G., Huvet,M., Toni,T., Sheng,X.,
            Stumpf,M.P. and Buck,M.
  TITLE     Managing membrane stress: the phage shock protein (Psp) response,
            from molecular mechanisms to physiology
  JOURNAL   FEMS Microbiol Rev 34 (5), 797-827 (2010)
   PUBMED   20636484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..478
                     /product="PspC domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49186
     Region          23..83
                     /region_name="PspC"
                     /note="Phage shock protein PspC (stress-responsive
                     transcriptional regulator) [Transcription, Signal
                     transduction mechanisms]; COG1983"
                     /db_xref="CDD:441586"
ORIGIN      
        1 mndaahvees apsdpagsap shpplrrsrr hkviggvcgg lgrqwdldpv ifrvvlavls
       61 vgglgliayg fawllipldg edenegrrll sgrvegpalt alllaligcg lflttlakgs
      121 mmsfaimltl aaagsahwsr rrrqveaegp qardtataqa vadappetka ppvpagpsww
      181 raqrgeaagp gylwgpdttp lpldityrae hgvatapygh dgrsdagrpp gapvppggap
      241 pardprrgrr sgrpiggwtf llallagcgt alavsrhdgp vpalqaglac alvvfglglv
      301 lsawfgrtgg gtvfmvvlta lllagattlp dnltaqwqkr twspttlsav qpqyelgsge
      361 geldltalpl kpsstvhtga evgagrlqvt lphgvtarlh islglgdvql pgesphdvdl
      421 taggqrtvtl padglkkgek prgsvelnle lgagqvaier aapapaapaa pttqgahr
//
LOCUS       WP_457682551             679 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682551
VERSION     WP_457682551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..679
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72080
     Region          269..668
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mgdggssgrp dtawpadadg salaaavgav larldahatr trttvrgnaa gdggaagpps
       61 aapaprpqed aalspgralp aldalaacfg lspferevil lgaaaeldpt agarcaaass
      121 dpghayptfs lalaalgaph wsaltpvapl rrwrlveldd etrlttsrlr lderilhflv
      181 gspyldarlh gllrrttapa tlpasydaaa drvaagwada gpdaplrvel vggdlrtrad
      241 iaataarrtg lglysmaadd vpadaaerdr larlwqreai llpaalliev geldreqhaa
      301 adsfiagsav plvvsgpdpr qtghprgqrv tvpklndeeq vglwtdafad vpevtardvq
      361 alvaqfqlpp hvvrsaaatv rrelsdpggp dgpdaaglaw qagltearmg ldelgrriep
      421 ragwedlvla grqlgilqei vahvrqrgtv yqdwgfakal rsglgvtalf aggsgtgktl
      481 aaevmakelg ldlfiidlsq vvskyigete knlsrvfdaa erggalllfd eadalfgkrs
      541 evkdshdrya nlevsyllmr meayrglavl ttnmkkalds afmrrirfvv dfpfpgeker
      601 aeiwrrvlpa qaptkgidts llaqltvagg sirnialsga flaaeegdrl rmrhmlaaar
      661 teylklersl tpsevhgwv
//
LOCUS       WP_457682560             973 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682560
VERSION     WP_457682560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 973)
  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 973)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Rosinski,J.A. 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 973)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..973
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=103526
     Region          <15..917
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          902..956
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtfahsrdac gddwplvgre relaamdava advlsggprv vqlegsagig ksallstwwd
       61 rnaqfrvlra rchplerefa fgavrqlfkp llaavsdtdr arllegsaaa tlralddaav
      121 pdpppeaanv taatlrelda lvsrlsrrqp lllavdalqw idqpslrwlv hfvgradsds
      181 lpvliavttr saegrrldpl caelvrpanc htlvvepldv dgvgqlvrtl wgaeepdeaf
      241 caachaatgg hplfvrallh qaqrsgvkpt tefrdriptv tlstlggeis hrlcqasdev
      301 valaralafl gdrkppella aycgtgravv qsaagelrsl gllradgnpr fthpvvrdtv
      361 latlspeelg vgharaaqvs clsgrpdeev aahllaagpv hgswvlpalr raatealrrg
      421 apetavtylr salhqpldes erarvllelg taashydaal aiscvtgale gltdeaarsd
      481 algvlaysll lsrgsrtdls svdrkiaals erptsgtgaa drelalrmsa lrswmeferp
      541 svtgpapaps pgadddladr tagerqllai rafhalraal papyvaalie rasvnlpafs
      601 hdlfplhyfv aqtllyldel dtadrlnrhl treisgrgme llvssltvyr avlalrrgni
      661 aealgaaqda adhasptgrl pyaltvdtir idallaqgrv eaaeriaath avagqtevaw
      721 erprflmsla alriaqgelr tglsllresg hhcealgtvs pamspwrsra vavhlalgdp
      781 gaaralaeqe ldlarrcrip ralgvalrat gtvtdglrgl dmlaeavtvl rttparlela
      841 rachdfgval lrrddkrgar galrdgldla vgcgatalav rleerlhlag grvarsgsqg
      901 irgltageer vctlaaqgys nkqiaellvv slrtvethlt gayrklgitg rpqlaaamat
      961 tdrcrggsep ads
//
LOCUS       WP_457682565             467 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682565
VERSION     WP_457682565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..467
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50467
     Region          191..464
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtyvsadras gptrrttltg lvggagalla agcsaspaaa ptarrtaray asasdptpgv
       61 mtlfkdpafn fngllalggs gygasevgev ltavntinka glsaqtytet fknlgdqlrk
      121 ppssgepgte ttrfralraa qyyaqalffv lgsdtpgtee elykagrgsw dafcercdpv
      181 pvtaripygk tplpvwffrp dssgerrptv iltngsdgqd vdmwtygvaa alqrgwnalv
      241 ydgpgqgqll fvdqvvftpr wetvvtpivd wltarpdvds rkvgltglsm agdlapraaa
      301 fehriaalva mpgvlspwlg fppeireilt pdkektnniw nkevvpelpp saaatmkkrf
      361 epfsvpamla arqgkmftdf ytpatliksl ditdvvgrik mptlvldydf eqfypgqprq
      421 lfdkltapkd yvkltaatga qlhcspmapq qhcevvfdwl qeklsgr
//
LOCUS       WP_457682563             336 aa            linear   BCT 27-JAN-2026
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682563
VERSION     WP_457682563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35347
     Region          21..>237
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 msgqlterag ragpqalpal rivapeiegp edvvadadgn lfagaadgti wrlrlpapda
       61 agratavaht ggrplglqpl pgggllvcda rrgllridpr hgtvrvlade vdgaplrfcs
      121 nvttavdgtv yftvssrryg ldewlgdfle htgtgqllrl rpdgtpevll eglqfangva
      181 lapdesflvv aetgarrlsr yrltgpragt adtlaadlpg ypdnisrgpe gefwvalarp
      241 paagvellhg mprgvrraaw evskrlrlsl pphptarvla vrpdggtvrd lravrspyrm
      301 vtsvcrterl lamgsvaerg iavcalpgad gtasah
//
LOCUS       WP_457682575             342 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682575
VERSION     WP_457682575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33590
     Region          17..321
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mgepagrgpd tlgaghvlgv dsggsglria varaddaear plavrasdep vrtgpagida
       61 ehllsqllpa aaelaretga dgfaavcvga agmatlgeel rarlpdalat afgvrrlala
      121 adavtayaga lgqrpgavia agtgmialgt dltpaggwrr adgwghllgd cgggawigra
      181 gleaalrayd grpggsaall araeavfgpv tglpgalypr pdrpavlasf apevarcaae
      241 ddtvalgvlr aaaghiadaa aavcppgagt tvactgglfh mgepllaplr talaellpda
      301 rtaaaagspl dgslaiaaal ardrltlptd rkllqitrpa pg
//
LOCUS       WP_457682576             247 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457682576
VERSION     WP_457682576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26085
     Region          7..121
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          135..243
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 malrpvqvni kaldastvgr fwaealgwsa yspgvttyvg paggpvwpdp vavgidavpv
       61 pepktatknr vhldlattsa ahqaelvarl qalgatpadv gqgsvpwtvl adpegnefcv
      121 lepreiyrdt gpiaavvvdc adpramarfw geamdwtphe vtddqavlrs akgagpylef
      181 lrtpgvqtvp drvhldllpy pgddkaaeva rlralgatdl dlgqgdvpwt cladpeghef
      241 cvlapsp
//
LOCUS       WP_457682582             462 aa            linear   BCT 27-JAN-2026
DEFINITION  carotenoid oxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682582
VERSION     WP_457682582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..462
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50458
     Region          6..448
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtgnrylsga ftpvteeita ydlpvtgrlp ahlngrylrn gpnplgieda athlwtlgag
       61 mvhgvrirdg raewyrnrwv rstavadrlg eprlgtpvde lmdispnvqv vglagrtfal
      121 ieggirpyel tydldtigpc algatpqgys anahslfdpr trelhslafr ygsdqvqhiv
      181 mdesgvvlra taievpgnpy mhdfaltdrh vllfdspvvf saahlptgip fvwdgnrpar
      241 vgvmpragga vrwfevapsl vghtlnayed gsevvidvvr hpegfdirdv gtsrptldrw
      301 tvdltagklr edrlddrvqe fprlnsrysg rpyrygytaa velyappagp gdtrpdegfs
      361 nallkhdllr gtseahefgr ygavsegvfv pagspnaedd gyvmayvfdp ergatdlvll
      421 saldftgepi arihlpvcvp lglhgswvpg derevpryal ag
//
LOCUS       WP_457682580             252 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682580
VERSION     WP_457682580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26473
     Region          17..216
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mstspaspvt svppapvifd ldgtlvdsep nyyeagrrll adhgvpdfsw ehhtrfigig
       61 tretletlrr efgldapvee llagknrayl elarahtevf pemrvfverl saaghpmava
      121 sgssraaiea vlagtgldal lttvvsaeev ahgkpepdvf leaarrlgva padcvvleda
      181 apgalaahra gmrciavpyv agtvddpafa ragllfkggq geftaqaahd wlrrggtaav
      241 eerpcrggra gs
//
LOCUS       WP_457682585             666 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-galactosidase [Streptomyces nigrescens].
ACCESSION   WP_457682585
VERSION     WP_457682585.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..666
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72836
     Region          1..609
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          601..665
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mgihfggdyn peqwpeevwa edlklmkaar vtlvtagifs wakveprpga wdfgwfdrvm
       61 dglagagiav clatmtaspp pwlsrahpei lpedadgrrr wpgarqhycp sspvyrahav
      121 rlveqlapry aghpalamwh igneygchtr hcycevsadd frrwlreryg svdalnaaws
      181 tafwsqaygd fdevlpprta ptfpnpaqql dylrfgdeal racylaekav lervtpgipa
      241 ttnlmpqhkp vdafawsshm damaldfyqd phvpddhvra gyvfdlmrsa rsgqpwmlle
      301 qapgavnwrp rngpkppgam rlwswqavaq gadavlffqw rqslggaekf hsamlphggt
      361 dtrvfrevsd lgrelasvpg iegtrsragv alladwhsww aleldskpst aldhsriald
      421 hyrplfeagv acdvlppqrd lsgyrlvvap nlyllttrda erlaayvrdg gqllvsffsg
      481 ivdahdrvhp ggypaplral lglrvaefwp leagrsvavd gdyagqadlw sealdlegae
      541 alahftdgel agrpavtrhs ygrgtvwyva trlepalmra lldevraaag vepvlpglpa
      601 gvqatvrega ggrylfllnh gteatevglp aplrdalaar gtagagagav dritlgargv
      661 avltrp
//
LOCUS       WP_457682592             240 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457682592
VERSION     WP_457682592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  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 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   Rosinski,J.A. 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 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 13297907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..240
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24857
     Region          <79..204
                     /region_name="PRK10403"
                     /note="nitrate/nitrite response regulator protein NarP"
                     /db_xref="CDD:182431"
     Region          <145..217
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mgvrlmvvdd hrllaealas alklrghrvl aaaapsagaa elvvsrapev cllgtaapar
       61 pgafdpvvri kkerpqvavv vlgpvpsprg iaaafaagas gyvrnderie gverammkar
      121 agesavspql lqqafeellh paaqpddega rllelltpre vevlmrvadg edtrliaagm
      181 diapstarth vqrvlmklev gsrleaaala artglldrag grgargaaga gpdepvlppr
//
LOCUS       WP_457682598             599 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457682598
VERSION     WP_457682598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..599
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66266
     Region          8..507
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          537..597
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mavnlvnlea vgkvygtral ldgvslgvne gdrigvvgrn gdgkttliri lakledadng
       61 rvthngglrl gvltqhdsld paatirhevi gdladhewag nakirdvltg lfgdlhlpgf
      121 iqgldtvigp lsggerrria laklliaeqd livldeptnh ldvegiswla ghlrarrsal
      181 vvvthdrwfl dqvctrmwdv qrgdvheyeg gysdyvfara ereriaatee akrqnlmrke
      241 lawlrrgapa rtskprfrie aaneliadvp pprdnaelmk fassrlgktv feledvsvqa
      301 gpkillkhlt wqlgpgdrig lvgvngagkt sllralaeat rtqgevqpma grivvgktvk
      361 laylsqevge lpptlrvlea vqqvrervdl gkgremtagq lcekfgftke kqwtpvgdls
      421 ggerrrlqil rllmdepnvl fldeptndld ietltqledl ldgwpgsliv ishdryfier
      481 ttdrvhallg datlrmlprg ldeyldrrrq vieaatpapa pqttapkkaa avnraaqkel
      541 qkierqldkl gdketklhaq iaenatdfek vagldaqlre lsaekdelem rwlelaeea
//
LOCUS       WP_457682600             493 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682600
VERSION     WP_457682600.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..493
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53639
     Region          91..>301
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          391..486
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mgltasagvv alagsllvps sagaspgggk apvrsiqwsa cpkaeppfpa pskrtrcgtl
       61 evpvdwakpd gptmkiavar qkatdpkkrl gvllsnpggp gstglddayf adnpvegyrd
      121 sirsrfdiig fdprgigrsg qlrcddklaa kiphrpksaa efqrmrtlnq rlaescrags
      181 gavvdhmdsv svardmdair aalgekkinf lghsygtlig rqyarlfpqk lralaldsam
      241 dpsrpdaerf lrdgsravdd avrqladwca kdkscalkgr dvpalvrglf aradadrlfe
      301 pgrhgptrkk vtadqltdfl tsylmkwnpq ttaeqlsaln sgrgevswta gsvniawrsv
      361 mcrdydfrlr gwdqyrelrq rarsdapiar ynsqaldmil gcqgwpaape peparakgpl
      421 ppvlvvnagh dlatplagar rmarefpqgr lavldavdhw lyrkcqsplp aravdtylrt
      481 lktppdgtvy prr
//
LOCUS       WP_457682624             539 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682624
VERSION     WP_457682624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57572
     Region          194..>328
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          413..505
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mlisgriagr rrgaavltav vtcstvltgp dlavaggpps ppasapqlew kpcvrgkafd
       61 catakvpldy rdpggrtiel avvkrkatgp grrlgtlffn pggpggpgtv qmpqnyrffp
      121 revrerfdiv swdtrgvghs tavncfarpg daaaweaskp agfpvgaqer ktwiaafedl
      181 arrcrqrdpe llrhmstadi ahdldrlrra vgdtqltylg tsygsflgat yanlfpgkvr
      241 alavdstidp qawtdhasht aprrpiflrm gadlgaaail drflalcgat ttarcafsag
      301 spkatrdkfd rltrrlrehp vgtwtygktv ddvvsgldiv hpgwtdlagr lqdlwrgrvp
      361 rpptplpapp vpnpytgveq asailcsdsp nprdpgvyha leeasalrag dtgrfwtwaa
      421 epcatwpvaa dryrgpwnrp tahpvlvigt vydpatpysg aqamtkelah arllthhgyg
      481 htallnpssc ikeyesryfv dgtlppagav crpdtppfsa pgpsggvatg ggamagpvs
//
LOCUS       WP_457682620             595 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c biogenesis protein ResB [Streptomyces nigrescens].
ACCESSION   WP_457682620
VERSION     WP_457682620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Dreyfuss,B.W., Hamel,P.P., Nakamoto,S.S. and Merchant,S.
  TITLE     Functional analysis of a divergent system II protein, Ccs1,
            involved in c-type cytochrome biogenesis
  JOURNAL   J Biol Chem 278 (4), 2604-2613 (2003)
   PUBMED   12427747
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Le Brun,N.E., Bengtsson,J. and Hederstedt,L.
  TITLE     Genes required for cytochrome c synthesis in Bacillus subtilis
  JOURNAL   Mol Microbiol 36 (3), 638-650 (2000)
   PUBMED   10844653
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Inoue,K., Dreyfuss,B.W., Kindle,K.L., Stern,D.B., Merchant,S. and
            Sodeinde,O.A.
  TITLE     Ccs1, a nuclear gene required for the post-translational assembly
            of chloroplast c-type cytochromes
  JOURNAL   J Biol Chem 272 (50), 31747-31754 (1997)
   PUBMED   9395519
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..595
                     /gene="resB"
     Protein         1..595
                     /product="cytochrome c biogenesis protein ResB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=63691
     Region          39..531
                     /region_name="ResB"
                     /note="Cytochrome c biogenesis protein ResB [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG1333"
                     /db_xref="CDD:440944"
ORIGIN      
        1 mstktgtprd egpaadtgsd lgaagsqlst aptedvtlps lgplgwarwf wrqltsmrva
       61 llllfllsvg aipgslipqt sidpvkvdqf ksehttladi ydklgmfhvy ssvwfsaiyl
      121 llfisligci vprswqfvgq lrgrppaapr rltrlpaytt wrtdaapeev lgaaqrllkk
      181 rrfrahldgt avaaekgylr evgnlvfhla livmlvafav gslwkseggk litegdgfan
      241 sltqyddfks gaffdtdtle pfgftlnkfe atyersgpqk gtprifrahi tyfsgadgke
      301 hktaievntp ldiagskvyl lshgyspevt vkdgrgkvvy kgavpflpqd pknftstgvv
      361 kvpgaqtedg krnqlgfqgf fvptfggkgs gsmfsqfpal dypvltltay hgdlgvgsgl
      421 pqnvyqldkk rlkqykdkgr pvakmmlpge tmklpngdgs iqftgikswa sfkishqpgn
      481 glaltgaaaa lvglagslfi qrrrvwvrae adadghtvve laglgrsesa rlpeelaela
      541 lalepdapla patgddgpap dpkpgpapdt gtdsedpaep tdsdgpadps egara
//
LOCUS       WP_457682636             222 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682636
VERSION     WP_457682636.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23654
     Region          6..217
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mryglvifdn dgvlvdsepv snriladylt elghpttyed slrdymggam hrihevvler
       61 sgkwlpagfd esfharvfee frrslepvag vgevlgklda dgvpycvgss gsherirval
      121 tktglwerfa gagsaagari fssqdvgrgk papdlflyaa qemgvaperc avvedsplgv
      181 raavaagmdv ygftamtsae klaeagatal faqmaelpal lq
//
LOCUS       WP_457682642             470 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682642
VERSION     WP_457682642.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=51171
     Region          12..468
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnakifapds vrtlsefehd alriaqvlge rgvgpgdrvm lkagnsaawv atllglmhig
       61 asivlidqqe haeqtrkiil rtgtklvlsd edspldssqe avhlyellvs aagrqiadep
      121 ltvdawcelp dglimwtsgs tgtpkgvvks grkflknler naaqvghred dvllpllpfa
      181 hqyglsmvli awlkrcslvi apykrldral lmaeesgatv idappssyrs mlnlvsrkps
      241 lrpglerarm fcvgaapldd plvgqyaaef grplldsygs telgniafat pdnpvacgqa
      301 mdgiqvrvvd dagravpage pgevevntpd alegylaedg tlqpspqgwq rtgdlgclda
      361 dgnlfvlgrk yavhrmgytl ypeliersva aqgcsariva lpderrgaql vffveddqgq
      421 edaywrerlc gmlaayehpd rvvvldhfpl nrngkpdkrq lehlarahgr
//
LOCUS       WP_457682632             412 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682632
VERSION     WP_457682632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42548
     Region          15..392
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,142,
                     145..146,149,222,225..226,229..231,234,262,266,315..316,
                     320,324,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtaprvpgaq prhgraalal sffiqgavfa llvtripaiq drygisdgll paflaavpvl
       61 agvgsvvter lvrrvrpslv lravqpvvcl alaavgsvgs maqaavalav fgltvgalda
      121 smnmlgvslq raygrsimlg fhaayslggi vgaslawaga hwklslally gpavavlapl
      181 allvgrwfvd rgrraqegre eapagavgpl amrlllplcl vmafayigds tvsnwsakyl
      241 qdvlgsseql atlpynvymv ttllgravgd lgvrrfgava vvragavvaa ggfavvaaap
      301 gpwagmagft llglglcvlv pqtfaaagry ayekhgpeaa dmavarlnif nyvgfligsp
      361 lvgalgdaws yrgamlvpma lvlvtllyar sfgapearyg dgherprtad vg
//
LOCUS       WP_457682650             338 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457682650
VERSION     WP_457682650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 338)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36901
     Region          260..332
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrirftled lartrvallg plaetqlslr mlqrreekvl fdgwrrrtrp rvppdarqla
       61 afvaspqgwm vdlftllgpv ssieegrerl lsapraqlra elspdarldr lrpswlshpg
      121 agdgavverl angladyhva svapywdrih qhlsahahlv gklmaahgvg aaleslapyl
      181 rwkppvlelp dyrpwqgpdd ygyhlggrgm vlapslfcgp vpqlfapatd aeslliypap
      241 rdpatirsiw spprpvashk alaallgttr aailatlvdg ytttdlarrl sispssasqh
      301 tgvlrqaglv sttrhrntvh htitpqgral ldgtsttp
//
LOCUS       WP_457682654             358 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682654
VERSION     WP_457682654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36872
     Region          63..348
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mstatgtpta sadttaspat taspiadrda attaataada lrgatttaap targrargwq
       61 frfavlslvw gfsflfikvg tqgfaplqvt lgrvafgalv llavlvvkre rlprsartwa
      121 hltvaaflln alpfslfaya eltipstlag icnatsplwg malsvvalse drptrrrvag
      181 lglgflgvlt vlgawqgfag tdltgtvmal gaslcypigw iyvrrtlagv phshlsmsga
      241 qlllataqla vvtplfttap tsypiiplla vfalgalgtg lafliqyglv aeigpttaqm
      301 vtyfipviat aagvallheq lswntpvgal ivlagaaltq srprpsrpav pptgstth
//
LOCUS       WP_457682656             221 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682656
VERSION     WP_457682656.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23354
     Region          25..172
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mtraesyept arttptrard raaydhetvh aildagyvch lgfvrdgspv vlptlygrvg
       61 drlylhgstg srplrmagaa pdpglevcvt vthvdglvla rsafhhsiny rsvvvhgtah
      121 qvtdeeekta aldalvdhvl pgraadsrpg nakelaatsv irlglreasa kirsggpnde
      181 pedlglpyws gvlpvapvyg apipsddlap gtpepaylsa r
//
LOCUS       WP_457682657             327 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682657
VERSION     WP_457682657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32256
     Region          40..313
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mhatpssalp vgrgllyvtl aatawgtaga aaallyrgsg lgplaltfwr tfgglvllla
       61 vrallrrrsg tvavpapapy eplrrrlpri vmtgvalavf qaayfaavea tglavgtvvt
      121 mgagpvliai garvtmgerl gaggvlavag alaglavlvl ggdggttvrp agigyallsa
      181 agcaamtlit rrlgkgggsd pyastvsafa vgalcllpla vveglwpqah dlgrslwllv
      241 yiaavptala yglyfaglaa vraatasvis liepvsaaai avlflgerlt mataigtgvl
      301 ltavaalavt eargavtaar taapvag
//
LOCUS       WP_457682659             388 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682659
VERSION     WP_457682659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38215
     Region          43..343
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mhassgspag tstgsgqgis gslggrqssp algvrrlrvp ggrgaglgia llsalafggs
       61 gvaakplisa gleplqvtwl rvagaalvml piawrhrglv rrrpallagy gllavagvqa
      121 cyfaalsrip vgvallieyl apalvlgwvr fvqkrpvtra aavgvvlavg glacvvevws
      181 glsfdavgla lalgaaccqv gyfvlsdhgs dgddavdplg viayglltga vlltviarpw
      241 gmdwavlggg admngtqvpa vlllawivli atvaayltgv vsirrlspqv agvvacleav
      301 iatvlawvll gehlsapqiv ggavvlagaf iaqsakpkat etvrvagagt gtgdgagapg
      361 gsgspetpat pasaprtgdd lsagscat
//
LOCUS       WP_457682668             375 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457682668
VERSION     WP_457682668.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39839
     Region          148..371
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrlgtaaava aitvigagaa avavgryasd ialkpspdqp fpgdsrltvh sateerialt
       61 rslaslrpgt ygltgsgcha vigdvvhgvp hpadavvrrl vrvthgtlgp gnrmlltpqv
      121 hignprdalg ldcadvdipg elgplpawfv pgvrdtwvit ahglgatreh pmvvmpflhr
      181 hrlpvlalsy rndpgaprta dginhlgdte wrdldaairy alrygahdvv lhgwstgatm
      241 alraathsal rdrisglvld spvldrnatv ralagarrip rallplvvra aegstglpld
      301 hpayavdpde leiptllfhg pddriapwta srsfaarrad lvtlqpvpha phaamwnadp
      361 sgyeealrrf ltplm
//
LOCUS       WP_457682682             470 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682682
VERSION     WP_457682682.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51781
     Region          119..417
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mtdpqtstgp qaptgpqapt gpqvsidlqv ptnpqaptdr pdsrpgphep yliissdcha
       61 glpteeyrpy ldarfhrafd aflgerdarr aeatrlgirn dafaarwfqe heeglrggwd
      121 paqrlkeldg dgvaaevvfp dadavdsgta apfgvglgls gdhdpdlgma gaqahnrwla
      181 dfvsghperh cgvallpvta dtdrvvaeih rakesglgal mipsmwggke pyhdrrydpv
      241 waaaaecamp vlthsgaapr heygdhlgiy vsevtwwpar plwfllwsgv ferhpglrfg
      301 iaesgcwwlp nllwfmdrly lgahggkkls pfaalkrpph eyldrqvfvc atntkrrela
      361 qryeigvgni lwgsdfphpe gtwpdtrgwl kktfhdipva etrrmlglsa aeafgfdtar
      421 laplarrigp tpaelgqsad qpsveaswar srevgrhwlt dhdfpvlgaq
//
LOCUS       WP_457682691             439 aa            linear   BCT 27-JAN-2026
DEFINITION  CynX/NimT family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682691
VERSION     WP_457682691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44195
     Region          52..431
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(62..63,66..67,70,102,152..153,155..157,160,179,
                     182..183,186,263,266..267,270..272,275,302,306,355,359,
                     363,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 madddlatlg paagprttst dpadgpqqpq pgpghgapaa gpagrwlprl viaglvlaal
       61 nlrpaitslg alleevragl gmsgtvagll tsvpalcfaa fgiaaprlar rwgpgaivca
      121 gmaaitvgvv arpylggtgg flaasalala giavsnvlmp vvikswfpgr vgsmtglysm
      181 alalgtslaa altvpmteal ggswrtglav wgalaavavl pwlvvvrqrr alagadasta
      241 arppeapvri tssptawala vffglqataa yitmgwmpqi frdagvsagt agvllavtma
      301 mgvplsfvlp rlatrmrhqg plvvllglcg lagytglwla paagawawal lmgisncafp
      361 laltmigmrs tssagvvkls afaqsvgyli sipgpllvgt lyqhsggwgl pialmaglmv
      421 pqiavgvlag rdrriedea
//
LOCUS       WP_457682697             505 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682697
VERSION     WP_457682697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..505
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53239
     Region          25..495
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag mgamaaaarl avaghrvavf erdathggav rrlardgftf dtgpgllhlp
       61 avyrdlflkt greplescie ltqvdpaarh vfadgtavsl pnasragvla aldealgtgs
      121 gerwselvgr areawdatrr plleeplwtd wrvlgrdpyp avrrrglfgr gkgpttatla
      181 evarreladp rliallesha laygfdprsa pasavvlpym eqtfgswypr ggmraladal
      241 yercvarkve fsfgaavtgi vekdgraagv eladgrvsea efvvagvdpv rlvelcrgre
      301 pwgaddvrpa lgpgdratgr ltvclalrga rpgdaahrtv vhaadrtael agvfgdgsgl
      361 rtpcdrptvt vlrpddpatr pdeaheavtl tatvaphgpv drqdgeavaa daermveiae
      421 aavpglrerv lwrevlppte dalvpgpala gqegrflrpg nrtripglya vggwshpggg
      481 pahagmsgai vaglivngdd whgst
//
LOCUS       WP_457682709             257 aa            linear   BCT 27-JAN-2026
DEFINITION  TraR/DksA family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682709
VERSION     WP_457682709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26629
     Region          139..257
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvakktaaek sttpadeava kqpaakktap kkaaakktaa gkttpekata kkaapkraaa
       61 kktaakktvv kktaakkaak kapaktaavp akktgaktvv akktaaasvt ahgddsavpm
      121 arvaaapdel avrpgedpwt paevaearte lmeetsrlrl eivsaedaia glmrdsgdga
      181 gddeadtgsk nitrehelal asnaremlhq teralgrlda gtyglcencg npigkarmqa
      241 fpratlcvec kqqqerr
//
LOCUS       WP_457682714             432 aa            linear   BCT 27-JAN-2026
DEFINITION  NYN domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682714
VERSION     WP_457682714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45655
     Region          2..172
                     /region_name="LabA"
                     /note="NYN domain, predicted PIN-related RNAse, tRNA/rRNA
                     maturation [General function prediction only]; COG1432"
                     /db_xref="CDD:441041"
ORIGIN      
        1 mdrcvvlvda gyllgaaasl lageparsri tvdhaaliqg lrqraeaete rpllriywfd
       61 gapdrvpqpe hrrlrvmprv tvrlgaltrs dgrwaqkgvd aamhaeltel arnracsdiv
      121 lvtgdgdllp glmsakehgv avhlwavqaa dgdynqsedl vaeaderrvl drtwiiravr
      181 akelggpcap ppvprpeiaa ilsaplpesa aaaaaaaava aagpesaeht hehngangvs
      241 rpaavagngt aaggepgaag skvvptpkdl aglgrahaag qqpagtgpap aagatlrwss
      301 dkgwverggp agepdgtaal ptlaqltsae qrwadreedi tavsgdpfev gqvfarrwtd
      361 rlsdtahlqq lsteypriph ridgellrya arfgllahkd dqidehdrya iragfwrevd
      421 lrtaaehapa gd
//
LOCUS       WP_457682716             389 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682716
VERSION     WP_457682716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40463
     Region          49..276
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttrpddtpp dtpvpgappa saprpaatsl aelerraasr rgqpayghda liacdrlvrv
       61 fatdgvevqa lqgldllvae gelmalvgas gsgkstlmni lagldvptag aatvagrdll
      121 tmdakarlgy rrevvgfvwq qtarnllpyl taqqnvmlpm qlrggrrraa rakaaedlls
      181 mlsldhcgdr rphqlsggeq qrtaiavala ntpsvllade ptgeldshta eqvftafrta
      241 neelgttivi vthdqavase vrrtvairdg rtssevlrrt erdaatgqes lvareyamld
      301 ragrlqlpad ytsslgmahr vllelesdhi gvwpdhtadg aarggggaeg gggaegvseg
      361 adgsggsger ggtderggaa erggtdegg
//
LOCUS       WP_457682720             552 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682720
VERSION     WP_457682720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=55455
     Region          454..552
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mptcpsghqs vaedwcevcg qrmagavppp pslpagflnt pppgqptgqp gppqgqpgpp
       61 pgqpgpppgg pgpgfggpgg pdsqggqggy gfpppqqpgp gapgpgtqgg qggygfpppq
      121 pgpdsqggqg gygfpppqpq ppqggpgpsg qpetcpqcgt preamapfce gcrynfltns
      181 ptsyapppgq qpgpppgapg pgtqggqggy gfpppapgpq ggpqqggqgg ygfpppqpqp
      241 pqqqgmppgg pgpggfpdqp gpggfpdqpg pggfpdqpgp ggfppgpppg mpgpgpqggp
      301 ppqqggddwt lnppsaqaap ppmapappgp gpqapyeqqq ppapfppqqp gpyeqqppfe
      361 qqqppfeqqq qqppyeqqpg pyeqqqmppq qqpgpdqqwn ggpgqgpaap pqgpppvvga
      421 gwvvavapdr eyfmammgrs gpeaaglnlp syspeqvlpl ngqiavgrrr nstgespdid
      481 lgsapedpgv shqhallvqq qdgswavvdq nstngttinl aedpiqpyvp vplhegdrvh
      541 vgawttltvr rg
//
LOCUS       WP_457682733             556 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-L-fucosidase [Streptomyces nigrescens].
ACCESSION   WP_457682733
VERSION     WP_457682733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..556
                     /product="alpha-L-fucosidase"
                     /EC_number="3.2.1.51"
                     /GO_function="GO:0004560 - alpha-L-fucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60492
     Region          70..544
                     /region_name="AfuC"
                     /note="Alpha-L-fucosidase [Carbohydrate transport and
                     metabolism]; COG3669"
                     /db_xref="CDD:442886"
ORIGIN      
        1 malrstrrtl calvltaaaa lapvqsslar spsaalagpc drpvrpasqm avepcdtpar
       61 iidkaarivp tkgqlawqqr evtafthfgm ntftdrewgs gaedeklfrp sridagqwmr
      121 aykaagaeqv mltakhhdgf vlypsrytph svaaspgspd vvgayvkaar raglkvgiyl
      181 spsdgaelph awharwvaei rkkqqegipl slpervaled ggraprglgr fgngsevaer
      241 tiptlvpgdd raaavrsgal pafrvraddy dayylnqvye lftrygplde lwldganpws
      301 dagitqkyhv aewfrmihrl spdtvvfagp qgarwvgnen giaretewsv tpsaddpwtv
      361 magglpndst dpdigsrakl lapitkylqw ypaeadvslr pgwfhhpger pktpaqlmdl
      421 yeksvgrnas lllnvppard griaaedvas ltafgtavre tygrdlrtag pgpwtfdrig
      481 iaedirhgqr verftvrart ggawttlahg ttighrrilt lprpvtadav rvvveesrgp
      541 grvapvtlhr sraagg
//
LOCUS       WP_457682745             211 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682745
VERSION     WP_457682745.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23400
     Region          6..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprrrlapa errsqlldtg aqlfaakpyd evfmeeiaer agisrallyr yfpnkrdlfa
       61 avyqqaadrl ltrteldpar pvgeqlragl dahidyftan rntvlaanrv lagdpviqtv
      121 itdeltelrr rlldstglgd gpgepvsaal mgwlvfvrtl cvdwlthqaf srtelremcv
      181 gallgalrpv mdpdrlltgd eespadarpm p
//
LOCUS       WP_457682756             313 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457682756
VERSION     WP_457682756.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32150
     Region          1..284
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mttlrigllg tgpwarsvha palaahpgve ltgiwgrrpe aaaalaqvhg srpyeapdel
       61 fadcdavafa lppsvqapla vraaeagrhl lldkpvatsv pearaltdaa dragvasvvf
      121 ftarfgeqeg ewiaaqaaag gwftahadwl gsvfaddsss pyadspwrra kgglwdvgph
      181 alsvllpvlg daeavtatrg padtvlltmr hssgaastat vglaapaaaa gvevtlrgta
      241 gittlprrpg gpepayhrav dallaavgtg lpnacdvhfg lrvteilaaa egeaepahas
      301 rgmttwrnws wra
//
LOCUS       WP_457682774            1042 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-N-acetylglucosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457682774
VERSION     WP_457682774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 20657218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1042
                     /product="alpha-N-acetylglucosaminidase"
                     /EC_number="3.2.1.50"
                     /GO_function="GO:0004561 - alpha-N-acetylglucosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0030200 - heparan sulfate proteoglycan
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=111844
     Region          53..114
                     /region_name="NAGLU_N"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) N-terminal
                     domain; pfam12971"
                     /db_xref="CDD:463762"
     Region          135..455
                     /region_name="NAGLU"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel
                     domain; pfam05089"
                     /db_xref="CDD:461545"
     Region          463..723
                     /region_name="NAGLU_C"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) C-terminal
                     domain; pfam12972"
                     /db_xref="CDD:463763"
     Region          <731..1013
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mlgtagaiga gaafggaapa aasgapsarr qerapaydta paraalarll prhadqfale
       61 pltpdgdgdr frvagrtgri tvsgttpavl ltgvnwylky tcrahlswag dqvelparlp
      121 apaapverat slphrfalnd thdgytapya dwprwerlid alalrgvnev lvtpgteavy
      181 hrlltgfgys daearswlpa pshqpwwllq nmsgyggpts peliakrael grritgrlre
      241 lgmrpvlpgy fgtvpdgfaa rnpgartvpq gtwaglkrpd wldprtdaft avaaafyrhq
      301 eqllgpadhf kmdllheggd pgdvpvpdaa ravekalrta rpgatwvilg wqdnprrell
      361 davdhdrmli vdglsdldtv tdrerdwggv pyafgsipnf ggrttlgakt hiwaerftaw
      421 rdkpgsrlvg taympeaaer dpaacelfge lawrerpvdr eawfdgyadl rygapddhar
      481 aafaalrtst yaisskdgrp hdsvfaarpn laarsgtvya thtpafdpav fdtafaalla
      541 vrpalrgsda yrhdltdaar qalanrswql igqlqdayrr kdrdtfrals alwlrlmrls
      601 devtgahrqf llgpwladar amatgpeeea rlehsarali ttwadratad ggslanyanr
      661 dwhgligevh lpqwqaylde ladalaadrp pktfdwyate epwtrartsh plrpttdahr
      721 tarrvhdtla kapyqgtltv tadpaalppg gratvtaalr nvnglratgr vdfalagvea
      781 tasgpvslps vppggtgrah wrvtappgpl enplrplpyd ltvdygpqga prvrtarhgt
      841 lfvagpldpa lrtvttnaav fgqlddrfai hgagadlwka taefgavyrp galtaggtvt
      901 vevtaqdptg pwaragivvr nrltpsapgs adalgflnls vtpangvvls ydangdgtld
      961 tyrrltgita pvllrltrgk dtagsgtytg acstddgatw reiatvtvpg aaarqdtglh
     1021 qsaansatgd ggtaafrrwk lv
//
LOCUS       WP_457682784             246 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457682784
VERSION     WP_457682784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=24671
     Region          6..>64
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 mserrnpeal heaaagwrem gkhldglvrd ldrhvgtaaa anwhgpagea fagewhrlkr
       61 svddalpafe laaadlenaa aappedkgge ehheappvks sattqsssgp evaygfmalg
      121 qlanglggaf gkrgggggqs rgpvvrhtwe tstaaqgpdp fgpakngdak trggegiakg
      181 artqpdvaep apgeerapka gqdkkgtaae paaatggdar akgapasgge apgqpapdvt
      241 qhgafg
//
LOCUS       WP_457682787             531 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682787
VERSION     WP_457682787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..531
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55905
     Region          7..499
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 methdraaav haegivkryg ptvaldgarl tvrpgeahal vgrngagkst lvsvltgmer
       61 pdagrvtfgg epapgwgdta awqrrvacvy qksmtvpelt vaenlylgrf qgartirwra
      121 lhtrarella eygvevdtaa rirdlgveqr qfveiarals fgarliilde ptarldaggi
      181 drlfaklral raqgvaflfi shhlqevhel cdtvtvfrda rhvltapvpg lakdalvaam
      241 tgeepaavrq prpevrrtge pvlrtealav dghfapldlt vragevvgla gataggstai
      301 getlvglrtp dagriavrgr pvrtgsvpha ldagigyvpe drhreglvph rsvaenatlt
      361 vtgrlgpmgt vlpsrtrafa rrmiealdik atgpgqpvsg lsggnqqkvv iaralarepa
      421 vlvairptng vdvkskdall gvvrevadgg sgavivsdel ddlrvcdrvl avfhgrvtae
      481 fpagwrdhel vaamegmaag grgqdqppgt gggrdaapgs pdregtegta p
//
LOCUS       WP_457682788             344 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682788
VERSION     WP_457682788.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35788
     Region          29..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtetasppat davdrppprr rprieparwr dfslvpvifv lgvigfivsp aflaqdnlig
       61 viqqstelgl lvlgealili sgrmdlsles tiglapvlal wlvmpadgar faglelfpaw
      121 taiplclavg aavgaangfl iltlrvngfi atlgmltmlr glqvgisegr signvpesfa
      181 ylgkadwlgv paavwiclal falggaalgy lrhgralyai ggnpeaaraa girvdrltwi
      241 vlalggvlaa fagilytghy gavsasqgng wifqvfaaav iggiglkggr gtlfgaltgv
      301 ltlqlvinvm tlggvpplwt qflngmiiiv alvisrftsg ekqd
//
LOCUS       WP_457682762             604 aa            linear   BCT 27-JAN-2026
DEFINITION  choline/carnitine O-acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457682762
VERSION     WP_457682762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   van der Hoek,M.D., Madsen,O., Keijer,J. and van der Leij,F.R.
  TITLE     Evolutionary analysis of the carnitine- and choline
            acyltransferases suggests distinct evolution of CPT2 versus CPT1
            and related variants
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (8), 909-918 (2018)
   PUBMED   29730527
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10466051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="choline/carnitine O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65562
     Region          14..588
                     /region_name="Carn_acyltransf"
                     /note="Choline/Carnitine o-acyltransferase; pfam00755"
                     /db_xref="CDD:459926"
ORIGIN      
        1 mttfaqedsl prvplptlea scerfldwca plltaderaa teaevaaflr pggpgrvlqs
       61 aleeydateg vhswldtfwp yrylgrrdri alnanffflf qdpapgqpqs qveraaglia
      121 gavdykrqld qelippvvqr gvpqsmvqnk ylfsatripg aqqdtvrspy tdawpgpsga
      181 rhivvfhrgt mfrmevlgad gvphslddle aglravqkag aepaaagtsv ghlttmaraq
      241 wadareslra hhprnadald dietalfcvc ledsapadtq eacdqllygd rgnrwfdkav
      301 slivfadgra ginvehceld gttilsftda llstpaeehs hrsgarsqgl palepvvfel
      361 ddalraqvrs aadafaeyga atatrtvafd dfgsttakal gaspdafvql ayqlahqrak
      421 ghlgatyesi atrqwrrgrt eamrvvtpei qafvaamedp aasadarraa fraaagkhva
      481 rakecqagea peqhlwelel iqrrrgaelg vteqpalyrt pgwltmrddy lstssapsah
      541 iqyfgfgsts srcigvayvl lpdslhvyls tpqavagpmq vfadrlreav aelrellasd
      601 gseg
//
LOCUS       WP_457682790             285 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682790
VERSION     WP_457682790.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30109
     Region          2..275
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mridahhhlw dlsrreqpwm dgpwadpirr gyalsdltph laehgidgtv lvqssssyee
       61 taellalaag egpvagvvgw adlrdpalae vlaalpaglv girhqvqdep dpdwltrpdv
      121 lrglgalaga glvydllvtp relpaahtav ralpqlafvl dhagkppvvt gewqpwadav
      181 talaalpnvs cklsglvtea dreawrpqqi lpyarhvlda fgpgrvmfgs dwpvctlaag
      241 yedvvalaea atgqlaaaer sdvfggtagr vygigtppap dlpgr
//
LOCUS       WP_457682792             269 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457682792
VERSION     WP_457682792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26787
     Region          26..269
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtatatatat vlttaattea gdgtrpltgk aalvtggsrg igraialrla adgaavalty
       61 rngqdraeqv vkeieraggq awavradsed aeavwasvag tvdrfgrldi lvnnagvgvi
      121 gpfegisldd vdrvlgtnvr apflaaqaaa ahlteggrii sigscmaerv afpggtlyat
      181 skaaltgltk tlarelgprg itanlvhpgp idtdmnpadg esaamqagft algaygrasd
      241 vaatvahlag dggryitgas iavdggfav
//
LOCUS       WP_457682794             318 aa            linear   BCT 27-JAN-2026
DEFINITION  RecB family exonuclease [Streptomyces nigrescens].
ACCESSION   WP_457682794
VERSION     WP_457682794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Steczkiewicz,K., Muszewska,A., Knizewski,L., Rychlewski,L. and
            Ginalski,K.
  TITLE     Sequence, structure and functional diversity of PD-(D/E)XK
            phosphodiesterase superfamily
  JOURNAL   Nucleic Acids Res 40 (15), 7016-7045 (2012)
   PUBMED   22638584
REFERENCE   2  (residues 1 to 318)
  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   3  (residues 1 to 318)
  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   4  (residues 1 to 318)
  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 10006768
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="RecB family exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_component="GO:0009338 - exodeoxyribonuclease V complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008854 - exodeoxyribonuclease V activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34606
     Region          40..291
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mgwsteqaea gtrsgqsggg pgaeaagaga rsgeqprppv alspsrasdf mqcpllyrfr
       61 vidrlpeqps aaatrgtvvh avlerlfdap aaertaagar amvpgewekl lakrpelagl
      121 faedpegerl agwlaeaeal verwfsledp trlepadrel yvetvlesgl qlrgfidrvd
      181 vaptgevriv dyktgkaprp qfaegalfqm kfyalvmwrl rgvvprrlql vylgsgdvvt
      241 ydpdeadlrg verkllalwe aiqlatatgd wrprptklcg wcdhqahcpe fggtppvypl
      301 qvrpaeggvp pqgrmgei
//
LOCUS       WP_457682796             370 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682796
VERSION     WP_457682796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 370)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..370
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37731
     Region          30..357
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtsneaappp gantgaagaa ppgrpaaarv tsrdvaraag vsqaavslvl gdkwrgrvsp
       61 gkaeavraaa relgyrpnla arslrmgrtr tvllvvpvlt teffarvytg aaraaadhgf
      121 gvvlypspeg igparnpfds aaatldgvia ssmaaealta lreadlplvm ldsdpgddra
      181 datvnldiad garqlighls alghrrithl aadvpswtfe lraravadsl hgvpgaalrr
      241 qptalsvdag lhaahaaltg pgprptallc dddiiaagac kavrrlglrv pedvsvtgfd
      301 dlalavavep elttvrlpae efgeagmral mtvldgrpad tptlpvelvp rgstappvda
      361 pgnaarpggk
//
LOCUS       WP_457682800             316 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682800
VERSION     WP_457682800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /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=34429
     Region          7..315
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 matnaidqtr rmlslvtylr erpgarvgdv arafgitede liadldvlpm cgtsfrggdl
       61 ldidtdgdri wwhnpddvae plrlaadeat allvaarava tlpglregdr qallratakl
      121 eaaageaaga ssrlsvtfes eggvfadvdr aiaerrrlwl ryyspardel terevdpirl
      181 favghtymea wcrlsearrt frldrvaeik lldapadppp velrdlsegl vqpaaedpev
      241 sievgpggrw vaeyyphdsa nelpdgglri tlrtpdpasl rrlalrlgrd grivapqala
      301 dsarqaaeqa laayge
//
LOCUS       WP_457682802             938 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457682802
VERSION     WP_457682802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 938)
  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 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=104065
     Region          12..935
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtedmspaer yaaaklraae qatalapfre mydfgldpfq veacraleag kgvlvaaptg
       61 sgktivgefa vhlaleqgrk cfyttpikal snqkyqdlvk rygaekvgll tgdnsvnsea
      121 pvvvmttevl rnmlyagsqs lvglgyvvmd evhylsdrfr gavweeviih lpesvtlvsl
      181 satvsnaeef gdwldtvrgd tavivsehrp vplwqhvlag rriydlfeer dgqsggrrev
      241 npdlerlarm ensrptfgrd krrgrnmrea drererrqra riwtpsrpev idrldnegll
      301 paitfifsra gceaavqqcl vsglrlndqe greqvrrive artagipddd lhvlgyfewl
      361 eglergiaah hagmlptfke vveelfvkgl vkavfatetl alginmpars vvleklvkwn
      421 geqhaditpg eytqltgrag rrgidiegha vvlwqrgmnp galaglagtr typlrssfkp
      481 synmavnlvs qfgrhrsrel lemsfaqfqa dksvvgisrq vqkneegleg yrgsmtchlg
      541 dfeeysrlrr elkdretela kqgaaqrrva aaaaleklkp gdvihvptgk yaglalvldp
      601 gmpsgrtngh rgfdaqdgpr plvltaerqv krlasidfpv pvkaldrmri pksfnarspq
      661 srrdlasalr tkaghvvpsr hrkprseaad dreiarlrte irahpchgca eredharwae
      721 ryhrllrdtr qlerriegrt ntiartfdri callteldyl egdtvtdegr rlarlygeld
      781 llaseclrdg vweglgpael aacasalvye arqaddavap klpagmarda lgemvriwgr
      841 ldaleedhki nqaegvgqre pdlgfawaay rwasgfglde vlreaempag dfvrwckqli
      901 dvlgqiaaaa ppggtvarta rkamdgvlrg vvayssvg
//
LOCUS       WP_457682798             322 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457682798
VERSION     WP_457682798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /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=35699
     Region          4..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maiakaerlm nlalcllgtr rpltkrelrs sieayieass ddsfnrmfer dkddlrelgl
       61 vietvegieg digylarrds nrlppitlda eeaaalglaa kiwqqarlag aasgalqklr
      121 aagmplaadg adydagqphs alepripahe aafeplmlac rdrrpvvfdy rkstaahpeq
      181 rqvepwilec wrghwyvagw drerkaervf rlsritgkvr srqgaftapv pdhvtvretv
      241 eswagetatg tariklraeh gyplraralt lrelgdgwde leipnghgld awlvefgsdv
      301 vvlepaelra dvidrlrava kg
//
LOCUS       WP_457682806             250 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682806
VERSION     WP_457682806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26362
     Region          37..>186
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mttdatfsag vgtpeadwas wpaldrlpav plpagpvvvv aahpddevlg fggtmaalaa
       61 hgtdvqvlsv tdgegshpgs trltaarraa vraaelrdal gdlglpslrp qrlripdtqv
      121 hrhetavrhq itarlyavna alcvapwtgd lhsdheaagr aaaaacrssg vplwmypvrm
      181 whwarpadpr vpwdsaarll lpagaarrka aalgrsvsri hplgdgdgda ailppeelah
      241 htrpfevvfr
//
LOCUS       WP_457682804             178 aa            linear   BCT 27-JAN-2026
DEFINITION  Dps family protein [Streptomyces nigrescens].
ACCESSION   WP_457682804
VERSION     WP_457682804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=18916
     Region          1..150
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mteseggevi grlrlrlhal ndlaltlkhv hwnvvgphfi avhemldpqv davramvdat
       61 aeriatlggs ptgtpgalaa ertwedyslg raqaiehlga ldvvysgvir dhraavaatd
      121 gvdpvtqdll iehlrslelf qwfvrahles aggtlstgsa nglseaghaa aeqarrqp
//
LOCUS       WP_457682808             322 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457682808
VERSION     WP_457682808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33485
     Region          9..276
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrvlpaapsi egltavvtgg srglgllmar qllrrrcdvv llardeaelg ravgklrqwg
       61 ggtvravvcd vrdrtavqdr laeiardqng ldivianagi iqvgpadalg sdgfeeamds
      121 vfngalntal aalphlrrsp aggrlalvgs vggllavphl lpyscaksav aalaeglhae
      181 eaphgvtvta vhpglmrtgs hvhalfggdr rreyawfsal agapvlsmna eraaerivta
      241 lqrrrprivl tpaarlgata hglapvtttr lvsavarvlp rngargtvdg stvaagekpp
      301 arhlrgvlga lneraadrfn qr
//
LOCUS       WP_457682825             255 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682825
VERSION     WP_457682825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27475
     Region          1..236
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mrpnevrhkl gageevyglf stlpeptmve migcagydfv ildtehtlvd pqrlenlira
       61 aetagltpfv rvpeadpgav lraldagamg ivvphvrgra didatiraar yapegmrsln
      121 ggrgpgfgli dpaeylrran aeimvialle daegveaide ilspggvdlv lpgpgdlsrs
      181 ygvpwqvrhp rvqeavrtlr eacarhtvpf camsttpdrr aewradgvta fvvgedrdlt
      241 aralrghlar tagre
//
LOCUS       WP_457682821             396 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682821
VERSION     WP_457682821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  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 396)
  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 396)
  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..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /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=42936
     Region          52..306
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mrmyllalnp tdsvtdgflp aaarlgldvt vltdqpeahr rgypeievle cdvhdfravi
       61 triathhpad avftnsdhlq tqaalvadyf glpgkdwraa lraknkaemr rhlaaagadt
      121 vrsaelapgq dpsaftaagl pypcvlkpre gvasedvvla egpdelvala keiqarrpqa
      181 alvaeeflag elytletlgd grvrhvlggf httvsappaf ieerldfvaa hpqpvveqvl
      241 aqldalgvgf gachtefvvh egrarlievn yrvigdqcdl mlaqvldipl fehilrthlg
      301 eplpadlgar rdgagrvdya cadragtlta apaaadrtvd gvrltyrplr evgtehphyr
      361 tnrdylgvlr atgtdrsavd rvsdaffaae rweist
//
LOCUS       WP_457682831             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682831
VERSION     WP_457682831.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30883
     Region          35..271
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 matdvhgsvt dvhrsvtdvh gsvtdtaagk dpgsapsgaa vqvaglvraf gdraviddlq
       61 ltvqpgefva llgrsgcgks tllrvlagld reiegevlvp rrkavafqap rlmpwkrvwr
      121 nvllglpgrp ereaavtald evglghrada wpktlsggea qraslaralv repdllllde
      181 pfgaldaltr ikaqrlvael wrergcavll vthdveeall ladralvmeg griayettvd
      241 lprprdiadp rfgalrarll drlgvegstd dgaggtdpae aeatedrsaa aa
//
LOCUS       WP_457682833             307 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682833
VERSION     WP_457682833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32120
     Region          52..301
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 msldqavagh appdsaadaa rpslskgvka raesasrggg pvldrvvpvs grrrsvprwl
       61 rravgpvall vlwqvlsasg aleedilasp gtiaatagdl lsdgtlpsam lmslqrvavg
      121 lvlggvtgvv lalasglsrl gedlvdatvq mlrsipwvgv iplfiiwlgi geapkialis
      181 lgvafhlyln vyagirgvda qlveagtslg lgrwglirhv vlpgalpgam tglryslata
      241 wlalvfgeqv naddglgflm nqareffrtd vivvclvvya ilgliadflv rtlerlllqw
      301 rptftgq
//
LOCUS       WP_457682835             878 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457682835
VERSION     WP_457682835.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..878
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=97681
     Region          76..>819
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 meaaaigarl assvvaplik rlfvadgpga glvdkplrvs klvsfkgekr vlsdedlhki
       61 aeelvnraaq stgvkerlpa yeqravahav adslrtlgyi dmddvqavql ghlalsrhlr
      121 sqspsatlgl ssdavtlhas vldtaclhil qfftqrstfv artliehsrr ieelslkids
      181 liartpspad gpfeeryaey iaskhgklti fgldlseape nwpldaayls ldaaggrthd
      241 lptllpadhi lagrdrvllr gvagsgkttl vqwlavstar kalderllyl yglvpfvlpl
      301 rtltrggakl ptpdgflasv dcpianlqpt gwidrvlrsk rglilidgid eipeserqea
      361 rrwlqelvsa ypnnrwlvts rpsavrqdwl vgddfaeldl apmsrenvve fikrwhkaag
      421 igdryatdll qsvrdkqdlg rlatnplmca licalhqdrr gylpddrkei ydaalsmlls
      481 rrdrergiyk pgtirigeeh hiqliqklay wmirngrsem dradaielle halpampkia
      541 dqgtaeeiyr hllirsgllr epstgsmdfi hrtfqdylga kaavegldfd fliahahldq
      601 wedvirmsva harimertrl ltgliergdt sekdsrrlhl laaaclehat elnpdvrmev
      661 eqraaalipp rsadqarala dvgpvvldll pgpqalsdde ayftvlsatr lptdaaisvl
      721 aqyrdlsdlr vrselarvws rfecdrfaee viahlgeedl yfcvsnaqel halrrfggrs
      781 rirvtgtitp eefqtacdps rlthlwveae sgatwewlay fpnlntitfe splasidvss
      841 lkkvrslrti rlpeesvfvg sealppstki vraclttt
//
LOCUS       WP_457682846             227 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457682846
VERSION     WP_457682846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Identification of a PD-(D/E)XK-like domain with a novel
            configuration of the endonuclease active site in the
            methyl-directed restriction enzyme Mrr and its homologs
  JOURNAL   Gene 267 (2), 183-191 (2001)
   PUBMED   11313145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="restriction endonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24444
     Region          105..218
                     /region_name="Mrr"
                     /note="Restriction endonuclease Mrr [Defense mechanisms];
                     COG1715"
                     /db_xref="CDD:441321"
ORIGIN      
        1 matparrrsa atrrptrpkr rprgkaarrr eregkalaav ligafgiavv saypvvstiv
       61 ivlaaaaalt iylartgrlh lpagiagaag vgprrdftht iaayqamsyt efehavadla
      121 rrdpavrktd vsggkndrgl dvlvhlhsgd ryllqckrwk grvgseevmk ingtyrdihn
      181 cfgaaiitts aftadaertn amlpkslrli dgrglarwas ggrppwa
//
LOCUS       WP_457682849             108 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682849
VERSION     WP_457682849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..108
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11920
     Region          10..73
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
ORIGIN      
        1 msrqityrwr lrelmaargm ftvpelmphl aergitlsas qvhrlvsgtp erlslpvlaa
       61 lcdildctas dliptstenv rlrrtagqda pinlaarrpt rvrltdeg
//
LOCUS       WP_457682853             401 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682853
VERSION     WP_457682853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /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=43105
     Region          176..398
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrnrpyepsa vdtrwlgavm htafflllgg alarfllrhp geprtpwiia lcvvlavlhl
       61 lgpgmgdadp rptrrrsawl alvvvvwmvl vvlapsfawc avplfytglr tlppraalvl
      121 vavltalvva aqlqlagrfd pnlvlappav aalatavflq merhtarqrv liddlirtrr
      181 elaaserreg tlaerqrlsm eihdslaqgl ssqrmllqaa drvwdtepdk arahvrtaas
      241 vaehnlaear rfvhdlaptd largsgldqa lralaaresg adltvrvhvd ddgrlprlpd
      301 rvqsallria qgalanireh aaassatltl tllddevvld vsddghgfdp aalpdspgsg
      361 rghglpaira rlralggtlt vestpgegtv lsaaiplevp r
//
LOCUS       WP_457682851             192 aa            linear   BCT 27-JAN-2026
DEFINITION  GlcG/HbpS family heme-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682851
VERSION     WP_457682851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=18906
     Region          82..191
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkamnpvrkk fsrrarvatg gavltavavs gfgavsanas apattsataa sasvparatt
       61 tsthltidaa akaaqaalda aekenqrvtv avvdrngnti vtlrgdgagp qsyesaerka
      121 ftaaawnapt sqlaerlqqt pnlkdipgtl flaggapvta gnapiagigv agapsgalde
      181 kfaqaganav ar
//
LOCUS       WP_457682857             354 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682857
VERSION     WP_457682857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37605
     Region          87..352
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mgsharpnri hrtgvriamv alvgaalpit sgglaeaats gaahsadeng qqgseatstv
       61 aqkqgtqrqf qsvqaaphav kdkaadaqda kdqaapqina dhaflldard gsqerelwgg
      121 akadesvsma sttkimtaiv alkhpewlnr qitvkqeyrd yvqkvggsta dlqtgdtltv
      181 eqllyallip sgddaamala dnlgsgdtad ariadfvnqm naeaqqlgln gthfdgfdgi
      241 shgnnhstar dlarlgqram lqpvfadivk nkqfkteapa angrtryytw dntnkllssy
      301 dgalgiktgs gpeagyslvf aakrdnrtlv gailkddqgr fddatkmldw gfah
//
LOCUS       WP_457682862             414 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457682862
VERSION     WP_457682862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45114
     Region          1..414
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 meirsttded ldvfvdtvha afgrfpetpt eggwlwwsal emdrgllalt adgrpvgtaa
       61 ahsfeltlpg etlvpaagvt avgvlpshrr qgvlsammrh qltelrtrge flsvllasea
      121 piygrfgygp atytarltvp rhkaalavpr argvadapaa gsdngsdngs vevlrraecg
      181 eileevydry rrtqpgalsr phhwwarrag qppiapapry vavhrdadgv pdgyasysig
      241 esqtltvdet iatddavfta larfvlghdl vsqvvfkhvp pehplrwqfa dfragevsgd
      301 tdwlwvrlld vpraltargw fmdgelvldv edpflgehgr ylltvrdska dcvptdrepd
      361 lsldvsdlgs vylggtapst lvraghirah rpgaaalada lfraeraphc lhwf
//
LOCUS       WP_457682867             268 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682867
VERSION     WP_457682867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28099
     Region          18..268
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpktsdtadd rseerrggag svqsvdravs vleilaklge agvteiseel gvhkstafri
       61 lgvlenrglv eqekdrgkyy lgagvlrlag aaairldisq egqpvcrala edtgetania
      121 vldgdaavni mqargsaavt aynwlgrrtp lhatasgkvl lahlpaprre tlvtrklprf
      181 tehtlttaag lreqlaaale dgfactseel eiglnavaap vwahdgavig aigvsgpayr
      241 merqllpela eraakaaadl srlmgyag
//
LOCUS       WP_457682871             287 aa            linear   BCT 27-JAN-2026
DEFINITION  5-oxoprolinase subunit C family protein [Streptomyces nigrescens].
ACCESSION   WP_457682871
VERSION     WP_457682871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="5-oxoprolinase subunit C family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29195
     Region          5..283
                     /region_name="PxpC"
                     /note="5-oxoprolinase subunit C/Allophanate hydrolase
                     subunit 2 [Amino acid transport and metabolism]; COG1984"
                     /db_xref="CDD:441587"
ORIGIN      
        1 mtdrafsvvr agalttvqdl grpghahlgv pragaldapa hrlanrlvgn pasaatlett
       61 ltgcalrvrt attvavtgap cpvtvdgrpa pwgapvrvra gavldagpat hglrsylafa
      121 ggidtepvlg sraadllsgl gpdpltdgav lplgdphgpp agadavphhg pvpelvlpfl
      181 pgprdawftd tglrtlttgr flvspasnri glrtegpple rarsgelpse gmplgalqvp
      241 pnglpvlflh dhpttggypv igvvpercla paaqaapgtp vrflrmr
//
LOCUS       WP_457682875             282 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682875
VERSION     WP_457682875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29735
     Region          29..282
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 msatrhepra rgrlaallap pllwlvlayl gslavlllsa fwttdpftsd vvhtwttdnf
       61 rgilttpvyr tvalrtlgia vavtlldall alpmaffmar vaagrlrral lvavltplwa
      121 gylvkayawr vmlgehgiin aalaplglhg pgygtaavvl vlaylwlpym ilpvhaaler
      181 lpahqleasa dlgagtvrtl rsvvapavrp allagsvftf slslgdyltv qivggrtqll
      241 gnviasqvtl dlplaaalsa vpvalvvcyl aavrragald sl
//
LOCUS       WP_457682882             393 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457682882
VERSION     WP_457682882.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 393)
  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 393)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=41194
     Region          15..>127
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          142..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgetvrragr ataqlmtagg lallsylflg vllftavatv ivigagvlpe tvlllrrmag
       61 fkrrrvaawt gtavpeaylp ltgglservr taladpgtyr dlrwlaahfg ygwllaylal
      121 plwavgllad gvwcgllrqr avvlpligrl adldaawsra llrpspdsgn rarlaervee
      181 ltvtragava ahgaelrrie rdlhdgtqar lvalsmrvgl arraydkdpe aarkllddaq
      241 nqaevaltel rhvvrgihpp iltdrglvga vralaassgl evavgedgla egprapaave
      301 aaayfvvaea ltnaakhsga drarvelvrg pgrltlsvrd egrggaetgs agasggsgll
      361 girrrvaald gtvevtspag gptvidvelp caw
//
LOCUS       WP_457682886             552 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457682886
VERSION     WP_457682886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57871
     Region          11..460
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mskpavvgsd svgggrhlrr vvgfwglmfi clgsiigsgw llgalttavv agpasliswa
       61 lasvmlavla lahaelgaty piaggtarfp ffafgplagf sagwmswlrs vliapiqvea
      121 tlsymdrigw ihdradllra ngtltaagll igsglmlift iinilgvrll aginsvtavv
      181 ktvvplltva vlmtlafhps nftagggfap hgahgvfaal pagvvfallg feqaiqlage
      241 ardpqrdisr avivamaiat tlylllqvaf iaaldpgalt rgwdnpvgag nfgpyatlaa
      301 aagaawlati lyvdavispa gtglvymaga arlsyamgre rvlprplari grsrvpvvst
      361 flafvvgela flpfpswqal vglvtsaaai myafapvslh alrvrdgdrn rpyrmpsgmv
      421 laplgfvfan lifywsgyea dwklgiaali gfvflaltrr gipsgersgl rgksaawvwp
      481 wlggmiliay fgryggtgal pewwdlvivi vfslavhyta vrlavpaeav daavrreeeg
      541 esvppppaas ar
//
LOCUS       WP_457682885             643 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682885
VERSION     WP_457682885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 643)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 643)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 643)
  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 643)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..643
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69648
     Region          49..623
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mskqdddasa lpgvgpraaa qptletgadr vlgsglvada pirtrrvgfk esvrrfwplt
       61 rgdrrwillv flsailaafa etvailvfae ltdnalqkgs vsafwapagl wlgvavaggi
      121 vgylgnslaa wtaerfvmrl rarvfahlqk lpphffqrnr rgdlvermtg dvdaiealvv
      181 sglvqaatav fgvifyagaa fwlrwdmalv tfalaplfwi atkrftgrvk evsrreraad
      241 gaitsvveeg lvnvvltqay nrqrdeqerl grearrwlra svtsarlnel yeqivevlet
      301 lcvlaiiglg aweistgrmt lgellafaaf vgylyppird lgqlgltvte atagserlle
      361 ildarpavtd pdpavvvpap sravgaveac rvhfrypggk nevlqdfsfg avpgelvvit
      421 gpsgagkstl aalllrfydp dtgsirldgi pvnrmpldrl rrnitllpqe tlvlhdtvee
      481 niacgrdqvt hgdvvraara adaevfiaal pdgydtviap gtsrlsggql qrvaiaraml
      541 rdapvlilde pttgldtlat qrilaplrrl aegrttivit hdldlamdad rilvldegrl
      601 vesgthtqll agsglystlf hthppprngs phplahpsss hwr
//
LOCUS       WP_457682889             398 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682889
VERSION     WP_457682889.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42268
     Region          62..398
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mraqtrqglr sstrqqggrr rravsaaaav aigvmtlgal appaasdsaa saaaaaarpd
       61 avqqalntlv rddgmpaala svkdrdgrir tytagvgdlt tgskvprdgq vrigsntkaf
      121 tavvvlqlvg egkigldacv dtylpglvrg kgidgrritv rqllqhtsgl peygihvddd
      181 eirnryfepr elldialryk adaapgakwg ysntnyvlag livqkvtgrp laeemdrrii
      241 kriglrhtyf ptpgemsire phphgyhrnp antplrdfte mdpsvgwaag qlistnsdln
      301 rfftallagr llpaaqlaem rttvpagtsg lryglgltsr plscggvywg hggdiagyet
      361 rggvtddgra anvavtnipt deaatqhvkd avdralcg
//
LOCUS       WP_457682890             249 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457682890
VERSION     WP_457682890.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..249
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27460
     Region          5..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtqfvsivtp vhdtalsflp eafaslraqe lpdswewewl vqvdggkqtd vpvdiredsr
       61 vkvsdnrrgg pgvartlawg rsrgelvkvl daddilpsga lardievmet hpsvgwtvcr
      121 vldlmpdgsl rhntlgdpea gllargdlya ywksthrpqv hpaslcvrer liaeaggwma
      181 lpasedtall maldvmadgw figetglhyr khqgqttahp dhrsgaewea rmaairkhae
      241 alalrhrit
//
LOCUS       WP_457682892             270 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457682892
VERSION     WP_457682892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29827
     Region          2..264
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mapktpqwrg laeqiaqeia agtagyrpgd qlpqirelva qgkgskttil aaykaleaeg
       61 lvsmvrghgt kvrerpphqi rrhqeryvwe krlarrpgev rrsqgvidkd tnldhdqiet
      121 hatfstipad anlaerfgve tgtlmlhrqy whstsgdtta lslidsylvh evaarnpdll
      181 dsskepwpgg thhqlstigi eidriddgvr trlatqaear klgipvggav illdktsvst
      241 dgdvveyshv vlagertelq ysvplerwtq
//
LOCUS       WP_457682915             547 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682915
VERSION     WP_457682915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..547
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=56441
     Region          20..>195
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mnasstssnn glefthpyla vvlgggftgm laaaalsgha dvivverdrl prtparptdl
       61 pqarhahllt adgvrlidtl lpgsaarwla egarrmplpa efagrapkvr pgrrassryl
      121 lacsrdlldr virrqasalp gvtvldgtea teltgtaehi tgvrvrdtts gathlldadl
      181 vvdatgrhst arewltalgl psahedvvds givsatrifr apegtencpv ltarsglggp
      241 ppspgaphrp vpgrtatlvp ieggrwlvtl tstgddrpce hagrfvpfah rtghsvigdl
      301 iaaaeplsev rltrdtsdlr rryeqlsswp tgfialggav vslahdcgqg lslaahgaaa
      361 lrgalrrhgm depslarkvq rtigrlvqep wsvatgellp sptagravrg syvdvlapaa
      421 ptapflrpaa algllwekar irptaggaag rqtspgpvpa pltaapgspa aagphppaaa
      481 gaasarsarp taalsaappa papgqppapp hhsgsaptpr rlprplsfgp talrrisgat
      541 rrkpadg
//
LOCUS       WP_457682911             981 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457682911
VERSION     WP_457682911.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 981)
  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 981)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..981
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103856
     Region          284..957
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 marrweptag etrpsdgpat ampggagega grgtgeaala gcaavflpar ppragkvafw
       61 rpdggplpdl atgggegasd kdgaaepgrl tvarrhgnga rsrtvpavll ptaaavpllv
      121 rarhdpaahp aaacwgaatl halhlaargr llpgltledt dawragpldp ediahlraia
      181 aampadayav pipgsrplqv tdpavlvrly vdavvdalpr tpaagmvaga pyaasapqhl
      241 pgarewaaev aagvdagvrl slrldlaphk lfdaaeasga gsteersaaa avlqvhsltd
      301 ptlvadardl wegegpdhfg prsrvdtlla lrraariwap lgrllerpvp dvlplgedel
      361 yellgeaapr lgaagvavhw pkelarglta aavlrpapgs aadgfgffdt rellqfrwqm
      421 amdgvpltea emdalaeahr pvvrlrdqwv lvdpglvrka rkrelgylep adalaatlng
      481 taevdgeeve vvpqgalaal rgrltaearp lpqppglrat lrdyqlrgma wldtmtslgl
      541 ggcladdmgl gktitvialh lhrrpgapvl vvcpasllgn wqreierfap gtpvrrfhga
      601 grsldgldgg fvlttygtmr ssaaqlagrs wawvvadeaq hvknprssta kalrsikapa
      661 rialtgtpve nnlselwall dwttpgllgp lktfralhar eveggedpaa aerlarlvrp
      721 filrrkksdp giapelppkt etdhpvalgr eqaalyqavv retltrieta egiarrglvm
      781 klltalkqic nhpaqylkea apglaarsgk lelldelldt ilaeggatlv ftqyvgmarl
      841 lerhlatrgi paqllhggtp vaerekmvdr fqsghapvfl lslkaagtgl nltraghvih
      901 ydrwwnpave eqatdrayri gqtqpvqvhr liaegtvedn iaqllsakra ladavlsgge
      961 taltelsdae ladlvslrrp g
//
LOCUS       WP_457682918             197 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457682918
VERSION     WP_457682918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20396
     Region          33..195
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtyaeqdsgp atppaaapdt aarrdwarrr latpigpllv aasreglvrv vfhadertar
       61 reltrleqlf ggpplagiph lttaatelta yfagelraft vpldwslssg fnarvlhala
      121 dgvpygsvvg yqdladrvge pgaaravgaa mgsnplpvvv pchrvvasdg giggfgggle
      181 tkrlllaleg vlpaplf
//
LOCUS       WP_457682917             314 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457682917
VERSION     WP_457682917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  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 314)
  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..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /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=32596
     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 mraivmrefg gpdvlrledv pepaprgghs lvdvalagin yadvhvrgds ylapvelpyv
       61 pgnevvgtvd ggrrvvglcr gggyaertll hrrvtwdvpd aisdeqaval alqgnsawhl
      121 lftslrlteg etvvvpaaag gvgslavqla aragakvial agspekrela gklgahavvd
      181 staedlteri leaaggpvaa alemtggvtf ertltavapr grlavygfag gelasvptre
      241 lmersitvsg fwlpqlyadr talptsmral fdaviegtlt pqtgavyglg eaarahhdla
      301 artgtgklal dvtr
//
LOCUS       WP_457682919             355 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457682919
VERSION     WP_457682919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Nocek,B., Tikhonov,A., Babnigg,G., Gu,M., Zhou,M., Makarova,K.S.,
            Vondenhoff,G., Van Aerschot,A., Kwon,K., Anderson,W.F.,
            Severinov,K. and Joachimiak,A.
  TITLE     Structural and functional characterization of microcin C resistance
            peptidase MccF from Bacillus anthracis
  JOURNAL   J Mol Biol 420 (4-5), 366-383 (2012)
   PUBMED   22516613
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Korza,H.J. and Bochtler,M.
  TITLE     Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with
            a Ser-His-Glu triad and a nucleophilic elbow
  JOURNAL   J Biol Chem 280 (49), 40802-40812 (2005)
   PUBMED   16162494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="S66 family peptidase"
                     /EC_number="3.4.-.-"
                     /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=38815
     Region          21..344
                     /region_name="Peptidase_S66_mccF_like"
                     /note="Microcin C7 self-immunity protein determines
                     resistance to exogenous microcin C7; cd07062"
                     /db_xref="CDD:132883"
     Site            order(97..98,224..225,227..228,257..258,260..261,264..265,
                     312..313)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:132883"
     Site            order(119,248,329)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:132883"
ORIGIN      
        1 mpisspsasv lrhppkprpg drvavlspss glpqrfpvpy elglarleke fglipveypt
       61 trkwgagaqe raadlhaafa dpditavfas iggddqltvl phldrevfrd hpkpffgysd
      121 ntnllaylwn tgivgfhgaa vmcelgrpga mhpltadalr aalftpgpye lrpaerygde
      181 ngdwddpdtf aaepalwpgg gwwwhgperv vegpswggsi evlswmlmad reiqedpaay
      241 dgcvlflets eelpgadevy fvlrsmgerg llrrfpallm grpkawslsr plsgeakasy
      301 vreqraavlr alaayapdtv tvfdvdlght dpqlvipygg tirvdgvarr itvty
//
LOCUS       WP_457682925             137 aa            linear   BCT 27-JAN-2026
DEFINITION  Rieske (2Fe-2S) protein [Streptomyces nigrescens].
ACCESSION   WP_457682925
VERSION     WP_457682925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Schneider,D. and Schmidt,C.L.
  TITLE     Multiple Rieske proteins in prokaryotes: where and why?
  JOURNAL   Biochim Biophys Acta 1710 (1), 1-12 (2005)
   PUBMED   16271700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13681
     Region          43..135
                     /region_name="Rieske"
                     /note="Rieske domain; a [2Fe-2S] cluster binding domain
                     commonly found in Rieske non-heme iron oxygenase (RO)
                     systems such as naphthalene and biphenyl dioxygenases, as
                     well as in plant/cyanobacterial chloroplast b6f and
                     mitochondrial cytochrome bc(1) complexes; cd03467"
                     /db_xref="CDD:239550"
     Site            order(82,84..85,99,101..102,104,106)
                     /site_type="other"
                     /note="iron-sulfur cluster [ion binding]"
                     /db_xref="CDD:239550"
     Site            order(82,84..85,99,102,104)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239550"
ORIGIN      
        1 msqspdrrtv lrgaalagaa gfglvacstg dsganasavp depvelgaaa evpvggakly
       61 redrlvvsqp akgtykcfsa kcthagcvlt dvekkegscp chgsrfdvtt gevlqgpase
      121 plpevpvkak ggkliag
//
LOCUS       WP_457682929             171 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457682929
VERSION     WP_457682929.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..171
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18641
     Region          7..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mgtsvtisaa tdqdaeqilk lqylcyqqea alyddygiep ltqtlqalra elvegcvvva
       61 rlgeevvgsv rgtvdedgtg riaklivhpr mqrhglggrl ldavegrlaa ersatryrlf
      121 tghrsegnlr lyrsrgyvpv gteqltprln vvtlekevhr pagaeelvaq a
//
LOCUS       WP_457682942             258 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682942
VERSION     WP_457682942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26483
     Region          72..244
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(77..80,130..135,168,170..171,194,200..201,224,226)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(79..80,130,134,170..172,194,224,226)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mlraaasaaa agalvtgcdp trdqdpgaar saggpgpsga ghaspapvra arpptrvpgl
       61 pvqiehgprn gravaltfhg rgdpgmatal lgeaersgvr vtvlaigdwl deqpamarri
      121 ldgghelgnh tlhhrnical paadayaeis gcadrlrklt gtigswfrps qtrratplvt
      181 elarkagyph vlsydvdsld andpgaaavq rtvldavepg svvslhlgha gtvaalppil
      241 dglrrrglra vtttelvt
//
LOCUS       WP_457682948             495 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682948
VERSION     WP_457682948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50712
     Region          25..475
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 metndlalps apapldpaal aalvdrvrgp vlvpgddgyd aersgfqlar qhrpavivga
       61 rgaedvvaav rfardqglpv avqatghgls aatdggllis trrmagvrvd aaagtahvea
      121 gvvwgqvvea aaphglapln gsspgvgvis ytlgggvgvl artygfaadq vrsvalvtad
      181 grlrhltadt dpelfrallg gghglgvvta mefglvpvar lyggqlvfga eqidealaay
      241 lrwtetvpda ltsslaliay pdlpqlpgsl rgrylahiri actgsaaege rlvaplravg
      301 prvsddlrem pyaeshtihr dpsdphaydg dnallsglda aalrrvaalt gpsapvmtvv
      361 qlnhlggals agtgavghrd aryalrllsp lrgaaagdgp gnegsdpala tvralhaeal
      421 aavapwrlgr svnflfgghg drpdaaevar svhgtdehrr laglkarhdp envfrfhpag
      481 aaaadrtpap atsss
//
LOCUS       WP_457682951             111 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457682951
VERSION     WP_457682951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..111
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11787
     Region          6..96
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mttqpeirst pasprdmara ftpaltelve dplysqvwad palsprdrsi atvaavvaly
       61 rpdelpaqlr ravdngvtqa elaalithia fytgfpaais asaiaaralr d
//
LOCUS       WP_457682956             312 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457682956
VERSION     WP_457682956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31087
     Region          31..309
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mpadhgglph pipsspevlt aeaqagtaga tgargrigsv alviggivsl qfgasvavll
       61 fpragalgvv tlrlvvaslv lllvcrpkvr ghargdwatv lafgialagm nslfyeaidr
      121 iplgaavtle flgplilsva tsrrllslvw aslalggvvl lgregfdgln lagagfalaa
      181 gglwaayill sartgqrfpq adglalamtv aallslplgi vsagsallnp vtlglgaava
      241 lmssvlpytl ellalrklpa sgfavmmsle paaaatagfl vlhqalgwae vlaiglvvia
      301 svgavrsaaa hg
//
LOCUS       WP_457682960             793 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Streptomyces nigrescens].
ACCESSION   WP_457682960
VERSION     WP_457682960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..793
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=82594
     Region          42..531
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
     Region          362..676
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC C-terminal domain,
                     metallo-beta-lactamase superfamily [Intracellular
                     trafficking, secretion, and vesicular transport]; COG2333"
                     /db_xref="CDD:441904"
ORIGIN      
        1 mlrvtaeapp vkvgapdalq rlagslragl reasdglrpd arallpglvv gdtsrvppdl
       61 ddafratdlt hllavsgsnl tivlalligp phlasraerr glaprlglsl rgtaviggal
      121 alafvvvcrp dpsvlraaac glitllaigt grrrsllpal aaavlllvly dpwlarsygf
      181 llsvlatgal lllaprwsaa lqrrrvpprl aeviaaaaaa qavcapvvav laarvglvav
      241 pcnllaelav apatvlgfaa laaaavvppv aqalawcagw paewiagvar tgaalpgaef
      301 awpggwvggl alaaamvvlv pvgrrvlrrp wlcvlcalav ilavcrpapf trvltgwppp
      361 gwravvcdvg qgdglvlaag dgtalvvdtg pephamdrcl tdlgirripl lvlthfhadh
      421 vdglpgalrg rsvgaiettt lqeppgqaqf vrntaaaarv pivratpger rhlgpltwev
      481 lwppappalp gpsdpigprd stnptephgs tkatdlrgsa satephgstd lydptgfays
      541 hrqepgpggp ydsgssgspg spsgtdpldg pndasvtllv rtggltilll gdleppaqrg
      601 lfaahpelgg vdvlkvahhg sayqdpplih rlaprlalis cgadnpyghp aprtiaalra
      661 qgarvlrtdt dgaiailgte aglsatvtgh rvkvrladgp rtrarthpga rraevrtagn
      721 rrsrsrtrpv dnrqpsrprr qprcqprrqp grrrrrttrs mrrclsrprc ppggrrsgsn
      781 grteggepln qdl
//
LOCUS       WP_457682971             238 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457682971
VERSION     WP_457682971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25305
     Region          3..205
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(11,14)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mrveiwsdia cpwcyigkar feaglaafah rdevevvqrs feldpkapaa tdvpvldmla
       61 tkygvsraqa eamearvada aagegldyrs drihgntfdl hrllhlgrah gvqealldaf
      121 yranfaearl lgdpavlrei avgaglpsee varvladpga yarevraeer eaaelgatgv
      181 pffvidrryg isggqpaevf realerayad gaepsqpagd eagaapvcgd dgcavpgk
//
LOCUS       WP_457682973             258 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682973
VERSION     WP_457682973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27867
     Region          1..74
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mtttavvpnd vlravrlglr msqdelatal rragaelgep neaskrlvqr weagvsrtpr
       61 gvyaralerv tgrpvealgf slpvpmarvh adgkgghdmd gggestaavv dpqhaarpga
      121 esytgvwlsr yefysssrda tyegrhyvvi vqhgnrltaq slpgassnpd spltldltvd
      181 rnvitgswve qtaadgyyng aryhgavqml veptgrrmtg kwvgfgkefd vntgpwelrl
      241 vdrstskaal aqystppe
//
LOCUS       WP_457682966             652 aa            linear   BCT 27-JAN-2026
DEFINITION  S53 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457682966
VERSION     WP_457682966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Siezen,R.J., de Vos,W.M., Leunissen,J.A. and Dijkstra,B.W.
  TITLE     Homology modelling and protein engineering strategy of subtilases,
            the family of subtilisin-like serine proteinases
  JOURNAL   Protein Eng 4 (7), 719-737 (1991)
   PUBMED   1798697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..652
                     /product="S53 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67704
     Region          55..646
                     /region_name="COG4934"
                     /note="Serine protease, subtilase family
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:443961"
ORIGIN      
        1 mrssrtrspr araglawaat lplvagalal gapaadaagh dggrhalqgt kplwatrqad
       61 qgatsasaav tarvylagrd akgladrara vsdphsaayg kylspaqvra rygathdqia
      121 kvtdwlktsg ltvtgttnry lavegdvaaa erafatdlhn yrkkghvyha psttasapas
      181 ladavltvtg lnnaprparh hsgelpppeg vfrnsgpfss yygsrtdkal psaygskapy
      241 aikgytgkql raaygakkwt gknvtvaitd ayasptiard adtyaarhgd pryrrgqlsq
      301 vlpqdythik ecgaagwyge etldveavha vapdadivyv ggascmdddl ldslgkivdg
      361 hladlvsnsw gdieanetpd vaaaydqifq qgavqgigfy fssgdngdev antgtkqvdt
      421 pansawvtav ggtslavgkh dsyqwetgwg trkavlskdg ndwtgfpgtf nggagggtsk
      481 tvaqpfyqrg vvpdglakan gggamrtvpd iaavadpntg flvgqtqtlp dgklgydeyr
      541 iggtslaapv iagvqalaqq arhgvalgfa npgiyqrygt aayhdvtdhp lgagrdlavv
      601 rvdyvngtda skgtttslrs lgqdsslrav vgyddvtgvg tpgagyvssy rp
//
LOCUS       WP_457682976             417 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457682976
VERSION     WP_457682976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10867669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..417
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=42332
     Region          12..161
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cd06974"
                     /db_xref="CDD:132992"
     Site            order(26,28,67)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
     Region          235..399
                     /region_name="TerZ"
                     /note="Stress response protein SCP2 [Signal transduction
                     mechanisms]; COG2310"
                     /db_xref="CDD:441884"
     Site            order(272,274,318)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mtamtpgsnl plsavrvavd vtapvrldvs glllaadgkv rsdddfvfyn qpagpgvths
       61 aaagggdtit vdtaavpdgi ekivvtasld qpgatfagte ptgtvrnadd nsvlasftpp
      121 qlgaetalvv veiyrrsgaw kvravgqgya nglagiatdf gvsveepaap aaapqappap
      181 papaapaapa apagqwgppa gtpapaappa appapaaapa apaapgkinl dkgrvslqkn
      241 qtvslvkggr pllssvrmgl gwepafrsks idldasviay gpdrkkvdnc ffgklmilgg
      301 aiqhsgdnlt gegagddeai tvhlgglppe vtglvfvvns fsgqkfsdva kaycrlldaq
      361 sgeelvrfdl thseprtgvm maklirqfsg ewemtalgey vdartvrgmv kpagkal
//
LOCUS       WP_457682978             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457682978
VERSION     WP_457682978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33506
     Region          19..245
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mpstspggdp rppgrepave itglvkrygt ktavdgldlt vargavtavl gpngvgkttt
       61 vetcegyrrp dagrvrvlgl dpvadaaalr prigvmlqsg gvyagakaee mlrhtatlha
      121 hpldvgtlid rlglgscgrt pyrrlsggqq qrlalamavv grpelvflde ptagldpqar
      181 hatwdlvrel radgvstvlt thfmdeaeql addvaiidgg rviaqgspde lcrggaensl
      241 rftgrpgldl asllkalpad saaaepasgv yrvhgkvnpq llatvaswca qngvmpdaia
      301 verhtledvf leltgkelra
//
LOCUS       WP_457682980             268 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457682980
VERSION     WP_457682980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27453
     Region          77..268
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttteaggvt gtfsprpgaa plprmiraqa aletrmllrn geqllltvii ptlllvvfsa
       61 vdivavptgt aagagrsvdf lapgvlalav lstaftgqai atgferrygv lkrlavsplp
      121 rwglmtaktc avlvtevlqi alltavalal gwspqgsplt vvlllllgta afsglgllma
      181 gtlkaeatla aanlvfllll vgggvivpld kfpeaaqsvl gllpitalsd glrevlqhga
      241 gipwpdlgil avwavlglga aarffrwe
//
LOCUS       WP_457682984             416 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457682984
VERSION     WP_457682984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42241
     Region          13..376
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,118..119,121..123,126,146,
                     149..150,154,230,233..234,237..239,242,266,270,324..325,
                     329,333,349,352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 madagvlvrr ggfgrlwgaa avsrfgdalr gtalpllaya ltdspllisl vtacgflpwl
       61 ffgllggava drvdqrramw avdvlrgvlm agfalavvld rvgiglllal afalttlqtl
      121 fdnaatallp avvpeealaa anarlmtgqe lagrfvggpl apvliglgaa lpfladaaty
      181 fvaaalvasl rtrppdrppa tsgrtvrrei gegirqlwrd rvlrafcvsv algnvgigal
      241 iatlvvvvkg wlgagdfgya vvttgygigm vvgglladrt iavaggkgrt llvagvlqav
      301 tlvgfgtlrt vwlaavllgl fgfagmvwnv vettvvqqrs pagmlgriss afrtvsvagt
      361 plgalcggaa ataygpnapa llaaallalg aaalipvlqt adgassdsrq iprtar
//
LOCUS       WP_457682990             301 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457682990
VERSION     WP_457682990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 301)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=33326
     Region          11..282
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mpartweppg pfdlhrtlgv lqrgpgdpaf avrdgelwra crtpegpgtl riaarpaagq
       61 veaeawgpga dwllerlpel lgesddpaql tarhrivhea rrrhpgvrla rtglvlesli
      121 psileqkvts deayrawrll lqrhgepapg pwarmrvmpe prgwalipsw ewhragvdak
      181 rssailravr aarrmeeaar mdladatrrl malpgigpwt aaetlqrtlg apdaitvgdl
      241 hlpkiigyal tgrrgttdee mlellapyes qrhraarlil lsgrvpprra prfpvgdiar
      301 l
//
LOCUS       WP_457683010             400 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457683010
VERSION     WP_457683010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10145376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40890
     Region          19..378
                     /region_name="M20_ACY1L2-like"
                     /note="M20 Peptidase aminoacylase 1-like protein 2-like,
                     amidohydrolase subfamily; cd05672"
                     /db_xref="CDD:349921"
ORIGIN      
        1 msaaapspav ppralsaeva alrprmervs raihaepelk feefaaqkll tewlaeagfa
       61 vaapagglgt afvathegst pgpyvavlae ydalpgighg cghnliasgg aaaaiaavra
      121 lpdhpgtvav igtpgeemgg agkirlarag vfdgvdaavm fhpadrsltt rhglaaahlr
      181 vgftgvsaha akspwegrsa laaaqlflna ldslrqfmpp tarihgivtd ggqapnvvpa
      241 daavdlyvrd rtaasaealv arveraahgv amatettaev setgpmyadr rnntvlaelf
      301 gqtvralgld ivpgdpatpa gssdignlsq llpvihpyvq iaergtpghs eamreaaata
      361 yahdrteiaa tglarvvldl ltepgflsav raefdaaeav
//
LOCUS       WP_457683014             458 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105755].
ACCESSION   WP_457683014
VERSION     WP_457683014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 458)
  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   4  (residues 1 to 458)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19948164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..458
                     /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=48040
     Region          10..439
                     /region_name="cztS_silS_copS"
                     /note="heavy metal sensor kinase; TIGR01386"
                     /db_xref="CDD:273593"
     Region          229..457
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnglvrrlap rtlrgrlslv avttaallmt vltvafntvm drhlrhqada elgsraaava
       61 ttvdtsgsrv rvletvndrl ldsnvwiytg krllekppsa taggalteaa arlaahgdgt
      121 cttvtaaepr svrlcarsva grgstativt aldlgpyrns adavllgslv ldslmlacty
      181 altrlavgra lrpvrtmtdq aaewsaagsd erfgaagqpa elarlgasld alldrirnvl
      241 rherqltgel shelrtpltr iiveldwwra rprsgaetrs theviaeaaq amrticdtll
      301 ddareeahta atapgatavv pvlhrlvdrl gtpervtavv daagpepaag vrpalieriv
      361 spllanalry aastvtvsac pvpggvrisv tddgpgvpea fvddlfqpgr radpgdghdg
      421 aglglplarr larsvggevt hdpthttgar fladlpag
//
LOCUS       WP_457683019             521 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683019
VERSION     WP_457683019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..521
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54907
     Region          5..520
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mpertsydvv ivggghnglv aaaylaragr svlvlerldh tggaavstra fagvdarlsr
       61 ysylvsllpp kivqdlglrf avrkrtvssy tpavrdgrpt gllvgggear trtafaeltg
      121 sdreftawqr fygstqrlae rvfptltgpl psraalratv dddalwhalf erplgelvee
      181 tftddlvrgv vltdaligtf agahdpslrq nrcflyhvig ggtgdwdvpi ggmgaltdal
      241 adaarragae ivtdcavtgi atdghsaevt cdqgtvgarr vlvnaaprel arllgeappp
      301 paegaqlkvn mlltrlprlr dtgvdpreaf sgtfhiaegy rqledayqqa asgglpvspp
      361 seiychsltd psilgadlvr qgyqtltlfg lhaparlfta dndatrdrll aatlaeldth
      421 laeplagcla hdadgrpcie arspldldre lglpggnifh rdlafpyaep addaaegtap
      481 arwgvatthp nvllcgagav rgggvsgipg hnaamavlee g
//
LOCUS       WP_457683015             423 aa            linear   BCT 27-JAN-2026
DEFINITION  toll/interleukin-1 receptor domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683015
VERSION     WP_457683015.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=47428
     Region          4..>101
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 mtrvfishss kgdpraesvr khvveglrak rydvvvdtda lgpgrdwcpl lyqwlgecda
       61 avvlfnsaal dsawvrrevs ilmwrralnp aflvvpvlig evrsthlrek gftdvlpvef
      121 arvppgeptd eaqalservl hefadlpdtr ndsdhlrdwi sdiaaylrqa gdpgalrraa
      181 drlgihaddl rhveslvgsc tflahqmigt adrrlvhalh alasslsddt lnrlvqqiip
      241 twinaesarl llppaapdrr tvalnarypq taqhyldrav clrldlyylk saggiplged
      301 aaeefteqcv davrdllnfp pdvpvsrfrp rdddawqfls idvrgvrpal vahvvrelht
      361 lfpwlllill tgeslpdeet lrswrvddlv vvtphlgede ellghqltrd lsdlpgrlhg
      421 rrr
//
LOCUS       WP_457683021             367 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457683021
VERSION     WP_457683021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=38759
     Region          22..357
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mqtelsntlg aehavfgftp fpavaaaitr aggfgvlgav rytapdelar dldwmqehtd
       61 glpygldvvm pakkvagvse aeveamipeg hrrfvaelle khrvprlaeg easgwritgw
      121 meevartqld vafdypikll analgsppad vierahghgv lvaalagspr halhhkaagi
      181 divvaqgyea gghtgeiatm vltpevvaav dplpvlaagg igtgeqiaag lalgaqgvwl
      241 gslwltteea qlhsrrltak llaagpgdtv rsraltgkpa rqlrtawtda wddpsgpgpl
      301 pmplqgllva eansriqrhe vepllgtpvg qivgrmnser svqavfdelt rgferaidri
      361 nriagra
//
LOCUS       WP_457683030             315 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683030
VERSION     WP_457683030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34196
     Region          26..127
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
     Region          186..292
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 msevltaplv vefpftrslg pvqsafltgl rertvlgvta sdgrvvvppt eydpvtaeei
       61 relvevgsrg tvttwawnps prrgqplttp fawvlvrldg adtallhald apgpdavrtg
      121 mrvrvrwaaq rtgaitdiac fepddtpaga hepaphsgef anavtgittp arldytyspg
      181 raqsryiqal sdhktigerc pscrkvyvpp rgacptcgla tdtqvevgpr gtvttfcivn
      241 ikaknldiev pyvyahiald gadlalhari ggipydrvrm glrvepvwte hgrfpdhyrp
      301 tgepdadyds ykeli
//
LOCUS       WP_457683034             668 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457683034
VERSION     WP_457683034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..668
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..668
                     /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=71612
     Region          291..447
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mqgsapedek rvprpalrrs atavaaavll lplsgapsaq agqprtdalq qaftdaaarf
       61 hvprsvllgv sylesrwdgh ggapsvsggy gpmhltdart altrtpefse gdedargdea
      121 rgrkrvpaga aqraalptel parlrtlpta akltgipagk lrtdpaanvl ggaallaaeq
      181 rklgmpagsd parwytavar yggqdsahsg kafadevyav mrqgqarttd agqrvtlaaa
      241 pgltpdaaqq krlsaptaka paapatrkpe cprnvacesv papyeefgdg dygnhdkadr
      301 padqrvsaii ihdtegswet tlklikdpay vswnytirsa dgliaqhvpt kdvawhagnw
      361 yinshsvgie hegflaapda wyteamyras arlvkylsrk ydvpldrqhi lghdnvpgtt
      421 tatipgmhtd pgpywdwahy fallgkpfka tagprgglvt irpdydenqp vytgcakpgd
      481 tcaphgstav rlysapdeda plvkdvglhp dgrasttgvn dtgarattgq rfavagrsgd
      541 wtaiwylgqk awfhnphdep vavpakglia vpksgreeip vygraypeke aypagvpyqa
      601 vsplpyklaa gqqyavgdrm rgeyfysptf dvtkhavvrg kdvyyeiqlg hrvgyvradd
      661 vevrrsas
//
LOCUS       WP_457683036             377 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683036
VERSION     WP_457683036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  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 377)
  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..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /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=40803
     Region          91..306
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 myaassavtv ptrphrphpt gggpyldpsp svgavtglpg grtrrvqgtg aqplsgrldl
       61 sgpqgaqlra avasvhricp efnpvqvlrr sgrsvllvgt tgrmtavakc lldqspawte
      121 rfrqeisayr afvrhrppvr vprlvaadpd nctlimermp grvasltrhp seappradvr
      181 aalgaicrin lwrppsglfd tpldyagrig ryhdlglltd rdlgdlqklm hglshtqgqf
      241 chgnallnnv llspagpvll dwdnagwylp gydlatlwsv lgdapvarrh isqlaqnagp
      301 asrdaflvnl mlvltreirr yetavqrtmr eptptgtpgp gqpgvpaage eqrlllrrlh
      361 ddcqmarrav raavgtr
//
LOCUS       WP_457683038             488 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457683038
VERSION     WP_457683038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..488
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=52145
     Region          47..486
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpsplfadhs adrpperetv ealitqarrl rggldavrre stvdtdllad pqlrwqralc
       61 dlavhhlddl gghldqlreg lpagsadapa petgpppapp epephergal lrrvgsaewn
      121 lltdevswsd elftmfgrap sdgpltldel pslvhpedqd glatmvtdcl vdgrpidgef
      181 rivrpdeslr tvhmvgepvl dadgstacmw avlrdvselr rsqqavretr dslhrerqia
      241 qtehrlavel qeavlppwrg slrfphggpv aldlagrylp sgtrdliggd wydalqlpdg
      301 stllsvgdlt ghgvtatsgm amvlgalrgm avaghrpgpl mgflnqllds aaqpalgsav
      361 cgrfdpaart lewaqaghpa pllfrggtgr aldppegvll gatsgasytq hteqlepgdl
      421 lvlhtdglvp rraqgadaah egaerllala prfaaarsaq dsvrivveef gtaereddac
      481 vliarvgg
//
LOCUS       WP_457683048             605 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457683048
VERSION     WP_457683048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67231
     Region          20..600
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtapsdgtlp lsardavahl tpglwaranr llirkglaef aherlltpkr lpqdghyair
       61 sddgtteyrf aarrraldhw qidadsitrh rddselplda laffielres lglgdailpv
      121 yleeisstls gtayklaagr sgaaelakap fqaietgmte ghpcfvanng rlgfgiheyh
      181 ayapetaapl rliwlaarrd hatftagagl dydalirdel peetrtrfaa tlitlgldpa
      241 dyyffpahpw qwwnklsvtf aaevaqqhlv clgpgdddyl aqqsirtffn ttdpakhyvk
      301 talsvlnmgf mrglsasyme atpaindwla rlidaddtfr aarfsiirer aaigyhhrqy
      361 eaatakgspy rkmlaalwre spvptlepgq rlatmasllh vdhdggslaa alieesglep
      421 avwlrrylda yltpvvhafy aydlvfmphg enailvvedg avarvifkdi aeeiavldpd
      481 avlpptveri radvpedkkl lsvftdvfdc ffrflsstld dhgildedtf wrtvaacvtd
      541 yqtanphlad kfdrydlftd efalsclnrl qlrnnqemvd lqdpagalql igtlrnplap
      601 yapas
//
LOCUS       WP_457683049             189 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683049
VERSION     WP_457683049.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20911
     Region          22..166
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mntplftrtd atlgefslrp vdpygdaell hrwvthpkaa fwlmqdcdla avekefaria
       61 adpfhdaflg lhngtpaflm erydpthrel vgihaaepgd vgmhflsapt dtpvhgftla
      121 vittvmemlf ddpatrrvvv epdarntavh alnkavgfei lrtvslpskd aylstctrdq
      181 flatrgdhr
//
LOCUS       WP_457683053             296 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457683053
VERSION     WP_457683053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32357
     Region          12..280
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtttaapata pfrffdvyvv rarrvspsvv ritfggdrld elasggrdqr fklflpqphq
       61 erpvfhdmgd swyttwraqd paeravmrsy tireqrhdpr efdvdfalhg agpgadplag
      121 gpasrwaaha ragdrltvla pavednggvd frppagtdwi litgdetalp aiagilswls
      181 pgthakvwie iaheddrqql psfadaditw lvrdgataar cepvldalra adlpegtpya
      241 wvagesgtvk avrrhlvrer gidrravkft gywrrgasee dllaeltaga passed
//
LOCUS       WP_457683051             509 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457683051
VERSION     WP_457683051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 509)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55437
     Region          27..494
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msllahsaed padnraylln ngtagryhsa vtesvtrisa kiagttrpft gitvdgltpt
       61 vsgvdldapl hdaaaaldel eevylrdavy fhhprylahl ncpvvipalv geavlsavns
      121 sldtwdqsag gtlierrlid wtaeriglge aadgiftsgg sqsnlqamll ardeacrrem
      181 trqgatdarl tdvlprlril tsecshfsir ksatllgmga eaviavpsde nkrmrtdela
      241 aqlarcerdg lipmavvata gttdfgsidp lpeiaglcag ygawmhvdaa ygcgllvsrr
      301 rdllsgiera dsvtvdyhks ffqpvsssai lvrdratlkh vtyhadylnp rrmveqripn
      361 qvdksiqttr rfdalklwlt lrimgaqavg elfdevidra adawkllhdd prfdvvvepr
      421 lstlvfryvp ttdqdpelsd rvnlhareal fasgeaivas tvvdgchylk ftllnpettl
      481 ediatvldli aehagsflae qprpalsar
//
LOCUS       WP_457683055             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683055
VERSION     WP_457683055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36219
     Region          66..339
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mstsrnvtps rrgilaaggv vgigallaac gggkdsggan gdaktgpwsf tddrkekvsl
       61 kstpqrivaf tgtaaalhdf giddqivgvf gptklkngkp dpqagdldvd kvtiignayn
      121 qfnvekyasl rpdllvtnmy epgalwfvpd dskdkitpla ksvaitsarv pllkiierya
      181 dlakslgadl gakkvtdaka rfekasealr kaakshpvkv lacsgspdlf yasnpginad
      241 lmyykslgvd livpdhldkg gyfeslswen adkykadvll ldnrtatlqp kdlaakpswa
      301 klpavkagqi tpwsseprfs yagaaplies ltkaiegakk tk
//
LOCUS       WP_457683057             377 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457683057
VERSION     WP_457683057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38616
     Region          32..351
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msatvksgkg tgpeaenvpa avrrvravrt kggvslrldv ratvvgllll avalaagial
       61 igsgdypmtp aevfatltgd gdpgqqyivh elrlprvlvg llvgaafgis gavfqtvsrn
      121 plgspdvlgf aqgssvgalv aivyfqagaf gvaagavagg vgtgvaifll awkrgihgyr
      181 fvlvgigasa mlyamvlflm tkaniveatr attwmtgsln grdwdqvqpl avvcavlvpl
      241 llfhgrplrm lemgddaaya lgvrvdrvri tvllaavvlv aaataaagpi sfvaltapqv
      301 arrltlprwl kggggapmpg pnlvlsalmg svllvaadwv sqrlfgadql pvgvltgvlg
      361 ggyllwllat erkagrv
//
LOCUS       WP_457683059             286 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683059
VERSION     WP_457683059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30412
     Region          3..256
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msrltaenvt laydqrviae nlsvaipdhs ftvivgpnac gkstllrals rmlkpvkgsv
       61 lldgaaissl pakkvartlg llpqssiapd gitvsdlvar gryphqgllr qwspederiv
      121 eesmaatgvg eladryvdel sggqrqrvwi amalaqqtpl flldepttyl diqhqievld
      181 lcaelheeqg rtlvavlhdl nhaaryathl iamkdgavia egapsdivta elveqvfglg
      241 cqiiddpetg tplvvpaark prnggsrtdr ptaekapaga gqaggr
//
LOCUS       WP_457683065             226 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457683065
VERSION     WP_457683065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22959
     Region          1..223
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtaavagfal fallvtmapg pdtllvlrnc vrggrrtgaa tavgaavgsl awavaaavgl
       61 aaalqrwdaa fmvvrlagaa ylavlggqal wahrrsaaad rpesgpdpld tpepnghaap
      121 plahlaplra frqgllscll npkvgiffva vvpqflpegh svlgttlllg avdaviaagw
      181 lllvvvcagr llrglrrprv hrnlerttgg vlialgmgta aetvag
//
LOCUS       WP_457683067             350 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457683067
VERSION     WP_457683067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 350)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37536
     Region          9..349
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mvsepngprp tleavaalag vsratvsrvv nggagvraav qervrqavte lgyvpnsaar
       61 slvtrrtgav avviaepetr vfsdpffgrq lrgisrelaa adtqlllmfv ehrddydrig
      121 rylsaghvdg almfslhrdd plpamaerag lptvyggrpg wagadrvprp lyvdtdnrgg
      181 arqavrhllg rgrrriavit gpldqtsavd rldgyrealg taepdprlia dggftahgge
      241 ramaelldaa tdldavfvcs dlmasgalrt lrargrrvpe evavvgyddl epaawadppl
      301 ttvrqdveem grlmarlllr lldprktegs davelapvit earlvvresg
//
LOCUS       WP_457683069             349 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 16 protein [Streptomyces nigrescens].
ACCESSION   WP_457683069
VERSION     WP_457683069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Henrissat,B. and Bairoch,A.
  TITLE     Updating the sequence-based classification of glycosyl hydrolases
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 695-696 (1996)
   PUBMED   8687420
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10115061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..349
                     /product="glycoside hydrolase family 16 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36786
     Region          55..323
                     /region_name="GH16_Strep_laminarinase_like"
                     /note="Streptomyces laminarinase-like, member of glycosyl
                     hydrolase family 16; cd02182"
                     /db_xref="CDD:185691"
     Site            order(126,129,131,165,167,169,187,189,192,203,205,285,287,
                     289)
                     /site_type="active"
                     /db_xref="CDD:185691"
     Site            order(187,189,192)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185691"
ORIGIN      
        1 msmrirpgnr vhhragasll avgaalvttc altlptasae qaapvpkaka asaafqevwr
       61 tdfdgaagsr paaddwiidt gtgypsgppn wgtgerqtyt drpenlqldg aghlritark
      121 dgttwtsgri esrrsdfaap sggtlriear irmpevsgdd algywpafwt lgadyrgtyw
      181 nwpgigefdi menvngvnkv wgvlhcgvnp ggpcgesqgr gnsrecpgsa cqagfhtyal
      241 eldransaae alnwyvdgqk fhtvsaaetd adtwarathh ghflllnlam ggafpdgaag
      301 fatptdatrp ggsllvdhva vsvrqpagar tdraatptdr hpapqgats
//
LOCUS       WP_457683078             542 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457683078
VERSION     WP_457683078.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..542
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56712
     Region          44..439
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(51..52,55..56,59,90,140..141,143..145,148,168,
                     171..172,175,300,303..304,307..309,312,340,344,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mgksqhatpt gdgqtsvqkg rpdaapgggq ekqpasvrmv lfalmiamll amldnmivgt
       61 amptivgelg glehlswvvt aytlataast piwgklgdmy grkgvfltsi vifligsals
      121 gmaqdmgqli gfravqglga gglmvgvmai igdlipprer gkyqgmmagv mavamiggpl
      181 vggtitdhlg wrwsfyinlp lgaialimvt avlhlpkkrs qtridyigat lltvgitalv
      241 littwggtey dwlssqiigl gvlgvvalal fvaverkvge pvlplhifrn gnfslvtvig
      301 flvgfvmfgs mtflplfqqt vqgasatnsg llllpmllam mvvslfagrv ttrtgkykif
      361 vvvggglitl gltllslmdt dttrftsgay mavlgagmgf lmqttmliaq nsvemkdmgv
      421 gsssatlfrt iggsfgvail gaifthqvqa tmverigkag ekmtsggaqm dpkglaqlpp
      481 mikdaymhav atgthhvflw gavisiagfa aawflkevpl rggpatpaet pqtdriavae
      541 tv
//
LOCUS       WP_457683080            1080 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457683080
VERSION     WP_457683080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1080
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=117579
     Region          273..1020
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mdpsavgvrl asgvvaplvr klfvkegpga glvakpvris glvsfkgerr tlsdkdlrkl
       61 aaelvdravr tagpgerpla adeeravaea lattlhglgd ldmddvqavr lgatalaarl
      121 eaarphavhg lsrdaellha tllgtaclhi vhfftqrsaf vartlvqqsr sldslitlid
      181 eflerhpspr aadaafergy layiarkhgr ltiygidlah spdrwpldaa ymsleatapa
      241 arevtavgpf dgvggpggap papvpvpadq alagrdrvll rgvagsgkst lvqwlavsct
      301 kapgetalph lygripfvlp lrtlardgap lptpdrflas vgcpvsgsqp egwadrvlts
      361 gralllidgl deipdrerel trrwlrdltd afpdnlwlvt srpsavrddw ltadgfgelt
      421 lsamsraeva afigrwhdaa rcdaeeperl dayeqsllaa vhtkqdlarl atnplmcgli
      481 calhrdrrgy lptgrkelyd aalgmllsrr drerdmaapt gielsdepqi qllqrlaywl
      541 irngrseldr eraerilgea lpavpaaaeq gdataifrhl llrsgllrep apgavdfvhr
      601 tfqdylgaka avedgdfgll vahaedsqwe dvirmavaha rprerveilr glmergdgie
      661 drrarlrvhl lamaclehat eidprvrdev teragailpp rnheesqlla gvgplvlell
      721 pgpegladde aqevvataal igsdaalevm krfrdhpaig artqlasswp qfdtatyare
      781 ilqhldaevt vtatshaelh alralgrprv svsgpflaae llgalplgli esldirknpe
      841 iadlaflref pslkrlslwd cpavesvtpl adlqlrtlsi tgpldknvpi prglhrlrha
      901 rtlqlhstlp peglatlpad aplshlalsr pvgaeftdit cwpqmriiql rflthdfgad
      961 qwsalaslse ledfsfgvae egvtlqlpag lrlpqvtrlg vlntkrlpis dmsrllrsal
     1021 pafpgvrnlq lygfidgpid lspvaalpel qevflsylrp epghtlpphi kltryprprt
//
LOCUS       WP_457683096             412 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683096
VERSION     WP_457683096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43752
     Region          1..296
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
     Region          258..371
                     /region_name="CBS_pair_SF"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains superfamily; cl15354"
                     /db_xref="CDD:449531"
     Region          258..330
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341358"
     Site            order(282,294,317..318,321,335,357..359)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341358"
     Region          335..371
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341358"
ORIGIN      
        1 mirfehvtks ypdgttavdd ltfevaegel vtlvgpsgcg ktttmkmvnr lieptsgril
       61 ldgedisgld pvqlrrrigy viqqvglfph ktvldntatv phllgrprre araraaelld
      121 lvgldpstys drypeqlsgg qrqrvgvara laadppvllm depfgavdpv vrehlqnefl
      181 rlqstlrktv lfvthdieea vrlgdriavy gagrieqfdt patvlgapat pytaefvgad
      241 rglkrlsvtp vepgdleqpp vvrlddpvdr aagrlsadga swavvldadg alhgwvpaaa
      301 ltgapaapad gtgpglrkra pqgatvrdha rrmdarlplg aplrqalstm lqhdagwvav
      361 qdgdhflgvl tparlhtalr rattadaanv ardevsldtv pgpgvpapgp ag
//
LOCUS       WP_457683095             250 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457683095
VERSION     WP_457683095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25408
     Region          22..217
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mgaiagawqw lttaahwage kgvghrlaeh lwlsglclal sclialpval wlghlgkgga
       61 lavnlsnvgr avptfavlvl ltlsplgtrg dwptiialvl favpplltna ylgmreadrd
      121 vveaargmgm sgpqlllrve iplayplimt glrsatvqvv ataalaalag ggglgriita
      181 gfgnydtaqv vagallvavl altvegvlvl aerlldpmrg rrraacrasy pakgagpgat
      241 raapasapap
//
LOCUS       WP_457683104             381 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683104
VERSION     WP_457683104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41163
     Region          43..371
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mraafrgarr vlsegvgret vrermdrlva dapaaydldg wtdlygnddg iigelerrta
       61 galgteaaaf fptgtmaqqv alrcwagrtg natvaghpls hmevherdaw avvsglrmvh
      121 ptsaprppta aeiydlpepf galalelplr dagfvlptwd eltatveaar dreavvhfdg
      181 arlwecgphf grtlpeiaal adsvyvsyyk slggisgaal agteefieea rawrhryggq
      241 lfqqwpaala alagldrelp rlpeyvahak avaraldegl aeagvpwfrv hpgvphthqf
      301 qvwlpyppel lneavvrqae etgtalfgnw yepgpagppg valteimvga salawtddai
      361 rsaagkfvef vdfvnglrrv g
//
LOCUS       WP_457683110             288 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional DNA primase/polymerase [Streptomyces nigrescens].
ACCESSION   WP_457683110
VERSION     WP_457683110.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Iyer,L.M., Koonin,E.V., Leipe,D.D. and Aravind,L.
  TITLE     Origin and evolution of the archaeo-eukaryotic primase superfamily
            and related palm-domain proteins: structural insights and new
            members
  JOURNAL   Nucleic Acids Res 33 (12), 3875-3896 (2005)
   PUBMED   16027112
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Lipps,G., Weinzierl,A.O., von Scheven,G., Buchen,C. and Cramer,P.
  TITLE     Structure of a bifunctional DNA primase-polymerase
  JOURNAL   Nat Struct Mol Biol 11 (2), 157-162 (2004)
   PUBMED   14730355
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Lipps,G., Rother,S., Hart,C. and Krauss,G.
  TITLE     A novel type of replicative enzyme harbouring ATPase, primase and
            DNA polymerase activity
  JOURNAL   EMBO J 22 (10), 2516-2525 (2003)
   PUBMED   12743045
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Koonin,E.V., Wolf,Y.I., Kondrashov,A.S. and Aravind,L.
  TITLE     Bacterial homologs of the small subunit of eukaryotic DNA primase
  JOURNAL   J Mol Microbiol Biotechnol 2 (4), 509-512 (2000)
   PUBMED   11075926
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="bifunctional DNA primase/polymerase"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /calculated_mol_wt=30178
     Region          17..190
                     /region_name="Prim-Pol"
                     /note="Bifunctional DNA primase/polymerase, N-terminal;
                     smart00943"
                     /db_xref="CDD:214927"
     Site            order(95,107,109,129,131..132,134,152,159)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:238291"
ORIGIN      
        1 mtqptpirra pghlavalnl arrgipplpl ragkvpfgnc pacrdnacgg rpnmkhagpc
       61 rcpgvchawa aattipavia spawgaawrq avcvgyhpgg agltvvdldn adaiawahga
      121 lpatrtvptt rgehwiyqgt mgssnavrpg idikstmsya rwlgpgtgtm ttlpdavral
      181 avkepptvqp aphvttvpap vgggecrhrt payldrgiam aeqritears tvhttvyrtf
      241 lavlsahgrc gcltdahitr lfaaaqakge sprhctdawa nartrlgl
//
LOCUS       WP_457683114              80 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683114
VERSION     WP_457683114.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..80
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8392
     Region          22..71
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mtttaalvsg aeaefdptll altveeaarr lsvgrttmya lirdgavetv pigrlrrvpv
       61 kaisayldah mqprpksaaa
//
LOCUS       WP_457683116             419 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457683116
VERSION     WP_457683116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46936
     Region          74..396
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgkrakrpdg assiyfgkdg ywhgrvtvgv rddgkpdrrh vmskvseaev ikkvrelekq
       61 rdagkvrkpg rpwtvkawll hwveeiakps vrestyagye vavrvhlvpg vgahrldkle
      121 pehlerfytk mlangskpat ahqahrtirt alnhamrrgh vtrnvatlav ppriedeeve
      181 pydieevqrl lseasklrns arwsialalg lrqgealglr wsdvdlkagv lrvrknrlrp
      241 kylhgcggec grkpgyckqr vrknedtant ksragrrvig vpdelvrlle lhrqeqerer
      301 vraaqewqet gfvfaspvgq plvpstdyda wkqlltdakv rdgrlhdarh taatvllilg
      361 vpervvmqim gwsstamaar yqhvtggila dvaqqvggli wevakiaddd gpngsarar
//
LOCUS       WP_457683121             303 aa            linear   BCT 27-JAN-2026
DEFINITION  SURF1 family protein [Streptomyces nigrescens].
ACCESSION   WP_457683121
VERSION     WP_457683121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial respiratory chain
                     complex IV assembly [Evidence IEA]"
                     /calculated_mol_wt=31922
     Region          3..257
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 myrflltprw wginvfavla ipfcifmgsw qlsrfedrvd thqqqedrsa raktaaarpl
       61 erllpvdkvt sgrqasargr ydtghqllvp grtlkdkhge rqgfyvlnll rtdggkalpv
      121 vrgwlpgdag tkadtakvpa ppkgevnvtg alqasenqgt dgvqagggla pgqlgmisaa
      181 slvnivpyev ydawitltda qaplravppa aaegsgldlk afqnlgytge wfvfagfvvf
      241 mwfrlfrrdt eaakdaalgi vvevegeggg lgsgiaaglg edglgrgegs gdgqgeaaga
      301 gkv
//
LOCUS       WP_457683129             431 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457683129
VERSION     WP_457683129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=45432
     Region          153..426
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mtdwlegpld gnwrggeaqa ehisgqiwsp adhppqvhqa pppnlgppga apqapvpvpp
       61 prlnghpgng hpgngrpavr tgptgpgggn tghgrrapsp psrrrritra livlatvlgl
      121 gsagtyvwad telnrevdlg kiadrpssgg gtnylivgsd srvglsdrar knlhtggsad
      181 agrrtdsmil lhtgehgttm vslprdswvt ipshirpetg khyrasknkl naafsfggpd
      241 llvrtiehnt gvhidhytei gfagfvgivn avggvpmcld rdikdeksga dlkkgchtld
      301 grtalafvrq rhqeakgdlg rgenqqkfla alakkaatpg vlldpstvyp tmsaglgtli
      361 vdkdtglpnl talfkamkav ttgdgkrltv pvsnlafqtp kgsavkwntr lanqlfteln
      421 ndrpvtvgak k
//
LOCUS       WP_457683132             252 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457683132
VERSION     WP_457683132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27452
     Region          16..210
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrrriiivta vhapsahflp eaykslcqqd lpdgwewhwv iqedgksndv aphvpdderv
       61 tfrqgrpggp gvartialah aegeyikvld addqltpgvl ardlaalegg ngiswttsrv
      121 ldllpdgsta gfpgdpepgp vergavldfw kangfraqvh patlcvrrdl llalggwmal
      181 pasedtglll alnatsrgwf ssevglhyrk wpgqatgqas htdtaerdar mavveararq
      241 ltrfkwhypa td
//
LOCUS       WP_457683136             610 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457683136
VERSION     WP_457683136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..610
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65418
     Region          28..183
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          366..606
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpdwekrfra priglpdwae dapdrslfvs natgtfelya wdratgeqrq atdrpngttd
       61 gtlspdgrwi wwfsdtdgde fgvwmrqpfe ggpdepatpg ltpsypggla igrdgtsvvg
      121 cstdeegstv hvvrpgeppv eiyrhresag vgdlahdgsl ialehtehgd amhsairvvr
      181 pdgstvaeld dtkggteelg lsvmgfapvd gdsrllvghq rrgrwepmiw dpltgvetal
      241 didlpgdvga dwypdgsall veheyqarse lwryelgtpd gngapagaga gaaaaaaggr
      301 ltrvetpags vsgatarpdg tveflwssaa qppevrstsg evvldppgmk apgsvpvrdv
      361 wvegpggrih alvqqpageg pfptvfdihg gptwhdsdaf asspaawvdh gfavvrvnyr
      421 gstgygrawt dalkhrvgli elediaavre wavssgladp erlvlaggsw ggyltllglg
      481 tqpdawavgl aavpvadyvt ayndemealk amdrtllggt peevpdrfea sspltyvdav
      541 rapvyisagv ndprcpiqqv enyvqrlesr ahphevyryd aghgslvvee rikqvrleld
      601 faqrhviers
//
LOCUS       WP_457683149             480 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457683149
VERSION     WP_457683149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..480
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49449
     Region          1..452
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msnpprtrkl rlwealtlsv glmgptlamg lngagvattv gkavplvfll gllgvglvay
       61 gfwrltqhfn qagsvyalag atigpragff ggfallgtyl aflvctlaat gvfaqaflha
      121 mdirstgpwv avaflaalgv talnsrdgrt tartlliveg igilamlvla avimgrattg
      181 saprhqsldl svftaggtty savmtatvfa flswagfeac aslgeetddp krnipralag
      241 svlltgclyv lmmfaqtigf gtdaqgvref gaaesalstl sgqyigtwfa lviaftavas
      301 afaaalsssa aaarmvqala rdgfgprala rthpvtgapt talrvcgava aaltavmygt
      361 gaaafdtyyw yatigvlcvl vvyavagvgv ivftlsgrgs iprwelvvpv aglgylgfvf
      421 lqqstgqsap ytyfpwiaaa wclagvavvl aapsltrrig armtsvlvad ahptdrkvps
//
LOCUS       WP_457683153             391 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683153
VERSION     WP_457683153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40363
     Region          10..367
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 msldhtlttl aaqlereldd avelrhqlha rpclsgdeaa aralvlaalp gghtaaevag
       61 tgavvrvggs gpavavrgel dalavheetg vpwasqhpgv mhacghdvhl aalvalarav
      121 draggpapll avlqpreety psgaqdvted gilereqcra tigahvqpll aagtvactag
      181 gvnasadeft vtvrgrggha ayphltrdpv vtlahvvval qslvsrgidp mssvvlsvtt
      241 laagtaanvv pgsaeaggtl ramrtadrev iherlvetae lvaqaygcta dvritrgepv
      301 ldndatltaa trpllaslgl kvdadlrsag addfsyfser mpslmlfvgt hggteqlhsp
      361 tflppdervr dvahallagy laaaeqfipq h
//
LOCUS       WP_457683162             372 aa            linear   BCT 27-JAN-2026
DEFINITION  methyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683162
VERSION     WP_457683162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Kagan,R.M., McFadden,H.J., McFadden,P.N., O'Connor,C. and Clarke,S.
  TITLE     Molecular phylogenetics of a protein repair methyltransferase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (3), 379-385 (1997)
   PUBMED   9253175
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1009584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="methyltransferase domain-containing protein"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=39720
     Region          16..359
                     /region_name="methyltr_grsp"
                     /note="methyltransferase, ATP-grasp peptide maturase
                     system; TIGR04188"
                     /db_xref="CDD:275041"
ORIGIN      
        1 mtttatpsag elrlamadkl vadgavqspe wrrafaevpr elfvpefsvr treglrtyre
       61 gdpdwlttvy rdvslltqfd asgtatssst qpslmarmle aldvspgktv cevgagtfyq
      121 lallclicgt envtaidvdg dlveagiprl qragysptvl vgdgmqgcpd rapfdallaa
      181 cgvgrtpraw reqvrpggri vanlgcgivh ltveddlsar gsflpelatf mnaratveav
      241 stragwytst lvhaegktrt vpltvdpasd gprflgslvq pdavelsldl dgrhthgiid
      301 padgswarlt pagsgtahld hggprdlwae repllshwsq ggqpspdayg ltvhpdgrhe
      361 lttgdtrwnl pe
//
LOCUS       WP_457683175             268 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683175
VERSION     WP_457683175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     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 268)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30271
     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"
     Region          93..260
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 magrskplpp ptsvaellgk kvrhrreerg wtqealgakv hvshnriaqv ergtdpppgq
       61 laelldvvld fhgeivelwk lianegfkdy aktflkrqav arsihefslt vpgllqtasy
      121 ahsimeygdy tedlgdavrr rmerqhvlds edppwlwvvl eesvlfrstg srtimreqle
      181 rlleyskrpn ihlqvlrkdr pcvpgsisll tmhdgsrgay tegfntgqff edpkdveqyq
      241 riydrlhada lgtgasagli qaalrkht
//
LOCUS       WP_457683189             783 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein [Streptomyces nigrescens].
ACCESSION   WP_457683189
VERSION     WP_457683189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Plisson,C., White,H.E., Auzat,I., Zafarani,A., Sao-Jose,C.,
            Lhuillier,S., Tavares,P. and Orlova,E.V.
  TITLE     Structure of bacteriophage SPP1 tail reveals trigger for DNA
            ejection
  JOURNAL   EMBO J 26 (15), 3720-3728 (2007)
   PUBMED   17611601
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..783
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=77867
     Region          15..713
                     /region_name="COG5412"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444167"
ORIGIN      
        1 msltigeltg yieldasgar rgvaqtnqal qglqrgtdgr lrdmrgrfva asaqlgaavg
       61 ngiangttqa raeidelgda lasgvadgaq qarasaaglg dqignelsgg aqraraalga
      121 igpaltalkv smaalsggal iaggalaavp alfagigika aassaevkda ftslkdhats
      181 evrgmvgpie qqlvgiagka rqtfdqiaps lktafaavap qigtladgvl gmvqklapal
      241 aqavgaatpv iaaigsgles lggglagffq glttgaagaa qglsglfsgi sqilpalgql
      301 igqlaqaggp vlstlmgala plvsqiagal gpalaqlgpp lqtlirafaa glkpvmtalg
      361 pvlsaaagal gqlvtavspl lpmigqlaaa llpaltpilk avgtifaqla pvvqqlgqal
      421 msllapvlaq lpvivrplvg ifttlakgvl piltqliaal apalgtigka faqimvalsp
      481 vltalgelvg svlkalmpil tpiigligkl asifanvlak yisgivvptl kiltsllrgd
      541 fsgawnqaka lvanvgaflh slflklglwa kagidkavaw ikglpgrais alaplagrlf
      601 taatnafnrf nlalinkanq alawlrglpg rmasalgdlg sllvakgqdv vrglwrgiqs
      661 mgswlrstlt swaknlipgp iakalgiasp srvmarevgr wipagiaagi tggqgavega
      721 mrrlvpvpav pgvpaaagpa gygssaygra ggpllhienf hnaagstpdq taaalnwrmk
      781 arg
//
LOCUS       WP_457683197             140 aa            linear   BCT 27-JAN-2026
DEFINITION  minor capsid protein [Streptomyces nigrescens].
ACCESSION   WP_457683197
VERSION     WP_457683197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10577426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..140
                     /product="minor capsid protein"
                     /calculated_mol_wt=14797
     Region          11..131
                     /region_name="Minor_capsid_3"
                     /note="Bacteriophage minor capsid protein; pfam12691"
                     /db_xref="CDD:432722"
ORIGIN      
        1 madlldgiah llaeqqlaty dpkgvtgdlf iesmppapdc avglwlygge apdarnaydr
       61 prlqvrvrgg pdprtsrarc waiysalhgl agagladgtw lvlaaarstp apmgpdstgr
      121 hehvvnfdld vsaptshrdn
//
LOCUS       WP_457683232             200 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683232
VERSION     WP_457683232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22318
     Region          81..126
                     /region_name="HNH_3"
                     /note="HNH endonuclease; pfam13392"
                     /db_xref="CDD:433169"
ORIGIN      
        1 mraifhlwmv idhhwkdiqa dyipqevrtm drttpaerfa akvdtagplp lirgvlgpch
       61 lwtgslnnng ygtfwahgrt vkahryayeq angpipdgle vdhrcrrrnc valghldavt
      121 hrvnilrstn hvaaraavth cpaghpydda ntyrapngtr kcrscknahn raaraakrap
      181 qlapvepirp rtdhtleraa
//
LOCUS       WP_457683252             541 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683252
VERSION     WP_457683252.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..541
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=61038
     Region          24..422
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mtpldtaptf rgsptdedse pwlayirvst wkeekispel qrdaitkwar qsgrriigwi
       61 edldvsgrhf krkimrcier veggeargva vwrysrfgrd rtgnainlar lqqaggeles
      121 atepvdasta igrfqrgmil efsafesdra geqwrethnh rryklhlpaq grkrfgyiwh
      181 rrydpntgkl qkekyepdpa vgpvvadlyr ayvaafgfsi lcgrlnaagh rttqgklwst
      241 etlrrymdsg faaglltvhn pecrcrktdg tcknhvfiqg aqeelidvdl wkaylqrrke
      301 vkattprsrn giyeltglck cngcrlgtgl ntktrdgqni pgfayrcnqr aksgplacdg
      361 iliertevek evkrwlrrea atgidnapps edapepnrad elaahtaara haqrevdrqr
      421 qalarlraeh aanpddfgpg eyeeaadvir kkraeaqall dstpeaepvp drqefvplvv
      481 gtvaewptld trernnmlrq lirrvaivrh gpgaenheiq ihpmwepdpw atpkvasata
      541 g
//
LOCUS       WP_457683259             387 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Streptomyces nigrescens].
ACCESSION   WP_457683259
VERSION     WP_457683259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   4  (residues 1 to 387)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - obsolete lipid glycosylation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=40031
     Region          4..352
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mrtplsvvig aggtgghiyp glaladalrr avpeavisfv gtergletrl ipqagyrlht
       61 vdmipfdpal garryllpaa llrsggqcra llkeqnaqva vgmggypsap vivgarlagl
      121 pslihesnav pgrankfaar ltphlalafd rsrehlagge raetvgmplv gplaqldrtg
      181 lrptarqafg vpddarlllf nggslgaarl teaavglagr yrsrkdlrll iktgptalee
      241 trarlaangg davaeavpyl drmdlayaaa dlvvcragsa tvaelatigm pavlvpypha
      301 pgdhqthnar vlsdagaall lpdpetsder ldalvtplld dpgrlaamge aadpgthaqa
      361 adllaakvla laghpqtahp ltlketa
//
LOCUS       WP_457683263             352 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces nigrescens].
ACCESSION   WP_457683263
VERSION     WP_457683263.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34958
     Region          138..>348
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtqsyrrsgd empqdrpyay gddhgqgygq gygheayggt pgagfseqav ppppyaperp
       61 rrarrpvali aavalasgli gggsaaliag atqpsaqnss stplvnagkt sgsgvsgvak
      121 avspaiveir aqsakgestg sgvvvnsdge ivtnnhvlag adtvtvtfhd gsrktaevvg
      181 tdpgkdlalv kvrgaknlta aslgdsskit vgdqvvaigs pegltgsvts givsaldrdv
      241 tvpkeegqgq qggpggrggw pfefggnqyn gdtgssktsy kaiqtdasln pgnsggalin
      301 mqgqiigins amyspssess ssagsvglgf aipintvkdd ldalrgggns gv
//
LOCUS       WP_457683265             285 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457683265
VERSION     WP_457683265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29504
     Region          1..211
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mivvtgatgn igralvarll adgaavralt rdparaglpa etdtvradla dtsdltpllt
       61 gadalflnla aggdraaval tgaavragvr rivlnssmav tdtpaddthh iarlhagler
      121 avrgsglewt firggnyatn alawapsira tgvvrdahpd argvpvhead ladvaaaall
      181 drtgahlgqa ypvtgpeelt vaqqvaeigr atgketrveq iseeaaaeam agphfpkeaa
      241 lelvrmfgrt veapafpvsd averitgrpa rtfaqwardh aadfs
//
LOCUS       WP_457683269             308 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683269
VERSION     WP_457683269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=33849
     Region          38..263
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mlprvdtdde wdaivpdeav mrpgaaalct rlgiradslt rypagsqpvy avgqrfvlkl
       61 fpaaaaddgv tearvlthlq gqlplptpyv hdageyengw ryvlmsrlrg tdlavtwprv
      121 pradqdriat eagetlaalh aldpspltgf lgpgdwgafl drqrgtavar qrdhglpepw
      181 leqipaflas vapsaagpgv llhtefmrqh ltvdehddwr ltglldfepa migqraydfv
      241 avglfvsrgd prllsrifra ygetftptdl lahtllhvys nlprylrelp appeptlesl
      301 aetwfgtg
//
LOCUS       WP_457683271             348 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457683271
VERSION     WP_457683271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36764
     Region          <123..242
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mtttahlgan gtgptagdpg garepgvrgp lgglvwlvrr qhrlffglll aaaaggavwc
       61 avlrgraaaf idahhidgcs mislvarcdg tqdavvefrn tygpalqlae agllllpvli
      121 glflgaplia releagthkl vltqsvgplr wlaaktalpa lvvlavttal savfawlwqv
      181 vgdevsgsyw ystldfaalg pvpvayslla lavgvlagll lrrtvltmgv tlgamvllqv
      241 alkqlrpylm psgstefgpk esaqlpdnaw lvgqgyytrs gdhlpmevcd sagdqesclr
      301 shdvvgqymd hhpashhwpl awiesgivla ltavltvlaf rvmrhrhg
//
LOCUS       WP_457683275             287 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457683275
VERSION     WP_457683275.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31375
     Region          <41..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          110..277
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mlyaeieiss flkarraald padlglpggv nrrrvrglrr eevaqlagis vdyytrieqg
       61 rapaisdsvl daiaralrls ggevtylrni avprrpgadc aagaapgrtv rpeirqvlda
      121 mgatvpamvv grgldilawn tlgariafdl ealapdrrnt allvfldpaa rtlhpdweak
      181 aeevvgnlra dsgrhpddpr icevvnella hspdfrriwe tqsvheclrg tkrilhprvg
      241 eldvtfesfr lstdpdqalv tytaprgset errirelgal tdpvlta
//
LOCUS       WP_457683277             461 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457683277
VERSION     WP_457683277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47050
     Region          30..401
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(39..40,43..44,46,79,129..130,132..134,137,157,
                     160..161,164,245,248..249,252..254,257,284,288,337..338,
                     342,346,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 msastsgptr raglrqavve svsglprqfw wlwtstlinr lgafvatfla lyltvergys
       61 asyaglvaal yglggvissv gagvmadrlg rrptmliaql staasvallg fmtdpvaiaa
      121 vaglvglatn asrpavqamm adivapedrv rafslnywai nlgfaissta agliaehgyl
      181 tlflgeaalv lacalvvfwk lpesrptpgt pggpddadgg gpapapvsml tvlrdgrfmt
      241 vvglnlllal lfqqayvsmp vsmgqdgfss tdfgmviavn gvlvvllqip vtrfiehrsp
      301 amlligsall agygfgltal agsvamyava vtvwtlgeii nsptqmglvv rlsplhgrgr
      361 yqgmyslsws vasltapllg glvidhygad alwagcaaig tlaalgygll lrglpaqtga
      421 gagavagsqa vtapvqsata kgqaasataa qepsepsepv a
//
LOCUS       WP_457683285             157 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457683285
VERSION     WP_457683285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16587
     Region          23..149
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mgersttkfp qeildqwtgl gldlpsffsa ghlgermsvq vteaaperiv gtmpvegntq
       61 pygllhggas avlaetlgsv gamlhggptk lavgvdlnct hhrgvrsglv tgvatpvhrg
      121 rstatyeivi tdeqdkrvct arltcmlrev dtdayrg
//
LOCUS       WP_457683292             604 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683292
VERSION     WP_457683292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Scheurwater,E., Reid,C.W. and Clarke,A.J.
  TITLE     Lytic transglycosylases: bacterial space-making autolysins
  JOURNAL   Int J Biochem Cell Biol 40 (4), 586-591 (2008)
   PUBMED   17468031
REFERENCE   2  (residues 1 to 604)
  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 604)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   4  (residues 1 to 604)
  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   5  (residues 1 to 604)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     'Holy' proteins. II: The soluble lytic transglycosylase
  JOURNAL   Curr Opin Struct Biol 4 (6), 810-813 (1994)
   PUBMED   7712284
REFERENCE   8  (residues 1 to 604)
  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
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     A conserved domain in putative bacterial and bacteriophage
            transglycosylases
  JOURNAL   Trends Biochem Sci 19 (3), 106-107 (1994)
   PUBMED   8203016
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14419880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=61756
     Region          117..258
                     /region_name="Slt35-like"
                     /note="Slt35-like lytic transglycosylase; cd13399"
                     /db_xref="CDD:381602"
     Site            order(127..129,131,148,176,183..185,188,224,244..247,251)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381602"
     Region          390..>437
                     /region_name="Big_1"
                     /note="Bacterial Ig-like domain (group 1); pfam02369"
                     /db_xref="CDD:460541"
ORIGIN      
        1 maatfrrrlq rgaastavaa lvlaaltasq apgatgdaaa krqpapppad vpidggsgyy
       61 tdlpplnspv pphgsdhngq gpatgrgpae aglpatvlaa ykkaasalat ddpgcrlpwq
      121 llagigkves gqarggavda egttlrpilg pqlngrgfar itdtdngryd gdlthdravg
      181 pmqfipstws tggpdgagwg adgngdgkkd phnvfdaala aggylcaggr dltaqddldr
      241 ailgynhsee ylrtvlswya fyrngthevp dgkgvlpvhr dagrhddngg rsegrrhhgh
      301 ggkpdksprp ggsgkpgkgh kpgkgqqhdp gkpgrpdgtg ptpggtepps qkptptpepp
      361 tgpahptalv rvgdkdlstt ggaefatppq vraqdaegka vagtpvrftl paatdarfpg
      421 datavtvktd knglataptl ragdrtgafr irvttvahta pavelgatvk arpapkadkl
      481 artsdkelta tagkafaeda veikatyqdk iaagvavtat mvtddpkqpv endkgpyfkd
      541 peatgaakhk pvrtltgltt dadgllklpk iytdahpgtf llrlttadga vltvklkvaa
      601 aags
//
LOCUS       WP_457683296             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457683296
VERSION     WP_457683296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23365
     Region          19..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mteeekkkgp gagkgaaltr qgsvrrtsll daaetvlvan gadaslraia geagvrvghl
       61 qhyfptrael ikavlerald rslerlaatt glravrddps alegpagaad adevvavvla
      121 eqedpqlvrl yvevwtlaar daeiaavvre fyrkyvaqve afvrygrpdw pdelcrarae
      181 tfvalvegaa llrsgiagcr saamdeqlvr cavqllrd
//
LOCUS       WP_457683298             533 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457683298
VERSION     WP_457683298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..533
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=55130
     Region          62..526
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mkrrtllqag gglaatsval atgcdnktga aasateaaag tgaaqtnaaa aggaakgras
       61 gsawtalgks ldgklvrasd aayatarrly ntrydtlkps aiayvkhpad iaeclsfarr
      121 ydtpiairsg ghsyagwssg nnkliidvsa lskvgapsgg ttrigagakl idvyeglgah
      181 gvtipggscp tvgisgltlg gghgvasray gltcdslvga tlvtadgktv dcdrkqhadl
      241 fwalrgagng nfgvvtelrf rthpapravm ayltwpwaka akvvaswqkw gpvqddeiws
      301 achldarpgn tpsvsvaafs lggyrelqna ldkladqpgg pgpaksvhlt ptgyldames
      361 yagcstksta qchmpgslpg qtgagqlgre tyaarshffd rslsaagirt lmdqieaggr
      421 kgvsgnvalt alggavnrvg rtdtafvhrg skflaqylts wpangspgtr tawlnsfhda
      481 mrrhssgaay qnytdpgltn wksayygaaa trlaevkrty dpqrlfstfp qal
//
LOCUS       WP_457683304             108 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683304
VERSION     WP_457683304.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..108
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11340
     Region          22..100
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 mtetrhgahp rheldeviha pvrfsivatl aaaekaefaf vrdavevsds vlsrqvatle
       61 kagyvavtkg yvgkrprtwl altsdgraaf aahcqalrai agdgadgg
//
LOCUS       WP_457683306             330 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457683306
VERSION     WP_457683306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  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 330)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 330)
  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 330)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35376
     Region          7..306
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(24,205..208,211,261,279..283,286,289..290)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(54,59,84,126)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mtttniptrh lgelvvsaqg lgcmgmshgy gesddaqsva tihhaldlgv slldtsdfyg
       61 aghneeligr aiagrrdevv latkfgfanr lgeptmirgd aayvreacda slrrlgvdhi
      121 dlyyqhrvdp dvpieetvga maelvaagkv rhlglseasa atlrrahavh piaalqsews
      181 lwtrdledei apvcrelgig lvpfsplgrg fltgrytsvk glpesdvrrs qprfahgnle
      241 qnlaivekld alaaekgvst gqlalawvqh rgadvvpipg trrqkyleen lgaltielta
      301 eeltaidaaa pagriagtry devsmtfvdg
//
LOCUS       WP_457683312             669 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457683312
VERSION     WP_457683312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..669
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=68467
     Region          14..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,72,77,82..85,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,80,96..99,103,105,142,144,
                     146..147,149,160..161,164,181..184)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,80,96..99,103,144,146..147,
                     149,160..161)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,103,105,142,144,146,164,181..184)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(160..168,177..184)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgifggegrl iggryrlgir lgrggmgtvw ratdevlgrq vavkelhlde gtaepearvq
       61 reramreart vaqikhpnvi vvhdvveqdg rpwivmelve gpsladrlqs ggpvapreaa
      121 rigiallgal raahtrgvlh rdikpanvlm esgsgrvvlt dfgiaqvpgv ttltdaggfv
      181 gspeytaper magrgtgpea dlwslgvllc aalsgaspfh rdslggvlha vvydeielpe
      241 sarplhavvh gllereperr lgvaeterll rgylqsgrap ergpgghlgq gagrghgahg
      301 ahgghgghgg hgaadggvgd ggaaglaaea vagaggpggl ggpggpflgg pdvprypgpd
      361 vhaplydvpd gglpgehpps ghppsegapv agtpppgpat partpaggga grpggrtggr
      421 tpgmpirdal ddralaaaar phtgrartal lvalaavvig gvgagiavll mnqggtdggt
      481 gtggrpsrsq qasdtgspqs ggsgsaeptv tappasggtg kipagyrlvr dpegfalavp
      541 egftrsyend rvyyysqgkr frigvqlqqq vpegplgamr tahtkgpady rgyrqgqvte
      601 tthnglqagl wefvwdgsaq dggsrytydl swdeggrmid vwisspvasr teakrhfdta
      661 ldafrlsga
//
LOCUS       WP_457683315             188 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683315
VERSION     WP_457683315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20022
     Region          7..161
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          88..184
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtperpivyr eaqpadkeqi daiddsfttd tvyevvagde gfalrsafvd pplvktfpdd
       61 edgedgeddg aadgvhveva vddgtvcgfv avgveewhrr lvvqqiavas thrglgvgaa
      121 lmqracaygs rlgartawle ttnvnvpair ayrrmgfsfc gldttlyrgt ssegetalfm
      181 skelgagg
//
LOCUS       WP_457683336             298 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683336
VERSION     WP_457683336.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31801
     Region          36..80
                     /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"
ORIGIN      
        1 mrdvpghqnh ahvrrkplap lpdelsgpvr dfvaslrrmh gelgyslkql esrlpvsrss
       61 lsrylrgqsl pderllvqwc tlsftgedrl palvellhra qeaadagepa erdggpdgep
      121 radaegragg dgtetgaaat agrrrrglvl aglgtaatvl aaalavpalt ssngapdngg
      181 dgrapgtksa asatgsarlt vhnverdcqh rrtencalgl ardpyrlyrr snvvghvwhg
      241 emlravcria ngitvtdevg ghssmwfrvg hdrdqvwvpa irirpeqven talpgcpg
//
LOCUS       WP_457683343             187 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683343
VERSION     WP_457683343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20407
     Region          14..149
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mteahlttpr mtdvriahta dldaatlkaa rtllydvfdd mtaedwehsl gglhalihed
       61 gelighasvi qrrllhdgra lrcgyvegvg vradrrgrgh gaalmdaler vvrsgydlga
      121 lgaadeaatf yaargwqqwr grswaltpdg iqrtadedgc iyvlpnaaap ldldtdltcd
      181 wrdgdvw
//
LOCUS       WP_457683396             336 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683396
VERSION     WP_457683396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34112
     Region          18..334
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mspaphppgq alaptpltwl yvpgdrpevv akalgcgadv vvvdledava pdrkdhalra
       61 taellsgpvp vpvhvrvnal dgplaeneir tlaplpglag lrlpkvqgpa dvhraagwat
      121 taapvpehlp yaaegpvrpa ghavaghpap vrtpgvtatl apagppaasa lpatpalyal
      181 lesalgieha faiatahpal rgialgeadl cgelgvrdda glawprsrtv vaaraaglap
      241 ppqsvhpdvh dldglarsca rgralgflgr aaihprqlpv ieaaylpsae eiataeeivr
      301 aateeggala lpdgrfvdaa vvagarrvld lagrrr
//
LOCUS       WP_457683400             193 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457683400
VERSION     WP_457683400.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20851
     Region          48..176
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mareseaegg dgrpeaeasp ypveeiaaaw ererpgtpvs sigivtpiwq lakllgddrr
       61 rvlaragmdp atldllsvlr rsgepytltt relgrrsmvt agavsqrvar aereglvtrr
      121 pgegrprtvl veltpaghdl ieatvgqvlh reaelidglt paqqeqlagl lrillqdtqr
      181 klgddrigqv gea
//
LOCUS       WP_457683402             387 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457683402
VERSION     WP_457683402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  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 387)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /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=39722
     Region          163..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpraprsgwp tnlprhraaa kagpallllf lvgleavgma hqparphatm aaiavavclc
       61 avpsariplt vraaaaavis ltgsavllag phpaqvwglg eglallllla gvvrrapart
      121 aavlgpllgl acvltplrdl rpgiftvvqa vltvvvaays ltlrrqdaqr lrdlaavraa
      181 erlelarelh dlvahhvtgi vvqaraaryt aldgppagat ferietagse algamrrlvr
      241 vlredgarah plaglaevra mtdtfsrtgp pvvlaletga analpaevaa avhrivreal
      301 tnirkhaada tavriglrsv prgvelrvan dggaparlse qargggfgla glteraeamg
      361 grltagpape ggweltavlp ldggata
//
LOCUS       WP_457683406             595 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 35 protein [Streptomyces nigrescens].
ACCESSION   WP_457683406
VERSION     WP_457683406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..595
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64156
     Region          10..326
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtrfevgerd flldgrpvrl lsgalhyfrv heaqwdhrla mlramglncv etyvpwnlhe
       61 prpgefrdpe algrfldaar aaglwaivrp gpyicaewen ggmpewltgp lgrrvrtrda
      121 eylravdawf grllpqvvar qcdaggpvim vqaeneygsy gsdsaylawl vdrlralgvr
      181 vplctsdgpe dhmlsgggvp gvlatvnfgs garealaalr rhqaggplmc mefwcgwfth
      241 wgraqeprap eeaagalrei lecgasvniy mahggtsfgg waganragel qdgvlrstvt
      301 sydygapvde rgrptekfwr frevlagyae gplppvpepp rvladpvrav vgewapaedv
      361 maalggaeve gggpatfeel gvdrgvvryr vavpgprgry plrvrglrdr avvcvdgelr
      421 avvdtedavv gevagpasve vwvaslgrvn ygprlgeskg ivggllherq flhgvrsrgl
      481 rldaleeaga larvpfrave gagggaglyr gtltvagrpg daglalpgwr hgfawingfc
      541 lgrywdegpq rtlyvpgpvl regvnellvw ewegapapvg eeagapglyp caagr
//
LOCUS       WP_457683408             348 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457683408
VERSION     WP_457683408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=35627
     Region          32..335
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 maeklrsrsd setetlgegn vtplttplcr qlgievpvvq apigsavttd lvaavaeagg
       61 lgtlaltwvt adeavrrire vrrltprpfa vnlvldfpvd eildaclaeg vpiistfwgd
      121 psavaerars agavhlhtvg svseaerava agvdvivaqg ceagghvrge attmalvpav
      181 vdavhpvpvi aaggiadgrg laavlalgaq agwlgtrflt aceaathevy rqaviraapq
      241 davhtrcfdg gwpdaphral rnstlstwea agrpaapnrp gegavlagsa dgrtwsryed
      301 mvpvpgmsgd lealalyagq saglvhdvap agrivadiaa raaalrgv
//
LOCUS       WP_457683414             423 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457683414
VERSION     WP_457683414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  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 423)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /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=45045
     Region          171..422
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrqvvswmag acvgfaracv vvavsmlvpa vwaaavavai rwgaanpwsw mpmlvlgsvg
       61 tpalsrpvcr mfrflvatwt atdipagyrr aepvvrmstg ywwngfsyer trrdalldqr
      121 wrirwsdpat wrdlrftgia pitagviaal ppagvavavl gfgqpelsar lvgvlglvaa
      181 vagapyawrs aepvavrflr aspamvladr vaeltaqrad ttvaqaaeir rierdlhdga
      241 qarlvglgls lataeklmet dpdqakalmr earagaatsl telrelvmgi nppvlnergl
      301 idavralald spleaevsae vplrldppie salyfgiael vtnatkhara trarislsrd
      361 dtgtgtgivv dveddgrgga dvragggleg lrrrlavfdg tleitspagg ptrvrmmvpc
      421 asl
//
LOCUS       WP_457683416             243 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683416
VERSION     WP_457683416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25647
     Region          20..210
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrftsetssd gvseqfftlg eipgvlwtpe gaagtrplvl mghgggqhkk apgivararr
       61 lvaecdfava amdvpghgdr pkdeeydria tenqarvaag eelapliagf qalvarrtvp
      121 ewravldavq glayvgagpv gywgvslgcg lgvpfvaaep rvraavlglg gaqasaetaa
      181 ritvpvefll qwddervpra eglalfdala sdektlhanp gkhgeipafe ldsmlrfftr
      241 hlg
//
LOCUS       WP_457683418             205 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457683418
VERSION     WP_457683418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22215
     Region          1..167
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mritkythsc vrlehpgggt lvidpgiwse aralhgadai lvthehadhv dvlrlrglga
       61 pvyaprgadf gglldvieve pgeefsaagf avtahggrha riygelpdca nlgyliderl
      121 yhpgdslhvp dqpvetlfvp mqaswlrtse aidfvravkp eraygihdaq inerglhsvn
      181 gwldeevggc yswlppgals pcser
//
LOCUS       WP_457683422             453 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter, partial [Streptomyces nigrescens].
ACCESSION   WP_457683422
VERSION     WP_457683422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         <1..453
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          33..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(47..48,51..52,55,87,137..138,140..142,145,165,
                     168..169,172,259,262..263,266..268,271,299,303,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 plkrcpptga rgrkarltrk gwrtlveprg rtrwaiggll aggivvnfld rtaisvasss
       61 iadefgldlq qlgvvlsaft wsyclvqlpa gmlvdilgvs rltriasalw avaglltava
      121 ggvgpiilar lllgvaegps mvgaskataa wfpvsergma talfdgatkl anmvsfpvla
      181 fvmsewgwra gflfsaavsl lftvvwwwgy rdpseyrslr paerefilrg gardtdrggl
      241 rqfrsalrsg rvwtvacgfa cygytinivl twmpeflqre fhvrllqsgf ysmvpwaiat
      301 vaelavggwl vdrlirrgrd pwvvrrtvlt cglalggtig aagsagspav avcwmsvsla
      361 glaiaapvaw alpgllappg avgavsglmn flntaatagg vlltgwlaqm tgsfdapflf
      421 avavlavgva lywralrpvp vreqdparql hkv
//
LOCUS       WP_457683424             252 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457683424
VERSION     WP_457683424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 252)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28602
     Region          4..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          131..247
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mshsvgqvaa fagvtvrtlh hydeigllqp gernhaghrr ygdddldrlq qilfyrelgf
       61 pldevaalld dphtdpqqhl rrqhdlltar idklqkmaaa vehamearrm nvrltpeekf
      121 evfgdfdpde haaeveerwg hteaykesqr rtaaytkedw krvtegldav hrkmadllgq
      181 gaaadsaaam dvaeehrqfi cgtyydcspe mhtclgemyv tderftatye airpglavym
      241 rdailanavr hv
//
LOCUS       WP_457683428             382 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683428
VERSION     WP_457683428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40271
     Region          64..358
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 merlnvvlvg glhtdarraa verllrtvpg svalhhdlas atdgtvrrtv rdaggtldtg
       61 eaplvndcac calredlvpe lerlaagrtc rlaivelwds vepkamaevv tacgsenlal
      121 tgvltavdpa lllpylgcgd dlaeaglaaa asdqrtvadt warqleyapv laiatgeepa
      181 epadlallgq lhpmahqvpv eseelaaaat agfdvaaaad rqhpacallp qeaeaegvst
      241 lvwrhsrpfh perlyaaled ltcaaarsrg rfwladrpdt llswdaagga lcvenagpwl
      301 aslpdaawem vppmrraaaa ldwhpengdr tqhlvftspg ldreglrsll gsclltdaey
      361 aggppawksl ppafdalldp vs
//
LOCUS       WP_457683433             484 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683433
VERSION     WP_457683433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50413
     Region          <74..484
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnkplrraav fclalivalm gwttwlqgak asdykedphn prvtigkyaa plgnilvdgq
       61 pvtgsaatss slkykrtykd gplyapvtgf tsqifgsnql enlngdlldg sdsrlqspad
      121 altrqrakgg dvattidskv qkagyralgg kkgaavamdp atgrilgmvs tpsydpgtfa
      181 gsaatdqkaw rkmsgdadhp evnralrqpl ppgstfklvv aaaalengly psvdeptdsp
      241 dpytlphtrt kltnenkaap cknadirtal qyscntvfak mavdlgkdkv kaqaekfgfn
      301 dgevdtpvra gksvypgnmd daqtalsgig qfddqatplq mamvtsalan ggelktpqlv
      361 dkltdgggnt ieengpktyg dgkalsarsa relqsamqtv vdkgtgsgak iggltvggkt
      421 gtaqhgvdns gtpyawfvsn aedgkghrva vavmvedgha arnevsgngl aapiarammk
      481 aalp
//
LOCUS       WP_457683434             554 aa            linear   BCT 27-JAN-2026
DEFINITION  CYTH and CHAD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457683434
VERSION     WP_457683434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Lorenzo-Orts,L., Hohmann,U., Zhu,J. and Hothorn,M.
  TITLE     Molecular characterization of CHAD domains as inorganic
            polyphosphate-binding modules
  JOURNAL   Life Sci Alliance 2 (3) (2019)
   PUBMED   31133615
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Tumlirsch,T. and Jendrossek,D.
  TITLE     Proteins with CHADs (Conserved Histidine alpha-Helical Domains) Are
            Attached to Polyphosphate Granules In Vivo and Constitute a Novel
            Family of Polyphosphate-Associated Proteins (Phosins)
  JOURNAL   Appl Environ Microbiol 83 (7) (2017)
   PUBMED   28130300
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Martinez,J., Truffault,V. and Hothorn,M.
  TITLE     Structural Determinants for Substrate Binding and Catalysis in
            Triphosphate Tunnel Metalloenzymes
  JOURNAL   J Biol Chem 290 (38), 23348-23360 (2015)
   PUBMED   26221030
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Bettendorff,L. and Wins,P.
  TITLE     Thiamine triphosphatase and the CYTH superfamily of proteins
  JOURNAL   FEBS J 280 (24), 6443-6455 (2013)
   PUBMED   24021036
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Kohn,G., Delvaux,D., Lakaye,B., Servais,A.C., Scholer,G.,
            Fillet,M., Elias,B., Derochette,J.M., Crommen,J., Wins,P. and
            Bettendorff,L.
  TITLE     High inorganic triphosphatase activities in bacteria and mammalian
            cells: identification of the enzymes involved
  JOURNAL   PLoS One 7 (9), e43879 (2012)
   PUBMED   22984449
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The catalytic domains of thiamine triphosphatase and CyaB-like
            adenylyl cyclase define a novel superfamily of domains that bind
            organic phosphates
  JOURNAL   BMC Genomics 3 (1), 33 (2002)
   PUBMED   12456267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18995808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..554
                     /product="CYTH and CHAD domain-containing protein"
                     /EC_number="3.6.1.25"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050355 - inorganic triphosphate
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=59237
     Region          7..188
                     /region_name="CYTH-like_Pase"
                     /note="CYTH-like (also known as triphosphate tunnel
                     metalloenzyme (TTM)-like) Phosphatases; cd07374"
                     /db_xref="CDD:143620"
     Site            order(7,9,11,44,58,60,62,73,83,117,119,138,165,167)
                     /site_type="other"
                     /note="putative active site"
                     /db_xref="CDD:143620"
     Site            order(7,9,136,165,167)
                     /site_type="other"
                     /note="putative metal binding residues [ion binding]"
                     /db_xref="CDD:143620"
     Site            order(7,9,11)
                     /site_type="active"
                     /note="signature motif [active]"
                     /db_xref="CDD:143620"
     Site            order(9,11,44,58,62,73,83,119,165)
                     /site_type="other"
                     /note="putative triphosphate binding site [ion binding]"
                     /db_xref="CDD:143620"
     Region          262..548
                     /region_name="CHAD"
                     /note="CHAD domain, binds inorganic polyphosphates
                     [Function unknown]; COG5607"
                     /db_xref="CDD:444338"
ORIGIN      
        1 madtvreier kyeadndtql pdlagigpva avaeagtedl dalyydttgl slaadgitlr
       61 rrtggrdagw hlklpvapgv rdevraplsd vpppeltalv rsraldqelv pvvrlrtrrt
      121 vrvlrdaagt plaevaedav hawpaagavg agesgagrag arwreievel lgegdtglld
      181 eigralaaag vrpasaaskl aralaetgqg rdgaaaphta gpdgrradgs gkaaakaksr
      241 akskgkgaaq gkaagagkkg qtagdvvlry ayeqvraiie lepavrrdlp dsvhqmrvat
      301 rrlrsafrsy tkvldravtr pigvelkwla aelgverdre vltgrlqeal agvpgtlrlg
      361 pvdarlriws errragardq llavldgprh lsllkslhaf leepplrkaa grpapevvag
      421 avlkdyrrla rrteaalaap agrerdealh garkaakrtr yaaeaarpal grpakkfakr
      481 tkrvqqllgd hqdsvvarat lrelatqaqr ageggftfgl lygreealaa dreralpdlw
      541 rkvsrrkhra alrp
//
LOCUS       WP_457683450             501 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683450
VERSION     WP_457683450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51809
     Region          11..496
                     /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 mqerssgael aailraelnr yspgeklpss ralverhrvs pvtvsralae laaeglvttr
       61 pgagafraep rseaprpvdt swqeialsae pggdqvprsv dasgvvatlg vpgpgvieln
      121 ggylhsdlqp eralaaalar agrrpgvwgr ppvegvpelr awfareiags ggplaasdvl
      181 vtaggqsalt aalralaapg apvlvespty pgmlavaras glrpvpvpld adgvrtdlla
      241 dafrvsgarl fvcqplfqnp tgavlaaerr revlrvaraa gafvieddfa rllvhgdapt
      301 lpptliaddr dgtvvhvrsl tkatsanlrv galaargpvl drlraiqvvd sffvprplqe
      361 aalelvgspa wprhlrliag eltarrnalt aalhqqlpal agpepgtgaa yghdaapggl
      421 yvppggyhlw lrlpdgtdeg altgaalrag vavaagrpyf paeppaahlr lsfasasgtg
      481 eitegvrrlr aaceelgvpv s
//
LOCUS       WP_457683451             321 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457683451
VERSION     WP_457683451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32522
     Region          52..297
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrsndsatat vtiavstpda agqdtptaaa apargtlvsr gallaalgva afsltfpata
       61 walegmgpwt vvmlrsvlaa vlaggalavf rvrlperrhw tgiavvaggv vlgfpllttl
      121 alqtsttsha avvigllplt taafsavrtg arpsrtfwia slvgavvvig favqqsggap
      181 grsdlllfaa llvcaagyte ggrlarhmpg wqvigwalvl alpvtvagaa valsteplrl
      241 tahaiagllw latgsqflgm vawyrgmaai gihkasqlql aqplltlvws vlllgeqlpp
      301 aapaaslavl aciavtqrsr g
//
LOCUS       WP_457683453            1176 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457683453
VERSION     WP_457683453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1176)
  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 1176)
  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   3  (residues 1 to 1176)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1176)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1176
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=125325
     Region          1..237
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          173..1129
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhygilgttq agradgtpva lggarlrall aalalrpgra lspelligdi wgaeppadaa
       61 galqalvgrl rralghaaia svdggyrlca epdavdlhrf erlateggra lgeadparaa
      121 allddalalw rgpaladlpd asveasraer rrldaqctri aadlalgrat qslptllalc
      181 edhpldeplq alrlhalraa grtaealaay eeirtglaer lgadpgpelr tlhaellrpp
      241 pptdrpplap ipgtpaaapa pngtgtsygt gmgtsygtgt aygsgtphsp gtpspgtsst
      301 epphshphph phpqphphtr pgnlrarlts fvgrdtdlaa iradlaahrl vtllgpggag
      361 ktrlsqegae taaaalpdaw phgvwlaela pvddpqtvpe avltalgare tvvrgttadg
      421 lraaadptal dplarlaehc agrrmllvld ncehvidaaa elaerlladc pgvtvlatsr
      481 eplavpgevl rpveplpdpv alrlladrga aarpgfrved dpaacteicr rldglplaie
      541 laaarlrlls prqladrldd rfrlltsgsr tllprqqtlr avvdwswdlt deperavlrr
      601 lsvfaggcdl aaaeevcagd gvdgrevagl lgslidkslv vaapagqegg agraagtggq
      661 mryrlletvg eyagerldea geragaerrh lvayrelart tdpllrgpgq ragmerlele
      721 hdnlrtalrr alaahdehea lclvlslqwf wslrdhrsda rhwstaaaal gpnpfaapae
      781 papdlherpi dtpppmapeq llearreirl valasrdsdi talrdpamqe eltgmltayr
      841 sgmpqtckvp gvmwyyavli tgefdelael vdgavracrd fgydwelayv lqlrskifnd
      901 rpgglaqaar dadealrlfl rlgdawgaae alsgrgenhe krgaygaaar dyraamvhae
      961 dlgahgqill lrcrlgavli edgqaetger mlrevladae kgnsvrdtep farltlamwl
     1021 taterlqear aqlrrvqelf tsrapdlfag llqalsisld vdeghregll prfrqslelm
     1081 qdslaqivap dlpvvqlltg arvlmaerge kggwdaarlv gaydvmradg qvppllvrrd
     1141 rdrteaaara llgdtayara haeggglslg eatali
//
LOCUS       WP_457683463             193 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457683463
VERSION     WP_457683463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 193)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20869
     Region          20..183
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(32,48,91,119..120,132)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mtamahapmp tdeetlldyf laletplgfr aeliegeivv tpptdgtheh cfsgivsqim
       61 rqsavdmdvs gykglemprg grcpknhvip datiapralp lfhgappwmp sdgvamvvev
      121 tssnperdrk akrhcyarag iplyllvdrs raeitlfsdp sgddyaghst apvgkplplp
      181 apfsfdleta efl
//
LOCUS       WP_457683465             198 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457683465
VERSION     WP_457683465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=20468
     Region          23..101
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 msielpgevv wimelmglew pdidedelra waghvrefgq slkeshddtd sllkgladay
       61 egasydalls rwgkasgehl ttlttccdvl atalevtatg vvvakgvvia qlvitaveia
      121 aaaaatvatl giaaaaeaaa ieigkriire iiqeiedvli aelvsmaiep fqaeiekavs
      181 glvfkgvdaa lgaaggaa
//
LOCUS       WP_457683472             400 aa            linear   BCT 27-JAN-2026
DEFINITION  FUSC family protein [Streptomyces nigrescens].
ACCESSION   WP_457683472
VERSION     WP_457683472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44332
     Region          36..234
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 magevsgrrt rpartgrmar vrrwwgralg segherstvl liakgtlaat iawvisyhll
       61 haqspafapf savlimqvtv yqsllqssry vgavvagvav qaalgflvgp dvpafalval
      121 valtigrwpa lgsqgsqvat aaffafstyv satstldkvt qlgqiillvl igcgigvlvn
      181 vtvlpplryr saehgirtla halcdlvsdi ypalrergld eertgrwrar aeqtgelvtq
      241 artglrmare slhynprrlf rrgrahtyfe gyaavleale rtlrqvaalt rsldkwsade
      301 dryrygafla sytdflesls hitrvfadld edrlgdqtsq lhqladeaqn yrrrlaeqae
      361 rddlpltdpg rpygvlviea arlmeefqyt cdvlqhhver
//
LOCUS       WP_457683475             120 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457683475
VERSION     WP_457683475.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..120
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12566
     Region          20..103
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(28,30..32,38,63,65..67,69..71,74..75,97,101..102)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            66
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mtappsddrs atiatpdrrt ahlhlsgdld httadellal avrqmaaqpg lrdlhlncaq
       61 vracdpmgls vlltlhrrts aagihlhldd rppaldrllt vtgtlgplts ppgrsssttg
//
LOCUS       WP_457683476             403 aa            linear   BCT 27-JAN-2026
DEFINITION  cobalamin B12-binding domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683476
VERSION     WP_457683476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Krautler,B.
  TITLE     Vitamin B12: chemistry and biochemistry
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 806-810 (2005)
   PUBMED   16042603
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Marsh,E.N.
  TITLE     Coenzyme B12 (cobalamin)-dependent enzymes
  JOURNAL   Essays Biochem 34, 139-154 (1999)
   PUBMED   10730193
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472039
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="cobalamin B12-binding domain-containing protein"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42537
     Region          15..219
                     /region_name="MtbC1"
                     /note="Methanogenic corrinoid protein MtbC1 [Energy
                     production and conversion]; COG5012"
                     /db_xref="CDD:444036"
ORIGIN      
        1 mtlspapmte slagyvdhlw davvavdeht avrgvfdavd agvppedvll diiapvqhrv
       61 gehwaanrmt vaqehaatai ndrviaalah hrppaaaaer gritvacvdg ewhalparll
      121 aevlrlrgwr vdflgaqvpa phliahlhrt gpqavglsss iatrlptaha aitacqavgv
      181 pvlvggaayg pdgryarllg adawapdart aadflsrgmp dtrppalghq pvddlphlsd
      241 qeyslvtrta pqlvketltq leerfpalrd ysdrqrqhta edlahitdfl atalytddde
      301 lftgfltwtg siltargvpa hslhpaldal saqlkdfpra rrilgharrs ldtgtrtgpg
      361 tgpgtrvdtg pgpgpgpgpg tgtgtridtr tdtgpssglg ssv
//
LOCUS       WP_457683478             555 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457683478
VERSION     WP_457683478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=58088
     Region          97..534
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mvkssgvsaa tatasvagvd vgaawqsaph pvlvispsgv vravndaaap lfpamragap
       61 fddaparwla dahqrftdpl rsedgdpvrg pvgdrsfear psraengdvv wwlvddtarr
      121 saedalraer ertgflaqas tellaslnag rcmdvtarla aqhladaavv vtppagrrwt
      181 vsfcgpdgqv vrdkavadpa svpglaealr gfppvpsrwi dpaavpdrfk psalgdigsv
      241 vvtplpghgv aagalilmrr sghaafnese etfarlfaar agaamsaarl yaeqaaitrt
      301 lmrellpprl eqvsgvefag gyrasndtdr vggdfydvha gagpdeeslv vlgdvcgkgl
      361 eaavqtgkir ntlhallpla tdhqrvlrll ngalldsdht rfatlvlasv arrggtvrlr
      421 vtsaghpapl vvrvdgrvee adtrgslvga lpevtsktas ldlapgescl lytdgiteam
      481 ggpmgeelfg eerlrsalse caglpaeavv erirmlsaqw vgtgrhddma vvaitaphha
      541 hlsavdghtr gryta
//
LOCUS       WP_457683484             215 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457683484
VERSION     WP_457683484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22374
     Region          7..201
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 maahsltvgf dldmtlidsr pgiraayhel sartgtfvda dlavsrlgpp leeeirrwfp
       61 aervaetadl yralypahav tattalpgar ealgavrsag grtlvvtaky epnaklhlah
      121 lgldvdalfg slwaegkaea lrkhdaqiyv gdhtgdivga htagalavav atgpcdatel
      181 haagaevvln dltefpswla ryvaegadgg eaaat
//
LOCUS       WP_457683491             702 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces nigrescens].
ACCESSION   WP_457683491
VERSION     WP_457683491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..702
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75859
     Region          24..701
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpshahhptt eprtessgpr pgsddplqre kshlaasrsa lramradaea lniadvtanw
       61 vnaevlqgei darikaladl shtplffgrl dylhapglel aegaagenfy igrrhvhdad
      121 gdpmvidwra pvsqpfyras kkdpmdlklr rrfgytggel tayedehltd pteavrtsal
      181 lqseierprv gpmrdivati qpeqdeivra giggsvcvqg apgtgktavg lhrvayllya
      241 hrerlarsgt lvigpnrsfl hyieqvlpal gelevkqatv ddlvghvevr atdeaaaatv
      301 kgdarmaevl rravrshitm pqepcvvvrg srrwrvpaye leeivqelrd reirygaare
      361 alpqriahav lvrmeqagea pddrvqdava rntavkaavk avwppvdpak lvlrllgdae
      421 fladqaegil tpeeqktilw tkparsvksa kwssadavli deamdlvart pslghvvlde
      481 aqdlspmqyr avgrrcttgs atilgdiaqg ttpwatdtwe ealthlgkpg saveeltqgf
      541 rvpreviaya srllpaiapd lteatsires agdfairtve padltaatlt acgdalakeg
      601 sigliaaear ipalrtalea agvsclapge etsaearltl vpatlakgle ydyvvldepa
      661 aivdgepder tglrrlyvcl trpvsgltvv haaplpeqla dr
//
LOCUS       WP_457683504             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683504
VERSION     WP_457683504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27170
     Region          34..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtstettpaa paqapapglr ltlddaalgr pgapvldhld ldvaageilt vvgpsgcgks
       61 tllrtlagll pllggrltqd gepvggpaad ralvfqedal lpwrslranv elplairgva
      121 raqrraradd wlarvglteh aarlphqvsg gqrqrtqlar alagrpravl mdepfgalda
      181 qtragmqqll vtalsgtrat vvfvthdvde alflgdrval lgsgrvldvp rprlrgahsd
      241 patvalrrev ltsldgrpgs
//
LOCUS       WP_457683508             374 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457683508
VERSION     WP_457683508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39646
     Region          7..358
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpslsprwpr yvesapsvlv agglvwdafs padywgdpml taasvtagal lslrhtlaig
       61 aaivggvfal tvkdgtagdi vgylelintv faalmgvgvn rviarhgrrl dvvrsvaeaa
      121 qravlpappe rigplsiaar yqaaqseari ggdayavqrt pfgvrlliad vrgkglgavg
      181 avsvllgafr eaaeeepdla tladrmeral lresehtsee drlegfital lcevlpgaag
      241 lrllncghpa pylchddevr vleagdpglp lgmgtlgver tcpadrpfpv gstlllvtdg
      301 vteardrtgr fydpatqlas qgpfrgpqdv idqlvrdver wtggprdddm avlaltrqre
      361 grmriprsgs spdh
//
LOCUS       WP_457683513             601 aa            linear   BCT 27-JAN-2026
DEFINITION  M4 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457683513
VERSION     WP_457683513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 601)
  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 601)
  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 601)
  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 601)
  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..601
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..601
                     /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=62823
     Region          37..597
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrrphirrhr laiavavtta atltagvags asatppaspv aassstpasq kvvdtaraaa
       61 fahtsatgvs kkdtleatdt lvdpdgrqhv rfvrthrgmp vlggdlvvhl taksayegvt
      121 rayrhqvdvs gtdaklsage artkaaavak gragdaelvv darngrttla yqvevadsgt
      181 aesggvrtvv ldaasgtvls nvqaddsfls palqrklrar gerlnpatgl ftpaapaagk
      241 aakaagfpaa akgtgasffv gsvplsttqt akksftlkds trgntetrda gdkelekfss
      301 gkaftsttnr wgngttsnra taavdaqygi astldfykka fgrkgikndg rgaralvhfg
      361 kkvgnafwsp dcgcmlygdg dgrtftkplv vldvtghels hgvvdatanl qptrvdiegn
      421 qfgepgslne sladifgsav efsannpknp pnyllgeklg ldqkflrrld kpsldklega
      481 vdywskasyd tevhagsgvs shayyllaeg sgkktiggva ynspthdgsk vtgigrnkat
      541 aifyraltry mvsttdfhda rtatlhaakd lygaksteyk tvdkawaavn vkasntpsak
      601 h
//
LOCUS       WP_457683520             296 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces nigrescens].
ACCESSION   WP_457683520
VERSION     WP_457683520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=30269
     Region          2..259
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mttppallia ghgtrdegga dalralvhll gerhpevpva ggffgvpasp lplddaidgl
       61 vgeganrlav iplltaptgp vpealpqvle ragerhpglg hvcgtelgph pklldvlerr
      121 ldealgsgar rpadrarttv llvgrgaadp yanaevvraa rllwegrgfa gvetafvtqa
      181 apdvpagldr cralaaaagt ggparvvvlp yflfaggpve rlwmqaegwa aahpdtevya
      241 aqvigpeaev advvmeryra avagascgcr aaaedarpah gapresasla agtger
//
LOCUS       WP_457683533             225 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457683533
VERSION     WP_457683533.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..225
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24811
     Region          6..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mpaggdssvi rrstlrqqia dalrdevlag rlpsghpftv keiaeqygvs atpvrealld
       61 lcaqglldve qhrgfkvhaf taedframve artliiegif rsgadqalra tsagvlisir
      121 rradeaeraa ragdldvlig ydlrfwrels sivnnayisd fldrirvqtw mfavpllrre
      181 pdlkgllwqg hsaladaliq hdlataqrli aeynehslal vgtrg
//
LOCUS       WP_457683535             207 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683535
VERSION     WP_457683535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22257
     Region          4..181
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mkpvtltter lvlrpfepsd apavhtacqe pdiprwtnvp spygvadaeq fvgtavpesw
       61 rndtayhfav vtradgalag amglvslarl htperqaelg ywaakeqrgr gytveaarav
      121 lgwafrdlgv ermewhaeag negsravark lgfrmegtlr aklvregtrr dvwigsllps
      181 dlpegpgpsg sggpaapdat pylpypg
//
LOCUS       WP_457683537             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ComF family protein [Streptomyces nigrescens].
ACCESSION   WP_457683537
VERSION     WP_457683537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=24694
     Region          1..201
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mqgvwrelag lvlpvdcagc grprtelcae crrvlardgr garrvrpwpe pgglprvwag
       61 apyadevrav llahkergal rlagplgaal agavrglrag ggplllvpvp sarrsvagrg
      121 hdpvrriala aagelrrtgt garvltvlrq rrvvadqagl sarqrlanvt galevragag
      181 rlltgraavl vddlvttgat laeaaravta aggrvagaav vaapssafes dgariealpr
      241 gk
//
LOCUS       WP_457683553             516 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683553
VERSION     WP_457683553.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..516
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55239
     Region          6..503
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtgttfwdlv arraartpda paliqgaesa rqerritfga lhrraervaa glyetgvrpg
       61 srvvwqlptr ietvlfslal arigavqspv vplyrahevg qvlrrtraaf favpgvwrgf
      121 dhramadrla aglpgpltvi eaydtlpdad pavlppppad ddevrwiywt sgttaapkgv
      181 lhtdrslrta grwlgaalrl gpsdigsmaf pyahvagpdy tvmllehgip avllehfalp
      241 galaayrrhr vtlaggstaf yalflaeark lppgrrllps lrllagggap kppalyhevv
      301 aglgcqlthg yamteapmvt mgdpydspgh lagtdgrppa gmeiriapgs geirlrgpav
      361 crgyldepap fdadgflptg dlghltpsgh lvvtgrlkdi iirkgenisp qeieellsrh
      421 pdiadaavvg lpdttrgerv cavveqppga reltlatlsa hllshglaph klpeqlellp
      481 alprdttlrk vrkqqlrerf gdggpgrgea pdpppq
//
LOCUS       WP_457683558             308 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683558
VERSION     WP_457683558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32883
     Region          86..308
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mplpqefhei akrvnnwgrw gaddeigtln litgqvvrea aagihsgrri plalplrhdg
       61 vqtglipgrv nplhtmtain qeifgpgtva tsddavtmgl qsathwdglt hvshsgrlyn
      121 nrpadsvtah dgatclgiek atplvsrgvl ldvarargtd vlpgghavtp edldaaeela
      181 gttvragdia lvrtgqlrhy lagdrqayaf pspglslrtp ewfhardvaa vandtltfei
      241 fppeienlwm pvhalhlvem gmlqgqnwnl eelstacaee gryafflsam aepfvgasga
      301 pvapvail
//
LOCUS       WP_457683574             413 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683574
VERSION     WP_457683574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 413)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 413)
  AUTHORS   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 413)
  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 413)
  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..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /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=43552
     Region          1..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 msrlqaehly kvfgrrpeda vrkleagagr eelraegtta avidasievd egqifvvmgl
       61 sgsgkstllr tlngllepta gtvrfdgqdl tslsakelrk vrsekismvf qhfalfphrs
      121 vlenaaygle vqgvpraern rratealelt glkgwekswp delsggmqqr vglaralatd
      181 adlllmdesf saldplirrd mqdqllelqk tlkktivfit hdlneamrlg driavmrdgr
      241 ivqigsaedi lvtpandyva sftqdvdrtr vltagaimae vgtvlgattp egrklttaae
      301 fraaapatvg vdtplvelft pcststvpva vtdehgdlvg avaaerllav lgegdrqaaa
      361 ggvpaqapaa dgtavalgkt pavdapagdp aaakdsvatp gdndpedkvi aga
//
LOCUS       WP_457683582             230 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457683582
VERSION     WP_457683582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 230)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..230
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23914
     Region          1..87
                     /region_name="HTH_MerR-like_sg5"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04780"
                     /db_xref="CDD:133407"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133407"
ORIGIN      
        1 mrigelsret gvaiptikyy vregllpagr ltspnqasyd dghvrrlrli rglidvgglt
       61 vsavrevlaa vdspgepvhe vlgaaqhait prpaatpegm erarqsvael irhrgwrvgp
      121 dhpafealav alatfrgvgr gefeeilddy aaacervaaa dlawlgrnae vdgmvecvvv
      181 gtvlgdavla amrrlahvea sarkfegaae gaaaegaage gavaegaggr
//
LOCUS       WP_457683586             174 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457683586
VERSION     WP_457683586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17775
     Region          1..168
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtlyttldsp lgelllvgee satapgglal aslsvpgqkg gatvqdgwty apaafadiah
       61 qlrayfdgkl trfgiayapa rgtdfqrrvw qaleaipygt tttygkiaad igaargavra
      121 igtaiganpl lvvrpchrvi aadgslsgya ggpvrkrqll giegalpgvt pdal
//
LOCUS       WP_457683590             865 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457683590
VERSION     WP_457683590.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19095030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..865
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86401
     Region          41..483
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide)-like multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17504"
                     /db_xref="CDD:341047"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,165,
                     168..169,172,296,299..300,303..305,308,342,346,396..397,
                     401,405,421,424..425,428..429,432)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341047"
     Region          <618..>852
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mnrtttdqlp ertvgtpavp pvsdpavvgk rrssggvvpv lafsgivvav mqtllvpvik
       61 dlpvllntta gnatwvmtat llagavstpi mgrlgdlygk rrmlltslav mvvgslicgf
      121 tsdlvtmivg ralqgfamga iplgigimrd elprerlgsa mglmsssigv ggglalpaaa
      181 lvaqhadwha lffgaaglgv lsmlltllvv petairaqgr fdvagaigls aglvalllpl
      241 tkgsdwgwgs pttlvlfgva vlilvlwgvm elrladplvd lrttarrevl ltnlasitvg
      301 vafyaislvl pqllqlptst gyglgqsmvv aglcmaplgl tmmfvaplya riaarrgpkv
      361 slllgmlvia igygagiglm naawqtviia vvvgagigla ysslpaliig avdasetgaa
      421 nglntlmrsi gtsvssavig mvlahmsksv gpvtvptmag frvsfliata avligvalas
      481 flpsqrkapr ptliaqstdg eaagaadtdg argaarpage taaplaatlp apadppapae
      541 paavaeaaep aeltasagql aplvkpapsw aqpvterhta parpapdatt gvagavavag
      601 agagagadaa gfrgrvvdts gspvpgasvt lidrqgrqag vttadadgry aldassagiy
      661 vltgaapght pyaasatyhg kggstrvdli laptgglggt llggaegtpl aggsivvtda
      721 egavvtrtts gaegswhvpq lppghytlvl savghqpqar amelsggape rqnahlqpma
      781 tvrgtvrgpg grpltdaavt lvedgtvagh tvtgpdgafa fsdlrgrhyt ltaagypphs
      841 apisltagas etldlelaqq ptaag
//
LOCUS       WP_457683592             607 aa            linear   BCT 27-JAN-2026
DEFINITION  2-isopropylmalate synthase [Streptomyces nigrescens].
ACCESSION   WP_457683592
VERSION     WP_457683592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Frantom,P.A.
  TITLE     Structural and functional characterization of alpha-isopropylmalate
            synthase and citramalate synthase, members of the LeuA dimer
            superfamily
  JOURNAL   Arch Biochem Biophys 519 (2), 202-209 (2012)
   PUBMED   22033339
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11480026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..607
                     /product="2-isopropylmalate synthase"
                     /EC_number="2.3.3.13"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003852 - 2-isopropylmalate synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65461
     Region          38..602
                     /region_name="PRK03739"
                     /note="2-isopropylmalate synthase; Validated"
                     /db_xref="CDD:235154"
ORIGIN      
        1 mprttsadrt aaggfptlrt pagpvpadap awnpqrgsam pahryrpaqd rvevpltgra
       61 wpaarierap lwvpvdlrdg nqalaepmdt prkrrmfdll vamgfkeiev aypsasrtdf
      121 dfvrhladsg avpddvtvvv ftparrelie rtfaaieglp rtvvhlytpt aptwrevvlg
      181 rgraevrdlv ldaathmarl aaarpgadir fqfspevfnl tepdlvleic ngltdlwdas
      241 pdrpvthnlp atvevatpnv yadqieymhr hltrrdavvl svhphndrgt gvacaelavl
      301 agaqrvegcl fgngertgnv dlvtlalnlh tqgvdpmidf ldlstvrrtv edcirlpvhp
      361 rhpyagelvh tafsgthqda iskglahhar raaglgvpes eapwtvpylp vdpadlgcty
      421 eavirvnsqs gkggiahllq lhhgldlpqd lrpdfsrtvq ratddsgqea tpkelwelfr
      481 gtylapgeeg pltldswsat epapgehrvv csfgggnaad grrryegsgn gplaaftdal
      541 aaarhpvgil syaehalapg pdsaavayvr criggatywg agrdtsvlma svravlsavn
      601 rakgevs
//
LOCUS       WP_457683605             451 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683605
VERSION     WP_457683605.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..451
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48195
     Region          64..448
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mtfaalaqap drrrtearll alvvviavfg ytytglsmsg rlpdglavft vsmllmallp
       61 hlvlrrfapr adplilpvat lltgiglvll hrldityaqt prlktaaaan gqlvwtaigv
      121 avciaillil rdhrilqryi yltmvialvl lmapaffgad mygakrwill gplslqpgef
      181 vkimisvffa gyltvnrdal alagrralgi qlppgrqlap iftiwaisll vliferdlgt
      241 sliffgvfvi mlymatdrts wvvcgllmat vgaavvgsle phvhgrvtaw ldpmraftka
      301 gqaehmsdql gqallsfgsg gisgsglgqg hpeligfasn sdfilttvge elglagvmav
      361 imlyvllaqr glrvglsard pfgkllavgl sgalllqvfv vsggvtglip ltgkalpfla
      421 kggsslvanw vmvalllris dhaqrrrepv r
//
LOCUS       WP_457683607             263 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces
            nigrescens].
ACCESSION   WP_457683607
VERSION     WP_457683607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27397
     Region          110..212
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mrrepvdika mawfltvafl aagvlgalqp atripgeviq ltqfgpalgv glaallwpgr
       61 vrevlagpep drrgrgvlll vtapviials vlayaaltgd ahsarpgapf lliavaqlig
      121 acgeeigwrc flqpllrtrl gplaasvtvg vawgvwhvqv farhpvyaga fitaavsmsv
      181 vmgwalegvr asrlllaggf halinlgmll fmdeesgavl pmvlfgascl aaagvwtwrs
      241 vgrqgsagss apakippvmd dvr
//
LOCUS       WP_457683609             424 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457683609
VERSION     WP_457683609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 424)
  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 424)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45018
     Region          48..197
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          175..415
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfdnprtgas racvavgrcq laslhalavs amgslvvlal llvpvgvgfr llppaaralr
       61 vlsdrsrsra erwtgvrigp peplpvdral narkrsgaii adegfwrdla wawlepvigg
      121 llvavplali eygafgalvq pfiwrlindg nwyafipvhs tatmcgalvl glafmavgll
      181 aapavlrlht rvsrpllsap rssrlaqrve rltdtraral daqaaelrri erdlhdgaqa
      241 rlvalgmtld ratrlmetdp aaarellldv rrtsegalqd lrelvhgihp pvladrglgd
      301 avrslaldsf ldvhvetrlp gkppapvesa ayfavseala naakhsgare vgvaltyeng
      361 slratvtddg hggadpsrgt glagvrqrld tfdgtldlhs pqggpttvtm eipcalsspk
      421 tsss
//
LOCUS       WP_457683613             495 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457683613
VERSION     WP_457683613.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53797
     Region          46..456
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(154,156..157,290..294,314,317..318,321,336,340,395)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mrhrllvpga aalslllavp asaadftpga pgvgdtyype sgnggydvsh ydlrlkyqpk
       61 tdllegtatl latttqdlsr fnldfglkvs eiringkkas fatsgkhele vtpatplekg
      121 kqisvvvrya gkpsevkidg ysawartpdg gvvaqepdaa vwwfpsndhp tdkatydisv
      181 avpdgtqals ngvlasqssk lgwtrynwrs dkpqatyltt lavgkfditt dktanglpvi
      241 navskdlgsh egsakasier tteitewles vfgpypfnav ggyvpnvpag yaletqtrpf
      301 ygkkvfdrgt nvsvvvhela hqwygdnvsl kdwkdiwine gfaaysqwlw sekegegtaq
      361 eladwvysqh paddpfwtvk pgnpgaenqf dgavydrgal tlqalrnkvg dkaffgilks
      421 wqtenkygna svadfvkfae kksgkelagf fdtwlfqpsk ptagaakkal garqtpvaep
      481 kswkqiaath dthgh
//
LOCUS       WP_457683615             447 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457683615
VERSION     WP_457683615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 447)
  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 10154696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..447
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48548
     Region          103..327
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06242"
                     /db_xref="CDD:349461"
     Site            order(113,116,163,172..173,202..203,208,294)
                     /site_type="active"
                     /db_xref="CDD:349461"
ORIGIN      
        1 miprphrlav vpltigltat lgatppaapt aptatpaprt gfetshgarw tgqaeeqdfl
       61 ravdrgsvrv ridrigttgq grpvqlvrig apapdrpaev rrgnsvllic sqhgdepsgr
      121 eaclttvrdl ayardaatrr flertsvlvv ptanpdgraa dtrgnadgtd inrdhialqt
      181 aegramaevi rdyrpdtvyd lheygptvpy ymkdvlslwp rnlntsggvh reagalsqdf
      241 vrpavhragf stgvygiwtd petgdpvkqv agdgqerilr ntagvkgsvg llvetrvdal
      301 teaekadpaf nnrrrvdsql aaldgaftff drhrsrieaa ttaarlagyn dhgpvylgga
      361 dnepatdaqi lahppcayrl eerqfaqvre elvrhgvvwr rdrdgvvvpl rqplrklipl
      421 lldqragyhl tvatplnvcr rvvggng
//
LOCUS       WP_457683617             565 aa            linear   BCT 27-JAN-2026
DEFINITION  BCCT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457683617
VERSION     WP_457683617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..565
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59649
     Region          6..522
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mtdlpdgpqk ngppqtdrvv fgvtalltla figwgasste slknastsml nwvidnlgwa
       61 fvlsasafvi faiwlavsky gritlgkege epefrtvswv ammfsagmgi glmfygvsep
      121 lghfttpppg tdpqdaaqam dtamattlfh wtlhpwaiya vvglaiaysc frrgrrqtis
      181 avftpligsr rangwggrvi dilaifatlf gsaaslglga lqigsgikvl gwmdsvsttl
      241 lvgvitvlti afilsavsgi akgvqmlsni nmvlalilav fvfvvgptil ilnllptslg
      301 sfigelpqla grteagsgdd vggwlrswtv fywawwiswt pfvgmfiari srgrtirqfi
      361 ggvilvpsvv slvwfavfgg samklqeskq lsgsstpegq lfdvlhqypl atvtsvlvmi
      421 lvgiffvsga daasivmgtl sqkgtfeptr lvvifwgvvt gavaaimlli gggsgdaltg
      481 lqnltilvav pfmvvmiamc walmrdlrsd plivrgqkge eavelaviag heqydgdfef
      541 qigpggtgng dgtgedsgag vksgg
//
LOCUS       WP_457683619             638 aa            linear   BCT 27-JAN-2026
DEFINITION  Xaa-Pro dipeptidyl-peptidase [Streptomyces nigrescens].
ACCESSION   WP_457683619
VERSION     WP_457683619.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11480810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..638
                     /product="Xaa-Pro dipeptidyl-peptidase"
                     /EC_number="3.4.14.11"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008239 - dipeptidyl-peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67521
     Region          <22..600
                     /region_name="PRK05371"
                     /note="x-prolyl-dipeptidyl aminopeptidase; Provisional"
                     /db_xref="CDD:235435"
ORIGIN      
        1 maavaallsa ligpasahaa pgesrpvysy drairesvwv dtrldgdadg rtdrvavdiv
       61 rpaepaqqgr ripvimdasp yysccgrgne sqkktyddrg rpvgfplfyd nyfvprgyat
      121 vlvdlagtnr sdgcvdvggr sdirsaravv dwlggrgray tartggkpvt agwsngstgm
      181 igkswdatia ngvaatgvkg lktivpiagi sswydyyfak gaplydsgpd sladavdspe
      241 arkrcaavqk kladgaprtg dwtglwserd yvrnagkvra svlmvhgmqd lnvrtrhagq
      301 wwdalarhgv erkiwlsqtg hvdpfdfrrg awvktlhhwf dhyllgyhng iertpmadie
      361 rapgtwstdp kwpapgttpt tlrprggtap gvgvlgtrka phgatetftd dpklseadwa
      421 aridtstaak agfrtgplra plrlsgsgtv tvtvtpstst ahlsavlvdl gpdtirnyaa
      481 dgegittldr rtcwgagttg dtgcfketaa dtqkvahtvf srgwadlgny adahkgrplt
      541 pgkpytltld laasdhvvpa ghrlalivag tdaglidppa stpkltldls rtwaelpltg
      601 gapafarata gapghpdaaa pldgiappps isrlpavg
//
LOCUS       WP_457683625             364 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457683625
VERSION     WP_457683625.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36281
     Region          42..357
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mattsahptt dgtgappaar rlpvipllav ltavllgsll cgvglgaagl swaevlrylg
       61 agltggtiss deaaaytivw elrfpravla avvgaglaal gvavqalvrn aladpfvlgi
      121 ssgaavgana vllfgalgal gvwalsaaaf vsalaamalv yaaartahgl tplrlvltgt
      181 amyygfsalt tlmvftadrg eaarsammwl lgslsgagwg svpiaaaava galahlllsa
      241 grlnalamgd etatalgvqv nrlrrelfvv aaagtgavva vsgaigfvgl mvphvarmlv
      301 gadhrrvltv apllgavllv wvdllsrvll apvelpvgvl tavigvpcfv vlmrrrgytf
      361 ggga
//
LOCUS       WP_457683627             233 aa            linear   BCT 27-JAN-2026
DEFINITION  LmeA family phospholipid-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683627
VERSION     WP_457683627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Rahlwes,K.C., Osman,S.H. and Morita,Y.S.
  TITLE     Role of LmeA, a Mycobacterial Periplasmic Protein, in Maintaining
            the Mannosyltransferase MptA and Its Product Lipomannan under
            Stress
  JOURNAL   mSphere 5 (6) (2020)
   PUBMED   33148829
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Rahlwes,K.C., Ha,S.A., Motooka,D., Mayfield,J.A., Baumoel,L.R.,
            Strickland,J.N., Torres-Ocampo,A.P., Nakamura,S. and Morita,Y.S.
  TITLE     The cell envelope-associated phospholipid-binding protein LmeA is
            required for mannan polymerization in mycobacteria
  JOURNAL   J Biol Chem 292 (42), 17407-17417 (2017)
   PUBMED   28855252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10567863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..233
                     /product="LmeA family phospholipid-binding protein"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24314
     Region          20..225
                     /region_name="LmeA"
                     /note="LmeA-like phospholipid-binding; pfam11209"
                     /db_xref="CDD:431728"
ORIGIN      
        1 mralrvllvl vvilgglfva adrvavglae dkaaekiras qgldktptva ikgfpfltqv
       61 agrslqevda dlggiearae grslridrls ahffevglts dytsiesaat atgnaritya
      121 dltkaagggv kisyggekng rsqvkispnv plpvslnvtg sltivngttv rlradglpam
      181 ckalpscetk vraqtdhdwk laqlpgnlkl dkvvtmhegi sisasgkdvk lpg
//
LOCUS       WP_457683629             475 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457683629
VERSION     WP_457683629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52776
     Region          59..466
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(169,171..172,305..309,324,327..328,331,346,350,405)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 msadpgsavn rrpirscgat aalsvallls sctssgargv agsggvgdpl fpalgnggyq
       61 vrhygldldy dikrrhldat aeitaeatad lrsfqldlqg lrvtdvqvdg edaefsrkgh
      121 kvivrpeesl rkgaefrtrv dyegtpqelk dpdkstegwv ktrdgafvvg qpagsmtwfp
      181 gnnhprdkat ydftltvpkg ytavangelr sertakgrtt frwhngrpma sylatatigr
      241 fevhtsrtpe glplyvavdp aeakaskgpl eklpeivkwe sklfgpypfs sagaivddtp
      301 kridwlales qtkpvyagap dtatvvhema hqwfgdsvtp ktwadtwlne sfatyaewlw
      361 eereggktpq eqfdalyddt kdpkrwafpp gkpgkaknvt gtpvyergam llqelrnavs
      421 dkafftilre wpteyryrna daqdfidfcq ehtdedlepl fkkwlyekgk pered
//
LOCUS       WP_457683632             279 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683632
VERSION     WP_457683632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29489
     Region          52..172
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpqpseqeql pltpqplqsa tpprhatlar afdavaaqya aarpgyppal fdaieelagq
       61 plagarvldv gagtgiatrl laergarvta lepgaamate lrtahpaipl vralgdalpf
      121 rddagfdlvg yaqawhwtdp arsvpealrv lcpggalalw wnipdpdvdw aaeqeariar
      181 clpdyhshsv apeaadlirg lglglrpvsr vlhwtrrvpl dthlamlgsr syfsaigpaa
      241 aapvlaaera alhdvfpdgi veeayalnlt vtlrppaps
//
LOCUS       WP_457683636             409 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683636
VERSION     WP_457683636.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43866
     Region          1..409
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 matelrmlrd vewdswsdtl nrafgepppt peqravrrev tetgrsfgvw dgadcvatag
       61 afsfgltvpg gaevptagvt mvsvqpthrr rgllrammrh qladvrerge plavltasep
      121 aiygrfgyga aaqdmqltvd tlrlaapelp gvdevglrlv dpaaaladce rvyaqlvpar
      181 pgmlarrpgw armavldppg eregagelqc vvaevdgevr gyvryavkpv wddagpagvv
      241 rvrhiealdp vvyaalwrfl fgidltssvs vrtrpvddpl phlvgdmrrc vpvlreslfv
      301 rpvevgaala artyrtpvdv vlevtdpfcp wnegrwwltg dgtgascart tdpaglalsv
      361 relgsaylgg fsltalaaag rvrelrpgal aaasvafgsd vapwlphgf
//
LOCUS       WP_457683649             959 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457683649
VERSION     WP_457683649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 959)
  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 959)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Rosinski,J.A. 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 959)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..959
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=102054
     Region          <7..923
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          896..952
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtdgiyaeaf ecrrdrltla nreeemsslt alvqdarags ggiallegvv gigksllldr
       61 lvsalpadgl yvltarcdal ehdfpfgvvr qlfepllatl depqltrlls gsartaaqal
      121 sgeklpgdal lptedmsyav lhglywftcn laaeaplviv vddahcadma slrflthlar
      181 rieglpvllv lsqrtgdvat daallsdiag qplcrvlrpg plthqgvghl vktvfghead
      241 defheaclai tggnpllvhs llsvlrlggr pptveglpyv tahdgaffhe avrsvlqqqp
      301 esaaaaaral avmgddalpe vcarlagldd athsaamral rsnglvsevd dgrrwsfnhg
      361 lirevivadl ppeqlaqahr haarllldag araeqvaghl lmtplpated wavtvlreaa
      421 reasfrgapa lavdllrhcl ppegptpedt pvlvelglae agvdpqasvr hlqaalehvh
      481 epplrfrlls slasglirsg qslqavrlls eeaptvrdad lqrllegqrl masaedltsf
      541 tvtlqeypfd isrpgdtpge raliaagagl csvravraqe saaaarrvle ssvpgvdspf
      601 flttaatall yaglpdeada ayqrvmgitl qsqrlllhgl cqalraeaqy rlgalseala
      661 atrsalnvvp prhwgrtlal pvatqihali dsgdlagada aaaqafpsts ldtwqwnefl
      721 cargrlrlth qdpkgaledl leagrrqhlw trtspavssw wfwagrahla lgapaaarel
      781 aedaverark gkltdalgag lrllattesg arklgvleea lsaldgspar lerartlvdy
      841 gstlhacgrt eaaretlrqg ldlayalgaa qlhaqandal latgarprrv tssgvesltp
      901 seaqvarmaa aggtnreiae elfvtqrtve qhltsvyrkv gvsgrrglgr ffgpgstak
//
LOCUS       WP_457683651             672 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683651
VERSION     WP_457683651.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 672)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 672)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 672)
  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 672)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..672
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71990
     Region          48..666
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mttadkgaaa raeapaatee tppmasrrgp apavgpgrmm ggqpteksmd fkgsgkrlla
       61 qmrpergims lalalgalsv altvvgpkvl ghatdlimsg iigrrlpdgl traqaaeqlr
      121 ahgqdgladm igtmpvvpgh gidfgavgqv llwvtliyaa aslfgfvqar iatrvvqrav
      181 frmreqveek larlplsyfd kqqrgevlsr atndidniqq tlqqtlsqiv aslltivgvl
      241 ammfwispll alvalitvpv svvvatkvgk raqpqfvqqw kttgklnahi eemytghslv
      301 kvfgrqresa elfreqneal yaagfkaqfi sgiiqpammf ignlnyvlva vvgglrvasg
      361 alsigdvqaf iqysrqfsqp ltqvasmanl vqsgvasaer vfelldateq dpdpaqparp
      421 eriegrvefe dvsfryapdk pliedlslav hpgqtvaivg ptgagkttlv nllmrfyevs
      481 ggritldgvd iaamsreelr ahigmvlqdt wlfggtiaen iaygapagtp mdkivaaara
      541 thvdrfvrtl pdgydtvldd egsnvsvgek qlitiarafl aepailvlde atssvdtrte
      601 vliqhamaql rtgrtsfvia hrlstirdad vilvmengai veqgphdall aangayarly
      661 aaqfaepvse tg
//
LOCUS       WP_457683655             879 aa            linear   BCT 27-JAN-2026
DEFINITION  CHAT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457683655
VERSION     WP_457683655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..879
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=97002
     Region          <616..877
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 madeldnvmp sheealekar ryldeaatll dgsnlgaifa ntafllysse yadgrfdess
       61 ilkncrksak llsreggdfl acmrllwmli sfgdstevea rfpidrwhci tavghygmhl
      121 gvaahntmir vllgvggaee vpslvdevrg adlvegeafa ahapiasrlr etdrrflela
      181 rihalpgdpg scseyrrigd laafldrakq elwrpdqiar avphallhtp klgsegaiei
      241 iasaevpnli ehlpavaadv siclaadaid rdspadalry lnvgldsylg mgykdipsal
      301 iramhwille ksfydierig gnlsqetfnl llkvsdkayr hlgetsrgfl rrswvhilaa
      361 lsleqrcgad elirimqalk grplsialaa pgplqettqq rsllaemdrl eradsghlas
      421 eadnatrsla gipmvdqegv ltsfmseref qhgkspveml rnmrreyqrl darqlvspav
      481 ppvsggkslg fpyrssgevs qalpdttlla slcfgvvalr spdtgalrrk angffallcg
      541 rsekllmsvh dpddiaffdt hvlslpsgra egremlhisp fglrvaalrr tiledpmhrr
      601 vgreaakalk gmasyfspll nhledldver fkhlcfwpqw elyflpfhll pwrdgiiadh
      661 ftvtlipsle aivvprhdve drrflvvaca dggveyglhs epslhvqaes issttgarml
      721 igddatpsdv cafmqsshyi hiaahgaqnv dapafhslfl sradgsrgrl cshhiakcdl
      781 rgvqlvtlsa cesallrfdv ndnlfgiasa flragaravl galwpvkaev adlffrvlys
      841 diaagrdkla sysraqlvtr rtypeyrdwa afsflgdwr
//
LOCUS       WP_457683661              73 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine hydrolase family protein, partial [Streptomyces
            nigrescens].
ACCESSION   WP_457683661
VERSION     WP_457683661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         <1..73
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <1..70
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 fygtaldadl rtrgvstlvm agisttgvvl scvawasdad ydvrlvqdcc ydpdrdahea
       61 llrsgfggrv qvv
//
LOCUS       WP_457683961             472 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457683961
VERSION     WP_457683961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49404
     Region          20..450
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtieesafrg rmparpgdla verhgigpvp esnrygkaar lftvwfapnl tmtgvfsgtv
       61 gislgldfwt aftamvlgtv vgavpaaylg twgsqtgtgq lplsrlafgr gvalpgimqw
      121 lssvawdali glfggealaq llgwpfwlga lvvlllqgvv gvfgyealhq lqtvmtfvlg
      181 aaflvlsvql lsgvplpvsg sahggerlga fvltstials laiswapyas dfsrylprtt
      241 srprmfwysl lgmvlsfawv qalglwgael ftdqtaagvh gllgggvlga fgllaiaaaa
      301 vcsnamndys gslalqaagi riprplaaga aavlgfllvl wmhaadttlr fqnlllfvgy
      361 wipgfvgivl vdarlrakar rgapidveae fgrpqpwwpa cvafvaafaa avpfmdttlf
      421 vgpvaaalhg adfayyvafl vsvavyaplr lfvrtangea aepvvaapgt gg
//
LOCUS       WP_457683958             289 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457683958
VERSION     WP_457683958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30876
     Region          208..288
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 matalgkpgv dglgeavgvl rewqydgapm qlhpgdlgwf wrlgaeataa avrtwsrdgq
       61 ilavglldgp gllrltiapd aqrdeelaqq lvddvtepar gvlpegkvni eaptgalvqd
      121 llfedgwnad epwtplrrdl repvkdpgvr ievvgpkqah vfaavhraaf dgsrftderw
      181 hamaaglpya darclvaydd qgdavaavtv wsagpgrpgl lepmgvhreh rrhgygeait
      241 vaaaaalqel gsssanvctp ssnagavaty tsagfqqrpe vrdqyrdty
//
LOCUS       WP_457683965             326 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457683965
VERSION     WP_457683965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="trypsin-like serine 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=34928
     Region          102..305
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 msrpiavrgr lalllttlll glsftlapap pahaektphg hghglrpaaa statywtpqr
       61 mrearpaaat ksaavrrpat datppshpfd glpqvgtffw tdgsntgrfc ggtvvrsphr
      121 dlvvsaahcl rspdpkrhls fvpqyhdglk phgiypverl yldqryydlg tdagarwdya
      181 vvrlgaredg aeveevtggf gllpypgyah rnvrligypg nkdtthpkpl dctssthryt
      241 stdpaapgdf leiscagyig gtsggpflvr dftgyaligv iggyhtggdf pdvsyssyft
      301 adtlalylha vhgdppatpr qgvstr
//
LOCUS       WP_457683966             165 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces nigrescens].
ACCESSION   WP_457683966
VERSION     WP_457683966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=17922
     Region          32..113
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mvpsfllsvl nrlfrneawr rlhaqaallv tvvmtavlla gaalvvvaes gaphanitsy
       61 pkalwwsiet attvgygdfy pvtlwgrvia sllmlsaita fgvitaalat wfvghaeqdm
      121 vrlsksvgsh aredaealrs elrtlherfd hvenlirdkg thsas
//
LOCUS       WP_457683964             439 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683964
VERSION     WP_457683964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47276
     Region          75..>342
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mfrksvdege raggssaler glegvpgggq magvnrravt ksaalaatml lagggiaqaq
       61 pgkartakdl tvrlpaptgp hpigvttlyl vdrarrdpwe plpvrevmvt vfypartvrg
      121 ypvapqmtrg aaerlpfiep lfheglpakg vnwaatrtha htgapaqtvr rpvllyspgg
      181 gdprtfgtai aeelasrgyv vvtidhpgdg sevefphara grrkvretvf rgdprsdpkm
      241 frtvvgtria dtrfvlnqle alaagrnpda egrplperlg raldlrrvgi yghsaggtta
      301 aeamyedrrl haainlegfl dhppaspgqe gqlfpiaryg tdrpllllgt dgfrykkele
      361 rswsamlahq hgctsrrqld htahgvftdy aaivpqlqaa glmtaahrtq lvgaldpavs
      421 vplvrhhvls ffarhlpvc
//
LOCUS       WP_457683960             224 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457683960
VERSION     WP_457683960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23419
     Region          1..223
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mltatlafag vaalinltpg ldtllvvrts vthgrtggra aaagiitgcl awglatavgl
       61 talltasrla ydalriagag ylawlglsal wrcrrqkahd gqrrpkgvav matsdeepag
      121 sfasgrgsaf raglgtnlln pkagifymsl ipqfiphgap vfgttlllta idvielalwy
      181 wvvssaasvl seratrpsfr rrmeqlsgvt flgfaahlll adrt
//
LOCUS       WP_457683967             878 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683967
VERSION     WP_457683967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..878
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93510
     Region          2..848
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          620..648
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(621,624..625,628..629,631,655,664..665,668..669,
                     671..672,700,703..704,707..708,711)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          653..689
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          699..722
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpgrglppal dafvgrerel srlrtllrss rlltltgpgg vgktrlarel agrvrggrtg
       61 raqwvaldsl qdgellpqal aaalgvrerg gragiealvh algtrttliv ldncehlaea
      121 carlaatlla rcprlrllat sreplrvpge vvfrvgelsl spageehdta allrseavrl
      181 flarartsda afelgsgear tvaeicrrld glplaielaa grvgslslpg ilhglddqls
      241 lltegsrtgp grhrelgaai dwshrlldpl ervvfrrlsv lgggfdaega aevcangggd
      301 dergrdpdrd wdwdrdrdwg rdrngdgdvr gdgeravsge irgeggahgg gtgrgdgvhr
      361 wdgvhhgddv hcedgahree dvhrgehvgq gppilvrpeq vlrvvcalea kslivrvrgd
      421 epqgtaryrq lsairaygmd rlaeagelsd twnraldwla gkaagavtpg vfldtvegpl
      481 areqenlaaa vahsaarsdh rhvplavala rlqyqqeqlt sartllsgvl ervrgpedrs
      541 aalalaarsa clqddhtaal afaqeavaag rtgrhpgrla naldalaaar lcrgefsdav
      601 avfaecldvv rtlgcpldla lcrhhlawal lqagraaeae qlmqeclpel etnappgqvt
      661 aalhtagair lalgdvdaae rrfaevllka ppgesfhgly pleglaivaa ergdlqrslr
      721 lyaaaaamrr ridtepeahw wgqveavvar vrervhpsgv saamaagrrl rgarlvayal
      781 rgtqvrsvrq esvqtagsgr vdavgqpplt gresavaelv aegmtnqqia shlglakstv
      841 aghldrvrdk lgvrsrtqia vrvtgrvagp epglhtdv
//
LOCUS       WP_457683972             414 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683972
VERSION     WP_457683972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44157
     Region          25..391
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mvhlidstae lgqesvfsla ecigaltsrq pavvavhqga pigaalacva gergwvmria
       61 issawrgrgl asallveler rliaarvsri ayvlpeedll gegllnagyt rqpavayfek
      121 vephhgpaas lledlggrfl ptdlwakvag meaekdlier rvvlplaepe raarhgvrpp
      181 raialfgppg tgkttfargi aarlgwpfve llpsrladeg nlaaalrsaf ariaelervl
      241 vfideveeia pvrhepaqpg glhgvtnell klipgfrerd erllvcatns lrsldpaflr
      301 pgrfdylipi gtpdaaarsa iwsrytdgra dvdvaalvaa selftpadie haarvaaqas
      361 ferdleaigv gagahgrlga stddylaala qcrptvtpam idefsadita harc
//
LOCUS       WP_457683973             397 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457683973
VERSION     WP_457683973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 397)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43487
     Region          18..395
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,83..84,91,95,102,230..231,234,238..239,242,
                     275,280..281,284..285,287,310,337..339,342..343,345..347,
                     351)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,82,84..85,169..170,178,229..230,233..234,238,281,
                     284..286,385)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 madivdleay gkdftadpyp yyaklraqgp vhrvrlpyap eawlvvghqa vraalsdprl
       61 nknwraaglq sdageesalw tnmldadpph htrlrklvak eftarrveal rprvqqitde
      121 lldtmlaape gradlveala fplpmtvice llgvpdmdre afrawsneiv aptseqaaqe
      181 avvamsgylv dlietmrnap gdgllsalir tsdedgdqls rdelvgtafl llvaghettv
      241 sllangvral lqhpaqlaal radyslldna veemlrydgp vetatwrfta epveiggtli
      301 pagktvaivl asasrdrehf daaddfditr darghtafgh gihfclgapl arlearvalr
      361 sllercptla mdadfddltw rtgmlrgieq lpvrwng
//
LOCUS       WP_457683975             178 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457683975
VERSION     WP_457683975.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19006
     Region          16..176
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mispetttvt tsyttfdspl gelllvgees atapggtalt slsmpqqrgv tvqphwrrdp
       61 gpfaeavrql rayfagertr felafrtagt gfqervwral eaipygtttt ygrladvvgl
      121 prgdvralga aiganpllil rpchrvigad gtmrgyaagv erkiallthe galqptli
//
LOCUS       WP_457683977             272 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457683977
VERSION     WP_457683977.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=28560
     Region          62..270
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mstplpgfed fgepdgakgp grpvvsgepg gpdgsggage sggsgglhsp tanrsrartg
       61 srqeiapgav hvpgwltmaq qrelvtacrd wargpapirh tklprggvms vqtvcigwhw
      121 qpyaytrtad dvngarvpef pdwmvelgrr alveayqdsa agdgytpdta linfydgqak
      181 lgmhqdkeer sgapvvslsi gdtcvfrfgn petrtkpytd ielasgdlfv fggpsrfayh
      241 gvpkvrpgtg dpasglaggr lnitmrvtgl dg
//
LOCUS       WP_457683978             284 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457683978
VERSION     WP_457683978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31536
     Region          30..282
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(35,70,162,196,198,247,274..275)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(70,274)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(162,198,275)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 maaaavvagp vvavhgpgna yaadggralr vmtfnlryas dvrphswaer rpvmrsllrh
       61 eaphllgtqe glygqlrdva vdlgphydwv gtgrgggsrd efaavfydar rlvpveydhf
      121 wlsdtpylig satwgntvvr mvtwvrfrdm raggefyaln thldhanqys rersarline
      181 rlggldlslp rivmgdfnva ahknsvyeam ldggslvdsw dtaderstqy atfhgyrplv
      241 ldgdrvdwvl tspgvrtrra tintysahgq fpsdhlpvqa lldw
//
LOCUS       WP_457683979             206 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683979
VERSION     WP_457683979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22003
     Region          16..166
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mrtdfdpaam srnefykllt avvvprpiaw vstispdcas anlaphsfft iasvappvvq
       61 ftsvgrkdtl rnieatgqfv vnlapeglfe qindtgtdfp ygvsefeaag vgsepslrvk
      121 pprvaassva lecevhttlg igdstvvfgr vvhavvaqdv lvdghpeiar mkplsrlgkd
      181 ewgtvgdvre isrirhadwp gpagvr
//
LOCUS       WP_457683986             241 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase [Streptomyces nigrescens].
ACCESSION   WP_457683986
VERSION     WP_457683986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="nitroreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25550
     Region          16..237
                     /region_name="PnbA_NfnB-like"
                     /note="nitroreductase similar to Mycobacterium smegmatis
                     NfnB; cd02136"
                     /db_xref="CDD:380313"
     Site            order(16..18,20,37,40..42,44..47,49..53,55..61,143..144,
                     146..150,163..164,167..168,171..172,174..175,179..180,188,
                     191,193,209,228..231,233,236..237)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380313"
     Site            order(20..22,24,47..51,132,165,168,185..189,210,228,230)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380313"
ORIGIN      
        1 mslshptels gyaeklirgr ratrafrpdp vpeetlravf alagaapsss ntqpwqvevv
       61 sgslrdrlad alqaahaeqr ttvdfpyred mysiaqqrrr aafgtalyga lgigrndhaa
      121 raafdaeslr fygaphvafl ftagdtgdtg dagdagdaga rlaadvgiya qtlllamtay
      181 gldscpqgll sfyadtvrge lgldrgkllv gisfgyades apvnhittdr aaldatttfr
      241 c
//
LOCUS       WP_457683987             224 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457683987
VERSION     WP_457683987.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23981
     Region          19..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meaattktqr rgrggreril gaaallfakq ginatgmeqv aeaapvskrt lyahfpaksd
       61 lviahlqela asgrtlesvl tredldprer ilrlfdlpap daspvrgcpf idaaaefpdp
      121 hsaihtyare qkllmaqlvt elaaelgaae paalaeqlvt ladgaasram vldqpdygrh
      181 araaaeilld ralmpmsreg ygrprggrln lpplptaape erpe
//
LOCUS       WP_457683974             266 aa            linear   BCT 27-JAN-2026
DEFINITION  chitinase [Streptomyces nigrescens].
ACCESSION   WP_457683974
VERSION     WP_457683974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Flach,J., Pilet,P.E. and Jolles,P.
  TITLE     What's new in chitinase research?
  JOURNAL   Experientia 48 (8), 701-716 (1992)
   PUBMED   1516675
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="chitinase"
                     /EC_number="3.2.1.14"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28520
     Region          65..266
                     /region_name="chitinase_GH19"
                     /note="Glycoside hydrolase family 19, chitinase domain;
                     cd00325"
                     /db_xref="CDD:381595"
     Site            order(118..119,125,127..129,159..163,165..166,199,
                     228..229,233,241,245)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381595"
ORIGIN      
        1 mappcqevgp rrshrnevty craaecrdrs rghsacradd acgchdglcr lcpagadara
       61 egfvvseaqf nqmfpnrnaf ytysgltaal saypefantg sdtvkrqeaa aflanvshet
      121 gglvhvveqn tgnyphycda sqpygcpagq aayygrgpiq lswnfnykta gdalgidlln
      181 npylveqdaa vawetalwyw ntqtgpgtmt phhamvsgag fgetirsing slecnggnpg
      241 qvqsrinsyk sfvqilgttp gdnlsc
//
LOCUS       WP_457683988             514 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA synthetase [Streptomyces nigrescens].
ACCESSION   WP_457683988
VERSION     WP_457683988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..514
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0032787 - monocarboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=54715
     Region          10..497
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(164,167..172,174..175)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(167,282..283,303..308,388,400,403,414,494)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(167,207..208,255,257..258,261,282..283,303..308,388,
                     400,403,411..414,475)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(207,257..258,261,282,411..413,469,475)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mlnqgigswp trrarktpdr vavihedraw tyrefhqrvl rlahglqdvg vvrgdriayl
       61 gpnhpsflet lfaagllgav fvplnnrlta pelaynlsds gstvlvhape qacaaraaad
      121 eagvrhritl dgshegalgy eevlagggtd pldepvapdd pcmimytsgt tgrpkgavls
      181 hanivwnsvn vlvdtdlggd evtlvaaplf htaglnmtcl ptllkggrvv lltafdatrv
      241 letieslrvt ymfgvptmyd amaaqprwst tdlsslrtln cggapvpart iatylargla
      301 fsqgygmtea spgilfldke qtsakagsag vphfftdtrv vlpdgldagp gqrgemlvqg
      361 phvmtgywnr peeteavfad ggwlrtgdva rtdtdgyayi vdrakdmfvs ggenvypaev
      421 eeavlshpav aecavigvpd qtwgevgrav vvlgpgahad epgildhlhg klakykipks
      481 viltdslprt atgkivksav rasyantpad ephr
//
LOCUS       WP_457683989             292 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683989
VERSION     WP_457683989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32111
     Region          44..292
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mgdlaldldq ltaidmhtha evskdghgal spellgasae yfkahghrqp tieemaghyr
       61 errmaavvft vdaehatghp risneeiads caahpdvlip fagidphkgr agvrearrlv
      121 eeygvrgfkf hpsiqafspn drlayplyea ieelgvpalf htgqtgigag apggggirlk
      181 ysnpmlvddv avdfpqlrii lahpsfpwqd ealavathkp yvyidlsgws pkyfppqlvr
      241 yantllkdkv lfgsdypvit pdrwladfek ldikpevrpk ilkenaarll gl
//
LOCUS       WP_457683990             403 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457683990
VERSION     WP_457683990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42374
     Region          50..296
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtivygasea tadattnstt dsttkpkpgd rasltsyela pgllkitsrp pgnptqvhgv
       61 lgmpkgegph pvvvvmhglh hncafsdkpp yfprkpvkar wplvcaapge phnpnlgpdy
      121 lrhdvglspv vqaltrkgfa avsidvvspe hwwagetvpe kgytdlvnah lrllsdlnkg
      181 vnhgldipgv kgridtsrvg lvghsrgggy vlspkaaqra glfgvvalep avgaekvphk
      241 vpvlnlrggc dedvdpsagl eemkelaksg stkvaadvll agtghrmlnt nlpptdtkeg
      301 gvgdcpaskv aapaaaqaqa aqitasfldq arhksksyrl paledldpkg gnlrkggpav
      361 tfhrapqqtf tdpltihevt skqrllpaip kdlkvnkrpg ddi
//
LOCUS       WP_457683993             452 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457683993
VERSION     WP_457683993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49581
     Region          11..430
                     /region_name="FMN_nitrolo"
                     /note="FMN-dependent oxidoreductase, nitrilotriacetate
                     monooxygenase family; TIGR03860"
                     /db_xref="CDD:274819"
     Site            order(14,18,75,128,150,223..224)
                     /site_type="active"
                     /db_xref="CDD:238528"
     Site            97..98
                     /site_type="active"
                     /note="non-prolyl cis peptide bond [active]"
                     /db_xref="CDD:238528"
ORIGIN      
        1 mpaagprrlh lnaflmnagh hdaawrhprt qperltdlry fqhlaqtaer gkldsiffad
       61 glalwgkvkh nalggfeplt llsalatvte rigliatvst tfnepfhtar kfasldhlsg
      121 gragwnivts gtvdearnfg qdehlehslr yararefvev atklwdswed davlldrvrg
      181 iyvdagkvqp ldhwgehfav qgplnvqrsp qgypllvqag ssedgkefaa qyaeavftaq
      241 qtladgqafy kdvknrlsry grseddlkil pgicpvigat eaearaleqe ltdlpvpeyg
      301 laqlsgmlgt dltglpldgp lpvlpeerdi ngnksrftlv aelarrdglt lreliarlgg
      361 grghrvfagt peqvadqlee wftqgaadgf nvmpphlpgg ledfvdhvvp ilqerglfrt
      421 eysgrtlreh yglprpagrl asavtategq pa
//
LOCUS       WP_457683994             338 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457683994
VERSION     WP_457683994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=35766
     Region          96..333
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mslasgsstr rrtpeelktp edfttaeept pseeltttee lttpeelsap atgtssaste
       61 esaavlpaap srprlprppa lprilraalt gatksaaiva lllvwelapr fglvdrtflp
      121 pfsevaqaww elvangqlad naraslvrsf sgfgiavavs vplglligwy rpvadllnpl
      181 lqvflntaal allpvfvlll gigetskisi vvyacawpil fntisavrtv dptllrlaks
      241 mdlsaprlfq kvilpasvpt iftgirlaga vsivvlvaae migakaglgy linasqynfa
      301 ipqmyagivt isvigvafnq llvavekrls swrvpats
//
LOCUS       WP_457683995             283 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457683995
VERSION     WP_457683995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31067
     Region          1..273
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msgittpkie fervrktfpa krgraqgrgs ahgdgeftal dgvdlridag efvvvvgpsg
       61 cgkstlldll gglarpsagr illdgepvtg pgldrgivfq qyallpwrta lgnvefglea
      121 tgvprreraa rareyldlvg lsgfenrhph elsggmrqrv aiarslayap dvllmdepfa
      181 aldaqtresl qdellriwqr tgktvvfith gieeavylgq rvavmtsrpg rikqvvpigf
      241 dsrtatddlr sspefaryrh eiwtllhdev trtqllekee vsv
//
LOCUS       WP_457684001             423 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydroxymethyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684001
VERSION     WP_457684001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Stover,P. and Schirch,V.
  TITLE     Serine hydroxymethyltransferase catalyzes the hydrolysis of
            5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate
  JOURNAL   J Biol Chem 265 (24), 14227-14233 (1990)
   PUBMED   2201683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..423
                     /gene="glyA"
     Protein         1..423
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0070905 - serine binding [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=45129
     Region          8..423
                     /region_name="glyA"
                     /note="serine hydroxymethyltransferase; Reviewed;
                     PRK00011"
                     /db_xref="CDD:234571"
     Site            order(12,14,21..22,31,36,54,72..73,81,96,103,138..139,264,
                     282)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(35,55,65,98..99,126,176,201,204,229..230,236,367)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(35,126,230,367)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(57,64,121,125,127,256,351)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 msvldrrlad fdpevhtavr aelarqqntl emiasenfap vavmeaqgsv ltnkyaegyp
       61 grryyggceh vdvierlalt rikalfgasf anvqphsgaq anaaamtall qpgdtilgld
      121 lahgghlthg mrinfsgkly ntvayhvsae dnrvdmaeve rlamehrpql iiagwsaypr
      181 qldfaafrri adrsgaylmv dmahfaglva aglhpnpvph advvtttthk tlggprggvv
      241 ltnradvakk vnsavfpgqq ggplehviaa kavafkmase pafrrcqert lagarllaer
      301 lsgpdvadag vsvlsggtdv hlvlvdlres eldgqqaedr lhdigitvnr navpfdprpp
      361 mvtsglrigt palagrgfae aefaavadii aealkpaytp slaaelrarv atltdahply
      421 pel
//
LOCUS       WP_457684005             424 aa            linear   BCT 27-JAN-2026
DEFINITION  SagB/ThcOx family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457684005
VERSION     WP_457684005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 424)
  AUTHORS   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="SagB/ThcOx family dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46362
     Site            order(207,230,233,272..274,345..346,349,357..358,361..362,
                     365..366,368..370,372..374,386,388..390,405..409)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380318"
     Site            order(207,209,211,274..276,278,359,362..363,368,372,
                     383..386)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380318"
     Region          242..414
                     /region_name="antibiot_sagB"
                     /note="SagB-type dehydrogenase domain; TIGR03605"
                     /db_xref="CDD:188352"
ORIGIN      
        1 mgrltaeqrs llqvlstdrs aeeltrrcpr dqaerllaml ssggwlittv vcgdrplfss
       61 rplvphrkpl ppveprrlsr fasvrrdgde ivvespaaga evrlydrrlv epvlapgaeq
      121 ersdlpleav rllageladr gflataaedh slssvqwsph elafhhgsrl radhrmgqdf
      181 ggsywakgrf dappgkhprw peaaielprp dlaglrakdp alaevmeerr slrsydedtp
      241 ltveelgefl frtarvratg rdtegldvss rpypgggaay elevyplvrn vrgldaglyh
      301 yaphghrlhp vpasatalrr lmkasaagmt gdatpqvllv iatrfgrlaw kyqamgyalt
      361 lkhvgvlyqs mylaatamrl apcalgvgds dafaeatgld yfeetsvgef algslpaarr
      421 estg
//
LOCUS       WP_457684007             471 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457684007
VERSION     WP_457684007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49976
     Region          29..457
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnhpdrlgas hgslarsapl tpvvppvasf adlelpaevl rtltelgvre pfpiqaatlp
       61 halagrdvlg rgrtgsgktl afglpllvrt agrraepkqp laliltptre laqqvteala
      121 pyaealrlrm atvvggmsig rqaaalrdga evvvatpgrl hdlierkacr lggvritvld
      181 eadqmcdmgf lpqvtevldq vhpdgqrmlf satldrdvdh lvrrylhdpv vhsvdpsaga
      241 vttmdhhvlv vhgpdryavt teiaardgrv llfleskhav dqltrhlras gvhaaalhsg
      301 ksqpqrtrtl aqfkngqitv lvatnvaarg lhiddldlvv nvdpptdpkd ylhragrtar
      361 agesgsvvtl vlsgqrrems rlmsgagiea titkvrsgea elsritgaka psgtpldggp
      421 aaprakntna pfrglgtskd asrgsggksr kagearklae arkaarvrrg n
//
LOCUS       WP_457684009             619 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684009
VERSION     WP_457684009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..619
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=66599
     Region          6..421
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mirtgagala elpagarvvi rlpngsalad vllacfdrrl vavplhprat dravagiaer
       61 vsaaalvdvh glhrtalpdv htvpddlafi mftsgstgpq kgvmlsrrav lgnaaktaal
      121 hglsperphg tclplyhcna lvmsllgthl tgtpltqqad fdpagyfaal gaagartasi
      181 vpalladlle vgpdwpdgle ylitaaaplt sdlarrfhrr ygprlrqgyg lteavnfsft
      241 mprlddaefr dhylehvppv gaplpdtelr lesgevwirt pdlmtgywqd srttaatvtd
      301 dgwlrtgdlg elrdgllvlr gragerinrg gekhypldie hgwrraglsg rfaavavdep
      361 slgqdiglia teqpvsaird lyeraqlrpa alqfggllat stgkpqrkam srglaarrla
      421 paryerllry aaatahdllh sgadhpglra latqagnrrp hpdeetvfga fdflrehwhh
      481 eddaelsrak ahwrttlrte wplavhaela aevaarhgfe gppvpfgtea lfgdgalqvl
      541 phgpaadgpv wplgpllsfl dgplggcerd rwtrlarlrd rgflttgcsv lragrhdlgg
      601 vlwarqpdsg pnehagatg
//
LOCUS       WP_457684011             609 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684011
VERSION     WP_457684011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 609)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 609)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 609)
  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 609)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..609
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64928
     Region          16..581
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtdrqsvprn aavprlrilw sfarphkgal iralllalva salglatpmv tkwvldalgd
       61 asplkgplaa llvllvvgva vrfwqwtllg avgervvlea resmvrrflr atvpaitrrp
      121 tgelvtrvts dtvllreaat dalvglingt vmllgtlvlm gvldvvllgt tlasvalvgv
      181 lfavlmpgia taqqraqehl grlggalegt lrairtvkvs raedrtaeri aadarasaey
      241 giravrreal awtvswsgie laiivilgvg awrvgegqme vssliaflly afglmdpite
      301 lssnvtalqa gmaaaerire tddlqtesta ahpapptgld hrhdvpvlal rqvsaaygpd
      361 aepavrgidl tvprrghtai vgpsgagktt lfslvlrfle ptqgellldg rpyrdlthde
      421 irarlayveq dtpivpgtir dnlllsrpda tdeelrrvlr dvrlaekina lddgldttls
      481 tttvsggerq rialarallr tpdvllldea taqldgitea avhdcirsra aagavvtiah
      541 rlstvidant ivvmeagrvr vqgsheelle tdllyrelve aldisaspap apeaeavsvt
      601 sggsrpqat
//
LOCUS       WP_457684019             292 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457684019
VERSION     WP_457684019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32270
     Region          2..232
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mpdpridvvl ltmndrptee aaaqatllaq tnvelricvd gctpalvppg aitvalpenl
       61 gipggrnaga ealrkagdpa gllffldnda tfprpdvlar lvaeaerrpk aayvqprltg
      121 pddvttprrw vprlrashpe rsgiittmte gvvllrreaf daaggwaaef flyhegiala
      181 qqlwaqgyig wyaaevrmhh pvtssarhal fhrcsarnrv wvayrnlpaa lipayltvwt
      241 vitlvrsarg gqvheslrgk regwarrheq qrrpmswrtv wrltaagrpp vi
//
LOCUS       WP_457684020             292 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684020
VERSION     WP_457684020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31585
     Region          203..287
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mrpddwqlte dvddflarag dflrsrpdlh tmpltvtekl rthgadayga qptvfgrler
       61 agtvratfhr lpsrglsvts ltpeqadtla ahlaalghsl pyvsadhsta tafaeawqrh
      121 tgaaptlskr irlyrlgtlt ppeplpegrh rvageqdhkq vvcwcgefvd tvgevptvda
      181 gswagsrfad khftfwetpd gnpvsmaavt smlagmvrvd pvytparlrg rgyagavtve
      241 vsraaltaga rdvvlfadpa nltsnalyqr igyvpitdfa vydfsraapd vs
//
LOCUS       WP_457684024             149 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457684024
VERSION     WP_457684024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790656
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16589
     Region          1..145
                     /region_name="SRPBCC"
                     /note="Ligand-binding SRPBCC domain [General function
                     prediction only]; COG4276"
                     /db_xref="CDD:443417"
ORIGIN      
        1 mpnfevvtav aappdqvfav cldvqahtrs maasseravg gktrgelalg dtvtfrarhf
       61 gltwrlkari taydrprrfv deqesgpfkr wrhahhfepd gdggtvmrdv idfasplgpv
      121 grivdrills rymphlirtr naylagtfd
//
LOCUS       WP_457684031             567 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457684031
VERSION     WP_457684031.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  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 567)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /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=59487
     Region          196..409
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mssstppvae nrptrsffag pgeqgrwllw raageallag alvllvhegv stidgrlegg
       61 apalgligia lvlvrrrfpv acvaglaalm gvvpavallt avaaytaarq trtprrrigv
      121 llgaaaltml tcaaftpele mgsrlfglal gavfavttvv lpglagtagg qqdrllralr
      181 eraaaaeear rladsesrmr ersriaaemh dlvghrlslv slhagglema llkeapelrd
      241 eaavvrratr damqelreal gvlgplgsdt gtgaltdatg tradiealve esrsggipva
      301 fswegpdlda rpaqvrravh rvvresltnv hryaaeahvt vavrhtdqrv avrvrngvpp
      361 trpaavtglg sgrgltglme rvtllggsle agrtsgggfa vaaeipttpg pgaetadaap
      421 ddsgsapvde srsrlsvlqr rvagavigll glagvgvmml favllvdhsr yelayqspek
      481 prlgmtrgqv eravapddda sraaaagrep prpasatdcm ypyaggkrkg grmelvrycf
      541 rsdtlitidr ftvpivtepp hesrmhd
//
LOCUS       WP_457684033             241 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684033
VERSION     WP_457684033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 10004355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25750
     Region          17..89
                     /region_name="MJ0604"
                     /note="Predicted nucleotidyltransferase, MJ0604 family
                     [General function prediction only]; COG1708"
                     /db_xref="CDD:441314"
ORIGIN      
        1 mndpaaptal alglvtsrfp halgatlggs aaqgratpts dldvavllpd sdtsrrevvr
       61 hdgrlaelfl htladlpglf ardrarrrgt vlflydqgvp lmdpqgqvsr araqaravla
      121 agpppltpae wergryyltc fmddlidtqp adryeqlala dstlgesahl ltahhgawtg
      181 igkwlprrll sadpergral ldghravaeh gdpaplaaaa eqvldlrggp lregytqpwg
      241 g
//
LOCUS       WP_457684035             363 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional class I SAM-dependent methyltransferase/NUDIX
            hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684035
VERSION     WP_457684035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 363)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
REFERENCE   4  (residues 1 to 363)
  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   5  (residues 1 to 363)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18603225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..363
                     /product="bifunctional class I SAM-dependent
                     methyltransferase/NUDIX hydrolase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38698
     Region          44..159
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          221..344
                     /region_name="NUDIX_MTH2_Nudt15"
                     /note="MutT homolog 2; cd04678"
                     /db_xref="CDD:467561"
ORIGIN      
        1 msgslktlkg siamgnvtre aqeargthyg egrtfrplgd aeltflrelv pappggghal
       61 dvgcglgdla rhlaatgytv davdfaasal siaeqtppas gtvrfvqcdi erdpldglrs
      121 sydliafrls yafigdrtrv mhrlrerlrp ggavvvitpv vegvpadrra ialdeeeitl
      181 lsagwhtver rdaeglaflv lrdpapgpva yrgkgrpsph altgagvvvt deagrvllgr
      241 slrgtwelpg gkndggesfv eaavreleee tglrakaada rllailmdav hgmprvtaav
      301 rvvdfcgkpa vrepdlihrw ewhdvadlpt laaalftpsa hvldvvwpgl lpglppvhrh
      361 plv
//
LOCUS       WP_457684038             380 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457684038
VERSION     WP_457684038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41893
     Region          2..368
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mriaylhsgs ipsvyangvh vmrmcdaftd aghevvlhal pgttpaddih ayygtrnrfe
       61 vrphgqpavp gagkwirarq iradlrrrgv pdllygrdpf allacsglap lvyethllwp
      121 srtiravers lfrrpnlrrv vcvsqaladd yraafpelta lnnvdlvaah dcadpvpldg
      181 pvaplpgrer alrigyvghl ypgrgtdvil glaeqlpdad fhlvggttad rthwqsrcrq
      241 phvyfhghrp paelapfyra fdivlapyqr raycaggvge isrwvspmkl feymaygkav
      301 iasdlpvlre vltdgvncll rppgsvadwa qavtqlaedt alrtalgnea rrqlterytw
      361 raradrvlpa vpaaagpesr
//
LOCUS       WP_457684049             476 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684049
VERSION     WP_457684049.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49964
     Region          71..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mardplfhas gagtearege esspraagra aavrnnvdwd glrrrmtgal lrpgdagfet
       61 arklfnplnd dlvpaavaqc asvgdvreav laaanrvpla arsgghsyvg ysaphggltl
      121 dlrrlstvra hpdgtatiga gatlqavyta lgqanrclpg gscftvgiag valgggigvl
      181 qrkfgltcdh lvsaevvtad grtltasatq npnlfwalrg ggggnfgvvt qftfatdpap
      241 altvfrldfp agsvtkmlta wqpwitaapr elwanlnvsg gaiprckvag cfvgpssacn
      301 pllndlvtra dvrpdlrrve drdyfkamrf fsgspdrqsf vassrvltsh aanpgavvsl
      361 lkdrlgmdli ldplggavad vdvqqtafph rkafataqiy asataaseaa vtrsvgqvva
      421 gladqgikdg yinyidpalp dwakayygpn lerlrtvaye ydpdrvfdfp qavtht
//
LOCUS       WP_457684051             512 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684051
VERSION     WP_457684051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..512
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=54189
     Region          16..511
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mhdapdripp phhgleplvr irglskrfgg tlaldavdld ihsgsilall gpngagkstl
       61 ikvlagvhha degevtvagh plgteaaart msfihqdlgl vewmtvaeni algtgyprra
      121 gllswrltre rcaealsiva ahldprtvla dlpraerslv aiaralstra elivldepta
      181 slpaadcarl fevlptlrdq ghalvyvthr ldevykvaea favlrdgrli sqgplaghsp
      241 arlvhdivgh epvgfrrapa agsvvlsldg vrtentapvs lelrtgeilg mvgltgaghm
      301 elgralagar pvvggrvrln grpytpgtvt aavgsgvgfv tsnrqeegca aeltvrenfl
      361 anpradglra fhwisprrer agatalaerf svfprdseap iatlsggnqq kvmvgrwlri
      421 hrsllileep tagvdigakt avyrllqeal aeglavllis tdfeevaqvc hralvfvrga
      481 vteelsgkal tvaglahass amaaltgetr rp
//
LOCUS       WP_457684055             370 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684055
VERSION     WP_457684055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  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 370)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..370
                     /product="glycosyltransferase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40077
     Region          92..355
                     /region_name="YjiC"
                     /note="UDP:flavonoid glycosyltransferase YjiC, YdhE family
                     [Carbohydrate transport and metabolism]; COG1819"
                     /db_xref="CDD:441424"
ORIGIN      
        1 msaldyvtcp aheqghqvtl haplmfrrea rrrgvefsga gtnwtcdplv qqaasevwqr
       61 hgntsfnryv fghlwpgqae akahdlltaw tqerpdlvia ecsdlgahla aralqlplla
      121 adnglgpvll dlwdthivpa llplykqheq dtptlppmlt papvhwfyet pppsaravrr
      181 tvadfrtalp ewldrapslr psrplvyvsl gtlttamsgl rtavgnvyre imaalraidc
      241 daivsagdla qhlpsasphi kvvkhapqpa llhradlfvt hggrasllda vqgttpvlgl
      301 gvladqpdna aaftrsglgr sldltarhde iadaltdlld tprygaamse acaelsqlpp
      361 ldlteirdsl
//
LOCUS       WP_457684057             405 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457684057
VERSION     WP_457684057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 405)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45815
     Region          20..404
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(69,94,96..97,180..181,190..191,194,197..198,201,234,
                     237..238,241..243,246,289,291..294,318,394)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(95..96,103,107,114,159,162,238..239,242..243,
                     246..247,250,288..289,292..293,295,318,345..347,350..351,
                     353..355,358..359)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mvhepkapvi pykrtcpfdp aaeyarlree dpispvtfel aprekngwlv trhdhirqim
       61 tdprfshrse llalvhsppf pvedyspeps apgnfvrmda pehtryrrll tgfftvrkiq
      121 qyeptlvrii dgvldemaam eppvdlvkvf aeqisarstc simgvaesdl aalaqhfsvi
      181 mginytldef ihhnselnat lermmaerfa gdptddllgr liatgelteq emfniawiai
      241 ggaldttpnm falgtfalle hpeqlakvre rpelmentve ellryltish fgasrvaled
      301 veidgrtika gqtvvlslps anrdpryfen adefdidrps rrhlafgfgi hqclgqhlar
      361 aslrigfqkl fdrfpdlrla mpaeqvplre tamhygvyel pvtwg
//
LOCUS       WP_457684058             360 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457684058
VERSION     WP_457684058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..360
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37715
     Region          30..275
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mptrrstppq slsahsgpvp dreavdtaaa rpvrfgalgt ssfggrrvlp amtacpqtel
       61 vavggrsper sqrfadrfgc agssmaalle rddidavyis lppslhgewa aralhagkhv
      121 lvekpiatta tearavvrla edrdlvlren fmflhhpqhd avadliaegr lgglrsfrga
      181 fcfpplpted iryvpglggg alldagvypl raaamllgpg lrvagatarv rqsdgldlsg
      241 qallvspsgv lasvefgfeh aygssyslwg egakltvgra ftppaayqpv lvleeqdhve
      301 kftlpaadql taslagfaaa vtaggaaasp rearwlqdav ammelvdavr aqavrvtveg
//
LOCUS       WP_457684040             191 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684040
VERSION     WP_457684040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Chapman,E., Best,M.D., Hanson,S.R. and Wong,C.H.
  TITLE     Sulfotransferases: structure, mechanism, biological activity,
            inhibition, and synthetic utility
  JOURNAL   Angew Chem Int Ed Engl 43 (27), 3526-3548 (2004)
   PUBMED   15293241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16049904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..191
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21373
     Region          10..189
                     /region_name="Sulfotransfer_4"
                     /note="Sulfotransferase domain; pfam17784"
                     /db_xref="CDD:465504"
ORIGIN      
        1 mtedrptrpk vfglglsrtg trslttalrt lgfdvahypc dpgtyqalvd gtarfpllae
       61 rdgitditva pyyeeldlaw pgakfiltvr eeqswlrsca yhwgrpvtsk aapgsvyvrv
      121 qrflraavyg chefnaarfa rvhrrhieqv rrhfagrddd llvldivggq gyerlapflg
      181 vpipdepfpg f
//
LOCUS       WP_457684068             366 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684068
VERSION     WP_457684068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38329
     Region          13..314
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msgaqapdgt hrrvivlgat gafgrhvcaa vgaagkdvlr varrpgtatg agrffpmdlv
       61 gegpdglarl idaerpyavv naagavwlcs peamrqanha lvatvlaama aaswrprlvh
      121 vgsvheyapq ppgtsldert ptrpttlygr tklqgteavl tasaagqvea vvlrvsnaig
      181 agtspgsllg rvaaqlraae adreavvrvs plrasrdfvd ardaadavla aaalpvggel
      241 inigrgeavp vrtmverlit asgqrarive eaepgarpat dqdwmrvets rarrllhwtv
      301 rhsidssard lweatapgae psppghpaat vpvpprpeta dhrprggstr ttrtwppqtr
      361 pvqqpe
//
LOCUS       WP_457684075             959 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684075
VERSION     WP_457684075.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 959)
  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 959)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Rosinski,J.A. 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 959)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..959
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=102143
     Region          <8..923
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          896..952
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtdgiyteaf ecrrdrltla nreeemsslt alvqdarags ggiallegvv gigksllldr
       61 lvsalpadgl yvltarcdal ehdfpfgvvr qlfepvlatl depqltrlls gsartaaqal
      121 sgeklpgdal lptedmsyav lhglywftcn laaeaplviv vddahcadma slrflthlar
      181 rieglpvllv lsqrtgdeat daallsdiag qplcrvlrpg plthqgvghl vktvfghead
      241 defheaclai tggnpllvhs llsvlrlggr pptveglpyv tahdgaffhe avrsvlqqqp
      301 esaaaaaral avmgddalpe vcarlagldd athsaamral rsnglvsevd dgrrwsfnhg
      361 lirevivadl ppeqlaqahr haarllldag araeqvaghl lmtplpated wavtvlreaa
      421 reasfrgapa lavdllrhcl ppegptpedt pvlvelglae agvdpqasvr hlqaalehvh
      481 epplrfrlls slasglirsg qslqavrlls eeaptvrdad lqrllegqrl masaedltsf
      541 tvtlqeypfd isrpgdtpge raliaagagl csvravraqe saaaarrvle ssvpgvdspf
      601 flttaatall yaglpdeada ayqrvmgitr qsqrlllhgl cqalraeaqy rlgalseala
      661 atrsalnvvp prhwgrtlal pvatqihali dsgdlagada aaaqafpsts ldtwqwnefl
      721 cargrlrlth qdpkgaledl leagrrqhlw trtspavssw wfwagrahla lgapaaarel
      781 aedaverark gkltdalgag lrllattesg arklgvleea lsaldgspar lerartlvdy
      841 gstlhacgrt eaaretlrqg ldlayalgaa qlhaqandal latgarprrv tssgvesltp
      901 seaqvarmaa aggtnreiae elfvtqrtve qhltsvyrkv gvsgrrglgr ffgpgstak
//
LOCUS       WP_457684079             402 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684079
VERSION     WP_457684079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..402
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42516
     Region          147..392
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msqrsasppq asepgedire qvvrmaarle pginqltrlv verqraevpg fdrlpgdmqd
       61 leiasaarht irgflrsvqg ladtdaevlr eraiqraseg vhltgllrgy hvatevvtda
      121 lcaaarpgee aallwltrrl fttvnslveq ateayllgma gqqeakrela aallrgdapq
      181 evaarcglpl epgylvlsvr apvpqepvaa rrllhqvlvr lapaadgrvl slpneqgghi
      241 llplgtphad lvghlstgps rpviagaala atpgdvpaaa eqahriaaia rtpgvhrlqd
      301 vlldyhlags kdsaaelaal ldpldghagl veavaafldc dldrrrtaqa lrvhpntvdn
      361 rlaraaqltg ldphtthgvq lfgaaltlrr laegsatgfl pg
//
LOCUS       WP_457684081             338 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684081
VERSION     WP_457684081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34796
     Region          4..336
                     /region_name="CurA"
                     /note="NADPH-dependent curcumin reductase CurA [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG2130"
                     /db_xref="CDD:441733"
ORIGIN      
        1 mtvpstgtev rlaarpegwp ttgnfsvvra plpavgagqv lvrnlvmsvd pymrgrmnnt
       61 rsyvppfavg kvldggavgr vvvsksprhs vgdlvlhglg wreyavvgaa gavtvdpala
      121 ppgaylgvlg mpghaayagl lkaaefrpgd tvfvsgaaga vgslvgqiar lcgaqrvigs
      181 agsaekvayl teelgfdaaf dykagpvldq lakaapagid vyfdnvggdq ldaalalarm
      241 garfalcgtv sqinekdgpa gprnlvqaia kgitlrgflv snhaglkdef tarmggwlte
      301 grisyretvv kglenapaaf idmlrgantg kmlvriad
//
LOCUS       WP_457684089             357 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457684089
VERSION     WP_457684089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..357
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38959
     Region          44..356
                     /region_name="COG3435"
                     /note="Gentisate 1,2-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442661"
ORIGIN      
        1 mkpallgaip pqqqgptepe sfagrlrrhh avgrwgaane nqswtpnprs vpalwryael
       61 rpfaveaaef vkgedaalrv ithlnpghpd yeaavghlys glqtlkpher mtahrhaasa
      121 irfvmegegg wtavdgdrmt vgpgdvvitp gglwhehgnd sddglviwqd ctndplvntl
      181 ganffelhpq rshlgtqdrt dtlaryggll lpdtrrrsea splfsypwdk cyealvaaar
      241 agnhspfdgv imeytnpvtg gpvthtlgak lqmlapgeht rshrhtgsvv yvaargsglv
      301 tingvvhpws agdtfcvpsw swhshanpgt deavlfsyne fplldklgly teeader
//
LOCUS       WP_457684090             282 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457684090
VERSION     WP_457684090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=29950
     Region          28..279
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mtaeqlgtse saisesgtse sataaetaty vyavsrrldp aalsglagla egfpvrtlpl
       61 gpltavvqhv paaeftqdaw qqrlsdrael ercarahhev vtaaaacgpt vplplatlyr
      121 gderaqqvlg adrdrfaaal arieghaewg vkvslptaap epprvgspgs gggpsggagr
      181 ayldrkrglh rareqhhdra lqtaedidaa lsrlatatrr lrphtpemtg erhrlqvlna
      241 aylvttvrek ellaavetlr hrtgaevevs gpwvpysfvg ev
//
LOCUS       WP_457684091             449 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684091
VERSION     WP_457684091.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..449
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45782
     Region          19..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(29..30,33..34,37,69,124..125,127..129,132,152,
                     155..156,159,232,235..236,239..241,244,268,272,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mgvkralidv tplrrsapfr rlwlgqtlsr lggqmtlvav mfqvwqtths tvwtgavgla
       61 ravplivlgl fagslvdrvd rrtfylittt gqavcvslla lqdflgnfpt agvlllvavq
      121 scfaagsgpv srtflpcllp kqqlaaglal nriafqgaml tgpvlgglil gglgaggvyl
      181 idaltfaaaf hgafglprmr pgdeparpgl rgvadglafl vrtpvirgal ltdlattvls
      241 mpislfplvn aerfgndprt lglflsavaa ggvlaslfag tftrlsrpgl vmlggsatwg
      301 aalalfglsa dpwtgpaflv lagaadtvav vsrstlvqlh tpdellgrvs aaeqivgqag
      361 pdlgnmrggl madatsgtaa lvsggllcig avalvgtttp glrfsrspsp spapapspap
      421 apapspapap apspapapcr akwwslwak
//
LOCUS       WP_457684092             688 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457684092
VERSION     WP_457684092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Levdikov,V.M., Blagova,E.V., Rawlings,A.E., Jameson,K., Tunaley,J.,
            Hart,D.J., Barak,I. and Wilkinson,A.J.
  TITLE     Structure of the phosphatase domain of the cell fate determinant
            SpoIIE from Bacillus subtilis
  JOURNAL   J Mol Biol 415 (2), 343-358 (2012)
   PUBMED   22115775
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..688
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=73936
     Region          21..260
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          257..684
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpsdrpsdeq argplwsepg sllehvavav fgidddnric ywgpgaqhlf gyraaellak
       61 pgallfpaap gdgsdacarl aergrtegyw rgrllathld gsvfdcgfrv fpvagaagrs
      121 vvmalasrgd eldrvktnla fldalfetcp iglvmldeel ryahlnqgla dinglpiedh
      181 lgrriteimi tadggeyerm lrgvaeegkp vagvrvgmrt rghpdrdkvl svsffplsra
      241 ggtrpgvggl lvdvtdreqa iveatatrqr lalldqastr igttldvqvt aqelvdavvp
      301 vfadaavvel vewlderesf dpalpvitrr lahgtvlppp atelvsgveg vhyppgsaih
      361 rmlrtgrpis apvnqefilr tvldeerarv ladsgltcll lapliargtv qgiaifgrsa
      421 arpafteqdl slaaelasra alcldnarly srernialtf qrallpsslg tcpslhlahr
      481 ylpgshvtev ggdwydvial peqrvalvvg dvmghgvsaa asmgrlrita kalarhdqep
      541 eellteldqc aqeagielat clyirydpvt ghtriasagh pppllrypdg rtevvdevlg
      601 vplgvggcpy rsteiglpdd ttlvlytdgl ieargqdide gltalrtelg rlpdsleaaa
      661 dhilarlvps spaddtvlll arvhrlrl
//
LOCUS       WP_457684093             518 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684093
VERSION     WP_457684093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56169
     Region          1..513
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mydyiivgag sagcvlaarl tedestrvll veagpvddaq eihvpaafsk lfqtkydwsy
       61 lsdcepgldg rrrflprgrm lggsssmnam iyirgnrrdy dawaaagaeq wgwddvlpyf
      121 lraedfrget spwhaaggpl tvsegrsrhp lmaayvaasq eaghpytadf ngpeqdgvgy
      181 yhltqrdgmr cstavaylrp alerpnlevl tgaqctrvlf egsratgvel erggdllqlr
      241 aerevvlsag aynspqllml sgigvadela argitprvdl pvgenlqdhp higlsyltdt
      301 eslltaetpd nvrmletegr gplssnvgea ggfhrtregl dapdvqvhat pvmfheegis
      361 pvtdhafmfg avlltptsrg kvslrsaips akphilhnyl tteedrttvv ralrmlldia
      421 dqpslrkhrr adfrvpratd dagllefarr elqtlyhpas tcaigpvvds rlavhgvsgl
      481 rvvdasvmpt vvrgntnapt imiaekaadl irglpapa
//
LOCUS       WP_457684063             139 aa            linear   BCT 27-JAN-2026
DEFINITION  cold shock domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457684063
VERSION     WP_457684063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Sommerville,J.
  TITLE     Activities of cold-shock domain proteins in translation control
  JOURNAL   Bioessays 21 (4), 319-325 (1999)
   PUBMED   10377894
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Phadtare,S., Alsina,J. and Inouye,M.
  TITLE     Cold-shock response and cold-shock proteins
  JOURNAL   Curr Opin Microbiol 2 (2), 175-180 (1999)
   PUBMED   10322168
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Wistow,G.
  TITLE     Cold shock and DNA binding
  JOURNAL   Nature 344 (6269), 823-824 (1990)
   PUBMED   2184368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10138668
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="cold shock domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15165
     Region          3..59
                     /region_name="CSP_CDS"
                     /note="Cold-Shock Protein (CSP) contains an S1-like
                     cold-shock domain (CSD) that is found in eukaryotes,
                     prokaryotes, and archaea. CSP's include the major
                     cold-shock proteins CspA and CspB in bacteria and the
                     eukaryotic gene regulatory factor Y-box protein; cd04458"
                     /db_xref="CDD:239905"
     Site            order(8..14,21..24)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
ORIGIN      
        1 mrfdevrgyg fiapdagged vfvhvndlrd dkhlfdsglr veyttevger glkasdvkll
       61 gparpaamrr qapvgsgper vgsadsdedm mcdvlshaef rneltealld aapsltaaql
      121 vqvrqrvmel vqahnwtea
//
LOCUS       WP_457684094             577 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457684094
VERSION     WP_457684094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..577
                     /product="trypsin-like serine 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=61991
     Region          88..291
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkpskgvtqe eirkaqeler ywtperiraa vpvdavrage kgqdppssad vagrsgvfap
       61 shqvasgaat vgvflirsed gsatpnqfcs asavtsptks lvltaahclk ggksyrnvaf
      121 vpgyrggasq agqpgerpyg lfpmelgkvw iderylsssp sddvdfavlr vgpnsqgqll
      181 edavgrgntl tavraadlar revtlmgypg gqktplqctn atrafqgrfm eiscagfrtg
      241 vsggpflegf dgsrgnlvga iggyktgglq ddvsyssqfd ndvfrlyqqa vtdaapdtvn
      301 plgdattwqh astvltgrfh sdsvrnntgd livrwsdgev slypgnrayg lrkdiqlvkk
      361 gpvwkkakav tageftgnst ddllvrwddg rltlykdvne tnkltqaiql kgpngtwtha
      421 esitagrfgg gntrrddlvv rwsdaemtly tnvdgrglha ekqlakrknt twshardsva
      481 gnfaatagdq dlfvrwsdge vtvyeniaak gfkaehrlrp aksawrysnl vtagafgggt
      541 rqddlialwp ggklvmygdt takalglerl lvparis
//
LOCUS       WP_457684096             264 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684096
VERSION     WP_457684096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27685
     Region          1..263
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mrafivdaft nrpfagnpag vclldepada awmqrvaael nlpetafvhr taentyglrw
       61 ftptvevdlc ghatlatthv lhttqgaapd aalhfdtlsg altarrddqg visldfpada
      121 ptatpapphl aealgaepkw tgrarhdllv elpdaatvrd ltpdiaalad fsgravivta
      181 sapdgadhdf vsrvfapaag ipedpvtgaa hcvlaplwsg rldrttltgv qlsprggrvg
      241 velrgdrvtl lgqavtvfdg elra
//
LOCUS       WP_457684098             552 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684098
VERSION     WP_457684098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57340
     Region          28..547
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mthrmhdlvp galrrtwaaq ghcpdldlya lfrahrmrdp lrtavidaqg easyaeldte
       61 arclaaglae agirpgdvvg vqlpnsraav aadlalaalg aialpfpvgr ggreavsllg
      121 rsgaraviaa ttyrgtehar elaerardlp alhtviaagp gpvpagcrsl adltgdertg
      181 ftperpdpds aarilvssgs eaepkmvays hnalaggrgn flasllvdgt pprclflvpl
      241 asafgsngta vtlarhggtl vlldrftped alaalrthrp thvlgvptmv rmmvercate
      301 grtadgpkal vlggsaldaa thdeaarvfg cpvvnlygsa dgvnchtgtt qrpplpddgp
      361 givvgrpdpa vceiriappp gaasdgtgei largpmtplc yvgapelnmr yrtadgwvrt
      421 gdlgtlaadg tlrvvgrlkd ivirgganis paevegelss hpdvrdvicv gvpdplmger
      481 laacvvprag reitlqslca hldarglerr khpehllpvt galpltpagk pdraalrdrl
      541 aaglpdepar tg
//
LOCUS       WP_457684100             413 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684100
VERSION     WP_457684100.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43243
     Region          25..404
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnagqqlsat dpplgsaglg qpdcppeida lrgrvmafvr ervmpcepvl daggaaarte
       61 lrglqaeakr eglwalplpe ewggqglalp lyshiaeaeg asdhgpaalg saplldvlml
      121 drhaddtvke rflrriadge vqtcyamtep etpgtdpglt atkavsdaag gwvlhgrkwf
      181 isgagdadll tvlaraddeg pgtdslslfl vpssaagftv vrelpvlgag gqweieldgv
      241 avppehavga pgqalriage rlvlgrvlrc lrwlgqaera fdlmclrars rsqsagplad
      301 rqlvqqmvfd sllairstrp lvheavarla aggdarletg lakvaaarml qqvadaaiqv
      361 hgaaglgpdt alpglfrtgr tarlldgpde lhitavarrv lrgypvtscp vts
//
LOCUS       WP_457684103             613 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684103
VERSION     WP_457684103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Zamocky,M., Janecek,S. and Koller,F.
  TITLE     Common phylogeny of catalase-peroxidases and ascorbate peroxidases
  JOURNAL   Gene 256 (1-2), 169-182 (2000)
   PUBMED   11054546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..613
                     /product="peroxidase family protein"
                     /EC_number="1.11.-.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=69415
     Region          90..611
                     /region_name="PIOX_like"
                     /note="Animal heme oxidases similar to plant
                     pathogen-inducible oxygenases; cd09818"
                     /db_xref="CDD:188650"
     Site            order(271..272,386,389..392,395,419,469,472,476)
                     /site_type="other"
                     /note="putative heme binding site [chemical binding]"
                     /db_xref="CDD:188650"
     Site            order(321,389,555..556)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:188650"
     Site            order(322,325..326,330,385,389,391,541,545,549..550,
                     553..554,557)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:188650"
ORIGIN      
        1 mstaprgsgr rsdprqagda pspflalynr lmlavdhrig wqnlpkplgl ltllglrnil
       61 rrqnlfdtsg ypsqdlpdtg ppearhrter tadgtyndld dprmgmarsr fgrnvpptaa
      121 fpepepeils pspreisral ltrhtfipae svnalvaawl qfmirdwvsh gqgsmdrpwh
      181 ieladddpwp aspmpvartl pdptrpangd glppthlnen shwwdasqly gndpaaqqal
      241 rsgtdgklrv phngslfpde perdpahtpg fwlglammhl lflqehnaic drlrheypgw
      301 sdeqlfqrar linaaliaki htvewtpavi shpttiaalr anwfgilger vhkllgrisg
      361 sevlsgivgg rtdhfgvpya lteefvavyr mhplipddws frsaadnsll qeatfrelsg
      421 pyaydilrkh alpdlfysfg tshpglvtlh nypkflqefq rpddqlmdla avdilrirel
      481 gvpryndfrr llhlkpaedf asltddpswa eelrrmyddd iervdlmvgm yaeprpkgfa
      541 fsdtafrifi lmasrrlnsd rfltrdytpq vytqtgldwi ennsmttvll rhfpelrssl
      601 rsvdnafapw kas
//
LOCUS       WP_457684104             419 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457684104
VERSION     WP_457684104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45441
     Region          2..418
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 msrervrrpe ldhaalfaat psaclvldpe lvivdvnqay leatgrtrdd llgqyvfdaf
       61 pdnpadpdae gvqnlhpsll rvlstgepdt mavqrydipv teqpglfeer wwstintpvp
      121 gpdgrvawii hrvedvtafv hsrrtrpapg gklsereeam eaelyvrara lqhlneelrr
      181 aharerqvav tlqeamlhsp dlaghrdiav rylpaigsln vcgdwydivd lpedgfalsv
      241 gdvvghglea aavmgmlrsa lsaaarsveg paqalkvlgl yarsvdkala ttavqalidt
      301 ggrqvtyssa ghpppvllha dgthelldra tdpplgahpe qvprpqahlp yvpgdtlvly
      361 tdglierrde didtglarlt dalapysrls perladalla rlgvsagard dialvivrl
//
LOCUS       WP_457684107             428 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684107
VERSION     WP_457684107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46829
     Region          16..410
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mspwrvrnlg eddldqvvri weesrdtvre pavslaevvs alrgrmpavv avvgdrvvga
       61 avssvaqera wvlrlaiarq wrrhgigsal laaleerlae agvrrigall pegevgeqaf
      121 knsgytgrpd lsyfekllsa dsaeatlldq lggvvpeagl wdgiagmtge kalierrlvl
      181 plenpavaer yqlvppravv lfgppgtgkt tfaravasrl rwsfievfpy qlaedahgva
      241 aalrrlfarv ehldevvlff deaeeiaser qdptslahrv tnellklipq frrgerrlli
      301 catnavrsld paflrpgrfd ylipvgppda earraiwiry igpdrvagid ldalvgasgr
      361 ftpadieyaa rtaaqsafer hlaagpgqag dptqltddyl qaiartrttl teedirafdr
      421 dlraagrv
//
LOCUS       WP_457684109             365 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684109
VERSION     WP_457684109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37885
     Region          39..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matqkkdrip aalsaeahhd vvvvgggaag lsgalalara rrsvlvvdag eprnapadrv
       61 hnylgregtp psellaagra evaayggsvv sgwvvsarrr tgdggehegf dvaladgtrv
      121 rarrllvatg lvdelpevag laqrwgrell hcpychgwev rdqpigvlat gpngvdkall
      181 frqwsaevtl flhtapepse eqweqlaarg iavvdgkvtg veltddrltg lrldsgrvvp
      241 cravvvaprf aargavlarl glevdeqkgg eqvlgsavaa gpagatripg vwvagnvtdp
      301 yagviqaaaa gltaatsing dlvkedtara vaahraripa prepfaarte aevcarvlgg
      361 rrhgl
//
LOCUS       WP_457684111             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457684111
VERSION     WP_457684111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=26206
     Region          2..237
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mgtylyaita aghplrlsgi sgvgepaaql rtvrtkdlca vvsdappqlr akrrdvaahq
       61 dvqdrlladg aalpmrfglv gtddaqvasv leqdrdsylr rleevdgcre yhlkvarded
      121 dllreimres aevrrlndrt renpgayddk valgelisqe vearherars divarlagta
      181 vrtadveptk rhflsvsflv erekatafse avheeagqrg dtydfslhgp lppysfv
//
LOCUS       WP_457684114             296 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457684114
VERSION     WP_457684114.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=31509
     Region          35..288
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mnshlqgeae taaaprqplr lpteqresgp lwssyvyaig ragtglgtaa prltglrdgr
       61 lrtvtagplt alvssvpada fstegmkaql enlteleeia rthhtvveaa htgttvlpmr
      121 latvyldddr vrsmlrerga efgallsrle ghaelgvkvy adprataaep ppapdgpdpa
      181 aspvspgray lqqrraqrrt qrdayraaga laddvrvrva alardrvvhr pqqgelasga
      241 genianeayl vptdrirefh ralagladgv pgvrvevtgp wapysfatpp aesrsa
//
LOCUS       WP_457684118             369 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Streptomyces nigrescens].
ACCESSION   WP_457684118
VERSION     WP_457684118.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  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 369)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..369
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=39415
     Region          6..354
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mgsdlltlfl cgdvmlgrgv dqilphpgdp alregyvrda rayvelaaar ngpipcpagf
       61 swpwgdalev lddaapaarv lnletsitqy ggfapekeih yrmnpanlpc laaarpdvcv
      121 lannhvldfg rqglaetlga lagaglrtag agadpcaarr pamvpvadgr rilvfsfgmp
      181 ssgiprdwaa agsrsgvdfv arptpaaage iigrvrqlkr pgdlavasvh wgpnwgyhvt
      241 rseagfahal leggvdvvhg hsshhprale ayrgklvihg cgdfiddyeg itgyeayrdd
      301 lrllflvtvd pdtgrlhdvr iiplqsrrmr lrhaspedsr wlrglldrig sgfgpcaaep
      361 egtltlrps
//
LOCUS       WP_457684122             272 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684122
VERSION     WP_457684122.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28328
     Region          21..269
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mseseapgtg rtpgggssge raagaldrgl ailthvagnr gvstpeiaqa lgltrstayr
       61 lvdrleeqgw lthapaagqw qlgptavrla saavastnlr dtaapalrkl aeltqetvsl
      121 gvpngltmvf vhrergtrpa vvtaelgasr plhssslgra ylaalpqqkl edtlielvrd
      181 pmspvsaatv sevhaevert rergwsqdlr dfdesscccg aaiydhtgmp vacisvagva
      241 ermaplvpty gpvvaqvcre lssslgylpp gs
//
LOCUS       WP_457684131             461 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces nigrescens].
ACCESSION   WP_457684131
VERSION     WP_457684131.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659804
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49998
     Region          44..160
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          193..440
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cl00279"
                     /db_xref="CDD:469704"
     Site            order(256,273,285,370,401,425)
                     /site_type="active"
                     /db_xref="CDD:238514"
ORIGIN      
        1 mtsrtaplht gshdlpvsda ladfmagqwa atplpagsrv pgfalfagrr drlaarfpge
       61 rllvpagelt vrshdcdhrf rphsayawlt gltgedqpgh vlvlepdgea vlylrprspr
      121 dgggefyrdr kygefwvgrr pdlaeagrlt gircahlddl vrheagrdas rdpelacals
      181 elrlvkdpwe vgqlqqavdh tvtgfedvvr slptalrhpr gerwiegvfq lraraegngt
      241 gyetiaaaga hacvlhwirn dgpldpdqll lldagvetds lytadltrtl plsgrfspvq
      301 rrvyelvlaa qdagiaalkp gasfrdfhra csgvlaegla dwgvlpvpat ealapdsgly
      361 rrytlcssgh mlgldvhdcg raraeqyldg vltegqvltv epglylqpdd etlprelrgi
      421 girieddlvi tadgarlmss alprtadgve ewmdgllagg a
//
LOCUS       WP_457684133             480 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684133
VERSION     WP_457684133.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49955
     Region          30..465
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,246,249..250,253..255,298,326,330,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrprvapqve tadaggsfsh rdraviaaaa lsmlivqmdw faldlmlpvi ardfgtsstd
       61 lqwlvsgyml aigalmivgg rtadvhgrrr vivvglvvfa vmsvvcsaaq sapwlvgarv
      121 vqgvgaalif pvsvavvtsy frderqgpav gtvlafssvg talgpfvggv faehvswrav
      181 fllnvpvcla avllvlrfvp esrdehatrh ldlpgaaava lglaclmlav dqgqgwgwas
      241 aptlvtlvlg vaflvlfvav errapeplie lslfrnvkfd vitlagslsn vvycliavla
      301 alylqqargl spfhagvifl alscgvgaas ywagqlalrw raellmacgm ltsgagllal
      361 twvrplgwya vvfavcgvgi glgwaltnva tqahvpaert gaasglvlts lvlfgavsvt
      421 iaatvletis gspttaasdg paietvlrgt svlaflgafg lfaicrprll trrvavedtg
//
LOCUS       WP_457684138             298 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA/RNA non-specific endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457684138
VERSION     WP_457684138.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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 11448985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="DNA/RNA non-specific endonuclease"
                     /EC_number="3.1.30.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32495
     Region          24..270
                     /region_name="NUC1"
                     /note="DNA/RNA endonuclease G, NUC1 [Nucleotide transport
                     and metabolism]; COG1864"
                     /db_xref="CDD:441469"
ORIGIN      
        1 mipsdspraa gatagtasrp plvdragyde hflgvpvplp vpsrpevetv vlpythftvv
       61 lrpdrrmaaa tavcidgrrl lenvpresgw qfdprldeah qtgndvyrdn sldrghlvrr
      121 ldpvwgtaae anqanedtfh ytnaapqadv fnqgkqlwqg lenylldhaa dfdrklavlt
      181 gpvlhdsdpp yrgvqvplrf wkvaaflqdg alaatayvld qspdltrdae ralagaqaga
      241 ppplgafrtf qvpvkdvael tsldlgplpa vdlmpvvlap aerwkrlash ddimlqrg
//
LOCUS       WP_457684140             586 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457684140
VERSION     WP_457684140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
REFERENCE   7  (residues 1 to 586)
  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   8  (residues 1 to 586)
  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   9  (residues 1 to 586)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20761992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..586
                     /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=62293
     Region          39..174
                     /region_name="sCache_3_2"
                     /note="Single cache domain 3; pfam17203"
                     /db_xref="CDD:435783"
     Region          197..537
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mrirwprrvf aqvltaqval ttgvmvlats lflaplstel ddqamrrals iaqttaadpd
       61 larklvttep dahgpvqaga erirtatgal yivvmdthgv rwshthpaei grhvstdpgr
      121 alagrqvrqi dtgtlgrsar akvplrddrg rivgavsvgi aydsvqsgll gtipgllrya
      181 gaalavgvla aivlsrrlrr rthgvaftdi salldeream lhgiregvva fdrrgrirlv
      241 ndeagrllgl daqaagrpld evlppgrttd vlagrvagtd llavsggrvl vanrmptqdg
      301 gavvtlrdrt elellgreld stqglldalr aqdhehanql htlrgllelg ryekavefvt
      361 evasaqrasa eeiaervpdp llsallvgka aiaaergvsl rvspstllpd tvvdprdlvt
      421 vlgnlidnal daaaerrrad pfvevelrae hstavlrvsd tgpgvppelr drifaegwst
      481 kaarplpged sptgpvafhr grgiglalvr rlaeryggma rvtaraggga vftvvlpeal
      541 apedgspgrr htaageaavt gaprrperpe rtesrkrrpt gsgasq
//
LOCUS       WP_457684145             293 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684145
VERSION     WP_457684145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32228
     Region          7..293
                     /region_name="F420_MSMEG_2516"
                     /note="probable F420-dependent oxidoreductase, MSMEG_2516
                     family; TIGR03621"
                     /db_xref="CDD:200301"
ORIGIN      
        1 mplqrpfrfg vnmfvpgsrr ewsakcrrae elgfdvvgva dhlefsapfp amvlaaemte
       61 rvrlstfvln tpfynpvlla rdvastdqfi dgrmelglga gyvkaefdta gipfpsggsr
      121 veqleqtvtt lrrlfedtey qprpaqpsgp plliggwgdr llrlaaahad iialtggwan
      181 ttgdvlqlag aaqteervay vrgllgdrad avelnlmvqq vippaertav pdrfeplppd
      241 aersseepps vltgtpadma qqikerrery gftyftvmey nmenfapvia alr
//
LOCUS       WP_457684149             255 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684149
VERSION     WP_457684149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27206
     Region          <2..241
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrialfatcl gdtlfpeavk stavllarlg hdvvfppqqt ccgqmhvntg yqrepvplvr
       61 nfaeqfgdps ieavvvpsgs cagsvrhqhq dvaerygdaa lragvatvra ktyelseflv
      121 dvlgvtdvga yfphrvtyhp tchslrmlrv gekplrllra vegidlaelp eadvccgfgg
      181 tfavknaets tamlrdkmgh itgtgaevct agdssclmhi agglsrirag trtlhlaqil
      241 astrtvphvl teaar
//
LOCUS       WP_457684150             267 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684150
VERSION     WP_457684150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..267
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29102
     Region          6..236
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtaewrpvrq srthelvler ieervlagel kagdrlpper elapvlgvsr salrealrvl
       61 etigvlvaqa grgpdagari vrnpddalgr llrlhfalgs yrlhdvlear vvlerssfea
      121 aaehasaadl deaetllghm repgvaaadf ndldtrfhva iarssgnqlt stltsavres
      181 vrplilrale taedwpatae alnaehtell rlvragkgaq aadlaeahir gfhgrlvden
      241 apqeqeqeqe qqeaqeqgdd graatdr
//
LOCUS       WP_457684154             382 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces nigrescens].
ACCESSION   WP_457684154
VERSION     WP_457684154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40645
     Region          12..341
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(32,34,66,108,235,305,325,327..329)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(32,34,66,108,110,117,185,188,235,240,305,325,
                     327..328)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(34,110,185,188,328)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msstlpttad qpllqradlg glslpnrvvm apltrgraan aalvptelha ayygqratag
       61 liitegtwvs eravgfvhvp giyredqiag wrrvtdvvha lggrivlqlw htgaashpdh
      121 lggelpggps avnprtrsft aggfketvtp remttadiaa tvadfraaae narragfdgv
      181 eigalgafli aqflnprlnr rtdayggdrt grrrllldiv davaepwhgr cvgvrlapyw
      241 negehfrade etladhdalv telndrpvay lhlrgrdrta adeapdlaal aryrrrfdgp
      301 lianngfdre sgnavldagi adavsfgthf ianpdlvtrf alrqepavgd patyytggag
      361 gyvdyalsgs gagvadalvp gv
//
LOCUS       WP_457684155             616 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684155
VERSION     WP_457684155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..616
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66592
     Region          1..588
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
ORIGIN      
        1 mnhrpvsvai vgagsrglgv ferlvahclt qpapltvhli dpqpfgagfh lpaqpdhlll
       61 ntvcaqltaf adphmvdgpv pisgpslhew crrrdlrlad dgytvrpgag reiqpndflp
      121 rrllseyltw aageitdaap enltlvrhrt taidihpgtp dtetvvladg tridadavfv
      181 tvghhslyrp aapapdprlv trpyplpeal dsigpgerva vlgmgltamd viatltlgrg
      241 gahttvehgm rylpsgqepl ivltnrsgmp srsrprlhpg rmrfaplalt tehldeirtr
      301 radrridfaa evlplveaem elayyrvllg remgdttdag lemarrcara ghktlldelr
      361 arfgtspvpg ilsagladrq wteysayrdw ftaevaadla eareglgvsp lkealevlrd
      421 hrdvlravid ppgvddasla affgefastv nrqvigpqld rsaellslid agivrlgpgp
      481 qpkivapagq gpwrlestcl aeplrievdh vvqahvtepg adrapgtllg tlvaagrvrt
      541 lvhrggtvhg ldvtrqgqgi drtgtpqprl fflgphtegs syynhyvpsp gapsrallda
      601 eralstalpe lmtrkr
//
LOCUS       WP_457684156             806 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457684156
VERSION     WP_457684156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..806
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82512
     Region          20..785
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtpepgpgtp spdlapapar sttltvggmt caacvgrvek klgrldgvaa tvnlatgrat
       61 vshpatvsvt dlittveaag ftaqlpepap eadpdpeadp edrlsptdrp dapssqdsqg
      121 spasqdaqdd garaerhrll vtallslpvl vlsmvpgwqf rdwqwlcfvl aapvavwgaa
      181 pfharalrgl rhgaatmdtl vslgvaasfl wsayalffgg agvpgmtmpf sllptagdga
      241 ahlyleaavg vplfvlagrr meararrgtg aalralaela akdvavrtpe gerripvsrl
      301 hvgdhflvrp gervatdgtv vegssaldls lisgesrpve agpgtavvgg avnsggllev
      361 radavgadtq laritrlved aqtgktkvqr ladavaavfv pavmtvsvsv lgfwlgagae
      421 pqaaitaava vlvvacpcal glatptalla atgrgaqlgi lvrgpealer lrridtvvld
      481 ktgtlttgrm svtaltprtg gldataalrl aatveqgseh plaravtaha eerqpgqplp
      541 pvadfsatpg hgvrgtadgr rvevtrpgdv tglpaplpda vhtaeaaght avlvtvdgtp
      601 eavlavgdal rpdsyravdr lrrlglrpvl atgdraatar avaghlaite ihaearpedk
      661 aalvttlkeq ggrvavvgdg vndaaalala dlgiamgsgt daaigaadvt lvredlqaia
      721 davhlarrtl gtirgnlvwa fgynlvtvpl aavgllspmv aaaamsassl lvvgnslrlr
      781 awrprgagts arrphspraq arwetr
//
LOCUS       WP_457684158             523 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457684158
VERSION     WP_457684158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..523
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48182
     Region          103..>141
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          240..424
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(271,297,332,335..339,341,349..353,356,360..363,365,
                     374,379..384,399..401,407,410)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(271,361,363,365,379..384,399..401)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mnkrlrtgai atagvgavaa aaillpnana stdqpaalkt lsahsatqla tslkadlgdq
       61 sagwyldssn ghlvmnvlse ddaasvkakg avakvvqnsm talksgaktl rdnasvpgta
      121 wsidpktnki vvvadrtvtg akmatltktt ngmgegmvtv krsqgefkry dggdagsaag
      181 gaagsaagga gdaaggagda aggagdaagg agdaaggagd aaggagdgga ggggqaagpi
      241 ggsaifggna rcslgfnvtv kgapafltag hcgndsktwt adqggsqplg tvsdskfpkt
      301 dfalvtydda naqpqsavdl qngstqeitk aaeaavgmkv qrsgsttgls dgtvtgldat
      361 vnygngdivn gliqtdvcae pgdsggamfs edsavgltsg gsgdctsgge tffqpvtdal
      421 katgaeigag gggagggdng gdngaaggng agggdagagn agagnagagn agagnagagn
      481 agagnagagn agagagdpga gagaedpgag aqdpgaaggd aln
//
LOCUS       WP_457684159             803 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457684159
VERSION     WP_457684159.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 803)
  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   3  (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   4  (residues 1 to 803)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 803)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 803)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..803
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=86207
     Region          6..260
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          253..664
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          676..786
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mnawnaaesa dfrgpldvtr aatavldaqd liigwspaaq rllgylpeei vgqpletlvp
       61 pavkeagqap eeslsgdrel tvrhrngrlv rmaamicpla kvsagsgpqp arvlvaaele
      121 ahrmwesrqa mlhglatqsp vglgiydtdl rltwanaayt revglplref lgaradelyp
      181 dgefmtegyp rtldavmhhv idtgepildl hfvgqqpsdp gpdhvwscsy yrlqdahgqv
      241 lgvcedafdi tgryqaqrrl nllveagari gttldmtvta rettevavpg fattvtvdlm
      301 qsvlngeepe aaggplptlv rvaarsaqag pdgpphsphr veyppgslqy rsmssggmvr
      361 dentivvplr aggtpmglvt frrsapmtpf dkgeielade lvtrtavcld narrfareht
      421 aaltlqrnll pqhlaspsav dlayrylpsd dragvggdwf dviglsgtrv glvvgdvvgh
      481 glqaaatmgr lrttvralar ldlapdellg rlddlveqta eeqaatvgtd igtddvatgv
      541 tclyavydpv srrctmarag hlppavvdpe ggvsfpdlpa gpplglgglp fesleielpv
      601 gsllalftng lvearnhdvd egldtlgrvl gehrrpldel cdhalaellp dgpaaddsal
      661 llvrtrelda gqvaawelpa epaavgkare latgqlrewg ltelsyatel vvselvtnav
      721 rhasgpvhlr llrdrtllte vsdtghtsph lrhsasddeg grglfivaql vqrwgtrytp
      781 ygktiwteqa fpphysgvpr par
//
LOCUS       WP_457684160             360 aa            linear   BCT 27-JAN-2026
DEFINITION  protein kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684160
VERSION     WP_457684160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 229378
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..360
                     /product="protein kinase family protein"
                     /calculated_mol_wt=39280
     Region          <158..>247
                     /region_name="PKc_like"
                     /note="Protein Kinases, catalytic domain; cl21453"
                     /db_xref="CDD:473864"
     Region          <206..>293
                     /region_name="PKc_like"
                     /note="Protein Kinases, catalytic domain; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 mddreplcaa rlagygtvat qlsllsdhrl qevvasavpl gsgiggrsae ldvdgvrvfv
       61 krvpltdiel rpehvrstan vfglplfypy gagsagfgaw relavhtmtt hwvlgnayag
      121 fplmyhwrvl pdsppegftd efgglegava hwegspavre rlealgrsss slvlflehvp
      181 htlagwladh ragvtesgig spypwvaeal argtaflrar glvhfdahfa niltdgrrly
      241 fadfglalss rfdlsadeaa fhsdhlaydh chtathllrh hlldgvrgdt erdvflrdwi
      301 agrrpgglpp etvalidrha rpavvlgdfh rrflteskrt pfptaeiera vgvrgravta
//
LOCUS       WP_457684164             489 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457684164
VERSION     WP_457684164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50403
     Region          14..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstpkvtsaa psprtaktlg rnaigtgdlv ffvvaaaapl tvmagaapva igmagqaapl
       61 gyllsgllmi vfaagftams rhvrnagafy ayigrglgra tgvgaayvav lsynaieval
      121 lavfgwfses gfqdltgvrv pwwvwamagl iaigvlgclk vtlsakvlav alalevlill
      181 vfeaavyahg ggpdgpgfga lspahlgtag aggmfvlsvg afigfeatav yaeearrper
      241 svpratylav gflalfytft vwtvlnayga dragtvanga agtdmvfaat arfagawaad
      301 amrllivtsa faatlafhng atryfyalgr erllprrlgt vtarhrspaa avvlqsaial
      361 vvvlatlvsg qdpyavtflw sngtgivgim llqtlaalav ygffrrdrrg lpawrvvaap
      421 ltacaglavl ivlvcrnfgl lteastgvnl allaslplvf vlgvgvalri rrrapraysg
      481 lttvdvesg
//
LOCUS       WP_457684166             284 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684166
VERSION     WP_457684166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29211
     Region          <65..284
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mhdhdllqld spdpggcasg hegraesage iphttgcpaa dalvalaagg paegaaldaa
       61 lracglppsg pyrvvvattv geergpavsa ltealrcspg epfaagrlpg geavalvpvd
      121 pdaerrlslg elwptlyaeg pqtplhagis gpvrapegin salgqaryal tvsraqapdr
      181 arvtavedlg tlgallagvp aevrtafstr vlgplarggg shrmlvetle iflahhgswa
      241 rtaaalqlhv nsvhyriqri esltgrdlsr lehkldlqaa llcr
//
LOCUS       WP_457684167             173 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457684167
VERSION     WP_457684167.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..173
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18642
     Region          11..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 meqpdtsaeq pspsrtepae lagrlravlq qllplirgrs phrdltpsrt aalaalaahg
       61 plrigelaar mhialsttsr mvdlldtcgw iarrpdpadq raslislndd glallravrr
      121 ettgllaeri grlapdrqrl lydalpalee mvewtpppag ppsrrpaatd pap
//
LOCUS       WP_457684169             284 aa            linear   BCT 27-JAN-2026
DEFINITION  RibD family protein [Streptomyces nigrescens].
ACCESSION   WP_457684169
VERSION     WP_457684169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Stenmark,P., Moche,M., Gurmu,D. and Nordlund,P.
  TITLE     The crystal structure of the bifunctional deaminase/reductase RibD
            of the riboflavin biosynthetic pathway in Escherichia coli:
            implications for the reductive mechanism
  JOURNAL   J Mol Biol 373 (1), 48-64 (2007)
   PUBMED   17765262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="RibD family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29480
     Region          61..268
                     /region_name="RibD"
                     /note="Pyrimidine reductase, riboflavin biosynthesis
                     [Coenzyme transport and metabolism]; COG1985"
                     /db_xref="CDD:441588"
ORIGIN      
        1 mtelldaaaa wdrlrrirtt dealaagmaa dgdgglrwqq patpealela grylplclag
       61 prvavaqlgq sldgfiatrt gdadyvtgee drchlhrlra lsdavvvgag tavaddprlt
      121 vracagdnpv rvvldprgrv prgsgvftdg aaptlwvvgp evtptapgtg tevlvlpdaa
      181 afaperllaa larrglgrvl iegggvtvsr flqeralhrl yvtvapvllg dgipglrfpg
      241 tpvmrealrp plrrtllged tlfelelrpg ggpsggtgsg gtad
//
LOCUS       WP_457684171             367 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces nigrescens].
ACCESSION   WP_457684171
VERSION     WP_457684171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=37124
     Region          35..306
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkrsgwvawl rllaglgilv alvwhlgsqa flaglrridt vtllaalgig vlttvcsawr
       61 wclvarglgl rlplgravad yyralflnaa lpggvlgdvh ravhhgrssg dlgrgvrava
      121 lertagqvvl lvtgavvllv rpspvlapvv sflaspaval svaaagllvl avavrlrrrr
      181 gasrgeralr tvvaearqgl largvwpgva lssaavlagy lgmfvlaarv agatapaael
      241 vplvvlalla malplnvggw gpregvaawa fgaaglgaaq glttaviygv lafvaslpga
      301 avllarvspl starpatsga vprqaerppl aaatgmirqr aaevpsavag gvrsqtsqat
      361 aargdtp
//
LOCUS       WP_457684175             372 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457684175
VERSION     WP_457684175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38760
     Region          24..362
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtrtgataae rvvhfvlpgd vddpaapsgg ntydrrvcrd lpaagwrvrp yalpgswprp
       61 datacaalaq rlaalpdgav vlldglvacg vpevlapeae rlrlavlvhl plgdetgldp
      121 alaaeldare hrtlhtveav vatsewaarr lvthhglaap rvhavlpgad paplapgtdg
      181 atgllcvaav tprkgqhrli dalatvtelp wscacvgald rdpgyvaqlr gavdtfglgd
      241 ritftgprag adleasyaaa dllvltsyae tygmvvteal argipvlaaa vdgvpeavgq
      301 apdgsvpgll vppgrpaala dalrgwlgdp qlrdrvrssa rerramlegw emtshslagv
      361 leqlrhklrs tr
//
LOCUS       WP_457684180             287 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457684180
VERSION     WP_457684180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31218
     Region          1..264
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtavpvaliq vtdvrritph mvrvtfagdg lddfptwpdq qlkllfprpg hraprlpdaa
       61 adgdgmrwyq aflalpeeer pwmrsytvrs ydpvrhriti dfvlhgttat agpatrwaas
      121 aavgdllary gpaaqyakpl pldradwlll agdatalpai gslvealpag tralacveva
      181 gaaeeqhftt radltvqwvh adgrqdalpa avraltfppg avfawlagea gavralrrhl
      241 veergvgkrq idfsgywrrt lsqddaptee dlaeaqerla aarppqd
//
LOCUS       WP_457684183             162 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione peroxidase [Streptomyces nigrescens].
ACCESSION   WP_457684183
VERSION     WP_457684183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Arthur,J.R.
  TITLE     The glutathione peroxidases
  JOURNAL   Cell Mol Life Sci 57 (13-14), 1825-1835 (2000)
   PUBMED   11215509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..162
                     /product="glutathione peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004602 - glutathione peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17476
     Region          1..160
                     /region_name="BtuE"
                     /note="Thioredoxin/glutathione peroxidase BtuE, reduces
                     lipid peroxides [Defense mechanisms, Lipid transport and
                     metabolism]; COG0386"
                     /db_xref="CDD:440155"
ORIGIN      
        1 mslydiplrt ltgepaslad yrgkallvvn vaskcgltpq ysglerlqqr ygdrgfrvlg
       61 fpsnqfagqe pgtaeeiatf csatygvsfp lfektevnga drhplyaalt ntedaegaag
      121 dvqwnfekfl idgegkvagr frprtepeae elvtaieavl pa
//
LOCUS       WP_457684189             485 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces nigrescens].
ACCESSION   WP_457684189
VERSION     WP_457684189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..485
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49989
     Region          7..472
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mlsplknpah lrrdvlaslv vflvalplcv gvavasgvpa elglitgivg glvvgflpgs
       61 slqvsgpaag ltvlvfeavq efglgvlgav vllaglvqla lgamkfgrff raitvavvqg
      121 mlagiglvli fgqlytmagv eqprsgidki lgvphlvtei atssqaltaf aigagtiavl
      181 vlwkklpaqa qllpaplaav alatvattva gwsvprvevq gllsaiqppg msdfaslgsl
      241 aalgtvlafa liasaeslfs aaavdrmhdg prtdfdkelm aqgvgnaicg vlgalpltav
      301 ivrssanvqa gaktklsril hglwlvlfaa llpaaigvip laalagvlvh agcklvpvkd
      361 llplwrthrg ealvlavtai aiittnmfeg vllgiglavi ksawetshiq ldthettdgr
      421 llvtltgsat flrlprmlet lealphdkpv eldlselrhl dhacritlen walqrgttig
      481 elakv
//
LOCUS       WP_457684191             284 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457684191
VERSION     WP_457684191.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29024
     Region          14..272
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtaphpttle qpvrrrrsrg fvlrilpalv litaavtgpw lhphaidvpl tapyagpggg
       61 aplggdhlgr dvltrllagg relivtsllv allvtvvaal lgalgalrpa vgriversad
      121 vlmllpavlg illltlswpg ggrfaviaaa vvmgvpyavr laagaatpva asgyieaaav
      181 ggerlwhlvv revlpnlrat llalfglrfv aavyvvatag flqvgpqppa adwalmiren
      241 aggivlnpwg vlapslaigl lamsvnlavs alvpqtgrka vtal
//
LOCUS       WP_457684198             342 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine synthase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684198
VERSION     WP_457684198.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10107527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="cysteine synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_process="GO:0006535 - cysteine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=36165
     Region          19..309
                     /region_name="CBS_like"
                     /note="This subgroup includes Cystathionine beta-synthase
                     (CBS) and Cysteine synthase. CBS is a unique
                     heme-containing enzyme that catalyzes a pyridoxal
                     5'-phosphate (PLP)-dependent condensation of serine and
                     homocysteine to give cystathionine. Deficiency of...;
                     cd01561"
                     /db_xref="CDD:107204"
     Site            order(23..25,36,42,44,86,89,105..106,109..110,113..114,
                     172..173,266..268,269..271,295,305,308)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:107204"
     Site            order(49,79,185..190,229,275,301..302)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107204"
     Site            49
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107204"
ORIGIN      
        1 mpgalqrpsv vsrisdligh tpllelavse tgsrlllkle mfnptgtaki rmarqmilda
       61 eargalrpgg riiestsgnt glglaviaae rgytftavvd hhacadklra mkalgtelvh
      121 vrndgteela taareelaed larsqdntvf teqhnnpsng vgyfpvahel nealdgrlhv
      181 ligavgtgga lcgtarelrt lipsfrtigv epkgsiafgg pahdyyqsgt gtpegaeiga
      241 lvdfdlideg vkvgdveafa tcraiartgl liggsaggvv hvalsrlasl ppgttmvali
      301 ndggekyldt vfndewmrar gllapttere ieelltklrr nr
//
LOCUS       WP_457684201             333 aa            linear   BCT 27-JAN-2026
DEFINITION  McrC family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457684201
VERSION     WP_457684201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            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 10008445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..333
                     /product="McrC family protein"
                     /GO_function="GO:0032067 - type IV site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          3..330
                     /region_name="McrC"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, regulatory subunit McrC [Defense mechanisms];
                     COG4268"
                     /db_xref="CDD:443409"
ORIGIN      
        1 mawlayalht pvptaarrws tapdgyadlv aaalleecek llreglrrdy vrrqslepvl
       61 rgrldvvaqa trrfgqldql hvrtfdread igdnrvlgta lkaalslttd sglarglhgv
      121 adafprsgtp atalhalert qytrlnaryr pahtwarlll rgggvsdlls dhgttaggll
      181 lampalweav vrriateaaa phggrpvpsn ggtgitvrgd lgststfrpd lllslprpda
      241 nghvllpida kykrydrrgv sagdihqllt ysagytpada psavivhpqp ggyarrtlri
      301 gspqrglgvi yvlgidthas peqasawmra tlp
//
LOCUS       WP_457684202             128 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457684202
VERSION     WP_457684202.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..128
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14137
     Region          13..126
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mmggseqelv dewhgllslh atvhnaleqe lqtqhglsvs efealellts sehgkcrgqd
       61 ltqavhlsqs aasrlvarle rgglvervmc dldrrgifvv ltdeghrrys dakpthrsvl
      121 artlrgen
//
LOCUS       WP_457684210             122 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684210
VERSION     WP_457684210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 122)
  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 11450000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..122
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=12061
     Region          <2..121
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 maalrrpaer alyaaahtap rrllggclgm aaaqvpltrl acsalpcpgc ggphgrpava
       61 gppgeelhfs lshsggpall afaaarpvgv diervpggrd gpdaaaslht leqaelaalp
      121 pv
//
LOCUS       WP_457684216             403 aa            linear   BCT 27-JAN-2026
DEFINITION  McrC family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457684216
VERSION     WP_457684216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            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 10008445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..403
                     /product="McrC family protein"
                     /GO_function="GO:0032067 - type IV site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=44159
     Region          22..394
                     /region_name="McrC"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, regulatory subunit McrC [Defense mechanisms];
                     COG4268"
                     /db_xref="CDD:443409"
ORIGIN      
        1 mtsvveiveh apavsvalpd avgqalaaag vleaapdpya pgrwslrags kvgsvavglp
       61 gadetftvri vpktpiarlf flvgysldpk gpwrdgevev aeqrdllpal ahaverqvdq
      121 alrqgllqgy rateesalvv rgrireaeqi rrrfgatlpv evtydefttd iaenrllraa
      181 verllrlpgv prdvrrrllh qrarladaav vvrgqplpdw rptrlnaryh talrlarvvl
      241 qnasaehahg glridgflfd mnklfedfvt valrealrgs grtsrlqdah hldeaaevrm
      301 rpdfvlygad gapaavvdak yktekrggfp etdlyqmlay ctalglregh lvyargnash
      361 aahrvrhagi lihqhaldld qqpaglladi atlarqmvpd lrv
//
LOCUS       WP_457684220             361 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457684220
VERSION     WP_457684220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36649
     Region          48..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msitkgdrpk aervrprsrs pfrsrtavwa aaglvavllg fvllslligt gsssaarawe
       61 ylrgdpsara daqlrlavle vrlprtlaav lvgvclgtag cllqaatrnp laetgllgvn
      121 sgaafavvlg ltffgatsss alllwalvgg maasavvllf aasgrtagsp lrlvlagsal
      181 gatfhgmtsy vllgtqstyd tyrywtigsl agvetsdllp llpvvavgll ialgcarpls
      241 alglgddsar slghrpgrvr llvaaavsll agcavavagp iaflgllapy aaralagarm
      301 aaqlvlsali aadvmiladi larivirpwe tpvsvllafv ggpllvwiar ssrlstagaa
      361 a
//
LOCUS       WP_457684222             269 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684222
VERSION     WP_457684222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28654
     Region          10..261
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtsmtatpgl avralragys grtvvegaef aipagqvaai vgpngcgkst llrtiarlhr
       61 pesgevhadg adiwrlsrrq aarriallpq sprapeavtv aglvrygrhp hqgllrqwsr
      121 edehavreal eatgttglaa erldrlsggq rqrcwlamvl aqqtpvvlld eptsaldlgh
      181 vvdvlelvre vaaagrtvvm vqhdlaaaar yadtliamka griiahgepr dtvdealvkd
      241 lyaldadilr apgdaspvvv prtrnhtgt
//
LOCUS       WP_457684230            1031 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457684230
VERSION     WP_457684230.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1031)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1031
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=110661
     Region          3..>1029
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mqpmstplsr asqkeealwl ldklvpdsgv nnipaaiqva grlrttalre aaarllrkhe
       61 vlrtvfhdeg aglrkailap edapvdievs rstadgladd ltalaarpfk fngrpmlric
      121 qveapegdvl cvvahhlvfd vasaqivmge ltrlydavla gedlsgeavv pvaavaadep
      181 rpesfrfwrd hlsgfdagsl dlwmdrqgsa ettlkgatva hdlsdeardv vrrlrrelra
      241 sepvillaay ylllaqhgag pdivigspad irgqqaagai gyyvnilalr vrtdpaqsfr
      301 alvrqardvf leavshvdvh vdlllpeipr vnsawsttlf rhmfnylpgg lsaettiggl
      361 paralmvrng ysrmnlefdi lsekdritve alygleshrr ddvalllqry dallvavgae
      421 pdrpvgelss wserdrtvia aanrtatdtp apsvlrtvae raaaapdava ladgdrktty
      481 aelwqaasdt rellcasgvt agdvvavaar rgpelaaaal gvwlagcayl pvdpdhpadr
      541 isyqladsga ravlagdtvt lpegtprlem aglravrggt aelpadpdpa scayliytsg
      601 stgrpkgtrv shgnlanlvr hfldelkpgp gqvtlwmttf afdisalelf lplasggtla
      661 vapdearvng tllrellvrh dvgivqatpt twrtvieqvg dqlagrrvlc ggealpadla
      721 erlletaaev rnvygptett iwstvgklda adgavhagtp lrnttafvld pagrelplgv
      781 hgelciagag vaigyhnrpe ltaerfgehp eygrfyrtgd larwrdngtl evlgrvdrqi
      841 klrgnrlela eieavlrehp evtgaavvtv gdlsadavlv afvvahpteg iverlwehar
      901 aklpssavph dfvltdelpt nanekvdyph ltrlatarra aaghgaaaeh hedplvdall
      961 smfrellgre dvtadanffv lgghsllaal lvqriqesfg aemrlaeffa lptplglaaf
     1021 lrsrgvepgt g
//
LOCUS       WP_457684236            1843 aa            linear   BCT 27-JAN-2026
DEFINITION  type I polyketide synthase [Streptomyces nigrescens].
ACCESSION   WP_457684236
VERSION     WP_457684236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1843)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1843)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1843)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1843)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12098352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1843
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1843
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=193917
     Region          3..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          31..1386
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1211..1656
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1409..1410,1412,1433..1436,1461..1464,1488..1490,
                     1511..1512,1534..1535,1549,1576..1577)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1512,1536,1549,1553)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1672..1755
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 meneaklrdy lkratadlrr trqrlrevee kqhepiaiig macrypggvs speelwqlva
       61 dgrdavttfp ddrgwdlesl hdpdsgrpyt syvreggflh dalefdpemf gispheasam
      121 dpqqrlllea sweafehagi dpmalrgspt gvfaglmyhe yasrlnnvap eaagflgtgs
      181 igsvlsgris ysfglegpav tvdtacsssl vtlhlavqal rtgecslala ggvtvmstpd
      241 tfidfsrqqn larngrckaf asgadgttla egagmllver lsdaernghp vlavvrgsav
      301 nqdgasnglt apngpsqqrv veqalanarl sadqvdavea hgtgtalgdp ieaqallaty
      361 gqgrqedrpl wlgsvksnlg htqaaagvag vmkmvlamrh gvlpktlhvd epsshvnwsa
      421 gavelltear dwpesdqprr agvssfgisg tnahvvleqa ppvpapeale taddepveaa
      481 aragvvpwvl sarseqalaa qaerlasfva enpeldatdl gfsllstrag leyrsvvlga
      541 dreeslsgvr glaggldpag vvrgstgtga gtrvalvfpg qgsqwlgmad ellatspvfa
      601 qrmaecgaal sefvswklde vlsdedmlar vdvvqpvlwa vmvslaavwe acgvmpsavv
      661 ghsqgeiaaa cvagilslrd garvvalrsq aigrvlagrg gmvsvagsre avqdriakwg
      721 erisiaaing ptstvvsgep ealqellaec aeqevrarqi pvdyashgaq veelreelat
      781 vlaevtpaeg ripfysavna alisgeelda gywfenlrnt vrfeeaiqal ladghgvfve
      841 csahpvltpg iedtaqeags pvvvtgslrr deggwsrfaq slaqlwahgv pvdwstllpt
      901 grriglptya fqrqrywled tgtvgdvtaa glssaehpll gaavsmpgtq vltgrlslat
      961 hpwlaermvl nttvvpetaw vdlalragdq vgcdlvrelt vhtplvlpdr gavllrvlva
     1021 epgadearel tvysrsedap deqawtrhat gvltrgaepa afdartwppa eaerveledf
     1081 yreradlglg ygpvfqglra vwrrggelfa evalpegdtg dtagfglhpa lldaalqfag
     1141 pagahlplaw agvslhavga talrvaltpa gdgysvrlad tegdpvasia avtwdevpae
     1201 rlaeaagrre slygvdwvaa starvdpegs alvvlgdddg lgvgaalgad vmdldavkal
     1261 dptpevvvlp vpdsgvvgvs ggvrevaygv letlrawlae erfagsrlvv ltrsavsvtg
     1321 eevdlvtapv wglvrsaqse npdhfllvds delqasrsvl saavalgepq vairngelsv
     1381 prlttlepse kdggpvwkpe gtvlitggtg tlgtlvarhl vtehgvrnll ltsrrgpdae
     1441 gaaglrdelt algarvtlag cdtadrdala gllagipaea pltgvvhtag vlddgvlgsl
     1501 tpdridavlr pkvdaawnlh eltkdldlsa fvlfssaagv fgapgqgnya tanafldala
     1561 ayrrahtlpa eslawglwee ssgltgtlse adrqrkardg lrpmssaeal alfdasvagg
     1621 raltvpvrld ltalgaglra devppllrnl vrgtrrsaaa gqggadglpe rlrtasparr
     1681 arlllnlvrg hvvavlgyad adaveagraf kdlgfdslta velrnrlnrd tglklpatti
     1741 fdypnsrvla eylgthfapy gdtgtgaadd eetirrmlts iplnrlaeag lmssllelag
     1801 iteeasette dddresldtm dmeamiqlal dgsgaeddmt rgl
//
LOCUS       WP_457684242             678 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684242
VERSION     WP_457684242.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 678)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 678)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 678)
  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 678)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..678
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73053
     Region          56..652
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtsagprrda hqgarstaaa dgisnaerel yggrlrwdqt fvryegaltr lkfgqmaaal
       61 prmvgmvlrt gwevdrralt gvvtaqvgqg vtaawglvav nrvltqlfad gptadklrqa
      121 lpslvvlavv svgsallaaw stamsgrlep qveravsary yaavtrveve aterpevqrv
      181 leagrfgtds arsmlrlsvg vgsvligmva aavvlvslhw illpmllaia fpkgwgavrs
      241 arreytsrln wvdhrraiss llayltrpha agelrvhaag etllrgyeem srqteaeqrr
      301 laraqahtdl vaggfaglas lacygllwwl laagglplav ggtaviairn sterltslvq
      361 qvnrlyeell fltdtkhate laaehaiprr gtplpcptra vhmenvsfty pgadspalkg
      421 vslsvrrgtv talvgangsg kttltkilag lllptdgsvw wegepgrrve lreadrtevf
      481 smvgllgqdf phwemtaatn iaigagdrpr dmdrvkeaaq aadvhaliag lphgydsivf
      541 kgyergvqls ggqwqklgaa rsryrnapff lvdeptsald phteiaafeg lwalaerdha
      601 vvlvthrlaa takadhiyvl dhgrvveegt hdqlmsaddg lyrgmfaaqa aqygliqapg
      661 dvvpaprrgs aprreetl
//
LOCUS       WP_457684246             360 aa            linear   BCT 27-JAN-2026
DEFINITION  type III polyketide synthase [Streptomyces nigrescens].
ACCESSION   WP_457684246
VERSION     WP_457684246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..360
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39000
     Region          7..353
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mqgahpmavl ckpaiavpey vitqddtlel arrlhkdhsq lrlvlrlieh tgvrkrhliq
       61 pidkvlkhpg ldarsavyee eskarvpsvv rqaldqaele pqqidlivyv sctgfmmpsl
      121 tawlintlgf rsetrqmpia qlgcaaggaa inrahdfcta ypeanvliva cefcslcyqp
      181 tdlgvgslls nglfgdavaa avvrgnggtg vrlernssyl ipntedwisy avratgfhfq
      241 ldkrvpgtme plapalraia kqhqwdagel dfyivhaggp rilddlchfl evppeafrfs
      301 ratlteygni asgvvldala rmfdeasave gqrgllagfg pgitaemslg twastpdiaa
//
LOCUS       WP_457684248             351 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684248
VERSION     WP_457684248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36303
     Region          10..343
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 metpltrlvg vrhplvqtgm gwvagprlvs aaanagalgi lasatmtveq lraavhevks
       61 rtdapfgvnl radagdaaer vrlvvaegvr vasfalapsr eliarlkdag vvvipsvgar
      121 rhaekvaawg adavvvqgge ggghtgnvat tvllpqvvda vdipviaagg ffdgrglvaa
      181 laygaagvam gtrflltsds tvppavqary laaavkditv ttkvdglphr mlrselvetl
      241 ersgrgtall ravrhaasfr klsglswaqm vrdglamrhg rdlswsqvll aantpmllka
      301 smvegrtdlg vmasgqvagv iedlpscael vdrimaeara tlaalppdpp r
//
LOCUS       WP_457684254             630 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684254
VERSION     WP_457684254.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..630
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65345
     Region          24..488
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(29..30,33..34,37,75,130..131,133..135,138,158,
                     160..161,164,294,297..298,301..303,306,342,346,398..399,
                     403,407,423,426..427,430..431,434)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 magppprrap gprykwvals nttlgvliat inmsvmlial pdifrgigvd plrpgntgll
       61 lwlimsylva tavlvvsfgr lgdmygrtrm ynlgfavftv fsvllsvtwq hgtagalwli
      121 amrvlqgvgg amlmansnai ltdafparqr glalglnqva gitgsfvglv lggllgpvnw
      181 rlvflvsvpf gvfgtvwayr klrdtgirtp arpdwwgnlt faagliavla gitygiqpyg
      241 ghtmgwsnpa vlatmaggvl llavfcvvet rvpapmfrlg lfriraftag nlasllaslg
      301 rgglmfllii wlqgiwlprh gygftetplw agiymlpltl gflvagpvsg wasdrfgara
      361 fatggmllaa gtflalqslp vdfgypsfal illlngigmg lfaapnraav mnslppdqrg
      421 vgagisttfq nsamvlsigi ffslmiagla gtlpraltsg ltaqgvpvad aakvaalppv
      481 gvlfasllgy npvrtllgpq vldrlppdra ayltgreffp qlisqpfsdg lavafgfata
      541 acliaavasl lrggryvhdd drartgarqv papvttaaaa ekpgsaaaag pgtatgigtp
      601 tgtaaptgtg taktgapspp ppppphprsp
//
LOCUS       WP_457684257             541 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684257
VERSION     WP_457684257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..541
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56228
     Region          25..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
ORIGIN      
        1 mtpwnavper rneqgsrvgt etegfagllr llkersgrsy gvlagqlhms vstlhrycng
       61 davpmdfapa drlarrcgat adelvelhrr wiladearrr sratsaatkn spapaasstd
      121 epatssthea dasadaagas aapaadtsvg magasvaaad tsadtavpaa paadtsaadp
      181 hrapgsspap hpphsppaph pqaapdspat pasadesptd deqevvagpm avrrgpgrra
      241 llrivlavsa vaavavpaal aveerttvgs prksaqgegr tpaaggastr rpespspgrs
      301 sedrhpapdk karpstpgsa rsddsrasra pddvrggaap qvgissynwd epcgvnyllq
      361 qtpdhvpppp rapqdtrdwa ralggigggh mllqltatgn tddavvltsl nvrvvgkraa
      421 lswpvyalgd gcgsgvtpqt fdidlddsqp lakpvagqdg dvvvpaknfp fkvstrdpqv
      481 lnlnvhtegh dvswyleigw ssggqqgtvr vndggkpfrt saidgrekyg ywpekkrwnl
      541 q
//
LOCUS       WP_457684259             590 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457684259
VERSION     WP_457684259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 590)
  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 590)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..590
                     /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=61512
     Region          163..413
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 madpgralfd pgmwphgriv gelllsvvlg tlaagieslr nggavqivav alaaglllql
       61 rrvlpgtvll vtvvssaafa glapltplvg wsagrritgv gratgtfala yalsfglelq
      121 qelprispai lfvgvlvtlv atvvpglagr ywsqrrtlld tlreynaqll reramiagqa
      181 rmrerqriaq dmhdslghql alisvhtgal evdreltgrq reavgvlrea svgamhelre
      241 vvgllrdgth gpgdgatpsa ttggaptpal eamgeedaka sargvagier laevsrsagt
      301 avelrrsgev rplaptadha ayriaqeglt nahkhapgas itielryepd slvvevangp
      361 apgtaddcrs vvsggqgltg lgerarlvgg mvhvgptadg gfrlagvlpy tsseagatrp
      421 spgratatfv dptgdfrqqi sagspgesdp vidwnglpke ltkamstdkr ssgiaigcgv
      481 aaliallvvi gvvvggvflm kemdtvmiep keyaavkvgq seaevrkrlp dgssflaegl
      541 dkgappvpeg akclslnsse fgsswekdpv frfcfkdgkl iekksfevka
//
LOCUS       WP_457684271             561 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684271
VERSION     WP_457684271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 561)
  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 561)
  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..561
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..561
                     /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=58802
     Region          279..456
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 maraarsrtp hpdtpqsplh rllhtgldgv ralpaavrrg yrsrrtapta gltesphpla
       61 rslgliavtv vgawlgllli gsirvpvgpm dtsmalrpsl aggtridvap lgdlelsshh
      121 apvrldvdvd rldpvrsqal vdhperfagl qaevthdvtr galglalhsc vavvsgatal
      181 glavyrrprr alaagglalt llaasagtay atwnpqsvle pkfsglltsa psvvgnarni
      241 vsefhvyqke larlvtnvtk lydatstlpa yqpdpttirv lhvsdihlnp gawriiaslv
      301 kqyrinvivd sgdtmdhgsa aenhfldpas algapyvwvr gnhdscgtqk yltgrrhvtv
      361 ldhgkvtqva gvriagvgdp qftpdrsvva agdpaertag grladalrtq rlagtpvdia
      421 lahnpaavte adglaplala ghvhhrentl lpqgtrlmve gstgggglra vqnkkpepvl
      481 asvlyldrtt krlqawdeit lgglglsrae vsrhlprenq pgatpspsgs ppsadpssgp
      541 psgpssgsss rparspseha r
//
LOCUS       WP_457684276             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684276
VERSION     WP_457684276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37391
     Region          26..272
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnigektigg vgrggagsag sgagvievtg lrrsygaagr rerggrsges sgpsgpsgps
       61 gpsgprsfea vrgidfsver gelfallgtn gagktstlel leglalptag qvrvlghdpf
      121 rerrkvrprv gvmlqeggfp seltpaetvr mwagctsgar pvdealgsvg lerrrdvrvk
      181 qlsggerrrl dlalallgrp evlfldeptt gldtearhat welvrelrds gttivltthy
      241 leeaeeladr laimhggria aaghvadvva ahpshisfel ptgfhlgdlp plgelgvigh
      301 etdgrtvrlr tdelqraatg vllwaqdkgi algnldvrsa sleeaflhia kglena
//
LOCUS       WP_457684287             546 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457684287
VERSION     WP_457684287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 546)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..546
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55593
     Region          18..546
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mtavtaarpv raarprhlag tgtllrlalr rdrlmipawv lalgltvaam gasfeavydt
       61 aaqraglaas mnhngsmral ygpvfsdsvg glvawrmagf gavlaavmsl livvrhtree
      121 eetgrqells aamvgrrapl taalltalia nallaaliag gtalsgrpaa gslalglaig
      181 gtgtlfagla aiaaqltesa rlakgltgav lglafalraa gdaatadats pltwlspigw
      241 senlrpyage rwwilllfla atalagsaay altarrdlgm sflparpgpa laprslsgpf
      301 glawrlqrtt llgwttgflc agavfggiae gasdlvggnq qtreivermg gqqgltdafl
      361 atmagllgmv aslyaagavl rlrgeetger aepvlagavg rlrwagshlv iayggtavil
      421 asgglalgla hglsvddlgg qlgpvlaaal sqvpavwtlt glavlvfglf pkatpavwal
      481 vggclaigwl gpslkfppwa mnlspyshlp klpgadataa pfvwllalsa lfallglvgv
      541 rrrdig
//
LOCUS       WP_457684294             457 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684294
VERSION     WP_457684294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..457
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48675
     Region          57..384
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpqprparrr trvastatav llsltaaavp aqaatapapg ahaaagttah pghldhkald
       61 eklaavhtag mygsyaavre grdawrgaag vadiatkrpv gpqmrqrvgs itkaltsvav
      121 lqqvgagrid lddpiarylp dlvpgergrq itvrmllnht sgiadyipga fpsllkgste
      181 sidanrhrhf dpeelvrfgl qapptgkpge kwsyantnyv iagmllqkvt genpeeyitr
      241 nvirkaglkh tyfpaseris gphskmyesf fglitpardy stydlswagt agalvatmed
      301 vndfyrallt gkllapaelr qmqttveakd ekgdvlmhyg lgiaaidtvc grfwghtgsv
      361 wgaetvtyst pdgkrqmtig fnrakyqqvd atghikpgpi daaigafqak amcdndvpae
      421 pgtepgpsap patpapktla eqplpltqpr tlvspgr
//
LOCUS       WP_457684317             426 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457684317
VERSION     WP_457684317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 426)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..426
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46042
     Region          48..423
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(94,116,118..119,202..203,212..213,216,219..220,223,
                     254,257..258,261..263,266,309,311..313,337,413)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(117..118,125,129,136,181,184,258..259,262..263,
                     266..267,270,308..309,312..313,314,337,364..366,369..370,
                     372..374,377..378)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mqheqsaptp tptptpaptt eqtahgtavh pepvtlpvtr tpgcpfdppa elaelreqqp
       61 lrpmrypdgh vgwlatghsv vraiaadprf ssryellryp lpggpsgslp paplgdltgi
      121 dapehtryrr llagkftvrr mrqltarveq itadhldame rqgpvadlvq afahpipalm
      181 icellgvsps drarfqehta mlsspdaape eqmaamtala ecvrelvvak rahptddlls
      241 dlttsdltdd elagiggfll aagldttanm lalgtfalls hpeqaaalrg dpgladqave
      301 ellryltith tglraaledv eldgqlikag dtvavsvqaa nrdplkfpdp dtldlrrkat
      361 ghlafghgah qclgqqlarv emrvafpalf rrfptlrlav ppedvplrda mniygvhrlp
      421 vtwdke
//
LOCUS       WP_457684322             501 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684322
VERSION     WP_457684322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53263
     Region          91..>246
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          409..493
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mttyphrall ltlsvatvaa tltaaapavr adapgatvpa lawrpcaepg gpagqecarl
       61 pvpldyrdpd gpqlslavtr vrserpaarr gtllvipggp ggsgvqrlaa kgpalrkama
      121 gaydlvgldp rgtggstras celdaadrhl vtlrswpgpd geidgnaars rriaeacrrh
      181 ggavlrsftt vneardidrl rralgeekls awaysygtyv gavyaqkypr rtdrwvldss
      241 sdpdparvgr gwlantsagt ddrfpdfaaw aadpareseg lrlarrtrdv rplflalaak
      301 ldrepkestt pgvpltgnrl rqalqnalqs dalfagtarl iqqaqdpaae pvlpdtlagp
      361 lsdqdaaamt atvcndvrwp asvpahrrav aadrarhplt aglpvnitpc gfwqapaepp
      421 tritadgpsn ilmvqnrrdp yspyfgalrm rralgerarl ltlehgghga ylnngpacgd
      481 rtvtaflttg rrpqtdshcg g
//
LOCUS       WP_457684320             503 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457684320
VERSION     WP_457684320.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=54199
     Region          11..268
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,69,74,79..82,94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,77,93..96,100,102,139,141,
                     143..144,146,156..157,160,177..180)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,77,93..96,100,141,143..144,
                     146,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,100,102,139,141,143,160,177..180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,173..180)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msdlgrlvad ryrlvervgr ggmgtvwrae dellgrpvav kkllvpphln ddeietlyer
       61 trrearsaar ithphvivvh dvvddeglpc ivmeyipsvt lgdllkrkga lppdeaarig
      121 rgmaaalraa hdagvlhrdv kpanvllgnd grivltdfgi avqagtpslt rtgelvgsiq
      181 ylaperlrtn iaepgpacdl wslgatlyqa vegrppfgrd taietayaia teeyppprna
      241 gdlgpviegl lvkepggrma aheaerllgg htagtvtalg dqptrphrae vpavpsregr
      301 rgrrtvlwga aatalaaavt ggvllwpwgg tgatsarpag anasspppst spsapppvpa
      361 gyhlkkegsd fslpirdgwk rqdppgaeia yvsglaglri nivpfagesd plrhwretee
      421 dqtrrdnpny ervrmdpttf rgrpagywef tfdgskrkyr avelafsstd gtqyvvylva
      481 pnaqwneyrp vfdtavkgir lgg
//
LOCUS       WP_457684328             177 aa            linear   BCT 27-JAN-2026
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684328
VERSION     WP_457684328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=18401
     Region          35..144
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mggksfgkap ggggtpgree fgdsgrerar rrgqgqleaq vlaalheasg pataawvqer
       61 lggdlayttv mtilsrlhak qavtrersgr ayvwtpaade aglaalrmrr vldgepdrda
      121 vltsfvsals ahdeqvlrtl ldrattdgpa ttdgpvtadg papagdpaae sgtdrrr
//
LOCUS       WP_457684330             422 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684330
VERSION     WP_457684330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43019
     Region          41..409
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,244,247..248,251..253,256,285,289,338..339,
                     343,347,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mspatrtsga arsgstspgp savadataep grspwdgrla vlavmlgifs ivtteilpig
       61 lltaigadfg isdgtaglmm ttpgvlaala aptvtvatar idrrlmlcaf vlllalanfl
      121 aaaapaywlv llsrimvgit iggfwsigag laerlvcpea vgratalifs avplgsvlgv
      181 pagtfigdla gwrtafvvmg avavgvfvlt avvtpalpar qltrprvlre vlrrtptrfa
      241 llmtflivla hfgaytyvtp fleqvthlas pglvtvfllt ygaagiagnf lggatvarlp
      301 ratfgtaaal laaatlllpl lgrgawgala llvvwgiayg avpvssqtwf vkaapdapea
      361 asvlftasfq atislgalvg gvaldhtsps tvmtlggata vlvaltawlh fagrhdwqrg
      421 nd
//
LOCUS       WP_457684336             316 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684336
VERSION     WP_457684336.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 316)
  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 10194457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33286
     Region          41..308
                     /region_name="PBP2_ProX_like"
                     /note="Bacterial substrate-binding protein ProX of
                     ABC-type osmoregulated transporter and its related
                     proteins; the type 2 periplasmic-binding protein fold;
                     cd13606"
                     /db_xref="CDD:270324"
     Site            order(46,48,94..95,98,146,148,229,253)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270324"
ORIGIN      
        1 mraavaavag vavigisaca sgpsletrsa itaspdgsre lvigsagfte sellaqmyaa
       61 lldhagyrtr vvtvgnrely epalevgqid vvpeyaatfa dwlhaknkgs kaapvaspdi
      121 gatmaalrrl agprgltvlp agravdqnaf avsasyarkh hlktlsdlgr aklpvrlaag
      181 decvqrpfca pglkkrygih itaidpkgvg ttpakqavqn gqdqmvltts tdatldqfgl
      241 vlltddkklq nadyvvpvvn raraggerpa aalnrlnkvl ttadlaylne qvdswrrlpa
      301 dvarnyleae gllpke
//
LOCUS       WP_457684338             433 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684338
VERSION     WP_457684338.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46581
     Region          105..377
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltsqsley tvivlavlcv aatvwlwprl arrgvgavlg rlgaivvtqv sivcalalav
       61 ntnfefygnw dellgnteea pasvsqgggq yasvgnlkgg lvqpagpqgl drvtglpkgp
      121 adrvgkvesv kivgrrsrai npgfvylppq yfqqqfrrqr fpvmvvisgy pggimnlaqh
      181 lqvpqnagrl iaqgkmqptv ivmvrptiap prdtecvdvp ngpqaetfft kdlpdamksa
      241 yrvgrdpsaw gafgyssggt cslqlamrnp kvytsavsls gdyairddlt tgslfgpgpe
      301 garrerehdl lwrlknlpap qisalvassr kgeadygdtm kflraakspm tvdsiilpqg
      361 shqfttwrre vvpalewqsq qltfpqdtea vpqrkpgvak ggapgqrntp spapsstsdd
      421 kghrrveaer prg
//
LOCUS       WP_457684344             491 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684344
VERSION     WP_457684344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..491
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50206
     Region          3..467
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(10..11,14..15,18,50,100..101,103..105,108,129,
                     132..133,136,260,263..264,267..269,272,300,304,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mviaiaqlmv vldativnia lpsaqrdlgm sdanrqwvit aytlafggll llggriadlv
       61 grkrtfmigl vgfavasglg gaatgsgllf garalqgafg allapsalsl ltttftigke
      121 rskafgiyga iagggaaigl iaggllteyl dwrwclyvnv piaviafvga avflhdkter
      181 grvhldipga vlgcgglvai vygcseaqpr gwgdglvigl lvggavllav fawwqtraph
      241 pllplhivrd rnrggafltm glaviamfgm flfmtyylqt vlgyspvrtg maflpmvaai
      301 vvgstqisar llhripprfl mvpgallaaa glftlthlta lpayvshvlp amllvglgmg
      361 lifmpvmata tsgvaphdsg vtsatvntaq qvggsigtal lntiatstsa vfitdhlada
      421 arkggglglt pavrdqvvkd gvvhgftvai gvasvimlla alvaglmvng rapkhgrtpa
      481 gdsaesadaa v
//
LOCUS       WP_457684357             561 aa            linear   BCT 27-JAN-2026
DEFINITION  molybdopterin molybdotransferase MoeA [Streptomyces nigrescens].
ACCESSION   WP_457684357
VERSION     WP_457684357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..561
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=56933
     Region          129..532
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mtdgefsgep ggavgrprgg tsaegrgdpf ddalalangt aprwvrpgag peattvttpy
       61 aaggaaaats satgsggdap ytpddpfspd dpaaarsgps spsspsgtsr padptpptgp
      121 gprtapaavp whtaralaer avpgppapet svlgealgrt laapltaltd lpsfdtsamd
      181 gwavsgpgpw rldrpadape tglpsgilag hapaealldg haipiatgar vpsgatavlr
      241 sehgevrels dggrrlyapr pappgqdirp rgqecrrgdq llpagalvtp avlglaaaag
      301 ydeltayrrp raevfvlgde lldhglpheg rirdalgpml apwlhslgie aapprhlade
      361 adtlyaalag stadvvittg gtasgpvdhv hptlrrlgae vlvdgvavrp ghpmllarla
      421 prrhlvglpg nplaavsgll tlaepllrtl aarrpaapyr tplaagvagh prdtrlvpva
      481 yrdderhglt avplrfhgpa mlrgiasada lavvppggae rgtelellef pwsaswsagw
      541 tpgwaapggp yeppeatggr a
//
LOCUS       WP_457684362             492 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457684362
VERSION     WP_457684362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..492
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=50656
     Region          8..257
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,67..70,82)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,65,81..84,88,90,127,129,
                     131..132,134,148..149,152,169..172)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,65,81..84,88,129,131..132,
                     134,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,88,90,127,129,131,152,169..172)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(148..156,165..172)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgeifagrye lidpigrggv gavwrawdar rrryvaakvl qqsdahtllr fvreqalrid
       61 hphvlapasw aadddkvlft mdlvnggsla hligdygplp prfvctlldq llagltavha
      121 egvvhrdikp anilleatgt grphlrlsdf giamrkgepr ltetnyvvgt pgyfapeqll
      181 gaepdfpadl favglvalyl itgtkpdgea msrhfsehgi pnapegvpep lwqvlaslvh
      241 pdpearfkta tgarkamlsa vellpdatie eeivevfdhi gplpadfgpd gplrprntag
      301 patagatagt gatgqvsmsd tgsfqlappe pstpatpapt ptptpmpgav pgststghgs
      361 tptghgapst ghgasltghg gafphhggtp tghgvpagpp assgvpttpp pppapayept
      421 aaahpersat rpytagplpv pgqppagisv tvpamaypap rrkpgpppkv avpvlivall
      481 ciavgvwali aa
//
LOCUS       WP_457684369             365 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Streptomyces nigrescens].
ACCESSION   WP_457684369
VERSION     WP_457684369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38675
     Region          82..346
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mserrrglgr glgalipaap qstdhagaag qgatspssap vlapergvaa akvtslpahg
       61 vsreteapag aeastagvse vsgahfaevp ldaikpnprq prevfdedal aelvtsikev
      121 gllqpvvvrq tgpgryelim gerrwracre aglekipaiv ratddeklll dallenlhra
      181 qlnpleeaaa ydqllkdfkc thdeladrig rsrpqvsntl rllklspsvq krlaagvlsa
      241 gharallsve dseeqdhlar rivaeglsvr sveeivtlmg sapkgasktn gpragarvsp
      301 altglasrls drfetrvkvd lgqkkgkivv efasmddler ilgtlapgeg rvlgqtlaee
      361 nneee
//
LOCUS       WP_457684379             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684379
VERSION     WP_457684379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43932
     Region          16..415
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,69,123..124,126..128,131,149,
                     152..153,156,245,248..249,252..254,257,285,289,342..343,
                     347,351,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mhavralrvl lrlrdfrsll aarllsqaad gvfqvalatf vvfspekqts paaiasamai
       61 lllpysllgp ftgvlldrwr rrqvllygnl lrtllamata tlivskvpdw lfyasalsvt
      121 avnrfvlagl saalprvvdg eqqlvmansl tptagtlaat aggglafavr lassdvdafv
      181 vllaaalyfc salttlrmap ellgpdparl qphlrealls tvrglreglr hlaerrtpar
      241 aliamalirf cygaltvmvl mlcryswaet eseglallgi tvgvsgagff aaavvtpwav
      301 grltafgwia gcaalgavlv pslglfftpg pmlaaafvlg lstqgtkist dtivqstvdd
      361 afrgrsfaiy dvlfnvafvg aaavaalmlp pdgrsaallg ivtvlyalva aamvrsgrg
//
LOCUS       WP_457684381             445 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Streptomyces nigrescens].
ACCESSION   WP_457684381
VERSION     WP_457684381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..445
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45500
     Region          15..435
                     /region_name="MATE_DinF_like"
                     /note="DinF and similar proteins, a subfamily of the
                     multidrug and toxic compound extrusion (MATE)-like
                     proteins; cd13136"
                     /db_xref="CDD:240541"
ORIGIN      
        1 mtlapatprr tgrrhdreii alalpafgsl vaeplfvmvd savighlgtp qlaglgvaaa
       61 llttavsvfv flayattaav arrvgagdlp aairqgmdgi wlalllgaav iatvlptapw
      121 lveafgasgt aapyattylr isalgipaml vvlaatgvlr glqdtktply valggfsana
      181 alniglvyga glgiagsawg tviaqcgmaa vylavvvrga rrhgaslrpd aagirasaqa
      241 gvpllvrtls lravlmiata vaarlgdaei aahqivltlw sllafaldai aiagqaiigr
      301 ylgagdrdga raacrrmiqw givsglvlgv lvalarplfi plftadpavq gpllttllvv
      361 avtqpvsgiv fildgvlmga gdgpylawam vatlvlfapv alavpllggg lvalwwamtl
      421 mmtvrmltlw lrtrsgrwiv tgasr
//
LOCUS       WP_457684383             179 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684383
VERSION     WP_457684383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12134272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20130
     Region          18..153
                     /region_name="Acetyltransf_3"
                     /note="Acetyltransferase (GNAT) domain; pfam13302"
                     /db_xref="CDD:379112"
     Site            order(99..100,110..111)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 msslpamnsw ptrirtarll lrpaesadvk eftrlwtdpe vrrflggpve eqklalyqeh
       61 fasrphsfsv ttrdeapvig svsvdprsrf dgrrevsylf lpeywgrgya reavaalvdw
      121 aletvssdsp sviavtqean vrscrlleai gmrhidsfte fdapqamysv erqglrlgl
//
LOCUS       WP_457684389             279 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684389
VERSION     WP_457684389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29549
     Region          41..192
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlepshrigm tdpvriparg pgvnrfsggp avtdggvtps radarrnral vlqaarfafe
       61 eqglgvplge iarragvgag tvyrhfpske alfrativdr ielftdtard laevpdpgav
      121 ffrflssvvr lavrnkalcd aleaagagrf epspgvgqdf ddalevllrr aqeagavrqd
      181 vgiadlrall vgclsmerav pgsgseggap grmtalmcda lrperavtel evepvkrnes
      241 rcgvcgaaia aahtgrpary cggacrqkah rarertrqt
//
LOCUS       WP_457684398             454 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684398
VERSION     WP_457684398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..454
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47177
     Region          14..238
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(16..18,32,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(62,65,69..70,79,100,104,110,114,117..118)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 mtekppraey rtaeyriedl ahlsgatvrt irayqdrgll prperrgran vygaahlarl
       61 rqiadlldrg ytlasikell eawdagrdlg gvlglvaeid gpwtdeeasr isrtdldaaf
      121 ggspdetala eavelgvler ipdrddeylv pspqelavaa elhsagvplt aiaghlrevr
      181 gqvehiaarf ldfttehvfq qfldhpptea etaeaatlvr rlrplaqqti daelaramrt
      241 latqylrhhl sealpaearr psgraadtea stgaeavast gadaearnga dagattegsv
      301 eacakggieg gveagavgpl vdgagrgpgq agagsvpapr aapglppapp sapetvllpa
      361 eavqavralv gaentatfia aaahrevqar tmdalvatss gegigidtas adnagaprth
      421 ptppspptpp vpvkppattp sprpapqtrp pdrp
//
LOCUS       WP_457684405             524 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684405
VERSION     WP_457684405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..524
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52053
     Region          36..493
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,242,245..246,249,312..313,316,344,348,
                     401..402,406,410,426,429..430,433..434,437)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrstpergta aggrtpgagg kpgggpagkw wplvaialgn flllvdvtiv ntalpriadg
       61 lgatltslqw vldiyalala allmvagsaa dlfgrrrlyv agltlfalas lvcglapdag
      121 vlvaaraaqg agaaamvatn apllmaayqg rdrgvafgvw ggtngaaaai gpvlggllte
      181 yvdwraiflv nlplaavavw itvrrvpesh gtlprprtds agrtpltrid wpgtasftac
      241 agaltyglmr ggdqgwteag tltalggaal allvfvvver rvqrplldlg llrrpsfaal
      301 laaalllqaa afpyltfvgl wvqnilglsp vqaglavtpm alvsllvgal ggrllqrmap
      361 qlpvgiglll vgagvlleya llddgagwaa llpglaisgl gigaampvlv saalgaappq
      421 ragmasgavn tsqqlgyavg iaalgtvfag alhdvrpgas rtavaaahvs gltdillisg
      481 tvalaggvlv lavvrrgagg dgtadrpaar aaaaparaga pgga
//
LOCUS       WP_457684407             276 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684407
VERSION     WP_457684407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28736
     Region          14..273
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 msspapaaga plpykliatd ldgtllrsde tvsertrqal aaataagaah ivvtgravpw
       61 trhildaldy rglavcgqgg qvyhagehrl ltsvtldrql aglalskiea evgplylaas
      121 rdglegevlv gpgyrvqegp lpnvlmddpg elwaapinkv yiqhpslddd alaqaarqva
      181 gdlvgvtvag egivellplg lskatglsla arrlgltake tlafgdmpnd ipmfawaarg
      241 vamanahdel kavadeftas heddgvavvl erlyls
//
LOCUS       WP_457684411             762 aa            linear   BCT 27-JAN-2026
DEFINITION  copper resistance CopC/CopD family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684411
VERSION     WP_457684411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   van Sorge,N.M., Bonsor,D.A., Deng,L., Lindahl,E., Schmitt,V.,
            Lyndin,M., Schmidt,A., Nilsson,O.R., Brizuela,J., Boero,E.,
            Sundberg,E.J., van Strijp,J.A.G., Doran,K.S., Singer,B.B.,
            Lindahl,G. and McCarthy,A.J.
  TITLE     Bacterial protein domains with a novel Ig-like fold target human
            CEACAM receptors
  JOURNAL   EMBO J 40 (7), e106103 (2021)
   PUBMED   33522633
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Lawton,T.J., Kenney,G.E., Hurley,J.D. and Rosenzweig,A.C.
  TITLE     The CopC Family: Structural and Bioinformatic Insights into a
            Diverse Group of Periplasmic Copper Binding Proteins
  JOURNAL   Biochemistry 55 (15), 2278-2290 (2016)
   PUBMED   27010565
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Cooksey,D.A.
  TITLE     Molecular mechanisms of copper resistance and accumulation in
            bacteria
  JOURNAL   FEMS Microbiol Rev 14 (4), 381-386 (1994)
   PUBMED   7917425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18622140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..762
                     /product="copper resistance CopC/CopD family protein"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0046688 - response to copper ion [Evidence
                     IEA]"
                     /calculated_mol_wt=77784
     Region          <43..140
                     /region_name="CopC"
                     /note="Copper-binding protein CopC (methionine-rich)
                     [Inorganic ion transport and metabolism]; COG2372"
                     /db_xref="CDD:441939"
     Region          335..>471
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; COG1276"
                     /db_xref="CDD:440887"
     Region          <666..748
                     /region_name="FixH"
                     /note="cl46415"
                     /db_xref="CDD:480755"
ORIGIN      
        1 mvttglrprr savlrllvva lalagtliga lggaapasah aaltgstpaq gsvvdrapeq
       61 vtltfsegva mgddsirvld pqgkrvddkk lrnlssdhvv kygaglppgl rdgtytvawq
      121 avsadshpva gaftfsvgap skttapvaqq eaggglvgal ygiarylaya gfvllvggaa
      181 fvvacrpaaa lvrsvqrlvv ygwallagtt vamlllrspy tgsgdladvf dlgglqqvli
      241 tkpgaalisr llllaaaalf vavlfgayar ahepagadgp gaagesgerg aadgagrgaa
      301 daeesaadge epavdaaeqa rrrkdltfgl gfggvivatg laatwamaeh astglqptva
      361 mpvdvlhlla vavwlgglaa lvvslywgpp vertavrrfs rlafssvvvl vatglyqswr
      421 qvgtwqaltd ttygrlllvk valvvvlvgi awmsrqwtgr laevpaaelr apeeaekete
      481 qgaeqeagkg agkeagkedr qeaakeaekv tvgasaaaat agtapspape sgpapesgvs
      541 papdetpatn gttptaddaa spaggtpapd paraaqlarq qaalrtartk rrrdadperl
      601 glrrsvlaea svavvllvvt taltatepar teaavkatsg gqsaeagrpq vltipfdtgg
      661 prgkgtarvr lapgrsgsan tlqlrisdpa gkpmdvpeak vsftekakkl gplsvttrht
      721 gkgqwqasgv qlpvpgkwql slvvrtsdid qvteiknvki gs
//
LOCUS       WP_457684417             450 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684417
VERSION     WP_457684417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..450
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=46865
     Region          241..447
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(248,287,325,429,432)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(248,429,432)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(248,287,325)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mgffqfvpar rvvplvgmam vmalvgagga agggggaada atdadavada haagpraarw
       61 tevwgaavqq pvegdvddvp nwsgkgfrqq svrqvvrvsa ggarvrirls nrfgkaplrv
      121 dgaviarsgg gaqawpgttr kvtfrhsgrh sastvipagg eavgdavrls tsplenlvvt
      181 lyfagatgpa tfhrvgltts yraagnhlnd vlakayrqss essyflsgvd vsgpfrerrn
      241 tvvalgdsat dgvgstpeah ggftdglaer lvaarrnvgv vnagiagnml ltssscfgek
      301 gvtrfrrdvl drpgvrtviv elgandvgan watgpcfpss hkpvsarqia egyraliraa
      361 hgrgikviga tmvplkgypg ysakverlra qvnhwirtsg aydavvdfdk aladpadpdr
      421 prpgyvyedg lhpndagyqa ianafdlgel
//
LOCUS       WP_457684425             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684425
VERSION     WP_457684425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /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]"
                     /calculated_mol_wt=31011
     Region          43..281
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtdgpprtti sawrptvpgi aevfhahfte haypshthdt walmilndga vdfacdrhrh
       61 gaagsgtvvl lppgvahdgr tvtaagfrkr vlyldatvlp eeltgravdg pvfgdellrh
      121 rihqlhtslg hrdeghtaav htgeafeaes rlsfirerll fhlaalqppr tpgreanqla
      181 aalrdlldar lptgislqea aavlhthpth lircfkqtyg lpphtyltgk rierarglll
      241 dgrrpaevaa tvgfhdqahl hrhftrhvgt tpsryaatrr rp
//
LOCUS       WP_457684431             289 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Streptomyces nigrescens].
ACCESSION   WP_457684431
VERSION     WP_457684431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Rinaldo,S., Paiardini,A., Stelitano,V., Brunotti,P., Cervoni,L.,
            Fernicola,S., Protano,C., Vitali,M., Cutruzzola,F. and Giardina,G.
  TITLE     Structural basis of functional diversification of the HD-GYP domain
            revealed by the Pseudomonas aeruginosa PA4781 protein, which
            displays an unselective bimetallic binding site
  JOURNAL   J Bacteriol 197 (8), 1525-1535 (2015)
   PUBMED   25691523
REFERENCE   2  (residues 1 to 289)
  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 289)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="response regulator"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=30133
     Region          1..>145
                     /region_name="RpfG"
                     /note="Response regulator c-di-GMP phosphodiesterase, RpfG
                     family, contains REC and HD-GYP domains [Signal
                     transduction mechanisms]; COG3437"
                     /db_xref="CDD:442663"
ORIGIN      
        1 mtttpdtsss ilivddmeen lvaleavlgs ltqkvvrars geealkamlr eefavvlidv
       61 lmpgmngfet aanikgldqt kdvpiilltg asvdpnyayr gytvgaadfl ikpfdpwllr
      121 tkvnvfldlh rknrqlaaqa eqlkrlltsd erpggegppp aattaattat tgtdtgappa
      181 ppmvsasapa sptapqefpd pqhrpapggq aghppippeg pgapapsepl pqpappaagd
      241 asrlaeiagq laevelllrd akgsdkerla driaeleasv grlmvsrgt
//
LOCUS       WP_457684434             484 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684434
VERSION     WP_457684434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51471
     Region          9..372
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msrylkqeaa kagsplrgag vdvpafdsar wqtrldella ahhvpgaala vvsdgavhel
       61 asgvlhtgtr vavtpdsvfq igsiskgyta tlvvllahag kldldapvtd vlpdfavada
      121 eatktvtprq llnhtsgieg dfvsdtgrgd dclaryvegv rdvgltnppg atmsysstay
      181 nilgrivevv tgrtwdealk emlcvplgla htmtlpeevl rfraamghmg epgedpvptp
      241 lwnmlprsag pyggicatag dvarfarlfv dggrtpdgsq vlaaeaveam lrrevempdq
      301 wylgahwglg wglfewdgvr gfghdgstfg qlaylralpe agiavalltn ggaaapkvfe
      361 tlcreltael agvgmpefgp ateepamdpa lfvgsyrreg flmtvtdrpa gegvlrmkye
      421 gadglkdtfe plfwnlvpvs dtpsktvfag rrndkdgwip vvfyaladgs ryvhfgvrat
      481 akss
//
LOCUS       WP_457684441             568 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457684441
VERSION     WP_457684441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  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 568)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..568
                     /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=58330
     Region          <191..500
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mttptpaatp agpiptprrr wslrtrlvvs avaliavvga vigtvtaial hsymqrqldg
       61 kvhefvvraq lprphepspv qggldfvamg gqplgtvgar igtggtveag akldnpsgpl
      121 pdrlaeltra qlaalnkvpr dgrshtaelp glgsyrvesa qngslvlglp ldsvqktvgt
      181 lilieacvtv aglvaagmag samvgialrp lrrvaatatr vselplhqge valhvrvpas
      241 esdgrtevgq vgaalnrmlg hvgsalaarq esetrvrqfv adashelrtp lasirgyael
      301 trrgreqpgp etrhalgrie seaermtglv edllllarld sgrplayart dlsplvidav
      361 sdarvagagh rwrlelpeep avvygdagrl hqilvnllan arthtpegtt vtarvraaad
      421 aaagcggvvq leveddgpgi paallphvfe rfargdasrs raagstglgl aivqavvaah
      481 ggtvrvgsep grtvftvtlp taaanstaaa tsavwdaagr kspvpgrksp vtgrealsvg
      541 geapsaggea lsvgreapsa dqaapsad
//
LOCUS       WP_457684448             519 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684448
VERSION     WP_457684448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52440
     Region          28..492
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,284,287..288,291..293,296,324,330,381..382,
                     386,390,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mspvasdatt tlqppgrtaa rwlilavicl aqltvildnt vlnvaipslt edlgastadv
       61 qwminayslv qsgllltagn sadrygrkkm lavglvlfgv aslgaalaqs pgqliaarag
      121 mgvggallvt ttlavvmqif ddderpkaig iwssvnslgf aagpliggvl ldhfwwgslf
      181 lvnlpvavva laavltlvpe sksragerpd lvgallsmig mvgvvfaiis gpvtgwlsgr
      241 vlvsaaiglv glavfalwel rvpypmldmh ffrnrrfiga vsggilvafg mggsmflltq
      301 hlqlvlgygp ldaglrmapl avtvillnft glsarllprl gtpgmivsgm sllaaglaai
      361 sllggdsygg mltglimmgv gvalamptma naimsaippa kagvgagvng tlmefgqglg
      421 vavlgavlns rfvallplaa agagslpaal artrtdaert avhdafaagi gtsqlvgaaa
      481 vflgglvaav llrraersgq dteapatpsa aepaaasae
//
LOCUS       WP_457684462             189 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684462
VERSION     WP_457684462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 189)
  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 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   5  (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 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20837
     Region          1..85
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          92..180
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 malrhavlaa lldgeysgyq lakafdagva nfwhalpqql yaelaklead glvagrqviq
       61 etrpnkrlfh vteeglaele rfaattakps firddllvkv qavdridaap vieqldarar
      121 taaakveile qlavrlrggr deaeflahga rlgpyltclr glaferetrd wcersagilr
      181 arhdghqqs
//
LOCUS       WP_457684466             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457684466
VERSION     WP_457684466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /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=35333
     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 yrhdgmplev ihqlrawdhq vdvvwpgrsl iriseaiqag shdawvlktv
       61 sggpgltlle aaasvglttv ndvrairgvr dkalaaviar skglpvpvty aaarpeefae
      121 ipeaefplvv kpadgssgra vrlvatpdrl pvpvapggpd apdgphggll iaqpyvpnsg
      181 tdlkvysvag elyatercsp lhpahavrer qvpltlevar itaeigdvfg ldlygvdill
      241 gpdgpvivdi ndfpsfrqvp davarvsaav ldlarhgtrg rdasvgeasv revsvgatsv
      301 reareasvre aapaapftvq plprparpaa sigggr
//
LOCUS       WP_457684456             538 aa            linear   BCT 27-JAN-2026
DEFINITION  apolipoprotein N-acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684456
VERSION     WP_457684456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Bork,P. and Koonin,E.V.
  TITLE     A new family of carbon-nitrogen hydrolases
  JOURNAL   Protein Sci 3 (8), 1344-1346 (1994)
   PUBMED   7987228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..538
                     /product="apolipoprotein N-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016410 - N-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58265
     Region          54..519
                     /region_name="Lnt"
                     /note="Apolipoprotein N-acyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0815"
                     /db_xref="CDD:440577"
ORIGIN      
        1 mlgtrerrre gegkgeargr gpergertar arpagrwlwg agtvllvlav hgnwhlapaa
       61 wlfpvfllry srlrparrgl lrvgyalgla qlvwltstgm vfvpsvlavf avlavvqtlp
      121 faadrlvaar sgsawstlvy pvvlvcgeyl ftqladfgdy gvlgftqhgf lplvqlasvt
      181 gvygvsfvva wtasvahwaw grgfrwreir rgalvwagvl alvlgaggvr lvccapttdt
      241 vrvagisagr aaerateral rtagqelwrp rnlvradprr vraalapvad dlvaatdrea
      301 ragarivvwp etqagvladg qrrllgrvse iarkrqvyvn tafalytprp pyvrnvaalv
      361 tpegkvawty dkthptpmep mtpgkgavpv tgspygrlat vicydadfpg lmrqaadrdt
      421 alimvpandw agfeslhaqr avfrsveygy amvrqsvhgv atavdhqgri rgmadyftad
      481 rqtlvsempv rprtdtlysr tgdlfalqca ggtllvvalg vrgrraraga pgagddrp
//
LOCUS       WP_457684473             211 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684473
VERSION     WP_457684473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22297
     Region          7..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maerkarada lrnretvlaa adqlfarsas prgvsmddia aaagvgkgtl frrfgdrtgl
       61 iravfearie plrqavaegp pplgpsaapr ervpalldav lcfkwdhrhl slaleeagsg
      121 spyegahyaw whgilremle rwwgaeggag qgvaagsapl dgdftahvll aatradlveh
      181 lagqdgmtre rmraqlaafv gkllgdgegg a
//
LOCUS       WP_457684477             252 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684477
VERSION     WP_457684477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25968
     Region          44..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          101..229
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 msaastpspp sppippssps spgarsaapt grgrppkldq vrtveaalal ldevgldalt
       61 mrrlaeamdv ragalyryfa tkhelltama evlladcler plsspdwser laelarrmrt
      121 allgrrdgar vyagthatga htlgfadali gvlreagfaa daaaraaltl vnftlghtle
      181 eqaalqgaad egpadpdllr aavtpgqyph laaalpvlts tdftahfefg lglllqglra
      241 lgpgstppgt gg
//
LOCUS       WP_457684478             266 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457684478
VERSION     WP_457684478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29380
     Region          2..258
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpdveaf rgilascaqg rlirrtevyd agvlhgvsar rlrreltgrr faeperrgkw
       61 llahtdgptv llhfgmtgel vcagpadpph ahdrvvftvg rerqlryrdq rklqglwlvd
      121 eagldrmlsd qgpdaatvtr ktfeavlagr rgslksalmd qsalaglgnl lvdeilwrar
      181 lhparragal sadecgrlyt elrrtlrsav ragrvpprrs wltgrrddpg atcprcgatl
      241 crrrlagrgt vwcprcqpdr targga
//
LOCUS       WP_457684488             388 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684488
VERSION     WP_457684488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41491
     Region          34..388
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrgqtrqglr spgrqqgtrr ralpaavava igvmtlgala ppaasaarpd tvqqslnalv
       61 rddgmpaala svqdrdgrir tytagvgdlt tgskvprdgk vrigsntktf vavvvlqlva
      121 errvhldasv dtylpglvrg egidgrhitv rqllqqtsgl pnysdhlgdd vryytprell
      181 atalqhpadf apgtswkysn tnyvlagliv qkvtgrplae eidrrvvqra glrhtyfpap
      241 gdasirephp hgyyresada plrditetdp swswaagqmv stgsdlnrff tallagrllp
      301 saqlaqmrst vpaeatfgpg aryglglvsr plpcgglswg hggsfpgyet rggatddgra
      361 tnvavtlqlt deaarrnler avdtalcr
//
LOCUS       WP_457684494             303 aa            linear   BCT 27-JAN-2026
DEFINITION  SURF1 family protein [Streptomyces nigrescens].
ACCESSION   WP_457684494
VERSION     WP_457684494.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial respiratory chain
                     complex IV assembly [Evidence IEA]"
                     /calculated_mol_wt=32111
     Region          3..257
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 myrflltprw wginvfavla ipfcifmgsw qlsrfedrvd thqqqedrsa raktaaarpl
       61 erllpvdkvt sgrqasargr ydtghqllvp armlkdkhge rqgfyvlnll rtddgkalpv
      121 vrgwlpgdag tkadtakvpa ppkgevtvtg alqasenqgt dgvqagggla pgqlgmisaa
      181 slvnivpyev ydawitltda qaplravppa aaegsgldlk afqnlgytge wfvfagfvvf
      241 mwfrlfrrdt eaakdaalgi vvevegeggg lgsgiaaglg edglgrgegs gdgqgeaara
      301 gkv
//
LOCUS       WP_457684504             405 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684504
VERSION     WP_457684504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45436
     Region          110..401
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 misnesgtae lprvisvddh viepahlfqt wlpkkyqdrg pkpftagige leyvggkyrf
       61 ttdpegqitd wweyeglifp ykriiaavgf srdemtldgi treqmrrgcw dpkarladmd
      121 lnhveaslcf ptfprfcgqt faeaedkevg lacvrayndw mveewcgdsg grliplclip
      181 lwdidlavae irrnaargvr avtfseipty lglpsihsgy wdpffaacee tgtvvnmhig
      241 sssqmpaasp dappavqasl sfnnamasmm dflfsgvlvk fpqlklayse gqmgwipyal
      301 eraddvweeh rawggvkdli peppssyyyr qifccffrdk hgvasietvg vdnatfetdy
      361 phvdstwpht kqvaaehvag lpddvtykil rgnairmldl sfdqe
//
LOCUS       WP_457684508             262 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684508
VERSION     WP_457684508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29475
     Region          5..250
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mavayeriad elreairage lkpgdklpae sklaerfrrs vptirealra lrdegliekq
       61 hgrgnfvrrq rtsalrtnrr hqweknrare plaeraqtga tehetgltvd dlvfhasyrk
      121 veadkglaea fglpegtall ertyrtryaa esapfslvts ylvhdlvarn palldesnep
      181 wpggsqsqly tvgieldrve ervtarpptp eeaaelelwp gtsvlalrkt sidindrvvd
      241 vsdvilpgdr temlfttple rw
//
LOCUS       WP_457684514             242 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684514
VERSION     WP_457684514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25952
     Region          61..220
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mrstreqqyg keadvgepas greatvtaeg lpewldpvaq vaatieppql srflppesgg
       61 rqsavlilfg rgprgpelll meragtlrsh agqpsfpgga ldpedgdpeg sgpvraalre
      121 aqeetgldps gvqvfavlpr lyipvsgfvv tpvlgwwrrp spvgavdqae tarvftvpva
      181 dltnpahrvt trhpsghigp aflvenalvw gftagvidri lhyagweipw drdkavpldw
      241 rs
//
LOCUS       WP_457684518             297 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684518
VERSION     WP_457684518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..297
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32361
     Region          14..237
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mltpvenhsv phstprtaaf fdldktviak sstltfsksf yqgglinrra vlrtayaqfv
       61 flaggadhdq mermreylss lcrgwdvaqv reivaetlhd lidpiiydea aslieehhaa
      121 grdvvivsts gaevvepige llgadrvvat rmvvgedgrf tgeveyyayg ptkaeavqel
      181 avsegydldr cyaysdsatd vpmlaavghp favnpdralr reavargwpv lsfnrpvplk
      241 qrlpalsmps rpvlavmaaa gaamatatlv wyasrrkttk prlligrsgr tarnarv
//
LOCUS       WP_457684527             529 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684527
VERSION     WP_457684527.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..529
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55801
     Region          124..365
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          427..522
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 matsrllras aavlaatall isgcssgsss pgseaspghr teagvqrpae aaslaplpas
       61 tpaslrpyyd qklswrpcsv agfecatmka pldyakpsad tdlklavark katgpgsrig
      121 slqvnpggpg gsaidylqqy apqpapvrar ydlvamdprg vdhsepvecl tdkqmdrytq
      181 tdvtpdspae vnklisayrs fakgcasrag kllshvstie aardmdvlra vlgdkkltyv
      241 gasygtflga tyaglypsrv grmvldgamd paldsrtvnl nqtagfntaf safaadcikh
      301 kdcplgttsv edagrqlsal fkkldahpva tgeerkltes lattgvvaam yderawpvlr
      361 eylaqakagn grgllslsds yyerdpngty anqmyanpav ncldlasafn gpdqvraalp
      421 sfrkaspvfg enfawaalnc aywpvkptgt ahrieakgaa pilvvgttrd patpytwaka
      481 laaqlssatl ltyegdghta ygrgsqcidt ainnyllkgt vppkgkrck
//
LOCUS       WP_457684528             284 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684528
VERSION     WP_457684528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30803
     Region          190..282
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtlrpygptd qtavlvlida drlpgqpqvt pamlaeamrg svaqeepwwg efgppsvqva
       61 vsaagglvgv iscarrtkdd tgliqwlhcr edatvaeali ahalttlppr pveafqfata
      121 ltqglealpv rhrpvtraal ehagfagerl wrcmradlpr pelprvsdir ivaeperraa
      181 rklqvrrddr tvaeaviglp lqgigvlwwi evspdarghg lgravlgsal qalsdlgadq
      241 vvlyvdddes pggerdrtaa nalyesagfi evdhlwsytl rrgr
//
LOCUS       WP_457684535             475 aa            linear   BCT 27-JAN-2026
DEFINITION  SagB/ThcOx family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457684535
VERSION     WP_457684535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  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 475)
  AUTHORS   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="SagB/ThcOx family dehydrogenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50523
     Site            order(258,260,283,286,328..330,401..402,405,413..414,
                     417..418,421..422,424..426,428..430,442,444..446,461..465)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380318"
     Site            order(260,262,264,330..332,334,415,418..419,424,428,
                     439..442)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380318"
     Region          294..470
                     /region_name="antibiot_sagB"
                     /note="SagB-type dehydrogenase domain; TIGR03605"
                     /db_xref="CDD:188352"
ORIGIN      
        1 mtvhllslhp gttlhdergl ltvrhrwgat ttgpytpqla aalrtladgp asldglaeri
       61 raaaraetpa epqlallrha vdrlghtllr hitadaqvla tavplapeat fgrepapdap
      121 vvlaraahlr pvgdslales prsrfrvrie dgraaaalaa larpltaael qssvrglpad
      181 svdalrsllh atgflhpadd rsraaaaelp agwsfhella hdgsraglrd rqygpvyplr
      241 dtepppppva parpgrtvrl hrpdlgrvar edrsftdvle nrasrrayge hplslaelga
      301 ylyraarvrt lldarpeegr hyavtgrpyp sagsahelel ylavhrcdgl drglyhydpl
      361 ghaltalpgg pgtvdrllhe saaatggapp pdvhltvvsr ikrlswkyaa hayaltlkns
      421 gvllqtlylv gtamglsvca lgggdsdtpv hafgldpyde ipvgafligs aptap
//
LOCUS       WP_457684536             421 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457684536
VERSION     WP_457684536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   3  (residues 1 to 421)
  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   4  (residues 1 to 421)
  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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44982
     Region          64..324
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          335..400
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mrylvlnrtp ltgrpfpdwl gadheavllt daaavsaepd vrsaqlggya hveviddfhf
       61 nplvesralt lhrkggfdrv ialsefdilr aarlrelfgv pgqdvasata frdklvmkri
      121 lakagiplap fapvanlqdl lgfieqqgfp vvvkprrggg smdvhvlhdp qdvesllaah
      181 rdlgtddgaq llaekyiehe lvhvdgivta getrlmwpst qgdstcldik qgqalhscll
      241 daddplldpv reltgralaa lpvpdtfmfh aevfldadrr lvfnevasrm gggmiehvlq
      301 lgfgitlpev yvrslggnap aavpavperi aglslfppra gtlvaipdtc pvpgidtytr
      361 haapgtvlep arlsvekigs vlatgrtrge vekalaeala wferstvirp gtdgtgagsa
      421 s
//
LOCUS       WP_457684548             840 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457684548
VERSION     WP_457684548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..840
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=91208
     Region          2..836
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 maadrvfwqr vlgggftplp rwsripadlp avrrtaipag taeallllse rpglsegqgl
       61 spdtlllaay vrvlaavtgd ssvvtgylpe dspeksplpl waalsqgswa elvtevaqla
      121 devgrhapqa ldelraetgr teplfdtvlv tgrapapedl tdgtvlaagl arsgdrlelv
      181 lshrpdaldg eqadrfagyl laalrelaer pgadhqewsp vperevaqql aefagprrel
      241 pdrrvhelfe dqvrlrpddi aavhgteswt yrelneranr vahalrrggl hdedvvavvt
      301 ernlpwlvav lavfkaggvy lpvephfpad risgmlvrad crrvlterda spgltealag
      361 lpavradhld tllaedhpvt dpgipvtagq sayiyftsgs tgapkgavce hagflnhlla
      421 kiddleiaeg rvvaqtapqc fdislwqlva alavggrtli igqpdildta rfietldtgg
      481 vevlqavpsy levvlteler spralprlrh vsatgealkk elverwfatf pdvalvnayg
      541 ltetsddtnh evmrrvpeqa svplgrpvan vrihvvderl rlvplgspge ilfsgvcvgr
      601 gyvndeertr aafmpdpllp germyrsgdf grwlpdgrle flgrrdaqvk irgfrieige
      661 venqllrvdg vrdsavvvtg egesrqlvaf hsgeelsdat lleslgaalp symipsrfrr
      721 ldvlpltang kidrkaltrl agqeesagdg velrtgterr laelwsqvlk vpagrigras
      781 hffdsggtsl smlrlaiald rvvtpvelqq hpvlaecaal ldrraaeapn pgrqpvdshv
//
LOCUS       WP_457684552             989 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684552
VERSION     WP_457684552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 989)
  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 989)
  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   3  (residues 1 to 989)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 989)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..989
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=108298
     Region          10..257
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          139..989
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          807..835
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          847..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(848,851..852,855..856,858,888,891..892,895..896,
                     898..899,928,931..932,935..936,939)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          886..916
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          927..953
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpedrsipra ikysvlrpll vitgsgriig vhgprqrtil tmlilawgrv vsvdslvdav
       61 wgdeppatar tqvaicigal rksfkqagve gdviltthpg yrlettgsdl dalqftslva
      121 eaaahvkqgr heqgrvlyrq aldlwkgpal agvtgrpved eatrlderry aayeawseve
      181 lalghhqdii seltsianss plheqlrynl mlaqyraglr aeategfrmw rrnfvdelgl
      241 epsvaikelh asilqddpgl tlpvqvkpmv vpaqlppdvd lfqgraaelg eldrllgeka
      301 pgmglitgva gvgktglivh wahkvagefp dgqlyadlsq ydgkqpefva gallgrflra
      361 lgvpgdqips dpaelaslyr svladrksli vldnvrtmsq itallpgtgr scvlaasreq
      421 laadsgtvrv dlglmtahes qtlitkiage gratsekaav nelcrlcdgl plalriaaar
      481 lvakqhwsvq hlvdrlrdeh rrldelstgg levrasfals yrglteqtar myrllglldv
      541 pdfpawvgga lldvspaeae dmierlvdah lltpigsdat gtmryrfhdl lrlyarerae
      601 sdeaedkrra alhrvfrtyl tlaeqghire yggdfaiihg stprrhldap lvgrllgspl
      661 dwfeaerpsl vasilqactl rmeelawdla mssvvlfetr nyyddwravs ekaleanrna
      721 gnirgeaamc yelasvemfq qrfdsatplf trafqlfdsv revhgraltl rnmaitdrvq
      781 gglrsamsrl dearntfrvv gdasaeahtl nqmsqielew gnpdaavrls leavriatal
      841 getrgaaqal nrlaaayvkq grfdaakqsy dgvlrivrsk gdtrgeayal lgigetlvas
      901 gqydeaesil adaleiaerv ddlfllakvh lalgtcsqql nqltrasqhl liarntfhei
      961 gsvwgelqas adisrlsaet cggrtlpgr
//
LOCUS       WP_457684554             431 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684554
VERSION     WP_457684554.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /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=45439
     Region          51..334
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtdlelrpps pvrrpplptg plrplptrrt pwqalhtavl ridaatpter draidvlral
       61 aiagvvlghw lvsgvvlqag ghlvgdsplg hlpglapvtw llqplavffl vggrvsarsy
      121 atarargigy rpwlaqrlar llrpatafal twglvwlglv lagtahetih tlmwlayspl
      181 wflgvyalli aatplvhkag ariavvaclv vaaldasrvl fadsgwpdtl rllnipagwl
      241 vpyclgavwa aggftrrrpa valllgggga maalilwggy pasmvgvpgs tlsnlspptl
      301 aavafglaqt gaalllrgpl rravtapapt gpataprsra twaqflwaav allnlsavtv
      361 flwhqtamlt ttviplglgh tfpglhtspd slawiaarfg wiavfavall vlatafrdre
      421 gargnraiin q
//
LOCUS       WP_457684559             440 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684559
VERSION     WP_457684559.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /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=48877
     Region          100..371
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnnefpayge rrvplppprq mshdtlsrth tpappqtgga tatatlapet ataaapgaat
       61 aggahthtgp rshakgrgkd raktgakada ktdakadaka kprdaffdna kylaivlvam
      121 ghsweplrdd srsaaalyit vyafhmpafi iisgyfsrsf dmrkdrlqrl itgvavpyil
      181 fevaytlfkk wadddpgypi sltdpwyltw fllalfvwrl ttplwkivrw pvplalsiav
      241 laslspdigd dmdlqrvlqf lpffviglsl rpehfklvrr kkarilavpv faaalvfayw
      301 aaprmnaawf yhrdaaqela apwwsgavmt lamfgcslvl vacffawipg rtmwctalga
      361 gtlygyllhg flakgsrfwd wydnpwmhtp wgavlltlia gtvvtvlctp pvqrafrwam
      421 epkmtwafkk dpvgmarsrn
//
LOCUS       WP_457684562             292 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684562
VERSION     WP_457684562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30525
     Region          63..267
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 matqpgapqp helsapeara aldgmwaqlg gepaavarte davangvpvk lywpegegph
       61 pvliwihggg wvlgsatasd atardlsrla gylvvsvdyr lapehpfpaa vedvmavakw
      121 vsgeigalgg dttrtavggd saggnlsavl anelpgtftl qalvypatdl thpfpsyeen
      181 geglmltkda lawfqghylg edvdpkdprv splhadaatl aaappalvit agydplrdeg
      241 eayaqrlrea gvaveqvrye gqihgffsmp aaipeareai drvasalrra ra
//
LOCUS       WP_457684570             256 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684570
VERSION     WP_457684570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27460
     Region          10..245
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvngesashp tligsvqral rlleavgaha dgapakqlar eaglplptty hllrtltheg
       61 ylrrengvfv lgeaaeaigg agarrrqrah isealavagr elgaavyfav yregevevva
      121 vtddparppv tewvdfrata hahaigqcll aqldeatrke hlarhpvqpi tpfsvrtedd
      181 llhrldtvrr gqvayerqgy algtvcsalp vqvgaaaatl avslpvdelh rlrsvtdrlr
      241 kmaeatlttl afsisi
//
LOCUS       WP_457684575             466 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684575
VERSION     WP_457684575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Seibert,C.M. and Raushel,F.M.
  TITLE     Structural and catalytic diversity within the amidohydrolase
            superfamily
  JOURNAL   Biochemistry 44 (17), 6383-6391 (2005)
   PUBMED   15850372
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..466
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48847
     Region          47..429
                     /region_name="SsnA"
                     /note="Cytosine/adenosine deaminase or related
                     metal-dependent hydrolase [Nucleotide transport and
                     metabolism, General function prediction only]; COG0402"
                     /db_xref="CDD:440171"
ORIGIN      
        1 mgatgasgfl ggtaaadaph gkgalrperl hgtrqllvpe vlllpegpvr gravlvdggr
       61 fravgparql laqhrdlqpv rldghllmpg fvdahhhltq sfgkaqsfgq pseifktiwe
      121 plehaldees ayvsaklaal ealrggfttv adagtrapvd vravargtee agircvlski
      181 vsngtggpah larwdghpli hpslaiavpe dapgkvikrt adlcaeagav lqvhvnehla
      241 sverslksvg rrplehlhhl galgphtlga hatlltpaem rllagsgaai synpvasawk
      301 gngvahatml aamgvrfgmg tdgtradgfr lldagetaqr laygmaagds vcgagrlwle
      361 hatarsadal glgrvtgeia agkaadylvv dldvpeltps ydlewelvrl agrdqitavv
      421 vngklrlwqg wppdwdgpal varaarlgpe vvrraglqrv epaqnp
//
LOCUS       WP_457684572             331 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684572
VERSION     WP_457684572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35414
     Region          1..309
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mlpievgivh rifgearsad geplyelvtc alepgevrtd tdftvnvahg pealaeadtv
       61 vvpasgadyd lgaersagrl spamagalgr irpgarvasi ctgafvlaaa glldgrratt
      121 hwrsvddfrr lfpaveldae vlytdegevl taagvasgid lclhmvrcdh gaavandvar
      181 rtvvpphreg gqaqyirrpm pepqisstgv arawalehld rplslrelaa resmsvrtft
      241 rrfreevgis plqwltqqri erarqlleet dltvdriaae agfgtaaslr qhlqsalgvs
      301 prayrstfrg pggvgvgwwl egvgglrglg a
//
LOCUS       WP_457684576             301 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684576
VERSION     WP_457684576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30623
     Region          87..296
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 malviallca gaalrsgggr pedvrrrara lfggreeavp pggwraclrg egvrkwcagr
       61 lvegeagrrw svgrrwdvgr evwclsaglv lgvlggsvvp viasmgavyl vrrwlvtrga
      121 grvrdrraaa viglcaavag elragrqpaq allavgapgl gaegsavlaa aryggdvpra
      181 lrvaarqpga agltgmaacw qvaveggagl asgleriaag lrtqrdqrde lraqlagpra
      241 talmlallpa agllmgsalg adplrvllht pagwgclvvg gllewggvaw tarivaaaeg
      301 a
//
LOCUS       WP_457684603             288 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684603
VERSION     WP_457684603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=31073
     Region          4..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 mrygqalrde iaaegttpli gvhdmyaasv aaghyngffv sgfgfaasyy glpdigfiaw
       61 pdmaafverl rgafphhhll vdiddgyvdp evachvvrrl ertgasgvil edqkrprrcg
      121 hadgklvlpl eeylekldlv lasrtdllvv artdateede ilrraaalag teadvvlvdg
      181 vrsvdgirri rqvvgdkpll fnqiaggksp rlslteltal gvdvaiystp clfaahrame
      241 talaelkyad grlpstgeag geigvreate llarnlsrhh pgrravpv
//
LOCUS       WP_457684607             322 aa            linear   BCT 27-JAN-2026
DEFINITION  1-aminocyclopropane-1-carboxylate deaminase/D-cysteine
            desulfhydrase [Streptomyces nigrescens].
ACCESSION   WP_457684607
VERSION     WP_457684607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Thibodeaux,C.J. and Liu,H.W.
  TITLE     Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase:
            characterization of an unusual pyridoxal 5'-phosphate-dependent
            reaction
  JOURNAL   Biochemistry 50 (11), 1950-1962 (2011)
   PUBMED   21244019
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Nagasawa,T., Ishii,T., Kumagai,H. and Yamada,H.
  TITLE     D-Cysteine desulfhydrase of Escherichia coli. Purification and
            characterization
  JOURNAL   Eur J Biochem 153 (3), 541-551 (1985)
   PUBMED   3908101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34251
     Region          15..308
                     /region_name="Acd"
                     /note="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase, PLP-dependent ACC
                     family [Amino acid transport and metabolism]; COG2515"
                     /db_xref="CDD:442005"
ORIGIN      
        1 mdrvtstapg pppdprtlrp rlpspvqeve daaftrrgvr lllkrddlih pelpgnkwrk
       61 ltpnlraaaa ageralltfg gaysnhlrat aaagrllgfa tigvvrgdel agaplnwsla
      121 rcaadgmrlh fidraryrrr tdpevlaelh drfgafrlip eggsnalaaq gctelgrelr
      181 gaadtvavac gtggtlagla aglgpgqral gfpvlkggrp hflqetvedl qraafggprg
      241 dwrledrfhc ggyarrtpel dafaaafedr hglpleriyv akllyglttl aeegaftpgs
      301 tvaavitgtp ertpdasadr gt
//
LOCUS       WP_457684609             209 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684609
VERSION     WP_457684609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22255
     Region          11..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matketkqrg rprsfdreta leqavrsfwe rgyeatsisd ltramgisap slyaafgdkr
       61 alfdevvvey grlyggflsr avaeeptarr gveralreaa aeytlpgrpr gclvisaaln
      121 ispasaevad slremrlanv raiaaairad iasgelppdt dagalaaftg aviqgmsqqa
      181 rdgaertele aiaelalkaw prkaggasr
//
LOCUS       WP_457684612             516 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces nigrescens].
ACCESSION   WP_457684612
VERSION     WP_457684612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..516
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52746
     Region          55..487
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mtplvrsvrs adtltrdala vlqpgftgtt apdwllrrlg eglvsvglfg rnvadpaqla
       61 altgrlraer eelivaidee ggdvtrlevr ggssfpgnha lgavddtalt ravarelgrr
      121 ladcginlnw apsadvnsnp gnpvigvrsf gadpqlvarh taayveglqs agvaactkhf
      181 pghgdtavds hhdlpriavd lptlqerelv pfraavaagt ravmsahill paldgehpat
      241 lspaalhgll rapategglg fdglivtdgm emqaisatyg iergsvlala agadaicvgg
      301 gladedivlr lrdalvravr dgelpeqrla daaarvrala grtrsadvge gvapapgigl
      361 taarralrlt aagpyaplae payvaaftpl aniavgdetp wgvaaelarl lpgtetatct
      421 aeaaaaagta alvdglltaa agrrvvavvr dvhrhpwmae alstllaarp dtavvemgvp
      481 qappqgalhl athgaarvca qaaaealtdq rlspge
//
LOCUS       WP_457684617             224 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457684617
VERSION     WP_457684617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25134
     Region          54..219
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 msdhtvsvsg lgygrlhglg lagrsrrrlh drtrrpaahh gdrafrrgrp dtcrlekgar
       61 leftdgkirs kavpdgshgr imewltrrcv qarpelwlyr dqglkvqahr vgrarpdgel
      121 apsgafagrg ewadpdpalm vvavtshdad tdqrdrvemp rvyaetgipl yllvdresrq
      181 vlvhsepdgg ryavrhsvsy grrirlpdpv gitleterlk dwvs
//
LOCUS       WP_457684614             330 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457684614
VERSION     WP_457684614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36697
     Region          55..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavqldgvvd rtaprtgkgg apptrrgggs rraargapyl lllpallata vllgwpmvrn
       61 illsfqnlnm keliqhltdw rgfgnyqeil gseqfwrvtl rtlvftavnv vlimvlgvli
      121 glllarlgkk mrltlslalv ltwampviaa ttvfqwlfds rygvvnwlld klgahsmahy
      181 dwvgsqlstf fvitvlivwq slpfvalnly aatttipkel yeaarmdgag twkvftsvtf
      241 pflrpfflat tfleiiwvfk afpqifaine ggpdrltetl piyaftegvg nlhfgmgaai
      301 slltivvllv mtayylrltv kqeqqeenel
//
LOCUS       WP_457684620             277 aa            linear   BCT 27-JAN-2026
DEFINITION  SOS response-associated peptidase [Streptomyces nigrescens].
ACCESSION   WP_457684620
VERSION     WP_457684620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=30407
     Region          1..268
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgryaasrr pedlvgdfgv qqwepeetla pswnvaptdp vhvvlerplk gaaaadfppg
       61 spvrqlralk wglvpswsks peaaakmina rsetvhekps frqafatrrc llpgdgyfew
      121 vtdaaerqle eqgrkkrprk qpyfvtpadg svmaiaglye fwrdrtlpgd hplawwvtct
      181 vvtteaettp lagadggdgp qsladihprm plvltpdrwd awldpartdp devrallapp
      241 paglmrahpv ptevsnvrnn gpelvteldg pevgtlf
//
LOCUS       WP_457684624             487 aa            linear   BCT 27-JAN-2026
DEFINITION  zinc-dependent metalloprotease [Streptomyces nigrescens].
ACCESSION   WP_457684624
VERSION     WP_457684624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Lenart,A., Dudkiewicz,M., Grynberg,M. and Pawlowski,K.
  TITLE     CLCAs - a family of metalloproteases of intriguing phylogenetic
            distribution and with cases of substituted catalytic sites
  JOURNAL   PLoS One 8 (5), e62272 (2013)
   PUBMED   23671590
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="zinc-dependent metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51060
     Region          65..440
                     /region_name="Zincin"
                     /note="Zn-dependent metallopeptidase, zincin/DUF2342
                     superfamily [Posttranslational modification, protein
                     turnover, chaperones]; COG5282"
                     /db_xref="CDD:444093"
ORIGIN      
        1 msdtpfgfgl ppeepedgdn gkkkggqggs qgpadpfgfg ggsggadnpf aalfggmggp
       61 ggemnpgdlg aafqklgqml syeggpvnwd makdiarqtv aqgtedgskd aslspgersa
      121 veeavrladl wldgvtslps gsgsvvawsr aewveetlpv wkdlvnplae rvgaamgdvl
      181 pgemqamagp llgmmrsmgg amfgtqigqa lgvlagevvg stdiglplgp agkaallpgn
      241 iatfgeglgv peeevrlyla lreaahqrlf ahvpwlrshl fgavegyarg ikvdttkled
      301 vvgqidpqhp eelqsalqqg mfqpedtpeq kaalarleta lalvegwvda vvhaaakphl
      361 psadrlretl rrrrasggpa eqtfstligl qlrprrlrda srlwasltda rglegrdglw
      421 ehpdmlptaa dlddpdgfvh heqpdfseld kmlgeaasgg kpdldkpare ndgpdetpge
      481 skgdgdk
//
LOCUS       WP_457684633            1231 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Streptomyces nigrescens].
ACCESSION   WP_457684633
VERSION     WP_457684633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1231)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1231
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=130790
     Region          40..946
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          966..1226
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 msssfsaapp tqqphraarr aaagayrlvr tppgrvdppd ldaaqravvd hrhgpllvla
       61 gpgtgktttl vesvarrvra gddperilvl tfsrkaavel rdrlaarlaa legqpdgrpg
      121 tavggrragi pqattfhsfc yalvrahqda dlfadplrll sgpeqdlvvr ellegqaela
      181 gagralvswp delraclttr gfadevravl arsrelglgp ealgafarrt grpdwsaaaa
      241 flaeyldvld aqgvldyael vhravllaeh tdvaaqlars ydavyvdeyq dtdvaqvrll
      301 ralagnhgat gtpgspgrtl iafgdpdqsi yafrgading ildfpetfrr gdgtpapvav
      361 lgtsrrsgat llaatrlltr rmpltrlpaq kvrahrepap vrdggrvevy typtpgaeld
      421 niadilrrah ledgvpwrem avlvraggrs lpavrralts agvpldidgd dlplrhepav
      481 aplltalraa araalrqepg gaadgesaea vegelvdaad ggagagsgea ggdeagggea
      541 gvgasvvdal ragepggdea dggeagpggs dadeagpgdp dvnepvpdap gagastgvtp
      601 tpatprwlda etaldllasp lggmdsadlr rlgralreee raagqplprp sdeliarala
      661 epqrlvahdp ayargaqrlg lllrkarell agggtaeqal welwdgtpwp qrleraahrg
      721 gaagrnadrd ldavvalfet aaraeertgg rgalnfleel daqdiaadtl trravrpdav
      781 rlmtahrakg lewrlvvvag vqeglwpdlr rrgslleadr igrdglaepl tpgallaeer
      841 rlfyvattra rerlvvtavk aaaddgdqps rfltelgvtp qditgrprrp lsvaalvael
      901 rattvdpaat palreaaaqr laklaalhdd dhhplvpaah pdnwwglhep thssvplrdr
      961 drpvvlsgsa ldqlahtcsl qwflgrevka dtpataaqgf gnvvhvlade vasgrtpadl
     1021 tvlmerldsv wdalafdapw ksrqekdhar aalerflrwh vmeretrgrd tvatehgfdl
     1081 tlragayevr irgsmdhvsq dtqgrayvvd fktgkqkptg pevarhpqla vyqlavrega
     1141 vddafdgrtp epggaelvhl rlgapqkegg dalpavqaqq pldgewvgel lataagrvle
     1201 erftpttgsh cthcsfrasc saqpegrhiv e
//
LOCUS       WP_457684639             803 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457684639
VERSION     WP_457684639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..803
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=84922
     Region          45..423
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mperwqwsrp tgrlrpartn pyegavrpps pphaashrrg kilstfrdlg ifpetaeale
       61 avgiispfpi qeltlpvals gndvigqakt gtgktlgfgl pllervrvpa dveagrarpe
      121 elteapqalv vvptrelcqq vtndlltagk vrnvrvlaiy ggrayepqve alkkgvdvvv
      181 gtpgrlldla gqkklnlsqv kslvldeade mldlgflpdv ekiiqllpak rqtmlfsatm
      241 pgqvislarr ymsqpthira tapddegqtv rnttqhvfra hsmdkpemva rilqaegrgl
      301 amvfcrtkrt aadiadqlar rgfasgavhg dlgqgareqa lrafrngkvd vlvctdvaar
      361 gidvegvthv inyqspedek tylhrigrtg ragakgtavt lvdwddiprw klinkaldla
      421 fdepeetyst sahlyaqlni pegtkgvlpr aertraglaa eevedlgetg grgrgprkga
      481 vveeerpart rtprqrrrtr ggtpldgpag seaqttgspa aaessegtea agprqprrrr
      541 rtrsgqsgaa apapvaeaap ttavvteaat vvtesaavva eapaepakpr rrrarvarpv
      601 dtesfqtvev aaralaaega aiaaesvavp epaeapakpr rrsrsaakaa vetapavvte
      661 svveaadtvv eapakpkrtr ktaaakaaea avdtaegtve apakpkrtrk taaakaaeaa
      721 adtaegtvea pakpkrtrkt aaakaaeaav dtaaaeatpa kpkrtrksaa akpaadapea
      781 aeakpvrrrt rakaavaeat pes
//
LOCUS       WP_457684654             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457684654
VERSION     WP_457684654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34100
     Region          51..326
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mpepyvpkea mghgdggsaa laigeaesle rrpgaappga gppggvpagk prslwsdawh
       61 dllrnpvfvi salvivflvi iaiwpqliat gnpyradlak aqqgsqpghp fgfdtqgrdv
      121 ytrvvygara sitvgvcatt gaallgsllg glagffggwg dtllsrladi ffgipvilgg
      181 lvflsmvtgt tvwpvvgfiv llgwpqvsri argsvvtakq ndyvqaaral gagngrlllr
      241 hiapnavapv ivvatialgt fialeatlsy lgaglkppti swgidistas tyirsaphml
      301 lwpagalsit vlafillgda vrdaldpklh
//
LOCUS       WP_457684658             143 aa            linear   BCT 27-JAN-2026
DEFINITION  (deoxy)nucleoside triphosphate pyrophosphohydrolase [Streptomyces
            nigrescens].
ACCESSION   WP_457684658
VERSION     WP_457684658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="(deoxy)nucleoside triphosphate
                     pyrophosphohydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15542
     Region          5..124
                     /region_name="NUDIX_MutT_NudA_like"
                     /note="MutT pyrophosphohydrolase; cd03425"
                     /db_xref="CDD:467531"
ORIGIN      
        1 mttvrvvvgg avcergrlla arrsappala grwelpggkv eddetperal erelreelgv
       61 eaaaleripg ewvlrpgyvl qvwtarlvsg vprplqdhde lrwllpgees qvdwldqdrp
      121 avaeamrrla apagatgvtg vrp
//
LOCUS       WP_457684663             520 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457684663
VERSION     WP_457684663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51659
     Region          29..422
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpvtggggee gaaggaaggg ggsaatgalr rtlsfrdllv ygllfiapma pvgifgalqa
       61 tshgavtlvy lvatvamaft afsyaqmvrv apragsvyty arvglgegag fvagwmamld
      121 yllipavayl fsgialhalv psvhpwvwta lavavttlln lsgvrtaara gfavlameiv
      181 vlavfvvsav velvvhgapr gwaepltgeg gfsagavlaa vsvavlsylg fdaiasfaee
      241 agggeggrgp ggpdrvarav lsclvvagvl favqtylaal lmpvsaaela arpaeqgaaf
      301 yatadsavgr wlqdlvavsk avgaafaala gqaaagrllf amardrrlpg amskvdagsg
      361 vprrallgaa lvtlvaavga arrddglaql ssivnvgalt afgllhasvi gwfwirgrrg
      421 rpplgrsgel vgrsgelggr ggglvgrtge lggrtgelgg gppsvlrhav vpllglavvv
      481 avvveasata qlvggvwlva glvvlavqhg graraggmrg
//
LOCUS       WP_457684673             475 aa            linear   BCT 27-JAN-2026
DEFINITION  class II fumarate hydratase [Streptomyces nigrescens].
ACCESSION   WP_457684673
VERSION     WP_457684673.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50494
     Region          19..474
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msengdfsgs gdsdsdgfrt ehdsmgevrv pahakwraqt qravenfpis gqrlerahia
       61 alarikgaaa lvngelgvld keiaeavqea anevaegrwd ehfpidvfqt gsgtssnmnt
      121 neviatlase rlgrqvhpnd hvnasqssnd vfpssihiaa tsavlddlip alehlaesle
      181 rkaeeftevv ksgrthlmda tpvtlgqefg gyaaqvrygv erlraslprl aelplggtav
      241 gtgintppgf staviaevar atglpltear nhfeaqgard aivetsgqlr tvgvgltkia
      301 ndlrwmasgp rtglaeialp dlqpgssimp gkvnpvipea vlmvaaqvtg ndatvaaaga
      361 agnfelnvml pviarnvles vrlianvsrl ladrtvdgit anverareya esspsvvtpl
      421 nkylgyeeaa kvakrslaer ktirevvleg gyverellse aqldealdvl rmtrp
//
LOCUS       WP_457684687             193 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684687
VERSION     WP_457684687.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20426
     Region          2..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprkfdeg qaldaamdaf waagyaatst qdlcdatglg rssiyhtfks khdlferala
       61 rymehksael ftlleselsa rqkirallqr videecaddg dgrgclvvnt cievsahdps
      121 vaasleqdyg vrlaalravi esgqrdgdia pgkdagtlah lviasvgglr vsarsgvgra
      181 aleavadatl stf
//
LOCUS       WP_457684696             342 aa            linear   BCT 27-JAN-2026
DEFINITION  chitinase [Streptomyces nigrescens].
ACCESSION   WP_457684696
VERSION     WP_457684696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Bourne,Y. and Henrissat,B.
  TITLE     Glycoside hydrolases and glycosyltransferases: families and
            functional modules
  JOURNAL   Curr Opin Struct Biol 11 (5), 593-600 (2001)
   PUBMED   11785761
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Fukamizo,T.
  TITLE     Chitinolytic enzymes: catalysis, substrate binding, and their
            application
  JOURNAL   Curr Protein Pept Sci 1 (1), 105-124 (2000)
   PUBMED   12369923
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Aronson,N.N., Blanchard,C.J. and Madura,J.D.
  TITLE     Homology modeling of glycosyl hydrolase family 18 enzymes and
            proteins
  JOURNAL   J Chem Inf Comput Sci 37 (6), 999-1005 (1997)
   PUBMED   9392855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007435
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="chitinase"
                     /EC_number="3.2.1.14"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008061 - chitin binding [Evidence IEA]"
                     /GO_process="GO:0006032 - chitin catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34864
     Region          <10..339
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
ORIGIN      
        1 mtglparlla gltaavlasa givgtgtaqa agtrspapat ssapaaptaa vprhavtgyw
       61 qnfdngatvq klkdvddayd iiavsfadat gqpgavtfrl dpavgygstd efkadikakq
      121 aagksvilsv ggergavsvn daasaknfad svsglmdeyg fngvdidlen glhstymtqa
      181 lksvhdrhgd vvvtmapqti dmqspqneyf ktalgikdfl tavnmqyyns gsmngcdgkv
      241 ysqgtvdflt alaciqlegg ldpsqvgigv pasaraaggg hvapsvvnaa ldcltrgsnc
      301 gsfkpsrtyp glrgamtwst nwdaangnaf asqvgahvhg lp
//
LOCUS       WP_457684698             450 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457684698
VERSION     WP_457684698.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 450)
  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 10133673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..450
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49053
     Region          129..426
                     /region_name="M14_CPT"
                     /note="Peptidase M14 Carboxypeptidase T subfamily;
                     cd03859"
                     /db_xref="CDD:349432"
     Site            order(189,192,249,266..267,324..325,331,375,397)
                     /site_type="active"
                     /db_xref="CDD:349432"
ORIGIN      
        1 mrprirggrt tvlaallslt laapiaaaqa qdapspgstt gaarhaelph qyevtgpatr
       61 aartallatg vsidevhtra vvitatrsqa atvhelgytl rklpdppgfa taaphkprvk
      121 dfpagyanyh tydeatkeid alvakypeil skqvigtshe grnilalkls knvtkdeqep
      181 evlftahqha rehltvemsl yllkeftsky gsdsrvtkml dsreiwiipd lnpdggeydi
      241 asgqfrswrk nrqpnagssg vgtdlnrnwd fkwgccggss sspssetyrg kapasapevq
      301 vvskfvhgrn vggkqqikaa idfhtyselv lwpfgftndd tgpgmtqddh dafatigknm
      361 aatngytpeq ssdlyitdgs iddwlwgdqk ifaytfemyp ssfgsggfyp kdsvipketa
      421 rnreavlqll etadcvyrai gkeeqycsgn
//
LOCUS       WP_457684702             544 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684702
VERSION     WP_457684702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..544
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58236
     Region          1..542
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdtvfrdvrv idgsggpsyr advalsggri aeihresdgg prpgaarvve gqglalspgf
       61 idmhahsdla llrdpgheak aaqgvtlevl gqdglsyapv ddrtlaevra qiagwnggap
      121 gdtsldfswr tvggyldrld hgfdgrgiav naaylvpqgt vrmlavgwdd raatadelar
      181 mrqlvaegle qgavglssgl tytpgmyasd aeltelcrvv arydgyycph hrsygagalq
      241 ayeemvaltr eagcalhlah atmnfgvneg rapellalld raldagadlt ldtypytpgc
      301 ttlvamlpsw aseggpgvim arlrdeataa rirhvmeveg adgchgvpid wdtieisgvs
      361 dpaladhvgk tvarsaaerg eepwqtarrl liedrlgsti lqhvghednv rrimrhrvht
      421 ggsdgilqgd kphpraygtf pqylgryvre lgvlsleecv ahltarpaar lrlpdrglvr
      481 egyradlvlf dpetvaagst fdaprtlptg iphvlidgrf vmedgrrtdv lagravrrta
      541 sgrg
//
LOCUS       WP_457684708             335 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684708
VERSION     WP_457684708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  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 335)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="MDR family NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35347
     Region          5..333
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(50,132,156..158,178..179,183,199,222..223,244..248,
                     250,277..279,322..323,325,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(51,250,280)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(54,58,238,243..246,249,267..268,271..278,281)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 mthrthrevr ltarpqgpvt ddlfeivevp vpepgpgqvl vrntvmavaa vmrtlmdenn
       61 vvpvpafevg eplngpalge vvaapgtdlt pgdlvehrlg wreyalldad gvhrcdpglm
      121 pdpaaylsqg ptawmgivrg aevrpgdtvf vtgaaggvgs lagqvarlrg aarvigstgs
      181 qekadrlike fgydavvirg agpieeqlra aapegidalf dnvggeqlga aiavantgar
      241 lalvgalssq lsedgkphrt eidtlsllar nitlrgvalh ahmdllpewn qrfgeglrdg
      301 tltfphtrlh gieqapralr eltegrhlga vlvel
//
LOCUS       WP_457684744             259 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457684744
VERSION     WP_457684744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28663
     Region          94..246
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mntlhgttss avitrlhdvv rsgeksgavr gctrgtarqr ppfmvaidar ghggnaahgg
       61 enggntggae yreatgerrs paetaeaeaa ftayvqerra slyatayhlt gdryeaedll
      121 qsalfstyra wdrisdkaal ggylrrtmtn lhisawrrrk lneypteelp etagdvdamr
      181 gtelravlwq alvrlpetqr tmlvlryyeg rtdpeiadil nisvgtvkss iwralrrlre
      241 devlsfgrde eesfgelva
//
LOCUS       WP_457684746              70 aa            linear   BCT 27-JAN-2026
DEFINITION  PspC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457684746
VERSION     WP_457684746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Joly,N., Engl,C., Jovanovic,G., Huvet,M., Toni,T., Sheng,X.,
            Stumpf,M.P. and Buck,M.
  TITLE     Managing membrane stress: the phage shock protein (Psp) response,
            from molecular mechanisms to physiology
  JOURNAL   FEMS Microbiol Rev 34 (5), 797-827 (2010)
   PUBMED   20636484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..70
                     /product="PspC domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=7393
     Region          5..64
                     /region_name="PspC"
                     /note="Phage shock protein PspC (stress-responsive
                     transcriptional regulator) [Transcription, Signal
                     transduction mechanisms]; COG1983"
                     /db_xref="CDD:441586"
ORIGIN      
        1 maaalvrpsn nrviagvcag larrfgmtpt tmrvlfvvsc llpgpqflvy lalwiflpse
       61 ekaatgataw
//
LOCUS       WP_457684753             184 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684753
VERSION     WP_457684753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18096427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20187
     Region          18..183
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          <97..163
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mtapeaitie pldgpaaara epafrlvyae vfaeepyeet pksvaatfrr frsqvrkstf
       61 raalartagg epvgiayghp lsaaadwwnr lvtpvpaeir redgqrtfgl mefavrkrwr
      121 qlgvgrrlhe allaganeer vllnalpaae aahaayrswg yrkvgearpw egaalhdvma
      181 lqlg
//
LOCUS       WP_457684764             400 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684764
VERSION     WP_457684764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=45108
     Region          15..390
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 matpqgteea gharytyrlr vsstnrralm sewdrcrwvw nqcvaesraa ygagekcgpa
       61 lldkmltgwr mehewlrega svpqqqiird faksrakalk dvtarlpmrq ragmprfkkk
      121 gladptinyt rrgfrlqdgr lhlargialt vvwsrglpse ptsvriyrds lghwyasfvv
      181 kvkaqplart grcigidwgv ketatttsdd hdlphaehgk kaaerlayyq rmmarrrpgr
      241 gqpaskgyrk vrrqaarvhk kiarrrqdda rkwakrvvvd fdriavenfc pkflgrstma
      301 rkaadaaist tkhelinmar khqralhlvh pahttmdcgr cgartkhalp lsertytcia
      361 cgaesprdkn sarvmlvrag lapsgadrvs ldrslngrva
//
LOCUS       WP_457684765             398 aa            linear   BCT 27-JAN-2026
DEFINITION  S8 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457684765
VERSION     WP_457684765.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40731
     Region          23..351
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrvtrtlrat igaaltgalf lgtggsavad qnrdaqwplt afgaqdiwkk stgkgvtvav
       61 iekafrkthq dltgqflpgk dfpnptneda agaqlkpged lrdhgtsmag liagqghgpg
      121 gsagmkglsp gakilpltav gtvptavrya vehgadvinm sflsdpttpd mcesihyave
      181 kgvvvvagvg ndgtseknlp sacpgaigvg avdeygnawe nsnynsavdl lapgvdvpvl
      241 ggksdshygt tdgtsvatay vsatvallre kypnltpgqi anrlvktagl spsvkkkhlk
      301 lpddhygygy ivpeaalned ipagpaqgpl pmpkgkaskt pvtagvkngp npnppmsmge
      361 kltlfggigl gvlvvigiii avvvavrrrn npgpqawg
//
LOCUS       WP_457684769             437 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457684769
VERSION     WP_457684769.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 437)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46069
     Region          53..435
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(82,89,117..118,125,129,136,267..268,271,275..276,
                     279,312,317..318,321..322,324,347,376..378,381..382,
                     384..386,390)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(89,111,113,116,118..119,205..206,215,266..267,
                     270..271,275,318,321..323,425)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtdgqpisdd drrtapaplp ppgatcpvrp gggsphrlap ggagraaada llreagavvp
       61 vllpgevpav avthhavlre vlahpevakn achfaalhdg tvppgwpltt fatvdgmtta
      121 dgadhrrlrg lvtkvftprr vaalrprvve ltaglldglp gaaaadgtvd lrrhfayplp
      181 msvicellgv daalrdrlhe lsnlivgttg tadevqaanr eitavlgeva earradpgnd
      241 ltsalitaqe edggrlsare lvgtlllmii aghettlnli tnavralctg reqlelvrag
      301 ratwddvvee tlrhdspvah fpfrypvrdl elggtvvprg tpmlasysaa grdpeaygrd
      361 adrfdvtrrp atrhlsfghg phyclgapla rleatvalea lftrypalgl avpdaelpph
      421 qsfignsthv lpvrltg
//
LOCUS       WP_457684801             310 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684801
VERSION     WP_457684801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33113
     Region          100..202
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mqalpflsap lliarlvatp lrcvrllptr asslplrstv vdlavlaghl llyptgisqe
       61 rplprpaphp aagppegfta peapqpapga ptmlptegra hppvlllhgf idnrsvflll
      121 rrslhrhgwr hvealnyspl tcdlrkaael lsrhveevca rtghrrvdlv ghslggliar
      181 yyvqrlggda rvrtvvtlgt phsgtriapl msahplvrqm rpdseviael srpapncrtq
      241 fvafwseedq vmvpattari shpdliahnv hvagvghlal pvngavaagi realtsaeta
      301 egaadaisva
//
LOCUS       WP_457684810             681 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457684810
VERSION     WP_457684810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..681
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69487
     Region          14..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,72,77,82..85,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,80,96..99,103,105,142,144,
                     146..147,149,160..161,164,181..184)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,80,96..99,103,144,146..147,
                     149,160..161)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,103,105,142,144,146,164,181..184)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(160..168,177..184)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgifggegrl iggryrlgir lgrggmgtvw ratdevlgrq vavkelhlde gtaepearvq
       61 reramreart vaqikhpnvi vvhdvveqdg rpwivmelve gpsladrlqs ggpvapreaa
      121 rigiallgal raahtrgvlh rdikpanvlm esgsgrvvlt dfgiaqvpgv ttltdaggfv
      181 gspeytaper magrgtgpea dlwslgvllc aalsgaspfh rdslggvlha vvydeielpe
      241 sarplhavvh gllereperr lgvaeterll rgylqsgrap ergpgghlgh gagrghggld
      301 ahgvhgghgg hgghgghggh gaadggvgdg gaaglaaeav agaggpggpg gpggpggpfl
      361 ggpdvprypg pdvhaplydv pdgglpgehp psghppsega pvagtpppgp atpartptgg
      421 gagrpggrtg grtpgmpird alddralaaa arphtgrart allvalaavv iggvgagiav
      481 llmnqggtdg gtgtggrpsr sqqasdtgsp qsggsgsaep tvtappasgg tgkipagyrl
      541 vrdpegfala vpegftrsye ndrvyyysqg krfrigvqlq qqvpegplga mrtahakgpa
      601 dyrgyrqgqv tetthnglqa glwefvwdgs aqdggsryty dlswdeggrm idvwisspva
      661 srteakrhfd taldafrlsg a
//
LOCUS       WP_457684829             387 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684829
VERSION     WP_457684829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41157
     Region          8..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtptiesee hralrkavaa lgnrygreyf arvvaegaht delwaeaakl gylgvnlpee
       61 hggggggive lsivleelga agcpllmlvv spaicgtvla rfgteeqkrt wlpgladgsr
      121 kmafgitepd agsnshritt tarkdggdwv lngrkvfisg vdiadatliv grtedartgr
      181 lkpclfivpr dtpgfgrspi amelsapekq feltldevrl paealvgded agllqlfagl
      241 nperimtaaf algmgryalg ravdyartrq vwkepigthq slahplaqah ielelarlmm
      301 qkaahlydag ddmgageaan makyaaaeaa vhavdqavht lggngltqey glasmitaar
      361 variapvsre milnfvshqs lglpksy
//
LOCUS       WP_457684831             532 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces nigrescens].
ACCESSION   WP_457684831
VERSION     WP_457684831.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..532
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56332
     Region          21..530
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvlgtgldp sgaeyaerrt amlaklaeie aehakategg gekyvarhrk rgkllareri
       61 ellvdpdtpf lelsplaawg sdyqvgaslv tgigtvagve cvitandptv rggasnpwtl
      121 kkslraneia fanrlpvisl vesggadlps qkeifipgga lfrgltrlsa agiptvavvf
      181 gnstaggayv pgmsdhvimv kerakvflgg pplvkmatge esddeslgga emhartsgla
      241 dhfavdepda lrqarrvvar lnrhkaqpdp gpaappkyde eellgivpgd lkapfdprev
      301 iarivdgsdf defkplygps lttgwaelhg ypvgvlanaq gvlfsaesqk aaqfiqlanq
      361 rdipllflhn ttgymvgkey eqggiikhga mminavsnsk vphlsvlmga sygaghygmc
      421 grafdprflf awpsaksavm gpqqlagvls ivarasaaak gqpyddeada glramveqqi
      481 eseslpmfls grlyddgvid prdtrtvlgl clsalhnapv egarggfgvf rm
//
LOCUS       WP_457684854             240 aa            linear   BCT 27-JAN-2026
DEFINITION  copper homeostasis protein CutC [Streptomyces nigrescens].
ACCESSION   WP_457684854
VERSION     WP_457684854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..240
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24123
     Region          4..233
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mskrallevi algpqdavaa eaggadrlel vtdmaadglt ppratfaavr aavglplrvm
       61 lraadgfaag dvaalceeaa glraegaeef vlgfltpdgr pdlaavaalt evidgcpwtf
      121 hraidraadr dalrkelaga agaagldtyl tagsaqgvdg glptllaeqa rtaagepgya
      181 prilvggglg lghlpalraa gldafhigga arpagwsapv eaaavrewre aldlpvaqrv
//
LOCUS       WP_457684837             283 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684837
VERSION     WP_457684837.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32133
     Region          7..>65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          109..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mstdyqqara algvrlrelr isrpggrltg pqlaqrlgwt hskiykleng kqtaspedlr
       61 awvdateqpe afaelyarlq gfesqirswr rqlasghrpv qenwnteiar tkvihgwqes
      121 iiegmlqtad yarhiftrya elqnsprdtd aavrarlrrq ellyqpgrkf riimweaalh
      181 arlcppsala aqldrltgmi gldtvelgiv pfsaslkipt angfyvldnr lavtedwhae
      241 lwledadsia lylnvwntlr esavfgteaq nvinrarrsl csp
//
LOCUS       WP_457684866             242 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684866
VERSION     WP_457684866.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /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=26201
     Region          11..237
                     /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 mtgaphpspt qavilaggqg srlrpytddr pkpmveipgt gtpiighqln wlaeegvtda
       61 viscghlagv lqdwldraql plrvttvvet eplgrggglk yaagslprpd epwyatngdi
      121 wtrfplrdma afhheraaea tlalarphip wgavetdafg hvldfiespp spylinagvy
      181 vfsaaftell pdcgdhertt fprlarerrl agfplpqgay wraidtakdl teaakelsaq
      241 gr
//
LOCUS       WP_457684870             457 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684870
VERSION     WP_457684870.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..457
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46611
     Region          30..400
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(39..40,43..44,46,79,129..130,132..134,137,157,
                     160..161,164,244,247..248,251..253,256,283,287,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 msastsgptr raglrqavve svsglprqfw wlwtstlinr lgafvatfla lyltvergys
       61 asyaglvaal yglggvissv gagvmadrlg rrptmliaql staasvallg fmtdpvaiaa
      121 vaglvglatn asrpavqamm adivapedrv rafslnywai nlgfaissta agliaehgyl
      181 tlflgeaalv lacalvvfwk lpesrptpgt pggpddadgg papapvsmlt vlrdgrfmtv
      241 vglnlllall fqqayvsmpv smgqdgfsst dfgmviavng vlvvllqipv trfiehrspa
      301 mlligsalla gygfgltala gsvamyavav tvwtlgeiin sptqmglvvr lsplhgrgry
      361 qgmyslswsv asltapllgg lvidhygada lwagcaaigt laalgyglll rglpaqtgag
      421 agavagsqav taagqsatak gqaasataaq epsepva
//
LOCUS       WP_457684878             348 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457684878
VERSION     WP_457684878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36722
     Region          <123..242
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mtttahlgan gtgptagdpg garepgvrgp lgglvwlvrr qhrlffglll aaaaggavwc
       61 avlrgraaaf idahhidgcs mislvarcdg tqdavvefrn tygpalqlae agllllpvli
      121 glflgaplia releagthkl vltqsvgplr wlaaktalpa lvvlavttal savfawlwqv
      181 vgdevsgsyw ystldfaalg pvpvayslla lavgvlagll lrrtvltmgv tlgamvllqv
      241 alkqlrpylm psgstefgpk esaqlpdnaw lvgqgyytrs gdhlpmevcd sagdqesclr
      301 shdvvgqymd hhpashhwpl awiesgivla ltavltglaf rvmrhrhg
//
LOCUS       WP_457684882             207 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457684882
VERSION     WP_457684882.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23465
     Region          19..191
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 matssaptnp plpytpaypi rterldlrpv tdddfaaiha yqhlpevcry lywgphdeaa
       61 srasvadkat rttlrasgdf lqlavvvret gtlvgdvtfv wssrehrqgg igyvfhpaht
      121 ghgyateasr allklgfeel qlhriqaeld grntasarll erlgmrregh lrenefldge
      181 wsdeviyaml arewrdrree rpegrre
//
LOCUS       WP_457684887             308 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684887
VERSION     WP_457684887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=34016
     Region          39..263
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mlprvdtdde wdaivpdeav mrpgaaalct rlgirpdplt rypagsqpvy avgqrfvlkl
       61 fpaaaaddgv tearvlthlq gqlplptpyv hdageyengw ryvlmsrlrg tdlavtwprv
      121 pradqdriat eagetlaalh aldpspltgf lgpgdwgafl drqrgtavar qrdhglpepw
      181 leqipaflas vapsaagpgv llhtefmrqh ltvdehddwr ltglldfepa migqraydfv
      241 avglfvsrgd prllsrifra ygetftptel lthtllhlys nlprylrelp appeptlesl
      301 aetwfgte
//
LOCUS       WP_457684886             602 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            nigrescens].
ACCESSION   WP_457684886
VERSION     WP_457684886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  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 602)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..602
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62843
     Region          46..582
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mpatpqrrrt vrrltigaav laaaglaaga lpagadtgha artgrtvdvq llsfndfhgn
       61 leppqgssgt veevqpdgsk ksvpaggaey laqslrtare ghpysvtaaa gdlvgaspll
      121 sglfhdeptv eamnklgldv tsvgnhefde grkeltrlqk ggchpkdgcy edgkkfrgag
      181 fpyltanvtd dktgkpllkp ytvwkhkgvk igfigvtleg tpdivnaegi kglkfhdeve
      241 tinkyakvln rqgvksvval ihegglpast synyncdspg pgdgisgpit eiakhvtprv
      301 dalvtghthq ayactipdps gkprtvtsaa sygklytdtt ltydrrthdi vrtavkapga
      361 anhvvdrtqp kaadmtslia rwnklaapva grpvghisad iagrganape splgdvisda
      421 qleatkadgk ggaqlalmnp ggvrsdlafk asgsegdgvv tygeaftvqp ftnmmnvvdl
      481 tgaqlltalq qqvsgpnaas pkilqvsqgl tytldmtksg adrivkdsvk lngaaldpak
      541 tyrvamnefl agggdgfpaf kdgknkyvgp sdldaftayl tahssadkpl tppkadritv
      601 vk
//
LOCUS       WP_457684890             352 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces nigrescens].
ACCESSION   WP_457684890
VERSION     WP_457684890.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34915
     Region          138..>348
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtqsyrrsgd empqdrpyay gddhgqgygq gygheayggt pgagfseqav ppppyaperp
       61 rrarrpvali aavalasgli gggsaaliag atqpsaqnss stplvnagkt sgsgvsgvak
      121 avspaiveir aqsakgestg sgvvvasdge ivtnnhvlag adtvtvtfhd gsrktaevvg
      181 tdpgkdlalv kvrgaknlta aslgdsskit vgdqvvaigs pegltgsvts givsaldrdv
      241 tvpkeegqgq qggpggrggw pfefggnqyn gdtgssktsy kaiqtdasln pgnsggalin
      301 mqgqiigins amyspssess ssagsvglgf aipintvkdd ldalrgggns gv
//
LOCUS       WP_457684894             371 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces nigrescens].
ACCESSION   WP_457684894
VERSION     WP_457684894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39723
     Region          1..325
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(24..25,28,80,96,98,127,159,285,288,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(214,219,276,285..287,290,312,316)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mvtflprlpg rladvpsfdr aiggaesnva ctlartghtt rwisrvgtdg fgdhlltaia
       61 ecgvdvahvr rdplrptgvy frtagdratg thevayyrag saasamtadg ldaaalragr
      121 ilhlsgitaa lsadclgllr eltarrpgrp llsfdvnyrp glwrdtarar vlldlargad
      181 lvfvgddear dawglhgpra irralpepql lvvkqgraga tvfrrtggpd frrtgetdlr
      241 rtgepdlrrt getdlrrtge ldgrrddata tfvpalnvdl vaatgagdaf aagflsatlr
      301 glpdrdrlrh ghlwaaaalt vpgdlatpps rpyadrlaal ddtawerlhl gpgwtdadvs
      361 grradeevpt q
//
LOCUS       WP_457684896             278 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684896
VERSION     WP_457684896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31836
     Region          10..89
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          118..260
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mplqpdqrrq lgaflrsrra rltpaevglp qtarrrtpgl rreelallag isatwytyle
       61 qgreiraseq vltalaealr ldrherahll qlaghatade peerepltpe aaavplllqp
      121 npayiiggny dvlshnraae alfprlidnd tkqpanflrw vflepaardv vvdwepeara
      181 llarlrtqsg rhptdprytr lidelnehsp eartwwhqye vqarhsghkr lrhpqrgpve
      241 yaytafhlae qreqtlvvyv erehghghgr ergrgqrg
//
LOCUS       WP_457684899             443 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684899
VERSION     WP_457684899.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  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 443)
  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..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46133
     Region          37..408
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mvwgtagrav adgrgrpvgq gtaeqgavgq gaveqgavda evarihreli vlrrdlhrhp
       61 empgqeqrta gvvarelraa gltvatgvgg ghgvigilhg arrgrtvayr admdavppkd
      121 ivgggpaaah vcghdihttv algvarvlar lrrqlsgtvv flfqpaeetl sgaralidag
      181 vlertgvaei halhcgpfpv gtfavtpgyg lpgqdkaevt lsgpgapdaa rrlaaeigal
      241 atvappqtpa dierlladal tpdgplarfv avraraqeag vsvayrcwpq erygevradi
      301 rrlamswaga gvrfpaepfp amvcperdar mlahhlrram grgavtelha afppfsgedf
      361 alyldrvpgt ftflgvraph apitagyphy pdfapderav gvgvramagw iaerahrarg
      421 lpggsggsgr ggpttptgwr tsg
//
LOCUS       WP_457684907             393 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684907
VERSION     WP_457684907.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41257
     Region          1..390
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mdrivlvgas aagltaadal rregftgtlt lvgdelwapy drpplskqvl agswepertv
       61 lrqeadlqrl kldlrlgcra tglepaartv tladgdrlry dglllatglr prrlpfghdl
      121 agvhvlrtld daltlraqlg agprvvviga gflgseiaat arglgldvsl vdteptplar
      181 qvgtfvgglv adlhrdhgvr lhmghgvtev tgargrvtav llddgtrlpa dvvvvaigsv
      241 pavdwlagsg lplgdgvrcd shcraapgvy aagdvanwpd patggrvrle qrmnateqar
      301 aavrnllagp gdavpytpvp fgwtdqydak iqfhgscpad aevecvdgdp garsfvalyr
      361 lhgrvagalg wnrvralrey rghigtagpv kag
//
LOCUS       WP_457684913             219 aa            linear   BCT 27-JAN-2026
DEFINITION  LutC/YkgG family protein [Streptomyces nigrescens].
ACCESSION   WP_457684913
VERSION     WP_457684913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23173
     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 mssrdvvlgr vrraladvpr gegpddppvv rdyhrvhgsr taaqdvdlla enladyralv
       61 hrstagelps lirrllaerg artvlvppdl daswtagagv tlvgdrasst preldavdsv
      121 ltgcavaiae tgtlvldggp dqgrrritlv pdhhlcvvrv pdqvvgsvpe alprlaperp
      181 ltwisgpsat sdieldrveg vhgprtlevi llassraad
//
LOCUS       WP_457684916             478 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684916
VERSION     WP_457684916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   McLeish,M.J., Kneen,M.M., Gopalakrishna,K.N., Koo,C.W.,
            Babbitt,P.C., Gerlt,J.A. and Kenyon,G.L.
  TITLE     Identification and characterization of a mandelamide hydrolase and
            an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas
            putida ATCC 12633
  JOURNAL   J Bacteriol 185 (8), 2451-2456 (2003)
   PUBMED   12670968
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Vasiliou,V., Pappa,A. and Petersen,D.R.
  TITLE     Role of aldehyde dehydrogenases in endogenous and xenobiotic
            metabolism
  JOURNAL   Chem Biol Interact 129 (1-2), 1-19 (2000)
   PUBMED   11154732
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..478
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_process="GO:0006081 - aldehyde metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51937
     Region          28..451
                     /region_name="ALDH_F3-13-14_CALDH-like"
                     /note="ALDH subfamily: Coniferyl aldehyde dehydrogenase,
                     ALDH families 3, 13, and 14, and other related proteins;
                     cd07087"
                     /db_xref="CDD:143406"
     Site            order(134..136,162,191,209,308,310..311,314,355,357)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143406"
     Site            order(136,231,262,265)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143406"
ORIGIN      
        1 mrnqlfaggi qdtadvheaa eandaartvg rlretfatgr trslawrrrq lnalrallte
       61 qtpaltealr rdlgkspvet ltsevrlvtn eidhtlrhlh rwlrpqrvpv paallparar
      121 tvreplgvvl iispwnypvq lslaplvgal aagncavlkp selapatsae larllpryld
      181 qdavtvvegg vrqttqlleq rfdhlfytgn gtvgrivmta aarhltpvtl elggkcpvli
      241 cpgddlataa rriawgkfln agqsctapdh vlaigdtaga lerhlaeavr amygpdpars
      301 pdygriindr hfdrltallg hgrvvtgggh draaryiapt vladvepdap vmaeeifgpl
      361 lpilrmpdld taltfinahd kplalyaftt drrtrrrllt etssgavgfg lpnahltvpg
      421 lpfggvgesg lgryhgrhsv etfsnakavl dkplfpdtvr avyppfttak erlirrfm
//
LOCUS       WP_457684918             392 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457684918
VERSION     WP_457684918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..392
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=41890
     Region          184..390
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(191,230,268,371,374)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(191,371,374)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(191,230,268)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mndnttslfw nagwaaaiqr psegfhknwa qegfadqtvr qivrvtgsgt sariklshry
       61 gtaplelaga tialtdkgaa eragsvrplt fggarsvrvp ageeiysdaa evhvapfesl
      121 tvslyfarpt gpasfhaqay attyraegdq laaadpavfg ettvswyyla aveladggpa
      181 rddtvvvfgd sltdgfasti dgnrrysdal aerladqgtp rpvlnqgigg nlllndsawy
      241 gdragdrfrr dvldqpgvrs vvvlvglndi gfseielpty rpnpdqspae liagyrelir
      301 qaraagvrit gatimpfkga eyhtptaeak rrevnawirt sgefdavadf ataladpsdp
      361 dallpaydsg dhkhpndegy ramaaaidlt tp
//
LOCUS       WP_457684923             605 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684923
VERSION     WP_457684923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 605)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 605)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 605)
  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 605)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65435
     Region          21..591
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mrsdepqwtp ppkdpekpvp lrrilalfrp yrarlavvgl lvgasslvsv aspfllreil
       61 dvaipgrrtg lltllalgmi vtavvtsvfg vlqtllsttv gqrvmhdlrt avyaklqrmp
      121 lafftrtrtg evqsriandi ggmqatvtst atslvsnlts vlatvcamla ldwrltvvsl
      181 lllplfvwis rrvgnerkki ttqrqkqmaa msamvtesls vsgillgrtm gradsltrtf
      241 adeserlvdl evranmagrw rmatigivma ampaliywaa glvlqlggpv fslgtlvafv
      301 slqqgllrpt vsllstgvqi qtslalfqri feyldltvai tepaepvria aprgevrfen
      361 vtfrydpeaa ptldgieltv paggslavvg etgsgkstls ylvprlydvt ggrvtldgtd
      421 vrdldfdtla rsvgvvsqet ylfhasvadn lrfakpdatd aeieraaraa qihdhiaalp
      481 dgydtlvger gyrfsggekq rlalartilr dppvlvldea tsaldtrteh avqqaidels
      541 egrttltiah rlstvrdadq ivvldagria ecgthdella aegryaalvr rdayltpvgd
      601 qvmap
//
LOCUS       WP_457684932             142 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684932
VERSION     WP_457684932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15633
     Region          12..134
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mahkmtkdew qrflsegtrt gklatvrddg sphvapvwfl mdgdelvfnt gqetvkgrnl
       61 ardgrvalci dddrppfsfv vvhgsaeisn eladvrhwat riaarymgee raeeygarng
      121 vpgelvvrvr idkvialadv ag
//
LOCUS       WP_457684928             593 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457684928
VERSION     WP_457684928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 593)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 593)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 593)
  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 593)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..593
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63474
     Region          24..593
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 miglappdhd pdapqtlttl pvgspatvrs yvgglirrhr raftvliaan taaviasmag
       61 pyllggvveq lsagdrylql ertvavfaia laaqtlfvrm vrlrgamlge rmladlredf
      121 lvrsvalppg vleragtgdl lsrittdidr lssamreavp qltigvvwva lliggltvta
      181 pplalcvvia lpllivgcrw yfkrapsayr seaagyaavs avltesvdag rtveahrlga
      241 rrialserri rewtqwerft lflrsvlfpv vemthvlllg svlllggafv lqgwmspgql
      301 ttgallaqmm ieplgmilrw ydelqvaqvs iarlvgvrev apeatdtdrr pdgrdvhadg
      361 vsfgyragvd vlrevslrvr pgtrlalvgp sgagkstlgr llagiygprv gsvtlggael
      421 sampaerire hvalvnqehh vfvgslrdnl llartaaada elwaalgavd addwaralhk
      481 gldtevgsgg htltpaqaqq ialarlvlad phtlvldeat slldpraarh lerslgrvld
      541 grtvvaiahr lhtahdadvi avvengrite lgshdelvaa dgayaalwrs whg
//
LOCUS       WP_457684934             298 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces nigrescens].
ACCESSION   WP_457684934
VERSION     WP_457684934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10561995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34353
     Region          42..226
                     /region_name="MPAB_Lcp_cat"
                     /note="ER-bound oxygenase mpaB/B'/Rubber oxygenase,
                     catalytic domain; pfam09995"
                     /db_xref="CDD:462938"
ORIGIN      
        1 mrrydwlrei rrldperdfl riyriiathe fpwdftrale lalyrtyavp sigrllaeta
       61 eltdrtqkry ddtallldav vehgfdsddg rtairrinqm hrsydisned mryvlctfvv
      121 vpkrwldeyg wrrltaheqh avatyyrtlg rhmgitelpq tyedfeqcld ayeeahfgwd
      181 egarrvsdat ldlmagwygp lapvvrgasm allddsllda fryerpkpav qkavrtalkl
      241 rakavrllpp rrtphyarqn peikgypngf rvaelgtlpa srrtgscpvp hgegpaas
//
LOCUS       WP_457684937             996 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457684937
VERSION     WP_457684937.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..996
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=104962
     Region          253..971
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mtslpavtpa qlsalaqcaa vflpsdppra griafwrpdg epvgdaslgv alpdddggvs
       61 lcevpalvlt vadavpvltr aragrdthpa aafwgaasvl alqlaargri lpgvspagyd
      121 awrlgpldpe dlarlrdlaa amppyahaap lpdtdplqlp dperhvrafl davadglprs
      181 pgaalvtgap afavtapqhi peqrawaadv aaghdagvri slrvevhgae aeepmafdgr
      241 ggeqrgevda agsplrgdaa gvrspitfqa vlqlhsltdp tlvadaaevw agtstagqaf
      301 gararmdtll tlrraadawa pltpllsaav pdaldladee iaellgpaag alaaagvqvh
      361 wpkeltrtls aravvgppea gggdvsegrg aglpsllsad allsfswrfa vgdqevdrae
      421 ldrlaeagrp lvrlhgqwvl idpaavraar drqerkvtpl dalgaaltgs vedgdggrve
      481 vaasgwlarl rdrladpegg dttpvrqpaa ltatlrdyql rglgwlhrmt slglgaclad
      541 dmglgktitl islhlhrqtt pesvgptlvv cptslmgnwq reiekfapgt pvrrfhagrr
      601 slaeladgef vlttygtmrv dagklaevgw glvvadeaqh iknpfsatar alrtlpakar
      661 valtgtpven nlselwaild wttpgllgpl grfrthyaqa ieggaaaspe agaaaerlar
      721 lvrpfllrrr ksdpgiapel ppktetdrav altkeqtgly eavvreglae iagtdgfarr
      781 glvvklltsl kqicnhpaqy lkesgpaedg raagavriag rsgkvellde lldsilaega
      841 svlvftqyvq marlleghma argvptqflh ggtpvarree mvrrfqdgaa pvfllslkaa
      901 gtglnltraa hvvhfdrwwn paveaqatdr ayrigqtqpv qvhriitegt iedriadmla
      961 rkqqladavl gsgeaaltel tdaeladlva lrgner
//
LOCUS       WP_457684939             436 aa            linear   BCT 27-JAN-2026
DEFINITION  SWIM zinc finger family protein [Streptomyces nigrescens].
ACCESSION   WP_457684939
VERSION     WP_457684939.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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 10008453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..436
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45158
     Region          31..215
                     /region_name="COG4279"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]"
                     /db_xref="CDD:443420"
ORIGIN      
        1 mntpgdegpm yldegasaaa ertfealpaa rgrafaqsww gqawlkaled taldgaqvkl
       61 grrharagav gavsvrpgri tavvqdpdht rhrsdvllqq lsaadwdrfl dmvadraghi
      121 aalldrdmpp vlvedaaaag iellpgigdl epecscgawd hcahstalcy qlarlldqdp
      181 fvlllmrgrg erelldevqa rsasraelpa ggaaaepsga gvpaaeayaa rdilpplpaa
      241 pppvaapgap pvlgggtppa pgvevaalef ligdaaaraq rllaealstg hpdsppppvp
      301 apgqdavrla aagpgaaisa rlaagsgrda rglasavraw elggaaglav leeewtpepe
      361 alaratgrla aawededrpr lrvtrnrwtv vggaaqlryg rdgrwwpyrr eggqwvpagp
      421 atddpagala gvsaee
//
LOCUS       WP_457684945             321 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces nigrescens].
ACCESSION   WP_457684945
VERSION     WP_457684945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34542
     Region          1..320
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mftdlpldal rtycpprpep agfeafwrrt lvearthdld arfteidagl allrtydvtf
       61 agfgghpirg wfllpraang plpcvvqylg ygggrllphd wllwpsagya tlvmdtrgqs
      121 gpnrpgdtpd pvasgnpgvp gkltqglldp ygyyyrrlft davraveaar ghhavhtdri
      181 vvaghsqgga valamtglvp glagalidap flthirrave itdvgpygel tryfagardr
      241 idtalltldh fdglnfaara tapalfgtal rdevappstg faafhhyage kelkvwrfna
      301 heggggeqra aevaflrglf g
//
LOCUS       WP_457684948             393 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457684948
VERSION     WP_457684948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39678
     Region          5..391
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mtvaayrnli lattgcavtf wawnllppls htfrtglslt gaetaalvaa pllvgslggv
       61 pvgaltdrfg arvmfplvsg ltivpvllli parqsfamll avgfllglgg ttfaigvplv
      121 nawfpprrrg lalgilgtgt agialsghlt prihhydenl pylvvatala lfaflgalmi
      181 sdhpdqhlpr tsaaarpsra grlrgtwepa alyaiafggi vaagvylpvy lrtwyhlgvt
      241 eagtgaagcv lvaavfrplg gwcadrvhpa vvtawslgaa alcaiiqafd palnpmgavd
      301 llvmaaglga aagavvalva rvtpqerigg aagivgaagg lggflpalvl gavhrgkgty
      361 slgflllsdl alaggvyala rmrtagaapa ggs
//
LOCUS       WP_457684961             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684961
VERSION     WP_457684961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31146
     Region          8..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          108..273
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdtstagelg dflrsrrari qpeevglpgh grrrvpglrr eevaqlagvs vdyyirleqg
       61 rspsasdavl daigrvlrld dteqqylrtv arpaarrtst agpadrkvrp glrllldame
      121 kvpafvlgrr mdvlawnalg davvgfsqmp peernmprqv flnpqarely pdwpavaaet
      181 vaylrldags hprdkqlatl vgelslgsed frrlwadhqv kektygakrm rhpvageltm
      241 pyetltvsge pdqmlvvytp epgsrtadrl allaswtasp av
//
LOCUS       WP_457684963             174 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457684963
VERSION     WP_457684963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19192
     Region          32..165
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrrrgpkwrt gaygerekhv teaaesavgp dtavpfavgi tvrgyetdtq ghlnqsvylq
       61 yaeharwsll qasgirqstm vdrrvgpvtv ettirylrel ragdevevsc afvwdegktf
      121 rieqtvrktd gtvaaevsav cglldlterk llkdpraafr dladkpsllg ltdg
//
LOCUS       WP_457684970             332 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH:quinone oxidoreductase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457684970
VERSION     WP_457684970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34046
     Region          1..324
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(41..42,124,128,149,152..154,173..174,178,193,217,
                     239..240,242..243,264..266,316,318,320)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkawrvhang epravmrlee vpdpqpgpgq lllrvraani nfpdallcrg qyqvrpplpf
       61 tpgveicgev lavgegaage tgarvlaqpp lpdggfaarv vvdaatvrpa pdalddaeaa
      121 alhigyqtgw fglhrrarlq agetllvhaa aggvgsaavq lgkaagatvi gvvggadkar
      181 varelgcdvv ldrrtddlva avkeatggrg advvydpvgg eayaksvkci afegrivvvg
      241 faggaiptpa lnhalvknya ilglhwglyn tkdpaavdac heeltklaaq gvikpliggr
      301 vplaeaadav qrvadgtsvg rlvvvptaee ar
//
LOCUS       WP_457684975             224 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457684975
VERSION     WP_457684975.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24119
     Region          2..87
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mprrsydqyc avaraldavg drwtllivre llggprrytd lhadlpgvst dmlasrlkdm
       61 erdglvtrrr lappgaafvy eltargrall paltaladwg apalderrpt dairahwfav
      121 plmarlaghf tdgtdvidia ldegefhvvl ggggpescap dggagyadgp aerpdirlrm
      181 dtatcadiay drlslaqgie sgriavtlpe gsgerqrrkr ttta
//
LOCUS       WP_457684993             794 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457684993
VERSION     WP_457684993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..794
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86322
     Region          10..783
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mpwlsrtrlr tagavlaaal igsalavpaa qaeppggplt glvnpfigsq ndgntypgaa
       61 vpfgmvqlsp dtghfagysy dderirgfsa vhlsgvgcgl ggdlpvlptt gditetdyak
      121 yasgyrhdde sarpgyyrvg ltsyggitae ltatartgkq rytfpatdka nvllnagqsl
      181 hktvstrvev ldsrtirtai tgrgfcqdtq pytvhtitrf drpftsygtw dgdkvtagsk
      241 gstaggrhga yarfdtrsdr tveattalsy vdaagaarnl raeggssfdr tkaaadaawe
      301 rrlglvkaqg gdrtlrrtfy sslyrsflap nigsdvdgry tgwdrkthra kgftyyqnws
      361 lwdtyrtqaq llallapges rdmalsvlri dkesgwlpkw gygtvetnim tgdpvtpflt
      421 nayqqgllrg heeeayaalk knadgvppdg spavgreana pylkdgfapy ikgrphpkpg
      481 dsdfdhgasa tleyalsdam laqmardlgh gkdadryaar aqnyrkifeg stgffrarda
      541 qgaftgpadp aksegfhegt swqyqwlvpq dlpgmlrlig grdkaderld sffayrklle
      601 dpektarevw vngpydyyna dkynpqnepd liapytylst grpwkttdvv haaltlftda
      661 ptgmtgnddl gtmsawmvls sigvfpvqpg tdswglstpv fdrvdltldr ryypsghftv
      721 tapgtsaahr yvrsvrldga dhdrtyltte dlrsgrelaf tvgtepsrwg tgehaapppv
      781 gtgsaaqqqs drqr
//
LOCUS       WP_457684992             316 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457684992
VERSION     WP_457684992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33362
     Region          3..295
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mtlnlpqlra flavvdaggf saaaaelgms qsavshavas lereltapll iratpvrttv
       61 lgakvlphar malsavrsve qlaadaggtm tgtvrlastp tvcqglvpgl lrhwredqpr
      121 itvrvfegds aevaawledg tadaavlidp ppatagkypw sgpgielatd eyrallprdh
      181 pladeprvdi rdleddpfli spngcearvr tlhslaglrf spthrvrdla tlismvqagl
      241 gvtvlsevsr slipsdlvll plqpqtsrrl vltgpqarpw hpalrtlaes aaghlvrsvs
      301 rpaapaegdp ppsgsr
//
LOCUS       WP_457684997             443 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457684997
VERSION     WP_457684997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46036
     Region          23..433
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtarpiavvg asaaglaaae alrrggwrgp ltligdephl pydrpplskq llhgawepdr
       61 lllrteeqla plgldlrlgt ratgldvatr tltldgdepl rcagviiatg vgartlpgad
      121 riagvhtlrt ldealalrgr lahggtpglr lvivgngvlg ceaaavarel ghdvtlvgie
      181 ptpmaaavgt evgellaeeh rargvrlltg avdgfetapa dpdgsdpqit avrlasggpp
      241 gsgaaggssr lpadlvllai gsrpavewla dpaldttdgl rcdeycaaap giyaagdvar
      301 wdhpvhgrpl rfehrmnate qgmaaarnll aeltatadat gvaedapape rrpfapvpyf
      361 wsdqydlklq aygltagadr veatvldrae rrvlalygrd ghavgvlaag lpprriralr
      421 aviatplpwe earerigaat agd
//
LOCUS       WP_457684999             393 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Streptomyces nigrescens].
ACCESSION   WP_457684999
VERSION     WP_457684999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=41460
     Region          51..355
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 msaytryaaa allaalavgc tsphpvprpa prptpeptpr ahagapvted agrqsftlva
       61 agsvlpsdpe vlatarrdap hdgydyrpil kgvrpvisaa dlalchldap lgplggpftg
      121 hpvlqappqi atalkatgyd scatashhal drgvpgvqrt lealdtvglr htgsardaae
      181 garpallrap ggarvaqlay tygtgggrrp ayapwtvnll dekriikdar aarrdgadvv
      241 vvspswgtey rtapdarqir laraltaset agrpdidliv gtrahtpqpy ekvngtwvvy
      301 glgdqlsgvt kkprgnwgti arfrfapphr agqrwrvtta eylpqlveqg krvrvrnlat
      361 sgrhdrirts vgtsvgtvvl srgaaadglt rgr
//
LOCUS       WP_457685007             702 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-galactosidase [Streptomyces nigrescens].
ACCESSION   WP_457685007
VERSION     WP_457685007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16044983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..702
                     /product="alpha-galactosidase"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76001
     Region          22..256
                     /region_name="Glyco_hydro_36N"
                     /note="Glycosyl hydrolase family 36 N-terminal domain;
                     pfam16875"
                     /db_xref="CDD:465291"
     Region          260..592
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(304,335,379,445,449,483,502,505)
                     /site_type="active"
                     /db_xref="CDD:269892"
     Region          609..697
                     /region_name="Glyco_hydro_36C"
                     /note="Glycosyl hydrolase family 36 C-terminal domain;
                     pfam16874"
                     /db_xref="CDD:465290"
ORIGIN      
        1 mddllhfraa gtslvldlsg tglprivhwg adlgacapgr laglraadvp qtvpnaldep
       61 vplsvlpqqs agwlgtpgvs ghragraaap aftvhgtsvr desrsltvea vdpdgglalt
      121 lelgltgagl vrlraavtnt gegpyhltel tpalpvpaqa telldltgrh lrerapqrha
      181 ftlgthlres rrgrtgsdat llltageagf gfrsgevwgl hvawsgnhrs laertpagqa
      241 vlaggelllp geirlapgat yrspwlygsy grngldelag rfhrelrard ghpasprpvt
      301 lntweavyfd qdlatlerla rtaaeagaer fvlddgwfrg rrddhaglgd wyvdaevwpd
      361 glrplidtvr glgmqfglwv epeminpdsd larahpewvl aaspsrlppa srhqqvldla
      421 rpeayayvla rldtllrehr idylkwdhnr dlvdaaahhq ttaayrlmde lrtrhpqlei
      481 escasggarv dlgvlertdr vwtsdcidal erqriqrwtg lllppellga hvgapvahtt
      541 grrhtldfra gtalfchfgi ewdltaasaa erarlaewva lhrtlrpllh sgtvvhgdhp
      601 dpalwvhgvv agdagravfa lvqmatsvqs pagrvrlpgl dpdadyrlap lapgdrpegp
      661 atsalpwweq gvtlpgrvla evgvqaptlf perlvlleav rl
//
LOCUS       WP_457685011             474 aa            linear   BCT 27-JAN-2026
DEFINITION  lipase maturation factor family protein [Streptomyces nigrescens].
ACCESSION   WP_457685011
VERSION     WP_457685011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Doolittle,M.H. and Peterfy,M.
  TITLE     Mechanisms of lipase maturation
  JOURNAL   Clin Lipidol 5 (1), 71-85 (2010)
   PUBMED   20543905
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10535984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..474
                     /product="lipase maturation factor family protein"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=53659
     Region          121..463
                     /region_name="LMF1"
                     /note="Lipase maturation factor; pfam06762"
                     /db_xref="CDD:462004"
ORIGIN      
        1 mawfsdsgyw lgrlvfqrll avlyvvafla avrqfralig argmlpvpay varvpfraap
       61 svfhwhysdr ffalwswggv llaaavaaga adavplwasm vmwavlwvly lsivnvgqtw
      121 ygfgweslll eagslavflg naetappvti mwllrwllfr vefgaglikm rgdrcwrdlt
      181 clyyhhetqp mpgplswffh hlpkplhrve vaanhvaqla vpvllftpqp iagwaavamv
      241 vtqlwlvvsg nfawlnwvti alalsaaapl waqpsaplpa ppvwfevlvl latagvlals
      301 yrparnllar qqmmntsyes lhlvnsygaf gsitrvrrei vvegtadavt gpdttwlaye
      361 fhgkpgavrr mprqfapyhl rldwlmwfaa lspayarawf vpfvtrllen drdtlrllrg
      421 npfpdlppar irarvfryrf ttwrelrdtg awwhhteere flppvarsal hgrr
//
LOCUS       WP_457685019             484 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 30 protein [Streptomyces nigrescens].
ACCESSION   WP_457685019
VERSION     WP_457685019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="glycoside hydrolase family 30 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004348 - glucosylceramidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006665 - sphingolipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52791
     Region          30..484
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mrassvrril tgaagavvaa lvvlwavgpp asgpqqvqvy ltttsgaggr qvvkglekqa
       61 pltfapgggg giavdegkky qrfegggasf tdtaawllns sgalsdrara atmkklfdpa
      121 dgiglsfvrn pmgasdlarf gytyddrpag rtdpglqhfs vahdladvlp ltawarrlnp
      181 avtvmaspws apawmkdnrk ldqgwlraky ygvyaryfvk ylqayrdrgv pvdyvsvqne
      241 ptccsgypsm rwngsglayf tkhdllpals raglstkvla ldwnwdtyre faaptvddpa
      301 vrrhpnfggv awhgysgevt rqtrlhhryp glaaydtehs ggrwvgnqqr edmrnlidyt
      361 rnwgrswvkw slavdqnggp hhggcgnctg lvtvhrgdgr hgtvdytvey ytmghltkfv
      421 rpgarrigst asaalpnvaw rnpdgsrali vyndtgrtrr tginwhgqhv tyalpagasa
      481 tftw
//
LOCUS       WP_457685021             278 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685021
VERSION     WP_457685021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29446
     Region          21..270
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtgssgrvga alaaalgaag wvvrgvdrvp grwtsvvgdl rdrpvrlaal qsadvlvhta
       61 alhaphvgrl addefravnv gmtaglldda aglgarrvly isstsvygha lvptdravwv
      121 deqltplprd iydetklaae elvaacpiss vtlrisrcfp eplpvrarhl lhravdvadv
      181 aaagvlavth stvtgrfnis gphpfhredc lalsrdagav laervpdvvq afrdqgwpvp
      241 drldrvydst aaadalgyrp vrgvrqllrd vgggpvhe
//
LOCUS       WP_457685027             302 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685027
VERSION     WP_457685027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30544
     Region          4..300
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(41..43,46,122,126,147..152,171..172,174,187,
                     210..211,232..233,252..253)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mstaitysey ggpevlalsr valpepgpgq vrirvratav npidlrirag mmrgvfpvaf
       61 pavpgwdvag vvdkagegaa aavgdevfgv asaggysqya vldrpfakpa evsfetaaam
      121 itvgeaacra vehlgvrpgq tllihgaggs vggiavqvaa argitvigtt aerdiervng
      181 lgavavpyge gwvervmava pggvdcvfdt sgagvladsv alagdagkvi tiadpsfarh
      241 gvrftgmdpa drfpealpql agliatgkld vpvghvypla eaarahagie arrnqgkvvl
      301 lp
//
LOCUS       WP_457685031             262 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685031
VERSION     WP_457685031.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /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=27033
     Region          87..252
                     /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 mpmtrtrttt hpatartrlg arivallsav gvalgapaap gsaatpravs papriplpaa
       61 madtgggtql ltararttga ttgtvrwwqr hngrwrqvgs aparfgaggl aeggsrvqgt
      121 attptglydl pfgfgtapap pgtttpyrrv gaaswwcedn asasynrwve plppdcaage
      181 serlagyptq ysralvigfn yhrpvrgrga giflhvhgkg atagcvsipa gamarilswv
      241 rpsahphiai gtvsgptalt ry
//
LOCUS       WP_457685036             508 aa            linear   BCT 27-JAN-2026
DEFINITION  M81 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457685036
VERSION     WP_457685036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Bourne,D.G., Riddles,P., Jones,G.J., Smith,W. and Blakeley,R.L.
  TITLE     Characterisation of a gene cluster involved in bacterial
            degradation of the cyanobacterial toxin microcystin LR
  JOURNAL   Environ Toxicol 16 (6), 523-534 (2001)
   PUBMED   11769251
REFERENCE   2  (residues 1 to 508)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="M81 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53868
     Region          12..494
                     /region_name="COG5476"
                     /note="Microcystin degradation protein MlrC, contains
                     DUF1485 domain [General function prediction only]"
                     /db_xref="CDD:444227"
ORIGIN      
        1 msstpsgsrl rigiggmaie ssqfcphrsg yddfritrer alldrytwtr pdgelsglve
       61 wvplvhavav pggpveravy drikeeltgr ieesgpldgl vydihgamsv vglddaeadl
      121 taavraatgp gtlisaamdl hgnvsrrfae hldlltahrt aphedawetr eraarklver
      181 lvhgrgrphr awvqipvllp gektstrlep arslygrlas vealdgvmda alwvgyawad
      241 earcraavvv taddpelalt qagslarayw darrdfafag ptgdadtcia ravasparpf
      301 lisdsgdnpt aggagdlaym lgrllaheel asgrvtalhp gitdpeavav craagvgaev
      361 tlgvggrfsa gtgphtapyv ltgtvtavde pagpgpgapr gnpaydgggr saavtcggvt
      421 vvlterrkpf htradfgsld playdlvvvk igylepelye maadwllalt pggvdqdllr
      481 lghhrvlrpl ypfddegfed pgltpvll
//
LOCUS       WP_457685043             302 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685043
VERSION     WP_457685043.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31682
     Region          1..298
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mdtmrerfas vtsqllaedp rlalvladig aagfaeaekq hpdrvvnvgi reqlligvgg
       61 glaltglrpi mhtfasflve rpfeqvkldl ghqgvggvlv sagasydwps ggfthmapgd
      121 valldtldgw tvhvpghpde aeallryaaa agddkvyvrl svqtnaapra vdgahfrtvr
      181 egrdgvviav gpmldpvlaa teglsvtvly attvrpfdaa tlraaagaaa asdvvivepy
      241 lagtstrpaa ealedrphrl lglgvgrqel rrygqldehl aahgldprgl reriagflta
      301 gs
//
LOCUS       WP_457685050             394 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685050
VERSION     WP_457685050.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41909
     Region          4..378
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mpttpapria vigagpggla carvlqrhgi gvtvydrdas adardqggtl dlhadsgqia
       61 lqeagllddf halarpegqa mrmltrhgev lvdyrptdae daapeidrgr lrtllanslt
      121 pgtvrwghtl tsvtphpagt hrltfdngvt rdvdlvigad gawsrvrplv saatpvptgv
      181 tflearfdkv dtehpavael vgdgqvfatg dhkgliaqrn seqhvrayia lrddedryra
      241 agnglddtea vraallrafa gwderllvli tdndgpyvnr plfvlpapht wphtpgvtll
      301 gdaahlmtpl ggnganfall dgcelalala rhdtldeavt ayertmlpra aaagdgaaal
      361 ksllgpgdrg radvpdfaee keryrqgaaa yrsr
//
LOCUS       WP_457685052             468 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685052
VERSION     WP_457685052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..468
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49337
     Region          16..378
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 maehsngght aiviggglag mlavtaltgh vdtvtvierd rypegrafrk gvpqarhlhi
       61 llrggslale ellpgtvaal geagarrlyl srdlltrtpt gwqrrfderr hltlsvtrpv
      121 ldsvvrervl raaagsatrv evleateatg ltgdagrvtg vrvrsrdgap ggraerelpa
      181 alvvdasgrg srapqwfaal grsapqeetv dagiayatrm yrpkdpatap dagvnvpgwp
      241 ecprgaayvp vedgkwlltl sgvrghhppt daaeftafsa tvgdpyvhel ldraeplsav
      301 hgfrdtcnrr rhferpgalp egflvlgdag ctfnpvygqg msvaalgala vrttladggg
      361 lrpgiaaeaq ravaravepa wlaavgadrp yaspgdtkag vgerlstwyi arlsarasid
      421 pvvgaafrdv fsltapptrl vapqiflrtv flprrpglpg ppatieal
//
LOCUS       WP_457685053             338 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685053
VERSION     WP_457685053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=35193
     Region          14..302
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mtfqqvsepy daydvlvvgg sgvdtlvqvg alpvpladsy pvpplhegag htgtgvalgc
       61 aalglttgfv dflgddhpgt lvrerlagtg vdfrplisph gtrravnlva pdgrrmsfyd
      121 ardpadlrmp pehylpplrr arhvhlsimh farflyddie algipvstdl qdwdgltdhh
      181 refalrsdlv flstagager igsvmreilh egraeaviat agaggaylls addrtprpvp
      241 aaippgpvvd sngagdafts gflygrlagr sleecarlga vagayactsr gthtalvgpq
      301 elhaalgaka patvitspag dgprlpgppd aqvsrtga
//
LOCUS       WP_457685057             288 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685057
VERSION     WP_457685057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32026
     Region          18..74
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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          103..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 madprsagap tvlrvvlgkr lqdlrekagl sfeqaaaald vthatirrme kaevglklpy
       61 vekllatygv tdeeeiegfv slareankpg wwhrfrdvlp ewfsafvsle seanlirayq
      121 phyvpgllqt edyaaavlka gmphasakdi drivalrmer qslltrnhap mlwvvmdetv
      181 lrrpiggpkv mrgqvsrlme atalpnvrlq impfaagphp amygpfhifr fpipelpdia
      241 yaeslvgavy fdqrndvsqf lealdrmcaq aapahtteai lggfrkei
//
LOCUS       WP_457685059             269 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457685059
VERSION     WP_457685059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10595285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=29375
     Region          13..268
                     /region_name="Y_phosphatase3"
                     /note="Tyrosine phosphatase family; pfam13350"
                     /db_xref="CDD:463853"
ORIGIN      
        1 mtqqtpqvpq aqpeltevrn frdvgglptv dgrhvregrl frsghlahat etdaaflagl
       61 glhtifdfrn asdiklegpd valpgvrnvn ipltdpadga efwtmvrdge leqlrsalgd
      121 gkaaarmaat yrhiittrte dhsrvlhala edsvpalmhc aagkdragls vavtllavgv
      181 erdaieadyl ksndphrryk irrsdnsavg msqevmells plfgahtdyl taaydaiert
      241 wgstekyltd glgltpaare rlrdrlltd
//
LOCUS       WP_457685070             813 aa            linear   BCT 27-JAN-2026
DEFINITION  Tex family protein [Streptomyces nigrescens].
ACCESSION   WP_457685070
VERSION     WP_457685070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Amblar,M., Barbas,A., Gomez-Puertas,P. and Arraiano,C.M.
  TITLE     The role of the S1 domain in exoribonucleolytic activity: substrate
            specificity and multimerization
  JOURNAL   RNA 13 (3), 317-327 (2007)
   PUBMED   17242308
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Fuchs,T.M., Deppisch,H., Scarlato,V. and Gross,R.
  TITLE     A new gene locus of Bordetella pertussis defines a novel family of
            prokaryotic transcriptional accessory proteins
  JOURNAL   J Bacteriol 178 (15), 4445-4452 (1996)
   PUBMED   8755871
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..813
                     /product="Tex family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003729 - mRNA binding [Evidence IEA]"
                     /calculated_mol_wt=86991
     Region          13..738
                     /region_name="Tex"
                     /note="Transcriptional accessory protein Tex/SPT6
                     [Transcription]; COG2183"
                     /db_xref="CDD:441786"
ORIGIN      
        1 mtastepiga lgtieariag elgvkerqvk aavelldggs tvpfiaryrk eatemlddaq
       61 lrsleerlry lreleerrga ilesvrsqgk ldaaleaqir gaeskarled iylpfkpkrr
      121 tkaqiareag lepladglls dpsvepaaaa aafvddgkgv adpaaalega railterfge
      181 dadligelre rmwsrgrvaa kvregkeedg akfadyfdfa epftelpshr vlamfrgeke
      241 eildltlepe dpsaategps syeqsiahrf giadrgrpad kwlqdtvrwa wrtrvqvhlg
      301 idlrlrlrqa aedeavrvfa snlrdlllaa pagtratmgl dpgfrtgvkv avveatgkva
      361 atetiyphvp qqkwdaslat laklarehdv eliaigngta sretdklaad liaaqpelkl
      421 tkvmvseaga svysasafas qelpdmdvsl rgavsiarrl qdplaelvki dpksigvgqy
      481 qhdlsevkls rsldavvedc vngvgvdvnt asapllsrvs gigsglaeni vahrdsngpf
      541 rsrkalkdva rlgpkayeqc agflrirggd dpldassvhp eaypvvrrmv ksagtevgsl
      601 ignttvlrsl kaaefvddsf glptvsdilq elekpgrdpr pvfktatfke gvekigdlqp
      661 gmllegvvtn vaafgafvdv gvhqdglvhv samsksfvkd prdvvkpgdi vrvkvldvdi
      721 prkrisltlr lddehgkgas adggerrggg errggnggga reggrggapr qrqggggprg
      781 gdrrggrdag pandamadal rragllgkdr ggr
//
LOCUS       WP_457685078             346 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685078
VERSION     WP_457685078.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=36211
     Region          9..330
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mtsntesldi rvvgggvigl tsaialaedg hrvrvlsrda agdttsavag glcwpyriqp
       61 yeravewsvr sfqvlaalag rpeetgarmv tgtmtattgg grgasgkagd gaedglaawy
      121 davpglrrar aeelpeghas gwrartplvd mpshlryler rltaaggame rcevtsleea
      181 gaaadmvvnc sglgaralvp dpevhpvqgq lvivenpgie ewyvsadaga sdttyllpqp
      241 yglvlggtaq enawsrepdp avaeaivarc arrfpelara rvlahkvglr parpavrlaa
      301 erlsggvpcv hnyghggggv tvawgcadev lrmvravqee rgpvrg
//
LOCUS       WP_457685080             567 aa            linear   BCT 27-JAN-2026
DEFINITION  BCCT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457685080
VERSION     WP_457685080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59835
     Region          6..522
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mtdlpdgpqe ngppqtdrvv fgvtalltla figwgasste slknastsml nwvidnlgwa
       61 fvlsasafvi faiwlavsky gritlgkege epefrtvswv ammfsagmgi glmfygvsep
      121 lghfttpppg tdpqdaaqam dtamattlfh wtlhpwaiya vvglaiaysc frrgrrqtis
      181 avftpligsr rangwggrvi dilaifatlf gsaaslglga lqigsgikvl gwmdsvsttl
      241 lvgvitvlti afilsavsgi akgvqmlsni nmvlalilav fvfvvgptil ilnllptslg
      301 sfigelpqla grteagsgdd vggwlrswtv fywawwiswt pfvgmfiari srgrtirqfi
      361 ggvilvpsvv slvwfavfgg samklqeskq lsgsstpegq lfdvlhqypl atvtsvlvmi
      421 lvgiffvsga daasivmgtl sqkgtfeptr lvvifwgvvt gavaaimlli gggsgdaltg
      481 lqnltilvav pfmvvmiamc walmrdlrsd plivrgqkge eavelaviag heqydgdfef
      541 qigpggtgng dgdgngedsg agvksgg
//
LOCUS       WP_457685082             447 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457685082
VERSION     WP_457685082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 447)
  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 10154696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..447
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48560
     Region          103..327
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06242"
                     /db_xref="CDD:349461"
     Site            order(113,116,163,172..173,202..203,208,294)
                     /site_type="active"
                     /db_xref="CDD:349461"
ORIGIN      
        1 miprphrlav vplaigltat lgatppaapt aptatpaprt gfetshgarw tgqaeeqdfl
       61 ravdrgsvrv ridrigttgq grpvqlvrig apapdrpaev rrgnsvllic sqhgdepsgr
      121 eaclttvrdl ayardaatrr flertsvlvv ptanpdgraa dtrgnadgtd inrdhialqt
      181 aegramaevi rdyrpdtiyd lheygptvpy ymkdvlslwp rnlntsggvh reagalsqdf
      241 vrpavhragf stgvygiwtd petgdpvkqv agdgqerilr ntagvkgsvg llvetrvdal
      301 teaekadpaf nnrrrvdsql aaldgaftff drhrsrieaa ttaarlagyn dhgpvylgga
      361 dnepatdvqi lahppcayrl eerqfaqvre elvrhgvvwr rdrdgvvvpl rqplrklipl
      421 lldqragyhl tvatplnvcr rvvggng
//
LOCUS       WP_457685084             495 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457685084
VERSION     WP_457685084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53739
     Region          46..456
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(154,156..157,290..294,314,317..318,321,336,340,395)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mrhrllvpga aalslllavp asaadftpga pgvgdtyype sgnggydvsh ydlrlkyqpk
       61 tdllegtatl latttqdlsr fnldfglkvs eiringkkas fatsgkhele vtpatplekg
      121 kqisvvvrya gkpsevkidg ysawartpdg gvvaqepdaa vwwfpsndhp tdkatydisv
      181 avpdgtqals ngvlasqssk lgwtrynwrs dkpqatyltt lavgkfditt dktanglpvi
      241 navskdlgsh egsakasier tteitewles vfgpypfnaa ggyvpnvpag yaletqtrpf
      301 ygkkvfdrgt nvsvvvhela hqwygdnvsl kdwkdiwine gfaaysqwlw sekegegtaq
      361 eladwvysqh paddpfwtvk pgnpgaenqf dgavydrgal tlqalrnkvg dkaffgilks
      421 wqtenkygna svadfvkfae kksgkelagf fdtwlfqpsk ptagaakkal garqapvaep
      481 kswkqiaath dthgh
//
LOCUS       WP_457685086             283 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces nigrescens].
ACCESSION   WP_457685086
VERSION     WP_457685086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10007665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32094
     Region          7..273
                     /region_name="COG3662"
                     /note="Uncharacterized conserved protein, DUF2236 family
                     [Function unknown]"
                     /db_xref="CDD:442879"
ORIGIN      
        1 mnavkndpkp ppvggvlwsl agdirmlltl ppalamqvah pavgagvddh svfrtdpwgr
       61 gerslaslql wvyggeaaaa egrrlralhr tiqgtdahgr syhaltpayy awvhatgypv
      121 frhaqqylgr pfteaqeral yaewlqvgrv lgihdrdmpq tveefwpyyq kvldneleet
      181 vvvkellatd pplpapdrgp rwlrlllrls wpwlrprfar vrrfltiglm ppdarqaigl
      241 ewtdaqerrl rrlgrvvrav vpvlperlrf mpiarrarqa arg
//
LOCUS       WP_457685089             424 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457685089
VERSION     WP_457685089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 424)
  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 424)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=44995
     Region          48..197
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          175..415
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfdnprtgas racvavgrcq laslhalavs amgslvvlal llvpvgvgfr llppaaralr
       61 vlsdrsrsra erwtgvrigp peplpvdral narkrsgaii adegfwrdla wawlepvigg
      121 llvavplali eygafgalvq pfiwrlindg nwyafipvhs tatmcgalvl glafmavgll
      181 aapavlrlht rvsrpllsap rssrlaqrve rltdtraral daqaaelrri erdlhdgaqa
      241 rlvalgmtld ratrlmetdp aaardllldv rrtsegalqd lrelvhgiqp pvladrglgd
      301 avrslaldsf ldvhvetrlp gkppapvesa ayfavseala naakhsgare vgvaltyeng
      361 slratvtddg hggadpsrgt glagvrqrld tfdgtldlhs pqggpttvtm eipcalsspk
      421 tsss
//
LOCUS       WP_457685094             400 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685094
VERSION     WP_457685094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41473
     Region          3..366
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 maepgngpls gvrvvelagi gpgpfaamll adlgadvvrv drpggaglgi dpayditnrn
       61 krsvlvdlks pdgvaqvlel veradvlveg yrpgvaerlg vgpeeclarn prlvygrmtg
      121 wgqegpladt aghdigyiai tgalgmigpp dgppavpanl vgdyaggsly lvigvlaalq
      181 harteggkgq vvdaaivdgt ahltamihgm laaggwqdrr ganlldggtp fygayetadg
      241 ghmavgalek rfygefirll gieeeapsrd dlaawdelrt viaarfktrt reewtavfqe
      301 sdacvapvls lreaprhphl aargtfvehg gitqpapapr fshtpgavrr ppalpgadte
      361 eiardwqapg llaplpsass paapappagp srteqkdtag
//
LOCUS       WP_457685091             275 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces
            nigrescens].
ACCESSION   WP_457685091
VERSION     WP_457685091.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=28631
     Region          122..224
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 maadppdgiv gamrrkpvdi kamalfltva flaagvlgal qpatripgev iqltqfgpal
       61 gvglaallwp ervrevlagp epdrrgrgvl llvtapviia lsvlayaalt gdahsarpga
      121 pflliavvql igacgeeigw rcflqpllrt rlgplaasvt vgvawgvwhv qvfarhpvya
      181 gafitaavsm svvmgwaleg vrasrlllag gfhalinlgm llfmdeesga vlpmvlfgas
      241 claaaglwtw rsvgrqrsag ssapakippv mddvr
//
LOCUS       WP_457685097             254 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457685097
VERSION     WP_457685097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27015
     Region          2..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkkvdhear rqeisealwr iagsrgldgt slrdvaaeag islgrlqhyf rtrdemllfa
       61 lqhinrlaad rireriasla eeptprevlr aclsgmlpld eksrigllvg aayyaravhd
      121 ealraeakng ipplrtffad qlrlaadrge lpperatede amllismteg latyvllgvh
      181 dpedalllld lhlenlfgae ravgggadra vgggadrpvg gsavrtargg adraaevggg
      241 rgaeasassg rsap
//
LOCUS       WP_457685106             444 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457685106
VERSION     WP_457685106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47415
     Region          <301..439
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 metsttvpes aaalhagida ltdevidglr aqlpsyaavs adqirprvma slrnglslvq
       61 rwaeerrtar gsgrddgpay gipsahldev tdlarslpve diisayrigt divwrrfgee
      121 mtarggtaed llpiaetlra wvdantlriv rtcrvalqgd dpaadrrhaa mvralllgea
      181 rwdkspagfg awgagltgdr padgyrterq addaetedgs yvhsvlrlpf rarlpevspp
      241 gdpggapaaa ghagpgdraf rrtvdllrpw laldeagrpl vttvdgdvag llvgrpaglc
      301 rslmlglgap apasglatef tratqalraa agfglvgaft reelglratv valpavgeql
      361 vtlrlsplae rgedgaqlee aaaaylrqgl rleaaartly vhpntlrnrl rrfeeitgtn
      421 lrdpadlaev wwalthrrfh gpas
//
LOCUS       WP_457685112             527 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457685112
VERSION     WP_457685112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..527
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56127
     Region          29..502
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mvrvtgpess rpgtradgsh dddaiaelgy kpelkrtlgn fhtfaagisy isiltgtfql
       61 fyfgiahggp aywwswpmvf agqlmvalcf celaarypva gsvynwakkl ggphigwlgg
      121 wmmvtatmvs lsavalayqv tlpqisswfq figdgtgksa aenavllgtv litfttlvna
      181 fgvklmarin sagvaielia aivlilllaa hvtrgpdvvt dtfglgeges lgyfgaflta
      241 slasayvmyg fdtasslgee skdpgrnapr ailralvasf ligglillfa llsvpdlqae
      301 qlkvdglqyv vlstlgstvg qivlwcvvia itvcelavht agirlafama rdnnlpaasl
      361 lakvsprfqt pvlpavvigl vavgilvinv nqpqifsvit siaiimiyla ylsvtlpmlv
      421 qrlrgnwtpa kgkfslgrfg ipvnilavlw giamslnlaw praavynatg pqhwylrwga
      481 flfigvvaig gfayywfvqr krtgvlamha avrpdggtpd dagnptp
//
LOCUS       WP_457685120             314 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685120
VERSION     WP_457685120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  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 314)
  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..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /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=32253
     Region          1..314
                     /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 mrrvrfhsyg gpdvlrveet aeepvpgpge llvrteaigv tlpcvrrvrg dgngggdplp
       61 smpggeiagt vvalgpdvtg ftpgdrvtsl tftgsytela lapaflasri pdgasaveav
      121 alvrsghval aalstaaprg aesvlitgaa gatghlavql aklqgvprvv aavssaakae
      181 flrglgadev vtydqeswga padivldgvg gellpralaa lapggrliff nsgggtvpay
      241 ellagdktit gltmrrfstv qrelyeehra qlwelagsgr lraavhaelp ldeaakahei
      301 iearanlgkv vlrp
//
LOCUS       WP_457685124             608 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457685124
VERSION     WP_457685124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..608
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66192
     Region          1..607
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreftvppla taprvgglad avyehagsdp drvalarkdd agnwqnvtsg qfrdeviala
       61 kgllaqgvrf gdrvgimsrt ryewtlfdfa lwsigvqsvp lyptssaeqv fwmlhnagvs
      121 aclvehedha mtvgsvidrl pqlrklwqld adpvaeltaa gahiddevvh rhrmavtpda
      181 tatiiytsgt tgrpkgclis hanfmaesdn ivlryekvfh skpgdeaatl lflplahvfg
      241 rmvqvaairg rvklghqpel aarallpdlq tfqptfilav pyifekvfaa arrraeadgk
      301 vgpfdkavei avryaeaqeh kafgtgsgpg aslrmqhqff dkvvyskvra amggrvrham
      361 sggsamerrl glffagagvr ifegygltes taaatanppe rtrfgtvgtp vpgttvhiae
      421 dgeiwlyggq vfhgyhndpk atdavlhdgw fstgdlgald edgyltitgr kkeilvtsgg
      481 ktvspvglee rvrahplvaq civvgndrpf iaalvtldpe avthwlamrd kpempatdlv
      541 rdpdleteir ravvaantlv sqaesirtfr ilanqfseeh glltpslklk rkaiettyta
      601 evdalyqt
//
LOCUS       WP_457685129             459 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685129
VERSION     WP_457685129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49968
     Region          1..456
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mevalclfss dlrlhdqpvl haalraapqv vplfvvdtgi agagfmvpnr aafladalad
       61 ldaglrergg rlvirtgdvv tetcrvaaet gagevhlaag vsgyalrrer rlgaelaaag
      121 rslvvhdavi taqppgavlp sgpgkdhfav ftpyfrrwqa agrrsvlpap rsvrvpaevr
      181 seklpsaqvl cpdgepspal peggeragrr rfgawqrsgm agyqdrqddl pgdatsrlsp
      241 ylhfgclspv elvhkasgrs dagaeafvrq lawrdfhhqv laarpgaara dyrtkgdrwr
      301 ydgaevtawk egltgypvvd agmrqllheg wlhnrarmlv asfltktlyv dwrvgarhfl
      361 dllvdgdvan nqlnwqwvag tgtdtrpnrv lnplvqarrf dpegayvrrw vpelaglagp
      421 avhqpwklsg peraaydypd pvvdladalv rfkrargle
//
LOCUS       WP_457685142             442 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685142
VERSION     WP_457685142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   McLeish,M.J., Kneen,M.M., Gopalakrishna,K.N., Koo,C.W.,
            Babbitt,P.C., Gerlt,J.A. and Kenyon,G.L.
  TITLE     Identification and characterization of a mandelamide hydrolase and
            an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas
            putida ATCC 12633
  JOURNAL   J Bacteriol 185 (8), 2451-2456 (2003)
   PUBMED   12670968
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Vasiliou,V., Pappa,A. and Petersen,D.R.
  TITLE     Role of aldehyde dehydrogenases in endogenous and xenobiotic
            metabolism
  JOURNAL   Chem Biol Interact 129 (1-2), 1-19 (2000)
   PUBMED   11154732
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..442
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_process="GO:0006081 - aldehyde metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47036
     Region          13..438
                     /region_name="ALDH_F3-13-14_CALDH-like"
                     /note="ALDH subfamily: Coniferyl aldehyde dehydrogenase,
                     ALDH families 3, 13, and 14, and other related proteins;
                     cd07087"
                     /db_xref="CDD:143406"
     Site            order(121..123,149,178,196,295,297..298,301,342,344)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143406"
     Site            order(123,218,249,252)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143406"
ORIGIN      
        1 mapqnhttdl daasvvgrlr rtftthrtas pewrrgqlta lrtlltdhrd dllaalaedl
       61 gkgpeeayrt eigftlheid htldrlddwl eprpaelper llpatahtvr eplgvvlvia
      121 pwnyplqlal aplvgalaag ncavikpsel apaasaalar llpryldsda vavvegavpe
      181 ttallaqrfd hifytgngtv grivlaaaap hltpvtlelg gkspvvldpg tdlaaaarrl
      241 vtgkflnagq tcvapdyvla igdtareiep hlaaavrety gadpagaeey grivnerhfd
      301 rltalldsgr tviggahdra arylaptvla dvapdapvmq eeifgpilpi vpvpdldaai
      361 afindrdkpl alyaftased tkrrllaets sgaltfglpv ahltapelpf ggvgesgmgr
      421 yhgeysldtf shtkavldkp la
//
LOCUS       WP_457685139             149 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685139
VERSION     WP_457685139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16238
     Region          2..135
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mirrrhdsdl ddcvavlaev hthngyphhw pddparwltp dgltaawvae tdgtvtghaa
       61 lcgpevsrly vapaargagl ggrllravea eaaarglrpv levkttdtta ialyerlgwr
      121 rraterqdwg sgevvtvyry eaqparpah
//
LOCUS       WP_457685147             212 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457685147
VERSION     WP_457685147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22768
     Region          15..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdmaqqrvka prdssarqrl tardwadaal aamgegglaa vaveplaarl gttkgsfywh
       61 fsnrdaliea alehweetct eaviaeveae pdpgrrlrll lmqattlaat dplevsllas
      121 aadprvaaal arvtdrrigy vaalfealgf pgdearhrgl laytaylght qlghavpqsl
      181 padaardryl dgvidtlvrp rnggdrseld rt
//
LOCUS       WP_457685154             267 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457685154
VERSION     WP_457685154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..267
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28997
     Region          <91..240
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mteliaqslc drnpgfkevi erggpqqvar liqdvlrsgh plpekvravm lrtdtdihlv
       61 asalgdclvs tpgeapglli paaladgksg rarlkgvlrh raavvghava pteaeasvra
      121 asrlldlasa hdgpdagvvf vddhlsslvl lqdeslahtl iarrlrplag ltpercerle
      181 atllawlggm gapevakals ihpqtvryrm rqleklfgar lrdprtrfei emalrsrqlm
      241 aaarrrrtga trrprvttkp rkalprp
//
LOCUS       WP_457685156             283 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685156
VERSION     WP_457685156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30940
     Region          26..272
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mpgrvkadlk gvpetalwtl yhraaeaarp dtvlpdprav qllteiefpf rermgaarpw
       61 laqaialral gfdrvvrafl adrpdgtvva lgegletqfw rvdngraqwv tvdlngplal
      121 rkrvlphgar qrlvacdard sqwmadidps rgvlvtaqgl lmylqpaqvt rliaacadaf
      181 pggtmvfdtv srrfstrtrt rtkgpgghrl ppmpwgmdai drdrlrqahp aisevsevpl
      241 pagrgfigyl apraaalpll rtdrplitrl rfgaapaslt gqp
//
LOCUS       WP_457685158             844 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685158
VERSION     WP_457685158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 844)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 844)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..844
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86353
     Region          66..456
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(66..67,70,101,151..152,154..156,159,179,182..183,
                     186,311,314..315,318..320,323,351,355,408..409,413,417,
                     433,436..437,440..441,444)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          <587..>828
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mapatavpia papaiapapt ptpapvasge peepgrpgap apvgprrlrp vvaglmltll
       61 laalgqtiiv talpeiagel hgpgamswvv tsyllasvig lprygklgdl fgrkpvflfa
      121 llvftvgsal agwsrtmdel vvfravqgvg gggliigvqa iiadvvppra rgrytgllga
      181 vfglgfvagp liggfcadha swrwcfslnv plgvltflvi acvlklprpt rrakpdlaga
      241 lllaafsicl vllaswggtt yawdsrvvlg laagalgtal lflaveyfat epliplrlfr
      301 dsvfhvtglt gaavglalfg avsclpaflq radgatates gllmlpltgg lviaslvsgc
      361 lisrtgrhkv fpvlgcvpaa vgmwllsrwq qdtawevysl gtallglgig fvlpvlvlav
      421 rhsvrtpdlg aatgathcvr qiggsvgaal failladrla rrlgdrlpgs arlpapeslt
      481 prlvralpaa lrdspvaaya dampriflfl vpvlvlglvl afflkgkplv shaspapqaa
      541 pspqmpygdp adpaavpqar aaadtnavns hgpgspytra hrhtttghta vmagvpvcgt
      601 vqhhdgsivp raaltlidva grqigrgatg edgryalstp gagsyvlias agghqpqavt
      661 vtvgerpvel dvvlggagrl agtvttadgt pvrdamvtlt dvrgevvatt rsgreggyvi
      721 gelvageytl assapafrpa alpvtvqasr etrqdielag gavlrgtvra gggrpvedar
      781 vtlldaagnv vdtattgpdg lfrfvdlsag eytviaagyp pvatvlqvag ggrterdlql
      841 ghed
//
LOCUS       WP_457685161             263 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457685161
VERSION     WP_457685161.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26467
     Region          17..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 meqarnsgps apgthrrvvl vtgagtgigr atahafaaeg arvlavgrrp gplaetaaga
       61 gagdgeivpy aaditadgap eelvghavet ygrldvlvnn aavvgsgalg sftkegvapl
      121 latnlvapvl ltqaavphle rtggvvvnis tsvgqrgwpg nsvyaatktg lelltrswav
      181 elaprgvrvv avapgaietp iarhqgwspe qraavrkwqi ahtplgrvgr peevawavtr
      241 laapsasfvt gvvlpvdgga vvg
//
LOCUS       WP_457685163             606 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685163
VERSION     WP_457685163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..606
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=63761
     Region          20..297
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          327..603
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mgtqstpdls tqapslslst vaviglgtmg tgiaevltra grevigidtd eaaarhavsa
       61 lesataravq rerltererq dalarfrtft dlqaaadadl vievvpedye lkrqvfaeld
      121 avvrpdtila tgtnalsvtr laadsrrper vlgvhffnpa pamklvevvs svltaptava
      181 avtelardlg kdpiavgdrp gfvadgllfg ylnqaaamye skyatredid aamrlgcglp
      241 mgplalldli gvdtartvle amytesqdrl hapapilgql aeagltgrka grgfytyeap
      301 gsptvvpdae spasahelaa grtvtgvgva gsgtmasgia evfakagykv vlaarsleka
      361 ekakariaks lgrsvdkgrm saetrdaala aitpagslda fadvdlavea vaedlavkqe
      421 lfrtldkvck pgavlattts slpvvacara tsrpqdvigm hffnpapamk lvevvrtvlt
      481 addvhatvrs vctkvrkhpv dcgdragfiv nallfpylnn aikmveehya tlddidaamk
      541 lgggypmgpf elldvvgldv slaiekvlha efrdpglaps pllehlvaag clgrktgrgf
      601 reyarr
//
LOCUS       WP_457685165             320 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685165
VERSION     WP_457685165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34813
     Region          6..311
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtqahrlrpr rsclavpgsn prflekaqgl padqvfldle dacaplakeg arhhivetln
       61 egdwtgktrv vrvndwtthw tyrdvitvve gagpnldcim lpkvqdaqqi valdllltqi
      121 ektmgfevgr igieaqiena kglvnvdeia gasprletii fgpadfmasi nmkslvvgeq
      181 ppgygadayh yilmrilmaa rtydlqaidg pylqiknvdg yrevagraaa lgfdgkwvlh
      241 pgqveaanev fspsqedydh aelildayew htseaggakg samlgdemid easrkmalvv
      301 agkgraagmi rtskfeapea
//
LOCUS       WP_457685167             410 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685167
VERSION     WP_457685167.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45035
     Region          10..398
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtrlaqtegl tdiqqeilst vrdfvdkeii pvatelehrd eypsqivegl kelgvfglmi
       61 peeygglges lltyaltvee iargwmsvsg iinthfivay mlkqhgtqeq kdyflpkmaa
      121 geirgafsms epalgsdvsa isskgvrdgd eyvlngqkmw ltnggsstlv avlcrtdegh
      181 pegtaphksm ttflvekeag fgevrpglti pgkidkmgyk gvdttelimd glripadrvl
      241 ggetgrgfyh mmdgvevgrv nvaargcgva qrafelgvsy aqqrhtfgkp iaqhqaiqfk
      301 laematkvea ahammvnaar kkdsgqrndl eagmakylas eyckevveda frihggygfs
      361 keyeierlyr eapmlligeg taeiqkmiig rrlleeyriq gehpvwagma
//
LOCUS       WP_457685191             110 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457685191
VERSION     WP_457685191.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..110
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=11885
     Region          7..97
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 mvagkafdve pdvlrtqgna fvhigsdfsk askklqddle glgspwencd fgdifetiyt
       61 pirdgmfesm dslgerlegi gdklqnmavs ytesdeqgih tisavgrpai
//
LOCUS       WP_457685205             472 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685205
VERSION     WP_457685205.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51686
     Region          40..415
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maraamtpsa ahaladaept pfwladpdrp aarpalvgde tcdllvvggg ysglwtalia
       61 kerdperevv lvegaeigwa asgrnggfca aslthglgng larwpnelat leelgirnld
      121 aieeavaryd idcafertge idiatephqi aelrefaeda akvgldrhtl ldedelraqv
      181 dsptfraglw drngvamlnp arlawglkqa clglgvriye rtpatglasd gtgmavrtpy
      241 grvfarhval gtnafpslvk rvrpyivpvy dhalmtepls deqlaaigwk nrqglsdsnn
      301 hfhyfritad nrilwggydi vyrygggvra eydhhpatye klarhffrcf pqleglrfth
      361 twggaidtcs rfsaffgtah agrvayatgy tglgvgatrf gaevmldlls gertertele
      421 mvrskplpfp peplrwagig itqwsmtqad trggrrnlwl kamdkvglgf ds
//
LOCUS       WP_457685209             393 aa            linear   BCT 27-JAN-2026
DEFINITION  polyamine ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685209
VERSION     WP_457685209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Igarashi,K. and Kashiwagi,K.
  TITLE     Polyamine transport in bacteria and yeast
  JOURNAL   Biochem J 344 Pt 3 (Pt 3), 633-642 (1999)
   PUBMED   10585849
REFERENCE   5  (residues 1 to 393)
  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 10194417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="polyamine ABC transporter substrate-binding
                     protein"
                     /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=43969
     Region          52..387
                     /region_name="PBP2_PotD_PotF_like"
                     /note="The periplasmic-binding component of ABC
                     transporters involved in uptake of polyamines; possess the
                     type 2 periplasmic binding fold; cd13590"
                     /db_xref="CDD:270308"
     Site            order(57,267,270,293,295,331)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270308"
ORIGIN      
        1 madlsrrall rgmgglgvtg alaamtgcgv ppayveaadr ggpdrsardr klvfanwply
       61 idvddqhkqr rptldafarr tgvsvtytee indndeffgk ispalmnhqs tgrdlivisd
      121 wmcarfvrlg wvqemdraaq phvarhldpl lrsphfdpgr khsvpwqsgi tgiaynrkkl
      181 greikhtadl wkddlrgrvt llsgldesfa mlmqgngvdi trwtaddfyr mtdqirrlvs
      241 kghirrftgn dyikdldsgd vlaaqaysgd viqlqadnpd iefvvpqega elwaesllip
      301 nlaehkrsae rlidyyyrpe vaadlaawvn yvcpvpaare vlaaskdker aalaedplif
      361 pddamrkrla iarditsker tafakewnai vgl
//
LOCUS       WP_457685214             286 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685214
VERSION     WP_457685214.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 286)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29106
     Region          <35..191
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mdrvagraag raagraagra agraagraag raagvergev agraegvapv vravppaegr
       61 swpvggaggi rptvvrgwep ppapwtaghr gvdlgapada vvraaapgrv ayagtvagrg
      121 vltlevsrsg rpplrttyep vrstvrkgqr vtagqpvael qhggpfhcre pclhwglrrg
      181 ktyldplsll ppsmlgggps rllpifgvpv pagahtvppp peppettaqa sspaptttal
      241 aeavglaavt iwalgqlssa rsalseegtr rrwrgwgwrl lgrggg
//
LOCUS       WP_457685211             357 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685211
VERSION     WP_457685211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37602
     Region          9..352
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtaragstaq ellrlggvtv rfhaggrpal davdlevaah eivcvlgpsg sgkstllrvv
       61 aglqqadagq vllegrdqsg vpthrrgvgl mfqdhqlfpq rdvagnvafg lrmrrsprgd
      121 qertvaelld lvglpgaqrr avaslsggeq qrvalarala prprllmlde plgqldrglr
      181 erlvvelrrl fhelgttvla vthdqgeafa ladrvvvmqd griaqtgtpl evwqrpatef
      241 varflgfdnv veatvqgeaa atpwgkvpvp aatldgpcrl lvrpagvrlt aapeglpctv
      301 aartfrgthv alllqpsggp qveaacalrd apevgervgi afhaqdvvvl dasaaag
//
LOCUS       WP_457685207             415 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685207
VERSION     WP_457685207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=45574
     Region          29..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mehheqpepl spaeltamrr sltdgrlamt rrsllrasga vaatvgglga lsacgippag
       61 rtdagrstdh skaekrisfs nwteymdvsd dgkhrptleh ftkrtgiavk ytedindnde
      121 ffgkiqaqla agqdtgrdli vltdwmcarm islgwiesld panlphayan lspqfrspaw
      181 dpgrahsypw qgipaiiayn kkatggrkvd sisqlledpk lkgrvgflse mrdsvgltll
      241 dmgkrpedct addfdaaiar iqkgvdskqi rrftgndytt dldkgdlaac vawagdvvql
      301 qndnpdigfa ipeagymtss dnlmvpnkar hkenaerlid yfyepkvaak iaayinyvcp
      361 vegvreelak idkkaadnpl iipdremaer shsfralsak enkaftqkfs dltga
//
LOCUS       WP_457685221             407 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685221
VERSION     WP_457685221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=42220
     Region          1..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 midvlvlggg faglwsaaaa trllraqgsa rsvalltpdp dlvlrprlyq adparmrvpl
       61 drvlgpagvr riaatatavd tarrrvtalt sdgsrtevay rslvlatgsa vvrpelpgaa
      121 llhdidtlpa avrleehlrg lpeapagpgr wtavvagagf tgleiatelv grlraqaapy
      181 gaadevrvvl veraavvgag lgaaarpvit raldtlgier rlgttvtgld arsvhladgs
      241 tvpartavwt agmrastlta qipaprdalg rlavdrglrv rgieglyaag dtaaalaeed
      301 hpvlqscqha iplgkvaghn aaaallglpp vdfapdpyrt cldlgeagav atagwnrtlr
      361 egpegfakdl krainetwis ppvddpqell rradhrvgtr qeaapsa
//
LOCUS       WP_457685231             288 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685231
VERSION     WP_457685231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31535
     Region          8..226
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msrrrigfwy rlaavickpp llvlfkrdwr gmdhipadgg fitavnhnsy ldplsyahyq
       61 yntgrvprfl akaglfrsgf vglmmrgtgq ipvyrettda anafraavta idkgecvafy
      121 pegtltrdpe lwpmqgktga arvalltkap vipvaqwgan damppyakek klrlfprktl
      181 rvqagppvdl safydrepta evlraatdvi maaiteqlav vrgepapaep ydwrkaiare
      241 rraareatka tqgagadrtp aepaaatepa vgpqqarstq qaqedesk
//
LOCUS       WP_457685234             241 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685234
VERSION     WP_457685234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25819
     Region          4..228
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mplravlwdl ddtlfdytgs dragvlrhlr tegildaygg eevalerwrt ametefarfl
       61 agevglldhr rgrartflgt plsdpeadaw fgrylahyea swalfpdsap alaalaplvr
      121 qavlsnaata nqerklaalg irthfeavfc adglghakpa eeafkgacka lgltpdevlh
      181 igdkldidal gardagltav wldragtgee ppagvrrias laelpellhg vigfgapsti
      241 r
//
LOCUS       WP_457685244             455 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457685244
VERSION     WP_457685244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..455
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46974
     Region          <324..455
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrgdyqqlvd eisaalgapa tledrdfgli afgahegddd evmdpvrtrs ilqrrssaav
       61 rawfeafgia raktalripp dpaagvfkgr iclpvrhrgi vhgyvwlldd ghltdlelgs
      121 rgtppdpria qametaarig alladearag selgdllrel laappdgqpa aaaalrdalr
      181 dslrftpgap ltlvavvpwd tsdtdaaplp slpgllaaca lpagggpadg paagadetep
      241 aarpgsgrng ragsavlphs aapvpalaal vrlrasgasa pahtvaehll rsprasagpa
      301 egraprggar ggsahppppr pgaagiglgt reltdlpatw realdaaraa haeprlgpit
      361 qwdaigpyrm ltalpgtapd paigpllapa haelartaev fldcagqasr tahalgihrq
      421 tlyyrlgrve kltgldlddg ehrlllhmal kaarl
//
LOCUS       WP_457685246             213 aa            linear   BCT 27-JAN-2026
DEFINITION  PRC-barrel domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457685246
VERSION     WP_457685246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  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..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /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=22050
     Region          11..>58
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnaplgdapq sltglhvvda dgakvgtvqq vyrddatnep ewitvrtglf gmketfipla
       61 garrtgdelh vphakatikn apridanghl dpseeeelyr hygmtrpgma apdaagptsr
      121 pgpratgdtg ppaptggern kliegpmaga gagagagtra gpqagdtgdt argkeqmpet
      181 gaeerergrh pgerekgrdd gtgggregpd rpr
//
LOCUS       WP_457685251             743 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457685251
VERSION     WP_457685251.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..743
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77714
     Region          8..712
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mtalarwclr rrivvivlwl aafagvavaa gvtgaaysnn yevpgtesgq asarmakafp
       61 ersgdsdtlv whtdsgtvrs aavkktmrht lekiaalpgv sevespygrh adgtgarqis
      121 kdghtayasv lfdrrtddld vdqvqkvvdt aqtasrpglq velggagial teapraqlpe
      181 iiglcaaavv lflafgslaa tflpiitala avgtasagit llshamtvad fapmlgmlig
      241 lgvgidyalf ivtrhrkglr eglpvdeaat ravavsgrav vfagatvcia llgmlilrls
      301 flngvalaas ltvvltvaaa vtllpallgl igmralsrre rrrlaeqgpr perttgiaar
      361 wsgfverhpk llgtvaaavm lalalpafgl hlgtsdqgnn patsttrkay dllagdghgs
      421 gfgpgsngpl tlvgtldgak driafdalpd rlrdtpgvar vsrpvfdggh stgvitvvpt
      481 sspqsrqtsd lverlrtevl peaggaatlr vqvggitasy ddfaslivgk lplfigvvia
      541 lgsvllllaf rsigiplkaa lmnvaavass fgivvavfqw gwgsemlglg sagpiepflp
      601 vimvsvlfgl smdyqvflvs rmyeewqlth nnrravrvgl aetsrvinsa avimiavfga
      661 fvlsgdriia mfgiglaaav aldafvlrtl lvpalmhllg ganwwlpswl drwlprisie
      721 pppepgavrl pgpqdgekpl vra
//
LOCUS       WP_457685261             239 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457685261
VERSION     WP_457685261.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..239
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=26204
     Region          67..222
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgkrdgekgg gqeaasaitr rralwigggg avaagtaafa grdvlaqwww rlpgndkprk
       61 agavdhrgaq wvaaspenyr radrpadygi drvvihvvqg syataldvfq dpdheagahy
      121 vvrkdghvaq lireldvafh agnrgyners igiehegfvd rpesftdamy assarltagi
      181 crrygfpadr ehlvghvevp gtdhtdpgph wdwdrylrlv raelrkpvqt gespparkt
//
LOCUS       WP_457685264             445 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685264
VERSION     WP_457685264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45442
     Region          23..410
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(30..31,34..35,38,70,125..126,128..130,133,155,
                     158..159,162,246,249..250,253..255,258,282,286,340..341,
                     345,349,365,368..369,372..373,376)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtedapggdg isgrrslrsl ggllaamavs ltgtrisaia lpwfvlvtth satrtglvaf
       61 cemapyvvvk altgplvdra gprviswstd lvsaaaagav pllhaldlls lplllplval
      121 igaargpgdl akevmvpeaa ergrvplera tglsgvterl aatlgpaagg slvallgplt
      181 glavnaacfv lgsliialtl prgmgrasee aplsqgewes gywrrfgagc rflrseplll
      241 tlivmvgvtn lldaafttvl vpvwaaesgh gpaviglnst aggaaavags lvaaavahrm
      301 rrrvvffagf llagapkfli lashapmwav llvfaaggfg agflnpvlaa lsfervprrl
      361 lgrvnalgda lawagiplgg liagaavtsf glvpvlllgg aayflttnla glrpewremd
      421 rprgpgarer rpgagdradg srltk
//
LOCUS       WP_457685266             221 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457685266
VERSION     WP_457685266.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 221)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23884
     Region          25..105
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mtdshekppg pdsgttaavl dskglralah plrlqlvgll rkhgpstatr laerlgvnsg
       61 tasyhlrqlg aagfveedae rgnarerwwr pvhqstsfnd pdlaerepda amaylqsvaa
      121 tytlrtqral nelqtmpraw rdtfdmsdrp lrltpaeaaa lqdelrdvvs ryrrdtpega
      181 aeapegaerv svityvlpep gepsapagrp vpegatgakt s
//
LOCUS       WP_457685270             282 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685270
VERSION     WP_457685270.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  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 12150045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="thioesterase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29608
     Region          29..276
                     /region_name="4HBT_3"
                     /note="Thioesterase-like superfamily; pfam13622"
                     /db_xref="CDD:463937"
ORIGIN      
        1 malvthgnse fdrdtavtrr apgvydahls agwtiiqavn ggyllalmgr algdalphpd
       61 pmsvtahylt asvpgpavir tevvrtgrtm stgtasliqf aedgseverl rvlaayghlg
      121 alpddvrtta kppaippyeh clgtdsspgg rpaipgstai aerlalrldp atagwavgap
      181 sgkgemrawf gladgrepdp lsllltvdal pptafemgls gwvptvelta hirhrpapgp
      241 lrvaittrnl aggfleedae vwdsedrlva qsrqlaravl qg
//
LOCUS       WP_457685272             332 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685272
VERSION     WP_457685272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35456
     Region          30..328
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtapiettga aaeaqpeavl kgvegkrieg rslgqiawlr frrdkvavag aivvilliai
       61 aalsrplqsl lgldpnspnq slidpnttlp kgdfggmsgd hplgvdpkfg rdllarileg
      121 swvslivafg atllsvaigt vlgvvagfyr grvdafisrm mdvflafpll lfaiaisasl
      181 qggafglegl plhisvlifv igffnwpymg rivraqtlsl rerefvdaar gmgargpfil
      241 frellpnlvg piivystlli psnilfeaal sflgvgiqps qaswggmlnq avkyyevdpq
      301 ymivpglaif vtvlafnllg dglrdaldpr sr
//
LOCUS       WP_457685280             630 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685280
VERSION     WP_457685280.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 630)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 630)
  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 630)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..630
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66871
     Region          54..625
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttttgrps dgpedhpgar prpaphppep gdpapdafaq dalpapkgas rsllasllap
       61 hrrrvgavav llllqqaavq agpllvayal dravpalrag dhgpllavav agvlcavlsg
      121 glqfgfiela arvsqdvlld lrgrifrhgq alsldfhery tsgrlisrat tdveslrell
      181 deglqeliti vlstvyitvt lvwldwglga aalasagpla llvrsyrrrs hrahsaksta
      241 maavivkfte tlngirpvqa frrerpndaa farlnhrher ingdtllema ryvvasrlva
      301 naavaaivlw gayrvatggl algvlaaavl ylrrlydpid rlgmflnsye saaaslqkia
      361 gllarrpgvp epaasaalpp vaagrpgrev tfrdvrfayr tggevlprfd ltlaagttva
      421 vvgatgagks tlakllarfy dptegqvlld gvdlrelsta vlrrgvvmvt qeaflfsgtv
      481 adnialgrpd atraeiegaa kaigahdfit alpdgydtdv rkrggrisag qrqlvgfara
      541 lladpavlll deatssldip geravqramd tvlegrtalv iahrlstvnv adrvlvmadg
      601 rivedgppde liarrgrfaq lhqawrdsvg
//
LOCUS       WP_457685283             527 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457685283
VERSION     WP_457685283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  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 527)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..527
                     /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=57175
     Region          <3..479
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          169..387
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtpwrrpdar qlharrlyar apglvlwllv cgppalafgs lahthlwata aafpllgvcv
       61 llrrrrplta lalpiapslv isldlftvay caalavfgyl agirmprarp alwffsavaa
      121 gglplsavvg rtvwpwfsll ltlllnvmlp wllgryrrqy aelartgwql aermereqqa
      181 vadrtrlrer ariagdmhds lghdlalial ragalevdpr ldadrqaaag elraaagtat
      241 erlreiigvl rtddesaprv padesverlv drarasgmtv tleeaddtga rtlpamtgha
      301 lhrvvqeslt naakhapgaa vrvrigraag qvrvtvanta rpdgpaadpv sggsglvgld
      361 ervrlaggtl ragpapeggf tvsarlptad gtpaeplerp eptaaereld raqrqvqrrl
      421 rqtvivplal laalvvltst fhlvspswtv lerehydalr lgadrsrmds llpffaldap
      481 pdgtpppphg wtceyysvrp gsdtayelcf tdgdrlvkks vvhrrdr
//
LOCUS       WP_457685292             411 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate kinase [Streptomyces nigrescens].
ACCESSION   WP_457685292
VERSION     WP_457685292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011301
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="acetate kinase"
                     /EC_number="2.7.2.1"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008776 - acetate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006085 - acetyl-CoA biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43130
     Region          8..411
                     /region_name="PRK00180"
                     /note="acetate kinase A/propionate kinase 2; Reviewed"
                     /db_xref="CDD:234680"
ORIGIN      
        1 mtatatrvlv lnsgsssvky qlldmkpdsa ggsaagtrla vglverigee tsrlahtpla
       61 tggdkreteg piadheaalk avaaelsadg lgldspqlaa ighrvvhggl kftaptvidd
      121 avlkeierlv pvaplhnpan itgirtaqal rpdlpqvavf dtafhttmpe haaryaidva
      181 tadahrirry gfhgtshayv srktaellgk dpsevnvivl hlgngasasa vaggrcvdts
      241 mgltpleglv mgtrsgdidp avtfhlkrva gmseddvdvl lnkksglvgl cgdndmreir
      301 rridegdera rlafdiyihr lkkyigayta vlgrvdavaf tagvgenaap vraaavagle
      361 emglavdadl navrsgkprl ispeyarvav avvptdeele iaqqtyalvn a
//
LOCUS       WP_457685285             553 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457685285
VERSION     WP_457685285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
REFERENCE   7  (residues 1 to 553)
  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   8  (residues 1 to 553)
  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   9  (residues 1 to 553)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20761992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..553
                     /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=58152
     Region          66..181
                     /region_name="sCache_3_2"
                     /note="Single cache domain 3; pfam17203"
                     /db_xref="CDD:435783"
     Region          217..548
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mrlprprppr rlrgprslag qlfamqvvlv avvvmgcavf ayvsagrqae etarrqataa
       61 atavadspav vaaarskdpt aalqpyserl rrdagvdfvv imspkgirwt hpepsaigkk
      121 yfghigpalr geifpethlg vlgpsvrvva pvrdpghggr italvssgit iktisaqlrd
      181 qvlalvgvaa aalvlgglgt yvinarlrrh thgmnaqels rmhdyhqaal havregllml
      241 dgqrrvalin dggrellgls ddavgrrvte lglpepltet llapgprvde lqltservlv
      301 vnsapvsgge rrgsvvtlrd htelqalsge ldsvrgftea lrsqaheaan rlhavvslie
      361 lgraeeavef attelelaqa ltdqvvgava epvlaalllg kaaqanergv aliltpdsri
      421 ddgllppglp ardlvtvlgn lldnaidaaa ptqehgatep prvqvtarva dgelllrvad
      481 ngpgvaadaa eeifrrgwtt kpgtgaparg rglglalvqq avrrnggtvt ldrapeggar
      541 ftvrlplrag aar
//
LOCUS       WP_457685290             849 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685290
VERSION     WP_457685290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 849)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..849
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87739
     Region          2..846
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mlrtalrnvl ahkarlmmta lavllgvafv agtlifsdtv gsavkkasek nldgvavsvq
       61 aeaadnspdv gkdgkrttlv dekladtira lpgvesvrrn vngtatvagp dnvplghdwq
      121 nlaanfqpgk dghdprypll kgrgpaagne ialdeataka sgrkigdsvr latdgpvltk
      181 klvgivstdd pqvtaggslt lfdtataqkl flhpgqfdel vigaapgadq qaltakvsev
      241 lpkdratats gtdlaaeqsk mvasqneals qtlltfagia lfvgvfiian tftmlisqrs
      301 reialmraig asrrqvvrsv laeaallgli ssavgfalgt glavglravl eangagfpdg
      361 pvvispaavl salgvgvvvt vlaawlpsrk aakiapveal ntveappalr slvlrnslga
      421 vitglgiatm cyvstlkdad dlpiamvggm ltltgviila pllsrplvsl agvvttrlfg
      481 isgklakent lrnprrtaat asalmigltl itgmtvvgns agqamdkmta qglkadykig
      541 atssgldpkl sqkvadvpgv evaaplrntg fetpdsimsl mgtdlstigk vaqldftsgs
      601 lkgaggndia vsqkmakmkg whtgdtldat ffdkkkaklk ivgiyadnql lgdsigatsl
      661 aaphqlvpmv esllvkaqdg pseglekqir halgdspllk vqdhadlrke naadiemvln
      721 vsygllgmav iiavvgvvnt lamsvfertr eigmlraigl arsgikqmvr lesvvialfg
      781 aglgiavgvf cswaagnlvs qglptyelll pwgrlalfvl laaavgmlaa lwparraarl
      841 nmlesigaq
//
LOCUS       WP_457685296             456 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685296
VERSION     WP_457685296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..456
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46097
     Region          45..424
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(55..56,59..60,63,95,146..147,149..151,154,175,
                     178..179,182,261,264..265,268..270,273,296,300,353..354,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpspsgpaps grlpvcpdtg aadtgpqggp arpdgyravf avpefrfvfa ahllsslgvv
       61 vceialsvlv frltasplls altfalgllp yvvggtllsa vadryparrv lvgcdvlcal
      121 aaagmvvpgt pvvvllvlrc vlaaiapvfa gtraatlgei lgegelfvlg rsvirivnqs
      181 aqlagfaagg lllvvvspga vlaltagafl gsalllrlgt larpardgar gaergallaa
      241 slggirrlla drrvrallll twlppafvvi peallvayag llgvgpagtg llmcampvga
      301 vvaeslvgtf lgprararlt fpmgvfavlp slgfaaqpsl gwavlllvlt gtgisynfgv
      361 drwfvaavpd ellgqamtvm qagrmtvmgl amglagvgae yaplrvvmpa agvlgavcvl
      421 avifevrrte rvpvgadrac agavrgtdgp vpetgk
//
LOCUS       WP_457685302             868 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685302
VERSION     WP_457685302.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 868)
  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 868)
  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 868)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 868)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..868
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87826
     Region          36..>224
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          126..215
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
     Region          <252..571
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          <698..>860
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
ORIGIN      
        1 mdpnthrgpe eygeqgspae ppapafggaq sgstglarvv rlvsgpylvt vnpvdgseie
       61 pcppgerpaa pgrldpeera aaaraaappl ppgpsgfagh etaleerted terlvrllsr
      121 grsvrvtgps gsgrtrllda vatacadlap dgvvrlsgyh htstdllyal faavyrapqh
      181 rperaemlrm vaeigaivvl ddlefggaal delldatpec afliaatpdv aapsagshle
      241 evflggigrg acgrllerav drpltddees waadlwfese glplrfvqaa allrqydrlr
      301 aapgalddgy glfpeagqat adpaaedaep aeqpevplps lgeaaapapl lasrlteaar
      361 etlrfavalg gelphqahlp altqdthada algellacgl itpagshyrl aatvqdqlta
      421 agyadgapar ahtvaqhyaw waghpsvtpe raaaesdval aamgvltgsr esghasaavl
      481 lartaapafa aalhwsawer slrhgqeaar lagevaeeay fhhelgvlal ctgnldrara
      541 eleasiglrg vlsdrngava grralalvtd rtradsaaaa ttalpqaaga asasrraapk
      601 epaanpfdaa sapklrksrt eqtaqtliar gassttattg vpaatdsgag agkgvrrvfg
      661 garrnvvaag agallaavlg tvvtigatgg ddtpndkvnt eqttddsdgt dlpaeqpatd
      721 sslpptgpgt srpgtagqsd rpspspsgta psgspsapgt gsadptagpt epterptspt
      781 grptrpthpp tdeptgtpse eptepspsgt tptedptdkp stqspsqsas gpsagspsas
      841 gtsgttpsgg tpsdatatss gtesapvt
//
LOCUS       WP_457685304             251 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685304
VERSION     WP_457685304.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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 251)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26901
     Region          55..251
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mstllsdtal ifgryarqtl rsklqmlfgv lmpllyllff gplltdlpls ssgsswqvlv
       61 pglllqlalf gasfcgfgii vekrygvver mrvtpvsrla lllgrvlrda llfvfqavll
      121 vlaalamglr aplpgiligf afvavltval aslsyalaln vstpqefgpv inavtmpsml
      181 lsglmlpmal gpkwldvlsh fmpfrylvda vraafvgsya ssamlygvlv avafaalsvt
      241 yctrafrrsa a
//
LOCUS       WP_457685306             411 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457685306
VERSION     WP_457685306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 411)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /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=42556
     Region          137..407
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtarpraavg rpprfdvlia gggllgglll wtldlhggpp rlglpaaltl vslttmsaae
       61 lmrrtapmaa lalavpalal dlcagtlvat vlmftdvvya avlygpahva rripphsvlv
      121 tvlaaialaa lwqkpqvvma vigialitia pawtgimlrn hrdaaqaarl raeqiallae
      181 rdrdravage rarmarelhd mvanhlsaia ihstaaqaid dpaatrealg virensvqgl
      241 aemrrligll rgprtaegda epaatptldg lealieqart sgrssglafv lddarsptgp
      301 gtgphqaapa elaayrivqe sltnalkhaa pgevlvrlaq drggaltvav rspfadrpgp
      361 rapgtgtglv gmreraallg gafeagpesg pagrvwlvra alpaageevr r
//
LOCUS       WP_457685317             176 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685317
VERSION     WP_457685317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 176)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..176
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19779
     Region          23..156
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtavgregaa ddapetpsvr qvsrvvlldp ddrilllhgf epdrptdtww ftpggglegt
       61 esreeaarre laeetgitdv vlgpvlwkrh cafpfdgrrw eqdewyylgr tertathagg
      121 qtdlerrsvs glrwwtseel sashetvypt rlaellrtll degppdapvl leterv
//
LOCUS       WP_457685322             334 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457685322
VERSION     WP_457685322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  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 334)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=36151
     Region          2..310
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(21,209..212,215,265,283..287,290,293..294)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(51,56,85,129)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mkvrqlgthg ptvsplglgc mgmstsygvp ddaeslrtld ravelgvtll dtadaygrga
       61 neeflgrwlr srtaaqrdel vlatkfglrh daatgrvnev dtsaawvrea chaslrrlgt
      121 dhidlyymhr rdpavpieet vgamaelvad gavrhlglse ispqtlrrah avhpisavql
      181 eyslftrevv egemlatcre lgigivaysp lgrgmltgal aarddltaed arrrwprfae
      241 enidrnlrlv qavrttaesf gctpaqavla wllaqgediv pipgtkrrsy ldenaaaagi
      301 tltpeqtdql raavpadava geryplaale rlgh
//
LOCUS       WP_457685328             861 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685328
VERSION     WP_457685328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19095030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..861
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86104
     Region          41..483
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide)-like multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17504"
                     /db_xref="CDD:341047"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,165,
                     168..169,172,296,299..300,303..305,308,342,346,396..397,
                     401,405,421,424..425,428..429,432)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341047"
     Region          <614..>848
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mnrtttdqlp eraggtpavp pvsdpavggk rrssggvvpv lafsgivvav mqtllvpvik
       61 dlpvllntta gnatwvmtat llagavstpi mgrlgdlygk rrmlltslav mvvgslicgf
      121 tsdlvtmivg ralqgfamga iplgigimrd elprerlgsa mglmsssigv ggglalpaaa
      181 lvaqhadwha lffgaaglgv lsmlltllvv petavraqgr fdvagaigls aglvalllpl
      241 tkgsdwgwgs pttlvlfgva vlilvlwgvm elrladplvd lrttarrevl ltnlasitvg
      301 vafyaislvl pqllqlptst gyglgqsmvv aglcmaplgl tmmfvaplya riaarrgpkv
      361 slllgmlvia igygagtglm naawqtviia vvvgagigla ysslpaliig avdasetgaa
      421 nglntlmrsi gtsvssavig mvlahmsksv gpvtvptmag frvsfliata avligvalas
      481 flpsqrkasr ptlvaqstdg eaadaadtdg argaarpaae taaplaatlp apadapapaa
      541 paavavaavp aeltasagql aplvkpapsw aqpvterhta parpapdatt gvagagagag
      601 agadaagfrg rvldtsgspv pgasvtlidr qgrqagvtta dadgryalda ssagiyvltg
      661 aapghtpyaa satyhgkggs trvdlilapt grlggtllgg aegtplaggs vvvtdtegiv
      721 vtrttsgaeg swhvpqlppg hytlvlsavg hqpqaramel sggaperqdt rlqpmatvrg
      781 tvrgpggrpl tdaavtlved gtvaghtvtg pdgafafsdl rgrhytltaa gypphsapis
      841 ltagasetld lelaqqptaa d
//
LOCUS       WP_457685330             607 aa            linear   BCT 27-JAN-2026
DEFINITION  2-isopropylmalate synthase [Streptomyces nigrescens].
ACCESSION   WP_457685330
VERSION     WP_457685330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Frantom,P.A.
  TITLE     Structural and functional characterization of alpha-isopropylmalate
            synthase and citramalate synthase, members of the LeuA dimer
            superfamily
  JOURNAL   Arch Biochem Biophys 519 (2), 202-209 (2012)
   PUBMED   22033339
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11480026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..607
                     /product="2-isopropylmalate synthase"
                     /EC_number="2.3.3.13"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003852 - 2-isopropylmalate synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65376
     Region          38..602
                     /region_name="PRK03739"
                     /note="2-isopropylmalate synthase; Validated"
                     /db_xref="CDD:235154"
ORIGIN      
        1 mprttsadrt aaggfptlrt pagpvpadap awnpqrgsam pahryrpaqd rvevpltgra
       61 wpaarierap lwvpvdlrdg nqalaepmdt prkrrmfdll vamgfkeiev aypsasrtdf
      121 dfvrhladsg avpddvtvvv ftparrelie rtfaaieglp rtvvhlytpt aptwrevvlg
      181 rgraevrdlv ldaathmarl aaarpgadir fqfspevfnl tepdlvleic ngltdlwdas
      241 pdrpvthnlp atvevatpnv yadqieymhr hltrrdavvl svhphndrgt gvacaelavl
      301 agaqrvegcl fgngertgnv dlvtlalnlh tqgvdpmidf sdlstvrrtv edcirlpvhp
      361 rhpyagelvh tafsgthqda iskglahhar raaglgvpes eapwtvpylp vdpadlgcty
      421 eavirvnsqs gkggiahllq lhhgldlpqd lrpdfsrtvq ratddsgqea tpkelwelfr
      481 stylapgeeg pltldswsat epapgehrvv csfgggnaad grrryegsgn gplaaftdal
      541 aaaghpvgil syaehalapg pdsaavayvr criggatywg agrdtsvlma svravlsavn
      601 rakgevp
//
LOCUS       WP_457685338             126 aa            linear   BCT 27-JAN-2026
DEFINITION  hydrogenase maturation nickel metallochaperone HypA/HybF
            [Streptomyces nigrescens].
ACCESSION   WP_457685338
VERSION     WP_457685338.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Xia,W., Li,H., Sze,K.H. and Sun,H.
  TITLE     Structure of a nickel chaperone, HypA, from Helicobacter pylori
            reveals two distinct metal binding sites
  JOURNAL   J Am Chem Soc 131 (29), 10031-10040 (2009)
   PUBMED   19621959
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Hube,M., Blokesch,M. and Bock,A.
  TITLE     Network of hydrogenase maturation in Escherichia coli: role of
            accessory proteins HypA and HybF
  JOURNAL   J Bacteriol 184 (14), 3879-3885 (2002)
   PUBMED   12081959
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Olson,J.W., Mehta,N.S. and Maier,R.J.
  TITLE     Requirement of nickel metabolism proteins HypA and HypB for full
            activity of both hydrogenase and urease in Helicobacter pylori
  JOURNAL   Mol Microbiol 39 (1), 176-182 (2001)
   PUBMED   11123699
  REMARK    Erratum:[Mol Microbiol 2001 Apr;40(1):270]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="hydrogenase maturation nickel metallochaperone
                     HypA/HybF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=12905
     Region          1..111
                     /region_name="HybF"
                     /note="Hydrogenase maturation factor HypA/HybF,
                     metallochaperone involved in Ni insertion
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0375"
                     /db_xref="CDD:440144"
ORIGIN      
        1 mhemsialav vdqvesavrp agattvnsvr lqvgelagvv pdalafsfel acagtvlega
       61 elvtepvaar arcgpcadtw pvgmppqlsc pgcggatael msgrelqivs vcwndapvhv
      121 pthqer
//
LOCUS       WP_457685346             400 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457685346
VERSION     WP_457685346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10145376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="M20 family metallopeptidase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40991
     Region          19..378
                     /region_name="M20_ACY1L2-like"
                     /note="M20 Peptidase aminoacylase 1-like protein 2-like,
                     amidohydrolase subfamily; cd05672"
                     /db_xref="CDD:349921"
ORIGIN      
        1 msaaapspav ppralsaeva alrprmervs raihaepelk feefaaqkll tewlaeagfa
       61 vaapagglgt afvathegst pgpyvavlae ydalpgighg cghnliasgg aaaaiaavra
      121 lpdhpgtvav igtpgeemgg agkirlerag vfdgvdaavm fhpadrsltt rhglaaahlr
      181 vgftgvsaha akspwegrsa laaaqlflna ldslrqfmpp tarihgivtd ggqapnvvpa
      241 daavdlyvrd rtaasaealv arveraahgv amatettaev setgpmyadr rnntvlaerf
      301 gqtvralgld ivpgdpatpa gssdignlsq llpvihpyvq iaergtpghs eamreaaata
      361 yahdrteiaa tglarvvldl ltepgflsav raefdaaeav
//
LOCUS       WP_457685345             546 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457685345
VERSION     WP_457685345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..546
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57627
     Region          19..470
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 maesqvsgeg dgtdvpevqa qerrlrrdlg fwgltgigfs nivgsgwlfa amyaaqtagp
       61 aallswvgag llcglvalvm ielgasrpeg ggtvrwplfa sgrlvgtlig wstllsvggt
      121 aaeisaimqy aahylpgiyn ghtltlsgla laaglstvlt alnwfavrmf aqlnnlvsvf
      181 kivipvvtvi aliasgwhsg rltdhggfap ygyvacltal agggivysvn gfqapldfsg
      241 etrnprrtip aavltgigla vlmylalqla flftvpehll gngwqgvsfe spfgqlalil
      301 nlhwlaslly adavlspggs ayvgvainar htyalakngt iprffmkvne rfgiprrala
      361 inlvvimvfl lpfggwqdiv svmgtmylli yaasavavav fraepggrta gwipglgwia
      421 plsfvvasef iywsgwhdlr lalplvlggl liflvmrrsg ardkaalesd gagpsrslga
      481 elrtgawlva ylialtvlsw lgtfegsgrl papydsvtva alalavffwa vrsgvrhlev
      541 arpiav
//
LOCUS       WP_457685353             428 aa            linear   BCT 27-JAN-2026
DEFINITION  four-carbon acid sugar kinase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685353
VERSION     WP_457685353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11465537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="four-carbon acid sugar kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /calculated_mol_wt=43012
     Region          3..415
                     /region_name="OtnK"
                     /note="D-threonate/D-erythronate kinase OtnK and related
                     C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate
                     transport and metabolism]; COG3395"
                     /db_xref="CDD:442622"
ORIGIN      
        1 maqvlvigdd ltgsnatgal yarlglravt vgdlaqvary adrvdvlvvn tasrhwtpar
       61 ayaavraaae tagevplvvk rvdttlrgnp gseldavadv laarepaari rtlavpafpd
      121 agrstvgglh lvdgvpltrt avandpfdpv rhsrvaavlg aqsgrstgel aldvvergpd
      181 avaaalresp adivvcdate nahlgtvaaa aarlaaedri rwialdsgpf gaalaaelgl
      241 rpeggapatv lavvgsvtdr trtqlartet algarwadld paapdpgrvl aalraaaaeg
      301 atvlgvrvap eptgaasvpd pgtaarilra laeiarrava elcpgglyas ggdvaaavts
      361 algadgfaie tevlplaiag hlvggphdgl pfatkgglig gpdaardcle hlraactrrt
      421 lgptsiat
//
LOCUS       WP_457685355             440 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685355
VERSION     WP_457685355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47204
     Region          21..418
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,252,255..256,259..261,264,293,297,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtetgpqpip qsppsaipak rwayvipvaa imymlayldr nnvsvilpym hgdlelsnad
       61 kglvggiffv gyvflqipaa ilaqrwsark tvlllmvawg laasltglvq tksqfyvarf
      121 vlgffeggvw pavlillasw fplreraran alwmaclpls svlmaplsgw mldhaswrwv
      181 lvlqgvppll wavvwwfava drpdrarwis raeadhvers iaadeaakps agsgsyldav
      241 kqksvlvlig vyffwitgfy gfnlwlpsvi kelthdgspt evglltaipf tvalvvmian
      301 aawsdrtgrr rqavavplvv giaalllgqa vdgalprmll lcvtaaavya pygpfwaipg
      361 qllrfevvav amglinalgn lggfagpylv gwltdvtgss vtgfavlsgf lavavalvtl
      421 glrpsarpvr plsgqaaega
//
LOCUS       WP_457685365             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685365
VERSION     WP_457685365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27113
     Region          34..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtstettpaa paqtaapglr ltlddaalgr pgapvldhln ldvaageilt vvgpsgcgks
       61 tllrtlagll pllggrltqd gepvggpaad ralvfqedal lpwrglranv elplairgva
      121 raqrraradd wlarvglteh aarlphqvsg gqrqrtqlar alagrpravl mdepfgalda
      181 qtragmqqll vtalsgtrat vvfvthdvde alflgdrval lgsgrvldvp rprlrgahsd
      241 patvalrrev lasldgrpgs
//
LOCUS       WP_457685366             297 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685366
VERSION     WP_457685366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..297
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31830
     Region          14..268
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 msapattagr tgrtgprrgn wiryaritaa vlaalagwql laqfrvnlwl rfsqfptvte
       61 tarefarrlg tatywqdvsd sltrivggfa laavlgvaig talarspvvs dlcgpllevl
      121 rpipaialvp vaillfpsne qgivfitfta affpvtvstr havqaltpvw eeavrtmggg
      181 rwrvlrsvvl pgalpgilgg lsvgigvswi cvisaemisg eygvgyrtwq dytivdypgv
      241 fvgmatigll grltstvver lgrrltrwlp rtergpgasa ggrarwrtvr ttvgeps
//
LOCUS       WP_457685373             386 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            nigrescens].
ACCESSION   WP_457685373
VERSION     WP_457685373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42058
     Region          19..378
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mhpeatttpt aptapdapgq alsaryytdp aaaaaetqri fakswqlvch esdlpgpgar
       61 laatvadrev lvvrtengtl aghlnvcrhr gtrlvsapea sgkalrcpyh gwtykldgrl
      121 vgapearqip cldkpalglf pvrvesflgf vfanldpdav plaeqcagla eavghyagtd
      181 lvpvgrsrih dlagaevqha nwkvavdnyl egyhvpvahp glmrlldyqg ytseidesyv
      241 lfasplrdkp ssnwaerlyq rlaspmpglt eadrrvwrya viypntlidf ypdhvlawta
      301 iptavdrvav pgafytrrgt sartrlarrl nihigwitnd edaelvarvq kglgtpgfep
      361 gplsrreaav gwfadrvrtd lggamr
//
LOCUS       WP_457685379             331 aa            linear   BCT 27-JAN-2026
DEFINITION  D-cysteine desulfhydrase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685379
VERSION     WP_457685379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10012093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="D-cysteine desulfhydrase family protein"
                     /EC_number="4.4.1.-"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33066
     Region          10..318
                     /region_name="PRK03910"
                     /note="D-cysteine desulfhydrase; Validated"
                     /db_xref="CDD:179673"
     Site            order(52..53,81,190..194,275,304..305)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107202"
     Site            53
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
ORIGIN      
        1 msadsgtprr aalatwptpl epaprlaral glgaedlwvk redltglggg gnkvrklewi
       61 cgaalaegat tlvttgaaqs nharltaaag arlgldvvlv lagaagssts gnlvldglfg
      121 atvvwagevg gtqlaaaaee vaqrlrerga vpgliplggs splgaygyae cgrellgqap
      181 dldtvvvalg sggtmaglvd tlgpgkvlgv dcgavrdpad tvtglvtals gtvhapetlr
      241 lrreqvgagy stlteesmda ltlagrtegi aldpvytgra laglraavrd gsvapgqrtv
      301 llhsgglpgl fghsdavarc qealtvlpvh e
//
LOCUS       WP_457685385             205 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457685385
VERSION     WP_457685385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22104
     Region          6..187
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mdikaaiaae rreladlldg ltagqwdapt lcagwrvrdv vahmsmgfry slpkvaaell
       61 rvggnlhrmt drcarrdaaa astrelagfl rehahhpwkp pvggiaaalg hdvvhgldit
      121 valgldrrvp edrvrlllqk itpgtarffg aglrgiqlra ddldwsfgsg tplsgaaqdl
      181 llvaygrklp pgrlhgerhq hfvag
//
LOCUS       WP_457685383             900 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685383
VERSION     WP_457685383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..900
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92989
     Region          33..444
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(40..41,44..45,48,79,129..130,132..134,137,157,
                     160..161,164,227,255..256,259..261,264,335,339,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          <649..>879
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mstatsppga gteeisgpgv lshrqiltil sglmlgmfla aldqtivsts irtisddlhg
       61 lsqqawatta ylitstiatp lygklsdlyg rkpyylaait ifvvgsvlct fstsmtglaa
      121 fravqglgag glmslalaii gdivpprera ryqgymlgtf atssvagpli ggalagqdql
      181 lgitgwrwvf lvnvpigiia lfvvakvlni phtrrdhrid wwgaltlsvg vvplllvaeq
      241 grewgwdssr siacyvigvv giiawifver wigddalipm rlfrngtfsk tsvlsvligm
      301 gmfggmlmip qylqivkgas ptssglqmlp lmagmfiasi asgqitaktg rykifpiigt
      361 almiaamllf hfrvqwdtpl wetmiymlvf glglggcmqt lvlavqnavp prdmgvatas
      421 stffrqmgat agtavflsvl fstvgdkisa afkdavster fqaalhdpav lhdpankpvl
      481 dmlkhpgnad ssgvlsdssf iqhldprlae pfkrgfadsm htvflmgaiv valafvlmwf
      541 ikevplrqis glqaraqada eadadavaks aksaggavea vdgaaggaga dsagaddaav
      601 tpapaessga sgssgssdpa gtpgadpvpa lsgasappad rgfgttgpei rgtvrdgdgr
      661 pvaraavtli svdgrqlgrt steadggyal pttgagtyvl igsagarhpq avtvvvsgep
      721 vsfdlalgga aglsgevrae kgdapvpgal vvatdvtgev vasgvagpdg gfafgelapg
      781 sytlavsaer hrpsalpvev tsgnrnwyev rltpgaqvrg tvrtvhgspv ddarvtlldp
      841 agnvvgtats gqdgeyvftd ldsgeytlia sgyppvatpl rleaaghgef dielghdpvr
//
LOCUS       WP_457685387             676 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457685387
VERSION     WP_457685387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..676
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74064
     Region          1..676
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mttsnpffep sdlpyelppf arirndhflp aftrgmadql aevaaigaca gpptfentve
       61 alersgavlg rvcrvfsnka asdtdeeiqa leveitprla ahedllllds alfgrldalh
      121 aqreqlgldg eqlrllerhh tlrvragarl apeqqrrlre lnahiaalct efdqnlrvat
      181 adaalvldra eelaglpadq iaaaaenara lghpgkfvls lknfscqtel aaledpalre
      241 rllaaslgrg idsngpiavt larlraerat llgypshaaw evadrtagtt daveellgrl
      301 vapavanaer egaalaeaag vaqiraadwq yyservrker ydldaaalrp yleletvlhd
      361 gvfhaaglvy gitftrrpdl vsyhpdahvy evhdadgspl glyigdfhar eskrggawmn
      421 slvvqshllg qrpvvvnnln vakpppgepv lltwsevntl fhefghalhg lfsdvrypll
      481 sgtqvprdfv efpsqvnevw adwpevlahy arhhltgepm paelparlre aenfgagfrm
      541 vehqaaavld wawhtlsadg dvpgedevea feaaalerhg lamaaippry rtgyfahifn
      601 hgyaagyygy rwaevldadt vrwfrengrs iresgeifrr ellakggsvd plaafravvg
      661 rdaeigplla rhgltg
//
LOCUS       WP_457685397             647 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457685397
VERSION     WP_457685397.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10147902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..647
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=66966
     Region          56..541
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(195,198..203,205..206)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(198..199,313..314,330..335,361,429,441,444,535)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          571..630
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mtqpmtarta apttaagagr htpqpgtlsi ahgarpatdg aagvlarfee wvrrspeapa
       61 vidgahswty gqigsaadev aqalrarvrp gdlvgvcldr saalvvtava larigavylp
      121 lgprpgerrt davtedidvv cligdpgllp prhrtadrmd ltlpgegana tatvvaafaa
      181 pgpaahsapa gtfyavltsg stgrpkavav gepalgglld wyrattglgp gdrqslligv
      241 afdphllelw ggltsgaalv papdevrwds vvladwwrta gvsvsvaatp mveplldrpw
      301 pqdlrlrhlm tggdrmrrhp gaevtatvhn aygpaeatvi atthamhgtd gaagtdsapp
      361 igrpvpgvtv ivagqdgrpv ergtegelli ggsglalgyl dpeltarrft avpeglelpg
      421 vervyrtgdr vrmaadgqle flgrlddqvk isgvriepae veaafeqdpa vlsavvtapr
      481 sadgrarlva yvraaadsgl taeallpalr twlpeqavps dvrivgsfpl dangkvdrae
      541 ltrraaesaa prpggtapdd gapagatpge rlvlsavrdl ldrpgtslad nfteaggtsv
      601 laarlltvie kesgvrlrap ellrqpdlra vallvdqrca srqpaga
//
LOCUS       WP_457685398            1064 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457685398
VERSION     WP_457685398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1064
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=113292
     Region          2..1064
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mlplsssqei vwlheqvqpg sraynftaal dlwgtldtea lrhglaatld rhaglrlelv
       61 avagampgqr vaeacaprlr tmdlsgaadp eaafqellrt eaetpldtye apllrwtlvr
      121 lgddrhrlih vehhlihdgh sfaillrdvf tvyrgrvlge pvelppapsy adhvrarsgd
      181 qataerqegl efwsgalrem sydmplpgla kpgarrrhhg gqlrqsigad laerlrahar
      241 trgltpfatl lglfaemlrr hsgrsemvig tavgnrprgf eetvgmfvnt iplplrldpa
      301 apaeesmdev tdtliralph qevpiqeltr alglhtsgad nplfgvmfsa hdaelpdidv
      361 pglditlfeg fntgttrfdl dvvllpddrr gvgprhgaag mtlvwdydad lfgedvakll
      421 agrfldllra yldapgtala dlapppappa lpaaapqapr hdpldpatah drslpallvg
      481 arritygdla drvaalaqrm qaagvtagqp vaavlprgad svvtllaclr travycplsp
      541 sdpparltll lerlnpalvl tsadtavtvp dglpsatvdt avlpparaae avpgaaylih
      601 tsgstgipkp vavgraalen hltgvagrfg lgagdrvllf aqpsfdvale evlpslyaga
      661 clvaperevp tgtelaella aarvtvanlp tsyflatrqe mrpalrdghw aprllvlgge
      721 rlpadalraf ladtdstvln vygvteaais stvheitrdg ltdgaeiplg telpgervhv
      781 ldahhrplpd gavgelaiag aglaegyagn pevtearfrr iealggervy ltgdrgyrgr
      841 dgllyflgrl dhqvklrgyr ieleeveaaa saalggrsca vvldreapgg prlvgflesa
      901 dedgpwdeqa lhtelsrrlp salvpgrwar ldvmprlagg kpnrtaltrr aaalepaapa
      961 apaaepgdgq paepadpmta llvegwreal ghgrfdlssd ffrsgghsll aaqlaswlep
     1021 rlgqrpplrl lfqnpvltdq aaalaavgta tpvpaasttv tesr
//
LOCUS       WP_457685400             435 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685400
VERSION     WP_457685400.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44332
     Region          34..394
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(36,69,124..125,127..129,132,152,155..156,159,235,
                     238..239,242..244,247,271,275,331..332,336,340,356,
                     359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpaiprpaas gplrlrdfrl llagaaagql gaqvtlvalp lvavlelnap afqvglltaa
       61 etaafllvgl pagawvdrmr klplmiradv vravamasip laavadvltm aqlylvalvt
      121 gvatvffdva hqsflpqllp kdhlvsgnga letirssaqv agpglggglv qllgaslaiv
      181 adaagyvlsa lflwgikqpe srpsrvagss lrqdiaeglr fvcghrllrv iavttglanf
      241 ftatlmatqs vflvrvlgla pgvvglvlaa savggltgal cagrlaarlg qariiwlsal
      301 atgpfallwp lsgrgagaal favgsgvvff gavvynvaqv sfrqalcppr llgrmnatlr
      361 flmwgtlplg alaggalada fgartalawc aagilvvplp lllsplrrmr nlpaadaaed
      421 apadstdpae pasvg
//
LOCUS       WP_457685411             501 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces nigrescens].
ACCESSION   WP_457685411
VERSION     WP_457685411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54206
     Region          99..501
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mglfeaagar vidspagtaa eldrvpergg kgrnkpterr lrqlalavdt ggvllpvgll
       61 cavtqqpqpl ltaalasasw lavgasknry sreepagdda vlpvlrdwlt mlgvlavvcv
      121 aarvevslkv cvlallpcla lgvarrklvh ryllairrra qalrrvlivg eagavdvvla
      181 elahrtdhey vvvgsclvge ettdsavpvp arlasdgntp eaaldgetvl gcaaeldadl
      241 vfvapgrqls aarvrrlawa lhdggrnlai lpglidvsqh rvrlakaagl tvmhidpaar
      301 rgmpvllkqi tdrlgallll mllspvfalv aaairltssg pvfywqvrvg qdlmpfrmwk
      361 frtmvvtadr mrtaleasne hdgamfkirr dprvtpvgrv lrrfsldelp qlfnvlaghm
      421 slvgprpplp eeverydgte lrrlsvkpgl tglwqvsgrs dltwdetval dlsyvdnwsy
      481 trdigvlvrt vravvdgrga y
//
LOCUS       WP_457685420             386 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685420
VERSION     WP_457685420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /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=40721
     Region          17..359
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrelirriaa atpadrdrgv dalralailg vmlghwlvta lvadsgtvrv vsplhqlpql
       61 tpaswlfqtl avfflvggqm aakswaavra rggtyrrwlg artvrlfrpv vavvvvwgvv
      121 agallvagag lqtvhtlgkl alsplwfllv favltaatpl varlhplwpl tvvlhidlir
      181 fgmggpvwlg wanvaagwlv pyclgaawar gglrgratgw vlllggaatt aglvlwagyp
      241 aamvgvpgag isnlnpptla avtfglaqcg aallllgplr rilrrpavwa avalmnlsam
      301 tlflwhqtam mavtavgllt ggflpglhtl pdgagwvlar lawlpvfala llvcwaafrt
      361 yehgrrggtk vvregrpaea ravrsa
//
LOCUS       WP_457685425             116 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685425
VERSION     WP_457685425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..116
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=12552
     Region          21..>85
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mgheakkkss ykgtsskail hqydflgdfy rltlgpelvf syglreegdt ldsaqtrkld
       61 yhaeaahavg adrvldigcg ygsllhrrrp vpgvlpalpf laaagrapvr tgqrle
//
LOCUS       WP_457685423             546 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457685423
VERSION     WP_457685423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..546
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59641
     Region          10..494
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mhtaprspsp saapqldavi vgagfsglyq lyrlralglr trvleacddi ggtwyrnryp
       61 garcdvesta ysfsfspeld qewewserya tqpellrylh hvadrfdlrk ditlrtrvtg
      121 avydegghtw qvttdtgetv itrfvvlatg cmsavkepdi pgagtfagra lhtadwphed
      181 vdltgrrvav igtgcsgiqa ipllaeqaae ltvfqrtpvy alparnrpls aaetaelkar
      241 ypefraaqrr skggtlfepp trsalevdea erratyeegw dsgvlsgllr tytdilvdra
      301 anetvaefvr skirsivtdp etaetlsprt fpfgtkrpcl dtgyyatynk phvsvvdltk
      361 tpiveitprg irtsdrehav dviafatgfd altgsqvamd ivgkggttlr ekwadgprnh
      421 lgllsagfpn lftvigplsp svlsnavvai eqhvewitdc iahlrrngit eidatpraea
      481 dwcahvadla aqtlypsvds wymganvpgk prvflaytgg leryraecda aaengyrafa
      541 lsggad
//
LOCUS       WP_457685429             224 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457685429
VERSION     WP_457685429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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 224)
  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
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Bujnicki,J.M.
  TITLE     Phylogeny of the restriction endonuclease-like superfamily inferred
            from comparison of protein structures
  JOURNAL   J Mol Evol 50 (1), 39-44 (2000)
   PUBMED   10654258
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="restriction endonuclease"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23465
     Region          100..205
                     /region_name="COG1787"
                     /note="Endonuclease, HJR/Mrr/RecB family [Defense
                     mechanisms]"
                     /db_xref="CDD:441393"
ORIGIN      
        1 mrqltlvfgl vtsgvlgigl vlktlqgstl rpgavallgl vlvatalvvi rgrkrnrtvp
       61 lgagttgsqa pqaasepglr seegvpdeav yladdaelgp defeqvvall cerdgcreir
      121 vvggandlga dviavtpdgl rlviqckqyg edhkvgsqdl qrfggtcfai hgadiaavvt
      181 tstftepave yaeqsgircl dhdmlwawea gtgpapwqsg rrsm
//
LOCUS       WP_457685431             385 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457685431
VERSION     WP_457685431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..385
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41284
     Region          1..363
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mdtlravlae gygalsvell ladygatala pfgavgtaaa pvpvansaeg rafgsqqprq
       61 rsrhgdvveh hlpvtvrger tgiltvrlpv ersvpeavdg laqaagllgh elmvaerdtd
      121 vyqrarrisr ltlaaemqwq llparacsae eyaigahlep aydthgdnyd wasdadeltl
      181 avtdgmgtgv dasmlthlav nalrnarrag isiedqaala dqalyaqyrg aayvstlllc
      241 fdlatgrvqa vdagspqlwr lrrrtierie lepqmplgmf eethykaqef evlpgdrlli
      301 vsdgvyaahs pqgeayaera lartlhagrl lpaadvprav lrdlaayrda eslddslvlc
      361 vdwfgrqgdr pagtvqaagt gdgar
//
LOCUS       WP_457685433             433 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457685433
VERSION     WP_457685433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46191
     Region          31..425
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtphtfhnlp glrravrelc eahrlpshhg arlllsvsrt ataafdaggp vrlevveqsv
       61 pdgekllavt lhtgqtaasl sltdlplrgq atpdgtiawh lplgegedsp rpaavaaphg
      121 avpaqshtre sdgavayeae iaalegdlga alsrvdtltt elhrlkdela etnsgvlaly
      181 iqleerderl rrahgqilre ledalrpppi tvsglefavh yapadtdapt ggdfydwlll
      241 pdgtvhitvv dalghgvrst rsalnvthav rtlaleghpl esivarthdi lapfdpeima
      301 tvllaridpe tgalrlangs hppalvvrad gtadylevrg rgigfplpgs esvledtlhe
      361 gdllvlytdg ltesrrdpie gearlvksaw aharrpvdev pgaiakdmht vilhpddtla
      421 lavrragnpq gsh
//
LOCUS       WP_457685436             389 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457685436
VERSION     WP_457685436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41733
     Region          1..383
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtdridmgaa lrgalphall dtvrdhlasa ygatsvhlfl tdyggtvlsp cdspeggegs
       61 lpiagspegr algsqepreq qaphgeavdh hlpvtvrgdr igiltvrlpa grstpavlde
      121 lrqvagqlgh eilvaerdtd vyqrvrrvsr ltvaaemqwq llparacsaa qyavgaqlep
      181 ayavhgdnfd wasdgdelil tvtngmgqgv dasllthlav stlrnarrag vgladqaala
      241 dqavyghyrg rshvstlllr vdlatgrmei vdagspqmwr lrgksverie ldkqlplgmf
      301 eeshyaaesf tvepgdrllf vsdgvydaps prgrkyaega laralhatrl lpaamapgav
      361 lrdvaeyraa etlddalvlc fdwfgndlr
//
LOCUS       WP_457685441             413 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685441
VERSION     WP_457685441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42123
     Region          9..379
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,136,
                     139..140,143,214,217..218,221..223,226,254,258,307..308,
                     312,316,332,335..336,339..340,343)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 merslragrl atftffglng fvmgmwivhi psvehragig havlgwllll lgggafvgmq
       61 lvgrltdrfg arrvvpvsga lcslavtlpg latdgwtlga allvlgfgng cldvsmntha
      121 vqvergyrrp vmsafhavfs iggvfaalvg artlslgwsa aatlaatslf glvisafaap
      181 allppasara anpaaargaa prtppriwal aalammlmlc egvandwsvl dlrevldapp
      241 ataafaygaf stamtvgrll tdrvaarigp vavlrygasl aalgltavvl spwiplalcg
      301 wavfgaglsg cipqlfsaag hadqdaagan vsrvaglgyl gmlagptvig plthlvplnl
      361 tfllpvafca vaagtarlle prevtaagsa yvhprpeaga vprrglegda dgr
//
LOCUS       WP_457685443             329 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene/squalene synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685443
VERSION     WP_457685443.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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 329)
  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 329)
  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..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /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=35616
     Region          16..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtareldaag vtdprlreay ahcrrlnarh gktyflatrl lpagrrpavh alygfarwad
       61 divddpatgh ttadrahald alqrclddgl rggastepvv ravahtaavy didhrhfadf
      121 mtsmrsdltv tdyptyadlr rymhgsaavm glqmlpvlgt vvpqeeavph aaalgiafql
      181 tnflrdvged ldrgrvylpa dllaahgvdr allrwsrdtg lpdpritaal aaaaeltrgv
      241 yreaapglam ldpvsrpcir tafvlygail davrddgyav lhrravvsrr rraatalggl
      301 arlaaaratv rppgvrrggv phyaqeetp
//
LOCUS       WP_457685449             178 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685449
VERSION     WP_457685449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18976
     Region          24..177
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 madkgapisv tqpstletrg pgsvkvaldi ngvsrvlnle prvslldalr eqmaltgskk
       61 gcdqgtcgac tvwvdgrrvl scltlaisce grevttiegl aegdelhpmq raflehdafq
      121 cgyctpgqim savallnegh agtdgeitew msgnicrcaa yphirsaire mrdrktgq
//
LOCUS       WP_457685455             519 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685455
VERSION     WP_457685455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55948
     Region          131..>315
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          406..501
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 msafrtprwp raalsgmaaa allsavlpta sparaadrsg ppvparyahq rlnwqpcaak
       61 pslecarmtv prdwhhpgag adlsvavsrh raadparrrg vlmmaaggpg asgltrpadf
      121 aarspavgaa ydvvgfdqrg vgsstpvrcq tdaefqdfya hdfrdrspaa lrgvldrsrq
      181 lvagclrrsg dlipwltteq avrdmdlfra llgvrkisyy gpsyatwlga yyatefpqrv
      241 eravldsnld fsgtwqdveg gqprsfqrrf eqdflpwiar ydatyhygrt aaeakarwea
      301 rrralrdhpl tvgsltigpn qldnatlqni ynagqqfpql asalsaldhw psatpaertl
      361 agkvfgnyls pgfaaaffsv tcndtpwrrd lghwirrsae dtaahplaga relayaatca
      421 swpvpaaprv rvtgkglptt lmlnsvhdpa tyyegalaah ralrgsrlvt vtgggdhgqy
      481 qngnacvdgi vdaylldgaa pehdvacaag plpvppgrg
//
LOCUS       WP_457685457             382 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457685457
VERSION     WP_457685457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39589
     Region          13..377
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtdalslvde wgpektvvvs hrrtgmkgvl vidntargig kggtrmspgv tveevsrlar
       61 vmtwkwaavd lfyggakagi vadpaardke avlrafaral snevpreyvm gldmgltesd
      121 aaiiqdelgd rgaavgtpeh lggvaydklg vtgygvaeaa daaarhqglp lagsrvalqg
      181 fgavgsaaaq rfaelgativ avstahgvry dpsgldvgal laardehgdh fvtrhsagta
      241 lpsgaeltvd cdilvpaalq dvitrgtahe ikaklivega nlptsadars ilaergitvl
      301 pdfvanaggv vaaafamdar ysgfrpgtsg ifesvsarlr antvtvldea qqqditphaa
      361 grrlaeervr tamqskgrip rg
//
LOCUS       WP_457685464             305 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Streptomyces nigrescens].
ACCESSION   WP_457685464
VERSION     WP_457685464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31875
     Region          2..266
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 mprraasfqq ipvsdadagp yaltagpdga lwctlvhagq iarltpegql dryaldsasc
       61 gpsvitsgpd galwftrsqd hrigritvtg evtsfplptp gsgpygmvsa pdgalwftql
      121 hgdrigritt dgrvtefplp lsgafpsaia agpddalwft lnqahaigri sfdgeitlhp
      181 lptenaapvg itcggdgalw fveigagrig rittdgeide fplpdpasrp haiiagpagd
      241 cwftewgsnr igsitpdgri eeydlpiaas ephglafgpd galyvaleig avvrlalqge
      301 rgvrh
//
LOCUS       WP_457685470             415 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685470
VERSION     WP_457685470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43789
     Region          1..412
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(1,27,110,406..407,410)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
     Site            order(12..13,15,168,171..172,176,201,259,320,322,324..325,
                     328)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(12,259,320,322,324..325)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            13
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mhiliatags hgdvapytgl garlrqaghr vvmatharsa etvrrsglgf rplpldryat
       61 sgtgsqqgdg sgkgssgagl skveqiklar elapemadav aeacasgaev vllssslapl
      121 glvaaeglgl pslgvflqpl aptrefppvi fdmpsmgpft nraaarcaes lltrafapgv
      181 rhlqrrlgvp paalerrrat wpvqhgfspv vvprpvdwrp gmevagywwp sedpdwtpep
      241 rladflqsgp ppvyvgfgsm qpsdperlgr lvaralklag vrgvvqaswa glsvdgdevl
      301 tvgevphawl fprmaavvhh agagttaagl ragvpavpvp mmldqpfwaa rltalrvspg
      361 kvpfqrlsae nlaealrkav hdpryrhrar qvssligaed gagrvltave hlagr
//
LOCUS       WP_457685478             181 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Streptomyces nigrescens].
ACCESSION   WP_457685478
VERSION     WP_457685478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18581
     Region          49..165
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mpyltaavvf vgalsalnlv lalamvkrlr ehsglltgrr gapsaelevg triaefetvt
       61 eagepltras laddllvafl spgcapcvek lpafvahtrs lpggrrgala vvvgepreaa
      121 afaaplgpva qvvieepnga lsrafgvhsy ptllrigpda egrpvvtsna vdlkrptama
      181 a
//
LOCUS       WP_457685475             210 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685475
VERSION     WP_457685475.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22586
     Region          130..210
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mvpelvrtwv sgwavsrhtt rpaerpwgly vevgrpdqvg rhvlpdahel avreaaasvt
       61 vphtwlkvpm dpegvgrwlp agwvvdkget ghlmatdlra taprapegyt asvetrdgvt
      121 yvqvhdaage laakgqmall gkatvidsvt terahrrrgl gafvmralad havtegaalg
      181 vlgatdegra lyetldwkvy aplaaciyrp
//
LOCUS       WP_457685480             633 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685480
VERSION     WP_457685480.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 633)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 633)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 633)
  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 633)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..633
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67002
     Region          45..620
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mkpvpkpaap gpvphtppqs atdgaaplrl araactlvaa aapvlltgya vltlaagvlp
       61 vatawltklv ldaladgapl aqvarpamgl aaagvalvlt gevaqylraq lgrevavtaq
      121 erlyravdgf vglrrledpa fldrlrlaqq sggaspgqvl davltvagsv ftvtgflgsl
      181 fvlsplmtll vtaasvpvla aelwlsrlra rmawdlgpve rreffystll srmeaakevr
      241 lfgtgaflrg rmvadrravn earrgldlre arvqtalgll aalvsgggll wavaaardgr
      301 lsvgdvtifv aaiggvqgal aslatafart hqalllfghy tavvdagpdl pvppeprtlp
      361 alrhgielkd vwfryaddhp wvlrgidlfl phgtslalvg lngagkstli klicrfydpt
      421 rgavlwdgvd lrdtdpaelr srlgavfqdy mnydmtaten ialgdisasp dharvaaaat
      481 ragiapqlaa lpygydtlls riffagtdrd dpetgvvlsg gqwqrlalar aflrdrrdlm
      541 ildepssgld aeaeaeihss lkrhrsgrts llishrlgav readtiavlr dgriaelgsh
      601 dalmaaegay arlfalqaag yrdttaapng rqp
//
LOCUS       WP_457685490             307 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685490
VERSION     WP_457685490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31662
     Region          19..284
                     /region_name="F420_MSMEG_4879"
                     /note="F420-dependent oxidoreductase, MSMEG_4879 family;
                     TIGR03564"
                     /db_xref="CDD:274651"
ORIGIN      
        1 mtvgaalnat gadnqvdatv rlaeeaaaag lrsawfgqtf gadspqlaai vgravpglhv
       61 gtsaipvfgr hpllissqaq taqaathgry hlglalgtkl lteagfgiph erpiarlref
      121 ltalrqltet gtadfhgell tattpiparv pgaesgvpll vaamgpqalr vsgqladgil
      181 pylagprala ehivpavtaa aesagrpapr ivalvhgvvt ddvdavreka teqlafyeqf
      241 psyarvigls ggkraadvav igdertvaae vrryrdagat evvfsgteia gdadrrrtwa
      301 llgelag
//
LOCUS       WP_457685491             273 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457685491
VERSION     WP_457685491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27748
     Region          2..267
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mlgavlvgva lsvstagsvh amsggtqlpq rgaaprlatl avkgdapllq rascggalia
       61 pdrvltaahc ldgqdtrrae vhigssvlsq dpgtvrdirs vtthpryell pspvdpdnva
      121 lssaaydmae irlsapvrgv kplpvahhrp lpgtpvslfs hgttaapdps qpgkeirgdv
      181 lrrgdltvrt haqcaaqtpa vvdkasvlca rdisdggttm cfgdsgsplv iwgrrgpela
      241 gvfsfageta gkvcgqaada afadvpalla gvk
//
LOCUS       WP_457685493             578 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457685493
VERSION     WP_457685493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
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,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 578)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19831406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..578
                     /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=61716
     Region          85..578
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
     Region          355..578
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mspevagpat apaplpdrap pgpgplfrlp glpswwrpwg ataldvliam gcawfdaqfr
       61 tsfveeqlhs plpqgwavgl tvvgalllvl rrrfpaavta aitcglllgt gsvlatvvaf
      121 yslarhtprv rtvfvaapvg lllvlgvavl hlrqyaphhg tevtrepvli alvaltgvvv
      181 pvlaglypra prqpwwwehr samlfdvllv llfplanpva lvsglngpdd dpllvpapvl
      241 vllvmvqgva liwrrrypda laavavilip lvlpsfsilp vslyalakyg asrrnlllgs
      301 gaaavvlvaw tvvatefeae qfipysiflv vpsvvvpvlf gmyrgakrsl mvtlqdradr
      361 lereqhllas qarmeertri aremhdvvsh rvslmvvhag aleagaggpg vatdtgrlig
      421 dmgrqalnel rqvlgvlrld dgeqqvplsp qptpedlatl veesraagmq iafdvigeps
      481 atdstvqptl yrviqegltn ahkhagnvpa rvevryrkdt vrviveneap agpvptllps
      541 gghglvglge rvtvlggtfe agalenggfr itatvplr
//
LOCUS       WP_457685497             503 aa            linear   BCT 27-JAN-2026
DEFINITION  PepSY-associated TM helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685497
VERSION     WP_457685497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=53346
     Region          33..449
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msteqrlass dssgspdptr sgeertvrrt gwaalrplvl rlhfyagvli apfllvaavt
       61 gllyacsfqa ekvayahelt apagteklpl sqqvadarka hpegkiaavr papqpgdttr
      121 vllsdvpgvs ddhqlavfvd pytgnvrgal etygstgalp lrtwldalhr dlhlgeggrl
      181 yselaaswlw vvaggglalw igrrrksrtl ralalpdrta tgrrrtlswh gavglwaavg
      241 liflsatglt wsayaganig dlrealgqat ptvstavtks daghdghggs sgmagmpdmp
      301 gmggtkenps sgsapsdvgi dkvlraaraq glsdpvevgl ptdegtayvv kqvqrswpek
      361 qdaiavdpat gkvtdvsrfv dhpvlakltr ygidlhtgtl fgianqiala alalalifli
      421 lwgyrmwwqr rptrdralsf grpmprgawr qvplpvlipl vlalgavgwl vpllgislva
      481 flavdialgt larrrrvsat agd
//
LOCUS       WP_457685501             302 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685501
VERSION     WP_457685501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32375
     Region          11..299
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mttltwnsnr pwrgimvata lplrddlsvd hdayarhvrw lieqgcdgvv pngslgeyqt
       61 ltdeerarvv rtaveaagdg arvmpgvaay gsaearrwae qaaeegcgsv lllppnayra
      121 deravrahya evakagvpvv aynnpldtkv dltpgllarl hqdgsivavk efsgdvrray
      181 eiaelapeld lligaddvll elavagavgw iagypnafpa tcaelyhaav agdletalpl
      241 ykslhallrw dsktefvqci klsmdlvgrr ggparpprsp ltgeieaevr aatekaraag
      301 hh
//
LOCUS       WP_457685505             423 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685505
VERSION     WP_457685505.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=46472
     Region          32..414
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(45,73,259..260,288)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 mladwfrehs ttlttldpqq plddlealre ivddarvvai gegahfveef srarqrvlry
       61 laercgftvf afefgfseaf pldrwlqgdg edgdlakvsp aatewgasdl mhwlrrhnrt
      121 sgyplrfagi dvpeaggtlr palepvadyl hevdpdalrl vdtalevsdr flkgsgsgaa
      181 aaprwaglea aeqneltavl arlllrlraa eplyvsrssq rhfdiarrrv eaachtdymf
      241 qamnallsgr glaadlsvre iymaesvrwh ldhaepgari vlaahnshih kttlefdggl
      301 taltmgqhlh rmlgedyrtv afvhtadhvp emypdqsaav gftlaeahlq paepgsveaa
      361 ltdagladri tltdlrdapr dtqgapllns irsqssalst pvpeafdall avptvtrdrt
      421 vrf
//
LOCUS       WP_457685508             228 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457685508
VERSION     WP_457685508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24586
     Region          1..182
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mklltvnlgr praveyatgp sgttgifkep adgpvrvadp gppgrgasgv agdavcdlsr
       61 hggndqavya faredldfwe relgrplpng afgenlttsg ldvngarige rwrigpdvvl
      121 eatsgriscl tfqrrmgeeg wvrrftrhaa tgaylrvivp geiragdpie ivhrpdhrvt
      181 vamafravtl erqllpevla agealhtevq rvareyvtal keraqngt
//
LOCUS       WP_457685510             246 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457685510
VERSION     WP_457685510.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 246)
  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   3  (residues 1 to 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27219
     Region          12..>141
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtsselwtra tadrydaeet elsaaavlgp tlafladlag dgralefaig tgrvgvplre
       61 rgvpvvgiel sehmaavlrr kidedtlpva igdmattvvp geftlvylvy ntitnlltqd
      121 eqiecfrnaa rhlepggrfv ielgvpplrf lppgqvavpf dvseqhlgfd tfdlveqilv
      181 shhftrdgdd dryrrgnsrh ryawpaeldl mariaglele rrvadwdgap ftqdsakhis
      241 vwrkpt
//
LOCUS       WP_457685517             806 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685517
VERSION     WP_457685517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=88992
     Region          9..806
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mspppsrral lgtglagaav altgtlpagt asaqplrtqw kedegqrysv pglkkpvrvt
       61 vdvwgvshif adnvgdlfqa qgfnvarerl fqidtwrrrg lgrfsevlga syveqdraar
      121 lflyrgdmaa ewasygpear eaatrfvagi ngyidwlgdh pdalpaefqk lgyrparwsp
      181 edvvrirthg iggnlssqva rarlmsvggn kastyfhkle pdhmvqvpeg ldlslipadv
      241 lgvyslatsp mvfadgklrr mpdgrnvlre satgsnawav aatrtatgrp ilagdphred
      301 ytlpanryia hlsapglnii gagepwnpgi smghngmvaf gltnlpagqa dlyvyeldpd
      361 dhsryryrdr weklttvtek iavaggeprq aqlsftrhgp vvkideknhk ayavrtvwte
      421 pgtspylgsl nfqrvkdsre fveaisrwkt pgsnlvyadt kgdigwapga lipkrsgrgy
      481 dgllpvpgdg rfewdgfydn aqlptsrnpr sgffvsanef nfppgypipt ydwqpayrkd
      541 rihevlsqqr gtsiadtlal qndvksgvag qflpyvkklr stdpttvkal rllssydgva
      601 skdsaaaalf etwmmrflyp awaqlllpkp aadylvgisi efdlrvmnds fvrpddwfga
      661 dgarkrdell lstlpkayte vasklgvder awrwgamhih vfmhplggpn vgpterggsf
      721 dtvsvsyfhh ldhpyaevvg atfkmaldvg awdnsrvina pgqsgdqrsk hykdlqdkws
      781 ageyfpllys eqaiernggm rillqp
//
LOCUS       WP_457685519             210 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685519
VERSION     WP_457685519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22217
     Region          17..194
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mtgssavgsa ptpasgrrss egfrlgneil afrfvatlge rradpveria tpeqlrawli
       61 anelgsadmp asesllrdar alreaihrag taiasggvpd padeellnrw tarhrarlvl
      121 tggqarwhlp etdsaraala vvaldavatl gghgdgvikr ceqrtcgglf vdtsrgrrrr
      181 wcsmatcgnk vkkanlkaar dgtepgltdg
//
LOCUS       WP_457685521             452 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685521
VERSION     WP_457685521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48862
     Region          30..451
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 meqvtadvcv vgagfaglaa arqlaaagre vvvleardrv ggrvwnrelp dgtvvsaggt
       61 wlgkgqdrmf qlcrelglev ypqydkgdhl vrldgrnhry rgipktgpaa latlglaflr
      121 lnlmarrlpa dapwearrar twdartlgqw lshplnvpsa aahtllrstm nllfcadpae
      181 vsllgalvla rggggagfgy ytdnrktesh lvdggapela rrmaarlgta vhlsspvrri
      241 vqnttdvevi tdaltvrarr vivatppvla griffdpplp aahshlrqrv vpgaiirvht
      301 qysepfwrgq qlsgqtlspq spvpitidqt prsgvpgvls syafgagavr lgrlepkerk
      361 evwldalaer fgpearrpta yletdwseqp wslggmvahf ppgaltnygs alrepvgrih
      421 wastesatlm hglmegavrs geraarevlt an
//
LOCUS       WP_457685525             208 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685525
VERSION     WP_457685525.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21990
     Region          1..141
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mnttdavafw dgvyaarpaa ggpqpnarlt etgmglppgd aldlgcgdgg dalwlarlgw
       61 qvtavdisav averlaalvr shglddrvtt vradlhtsfp pggfdlvcah ylhtpfdldr
      121 atvlrsaaha lrpggrllvv dhgsaapwsw nqepgiryps prevaagidl apqtwtvera
      181 daprriatgp dgrtaevtdh vllirrta
//
LOCUS       WP_457685526             202 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685526
VERSION     WP_457685526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /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=22042
     Region          22..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..176
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(94,107,109,120,125,129,163,165)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdhrtddevl davgprlral rrargitlag laattgvses tlsrlesgqr rpslelllpl
       61 artydvpldd lvgaprtgdp rihlkpirrf gmtfvplsrr pggvhafkmi ipaqpeplep
      121 apqthegfew lyvlngrlrl vtgerdltlp pgeaaefdts lphwlgsadg gvvellilfg
      181 lqgvrahvrt dphradqagg rr
//
LOCUS       WP_457685528             389 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685528
VERSION     WP_457685528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41916
     Region          2..387
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 msttpriaia gaglgglvca rvlqqhglpa tvferetapd arsqggtldi hedtgqaalr
       61 taglfdefla lsrpesqewr lydrhatlir hdqageddls rpeidrghlr allldslapg
      121 tvrwghsvra vtplphgtar lhhhnhtted fdlvigadga wsrvrpalsd aqpsyagvtl
      181 veahfddvdh rhsgiarlvg rgtmsakagr rslvlqrnsn ghvrayinfr gpqdwhagvd
      241 ladteavrar llaqyqgwde slldilrdne ggfinrpmfv lpvphtwrcv pgitllgdaa
      301 hlmppagvga nlalldgael aqsvighsti aealdayesv mlpraaenak taqqmlvglm
      361 pdtdsddaaf pdslwpaapl pdsrpahts
//
LOCUS       WP_457685530             325 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685530
VERSION     WP_457685530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422978
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..325
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34836
     Region          24..203
                     /region_name="GloB"
                     /note="Glyoxylase or a related metal-dependent hydrolase,
                     beta-lactamase superfamily II [General function prediction
                     only]; COG0491"
                     /db_xref="CDD:440257"
ORIGIN      
        1 msgqpslppw vtwrqrpfpd anllllhgrq palvdsgfvg haedtaawar ahageiglvv
       61 nthwhsdhvg gnallqarga aiaagapeae aisrrdpgcc aaeyldqpva pyavdmsldd
      121 gqvlrlgdtd wevvrtpght pghlalwqpd erllvagdal sdydvgwvnl aldgldaatt
      181 alaslkrmad laprvilpsh gpipadptaa fgtalrraqr lvddpdgavw ygarrifafa
      241 lmirggiasd evepylhara wltdaarlld ltpealatel vaamlrnral vlrdgrlhaa
      301 adhtpvaaes lrvpyprawq atelr
//
LOCUS       WP_457685551             175 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685551
VERSION     WP_457685551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19327
     Region          9..150
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 miiqvpaldd lpalraiera agepfraldm asvaddepps peqltefqra grvlaayeep
       61 gpgregrrpv gyllwepvdg cthieqvsvh pdrahrrigr alidraerdg gpvpltlttf
      121 tevpwnapyy arigfrilpe aeltpglrai raheaalgld rwprtgmrre pgwsg
//
LOCUS       WP_457685553             125 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase TusA family protein [Streptomyces nigrescens].
ACCESSION   WP_457685553
VERSION     WP_457685553.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Tanabe,T.S., Leimkuhler,S. and Dahl,C.
  TITLE     The functional diversity of the prokaryotic sulfur carrier protein
            TusA
  JOURNAL   Adv Microb Physiol 75, 233-277 (2019)
   PUBMED   31655739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..125
                     /product="sulfurtransferase TusA family protein"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12589
     Region          <34..>72
                     /region_name="TusA"
                     /note="Sulfur carrier protein TusA (tRNA thiolation,
                     molybdenum cofactor biosynthesis) [Translation, ribosomal
                     structure and biogenesis, Coenzyme transport and
                     metabolism, Posttranslational modification, protein
                     turnover, chaperones]; COG0425"
                     /db_xref="CDD:440194"
ORIGIN      
        1 mtatspaapg papeadlavd gtgllcvall lrlraaiaea gpgtvvhvit tdpaapldlp
       61 awchmtghhy lgpvlddadg svddgdssvd dedssvyalr laadarptra dapwrtarps
      121 gdtgp
//
LOCUS       WP_457685556             483 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685556
VERSION     WP_457685556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49976
     Region          15..451
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,141,
                     144..145,148,271,274..275,278..280,283,311,315,367..368,
                     372,376,392,395..396,399..400,403)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msrsaapswa lllvlcgavf legldigmln valppirael glatgelqwv msgyvlgygg
       61 fmllggraad lfgrrrmflv pltvflvfsg lgglategwm liaarfvtgv caafmapagl
      121 siittnfpag prrdrallvy sgtagggfsi glvaggllta adwrwvffap iapallvlla
      181 alplvpkdsa prqprprvdv agaitvtvav lllvmtveqa ahapalrtmg tltaalalla
      241 vfvtverrtp tpllrlgilr srplvragvm gllftagffg fqflavlylq efrgwsaaet
      301 sfallpmgad avlaptltpr lvrrfgharv ivaglllaal gyalflpvga dwtyaamfps
      361 lllvgiafal vhgplaivat drvasceqgl aggllytsvq fgaalglsav tavttvaggg
      421 dvpltplagy raglivptaa vvialligvl gmrerrpgra vrsgrrasgs sepagtgsvt
      481 rpk
//
LOCUS       WP_457685560             461 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685560
VERSION     WP_457685560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46366
     Region          10..441
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,135,
                     138..139,142,261,264..265,272..274,277,305,309,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrkwwplvav clgtflflld ttvlsvvlpg tgeeldasls alqwvaniyt lvlavlmltm
       61 galvdrlgar tvyvvgltvf giaslvcgla pdagvliaar gvqgiggaam avttfaligs
      121 vyrgpdmgra mgifgavtgl aaavgpmlgg vltqylswra vfflnlplva vtvalslrvl
      181 aagrpgtgrr idlpgmaafa acagsltyal tlaadegwts paalglltla tlslvvftri
      241 elrsgaplld vrlfsrasfs gvmmcvaast aafaalvyts vwlqsglglg pvraglalmp
      301 lalasfatsl isgrrlhgrs prailatgll lsgigcalqa gldadssads laaglaltgi
      361 gvglmgpamg aavfaalppe rggmaagamt tfrqlgqtlg vaafgllfqh hggamsegln
      421 rvliaaaatg iigsalacaf vpkpaaakat gtrprnltgs r
//
LOCUS       WP_457685566             285 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685566
VERSION     WP_457685566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30906
     Region          29..269
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 madeqsevpd gtavrvalwr amhvqvdspp hviedeiglq laapeegwrr rpdmdprgts
       61 pfraaivara rfiedlvveq aghgvaqyvv lgagldtfaq rrpdiaarlr vfeidqpatq
      121 awkrqrliel gygipdwlrl vpvdfeaggd wweqlsdagf dpgrpavvvc agvtmyltkd
      181 anaatlrrla glspgstlam tfmlptdlvd dadrpaleat kpqaqaagtp fisfytpqem
      241 lalardagfe dahhvpgaal aaryfaerpd glrpssgedl lvatt
//
LOCUS       WP_457685571             507 aa            linear   BCT 27-JAN-2026
DEFINITION  long-chain-fatty-acid--CoA ligase [Streptomyces nigrescens].
ACCESSION   WP_457685571
VERSION     WP_457685571.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..507
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /GO_function="GO:0004467 - long-chain fatty acid-CoA
                     ligase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54792
     Region          5..505
                     /region_name="FC-FACS_FadD_like"
                     /note="Prokaryotic long-chain fatty acid CoA synthetases
                     similar to Escherichia coli FadD; cd05936"
                     /db_xref="CDD:341259"
     Site            order(167,170..175,177..178)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(170,284..285,307..312,392,404,407,418,498)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(170,210..211,258,260..261,264,284..285,307..312,392,
                     404,407,415..418,479)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(210,260..261,264,284,415..417,473,479)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mtfnlatalr esrrshpdkp lchladrtat yaqadeasgr iaatlrglgl rpgakvavhl
       61 pnvpqflfty ygilkaglvm vplnpllkap eiayhlqdse srllitfeef aaeavkgael
      121 aggvgtyvvh ppgsdrriag trhhdelyaa ddtgeiapts addtavllyt sgttgrpkga
      181 elthfqlhmn ctvsgelfgf rpddialavl plfhvfglss vlnmavrhgg tlalvprfgt
      241 davldalerh rctvfagvpt myaallqadt vkrdlgalrv gvsggaampg evirafeekf
      301 pgvvilegyg lsetastatf nisaeqrkvl sigkpiwgve vrivdpsgae lppgpehvge
      361 ilvrghnvmk gyhrrpeeta ealrdgwlht gdlghrdedg yffivdrkkd lvirggynvy
      421 preveevlht hpavaeaavi grpddrlgee viavvslkrd ttataedlta hckerlaayk
      481 ypreirivde lpkgptgkil kkalrag
//
LOCUS       WP_457685576             266 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457685576
VERSION     WP_457685576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28841
     Region          24..240
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mnsshpagra avgpavhrva vatetaafva aldgadlsvp vpgcpewtlr dlvqhtgsvq
       61 rlfsvllrrl vqepprsrev eldlptaedg wadwlsasaa eaadafaatd pdapmwawgv
      121 dqharfwmrr mlfetlvhrt daeravgrrp vidpalatdg vdeflanlpf atsfaphvar
      181 lrgkdetlrf rctdtdgdwl vrlrpdgfva eprtgdaaae sadagvrgta adllllvygr
      241 ldrgadtvet tgdeelltrw ftnsaf
//
LOCUS       WP_457685577             242 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457685577
VERSION     WP_457685577.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26609
     Region          41..237
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mcrtalppag rgrpalycsr scqarayrrr kqtpvpaagr pavgdpsgkr lriaealwri
       61 aaerglhaas lrevaaeagv slrsvqyhfe skhrllvdal qllhaeneri arsrirfdta
      121 eprgllravl eeflpvdtqr atalrvfaay yarsltdpal aevflpaeqp lerlvadlia
      181 aaqadgrtap gldpwreadl lvagavglgg dvlhdrrtld dvrrtldyhl dkifagdrrt
      241 gr
//
LOCUS       WP_457685589             300 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685589
VERSION     WP_457685589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31571
     Region          49..172
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mgqgndqgva gdggtplpde iaadnaeqgg awngddgryw vqhrerqear yrrltphlma
       61 aagiqadsrv ldigcgsggt sleaaraaae gavlgvdvsa pmlaearkqa agsglpqvtf
      121 ergdaqvhrf edgafdiais rfgvmffadp eaafaniara lrpggqlafl cwrsvrdnpy
      181 ltvpmgaiap yvqlpeleap gapgpfslvd tdriekllds agfdeitisa vdepmwmgtd
      241 pddvvayqlg ipasramlae asaearakte talrdalaeh qgpdgvtlgs aawlvtarrr
//
LOCUS       WP_457685595             184 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685595
VERSION     WP_457685595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19577
     Region          10..124
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtlpgdrhyt velhasaerv pqirrilaah lrywdlelhi ppvcrgvael ltnvhrhigp
       61 dapcvvelrw tgrhltasva dqgprlpkll sagggglsrv aalsdswgtc gtpdgkviwf
      121 trrveaarks pltsrtplrs vpdakgqpav ppavpveplv eplqeatgta aeatpeasna
      181 vslv
//
LOCUS       WP_457685596             397 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685596
VERSION     WP_457685596.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42165
     Region          17..390
                     /region_name="Beta-lactamase"
                     /note="pfam00144"
                     /db_xref="CDD:395092"
ORIGIN      
        1 mepatvnghc apeftgvrda fernfsehge vgaavtvtvd geavvdlwgg hadaagtrlw
       61 erdslvnvys tskgmtalca hllvdrgeld ldapvtrywp efgqagkqdi pvrwllshra
      121 gliapreplp aghaydwerv cavlaatppw wepgtaqgyh avtfgylvge vvrritgqsl
      181 gaflrseitg plgarvfigt paeeharcad mvgqldeari aeqfpgvpkq pfrsladhpl
      241 aivmlaltyi ptgdvnsaay rsaeipagna hagahglatv ygalaggtlv gpgtleamrr
      301 sqslpgerdl tidalapagy ehrwglgfml nhqgqagpnp rafghggagg sfafadpenr
      361 lsyaytmnky gggttgqdpr nagliravyq altqhrs
//
LOCUS       WP_457685598             180 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457685598
VERSION     WP_457685598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..180
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18379
     Region          19..161
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mghdahrvpr pagaagsgdd aldheveevi aavltasrml vgvsaralgr tapsltlpql
       61 ralvvldgrg pvklaalada lgvnpstalr madrleaags vtrqanpgnr revvlsltdr
      121 grglvaqvla drhaeiativ srlpaarrag lvealraltd aadeppvapr papppepsap
//
LOCUS       WP_457685602             558 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685602
VERSION     WP_457685602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..558
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60446
     Region          50..554
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mtphthdvvp rsgwvapsgk pplasrmmra twrglpakqh dvgwepglvv paadgsplrt
       61 dhyfprtkgd fptllvrspy grgvpwsply gilfaeqgfh vvlqscrgtg gsggrfdlwr
      121 neaadgqaav swlreqpwft gtlgtigpsy lgyvqwalal dpppelkamv vqvglddpha
      181 lfyeggalll enalavgagm tyqhrglmpf vrstlrlqrr lreitgarpl rgayesalge
      241 vpwldevmth pdaddpywhg asmaaaaeqa avptsvitgw hdvladqnlr qfarlrragg
      301 essllvgpwt htsalqqgwp evfseslawl rahlcgdrtg lrptpvrvhv ggedvwrdld
      361 dwppapatta wfpaengtls rqdpvesgpl vsfrhdpadp apsvggplls rsagprdnsa
      421 rearedvltf tgppltepvd ilgpvsarlr istdtghadv farlcdvdpe nrstnlcdgl
      481 vrlrttgqap sevtvamrat ahrfaaghri rlqvsagahp ryarnpgtge psaeatrflp
      541 vhltlhsgsa lmlpqetp
//
LOCUS       WP_457685607             211 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685607
VERSION     WP_457685607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22844
     Region          52..186
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 msisvttwhl eqtspadlsp aqappaeqdv rivrsevpsp efsrflytav ggdiawtdrl
       61 twpyaqwaef lgrpgvetwv ayergtpagf ielageadgs veityfglvp afrgrriggh
      121 llaygieraw dlaerwpgra ptkrvwlhtc skdgphaman yqrrgfrlyd tkvaeedgip
      181 apgpwpgagp itgpttgptt gpittgtpag e
//
LOCUS       WP_457685612             394 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685612
VERSION     WP_457685612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42362
     Region          1..394
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtelplsgit vvsveqavaa pfatrqladl garvikverp dggdfarryd ttvqgqssyf
       61 vwlnrskesl tldlkstrgr eileellvga dvfvqnlapg aaarleldaa slagrhktli
      121 pctisgygtt gpwadrkayd lliqcqtglv sltgtaeesa ragvsvadia agmyaysgil
      181 tslytravsg varavevslf ealaewmhqp ayytrfggtq pprlgtqhat vapygaytaa
      241 dgqevlfsiq nerewaalce rflerpdlvd dprfatgpdr vthrdalnai vaerfrrsds
      301 revtklldsa gianagvnsv eqfldhpvlr ergrwrdvgi pggtvpallp padlagtapr
      361 mdavpavgeh terilaelgh gtaeieslra dhvi
//
LOCUS       WP_457685610             334 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685610
VERSION     WP_457685610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35319
     Region          47..325
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mnavtssats satvargpap qpagppagtg prgggparms rrrrartgwf faspalivia
       61 avtvfpvlfs lllsfadvrl eyggfrllsl tgdhyaavls spewryalvf tfgftavtvl
      121 lelvlgtaaa lvlerlgaar gwvlavlllp walinvvaaq lwgylfngty ggltwifeqi
      181 lgrqpdilgq pasamgamvv vdvwkttpfv aivvlaglml ipgdvyeaae idgagawttf
      241 wkvtlpqlrp imaiavlfri lqafgifdlp fvltqggpgt ateslamlgy ktlfqnldig
      301 rgaavattta vivisccllf lrvfktqade ggra
//
LOCUS       WP_457685620             338 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685620
VERSION     WP_457685620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 338)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /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=35788
     Region          <84..>126
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          146..312
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdgvdhierm dgvddvddvd driegggegg gaiegaerag gvdgvgdarr alggflrarr
       61 grvapehvgl aggrrrrvrg lrreelaqla gisvdyyvrl eqgratqpst evldalagal
      121 gldaaerrhl atlagarrdp aprarvspll qrlldsmapf pafatnhrld vvawnglgae
      181 liggvadpgr rdrnnarylf ldpasrtvhp dwedrageav gqlrvaagry pddaeltalv
      241 gelsarsaef rriwetgevv mcaagrkrlr hpeaglltld yetlhvpaap getglvvhvf
      301 saeedseaav algrlamtvm asaqrsagad saegggpr
//
LOCUS       WP_457685622             460 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685622
VERSION     WP_457685622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46092
     Region          10..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(17..18,21..22,25,57,107..108,110..112,115,135,
                     138..139,142,265,268..269,272..274,277,305,309,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mhkwlplvat csgtfmllvy stivtvalpg vaddlhasfs slqwiidvyt lalaglllgm
       61 gslgdnlgrk rlyltgltvf avatlvcgla pdvttliaar avqglagaam fstllpligl
      121 tytgrdrgva favwgavaga aagignvagg iltqflswqw ifhvgvpvcl atlalsaavl
      181 tddartptri dylgivtftp aalgitfgii nggeqgwtsg pavlgfavga amlalfllae
      241 rtgsnpmiap alfrkrefng tlvaamgyyl agfgalpvis lwlqdgagls alstalvitv
      301 qpvaffatsa vagsmlhrlp ahrtlgggal avgagnvlml aigagsswta lipglvvtgv
      361 gagivspvlp saamsaapas qsgvasaaan carqlglalg iavlgsvfhr fsttsggtgl
      421 haayahglta vfavaaaigl gsgilalrll kpprpatqpa
//
LOCUS       WP_457685627             441 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685627
VERSION     WP_457685627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..441
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48643
     Region          33..379
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrhdrapgrp prftrrgllt taaalpaaal lpgcsdgrrr taggritlrf qslawqqdsl
       61 kankqlvaew nrqhpdvrvq yvqgswttvh dqlltsfegg eapdiihdas ddladfaygg
      121 dladltallp prlkrdipqr swetgtfagr ihgvpflqep rvlianrakl drsgvrvptp
      181 ehpwtwqefe eaaqrltrgt tygvawplke pvsatlnlal stggrifhrh rdgevevrfd
      241 avdqqvprti hdqvnvdrsa srttlgmggs dtlpgffagr yamvplgfsy rqqiaqqapk
      301 gfdwtvlpap kgtaldqgvs pqtlsiaedc phkeeamafi dfllsppnmv rlalgdwllp
      361 tgqealkdpa lraaeydwat gtalagslhs apaqsvrgyp ewkdkiatpg lqeyysgaiv
      421 ldtlrkrlve dgnlvlaryq r
//
LOCUS       WP_457685619             277 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457685619
VERSION     WP_457685619.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29198
     Region          1..198
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 milvtgatgn igralleelr acgagpvrgl trdaarvtfp egveavegdl grvgslnsal
       61 dgvrslflvq gmgaegevle aarqagvehv vlvssitvqt hphlpaagvn aaverllkds
      121 gmawtilrpt qfasntlwwa tsirehgtvh vpyadlglpt ihpadiaava raalvepghr
      181 grtypltgpe rvtarqqvaa laaalgqels lvgisreqah rqmasfmgde tanavldlmg
      241 gdlneellkv rdtvpqltgr patpfrqwat ehaaafr
//
LOCUS       WP_457685629             322 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685629
VERSION     WP_457685629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 322)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34289
     Region          57..321
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtatestggs erssaprgag sapvprgtpr rtstarrtst srrratprrt atragqyaal
       61 lgylaflafp flwllstafk pprelgsmhp twipeaptle nfrqafaqqp llaaagnsll
      121 aaavsallai llatpmayvl arfrnrlsra atgwvvisqa fplvlviipl flilkglhlv
      181 dsriglimvy vvwslpfalw mltgyvraip releeaaavd gagrlrtlvs vtapllapgl
      241 vatalfafit awnefffalv llkspekqtl pvvlthflga egvadlgpla aaallatlps
      301 lllfaaiqrr itggmlagav kn
//
LOCUS       WP_457685631             313 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685631
VERSION     WP_457685631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33741
     Region          9..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtlataprrs aapatdgaar prrdlgawfl vlpallpilv lsvgpllygi glaftdaqsg
       61 rtqatrfvgl lnfsdlfqds lfwdsfrigl iwafgvtvpq fllalglall lhldlrlrwl
      121 aralaiipwa mpevvvgimw rlvyhpdagi lnetlrglgl sgagdgrdwl sglatalpav
      181 ivvgvwagmp qttvtllagl qnvprelhea asmdgagawr rfrtvtwpal kpialavtal
      241 nfiwnfnsfa lvfvltdggp ggrtrlpmlf ayeeafrygq fgyaatmgla mvavisvlla
      301 vylagrlkgd ddr
//
LOCUS       WP_457685633            1133 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457685633
VERSION     WP_457685633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1133)
  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 1133)
  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   3  (residues 1 to 1133)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1133)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1133
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=120298
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          159..1111
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhfrvlapld vrsadgrpap vpetkvrall aallahhgrp vstarlvahl wgprpparpt
       61 aslqskvsql rraldtaepg arklvtatpp gyrldiapda ldaglftalt araraaatpr
      121 qragllgeal elwhgpafag fadsdlvrpv aesleeqrlt aleeraaarl elgehaplta
      181 elaglaarhp lrerlralql talyragrqs dalaaydeir arladelgvd pgpeltavhr
      241 ailrqepwrp hdggawqdgg awqgegaqre dgprhdhgar hdggttrptd rpepdlatap
      301 pagprprtnl ptpltallgr qdavrrieal laanrlvtlt gpggvgktrl aletagrlag
      361 sfpdgvwlve laalsrpdap eragskctaa qvaeavlavl giregasagp vaerligavr
      421 gkrlllvldn cehlveaaae vtaellgaap dlrvlvtgqe slgltgetlw pvpplepaga
      481 velftarasa adpdfvldad ataavaeicr rldgiplale laatrvralg vrelsarldd
      541 rfrllasgrr gvpprqqtlr amidwswell paaertvlrr lavhadgctl eaaetvcagd
      601 gvrrdevldl larlvdrslv tvaqtpygpr yrlletvaay clerlreage ltavrrrhhr
      661 hytelaeraa pllygpdqre wlerldqeta nlrdaldaav regaadhalr lvdalawywf
      721 lrgrlaeagr sltaalaaye aarataadag dpaaegrrlr aatwqvgmas lagddtdpve
      781 ratavlrqyg thddpgaraw aqwflgfaqv glgepavare rvadslaafr algdrwgiaa
      841 alssraqgsv ggdlrarlrd aeesaalfre lgdrwgqlqa adalgalaei tgdygraarl
      901 hrdglriaee lglwiqasyk lsglgriall tgdlaaardf hergmrlaae qshlrgemfa
      961 ecglalgarr egrlddaeah llpwlewclg rdgdpgtafv lselgflael rgdaetarrr
     1021 hldgfvaara tadpravala leglagaval tgrcavaarl lgcaaaarat agapqpaaer
     1081 gdvarstata rrglgdaaye aayasgagva pevlvkeatg sagargartt asp
//
LOCUS       WP_457685649             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457685649
VERSION     WP_457685649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37016
     Region          18..182
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          125..370
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvawrdlrf akgrfalmgt vivlitalvg llsglmaglg rentsaitgl padhlvfaap
       61 idgsklaftd srlpertvra wsrvpgvrha eplgiatara eaggrtaavs afgvrpgsrp
      121 apgrvgdgav vlsekaaasl gvraggrltl ggrsfevaav sgaamyshtp vvwtslgdwq
      181 rlaggsgpag agpgsgrsgp drgsvgatvl alsttgtsgl paadkelgtk tvttddavra
      241 igsftaengs lqlmrgflfv isalvigaff tvwtvqrsgd vavlkalgas tgsllrdalg
      301 qavvllvagt algtavvaav gaaiggtvpf vldpptvlvp alimialgaa gaalairrit
      361 svdpltalgs ar
//
LOCUS       WP_457685664             399 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457685664
VERSION     WP_457685664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=40230
     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 avrmagsltq aeiarstgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vvgvdfghsh lrvavgnlah qvlaeeaeli dvdasaaegf
      121 draeqlvnrl iaatgidpgk vvgvglgvpg pidvesgtlg stailpgwtg tnpgqelsgr
      181 lgvpvhvdnd anlgalgelv wgggrgasdl ayikvasgvg aglvisgqiy rgpggtagei
      241 ghitldeagp vcrcgnrgcl etftaaryvl pllqpshgpd ltmsrvvqla regdpgcrrv
      301 iadvgrhigs gvanlcnlln psrvvlggdl aeagelvlap iresvsryai psaarqlgiv
      361 pgtlggraev lgalalvlse mgdstlldga qtadapapa
//
LOCUS       WP_457685666            1135 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685666
VERSION     WP_457685666.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1135
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=122324
     Region          244..1015
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mrlrhrhspl rgiarpaala aaallvitvp gpaqaappqp pqgatefrss fesgepqpdw
       61 tdtvdtgpdg rprtsgvtpe tapaapgmnt gtdtgprdsp takahagftg ghalryagth
      121 ttpgrgysyn kifdvnvpvt aatslsykif pemaksdpay pathaavdla ftdgtylsel
      181 savdqhgapl tprgqaaskt lyvnqwnnre arigavaagk tvdrilvgyd apeaprtaaa
      241 frgwvddltl apkapdkpld rlsdyavttr gtlssgsfsr gntfpatavp ngfnfwtpvt
      301 nagsadwlye yarknnadnl ptlqafsash epspwmgdrq tfqvmpsvaa gtpdasrtgr
      361 alpfhhanet akphyygvtf dnglkteitp tdhaalmrft fpgdraslif dnvnnkggls
      421 ldtgrgvvtg fsdvksglsv gatrlfvygv fdapvtgggr ldggggkdvt gylrfrpgad
      481 rtvtmriats lvsvdqakan ldreipdgat fagvkeraqs qwddllgrie vegasrdqlt
      541 tlysnlyrly lypnsgfeqv gsrsryaspf spqvgqdtpt htgskivdge vyvnngfwdt
      601 yrttwpaysl ltpkragkmv dgfvqqykdg gwisrwsspg yadlmtgtss dvafadayak
      661 gvefdaeaay aaavknatva ppqpgvgrkg matapflgyt stdtregmsw alegylndfg
      721 iarmgkalye ktkkphykee sayflsraqn yvklfdrkvg ffqgkdsqgn wrlppgafdp
      781 rvwghdytet nawtfaftap qdtrglanly ggraalakkl dayfstpeta skefagsyge
      841 vihemteard trmgmyghsn qpshhiayvy daagrpwkaq ekvreamsrl ylgseigqgy
      901 pgdedngems awyvfsslgf yplvmgqgey avgsplftka tvhlengrdl tvnaprnnar
      961 nvyvqglrvn gkpwnstalp hrllarggtl dftmgdrpsa wgtgehaapt sltkddkvpt
     1021 ppadvtdpat gplfdntsgs saaltgapvd larparvtsy tltsadrata pagwtlegsp
     1081 dgqrwtrldh rdgepftwdh qtrvfgisdp gsylhyrlvp dgpgtlaeie llgap
//
LOCUS       WP_457685674             439 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685674
VERSION     WP_457685674.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44501
     Region          33..412
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(43..44,47..48,51,84,139..140,142..144,147,167,
                     170..171,174,247,250..251,254..256,259,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtatpepapa cpsppaatap psadpplwrd rrfvllaaar tisvlgngfa rvalsfavla
       61 lpgagpgqls lvlacqavpq lvfilaggvm adrmsrsrlm ivtdlvgaaa yaglaamvlt
      121 ghaplmalca laalagtata lfspamdgvi pllvpagrlq rangllrvgm nssmllglal
      181 sgvavavvga gwalalnavs fvvsallvrg lrlparartg ssgwadlrdg wrefagrqwl
      241 wvvvaqysvv vaalnanagv lgplvaenel ggarswsliv aaqalgtitg aglaarirvr
      301 rpvliavlat fplalpiall avrapvpwia lamfgsgiaa difgvlwatt iqrevpeaal
      361 srvssydwfg slafaplgll iagpvaartg vgpalagcaa livlasaaal lspqvrgvrt
      421 pgpaptgeer geceaerpr
//
LOCUS       WP_457685673             312 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685673
VERSION     WP_457685673.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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
REFERENCE   2  (residues 1 to 312)
  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 10144160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33771
     Region          56..>116
                     /region_name="NT_KNTase_like"
                     /note="Nucleotidyltransferase (NT) domain of
                     Staphylococcus aureus kanamycin nucleotidyltransferase,
                     and similar proteins; cd05403"
                     /db_xref="CDD:143393"
     Site            order(76..78,81,89..90,92)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143393"
ORIGIN      
        1 mtstpgpapl pepappgaaa eatgernpad ratpdgvppd rvtpvrpatd ratahlldrf
       61 laalrprlpl ralwahgsla ggdyqqgrsd ldliaivdrp ctpeeerqlg elhatldrtd
      121 plaaklhcsy laadetadpa hihltwahre lkrrtvtpvt rrelhtfgrv lygdaptall
      181 ppvtdaelat firtdlrefw rpaldepeew lqdiwvdlgm ltlaratvtl rdgtliskge
      241 alavlgelga pdeviadirh rrygpaappp ppgparpsdr varradltra flgpaidrtl
      301 atyghtfpap pg
//
LOCUS       WP_457685677             214 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457685677
VERSION     WP_457685677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=23596
     Region          <1..200
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlveigaglg lrqgeafgls medidfdaei vhvrrqvkmv rtklcfalpk grkvrdvplp
       61 ssvakalrqh veflapvpvt mpwddprppq tpveaklrrp rtykllvtgr ehkainrnyl
      121 nsyvwkpala evgviaalee sapdgsrawe psrehgyhal rhfhaseqlk agesvvslas
      181 wlghsdpgft lrkyahflpr agarggaaid avfa
//
LOCUS       WP_457685679              94 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685679
VERSION     WP_457685679.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..94
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9914
     Region          <27..93
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpprsleiap agkaaaraiv rartargysq rqlaarvsal grpmtatals riertvrrcd
       61 iddfvaiata lgvaphtlla spsrdrghae raet
//
LOCUS       WP_457685687             423 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685687
VERSION     WP_457685687.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45298
     Region          8..86
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maeaqsearr igevmrqarv lqrrsqknva aalgyhqskv srleagrgaq dvhmlrevar
       61 vlgipphhlg lgaapdatss npetedmhrr tflaagvaal aapttpagah qnliqsllpg
      121 pspaatdpvp dlpemrdhva aarrlfstch yaqlertlpg ligqlrqaig espgstdlsa
      181 llatayqtsa slllkqsdhg nawlavgram aeaersgdpv vlassvrvha hvlardghta
      241 qaitlvrhta dqltgaydqr spkylaalgl lllrgvtaas tgddrsatqd flteakevar
      301 yvaldrpdaw anfsptnval hgvsaavafg dagialqtar plmrrhipvp erraalwves
      361 araysqqgrl adgyqalria escaaqdirr pairelvadm aardrrrtlp elhhfsrrlg
      421 vpa
//
LOCUS       WP_457685688             147 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685688
VERSION     WP_457685688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  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 147)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13014796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=15446
     Region          43..126
                     /region_name="HATPase_RsbW-like"
                     /note="Histidine kinase-like ATPase domain of RsbW, an
                     anti sigma-B factor and serine-protein kinase involved in
                     regulating sigma-B during stress in Bacilli, and related
                     domains; cd16936"
                     /db_xref="CDD:340413"
     Site            order(49,53,56,78,80,82,84..85,98..101,113,115,119..120,
                     122)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340413"
     Site            order(91,101)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340413"
ORIGIN      
        1 mevhdirlsv fgtpaaaasa rrrlvaaird wglpagseal hvaelmagel lsnavqhagp
       61 gavtvtarcd gnairvevsd ssrdlprtrs psqddehgrg lsivaaladr ygteptasgk
      121 rcwaevrlqa vsspevalpv plprrrp
//
LOCUS       WP_457685694             179 aa            linear   BCT 27-JAN-2026
DEFINITION  dCTP deaminase [Streptomyces nigrescens].
ACCESSION   WP_457685694
VERSION     WP_457685694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10002283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="dCTP deaminase"
                     /EC_number="3.5.4.13"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008829 - dCTP deaminase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006226 - dUMP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006229 - dUTP biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19082
     Region          15..172
                     /region_name="Dcd"
                     /note="dCTP deaminase [Nucleotide transport and
                     metabolism]; COG0717"
                     /db_xref="CDD:440481"
ORIGIN      
        1 miltcpaiaa ahaageitid pydpdrlspn aydwrlgndl ricdgdldaa aptssaevsi
       61 prtgfvlepg vlylgvthek tgsetyaqll ngdratgalg iwvhvsaplg hqghairwtl
      121 eirasqpvri ypgmtfgklv flqplgaaas yqqhglkyta sqgietsrly eeipggcrp
//
LOCUS       WP_457685696             365 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457685696
VERSION     WP_457685696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39224
     Region          4..360
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mnakvatvld lpfpspggsv elfldlytgd rpliparafm lapaspgpql pagldllpvv
       61 gkclegpafh ryvaalqrsl aeaidpdhig vlhlqhltfg gtpaliralr ehprialvhg
      121 tdllfaeahr hqhkvltesv rladaivvpt pamadrllri apttdrakia hvpwgipdrl
      181 lanpphrgpr ppgspfrlly agrltpekgt enlllalaav qgvelsiaap qdqfrtlsra
      241 vrqsgvkiry lgwlrrpqlw rtftdhdllv mpsttleamg lvaleaqacg lpvlyqpvpg
      301 laemlaasgt atdftrpaav ardvdrlrtt pgllaalrqa grsnaarypl sataraltel
      361 ghqis
//
LOCUS       WP_457685698             345 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685698
VERSION     WP_457685698.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..345
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37626
     Region          1..344
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 medstdrikq lvadgvrdkv ypgavwatgn atgirargta gvldpaepdi pmrpdtvfdv
       61 asltkilavw stvgalwedg slpldeplgt fwpeatdrpl gqvtarhllt htagvplraq
      121 lknlygtdpa airagvlhea lhrppgeave ytdraalilg ylaehlsgqs ldklartriw
      181 qplgmthtrf gpllpeltvr capteldqdt grhlkgtahd fsarllggvc giagtfsvld
      241 dlarflryml dpttaptapg fgpswveesl svqtgtlepv rglfwhpgtd padrtyvhyg
      301 ftgtgmwisp krgtwaallt nklyytrdre pltrirnafr slifs
//
LOCUS       WP_457685734             377 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685734
VERSION     WP_457685734.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39430
     Region          4..372
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtvfalgpde qewcaelral taerlsplae kgeegrvnrp lvaalgelgl lrrlfpvqga
       61 lraldlcllr eslaqectea etalalqglg aypvvqsgta aqrdrwlpev aagravasfa
      121 lsepgagsda aalslaaepd gpdgwrltge kcwisnapea dfatvfartg gaagargvta
      181 flvpadrpgl tgahldmlsp hpigtlvfdg tpvaradvlg evdggfavam atlnlfrpsv
      241 gafavgmaqa aldaalthag artafggplk dlqsvghqla ematrvesar llvyaaasay
      301 dtgapdlarr samakllate taqyvvdaav qihgaralrr ghllehlyre vrapriyega
      361 tevqrsiiak elyrarp
//
LOCUS       WP_457685748             369 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457685748
VERSION     WP_457685748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38542
     Region          53..270
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttddeggrg rltgpagpde ephtpaapap dapgpnaplp dapgpnapvp davtcralry
       61 afgetkavdg vdlsvrtgev fgllgpngag kttaircitt llpvpagmvr vfghdaaker
      121 mavrrllgyv pqqlsadagl tgrenvalfa rvfdvsrrer aarvtqalaa vgltdaagrl
      181 aktysggmir rlelaqalvs aprllmldep tigldpiart svwehinavr aatgmtvlvt
      241 thymdeadqy cdrlalmhqg riralgtpde lrsalrarrr atrtpaaahp apltpgtptp
      301 aaapdtsatt apasapstps sppsapsrps dteptledvf rdvagsglde qsgdfrdvrs
      361 trrtanrvg
//
LOCUS       WP_457685752             403 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457685752
VERSION     WP_457685752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=43225
     Region          1..395
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mdrsgewile rigrdrgpdr graagrlaev vdsrgfevar ppawmrwlpv ayvvfvllle
       61 tvtptpwavs fllialpvia aytlgpvava aatvfavvle gvvagtpcct ghnihmlwen
      121 hhvaayvatg lvgalgvala ahrrrqerdl vrahsvaeal mrtllrpvph rvghllaagl
      181 yrsgevgtmv ggdlydlrat psgeraiigd vrgkglqavr tvadilgsfr eavhdegdlp
      241 avatrmerrl areaedlldd elfvtaalie ydavahrvti inhghiepvl isggevtpli
      301 gppalplglg aladeepvay thpfahgdvl llctdgliea rdqtgafypl ldrlrhrfgg
      361 rtapgpgpad vidflntdlp rhtrvfhddv allalapddg sev
//
LOCUS       WP_457685758             557 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457685758
VERSION     WP_457685758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..557
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=58250
     Region          99..536
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mvkssgvsaa tatatasvag vdvgaawqsa phpvlvisps gvvravndaa aplfpamrag
       61 apfddaparw ladahqrftd plrsedgdpv rgpvgdrsfe arpsraengd vvwwlvddta
      121 rrsaedalra erertgflaq astellasln agrcmdvtar laaqhladaa vvvtppsgrr
      181 wtvsfcgpdg qvvrdkavad pasvpglaea lrgfppvpsr widpaavpdr fkpsalgdig
      241 svvvtplpgh gvaagalilm rrsghaafne seetfarlfa aragaamsaa rlyaeqaait
      301 rtlmrellpp rleqvsgvef aggyrasndt drvggdfydv hagagpdees lvvlgdvcgk
      361 gleaavqtgk irntlhallp latdhqrvlr llngalldsd htrfatlvla svarrggtvr
      421 lrvtsaghaa plvvrvdgrv deadtrgslv galpevtskt asldlapges cllytdgite
      481 tmggpmgeel fgeerlrsal secaglpaea vverirmlaa qwvgtgrhdd mavvaitaph
      541 hahlsavdgh trgryta
//
LOCUS       WP_457685767             549 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685767
VERSION     WP_457685767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..549
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59510
     Region          79..>261
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          443..522
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mvtalatapa ggatgaaaap papvahrief grcaavehlp ssvecgrlav pldyarpdgk
       61 kihltvsrir atargerqga lvfnpggpga ssmefplyga lpkwsklara ydfvgyaprg
      121 vgrsaplscq dpkefakaps dsrmhpdaaf krqkraeake yargcvrrag adlpyynsin
      181 nardldmlra algekkltfm gasygtyfga vyatlfpghv rrmifdsvvn psprkiwyrn
      241 nldqdvafer rwgdwlgwva rhdkqyhlgt tkkavqhsyd kaayklrrkp lngkigagql
      301 qsaflktgyn dafwpmraea lsgylhgdpk pllaqalpra agaaadensn avytavecnd
      361 apwprdwgtw drdnteiari apfetwdnaw mnlpcaywpd rsasaaaeld aavrradhpa
      421 agqdlvdvag haartqvdda lhgrrgpldv htepgalppv lllaaerdaa tpyrgalelq
      481 rrlpgsslvt engagthgva fndnacvnky aeayllhgki pahkvycgpr aepvpgqqat
      541 raqhalpgk
//
LOCUS       WP_457685771             415 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457685771
VERSION     WP_457685771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41746
     Region          23..381
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,150,
                     153..154,157,238,241..242,245..247,250,278,282,331..332,
                     336,340,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mnqltdtgrr apatappqva rlrraislff aldgfvfagw vvripaikeq ihasagalgl
       61 allgvsvgsv atmlltgklc rrygnhpvtv vtaallslsv alpplthsal hlglvlllfg
      121 aaygglnvaf naaavdlaea vrrpilpsfh aafsagglvg aglggllapr lsplchllll
      181 tatglvvtay agrvllrtpg ppatgqvprr dgtdavpgcg raavgrtrlf vtvyglitlc
      241 taygegalad wgslhlsadl rtgpgaaaag yavfallmtv srmsgtwlle rlgdtpvlva
      301 ggllaavgml vgalapqlwl vylgyaltgl glanvfpvav ggagalagah gvavastlgy
      361 sgillgppsi gflaeayglp galttiaala alaallgrvv grgrvgrrgr rrapc
//
LOCUS       WP_457685756             395 aa            linear   BCT 27-JAN-2026
DEFINITION  cobalamin B12-binding domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685756
VERSION     WP_457685756.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Krautler,B.
  TITLE     Vitamin B12: chemistry and biochemistry
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 806-810 (2005)
   PUBMED   16042603
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Banerjee,R. and Ragsdale,S.W.
  TITLE     The many faces of vitamin B12: catalysis by cobalamin-dependent
            enzymes
  JOURNAL   Annu Rev Biochem 72, 209-247 (2003)
   PUBMED   14527323
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Marsh,E.N.
  TITLE     Coenzyme B12 (cobalamin)-dependent enzymes
  JOURNAL   Essays Biochem 34, 139-154 (1999)
   PUBMED   10730193
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472039
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="cobalamin B12-binding domain-containing protein"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41823
     Region          15..219
                     /region_name="MtbC1"
                     /note="Methanogenic corrinoid protein MtbC1 [Energy
                     production and conversion]; COG5012"
                     /db_xref="CDD:444036"
ORIGIN      
        1 mtlspapmte slagyvdhlw davvavdeht avrgvfdavd agvppedvll diiapvqhrv
       61 gehwaanrmt vaqehaatai ndrviaalah hrppaaaaer gritvacvdg ewhalparll
      121 aevlrlrgwr vdflgaqvpa phliahlhrt gpqavglsss iatrlptaha aitacqavgv
      181 pvlvggaafg pdgryarllg adawapdart aadflsrgmp dtrppalghq pvddlphlsd
      241 qeyslvarta pqlvketltq leerfpalrd ysdrqrqhta edlahitdfl atalytddde
      301 lfsgfltwtg silttrgvpa hslhpaldal saqlkdfpra rrilgharrs ldtgtrtgpg
      361 tgpgtrvdtg tgpgtgtgtd trtdtgpssg pgfsv
//
LOCUS       WP_457685778             153 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457685778
VERSION     WP_457685778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15576
     Region          24..141
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 magsgrtsae fdlaaaqqal aaqpfsrlmq aritefggga atleidiree lqqqhgfvhg
       61 gvlsyaadnt ltfaaatalg aaivtggfsi qyvrpargrt lraraqviqa grrqavcrce
      121 ltvldeegae svcavaqgta mplngpaggg geg
//
LOCUS       WP_457685791             439 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457685791
VERSION     WP_457685791.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45036
     Region          2..249
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(2..3,5..8,10,23,25,56,72..75,79,81,117,119,121..122,
                     124,134..135,138,157..160)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(2..3,5..8,10,23,25,56,72..75,79,119,121..122,124,
                     134..135)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(6,79,81,117,119,121,138,157..160)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,48,53,58..61,73)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(134..142,153..160)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mvgrgavgev wrafdeslgr pvavklllpq gsdpsaasrf rleaqtagcl nhphvvgvld
       61 fgehedrlfl vmelvegdsl arlagsgpll aervaliaaq aaaglaaahr qnivhrdikp
      121 anllldthga lkigdfgiar fvddpgaalt atgqivgtsl ylaperalgr pagpasdvya
      181 lgcvlyqllt grppfqadta lailhqhlda spvpprqlga slppafesyl lgllakqped
      241 rptadqaadw fgrgawrgap eplpqelpnq grrpapsavr gphitgpgta vpgtpipgta
      301 vpapsvgsvg gvsvraaete wkttvhraap hrprlpltrr srlvallgga alfsvallag
      361 ltwfspdtgt aqvpqaepsa lvnpslspsp assgtapsss ptpspsssaa qtadkktaap
      421 adpnkspkaa gkhggkgkh
//
LOCUS       WP_457685802             215 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685802
VERSION     WP_457685802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22481
     Region          7..201
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 maahsltvgf dldmtlidsr pgikavyqel sartgtfida dlaasrlgpp leheirhwfp
       61 eervaetaal frelypqyav aaspampgar eaidaihaag graivvtaky epnaklhleh
      121 lgldadalfg slwaagkaea lrkhhaqvyv gdhigdvvga htagalsvav atgpcdatel
      181 rnagaevvla dltefpswle ryvadgadgg dgaap
//
LOCUS       WP_457685809             566 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457685809
VERSION     WP_457685809.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..566
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=61427
     Region          274..564
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mattsgttgr sprtswgreh lanlyslfvl smimndapde sdvltralta vgalgpcrae
       61 aayltldngl trtpadwpda tphldaqvrr lggqggpvtv pdrewgwsla lrstadaigh
      121 lvvsapsrpt ddeyfllrvl aqqtaaaltq amarrterdr eqqlrqlsdd raatnarltt
      181 svselehqrs vhemltdasa nddgvqgiae alhrltgypv aiedrfgnlr awagpgrpdp
      241 ypkpeatphe ellqdaarrq rpvrvaeqvi alaqhrgevl gtvalidpea gageeerfal
      301 dyastalale lahlrnlaev elrlrrelvd dlitgtddas ayaraaavgh dlhgphylaa
      361 vqwtgrpadd tfvqavgrsa aglrmrslla rrsgmavlvl qgrpqakalh eavgrelgsp
      421 tgsigvggrc dtpseiprsf qealralevr qrsqsphgat tfdelglyri lgpgggyrev
      481 eqfvrewlgp lldydaahhs dlvqtlsqyf ecggnydata aalaihrstl ryrlqrirev
      541 sgsdlgavds rlnlhvatrv wkvlgg
//
LOCUS       WP_457685816             604 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457685816
VERSION     WP_457685816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63473
     Region          32..453
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtlglapkks hpkvprrhge ggkshltvlq glaalsldal ssvaygpeai vvvlvaagsg
       61 altamlpitl viagllavlv vsyrqviavh pdgggayava kkdlgrtvsl maaasliidy
      121 vltvavslaa gaaslasafp vlsdhllavc lialflltvv nlrgiadsar vlmlptvlfi
      181 vsvigvivvg lfrahpaatv gtsqsfpave algvllvlka fsagcsaltg veaianavpm
      241 frqprvkraq htelmlglll gamliglsll irshhvvprg gvtllaqlta galgtgwpyy
      301 aislivtlvl giaantsfgg lpvlmsvlak ddrlphlfal rserpvhrwg vvalavlagv
      361 mlvvvsadtq rliplfaigv fvgftisqig lvrhwsverp dgwlpralvn gvgavltava
      421 givllatkfl agawivvltv pllmllfsri eryytrvrdq lgldgtpprp trthslvivp
      481 lgrvdmiaaa alnaasslgd evvvvavfdd rtkadamrad warwnpgprl diidspqhsl
      541 vhpvigyveq varngrqvav lipqaeplhg ryrilqnqrg ilmagllssr tdvvvcllkl
      601 qldl
//
LOCUS       WP_457685820             453 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457685820
VERSION     WP_457685820.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..453
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=50302
     Region          77..444
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(90,118,293..294,320)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 mvrhrkrisr rgllvtavia tgavlapvav qavqaapadt aggkqnpvra leqaahplrs
       61 tepgrstadl ralgsmigea kvvglgeath gshefftmke rvfrylveek gfttfalels
      121 wsaglqiddy lqtgkgdark vaeealtntp wdheefvsli ewmrdynrrh pgrtvhfmgd
      181 digapavsde ffgrvtgyvr qnhpealprl nelytglrpi ddvfaylgkp laqrqqlatk
      241 aqqaleliss qkgsggeafe waeqnarsia qtakfltmnp ddpgtlpsfq rfrdevmaqn
      301 vtwwqqrtgh killsaqndh vghvagysel ypktqgsflr dtmgknylpi gftfnqgsfl
      361 skdaalggdw kkftvdgaep grnehtldqv ryrdfyldvr napaparawl nvarptlgvg
      421 tqfpvkprdv aiaksfdvli hlhevreadk rmp
//
LOCUS       WP_457685822             421 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457685822
VERSION     WP_457685822.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 421)
  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 421)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43857
     Region          31..202
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          213..421
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mairedaaas gpragfkdtv vrpataairq lasglgsals alfvllwlav tavtgpigvg
       61 llmapavlra lhalagrerd rlgrwgpevv apeppptqlr lalvdpttrr elrwlvrhat
      121 lgfllgvlgv llpisalrdg tfplwwrfap eevattslgl gnvqswpaav avgllglgwt
      181 avilgltpgm arlqarpgrr llvagpetdl slrvaeltat raaaldahat elrrierslh
      241 dgtqnrlvsv tillgaarrm vardlagade vlerahstae qalaelrava rgilppvlad
      301 rgltgalsgl aancpvpcri dvdvpercaa sveatayfvv aealtniakh sgadhatvma
      361 rsrggrlhlc veddgrggad edggsgltgi rrriaahdgn lsltspsggp ttlevdlpcg
      421 s
//
LOCUS       WP_457685828             280 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457685828
VERSION     WP_457685828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29922
     Region          16..>117
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          32..248
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 msqnlqtpla cqrtalsadg tpisyrtmgd gphlillgga lrtsddylpl asvlatsfrv
       61 hlverrgrga sgpqgphytl rkevedllav qsetgarlaf ghsygglvil etarsypvfd
      121 rtavyepgvp aapvptgwmg pyrerltagd sygafvhfiq gaggappila klpywylrya
      181 lrigfrgpsw qrmrpllaan laeheqvaaq qgklagfgav tasvlllcgs rsqlasktqf
      241 galreilpta vqetlnglnh fgpegktaav vaerarafll
//
LOCUS       WP_457685839             152 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457685839
VERSION     WP_457685839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16973
     Region          6..144
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 meyshsdtdl ikqpigywsw aaykaviart raalagigtt qpqwwalaqv asadtvktrd
       61 evsrllrnyl dvgpetmese idtitaqgwi iedaegrlgi taegrafydk aaalqgelwa
      121 erhadisdee ylttlkvlqr fihntggraw hh
//
LOCUS       WP_457685861              86 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy-metal-associated domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685861
VERSION     WP_457685861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..86
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9115
     Region          16..85
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mklfsrkdkt eadgprvell vegmhcnscg lliddeleei pgvrssttdm kagrttirlk
       61 egadldvaal vaaveqagey karpag
//
LOCUS       WP_457685876             250 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces sp. 900105755].
ACCESSION   WP_457685876
VERSION     WP_457685876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..250
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26326
     Region          5..183
                     /region_name="RNaseZ_short-form-like_MBL-fold"
                     /note="uncharacterized bacterial subgroup of Ribonuclease
                     Z, short form; MBL-fold metallo-hydrolase domain; cd07716"
                     /db_xref="CDD:293802"
     Site            order(36,60..61,63,65..66,141..142,162,182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293802"
     Region          <157..232
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
ORIGIN      
        1 mplsltvlgt aapyprpgrp csgylvrggg aevwvdagtg tfaelqrhtd parltaiwls
       61 hlhadhtadl aaaayayafg gltpaapipv yapqecaarl agffgrpdpg flsgifdfrp
      121 lydghavqhw nlrlaarava hgteayglra ecqgsvlays gdsgpcaalt elatradvfl
      181 ceadldrhre gervhltped agriareaga rellithvgp sltremaatr agavsgrlts
      241 varegeargf
//
LOCUS       WP_457685878             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457685878
VERSION     WP_457685878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20536
     Region          8..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msprgvatpd vrerlfaaae rvleksgpgg ltsraittea gcakgllhih fagldefvae
       61 lcldrfarta tkaqelpelv gqgavaanld avalalldsg gpviaglamt rpaaalrire
      121 aleggapgft aiqeaitgyl eaerrlgrla davdpptaal aivgtahhll mttwpgtpdp
      181 raqmtglvaa llgsppegap ap
//
LOCUS       WP_457685884              99 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy-metal-associated domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685884
VERSION     WP_457685884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..99
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9834
     Region          31..96
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 msncctpdgs cstsstnatq gatatvadar ttvyavagmt cghckttltk aigeiddvqs
       61 vevdiaagqv tvtsgdeldy avlakvvdea gyeltghaa
//
LOCUS       WP_457685885             747 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457685885
VERSION     WP_457685885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..747
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77663
     Region          9..746
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttiteshev elaiggmtca scaariekkl nrmdgveatv nyatekakvs yrgedlsvrd
       61 liatvegtgy taqesapvrt dspaaeakde pdelrplrqr lltavalaip viamamvpal
      121 qieywqwlsl tlaapvvtya awpfhraawt nakhgaatmd tlisvgtsaa flwslwalff
      181 gtagtpgmth afeltiarsd gagniyleaa agvtafilag ryfearskrk agaalkalle
      241 lgakevtvlr hgrevtlpts elqvgdrflv rpgekiatdg tvvegssavd asmltgesvp
      301 vevsvgdavt gatlnaggrl vveatrvgad tqlarmaqlv edaqngkaaa qrladkisav
      361 fvpiviglal atlgfwlgng ggltaaftaa vavliiacpc alglatptal mvgtgrgaql
      421 gilikgpevl ettrkvdtiv ldktgtvttg rmtliavhtd edetevlrla gslehasehp
      481 iaravaegaq qkvgalpape dfanvaglgv qgivdghavl vgrqkllaew eihlpaeler
      541 akaeaeaagr taiavawdge aravlevada ikvtspeavr rlralgltpi lltgdnrava
      601 esvaaqvgid eviaevmped kvdvvkrlqa egrsvamvgd gvndaaalaq adlglamgtg
      661 tdaaieagdl tlvrgdlraa adairlsrkt lgtirtnlfw afaynvaalp laaagllnpm
      721 iagaamafss vfvvgnslrl rafraqv
//
LOCUS       WP_457685894             353 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457685894
VERSION     WP_457685894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=35848
     Region          23..108
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 msgdesvaeq vyeagleiin pggepdvlrs aakgwrdlhe nlqtmfkdmd revqrtldsh
       61 wqgpaadafa ehwknldaam gktlpqlpaa aksldeaada ieeinsqihe iyleigisig
      121 vsvglsfltm gfsaaagaar aaqlatkaak laktlgtilr kvgqafntvs rlakehrflk
      181 nvlvtwasnt gstvmanslm gnetdlgdav wqgglsslag tgpalgigkv vggmrgavlg
      241 ggvgnvaggl avdgartalg envsggeflg nalvnsatga aggaavhaan thlppgregp
      301 hfsvdgiing tvygaggvag qplkdaltha geeskdtvap gdpakksvrd vfg
//
LOCUS       WP_457685927             378 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685927
VERSION     WP_457685927.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41377
     Region          8..358
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslthtgqdr pelqkaieei vdsgfagvql rvhdergewv gsagvrklge sakpptnghf
       61 rigsttktft atvvlqlvte grigldspvd dylprfgldr ritvrmllqh tsglfnhtge
      121 yyedgtvvpg ipwqgqewvd nqfhtyqpee lvrlalskpa rfepgtdwsy sntnyvlakl
      181 lieevtgrsl aeemqrlilq plglsgtvvp gaspdipeph ahgyyryeha gqwkvvdvtr
      241 fnvswvsaag dmisttedlh afvsalmsgk llpdsllaem rtphpksgyh ryglglfvee
      301 tdgggtifhh nggfagwaal mystpdgsrt ltaslttgda eldfaataea fqkahrrlvk
      361 evfcggqaev adkakpgq
//
LOCUS       WP_457685935             111 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457685935
VERSION     WP_457685935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..111
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11926
     Region          6..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mltlasevev larfgralad pircrlllal hdapahpsdl aeqlgisrtr lsnhlaclrd
       61 cglvvavpvg rrtryeladp rlghalddlr tavvaveadr scadaeekdc c
//
LOCUS       WP_457685965              91 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685965
VERSION     WP_457685965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..91
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9667
     Region          27..76
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mheqtneaqg arysptsira twagtgsved askalgfsra kgydlvrrge fpcrvlrigr
       61 strvvtasll rvlesgepey sgahtghcas s
//
LOCUS       WP_457685972             289 aa            linear   BCT 27-JAN-2026
DEFINITION  3'-5' exonuclease [Streptomyces nigrescens].
ACCESSION   WP_457685972
VERSION     WP_457685972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Viswanathan,M. and Lovett,S.T.
  TITLE     Exonuclease X of Escherichia coli. A novel 3'-5' DNase and Dnaq
            superfamily member involved in DNA repair
  JOURNAL   J Biol Chem 274 (42), 30094-30100 (1999)
   PUBMED   10514496
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="3'-5' exonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32660
     Region          121..>225
                     /region_name="DnaQ"
                     /note="DNA polymerase III, epsilon subunit or related
                     3'-5' exonuclease [Replication, recombination and repair];
                     COG0847"
                     /db_xref="CDD:440608"
ORIGIN      
        1 mnpnlplpds rppaprtles dpqtwndift ttidtvpvec irpidtdrps wgiyppgryr
       61 pddylgalha hdtdglwhvq ttgerhanfa davrtlrrpp twpherdrav awargllddp
      121 dllvidiqtt glrepfatqi samnahgelv ldellnpqad fepeastlhg ltrhntqhaa
      181 tfsnllstlt eifhgrhlva yniafdrdvl areltrhhhd avpadawlsa crwddailpi
      241 stwtglwsar hhtyrytrlg sryesaancr llfhrlqlla hsartlgdg
//
LOCUS       WP_457685979             307 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457685979
VERSION     WP_457685979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34565
     Region          31..92
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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          116..292
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpaarknqpe psasvlrlqa sdeqrpagrl lgdelrfhre rlgytladaa rvirgssskv
       61 srvergespa kprdvhdlal fyglsreqqg qldqllaqag ngdvyarfad vtpnflkrli
      121 rlertaqkif vfeprvvpgl lqteayarai vrmmevgtpd adieriialr mqrqvmldhd
      181 vptlavlice evlyrlygda gvmaeqigll lkatltdrvn vrivrkgamv ppypifhltf
      241 pdgdsqelay vehldaanyv tqkhqldkyr rildnvrada yervestaal eralqhweql
      301 aateqad
//
LOCUS       WP_457685987             418 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457685987
VERSION     WP_457685987.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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 418)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..418
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=44836
     Region          2..410
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mildlfagpg gwsralsvlg aqdlglewde wacktrtaag qltirtdvat yptwpfigrt
       61 hgliasppcq awsmagkrlg lidqplvhqa vsdlaagrdt realrgacrd vrsllaaepm
      121 rylhdlnsvg epewvameev pdvlplwkqy avilrswgfs vwtgilnaad ygvpqtrrra
      181 illasrvrta qppapthaki eepeglfgpg rtrwvsmaqa lgwgatdrpv ptvcagggpg
      241 ggaepfpsgs rkalstardr gtwtphpdap rqhssragte padrpsdqde qaagrpvpep
      301 dwswslrsnn qahatirpls epagtlffgh rsnectwvae paaspagdae ppvvpvpiri
      361 taqeagvlqt fpadypwagn kgqifsqign avpprlaahl laphlgktln pddftlaa
//
LOCUS       WP_457686037             373 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457686037
VERSION     WP_457686037.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..373
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39486
     Region          152..372
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkalaaclgv vvlspvllfg tatmmatasq aaqntgqfgd clttggntda atkkitkild
       61 gadskhvhik dltlpatqip naqtivttgi slnvsprgqv valatamqes rlrnldsgdr
      121 dsvglfqqrp sqgwgtaqql hdpvyattkf ykalekvhgw qqltiaqaaq avqksgfpda
      181 yakweslata ldkaitaslp hsaqgkntkg aspgassacv pgkdgsswgp ipegkvpkgy
      241 kipkgadpra rraigwamqq lgtpyqwggy ctnprgpdpm grcdcsslme kayahagvkl
      301 trttytqvhe gkavsanrlr pgdlifsrgt asrpehvgmf mgdglvieap rttkpvritp
      361 itdwtilaar rvl
//
LOCUS       WP_457686043             115 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457686043
VERSION     WP_457686043.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 115)
  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 115)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..115
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=12088
     Region          49..>109
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mrstriavsa amlgvlalpi asaavataas asaassaqva rpcdrpgpwv mgtkavtirs
       61 kpssksasvg vvyrghkftv hktrgnwhyi tdtttgergw vsgtyvyrqv ymcld
//
LOCUS       WP_457686055             397 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686055
VERSION     WP_457686055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          15..350
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,139,
                     142..143,146,219,222..223,226..228,231,258,262,311..312,
                     316,320,332,335..336,339..340,343)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msptaasarh srglltgyfl gmgvvmaiwg armpavqqaa hlttaqlalv llaaalgmva
       61 glkfggrlal perlptlltg gavglascla llgqchslvs llaaalafga thgvldvaan
      121 aaavrcqnay grsimsgfha ayslgalgga altattahtt htslflvtgl avavvalgaa
      181 patqtlsgad qpttptrrgt derrpplspa klwllgalaa gsllgegaaa dwaavhlhsl
      241 hattavsata fafysaamal grltgdrlht aigapavvra gamlaaagla tgvlaasvpw
      301 alagwavfgl glsttvpsli taagtggpra vatvavigyv gllagpalig alasatalpa
      361 alllpallaa avaalshral entapcpapp rtpaptp
//
LOCUS       WP_457686057             208 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686057
VERSION     WP_457686057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23474
     Region          12..202
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(16..20,117..118,149,174..175,178..179)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            144
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mprttthtsp davildyngv lgvqptttqw lrlahtatwe tdlaafqnaf wnarplydag
       61 qlsdqaywtq vlgfhpsrrl lrelrvadtn mwiitddrvl rvlhrahqtg lpmvllsnap
      121 ahlsdvldth dwrrlmthal ysarlevckp dpatyqhalh tlgsvhperv lfvddradnc
      181 saarrlglrt lhytgrpadl eaamlpse
//
LOCUS       WP_457686082             213 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686082
VERSION     WP_457686082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23855
     Region          22..89
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 mrhitthdap atglrsisdt swhtrgachg mdvedadavf fplprdheai aeakelcdwc
       61 pvrrdclnya lendlkegvw gglteaerrp whdglpqrld ysrviaffng rdvhlteser
      121 qivinhayvr gwhtdrlaaa lqighkhard llrqaalkvf drdrtlgvpr rkkkrtpstr
      181 ttrrptptkp dtkqpvsgpv pspstgaplg kaa
//
LOCUS       WP_457686092             439 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686092
VERSION     WP_457686092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47446
     Region          1..71
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mdalpkhpla iarflhglsq sdlaegikqa arrrdrragt tkqqvsvwer pggrapdawy
       61 qqliadvfgv dhdlvtalgw pywlpgneap valgtgatva alrkaqrram lnrrsllgla
      121 paalaalaqq watldpalas saadgqavap efvtwlessv khlagmatad rqhssqilds
      181 yydtvvglle nsrydqatgt rlyalassla qtigwhrfdh ehhtdaghyw saalhaahhl
      241 gdrdrgagil sdlayqsiwl dqagtaidvl dhalsrtqdp tarsllhlrk aralamngda
      301 racrrdlnaa ehalntataa ppawcswmsp adlavdsgrc lidlgetgpa lhqitqgval
      361 lptardktra vflayeaesl lnqgeidhsv atahealvla erigasrcvr qisdlardye
      421 phlkvqgvqq flhtvrtaa
//
LOCUS       WP_457686097             263 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457686097
VERSION     WP_457686097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27295
     Region          41..262
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mttpllappl tarplqgrva lvtgaatgig aataralasa gatvalghya qidqartald
       61 evrrlgadgi evsadltdpd avglmvsqvt sevgpvdilv nnagayprmt whetgeaaws
      121 raldvnltih yrmshavtpa migrqwgrii nvssvnarag rsgltaysta kagllgltrs
      181 larelgphgi cvntvlpgai qvdaenslpa hhrprpddqi arqcvprrgq pddvaaaiaf
      241 laapsasfit gqslhidggw llh
//
LOCUS       WP_457686101             373 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686101
VERSION     WP_457686101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 373)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109156
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..373
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39872
     Region          32..157
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18876"
                     /db_xref="CDD:467588"
     Region          230..>290
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
ORIGIN      
        1 mdtsasstsa aapgqpemsh eeyarsrhsv wlsaaalftd eigrvllvkp tyrtqwllpg
       61 ggaeagegpd qtcrrevqee lglsmppgrl lavhwlspgh pdltegmpfp gevryvldgg
      121 tltprdiatm rlpqdelsgy efldtraaae rmipvdaqim laalrarlag ttahlsggrh
      181 vgpvppldry qvhtrpragr dwpwhpghap ehlpipqawg wlfapdgrvv lvidpaepla
      241 mlpggtvept daspeaalvr eaaeeaqlal geverlgwvy datgevygri gecarlrlaa
      301 pitgagpslv dpasgrqfar llatphqaaa llgwgdqgyq qaeqaariar trwgiplaap
      361 spitelppkg gls
//
LOCUS       WP_457686110             315 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686110
VERSION     WP_457686110.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 315)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19271472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=34375
     Region          21..144
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          176..314
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 mneqtpqlap alppergqan asalihdgag ayllhlrdei pgiwepgsws ligggrepdd
       61 rsleetvrre lreeagldip dlvpfaveea rssdgtavpi qifagqwtgd paalpltegv
      121 mlhwfrpdvm prlrmapttl dlirrhaets saahrtphpr tarvatagrs tvlngigvhl
      181 ylenadgdvl lglrhpdsay agstwhflag hceqesalsc lvreaeeeag lliepgdvel
      241 ahvvhlvdsp ggrplmqvvf rarewsgtpa vrepdkctdw gwwhpdelpa pivpytraai
      301 egiragrlyt emgws
//
LOCUS       WP_457686112             673 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457686112
VERSION     WP_457686112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 673)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 673)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 673)
  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 673)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..673
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72310
     Region          67..658
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 msettpsadt pdprgkvpap rheplslppa ampagpasdd iaddmkeayw siydgaaaka
       61 tvgqilarlp rtvrqigqla wqadrratva vvvlqlvsaa msafglaasv avlqqlfaqg
      121 ptpdkirsai pqillvvafl saqalleagv avaqarvtpk irtalesefl rltahvrlev
      181 vddsdwhdda yrandrglfy arqivgqvvs lasaflglig tasvltvlhp lllpllplsv
      241 vpvgaaavrt ararfhsfrr wnamqrrvrv fswllldqys aaelradtaq qalldehhrl
      301 tsriaeedtr lgvsaalltl agrglggvga gityvalgam liagwlplaa gagaviaiqa
      361 srtsltrfvd vahlvyeham wvtdllafqe rcrtlqprrg kqvapetvka itlrnvryty
      421 pgkdspaldd isltlhaget vafvglngsg kstcsrliag lydpqegsvl wdgvdaadld
      481 teslqrrvat vlqdpvrfpf salanltvsr gtlteadpqr aldaarasga erviadlpgt
      541 wqallskrfr dgqelsagqw akiavargly kdapvlllde ptasmdprae hdvyqavlrg
      601 klrddqitvl ishrlasvvd cdriyvfdng riteagphqe lmalggdyaq mftlqaagyq
      661 ttsaasdsrt vhp
//
LOCUS       WP_457686114             208 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686114
VERSION     WP_457686114.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22825
     Region          6..192
                     /region_name="HAD_sEH-N_like"
                     /note="N-terminal lipase phosphatase domain of human
                     soluble epoxide hydrolase, Escherichia coli YihX/HAD4
                     alpha-D-glucose 1-phosphate phosphatase, and related
                     domains, may be inactive; cd02603"
                     /db_xref="CDD:319790"
     Site            order(10..14,111..112,144,168..169,172..173)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            139
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mppyeavifd fggvlttnld dcarafarrs alpddaylha vtvnpvgrhl faqlergdit
       61 qeawnvgiaq llgidgtdlm rraltplkpe apmveaarai raaglrtavl snsmgmspfn
      121 lyepwklede hdvvvlseqv rmrkpdpeiy qltlrqlgcr gpacifvddn eanlqpaqdl
      181 gittihaqqp dqtllrlgel lglpmtvl
//
LOCUS       WP_457686116             359 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457686116
VERSION     WP_457686116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36775
     Region          3..265
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnatqvrvgi igcgmvaaey attlaasdcv rlaacadlda eraatfayrh sipsapvddl
       61 lnpaavdlav vltppashsp larqaiaagl pavwvekpia vdpndaaeli ahaagagtll
      121 gvapdtllgp alqtaasalq rgligeihsa aatlystgpe rwhpapepfy aehvgplgdm
      181 gpyylaaldh llgplhvraa taatraerci rsgprsgtgf tahsptyiaa lletqegtpv
      241 tltasfdsag traphleihg algtlalpdp nfhtgdvlhr pygaptwsvv asvatagplg
      301 rgmgvvdlaq alhhgrsarc cpqraeritr laqtliatat ahppvpaqvi tntppspsq
//
LOCUS       WP_457685988             245 aa            linear   BCT 27-JAN-2026
DEFINITION  tryptophan synthase subunit alpha [Streptomyces nigrescens].
ACCESSION   WP_457685988
VERSION     WP_457685988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Watkins-Dulaney,E., Straathof,S. and Arnold,F.
  TITLE     Tryptophan Synthase: Biocatalyst Extraordinaire
  JOURNAL   Chembiochem 22 (1), 5-16 (2021)
   PUBMED   32677310
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Dunn,M.F., Niks,D., Ngo,H., Barends,T.R. and Schlichting,I.
  TITLE     Tryptophan synthase: the workings of a channeling nanomachine
  JOURNAL   Trends Biochem Sci 33 (6), 254-264 (2008)
   PUBMED   18486479
REFERENCE   3  (residues 1 to 245)
  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   4  (residues 1 to 245)
  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
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Miles,E.W.
  TITLE     Tryptophan synthase: a multienzyme complex with an intramolecular
            tunnel
  JOURNAL   Chem Rec 1 (2), 140-151 (2001)
   PUBMED   11893063
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Crawford,I.P.
  TITLE     Evolution of a biosynthetic pathway: the tryptophan paradigm
  JOURNAL   Annu Rev Microbiol 43, 567-600 (1989)
   PUBMED   2679363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="tryptophan synthase subunit alpha"
                     /EC_number="4.2.1.20"
                     /GO_function="GO:0004834 - tryptophan synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25389
     Region          2..235
                     /region_name="TrpA"
                     /note="Tryptophan synthase alpha chain [Amino acid
                     transport and metabolism]; COG0159"
                     /db_xref="CDD:439929"
ORIGIN      
        1 mfvpaglhpv saerrhldql aqaadlfevg latedavldg pviqtayhra lrrgnvldaa
       61 vravehaagl rptvvmtywe pvrrhgpehl arlfadagaa gvmvvdlpah qaarwhdtar
      121 eaglrtprli prtttdtslp aavagasgwl yapastaptg yqgaldlpal ghftrrlrga
      181 splpvvsgvg istpalaarv apvvdavvig tpvvralata pgraaevaas faqalhtpas
      241 letra
//
LOCUS       WP_457686117             372 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457686117
VERSION     WP_457686117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39159
     Region          38..326
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mpenarttpi yqyslltaap qhaivgdgil tgeistfdgk llpsleerva eltgratapa
       61 vdsgssalrl amrglgigpa heviipelgw vsigaaadml gatvrvapat dtltptweqi
      121 qplirpstra vvlvhlrgrp apgtseiaar ledlgiplie dcaqawgvdv egrpaggwgt
      181 latysthtfk liatgeggli vgddpdtmal mraiggdtrq htphavwrsk armtelaagl
      241 alpqldhlpt lltdlrslqq hvlealegih ginlvpdsts pvgngslvgl rlpntaaage
      301 lsgalfhagy rswwpgpgdl htaaawpvqp ehtltdpqry ldiqipwlpa pgrlawantl
      361 atcieqslag ar
//
LOCUS       WP_457686119             201 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686119
VERSION     WP_457686119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..201
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21052
     Region          4..186
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mtgsvlavma hpddlelwag gtlalhaqqa pvigavrahd dirdaeavts aeilgiqles
       61 lkdvdapavg elivrhrpdi lithpvddvh pdhraaaaav laglpdahia tgtprrlytc
      121 dtynsltlsg qvnasviidv tttfarkmra laahssqpie ehfgpmarhq sglwggrigv
      181 ahaeaftavp ilgrlpgaah l
//
LOCUS       WP_457686121             290 aa            linear   BCT 27-JAN-2026
DEFINITION  5'-3' exonuclease [Streptomyces nigrescens].
ACCESSION   WP_457686121
VERSION     WP_457686121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /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=31527
     Region          13..265
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mgavapshsq vaplllvdgf nvlwrghfgf papilsrdkq rnltglfaff allratirdd
       61 ldtppvevcv vldgengsae rkdsdadyka nrestpaale plqflapmke aldaygiawv
      121 eidnaeaddv iatltnrhpd rpirimsadq dyyqlldsdr vriinrarka skriitaaev
      181 herygvtpaq wpdyraltgd ksdnlpgvkg igaktaaall aggltldelp ssgrltgakg
      241 aaitdswtva lrcrelsrmr rdvpvgwqai ghvspalprp advieklgmw
//
LOCUS       WP_457686123             375 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457686123
VERSION     WP_457686123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  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 375)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39721
     Region          39..372
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtpnttrgiv fvlaswqmna pagierataa laaglaasgh haviatalat dpgpalpgvt
       61 vehldlsvdf pcadqllrka llrrtdaiqa rlweiiarhq adtvvftdal wglgrlaadl
      121 pdgvrrvlaa hvlpnqedap aaltradrvi ipseivraea eqagwpaksw rvvpnallhp
      181 psipdpvhid egrsgpvrvl arlghekgiv pllnaaadwd rplevtvaha gfeaasgsqa
      241 klldecralt gaadhitlhe rplawrdvpg wlagacvviv pslretfglv aleamssatp
      301 vvgyrvgnlp tlleqvdtgv qlladpglgp ntllgladal lqdpvaygrt akamyhlaqd
      361 yrpdriaqlf lkavs
//
LOCUS       WP_457686124             185 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457686124
VERSION     WP_457686124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Moynie,L., Giraud,M.F., Breton,A., Boissier,F., Daignan-Fornier,B.
            and Dautant,A.
  TITLE     Functional significance of four successive glycine residues in the
            pyrophosphate binding loop of fungal 6-oxopurine
            phosphoribosyltransferases
  JOURNAL   Protein Sci 21 (8), 1185-1196 (2012)
   PUBMED   22610485
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Vos,S., Parry,R.J., Burns,M.R., de Jersey,J. and Martin,J.L.
  TITLE     Structures of free and complexed forms of Escherichia coli
            xanthine-guanine phosphoribosyltransferase
  JOURNAL   J Mol Biol 282 (4), 875-889 (1998)
   PUBMED   9743633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0106130 - purine
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20010
     Region          19..166
                     /region_name="Hpt1"
                     /note="Hypoxanthine phosphoribosyltransferase [Coenzyme
                     transport and metabolism]; COG2236"
                     /db_xref="CDD:441837"
ORIGIN      
        1 mthipeheaq rvfrrrnpyl ltwdaceeal aqlasaiaet gpvtqvigia gggrtpaeml
       61 athlgapvch lqarhntsde lytqatgava vsipdsfpdt vrgrvlltdd icgtgatfta
      121 vtsaltprlt pdtriqttal crnvgsplrp rwwawdvddw vvfpwepgpd atgrplpape
      181 rirtp
//
LOCUS       WP_457686126             316 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Streptomyces nigrescens].
ACCESSION   WP_457686126
VERSION     WP_457686126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Grell,T.A., Goldman,P.J. and Drennan,C.L.
  TITLE     SPASM and twitch domains in S-adenosylmethionine (SAM) radical
            enzymes
  JOURNAL   J Biol Chem 290 (7), 3964-3971 (2015)
   PUBMED   25477505
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18433809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="radical SAM protein"
                     /EC_number="1.17.98.2"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33872
     Region          63..>180
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
     Region          70..306
                     /region_name="moaA"
                     /note="GTP 3',8-cyclase MoaA; cl47076"
                     /db_xref="CDD:481416"
ORIGIN      
        1 mtvrmfaaat ldatllvydp atelthlaph rlpvgrqlld dadvatwptv aqrqvstpvp
       61 fnicwspltr cnlqcpqcld dktlpelagt ertriarila gcgtlgldis ggeplllrdm
      121 thllktlasn gaavscttng whlqrraael apfldavrvs ldgpdaashd rwrgkgsfer
      181 aiagaraava ehvpvqlhav vmrstahraq sivdlahelg avgvtflqml pigdgaqlad
      241 aemvsdadaq htisslqapd gvrvrlrtre laegftvvra dgqvyrngqg atdirslrll
      301 tdpadlhipl pegkrp
//
LOCUS       WP_457686133             253 aa            linear   BCT 27-JAN-2026
DEFINITION  7-carboxy-7-deazaguanine synthase QueE [Streptomyces nigrescens].
ACCESSION   WP_457686133
VERSION     WP_457686133.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Bruender,N.A., Grell,T.A., Dowling,D.P., McCarty,R.M., Drennan,C.L.
            and Bandarian,V.
  TITLE     7-Carboxy-7-deazaguanine Synthase: A Radical
            S-Adenosyl-l-methionine Enzyme with Polar Tendencies
  JOURNAL   J Am Chem Soc 139 (5), 1912-1920 (2017)
   PUBMED   28045519
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Dowling,D.P., Bruender,N.A., Young,A.P., McCarty,R.M., Bandarian,V.
            and Drennan,C.L.
  TITLE     Radical SAM enzyme QueE defines a new minimal core fold and
            metal-dependent mechanism
  JOURNAL   Nat Chem Biol 10 (2), 106-112 (2014)
   PUBMED   24362703
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="7-carboxy-7-deazaguanine synthase QueE"
                     /EC_number="4.3.99.3"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016840 - carbon-nitrogen lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27375
     Region          19..246
                     /region_name="QueE"
                     /note="Organic radical activating enzyme NrdG/QueE
                     [Coenzyme transport and metabolism]; COG0602"
                     /db_xref="CDD:440367"
ORIGIN      
        1 mnagvlhlln qhatddrglf iaetfgptfq gegasvgrqa lfirlshcnl scgkgpgarw
       61 acdtpetwdf safdpadpki rrrlsldelm awvlsfppml vvitggepli qraglerlvt
      121 alhtvgrqie ietngtlhps sqlvaavtaf nvspklsaag ggegqrivpa alrafaesgk
      181 arfkfvvtgv aefreiaglv erfgmadvwv mpegtsadvv rqglrriade alvrgwnlsp
      241 rlhvelweaq rgr
//
LOCUS       WP_457686135             131 aa            linear   BCT 27-JAN-2026
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686135
VERSION     WP_457686135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Phillips,G., Grochowski,L.L., Bonnett,S., Xu,H., Bailly,M.,
            Blaby-Haas,C., El Yacoubi,B., Iwata-Reuyl,D., White,R.H. and de
            Crecy-Lagard,V.
  TITLE     Functional promiscuity of the COG0720 family
  JOURNAL   ACS Chem Biol 7 (1), 197-209 (2012)
   PUBMED   21999246
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..131
                     /product="6-pyruvoyl trahydropterin synthase family
                     protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14408
     Region          7..127
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mnvstgryri gksfafdaah rlaglpeghk cgrlhghtyt veivvtacgv tapgfvtdfg
       61 nlapvkkyld ehldhrslnd vlpceptsen larflaewfv eaveptidgr lekvrvsetp
      121 sswaefevtr p
//
LOCUS       WP_457686145             204 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457686145
VERSION     WP_457686145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=22104
     Region          22..203
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mdsatsyeat rvplpqtasr gvkvavaggf gvgkttfvga vseiaplrte aemtaasigt
       61 ddlsatpskt gttvtfdfgr atlsetmvly lfgtpgqnrf kfmwdtvlhg algvvvlvdt
      121 rrvkdcfpsl drvedeqlpy vvahnvfdde drahtlddir dalqmapgvp vlrcdardrq
      181 svqhvlialv qhvldrtdrr egra
//
LOCUS       WP_457686164             382 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457686164
VERSION     WP_457686164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43385
     Region          48..367
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mvdvgidpva gkrkqltrtf dtlkearaey aritsrrheg tfvppnkitv newidqwlam
       61 kaedleetti ynyritldrt rgklgqirlq elreedveew mhwalkhgrv rgdragtplg
      121 vtsvdmslar lkealgravt rrlvsvnaae hvtiprkark eerknkqevm pwnvqevqtf
      181 vhgimeerly aplllslmgl rpaevcglrw tdvdledasi iiantrtmmg nryvvekdtk
      241 smageralpl papvlaalts fkalqakekl algeayvasg yvlvhetgva ftikqlrrra
      301 yrlmdllglr rvrvydaras cftflankgv pdhilarwag htnvkttkrw yvkpdvedlr
      361 eaatawdglh gaptqhvrdc ei
//
LOCUS       WP_457686170             405 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457686170
VERSION     WP_457686170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42733
     Region          21..381
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maageevlvv gagvvgasva yhltrlgher vtvldsrgpe alpgstglap gfvgqlsatp
       61 elavlakdsv atyralsaaa depafwqvgc levatteerl aqahqdvahg rglgiearvl
      121 daaeavalap alvdaeralg alhipsdgaa dpaaltrllv aaaesagarf rwrtpvqale
      181 adrgrlvgvr tgtagellra drvvlatgiw gpvlaagvgv rlpmvdvqhp yvftaerpel
      241 ddtpidapiv rypdhavytr rhgrryglgs yahrplpwep satrdsaevp fqeadfgsal
      301 aearrlvpaf rqaspgrrln gvfaltpdel plvgpvaevp glwvaeaswv thaagvgrqv
      361 aamlletgrp tvdparlapg rfdhwsdrkv hetalghyrg iydah
//
LOCUS       WP_457686171             442 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686171
VERSION     WP_457686171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..442
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46511
     Region          18..436
                     /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 mddyrviaee laaeiaagrl rpgdrlpplr rfardrrias staarvyrel srrgltvgev
       61 grgtfvrtaa paiepalaep gearvdleln fpvlpgqpal lakslgyllr pdalagalrp
      121 vgavgtdvar qaaaahlarg dwapdprqll fagngrqava aaiaalvpag erlgvealty
      181 pvvkgiaarl gvtlvplamd ehgptpealr tapplravyv qpalhnplgh tmpagrrtel
      241 aeilreldly aiedaiygfl rhdlsplaal apertvvids lskrlapglt lgfltvpdga
      301 tqdfatalrt gtwtasrfal daatrwmadg taaaveeekr adaaarqria aerlagfrvr
      361 adpqayhcww elpdpwradt fvaaaarhgi avtpsgafai gpghapnavr lalasppldv
      421 lagaldvlag laqgapedtg ae
//
LOCUS       WP_457686165             605 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686165
VERSION     WP_457686165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=62209
     Region          392..597
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(399,440,486,579,582)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(399,579,582)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(399,440,486)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mrvrrwgtal tllltttalp atgpgtataa pagpaqsphr plplarhfdn ravsdnsapg
       61 aadfdgagrs lsaqdlaaag wspgsvltld gtrlglprta pgapdnvvad gqavavhgrg
      121 ealtflvagt ggtaagtgtv hyrdgsrssy eltapdwrsg plstkavalp hlntpggpsd
      181 esarlyavtv plragrevas vvlptadgaa galhvfavav rdsgrrtgsw aastagyrav
      241 gpwtdrtlrl vvhsgaggpr arirlantfa atpvdigaas iavrgagaaa drapvpltfg
      301 rghtgtriaa gaeafsdpvd ftvpagadll vsihlpgtvt aapvhqeaaq lsylsaagsg
      361 drtadaggta ypetltvwpf ltgveveggp gsivalgdsi tdgvkstsgt nrrwpdvlar
      421 rfqsqqalpr ygvlnhgisa nrivtdryqg dgvstdtggv saqhrlerdv laqtsartvv
      481 vfegindvrw gtssdeviag lralarrahe rglrvvvati apcegyhdct pavearrqav
      541 nafvranaga vfdatldfda virdpqrpqr mlpaydsgdh lhpgdaglka lgesvdlrkl
      601 lpgrh
//
LOCUS       WP_457686169             794 aa            linear   BCT 27-JAN-2026
DEFINITION  transglutaminase TgpA family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457686169
VERSION     WP_457686169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Uruburu,M., Mastrangelo,E., Bolognesi,M., Ferrara,S., Bertoni,G.
            and Milani,M.
  TITLE     Structural and functional characterization of TgpA, a critical
            protein for the viability of Pseudomonas aeruginosa
  JOURNAL   J Struct Biol 205 (3), 18-25 (2019)
   PUBMED   30599211
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Martins,I.M., Matos,M., Costa,R., Silva,F., Pascoal,A.,
            Estevinho,L.M. and Choupina,A.B.
  TITLE     Transglutaminases: recent achievements and new sources
  JOURNAL   Appl Microbiol Biotechnol 98 (16), 6957-6964 (2014)
   PUBMED   24962119
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Milani,A., Vecchietti,D., Rusmini,R. and Bertoni,G.
  TITLE     TgpA, a protein with a eukaryotic-like transglutaminase domain,
            plays a critical role in the viability of Pseudomonas aeruginosa
  JOURNAL   PLoS One 7 (11), e50323 (2012)
   PUBMED   23209712
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Aeschlimann,D. and Thomazy,V.
  TITLE     Protein crosslinking in assembly and remodelling of extracellular
            matrices: the role of transglutaminases
  JOURNAL   Connect Tissue Res 41 (1), 1-27 (2000)
   PUBMED   10826705
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     A superfamily of archaeal, bacterial, and eukaryotic proteins
            homologous to animal transglutaminases
  JOURNAL   Protein Sci 8 (8), 1714-1719 (1999)
   PUBMED   10452618
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Greenberg,C.S., Birckbichler,P.J. and Rice,R.H.
  TITLE     Transglutaminases: multifunctional cross-linking enzymes that
            stabilize tissues
  JOURNAL   FASEB J 5 (15), 3071-3077 (1991)
   PUBMED   1683845
REFERENCE   7  (residues 1 to 794)
  AUTHORS   Ichinose,A., Bottenus,R.E. and Davie,E.W.
  TITLE     Structure of transglutaminases
  JOURNAL   J Biol Chem 265 (23), 13411-13414 (1990)
   PUBMED   1974250
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12113409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..794
                     /product="transglutaminase TgpA family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016755 - aminoacyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83287
     Region          21..401
                     /region_name="TgpA_N"
                     /note="TgpA N-terminal domain; pfam11992"
                     /db_xref="CDD:463423"
     Region          371..547
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          668..737
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 msgrarlalt aaaatlmasc allplvspvt wlfqaafllt vqtgvgaaar rvplarpltv
       61 aaqalatllm ltvvfarsha iagvipgpdt frylgdllqq gsddvsryai papltpgirl
      121 mvlggvlvvg lvvdtlavtf rsaapaglpl lalysvaagl sdgptdwlwf lvaaagylml
      181 llaegrdrls qwgrvfggaa rtpggqesga vapvrtgrri gfavlslalf vplvmpsihg
      241 glldgagtgv gvgdgnggti savnplvslr dslnvdedrq vlsvrtssdd vsdlylrivs
      301 lddfdgttwk paqrhitgvp dkfptpaglg advrrttvts siaaadwyaq dwlpmpypps
      361 rvkvagtwry epvgmtlvgd hgqntrgety lvtsldvqpt aeqlaaapea saamkkeytk
      421 vpsslpsvva qtakevtags anhyeeavkl qdyfavtggf qydtqvevgr gegaianflk
      481 qkrgfcvhfs famaamartl giparvavgf apgtpqadgt vsvglkdaha wpelyfegvg
      541 wtrfeptptr gttpsytvsq tpgssvpdet lpskgasaap sasasqsesc tpqqrrqdac
      601 ggpsaaaavp sgdggppwwq lalwalggla vlavplspml yrqraravrl gahdrtpsgm
      661 aahtlavwle ltdtawdfgi lpdesqtprn aaarivrlgr ldpdaaasvh rvadaveqvl
      721 yaprpqptag laddvrrvta afngtvgvpa rlralfaprs svravwatsa gwarlrervl
      781 aarptlrkps eqeg
//
LOCUS       WP_457686173             381 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686173
VERSION     WP_457686173.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41938
     Region          32..331
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mphpdagnng gttggtsdaa tdgnvaygrk pfkrsrshfa drvtadgrdg wpveagryrl
       61 vvsracpwas ravisrrllg leeavslalt dpiqddrswr ftldpggrdp vlgirflsea
      121 ydarerdypg gvsvpalvdv psgqlvtndf qqitldfate wtalhrpgap dlypeplree
      181 idivmagvyr dvnngvyrag fatgqseyda afrdlfrrld llserlhdrr ylvgdtltea
      241 dirlfttlvr fdavyhghfk cnrfklaedp vlwayakdlf qtpgfgdtvd fhhikqhyyr
      301 vhtginptgi vpdgpdlsgw ltphhreelg grpfgdgtpp gpvppaeevp psgrpehllt
      361 gsdarphpgd gpdpgtpamr s
//
LOCUS       WP_457686175             773 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457686175
VERSION     WP_457686175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..773
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=80588
     Region          59..739
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mslprnpsga aalgasgdkg llrrtgewca rhfvvvlvlw lvalaglqfl qrtyggeysd
       61 dfalpgvqst rgrevlqehe pkaggyssqv vlhdaakplt dfrdeidgav talgklpdvl
      121 saqnplpspg appakpppgt pdvgplstdg rtayitvrfs vqpstlkpdy lhgvdsavrp
      181 lrsagvevey ggplgelarp epddrtsevi gfgvailvll vgfgsvlaag vplltaliga
      241 lcglaclgli aaafvfatvs ptlatmiglg vgidyalfli trhrqnlmdg adpvsgagra
      301 vatsgravlv sgctviialm glwvsgvsfi gklgvaaait vvsavlgalt lvpallglig
      361 rridrlrvrr piaetdagpg eaaqgtwhry aqrverrpww ylaggvvivv vlalpvfsiq
      421 mghigdgadp ksftdrrafd lmssafgpgs ngpltlvide savpqadrpm latqarkvlt
      481 dvpgaafitp lkatpdgavl tgtaystqap qnadttdlvn rlkhdllpea vkgtdahgyv
      541 tgttagqvdf ldivssrlpl iiavvvalaf viilavfrgv lvavkaavln vlsiaasygv
      601 vvavfqwgwg gpalgvsgtv piesyvpmmm faivfglsmd yeifllsrvh eawlrtadak
      661 asvahaleit arvitcaali mvsvfaafii sdnivvkmlg lglavsvlid atvvrlllvp
      721 avmtllgpaa wwtprwldri lphvrtegee qlpaegpprg daprsgarpg ggg
//
LOCUS       WP_457686177             643 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457686177
VERSION     WP_457686177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..643
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=68827
     Region          82..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msqffrpkrm mvgrpldsar lgetllpkrl alpifcsdpl ssvayateei llvvglggia
       61 llhltwyaaa aivlvlvvvv asyrqtcyay psgggayrvs aqnlgrsaal taasallvdy
      121 vltvavsvvs gvaaitsaip slgghdvals vgfvallalm nlrgvresgr vfavptygfv
      181 ffiylmfafa avrmatgahi raesadlplh avspytglal vllgmrafas gctaltgvea
      241 isngvpafrr pksrnaattl lvmgffsvtm fggitilaml ydvhvavqpt elglppgtpt
      301 stalaqiara tfgdldtlfy llqaftagvl ilaantafng fpmlasilae dgfvprqlhn
      361 rgdrlvfsng iillalaaig liilfdaelt rliqlyiigv fvsftlsqtg mvrhwrtvla
      421 apglpsrera rhrrsqaina vgavltgvvl iivlitkflh gawivviamp llflgmraih
      481 qhygrlerel avapgarpwe pagnhvrvlv nslhaptlka lgyaramrpt slealtvave
      541 pgdvrelraq wdahdidvpl qalsspyrdf tgpvidyild vcarypggav tvvipeyvvg
      601 rwweqplhnq salrlkarll ftpgvtvvnv pyrlpsgkep gea
//
LOCUS       WP_457686191             355 aa            linear   BCT 27-JAN-2026
DEFINITION  lipoate--protein ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686191
VERSION     WP_457686191.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kim,D.J., Kim,K.H., Lee,H.H., Lee,S.J., Ha,J.Y., Yoon,H.J. and
            Suh,S.W.
  TITLE     Crystal structure of lipoate-protein ligase A bound with the
            activated intermediate: insights into interaction with lipoyl
            domains
  JOURNAL   J Biol Chem 280 (45), 38081-38089 (2005)
   PUBMED   16141198
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Reche,P.A.
  TITLE     Lipoylating and biotinylating enzymes contain a homologous
            catalytic module
  JOURNAL   Protein Sci 9 (10), 1922-1929 (2000)
   PUBMED   11106165
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Morris,T.W., Reed,K.E. and Cronan,J.E. Jr.
  TITLE     Identification of the gene encoding lipoate-protein ligase A of
            Escherichia coli. Molecular cloning and characterization of the
            lplA gene and gene product
  JOURNAL   J Biol Chem 269 (23), 16091-16100 (1994)
   PUBMED   8206909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="lipoate--protein ligase family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="6.3.1.-"
                     /GO_process="GO:0009107 - lipoate biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /calculated_mol_wt=37776
     Region          106..354
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
ORIGIN      
        1 mqgrhhgeyk vpggklvvvd lavaggvlrg vrvagdffle pdealeaing alegapadaa
       61 ardlaarida alpagaalfg fsseavgiav rravadaaew tdfdwqiiha gpqppalhma
      121 ldevltseva agrrpptlrv wewdrpavii gsfqslrnev dergaerhgv tvvrrisggg
      181 amfvepgnti tyslsvpqsl vqglsfaesy aylddwvlaa lgdmgikawy kplndiatea
      241 gkiagaaqkr fasgagavlh hvtmsydida gkmtevlrig keklsdkgit sarkrvdplr
      301 rqtglpraev iermiasfra ryggsdgmas daelaraqel aagkfssrew lgrvp
//
LOCUS       WP_457686200             181 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457686200
VERSION     WP_457686200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19002
     Region          12..169
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtvhaaepaa pvthtvldgt pvgpltlvaa gealsglymt dqrhrppqet fgdpadpdel
       61 pfaetiaqlq ayfrgelttf dlplalhgtp fqrrvwaalc aipygetvsy gqlaerlgap
      121 sasravglan grnpvgiivp chrvvgangs ltgygggldr krrllafert edglfpaeac
      181 g
//
LOCUS       WP_457686204             183 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457686204
VERSION     WP_457686204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19174
     Region          17..154
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mqdeergpmg gpggrrivag vsgslgslta lhrataearv tgaelwavla weppggeish
       61 rggpcpapma awrrmanerl ltalkdafgs agpevplkcl virgkpgdal laaadrpddl
      121 lvvgagargr lrravwpcva rycvaraccp vlavppsplh haldavhrrn awklpldare
      181 lad
//
LOCUS       WP_457686229             501 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457686229
VERSION     WP_457686229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53117
     Region          28..482
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mthrlppssp rptgnehsgp ddsgpngssp dgsgpgnlhr glqprhiqmi aiggtigvgl
       61 flgsaealhd agpgllltya vagvvvffvm ralgellvyr pvsgsfatya eefignwagf
      121 atgwsywlmw vvtgtaelta agiyvqywwp evpqwlpgli alailgvanl aavrlfgefe
      181 fwfalikvlt iivllvmaaa ilifgfgplg esaslsniws hggffphgma gpllalqvvv
      241 fafvgvellg vtageskdpd ktlpsavrrv iwrialfylg alaavmalvp wnqldphvsp
      301 fvlvfakvgi paaagvvnmv vltaalsscn sgvfstgrml ltlardrhap aafgkvsrqg
      361 vpaagilasm avmllgvaan yfvpeeafay vtsvatvaav ftwgmiacah lryraavrag
      421 rlrpvafrmp lapvsnyfvl aflglvlvll afdtesrial yvapvwaaml vagyfltrhr
      481 raagpqdapp deeiaepsrs r
//
LOCUS       WP_457686231             540 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686231
VERSION     WP_457686231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..540
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56406
     Region          225..526
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpvmslqrll dsvgpavlsg vcapggtavp vgdvviaepd ggfdlrpgdv vlgvnltdha
       61 qslrllslca ersagalllk apaavdetvv taasaaglpl vqveqqagwa qvvsllravl
      121 dsegyvdsgs gtagaeagdl fgladaiaav idapvtiedr ssrvlaysar qergdearva
      181 timgrhvpde vnahfrrygv fhkiaqdtgp iyvpavvegt kprlvvpvha ggdvlgsiwa
      241 ivpgpvpaer aeafadtaat aalhllrrra gadverlvlt dmvatvlhgq egaadaarrl
      301 glttgpwrvi avgvrceddg eaerqrltvw ermsrfrgsr lrspaaivgg vvygivpaer
      361 vapgaddgsg wletllgtag rpaplvavgg laasvpglar sreqaddtld llrtgliard
      421 qavhdevwat vvlrhvarsa aatriagvgp lqqlvdhdra hgtncvptlh awleamgdpr
      481 aaaarlhihp ntlrhrmrrl qdvvalpldd pevrtalllq ltarqysteg gpddtvsasa
//
LOCUS       WP_457686236             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686236
VERSION     WP_457686236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21020
     Region          20..66
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          77..188
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mseerhgtrr sggprkaqei fdatldllae kgyegltieg vaqrsgvnkt tiyrwwpskg
       61 allgaaliga rrldftppdt gslagdlesl lrtvvtlltt rpssdiavsv lgaatqspel
      121 avhmreffad rialeqpvfd ralargelap dtdtmllvdl lagaawvrvv lrqlpldkdf
      181 vsravgtvln galart
//
LOCUS       WP_457686240             452 aa            linear   BCT 27-JAN-2026
DEFINITION  vanadium-dependent haloperoxidase [Streptomyces nigrescens].
ACCESSION   WP_457686240
VERSION     WP_457686240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="vanadium-dependent haloperoxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140905 - haloperoxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47928
     Region          201..425
                     /region_name="PAP2_haloperoxidase"
                     /note="PAP2, haloperoxidase_like subfamily.
                     Haloperoxidases catalyze the oxidation of halides such as
                     bromide or chloride by hydrogen peroxide, which results in
                     subsequent halogenation of organic substrates, or
                     halide-assisted disproportionation of hydrogen...;
                     cd03398"
                     /db_xref="CDD:239492"
     Site            order(304,311,347..349,398,404,408)
                     /site_type="active"
                     /db_xref="CDD:239492"
ORIGIN      
        1 mdtsrsrrra avgavtalll laltavagpt aaveshsppa adpaairdwn viatdtisan
       61 lgptrpsgqv viwhgfvsaa vynavvgiqr tyapykwrar gpstaspeaa avtaahrvll
      121 tyfpasqapl daayadslak ipdgrakrqg vafgeraaah lielreddgr fapveftaap
      181 apgvwrptpp ahlpfidpwl atlrplllts paqfrpgppp alssaryaqd vnevkvmgak
      241 tgsartaqqt etalffggnl avqfqsafrd htarhhldia dtarifaagn asatdavvta
      301 wdaklhygfw rpitavqlad tdgnpatdad pqwqpllvtp phpdylsght tvagavirtl
      361 tgilgtthid lnvpseitgt trhyaeagqf nedminarvw agihfrkadv vgcragtrig
      421 vwalthyfsp lrpagrhamp paqqlcppgs as
//
LOCUS       WP_457686250             495 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686250
VERSION     WP_457686250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52469
     Region          <185..>269
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          398..482
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mipavrrtgl lcaltataal lpaapapaap pppalhfgac pdsvptppap ervecgrlsv
       61 pldrshpdgq hldiavsrvr asgpaserrg vllvnpggpg gsglpyavtk raklpeqvrr
      121 sydvigfdpr gtgasapadc gpmgglfdsp gqdpvptgra aeqkyldglr rtaddcakhv
      181 kdalphlstt etardmdair ealgerrigy lgvsygsylg aayaaqfpqr vgrmvldsvv
      241 gpeewydfdl lqsramvrqr avffawaarh ekrfglgadg tavrtayqrv rdglaerpvd
      301 gfgaaefdra vyralgrter wagladglrt ylrdgttgpl rpaepfdgpa srtyeaanrt
      361 vkcadgpaps parvvadirr mrrldpqpvl tgmeasvcay whhkpahgtp lgspdappvl
      421 liasehdpvt piegaralqr rlpgsrlvsl hddyshgvfa srgngcvdga aaayltdgtv
      481 pradvhctgp glptp
//
LOCUS       WP_457686259             689 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457686259
VERSION     WP_457686259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 689)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 689)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 689)
  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 689)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..689
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73174
     Region          33..617
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mpdeaetgge elqfvdrtgs reragqqirl admarrlprl vrrsvalaws idrwaclgll
       61 vcqvasgamq algllavsgt iaallaggdi ygrllaawps lvmlagaaaa rallgitvaw
      121 lssrlgpqms reaelgllra vtevelsayd apgfnhrkea aergaevaqd lvtegqdlia
      181 slasliagag vltalhpall pllalasfpq avaqisaarv rylarlrsng dyrllsilrw
      241 hvgdryaadq iragtmssfl vgryrhitdr inradrraad tgarmsvlga lcggvasaav
      301 waavvwmlat grmsvghagt avfalqtvgm alrglvvgga rimrtglymd dwsaflreag
      361 gyrmnrgatv pgppqqitvq dlvfryeeaa ndavrgvsft lrrgevvalv gyngsgkttl
      421 akllsglylp ttgsvtwdgv ptgeldpqam wshvalvpqd yarwpltare nmtlgqptsg
      481 gdadihaaca rsgadevlte lrsgldtvla rdwlggqels ggqwqrialt rafyrpagll
      541 vldeptaald plgehrifag lrklaatrav vlithrltnv acadrilvlh kgrivqqgtf
      601 pelvaepgpf rdlwayqhtr eaadpadgrs addcvpsahp apgvpvpvpa pqpaphgdtv
      661 prtrkstege rtsasaeaet daeaeaeap
//
LOCUS       WP_457686260             407 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457686260
VERSION     WP_457686260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44665
     Region          4..406
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mpkataaevg rvfreeygra vavlvrvfgd idvaedavqd afstaverwp saglppspag
       61 wiittarnra vdrlrreasr ddrhaqaall haggepaeeg pvrddrlrli ftcchpalap
      121 aarvaltlrl lgglttaeia raflvteptm aqrlvrakgk irdaripyrl padadlpdrl
      181 ravlavvyli fnegytassg eslvredlcr eairlgrllt ellpdepeav gllalmllte
      241 srraartgpd gdlvlladqd rsrwdgtlva egqalvrrcl rrnrpgpyqv qaainavhsd
      301 aptaadtdww qilqlydqll aldpspvval nravavaeve gpeaalalvd slpldryhvf
      361 hairadllrr ldrnaeaaea yekalartdn taerhflqrs rqalprd
//
LOCUS       WP_457686274             431 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457686274
VERSION     WP_457686274.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43628
     Region          9..363
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 magsvgsvgp gelqrrlgvt davvvglgsm igagifaala paaaaagsgl lmglalaavv
       61 afcnatssar laarypasgg tyiygrerlg dfwgylagwg fivgksasca amaltvgsyv
      121 wpgqahavav aavvaltavn yagvqksawl trtivavvla vltavvctal tsgqadtvrl
      181 digddtsftg vlqaagllff afagyariat lgeevrdpgr tipraiplal gitlvayaav
      241 avaalvvlgp rqlaeatapl sdavraagad wlapvvraga alaalgslla lilgvsrttl
      301 amardrhlph vlaavhpkfk vphraelvvg aavaalaata dvrgaigfss fgvlayyaia
      361 nasrrgsprr pvcggrlrpa trrrererag ggpwrtgpag dvvvvvsngp prtlssdrir
      421 kawsagtcrp r
//
LOCUS       WP_457686282             314 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686282
VERSION     WP_457686282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33445
     Region          14..301
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msceadaaav arpplrsllf vpgtrtdwlp kaqaagadav ildledavpe qdrasaraqv
       61 geaiaqaaad sadhpalfvr inpldgwaea eelrtivrpg ltgivlpkvr haqdvrfadr
      121 lldwcereqg lhrgqialvp lletarglre aydcaaaasr vaylgaltga ggdveravgy
      181 rwspegtetl alrsrvlldv raagslhpva glwtriadla glrsfaeqnr slgyegmmai
      241 hpshisvine vfspgadela rcarliaave eaqangagav sfegemvdea maatarlmle
      301 rhtrhravrg srss
//
LOCUS       WP_457686283             447 aa            linear   BCT 27-JAN-2026
DEFINITION  CitMHS family transporter [Streptomyces nigrescens].
ACCESSION   WP_457686283
VERSION     WP_457686283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Korithoski,B., Krastel,K. and Cvitkovitch,D.G.
  TITLE     Transport and metabolism of citrate by Streptococcus mutans
  JOURNAL   J Bacteriol 187 (13), 4451-4456 (2005)
   PUBMED   15968054
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Krom,B.P., Warner,J.B., Konings,W.N. and Lolkema,J.S.
  TITLE     Complementary metal ion specificity of the metal-citrate
            transporters CitM and CitH of Bacillus subtilis
  JOURNAL   J Bacteriol 182 (22), 6374-6381 (2000)
   PUBMED   11053381
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Boorsma,A., van der Rest,M.E., Lolkema,J.S. and Konings,W.N.
  TITLE     Secondary transporters for citrate and the Mg(2+)-citrate complex
            in Bacillus subtilis are homologous proteins
  JOURNAL   J Bacteriol 178 (21), 6216-6222 (1996)
   PUBMED   8892821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..447
                     /product="CitMHS family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0046942 - carboxylic acid transport
                     [Evidence IEA]"
                     /GO_process="GO:1905039 - carboxylic acid transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=46664
     Region          1..447
                     /region_name="CitM"
                     /note="Mg2+/citrate symporter [Energy production and
                     conversion]; COG2851"
                     /db_xref="CDD:442099"
ORIGIN      
        1 mlaalgfsti gifllltmtk rvsvlvalvl lpvlaglagg fagelgemvl dglstvaptg
       61 imiafavlyf slmvdaglfd plirgilrva rndparitvg tavltmcval dgdgastfli
      121 tvsallpvyk rlgmsplvls gvvclaagvm nmipwggptv ramaalklds sevftpvlpa
      181 mgcglawvll asyligrrer crlgaltpqg eadagterdg cehptrmagd gpgtpwvpar
      241 prtwpsifnl vltiallvsl vlevmplpvl falaftlall vnrptwegqq allekhaksv
      301 vlvttmifaa gvftgvltgt kmitemaeaf vsvvpdslgg hlpvlvavtg mplslaftpd
      361 ayyfgvlpvl setaagfgtd qaevaraail gqmttgfpls pltastfilv gmsgvqlgeh
      421 qrfifrwafa ttlvmtaaal ltgafsl
//
LOCUS       WP_457686289             289 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase [Streptomyces nigrescens].
ACCESSION   WP_457686289
VERSION     WP_457686289.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29684
     Region          19..279
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mngpspgalp gplvgtdwva prlgtpglvv ldasigghrd ageripgarp fdidgalsdh
       61 sgplphtmpg gghftremra lgvddgdtvv vydgaglyss arawwmlram ghdrvavldg
      121 glpawraagl pletgaptpa arpgdftarp rpgliagsde vsaaltdpas avldarardr
      181 fagavaeprp glrpghmpga lnlpfgelqr dgrmrpasql rdafaplagd rrrlffscgs
      241 gvtacilalg aelagyddla vydgswsewg lpdadrpvvt gpqsggpsa
//
LOCUS       WP_457686295             539 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105755].
ACCESSION   WP_457686295
VERSION     WP_457686295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 539)
  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 539)
  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 539)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19857310
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..539
                     /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=59348
     Region          11..318
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
     Region          177..373
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mvsvqsppds relslarvll lpailmaaat vaavvlvags ariavgvcga vgmllvlata
       61 aeavrrgrrl qdaraehdrh raylerrlta seeeiehlgr evfptalyrl kagespkevv
      121 rqlfdvdprm rhapesqrrl irimldivde edlqrdsler sfvsvarrvq aivhqqahel
      181 remeedhgrn pevfddllri dhgtaligrl adsvsvlggg rpgrqwpnpv alysvlrgam
      241 srileyrrie lhsicqvnik gtsvepviha aaelldnatr ysppstkvhv tavevqsgvc
      301 ieiedagvtl neeardrleg llekakqgkd iqvlgenprl glsvvgrlck tynmdvslra
      361 sayggvravl ivpsdmmttd papgiahgig atgipkpelg alegpkrppk rrrptsprip
      421 agismeddvp evtewtaggl pqrrsrmktp lsqriaeqaa ieraeregnp tiwsqhkepe
      481 pepeperrep glwvdafweg lkknnpgvhp tdftrnptky lhlindpagt eaddegdlk
//
LOCUS       WP_457686301             304 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457686301
VERSION     WP_457686301.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  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 304)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10015415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32962
     Region          19..279
                     /region_name="mthyl_TIGR00027"
                     /note="methyltransferase, TIGR00027 family"
                     /db_xref="CDD:272862"
ORIGIN      
        1 mvgtahrntg vedveggvgl tallvaaara iethrhdsla rdvyaehfvl atpacagwpv
       61 rmqqvpdgda nplwgrfary fglrtrvldd fllrsmhaga rqvvllgagl dsrafrldwp
      121 pgcvifeidr egvlafkhkv lgglsatpka vrvpipidlr adwvgaltda gfdtaapsvw
      181 laegllfylp naaetylida vdrlstegsa lafevklekd llayrdsply tstkhqigid
      241 lltlfdrepr pdsagnlaak gwstsvhtpf dftrrhgrgp lpeqndalag nrwvfankpc
      301 aagt
//
LOCUS       WP_457686307             214 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457686307
VERSION     WP_457686307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  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 10172259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=23094
     Region          57..207
                     /region_name="SRPBCC_Smu440-like"
                     /note="Ligand-binding SRPBCC domain of Streptococcus
                     mutans Smu.440 and related proteins; cd08862"
                     /db_xref="CDD:176871"
     Site            order(59,61,63,72..74,76..77,92,104,106,108,110,127,129,
                     138,140,154..155,157,159,168,170,172,174,186..190,
                     192..194,196..198,201)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176871"
ORIGIN      
        1 msgirstgvr aalftaplll gllgtaaapa gavgshtshp dksltcrgkg vdpdalvrhr
       61 teivinaplr tvwklqtdve rwpswqtpve tverldhgpf rkgsafrwtt pippnpstpa
      121 tslditstvq qikrnscirw tgpaigeglr iegvhvwnfs kvkggvrvst eethtgaqve
      181 advptatkll regleawlrd lksaaearah nrpn
//
LOCUS       WP_457686310             300 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686310
VERSION     WP_457686310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32384
     Region          1..256
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msrhlevger ivrtealhgg itaemrrlti grpdggtrdl vlrtfvnveh aedwlnreag
       61 altlltgtgv papglvavdp aaahceypsl lmthlagrtv lddegletrv pllarqlvai
      121 halrpaerpr eyvawttadt vvtpkgadaa awaaaidvir rpapryegrf lhrdfqpgnv
      181 lfdvsppesa garitgvvdw aatswgpadl dvahcstnla llhgpawglr faeayeeagg
      241 vlaaaaserl ywqvrdglaf seevqlvaqp wreagraelt traveerlda yvtalmdalg
//
LOCUS       WP_457686315             243 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457686315
VERSION     WP_457686315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25183
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkfaviggtg ligsqvvkkl naagheavph spstgvdvit gqgmeeavtg adgvvnltns
       61 ptfddaspaf fqtsmdnlla aghkggvghf vilsivgadq vpdlayyrak vlqedilkag
      121 pvpysivrat qfmefinafm swstegdtvr lpttplqpia aqdvsdtvae vaagtplngt
      181 lnvggpdvhp ldelgritln arpdgrtvvt ddtagmfaav ngdalttkgd ariapthytd
      241 wlt
//
LOCUS       WP_457686321             734 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457686321
VERSION     WP_457686321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..734
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77130
     Region          28..708
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdvvvrsva ggrarltvpw vrarpgsagl vderlmgvrg fralrifprt gsvviwmapd
       61 lldidrlvaa ldeapptstp akatrsvpds stgelarlvv ggavlafval rrllrrprit
      121 agssgllgai tlftglpffr galrslrgrs hpgtdilvta atvislvlre nvvalavlwl
      181 lnigeflqtl tlrrtrraie elltigeerv wlvrdegadg agrveteval devtpgdvva
      241 vyehhripvd ghvatgealv dqaaitgeal pvyaragaev yagtivtsgs ltvratavga
      301 dttvgriisr veeaqsdrap iqtvatrftq rfvpvsfala altyvvtrda rramtmllia
      361 cpcaaglatp taisaaigng arrgtlikgg thlegvgrvs tvvfdkigtl tyghplvtsv
      421 vtlsdrhtan evlslaasce lharhplaqa ivahteeqhl raplhqacev vlgmgmrael
      481 dgtrllvgsp allrqhgvel tqqaqgwteq frgsgetvic iahddeligl lgvsdavrsg
      541 agsviqqltd lgvsrlillt gdapetaqvv adtlgitevh ahalpegklq lirdlqtegh
      601 tvamvgdgtn dapalaladv gismgahssh valetadial pgddlrqvpa vvelsrhtlr
      661 vvrqnyglai gvdllglvag aggsinpvla allhntssia vvansarlvn htphlpqtad
      721 dmltaapled rrvr
//
LOCUS       WP_457686328             271 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457686328
VERSION     WP_457686328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27739
     Region          22..244
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msekrvvlvt gggtgigaat arllctaghq vvisgrrpep lrrvaeetga lahpsdaadp
       61 eavrelvett vtaygrldgl vlnagigrgg avgdtavedw eelirtnltg pflllraalp
      121 hllaargvvv avasvaalrn svgnaayats kagllhlcrs lavdygpqgl ranavcpgwv
      181 rtemadqrma rfaaeaglag gaeaayeean rltpagrpgd peevakaidw llspaasyvn
      241 gavltvdggv ttvgvggaaf dhrieartpr l
//
LOCUS       WP_457686330             688 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 31 protein [Streptomyces nigrescens].
ACCESSION   WP_457686330
VERSION     WP_457686330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..688
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76383
     Region          142..245
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            180
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          245..577
                     /region_name="GH31_xylosidase_XylS"
                     /note="xylosidase XylS-like; cd06591"
                     /db_xref="CDD:269877"
     Site            order(262,290..291,329,404,406,459,473,476,509,539)
                     /site_type="active"
                     /db_xref="CDD:269877"
ORIGIN      
        1 msppdgtrpa psastsdaag tssrppassr pavclefgda ehvlrvepwg adsvrvrsar
       61 hrvrddlpga lsvppaaaaa elgvgphgsr iltvgrlrve lsprghlrfa rtpdgtellr
      121 esvghfawpg prqftpvgeg ryqleqrfaa ydgeqffglg qhshgrldhk hmvidlvqrn
      181 gevtipftls srgygllwnl pavgrvelaa hqtrwvadaa dqidywittg ptpagimany
      241 adatghapal pewalglwqs rlryrtqeel lgvareyqrr glplsviavd ffhwphlgdw
      301 rfdaadwpdp agmvaelasm gvrplvsvwp svsvvsenyp hmrderlllg tehgqpfqhv
      361 fpdsqvddks lpvvfydptd erardyiwsr ikrnyydlgf rlwwldacep emypeqfgnl
      421 ryaagpgrav anlyprehvr gffehmraeg edvpvslvrs awsgsqayga alwsgdipat
      481 fealaaqvra glsaglsgip wwttdiggfh ggdpddpdyr ellirwfqfa vfcpllrmhg
      541 hreprdafaa grtggpnelw sygqdayril trqlrlrqdl raylhrqmvs aadcgapvir
      601 plffgfpddp aawtvedqfl cgpdllispv trlgerrrqv ylpagadwra aatgtvqdgg
      661 rtttadaple cipvfvrrgs tldvrfpg
//
LOCUS       WP_457686332             414 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686332
VERSION     WP_457686332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 414)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Domain dislocation: a change of core structure in periplasmic
            binding proteins in their evolutionary history
  JOURNAL   J Mol Biol 286 (1), 279-290 (1999)
   PUBMED   9931266
REFERENCE   6  (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   7  (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 11450659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="sugar 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=43022
     Region          11..414
                     /region_name="MalE"
                     /note="Maltose-binding periplasmic protein MalE
                     [Carbohydrate transport and metabolism]; COG2182"
                     /db_xref="CDD:441785"
ORIGIN      
        1 mrtsvecrri rsigtlaatv taaglllisc ggdgspprpt esgkitltem dyyssepgrs
       61 alakqltrcg kpagvtikrq ivpdlrtkvl qlansralpd lilldnpdlq qlaatgalad
      121 lgaagvktdg mypnivaagk yrgkqygvap gvnqlalyyn tstlekagvk ppatwdelri
      181 aakkltqgdk vhgigfavpa teegsfqfes fffsagaslk kldspdavsa lsllkdlvas
      241 gsapkdvlsw nqmnvgeqfa ngslamming pwelpllrka gmkdfgivpv papaggtssg
      301 alggevwaag sggdksrkaa evikcmvskg nslewakltn yvpsdpevaa efsaavpamk
      361 tfvetigsak srtaevgpdy ptysqalwta vqaalsgsks pgaaltdaqk qatq
//
LOCUS       WP_457686340             375 aa            linear   BCT 27-JAN-2026
DEFINITION  tetratricopeptide repeat protein [Streptomyces nigrescens].
ACCESSION   WP_457686340
VERSION     WP_457686340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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 375)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18770923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42013
     Region          9..255
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          9..117
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(9,12..13,15,39,42..43,46..47,49..50,73,76..77,
                     80..81,84)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          9..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          37..67
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..102
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mttlhpaveq aqalidfery dqarallaqh lvedpgdtra wielgychlk mqqpeqalea
       61 adealkiape dfyvlilrak altsgpnssw raaepvlrea vradpqhwyg ytmladavcr
      121 msmvrffqan gsrkpephev dlvyreaadl asealrlgpe evyaheiahq iatfsgnitr
      181 adqlerailr ldpthaeala aqtrkaaeap gvkapqaadl yatglasapd stelqrgldq
      241 atyrmlrgvr wlallcvcls gagmdlfave gevqrelplp lgqrlwdlvp mtaiwlvgal
      301 lryrrrragv rlnvqslirr rrwarivvaq avwamlcall itqvpweert lpqvllwagi
      361 aptfatiwfd rnktr
//
LOCUS       WP_457686341             444 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457686341
VERSION     WP_457686341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 444)
  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 444)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 444)
  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 11440662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46662
     Region          144..412
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 msaespliks mrtavaaspd dvplrlhlae lllgaghgda avgevaaalq hapgdvqare
       61 lmvralahtp astpgeaalp pppqapvpar ppapagvppq dsvlgpppap asspgfdwka
      121 aqdqvgdavp prfveaplav dgggdpgdaa awdverpgpv rladvggmqe vkerleaafl
      181 aplrnpelrr lygkslrggl llygppgcgk tfiaravage lganflsvsv ndvldmwign
      241 sernmhelfq tarrqapcvi fldeldalgg krsrtqssgm rntvnqllte ldgveaaane
      301 gvfvlaatnv pwdvdialrr pgrldrtllv lppdgparea ilryhlrerp ienvdlgklv
      361 katdglsgad lahvceaaae halldsartg tvrligmkdl laaagqiaps teswfasarn
      421 vamyandggm yddlvaylkk krkl
//
LOCUS       WP_457686358             483 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686358
VERSION     WP_457686358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48790
     Region          40..456
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44,76,126..127,129..131,134,155,158..159,162,
                     285,288..289,292..294,297,325,329,382..383,387,391,407,
                     410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlldtepgt gtpdsgvpag rrrwvlvlla galaldvsgv avinaalpsi gdeynidgst
       61 lqwtmtayai afagfllfgg rvadvlgrrk ifavgialfa aaslgaalap tvgvliaara
      121 lqgigaalsg paslallsqi fpegpqrnwa lgvyaatggs sfsaglvagg altdflgwrs
      181 vfavsvlagv lilaavrall pagrrqphsl dipgailvtl giglvvygvs egsevgwwsa
      241 qvlislvlav iglagfvvwe mgrtepllpm sifrsrpvra asltgavfyt gaggllffsp
      301 lyaqgilgys pfesalavlp vgvvviissq itgrlmspaa ykplmaasll ligtgvtlwv
      361 gtpedgsywa hmlpgivvms tgqglgfgam taatleglpl hqhgvagavn vtaqqignsv
      421 glailvavst gvsggatnsa dqlsgfhaay wvagaigllg gltvlltrfp kadtapsase
      481 erp
//
LOCUS       WP_457686374             258 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457686374
VERSION     WP_457686374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  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 258)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="glycosyltransferase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28170
     Region          <30..101
                     /region_name="YjiC"
                     /note="UDP:flavonoid glycosyltransferase YjiC, YdhE family
                     [Carbohydrate transport and metabolism]; COG1819"
                     /db_xref="CDD:441424"
ORIGIN      
        1 mfsrgnpgkr stciglayst pstsarlhtr adrlqaivvd psgtlpeigd svlahrrvpq
       61 lpllervdav vchaghntvc etlwhglplv vapirddqav vdgwhidasf pgedldagst
      121 dyrrwwanve skdcalrmff lcsdvgedda ptriasaptw mphgcwspra rrawrpgnrp
      181 garslppgia rsrtprarpg tstsatrsrc tpanrtaerv raswasrssp rpgrsslrer
      241 tgpthpsrsr rptgghgw
//
LOCUS       WP_457686376             629 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457686376
VERSION     WP_457686376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 629)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 629)
  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 629)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..629
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66012
     Region          11..606
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtaattktpd rstwgavttm yrlttghras vvvatvltla gsalglaqpl laknivdagg
       61 hgrtfwplla llatlfvtea atgavgrfvl ermgegvvrg lrhgligrll rlemnqyhrh
      121 rtgdlisrvt tdttllrdvv sqalvdlvtg alaaagavvl mawidpllll lvaltvataa
      181 vvvasllkgi raasarmqgs vgavaaeler algalpmvrv hraeereaar igtrvdaayd
      241 agvrtaklas vmspavelav qgsfllvlvi gglrvnghan slgdlvafll yasylvlpls
      301 svfravglmq rgmgayqria qalalpaepe evvehaeaae avertgpggc vvraaprrae
      361 rtgkgeapal alhdvrfgyv pdrpvlngvs ftvprhgqva lvgrsgagks tifalvarfh
      421 epdsgtllfd grpaaelsrg acrariavvd qnthvvhgsl rdnityaapd agdaevrrvv
      481 elarldgvvr rlpgglsgvl gergntlsag erqrvalara llarpallll deptshldai
      541 netalttlmk eaaqecallv iahrlstvrh adriivleeg rtvasgshee llttspsyra
      601 laagqmlrpa hgtsgadaat aaherprtp
//
LOCUS       WP_457686389             342 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces nigrescens].
ACCESSION   WP_457686389
VERSION     WP_457686389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33661
     Region          17..321
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mgepagrgpd tlgaghvlgv dsggsglria varaddaear plavrasdep vrtgpagida
       61 ehllsqllpa aaelvretga dgfaavcvga agmatlgeel rarlpdalat afgvrrlala
      121 adavtayaga lgqrpgavia agtgmialgt dltpaggwrr adgwghllgd cgggawigra
      181 gleaalrayd grpggsaall araeavfgpv tglpgalypr pdrpavlasf apevarcaae
      241 ddtvalgvlr aaaghiadaa aavcppgagt tvactgglfh mgepllaplr talaerlpda
      301 rtaaaagspl dgslaiaaal ardrltlptd rkllqitrpa pg
//
LOCUS       WP_457686387             247 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457686387
VERSION     WP_457686387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26101
     Region          7..121
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          135..243
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 malrpvqvni kaldasavgr fwaealgwsa yspgvttyvg paggpvwpdp vavcidvvpv
       61 pepktatknr vhldlattsa ahqaelvarl qalgatpadv gqgsvpwtvl adpegnefcv
      121 lepreiyrdt gpiaavvvdc adpramarfw geamdwtphe vtddqaalrs akgagpylef
      181 lrtpgvqtvp drvhldllpy pgddkaaeva rlralgatdl dlgqgdvpwt cladpeghef
      241 cvlapsp
//
LOCUS       WP_457686394             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686394
VERSION     WP_457686394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23520
     Region          22..183
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msprsasvne elrrrsrerl lqatvelvae hgyeattlad iarragvarg lvsyyfpgkr
       61 qllqsavhrl mhrtlqaale raprpigpda gqelmaraid ailglahdhp llmrthmagi
      121 ltaagfiqcp eqqrlaqllr etvvaygssd pdadypllra llmgsvvaml lpgaampqar
      181 lraellqryg lawesgvppd egapggtrtp gparggqr
//
LOCUS       WP_457686396             467 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686396
VERSION     WP_457686396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..467
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50485
     Region          191..464
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtyvsadras gptrrttltg lvggagalla agcsaspata ptarrtaray asasdptpgv
       61 mtlfkdpafn fngllalggs gygasevgev ltavntinka glsaqtytet fknlgdqlrk
      121 ppssgepgte ttrfralraa qyyaqalffv lgsdtpgtee elykagrgsw dafcercdpv
      181 pvtaripygk tplpvwffrp dssgerrptv iltngsdgqn vdmwtygvaa alqrgwnalv
      241 ydgpgqgqll fvdqvvftpr wetvvtpivd wltarpdvds rkialtglsm agdlapraaa
      301 fehriaalva mpgvlspwlg fppeiretlt pdkektnsiw nkevvpelpp saaatmkkrf
      361 epfsvpamla arqgkmftdf ytpatliksl ditdvvgrik mptlvldydf eqfypgqprq
      421 lfdkltapkd yvkltaatga qlhcspmapq qhcevvfdwl qeklsgr
//
LOCUS       WP_457686397             470 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457686397
VERSION     WP_457686397.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49011
     Region          12..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msrtitrspq dspdagqnse svlshglkqr hlsmialggv igaglfvgsg vgiaaagpai
       61 vllfmgtgal vmlimrmlge msaarpstgs fsvhaeeeig swagttsgwm ywlmlcagva
      121 aeataagtim hswvsfipay gwvgifmvff casnltavkn fgefefwfsa vkvaaivafl
      181 vlgllgilgv fgsapgtshl tghggffptg vaglaagllt tisgfaglet vtiaaaesdn
      241 psrnvaravr tavwriavfy igsmavvvtl vpwndpkvat dgpyvtvldq lgipaagtim
      301 qivvlvalls amnaniygss rmayslvsrg qgprflgkvt rgvpaaavla scvfgfaavi
      361 agivwpttvf awllniagcs vlvvwsivcl tqlkmrrrle respellsvr mwgfpyltwl
      421 tlagilgvfa vmaanadgrh qligtavvva vlagaghlkq rrdrqaaesa
//
LOCUS       WP_457686402             172 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Streptomyces nigrescens].
ACCESSION   WP_457686402
VERSION     WP_457686402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15340566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17851
     Region          31..169
                     /region_name="LPMO_AA10"
                     /note="lytic polysaccharide monooxygenase (LPMO) auxiliary
                     activity family 10 (AA10); cd21177"
                     /db_xref="CDD:410624"
ORIGIN      
        1 mhnkrklala lgagiapllv vtlpvgpasa hgyvssppsr qaqcaagtid cgpikwepqs
       61 vegpkgltsc sggnsrfael dddskgwkvt pvgssqtfnw rltarhstst wqyfvggkkv
      121 aefndggaqp patvshivnf ggitgkqkil avwniadtan afyacidvti gg
//
LOCUS       WP_457686418             200 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686418
VERSION     WP_457686418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21444
     Region          19..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdavrpgra grvaklppre rildaaeelf hsegirgvgv qaiaekagtt kaalyrhfdt
       61 kdalaaqwll ivaadytsaf dkieerwpdd prtqiqglaa fiadslseis hrgcpfinsl
      121 aelpdrshpa rqvieahkaq qlrrltamct aagltdpega aaeitfaleg aqvsaqngsv
      181 dhvgerliaf veavmgwhga
//
LOCUS       WP_457686421             256 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686421
VERSION     WP_457686421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 256)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28576
     Region          60..199
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkldflllrd ntfgeyclyc haetvtwivv dgrkrctcss cgreaeravv idpricwwtd
       61 sdgeywhesa gvfvrdrrar flffqrtafp ysltvpaghv ergeepkcaa arelweevgi
      121 rdahgglrlv adehlkgdvc rrgsdahrwh ayllevdehr eagaqgevtv neegeapvwl
      181 tldearsrqt tfaverimdl hsgkllpggt rtptgprapg vprapgglrt padprtpgdl
      241 rnpgetwqdp sdgsra
//
LOCUS       WP_457686406             973 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686406
VERSION     WP_457686406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 973)
  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 973)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Rosinski,J.A. 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 973)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..973
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=103592
     Region          <15..917
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          902..956
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtfahsrdac gddwplvgre relaamdava advlsggprv vqlegsagig ksallstwwd
       61 rnaqfrvlra rchplerefa fgavrqlfkp llaavsdtdr arllegsaaa tlralddaav
      121 pdpppeaanv taatlrelda lvsrlsrrqp lllavdalqw idqpslrwlv hfvgradsds
      181 lpvliavttr saegrrldpl caelvrpanc htlvvepldv dgvgqlvrtl wgaeepdeaf
      241 caachaatgg hplfvrallh qaqrsgvkpt tefrdriptv tlstlggeis hrlcqasdev
      301 valaralafl gdrkppella aycgtgravv qsaaeelrsl gllradgnpr fthpvvrdtv
      361 latlspeelg vgharaaqvs clsgrpdeev aahllaagpv hgswvlpalr raatealrrg
      421 apetavtylr salhqpldes erarvllelg taashydaal aiscvtgale gltdeaarsd
      481 algvlaysll lsrgsrtdls svdrkiaals erptpgtgaa drelalrmsa lrswmeferp
      541 svtgpapaps pgadddladr tagerqllai rafhalraal papyvaalie rasvnlpafs
      601 hdlfplhyfv aqtllyldel dtadrlnrhl treisgrgme llvssltvyr avlalrrgni
      661 aealgaaqda adhasptgrl pyaltvdtir idallaqgrv eaaeriaath avagqtevaw
      721 erprflmsla alriaqgelr tglsllresg hhcealgtvs pamspwrsra vavhlalgdp
      781 gaaralaeqe ldlarrcrip ralgvalrat gtvtdglrgl dmlaeavtvl rttparlela
      841 rachdfgval lrrddkrgar galrdgldla vgcgatalav rleerlhlag grvarsgsqg
      901 irgltageer vctlaaqgfs nkqiaellvv slrtvethlt gayrklgitg rpqlaaamat
      961 tdrcrggsep ads
//
LOCUS       WP_457686431             421 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 18 protein [Streptomyces nigrescens].
ACCESSION   WP_457686431
VERSION     WP_457686431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Fukamizo,T.
  TITLE     Chitinolytic enzymes: catalysis, substrate binding, and their
            application
  JOURNAL   Curr Protein Pept Sci 1 (1), 105-124 (2000)
   PUBMED   12369923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="glycoside hydrolase family 18 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008061 - chitin binding [Evidence IEA]"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44210
     Region          55..420
                     /region_name="ChiA"
                     /note="Chitinase, GH18 family [Carbohydrate transport and
                     metabolism]; COG3325"
                     /db_xref="CDD:442554"
ORIGIN      
        1 mlrphrmrsp rrvlaavtal ctaalagtll agpasagpan aptapraaap aaaaggkvvg
       61 yftnwgvydr nyhvkniets gsaaklthin yafgnvqggk caigdsyady dkaytagqsv
      121 dgtadtwdng alrgnfnqlr klkklhpnlk viwsfggwtw sggfgeaakn paafaqscyd
      181 lvedkrwadv fdgididwey pnacgltcdt sgrdaftnvl kalrskfgqs nlvtaaitad
      241 asaggkidaa dyagaaqyvd wynpmtydyf gawdakgpta phspltsysg ipkagfnstd
      301 tlaklkglgv pasklllgig fygrgwsgvt qdapggtatg aapgkyeagi ddykvlksrc
      361 patgkvggta yakcgdqwws ydtpetigtk mafknaqglg gtffwelsgd ttngelikai
      421 k
//
LOCUS       WP_457686444             410 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686444
VERSION     WP_457686444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42240
     Region          5..367
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(15..16,19..20,23,55,105..106,108..110,113,133,
                     136..137,140,209,212..213,216..218,221,249,253,302..303,
                     307,311,325,328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mpravyvlam gifamvtsef vvaglmpqma vglgvsipqi gflitafava maaggpfltv
       61 avlklrqktp lmalfgifla gnvlaalapd ygvmlmariv tgvasqaffg valslcvqla
      121 rpevrgraia lvmnglmlgt llglplstlv gehfgwrmaf wvisgitvla alatfagipr
      181 lgrpeggggv rqelvvfrnp rlwlvlstst liigatfsaf syfhpiltev tgfaagtvpl
      241 llvgygaatv igntvvgrla drytvgvqlv gltlnflfla gfavfahlpv pavalmtgig
      301 lvgvtmnpam vtrvqrtgna rplvntvhss fitlgvivgs sgggmainsf glrgplwlga
      361 alavigvgtl vpdllrrspt apepfasvtd hpepaisaas eskvvcaacs
//
LOCUS       WP_457686447             341 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686447
VERSION     WP_457686447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36049
     Region          38..317
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mkrpyavala lalaasssll agcsdagkpv dfnaggkgdg aararpvddd tlmptgpksd
       61 fritrtlddg thiaratlrg qksgvtgsvw vwapkeygdp kyaksgfpvl ialpgglgsp
      121 kepggvtnyw vggdielqen laqwtaegks lpfivvmpml npdtryhdas dipgsqkmgt
      181 wltedvvqlt ranfrtfksr dgwafmgsss ggfaglksvl khpdkfkaai asgpdmapds
      241 plwaghqaek nandpeklaq rllqkggpdv ylafqagsse paavtapiqr frqaygkgpi
      301 htslqiipgg rhnawdyqkg maagsikfis drmkapvasg s
//
LOCUS       WP_457686451             431 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686451
VERSION     WP_457686451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46439
     Region          44..423
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(155,157,277,279,310..312,353)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrisrrraaa ttaalvtsal altacgssgg aggsdsasgk vegrvtfqtw nlkanfkkyf
       61 egviadfenk ypdaevrwvd qpaegypekl sadaaggtlp dvvnvspdla yplakaglal
      121 dlektagkyr geyldgawes hrmpgmtgvy afpwylntgp mfynkelftk agldperppt
      181 sydqlfedav tmarksdqki amlagtpsie dfgrygvrlm nargteftfn epkgvellkh
      241 ykelytagal dsqaltaqae sagrkfqqqs vamnpgsald lenfkkeapg lyrhigitda
      301 vnntgkanmy vqglmvnaqs kvkpaavafa hfvtgkknqm afakevtifp stkgslddpy
      361 ftkedgtdat rvrvasaksl ktavnytpvl lsdqmktvlr navakavqgk qspraaldga
      421 vaecnrllkt a
//
LOCUS       WP_457686452             386 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686452
VERSION     WP_457686452.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 386)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40808
     Region          13..384
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtapgeaarr kparrptikd iarragvses avsfalndrp gvsqdtrarv rrvaeelgwq
       61 ansaaralsg eragavglvl arpaqtlgve sfflqlvsgi qevlsarqia llfqvvedld
      121 tecalyrrww aerrvdgvlv vdprtddprp ellaalglpa vvvggpaapg pdpaepsage
      181 psatepatae psatepaatp phpllstvwa ddakamaril dhlyglghrr ivhiaglpgl
      241 ahtarriqsl rteadrrgld rrqvhsvttd ysdaegaeat rrlldaarpp taivydndvm
      301 avagasvaae rgipvpgals ivawddsalc rvthprltal vrdtpgfgrl aaqellavld
      361 ggplrtvqge lphlearest atpppg
//
LOCUS       WP_457686455             442 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686455
VERSION     WP_457686455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=45669
     Region          1..>50
                     /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..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 maertqrtvr dlrranrtav lqrlysdgpm srqelgpatg lssgsvsnvv aelveeglle
       61 eagvvgsdgg rprtllrvap gsgcligvdv getrvrvelf dlamgelars elplrhhgyd
      121 vdlivrhiad giatvlrese aspgrllgvg vgvpgildrs rpggavvhgq tigwdavple
      181 ellhhtvalp pgvgfflsng akalgqaemw fgggrgaena aivlfgsgvg aclvtdgvid
      241 ggardsagew ghltvsvggr rcrcgargcl eaytgseall qrwqeaggqp ppdadeetal
      301 aalvaaahpp aggpdadpva rsvldetaey lgagisdlin lfspervlig gwaglqlgph
      361 llpavrahat ayslvhpagr vtidlgrlgp davtvgaatl pladffangg rrraapadep
      421 gervtapcwr taleerarag rg
//
LOCUS       WP_457686457             451 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457686457
VERSION     WP_457686457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..451
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46669
     Region          <19..438
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mplprlrhlr errelshvlv lipigiivav ctidvlappd ihlgpllvaa paltaafagp
       61 rltaaigala vaaqvfigia rhvlftenle aqiaalvvvs alvvlftvvr drnerrlrqs
      121 rsvaavaqqv llrplpvhsg pleiaslyla aeeeaemggd lfavarttss trliigdvrg
      181 kglpayshaa lilgafraaa hreatlprla ihldgavrwd srqwnnapgp gagtdaagga
      241 gadavaetgt davaatetgt gtdavggsas evgsasevgs vpvpvsvpvp atplpgpdpv
      301 idtdetfatv illdlpdrwp vvqtitcghp pplllrdgrv rtlsaewpal pvglgglpga
      361 pdyevegfpf epgdllllyt dgvsearddk gtfyplvera aawsdcsprq vlrqlrtdll
      421 ahtngrlgdd aaavavrrlg ggpgggvpgt p
//
LOCUS       WP_457686462             684 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457686462
VERSION     WP_457686462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..684
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72233
     Region          2..651
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtarvdrrpl pgvvgraveh elvsgllgsa plvtltgpag vgksmlahav leehtarhdg
       61 tilrvgcwdg paegglpatl lraaqaadsa rrdtatalvr rtapscvgep vcgrtgrtdt
      121 ptgpspaddt aiaalaahcr qsratvlldd cdplrdecaq lvrqllradp tlrivatarg
      181 alglpeeriv eiaplpvtlg egiagpavel laartgaatp ellvavcqal egsplaiala
      241 aqqldrmslp qlaaqvgsdg plfwsgpaat vrhtslyaaq aagyalcspt drrvwarlsv
      301 lpgdfdpwla gcvctscdvp aaavegaler lltasvierv rdaggaqddt gaalppryrl
      361 praardfgrt qlreageesa alrrfrqaca alaaeaqiaw qgpnqqvavr lvedeqanld
      421 aaltrppqda edalgaleia vslwfhwaac gfrregrahl drllllsrdd talraralwl
      481 agylaaqeha pgaaealldq awtaavmhad sdglariaha hgvlalyrgd taaalaclee
      541 aarhrsrdpw fgpgpahswa llavalssld aeraraaarr awearhsdgd fwlystvlya
      601 caatervhge paaalracrt alaakeligd plfiagahhm laglrhevrg geplpdrdee
      661 dpwwrpggpd vppqpffsrl ragp
//
LOCUS       WP_457686465             254 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686465
VERSION     WP_457686465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26620
     Region          8..248
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 midnfktlav ahqgpllniq lnspdtgnal cepmldellt vlgalhdrpe irvvilsgag
       61 adfclggdrr efaeslaadg tgtalramgn karrvceala atsavtiarl hggvigagia
      121 lavfcdlrag ahscrfrlpe lalgmppawg gvlprllnec gaarirelil tgesfdaaka
      181 aeldllhkav pedeldevia rwtrplvrrs paalrtakvm mnayasanrl adatlfdael
      241 lttvlaaagp kslg
//
LOCUS       WP_457686471             503 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457686471
VERSION     WP_457686471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54264
     Region          10..455
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpelldervg fvrriglfqa tainmsqmcg igpfvtiplm vaafggpqav tgflagavla
       61 ladgliwael gaslpgaggs yvylrqafqy rtgklmpflf vwtamlfipl gmstgvigfv
      121 qylgylwpdm tsgqgdlvgi gvtvgivvll wrrveniakl tvvlwtvmit svllvivaaf
      181 thfsperaft ypahafelts shfwtgfaag ltigiydylg yntiaymgae irqpgrtipr
      241 ailfailgim tiylllqigt lgivnwqeml dphstasssv asavlerawg kgaagtvtvl
      301 ilitavasvf tgllggsrvp ydaarervff rpygtlhprh rfpvlglltm gtvmaagfll
      361 grhtdlatii qllttvmviv qalaqvaavt vlrrrqpglh rpyrmwlypl psvvaligwl
      421 viygyadrsa pgrhpiewsl awvgsgvvaf lvwaryekew pfgpkritee ylhgsdpdtg
      481 graggegrek gaggtavgat dpg
//
LOCUS       WP_457686473             837 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457686473
VERSION     WP_457686473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 837)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..837
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86688
     Region          2..837
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mlkamlrdll ahkgrvvmtl iaialgvtat vgswvvsdsi attlagqetr hdvgvsvqsp
       61 gkeslltsad rdrlartpgv graegvivgr agligrghkf vrtttvldra gtnwssdkrf
      121 tveagtaptg pgqvalhkad adsagiavgd taqvllsdgr sdtarvtalf tyhrlgprat
      181 tdaneasdav pvvaydtata tkllgprfhr velipasgas pgalkaaaqk gvsdeyhvet
      241 gsalaqaavq qsdseaqdlr mtmlpfaava llvgmfvian tftllvsrrt rqfallravg
      301 arkgqvragi vveagvlgla ggtlgtlagv algpsmiavm rpqddvdltv spfavllgyg
      361 vallvtvvaa yrsarraaav ppvaalrtad tapretkrtr hftglgcivt gvvmvamtad
      421 pstsnlgriv glmgavlgvi gmivlapffa eallrplmrl lgarsgpavr lglrnaasdp
      481 rrtsgtatal tvglalvcaf atlsasfsal iasttranvp ptttvlqsaa ggessltpae
      541 adkvrrlpgv tqvagsrdvl vgltykggrt errisaieps glkgvltphl tagspdlrrg
      601 vvisqnqadm ldlgmndrit lhldartsvt qsvvgiydat elqasifldv skapgslrkq
      661 ittlyasgpd petardsira afrdrpdvsv gsretlveqg vdqqslaftl myamfgvail
      721 iavsgvvntl vlsvmertre igviravgat rllvrrtirv esivislfga llgvivgvpa
      781 gavmqhamfg qrlgdfslpa giiglslagi tlaavlaaiw parraartdm laaiage
//
LOCUS       WP_457686494             438 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686494
VERSION     WP_457686494.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44363
     Region          35..398
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(45..46,49..50,53,86,139..140,142..144,147,167,
                     170..171,174,252,255..256,259..261,264,292,296,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 myladgrpap ppsvspggrr dgrgrrvraa vpstvlvlga vslitdisse mvtavlplyl
       61 vaelglsplg fgvldgvyng vsalvrlvgg rlsdrgggrg hkavaavgyg lsalckplll
      121 mvhtlpliga vlavdrtgkg lrtaprdami slaaepaarg rafgvhramd tagalcgplv
      181 afvllraaae gydavftvsf cvavlgvvvl llfvpgralp aaedtagrgp agprtpvral
      241 lrrpqvrrlt acavllgltt vsdsflylal qrrldlpagw fpllplgtaa aylslavpmg
      301 aladrigrrr lflaghlvll gayglllapf gggaglvcgv lvlhgafyaa tdgvlaaata
      361 davpedargs glavvqtgqt aarfvcslaf gaawtawgdh tavlaaavgl alaaalsarl
      421 lrpaapapap nspsehtp
//
LOCUS       WP_457686501             219 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457686501
VERSION     WP_457686501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21932
     Region          4..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdgqliaftg iaagmvtmpg adfavvvrna ldsrragvat avgvaggllv htalavagla
       61 avlvavptlf gavqllggvy llylgvgali aavrrtgaha dsatgpaaap adgpaallgt
      121 arslrqgflt nalnpkapvl flsllpqfvp agepalprtl llatmvvama lvwfpavall
      181 vdrlgnwlrr prvtraleat tgalltalgg vllielvla
//
LOCUS       WP_457686512             351 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686512
VERSION     WP_457686512.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=37525
     Region          7..311
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtsgsavvig asgqigraav ralardgwev raasrhggrd aswpgevrsv avdreddtal
       61 agligegcdv lldcvaygaa hakqltalad rigsavvvst cavyaddrgr sfstmdepdg
      121 spvyplpvpe tqptvppgdq dygtrkvale rallaqgdrl pvtllracav hgpysplpre
      181 lyfvkrvldg rrvrvlaygg ssrfhpvhvd nlaelvrlaa rrpgsrvlna adpqaptvae
      241 isaavdaamg apesevvrvd gappssdvgd tpwsvphplv ydmtaaerel gyravttyee
      301 slpatvawla dqvkgrdwwe lfprmagfyp deklfgyaae drwlaerggk r
//
LOCUS       WP_457686516             408 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686516
VERSION     WP_457686516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44228
     Region          6..406
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 maeftmelnd eqkevrnwih gfaadvmrpa aaewdereet pwpviqeaak iglysldfya
       61 qqffdptglg ipmameelfw gdagiglsiv gtglaavgvl angteeqigt wvpqmygdvh
      121 dvkvaafcss epdagsdvaa mrtravydea kdewvlngtk twatnggian vhvvvavvdp
      181 dagskghasf ivppntpglt qgqkfkkhgi rashtaevvl envripghcl lggkeklder
      241 lararenakk dgervknaam atfeasrpav gamavgtara ayeealeyak trsqfgrpii
      301 dnqgvafqla dmrtqidaar llvwraswma vtgkpftsae gsmsklfase vakkvtaqav
      361 qilggngftr eypvermhrd aaiytifegt seiqrlviar tlsgmpir
//
LOCUS       WP_457686513             254 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686513
VERSION     WP_457686513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27230
     Region          19..216
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlyqvlkyll lgpllrlvfr pridglghvp eeggaiiasn hlsfadhfvm paivprrvtf
       61 lakaeyftgp glkgrltaaf frgvgqipvd rsggrasqaa lssglavlrk grllgiypeg
      121 trshdgrlyk grtgvasmal tagvpvvpca migtfeaqpt grrlpramri tirfgapldf
      181 sryagleder tvvravtdei myailtlsgq eyvdtyagea kaeaqaqara waqaraqgra
      241 qgrrghgsgk gpar
//
LOCUS       WP_457686518             204 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686518
VERSION     WP_457686518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114819
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22538
     Region          6..157
                     /region_name="YdjA-like"
                     /note="nitroreductase family protein similar to
                     Escherichia coli YdjA; cd02135"
                     /db_xref="CDD:380312"
     Site            order(6..8,10,27..28,30..32,34..37,39,43,45..50,101..102,
                     104..105,108..109,112..113,116..117,120..121,127,129,
                     141..142,149,151)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380312"
     Site            order(10..12,35,37..39,102,105..106,126..130)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380312"
ORIGIN      
        1 meleaairtr rsehrliepa psdeefvdll gwaatapdhg hlrpwrwilv rgdsrtalgv
       61 sfasgatdae tvrremrkpl rapllatlvf vprrnhrvpd weqlaassam vnslmlllhd
      121 rgfgsiwrtg ssvdsaetrt llglaphegl igwlyigspd ptrrsvlrsp vpvshrvsrf
      181 tpegfpgqpg plrpsghqrv sdtl
//
LOCUS       WP_457686522             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686522
VERSION     WP_457686522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43226
     Region          13..391
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,118..119,121..123,126,146,
                     149..150,153,228,231..232,235..237,240,264,268,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mvrtvppwag rnyllltgat vianlgssga liatafavla aggsatdvgl vaaartipli
       61 fflliggava drlprhrvmv aanglscvsq glfallvlag epqlwqmall aalggtgqaf
      121 fapasegmvl asvsgdqagr afavyrmgmn ganiggaalg galvaavgpg wvlavdsaaf
      181 alaaalrafl dvsgvperap gggmlhdlrd gwrevasrpw lwavvvqfsl vnavvsaaea
      241 vygplvaeqh lggpgpwgla laafgvgtvg gallmarvrp rrmlltgalc ifplalpsaa
      301 lavplpvagl taimfgtgia vevfavmwmt alhqeipeek fsrvssydwl gslamvppat
      361 alagpvqdli grtaalwgcs avivlltaav lcvpdvrrlt rrpktepaag apaspaaeta
      421 apdtagae
//
LOCUS       WP_457686530             710 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457686530
VERSION     WP_457686530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..710
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74268
     Region          18..269
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(18,42..43,76,81,86..89,101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(25..26,28..31,33,46,48,84,100..103,107,109,146,148,
                     150..151,153,163..164,167,184..187)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(25..26,28..31,33,46,48,84,100..103,107,148,150..151,
                     153,163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(29,107,109,146,148,150,167,184..187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(163..171,180..187)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgdevemngk egrllagryr ladvlgrggm gtvwrardev lgrtvavkel rfpggveede
       61 krrlitrtlr eakaiarirn ngavtvydvv deddrpwivm elvegrslae vvrddgpltp
      121 rraaevglav ldvlraahae gilhrdvkps nvlmsddgrv vltdfgiaqv egdpsvtstg
      181 mlvgapsyis perarghkpg ppadmwslgg llyacvegvp pydkgsaiat ltavmtepve
      241 ppksagalee vifgllvkdp aarlddagar tllldvvhap eaqkpeppld etramvlptv
      301 pkerakakpe sapkpkpapk prvprkpkpk paaapvaepa agsgsasdgt kagksktgaa
      361 kpaaakaaat stperterpq qsatpaaeet taadragsgv srptltrpgf dtdaakerlr
      421 aalqtvrtaa taaadaarar adsrpgdgnr pstrasvtdv vprrtliiva vivalavlgt
      481 vlavalsggd ttknsgkpag khdkassaak akpstesagt gedakdgpas papqtpggvs
      541 paedkgdtgg kdgkggkavp dgfaqvsngr fhfgmampkg fkqtatagqg sgviysasgg
      601 fprvqvdyna epgtdaaasw rslepavrgs sedyhlisik svkwrdyptv adwsftrrqs
      661 gqkvrvldrg fkaddqhgya imitckadgw sekecqnvvr tafktfaikd
//
LOCUS       WP_457686534             516 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686534
VERSION     WP_457686534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..516
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55143
     Region          6..500
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtgttfwdlv arraartpda paliqgaesa rqerritfga lhrraervaa glhergvrpg
       61 srvvwqlptr ietvlfslal arigavqspv vplyrahevg qvlrrtraaf favpgvwrgf
      121 dhramadrla aglpgpltvi eaydtlpdad pavlppppad deevrwiywt sgttaapkgv
      181 lhtdrslrta grwlgaalrl gpsdigsmaf pyahvagpdy tvmllehgip avllehfalp
      241 galaayrrhr vtlaggstaf yalflaeark lppgrrllps lrllagggap kppalyhevv
      301 aglgcqlthg yamteapmvt mgdpydspgh lagtdgrppa gmeiriapgs geirlrgpav
      361 crgyldepap fdadgflptg dlghltpsgh lvvtgrlkdi iirkgenisa qeieellsrh
      421 pdiadaavvg lpdttrgerv cavieqpsga peltlatlsa hllshglaph klpeqlellp
      481 alprdttlrk vrkqqlrerf ggggpgrgea pdpppq
//
LOCUS       WP_457686537             327 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686537
VERSION     WP_457686537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34667
     Region          1..304
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqltdeqr alkdgtrell agrfgrdrlr aavedpgpdr alwrelgaag ffalrlpekd
       61 ggvglglpea vlvleeagra llpgplvacq llagvvdgva tgektvglce garepvlweh
      121 pagcdelilv eggevegdee egarertggv yrsasdrvsc apfasvdplt plarvldlpr
      181 tepvaldvpr lrreaallta aqqlgsavrt vemaaghare reqfgapigs fqavkqlcaq
      241 mlvraemars avyaasites vlditgakll adeaavrnar dclqvhggmg ftweadvhlh
      301 lkrawlraec wgaageaeel laaglia
//
LOCUS       WP_457686543             286 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686543
VERSION     WP_457686543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29617
     Region          29..279
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtpspspgsv ppaepgepaa raepvdslvl httdngvswl tlnrpdamna ltpdqrerli
       61 grladasadp dvravvltat gkgfcagadl rgspsagerv agdvarlird gaqrlitavl
      121 dcekpviaav ngtaaglgah lalacdlvla aesarfievf vrrglspdgg gayllprlvg
      181 pqrakellff gdavpaaeae rlglvnrvvp dgelaktare waerlaagpt ralaltkqlv
      241 nasldtdrat afaaeataqe inmttadaqe gvasfvarrh pafrgr
//
LOCUS       WP_457686541             443 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686541
VERSION     WP_457686541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46623
     Region          29..426
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(39..40,43..44,47,82,129..130,132..134,137,161,
                     164..165,168,254,257..258,261..263,266,297,301,353..354,
                     358,362,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtqtpelplr tadpapapap rrrrphraws vaavtfltii gaagfaslpg llieplhaef
       61 hwsrgtigfa vsvnlalygl tapfaaalmd rfgirrvvav altviaagag ltvfmtaswq
      121 lvlswgvlvg lgsgsmalaf aatvtgrwft arrglvtgil taagasgqlv flpllswiid
      181 rhdwrpaavt valaalavvp lvwlllrdhp advgvapyga tefvpkpppq rgaarravra
      241 lvsaastgpf wllagtfaic gattnglvkt hfvpaahdhg mpmtaaasll avigifdiag
      301 tiasgwftdr fntrrllaty yglrglslmf lplllsdtvh ppmvffivfy gldwvatvpp
      361 tialcrehyg ddgaivfgwv laahqvgaal iaflgglard afgtynpvwy asgalcavaa
      421 lmalvirqrr egpgdarvva aqg
//
LOCUS       WP_457686545             751 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate--CoA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686545
VERSION     WP_457686545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 751)
  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 751)
  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..751
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..751
                     /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=79564
     Region          61..747
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt thsrparvva cgeqpphtvh gmsephrdgg gqgacpvdrd vsgrplhapv
       61 pdldrffrpe svavigasdr egrpntgitr qliawaervg arlhpvnpgr tevfgrpcha
      121 gvadlpepvd lavllvgdpl pvieqlaeak vkfavafasg faetgergaa aqdrlaeavt
      181 rsglrllgpn tnlnafekfr tdldgpaial itqsghqgrp vfslqelgir lshwaptgne
      241 adletadfls yfatrpevga iaayveglkd grsfllaadr aarnkvpvva vkvgrtetga
      301 rtaashtgkl tgadevvdaa mrqfgvirvd gldelqdtaa llararkpta egvavysisg
      361 gtgahfadla taaglrlppl gaakqaelhq wipdylhvan pvdngghpvg dwrgrkilda
      421 iladpsigil icpitgpfpp msdklaqdlv daaeqtdklv cvvwgspvgt edayrstllg
      481 strvatfrtf ancitavray ldhhrfvdgy rspfddaprv lspsarkaha lmrpgqqlse
      541 haakqllray girvpreqlv tsaaaavraa slvgypvvmk asgpqlahkt elglvkvhlt
      601 sasqvrdayr eltdiaryed ipldgvlvcq miergvemvv gvtrdslfgp tvtvglggvl
      661 vevlqdvavg vppfgedqar amldelrgra lldgvrgapp adidalvevv lrvqrmalel
      721 gdelaeldin plvvlprgqg avaldalavc p
//
LOCUS       WP_457686550             472 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686550
VERSION     WP_457686550.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47366
     Region          1..431
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdaafteeqh eirrtlrell lkrcgpdevk aavrtpagyd tqlwqqlagr lglpglalpt
       61 ayggvgcgpt elalaceetg ravlpsplma taalaaplil algserqrta llpalaagel
      121 tatlavpggr latalaltgp ndggwagggr aggiqarrap qegeavpskn ggrpagggwr
      181 lygeagqvln ghtaevlvva ahtggfakgr tllflvraaa gggearpgaa pgvpgllrtr
      241 qtaldetrpq arlelrhvpa ellgegdgde aavagalaat gmtaaaalaa eavgaadaal
      301 artvahvqqr eqfgrpigsf qavqhrladl yvrlqaarsa ayyaawsagr gqsapgggps
      361 apggaagpyg aaepgvgala laqaleslra vaaeavqlhg gigftwehea hlyfkraacd
      421 elllgpvhrl raraaeeagl fpdgaeepsg agkpggsgep agapgrtaav ev
//
LOCUS       WP_457686582             293 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457686582
VERSION     WP_457686582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30008
     Region          5..290
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mttvkksvav lglgsmgaal adallvaghe vtvwnrtpgr aegfvargar raesvaeaia
       61 ageivivcil dygdigplle qqgvgraalq grvvvnvtng speearamae rvtglgasyl
      121 dggimavpei iaspeafvly sgsreafeah rgvldafars vylgeepgla plhdlallsg
      181 mygmfggflh aaalvrsagg svaeftttll qpwlaamagg lpamaaqids gdytvtgspl
      241 amqvahdsig evsraqgvsp elfaplfalm errvadgrgs eglagvvelv har
//
LOCUS       WP_457686595             314 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686595
VERSION     WP_457686595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31505
     Region          28..310
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 msvlvaltvl pcglliglll galggggsvl avpalvyllg qspheataga lvvvtvgavt
       61 gllchgragr vrwaagaafg algtagsylg srwsaaldpt vlmaafagll lvvaamlvtr
      121 grrerraaeg vrplrdpaes splreaaetv plresaetga lrdapeeavp lrdtpgpass
      181 gdpgggarrm plrpgrfvvt asavglltgf fgvgggfvvv paltlvlgle mpvaigtsll
      241 vilinsltal gtragtgald wpllaafaac aalgshlgnr ltnrlrpqvl atafaclvtv
      301 lavtmaatal prlw
//
LOCUS       WP_457686587             466 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686587
VERSION     WP_457686587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..466
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48003
     Region          59..454
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mpqphrpqpr ppadaapept gaeptgtepp gagtytappa gtapptdaap pgaaparald
       61 gilvadfsrv lagplaaatl adlgaevikv erpgtgddtr awgppfvadp psgeeppsge
      121 epapheggap rrgtaayfda anrskrglal dlgdpddaaa arelarradv lienfrpgsl
      181 akygldhtat raanpglvhc titgfgsgag arlpgydfvv qavgglmsit gepggtplka
      241 gvalvdvlta kdattgilaa lrhrdrtgqg qlvevnllss llgslvnqas ghlatgrdpg
      301 pmgnrhpsia pyetlacrdg qllavavgnd rqfrelaral gapelaedar farnedrvqn
      361 rtdlvkaler rlasdtphdw terltavsvp cgpvntvsea lelaqrlgla pvtpvgegri
      421 pqvtsplrls gtpvaqpfap prldehgtal rtwlsgpadh plpphv
//
LOCUS       WP_457686598             555 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686598
VERSION     WP_457686598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56458
     Region          21..403
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,269,272..273,276..278,281,309,313,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpksephpyl dararwalaa vatgafcvql dsfalnlalp vvrdalhgsa tatpwvvsgy
       61 llaagslmpv agrlgdlygr rrmltaglal fgvtavlcal apslpllvta rvlqgaggal
      121 impaglallt hacppgrgrr amgralglag latvcgpflg gvlarsvswr avfwltvpla
      181 laaalcarra aesrdpeagq sldgvgaiaa tgvvaclarw lehaadwgwa vgaaligalf
      241 vraerrssap lvdlalfrnr pyvaltvaga vansatvall yvvpwtlqra egwsvleagv
      301 vfvapagala vggplagrvr pgaavpvmal clasgavala attrgtgtla lltaataaaa
      361 algvagglal tgtqavvrre rageasgvtk avmtatagvg laltdagagg gagpslvlpa
      421 avclataaal vvarvlrlrl vrglvpvvgr vlglgralvl grvlvlgrap isvralasvr
      481 apvcvralrl vrvllpvgrr adrrrmdrcg vdrrgvdrrg vdrrgvdrrg agqrqadrrq
      541 aaqcrsvrcr tdrce
//
LOCUS       WP_457686601             159 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457686601
VERSION     WP_457686601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..159
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17587
     Region          7..144
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtstlrlekv tpdnveaacr lkvrpdqerl vapvvrslae ayaqpevawp rlifdgeqlv
       61 gfvmgfflvr fdpdnpedrl rsgiwrlnia aghqgrgygr favesvcadv rrrgqrrvtv
      121 twvpgedgpe rfylglgfrp tgemsgdqvv gelalttga
//
LOCUS       WP_457686608             426 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457686608
VERSION     WP_457686608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  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 426)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..426
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44428
     Region          3..424
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(13..14,16,167,170..171,175,206,263,328,330,332..333,
                     336)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(13,263,328,330,332..333)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            14
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            order(28,106,418..419,422)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mthilitaag shgdiapytg vgarlraagh evalathdsy aplvraagle frrlpadprt
       61 rradpedate qarrppapgg tralmrqaaa fikelgggia daarddtdll llsattaplg
      121 hhlaeargip slelplvpaa ptgdfapvvs ggrslgrwgn raagrlslrv idrlyadaar
      181 emrarlglpa atprtvrrra eaagrpvlyg fsevlvprps dwrtgldvvg nwwpwhapdd
      241 rlppvvedfl aagpppvfig fgsmaggege rlsalaaaal rrakvrgilq sgwaglttrh
      301 tsadddllti gevphallfp rmsavvhhcg agtaaagvra gvptvpvpvt adqpfwaarl
      361 aalgvatapi pfkdlstdha varlahaitq ataaparrdh ataaahrlat edgagevlka
      421 aerlla
//
LOCUS       WP_457686610             261 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686610
VERSION     WP_457686610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29156
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          132..251
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 msysvgqvsg fagitvrtlh hydkagllsp sdrspagyrl ysdtdlarlq qilfyrelgf
       61 pldeiatile dpqanaldhl rarhrllndq itklqrlvev aehamevqqt gveltpeerf
      121 evfgevafdl tyatqahlkw qhheghqrsm araaahsked wakimaesad wrvrllaafd
      181 agepadstpa mdlaeehrqh varwftpcpt dmhgriaddf atdprafalv vppteqrpgl
      241 apylrtavha navrqspphg g
//
LOCUS       WP_457686612             131 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686612
VERSION     WP_457686612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 131)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..131
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14457
     Region          7..119
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mvsvvefrid rrsgvatylq ivqqvqqalr lgvlvegdrl ptaaqvaatt kvnpnttlka
       61 yrelereglv eprpglgtfv srtlarpqsa adtllreelr swmdraraeg laredvqalv
      121 nsvlqdrypd g
//
LOCUS       WP_457686615             509 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457686615
VERSION     WP_457686615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55683
     Region          7..446
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mdgrerrhvr vavigsgfgg lgaavrlrrq gitdfviler adavggtwrd nsypgcacdv
       61 pshlysfsfa pnpewprnfs gqphirayle rvtdtfglrp hlrfnsevrs lrwngealhw
      121 evetasgplt advvvsatgp lsdpkvpdip gldtfpgkvs hsarwdhdyd lrgkrvamig
      181 tgasaiqivp aiqpdverlt lfqrtppwvl pradrkisaa ekwlhsklpa traarrgllw
      241 glremqvsaf tkrpnelgli eflarnhmkk aikdpglraa ltpdyrigck rillsntyyp
      301 alaqpnvdlv aagltevrgs tlvgsdgsev eadaivfgtg fhvtdmpiaq rvtgangttl
      361 aeewkdgmea lrgasaagfp nfltvigpnt glgnssmilm ieaqlnylad fmrqldvlgg
      421 kialdarpsa vqdwnrrvqq rmtrtvwntg gcdswyldan grnttvwpgt tsefkkvtrq
      481 vdlaeyevlr ppgtgpagrs tgeraevav
//
LOCUS       WP_457686621             257 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Streptomyces nigrescens].
ACCESSION   WP_457686621
VERSION     WP_457686621.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27373
     Region          13..238
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mdplstatpa pslavsglay aypdghqalf gvdltvgrge rvallgpnga gkttlvlhln
       61 gileagagta avaglpvare hlaeirrrvg ivfqdpddql fmptvredva fgpasaglrg
      121 aaldervtea ltrvgmeefa drpphhlsfg qrrrvavatv lamrpeilvl depssnldpa
      181 srreladilr sldvtvlmvt hdlpyalelc prsvvlsggv lvadgttqql lcdeelmrth
      241 rlelpfgfdp rsvdvpl
//
LOCUS       WP_457686626             250 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686626
VERSION     WP_457686626.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25620
     Region          25..219
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mapdmgttve terglvygps gkqldvyrpa eaprpaptvl lwhgigpder dvleplarta
       61 aahgllvlvp dwrsdaadgg rahlleslaf arkeagglgg dgescvlagw sagagaalgv
      121 alrpeiaegw rpravvgvag rydlparttg aapltdlaag repgvpvhlv hgsrdpvvea
      181 rysrdlaeal raagrtftlq epdtdhagvi mtaydpatdr cvpttaehav ragravaevl
      241 teaaggggaa
//
LOCUS       WP_457686630             599 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457686630
VERSION     WP_457686630.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..599
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66178
     Region          8..507
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          537..597
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mavnlvnlea vgkvygtral ldgvslgvne gdrigvvgrn gdgkttliri lakledadng
       61 rvthngglrl gvltqhdsld paatirhevi gdladhewag nakirdvltg lfgdlhlpgf
      121 tqgldtvigp lsggerrria laklliaeqd livldeptnh ldvegiswla ghlrarrsal
      181 vvvthdrwfl dqvctrmwdv qrgdvheyeg gysdyvfara ereriaatee vkrqnlmrke
      241 lawlrrgapa rtskprfrie aaneliadvp pprdnaelmk fassrlgktv feledvsvqa
      301 gpkillkhlt wqlgpgdrig lvgvngagkt sllraladaa rtqgeaqpva grivvgktvk
      361 laylsqevge lpptlrvlea vqqvrervdl gkgremtagq lcekfgftke kqwtpvgdls
      421 ggerrrlqil rllmdepnvl fldeptndld ietltqledl ldgwpgsliv ishdryfier
      481 ttdrvhallg datlrmlprg ldeyldrrrq vieaatpapa pqttapkkaa avnraaqkel
      541 qkierqldkl gdketklhaq iaenatdfek vagldaqlre lsaekdelem rwlelaeea
//
LOCUS       WP_457686641             264 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457686641
VERSION     WP_457686641.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27198
     Region          17..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msqqraphpa ngpygrrfeg rtvlvtgaaa gigaatadrl aaegagvlll diddargeht
       61 arriraaggr asyehcdvag eddwrravea arqrygpvdg lvsnafvpsv aaadrtplad
      121 wdrqlavnlt gsflgvraal adlrarggav vltssvhalv glpgrpayaa akagltglgr
      181 qlaveygpev rvnsvlpgpv ltaawdgige eerlasaaet aarrlgrpee iaaaitflls
      241 peasfvtgas lvvdggwsvy knss
//
LOCUS       WP_457686650             335 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA desaturase [Streptomyces nigrescens].
ACCESSION   WP_457686650
VERSION     WP_457686650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=37074
     Region          27..322
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtagpeaved ppipadsavg psagtpsatl ggeqrrsleq itlllfitvp fvalvaavpl
       61 awgwgvswld lglmvamyyi gchgitigfh ryfthgafka krplrialai mgslavegpl
      121 vrwvadhrkh hkfsdaegdp hspwrfgetv palmkglwwa higwmfdeeq tpqqkyapdl
      181 ikdsairtvs rqfvlwttvs llipplvggl vtwswqgals affwgslvrv allhhvtwsi
      241 nsichavgkr pfksrdrsgn vwwlavlscg eswhnlhhad ptcarhgvmk gqldssarli
      301 rwfekagway dvrwpdasrl darraekaag gasrr
//
LOCUS       WP_457686658            1112 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457686658
VERSION     WP_457686658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 1112)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 1112)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 1112)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 1112)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1112
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=120292
     Region          12..1086
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mparpdppgg sylrfphlhg gllcfaaedd lwiapiapdg eepgrawrlt vdrtrvghpr
       61 fspdgqqiaf ttwrsldpev hlapveggpa rrltfwgstd arvcgwtppd heghshilav
      121 sshgqpfsyy swayslptdg spggqlpwgp vsdiavadia gehrtlllsg kpphepaswk
      181 ryrggamgrm wlhgtrllpd lhghldsvmf vdgriaflsd hegianvysc lpdstdlrrh
      241 sdhgdfyarh astdgkriiy qcagelwlid dlapdavprk lavrlggpra grrsyqvpaa
      301 shvtalavdt tgrasavgvr gslywlthrd gpartihdvp gvrvrlpeml gasgriayvt
      361 daegadaiei tnlprasapg eprrlaagel grvhemtaap dgerlavaan dgrlllvdva
      421 rpeegasdee tasggvteli rstngpvrdl afspdsrwlt wshpgigrsl rqikmarlad
      481 rhivdvtngr fedeqpvftr dgrylaflsw rgfdpvydvh tgdlsfplgc rpylvplssa
      541 tpspfalspe grpaaggldp devpppageg pllvevegle nrvtpfpvaa skysslepvs
      601 ggglvwlrwp isgalgetfa npaetsgrpt lehfdltkar rteltssldg falsgdgsrl
      661 vvndegelra vpateqpdsd stvfldlrri lhdvdpvaew hqafeeagri trayfweprm
      721 cgidwdavla qyrplldrva spdefadllr evmgelgtsh ayvsgarrne gpphyqramg
      781 llganlvcrd grwvvtrilp gessdskars plagtgireg aalthvdgrp vdpvagpypl
      841 laaaggttve ltfsppedeg parrvavvpl iderplryqd wvakrravvr elssgrcgyl
      901 hipdmggsgw aqfnrdlrme vsrpalivdv rgnaggnise lviekltrti mgwdltrdae
      961 pvsytsnapr gpvvavadem tssdgdmita afklqglgpv vgmrtwggvv gmtgrhrlad
     1021 gtaitvpmna awfrlygwgv enhgvevdie alrsplhwae grhpqlgvai rtalellerh
     1081 paamppdlsd vpdlrrpplp prsggaaeaa ga
//
LOCUS       WP_457686671             183 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457686671
VERSION     WP_457686671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18282
     Region          41..158
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtsplgtlas sriatpirpa pslygydagl lllrlalglt maahgaqklf gwfggpgldg
       61 tgqfftmsgy pagrtmavva gltetlgglg laaglltpla gaavvgtmin alavkwgggf
      121 fapkgveyel lltavaaalt ltgpgrcaid rflpalraar pvhgvvalvl gvvmaagvll
      181 vrk
//
LOCUS       WP_457686673             408 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686673
VERSION     WP_457686673.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43421
     Region          15..406
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrttphprpw lvhdgaltgl kvldlsrils gpfctmvlad lgadvikved tvsgddtraw
       61 gppfqgedaa yfhsvnrnkr giavdlkdpd clrliqelat tadvivenfr pgtaarlglg
      121 yqevrdhnpa vvyasisgyg qtgpyrnepg ydaiaqavsg vmsvtgeptg ppvrfgvspa
      181 dlaagmwaai gilaalrnre htgtgewvdv slldgqvawl syvaggyfas gsvpqrygsa
      241 hptivpyqaf ptadghlmva agndglwrrf ataiglaglv ddprfatnpd rvrhraellp
      301 lieralsarg akewavllte aevpvgpint vdealrhpqv vargmvaelq htgagtlrti
      361 aspiklsghp atvrtppprh gehtapvlta mgvdprqlae lrarkaak
//
LOCUS       WP_457686681             206 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional 4-hydroxy-2-oxoglutarate
            aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Streptomyces
            nigrescens].
ACCESSION   WP_457686681
VERSION     WP_457686681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Fullerton,S.W., Griffiths,J.S., Merkel,A.B., Cheriyan,M.,
            Wymer,N.J., Hutchins,M.J., Fierke,C.A., Toone,E.J. and
            Naismith,J.H.
  TITLE     Mechanism of the Class I KDPG aldolase
  JOURNAL   Bioorg Med Chem 14 (9), 3002-3010 (2006)
   PUBMED   16403639
REFERENCE   2  (residues 1 to 206)
  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   3  (residues 1 to 206)
  AUTHORS   Gefflaut,T., Blonski,C., Perie,J. and Willson,M.
  TITLE     Class I aldolases: substrate specificity, mechanism, inhibitors and
            structural aspects
  JOURNAL   Prog Biophys Mol Biol 63 (3), 301-340 (1995)
   PUBMED   8599032
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Conway,T.
  TITLE     The Entner-Doudoroff pathway: history, physiology and molecular
            biology
  JOURNAL   FEMS Microbiol Rev 9 (1), 1-27 (1992)
   PUBMED   1389313
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="bifunctional 4-hydroxy-2-oxoglutarate
                     aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase"
                     /EC_number="4.1.2.14"
                     /EC_number="4.1.3.16"
                     /GO_function="GO:0008675 -
                     2-dehydro-3-deoxy-phosphogluconate aldolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008700 - (R,S)-4-hydroxy-2-oxoglutarate
                     aldolase activity [Evidence IEA]"
                     /calculated_mol_wt=20529
     Region          1..206
                     /region_name="Eda"
                     /note="2-keto-3-deoxy-6-phosphogluconate aldolase
                     [Carbohydrate transport and metabolism]; COG0800"
                     /db_xref="CDD:440563"
ORIGIN      
        1 mdfstalrte rlvaiirgrd aeasfrtvma laeaglplie vslsghdalt virraraelg
       61 daawlgagtv ltasdarraa eaganlivtp glgtgleesv rqglstlagv ltpseviaad
      121 algvsalklf pasvggpgyl qalrapfpel pfvpvggvda aaapayfaag avavgvgspl
      181 vgdaadggdl dglrkraaef kaacar
//
LOCUS       WP_457686690             152 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxiredoxin [Streptomyces nigrescens].
ACCESSION   WP_457686690
VERSION     WP_457686690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16745
     Region          3..149
                     /region_name="PRX_AhpE_like"
                     /note="Peroxiredoxin (PRX) family, AhpE-like subfamily;
                     composed of proteins similar to Mycobacterium tuberculosis
                     AhpE. AhpE is described as a 1-cys PRX because of the
                     absence of a resolving cysteine. The structure and
                     sequence of AhpE, however, show greater...; cd03018"
                     /db_xref="CDD:239316"
     Site            order(25..26,28)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239316"
     Site            order(43,46,117)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239316"
ORIGIN      
        1 maievgtkap dfelknqhge lvklsdfrge kavvllfypf aftgvctgel calrdelpqf
       61 vnddvqllav sndspfslrv faekegleyp llsdfwphge asraygvfde ekgcavrgtf
      121 iidkegvvrw tvvnglpdar dlndyvkalg tl
//
LOCUS       WP_457686696             414 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686696
VERSION     WP_457686696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /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=43703
     Region          31..>282
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msrllttarr grrtligaav avaertpadr draldglral allavptghw liggftldtg
       61 galhnasllt avgglapasw vlqllgiffl vgghasvlsf rratgrgest wtwlrgrlvr
      121 lgrpvlgvta vwavllplly glgvpeatlr tgatlviqpl wfvgvyavit altpcclraa
      181 rwmgawaaap laaavaavdf lrygpyadam ppwlsllnll pgwmfayqlg vswgerrlgg
      241 raawslllgg aavfaalllf fhypasmvgv pgqdrtnshp psllvlalaa aqsgaavllr
      301 erlarllrrp vlwapvaivn lsaltilcwh qtamlslavp asflgqvpgl tvapdtlgwv
      361 larlawlpvf aaallfigrt thrfeapwtg vdgvrraata llaagfgafa lgla
//
LOCUS       WP_457686693             217 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686693
VERSION     WP_457686693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24241
     Region          15..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matptphtap aglrerkkqr trdaliraal elfteqgyea ttideiaeav dvsqrtyfry
       61 fankedvafa vqemvearfl eeltarpate apltalrsav mvawddigsa iesvipvely
      121 mrsfrmiest palvaahlrr sseleeeiar liarregldv dadfrprvlv aafggvmrva
      181 grvwgegqdc svasirevtr syldhigpam eddwrvr
//
LOCUS       WP_457686698             394 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686698
VERSION     WP_457686698.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41798
     Region          126..388
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msepasrdah phsatlrrle nssgklaaaa iarmdatlpw yramppenrs wiglvaqagi
       61 aaftewfrhp etpqaistdv fgtapreltr aitlrqtvem vrttievmes aidevaapgd
      121 esvlreallv yareiafata qvyaqaaear gawdarlesl vvnavlsgea degavsraaa
      181 lgwnspehvc vvlgtapdgd seltveairr aarhaklqvl tgvlgsrlvv itggsdnplk
      241 aakaligpya agpvvagpvv sdllaatrsa qaaaaglrac aawpdaprpv laddllpera
      301 masdpvareq lveeiyrple eagsalletl svyleqassl egaarmlfvh pntvryrlrr
      361 vtdvtgwsps dvrsaftlri alilgrladg eaqp
//
LOCUS       WP_457686700             348 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686700
VERSION     WP_457686700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36700
     Region          21..338
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
     Site            order(74,85,110,180,182,240,280,306)
                     /site_type="active"
                     /db_xref="CDD:185696"
     Site            order(180,306)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185696"
ORIGIN      
        1 mktqvgrepf gtledgtqvd rwtlesgpgg vrvrvltygg iiqtveapdr dgtrgqlalg
       61 fadldsyvah ggsyfgavvg ryanriagas frldgrtwal tpndgrnslh ggsrnfsrvv
      121 wdarevdggv qlrrvspdge egfpgaldvr vtytlspgga lrivswartd aptvvnltnh
      181 tylnlggdgs gsaaghelrl aasrytpcdd sgipvpgapa evtgtrfdfr taravggafd
      241 hnfaldggvr haprtvaely dprsgralel attepglqly taghldgtlt gtsgvpygpa
      301 aglaletqrf pdspnrpdfp stvlrpggty rsetvygfsv rprsagnp
//
LOCUS       WP_457686708             530 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686708
VERSION     WP_457686708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..530
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=56757
     Region          14..509
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mtgvnddepg grellraegv tksfpgvral dgvdltlrtg evhvllgeng agkstlikml
       61 sgahrpdegr llvdgaeati rsaqdaerlg iatiyqefnl vpgltvaeni flgrqprtkl
      121 glvdrkamra raaellrrvr ldvspntpva elgiarlqmv eiakalslda rvlimdepta
      181 vltseevetl feivrelrdt gvgiifithh leeigalgdr vtvlrdgrsv aqvpaatded
      241 elirlmvgrd iaeqyprrrp depgapllrv rgltrngtaa gpvfegidfe vragevvgla
      301 glvgagrtev vraifgvdry dagtveidgk elargdvraa mraglglvpe drkgqglvld
      361 aslqdnltla rldrdtrggl vdrgaqrrea atvaaqlkvr msglgqsart lsggnqqkiv
      421 igkwlltdtr llildeptrg idvgakveiy qlineltasg ravlmissdl pevlgmsdrv
      481 lvmsqgrlag elpaeeatqd avmelalqsp ggtpentkhd esamegsdvh
//
LOCUS       WP_457686710             143 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457686710
VERSION     WP_457686710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15640
     Region          1..138
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtpradsltv evvdligtvv aryyeeyeqa aaehsltgaq arvlsllsle plpmrkvaer
       61 lkcepsnitg ivdrlesrgl verrpdpadr rvklaaptee gahtaaalrt sldfareplg
      121 rltvaertll kellqrmlgv ape
//
LOCUS       WP_457686715             410 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686715
VERSION     WP_457686715.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45084
     Region          150..406
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvtavrsawr evppyqvrqf aalaleevpa laqdilreir raypqlqlvp defgepralv
       61 girqslehfv ahltagpdrp hvhpqvfqef grgegiqgrs ldvlqavyrl gvrlawrrla
      121 eigqqvaipa pamyelaesg yeyldglvae svrgyaeaaa rqagerlrlq rrlmeqlftg
      181 pggrrrgaga adgvppalae raarigwplp ervavavllr pareavapav apdvlldmes
      241 erprmvvpep dapgrrella raaagwsgai gpavplldaa kslrwagaav dltergllpa
      301 gellqcteht ealvllppee liedltrrrl apldscgpah grrlaetlla wletrggape
      361 vaarlgvhpq tvryrlrqir elwgteiddp drrfelelvl rarrlrgels
//
LOCUS       WP_457686731             421 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457686731
VERSION     WP_457686731.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44578
     Region          22..419
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mvdahqtfvi vggglagaka aetlraegft grvilicder dhpyerppls kgyllgkeer
       61 dsvfvhepaw yaqaqielhl gqpavhldpg artvrlgdgt livydkllla tgaeprrldi
      121 pgtglagvhh lrrlahaerl rgvlaslgrd nghlviagag wiglevaaaa rsygaevtvv
      181 eaaptplhgi lgpelgglft dlhrehgvrf hfgarfteiv gqdgmvlavr tddgeehpah
      241 dvlaaigaap rtalaeqagl dlvdreaggg iavdaalrts dpyiyaagda aaadhpllds
      301 rlrvehwana lnggpaaara mlgqnvsydr vpyffsdqyd vgmeysgyap pgsyaqvvcr
      361 gdvakrefia fwlgadgrll agmnvnvwdv aesiqqlirs gaslapeala dpevplasll
      421 p
//
LOCUS       WP_457686733             290 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces nigrescens].
ACCESSION   WP_457686733
VERSION     WP_457686733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29520
     Region          43..269
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtapiphlps aplgtgdlaa eitaqlstql crvrlrgfpp petpgptlva vahgsrdpra
       61 lptvralldr vralrpglav rlghielnrp lladtldglr geavlvpllf ghghhvthdl
      121 paalagapql agrvaaplgp hpllaealhg rlleagfpga psprtavvla aagsraprsa
      181 rdtertaqll sarlggtpvl payasaadpt vadavrtlsa rghdriavag cftapgrfat
      241 qcadaapgta aaplgdhpal arlvlhrydq allartgsdp asvraatvav
//
LOCUS       WP_457686738             243 aa            linear   BCT 27-JAN-2026
DEFINITION  bleomycin resistance protein [Streptomyces nigrescens].
ACCESSION   WP_457686738
VERSION     WP_457686738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=26110
     Region          6..125
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,38,45..47,49,64..69,74..75,78,123)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(29..30,38,49,51..52,66,105,112,114,118..120,122)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 maettipilp cptiqpvldf ytalgfevtf qqkspnpfav vqrggielqf fgvkqyepad
       61 slstcyvvtd dvdglhdafr aglkaayrkv ptrglprigp lkdtsygmrq flmtdpggnc
      121 lrigqrtsed lhhrpapket faralhhasl qadskedlpa aakiidraln lderptpvqr
      181 lgllvlradv agrlgdaata atalaeaaai pltaeeresa rdsltrleel rdsdappapg
      241 ags
//
LOCUS       WP_457686742             650 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457686742
VERSION     WP_457686742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 650)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..650
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67711
     Region          63..480
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 makvsqpdgr peeppdtapa tvtttapsat ttatgpagap vaepdspaae pdarhrltal
       61 qglaalslda masvaygpes ivlvlaaags hglgftlpvt laiavlltvl vasyrqviaa
      121 fpngggsyav arthlgrrta lfaaasllld yvlnvavsvt agvaaltsaf palyddrvgi
      181 clavlalita lnlrgivdsa kaflvptavf vgailamvav glfraapaat vtadghasvl
      241 adnattvgal lllkafaagc saltgveava navpsfrapa trraqrteva lgvllgvmli
      301 glsvligrfh lqpvegvtvl aqladasfgh haafyvvqfa tmvllalaan tsfgglpvlm
      361 gllardnylp hvfglkadrq vhrhgvlala avaaallifs ggdmntlvpl falgvfvgft
      421 vcqigmvrhw rrersprwrg kallngfgal ltgvsavvvt atkfsegawl ilvalpllvl
      481 tfeavhraya rigtrlglgr lpepprraps lvvvpvshls rltaealnaa vslgdevvav
      541 tvthdtpedr patealrrdw elwspgvell elpsatrslg rpiaayvtgl tarrpgtrit
      601 vlipeaepah lwqrllqnqr gavvahavrr dtdavicrlr frltpparmw
//
LOCUS       WP_457686744             268 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457686744
VERSION     WP_457686744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29666
     Region          19..241
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mdaittdmdf ddhcaeivhq adllstglde gtrltasvps cpdwnlaqll rhlgeahrwv
       61 eelvrtrate pppdtalrhl prdttetpaa laawltegar llagtlrnag pdariwtplp
      121 sgsprffarr mahetvmhra datltlgtdf tvdqrvaldc ldewmelgsl pemfdyhpdr
      181 rdllgpgrtl hfhatdtppe aaadwlvdlt gttlawrrtq epaavsvrap ltdlllliyg
      241 rapsdngsyd itgdtellef wlsrvlfg
//
LOCUS       WP_457686750             326 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA dioxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686750
VERSION     WP_457686750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36834
     Region          56..325
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mppllalqed qlttladsaa prtpalrphr ipadglyegp rilrrtpdga dvrpyerfea
       61 vpqaatigae irgldlsrpl sgdlraelnr allewkvlff rgqrlssreq refaknwgel
      121 esnpllargd skdvvrfdka aggvatfenv whtdvtfrer pamgavlqlr evppaggdtm
      181 wadmaaaydn lppeirtrin garavhdylp gfarfyspaq lapfqeefpp vehpvvrrhp
      241 etgrrmlfvn asftthivgl aqeesdrllr llfqqaqvpe fqvrwrwqag dlafwdnrat
      301 qhyavndygt hrrvaervai agdrpy
//
LOCUS       WP_457686758             411 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457686758
VERSION     WP_457686758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 411)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44663
     Region          19..408
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,90..91,98,102,109,240..241,244,248..249,252,
                     285,290..291,294..295,297,321,349..351,354..355,357..359,
                     363)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,84,86,89,91..92,178..179,188,239..240,243..244,
                     248,291,294..296,398)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 maqqgqqpfv idpvgsdihg eaarlralgp vartelpggi eawsvtshtl lkqlltddrv
       61 sknprdhwpa wqreeirssw lqswigvtnm ftaygadhrr lrkliapaft arrtdailpr
      121 vesitmalld dlaahpagep ldlrarfnhp lpmqvicelf gfpegeqrae larlveaimd
      181 ttatpeqaaa taagvhalls elvgskrenp addltsllvs arddegqkmt eqelldtlll
      241 vigaghettv dllgnavhal lthpeqlelv rsgqvswadv ieetlrwaps iaalplrfav
      301 edidipdgpt irkgeailpa yaaagrdaaf hgdtaadfdi rrtrqehlaf ghgvhhclga
      361 plarmearia lpalfarfpd lqlgtadeel eptsgfisgg lrslpvrltp a
//
LOCUS       WP_457686776             435 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces nigrescens].
ACCESSION   WP_457686776
VERSION     WP_457686776.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43108
     Region          36..413
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(65..66,69,121,135,137,167,200,374,377,413)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(345,350,365,374..376,379,401,405)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtgqpaaags edqrgaprag atpgrpllpg qpgrpdvftf getmvalrgs gplklggtmn
       61 vsiagaesnv aiglarlghd vrwagavged eagqlvlrtl raegvgvsga stdpgaptgl
      121 llfeprlpev trvhyyrags agsrigadvi qrafsaappr vlhltgitps lsptaraaag
      181 lvlqlsresg slvcldvnfr arlwtaeaaa evlrewipfv dvliasddel plclpgsgdg
      241 ggegspggge gsqgakgttg aneglraega gagmgaewad gglgadggla rwasepeeat
      301 aagsaeacgd avplppqeva gdpaatvaaq arllldhgva evvvklgaeg atafthggsl
      361 hqpakpvrav davgagdafv agylsalldg egpagrlera vttgafavas pgdwegaptr
      421 aelgmlgapp gtvvr
//
LOCUS       WP_457686780             429 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686780
VERSION     WP_457686780.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Carrillo,N. and Ceccarelli,E.A.
  TITLE     Open questions in ferredoxin-NADP+ reductase catalytic mechanism
  JOURNAL   Eur J Biochem 270 (9), 1900-1915 (2003)
   PUBMED   12709048
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Dym,O. and Eisenberg,D.
  TITLE     Sequence-structure analysis of FAD-containing proteins
  JOURNAL   Protein Sci 10 (9), 1712-1728 (2001)
   PUBMED   11514662
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="ferredoxin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45943
     Region          2..429
                     /region_name="COG4097"
                     /note="Predicted ferric reductase [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:443273"
ORIGIN      
        1 mallrvlglg avvivalwla qaepsvrlda lfatlahltg llagygilvm lllmarvpai
       61 ehgvgadrla rwhalggrhv ltlclahtaf alcgyaahtg tdvlgatvdl mgypglaaaa
      121 vgtallvavg vtsartarrr vrhetwravh lltyvgaala fahqlagpdl aggpfavwlw
      181 tllhttvgtl lvwyrlvvpa rqalrhglrv tevrvegpdv vsvvmqglel dalraepgqf
      241 frwrflsrrl wrtalpfsls apvrddtlri tvkacgdhtr rirrlrpgvr vlatgpfgam
      301 tahrrtrrkv llvaggvgit pmralfetlp gepgdltlly ragnaaqlvl reelegiaaa
      361 rgaalhyllg psdgpfdpla pqalrnlvpd laqhdvylcg ppgmstaata aleragvpad
      421 rihseqftf
//
LOCUS       WP_457686782             495 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686782
VERSION     WP_457686782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50313
     Region          47..460
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,310,313..314,317..319,322,350,354,409..410,
                     414,418,434,437..438,441..442,445)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mplgapatap eaafpdapat peapaapgpa pqqqrptvlt plglltvllg aalpmidffi
       61 vnvalptidh dlhagpamle mvvagygvay amllvlggrl gdmigrrrlf lwglaafglt
      121 slacglapda wtlvaarvaq ggaaalllpq vlatiqattt gkrrakavsl yggtagvssa
      181 vgqvlggllv svdlagtgwr avflvnvpma aaawllaart vpetrsphpa rvdgpgtall
      241 atalialllp ltegraagwp lwawvllatf pfaatafvlv ehraerlgrt plvppsllri
      301 psvnsgllml vpftlgfggf mfvvavalqs glhfgpfaag lslvplcaaf flaslagprl
      361 vlrfgrrvvi agsliqgagl allaltvhag wpgisvagla psmavlgigq gmvmpvlmri
      421 vlselpmtqa gvgggamvtt qqsglalgva tlgtlflsll psvgirdall aalltqlaiv
      481 agttllalrl prtvr
//
LOCUS       WP_457686787             298 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457686787
VERSION     WP_457686787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30467
     Region          8..289
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msnahdprtp vtvlglgamg salagafvga ghpttvwnrt pgkaedlvar gavradtvae
       61 avaasplviv cvvdyaaahe ilepagprls grvlvnltsd tperarsaaa waaghgidyl
      121 dgsvmvpttd vgqpgatlly sgsrkafety ketlkvlggr aaylgddham aavydlalla
      181 ffysamaglv hafalagaes vpaeefvpft gaiadilppl aagmaqdldr gvlrgdqdni
      241 vmeaagmahi ieasvdrgin tdvlaavkgl adrtiaaghg kagflsiiee mrkpsakg
//
LOCUS       WP_457686793             383 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686793
VERSION     WP_457686793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40193
     Region          1..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnlelsaeqt aarqlakdft dreitpyata wdraeqvdrg ivkklgdlgf lgltvpeeyg
       61 gsggdhlsyv lvteelgrgd ssvrgivsvs lglvakavaa wgdeeqkraw lprltsgeav
      121 gcfgltepgt gsdaanlttr avrdgdsyvi dgakmfitng twadvvllfa rtgdapghqg
      181 isaflvpads pglerreihg klglrgqata elvldgvrvp aaamlgpegk gfsvamsala
      241 kgrmsvaagc vgiaqaalda algyagereq fgkpiarhql vqelisdiav dvdaarlltw
      301 rvadlidrge pfvtaaskak lfaseaavra asnalqvfgg ygyideypvg kllrdarvmt
      361 lyegtsqiqk lvigraltgv saf
//
LOCUS       WP_457686798             941 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686798
VERSION     WP_457686798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 941)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..941
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=101621
     Region          124..930
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mrrrtgrlrt aaaaalfalg atllapppta aaaaapqdan dycqgqcgdi lppgatgnat
       61 lveilgnklf gthpehstdq lapygalasg yqsltddtlg sffndasfgv padqvgkvtt
      121 prndvtitrd kktgvphikg ttrygtefga gyaagqdrlw lmdlfrhigr geltsfagga
      181 lanqgleqqf wpqapytedd lqaqverird tngergklam qdaqayvdgi nayreqskng
      241 ryfpgeyvlt ghvdaitnag eikpfkltdl ialasvvggl fgnggggevp salallsaqq
      301 kygvekgtev wesfrerddp eaaktlhdgs sfpyavkpak akgvalpdrg svtpeplvfd
      361 rtgaatvksg tqprdpvkap kkykkleglf kdgvlpkgsf dptqhrgmsn allvsgkhta
      421 sghpvavfgp qtgyfapqll mlqeiqgpgi sargasfagv gmyvqlgrgq dyswsatsag
      481 qditdtfave lcnadgstpt kdstsyryrg acvpmekler tnswkptiad ptaagsyrmq
      541 vfrtkygtvt hratldgkpv aytaqrstyr headsiigfq mfndpsyvrd aktfqkaaeh
      601 igyafnwfya dsrdiayyns glnpvrnpdv dpslpvkadd ayewkdydpe tntteytpsa
      661 qhpqsvnqdy yiswnnkqak dydsagygng svhrgnlldd rvraltkdgg vtrasltram
      721 seaavtdlrg edvlpellrv vnsepvtdpk lktavqqlea wrkdgaqrre taagshtyth
      781 pdavrlmdaw wplmteavfk pglggdlyda lranlgides psaghgptga hagsafqygw
      841 wsyadkdlra vlgdkvagpl grqycgngel sacrdtllat lqqasgktae qvypgddsck
      901 agdqwcadai ihrtvgglth atiswqnrpt yqqvvefpah r
//
LOCUS       WP_457686801             352 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686801
VERSION     WP_457686801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36573
     Region          63..266
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(122,124,126..127,200..201,219,256)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(122,124,126,200,219,256)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mddataphka artsatpsaa rsagpgttgp dateppgagt paapppaags pvpepyltel
       61 aagvhafiqp dggwclnnag fvtdgdatlv vdtaaterra rllrqrites gapaprtvvn
      121 thhhgdhtyg ngvfapeatv ighascrrel laaghqlhav wpeveygdir ltppevtytd
      181 eltlhvgeie vrlihpgvah ttgdtvvwlp rerivfagdl vfhggtpfll mgslagslra
      241 vrtlraldav tvvpghgpvt gpevydgier ylrfvgrlaq egraagrtpl etaqeadlgp
      301 faelaeserl vanlhrayae lagaapgvpl dpmaafadma vlnggvpvsc ha
//
LOCUS       WP_457686805             439 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457686805
VERSION     WP_457686805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44785
     Region          11..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(21..22,25..26,29,62,117..118,120..122,125,145,
                     148..149,152,230,233..234,237..239,242,266,270,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msgllrrhrd frllwcgeta gkfgaavsnv aiplvavstl hastfavgli sacgwlpwll
       61 iglpvgvwvd rlrrrplmla aaalsmvlfa avpvlarygg ldlglliava lltgaaavlf
      121 qtaysaylpt llapadqaeg naklhgsasa aqiagqgasg liaqlagavn glfahaatfl
      181 vallcllgir hreprpasre gtprsltgev aeglrlvagd rwfrtltlfg aasnlalmgy
      241 qsltavflvr evglapgavg gllalastgg iagafvvrrt agrigtaram llfelgvpca
      301 allipltspg agtllyvags fgvsagvvag nilkvsfqqs ycpppllgrl vasssflnyg
      361 tlplgallgg algsalgvrt amwimtagvp laslillfsp vrtvrelpvr paegergepg
      421 pgaaerdgaa erdgassrh
//
LOCUS       WP_457686807             266 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457686807
VERSION     WP_457686807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  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 266)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28544
     Region          20..229
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mhpatppsap pplpshgppr rvlvveddpt vaevvtgyls ragyttahaa dgfaaldraa
       61 dfrphlvvld lmlpgidgle vcrrlrrgdg pavpvvmlta rgeeadrilg lelgaddyvt
      121 kpfsprelvl rigsvlrrae sappaaapaa vlragdltad pggrradrag ralsltaref
      181 dllvflmrhp grvfareell hrvwgwefgd lstvtvhvrr lrekieadpa aprlvttvwg
      241 agyrfdavgd epppedgplr gdgpls
//
LOCUS       WP_457686820             531 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686820
VERSION     WP_457686820.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..531
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55815
     Region          7..499
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 methdraaav haegivkryg ptvaldgarl tvrpgeahal vgrngagkst lvsvltgmer
       61 pdagrvtfgg epapgwgdta awqrrvacvy qksmtvpelt vaenlylgrf qgartirwra
      121 lhtrarella eygvevdtaa rirdlgveqr qfveiarals fgarliilde ptarldaggi
      181 drlfaklral raqgvaflfi shhlqevhel cdtvtvfrda rhvltapvpg lakdalvaam
      241 tgeepaavrq prpgvrrage pvlrtealav dghfapldlt vragevvgla gatasgstai
      301 getlvglrtp dagriavrgr pvrtgsvpha ldagigyvpe drhregliph rsvaenatlt
      361 vtgrlgpmgt vlpsrtrafa rrmiealdik atgpgqpvsg lsggnqqkvv iaralarepa
      421 vlvairptng vdvkskdall gvvrevadgg sgavivsdel ddlrvcdrvl avfhgrvtae
      481 fpagwrdhel vaamegmaag grgqhqppgt gggrdaapas pgregtegta s
//
LOCUS       WP_457686821             344 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457686821
VERSION     WP_457686821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35831
     Region          29..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtetasppat davdrppprr rprieparwr dfslvpvifv lgvigfivsp afltqdnlig
       61 viqqstelgl lvlgealili sgrmdlsles tiglapvlal wlvmpadgar faglelfpaw
      121 taiplclavg aavgaangfl ilnlrvngfi atlgmltmlr glqvgisegr signvpesfa
      181 ylgkadwlgv paavwiclal falggaalgy lrhgralyai ggnpeaaraa girvdrltwi
      241 vlalggvlaa fagilytghy gavsasqgng wifqvfaaav iggiglkggr gtlfgaltgv
      301 ltlqlvinvm tlggvpplwt qflngmiiiv alvisrftsg ekqd
//
LOCUS       WP_457686822             333 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457686822
VERSION     WP_457686822.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  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 333)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35357
     Region          19..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(24..26,56,61,87,145..146,177..178,199,227..233,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(56,61,87,145)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mryppygpre lgrtgvtvpp lglgcaplgn lyravpeeqa revvhtalat gagyfdtaph
       61 ygvglseerl gralrghdra sytlstkvgr rlrplapger aagegfvdtp ararvrdlsr
      121 dgiratldas ltrlgvdavd ivylhdvedq lrevyetgfp alaelraqgv vraigfgmnh
      181 saplarlvad ldadvvlcag rwtllertaa gdllpvcarr gtsvvvggvy nsglladpsp
      241 gapynyapap aplldrarql aaccaefnip lkaaalrfpf ghpavaaavv gaatpeemae
      301 narlftqqip delwhtlvar glldpdlplp lnd
//
LOCUS       WP_457686823             285 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686823
VERSION     WP_457686823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30125
     Region          2..275
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mridahhhlw dlsrreqpwm dgpwadpirr gyalsdltph ltehgidgtv lvqssssyee
       61 taellalaag dgpvagvvgw adlrdpalae vlaalpaglv girhqvqdep dpdwltrpdv
      121 lrglgalaga glvydllvtp relpaahtav ralpqlafvl dhagkppvvt gewqpwadav
      181 talaalpnvs cklsglvtea dreawrpqqi lpyarhvlda fgpgrvmfgs dwpvctlaag
      241 yedvvalaea atgqlaaaer sdvfggtagr vygigtppap dlpgr
//
LOCUS       WP_457686828             370 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686828
VERSION     WP_457686828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 370)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..370
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          30..357
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtsneaappp gantgaagaa ppgrpaaarv tsrdvaraag vsqaavslvl gdkwrgrvsp
       61 ckaeavrtaa relgyrpnla arslrmgrtr tvllvvpvlt teffarvytg aaraaadhgf
      121 gvvlypspeg igparnpfds aaatldgvia ssmaaealta lreadlplvm ldsdpgddra
      181 datvnldiad garqlighls alghrrithl aadvpswtfe lraravadsl hgvpgaalrr
      241 qptalsvdag lhaahaaltg pgprptallc dddiiaagac kavrrlglrv pedvsvtgfd
      301 dlalavavep elttvrlpae efgeagmral mtvldgrpad aptlpvelvp rgstappvda
      361 pgnaarpggk
//
LOCUS       WP_457686830             328 aa            linear   BCT 27-JAN-2026
DEFINITION  FKBP-type peptidyl-prolyl cis-trans isomerase [Streptomyces
            nigrescens].
ACCESSION   WP_457686830
VERSION     WP_457686830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11425492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /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]"
                     /calculated_mol_wt=33858
     Region          225..326
                     /region_name="FkpA"
                     /note="FKBP-type peptidyl-prolyl cis-trans isomerase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0545"
                     /db_xref="CDD:440311"
ORIGIN      
        1 mnltkntrra avaltvpill ftaacgsddg kgasggavak vegkagekpk itvpkgakps
       61 dkavtktlie gkgatvkkgd lvrldfeaks mkgqnlggsw tpqpgskpgg prtqvvsevt
      121 dqmtqqmlpp kvlsavagqk vgsrfevegt akaligagln pqagikpedg lvwvvdvvga
      181 kkvdkkakae geqaepedgl pevtapdgka akvdvpkgek apkdlkeqvl vkgkgpevka
      241 gdgliaqytg vkwedgkkfd sswdhggata fqigtgqvvq gwdkalvgkh vgdrveivip
      301 pklgygaspq helakntlvf svdivgtv
//
LOCUS       WP_457686833             285 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457686833
VERSION     WP_457686833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31153
     Region          5..260
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maaerpsrkk paahrarvqr teqltphmvr vvlggeglae feageysdhy vklvfprpgv
       61 qypepfdiaq iraefprdqw pstrtytvra wdsvtreltv dfvvhgdegl agpwaaaaqp
      121 geeifllgpg gayvpeaaad whllagdesa lpaiaaslar mpagvpvhaf ievagpeerq
      181 eldapagaei swlyrggapv grelvaavra lefpsgrvqa fvhgeagfvk elrrllrver
      241 eiprealsis gywrkghded gwqaskrdwn qqveaeqepa taaas
//
LOCUS       WP_457686834             418 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686834
VERSION     WP_457686834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 418)
  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 418)
  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 418)
  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..418
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..418
                     /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=44037
     Region          1..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 msrlqaehly kvfgrrpeda vrkleagagr eelraegtta avidasievd egqifvvmgl
       61 sgsgkstllr tlngllepta gtvrfdgqdl tslsakelrk vrsekismvf qhfalfphrs
      121 vlenaaygle vqgvpraern rratealelt glkgwekswp delsggmqqr vglaralatd
      181 adlllmdesf saldplirrd mqdqllelqk tlkktivfit hdlneamrlg driavmrdgr
      241 ivqigsaedi lvtpandyva sftqdvdrtr vltagaimae vgtvlgattp egrklttaae
      301 fraaapatvg vdtplvelft pcststvpva vtdehgdlvg avaaerllav lgegdrqaaa
      361 ggvpaqapaa dgtavalgkt pavdtpddga pagdpaaakd svatpgdndp edkviaga
//
LOCUS       WP_457686846             321 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457686846
VERSION     WP_457686846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32598
     Region          52..297
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrsndsatat vtiavstpdt agqdtptaaa tpargtlvsr gallaalgva afsltfpata
       61 walegmgpwt vvmlrsvlaa vlaggalavf rvrlperrhw tgiavvaggv vlgfpllttl
      121 alqtsttsha avvigllplt taafsavrtg arpsrtfwia slvgavvvig favqqsggap
      181 grsdlllfaa llvcaagyte ggrlarhmpg wqvigwalvl alpvtvagat valsteplrl
      241 tahaiggllw latgsqflgm vawyrgmaai gihkasqlql aqplltlvws vlllgeqlpp
      301 aapaaslavl aciavtqrsr g
//
LOCUS       WP_457686849             351 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457686849
VERSION     WP_457686849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36451
     Region          115..321
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpgnggcgvd agdlrdtkda ggpragagaa tepgarpyvh pelaaafaal perpenpyad
       61 veavragfra lmaprmpahd prvtvrhasv pgpdgntvev qvlrpagaeg vlpgvlyvhg
      121 ggfvygeldg pspmardaca aagavvvnvh yrlapehpyp agaedcyavl ewmaaaagel
      181 gldagriavt gasaggclsa alclmardrr gpriafqcll vpclddrggt asarrvddrr
      241 ivngtgmrht wdtylgpgrg pdvpayaapa ratdlsglpp aylltcgldp lrdegldyar
      301 rlteadvpve vkdvpgawhf feayvpesgp arrttahwla alrsaltedd a
//
LOCUS       WP_457686852             274 aa            linear   BCT 27-JAN-2026
DEFINITION  zf-HC2 domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457686852
VERSION     WP_457686852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Laity,J.H., Lee,B.M. and Wright,P.E.
  TITLE     Zinc finger proteins: new insights into structural and functional
            diversity
  JOURNAL   Curr Opin Struct Biol 11 (1), 39-46 (2001)
   PUBMED   11179890
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="zf-HC2 domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28552
     Region          8..40
                     /region_name="zf-HC2"
                     /note="Putative zinc-finger; pfam13490"
                     /db_xref="CDD:463895"
ORIGIN      
        1 msgehasrql iddyargdat maadtvwale ahletcalcr shlaacvate apgiaalvdt
       61 vraglepqld aavrapsrry rprwvaawlt pvmapwlamt vlvtlmalvl davarpmflg
      121 gvspvlaiap vlplcgvaas wsrgldpahe ltastaragl plllrrttav lvvvlpalvv
      181 egwltgtmsa aqwllpslaf tstalalgsv vgvtraatgl vgawgvvvvl awatdhgpvn
      241 lervlqpdql pawglflalg igaviarrna ystl
//
LOCUS       WP_457686864             313 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686864
VERSION     WP_457686864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32239
     Region          <64..247
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mladrpdgtv vrsgrtvaka hapdadprel tarlriaahp llhgillppl sltaldgflt
       61 laeegraltr wpygspvppd dpdaapweda arllarlhcv dlrqlpgsvp pmrgpakaar
      121 alarlrtaqa saagpppgsr aprtaagals aaaaaveraw allppwarde apppgagtlc
      181 hgdlhlgqlv rhpagdgpwl lididdlgrg dgawdlarpa awfatgllap diwtrflaay
      241 rtaggpavgp dgdpwpdlei paraltvqta alavakataa aspldeaeta vvdacarmts
      301 ppqqlasagp dvg
//
LOCUS       WP_457686876             258 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686876
VERSION     WP_457686876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26571
     Region          72..244
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(77..80,130..135,168,170..171,194,200..201,224,226)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(79..80,130,134,170..172,194,224,226)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mlraaasaaa agalvtgcdp hraddpgavr pagrpsasga ghappapvra arpptrvpgl
       61 pvqiehgprn gravaltfhg rgdpgmatal lgeaersgvr vtvlaigdwl deqpamarri
      121 ldgghelgnh tlhhrnical paaeayaeis gcadrlrklt gtigswfrps qtrratplvt
      181 elarkagyph vlsydvdsld andpgaaavq rtvldsvgpg svvslhlgha gtvaalppil
      241 dglrrrglra vtttelvt
//
LOCUS       WP_457686914             215 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457686914
VERSION     WP_457686914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23718
     Region          32..210
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 msqllrvqnf tvssdgfgag egqslekpfg hadpgnllaw afatdhppin rsepggsrgl
       61 ddyftrdyar nigaeimgrn kfgpqrgpwq dhewqgwwgd eppfhtpvfv mthhkrpsft
      121 lsdttfhfvd gdpaavlaqa keaaqgqdvr lgggatiirq fleadlldtl hvavaptklg
      181 sgarlwespd elldrfhqdv vlspsgvthh lfwrk
//
LOCUS       WP_457686923             376 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457686923
VERSION     WP_457686923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..376
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38279
     Region          185..375
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkvaaiagg vvlapvlvia piavalagas naqaacgeag gagavdakav akqvesilkg
       61 ggkgsvsvpg ldnvkeqipn tktilatgvv mkvpargqii alatalqesg lrnldygdrd
      121 slglfqqrps qgwgtaqqvr dpvhastkfy eallkvsgwq smtvaqaaqa vqasgfpday
      181 akweplatal qkaiaknlps kgtsgkdstd akpeapaggc gtggdgsgfg pipagsvpkv
      241 ykipadapka vrmairwglg qlgtpyqwgg sctdahgqdp mgrcdcsslm qasykaggvs
      301 isrttytqvk egkavsvdal kpgdllftrg taavpehvgm figqglilqa prtgdvvkis
      361 tlsswrpdil aarrva
//
LOCUS       WP_457686945             597 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457686945
VERSION     WP_457686945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..597
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62709
     Region          169..560
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mssprtstps tttgtdllly lllavaglgm aggslawlfg nltnaiagsd pwaayhpeet
       61 llhpeqvwph lphpalitgc yvlpalvlia tavvaaklwl rfrsspsgla trrdleplla
      121 kqiaakaidl rpslagkkpk diapddrgvl lgtfkpgrde lrsswedvil aimaprsgkt
      181 sglaipailr apgpvlltsn kaardaytat vdaraevgtv wtldpqqiah apqtmwwdil
      241 adardlagar rlaghfvtas vdkssagdfw staaantlta fflaaaqarr pitdvlawla
      301 spadrtaidl lqdagfdava aqlqgtvaga vetrdgifet arqyasclld pgiaawvtpp
      361 kslekvrefk peafatskdt lyllskdggg sasaiiaaaa davmrtavaq aerdggrldv
      421 pllaildeaa nvckiadlpd lyshlgsrgv ipvtilqsyq qgvrvwgqsg mdsllsaati
      481 kvigsgmdda dfadkisrlg gehdvrtvsv stgesgksts vsmrqervlp ldvlrampkg
      541 tavlmatgir laridlkpwy tgqgakklga asakataais eraaakalrq ddfgpaa
//
LOCUS       WP_457686954             158 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RelE family toxin [Streptomyces
            nigrescens].
ACCESSION   WP_457686954
VERSION     WP_457686954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="type II toxin-antitoxin system RelE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0017148 - negative regulation of
                     translation [Evidence IEA]"
                     /calculated_mol_wt=17564
     Region          11..98
                     /region_name="RelE"
                     /note="mRNA-degrading endonuclease RelE, toxin component
                     of the RelBE toxin-antitoxin system [Defense mechanisms];
                     COG2026"
                     /db_xref="CDD:441629"
ORIGIN      
        1 msraryafaa hpealadlrs vpedirdlal lelqhlvhgn ergaalhrel agchkvyvdp
       61 etrwrlviqy rdapassqhk reiyllavge rqdqaayrta arrlererea saatqplgrr
      121 aeaararsph gssgsritah pqtpaapatr prgrrtrs
//
LOCUS       WP_457686956             167 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686956
VERSION     WP_457686956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18464
     Region          14..96
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpdhrisahd atlvskaidr laprwttwtl qtlaqhgqmr ftkiaaalpw lstqntqqil
       61 rrmhanglld rpghgvyevs pwgrnahsvh rtlaswhrtr avgsgpavae aertedalrq
      121 qrgegavevl qpslstapfr tancerrrds srapfttass ssrriss
//
LOCUS       WP_457686964             310 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686964
VERSION     WP_457686964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35499
     Region          39..101
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(45,49,74)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(48,73)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(55..56,67,70,74..75)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          125..302
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mdviqrasda eetgeggqka rdrvlflrde lapsapcmrl ggelrekreg mglqqqdvst
       61 algwskskvs rieggrnavk eqdlecllsl yrvdekdqep lrelaligkr pmwwkpwsgi
      121 ttaylqavls fedmaqrirs yeplylhglv qipeyaqali ergpdqgyha alaelrqmrq
      181 akfaaargke licvideasl rrpvgnahim rrqlrhlmel nedpryqlrl aelsrpnlpl
      241 evgpttifdf aeallptiay senfdgglvi qdeetvdrrv kkfdelrhmc lnprkttqkl
      301 hdllrskyyr
//
LOCUS       WP_457686967              79 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457686967
VERSION     WP_457686967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..79
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8777
     Region          1..76
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mhqtqhhigv vleqiclqar ltaeavarrs gfapcdvadf lsgkrfpssl filrfaqisg
       61 tdpqllfkvw edeherlsg
//
LOCUS       WP_457686985             196 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457686985
VERSION     WP_457686985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21905
     Region          17..85
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 mhhtknetpr tlgdltwhde aacrstgphq vdpddffpep demdriraak alceqcpvln
       61 tcldaaleng dqdgirggmt deeraplhrn frrrlsyarv navlaghdvh lthaerdavv
      121 caayldgipa eqlarilkit kehaqkryre trrqirdrav dqkeqadnge kkptsepavl
      181 kasrtkpsrd dlgtaa
//
LOCUS       WP_457686992             462 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457686992
VERSION     WP_457686992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..462
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=50891
     Region          32..94
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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          114..276
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 maarrraesd dtaakkgtst apvgvagqym gfggmlkrwr kaagvnqivl aralgigert
       61 yrniergatp rfsqpqcdal adllkldade rhalllynvg tylrastadg rpelgpalrl
      121 lidrqmpspt ylsdrnwnil aynkamaelw pwvmeprani irwalttpeg ratyhdwhkh
      181 aavfvrmlrf altthggdsd lqeliadvkk npeiqkiwda dadlvehrdg hvflasvptl
      241 gwktieivsh vaypaimpdc rfvvmtwvea epdaqrdalg gprnawaeet hntahersra
      301 qariaeadrl rdmdlhtarl vvdsaekaaa kagkdgiplp alsrlmgpas qltlspstrn
      361 vvwaveeapg ewgvsqvsps tliarvppaa ihgdaraelk rltrialpaa peaaadrvqq
      421 llseldqqqs llreiqrdld ghrsalrtpq giarevqael vs
//
LOCUS       WP_457686994             135 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457686994
VERSION     WP_457686994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..135
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15519
     Region          4..135
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mhqytyacpl rwsdadaygh vnnaqflrym eeartrmfqe vvatneegrr pnafvvsrti
       61 idyraplfyg pepvdvhvwv tkasaatfel ayairdaeql yveattkiva ynldtgsprr
      121 lseterafva rytkr
//
LOCUS       WP_457687008             264 aa            linear   BCT 27-JAN-2026
DEFINITION  2'-5' RNA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687008
VERSION     WP_457687008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29269
     Region          65..232
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mqrlqyeqas fppapppslt dpsviarhew aaldrvnemv nhwdrpgwts strayywmit
       61 fpgaaaliqr aqqcqqalrs lvfddipedg lhltlgrigp steislaqld sliasvqvav
      121 ssfslqavpm tasrgairfs vapwtplidl rimlakagas vglplrkpts gfrphigisy
      181 cnrlvpaasv rdvvrplral etvetevrqv hivelrreps ayrwevvrtl dlpaapqrrn
      241 egtragqard glhafehgdh rrlp
//
LOCUS       WP_457687010              60 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457687010
VERSION     WP_457687010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 60)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 60)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 60)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 60)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 60)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..60
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=5765
     Region          <3..54
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mtigdsledv rtglvggasv lgvtsgktsa qnlkeagaev vldslenvaq lvaaiaavtp
//
LOCUS       WP_457687019             317 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687019
VERSION     WP_457687019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34538
     Region          26..257
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mkppteqevl qaasrclrqe avsacrismg rshfvftvgl ksgesviari trhdraecfa
       61 gfaywrrqla rvgvpvprvl smdltgielp wpimlveqap gddlcnvyad ltaaekrtva
      121 gdlldirhrm sdlppgpgyg giasysdlrc hprwsdvlwe yftgaidqlt paqrqrpaig
      181 eirkaigelr sefdridplp ylidathqnv lvdggrvtai vdldelgfgd alyplgvara
      241 gllargpead cieqvaapvc vgpvrqrvfd lysaiaslkm lspsplsvtg ppsahskiat
      301 rlwtlldffa aaaahke
//
LOCUS       WP_457687012             219 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457687012
VERSION     WP_457687012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23711
     Region          5..210
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtqspvelvi fdcdgvlvds ericvkvdam imaelgctft eeeiiekfvg sstevytaav
       61 eeqlgrrlek nwlqqyehly qaafdaelta vdgvaealss lttpvcvasn thhagirrnl
      121 eiaalsdhfe erifsaddvp rgkpapdlfl haarsmgvep ercaviedsa ygvqaaraag
      181 mrafgycggl tsatrlegpg ttlfddmrdl pkllaiath
//
LOCUS       WP_457687017             398 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457687017
VERSION     WP_457687017.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  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 398)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43406
     Region          17..377
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mpgtvfvsld dftregftng lflqvrellq rvisrgrpar laciaqrtnp gterrtrtvq
       61 gctvhetlig apgqasayrq alrdllkdld pevillnsca vrlneahrav ldeclasgrq
      121 vavlvtdqly ptshdhpaae vrhyydlmrq asvhavsqti adafhsqtgv paqvlpnllp
      181 errtspapvg aagrcltlin hhpikgrrvw dalvrqrpgd aylvvetwpd vppyaspsps
      241 vqvasfspdp tpiynrtril lvpslgpegl prvaleames gvpvvahrig slpelgkaam
      301 fvspppiagy elegnvlypl vspddvkraa rdfgqtidai dhdpalrarl vangkalvrd
      361 yrshseavid rlldvwfgwr dsghsgahdd lgaarnnr
//
LOCUS       WP_457687023             560 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457687023
VERSION     WP_457687023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 560)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..560
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=60649
     Region          31..433
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 matdcsgygd gfadwrnglf lrpdgdnadv lvdlirgald ealshqgagp vyprwgqgng
       61 rspvgsghlp dgpvaseavl sqlrwwlags vkvhhhmfak nvvpppsfvn laalcavslf
      121 mpngvtgeda aetltaelsc aqamarlagy dpdqagglft fggtatnlya invgiskaqp
      181 dhaergiepg mavvgswpah ysqksacawl gigtqnyisa aslpdqttdl esmeaacrdv
      241 larghrlaci mgaggttsnm avddfveiaa mrdrlaaeyg ldymphvhad tvvgwaylcf
      301 ldydlhrnpl gfspsvvakl srlverlktv rhadsfgtdf hktgfapyts smiimrdgrd
      361 fsrlrrdggv mtplfhdkda ynpgtftlet srsaanmvat wvglqalgkq gmrkllghal
      421 etaealrrhv dalaardmtv inkhsygpdv flrcyppddp aateedfsdt ssvrrinqyt
      481 sdlfawlsrq rvpeaeqial sktsaafytp tgepvvalrv yslnpyfcgs harelivrll
      541 kgkrqfdaih patdvheaar
//
LOCUS       WP_457687027             216 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457687027
VERSION     WP_457687027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22886
     Region          6..211
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mqrlaifdld ntlvdrqgpl tdwvsafssq yalndhdrad llqvvharay psafetiraq
       61 yglapsaeal wrdycaymar svscpadvle glstlrrtgw kiavatngan eiqtekaams
      121 givdhvdavc aseaagvrkp evamfekaaa scgadlalgg wmigdgvdtd irggraaglr
      181 tiwisggrsw pggdaepdha ttdvcqaidl lltsvs
//
LOCUS       WP_457687033             107 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687033
VERSION     WP_457687033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..107
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11785
     Region          25..>86
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maaqktcpfv ptqvwtyedv kdalvqrnfg rlcqlvrerg hlrqedmall tglsqaflsm
       61 lesgqrrltn idriivlldg lnapadltgp mlrpvpltpa ppfqavs
//
LOCUS       WP_457687035             212 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687035
VERSION     WP_457687035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23258
     Region          8..95
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtnrewsptf tarvaeqmrr grkaagltvt eaaeacaalg lavpkttitn letgrrssid
       61 laeflvlaev yevppvsllf plgleasvev lpdrevstwd avawftgetr lerpapedsa
      121 rgvldtfrah sdavatalas trlakerrrk asttldsgrr ealleaagay eqlafddcre
      181 lrefrltmqq rgltppslpt elsfvdehdp ed
//
LOCUS       WP_457687047             694 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457687047
VERSION     WP_457687047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Levdikov,V.M., Blagova,E.V., Rawlings,A.E., Jameson,K., Tunaley,J.,
            Hart,D.J., Barak,I. and Wilkinson,A.J.
  TITLE     Structure of the phosphatase domain of the cell fate determinant
            SpoIIE from Bacillus subtilis
  JOURNAL   J Mol Biol 415 (2), 343-358 (2012)
   PUBMED   22115775
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..694
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74626
     Region          24..258
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          269..689
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 msasepfpag agrvqfassp pgglldllnv atvvldadgr ivlwspqaev lfgytvgeal
       61 gqyagrlmvh eehleqvlel faqvmggsgs wagvfpirhk dgstrlvefr nirllddrdd
      121 lyalglasdq atvqrverdl alctglvsqs piglvvmdtd lryvtcnpal eriygltaee
      181 lvgrrvrdvl phldheaiev smrqvlatgv ptldqeivgr tfadpdhehv wsvstfrled
      241 prgkvlgvak sivdvtdrhh maaeahharq rlaliadasv ligttldldr taheladivv
      301 pdladvaavd ildsaldrrs pprsargsal fralavkaay pteavraadp igdlahygad
      361 rlvtqcvtyg epvlvphver sdlsriardp agaallarag lhsylavplt argdvlgald
      421 lkrirnpapf deddlvlase laaraavsid narwyqrers taltlqrsll pqhpphrpgl
      481 eiayryqpag aasevggdwf dviplpggkt alvvgdvmgs gvtaaatmgq lssairslan
      541 ldlepaqvlh nldcstrgle qciatcvyai cdpghrqwri saaghlppvl mcpghapqll
      601 elptgvplgv gdipfdttal dlhpgdqlll ytdglvetrd qpidtrlhvl ldllaephgs
      661 leeacdrllh alrqpdghdd valllarvqn hppg
//
LOCUS       WP_457687065             241 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces sp.
            900105755].
ACCESSION   WP_457687065
VERSION     WP_457687065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13400505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..241
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25004
     Region          2..>169
                     /region_name="RpfG"
                     /note="Response regulator c-di-GMP phosphodiesterase, RpfG
                     family, contains REC and HD-GYP domains [Signal
                     transduction mechanisms]; COG3437"
                     /db_xref="CDD:442663"
     Region          5..220
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mssqirvlla ddrsiartgi rsvldgdggi evvgevsdla savgkarelr phlvlagvlp
       61 gtagagelvg elaaccgdeg pgvllmaheg gpdarlalga gvhgvvlhrv tpeqllsaih
      121 vvaagyriff eeqgpsgghd grfpgaaeip gvaaagfasl trrerevfrl laqglsntei
      181 saalvlsent vkshvqrlle klnlrnrvha vihayrtglv appcrepvrp ctgsrapral
      241 q
//
LOCUS       WP_457687079             391 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457687079
VERSION     WP_457687079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 391)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=42377
     Region          14..391
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(52,59,82..83,90,94,101,225..226,229,233..234,237,
                     270,275..276,279..280,282,305,332..334,337..338,340..342,
                     346)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(59,76,78,81,83..84,166..167,175,224..225,228..229,
                     233,276,279..281,381)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtdplhdplf fsdpystfar lrdaspvqki ptgskerysy lvtgyaearq afadprlskd
       61 tarffagqhs rrnlhpavsk nmlasdppqh trqrgvvakl fttgpvaemr pyiamvidgl
      121 ldgwksgtqv dlvqslaapl pvtvicqmlg vpeadhamva qwsndlfaag kpdcidaash
      181 aigdymtslv etvrvehngg llhtfvqhgn egllerdevv slavlllvag hetttnfign
      241 avlallqhps sltrlrqdpd liassldell rfdspvglat frfstealql ggveipagvp
      301 vliapgaanr dpasfvepqr ldldrnasnh lafghgihrc lgaqlarvea eealravvtg
      361 fpgmrlavps edlewrqtrl mrglkalpvi l
//
LOCUS       WP_457687084             151 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687084
VERSION     WP_457687084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..151
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16177
     Region          <36..96
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 meddqsptfa qlldylfqei hppsrgpyty aevaegirqa sagegrgvta saiqqlrtga
       61 krnptrhtik aladffgvpa gyffdgaaae rtkaeiglla amrdqdvrrv alranglsvd
      121 slnmlstvie qarkleglan dgspqgldld d
//
LOCUS       WP_457687088             343 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457687088
VERSION     WP_457687088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..343
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36148
     Region          149..337
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mspafrqmvk tnsrelfrdg ktafftlvfp llflamflgl gtltagssyr vavisapqqa
       61 apiaalqkvn gfhveawkke kpprsgdlag ydaivsvtat satvvidpgk fgalkdlrsa
      121 lsdggiseah mhittpdggp pfdplkaalp tgllmalmsi affgtatpli avrargtlrl
      181 lgttplsrmt fvlaqapvrl alvgaqlvvl ggvavwmdfl piagtlrlmg tgllgavmlf
      241 afgyliasrm rnaevvngll gllmplilfs sglflpmdml psaaetiska lpttylvdal
      301 nhdlnaaasa hsltadwlil iagaiifggl aarlfrwdqg eqr
//
LOCUS       WP_457687110             101 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687110
VERSION     WP_457687110.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..101
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10958
     Region          19..97
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 mtrpdhprhe lapllaspvr lsivaalaat draefafird lveisdsals rqattleegg
       61 fleivkgyvg rrprtwlalt ehgravyarh vaalraiadt s
//
LOCUS       WP_457687113             370 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457687113
VERSION     WP_457687113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..370
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41656
     Region          65..347
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 matvldkgag apgkrwvvry repggrsarq rqkafdrkkd avdfatkven dkrenmyidp
       61 nagkvslrry tedwlngvlm sggtwesyer ilrlhalphl grktiaqvta adveelyarw
      121 akggakpnti darsialssl fshavrhrri ssnpvkeaek pdnpvvpvde rslpsleeik
      181 aiahaigprl epavwlmacg glrigeslgv fpedfqdgll rlrrqvvryr dedglyvary
      241 aplkhrkdge wrdvpvpeff tavadrlpil nqqggmtypg lvraswdrai krlgltqytp
      301 hdlrrkwatv tltngvsihe vsrwlghrsi kvtvdqyghl tqdgrercrq vvattfrgyl
      361 peelavglaa
//
LOCUS       WP_457687116             150 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457687116
VERSION     WP_457687116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15818
     Region          66..138
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 msaplpslpv tfrptrtrvv lysvglaqla altaialalp klsggerlsf vltgllvlav
       61 llllgrpkvv arqegiavvn lttkrelawa qvlrvnlrag dpwvhldlad gtslpamgiq
      121 pgiardqair daralrdlte khgavdhtag
//
LOCUS       WP_457687119             466 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687119
VERSION     WP_457687119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
REFERENCE   3  (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   4  (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   5  (residues 1 to 466)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 466)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..466
                     /product="ROK family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45660
     Region          22..97
                     /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(22..23,37..39,48..51,53..54,57..58,60..61,74..76,
                     81..83)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(37,40,90)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          86..448
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mhppraaaag rtaspttarl indrlalqll qsegpltagq lksltglsrp tvadlverlq
       61 eaglitvvge sgaqrrgpna rlygivadra hlvgldlrth satvavadll grvraehtvl
      121 idpdgapdta vatalaavdk alaaagahap htvavgapgl vdpatgrfgg tdwipswhvg
      181 lvgalrartg vpvllenevn laaiaeqrdg aahdrdtfvl lwlgqgtgaa vvldgalrrg
      241 asggtgeigf lpvpgtgalp sasgcdggfh slagsaaica laaehgmpyg aavgpkgada
      301 sspgtgvhel ssgtganepp sgtgvhelss grgvheppsg tgapteaspt ealpaeslvr
      361 savaagdaga afldalaari algvaavcav ldpgcvvlgg eigrgggaal adrvaghlar
      421 lsplrtdvra gavggravll gavlaardaa qnelfgaagp gvsprp
//
LOCUS       WP_457687121             199 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457687121
VERSION     WP_457687121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..199
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21680
     Region          48..181
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 maparrtspt hpnstlrtns aarrekpgap pasveplqtt tvpygelvpv tvhfddldal
       61 gmlhnsrypl laerawaeyw heqgfgfdgd waaagdmcnv ikemhvsyer svtrpghyaa
      121 hlwverlgrt gltygfrlcs adgaetyarg hrvlvridaq tlrptpwsdr araiagrllr
      181 petsdagtga gtsteadaa
//
LOCUS       WP_457687127             170 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457687127
VERSION     WP_457687127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..170
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18193
     Region          <66..158
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mreterdgaa gakeaevaai eramvalrrs aarrtlarra arqggrpvpe gaafdvldvv
       61 eaaeergepa gvrevadalr vdqprasklv aaavqaghlr readqadgrr tllavtpagr
      121 erleaahtfr rsvvarvtrd wpaaeraafa rlftrfmddf gaangpsged
//
LOCUS       WP_457687129             311 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687129
VERSION     WP_457687129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33469
     Region          10..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..298
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(106,108..109,113,170,207,274)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(107,110..111,114..115,118..119,121..122,125..126,
                     128..132,134,196,224..228,231..232,235..236,239,253)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 miarnanidl nlltaldall eeqsvtaaad rlglsgpams rtlgrirrtt gdpvlvragr
       61 hmvptprale iraevrrlve aaqgvlapca padpaqlarv ftinandlfv tavgprlvar
      121 vareapqvvl rflgesyvdl pllrdgaadl elgvidspep eivteelfvd rsvavvrdgh
      181 plttgtltar rfadashlnf srrgrltgpv daalaarglr rkviatvptf taslmmvrds
      241 davgltsera gaatvrslgl rtlpiplelp pmtmemawhp rqeadaghrw lrgvvretvr
      301 eavrdvppae v
//
LOCUS       WP_457687139             732 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687139
VERSION     WP_457687139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..732
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=79523
     Region          2..710
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrrltrpgpl srpsperlra pgrqgnlpae lnrfigrdde laalarhles arlvtltglg
       61 gvgksrlagh gaailqdrfc dgvwlvelss lrephlldht vaealaladh sgrpvrtalc
      121 dhlagrelll ildgyehlvd acadltaell rrapglrvla agrrplgltg eqnvalapln
      181 tadatalftd raaavlggft vgaaneaavt elcerldgip lalelaagrl ralsvdqvlh
      241 rlddrfrllt gtargalprh qtlrtaigws helctpeerl lwarlsvfag qfdleaveyv
      301 csgpelpage lldviaelva qsvlvreeta agvryrmldt vraygagwla atpdgdrlrr
      361 rhrdwylgla twceldwfss rqaeiaarie aelpnlrval eqslecpadt hlgqylagtl
      421 wfywvgcgrl segrhwldra lelesdhdda rlkalwvagy vavlqgdtvg algalqecrd
      481 eaertgnata aayalhrtgc lalvcddmpr aeellrgalr ryreigelns nvllgqvela
      541 mavafrgepa davrlcedvl evcedhgerw trayaqfvla yaswsrgdge rartlleesl
      601 avhhafhdll gvvlaiella mvtlgegdae eaavlqgaag riwpsvglpl fgsryfrrph
      661 alceeqarqr lgaehygral rtgerlglda tvarvlrpag pvpaphrtvr ivppdtnepa
      721 aspsasgget ag
//
LOCUS       WP_457687154              91 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Streptomyces nigrescens].
ACCESSION   WP_457687154
VERSION     WP_457687154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 91)
  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 91)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         <1..91
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <2..90
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 vpeegwvevv tepqpgcavl vvantgpvvp ayevenlfep frrlrtertg sdkgvglgls
       61 ivrsvvrahd gtitarpreg ggmvmrvvlp q
//
LOCUS       WP_457687176             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687176
VERSION     WP_457687176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20645
     Region          8..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msprgvatpd vrerlfaaae rvlekdgpga ltsraittea gcakgllhth fegldefvae
       61 lcldrfarta tkaqalsela gqgsvvanlg avalalldsg gpviaglamt rpaaalrire
      121 aleggapgft avqeaitsyl eaerrlgrva dtvdpptaal avvgtahhll mtswpgtpdp
      181 raemtrlvav lmgpppggnp ap
//
LOCUS       WP_457687174             224 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687174
VERSION     WP_457687174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24653
     Region          51..149
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mrkpgddrlv etqrrhwqqt ytahpdmygt apsapavhaa evfrsvgvrt vlelgaghgr
       61 dalffarsgf dvtatdfsst gleqltahat esglaervtt lqhdvrnplp lpddsadaaf
      121 ahmllcmtls teeihsavae vrrvlrpgga fvytvrhtgd ahygtgiahg ddiyehggfa
      181 vhffdrvlve alatgwelre ihpfdegdfp rrlwrvtqtv prna
//
LOCUS       WP_457687178             282 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687178
VERSION     WP_457687178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30086
     Region          39..151
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mldvvnteqa qawngpegth warnqdrwna vnegfnepll daagiaedhr vldigcgsgq
       61 ttrlaalrap ggralgldls gpmlaeartr aeregisnaa feqgdaqvhp fdvgafdsav
      121 srygvmffad pveafgnigr alrpggrlaf vcpadaalng wvtamvalrd llpvgdfgrp
      181 glpgmfslaa pdrirevlaa sgftgitvnq aqmygvwghg addaadfllt tgpgrhlmeq
      241 vdtatrtrar rtledhlrth eaadstvrlr stswlvtadr la
//
LOCUS       WP_457687187             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687187
VERSION     WP_457687187.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23505
     Region          10..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpklwnetid ahrhavreat ldataalvae ngllsvtmsr iaqeagigra tlykyfpdve
       61 silgawherq vtehlahlte vrdqagspge rlkavleaya llsrgrhehh gtevaallhq
      121 gehmaqahqq lkglirdlla dgaatgdlra dvapdelady clhalnaagg mssraavqrl
      181 vkvtldglqp stdaveeavt dedttghsgh rhhrhaph
//
LOCUS       WP_457687179             149 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687179
VERSION     WP_457687179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16240
     Region          13..108
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(14..16,30,46..48)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(60,63,67..68,77,90,94,100,104,107..108)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mkssdgtqss stmtigavae rfglaahvlr hweamgllip drdgnghrry gqddlfrvaa
       61 ilrakeaglg ledvhamita dgplkrrevl keqhtaleqv iaaaqaqlel iqcaldcdhd
      121 dfttcphfrq maadrigvqa prhiplhta
//
LOCUS       WP_457687196             211 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687196
VERSION     WP_457687196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23567
     Region          14..157
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpeprnterl rrywdkhars ydrqmrffdr tlfagsrvwv csqasgdvle vaigtglnlp
       61 hyppgvrltg iewspkmlai arrradelgr tadlreadaq alpfadasfd tvvctlslca
      121 ipddrravae mvrvlkpggr lllldhvpst alpvraiqrl velvtvplgg ehllrrplrh
      181 vqdvglvier qnrsklgive rlaahkpaht p
//
LOCUS       WP_457687203             139 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal-responsive transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687203
VERSION     WP_457687203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 139)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140950
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="heavy metal-responsive transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15136
     Region          2..129
                     /region_name="HTH_HMRTR"
                     /note="Helix-Turn-Helix DNA binding domain of Heavy Metal
                     Resistance transcription regulators; cd04770"
                     /db_xref="CDD:133398"
     Site            order(3..5,19,36..38)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133398"
     Site            order(50,53,57..58,67,78..79,82,85,89,95,99,102..103,110,
                     120..121,126,128)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133398"
     Site            order(78,113,126)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:133398"
ORIGIN      
        1 mltvgrvakr tglspkavrl yeanglidpp ertasgyrty tdkvlpelhf irraqalgls
       61 lkeirrildl qrhgqqpcdl vidllddhla qvdqriadlq alkktlqdar haadqaagrg
      121 epgvicpiie saslapegt
//
LOCUS       WP_457687200             775 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457687200
VERSION     WP_457687200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 775)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 775)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..775
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80614
     Region          18..771
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtttpiages pgqtepaqtv dlsitgmtca scaarierkl nklpgvsasv nfatgnarvd
       61 ypadvtpqdl vavvkdlgyg atlpappata gpevakstae eaagaepaae eerhlralrd
      121 rllasavltv pvvvlsmvpv lqfrfwqwla falaspvalw gawpfhraaa lnlrhrattm
      181 dtlvslgvla awlwsvyalf lggagepgms mgfsllprad ehagsaeiyl evaaalttfi
      241 lagrffeara rrrageaira lmdlgakdvt vlrdgrevrv pieqlsvgde fvvrpgekia
      301 tdgvvvegss avdeslltge slpvevgpdd avtgatvnag grlvvratrv gadtklaqia
      361 rlveeaqtgk aevqrladri saifvpivil lavetlfgwl ilgypaaval taavavliia
      421 cpcslglatp talmvgtgrg aqlgllirgp evlestrrid tivldktgtv tegrmrlaav
      481 vaadgedrte ilrlagaveh asehpiakai adaatdelga lasvaefanh agrgvtgsve
      541 grgvmagras wladqwnlei paalgqaqqe aeragrtvvf vawdekvraa lvvadtvkpt
      601 saeavaqlke lgltpvlltg dntaaaehva aevgiekvia evhpedkvae vkrlqdqgkv
      661 vamvgdgvnd aaalaqadlg lamgtgtdaa iaaadltlvk gdlrgaadai rlarktlsti
      721 kgnlfwafay nvaalplaal gllnpliaga amasssvfvv tnslrlrrfq ptnqr
//
LOCUS       WP_457687213             436 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457687213
VERSION     WP_457687213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..436
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45686
     Region          15..382
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(25..26,29..30,33,66,116..117,119..121,124,143,
                     146..147,150,227,230..231,234..236,239,270,274,338..339,
                     343,347,363,366..367,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mkgtlaqvrs yersvqllmv nqftinlgfy mlmpylaahl sgtlglagwv vglvlgvrnf
       61 sqqgmflvgg tladrlgykp miiaglvlri igfatlglvd svpallaasa atglagalfn
      121 pavraylaad agerrveafa lfnvfyqagi llgplagmvl tgvdfrvtcl vaagifalls
      181 ivqiralpar raddakdstg tgrresvlaq wrgivanrpf llfsvamigf yvmqfqvyla
      241 lplevrrlgg dgtfgtaava vlfavsglst ilfqtkvtaw ckarmepgra ltwgllimgv
      301 gfvpllvpta vpvpdggvgl wllaavppsm salllalgtm iaypfemdti vrlsgdrlva
      361 thyglyntic gigitlgnll tgaaldaara agmsaipwia lcalglacaa alyglhrtgr
      421 lappnarnaq petvta
//
LOCUS       WP_457687224             152 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687224
VERSION     WP_457687224.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16352
     Region          4..127
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mrtsrvqrar rhtvdilrrw qltsdtieta rllvselttn avrhanpass vappaprevg
       61 tislrlhltg psvlilvsdc grrppsrrma dsdatcgrgl llteatasrw gydhptgdgg
      121 kvvwaevsaq ygslgerpvs ppppggqlkd tr
//
LOCUS       WP_457687226             137 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457687226
VERSION     WP_457687226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 137)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14734
     Region          9..117
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mtqqtaderp giaaaiivhe grvlmvrrri segklswqfp agevepgetc eeaavretke
       61 etglnvsave llgervhpat grlmsytace vlsgtahvad teelaelawv ahdqipehvp
      121 yglfgpvqqy ldtalag
//
LOCUS       WP_457687245             479 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457687245
VERSION     WP_457687245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..479
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=52701
     Region          147..423
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtnrsfkvrf yktevykgkr gttytvrwsv ngrrhgeafk taasadsfra vllvaannge
       61 pfdqdtgrpa shaapaaevt wydfalryvd mkwsrisann ristakaltk atlallraep
      121 tqydpvevrk alreyafnkn rrdeapselr ailawirrns lpmsaledtk hvdaalhald
      181 trldgtpaaa ssakryrrvl nvvlryairq nvladnplpk grdenaapkt sgavdkrsll
      241 npgqvaallv wiayrprtgh rltaffatly yaglrpeeav alrvedavlp stgwgelrvh
      301 taapevgkqw tddgevhetr dlkgrasgdt rtvpvhpala silhtlvaqd qltagdlffp
      361 gekggllags vyrrawdkar kavltereys spvgkrvydl rhtclttwln hgippaqvae
      421 wagnsvpvll styarcitgq tvelqqrieg pqklpdvpla pgpggslspp lprapgrar
//
LOCUS       WP_457687243              94 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687243
VERSION     WP_457687243.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..94
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9853
     Region          1..93
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpprsleigp agktaaraiv hvrtvrgysq rqlaarvhal grpmtatals ciertvrrcd
       61 iddfvaiata lgasphtlla gspsdrghae raet
//
LOCUS       WP_457687249             401 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687249
VERSION     WP_457687249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41607
     Region          49..276
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttrpdgtpp dtpvpgaapa saprpaatsl aelerraasr rgqpayghda liacdrlvrv
       61 fatdgvevqa lqgldllvae gelmalvgas gsgkstlmnv lagldvptag aatvagrdll
      121 tmdakarlgy rrevvgfvwq qtarnllpyl taqqnvmlpm qlrggrrraa rakaaeells
      181 mlsldhcrdr rphqlsggeq qrtaiavala ntpsvllade ptgeldshta eqvftafrta
      241 neelgttivi vthdqavase vrrtvairdg rtssevlrrt erdaatgqes lvareyamld
      301 ragrlqlpad ytsslgmahr vllelesdhi gvwpdhtadg aarggggaeg gggaegvseg
      361 adgsggsger ggaderggad erggadergg adergssdgg g
//
LOCUS       WP_457687261             334 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces nigrescens].
ACCESSION   WP_457687261
VERSION     WP_457687261.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33603
     Region          8..314
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mgltctalav dagnsktdva lvavdgsvla targggfrpp vvgagravdv laplvasvla
       61 ragapagpvg hlsaflanad lpveearlna eiagrgwart vtvrndtfal lraglpddge
      121 pvgvavvcga gincaglgrd gatarfpalg risgdwgggs cladealwca araedgrgaa
      181 telaralpah fdlttmreli ealhlhdipg hrrhelppvl favaasgdri aralvtrqae
      241 eiallagval erlgllgept pvilgggvla arhpllhdql tqlladrapk avphvvtapp
      301 vlgaaldtld ragaeagayg rvrgfggvgv gvgr
//
LOCUS       WP_457687254             568 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457687254
VERSION     WP_457687254.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..568
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=57470
     Region          470..568
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mptcpsghqs vaedwcevcg qrmagavppp pslpagflnt pppgqptgqp gppqgqpgpp
       61 pgqpgpppgg pgpgfggpgg pdsqggqggy gfpppqqpgp gapgpgtqgg qggygfpppq
      121 pgpdsqggqg gygfpppqpq qpqppqggpg psgqpetcpq cgtpreamap fcegcrynfl
      181 tnsptsyapp pgqqpgpppg apgpgtqggq ggygfpppap gplggpqqgg qggygfpppq
      241 pqqpqpqppq qqgmppggpg pggfpdqsgp ggfpdqpgpg pggfppgppp gmpgpgpqgg
      301 pppqqggddw tlnppsaqaa pppmapappg pgpqapyeqq qppapfppqq pgpyeqqppf
      361 eqqqppfeqq qppfeqqqpp feqqqqqppy eqqpgpyeqq qmpppqqqpg pdqqwnggpg
      421 qgpaappqgp ppvvgagwvv avapdreyfm ammgrsgpea aglnlpsysp eqvlplngqi
      481 avgrrrnstg espdidlgsa pedpgvshqh allvqqqdgs wavvdqnstn gttinlaedp
      541 iqpyvpvplh egdrvhvgaw ttltvrrg
//
LOCUS       WP_457687265             556 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-L-fucosidase [Streptomyces nigrescens].
ACCESSION   WP_457687265
VERSION     WP_457687265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..556
                     /product="alpha-L-fucosidase"
                     /EC_number="3.2.1.51"
                     /GO_function="GO:0004560 - alpha-L-fucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60468
     Region          70..544
                     /region_name="AfuC"
                     /note="Alpha-L-fucosidase [Carbohydrate transport and
                     metabolism]; COG3669"
                     /db_xref="CDD:442886"
ORIGIN      
        1 malrstrrtl calaltaaaa lapvqsslar spssapagpc drpvrpasqm avepcdtpar
       61 iidkaarivp tkgqlswqqr evtafthfgm ntftdrewgs gaedeklfrp sridagqwmr
      121 aykaagaeqv mltakhhdgf vlypsrytph svaaspgspd vvgayvkaar raglkvgiyl
      181 spsdgaelph awharwvaei rkkqqegipl slpervaled gdraprglgr fgngsevter
      241 tiptlvpgdd raaavrsgal hafrvraddy dayylnqvye lftrygplde lwldganpws
      301 dagitqkyhv aewfrmihrl spdtvvfagp qgarwvgnen giaretewsv tpsaddpwtv
      361 magglpndst dpdigsrakl lapttkylqw ypaeadvslr pgwfhhpger pktpaqlmdl
      421 yeksvgrnas lllnvppard griaaedvas ltafgtavre tygtdlrtag pgpwtfdrig
      481 vaedirhgqr verftvrart ggawttlahg ttighrrila lprpvtadav rvvaeesrgp
      541 grvapvtlhr sraagg
//
LOCUS       WP_457687276             562 aa            linear   BCT 27-JAN-2026
DEFINITION  CYTH and CHAD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457687276
VERSION     WP_457687276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Lorenzo-Orts,L., Hohmann,U., Zhu,J. and Hothorn,M.
  TITLE     Molecular characterization of CHAD domains as inorganic
            polyphosphate-binding modules
  JOURNAL   Life Sci Alliance 2 (3) (2019)
   PUBMED   31133615
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Tumlirsch,T. and Jendrossek,D.
  TITLE     Proteins with CHADs (Conserved Histidine alpha-Helical Domains) Are
            Attached to Polyphosphate Granules In Vivo and Constitute a Novel
            Family of Polyphosphate-Associated Proteins (Phosins)
  JOURNAL   Appl Environ Microbiol 83 (7) (2017)
   PUBMED   28130300
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Martinez,J., Truffault,V. and Hothorn,M.
  TITLE     Structural Determinants for Substrate Binding and Catalysis in
            Triphosphate Tunnel Metalloenzymes
  JOURNAL   J Biol Chem 290 (38), 23348-23360 (2015)
   PUBMED   26221030
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Bettendorff,L. and Wins,P.
  TITLE     Thiamine triphosphatase and the CYTH superfamily of proteins
  JOURNAL   FEBS J 280 (24), 6443-6455 (2013)
   PUBMED   24021036
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Kohn,G., Delvaux,D., Lakaye,B., Servais,A.C., Scholer,G.,
            Fillet,M., Elias,B., Derochette,J.M., Crommen,J., Wins,P. and
            Bettendorff,L.
  TITLE     High inorganic triphosphatase activities in bacteria and mammalian
            cells: identification of the enzymes involved
  JOURNAL   PLoS One 7 (9), e43879 (2012)
   PUBMED   22984449
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The catalytic domains of thiamine triphosphatase and CyaB-like
            adenylyl cyclase define a novel superfamily of domains that bind
            organic phosphates
  JOURNAL   BMC Genomics 3 (1), 33 (2002)
   PUBMED   12456267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18995808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..562
                     /product="CYTH and CHAD domain-containing protein"
                     /EC_number="3.6.1.25"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050355 - inorganic triphosphate
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=59923
     Region          7..188
                     /region_name="CYTH-like_Pase"
                     /note="CYTH-like (also known as triphosphate tunnel
                     metalloenzyme (TTM)-like) Phosphatases; cd07374"
                     /db_xref="CDD:143620"
     Site            order(7,9,11,44,58,60,62,73,83,117,119,138,165,167)
                     /site_type="other"
                     /note="putative active site"
                     /db_xref="CDD:143620"
     Site            order(7,9,136,165,167)
                     /site_type="other"
                     /note="putative metal binding residues [ion binding]"
                     /db_xref="CDD:143620"
     Site            order(7,9,11)
                     /site_type="active"
                     /note="signature motif [active]"
                     /db_xref="CDD:143620"
     Site            order(9,11,44,58,62,73,83,119,165)
                     /site_type="other"
                     /note="putative triphosphate binding site [ion binding]"
                     /db_xref="CDD:143620"
     Region          269..556
                     /region_name="CHAD"
                     /note="CHAD domain, binds inorganic polyphosphates
                     [Function unknown]; COG5607"
                     /db_xref="CDD:444338"
ORIGIN      
        1 madtvreier kyeadndtql pdlagigpva avaeagtedl dalyydttgl slaadgitlr
       61 rrtggrdagw hlklpvapgv rdevraplsd vpppeltalv rsraldqelv pvvrlrtrrt
      121 vrvlrdaagt plaevaedav hawpaagavg agesgagrag arwreievel lgegdtglld
      181 eigralaaag vrpasaaskl aralaetgqg rdgaaaphta gpdgrradgs gkaaakaksr
      241 akskgkgkaa akgaakgkgk aagagkkgqt agdvvlryah eqvraiiele pavrrdlpds
      301 vhqmrvatrr lrsafrsytk vldravtrpi gvelkwlaae lgverdrevl tgrlqealag
      361 vpgtlrlgpv darlriwser rragardqll avldgprhls llkslhafle epplrkaagr
      421 papevvagav lkdyrrlarr teaalaapag rerdealhga rkaakrtrya aeaarpalgr
      481 pakkfakrtk rvqqllgdhq dsvvaratlr elatqaqrag eggftfglly greealaadr
      541 eralpdlwrk vsrrkhraal rp
//
LOCUS       WP_457687297              65 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687297
VERSION     WP_457687297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..65
                     /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=7327
     Region          11..65
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mngssrsrdk itvdelcvel qvsrstfydw rqkgraprcv klpngslrir rsdlenwltd
       61 cegga
//
LOCUS       WP_457687286             269 aa            linear   BCT 27-JAN-2026
DEFINITION  arylamine N-acetyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687286
VERSION     WP_457687286.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29320
     Region          7..251
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mdtaatdayl drigagrpds pdadalralh lshlrtvpfe nlsihlgeei vlaeqpvldk
       61 ivgarrggfc yelngafaml lgalgyevel lsarvfgaeg rlgipydhla lrvqtpdgpw
      121 ladvgfgrhs hlplrwdsra eqtdpggvfr ieetetgdld vlrdgspqyr leqrprayad
      181 fevgcwwnqt sptshftqsl vcsrltengr itlsgrtlvt tavdgareer qvgadevlaa
      241 yrehfgiald repvvgevpp pavgakgrp
//
LOCUS       WP_457687293             186 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687293
VERSION     WP_457687293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..186
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20502
     Region          4..172
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mlwigtdtca lgpyradlve tywrweqdpt llvgygrqap esleariegm thqlrgenir
       61 ftvydrtsge pvpagvatll pdhavrtaey iimlapearg rglgtqatrl tldyafhitn
      121 lrmvwlkvla pntagirtye kagfrtagtl rkagywlgqt cdeaimdala eefegpsave
      181 alltgk
//
LOCUS       WP_457687300             427 aa            linear   BCT 27-JAN-2026
DEFINITION  6-phospho-beta-glucosidase [Streptomyces nigrescens].
ACCESSION   WP_457687300
VERSION     WP_457687300.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Varrot,A., Yip,V.L., Li,Y., Rajan,S.S., Yang,X., Anderson,W.F.,
            Thompson,J., Withers,S.G. and Davies,G.J.
  TITLE     NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases:
            structural insight into specificity for phospho-beta-D-glucosides
  JOURNAL   J Mol Biol 346 (2), 423-435 (2005)
   PUBMED   15670594
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..427
                     /product="6-phospho-beta-glucosidase"
                     /EC_number="3.2.1.86"
                     /GO_function="GO:0008706 - 6-phospho-beta-glucosidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45975
     Region          1..424
                     /region_name="GH4_P_beta_glucosidase"
                     /note="Glycoside Hydrolases Family 4;
                     Phospho-beta-glucosidase; cd05296"
                     /db_xref="CDD:133432"
     Site            order(9..10,12,36..37,41,81..83,106,126,142,144,269,291,
                     296)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(90,106,144,165,194,241,261,291..292,296)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(164,194)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(183,186,202,205,310,322,341..342,344,346..349)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(227,229,232..234,246,248..249,354..355,362,366,373,
                     391,394..395,405..406,408,410)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mklavvgggs tytpelidgf arlrdllple elvlvdpdte rlelvgglar rifarqghpg
       61 riswtgdlda gtdgadavll qlriggqaar nqdetwplec gcvgqettga gglakalrtv
      121 pvvldiaerv rrrnpaawiv dftnpvgivt rallthghra vglcnvaigf qrtfatllgv
      181 tpeqvelehi glnhltwers vrvagkdvlp ellaahgetl agkvrmpral ldhlgaipsy
      241 ylryyyqhda vvrelrgkps raaevaaler qlltlygdpa ldekpellsr rggafyseaa
      301 valtssllgd tgdvqivnar ndgtlpflpd davievpatv dstgaaplpv rplepryagl
      361 iahvtayeql aleaallgrd grttgwadgr navfsallah pligqldqad rltdeliahn
      421 rehlpwa
//
LOCUS       WP_457687307              80 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457687307
VERSION     WP_457687307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..80
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=7606
     Region          25..79
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mknikramav tvaasgfala gagiasahtp qaqgasvdsp givsgnnvqv pvhvpvnacg
       61 ttatvigaln ptfgapclnp
//
LOCUS       WP_457687309             381 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing sensor histidine kinase [Streptomyces
            nigrescens].
ACCESSION   WP_457687309
VERSION     WP_457687309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   4  (residues 1 to 381)
  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   5  (residues 1 to 381)
  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 381)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12128685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="GAF domain-containing 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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40141
     Region          22..166
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          154..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtngpgagip avstailams rhlevrdvlk tivasarell daeyaalgvp ddhggfaqfv
       61 vdgvsaeqwk aigplprqhg ilaamlhnat perladvred prfggwpaah pdmsdflglp
      121 vadgdeilga lflankrcpk paggcgftee derllgilaq haaialtnar lyersrelti
      181 agerarlahe lhdavaqklf slrltaqaat alvdrdpara kdelhqvaal aaeaaeelra
      241 avielrpaal dedglvatlr sqaqvldrah sarvtfaahs vralpaaqee avlrvaqeal
      301 hnalrhsgak tvevtltrng qgallriadd gcgfdpravr ragrhlglvs mhdraggvgg
      361 kltvesepgk gtavemevpg g
//
LOCUS       WP_457687311             295 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457687311
VERSION     WP_457687311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29801
     Region          1..272
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mpvaiitgas kglgralaaa lagrgwdlvv darsagplke aarelraagq gagrgaarvv
       61 alpgdvadag hraalvaaag elggldllvn nasalgaepl vrladhpldg lretlevnvv
      121 aplgliqeal plllmssylp syeefaapae rtfhdsgddn geaydshpyt enarnaglsv
      181 sppymgtgga ilnissdaav eayptwggyg aakaaldqqs avlaaeepgl rvwwvdpgdm
      241 rtdlyaaavp dddasgrplp gtvvpallrl ldgaapsgry taasaaaatg evsvr
//
LOCUS       WP_457687318             470 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687318
VERSION     WP_457687318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51753
     Region          119..417
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mtdpqtstgp qaptgpqapt gpqvstdpqv ptnpqaptdr pdtrpgphdp yliissdcha
       61 glpteeyrpy ldarfhrafd aflgerdarr aeatrlgirn dafaarwfqe heeglrggwd
      121 paqrlkeldg dgvaaevvfp dadavdsgta apfgvglgls gdhdpdlgma gaqahnrwla
      181 dfvsghperh cgvallpvta dtdrvvaeih rakesglgal mipsmwggke pyhdrrydpv
      241 waaaaecamp vlthsgaapr heygdhlgiy vsevtwwpar plwfllwsgv ferhpglrfg
      301 iaesgcwwlp nllwfmdrly lgahggkkls pfaalkrpph eyldrqvfvc atntkrrela
      361 qryeigvgni lwgsdfphpe gtwpdtrgwl kktfhdipva etrrmlglsa aeafgfdtar
      421 laplarrigp tpaelgqsad qpsveaswar srevgrhwlt dhdfpvlgaq
//
LOCUS       WP_457687323             210 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687323
VERSION     WP_457687323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22531
     Region          1..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrtaltgee vltaaarlvr aagpgaltmr rlatelgtav tsiywhvgnr eslldalver
       61 tvremgeihp tgqtphariv svaralhsal rerpqliamv hergltermf lpaqqalvhe
      121 mhaaglrget aaeavravqf qvvgfvlver nrerspeqhp segelwdspt aehdpalara
      181 lagpvdtgrl favslealvt sllspaapas
//
LOCUS       WP_457687325             209 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457687325
VERSION     WP_457687325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=22599
     Region          2..184
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mrigvylahp rpgsfnhavf davveelsgr gsqviahdly aegfapllsa eetetvgaas
       61 strdaqvmlh reevatldal vfvhpnwwgm ppavltgwvq rvlapgvayk lgtaegepig
      121 lvkagralvl ntsdtpaere esefgdplqs iwascvlpyv gvtdvrrvvf rtvtdaadet
      181 radwlrrarr eaaallarpg yrdtvptpn
//
LOCUS       WP_457687337             258 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687337
VERSION     WP_457687337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27939
     Region          1..74
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mtttavvpnd vlravrlglr msqdelatal rragaelgep neaskrlvqr weagvsrtpr
       61 gvyaralerv tgrpvealgf slpvpmarvh adgkgghdmd gggestaavv dpqhaarpdt
      121 esftgvwlsr yefysssrda tyegrhyvvi vqhgnrltaq slpgassnpd spltldltvd
      181 rnvitgswve qtaadgyyng aryhgavqml veptgrrmtg kwvgfgkefd vntgpwelrl
      241 vdrstskaal aqystppe
//
LOCUS       WP_457687339             229 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687339
VERSION     WP_457687339.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24376
     Region          27..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtssqgflgf wettgsaktf thpldpalld ayvprsarvl dygcgygrlt aelaglgyga
       61 vcgvdvsaal iargerehpe lellrcpgfp lpfedgafdt allfavltcv prdadqtaiv
      121 gelgrvvrpg gvlylsdvpl qgdalnrery arfaerygty gvfetpdggv frhhpperlr
      181 glvreagfsv lkeragsvat ldgrtaerlq liarrepaas apspgpasg
//
LOCUS       WP_457687344             414 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457687344
VERSION     WP_457687344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  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 414)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /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=42640
     Region          <200..405
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgrrwvhlvl ggallmpffl lasvvlplva dgadplrqvg wqlvafgcal ppaalaallf
       61 pllrplevaa vrslcgvpae rlaegpavsw aarrrtalwf vahlltggiv sgmtlsappa
      121 avvllllpfs dplrhtalgw pdvfqgvlgp laglallalv agtswgagal larvapvllg
      181 ptpadrlaaa erraadlasr nrlarelhda vghalsavtl qagaarrvld tdpefarral
      241 aaieettrda vaeldtvlgl lreedgsdpa mpaptldgle allgrtraag vpveatvegp
      301 caglapvvsr eayrivqegl snalrhagpv pvrlhlgvre gelqirvenp vaapaagsas
      361 paarpgggrg lrgiaerarl lggaavaeqr dgvwrltarl plagagmgtg teer
//
LOCUS       WP_457687349             334 aa            linear   BCT 27-JAN-2026
DEFINITION  COX15/CtaA family protein [Streptomyces nigrescens].
ACCESSION   WP_457687349
VERSION     WP_457687349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=35927
     Region          13..302
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mpntlnplel iarrwqpsaa fvrraamatv vmaviivvtg gavrlsqsgl gcstwpkctp
       61 dsltptaamg ingliefgnr mltyvlcavv glfiiaarar hprrrsltrl gwaqfwlvms
      121 navvggitvl tglnpyivss hflaatallt vavvswkrac egdeeprdlv arparqlawl
      181 lvaatgaltv igtvvtgtgp hagdakkvhr iplnwqeitq lhvdfvyivv glsvalwftl
      241 ravkapaapr rtllelfaci aaqgvigyvq yftglpeivi glhmlgsalv wiwvlrvcls
      301 lrdrgplqee dpaepapsge heapepqavs tlsr
//
LOCUS       WP_457687347             269 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687347
VERSION     WP_457687347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28671
     Region          6..229
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtaprtvllt gaagglgtlm rellppygyr lrlfdqrpve gapdavtael adtealreav
       61 hgvdaivhla gipleapfek ilraniegty hlyeaaraag vrrvvfassn havgftprpa
      121 dgsgaipvdt prrpdtyygl skgfgedlas lywdlhgiet vsvrigscfp eptsvrmlsi
      181 wlspadcarl ldaaltapgv ghtvvygssa ntrlwwdlst aralgytprd dsepyaaeli
      241 aaqgpldpgn pahdhlggaf ctdpprwph
//
LOCUS       WP_457687357             137 aa            linear   BCT 27-JAN-2026
DEFINITION  Rieske (2Fe-2S) protein [Streptomyces nigrescens].
ACCESSION   WP_457687357
VERSION     WP_457687357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Schneider,D. and Schmidt,C.L.
  TITLE     Multiple Rieske proteins in prokaryotes: where and why?
  JOURNAL   Biochim Biophys Acta 1710 (1), 1-12 (2005)
   PUBMED   16271700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13651
     Region          43..135
                     /region_name="Rieske"
                     /note="Rieske domain; a [2Fe-2S] cluster binding domain
                     commonly found in Rieske non-heme iron oxygenase (RO)
                     systems such as naphthalene and biphenyl dioxygenases, as
                     well as in plant/cyanobacterial chloroplast b6f and
                     mitochondrial cytochrome bc(1) complexes; cd03467"
                     /db_xref="CDD:239550"
     Site            order(82,84..85,99,101..102,104,106)
                     /site_type="other"
                     /note="iron-sulfur cluster [ion binding]"
                     /db_xref="CDD:239550"
     Site            order(82,84..85,99,102,104)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239550"
ORIGIN      
        1 msqspdrrtv lrgaalagaa gfglvacsag dsganasavp depvelgaaa evpvggakly
       61 redrlvvsqp akgtykcfsa kcthagcvlt dvekkegscp chgsrfdvtt gevlqgpase
      121 plpevpvkak ggkliag
//
LOCUS       WP_457687359             352 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687359
VERSION     WP_457687359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  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   2  (residues 1 to 352)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37619
     Region          1..329
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mttmvdvarr agvsvatvsh vlnetrpvrp gtraavlgam delgythntl arslvtsrtr
       61 siglvvsais npyfteilqg veagaleagy slliadphdd prheckvvrl lherrvdgmi
      121 vapsaepaem veylgrrkvp tvfldrlvgd ghdqvcaent gpmrqlvehl adlghtrigl
      181 vaglpglstt tervegyreg lralglpfvp allaggnsea agaqdatrql laaaepptai
      241 itannamtig alralrelgr evprdtalas fddfswaelf tprltaiaqp skdlgaaavr
      301 lllerleepd rpprtvrlpc tfvhrtscgc aepapptrpa apqaaqernr tp
//
LOCUS       WP_457687361             336 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687361
VERSION     WP_457687361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33569
     Region          1..326
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(49,274,277)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(201,244,272,275..276,279)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mivvageali dlvpspqnpl paaqdgspsa apdgplpall prrgggpynt avalgrlgsp
       61 aafcsristd afgealldgl hgggvdtslv qrgsepttla vadispdgsa gygfyadgta
      121 drlftlppvl paaaralslg tcslvlepga sayesllrre aqrgvftald pnirpglipd
      181 pdayrarfcs wlpdvallkl seedalwlag sgegpggavg ggregalsaa kewlaagpaa
      241 ivlthggdgl tvltpgggal tvpgepvtvv dtigagdtvn aallhrldah dalsrtavaa
      301 lgaedwqdil rfaaraaavt csragaeppf aaelaa
//
LOCUS       WP_457687370             703 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457687370
VERSION     WP_457687370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..703
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=72713
     Region          13..165
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cd06974"
                     /db_xref="CDD:132992"
     Site            order(27,29,68)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mtaelvrgqn hpldrtrvei rvaaggpvva gvtlgdeqgr lsgveavahp gaprrtgiev
       61 prqaaaehri avdldalsaa vhrvsvllal ptgiggltaf gaaaapsvtv tgldgtgiar
      121 ytitglgaes avvavelyrr qgtwkvravg qgyadglpam lrdqglpqaa elaaeieeav
      181 grgqaravpa paplaagrse rpgagpaapp aqdrpspapa taadgpapsg tgtgsaagpg
      241 pgpgsgagak aaagakagdl pparadggpi dyrhprrrst papaapapsa arpagtppsa
      301 agptapdgsp lpvagdaagw smderlynqv wgmfedlars vaayrsaadf aesrleqeld
      361 raladprhrl gtagedarat ardkhatlvt qaraaldrdl aqlmaesevv epalppafar
      421 wdnpvwqgyh vpaerpmalr lgdlhlpevl dlripmlvrl plerglwids gpdsyahggp
      481 gperdigrre lpgaltdgpp deselrrlam esavaiaarl laihpagdfa vqvidpagaa
      541 apalaplves galpafplpg aqgvtavlee ltrrvelvqm avrhraadal padldtaeql
      601 livhdfphgf ddraltrlry ladegpavgv hlmlvadraq sreygpvldp lwrsllritp
      661 vpdahladpw vghawtyepp lapkgsqvvr qvlgrlaaar kas
//
LOCUS       WP_457687372             295 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces nigrescens].
ACCESSION   WP_457687372
VERSION     WP_457687372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32137
     Region          34..290
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mrirpvatvv agglmglstl vlsptsaqaa aaghtpltva hrgassyape ntlaaidaad
       61 rlgiewvend vqrtkdgelv ilhdnslart tdveqvfpgr spwnvsdftl keiekldags
      121 wfgpkfrger vptledymde vehndqsllt elkspelypg ielqtltelr ragwldkghv
      181 khrlivqsfn adaiktvhml rsdiktgflg npsvadlpkf akycdqinpv htavtreyva
      241 avhglrgphg raldlytwtv ddpavavkva glgvdgiitn kpdvvrdale dhddd
//
LOCUS       WP_457687368             354 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457687368
VERSION     WP_457687368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Nocek,B., Tikhonov,A., Babnigg,G., Gu,M., Zhou,M., Makarova,K.S.,
            Vondenhoff,G., Van Aerschot,A., Kwon,K., Anderson,W.F.,
            Severinov,K. and Joachimiak,A.
  TITLE     Structural and functional characterization of microcin C resistance
            peptidase MccF from Bacillus anthracis
  JOURNAL   J Mol Biol 420 (4-5), 366-383 (2012)
   PUBMED   22516613
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Korza,H.J. and Bochtler,M.
  TITLE     Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with
            a Ser-His-Glu triad and a nucleophilic elbow
  JOURNAL   J Biol Chem 280 (49), 40802-40812 (2005)
   PUBMED   16162494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="S66 family peptidase"
                     /EC_number="3.4.-.-"
                     /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=38636
     Region          21..343
                     /region_name="Peptidase_S66_mccF_like"
                     /note="Microcin C7 self-immunity protein determines
                     resistance to exogenous microcin C7; cd07062"
                     /db_xref="CDD:132883"
     Site            order(97..98,224..225,227..228,256..257,259..260,263..264,
                     311..312)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:132883"
     Site            order(119,247,328)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:132883"
ORIGIN      
        1 mpisspsasv lrhppkprpg drvavlspss glpqrfpvpy elglarleke fglipveypt
       61 trkwgagaqe raadlhaafa dpditavfas iggddqltvl phldrevfrd hpkpffgysd
      121 ntnllaylwn tgivgfhgat vmcelgrpga mhpltadalr aalftpgpye lrpaerygde
      181 ngdwddpdpf aaepalwpgg gwwwhgperv vegpswggsi evlswmlmad reiqeaaayd
      241 gcvlfletse elpgadevyl vlrsmgergl lrrfpallmg rpkawslsrp lsgeakasyv
      301 reqraavlra laayapdtva vfdvdlghtd pqlvipyggt irvdgvarri tvty
//
LOCUS       WP_457687374             197 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457687374
VERSION     WP_457687374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20514
     Region          27..195
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtyaeqdsgp atppaaapdt aarrdwawrr latpigplll aatreglvrv vfhadertar
       61 reltrleqlf ggppltgiph lttattelta yfagelraft vpldwslssg fnarvlhala
      121 dgvpygsvvg yqdladrvge pgaaravgaa mgsnplpvvv pchrvvasdg giggfgggle
      181 tkrlllaleg vlpaplf
//
LOCUS       WP_457687377             314 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687377
VERSION     WP_457687377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  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 314)
  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..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /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=32566
     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 mraivmrefg gpdvlrledv pepaprgghs lvdvglagin yadvhvrgds ylapvelpyv
       61 pgnevvgtvd ggrrvvglcr gggyaertll hrrvtwdvpd aisdeqaval alqgnsawhl
      121 lftslrlteg etvvvpaaag gvgslavqla aragakvial agspekrdla gelgahavvd
      181 staedlteri leaaggpvaa alemtggvtf ertlaavapr grlavygfag gelasvptre
      241 lmersitvsg fwlpqlyadr talptsmral fdaviegtlk pqtgavyglg eaarahhdla
      301 artgtgklal dvtr
//
LOCUS       WP_457687379             547 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457687379
VERSION     WP_457687379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..547
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=56349
     Region          20..>195
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mnasstssnn glefthpyla vvlgggftgi laaaalsgha dvivverdrl prtparptdl
       61 pqarhahllt adgarlidtl lpgsaarwla egarrmplpa efagrapkvr pgrrassryl
      121 lacsrdlldr virrqasalp gvtvldgtea teltgtaehi tgvrvrdtts gathlldadl
      181 vvdatgrhst arewltalgl psahedvvds givsatrifr apegtencpv ltarsglggp
      241 ppspgaphrp vpgrtatlvp ieggrwlvtl tgtgddrpce hagrfvpfah rtghsvigdl
      301 iaaaeplsev rltrdtsdlr rryeqlsswp tgfialggav vslahdcgqg lalaahgaaa
      361 lrgalrrhgm depslarkvq rtigrlvqep wsvatgellp sptagravrg syvdvlapaa
      421 ptapflrpaa algllwekar irptaggaag rqtspgpvpa pltaapgspa aagphppaaa
      481 gaasarsarp taalsaappa papgqppapp hhsgsaptpr rlprplsfgp talrrisgat
      541 rrkpadg
//
LOCUS       WP_457687383             272 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687383
VERSION     WP_457687383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29861
     Region          56..175
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mnqdhepeat rrdasdtess rasrgwwdrn adeyqsehga flgddrfiwg pegldeaeaa
       61 llgpaaelkg rrileigaga aqcsrwlaaq galpvaldls hrqlqhalri adgaddatel
      121 veadagalpf rdhsfdlacs aygalpfvad pvrvlrevrr vlrpggrfvf svshplrwaf
      181 pdepgpegls vsasyfdrtp yveqdesgra vyvehhrtlg drvrdvvaag frledlvepe
      241 wpgwntqewg gwsplrghli pgtaifvcta ea
//
LOCUS       WP_457687387             604 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687387
VERSION     WP_457687387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Scheurwater,E., Reid,C.W. and Clarke,A.J.
  TITLE     Lytic transglycosylases: bacterial space-making autolysins
  JOURNAL   Int J Biochem Cell Biol 40 (4), 586-591 (2008)
   PUBMED   17468031
REFERENCE   2  (residues 1 to 604)
  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 604)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   4  (residues 1 to 604)
  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   5  (residues 1 to 604)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Dijkstra,B.W. and Thunnissen,A.M.
  TITLE     'Holy' proteins. II: The soluble lytic transglycosylase
  JOURNAL   Curr Opin Struct Biol 4 (6), 810-813 (1994)
   PUBMED   7712284
REFERENCE   8  (residues 1 to 604)
  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
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     A conserved domain in putative bacterial and bacteriophage
            transglycosylases
  JOURNAL   Trends Biochem Sci 19 (3), 106-107 (1994)
   PUBMED   8203016
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14419880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008933 - peptidoglycan lytic
                     transglycosylase activity [Evidence IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=61824
     Region          117..258
                     /region_name="Slt35-like"
                     /note="Slt35-like lytic transglycosylase; cd13399"
                     /db_xref="CDD:381602"
     Site            order(127..129,131,148,176,183..185,188,224,244..247,251)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381602"
     Region          390..>437
                     /region_name="Big_1"
                     /note="Bacterial Ig-like domain (group 1); pfam02369"
                     /db_xref="CDD:460541"
ORIGIN      
        1 maatfrrrlq rgaastavaa lvlaaltasq apgatgdaaa krqpapppad vpidggsgyy
       61 tdlpplnspv pprgsdhngq gpatgrgpae aglpatvlaa ykkaastlgt ddpgcrlpwq
      121 llagigkves gqarggavda egttlrpilg pqlngrgfar itdtdngryd gdlthdravg
      181 pmqfipstws tggpdgagwg adgngdgkkd phnvfdaala aggylcaggr dltaqddldr
      241 ailgynhsee ylrtvlswya fyrngthevp dgkgvlpvhr dagrhddngg rsedrrhrgh
      301 ggqpgksprp ggsgkpgkgh kpgkgqqhdp gkpgrpdgtg ptpggtepps qkptptpepp
      361 tgpahptalv rvgdkdlstt agaefatppq vraqdaegka vagtpvrftl paatdarfpg
      421 datavtvktd knglataptl ragdrtgafr irvttvahta pavelgatvk arpapkadkl
      481 artsdkelta tagkafaeda veikatyqdk iaagvavtat mvtddpkqpv endkgpyfkd
      541 peatgaakhk pvrtltgltt dadgllklpk iytdahpgtf llrlttadga vltvklkvaa
      601 aags
//
LOCUS       WP_457687394             605 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            nigrescens].
ACCESSION   WP_457687394
VERSION     WP_457687394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  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 605)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65399
     Region          50..581
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msldrrkflg ssvvtgagva laggapaaea vevreqggrg hghrreryaf tvmgttdlhg
       61 nvfnwdyatd aefddaahnd vglakistlv tqvrrekgrh ntllidagdt iqgtqlayyy
      121 akvdpitdpd gpvhpmaram navgydaaal gnhefnygip vlrkfeescd fpllganavd
      181 arslrpafrp yvlkrlrspr grvvtvavlg ltnpgiaiwd kahvqgklaf pglveqaakw
      241 vpklrsmgad vvfvaahsgm sgtssygdql pyvenaavlv aeqvpgidav lvghahvevp
      301 errvrneqsg revvlseplk wgqrltlfdv vvewrrghwe vgsvgsrvln snavaedari
      361 tgllraehrk vvayvnrvig rskaemtaae apvkdtpild fiawvqaevv rkalagsasa
      421 slpvlsqasc fsrtarvpeg dvtirsmaal ypfdntlear vltgaqlray lefsaryyvr
      481 tpagggpvdp skvtnadgip dynydmvygv syevdiakpa gqrigklmfd gkplddaarf
      541 vlavnnyras gggnfphvaa aeqvwstsde irnvmigwvq etgeidpaaf aaadwrltrd
      601 gvpvf
//
LOCUS       WP_457687415             242 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiX family flavin prenyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687415
VERSION     WP_457687415.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /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=25395
     Region          16..227
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mepphndtsk qgpgrrrpwv vgisgasgtp yaasvlrgll aageavdliv srasrltlld
       61 etgiafrdah wradlrewla rgadgkpatf pvteadladv rywpagdlaa gpssgsypvk
      121 gmlivpasta cvagaalgls kdllqrvasv tlkerrrlvv avretplngp tlkhlvtlde
      181 agavvlpasp afyagathiq dlvdfvagra ldaaevphgl yrrwegelrg gskdaeeape
      241 ap
//
LOCUS       WP_457687417             451 aa            linear   BCT 27-JAN-2026
DEFINITION  dicarboxylate/amino acid:cation symporter [Streptomyces
            nigrescens].
ACCESSION   WP_457687417
VERSION     WP_457687417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..451
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47236
     Region          24..428
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mstsaettes sqapqsprss ripkipfwaq ilaglalgvl lgwiaksgdv gwltttlqhi
       61 gdlfvqllkl avaplvffai lvsitnlrqv nnaarlasrt llwfmvtsli avaiglaigl
      121 lsnpgagtgl tpkdgkapde agswidfltg ivptdiitpf telnvlqivf maavagiaal
      181 qlgekaepvl kisrsvlell qkalwwvirl apigtvglig naiatygwnl igkyatftvd
      241 iyvgcalvlf gvyplllstv akvnplqffr gawpaiqlaf vsrssvgtmp vtqqvterlg
      301 vpreyasfav pfgsttkmdg casiypaiaa ifiaqifdvh lgigdyllia fvsvigsaat
      361 agltgatvml tltlstlglp legvgllmai dpildmmrta tnvagqavct llvaaregil
      421 drdayngaks inleaasade aeekvavaaa a
//
LOCUS       WP_457687396             477 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457687396
VERSION     WP_457687396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 477)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49066
     Region          19..472
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mpvppagtal aggtngpral rplldtvlda lttgaedrag plppggpetv artvrdachp
       61 llpdhgsgph aalrtlvhtl aagaadpadp hcaahlhcpp lalataadla aaalnpsmds
      121 wdqapaasal ealtsralaa lvypqatdpd alvttggtes nqlalllare aaatdgtatd
      181 phrparplri vcganahhsi hrsawllglp epltlptpdg lltpdtvhsc lanlagrtgp
      241 vllvatagtt dsgaidplpa ladlaerhga rfhvdaaygg allfsdthra aldglaraht
      301 valdlhklgw qpvaagllav pgpatltpla hqadylnadd dteaglpdll srslrttrrp
      361 dilkiavtlk algrhglgel vdrtlaaaqt ladlieahpr yvlhsrpsls tvlfrptgad
      421 httlaairrt lltdgqavlg rattptglwl katllnphtq pgdlttllkl veghtpr
//
LOCUS       WP_457687425             477 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687425
VERSION     WP_457687425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=54022
     Region          7..403
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mgklkpkrvg iyvriskdrk gqelgiqrqe kacrelcerm gwtvhkvype ndtsasttsr
       61 kkrpqyaemm rdardsmida ivvysidrlt rriteltafl eeqkehsfaf attegedtst
      121 angrmiltik gavaqqeter maervntsll qrrekgkpha ggprvfgfee gsnfqrlvpe
      181 evelirlgye mlmnrqtpgd ivrlwnakgs rtsgaqtaws iqkvkriyrs ervggivtyk
      241 gqdigdsvyp hpltreewen vqtildgrsg trkpgtakrk hlysgflkcg acgstmriqw
      301 atiqgrrfrr tfchsgavgr ngelgcgkvn rsyawiedrl nevveaalnh rapkptavpt
      361 edhsgeinvl eerirglrkr wkagemeded yfdslahlrg qlqdlrarea asavrearte
      421 tdalavwrdd sehnlerrra lvatvikeva iysvgrgrrk ppeidsikit pvgaesp
//
LOCUS       WP_457687428             656 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457687428
VERSION     WP_457687428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..656
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70341
     Region          56..656
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mshqesaptg pltaptltsa ptptsaptht saptltepqk tvvngtvrev yvpplappvr
       61 sgslgdlpfl nadeapadvv larkqpsgiw rdvtaaefaa evravakgli ahglrpgdrl
      121 aimarttyew tlvdfaawaa glvtvpiypt ssahqaqwil hnsgtracvv egvdetrlis
      181 glrtelpald ylwqfntgav sqlvsagrdv pdeavderra aagpyalatl iytsgttgrp
      241 kgcalthanf faeadnavel lhpvfksvse epaatllflp lshvfgrmva vgclrarvrl
      301 ghapslrtdd lladlagfrp tfllaipyvl ekvfntgrat aermgraasf dravriarsy
      361 geaveakehg tgpgpgvalk garklydplv yrriraalgg kvrhvlcggs plgrrlaafy
      421 tgagieifeg ygltettaat tvtpplrpri gtvgwplpgt avriaddgei lihgdhvfsg
      481 ywdaalgaar pvtdqgwfat gdlgaldpdg yltitgrkke iivttggknv apapledrlr
      541 shplvgqcmv igdnrpyita lltlepdgla hwrqmnkkqd lpperlvrda rlladlqrav
      601 ddanelvsra esirrfavlp vdfteetghl tpslklrraa vardfakeia dlyesr
//
LOCUS       WP_457687439             288 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457687439
VERSION     WP_457687439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10142960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="SDR family oxidoreductase"
                     /EC_number="1.6.5.2"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=29804
     Region          5..274
                     /region_name="TMR_SDR_a"
                     /note="triphenylmethane reductase (TMR)-like proteins,
                     NMRa-like, atypical (a) SDRs; cd05269"
                     /db_xref="CDD:187578"
     Site            order(7,9..12,34..35,38,52..55,73..76,139..141,172)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187578"
ORIGIN      
        1 msfvvtgatg algrlvievl lrrtapdeiv alardraraa dlaargveik hadysrpetl
       61 qgafaagdrv lfisgneagq rltqhrtvid aareagvgll aytsvlggpt atfsiaeehl
      121 ateqallasg vpycllrngw yhenytgala ttlktgavvg sagegrvata arrdyaeaaa
      181 vvltggghen tvcelsgdta wtmaeyaaev srqtgrriay rdlppeqyva llveagvpal
      241 gaqlvadada giargelsat pgelsrligr pttpvaeaia ealkgleg
//
LOCUS       WP_457687449             518 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Streptomyces nigrescens].
ACCESSION   WP_457687449
VERSION     WP_457687449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=53319
     Region          10..517
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mssitplvqs vdwvalappt vtaavalvvl vadlflpaar kpllgwiata glavsallll
       61 pllggdrrtf clpehpdvcs yvadpftlvi qflvlggall tallsidtik dqelpageyw
      121 flllssaaga allpasrdla tlvialevas lpafalvglr rgdrlsseaa lkfflssvaa
      181 tavmllgvsf lyaatgslhl sqvahgltal pdprlatlas agvaltlvgf afktaaapfh
      241 fwvpdtyvga plpiagylsv vgkavgfsgl ilvtvqgfps yadvwgpala vlaaltmtvg
      301 nvaalrqdpg rahsavrlla wssvgqagyl lvpiaaagys qdpahaigst vayalmyaav
      361 nlgafavaal varthpanri tdyrglyhqr pvvalalgff llclaglppg iiglfakvtv
      421 fsvavdagla wlavimavnv vialyyylqw ttvlfrgaet aeapetaear eaapaelqpp
      481 rtgipaplat aialatvlgi alsgapqlvl rfasgall
//
LOCUS       WP_457687463             269 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457687463
VERSION     WP_457687463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27570
     Region          20..265
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtntpsdtps daprhpglpd lrgqvalvtg aagvlgrgia lrfaaagaav vahyrtgada
       61 arelvaqiea dggsalalra dlaveeechr lvteaagwrg rltalvnnag vqptqelaam
      121 sladwravad pnvhsvfact qaaaavmraa gggsvthias ieadrpaprh ahycaskaav
      181 vmharaaale ygpdgirvns vspglidrpg laedwpegvr rwqaavpagr lgtpedvgda
      241 cvflaspmas witghelvvd ggvsarptw
//
LOCUS       WP_457687466             539 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 4 family protein [Streptomyces nigrescens].
ACCESSION   WP_457687466
VERSION     WP_457687466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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 539)
  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 539)
  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..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /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=55427
     Region          57..537
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mqlllaavvv lplvgalaal lpappglrgk npdqavlrhg vtvtgavlaa avalaagfdh
       61 dhparmqatt diswipaldi rihlgidgis lplvvltall tflcalysyf hmptgpspka
      121 fvallltlea gtlatfavld lmlfflafem vlipmyflia rwggagkqaa awkfilytll
      181 gsvvmllgll ligvksgtfd mvalatdngp ktqlshtvql lavlavgigl avksplwplh
      241 swlpdahtaa ptvgsvllag vllkmgtygf vrialpitpe gmqtfapyla alaavgiiyg
      301 slaclalvrk gakgdlkrli ayssvghmgf vllgiasmtp tgvngalfan iahglitgll
      361 fflvgalkdr ygttdldala gstgaalygr aphfggllaf gavaslgipg lagfwgemla
      421 mfgafrpaag lsrpafltfm vmaglgtllt aaylllvvrr vcmggtphla ptaplgtadp
      481 adgdpsgeta aapavpdiar yeyaawtpla vltvlaglwp aallgltdpa vqqllgggk
//
LOCUS       WP_457687496             194 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687496
VERSION     WP_457687496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20816
     Region          2..189
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkltyfigt tidgyiaapg gdfdfftphi tedyrpfltt efadalptpg raalgiadtp
       61 ntrfdtvvmg rgtydpglam gltspyaqlr qivfsgslat gpdpavevtd edpltlvrkl
      121 kqedglgiwl cggadlagql lpeidelivk qypivagtgi plfradfspy tfrladsrvf
      181 eggnvvltya kasd
//
LOCUS       WP_457687481             605 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457687481
VERSION     WP_457687481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10147745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=64552
     Region          31..510
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(161,164..169,171..172)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(164..165,281..282,305..310,328,394,406,409,508)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          531..602
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mteiledprh tapdhtvdll trfqqavaaa pdriavshhg altfaeldrh tarlagvlag
       61 hgaapgrrig islprgtdlv vallavwrtg aayvpldpay pqerlhamvr dagidvvltg
      121 gsdgpvwpeg vrtlpvappp eapehtpapp vpvsaqtpay viytsgstgv pkgvestrga
      181 vaalvaglee aglydqrhrv vawnasvsfd asvqqwarvc rgdtvvvlge aertdpallr
      241 avldengvhd ldltpshwpl lrdgllvrst egrplrlfmg gepvpegtwr elaaahdarr
      301 leavnlygpt ectvdvtaaw iedsaphigr plprvrchvl dtalrpvpfg eegelylagr
      361 qlavgyvnrp altatrfvad pfaadgtrmy rtgdlvrrrp dnsleyrgrs drqvklrgyr
      421 velgdieaal tthpgvaaav vtlhsgtaag eqlaayyvaa tgavgdtpat gtptpgtlra
      481 hlaavlpqfm lpttylalda ipltvngkvd laalpapepa saapesapeg eaetliaavw
      541 sevlgrehir adddffamgg hslialrvva rlkkqlgvam sarevyrhpr lrdlarhves
      601 lrtgr
//
LOCUS       WP_457687522             370 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457687522
VERSION     WP_457687522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 370)
  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 370)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..370
                     /product="MDR family NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38262
     Region          42..367
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(85,167,191..193,213..214,218,234,257..258,279..283,
                     285,311..313,356..357,359,361)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(86,285,314)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(89,93,273,278..281,284,301..302,305..312,315)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 marrtpgada agrpgpegrp gssgfgaagg gtgsvalpav hrevrlaahp grelrpehfe
       61 tvevplrrps agqvlvrnlv lrigaatrtl madaevlpmp scrpgralrg aalgevveap
      121 gtglrpgelv rhdfgwqqya llpagavrrv dsarwpdpaa clsqgfvgwl avtrggsvrs
      181 gdtvlvtgaa ggvgcvagqf arlhgagrli gtvgsrwkad ylerelgfda vlvrgegsig
      241 eqlraaapdg idvlvdtvgg eqfeaalaaa rrrarfmvvg algdqaaggt raeatvdnlw
      301 lvsrgitlsg lsavdhhasv dcweaefsga lrngtvrfph vrltgldrap galinlmagr
      361 hlgtvlvept
//
LOCUS       WP_457687525             346 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457687525
VERSION     WP_457687525.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35019
     Region          11..276
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mqqrsvdqgf savagkvpap clvlagvsgi qfgaalapsa ypqagaagvv flrlliagli
       61 lcvlwrprrq alkstkgawk tvlaagtlla ghhiaffeav nhiplgivat ieflgpfaia
      121 lagsrraldl lpaclaaggv lllsggdsts lpvvglvlav vaaccwagyi lvsarmatrl
      181 sggqglavai twaallsapy givhagsgll aphvlwvaav vavvssvlpy slnlealrri
      241 pprvfgvlts lepaagalfg llvlgqrldr cqwlgiaava casiaatylg pgkrriscvr
      301 atsgsltshr sadggcgrar apqpgaisrl aagprrtpge pdnhgg
//
LOCUS       WP_457687556             395 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687556
VERSION     WP_457687556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  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 395)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42059
     Region          1..389
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(1,28,116,384..385,388)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
     Site            order(12..13,15,146,149..150,154,181,233,302,304,306..307,
                     310)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(12,233,302,304,306..307)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            13
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mrilitaqai yshlaplvlp vaerakeagh evavatgagv vqhiekrglt altlpnvqsm
       61 gealqggrlq pppgmekags vtvelspkff asafvghlae agaqdlldva rswqpdlilh
      121 esteyggyla aeclgiphga ldiapmapya hpvvteelnr qrgklglapv sdawhtfraf
      181 ragvvpedfy ptdsrlpsar yyqvpaqsaq galdpdiaql stdrplvlat lgsnatrlpg
      241 gaqalletiv etlgelpvtg vvalgadrdp rqwdgarpdn vhltsfvqqe lllrssdlfi
      301 thagfngtre alaagvpmva vplfaeqshn agrlqqlgvg tridvqdvtr nslaeaarnv
      361 ledrsyrsra qglqrrshal pdlnrlveda aalva
//
LOCUS       WP_457687545             555 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687545
VERSION     WP_457687545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 555)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 555)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 555)
  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 555)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58520
     Region          15..538
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 msaaallgll wlgsqalvpv vvreaidqgl vpgemdavlv wsaallglgv vqaasgtirr
       61 rlsmhnalda gfrtvqlvvg hagrlgagle rrvddgelvs igtsdmttig nafdvvgraf
      121 gavvstllva vvlldqspsl glllivalpa iiltmgytlr plhrrqgayr dlqgeltsrl
      181 tdvvtglrvl rgvggetsfa rsyrersqrv rvagskvaga ealiratqvl lpgllvatvt
      241 wigaraalng svtpgelvaf yayaaflvep laiftdtadr farahvaarr aiavlslpaa
      301 spdtecgrtp lpadghdlvd qrtglvvtpg sflavvappa egvqladrlg gytdgpvrya
      361 glpltelrte qlrehilvvd nhsrlfrgpl rdsldphraa cdddvhaalr vaaaedivea
      421 lpngldteit adgarfsggq rqrlvlarav ladpgilvvv dptsavdaht edrvgrrlra
      481 arqgrttvlv ssspllldha eqvaflhggr vaatgshrdl latsahyrll iqretgedrt
      541 gdtpttsfvt rgpaq
//
LOCUS       WP_457687558             424 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457687558
VERSION     WP_457687558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43584
     Region          32..405
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(42..43,46..47,50,82,131..132,134..136,139,159,
                     162..163,166,241,244..245,248..250,253,281,285,335..336,
                     340,344,359,362..363,366..367,370)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mpgkseavtr rtearsgesg egsmfvlsrg vvmlfavacg aavanvyfsq pllvtmghdl
       61 gmspavvgsv vtlthvgygl glfclvplgd vadrrrliva qllflvvala vvaaahtaai
      121 llvgmaatgl lavvtqtlva faaslappag rgrvvglvts gvvigillar tasglmadla
      181 gwrsvylasa sltallalvl yrvlprhsda ppttlrygql lrstitlfar eqllrlralf
      241 gllvfaafsa lwssvalpls eapyflphsa igalgligva galaataagr lndrglsrrt
      301 tgialtllav swlplaftrs slwalvvgvi lldlavqavh vtnqtliyal hpdagsrlig
      361 gymvfysigs atgaiaatsl ytvagwgavc algatfsclg lvlwaftrhg tpdpaaevts
      421 rsgt
//
LOCUS       WP_457687578             150 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687578
VERSION     WP_457687578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16569
     Region          3..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtrtrfdds ecpvarsvda igdwwslliv rdafdgsrrf gefqrslgva kniltarlrt
       61 lvaggvlesv pasdgsayre yvltskgkal fpvivalrqw geqsffapge phsqlvdrrq
      121 grrlralevl sadgrrlnpd dttvhkvsar
//
LOCUS       WP_457687585             320 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotriesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687585
VERSION     WP_457687585.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chen-Goodspeed,M., Sogorb,M.A., Wu,F., Hong,S.B. and Raushel,F.M.
  TITLE     Structural determinants of the substrate and stereochemical
            specificity of phosphotriesterase
  JOURNAL   Biochemistry 40 (5), 1325-1331 (2001)
   PUBMED   11170459
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Shim,H. and Raushel,F.M.
  TITLE     Self-assembly of the binuclear metal center of phosphotriesterase
  JOURNAL   Biochemistry 39 (25), 7357-7364 (2000)
   PUBMED   10858282
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Kim,G.J. and Kim,H.S.
  TITLE     Identification of the structural similarity in the functionally
            related amidohydrolases acting on the cyclic amide ring
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 295-302 (1998)
   PUBMED   9537960
REFERENCE   4  (residues 1 to 320)
  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
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Tuovinen,K., Kaliste-Korhonen,E., Raushel,F.M. and Hanninen,O.
  TITLE     Phosphotriesterase--a promising candidate for use in detoxification
            of organophosphates
  JOURNAL   Fundam Appl Toxicol 23 (4), 578-584 (1994)
   PUBMED   7867909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004443
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="phosphotriesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32916
     Region          15..310
                     /region_name="Php"
                     /note="Predicted metal-dependent hydrolase,
                     phosphotriesterase family [General function prediction
                     only]; COG1735"
                     /db_xref="CDD:441341"
ORIGIN      
        1 mvnrapaggp aapavrtvlg diapaalgic dahdhlflrs pqlpgqeldd veaaaaelsa
       61 fraaggaavi qwtpygmgrr saelprlare sgvrivaatg lhqaahyspe llarvrpdla
      121 glfvaelteg iggtgpragm ikvaggfhgl drharhtmaa aaeaqratga aigvhlelgt
      181 galdvldllc gtlavppdrv ilghlnrspd lvvhrtaaea gaylafdgps rahhatdwrl
      241 pealaalaea gfgdrillgg dtttagarsv nggpgmpyll rrhrerleva lgadlvaqfl
      301 tanparafaa dwarapggsr
//
LOCUS       WP_457687582             444 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457687582
VERSION     WP_457687582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 444)
  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 444)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /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=46988
     Region          <7..442
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <212..409
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 menarppwar rcvgpvwerw laappgeprg rtgtrlpwls tlvvtlvvlv gsgfaghdqp
       61 grvpldslgr allvlggall lfrhrfprtv aigtatagaa ylaagypygp vflilalgaf
      121 aavvaghrkv awwalggvwv shvvvahwly rwlppphdgp apwgqellvi awvvavvals
      181 elvrvrreql akaqaeraaa errradeerl riarelhdvl ahsisvinvq agvglallds
      241 dpeqarsalt tikdaskeal gevrqvldtl rtpgdaprsp apgldrlpel teqarsagla
      301 vdlttegtpa tlppgtdlaa frivqealtn ivrhsgsrta rvllrhtpga leirvdddgp
      361 atagtgergg gngligmrer aavlggtvea gprpdggfrv raripltgtr amdrdpgadt
      421 vtpspspsps ptptppptat eeep
//
LOCUS       WP_457687587             210 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687587
VERSION     WP_457687587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22518
     Region          23..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstqeppgtq erlvrstqep pgtqerlvrs tqellwergy vgtspkaile ragvgqgsmy
       61 hhfsgksala laairrtaee lkhaseecla apgtaydrva ayllrerqvl rgcpvgrmtq
      121 drdvvqsael rrpldemfdw lreritevlt egqrrgelaa aldpaataat vaavvqggyv
      181 laraaddtap fdaavqgvla llaaqvpaag
//
LOCUS       WP_457687595             472 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457687595
VERSION     WP_457687595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=48057
     Region          11..472
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msmlkgsnvp vpapavrvel gwqaapgtpd vdasalllvs gkvrddadfv fynqpahasg
       61 avrhegkrpa ggamtdclav dlaavepavd kvvlaasadg gsfgsvpglh irvldaagga
      121 elarfdsqda gaetafvlge lyrrqgawkf ravgqgydtg laglatdfgi sveepappqp
      181 papapapaap appppamapa ppmappppap aapmapppaa papplptgqp aasvppppgq
      241 papapappav rltkvtltkd apavsltkqg gtsgamrvnl nwsagsagkr lgkklgrkam
      301 eamgargall pqsgeldldl calyqltdgs agvihplgnn fgalhappyi qldgddrtga
      361 vaagenmtin ldhqdrikrv lifvtvyaga rsfeglsatv tlqpqhgapv dftldactvp
      421 snvcalamit ntgselvvqr earylvpdpg vspqrtvdqa ygwgldwspa rk
//
LOCUS       WP_457687600             473 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457687600
VERSION     WP_457687600.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49095
     Region          15..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,75,133..134,136..138,141,161,
                     164..165,168,259,262..263,266..268,271,299,303,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 maapatsppa sanlrrivaa sligttvewy dfflygsaaa lvfnklffpg sdplvgtlls
       61 fltyavgfaa rplgalvfgh ygdrlgrkkl lvlslllmgg atfaigllpt hatvgtaapv
      121 lltalrlvqg falggewgga vllvsehgda rrrgfwaswp qtgapagqll atgvlsvmta
      181 llsdaaftsw gwrvpfllsg vlvivglwvr lsvdespvfr aalaraearr aegaalermp
      241 lvavlrhhwr dvliamgarm aenisyyvit afvlvyatsh tglsqqtaln avliasalhf
      301 avipawgals drigrrpvyl lgaagvgvwa fpffalvdsh hfgplllavs vglvfhgamy
      361 apqaaffaem fatrmrysga sigaqfssva agapapliat alladydspt pialyviaaa
      421 lltqlavgva retrsrdlta vdgnavegda vagegrtagp dggassavps gga
//
LOCUS       WP_457687603             422 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457687603
VERSION     WP_457687603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45227
     Region          60..327
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          344..419
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mpqrpkivlv gqlssfpwvf esaeragidl vlvprgddsv esagraksvv evlpldidgd
       61 pesalstlve rfrrdpfdgi mpgnekvvpf varaarmlgl pglpeevaav vrdkrsmrrl
      121 lreaglgapg fvsldgpdrw adaltlrfpv vvkpangyss lgvvrvddkd qlvpavartw
      181 elcetelrqa ggpadgvgvl veeyldgpei aaeslvhqgr vrvcaiewkg emtgpyfeet
      241 tvrapaqlpa dvlaaieaev igahhafgvt egathtelrl iggvrpvlle maariggagv
      301 nhylthiagg idlaaealri hlgqepvcws qepvptghaa aysvpvgkgg rivrvhglda
      361 vrsdprvdqv vqtvgpgall rpypdwagyp aivlshhesd aaavefrdhl vrtlhveyee
      421 es
//
LOCUS       WP_457687613             524 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxylesterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687613
VERSION     WP_457687613.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..524
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=54313
     Region          2..476
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mphrvrvkts agtvlgrqda gvsvfwnipy aaapvgtgrf aapvapapws gvrdagepgp
       61 tapaalragf gpldmsallg pgwvtgedyp gvnvwtpsph rdrlpvmvyv hgggflngsg
      121 raelydgtgf ardgvvlvtl nyrlgvtgwl dvpgapanrg lldviaalgw vrdnisgfgg
      181 dpdqvtvfgq sagamivaal laapqaeglf rraisqsgsg lcafaprqae rvtravavrl
      241 giapsagafa gipddrlvsa vaglgpvdva gdghydtslg sspfkpvldg avlsqqpvda
      301 vaggsgsavd lligtnadea nlyvvpagra ariteaevsa aaarrhpdpv alvaahraqr
      361 pdaspgella hlvtdafteg srqladahaa rsaagthayl frwrpaafgg slgachcvel
      421 pfvfdrtelp glrgprallg dgdlppdlas rmhrawisfa atgdpgwqly raegraegra
      481 edraedraed raeertedra edravqiidv rwtmsqvrga ssga
//
LOCUS       WP_457687615             403 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687615
VERSION     WP_457687615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43688
     Region          88..403
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslsslsrra vvgaalsgav vaatagpara asrpapapss ggparrippa papvpplnvp
       61 alraalsdle hpqltaaqlr vtgsaghwyg nagvadratg rgvherdtfr igsitkvfva
      121 tvvlqlaaeh rlspelpvqr llpgllpskf ppitvlqlln htsglpdeqd ppydptspee
      181 iarhrydrwt peqlvarvth grmkftpgtk qeyrsinyil lallierltg rrygeviarr
      241 ilrplglrht svpgndprih gphvhgymrm tdgslldite fdqsaawggg emishtgdld
      301 rfltalfsge llpphelerm ftlppdevrm vdggparyaa glqtvtmngi tlwgktgery
      361 gyssamvatr dqqrravfsf nptrrdatqi qasqriaeal tka
//
LOCUS       WP_457687620             465 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457687620
VERSION     WP_457687620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..465
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49300
     Region          38..460
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mrprgaavaa diegtlirrg dpgyedarmg avwnevtprr fpdvlvraat eadvvhaltw
       61 araqglrvsl rsgghnwsga plrdggllld lsglrqcait pahgseppta tvgpaatgqd
      121 lvaaltpqdl afpvghcptv avggfllsgg lgwnsrawga scadvreira vtadgrtvic
      181 sdteypelfw aargagpgfc aavtgfrlal hphpasimat gltfpldevs rvtewaepla
      241 rrlppyveta fvlassgppt esaprgprit vaatafaate rearqalepf adcpfgacav
      301 trqppapvsf aalhegaaai wppahryaad nlwspeshat qltriadava hapsgkslvl
      361 spvqpvsqep allrnmafap lgesylvcya iwddpagdqd narwlrdama aadprgdgcr
      421 yiaetdleag pararrsyap atwdrlqeik aqwdpenlfh sylap
//
LOCUS       WP_457687625             327 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457687625
VERSION     WP_457687625.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          22..299
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpirttetap aaevravprg gspaararrt ertknwarra pllpalvfli ivtqlpfvat
       61 vvisftrwna lapenrgfaa ldnyravftd pamrasvgtt vlltvtvvlv slllglglal
      121 lldrgfrgrg ivrtllitpf lvvpvasall wkhalynasy gllngsltwi wrlfgsddpp
      181 qpdwmtdspl aavevsliwq wtpfmmlill aglqsratda ieaarmdgas afdifrhltl
      241 phlrrylela allgtvyvvq nfdavftits gglgtanlpy tiyqtfyqah dygrasaqgv
      301 vvvlcsllva tfalrtvssl lreevtr
//
LOCUS       WP_457687627             471 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687627
VERSION     WP_457687627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50992
     Region          58..454
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(170,172,298,300,333..335,376)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mhvllvprkv ravrarppgp grggrplglt alavalalst tgcyrgagda gneshhsinv
       61 lmvnnpqmvd lqrltaehft ketgikvnft vlpeddlrdk msqdfssqag qydvasvsny
      121 etpiyarngw ltelgtraak drgfdqgdil ppvrssltaa dgkiyaqpfy gessflmyrk
      181 dllkeagltm parptwhqva alaakldgfr kgmkgiclrg qpgwgqlaap lstvvntfgg
      241 twftkdwqpk vdspeftrat rfyvdlvrkh geagapqagy teclndmqqg kvamwydata
      301 gagslesaes kvagkvgyap apvertrdag wlytwawgvq kaskhqdaaw kfirwasgkg
      361 yerlvgrelg wskvpggkra slyrdpayvk asgafagpte rairsarpga pgvqprpapg
      421 iqfvgipefa dlgtkvshei ssaiagkqsv sealrnsrrp aqevsdaytd h
//
LOCUS       WP_457687635             142 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457687635
VERSION     WP_457687635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15808
     Region          8..141
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mpsikqfqvt fdcaeperla rfwcevlgyv vppppegfat wddfhrslpp edqgswfaci
       61 dpsgvgprly fqrvpegkvv knrlhldvrv gtglvgeerl aaleaectrl vplgavrvql
      121 lydgndsciv mqdiegnefc id
//
LOCUS       WP_457687637             220 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457687637
VERSION     WP_457687637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23546
     Region          4..218
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 miamdalwaf almvglltlt pgldtalilr taalgsrrra wgvvlgiqsg tlvwgvltsl
       61 gitalltash layetlrwag aaylvwmggr llwgtwrrda vdeypeptgs dtedktgkgt
      121 ddtllggwrq glatnllnpk mgafyvavlp qfipadashl tagvllagvh illaviwaca
      181 litlarvfrd rlqrpsarrv ldrltgtvia afglrlalge
//
LOCUS       WP_457687639             775 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457687639
VERSION     WP_457687639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..775
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=88219
     Region          9..227
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          364..725
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mpetglrsap rfsiivpvyh vqgylracld sllaqdftdf eviavddcsp drsgeilaef
       61 aardprvihv rheenggiga arntgverar gdyllfldsd dtytpgalra madrlgased
      121 pdlllfdhvr tywwhavkps avrellaeag advfkpaert eflhmfavvw nrafrrdffv
      181 dngfrytdgl yedalmvytt mltaeravcl dhacveyrqr rhgnsmktpg rkhftifeqy
      241 qrlfdfldgr pdldhlrplf fermvshflf tgaresrvvv qdrpeffrrs vamyrrhkpa
      301 gftpppevda lqfqalergs yrvfqalnlv srtrqrgqqr lrkaqramsk rastrfyrme
      361 lkrpidqnla vfsaywnrtp scnplavyek akelaphlhg vwvvredvvd tvpdgmdhvv
      421 vntqrywelm arakyfvnnv nfaddvvkrk gqvhiqthhg tplkrmgidq qkypaaakgm
      481 smhkllerad rwdlsvssnq htseqwervy pcsftsidag yprndvffrt gareireird
      541 rlgiapgsta vlyaptvrdy qvgyvpqldl ekitrelgpd ivllvrthyf ygqnphlqel
      601 qeqgalidvs rhpsveelcl aadalitdys simfdyanld rpiinyaddw etyvrsrgvt
      661 fdllsgkpgd tpgivatted elieafrsgr wkgteaaelr aafrarfcmw ddghaaervv
      721 nraflgsqdl ipaplplser tvapapheae rtaegvglas gagassgrpe velss
//
LOCUS       WP_457687647             362 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Streptomyces
            nigrescens].
ACCESSION   WP_457687647
VERSION     WP_457687647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38820
     Region          31..321
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msrhadaaph stgtpdrhpg kdtedartav tvfvalganl vialaklagg lfagspalls
       61 eaahsvadsl nelfllaslk rsnrapdsrh pfgygkercf wsllaavgif vmggcfsffq
      121 giealrsdhs etrtgylvgl avlavalvae gssliralvq vrgqargsgh smreavraad
      181 dpalrtvlae dstacfgvlv amagvglhmi tgevrweawa smiigallvf vayqlakesr
      241 gqiigeaadp alrralrrfl eeqpeidtvt tlltmrlgtr stlvaartdl vggldseeve
      301 evlvrlksai raqwpiadqv fldvtdaspn drerarrerr qldetvaagr eepgtrqqed
      361 ae
//
LOCUS       WP_457687654             802 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687654
VERSION     WP_457687654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..802
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88720
     Region          18..802
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mhdaespagt tgppatagpl dtaelrrlda hwraanylsv gqiylmanpl letplrpehi
       61 kprllghwgt spglnlvhth lnrvikarel dalcvwgpgh ggpavvansw ldgtysetyp
      121 dvgrdgagma rlfrqfsfpg gvpshvapet pgsiheggel gyslthayga afdnpellva
      181 cvvgdgeaet gplaaswhat kfldpvhdga vlpvlhlngy kianptvlar iprdeldall
      241 rgyghdpihv tgddpatvhq alaaamdral driaaiqrra rdegvterpl wpmivlrtpk
      301 gwtgphevdg qpvegtwrsh qvplsgvrdn aahlrqledw lrsyrpdelf ddegrpspdv
      361 lacvpegsrr lgasphangg llvrdlplpp leryavevdk rgsvlheptr vlgglleavm
      421 dataerrdfr vvgpdetasn rlqalyeatg kawqaqtlgt dehlardgrv mevlsehlcq
      481 gwlegylltg rhglfssyea fahivdsmvn qhikwlrtar rlpwrrpias lnylltshvw
      541 rqdhngfshq dpgfvdhiln kspevvrvyl ppdantllsv adhalrsrdy vnvivagkqp
      601 gfdwltldea rthcargaga wewartedgs rdpdvvlaca gdvptqetla aaallrrhlp
      661 elavrvvnvv dmarllpsge hphgmpdpey dalftrdkpv ifayhgypwl ihrlcyrrag
      721 henlhvrgyk eegttttpfd mvvrndldry rlvmdvvdrv pglgvraval rqemadvrtr
      781 hhawirehgt dlpevadwtw ag
//
LOCUS       WP_457687664             435 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 27 protein [Streptomyces nigrescens].
ACCESSION   WP_457687664
VERSION     WP_457687664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Naumov,D.G.
  TITLE     [Phylogenetic analysis of alpha-galactosidases of the GH27 family]
  JOURNAL   Mol Biol (Mosk) 38 (3), 463-476 (2004)
   PUBMED   15285616
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14423446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46923
     Region          59..344
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(66,101..102,143,177,179,218,246,250)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          356..432
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
ORIGIN      
        1 mphpsvprig rtfagltava acsagllaap apasatpdpa rapgaprpag aypnlaprpp
       61 mgwnnwsyym cdldekvvld naralvrtgl arkgyrtvtv ddcwmsrqrd drgrlvadrt
      121 kfphgmahlg eqlhrmglkf giyadvgtlt cekypgslgh fqqdaeqfar wkvdyvkadg
      181 cnvpvtpghg keaayrdlyg qlsralratg rpmtfsvsap ayfqfdgdsv whrvmgwsae
      241 vgnlwrtgrd valekstpaa kwasivynfr ynsrlaglqr pgrwndpdfl lagaagltrh
      301 etqsqmslwa mmaaplisst dvgalspaar kvlgneqvia vdqdplgvqg rvvaqdddsa
      361 vlskplkngd ravalfnsgg sprtlsvsag aaglaksgsy elhnlvtgrr thsegnivar
      421 evpphstvly rvtph
//
LOCUS       WP_457687672             315 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687672
VERSION     WP_457687672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34177
     Region          26..127
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
     Region          186..292
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 msevltaplv vefpftrslg pvqsafltgl rertvlgvta sdgrvvvppt eydpvtaeei
       61 relvevgshg tvttwawnps prrgqplttp fawilvrldg adtallhald apgpdavrtg
      121 mrvrvrwaaq rtgaitdiac fepddspaga hepaphsgef anavtgittp arldytyspg
      181 raqsryiqal sdhktigerc pscrkvyvpp rgacptcgla tdtqvevgpr gtvttfcivn
      241 ikaknldiev pyvyahiald gadlalhari ggipydrvrm glrvepvwte hgrfpdhyrp
      301 tgepdadyds ykeli
//
LOCUS       WP_457687676             668 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457687676
VERSION     WP_457687676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..668
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..668
                     /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=71612
     Region          291..447
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mqgsapedek rvprpalrrs atavaaavll lplsgapsaq agqprtdalq qaftdaaarf
       61 hvprsvllgv sylesrwdgh ggapsvsggy gpmhltdart altrtpefse gdedargdea
      121 rgrkrvpaga aqraalptel parlrtlpta akltgipagk lrtdpaanvl ggaallaaeq
      181 rklgmpvgsd parwytavar yggqdsahsg kafadevyav mrqgqarttd agqrvtlaaa
      241 pgltpdaaqq krlsaptaka paasaarkpe cprnvacesv papyeefgdg dygnhdkadr
      301 padqqvsaii ihdtegswet tlklikdpay vswnytirsa dgliaqhvpt kdvawhagnw
      361 yinshsvgie hegflaapda wyteamyras arlvkylsrk ydvpldrqhi lghdnvpgtt
      421 tatipgmhtd pgpywdwahy fallgkpfka tagprgglvt irpdydenqp vytgcakpgd
      481 tcaphgstav rlysapdeda plvkdiglhp dgrpsttgvn dtgarattgq rfavagrsgd
      541 wtaiwylgqk awfhnphdep vavpakglia vpksgreeip vygraypeke aypagvpyqa
      601 vsplpyklaa gqqyavgdrm rgeyfysptf dvtkhavvrg kdvyyeiqlg hrvgyvradd
      661 vevrrsas
//
LOCUS       WP_457687683             255 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687683
VERSION     WP_457687683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27458
     Region          1..236
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mrpnevrhkl gageevyglf stlpeptmve migcagydfv ildtehtlvd pqrlenlira
       61 aetagltpfv rvpeadpgav lraldagamg ivvphvrgra didatiraar yapegvrsln
      121 ggrgpgfgri dpaeylrran aeimvialle daegveaide ilspggvdlv lpgpgdlsqs
      181 ygvpwqvrhp rvqeavrtlr eacarhtvpf camsttpdrr aewradgvta fvvgedrdlt
      241 aralrghlar tagre
//
LOCUS       WP_457687686             463 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457687686
VERSION     WP_457687686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..463
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49951
     Region          38..434
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,166,
                     169..170,173,286,289..290,293..295,298,325,329,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mtdttsstpe rrggtpigar aaarldrlpp srwhrritli vgigaffdly eiflggvlaa
       61 alaeqwhlgh takswviaag flgmfvganv lsvladrfgr rrmflvnlga yaffsllcaa
      121 apdlswllvl rflsglglga elvlvdtyla eflpravrgr yiawaytlgf vgvpvaallg
      181 arlvaahqlf giegwrwllv agalgaaflq lmrhqlpesp rwltvhgrge eaerivagle
      241 ervvrerggs lpsvpeaetv perkvplaem frgeqrrrtv mwwifqvlqt vgyygfgsla
      301 pvvltakght vtesllyaal sfcgypigsa lsiplidrie rrtliiasal giagcglafg
      361 fatatwaivt fgflltvcsn vfsnafhvyq telfptglrs saigiaysls rltsvvlpfv
      421 alsaltslga aavftgsall mlllcldval lgprstgrsl eri
//
LOCUS       WP_457687690             458 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687690
VERSION     WP_457687690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50123
     Region          1..346
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtldiprira rvagllaeya ipsaaigvlh dgeltefavg vrnvetrepa ttdtvyqcgs
       61 mtktwtalaf mqlvdegkvg ldepvrtylp gfavadpeas aqvtprhlln htngieeayg
      121 dpgededvya rmveniadap qvfppghthg ysaalgyail arilevhdgt hwddimrhrl
      181 fdpmgltstn swheqvdear aatghlirsl eegplvtpvr hlprafgpgg nltstsrevl
      241 amahvflnkg tapngkrivs aesiqkmlns rvpvpdpymf gpawalgliv cdwqgetvya
      301 tdgstvgqna rlrilpdsnt alalltnggp resfshavfn eiltdlgmvt vpdlpapdtt
      361 lnldlsryeg vygrpgarye vaaddgklyl tlfldpmqaa flhkpdriry ellpvsethf
      421 lmppadpled tqtvalydft ngsarylhtn crvhprqr
//
LOCUS       WP_457687691            1229 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457687691
VERSION     WP_457687691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1229)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1229)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1229
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=136290
     Region          311..1169
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 msepsgavad fcsvlrrlvr gcdvqqtela ralhrsnatv sellngrrat ppslddvlli
       61 vshcrarveg hpppglsldp awwrtrlael edtaearrqr pepraekprp rvesvafdfa
      121 gavdvliggr dgfdgladel leplqlngga avelrglmdg fgarvraghg ttrtallcaa
      181 dvvllvtafc davagsgigh stqlsqgagd ittevlqelg ridlgsarvr dtaelreeis
      241 aayssateiv hglgnahghp phdliqqakr ryeqllssat wdcpelrlts etydvdredg
      301 qprtgaggvg lhrlglllee fahgctapag rrerlrapia saegsgpaip tlaagyvnph
      361 frvaahpvdw elssdewwqr qplrddievf laahlltdra trapllvlgh pgagkslltk
      421 liearlpete ffclrvelrh vpadmdvqgq meealfratg rrtewpdavd pasgavrvvl
      481 ldgfdellqa gaerldmrrr wdylksierf qqretelgrp taivvtsrtv vadqvftpta
      541 stvirlepfd ddqiadwlei wavtnrrhfl aeglepltqd vvrphrelas qpllllmlal
      601 ydavgnplrr lggqgierve lyerllvefv rrqvvkhrgp lpraaeadav eqelhrlgvi
      661 aigmfnrrgq simareadad laalrgegss pllfgrfffv heaqavvteg elrsyeflha
      721 tfgeylvvrl igdelrrtlg egddqgwsqa ddgrlhalls cvpltdraev vriagerlsl
      781 ieteqraslt vllrelfrra hwgsdhrkdv pyrpvtrnrt erdavysanl lllavlaedg
      841 vnaseffeeg dpvdrwwrca qlwrsqfsea sweaftrtls lerrtldgrl drtwdlrigt
      901 revapgtsdl awslrmpswg ptayhdtkgv daadlirrms flcetdgqql lhalspllhr
      961 lpdsmrtyri hddqsglsaa halvslmcrd pghpddwdrr yhdvlsvlpy lpfedcapvv
     1021 dvlarhlvhd aarlpgdtvv qilhgltqpr fadtsqvpaq twiallgcvq dqvgraavpq
     1081 delgklagrl gtctvfalen eeapqlrlls llreagsthi whrtghapgr ealddgfavl
     1141 eripvaersp evvigllrla relgrddwla ehaepmllsl gieglgrlra tdvdslrdrv
     1201 rdtalrtalg siervwrgvs edgrrpssg
//
LOCUS       WP_457687694             201 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457687694
VERSION     WP_457687694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..201
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21315
     Region          <97..198
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 msdsvlvihg apayryglvl glkelgfdac egetaeaaeq aewdvcllht ptpdtslltr
       61 vrqsgqglvi alvdgltvdn crdvigagah gvapqdadfd diaealrlar wgetrvpvsl
      121 lrtlvdaspa apsgltlsqs etdvlcqlas grpiadmaat lgyserqmyr largiyfklg
      181 agnrseaiat aarwrlldds f
//
LOCUS       WP_457687696             604 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687696
VERSION     WP_457687696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 604)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 604)
  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 604)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64854
     Region          36..599
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mftslrparr sdaldsddal dtepadepee plrvglrdll rvtrghrkai avalvfslia
       61 aglglaqpml atktiqefsg grpyltlavl lgvlfvveav vagvasysle rsseglvlgl
      121 rlriidkllr lpmrryesqr lgdslsrtts dttmlrdsla ydlsevvvgl fvvvggvamm
      181 vwldaalfli vlaivgvigg ltllllagir kavedaqdsl ggmsadlera lsairtvrvm
      241 raedrereri gqlarqayqq nlqaakrdav igpmmtlamh gsmmvvlvig girvasgegs
      301 ladlvgflly ityisapian mfdvmatvqr glaalqriee vtqlpgeads tpatapaagp
      361 aavptaegtt pavefrdvtf sydadrpvlr qvsftaprht hvalvgpsga gkstlfalla
      421 rfydadegqi lldgiditrq msidecrskm slveqtapvm hgtlrdnity acpeatdeqi
      481 qrvvelasln dlvrrlpegl dtavgehgdm lsggerqria iarallprps lllldeptsq
      541 ldaaneealt raiaqisrec tllviahras tiraadtvia ldngrvtdtg tpeeitarra
      601 fafd
//
LOCUS       WP_457687704             839 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457687704
VERSION     WP_457687704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 839)
  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   3  (residues 1 to 839)
  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   4  (residues 1 to 839)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..839
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=89023
     Region          14..255
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          249..680
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          691..804
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mcasqsgrls gdgvfdltrt avvmadragv aqgwtkgaer llgyavseav grplaelfag
       61 vapaasqdnr wesrlaaadg wsgleavrhk dghrldlefr vlpvldater sarlvlaaem
      121 tqtpwsgasq sflegilgms pigvamvnae lefvwlndal ermggtsreq rlgkrladiq
      181 pglavealea emrkvlstgt psvgyeylgr pqsdpereha ystsffrled eagqvlgvcy
      241 mvldvtesyr arqrmallnk agerigssld vwqtaqelad aavpdladfv tvdlldallc
      301 geeptpgpvd aadlvtmrra gqqsvregcp eavvavgeat ayppsapvvl slvegnsalf
      361 qtldlaaggw aaddpvraah lrelgfhslm vvplrargvf lgaatfarwq htgpfqpddl
      421 vlaeefvtra aisidnarry trehnaaltl qhsllphdlp eqcaveaayr ylpadslsgv
      481 ggdwfdvipl sgarvalvvg dvvghgvhaa atmgrlraav qaladldlsp eevlahlddm
      541 lnrvahdana ddgvigatcl yavydpvgcr ctlaraghpa pllisptgng rllelptgpp
      601 lglggmpfes velplpegsl lalytnglll gkaldldggi trlrtalaap qapledlcdt
      661 vigglpggrp vddvalllar tralapaqla tweipadpsa vgqarrsaag rlaewdleel
      721 efstelivse lvtnairhas gpislrmira ralicevsds sstsphlrha rttdeggrgl
      781 fliaryaerw gtrytpqgki iwaeqplrsa agagpandls alldglddpa apftgaegr
//
LOCUS       WP_457687708             371 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Streptomyces nigrescens].
ACCESSION   WP_457687708
VERSION     WP_457687708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=38857
     Region          <41..300
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mtpaprppaa ppdppgaprq pgmlhvrfrt adgtpvsagc feqllgllaq ftpviealpp
       61 daaladvrga lryfdrdaag iaelvrlral awhgvrctig iganpllarm aaqgaapgei
      121 rgvpddagtv aafldrrpas alhgvgpata ralcayglds igriaaappa tlqrilgart
      181 grivyerarg idptpvtpna aarsmgaehr fahdeldpar rrrallslad dlgarmrasg
      241 qvaraltltv ryadrstttr trrldgptah gpalteaaya lhaalglqra rvrsvalrae
      301 dlcraeraar qltfdpsddr ahrieaavdr ararfgtgsv rpaatlgrtp pppgakplgp
      361 gvkgdrggdr p
//
LOCUS       WP_457687710            1199 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase III subunit alpha [Streptomyces nigrescens].
ACCESSION   WP_457687710
VERSION     WP_457687710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1199)
  AUTHORS   Kelman,Z. and O'Donnell,M.
  TITLE     DNA polymerase III holoenzyme: structure and function of a
            chromosomal replicating machine
  JOURNAL   Annu Rev Biochem 64, 171-200 (1995)
   PUBMED   7574479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1199
                     /product="DNA polymerase III subunit alpha"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=129148
     Region          2..1079
                     /region_name="DnaE"
                     /note="DNA polymerase III, alpha subunit [Replication,
                     recombination and repair]; COG0587"
                     /db_xref="CDD:440352"
ORIGIN      
        1 mpgfthlhta sgfslrygas hperlaeraa ergmdalalt drdglsgavr fakaaaeagv
       61 rplfgselav aeresaptpt arrrtpvrgg afldesaara vflardgaag waalcrlvsa
      121 ahtgqgeqpv lpwsalesat dgltvllgpd sevgralaag rpdraarlla pwrerygeal
      181 rlevvdhgrs gsgpgsprla artlgfavdq glravltnav ryadpgqgpv advldsarrl
      241 vpvdrhrpea rdsgerwlkd gatmshtaer vaeaagfrrg lahrllamte etageclvdp
      301 qddiglgrih fpeprlvgag hrtaarvlrs rcaagmvlrg ydhdrerwar lhdelrtier
      361 lgfpsyfltv aqvvddirem girvaargsg agslvnhllg iahadpvehg llmerflser
      421 raalpdidid vesarrlevy raifdrfgae rvatvsmpet yrvrhavrdv gaalgmdpar
      481 vdrlakafph irardaraal aelpelrgvr eaggeqlwpl vealdalprg iamhpcgvll
      541 sdatlldrtp vvptsgegfa msqfdkedve dlgllkldvl gvrmqsamah avaeigratg
      601 rridlddpaq vspgdpatyd lirstetlgc fqiespgqrd lvgrlqpatf hdlvvdislf
      661 rpgpvaadmv rpfiearhgr kavryphpdl eeplretygv vvfheqiiel lrimtgcgrd
      721 egdekrrals hpelqgrvra wfaqcaerrg yapeviartw eiveafgsyg fckahavafa
      781 vptyqsawlk ahhpaafyag llthdpgmyp krllladarr rgvpvlpldv nrsavahrie
      841 lvsgdgfrsd gpgdrsavwg lrlalsdvhg mseaeaqrie tgqpyhslqd lwqrarpgrp
      901 vaerlarvga ldafganrrd lllylaelhr hgrrapggql tlpgraldga gaepvdpvep
      961 aglpdlsdve rlsaelgvlg mdasrhlmad hreflaelga lparllrgar hgetvlvaga
     1021 kaatqtppir sgrrvifttl ddstglvdca ffddshaaca htifhswlll vrgtvqrrgp
     1081 rslsvvgaaa wnlaelaelr ceggleavaa rlaavpdaea aeadtpaaep gapaagqgag
     1141 eesgeesgtg repepaaapg rtirlstgye lhpwadlqpp geraatgrkl whsspgsag
//
LOCUS       WP_457687714             256 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457687714
VERSION     WP_457687714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25738
     Region          1..256
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnrfdgrrvl itgagsgigq atvhrilaeg grvvaadvda aglritadra aaegadgrle
       61 tvvldvadea avragvaaav aglggldvlv naagilraah thetgldlfn qvlsinltgt
      121 flmirealpa llegeapvvv nfsstsasfa hpymaayaas kggiqsmtha iaseyskqgl
      181 ravcvapgsi asgmtsgpvp glpedadmsl ftklfpaige gfagpetvag viamlasrdg
      241 afitgtevri dggthm
//
LOCUS       WP_457687716             277 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687716
VERSION     WP_457687716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28443
     Region          22..229
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mdtsapgsda gpnsarphga gvavlsdiha vlpaleavla epdvrtadri vltgdllagp
       61 lprqtlallr glgdravwis gnadremaav rqgtgdtpad pmdawaagql gpddldflgs
      121 lpatatlevt glgpvlfcha tprndteial vdsrperwae vlegvpdavr tvvcghthmp
      181 fvrfthgrlv vnpgsvgmpy grpgahwall gpgggavtlr htafdheaac ariaresdsp
      241 saaawadtyv rartsaeeal tafgpgdgre aapgtgg
//
LOCUS       WP_457687721             256 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687721
VERSION     WP_457687721.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27869
     Region          7..255
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mspqgamvev rsvhksfgpl dvlkgvdldv rtgevtvvlg psgsgkstll rtinhlekvd
       61 sgsvsvdgal vgyrrsgnkl yelrereilk qrteigfvfq nfhlfphltv lenvteapvs
      121 alrrpkkeav eaartllarv glaekadayp rqlsggqqqr vaiaralale pklllfdept
      181 saldpelvge vldvikdlah qgttmivvth eigfarevad tvvfmdggri veqgppgevl
      241 drprhertks flskvl
//
LOCUS       WP_457687737             218 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687737
VERSION     WP_457687737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22983
     Region          14..217
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtdsgrapsa agaavgrrig iglmyglwrp rvlgawrvps agpvilavnh ahgldgpmlm
       61 gtaprpvhfl ikkeafvgpl dpflrgigql kvdrntadrk aitdalgvlt qggvlgifpe
      121 gtrgegdfas lraglayfav rsgapvvpva vlgskerqsr ltpavpplrs rvdvvfgdaf
      181 eagdgsgrrt rkaldeatvr iqerltahle earrltgr
//
LOCUS       WP_457687738             241 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687738
VERSION     WP_457687738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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
REFERENCE   2  (residues 1 to 241)
  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 10007540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26746
     Region          13..228
                     /region_name="YcgL"
                     /note="Predicted nucleotidyltransferase YcgL [General
                     function prediction only]; COG3541"
                     /db_xref="CDD:442762"
ORIGIN      
        1 mseaaaghsl vtehtvyacv mgsrafglat etsdtdrrgv flaptrlfwg fekppthvdg
       61 preeefswel erfcqlalra nptvleclhs plveridatg rellalreaf lsrqvhrtfa
      121 gyassqlkql radvrqrgap rwkhamhllr llassrdllr tgvltldvgq nredllavrr
      181 gevpwatver rmarlseeae aavsgsplpp epdrarvadf lfrarrasal gspptfsavp
      241 p
//
LOCUS       WP_457687742             330 aa            linear   BCT 27-JAN-2026
DEFINITION  COG1470 family protein [Streptomyces nigrescens].
ACCESSION   WP_457687742
VERSION     WP_457687742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11444751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="COG1470 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33051
     Region          <60..>280
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mpfrprtavs gailataavl lcpaaaaarp aaapappgws aapapgdgat psaqdrpyfy
       61 legapgtvmn drlslrnptg ravtvrlrgs gawiafaake vtvpprtraa vpftvtvprd
      121 aapgdhpatl iataagpgrg aavrdtvpvh lrvsgpvlaa ltvenvsvrg rgeaaviryt
      181 lvnrgntvlt prlavradgl fgpvlrrgvr tlpgrlspgq saeltepwad ppgldavevr
      241 ltatadggah gsatasytal pwgvvagpaf llaagagglv ivrrrrraqv pgglrgggpv
      301 gsadggkrps grqaadpaae lastgsgars
//
LOCUS       WP_457687750             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687750
VERSION     WP_457687750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36075
     Region          29..246
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtttdhqpad psttapapta sptprqpvir vrdlrmsygs ahvlhgidld ihrgeifall
       61 gpngagkttt veilegfrqr sageavvlgt dparggdawr ariglvlqsw rdhrrwrvae
      121 llthfatyyp rprdpaella lvglteqagq qvdrlsggqr rrldvalaiv grpellflde
      181 pttgfdpear rdfhdlverl ardegvtill tthdlaeaer ladriamlvn grirahgtps
      241 elarraaaqa evrwtapdgt prrertedps qlvwglhqet ggpvadlevr rptledtylh
      301 mvhrdtgdga dagttdanea gssdgekraa
//
LOCUS       WP_457687752             420 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687752
VERSION     WP_457687752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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 420)
  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..420
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..420
                     /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=44158
     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 ypngttavdd lsldlpeggv tvlvgssgcg ktttlrmvnr mveptsgtis
       61 vggrdilead aaelrrgigy viqqsglfph rtildniatv plllgwgrrk araraaelle
      121 lvglpadagk ryphqlsggq qqrvgvaral aadppvllmd epfgavdpvv rtqlqnellr
      181 lqeelrktvv fvthdideav rlgdriavfr tggrlvqcap paellarpad dfvadflgae
      241 rglkllsltt ladvpyapgr eiradepvga isrdgdrwrl vtsprgeplg wldtdalpag
      301 gtageaplea vrplrdtdsl lsalneavss paaavarvta dgvltgltsr davhdragrs
      361 haeagraatt terapepape ppvakdaedg kdgrtakdad dpaslktasa pepsapepsa
//
LOCUS       WP_457687760             294 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687760
VERSION     WP_457687760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001217 - DNA-binding transcription
                     repressor activity [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31310
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..283
                     /region_name="PBP2_LTTR_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08436"
                     /db_xref="CDD:176127"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176127"
ORIGIN      
        1 melqqmryvv avaetggftr aaerchvvqs alshqiarle kelgarlfdr tsrsvrltaa
       61 geafvpvarq aleaaerara evaaatgevr grlavgaist vaavdlarel gafrtrcpqv
      121 rislqtamsd qlleqvrqgv ldvafvglvp aartvgvrek elargelvav vppghplavr
      181 ewttlsrmar etfvdftags aarrqredaf raagltseva yevttvefla klvraglgvg
      241 mvpeaiasel agldivrvrp apertervvw sglgpspaav aflsglgvdp ndrp
//
LOCUS       WP_457687762             432 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457687762
VERSION     WP_457687762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43727
     Region          26..391
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(36..37,40..41,44,76,126,128..130,133,153,156..157,
                     160,233,236..237,240..242,245,273,277,331..332,336,340,
                     355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 metehipepp ageapgtrpg lgrgtlllms vaaglsvagn yfaqplldli grdlhlsast
       61 aalvvtvaqv gyglgllllv plgdllerrr lavtltaata vfltvtasap hvallltgta
      121 ltgltsvaaq vvvpyaatla apaqrgrtvg tvmtglllgi llartaagll aelggwrtvy
      181 wvnaalmllm avllrlrlpa lrttaglryp allrstlalf gqepvlrwrg algaltfagf
      241 svlwtalafl msgpsygwqe saigllglvg aagslaasvg grladrglah rvtgaaafll
      301 lgswgllalg gsggswslaa llagvivldl aaqavhvsnq nlvyavrpea rnrlnsaymt
      361 syfvggavgs altsvvwgaa gwggvcvlga glaavvvalw avermrrras gggrtgpgqa
      421 aaaeapapsf ts
//
LOCUS       WP_457687767             948 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457687767
VERSION     WP_457687767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..948
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=109124
     Region          1..206
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          569..942
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mpdvsvvviv yndadrlpta vqsvldqtlr dvevvivddc stdrsfevaq rlaadhpgrv
       61 rafqlpensg aggeprnvgi qhtegryvmf ldsddvlein acrnmleaae esgsdivsgl
      121 cvrlhkdtrn qkrdewyswl ysttrtlksv telpdlfvwd tlstnkcyrr dfliennlrf
      181 pkgmfyedlm fiadaylaae ritlipnqvy fwhvyeraav ksvtnrrhem tnythrleih
      241 rridallaer gldelklakd vkflkhdlvl hlrdlpfrdd syrqefsels reylesiape
      301 ayervqpiqa icayllqqgd wdnlipavdt linrdkvssp laehdgriyw cdghfddpfg
      361 relldvtdig yhekpvnqlf lrnqltgfrs sgrtvslagr itnplgvvpp garlkgelef
      421 sarrrslqsf rfpvhelrhd gdtlhweaaa dltaklrplg ivdtiwdvrl rldvdgvrtt
      481 trltvadtgl seplpvrprl trmvadhlep hvsakghlaf rlvseghsae rvqelitrgv
      541 rgkpgtlakt gyrkakalrk kvtsgdnklr ayhevfcrlp vkkrtvvfes hlgkqysdsp
      601 ralyeemrrq gldfeaiwsy agspkdfpkd vtlvrrwslp ylkalaqaef wvdnqsyplk
      661 ltkrpettyl qtwhgsalkn mgfdqpalka qtrqqqaeqq rsldrfdrfl vrsehdvrtl
      721 akafrlqekt llrvgyprnd alvrarqrea ergvrergpl aaelgipedr tvllyaptfr
      781 kaggrhgrfe lpfdverfad qfgdryvllv rshylnhvvl pptvqgrvid vsarhdvtpl
      841 leladglitd yssvmfdyal ldrplvffty dydayvhegr gtyfdlleha pgpvvrnedd
      901 fhetiksfes qtleyaqrrk efvakfgeyd rgdaarsivd qffaqwsr
//
LOCUS       WP_457687773            1027 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional acetate--CoA ligase family protein/GNAT family
            N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687773
VERSION     WP_457687773.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Sanchez,L.B., Morrison,H.G., Sogin,M.L. and Muller,M.
  TITLE     Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming)
            gene from the amitochondriate protist, Giardia lamblia
  JOURNAL   Gene 233 (1-2), 225-231 (1999)
   PUBMED   10375639
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
REFERENCE   5  (residues 1 to 1027)
  AUTHORS   Mai,X. and Adams,M.W.
  TITLE     Purification and characterization of two reversible and
            ADP-dependent acetyl coenzyme A synthetases from the
            hyperthermophilic archaeon Pyrococcus furiosus
  JOURNAL   J Bacteriol 178 (20), 5897-5903 (1996)
   PUBMED   8830684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18515002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1027
                     /product="bifunctional acetate--CoA ligase family
                     protein/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.2.1.13"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0046356 - acetyl-CoA catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=108077
     Region          26..175
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          203..1018
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mqtppehayp thweadvvlr dggtarirpi ttddaerlvs fyeqvsdesk yyrffapypr
       61 lsdrdvhrft hhdyvdrvgl aatiggefig tvrydrineq glpaknpedd qaevaflvqd
      121 ahqgrgvasa llehiaavar ergirrfaae vlpanskmik vftdagythk rtfedgvvrl
      181 efdlepteqs mavmrgreqr aearsvqrll apgsvavigt grtpggvgrt alrslldsgf
      241 tgrvhavnha fpedlqrldp edvpavrtlr eitdpvdlav iavpadsvpd virdcgehgv
      301 qgvlvlssgy aeagpdgrer qrallrqars ygmrligpna fglintapdv rlnaslapqm
      361 pgaghiglft qsgaigiall sglhargpgd ggiagisafv sagnradvsg ndllqywyed
      421 pdtdvvilyl esignprkfa rlarrtaavk pvvvakgarh ngtappghav ptvrvpdstv
      481 aalmrqagvi rvdtvtelid aglllasqpl pagpriailg nseslallay daclteglrp
      541 qrprvlasaa tpddfraala ealsadgcda vvvtaipwvg egaavspggs egaaladalr
      601 taaaahpekp vtvvhlamdd laqtlaapap apapsaessa papdqaacpe paartinpap
      661 apapapapap apapapapap apapappppp ippapshfpr ppaptgpppt laarqatpar
      721 dteagiprrp rreplripay paaeravrsl aeavryaawr reaadpgrvp eyddiqeaaa
      781 gadierlldg lgpdvptsrs vpvppqdaea llarygihtl pvlpapdpdt avraaarlgy
      841 pvalkttaph lrhrpdlggv rldiageael rrtyaeltdy lgspeelrpv vqsmvprgvd
      901 tvvraaidpa agavlsfgla gapsqllgdi ahrlipatdr evaeqirsir aapllfgwrg
      961 sqpvdtaala elllrvsrlv ddhpevvgvd lepvvvaaqg lsvlgatvrl arppattdlg
     1021 prrlpvy
//
LOCUS       WP_457687775             386 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687775
VERSION     WP_457687775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41699
     Region          3..360
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 matqqipvvv lagflgsgkt tllnhllgng dgtrigaivn dfgsieidam tvagqvdsmv
       61 slgngclcca vdtseldtyl erlarpsari dvivieasgl aepqelirmi lasdndrivy
      121 gglievvdaa efddtrarhp eldrhvgiad ivvlnkadri gdaarqslmd tlaglapgrp
      181 victaygrvd pelffdrgpg edhdaavrql sfedllreaa angaaahdah dahdahdvhd
      241 addrcghpgd cghpghthha ghlhaayesv eftsaepmhp rrlmdfldsr paglyrikgf
      301 vhfdvpenrq kftvhavgdf lrfypapwpk geerctqlvm igsgidapal rkelencrqs
      361 apseadpnsm wgvlryvaar eeaeda
//
LOCUS       WP_457687784             539 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457687784
VERSION     WP_457687784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58575
     Region          7..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mptqislhdi tksygdrlll dgvslsvrpg erigivgeng agkstllril agaerpdegq
       61 vvlradggvg hlaqtpdlpp drtvqdaida aladlremer rlrslesrld ratpvgleey
      121 gdlltvfelr ggyeadarvd ralhalglar lghdrrlgsl sggeqarlgi acliaaapei
      181 mlldeptnhl dataldwleg allahrgtvl tvshdrlflq riatalvevd adrrglvryg
      241 ggygtfiaak daarrrweqd harwceqitq ltdfagtaar svaqgrpmkd gnkmaydrdk
      301 grvqasvssr vrnaqerlrr lrenpvprpp dpfrfraapd vgeaegtlvr ldgvrvedrl
      361 avdslavaag erllihgang agkttllrvl aglttpdrgt vlrrgrigfl aqeipvsrpa
      421 epllsvfrrg lagdveelta lllsfglfre cdlhvpvgal sagqrrrlal arllarpadl
      481 llldeptnhl alglveelea alsawpgalv vvshdrllrr rfsgrsyeir dgrpvlsah
//
LOCUS       WP_457687787             656 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase [Streptomyces nigrescens].
ACCESSION   WP_457687787
VERSION     WP_457687787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..656
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=70499
     Region          18..635
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtkpslpdll haavtavggt erpgqvamae avaeavdeqa hllvqagtgt gkslgylvpa
       61 lahgervvva tatlalqrql verdlprtve alhpllrrrp efamlkgrsn ylclhrlheg
      121 vpqeeedglf dvfeqatpts klgkdllrlr dwadetetgd rdaltpgvsd rawgqvsvss
      181 reclgaskca ygaecfaeaa rerakladvv vtnhallaid aiegapvlpq hevliideah
      241 elvsrvtgva tgeltpgqvn ravrraaklv nekaadqlqt asetferlme lalpgrleei
      301 pedlgyclma lrdaartvvs algstrdksv qdedavrkqa laavenvhav aeriangsey
      361 dvvwyerhdr fgaslrvapl svsgllrekl fddrsvtlts atlklggdfn gvaaslglap
      421 egtegedvpp wkgldvgspf dyskqgilyv akhlaqpgre gsrtdmldel telieaaggr
      481 tlglfssmra aqaaaeelrg rldlpillqg eetlgelira faedartclf gtlslwqgvd
      541 vpgancqlvv mdrvpfprpd dplmsarqka veegggngfm avaathaall maqgagrlvr
      601 atgdrgvvav ldprverary gsflrksmpe fwyttdrnqv rrslaaidaa aktaea
//
LOCUS       WP_457687789             229 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687789
VERSION     WP_457687789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24324
     Region          66..211
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mpptdpglsl ssadplgrql ppecralsdd drrppapasg plldnlagwg aadtpagpfa
       61 lvpvrpdrdl dritgwmndp avaafwelag ppettaahlr gqldgdgrsv pclgvlagvp
      121 msyweiyrad ldplarhyaa rpqdtgvhll iggagdrgrg lgsallrata dlvldhrpqc
      181 trviaepdlr ntasvaafls agfryadeie lpgkraalmv rdrarrhll
//
LOCUS       WP_457687794             311 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457687794
VERSION     WP_457687794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33068
     Region          66..278
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 msgasvlydv pgpkakarnl vysvvgslav lgliafvvmr lntegqlape vwnifnnagv
       61 rtnirdgvlt tlqvfavaav lslllgvlla varlsdhkpv rwlatgfiel fravplliti
      121 yalwvilltn reaigltgdq pqfwalvigl tvyngsvqae vlraginsvp tgqreaayal
      181 gmsktqvmtt vlipqavram lptiisqlvv tlkdtslgyi itfeellfta rqmstniivn
      241 gndtyvpfii vigtiyvamc lalsalanwi errgrraktg igvatagepv taadameaad
      301 ampdgaagtk d
//
LOCUS       WP_457687802             412 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Streptomyces nigrescens].
ACCESSION   WP_457687802
VERSION     WP_457687802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45054
     Region          23..368
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpesdeitsn dvprsedrtd armprwlpra mvlalalvac fqlatwgfhq linlllnvli
       61 afflalavep avdwmaargm rrglatglvf vgilgvaagf fallgsmlag qitnmveefp
      121 qyldsviswv nntlhthlsr vevqnnllks dwlqkyvtds annvlavsat vlgslfnllt
      181 valfsfyfaa dgprlrrtlc svlpphrqte vlraweiava ktggylysrg lmalisgiah
      241 yvllevlgvp yapalgiwvg lvsqfiptig tylagalpil iaftvdpwya lwvfgfvviy
      301 qqfenyvlqp ritaktvdih pavafgsvva gtalmgavga liaipatatl qaflgayvkr
      361 yevtddlrvh grrgrgvral armrrnlrdv qpsapledrk adgtqaegee vr
//
LOCUS       WP_457687809             258 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457687809
VERSION     WP_457687809.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26366
     Region          7..256
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mplpaydltg rtalvtgaas gigratatll atagatvhca dldeqgakat aaaitaaegs
       61 ahahrldvtr rdqvaavvda arsttgrldv maniagimhs apvletedad ldrvwntnfk
      121 gvlygcqeaa ramiatatpg slvnmasgai dtgapgllsy gaakaavvql tktlatevgr
      181 hgirvnavap gwirtamtdr htaeaqqqae gpmirmsplg rvgepedvah tvlhlasdas
      241 sfmtgqvlrp nggvampw
//
LOCUS       WP_457687806             292 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687806
VERSION     WP_457687806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 292)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31308
     Region          34..164
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          205..287
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvmvsgeqaa gggpgaavpr argewarhwr ydglpgldll raryvrhsfp rhahdgyvvc
       61 avtagieevg lregtvragh ggvimlnpev ahtaragape gwayatlyps yevvaeiaee
      121 ttalrgtagf drtvaedpql agviteihra aetgnalaad sllriavarl lrryggplpt
      181 rtprtagart aararavlee rmadppsler laqelgtgpf allrafkgay gmpphtwltd
      241 arvrrarrll eagrtpadta vavgftdqph lnrhftrivg vppgayrrer sa
//
LOCUS       WP_457687804             279 aa            linear   BCT 27-JAN-2026
DEFINITION  AzlC family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457687804
VERSION     WP_457687804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28065
     Region          27..247
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mpeqteirtt eraappppap patsdaavir dalgvgvavg lsgfafgvts agvglsllqt
       61 calsllvftg asqfalvgal aaggnpltaa agafflgarn afyglrlsav lgyrstvkpf
      121 aahwvidets avtlaqpdrr tarlgftvtg ltlyvlwnlt tlvgalgaea lgdteawgld
      181 aagpavflal lapmlkdtve rvaaglavvl vmvtlpllpt gvpvlisala apavlvvqgr
      241 rerakeagta qepgagpaap parpdgapds rtateedra
//
LOCUS       WP_457687812             924 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA translocase FtsK [Streptomyces nigrescens].
ACCESSION   WP_457687812
VERSION     WP_457687812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..924
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=96857
     Region          401..914
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 masrtsgkgt qstagpskqr agrtagaakk taakkapakp pakkaaaakk apakrapakk
       61 aapkpapspt ggvyrlarac wlglahgiga vfrgmgrgak nldpahrkdg lallllglal
      121 viaagtwsnl sgpvgdlvel lvtgafgrld lvvpillggi avrlirhpek peangrivig
      181 lsalvvgvlg qvamacgspg rddglaaiqd aggylgwvas kpliftvgqt lavallallt
      241 lfgllvvtat pvnaipqrlr algiklgvvh pvadeadyde veeyaeewre qpvrrprrsa
      301 aaapaandpd aieeaalakr rrprrasaqp apdrpmdavd vaaaaaaald gavlhgvqps
      361 plvaglsssi sgdrrghdge dtagesgtvp pardaepepp aaertpavpd ftkappersg
      421 elparaeqlq lsgdityslp sldllsrggp gktrsaanda ivtslttvfq efkvdaavtg
      481 ftrgptvtry evelgpavkv ekitalakni ayavaspdvr iispipgksa vgieipntdr
      541 emvnlgdvlr ladaadddhp mlvalgkdve ggyvmanmtk mphilvagat gsgksscinc
      601 litsvmmrat pedvrmvlvd pkrveltaye giphlitpii tnpkraaeal qwvvremdlr
      661 yddlaaygfr hiddfneavr sgkvsspegs erelapypyl lvivdeladl mmvaprdved
      721 sivritqlar aagihlvlat qrpsvdvvtg likanvpsrl afatsslads rvildqpgae
      781 kligkgdglf lpmgankpvr mqgafvteae vgavvqhckd qmapvfrddv tvgtakkkei
      841 dedigddldl lcqaaelvvs tqfgstsmlq rklrvgfaka grlmdlmesr nivgpsegsk
      901 ardvlvkpde ldgvlavirg eate
//
LOCUS       WP_457687816             460 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457687816
VERSION     WP_457687816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48177
     Region          6..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mdfhpqpqgg apkpwafpap ersqlpnglt lltshrpgqq vvaveinlva pldaepegld
       61 gvatimaral segtdthdae efaaelercg atldahadhp gvrvslevpa srltralgll
      121 adalrapafp eseverlvrn rldeiphela nparraamal skelfpatar msrprqgtee
      181 tiaridaaav rafydahvrp atatavivgd ftgvdlgaal adtlgawsgs taeplkaspi
      241 vaddtgrvvi vdrpgavqtq lligrigadr hdrvwpaqvl gayclggtlt srldrvlree
      301 kgytygvraf gqvlrstapt spegstgaal laisgsvdtg stvpaledlw kvlrtlaaeg
      361 ltdeerdvav qnlvgvaplk yetaaavagt ladqveqqlp ddfqaqlyar laetgtveat
      421 aaavnafpvd rlvtvlvgda aqiaepvkal gigevtvvsg
//
LOCUS       WP_457687821             419 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687821
VERSION     WP_457687821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 419)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11660203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44349
     Region          2..320
                     /region_name="Glycosyltransferase_GTB-type"
                     /note="glycosyltransferase family 1 and related proteins
                     with GTB topology; cl10013"
                     /db_xref="CDD:471961"
     Region          274..374
                     /region_name="RfaB"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0438"
                     /db_xref="CDD:440207"
ORIGIN      
        1 mkvlhvitdl dvggaeqqlr lllrrlpahc evltltgpgp vaegieadgt pvrhlgmtgn
       61 rdltalprla glirdggydl vhthlyracv ygrvaarlag vravvatehs lgdaviegrr
      121 ltrgvrtlyr aterlgtatv avsdtvaarl rrwgvpeqri hvvpngieah rfgfdpaara
      181 lvrtrlglpl dafvvggagr lvpgkrfdvl vravtqlpgv hlllagagpe remlrrmaeq
      241 fgsgdrihll gerdgavdta aagrgaagpd ipgllsaidv fvspspdeaf glavlealas
      301 glhvlygscp avdelpadra pgarhfglnv helgtalrdl rrqgpgrlpv ppvvrrydis
      361 rsaealmsvy eqavtvtsar rrtpavvppp qgraavlpaa svslpdpsrs pdpsplpnr
//
LOCUS       WP_457687825             604 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces nigrescens].
ACCESSION   WP_457687825
VERSION     WP_457687825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 604)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65225
     Region          33..600
                     /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 mterdettke saearpapsg rcddtaaslg dyratfhaar vamavlnrdg lvlaanpafg
       61 elvgadpael vaatasdltd lgadprvwta yrevlcgrsd rlrctrrlkh peghsvwvev
      121 tvepltpepl sgeermllsv adisdrhdll arlrhlqmhd pvtrlpnral fferlssale
      181 tasfepsgtg riglcyldld gfkavndtlg hrvgdrllsa vaqrltrcae saadrgagrg
      241 ghlvarlggd efallvedst gtdqlaelaq cvldalqrpf dlagqrlsvs asigvveraa
      301 tgttatglmq aadttlywak edgkarwtlf dpernahrmt rqalsstlrp avdrgeftle
      361 yqplvglgdg raqgvealvr wrhpqfgtls pnrfialaee ngaivelgrw vlerachqar
      421 awqlahpgep lfvsvnvavr qvwdsdlvad vagilaetgl ppellqlelt esavmgsagr
      481 plqalqalsd mgvriaiddf gtgysnlayl srlpvsvlkl dgsfvrgfrs qehpnpadem
      541 ivealvalah rlgltvtaec vesaeqaerl rrigcdtgqg wlysrpvapd rvaalldagr
      601 htga
//
LOCUS       WP_457687826             374 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457687826
VERSION     WP_457687826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39209
     Region          31..369
                     /region_name="oxido_grp_1"
                     /note="luciferase family oxidoreductase, group 1;
                     TIGR03558"
                     /db_xref="CDD:274646"
ORIGIN      
        1 msgedeeirg sgetagdgir gtapgtapvp lsvldlvtvg agstasaavr tavdiartae
       61 rrgfhrywva ehhsmpgvas sspavllahl aahttrirlg sggvmlpnha plviaeqfgt
      121 leamapgrvd lglgrapgtd gataaalrrt erlhegadef pqqlaeltrf lddsfpdghp
      181 yakihavpgp vqatspggvq dphrpplwll gssgfsarla gslglpfafa hhfsaantlp
      241 aldlyrasfr psevlsepya ligvaalaae seqearrqvm tgalsmvrlr tgrpglvpsp
      301 eeaeayrfne lergfidswl gnvvhgtpda vrqglddlak rtgadelmit anahggaarl
      361 rsyeliadey glpa
//
LOCUS       WP_457687834             285 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687834
VERSION     WP_457687834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30355
     Region          68..280
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkllrvgtvg aerpalldgt gtlrdlsglv pdidgallad eaklaqlrta aasgelprld
       61 paglrtgppv arigkivcig lnyhdharet gaatpaepil fmkapdtvvg pddtvlvprg
      121 svktdwevel avvigrtary lesdaqalaa vagyavahdv serafqierg gqwdkgknce
      181 tfnplgpwlv tadevpdpqn lglrlwvnge lkqdgttaeq ifpvaevvry vsrfmtlypg
      241 dvintgtpag vamghpepkp ylrsgdvvel eidglgrqrq elkda
//
LOCUS       WP_457687832             372 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687832
VERSION     WP_457687832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=37041
     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..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 mgstgatgnp gvnlpalrgh naalvlgllr aaggqgvsrl elaahtgltp qavskitarl
       61 rteglaaeag rrastggkpa tvlrlvpgar havglhldrd eliavladlt gapvaerrap
      121 lafeagagqv ldtagrevaa lraeaggppv lgagvacpgp ldhtagvlhr vtgapqwdgf
      181 plrdalterl glpvvldkdt naaalglaqg mpsgagsfgy lhlgtglgag lvlggslyrg
      241 prtgagefgh qtvqwdgprc scgrrgciea lclaavargd ltgaaqvlgt gaanlvelld
      301 idrvllggrt vlenpdgfrt gvaaaldaqa rargrtavpv alarggarvv adgaaelvla
      361 plfgtrqpal va
//
LOCUS       WP_457687836             403 aa            linear   BCT 27-JAN-2026
DEFINITION  YidC/Oxa1 family membrane protein insertase [Streptomyces
            nigrescens].
ACCESSION   WP_457687836
VERSION     WP_457687836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Hennon,S.W., Soman,R., Zhu,L. and Dalbey,R.E.
  TITLE     YidC/Alb3/Oxa1 Family of Insertases
  JOURNAL   J Biol Chem 290 (24), 14866-14874 (2015)
   PUBMED   25947384
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Keil,M., Bareth,B., Woellhaf,M.W., Peleh,V., Prestele,M.,
            Rehling,P. and Herrmann,J.M.
  TITLE     Oxa1-ribosome complexes coordinate the assembly of cytochrome C
            oxidase in mitochondria
  JOURNAL   J Biol Chem 287 (41), 34484-34493 (2012)
   PUBMED   22904327
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Funes,S., Kauff,F., van der Sluis,E.O., Ott,M. and Herrmann,J.M.
  TITLE     Evolution of YidC/Oxa1/Alb3 insertases: three independent gene
            duplications followed by functional specialization in bacteria,
            mitochondria and chloroplasts
  JOURNAL   Biol Chem 392 (1-2), 13-19 (2011)
   PUBMED   21194367
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Ravaud,S., Stjepanovic,G., Wild,K. and Sinning,I.
  TITLE     The crystal structure of the periplasmic domain of the Escherichia
            coli membrane protein insertase YidC contains a substrate binding
            cleft
  JOURNAL   J Biol Chem 283 (14), 9350-9358 (2008)
   PUBMED   18234665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="YidC/Oxa1 family membrane protein insertase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0032977 - membrane insertase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40533
     Region          3..234
                     /region_name="YidC"
                     /note="Membrane protein insertase Oxa1/YidC/SpoIIIJ [Cell
                     wall/membrane/envelope biogenesis]; COG0706"
                     /db_xref="CDD:440470"
ORIGIN      
        1 msmfgflgea lahgaqaiap lfgtaamaaa ivlftlgvra alhplaraaa rgekartala
       61 pqlaelqrkh kgnperlqka tadlyaktgs splagclptl lqlpvffvmy hlfstgsggl
      121 ldhtllgapl gghwtgalad gglfgpqglv ylglfaliaa vatwnfrrar atmakapqpa
      181 agnaalpgma smakvmplls fgtlitvavv plaaglymvt tttwtacera llhrdraarg
      241 aqetgiegav aakgktasak gkvtpapkgk aapageqtsp agapagapaa vaadvaadga
      301 sgeraprqgp aqqragrrtp ksraarqraa raransqans qansqansqa nsqgssharv
      361 aapvgsrans rteadsrngs rpageagsrs gggapghivt tpq
//
LOCUS       WP_457687838             732 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687838
VERSION     WP_457687838.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..732
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78073
     Region          1..672
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msgqrtgwrr viptwrtvlg tgllflllvv ggmiagyllv gippansaak aqsniylysd
       61 gselahdgei nrqnvtlsqi prpvqqavla aedrdfyses avdpaamvra awntltgkgk
      121 qsgstitqqy vknyylgqeq tltrkakeff iaikldrevs kdnilegyln ssyygrnayg
      181 iqaaartyyg rdaealttaq gaylasllna psaydltahp enrqrvlsrw nyvldgmvtk
      241 kwlapaeraa lefpttkpak pspglsgqrg ylveavknyl tghhildedt lrgggyritt
      301 tiskkrqnaf vkavntrvmd rlddsrkvdr yvraggasid pasgrvvaly ggidyakqyv
      361 ngatrndyqv gstfkpivfa savqhrsttq dgtritpntv ydgtnkrmtv shgratgfap
      421 aneddrsygp itvteatdks vnavyaqmgi dvgpakvkat avalgipadt pslassqgav
      481 slgtatpsvl hmaqayatla dhgthrpytl vdkvtksdee ielpereeta avprtaadtt
      541 tailrgvvdg gtgtaaqgag rpaagktgta eedkaawfag ytpelatvva vlgqnpesat
      601 qeplygaggl srvnggdypa qiwadytaaa lngrpvrdfd lrleagaeps spepsgsdsl
      661 spgasgtptp gstesptdpv pptvaptrpt vepptptlpt epgpttpptn dfptvqpqsd
      721 elerqmqwrw dg
//
LOCUS       WP_457687859             280 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457687859
VERSION     WP_457687859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29607
     Region          21..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 matdvhgsvt dtaagkdpgs apsgaavqva glvrafgdra viddlqltiq pgefvallgr
       61 sgcgkstllr vlagldreie gevlvprrka vafqaprlmp wkrvwrnvll glpgrperea
      121 avtaldevgl ghradawpkt lsggeaqras laralvrepd lllldepfga ldaltrikaq
      181 rlvaelwrer gcavllvthd veeallladr alvmeggria yettvdlprp rdiadprfga
      241 lrarlldrlg vegstddgag gtdpaeaeae atedrsaaaa
//
LOCUS       WP_457687864             326 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687864
VERSION     WP_457687864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 326)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=33988
     Region          59..305
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mpavtltpag pfslasgirf legfgpasyd haadgilrla fpaddgasvv aaavrqevra
       61 dggtgtvrae ftvhpgtphp atavtaeaaa nqavraqlar ilsldvdatg fpglaadpvv
      121 agltadhpgl rpvcfhspye aatwaiignr irmtqaaaik ariahqhghr vhiagqtlha
      181 fptpaalrti thvpgltgik iqrlhalaea aldgkldaph lralpadhal aelrtlpgig
      241 pfsaelilir gaghpdvfpr heprvhkava tayglgaptt dddvtqlaki adrwkpyrsw
      301 vafllrvrah dtsppgpvch gsppss
//
LOCUS       WP_457687866             153 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457687866
VERSION     WP_457687866.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16352
     Region          10..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mlenvsaeps rptkdvtqhv gyllkrtqaa lrgamdkvlr ehgltvpqya tlellalhpg
       61 msnadlarat fvtrqsgnvv lrglqeagli arpatadhgr arpahlteeg narlaavqaa
      121 vyaieqrmve aipaqrlavf ladlgrmaaa lee
//
LOCUS       WP_457687870             233 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457687870
VERSION     WP_457687870.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  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
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Identification of a PD-(D/E)XK-like domain with a novel
            configuration of the endonuclease active site in the
            methyl-directed restriction enzyme Mrr and its homologs
  JOURNAL   Gene 267 (2), 183-191 (2001)
   PUBMED   11313145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..233
                     /product="restriction endonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25115
     Region          111..224
                     /region_name="Mrr"
                     /note="Restriction endonuclease Mrr [Defense mechanisms];
                     COG1715"
                     /db_xref="CDD:441321"
ORIGIN      
        1 matparrrsa atrrsaatrr ptrpkrrprg katrrrereg kalaavliga fgiavvsayp
       61 vvstivivla aaaaltiyla rtgrlhlpag iagaagvgpr rdfthtiaay qamgytefeh
      121 avadlarrdp avrrtdvsgg kndrgldvlv hlhsgdryll qckrwkgrvg seevmkingt
      181 yrdihncfga aiittsafta daertnamlp kslrlidgrg larwasggrp pwa
//
LOCUS       WP_457687874             362 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457687874
VERSION     WP_457687874.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41322
     Region          29..310
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mggdtlvpgs arlhlvdclp llrpeeqvfe amlagwrnqq ltrnlsfgyv sdqertvraf
       61 arhadglpwk wapqhveews mdlrsvrgca rstvrnyqga vrqfcdfvtn paygwaeecl
      121 lrfgahpvqv vhdwnaavha degegeperr afirpeleaf fdyadeqvvr vrgkgckgwl
      181 ptfrdatlfk taygyglrrn etrmlnevdf gpnphgrefg dygtlmvrhg kakkgsppkr
      241 rsvltvcqwt pvvieewvte vrpgmrhahg palwpsergl rvglqrldsr faayrdalgl
      301 dpalefhslr qvvhhppdrr rlrsavrpaa grprvrihhr dlhvrllrlp nphpspgpgr
      361 hr
//
LOCUS       WP_457687876             401 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457687876
VERSION     WP_457687876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /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=43020
     Region          176..398
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrnrpyepsa vdtrwlgavm htafflllgg alarfllrhp geprtpwiia lcvvlavlhl
       61 lgpgmgdadp rptrrrsawl alvvvvwmvl vvlapsfawc avplfytglr tlppraalvl
      121 vavltalvva aqlqlaghfd pnlvlappav aalatavflq merhtarqrv liddlirtrr
      181 elaaserreg tlaerqrlsm eihdslaqgl ssqrmllqaa drvwdtepdk arahvrtaas
      241 vaehnlaear rfvhdlaptd largsgldqa lralaaresg adltvrvhvd ddgrlprlpd
      301 rvqsallria qgalanvreh aaasgatltl tllddevvld vsddgdgfdp aalpdspgsg
      361 rghglpaira rlralggtlt vestpgegtv lsaaiplevp r
//
LOCUS       WP_457687878             353 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687878
VERSION     WP_457687878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37532
     Region          86..351
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mgsharpnri hrtgvriamv alvgaalpit sgglaeaats gaahsadeng qqgseatstv
       61 aqkqgtqrqf qsqaaphavk dkaadaqdak dqaapqinad haflldardg sqerelwgga
      121 kadesvsmas ttkimtaiva lkhpewlnrq itvkqeyrdy vqkvggstad lqigdtltve
      181 qllyallips gddaamalad nlgsgdtada riadfvkqmn aeaqqlglng thfdgfdgis
      241 hgnnhstard larlgqraml qpvfadivkn kqfkteapaa ngrtryytwd ntnkllssyd
      301 galgiktgsg peagyslvfa akrdnrtlvg ailkddqgrf ddatkmldwg fah
//
LOCUS       WP_457687885             414 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687885
VERSION     WP_457687885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44998
     Region          1..414
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 meirsttded ldvfvdtvha afgrfpetpv eggglwwsal emdrgllalt adgrpvgtaa
       61 ahsfeltlpg etlvpaagvt avgvlpshrr qgvlsammrh qltelrtrge flsvllasea
      121 piygrfgygp atytarltvp rhkaalavpr argvadapaa gsdngsdngs vevlrraecg
      181 eileevydry rrtqpgalsr phhwwarrag qppiapapry vavhrdadgv pdgyasysig
      241 esqtltvdet iatddavfta larfvlghnl vsqvvfkhvp pehplrwqfa dfragevsgd
      301 tdwlwvrlld vpraltargw fmdgelvldv edpflgehgr ylltvrdska dcvptdrepd
      361 lsldvsdlgs vylggtapst lvraghirah rpgaaalada lfraersphc lhwf
//
LOCUS       WP_457687895             243 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687895
VERSION     WP_457687895.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25482
     Region          20..210
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrftsetssd gvseqiftlg eipgvlwtpe gaagtrplvl mghgggqhkk apgivararr
       61 lvaecdfava avdvpghgdg pkdeeydria tenqarvaag eelapliagf qalvarrtvp
      121 ewravldavq glayvgagpv gywgvslgcg lgvpfvaaep rvraavlglg gaqasaetaa
      181 ritvpvefll qwddervpra eglalfdala sdektlhanp gkhgeipafe ldsmlrfftr
      241 hlg
//
LOCUS       WP_457687893             215 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457687893
VERSION     WP_457687893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23042
     Region          3..125
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          148..209
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrivvaedly llregmvrli eayghqvvat aatgpetlda lltwrpdaav vdirmpptqs
       61 deglrvalaa rselpglpil ilsqhvvqly arelladgag gigyflkenv fdaeqfidal
      121 ervagggtam dpaviaalls sgsshrrleg lterehsvls lmaeglsnqa igrrlflsds
      181 aiskyttslf gklgitddgt tnrrvlavlt ylnep
//
LOCUS       WP_457687906             388 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457687906
VERSION     WP_457687906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41186
     Region          162..383
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mteerervrq qliadpraaa tivaavreqv payaalddsr lhevraiaaw aldrllhlwv
       61 tdgaltpadl rrfrgiaaar aadgrpmpav lrayrvaatv ltdeiatatp plgapdafal
      121 trmalatldt laeematayt atsedlagdr dralrllldd litgrhasig altdraarlg
      181 vqlpdpycll aaeptevagp avtqeaalgl laalngpgga stfpatvrgs rlvlllpaaa
      241 ggrapevlhe rglrgcaisg esldriavay rlaadaldta pahahhparv ltdgdaqvla
      301 llggrpaatp ehlsrlilgp lvqpgrhhlm ealttyldtg sanaaarrlg lhpqslryrl
      361 rrisdltqrd prdpwqrltl diartiah
//
LOCUS       WP_457687908             462 aa            linear   BCT 27-JAN-2026
DEFINITION  carotenoid oxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457687908
VERSION     WP_457687908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..462
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50540
     Region          6..448
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtgnrylsgs fapvteeita ydlpvtgrlp ahlngrylrn gpnplgieda athlwtlgag
       61 mvhgvrirdg raewyrnrwv rstavadrlg eprrgtpvde lmdispnvqv vglagrtfal
      121 ieggirpyel tydldtigpc algatpqgys anahslfdpr trelhslafr ygsdqvqhiv
      181 mdesgvvlra taievpgnpy mhdfaltdrh vllfdspvvf saahlptgip fvwdgnrpar
      241 vgvmpragga vrwfevapsl vghtlnayed gsevvidvvr hpegfdirdv gtsrptldrw
      301 tvdltagklr edrlddrvqe fprlnsrysg rpyrygytaa velyappagp gdtrpdegfs
      361 nallkhdllr gtseahefgr ygavsegvfv pagspnaedd gyvmayvfdp ergatdlvll
      421 saldftgepi arihlpvrvp lglhgswvpg derevpryal ag
//
LOCUS       WP_457687919             336 aa            linear   BCT 27-JAN-2026
DEFINITION  ACP S-malonyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457687919
VERSION     WP_457687919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36957
     Region          26..295
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mgrteaqgwd sptapavgra sgaeprtavl fpgmgrfdfa sagrflvldr yardrlatad
       61 evlgfsvler fhdagadyse yaqlaflias laaadraedr fgmrpdvcag asfgqkaaaa
      121 yagsldfadv vrmtaelarc ekeyfstehs dvvthsvyrv pdeefhalld dmrargewfd
      181 isgvlergfy mvslresrle dfiravrdlg gyslytmrpp vhagafgalr rkaeaeviak
      241 yriraprlpv isdadgtvvd saeamrtmll dtfdrairwp dmvtsmtglg veslyvtgad
      301 dmfhrlnctv rnfdvitvnp knalrpgppk lraraa
//
LOCUS       WP_457687922             632 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457687922
VERSION     WP_457687922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 632)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..632
                     /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=69373
     Region          378..628
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfgrhlwapl rglalfglgl tagpmlaavg lgtlfgiqal aqwyrdplnv yrtlasrwcg
       61 vdipvpyqpp ppppepehdg wyryknrlyl tpkklsyerr wdwlvkdpat srdilwmlin
      121 pfvgsvtall pltlvvvgtt fpwswpghpg itvpitvata lagfgfgpvl lhlhgrwtcq
      181 llaaatdsgi rraliwigrg glatwrlalt aglavaelaa almhllamvp illwawptvl
      241 vagrqltswr rhqiqewtgi ridrpylpep alppprpdgt yqigrtlhrt pemalrslry
      301 rqnardlatw rdllwllldp vvgvllaalp vvvtgycffg liwswawasl lqpfvdfhtf
      361 eswpliihvi pvigdypiat apligvigtl igsllaipll rlhglwswll lgptksallg
      421 rrvdqltetr tearetlsse lrrierdlhd gaqaqwvamg mklgaieali erdpasakmm
      481 vgtareasak alielrhlir ginppvlaer giadairgla ldsplsvglr idlpgrperp
      541 vesaayfavs elltnvskha dadrvridvr htaqhlriai tdngaggadp akgsglrgvq
      601 rrlatfdgsl avhsplggpt tvtleipcvl ss
//
LOCUS       WP_457687930             250 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457687930
VERSION     WP_457687930.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26991
     Region          3..>103
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          4..245
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 matfvlvpga wlgawaweat aqalrerghv alpmtltglg ersglatpev gldthiddit
       61 afvverdlhe vtlvahsyaa vpvtgaagrl gprlerlvyv dsapfaegtc lldvmsddvv
      121 dqlhqqvaeh gdgwrlplpp fellsefstl egldedqldl mrnratpqpf rtfaqrltrp
      181 ddlgpdvdhv vvachdakal ldagvptlaf lnqppwrrfh lstghwpmls tpvelattld
      241 avassggsgr
//
LOCUS       WP_457687932             320 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457687932
VERSION     WP_457687932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /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=34826
     Region          3..312
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrvlallel lqthpgltga qlsdrlgtdv rtvrryaarl relgipvesd rgrfggyrla
       61 rgyrmpplml tneealvvml gllagerlgm gttapagaga lakiervlpd plraplaamr
      121 dtlsfttntv laqapeagvl ltlaqacrsg htvglryrsw hqehterdvd pygvvfhsgc
      181 wylvghdhlr dglrtfridr itsattgaat ftapddfdpv thltaslart papwqvevli
      241 egpiediarr lprttvtlta tptgvlmraq aaqldsvarl laslewpfti hspdqlrqsl
      301 kdlarqltaa aerplgdtpk
//
LOCUS       WP_457687934             338 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457687934
VERSION     WP_457687934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 338)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36887
     Region          260..332
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrirftled lartrvallg plaetqlslr mlqrreekvl fdgwrrrtrp rvppdarqla
       61 afvaspqgwm vdlftllgpv ssieegrerl lsapraqlra elspdarldr lrpswlshpg
      121 agdgavverl angladhhaa svapywdrih qhlsahahlv gklmaahgvg aaleslapyl
      181 rwkppvlelp dyrpwqgpdd yryhlggrgm vlapslfcgp vpqlfapatd aealliypap
      241 rdpatirsiw sppwpgashk alaallgttr aailatlvdg ytttdlarrl sispssasqh
      301 tgvlrqaglv sttrhrntvh htitpqgral ldgtsatp
//
LOCUS       WP_457687941             358 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457687941
VERSION     WP_457687941.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36902
     Region          63..348
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mstatgtpta sadttaspat taspiadrda attaataada lrgatttaap targrargwq
       61 frfavlslvw gfsflfikvg tqgfaplqvt lgrvafgalv llavlvvkre rlprsartwa
      121 hltvaaflln alpfslfaya eltipstlag icnatsplwg malsvvalse drptrrrvag
      181 lglgflgvlt vlgtwqgfag tdltgtvmal gaslcypigw iyvrrtlagv phshlsmsga
      241 qlllataqla vvtplfttap tsypiiplla vfalgalgtg lafliqyglv aeigpttaqm
      301 vtyfipviat aagvallheq lswntpvgal ivlagaaltq srprpsrpav pptgstth
//
LOCUS       WP_457687945             327 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457687945
VERSION     WP_457687945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32286
     Region          40..313
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mhatpssalp vgrgllyvtl aatawgtaga aaallyrgsg lgplaltfwr tfgglvllla
       61 vrallrrrsg tvavptpapy eplrrrlpri vmtgvalavf qaayfaavea tglavgtvvt
      121 mgagpvliai garvtmgerl gaggvlavag alaglavlvl ggdggttvrp agigyallsa
      181 agcaamtlit rrlgkgggsd pyastvsafa vgalcllpla vveglwpqah dlgrslwllv
      241 yiaavptala yglyfaglaa vraatasvis liepvsaaai avlflgerlt mataigtgvl
      301 ltavaalavt eargavtaar taapvag
//
LOCUS       WP_457687947             388 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457687947
VERSION     WP_457687947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38235
     Region          43..343
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mhassgspag tstgsgkgis gslggrqssp algarrlrvp ggrgaglgia llsalafggs
       61 gvaakplisa gleplqvtwl rvagaalvml piawrhrdlv rrrpallagy gllavagvqa
      121 cyfaalsrip vgvallieyl apalvlgwvr fvqkrsvtra aavgvvlavg glacvvevws
      181 glsfdavgla lalgaaccqv gyfvlsdhgs dgddavdplg viayglltga vlltviarpw
      241 gmdwavlggg admngtqvpa vlllawivli atvaayltgv vsirrlspqv agvvacleav
      301 iatvlawvll gehlsapqiv ggavvlagaf iaqsakpkat etvrvagagt gtgdgagapg
      361 gsgspetpat pasaprtgdd lsagscat
//
LOCUS       WP_457687966              91 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687966
VERSION     WP_457687966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..91
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9881
     Region          7..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mspslpdpvl hafgmhlrri redrgltlee ladhsglsfr gvvyiehgqr npslttlinl
       61 arglhvqpsr llavfdaeqg tfpeagspaq d
//
LOCUS       WP_457687994             551 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457687994
VERSION     WP_457687994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..551
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=60546
     Region          4..530
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mpetdptpta pggglvpapl sidgpyrsav rlgedtvlaa epgtedtarw lratlgaafg
       61 lplppgsgka tdalalaldp slppegyrla adarwgvrit gggpagvfwg aqtlrqllgp
      121 qafrraplap eraavlpqqt iddgprfawr gmlldvarhf lpkdgvlryl dllaahklnv
      181 lhlhltddqg wrieirrypk ltevgawrer tklghraspl wderphggyy tqddireivs
      241 yaaqrhitvv peidipghsq aaiaaypelg ntdvidttsl kvwdtwgvnp nvlaptdntl
      301 rfyehvleev lglfpspfvh iggdecpkdq wrasataqar iaelspaged elqswfirhf
      361 drwladrgrr ligwdeileg glaegaavss wrgyaggiaa aksghdvvmc peqqvyldhr
      421 qdpspdepvp igfvrtledv yrfepvppel tadqaahvlg tqanvwteam dsqqrldyqv
      481 fprlaafaev awsrlpapad rdyqdftrrm aahytrldal gvdyrppggp lpwqkrpgvl
      541 grpidgappn v
//
LOCUS       WP_457687996             283 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457687996
VERSION     WP_457687996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30100
     Region          <1..151
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          <80..>179
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 menptakpea grsphlpapt vaacrsphsg ghagqrppfp srssprfspr apqrrppygp
       61 pvsnrtpthc gtpaspacrp dwkhptgyap sndgrritlr qllrhtsglp dylkdvvpep
      121 gaagyrhhrw ttytpgqrva lalrhppasp pgtrweysnt nyllagmvik avtgrswerd
      181 dhgappgtra glglvwtpls cgggywghag tgfgyvmwpa vtpdgrttlt vsthsrpgdn
      241 dtavrqirgv tdladhalca aqdgrdgpfg grgpggppvh pgr
//
LOCUS       WP_457687998             858 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces nigrescens].
ACCESSION   WP_457687998
VERSION     WP_457687998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..858
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92194
     Region          16..843
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 maahnathap dhasdsvrdr eieaeqthld rvyrrleeki heaeflmdda akrgqvgtpg
       61 alaerdaqvf qagvhlhrln seyedflfgr idlllgkdgk kgpdgaftsv epadgaiedg
      121 ratiaetlhi grlgvldady splvidwrap aaapfyratp vapgrvvrrr virskgrkvl
      181 gveddlmrpe vtatldgael paigdgalma algrarshtm rdivasiqae qdkvirapaa
      241 svteveggpg tgktavalhr aayllyqdrr ryaggilivs ptpllvayte gvlpslgeeg
      301 qvairalgsl vdgaeatayd ppavsrikgs srmqkllrka argalelaap gaphtgreaa
      361 taaangsngg gapdgdaqls ledlfeasgd dserdaaang srrrrhrapr paqpaagppa
      421 hlrvvafggr ieldadelra irqsalggta pvnllrprar rlildalwtk sgaarrytdp
      481 elaaearegf dedittepdf qefldawwpe ltprgvlaam aderllgrwa rrllnprevr
      541 qlarslqrld rgghgplsvh dvalldelqm vlgapmrppr preadpldhl tgleelttha
      601 drmgggrsrr erleeertdy ahvivdeaqd ltpmqwrmvg rrgrhatwtv vgdpaqssws
      661 dpdeaavard ealgtrprrr ftltvnyrnp aeiaelaarv lalampgmas pkavrstglq
      721 prfalvadgn gtgtgngngr arsgddtala qatvaeaerl lgevdgtvgv vvamnrraqa
      781 rrwlaplgdr vvalgsleak gleydatlvv spaeiadesp aglrvlyval tratqqltvl
      841 saerdepdaa gvpdllrd
//
LOCUS       WP_457688000             246 aa            linear   BCT 27-JAN-2026
DEFINITION  anti-sigma factor family protein [Streptomyces nigrescens].
ACCESSION   WP_457688000
VERSION     WP_457688000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25707
     Region          5..>109
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mipptqpdrh sdvgayalgv ldaadterfe ahlvgcdrca aeleelmalt pvlaefkqsa
       61 ptpqtitavp gprvldglld evhatrrgrg rrrlflvaaa vvlivggpla tfslkgegde
      121 aptpplanav raqyaagekv tstdpdtkvs agvsmaarpw gtqvvlelan vkgplscdlv
      181 avgkdgkrqt ittwavpkgg ygipgsaakw nreplyatgg aalnrgdidh feintldgkr
      241 latvka
//
LOCUS       WP_457688004             405 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457688004
VERSION     WP_457688004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41671
     Region          68..386
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 msgpcsydrp rrirrgaalt lflasvlatg vvtgtwsdea egaagrtape hrssgahtra
       61 sladraaver aaseavedgk sgaqaaaevv srsgdrwsti ytpgeyedfq eqlgggyvgv
      121 glwvrqaagg rivvsrvqpg gpaeragiav gdrlravdgr ttrgapvtdv varlrgnapd
      181 gsrgpaaaag tpvtldlqrg drrwtetlhr arvkvrnvvv drpagdrgpt rvkitaftkg
      241 tgdavrravr qaspdegmll dlrgntgglv teavatasaf ldgglvatyd vrgsqralya
      301 erggnthvpl vvlvdggtms aaellagalq drgravvvgs ptfgkgavqm pselpdgsva
      361 eltvghyrtp sgrtvddtgl tpdlvvgnga ekrartvlsg lgggs
//
LOCUS       WP_457688008             417 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457688008
VERSION     WP_457688008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..417
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44003
     Region          14..393
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mfllpallll galvvypivf svhrslfdas gdgfvgldny gamfsdegir talrnnvvwv
       61 vvaptvstal glifavlter irwgtafkli vfmpmaisml aagiifrlvy dqapergvan
      121 avwvgvhdtf adpapfpgak prpradlkps gggafttgsa vrsgspvllp lvavqpgdlr
      181 garsaaaarp qpgritgtaw ldftrggggr pnavdgseka laglrveavr ggrvvasatt
      241 aadgtfalpa gkaegarlrl paanfaetyr gvdwlgpalv tpaiigsyvw mwagfamvli
      301 aaglaavpre lleaarvdga gewqvfrrit vpllapvlvv vlvtlminvl kifdlvyiia
      361 pgssirsanv lalqlfqssf gtdvdeglgs aiavfllllv lpvmyvnlrr lrkerrr
//
LOCUS       WP_457688010             318 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457688010
VERSION     WP_457688010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35056
     Region          51..172
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mtapiadqsa eqlprptrls evkgwfftad qllfdwflkr qqersepgdl lelgaymgks
       61 aiflgarrra gerftvcdlf dspaedssns qemkksyatl trrafeanyl afheelptiv
      121 qglssivgdh veegsvrfah idashlyehv hgdilavrel ltshgvvvmd dyraehcpgv
      181 aaatwqavan eglrpicitg tkfygtwgdp eplqqalvdw ikargdiwhe vqyvndaplv
      241 rlsakgakep ahpvsrytsg ggrslsrpsa rapkasaarp gpraplpars tlrrvaldvl
      301 ppvvtravvn arrrartr
//
LOCUS       WP_457688012             228 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457688012
VERSION     WP_457688012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23775
     Region          72..167
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpgrtdssaa tdspdagppg sdvrtarpap aagtapsast arlpaerrrg gparllpars
       61 pfrsqlrrig tgrvleigcg tgdtladcap gsvgvdhdpq svahcrqrgl taytadtfla
      121 spharpgafd alltahvleh lddeqvegll rayvpyvrsg ggvllitaqe aghragpapv
      181 rftdfpllra faesagltvr rtyshplprp agmllrsnvf vlvgqvpr
//
LOCUS       WP_457688013            1215 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457688013
VERSION     WP_457688013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1215
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=131300
     Region          2..>192
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          839..1213
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mkprltvvvp vhriegsern veeclesvaa qtlteldvvl vdgppaagra dagaaesapa
       61 alarrfaard prfrivhhsg dgpapgcgav rntgarhayp htdylaflda gedvllpray
      121 edlvglldrs gsdlatgnvy rlgaagrsqs ahhpagretv lrtrvgddlt llsdhvarnk
      181 vfrrtfwdrh gfafpegewc hdaavtlpaf flaeavdvlh ehvcyrrlpe gpdrhrrlda
      241 rgvrdrfaav agirrfladp ardrlsghrr dydraqlteg lldlvealpg aapecrtafl
      301 dcardflsgv dprlfptlpv elrmrwylir agrladllal lthearnpag ftvagpplrk
      361 ravlpltppl elppgvtrld radfpvvarv reavwrdgal vlrgyaylrn ldaaarhryl
      421 rtavlscgrr rillplrava mpeataesgq elhcydwsgf emrldparlr rgghweegdw
      481 tvgvllasag vvgsgalqap dtgsgaapra hdvagggadd gvritpwyag grlrlsvhrr
      541 trrlaghraa aagdldltvt vpgpppaalr lthqgtgtvv sfpvetappe epepgeagpg
      601 eagevsggay gapssthtfr irldalaaar ptrdgaprai ppahtvswaa elvlpgggtd
      661 pvacapgltp vpyplphgre lvvaatpagh lvlddripqp yldrllwrtd gtlllsgglp
      721 aaaphatelv lkhgahaael afptthdegr fhgtlplgal pslagtlplr egrwtlhlre
      781 rgavgsplda pvrcapsvld glpacrtvrg kplaldrhrq dealvvagpa lpatdrgpyr
      841 rrmlreqhys lhrsrplrdt vlyssfggra ygdspravhe elvrrgmeve hlwavrdaqt
      901 avpetaravl vgsaewhgal ahsrwvvtnt hlprwftrrg gqriiqtwhg tplkrigadl
      961 agtlcaglah laprprvsrq wsvllspnah stpvlrsalg ysgrlletgl prtdalfapd
     1021 reltaaavre rlgiepgrkv vlyaptprdd laydaghhrl hlpldlelar relaedhvll
     1081 vrghpmvadr lpahhapfal dvsahpdate lllaadvlvt dysslaadfa ntgrpmlflt
     1141 pdlphyrdtl rgftldfear vpgpllsstg elvdalgdlt aiaaagaeay adfretfchr
     1201 ddggaagrva dlmer
//
LOCUS       WP_457688015             224 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457688015
VERSION     WP_457688015.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 224)
  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   3  (residues 1 to 224)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24049
     Region          9..195
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtepdflrtt rtfydavadd yaehfrdala arpldravla gfaelvrdad agpvadlgcg
       61 pgkvtahlag lglpvfgvdl spqmvalarr thpevryevg amtdldlpdg alggivayys
      121 iihtpqerlp elfaefhrll apgghalvaf qvgdeplhva epfghpvsld frrrrpdrva
      181 gllagaglev rtrllhepde glgestrqac liarkpagta drhv
//
LOCUS       WP_457688016             651 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457688016
VERSION     WP_457688016.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..651
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70652
     Region          19..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msvpddlaaa aptgtdapap tvsvivpvhn trryldrslg svfaqtldrr hieviavddg
       61 stdgsaewla eqarrhpqlt vlrqeasggp gkprnaglah asgdyvffld sddrldpqal
      121 fwltrtaqry gsdivygria gadgraapvd lrttsahvsv fdspvywsla ayklfrrsfl
      181 arhqlrfveg rllgedlpfg stallraevv svfaertcyy lhgrednsna srqetdwcey
      241 lgyigtvldp vaaavppgan rdklmvrhfh geilmpfgap ylardpagrt amaaaarplv
      301 eryltdrvla alpprlrlra hsiragldde ltavvradte nrpdpphldd dgrvyagypy
      361 frdprralpd tcydltdrvv lrqrlirqrw aggvlhlrgt aalpwlggdt veillrrggt
      421 thriparaad gawraavdpa taadgaplad gvwglkiavt ahgpggatgp avrreawlvp
      481 ederddeddt gfaprivgrg pagpavaalf rsrphghlhl dldrdgvrrp lggdlrgtad
      541 ctrsgratlt arltlpgcpv daelrlilyd atrtvalrtt veraagdryt vrsllrsgpt
      601 gtwrvalrvt agplrrelpv rtagrgadgr tpltltvpgg spagllrrar r
//
LOCUS       WP_457688018             796 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457688018
VERSION     WP_457688018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..796
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=88961
     Region          10..222
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          365..726
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 msetgvdagp rfsiivpvfr vqgflrecmd svltqeftdf eliaiddcsp drsgaildey
       61 aahddrvrvl hlpenaglgp arnaglarar gdyllfldsd dtlvpgalga laerlaatgt
      121 peilifdyar tywdgssrrn alsalldesg apsfplaerp rlldllqivw nkayrrdfve
      181 ehgfafpegy yedapwtfct litaqriavl drvclhyrqr rqggnilrtt srkhfdvfdq
      241 yarvfdylda hpelsrwrph mfrkmvdhyl tvldkpgrlp qhaqaeffhr aardyrlrlp
      301 agfvrpsgva ggkyallard aypalaglkv agkvqrtvrk hagkrvrqak rkamdlryqa
      361 llrqpldenl avysaywnrl pscnplavye kakelapdvh gvwvvkkqla dsvpagidhv
      421 vlnsprywev varakylvnn vnfadnvvkr egqihlqthh gtplksmgtd qkrypaaakg
      481 msfrkllara drwdfslsan rhtteqwerv ypcdfasvda gyprndvyyr ataqdvldir
      541 erlgiapgrt avlyaptmrd yqvgyvprld leklsrelgd tfvllvrthy fydrdpglqk
      601 lqergalidv sghpvveelc laadalvtdy ssimfdyanl drpiityadd wdtyvrsrgv
      661 tfdllsglpg dtpgviatte delieafrsg rwddeaatgl raafrarfcp wddghaaerv
      721 vrrvflgqea tpeplpqder tiapspraaa aatgllklpa prtaahddvt psgtsgtsgt
      781 sgtsgtsgts dvemag
//
LOCUS       WP_457688022             408 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688022
VERSION     WP_457688022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44757
     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 mtavtqpaal pppvtglsrd darrialraq gllgapdrra gvrgvlrhlg avqldtisvl
       61 arshelvpya rlgavgrpav eaaywataps gapaarphsf eywshaacil pieewphfaf
      121 rrrawrargh rwhvmedser scaavldrlt adgplttsdl gggrkggeww dwsetkiave
      181 wlldtgqvvc tqrrawkrvy dlaeravpda llhddlddae clrrlvaqag aamgvatrad
      241 ladyhrlkae qvdavvadsg lvpvevegwg kpawadpaal aapprgrhrt tllspfdsli
      301 wdrprterif gfthrleayv prpkrihgyf ampllaggrl vgrvdpareg ttlvarqvsm
      361 qgpkavapma qalreaatwv gcdsvrverc ddrkladalr selthmsd
//
LOCUS       WP_457688034             550 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457688034
VERSION     WP_457688034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..550
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59616
     Region          19..223
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkealeplpg ptitpsaqvs ivviafndag hvgdavrsal aqgapgetvt eviavndast
       61 dgtgaaldal ahdeprlrvi hrdtnsggcg tprneglraa tgrfvmflds ddvlppgaar
      121 allaaalehd apvvagacvr relpahrdvp wqpglyrepa vhdspdaspq lvrdtlcvnk
      181 lyerafldkh aitfpegrft yedfvftarv laaaprvati pdhvyvwhvr rsaarqsisl
      241 drkdvanwqa riaahrasvq ifqeaghkal ahaastkfld hdlrmyvrel htrgadyrge
      301 wwrltrdyla gfdeadlraa raparwlarv vlaspaprdl grltqlaarp grllppyaea
      361 ggravwsqdl peveldaigt kpmhrlpvti daepalsspg vlrlrvhdly grlaaagpes
      421 idielrrrrd drrgpvhtaa ltpapaagas eacwtaevvl dlgalvergg phradpepwd
      481 lmaqvscadg agfraalrai gpglrrrvlp srrhllllvq pyattggals lrvasglrsv
      541 wrigarrlrr
//
LOCUS       WP_457688039             278 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457688039
VERSION     WP_457688039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29466
     Region          10..207
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mmncgrdpav hargltvvrg grtvldalaf dvprgrvtgl lgpsgcgkst lmraiagtqa
       61 kvtgtldvlg hpagdlrlra rigyvtqdps vyddltvrqn ldyfaavlhp grsargrrre
      121 svtraiedvd ltrhagalag nlsggqrsra slavallgap ellvldeptv gldpvlrrdl
      181 whlfhtlaad rgttllvssh vmdeaerchr llllregrll aggtsttesg gdtpdalrdr
      241 tgsdtveaaf lhlvdeaeaa atrppepahp ttpqepar
//
LOCUS       WP_457688038             286 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457688038
VERSION     WP_457688038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 286)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30033
     Region          93..267
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtttphtega phnegapete gapqavgape tvgaphptpa pfspsralat aarvlrqlrh
       61 dprtialmlv vpcvmiallr yvfdarpetf dsigasllgi fpmitmflvt siatlrerts
      121 gtlerllamp lgkaelisgy alafgllaiv qsalatglsl wllgldvtgs pwllllvavl
      181 dallgtalgl fvsafaasef qavqfmpavl mpqlllcglf tprdtmqpal ealsaalpms
      241 yavdgmnevl ahpditgdfv rdtvivtaca llvlalgaat lrrrtk
//
LOCUS       WP_457688041             467 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457688041
VERSION     WP_457688041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..467
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52033
     Region          51..458
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(161,163..164,297..301,316,319..320,323,338,342,397)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mnrrpirscg ataalsvall lssctssgar gvagsggvgd plfpalgngg yqvrhygldl
       61 dydikkrhld ataeitaeat adlrsfqldl qglrvtdvqv dgedaefsrk ghkvivrpde
      121 slrkgaefrt ridyegtpqe lkdpdksteg wvktrdgafv vgqpagsmtw fpgnnhprdk
      181 atydftltvp kgytavange lrsertakgr ttfrwhngrp masylatati grfevhtsrt
      241 peglplyvav dpaeakaskg pleklpeivk wesklfgpyp fssagaivdd tpkritwial
      301 esqtkpvyag apdtativhe mahqwfgdsv tpktwadtwl nesfatyaew lweereggkt
      361 pqeqfdalyd dtkdpkrwaf ppgkpgkakn vtgtpvyerg amllqelrna vgdkafftil
      421 rewpteyryr nadaqdfidf cqehtdedle plfkkwlyek gkpered
//
LOCUS       WP_457688048             390 aa            linear   BCT 27-JAN-2026
DEFINITION  RICIN domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457688048
VERSION     WP_457688048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42554
     Region          52..176
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(55..57,72,74,83..84)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mrflliafaa maftagmmsp lgavqaraad gecttelecl vayskleapn wrvldigrgw
       61 ggdgmaalgs ayvypkngng sdnqrfqfrn tgdgsfqmvv rdskkcvsrd spiqlrevdc
      121 annedqkwyl qpspsggfmi rsvkddmcln argghsgqnf vyhsnqvttn tcaqgdqasf
      181 fsiqdmslpe esghntqamr tlaaeyamtk cdkdksyckw ettqqgeavp gnpicrgnpv
      241 knsgtepatt kfvqsetsin setvggfiqn siesgvelsl gksdvaslki sqkfsrtwqs
      301 nyarttgeqk twsqevtpti pagqwawlee rpmtrkltgk fvfgmndwaq wefsgdsnnp
      361 mvanivlggd gsknnslwei ktgttppasc
//
LOCUS       WP_457688064            1080 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457688064
VERSION     WP_457688064.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1080
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=117555
     Region          273..1047
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mdpsavgvrl asgvvaplvr klfvkegpga glvakpvris glvsfkgerr tlsdkdlrkl
       61 aaelvdravr tagpgerpla adeeravaea lattlhglgd ldmddvqavr lgatalaarl
      121 eaarphavhg lsrdaellha tllgtaclhi vhfftqrsaf vartlvqqsr sldslitlid
      181 eflerhpspr aadaafergy layiarkhgr ltiygidlah spdrwpldaa ymsleatapa
      241 arevtavgpf dgvggpggap papvpvpadq alagrdrvll rgvagsgkst lvqwlavsct
      301 kapdetalph lygripfvlp lrtlardgap lptpdrflas vgcpvsgsqp dgwadrvlts
      361 gralllidgl deipdrerel trrwlrdltd afpdnlwlvt srpsavrddw ltadgfgelt
      421 lsamsraeva afigrwhdaa rcdaeeperl dayeqsllaa vhtkqdlarl atnplmcgli
      481 calhrdrrgy lptgrkelyd aalgmllsrr drerdmaapt gielsdepqi qllqrlaywl
      541 irngrseldr eraerilgea lpavpaaaeq gdataifrhl llrsgllrep apgavdfvhr
      601 tfqdylgaka avedgdfgll vahaedsqwe dvirmavaha rprerveilr glmergdgie
      661 grrarlrvhl lamaclehat eidprvrdev teragailpp rnheesqlla gvgplvlell
      721 pgpegladde aqevvataal igsdaalevm krfrdhpaig artqlasswp qfdtatyare
      781 ilqhldaevt vtatshaelh alralgrprv svsgpflaae llgalplgli esldirknpe
      841 iadlaflref pslkrlslwd cpavesvtpl adlqlrtlsi tgpldknvpi prglhrlrha
      901 rtlqlhstlp peglatlpad aplshlalsr pvgaeftdit cwpqmriiql rflthdfgad
      961 qwsalaslse ledfsfgvae egvtlqlpag lrlpqvtrlg vlntkrlpis dmsrllrsal
     1021 pafpgvrnlq lygfidgsid lspvaalpel qevflsylrp epghtlpphi kltryprprt
//
LOCUS       WP_457688071             401 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457688071
VERSION     WP_457688071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /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=43618
     Region          138..400
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mqrlydflrr hptgvdtfwa vpllgisslw vgsriegyqq piaaiftigl clvvalrrka
       61 pvkmllltaa igvgqlvfri etypgdaamf aitytvasgp tvprwasrca lagavfgpal
      121 sfwrfrdeeg sqsvgeslfv tvlltvpfvl awvlgdsmrt rraywaqlee raarlekere
      181 aqsriavaae rariarelhd vvahnvsvmv vqadgaayvl daapeqtrqa letisgtgrq
      241 alaemrrllg vlrtgeqpeg geyvpqpgve qltdlmdqvr saglpvdfrt egeprelpss
      301 valtvyrivq ealtntrkhg gpdvcatvrl syreddldll veddgrgaqr elyedggedg
      361 lghgligmre rvgmvggtlt agprpgggfr vsavlplkpa r
//
LOCUS       WP_457688074             316 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688074
VERSION     WP_457688074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 316)
  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 10194457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33217
     Region          42..309
                     /region_name="PBP2_ProX_like"
                     /note="Bacterial substrate-binding protein ProX of
                     ABC-type osmoregulated transporter and its related
                     proteins; the type 2 periplasmic-binding protein fold;
                     cd13606"
                     /db_xref="CDD:270324"
     Site            order(47,49,95..96,99,147,149,230,254)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270324"
ORIGIN      
        1 mssrsrvart avaagavitl aaglaacggk sleekgggkg elvigsagft eskvlaeiys
       61 rvladagyrt rvqtlanrel yepalekgqi dvvpeyastl aeflnakkng skakpvassd
      121 idktvtalek lasprglkvl pagratdqna favskefaae nklktlsdlg askqkiklas
      181 geecetrvfc kpglektygi ditaldpkgv gtpqakqavk dgtdqlvltt ttdatldnfg
      241 lvllkddkkl qnadnvlpvv naksagdkei aaalgkltra lttedlitln rkvdaerlkp
      301 tdvaqayles kelvkk
//
LOCUS       WP_457688077             244 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457688077
VERSION     WP_457688077.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25044
     Region          20..199
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mrgsaagpsc letndwvcge ylrtrsqelv datvqhlgit avsvaiglli afplalvarr
       61 wrgaagpvlg lttvlytips lamfalltpv fgvsaavvvt glvlysltil vrnilaglqa
      121 vpaevreaar gmgygparll cevevplalp alvaglriat vstvamttig svvgygglgn
      181 liasgmagff kaevltasvl cvllalladl llmglqrllt pwtraqgraa ararrgarva
      241 kagg
//
LOCUS       WP_457688078             412 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457688078
VERSION     WP_457688078.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43685
     Region          1..296
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
     Region          258..371
                     /region_name="CBS_pair_SF"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains superfamily; cl15354"
                     /db_xref="CDD:449531"
     Region          258..330
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341358"
     Site            order(282,294,319..320,323,335,357..359)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341358"
     Region          335..371
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341358"
ORIGIN      
        1 mirfehvtks ypdgttavdd ltfevaegel vtlvgpsgcg ktttmkmvnr lieptsgril
       61 ldgedisgld pvqlrrrigy viqqvglfph ktvldntatv phllgrprre araraaelld
      121 lvgldpstyg drypeqlsgg qrqrvgvara laadppvllm depfgavdpv vrehlqnefl
      181 rlqstlrktv lfvthdieea vrlgdriavy gagrieqfdt patvlgapat pytaefvgad
      241 rglkrlsvtp vepgdleqpp vvrlddpadr aagrlsadga swavvldadg alhgwvpaaa
      301 ltgapaapad gtgpglkkra pqgatvrdha rrmdarlplg aplrqalstm lqhdagwvav
      361 qdgdrflgvl tparlhtalr rattadaanv ardevsldtv pgpgvpapgp ag
//
LOCUS       WP_457688083             381 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457688083
VERSION     WP_457688083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41134
     Region          43..371
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mraafrgarr vlsegvgret vrerldrlva dapaaydldg wtdlygnddg iigelerrta
       61 galgteaaaf fptgtmaqqv alrcwagrtg natvaghpls hmevherdaw avvsglrmvh
      121 ptsaprppta aeiydlpepf galalelplr dagfvlptwd eltatveaar dreavvhfdg
      181 arlwecgphf grtlpeiaal adsvhvsyyk slggisgaal agteefieea rawrhryggq
      241 lfqqwpaala alagldrelp rlpeyvahak avaraldegl aeagvpwfrv hpgvphthqf
      301 qvwlpyppel lneavlrqae etgtalfgnw yepgpagppg valteimvga salawtddai
      361 rsaagefvef vdfvnglrrv g
//
LOCUS       WP_457688087             306 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688087
VERSION     WP_457688087.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34028
     Region          14..304
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpvphaaqpv ldrirvgsap dswgvwfpdd dqqvpwqrfl devaeagyew ielgpygylp
       61 tdpavlreei trrslkvsag tiftslhhgp svwdktwahv sevatltqvm gaghlvvips
      121 fwrddktaee lepreltaeq wkhlttgmer lgkrvrdefg ldivvhphad thidteehve
      181 rfldatdsgl vnlcldtghy aycggdsvkl irtygerigy lhlkqvdpdi lgevvakgtp
      241 fgpavkqgvm cepplgvpal ppvleaaqel nvdlfaiveq dmypcppdqp fpiaertrrf
      301 lrscga
//
LOCUS       WP_457688092             122 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688092
VERSION     WP_457688092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..122
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12920
     Region          59..120
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mktnalshav krtavltata glltaglltg pasadspagg radtraacay yngnaltvyg
       61 qrggrvrqvq cllanrrylp wgdvtgyfgp ktraavkkfq srhhltadgk vgkktwyaly
      121 ha
//
LOCUS       WP_457688089             339 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457688089
VERSION     WP_457688089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36164
     Region          5..330
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtshetlgva vigtgrmgad hvrrinevis garvaavvdi daarvkhlad giegctpytd
       61 paaamddpgv davliaspgp aheatlldaf ardlpvlcek pltpdaasal rvleaeqslg
      121 hrrvqvgfmr rydadyralk slldqgtygr plmlhnkhrn agstpgftna mmindsvvhe
      181 idvtrwllge eitavralrp aptgnapegl sdpqlilfet aggqvvdtei fvncgfgyqv
      241 sceavceggt arigddhgvf sntagrwgga itpgfverfe eaydrqvqrw vnatrrgeie
      301 gpscwdgyaa aavceagvra qttgervave lierpalyg
//
LOCUS       WP_457688093             381 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688093
VERSION     WP_457688093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 381)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40628
     Region          36..379
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mersneradg rtdgradgrn gtrtgtrtst plgadrppti rgvaeragvs kslvslvlqg
       61 sprvsdgkrq avldaieelg yrpnaaarsl varrthtvgv llndmrnpwf vevldglnsl
      121 lqahglrmlm adgrldrrag qdfartfqel rvdglvvvgt lpdtdglaev aarlptviag
      181 nheprlphtd lvandderga rlatehligl ghrriahiag kglvgelrrr gfetamrahg
      241 laesavvasg dgteeggyra avrlltpppv tarpgdgpaa aqrptavfaf ndisgvgals
      301 aaqelglrtp adlslvgydn tylarirhlw lnsvnnashe vgrraarcll drmerpdapa
      361 gqqlvapele irgstapprp d
//
LOCUS       WP_457688098            1302 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457688098
VERSION     WP_457688098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1302)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 1302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 1302)
  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 1302)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1302
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=139511
     Region          13..595
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
     Region          729..1297
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 magtdterag warrltrdcw qyrkdvllal gsslagmavl alvplvpkli idevivrher
       61 algpwaallv aaavvvyvlt yirrfyggrl aldvqhdlrt rmfgaiarld grrqdelstg
      121 qvvgratsdl qliqsllfml pmmignvllf vislvvmavl splltvvala aapalwfiaq
      181 rsrarlfpat wyaqgqaaav agvvdgavsg vrvvkgfgqe eqetgklrev srrlfagrlr
      241 tvrlnarytp alqavpalgq vamlalggwm atqgqvtlgt fvafstylaq lvgpvrmlam
      301 mltvgqqara gvervyelid tepsiaerpd ahelpadapa tvefnrvtfg yaplhegade
      361 dadedagpar eappavrpvl edfslrieag etvavvgtsg sgkstvslll prfydvsagr
      421 vlvgghdvre ltleslraai glvpessflf sdsvrdniay ghpdatdaqv raaaraaqad
      481 gfiselpegy dtkvgeqglt lsggqrqrva larailtdpr llvlddatsa vdarveheih
      541 ealrgvmagr ttlliahras tlaladrvav ldggrlvdlg tqeeleercp lyrrlltdpe
      601 elggverdpa galagafdge faaggllerd paadtdgpeg vrddaaartg adgtitpelw
      661 vrreqeaeag gagmaaraav aagpgmgaam aglpatpell aqvaalppat dnpdvdedqa
      721 vrpersyglr rllhgfggpl afalalvavd alaglllpvl irqgidegvr rgaligvwta
      781 aaialvvvla qwaaqiggnr mtgrigervl yslrlkifaq lqrlgldyye reltgkimtr
      841 mttdvdalst flqtglvtal vsmltffgil vallaidlql alvvfatlpp livgtyffrk
      901 qsvkayelar erisvvngdl qesvsglriv qafrrerqga erfaarsddy rrarvrgqfl
      961 isvyfpfvql lssvaaalvl ivgagrvgse tltagalvay llyidlffap vqqlsqvfdg
     1021 yqqasvslgr iqellreptt tpaverprev palrgditfd dvhfhygede dpalagialt
     1081 ipagqtvafv getgagkstl vklvaryydp ssgavrvdga dlreldltgy rrrlgvvpqe
     1141 sylftgtvrd aiaygrpdat daeveaaara vgahamiatl dggylhevae rgrnlsagqr
     1201 qllalarael vdpdvlllde atasldlate avvnqatdrl vgrrttlvva hrlttaarad
     1261 rvvvldrgri vedgshaqll ardgryaelw rtftgeeeel aa
//
LOCUS       WP_457688119             394 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688119
VERSION     WP_457688119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43274
     Region          10..>67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpslhddhtg ariahtrkvr rltqreladl ahvsystltk veqgvlpasp svlgalarsl
       61 svpvteltgq pyleelrqdq ldglinpire alniydlgpd pevlprtvee laahadrlca
      121 mvratnikqv aaelpglihe atttahlhpt drnwrllast yrtaydvtak lgfsdlgmva
      181 ldrmgwsaer asdavlsgvr qymrgvaylr agdyrtgkrl vrlgltdldq aapgrvfdav
      241 tgqlhlgaav lagrdkdrdt aeghlgeaqr iaertgpaek vhwlsfgptn vgvhrvsvla
      301 eldlypeavq caqeiaipdg wppsrlahhh aevaralmwt grtdaafksl lkarkvapqq
      361 tryhpavret yagldsarrr mpetfgnygs wlrm
//
LOCUS       WP_457688141             288 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457688141
VERSION     WP_457688141.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=31008
     Region          2..272
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpevesl arfladhlag ravervypva vhalktydpp vtaleggace gvtrygkfld
       61 cqvgglhlvl hlaragwvrw sdklpavppr pgkgplalrv rlagadgagf dvteagsqkh
      121 lavyvvrdpr evpgvarlgp dplsadftpe afralleger rqikgvlrdq svlagignay
      181 sdeilhaarm spfklaakls eeeverlyav igatlqeave rsrglalkdl kaekksglrv
      241 hgrkgepcpv cgdtirevsf sdsalqycpt cqtggkplad rrlsrllk
//
LOCUS       WP_457688143             604 aa            linear   BCT 27-JAN-2026
DEFINITION  choline/carnitine O-acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457688143
VERSION     WP_457688143.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   van der Hoek,M.D., Madsen,O., Keijer,J. and van der Leij,F.R.
  TITLE     Evolutionary analysis of the carnitine- and choline
            acyltransferases suggests distinct evolution of CPT2 versus CPT1
            and related variants
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (8), 909-918 (2018)
   PUBMED   29730527
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10466051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="choline/carnitine O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65554
     Region          14..588
                     /region_name="Carn_acyltransf"
                     /note="Choline/Carnitine o-acyltransferase; pfam00755"
                     /db_xref="CDD:459926"
ORIGIN      
        1 mttfaqedsl prvplptlea scerfldwca plltaderaa teaevaaflr pggpgrvlqs
       61 aleeydateg vhswldtfwp yrylgrrdri alnanffflf qdpapgqpqs qveraaglia
      121 gavdykrqld qelippvvqr gvpqsmvqnk ylfsatripg aqqdtvrspy tdawpgpsga
      181 rhivvfhrgt mfrmevlgad gvphslddle aglravqkag aepaaagtsv ghlttmaraq
      241 wadareslra hhprnadald dietalfcvc ledsapadtq eacdqllygd rgnrwfdkav
      301 slivfadgra ginvehceld gttilsftda llstpaeehs hrsgarsqgl palepvvfel
      361 ddalraqvrs aadafaeyga atatrtvafd dfgsttakal gaspdafvql ayqlahqrak
      421 ghlgatyesi atrqwrrgrt eamrvvtpei qafvaamedp aasadarraa fraaagkhvt
      481 rakecqagea peqhlwelel iqrrrgaelg vteqpalyrt pgwltmrddy lstssapsah
      541 iqyfgfgsts srcigvayvl lpdsfhvyls tpqavagpmq vfadrlreav aelrellasd
      601 gsgg
//
LOCUS       WP_457688151             237 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457688151
VERSION     WP_457688151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24075
     Region          20..>154
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mfdqldqlta plqgmlgspw lwlvvllvsg ldallpfmps ettvvlvavl igpdpsllal
       61 lagvaaagal agdclgyavg ryagprasar llrgergrar hlrarakver naalliiagr
      121 fvpggrvvaa lstgsvrfpl rrfvvldavg agiwalgsaa lgglggaalt dspakgmllv
      181 sgiglvaacg agylhrrgat adrgtpkrcg pragaasgra gerlparpgl rrrqegv
//
LOCUS       WP_457688153             295 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688153
VERSION     WP_457688153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30818
     Region          30..238
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mngpfdvrsd ctpdcaahal prvpathiar rgaafarsvr raltdgarma epgrlrthar
       61 alldalgihv egaapltvgd gpgtlvvvnh vswldilall svepvtllak revggwpvvg
      121 glarragthf idrthprrlp htvrevsell gagrsvavfp qattwctaea gtfrratfqa
      181 aidagapvrp vtldytqqgl pstvaafcge dtfagslrrv laaraltvrv tahpaltpwd
      241 ggldrrelae laaraalrgr pvtaatgsga prpaaalrpa apvphapprd apahv
//
LOCUS       WP_457688156             304 aa            linear   BCT 27-JAN-2026
DEFINITION  metal-dependent hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457688156
VERSION     WP_457688156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10562449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="metal-dependent hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33955
     Region          20..278
                     /region_name="Metal_hydrol"
                     /note="Predicted metal-dependent hydrolase; pfam10118"
                     /db_xref="CDD:431068"
ORIGIN      
        1 msntaslrpq paasehtplk arnvafdwad tplhwipgdp fsthtinvlh lllpagerwf
       61 vhvykqvlpy irdprlredv igfigqeamh sqahdevlph lkeqgldpap ytaqvdwlfe
      121 kllgdrtlpp grarrwwlle rvaliaaieh ytaflgdwvl naraldakga dptmldllrw
      181 hgaeevehrs vafdlfihld ggyrrrvrtw ataftalvfl wqrgtrffma ndpsladgka
      241 sfpefvragr rgtlpttgam arsipqylsr tyhpsqhgst eqavaylaas paataaeart
      301 tgga
//
LOCUS       WP_457688158            1042 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-N-acetylglucosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457688158
VERSION     WP_457688158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10585580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1042
                     /product="alpha-N-acetylglucosaminidase"
                     /EC_number="3.2.1.50"
                     /GO_function="GO:0004561 - alpha-N-acetylglucosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0030200 - heparan sulfate proteoglycan
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=111692
     Region          53..114
                     /region_name="NAGLU_N"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) N-terminal
                     domain; pfam12971"
                     /db_xref="CDD:463762"
     Region          135..455
                     /region_name="NAGLU"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel
                     domain; pfam05089"
                     /db_xref="CDD:461545"
     Region          463..723
                     /region_name="NAGLU_C"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) C-terminal
                     domain; pfam12972"
                     /db_xref="CDD:463763"
ORIGIN      
        1 mlgtagaiga gaafggaapa aasgapsarr qerapaydta paraalarll prhadqfale
       61 pltpdgdgdr frvagrtgri tvsgttpavl ltgvnwylky tcrahlswag dqvelparlp
      121 apaapverat slphrfalnd thdgytapya dwprwerlid alalrgvnev lvtpgteavy
      181 hrlltgfgys daearswlpa pshqpwwllq nmsgyggpis peliakrael ghritgrlre
      241 lgmrpvlpgy fgtvpdgfaa rnpgartvpq gtwaglkrpd wldprtdaft avaaafyrhq
      301 eqllgpadhf kmdllheggd pgdvpvpdaa ravekalrta rpgatwvilg wqdnprrell
      361 davdhdrmli vdglsdldtv tdrerdwggv pyafgsipnf ggrttlgakt hiwaerftaw
      421 rdkpgsrlvg taympeaaer dpaacelfge lawrerpvdr eawfdgyadl rygapddhar
      481 aafaalrtst yaisskdgrp hdsvfaarpn laarsgtvya thtpafdpav fdtafaalla
      541 vrpalrgsda yrhdltdaar qalanrswql igqlqdayrr kdrdtfrals alwlrlmrls
      601 devtgahrqf llgpwladar amatgpeeea rlehsarali ttwadratad ggslanyanr
      661 dwhgligevh lpqwqaylde ladalaadrp pntfdwyate epwtrartsh plrpttdahr
      721 tarrvhdtla kapyqgtltv tadpaalppg gratvtaalr nvnglratgr vdfalagvaa
      781 tasgpvslps vppggtgrah wrvaappgpl etplrplpyd ltvdygpqga prvrtarhgt
      841 lfvagpldpa lrtvttnaav fgqlddrfai hgagadlwka taefgavyrp galtaggtvt
      901 vevtaqdptg pwaragivvr nrlapsapgs adalgflnls vtpangvvls ydangdgtld
      961 tyrrltgita pvllrltrgk dtagsgtytg acstddgatw reiatvtvpg aaarqdtglh
     1021 qsaansatgd ggtaafrrwk lv
//
LOCUS       WP_457688164             139 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Streptomyces nigrescens].
ACCESSION   WP_457688164
VERSION     WP_457688164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14797
     Region          46..137
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtglmvciav laaasafgvw hrrrngrltv rerddtarlg aaeigealge ratllqfssa
       61 fcqpcratrr tltevagmve gvahveidae dhldlvrqln vlrtptvlvl daqgaivrra
      121 sgqprkadvi aalgaavrd
//
LOCUS       WP_457688179             694 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457688179
VERSION     WP_457688179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..694
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72582
     Region          283..684
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 msgaavsgat vtenaggalr grlaglrerv aglvegrsad dptaadplrg lyvtpetarr
       61 laaqapaedt gtpytaggap tggpadeapg psdrsvalag rfglsaldlq illaalapdv
      121 drsfeplygy lnddvgrrra tvalaldlag tgpyeagara rfhpgaplls ggllvieded
      181 rplpgralrv pervvahllg degldpelsg gevellsagq raagdmgsaa rtddasfagr
      241 laalagerpl avhlrerrpg taaepvtdrl rraglpvlry rpdghhgdga glagallrea
      301 rlrgaavvvg plperpgalv ralaggdvpv vffgsepydp dwapdsglfa ldapddgaaa
      361 devwstelgs vdegfdlaaa vapyrlgaaq irraaraata laafdgtpvt aahiqhsarq
      421 qsaplldrha rrvrpavgfd glvlppepls llhelvqrar hrekvlgtwr lrtgggrgrg
      481 vvalfagesg tgktlsaevm agalgldlyv velssvvdky igeteknler ifseadrtda
      541 vllfdeadav fgkrsevkss hdryanlesa yllqrleafd giavlttnlr anideaftrr
      601 ldlvvdfpfp ddgrrlalwr sclaatpcad dlgldvcake felsggairs aavtagylaa
      661 grggpvtaad vragarreyr kmgrlvpdas plwd
//
LOCUS       WP_457688182             963 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688182
VERSION     WP_457688182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 963)
  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 963)
  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   3  (residues 1 to 963)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 963)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..963
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=101624
     Region          34..282
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          208..956
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 maggqgqgse ravrggadvl kgaegagspd rgdrlrfqll gpvrawrgdh plnpgppqqr
       61 avlavlllha grpvsvpqlv dalwgeqppp ravgtlrtyv srlrgllepd rrprqqahll
      121 vssgggyalr vpgealdasv feerlatarr lreaddtaga yeqlrgalal pagmalaglp
      181 gpyaqrqrnr ltelcvtaqe elfdcvvelg gqagaiaglr afaaehplre rtqallmral
      241 hragrqaeal avyaatrrtl daelgaepgr elralyeevc agsrgsgtgs rpgpgtgpvg
      301 dqarpdrdrt gdsrdhrphp prparstsri gppppvpaql ppdiadfagr aeavaqlapa
      361 lrgaagvrap vvatlsglgg vgktalavhv ahsvrahfpd gqlyvdlqgs glapedssav
      421 lthflhalgv aesavpdgpa qkaalyrsll adrevlvlld nardsaqvrp llpgapgcav
      481 lvtsrartla lpgadrvdve vmaegealgl lgaivgaerv aaepiaarel vavcdglpla
      541 vriaaarlts rpgwamaglv arlseerrld elrvgdlgve atfrvgyevl gpglahafra
      601 lalrgmpsfc rgaaaalldt tddeaeeave tlvdaglvel hgedryryhd lvglfarrlg
      661 erhdspcera aaqrrffdyv latvltavrl iephrvlpgl lrhpdspgrt ladadaaraw
      721 lhdahprlya avewalgaap gllgsavdll tawsqvlggt arhsaleplv rravdtarrh
      781 gddtatahal rllrvphhgt aphygtaphh gtgtyawaer apgeslrpah asagppvsal
      841 aerelavvpv ttdqeraapp lrtaapdgse yrlrqiryra rcalrrdgpp rqaaapcrqa
      901 rrrcrlraar drarlgpges ergpplptpa pppgrgcgcg sanmgecrgr psaatlpgsr
      961 evp
//
LOCUS       WP_457688186             525 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail sheath family protein [Streptomyces nigrescens].
ACCESSION   WP_457688186
VERSION     WP_457688186.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Bock,D., Medeiros,J.M., Tsao,H.F., Penz,T., Weiss,G.L.,
            Aistleitner,K., Horn,M. and Pilhofer,M.
  TITLE     In situ architecture, function, and evolution of a contractile
            injection system
  JOURNAL   Science 357 (6352), 713-717 (2017)
   PUBMED   28818949
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Ge,P., Scholl,D., Leiman,P.G., Yu,X., Miller,J.F. and Zhou,Z.H.
  TITLE     Atomic structures of a bactericidal contractile nanotube in its
            pre- and postcontraction states
  JOURNAL   Nat Struct Mol Biol 22 (5), 377-382 (2015)
   PUBMED   25822993
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..525
                     /product="phage tail sheath family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=56016
     Region          241..515
                     /region_name="COG3497"
                     /note="Phage tail sheath protein FI [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442720"
ORIGIN      
        1 mptylspgvy veevasgsrp iegvgtsvaa fvglaptgpl neptlvtnws qyvaafgeft
       61 dgyylahsvy gffnnggtaa yvvrvggtge gepqaaaapq tpraltagep talgafkvsa
      121 iaagsangga ltvevqdveg egsadrfklv vrdgdkvves fdvsakkssr nyvvaqvkqr
      181 skaiaieeav paaqvtkpda qavtlappap apaapagtga veqlasgqfi gdsadrtgfg
      241 glealdevnm vavpdlmaay qqglidleqv kavqlglish celmgdrmai ldpppalnar
      301 dirkwrqeia gydsryaaly ypwikafdpa sgqtriipps ghmagvwarn dsergvhkap
      361 aneivrgaid lelqitrgeq dllnpvgvnc irafpgrgir vwgartmasd pawrylnvrr
      421 yfnyleesil igtqwvvfep ndqalwarir rnisaflvne wrsgalfgqr pedafyvkcd
      481 tetnpvesvd vgrvvceigi apvkpaefvv frlaqfsggg gelee
//
LOCUS       WP_457688193             719 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457688193
VERSION     WP_457688193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..719
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=71016
     Region          26..300
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(26,50..51,84,89,94..97,109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(33..34,36..39,41,54,56,92,108..111,115,117,154,156,
                     158..159,161,182..183,186,208..211)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(33..34,36..39,41,54,56,92,108..111,115,156,158..159,
                     161,182..183)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(37,115,117,154,156,158,186,208..211)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(182..190,204..211)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mpgaaaasgp rrgkdadltg rllggryrvt drigrggmgv vcravdevlg revavkvlra
       61 ytdasapela dlrtrmqrea raaarirhsg vitvhdvide dgrpvivmel vdgpslddal
      121 eqqgpldpre iarigaevmd aldaahqagv lhrdvkpgnv lldrwghrpd rsgagggrvv
      181 ltdfgiasie apgdgatthl trsgelvgsl dylpperaqg qdptpasdiw slgmtlyaav
      241 egggapfrrt svwstltaiv tealpeprra gpltpvlhal maknpadrps aaqarsllaa
      301 vaegreptpl ptpgashspt vtdvraaapp aapgehgptv gvggpegaaa gpagaagpga
      361 tgsgaggagp tgpsptgptg pvnagaptag wpsgpgaqga patqptplsp papapvpapa
      421 paptppsapa ghptpppgaa gpypassaer dpgrdtghap erdtervpar grrrvlpava
      481 avlavlaagg gltyalvggg asetvadrgr qsappagtpg gpdsrgaaeg kaggeegdkg
      541 nakgsdkgkg ggksaspsas drpsegdgte dpkpggaggs pggqdgdsgg tqggtdggsg
      601 sdggqggasg gsggdsgsgg geptqgpsce sigggkancd vwrsansyta sfqqvgtlnm
      661 gtnyfycqsk lgrretygkw tnvwwaktdd dsgnsgvyis vvylkggand qpvpglptc
//
LOCUS       WP_457688196             344 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457688196
VERSION     WP_457688196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="trypsin-like serine 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=35633
     Region          135..343
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrrtvrgipa vhgipaphpa rrsraalgtl taagtllall lptgqagaap qpghhssatp
       61 qttlgafwta drmraaapld latptkrsap aavprsaplk vaptlprlpk agsllpgslp
      121 qaggpwtggg avvkttgrvf ftyqgrnasc sgdavtsgnk stvitaghcv klqgawhtnw
      181 vfvpgyhdgq apygkwpaak tlatpqwtas edinydvgaa vvapldgkkl tdvvggqgls
      241 fnsgynkamy afgfpaaapy dgskviycsg ntikdplfss dhglpcnmtg gssggpwfts
      301 fdektgtglq ssvnsfgyqf wpnnmfgpyf gddaknlynq aqts
//
LOCUS       WP_457688203             270 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457688203
VERSION     WP_457688203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29229
     Region          1..93
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(49,52,56..57,66,79,83,89,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrigelagli gvstravrhy hhlgllpepe rrangyrdyg lrdavalarv rrltelglgl
       61 devrdvladd agrelhevld eldadlarqe eelrarrarl aavrrqaeeh gglpaegpvs
      121 delaalfaem artsaarpgp esamaskere vlallesmgg eegnkrmlel igematapga
      181 iertyevygl ldalveagtd dprveeaara ladcipdavi aevdreqwer aagpgaevdg
      241 gflaayyghf apaqaravrr aiqlvaerar
//
LOCUS       WP_457688210             759 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457688210
VERSION     WP_457688210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..759
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78982
     Region          1..388
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
     Region          385..748
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(470,500,502,534,536,730..732,734,736)
                     /site_type="active"
                     /db_xref="CDD:173838"
ORIGIN      
        1 mgigitqdqr dlaeaaggwa aravppeavr klldtapart grpaywdqla aqgllglhlp
       61 eadgggggel ldlavvleel graafpgpcl pttlaaallh rggapalvra latgarigav
      121 algtgsltav espdgyvldg tappvlsgad adlivlaaev ageagltgea egaggakgaa
      181 dgagrdgggg rragetvwla vdagaltvrv qesadptrpt aevrahgvpv paerrlavds
      241 dlvrdlagvl waaescgtas walhtaaeha avreqfgrpi gqfqavkhlc admlvryeqa
      301 aalvwdaara lheppavrgl vaalatatal daavscakdc iqilggigft wehdahlhlr
      361 ratvarqllg sgdthrlraa ryaadgarrp lhlelpaeaa efraeartvi dgvrgldpaa
      421 vrrtlaptgy aaphlpapyg lgagpvqqla iqqelaaadv risdlgiatw vvpsliahgt
      481 peqqercllp slrgdllwcq lfsepeagsd laslrtraer tadggwring qkvwtsaaqw
      541 ashgillart dpdapkhkgl tfflvdmktp gidtrplkei tgeslfnevy fddvllpada
      601 vvgevdngwk varttldner vhmadqltfd tgltalldra aeldgsvrar vgalaaeaha
      661 lgciglrttl qqvsglepga gasirklvqt phqqkvaela lellgpdgav regageralh
      721 gflmsrclti aggttqvqln vvaerllglp rdpeprpli
//
LOCUS       WP_457688214             266 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457688214
VERSION     WP_457688214.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29069
     Region          15..239
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mtlhgslshd aycthlleet tkfretvrga dlsatvptcp dwtladlarh vggahrwvga
       61 ivatrtatdi deadipesdg pekddaaald awlaagvdqa vaalreagpd tevwtwspvq
      121 rtgfwarrmt hetvihrada altagaafdv ppevaadcle ewlqlcalpq vtahhaergq
      181 lfgpgrtlhl hatdtppeln aewlldltgd rpvhrrahek aavalrgplt dllgvmyrrl
      241 padsdrvevl geralldrwl ewasfq
//
LOCUS       WP_457688216             470 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457688216
VERSION     WP_457688216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49736
     Region          30..434
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtaeavqaaa prpaeaspas aptngerplr iamltykgnp fcggqgvyvr hlsrelarlg
       61 htvevigaqp ypvvddgvtl telpsldlyr qpdpfrtpkr geyrdwidal evgtmwtggf
      121 pepltfslra rrhlaarrgq fdvvhdnqtl gygllggpga lgaplvttih hpitvdrrld
      181 laaadgwkrr asvrrwygft rmqkrvarrl psvltvsgss rreivddlgv rpghihvvhi
      241 gadtdlfspd asvpevpgri vttssadvpl kglihlveal akvrtenpda hlvvvgkrad
      301 dgpvaaaier lglsgaiefv kgisdtelvd lvrsaqiacv pslyegfslp aaeamatgtp
      361 llattggaip evagpdgetc lavppgdaga laggllrllg deelrrrlga agrervlarf
      421 twrqaalgta eryreaialq rdrsgartlp raasagaagt apapsaaghv
//
LOCUS       WP_457688218             435 aa            linear   BCT 27-JAN-2026
DEFINITION  prenyltransferase/squalene oxidase repeat-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457688218
VERSION     WP_457688218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="prenyltransferase/squalene oxidase
                     repeat-containing protein"
                     /EC_number="5.-.-.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43368
     Region          <72..>185
                     /region_name="ISOPREN_C2_like"
                     /note="This group contains class II terpene cyclases,
                     protein prenyltransferases beta subunit, two broadly
                     specific proteinase inhibitors alpha2-macroglobulin (alpha
                     (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and
                     C5 components of vertebrate...; cl08267"
                     /db_xref="CDD:415487"
ORIGIN      
        1 mapmasmahq aplthpaafl arraatalaa avvlgtaaap aayadspsas pkklpdglyg
       61 tkdpkydgvw rqslallaqd avglrpaasa vrwlvgqqca dgaftafrae pgkpcdgktm
      121 rdtnqtaaav qalaalgghg dtvkkavgwl ksvqnedggw ssmagspsda nstsvvigal
      181 aaagekpqsv tskkgdktpy dglltfqlgc dakegergaf tfqlkgaapn adataaaatg
      241 algkgfvvap adqrakapvk plnckdagge kagkgdpaqa aeggdaflva qldkngqhll
      301 sampgaekqp dvgntadavv alaagghgaa aakplkwlek naaewaeqsg paayaqlvla
      361 ahatgtdprs fggtdlvaal natgpkpaaa pkkdagdsdd sadggaisvw wvigvglaig
      421 agigfllssr kknql
//
LOCUS       WP_457688229             438 aa            linear   BCT 27-JAN-2026
DEFINITION  multidrug effflux MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457688229
VERSION     WP_457688229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="multidrug effflux MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44980
     Region          43..417
                     /region_name="MFS_MdfA_MDR_like"
                     /note="Multidrug transporter MdfA and similar multidrug
                     resistance (MDR) transporters of the Major Facilitator
                     Superfamily; cd17320"
                     /db_xref="CDD:340878"
     Site            order(45..46,49..50,74,77..78,135,166,169..170,253,256,
                     378)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340878"
ORIGIN      
        1 mtepgaaetq dlppiaerga aaapaasrrt sllvtlvlgg ltavpplsmd mylpalpqvt
       61 aalhspaatv qltlttclag malgqmivgp msdkwgrrrp llagmviyvl atalcalats
      121 aelliafrll qglagaagiv iaravvrdly dgvamarffs tlmlisgvap vvapliggqi
      181 lrltdwrgvf vvltavgval tllvwrtlhe tlpperrhsg glgqtlrtmr dlladrvfsg
      241 yalvgafafa alfayisasp fvvqeiygas pqtfgllfgi nsvglvavgq ingkllvgrv
      301 gldkvlgtgl avialaatal llmsagvfgh vglvptaagl fvlmaamglv mpstntlall
      361 rtphaagsas allgtstfll gsvasplvgi agertavpma lvqlscavla lvsflgmcrp
      421 wqrrgesngs tagertrl
//
LOCUS       WP_457688231             409 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457688231
VERSION     WP_457688231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43499
     Region          86..>238
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlaalttapa laapaafttq raesgesvhs vaaprsgqgr gtllsltplg rqsraevigq
       61 aqkqgletgt arhgvaayrl tyrtitpdgr pttasgllal ptggdsrhlp pvvhthgtla
      121 yrgyapsmad gpdravsvly asagrvalap dylglgtspg rhpymdarss vsasldmlra
      181 ahsaapklga tldrtvsvtg fsqggqvama lgrelhrgad prfrlgmlap vggpydlvga
      241 elpgmfdgri dprsavfyls ffltaqnrlh plytdpaevf rapyadrved lfdsehpaed
      301 iagklperle dlltdtwyrk lrhpsgalle alrvnnrtcd wkpgrgvrit lysatgdrdv
      361 piantrscar qltghgvrak avdqgadadh yvsflrsqps iartlpvar
//
LOCUS       WP_457688247             292 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688247
VERSION     WP_457688247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /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]"
                     /calculated_mol_wt=31551
     Region          27..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myhtwmryft pslvhhrlgl vclgvglqhg tlptvgprtl dhhvalvisa grgwftapdg
       61 rrrpvtapal lwlvpgvphh ygadpetgwd esfvdftgpa aatytelgyi epdrplvpla
      121 dtgpartaig riaraarrgn pllevetsaa vhellvalrr aradtdadgd pvlqalarda
      181 flplsvaeha arhgmtpael rtavrrgagc spkdyllair lgrakellvg telpvsavar
      241 rvgyddpayf srlftrrvgt apvhfrnrqv hnvpggwstq ipdpddppvv sg
//
LOCUS       WP_457688248             595 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 35 protein [Streptomyces nigrescens].
ACCESSION   WP_457688248
VERSION     WP_457688248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..595
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64072
     Region          10..326
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtrfevgerd flldgrpvrl lsgalhyfrv heaqwdhrla mlramglncv etyvpwnlhe
       61 prpgefrdpe algrfldaar aaglwaivrp gpyicaewen ggmpewltgp lgrrvrtrda
      121 eylravdawf grllpqvvar qcdaggpvim vqaeneygsy gsdgaylawl vdrlralgvr
      181 vplctsdgpe dhmlsgggvp gvlatvnfgs garealaalr rhqaggplmc mefwcgwfth
      241 wgraqeprap eeaagalrei lecgasvniy mahggtsfgg waganragel qdgalrstvt
      301 sydygapvde rgrptekfwr frevlagyae gplppvpeap rvladpvrav vgewapaedv
      361 maalggaeve gggpatfeel gvdrgvvryr vavpgprgry plrvrglrdr avvcvdgelr
      421 avvdtedavv gevagpasve vwvaslgrvn ygprlgeskg ivggllherq flhgvrsrgl
      481 rldaleeaga larvpfrave gagggaglyr gtltvagrpg daglalpgwr hgfawingfc
      541 lgrywdegpq rtlyvpgpvl regvnellvw ewegapapvg eeagapglyp caagr
//
LOCUS       WP_457688263             337 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688263
VERSION     WP_457688263.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34209
     Region          18..335
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mspaphtpgq ppaptpltwl yvpgdrpevv akalgcgadv vvvdledava pdrkdhalra
       61 taellsgpvp vpvhvrvnal dgplaeneir tlaplpglag lrlpkvqgpa dvhraagwat
      121 taapvpehlp yaaegpvrpa ghavaghpap vrtppgatat lapaappaas alpatpalya
      181 llesalgieh afaiatahpa lrgialgead lcgelgvrdd aglawprsrt vvaaraagla
      241 pppqsvhpdv hdldglarsc argralgflg raaihprqlp vieaaylpsa eeiataeeiv
      301 raateeggal alpdgrfvda avvagarrvl dlagrrr
//
LOCUS       WP_457688265             328 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Streptomyces nigrescens].
ACCESSION   WP_457688265
VERSION     WP_457688265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34605
     Region          91..256
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msqknhegkk sarerlqeqr ekekararrg rqaivagavv avlavaggia vwassssgkp
       61 aandnevavp kqasggdrpa vpvgsadaps tltvwedfrc pacqqfetgf rpviheleds
      121 gqlkseyhlv tiidgnaggq gsrnaanaal caqdagkfra yhdllyshqp pepqdkfgdk
      181 kyllqlagkv kglvtpaftk cvndgtydrf vkksndafat sgyrgtptvl lngkdlskek
      241 ggqfgpadlk kmvldankak qpgnkqpgkk satphtgasp qdkhpgtpqd khpgtpqdkh
      301 pgtpqdkhpg rsaapqgelt grsgapas
//
LOCUS       WP_457688272             299 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457688272
VERSION     WP_457688272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32218
     Region          229..298
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mqrheytgpv alramqslag rlfpdtgyrh igdlawawcl aldrdsenpt avwtdgdgda
       61 paagsptahr plawawlelp gslqfqvdpa hpeladevla waagrtagga lsaevaetep
      121 hlraalerhg ltrtdggpfm vglgrsladl pdapplpdgy riraqqtrae vagraaahra
      181 afgstrvtte rharmrqiwp yraefdlvva spagdvaayc qgwydaalgt gvfepvgthp
      241 ehrrrglara vclavlrafa aaggrravvq crgdaeypvp krlydslgft pytrthaya
//
LOCUS       WP_457688290             329 aa            linear   BCT 27-JAN-2026
DEFINITION  MASE1 domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457688290
VERSION     WP_457688290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Pfiffer,V., Sarenko,O., Possling,A. and Hengge,R.
  TITLE     Genetic dissection of Escherichia coli's master diguanylate cyclase
            DgcE: Role of the N-terminal MASE1 domain and direct signal input
            from a GTPase partner system
  JOURNAL   PLoS Genet 15 (4), e1008059 (2019)
   PUBMED   31022167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Lacey,M., Agasing,A., Lowry,R. and Green,J.
  TITLE     Identification of the YfgF MASE1 domain as a modulator of bacterial
            responses to aspartate
  JOURNAL   Open Biol 3 (6), 130046 (2013)
   PUBMED   23740576
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Nikolskaya,A.N., Mulkidjanian,A.Y., Beech,I.B. and Galperin,M.Y.
  TITLE     MASE1 and MASE2: two novel integral membrane sensory domains
  JOURNAL   J Mol Microbiol Biotechnol 5 (1), 11-16 (2003)
   PUBMED   12673057
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /product="MASE1 domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34709
     Region          1..>309
                     /region_name="MASE1"
                     /note="Integral membrane sensor domain MASE1 [Signal
                     transduction mechanisms]; COG3447"
                     /db_xref="CDD:442670"
ORIGIN      
        1 mrrtewlgrh gataarilgv aavyyggakl gllqelvrgq vtplwpptgi altalllfgp
       61 rialgaflvn vslgpslsvv laivvgntlg pllsyrllrr agfrveldrl rdavalvflg
      121 altgmlvsav igsgvlvlsg alptgdfwpt wavwwtgdam gvlvitpvll llaaarrprw
      181 agvrplrwle aallaactct vtllavsspm nllylvspcl iwaafrfqra gaapcallvs
      241 tiaivaaage wgpfaghdll tnmatlqafn gitaltalll savvterrnt heeirrvcaq
      301 laealsrldp gaaaeqwppp rkqkpdggg
//
LOCUS       WP_457688298             287 aa            linear   BCT 27-JAN-2026
DEFINITION  5-oxoprolinase subunit C family protein [Streptomyces nigrescens].
ACCESSION   WP_457688298
VERSION     WP_457688298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="5-oxoprolinase subunit C family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29208
     Region          5..283
                     /region_name="PxpC"
                     /note="5-oxoprolinase subunit C/Allophanate hydrolase
                     subunit 2 [Amino acid transport and metabolism]; COG1984"
                     /db_xref="CDD:441587"
ORIGIN      
        1 mtdrafsvvr agalttvqdl grpghahlgv pragaldapa hrlanrlvgn pasaatlett
       61 ltgcalrvrt attvavtgap cpvtvdgrpa pwgapvrvpa gavldagpat hglrsylafa
      121 ggidtepvlg sraadllsgl gpdpltdsav lplgnphgpp agadavphhg pvpelvlpfl
      181 pgprdawftd tglhtlttgr frvspasnri glrtegpsle rarsgelpse gmplgalqvp
      241 pdglpvlflh dhpttggypv igvvpercla paaqavpgtp vrflrmr
//
LOCUS       WP_457688296             260 aa            linear   BCT 27-JAN-2026
DEFINITION  LamB/YcsF family protein [Streptomyces nigrescens].
ACCESSION   WP_457688296
VERSION     WP_457688296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Oke,M., Oni,O., Bello,R., Samuel-Omoyajowo,K. and Senbadejo,T.
  TITLE     Structure-function relationships of the 5-oxoprolinase subunit A:
            Guiding biological sciences students down the path less traveled
  JOURNAL   Biochem Mol Biol Educ 47 (6), 620-631 (2019)
   PUBMED   31520514
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="LamB/YcsF family protein"
                     /EC_number="3.5.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0017168 - 5-oxoprolinase
                     (ATP-hydrolyzing) activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27441
     Region          12..259
                     /region_name="PxpA"
                     /note="5-oxoprolinase subunit A [Amino acid transport and
                     metabolism]; COG1540"
                     /db_xref="CDD:441149"
ORIGIN      
        1 msersmgvpp vidlnadlge gfgrwqltdd eallsvvtsa nvacgfhagd patmrrvcel
       61 aaergvviga qvsyrdlagf grramdvppd elaaeiayqi galevfaraa garvgyvkph
      121 galynrcvhd aeqaravidg irtaggglpv lglpgsrlhe tarearlpvv geafadrayt
      181 pegtlvprre pgavihdpde vvkralgmar dhtvtardgr rvgitarslc lhgdtpgaad
      241 larrvrselt aagvhvrsfv
//
LOCUS       WP_457688309             310 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457688309
VERSION     WP_457688309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=31439
     Region          17..204
                     /region_name="SGNH_hydrolase_like_1"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01832"
                     /db_xref="CDD:238870"
     Site            order(23,185,188)
                     /site_type="active"
                     /db_xref="CDD:238870"
     Site            order(23,185,188)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238870"
     Site            order(23,64,93)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238870"
ORIGIN      
        1 mpaqapdggw saapgcfval gdslteglgd pvpgggwrgw aallaealge rpgsvplvnl
       61 arsgaqaadv aerqlpaara lgprfasllv gandtlraaf aieriaaald rahgalsadg
      121 avvltaclpd pgrmlglpap larplgrrmr avntvvhavs aryggvhlhl adhpwvadra
      181 swsvdrlhps ehghrllarg fhtalaatgl pvgpppaltl dgppptrags alwmatrgtr
      241 wvadrctdll pglvglafqe crhglagsgr lldaaadrat rsalaalgrt dgagagkdps
      301 mtkgaatmag
//
LOCUS       WP_457688303             801 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 31 protein [Streptomyces nigrescens].
ACCESSION   WP_457688303
VERSION     WP_457688303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 801)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11605349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..801
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86739
     Region          174..301
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            212
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          284..725
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
ORIGIN      
        1 mdgrdlvrsv rmiravgpaq glrsvrsawr awrtdaralp rrgaerarvp gpalraepqp
       61 gggvihfars slrvrvaagg avfcgwdgae pepsyalaga cpevdaravl epdteggwrv
      121 vservlvvvs rhgavevrtp ggavlrrelp prwwdragde gadertgrpe gcgvsrwvqr
      181 sevaadgrff glggrahgpr lrdgayrlwn tdpggafepg ddplsltmpv qlvvadagth
      241 lvfhdnswdg rvtlregaeg agsghdrpgt celrmdggpl rywvlagspa rvlqvwtalt
      301 gapalppqwa lgyqharwgf ggeaevrrvv agykerelpl savhldidhy drhrvftvdr
      361 qrypdlpgla relradgvrl vsivdpavka epgdivyegg vvadafvrda rgrevrgvvw
      421 pgesvypdft darvrkwwga lyaerlaqgf agvwhdmnep asfaafgert lprsarhale
      481 grggdhreah nvyglamara gfeglcelrp aerpflfsrs gwaglqrygg swsgdvatgw
      541 pglraslslv lglglcgvpy sgpdiggfsg vpcpelylrw fqlgaymplf rthsaigagr
      601 repweygsev lahartalre rqrllpyfgt lgqlarltga pyvrplwwsa ardralrdce
      661 dafllgdall vapvlaagvt rrpvrlprgr wydtatgray dgpgqvwvea plsripvlar
      721 agavlpvaga dggtelevwa pvagrggsgl vvpdagdgwq rptverftsr rsggrvvver
      781 rdggavgypv rvrgledgvg a
//
LOCUS       WP_457688324             371 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688324
VERSION     WP_457688324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40825
     Region          8..328
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msvtltgqdr pelqkaieei vdsgfagvql rvndergewv gsagvrklge rakpptngrf
       61 rigsttktft atvvlqlvae dkirldspad dylprfgldr ritvrmllqh tsglfnytge
      121 yyddgtvapg ipwqgqeyvd nqfhtyqpee lvrlalskpa rfepgtdwsy snsnyilakl
      181 lieevtgrsf aeemqrlilq plglsgtvvp gsspeipeph ahgyyryeha gqwkvvdvtr
      241 fnvswisaag dmisttedlq tffsalmsgk llpdhllaem rtphpklgyg lglfveetdg
      301 ggtifhhngg ffgwaalmys tpdgrktlta slttgdaeld faatadafqk ahqklvkevf
      361 cggktevaaa k
//
LOCUS       WP_457688334             342 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457688334
VERSION     WP_457688334.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36853
     Region          14..319
                     /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 mvvaedigvp swdlyelsip ctvfgkpqpd ladpwydlrl cstgereqds saagaglsmr
       61 tryglddlag adtvivpsvp dacvedgrpl ppalitalrh aydagarmvs lctgafalae
      121 aglldgrrat ahwmhtaqla erypkvdvdd svlyvddgdv ltsagltagl dlclhlvrrd
      181 lgahvanqla rrmvvpahrp ggqaqfidls vpttddgslg pvldwarrhl dqpltvedla
      241 qraamsprtl hrrlqavtgt tplqwllnqr lgraqnlles tdlpiekige lsglgtannl
      301 rhhflkqigv spsnyrrafp rtmpdsepsp slpesregag eg
//
LOCUS       WP_457688352             412 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457688352
VERSION     WP_457688352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=44038
     Region          97..370
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mdaqvtespe psrfagwaar paggpgaggp gpggtpphrr hlrrlaavgi tgvvlagagt
       61 gwavyaklns nirtdsater elrkweserp pagppnaanv lligsdsrng gngryghsrg
      121 qrsdttmllh laadrksata vsiprdlmve vphckrpdgt etapraaqfn gafaaggpac
      181 tirtvekmtg irvdhyliid fvgftkmvda vngvevclpr pvhdpeahla lpagrqtlhg
      241 eealgyvrar kslgngsdtq rmerqqrflg alvkkvqsng vllnptrlyp vldaatsslt
      301 tdtalaslkg lyelvrsarr iptdriqfmt vprreyrldp nrdelvqpda arlfgqlhrd
      361 lpvtvtpprd dgeervrtgn gssddrpgep papspssgpt fpgttaehgi ce
//
LOCUS       WP_457688349             297 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 900105755].
ACCESSION   WP_457688349
VERSION     WP_457688349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19790410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..297
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33480
     Region          147..284
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
     Region          230..294
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtdpvirtid dsthhlfdtl pdplrmrerh rtagfradwk rvalrdgrvv araawwgapg
       61 atepllinwf dvaegeeeag aellrsapwr veeleldlpt gwretpavrt aaetsfsaar
      121 kagfellver ynyrwtpeyg lperpgrlvf tpdpddgvff dalrrihsvt ldtharrave
      181 qggvdqaaqe emdffhwmps prewwqigrt pdgepvgihi pgrnpggpci gfigvlpeqr
      241 ghgyaydllv ectrflaeqg aefiaaatdq gntpmaahfa ragypvarer vnfwarr
//
LOCUS       WP_457688360             605 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457688360
VERSION     WP_457688360.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67251
     Region          20..600
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtapsdgtlp lsardavahl tpglwaranr llirkglaef aherlltpkr lpqdghyair
       61 sddgtteyrf aarrraldhw qidadsitrh rddselplda laffielres lglgdailpv
      121 yleeisstls gtayklaagr sgaaelakap fqaietgmte ghpcfvanng rlgfgiheyh
      181 ayapetaapl rliwlaarrd hatftagagl dydalirdel peetrtrfaa tlttlgldpa
      241 dyyffpahpw qwwnklsvtf aaevaqqhlv clgpgdddyl aqqsirtffn ttdpakhyvk
      301 talsvlnmgf mrglsasyme atpaindwla rlidaddtfr aarfsiirer aaigyhhrqy
      361 eaatakgspy rkmlaalwre spvptlepgq rlatmasllh vdhdggslaa alieesglep
      421 avwlrrylda yltpvvhafy aydlvfmphg enailviedg avarvifkdi aeeiavmdpd
      481 avlpptveri radvpedkkl lsvftdvfdc ffrflsstld dhgildedtf wrtvaacvtd
      541 yqtanphlad kfdrydlftd efalsclnrl qlrnnqemvd lqdpagalql igtlrnplap
      601 yapas
//
LOCUS       WP_457688363             509 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457688363
VERSION     WP_457688363.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 509)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=55420
     Region          27..494
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msllahsaed padnraylln ngtagryhsa vtesvtrisa kiagttrpft gitvdgltpt
       61 vsgvdldapl hdaaaaldel eevylrdavy fhhprylahl ncpvvipalv geavlsavns
      121 sldtwdqsag gtlierrlid wtaeriglge aadgiftsgg sqsnlqamll ardeacrrel
      181 tregatdarl tdvlprlril tsecshfsir ksatllgmga eaviavpsde nkrmrtdela
      241 aqlarcerdg lipmavvata gttdfgsidp lpeiaglcag ygawmhvdaa ygcgllvsrr
      301 rdllsgiera dsvtvdyhks ffqpvsssai lvrdratlkh vtyhadylnp rrmveqripn
      361 qvdksiqttr rfdalklwlt lrimgaqavg elfdevidra adawkllhdd prfdvvvepr
      421 lstlvfryvp ttdqdpelsd rvnlhareal fasgeaivas tvvdgchylk ftllnpettl
      481 ediatvldli aehagsflae qprpalsar
//
LOCUS       WP_457688365             296 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457688365
VERSION     WP_457688365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32333
     Region          12..280
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtttaapata pfrffdvhvv rarrvspsvv ritfggdrld elasggrdqr fklflpqphq
       61 drpvfhdmgd swyttwraqd paeravmrsy tireqrhdpr efdvdfalhg agpgadplag
      121 gpasrwaaha ragdrltvla pavednggvd frppagtdwi litgdetalp aiagilswls
      181 pgthakvwie iaheddrqql psfadaditw lvrdgstaar cepvldalra adlpegtpya
      241 wvagesgtvk avrrhlvrer gidrravkft gywrrgasee dllaeltaga passed
//
LOCUS       WP_457688367             286 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457688367
VERSION     WP_457688367.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30366
     Region          3..256
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msrltaenvt laydqrviae nlsvaipdhs ftvivgpnac gkstllrals rmlkpvkgsv
       61 lldgaaissl pakkvartlg llpqssiapd gitvsdlvar gryphqgllr qwspederiv
      121 eesmaatgvg eladryvdel sggqrqrvwi amalaqqtpl flldepttyl diqhqievld
      181 lcaelheeqg rtlvavlhdl nhaaryathl iamkdgavia egapadivta elveqvfglg
      241 cqiiddpetg tplvvpaark prnggsradr ptaekapaga gqaggr
//
LOCUS       WP_457688372             229 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457688372
VERSION     WP_457688372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23308
     Region          1..226
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtaavagfal fallvtmapg pdtllvlrnc vrggrrtgaa tavgaavgsl awavaaavgl
       61 aaalqrwdaa fmvvrlagaa ylavlggqal wahrrsaaad rpesgpdpld tpepnghaap
      121 plaplanlap lrafrqglls cllnpkvgif fvavvpqflp eghsvlgttl llgavdavia
      181 agwlllvvvc agrllrrlrr prvqrnlert tggvlialgm gtaaetvag
//
LOCUS       WP_457688374             543 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457688374
VERSION     WP_457688374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..543
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=58032
     Region          16..136
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          247..538
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgqeakieae itvrralelp alrrglpevl aggdrmdrav rwvhagevph iasllkggel
       61 llttglglga rpseqrafir kladreiaal vvelgsrfas lptalvdaar dcglpliqlh
      121 revpyvtvte aihteiinsh yallrradei lrrctdvllr gggvpevlrl lavftgnplc
      181 leapdgsply aagpegdddg padadpllaw eglrdtglrv dvpggghgpd avrarlvllp
      241 vnaplapvhr iaaeraadll avvmlqsrqe evlaargrgd fladlaegri saaeapaqar
      301 llgfrpgdep vfpvvmrlpa glpspgswal laqalreela apgvpvllgv rpvegrvpml
      361 valragqdrd alagriaeam ragivragld rpathrpvvv vgtpgdwaaa gpglqhaaea
      421 aaaaqglpeq pwydarrldi elllwrmreh geqgvltdfv eraigpllah draarqpllp
      481 tleaylasag rkaetardln vnrqtlydrl ariaqllgtd lddpqtvlgl rlalrarrht
      541 dkp
//
LOCUS       WP_457688376             342 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 16 protein [Streptomyces nigrescens].
ACCESSION   WP_457688376
VERSION     WP_457688376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Henrissat,B. and Bairoch,A.
  TITLE     Updating the sequence-based classification of glycosyl hydrolases
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 695-696 (1996)
   PUBMED   8687420
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10115061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="glycoside hydrolase family 16 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36189
     Region          55..323
                     /region_name="GH16_Strep_laminarinase_like"
                     /note="Streptomyces laminarinase-like, member of glycosyl
                     hydrolase family 16; cd02182"
                     /db_xref="CDD:185691"
     Site            order(126,129,131,165,167,169,187,189,192,203,205,285,287,
                     289)
                     /site_type="active"
                     /db_xref="CDD:185691"
     Site            order(187,189,192)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185691"
ORIGIN      
        1 msmrirpgkr ahhragasll avgaalvttc altlptasae qaapvpkaka asaafqevwr
       61 tdfdgaagsr paaddwiidt gtgypsgppn wgtgerqtyt drpenlqldg aghlritark
      121 dgttwtsgri esrrsdfaap sggtlriear irmpevsgdd algywpafwt lgadyrgtyw
      181 nwpgigefdi menvngvnkv wgvlhcgvnp ggpcgesqgr gnsrecpgsa cqagfhtyal
      241 eldransaae alnwyvdgqk fhtvsaaemd adtwarathh ghflllnlam ggafpdgaag
      301 fatptdatrp ggsllvdhva vsvrqpagar tdraatptdr hp
//
LOCUS       WP_457688387             400 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457688387
VERSION     WP_457688387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Castillo,R. and Saier,M.H.
  TITLE     Functional Promiscuity of Homologues of the Bacterial ArsA ATPases
  JOURNAL   Int J Microbiol 2010, 187373 (2010)
   PUBMED   20981284
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 400)
  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 400)
  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 400)
  AUTHORS   Zhou,T., Radaev,S., Rosen,B.P. and Gatti,D.L.
  TITLE     Structure of the ArsA ATPase: the catalytic subunit of a heavy
            metal resistance pump
  JOURNAL   EMBO J 19 (17), 4838-4845 (2000)
   PUBMED   10970874
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Rosen,B.P., Bhattacharjee,H. and Shi,W.
  TITLE     Mechanisms of metalloregulation of an anion-translocating ATPase
  JOURNAL   J Bioenerg Biomembr 27 (1), 85-91 (1995)
   PUBMED   7629056
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Rosen,B.P.
  TITLE     The plasmid-encoded arsenical resistance pump: an
            anion-translocating ATPase
  JOURNAL   Res Microbiol 141 (3), 336-341 (1990)
   PUBMED   1704144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14288110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="ArsA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42499
     Region          29..296
                     /region_name="ArsA"
                     /note="Anion-transporting ATPase, ArsA/GET3 family
                     [Inorganic ion transport and metabolism]; COG0003"
                     /db_xref="CDD:439774"
     Region          327..389
                     /region_name="ArsA_HSP20"
                     /note="HSP20-like domain found in ArsA; pfam17886"
                     /db_xref="CDD:436117"
ORIGIN      
        1 mrivlvtgsg gagrttlaaa talagarrge ralllttgss apetvlgtpl gadaptpiap
       61 glharridpg drfrqeflaf qeragaaldl lgaapldede ltelpgsedf allhalraeh
      121 asddwdlvvv dmpsadetvr llalpaqvrr ylrrllpper qaaralrpvl aqlagvpmpa
      181 qklydaaerw eaelaavqrt iddpgtsvrl vteagpvaaa tlrtlragla lhgrrtdgvv
      241 vnrllptgsa dpflaalsgs qqtalkalre efpdlpvhev phlgrdpqgv deldeliggp
      301 ageidaaapa dgprpdpwtv edrlaadgil vwrvplpgae rrglglvrrg deivvtvgrf
      361 rrirtlpsal rrctvsgagl rdgaleirft pdpdlwpksd
//
LOCUS       WP_457688404             625 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457688404
VERSION     WP_457688404.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..625
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=64120
     Region          22..441
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mvnsaggsgi fqplegddpr aiagyrltar lgsggmgkvy lsytpggrpv aikvirpefs
       61 edaefrrrfk qevqsaqrvq glftapvids daegpspwla tayvpgpsla aavaghgklp
      121 vptvlllvag iaealqvihg agivhrdlkp snvllaadgp rvidfgiara adatsltssg
      181 vtvgtptfma peqaagstis patdvfalgq vaayaaigtp afgegtshgv lyrivheepd
      241 ltglpdelre lvtrclskea sdrpsvaevi alcgaasgqt qlrrpeewlp tavaadittr
      301 aaapapaqtp pppleaptaa apaqppnppa pspgrptqpp apptapvapv ptelnhpqtp
      361 ppgfgpaaya ptvagtgapt atgptaavpt aavpmatgpa vtgptsavpa pqppkkkrkg
      421 liavlavvcl lafagaggal vytfmkgegq kkgnqsaggs ktankdsspt ptgdptaspg
      481 dggsgapvkd ptpvdyktin lpddyhisls depvhptdsd ndtdidfsyt dnsytddevd
      541 tetgklvlln agqegtlatc rnetrftdsi ltkrlskgaq mclttkyghv alitfkgyap
      601 ktdpssymti dvrvwrnave peqes
//
LOCUS       WP_457688408             482 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457688408
VERSION     WP_457688408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49685
     Region          1..452
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msnpprtrkl rlwealtlsv glmgptlamg lngagvattv gkavplvfll gllgvglvay
       61 gfwrltqhfn qagsvyalag atigpragff ggfallgtyl aflvctlaat gvfaqaflha
      121 mgirstgpwv avaflaalgv talnsrdgrt tartlliveg igilamlvla avimgrattg
      181 saprhqsldl svftaggtty savmtatvfa flswagfeac aslgeetddp krnipralag
      241 svlltgclyv lmmfaqtigf gtdaqgvref gaaesalstl sgqyigtwfa lviaftavas
      301 afaaalsssa aaarmvqala rdgfgprala rthpvtgapt talrvcgava aaltavmygt
      361 gaaafdtyyw yatigvlcvl vvyavagvgv ivftlsgrgr iprwelvvpv aglgylgfvf
      421 lqqstgqsap ytyfpwiaaa wclagvavvl aapsltrrig armtsvlvad ahptepnrkv
      481 ps
//
LOCUS       WP_457688406             310 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688406
VERSION     WP_457688406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33183
     Region          27..270
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mddrpgdhge ppatggdagg easagqepgm tvaervrrvq gslspaelki aralmahypa
       61 aglestsgla gragvspptv vrfvarlgfe gyrqfqqslr devqarrasp ltlrpviset
      121 sptsdlveaa aevglgalsh tfaalpeqef dravelicdp akrivsfggr fsrllaeyld
      181 lhlrllrpgt qvhipapggd ggfrvdlgrr evcvvfdfrr yqrdtvelar faqergarvv
      241 lftdpwlspv aefadvvlpv rveapspfds ivapvavvea lvaavhvrlg saaeermraa
      301 eeasgdrtme
//
LOCUS       WP_457688412             391 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457688412
VERSION     WP_457688412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40393
     Region          10..367
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 msldhtlttl aaqlereldd avelrhqlha rpclsgdeaa aralvlaalp gghtaaevag
       61 tgavvrvggs gpavavrgel dalavheetg vpwasqhpgv mhacghdvhl aalvalarav
      121 draggpapll avlqpreety psgaqdvted gilereqcra tigahvqpll aagtvactag
      181 gvnasadeft vtvrgrggha ayphltrdpv vtlahvvval qslvsrgidp mssvvlsvtt
      241 laagtaanvv pgsaeasgtl ramrtadrev iherlvetae lvaqaygcta dvritrgepv
      301 ldndatltaa trpllaslgl kvdadlrsag addfsyfser mpslmlfvgt hggteqlhsp
      361 tflppdervr dvahallagy laaaeqfipq h
//
LOCUS       WP_457688421             488 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleobase:cation symporter-2 family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688421
VERSION     WP_457688421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..488
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49605
     Region          27..437
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mtgqksegdr khpvdetlpp lkmftsglqh vaamyagvva ppmivgpacg lnatetaflm
       61 gaslftagia tllqtlgfwk vgaklpfvng vsfagvtpmv aigkaqspdn alpiifgavi
      121 vagvlgflva pyfsklvrff ppvvtgtvit ligvsllpva fnwsqggndr apdygsltni
      181 gmaaltfliv lvlrrvlrgf lqqiaillgl iagtliaipv gitnfsalse aslvgfptpf
      241 hfgapqfdia aivsmcivml vcmtestadm lalgrivgrp adertieggl radtlgtals
      301 plfngfansa faqniglvam tkvrsrfvva tgglilivlg lcpvaasvis lvplpvlgga
      361 givlfgsvaa sgiqtlasaa mekgdnaliv aaavgiglip iaapdfyhhl pkdllvvlds
      421 gistgclvai vlnlafnhfg rktadggaad edtadgtaaa ahgdpetppq pdagttdeag
      481 apaaapah
//
LOCUS       WP_457688439             241 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688439
VERSION     WP_457688439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26499
     Region          18..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mseidrsraa raeartriee vaarlfaerg fagttigeia aeaglskpml yrhfdskqel
       61 hlallerhrd elaaapvrel lhgegnldtr mtamydawfg yveshpytwr mmfrdttgda
      121 qvqafhrelq rrqretdmal lrefvpglpe aeleplgeai rsalyglalw wldrpeqpre
      181 llvatmtrit rglistvegp naedpnakmp gakmpdatst gtpdapgpsg aspsgaaggt
      241 d
//
LOCUS       WP_457688437             346 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457688437
VERSION     WP_457688437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36633
     Region          106..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msvppemqlr samqvhpelv payeslppss dpyadieaar egvhkmlaaf padrtgvsse
       61 rfeipradgs altvevyrpe ggadtgtgqd argaapegag ralpavlhfh gggfalgrsl
      121 pgqdraaial crelpavvlt veyrlapehr ypagvedcyr alewaaeraa dlgidparia
      181 ltgrsagggl saavalmard rggpaivhqs lyvpdvddrv gadeaasdae edvetrvtta
      241 rdiqrawrhy lpegtaeaea yaaaaratdl sglppayvlv cdldplrdag layarrlmda
      301 gvpvtvrnvp gawhgfelft pdtrvakemt ahwtgqlrea lypvgg
//
LOCUS       WP_457688441            1176 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688441
VERSION     WP_457688441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1176)
  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 1176)
  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   3  (residues 1 to 1176)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1176)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1176
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=125287
     Region          1..237
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          173..1129
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhygilgttq agradgtpva lggarlrall aalalrpgra lspelligdi wgaeppadaa
       61 galqalvgrl rralghaaia svdggyrlca epdavdlhrf erlateggra lgeadparaa
      121 allddalalw rgpaladlpd asveasraer rrldaqctri aadlalgrat qslptllalc
      181 edhpldeplq alrlhalraa grtaealaay eeirtglaer lgadpgpelr tlhaellrpp
      241 pptdrpplap ipgtpaaapa pngtgtsygt gmgtsygtgt aygsgtphsp gtpspgtsst
      301 epphshshph phpqphphtr pgnlrarlts fvgrdtdlaa iradlaahrl vtllgpggag
      361 ktrlsqegae taaaalpdaw phgvwlaela pvddpqtvpe avltalgare tvvrgttadg
      421 lraaadptal dplarlaehc agrrmllvld ncehvidaaa elaerlladc pgvtvlatsr
      481 eplavpgevl rpveplpdpv alrlladrga aarpgfrved dpaacteicr rldglplaie
      541 laaarlrlls prqladrldd rfrlltsgsr tllprqqtlr avvdwswdlt deperavlrr
      601 lsvfaggcdl aaaeevcagd gvdgrevagl lgslidkslv vaapagqegg agraagtggq
      661 mryrlletvg eyagerldea geragaerrh lvayrelart tdpllrgpgq ragmerlele
      721 hdnlrtalrr alaahdehea lclvlslqwf wslrdhrsda rhwstaaaal gpnpfaapae
      781 papdlherpi dtpppmapeq llearreirl valasrdsdi talrdpamqe eltgmltayr
      841 sgmpqtckvp gvmwyyavli tgefdelael vdgavracrd fgydwelayv lqlrskifnd
      901 rpgglaqaar dadealrlfl rlgdawgaae alsgrgenhe krgaygaaar dyraamvhae
      961 dlgahgqill lrcrlgavli edgqaetger mlrevladae kgnsvrdtep farltlamwl
     1021 taterlqear aqlrrvqelf tsrapdlfag llqalsisld vdeghregll prfrqslelm
     1081 qdslaqivap dlpvvqlltg arvlmaerge kggwdaarlv gaydamradg qvppllvrrd
     1141 rdrteaaara llgdtayara haeggglslg eatali
//
LOCUS       WP_457688444             328 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457688444
VERSION     WP_457688444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35234
     Region          42..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msrdtlsrpe pvtprparrn trgprrrdsr tgarnaraaa afvlpffalf alcflapigy
       61 alhqslftte rtgplglggq erevfaglan yaqalsddrf ltgfgrvlaf gavqiplmiv
      121 latalallle sasaravpff rsafflpygv pgviasilwg flyvpgispl vkiagsvgwd
      181 ldflsrgtvl wslanivtwq ftgynmlvli aqlkavpgel yeaaridgan awqvarylki
      241 plirpalvlt gvfsiigtlq lfaepmvlrp lassidsgft pnlhayseaf vgnnphaaaa
      301 eavllalvac vlsfgflrlv ggrtkerg
//
LOCUS       WP_457688446             375 aa            linear   BCT 27-JAN-2026
DEFINITION  sialidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457688446
VERSION     WP_457688446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40000
     Region          9..373
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
ORIGIN      
        1 mayessvpyr agtegytsfr ipavvrarsg hllafaegrv ssaadsgtih ivlkrsadag
       61 rtwgplqvva rngngtagnp apvvldsgrv lllqvhnaad atedrirrgr vppadgrrvw
      121 lqhsdddgas wsppreitdq aklpqwrwya tgpghalqlr hgpyagrllv panhstpptg
      181 pqdsgtepry ngghallsdd dgatwrigys ysysyshshs ggdsdtdrsv apnettaael
      241 pdgsvylnar neaaaawrrv davstdggeh lvrpfrpqag lagpavqgsa lhlgdrgall
      301 fsgpahpaar almtlrtsrd ggltwrtaht vgglpaaysd lvrldrhsvg llyetgdfsa
      361 ystitfrrip veept
//
LOCUS       WP_457688448             228 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688448
VERSION     WP_457688448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25140
     Region          1..227
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 margtmsedv qaqikqlilq grltpgdplp teaelvglld vsrnsvreal kalqamrive
       61 irhgfgtyvg pltlepfveg vafraavrhq qgesslyelm evrealeagl igavarnlpa
      121 edlavlkglv qrmaeeargg qvqsatdraf hlalyrslgn hllsevldaf waalrrvreh
      181 lsddrpdpvv thrqhqeivd aleagdgdra veaihrhfdg irrrlaeq
//
LOCUS       WP_457688450             321 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457688450
VERSION     WP_457688450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33240
     Region          6..316
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 malpaplhgv ippvctpldp rgeidtasla rlvnhlvdgg vhglftlgst sevayltdaq
       61 rgtaleavik aadgrvpvla gvidtttprv ldhartaaal gadalvatap fytrthprei
      121 aahfrhlrta vdlplfaydi pvsvhskltp slvrelaedg tlaglkdssg degslrrllt
      181 alggrtarrt gsapefsilt gseltvdaal lagadgvvpg ignvdpaayv rlydaaragn
      241 weqaaaeqer lvalfslvdv gpetdmgrss salgafkaal hllgvidrga tafpqrplse
      301 eavaevgrrl maagllprrg g
//
LOCUS       WP_457688468             237 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457688468
VERSION     WP_457688468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24645
     Region          37..84
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          94..207
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 msraaedpeg aaaegrpgpa apagrgrprs aaadsaiiea vlrliedgvs igelsmeria
       61 reagvgkatv yrrwsgksal lldvmrsldv pspppaglsv rddlvsllef lrrrglakrs
      121 sallrtvvsh vqaqpelwae yhdtvvrarr eallallrrg vasgeirgdr dletladlfv
      181 gpmlarallh ewkelpegla adivdtvleg vrppagtagt agtagtagta gtagtag
//
LOCUS       WP_457688582             174 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 900105755].
ACCESSION   WP_457688582
VERSION     WP_457688582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..174
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18814
     Region          7..156
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          84..171
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 milapvpltp dhdipapvlt eltalyasnr efhalsgdfp dpdgirpeqv aaaladelan
       61 pdaevllara egrligvvvt larhpdpadp dpwigllmvd aaaqgrgygr riaerveerf
      121 raagrnavrl avlennpkgl afwtalgyav tdhrpdrehg rpctvlrkel skra
//
LOCUS       WP_457688635             796 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces sp. 900105755].
ACCESSION   WP_457688635
VERSION     WP_457688635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..796
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=79070
     Region          <106..327
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          <661..784
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mapesrdevr qridslydqa enatgnynat ramsggsrsr gvplfkrprr ddpgldniar
       61 ewfegarskl gpsvpaalps drqparsgpr rpvsamaadl lgqledsgpa rleltagpsa
      121 qseievvrel parpklelta gsaaalpagt pgapralpaa gqqrptpgas ktrnqlklak
      181 arevlsqrtg qraiaaldaa papvtqgvpq spspwpapea qappqqwqap aagipnqrtg
      241 sgsarsdspa atralpavte tggipivsps dtgtfrimtp ggadraptra aadmggfrlm
      301 tpggsgggty qsapamdtga aqapapvdtg sfrimtpgat gsfpmptpad aggfptadpm
      361 astsvfptad pmtgssafpt adpmtgtsvf ptadpmtgts vfptadpmtg ssafptaapt
      421 nsgafptaap aapapapspm daggfrimsp naaasytdvp pvaadtaygt ggypvtapav
      481 papptaampm aampmaapfa aapaadmaga ypagmqagay pagmqagayp agmqagaype
      541 gmpsadgaya yaasmampta maapaaampa pmampmaapa aapmtapmaa pmaappappt
      601 aamppamtap peamtaaapa mampmaapap vvtaplpttp lptappqvpa pvpaaaapvp
      661 ggyaeagafl qpgvaaepgk amkalafare qigrpcvwga tgpgaydass ltqaawraag
      721 vtlprtaaeq tlagtpitla avepgdlvff fdddshvgiy agggtmvhap spgalirees
      781 iynagesaih rvirpa
//
LOCUS       WP_457688675             313 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457688675
VERSION     WP_457688675.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   di Salvo,M.L., Safo,M.K., Musayev,F.N., Bossa,F. and Schirch,V.
  TITLE     Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate
            oxidase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 76-82 (2003)
   PUBMED   12686112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1562906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..313
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33947
     Region          9..112
                     /region_name="YzzA"
                     /note="General stress protein 26 (function unknown)
                     [Function unknown]; COG3871"
                     /db_xref="CDD:443080"
ORIGIN      
        1 malldsapld vldayrtcef atlgrdgtpl awptavrrrp dgtlllstsl afaqkalnir
       61 rdgrvallfs dptgsglenp pqifvdghae cpdeimtgpq gaedywrmlf erqphsrsyv
      121 tapmrlvmdw yylrllitvt pqqvvvrspl plsgtpaapp gelvgaaqla rfptavlaar
      181 daagapvlar trpvptgegf avdvpadcpa aegpaallvh rhderlnhmh nalvrgelra
      241 dgarwvlvpa kvvepmgsgr vsdavsvlrs trqatdrylr rrglprprvr waqfralaqd
      301 arrsgargep lga
//
LOCUS       WP_457688849             423 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105755].
ACCESSION   WP_457688849
VERSION     WP_457688849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  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 423)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..423
                     /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=45059
     Region          77..>152
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          106..129
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          193..419
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstvsgdisi rtfegrrwlf psaviheldp eagpagrrpr rtardwlvdf scfllavllg
       61 aaaantmrqd pnvphglava dqligglaca avwlrrrwpt glaiamipvs fasdtaggas
      121 mvalftlavh rpfrhvawit aanlvlvplf ywlrpdpdlp ylavvilvvl ltllvvslgm
      181 fvrskrqlmv slrdrarrae teaglraera qrlareaiar emhdvlahrl tllsvhagal
      241 efrpdapree varaagvire sahealqdlr eiigvlraad gdeaagrpqp tlaaleslva
      301 esrgagmkvv ldnhvgdpaa vpasvgrtay riaqegltna rkhapgaevt vrvtgapgdg
      361 lditvhnpap ateapqvpgs gqgliglter atlaggrleh rsvgdggfev rawlpwaaps
      421 paa
//
LOCUS       WP_457688956             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ComF family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457688956
VERSION     WP_457688956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..309
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=31804
     Region          1..238
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
     Region          <212..292
                     /region_name="PLN02297"
                     /note="ribose-phosphate pyrophosphokinase"
                     /db_xref="CDD:177934"
ORIGIN      
        1 mrgwwqdltd lvlpaecggc gtprtvlcdg craalsgavp rrvrpvpeps glpavyaaap
       61 yadevraall ahkergalal agalgaalag avraglrdgy qdgpaglrdg ravrivaswh
      121 gaagdagasg pvllvpvpsa pwavrarghd pvrritlaaa aelrragipa rvvpvlrqrr
      181 avadqsglna rqryanlaga levtaggarl laggrvvlvd dlvttgatla eaaravreta
      241 raegageatt avyrraaweg reerktgpee erakwarnts gmaevnglag pvraavvaaa
      301 pdsfemnrn
//
LOCUS       WP_457688992             204 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457688992
VERSION     WP_457688992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   3  (residues 1 to 204)
  AUTHORS   Nasser,W. and Reverchon,S.
  TITLE     New insights into the regulatory mechanisms of the LuxR family of
            quorum sensing regulators
  JOURNAL   Anal Bioanal Chem 387 (2), 381-390 (2007)
   PUBMED   16953322
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Rosinski,J.A. 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 204)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10361480
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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=21028
     Region          7..123
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(101..104,106)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
     Region          143..198
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mstvirvlla edehlirqsl aallaleidl evvaqaatgg eavtaarrhh pdvavldlqm
       61 pgtdgitaar amiahdsdck tlivtshglp ghlkraleag ikgfvpktvs aaqlatvirt
      121 ihnghryidp tlaadaiaag dsplsaread ilalaadgat vteiagraal apgtvrnyls
      181 qavakigapn rhsaahiars hgwi
//
LOCUS       WP_457688994             387 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457688994
VERSION     WP_457688994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  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 387)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /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=40597
     Region          155..381
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtgpqhaevq rvtlvsrwal alaitapsta fawpvagrla ttvpgllilt vyvalavaai
       61 haatltlrtp ptrprpllla vtgitaaagl asvlpaldhg wlpatpnspi aacvlavvpa
      121 aaawagthwr vssalalatt lttawvtspd plpgagvvla lwivttlgvr tsqwslqvmh
      181 qlnaarqaet rlavveerlr fardlhdtlg rtlagialka elaarlphgp qarfemtqiq
      241 rlaresqqei revvrgyrtt dleteldgar svlaaagitc rirttgsepg dairtalgwa
      301 vretatnvir hsqatyctit lahtadgtsi ltvtnnnprp avdstsgtgl dglaqrlaah
      361 agtlthgpap dgtytvtari ppqehal
//
LOCUS       WP_457688996             254 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457688996
VERSION     WP_457688996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  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 254)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27088
     Region          60..251
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mssparqlvs lgraeatlff rtkanfvnvl fipvftlaal hitmgkfdlg dlglsmgpvm
       61 vatavgivlv fslyvplttt yvarrdelll krlrtgevad ptvltgtalp saaivlvqta
      121 liaavllplt gagappgvhw alaavvlgil lmcalaaats alarttenvq vavlpllfll
      181 pttsgtffpl eampqlmqdi chwlpmtpvi dlvrsawtht lttteallrl vvlagwtvla
      241 lgaarrwfrw eprt
//
LOCUS       WP_457688998             322 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457688998
VERSION     WP_457688998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35151
     Region          10..231
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mthhsqgnvi evtdvwrryg vgtktfdavr gvtfavkege lfgllgtnga gktstielle
       61 glaqpaegti rlfgrhdpyr drkhtrprtg amlqhsgfae qltvaetarm wagcttrprp
      121 vrdaialvgl thradvqvkn lsggekrrld lalatladpd llfldepttg mdpegrhdtw
      181 rlikslkdmg ttivltthyl eeaealadhl aimhagriaa hgtvpqivge hpatltftlp
      241 vthqatdlps rerlaathin aqglslriet phlqhtttel lnwardqdvi laglnarsas
      301 leeaflhiaq ngltrseepq va
//
LOCUS       WP_457689008             259 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689008
VERSION     WP_457689008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28017
     Region          32..158
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtepvadigy grqfdgwydr lfpdpqaaqe tarvlaaihp dpaagtcefg vgtgriaipl
       61 srlvgeitgv dsspemlntl aqaaleqdgk vtsvpadirt frgrrrfglv yavcatlnqv
      121 vsreeqqetv rraadllvpg grlvlechnl pcvealhegr arttlftpyp dpgtglqths
      181 tldtarglwq cshiwyekdg ttrvgteysl lltpqdteey agfaglrpva eggcyggwdl
      241 sgytdsspaf itvyekpap
//
LOCUS       WP_457689010             464 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689010
VERSION     WP_457689010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..464
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49600
     Region          2..443
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 myeahdtmgg glrteplfes givhdicsav hpmacaspff safdlpargv elchsdaaya
       61 hplpggeaai ayrhlprtce rlgadgprwr hlmqplldhs edivrlilqg ptaltqvapp
      121 alavlaarvc ahgtplaprq ftqeparall tgvaahavgr lptlasgtva vllahlahtt
      181 gwplprggsa riaqaladdl trhggtvhtg vrvndlrdlp qgrivlldvs pkeflriagh
      241 llptryarsl hrfrygpgaa kadflvsdpi pwadpstada atvhlggtqr dmfrqenlta
      301 rgtpsnepfv llvdpaaadp srarpgkrpv wayahvphgs trdglplirs rieryapgft
      361 dtiiaqrats asalehynpn yvggdigaga mtlpqslfrp tlqlapyrtp lpgvylcsas
      421 tppgpsvhgm sgylaarasl rrevgmrtlp slsprarhps heei
//
LOCUS       WP_457689026             396 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457689026
VERSION     WP_457689026.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 396)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43325
     Region          20..396
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(66,86,88..89,172..173,182..183,186,189..190,193,225,
                     228..229,232..234,237,280,282..285,309,386)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(87..88,95,99,106,151,154,229..230,233..234,237..238,
                     241,279..280,283..284,286,309,337..339,342..343,345..347,
                     350..351)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtntqplktq ptvrscpfdp peeyrtlreq epvapvtfpd gaagwlvtry edvrtvlgdp
       61 rfsskdtllr rggagtddap apppgnflal dppehtrfrr lltgrftvrr mrqltpvveq
      121 ivaeqldama aaegpvdlvq afalpvpslv icellgvpya dreefqrnsa tivqlnpspg
      181 efqraqvamr gyihqlavsk rdnptddils elvhsgeltd eelagvgvll llaghettan
      241 mialgtmcll qnpeqlaalr adpslmdsav eellryltiv qlgvrrtale dvelhgrqik
      301 egslvvvsla sgnrdaahla ddpdrldvgr phsphlafgh gihqclgqql araemkaals
      361 alldrfptlr lavpveevpm rddmlaygvh elpvtw
//
LOCUS       WP_457689029             390 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457689029
VERSION     WP_457689029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41300
     Region          1..388
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mdhivlvgas aagltaadal rregftgtlt lvgdelrlpy drpplskqvl agdwephrst
       61 lrqdtdllql rmnlrlgcra tgldtaervv tladgdrlgy dgliiatglr prrlpfghdl
      121 agvhvlrtld etltlrarlq agprvvviga gflgseiaat trglgldvtl vdveatplar
      181 qvgtfvgglv gemhrdhgvr lcmgrhatgm tgedgrvtav tlddgtrlaa dvvvvaigsv
      241 patewltgsg iplgdgvlcd htcraaprvy aagdvanwph psaggrvrle qrtnatqqai
      301 taarnllsgp aeavpyapvp fgwtdlyytk iqtcgwcpsd atvevvdggp qehrfvalyk
      361 vdgrvvgalg wnsaralrqy rshlagniaa
//
LOCUS       WP_457689027              64 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457689027
VERSION     WP_457689027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..64
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6513
     Region          1..64
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mkilidegkc vgagtcvlaa advfdqrded givvlldadp phallpqvtd aaarcpalai
       61 evve
//
LOCUS       WP_457689033             490 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457689033
VERSION     WP_457689033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..490
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52090
     Region          63..444
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnrtrthdry trtrqggags gsgggrigap rrsggygrrp aavqgefalp ktvtpalpav
       61 eafadldmpr ellaalgaqg vsvpfpiqga tlpntlagrd vlgrgrtgsg ktlafglall
      121 artagqraep rqplalilvp trelaqqvtd altpyarals lrlatvvggm sigrqagalr
      181 agaevvvatp grlkdlidrg dcrlnqvgit vldeadqmad mgfmpqvtal ldqvrpegqr
      241 mlfsatldrn vdllvrrylt dpvvhsvdps agavttmehh ilhvhgadkh ratteiaare
      301 grvimfldtk havdrltehl lrsgvraaal hggrsqpqrt rtltqfkngq vtvlvatnva
      361 argihvdhld lvvnvdppsd hkdylhrggr taragesgsv vtlvtpdqrr gmvrlmsdag
      421 irpqttqvrs geealsritg aqapsgipvv itapvaerpq rratasrgrr raapttrrtp
      481 aqrsavdpaa
//
LOCUS       WP_457689044              76 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457689044
VERSION     WP_457689044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..76
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7535
     Region          1..64
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mqlsidrdrc igagmcalta pevfdqdted glvvlrtaap ppglratarl aaglcpaaal
       61 tvieqggtgs sapdgr
//
LOCUS       WP_457689045             416 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457689045
VERSION     WP_457689045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 416)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44955
     Region          38..413
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(84,106,108..109,192..193,202..203,206,209..210,213,
                     244,247..248,251..253,256,299,301..303,327,403)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(107..108,115,119,126,171,174,248..249,252..253,
                     256..257,260,298..299,302..303,304,327,354..356,359..360,
                     362..364,367..368)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mqhepsapat eqtaeetaah pepvtlpltr aagcpfdppa elaelreqqp lrpmrypdgh
       61 vgwlatghsv vraiaadprf ssryellryp lpggpsgalp paplgdltgi dapehtryrr
      121 llagkftvrr mrqltarveq itadhldame rqgpvadlvq afahpvpalm icellgvpqs
      181 dragfqehta mlsspdagpe eqmaamttla ecvrelvvak rahptddlls dlttseltdd
      241 elagigsfll aagldttanm lglgtfalls hpeqaaalrd dpgladqave ellryltiah
      301 tglraaledv elagqlikag dtvavsvqaa nrdplkfpdp dtldlrrkat ghlafghgah
      361 qclgqqlarv emrvafpalf rrfptlrlav ppedvplrda mniygvhrlp vtwdke
//
LOCUS       WP_457689047             263 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689047
VERSION     WP_457689047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  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 263)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27616
     Region          65..263
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttltyagrd artmlrrnlk halrypsmtv sviampvlml llftyvfgga lgagiggtgg
       61 gspeyidyva pgiilmaats galvtavgvc vdmtegivnr frtmaisras fltghvvgsv
      121 lqtlvsiafv igvallmgfr thatplgwla aaglltlltl altwvaaaig lvaknpetas
      181 niplpfqflp flgsaivppe smptglrwfa eyqpftpvie tlrgllmgtp vgaeaiaava
      241 wcvgltlvgy lwartafrrs atr
//
LOCUS       WP_457689061             131 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457689061
VERSION     WP_457689061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 131)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..131
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14074
     Region          27..117
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mskqelavlg qdgadaccpt lltapldedq avelakvfka lgdpvrlrll smiasrsgge
       61 icvceltpaf dlsqptishh lkllrqagli dcerrgtwvy ywllpettdr lagiltrpgg
      121 mprpeatdaa s
//
LOCUS       WP_457689065             144 aa            linear   BCT 27-JAN-2026
DEFINITION  arsenate reductase ArsC [Streptomyces nigrescens].
ACCESSION   WP_457689065
VERSION     WP_457689065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..144
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=14852
     Region          9..131
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(13,15..20,106,108)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 msdsappsvl fvcvhnagrs qmaaaflthl agdavevrsa gsapadtvhp vvveamaeag
       61 idlsaetpkl ltteavqasd vvitmgcgda cpvfpgttyl dwalddpagq gldqvrpvrd
      121 eierrvrgll atlgrtpeqp dads
//
LOCUS       WP_457689067             501 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457689067
VERSION     WP_457689067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53465
     Region          91..>312
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          409..493
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mttyahrtll lalsvatvaa tltaaapvvr adapgttgpd ltwrpcaepg gltgqecarl
       61 pvpldyrdpd gpqlslavtr vrserpaarr gtllvipsgp ggsgvhrlet kgpalrkama
      121 gaydlvsfdp rgtggstrag celdaddrhl vslrswpgpd geiggnvara rriaeacrrh
      181 ggavlrsftt vneardidrl rralgeekls awatsygtyv gavyaqkypr htdrwvldss
      241 gdpdasrvgr gwranmsaga ddrfpdfaaw aadpareseg lrlarrpeev rplflalaak
      301 ldrepkkstt pgvpltgnrl rqalqnalys dglfagtarl irqaqdpaae pvlpdtlagp
      361 lpdqdaaatm atvcndvrwp asvpahrrav aadrarhplt agmpanitpc sfwqapaepp
      421 tritadgpsn ilmvqnhrdp anpyfgalkm rralgerarl ltlehgghga ylangtvcgd
      481 rtvtaflttg rrpqtdthca d
//
LOCUS       WP_457689069             246 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457689069
VERSION     WP_457689069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Almo,S.C., Bonanno,J.B., Sauder,J.M., Emtage,S., Dilorenzo,T.P.,
            Malashkevich,V., Wasserman,S.R., Swaminathan,S., Eswaramoorthy,S.,
            Agarwal,R., Kumaran,D., Madegowda,M., Ragumani,S., Patskovsky,Y.,
            Alvarado,J., Ramagopal,U.A., Faber-Barata,J., Chance,M.R., Sali,A.,
            Fiser,A., Zhang,Z.Y., Lawrence,D.S. and Burley,S.K.
  TITLE     Structural genomics of protein phosphatases
  JOURNAL   J Struct Funct Genomics 8 (2-3), 121-140 (2007)
   PUBMED   18058037
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001918
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=25114
     Region          4..246
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 meyvtvtals hpglirehne dslvagpwtl cgtmtenpqt lvfplgtplv vavadgiggq
       61 pagevasala vrqlaalgpt ldteeavrda ltlcngavya aagrdpeltt mgttvagavv
      121 laesllvfnv gdsrvldata dglrqvsvdd spplspgrrt tslvtqalgg tpefsavtph
      181 vteaplsagd rylvctdglt dpvpedalnd llqlhsggra afelwrsaie aggpdnitla
      241 ligige
//
LOCUS       WP_457689079             394 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457689079
VERSION     WP_457689079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /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=41500
     Region          121..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgffagclil yvvggprvmg gdipawqavl pvlvlctata frsalplaal avgtltvave
       61 ivagggmgpv lvytdllyag alygapwlcr alqfgtvaat laatvalvlt gdrsegvttg
      121 viiavllisp vwtavlirnh keradaerer aaqidrlael drktvlqter trmarelhdl
      181 vanhlsaiai hssavlslte aqrakdgaae edpvlralav irensvqgla emrrmvvllr
      241 sergvsddwd rpqlnalgal veqarpaada agltlhtelp etfpevssvi evtayrivqe
      301 altnvlkhas agrvrihcea gteqltlsvd splprpggra rqrpveqlta gagagltgms
      361 eraalvggsf dagpdatapg rwrvravlpl tqnp
//
LOCUS       WP_457689088             328 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA desaturase [Streptomyces nigrescens].
ACCESSION   WP_457689088
VERSION     WP_457689088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=35882
     Region          25..321
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtstartvps aqdydgtspf pdsgtaspps sgrrmyvtvt giivvapfvg lavaipllwg
       61 svvhltdlvl lavfyvisgl gvtigfhrgl thgsytaapa lrialalags lsfqgdvidw
      121 vathrrhhay tdrpgdphsp yrygtslrgq lrglvhshig wlfgddptsh rrfapdllad
      181 rgiravdraf palclltlgl pfalgwalgg swvtaltall wagfiriall hhvtwsvnsl
      241 chvigdrpfr trrhdratnl wplallsfge swhnlhhadp tcarhgvdrg qldvsaavir
      301 lferlgwvwh vrwpdperva arrlrsta
//
LOCUS       WP_457689094             175 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689094
VERSION     WP_457689094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19082
     Region          24..170
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mkqnhygrlg avlsadlinl pemsaagvqg lleaheirrp avfeadvdgf rswrdqlarv
       61 fgstdaaeqc savndllvaa tirpwvtthd glqphlhfvp dsadvvsrvk avtagglafv
      121 lcweggarlg rclrpecsra yvdtsrngrr ryctarcgnt eavmrhrsrq pggkr
//
LOCUS       WP_457689097             422 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689097
VERSION     WP_457689097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42946
     Region          41..408
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,244,247..248,251..253,256,285,289,338..339,
                     343,347,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mspatrtsga arsgstapgl pavadatavp arspwdgrla vlavmlgifs ivtteilpig
       61 lltaigadfg isdgtaglmm ttpgvlaala aptvtvatar idrrlmlcaf vlllalanfl
      121 aaaapaywlv llsrvmvgit iggfwsigag laerlvrpes vgratavifa avplgsvlgv
      181 pagtligdla gwrtafvvmg avavgvfvlm apvtpalpar qltrprvlre vlrrtptrfa
      241 llmtflivla hfgaytyvtp fleqvthlas pglvtvfllt ygaagiagnf lggatvarrp
      301 ratfgtaaal lagatlllpl lgrgawgala llivwgigyg avpvssqtwf akaapdapea
      361 asvlftasfq atlslgalvg gvaldhtsps tvmtlggata vlvvltawlh fagrhgrqrg
      421 sd
//
LOCUS       WP_457689109             274 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689109
VERSION     WP_457689109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30563
     Region          17..78
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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..267
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mveknseeda gsarwvlace lsrlressgr slaqlsdean ydrtylhrle tgerlsklpv
       61 metldriygt sgllvrlwgl arldafkdky refmryeaka timqkyamvv pgllqtddfa
      121 realalapap isadeleenv aarlsrqell hrnpppdvri ildesalrrp akdpkvwheq
      181 lkrivdaada pnmtiqvipf saglhgllgg sltllwmadg ssvaylegnn sgdlieepge
      241 varyrlaydr lrdaalsppd saafmrqlve dsrp
//
LOCUS       WP_457689122             339 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Streptomyces
            nigrescens].
ACCESSION   WP_457689122
VERSION     WP_457689122.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35782
     Region          19..296
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mtehahshgh shshahgvsp dadrrwlraa lilltsymav evvigvvaqs lalisdaahm
       61 ltdavsivla liamrlaarp arggytyglk raeilsaqan gitllllsvw layeaverli
      121 sppkvtgglv lvtalsgivv nlictwllsk anrsslnieg ayqhiltdlf gfvatavagl
      181 vvlttgfera dsiatlvvva lmlragtglv resgrifmea apagidpdal gdhlvaadev
      241 vevhdlhiwq itsghpalsa hilvapggdc hkvrrslqel lsgeygitha tlqvdhvgeq
      301 gapdevltls prpgpgperq aghcedahgp vhrpgphrh
//
LOCUS       WP_457689125             313 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457689125
VERSION     WP_457689125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32135
     Region          1..311
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(38..40,43,127,131,152..157,176..177,179,193,
                     218..219,240..241,259..261)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mravavsafg eqpqlmdlpq pepgpgevlv rlsaaglnpv dwkladgmfg davpaafplv
       61 lgsdgagevl aigsgvrrft igdavfgqfq rpeqgggsyc elavtdedri ahaarsvtya
      121 tsaalptagm taynlveetr iaegrtvliv gatggvgtfv tqlaagrgae viatarpaka
      181 elmrtlgaae tvdhtegpia dqvlahhpgg vdvlidmasg paefaeltrt vrdggtavsl
      241 igsadadelt ehnlrgfnfv nrpspqllei laghvdagrl tvlvgrevsl eeapdalats
      301 rtgraqgktv lai
//
LOCUS       WP_457689126             235 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457689126
VERSION     WP_457689126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  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 235)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..235
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24860
     Region          1..205
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrvlvvedee cladmiaael rraaivvdia hdgraalagl rlggydvlvl dgelpaphgd
       61 alrryvvehg lptrvlllta sgpddraadp epapddclar pftheellar vltlgrpgrr
      121 vvpqvierag vtvdtahrla trdgrplals rtefgvlevl lraqgavvsg delieevwee
      181 htsfggnavr vtlgalrakl gdppvieavp gagyrmtdgp gaggepepga rrepv
//
LOCUS       WP_457689129             316 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689129
VERSION     WP_457689129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 316)
  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 10194457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33261
     Region          41..308
                     /region_name="PBP2_ProX_like"
                     /note="Bacterial substrate-binding protein ProX of
                     ABC-type osmoregulated transporter and its related
                     proteins; the type 2 periplasmic-binding protein fold;
                     cd13606"
                     /db_xref="CDD:270324"
     Site            order(46,48,94..95,98,146,148,229,253)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270324"
ORIGIN      
        1 mraavaavag vavlgvsact sgpsletrsa itaspgdsre lvigsagfte sellaqmyaa
       61 lldhagyrtr vvtvgnrely epalevgqid vvpeyaatfa dwlhaknkgs kaapvaspdi
      121 gttmaalrrl agprgltvlp agravdqnaf avsasyarkh hlktlsdlgl aklpvrlaag
      181 decvqrpfca pglkkrygih itaidpkgvg ttpakqavqn gqdqmvltts tdatldqfgl
      241 vlltddkklq nadyvvpvvn raraggerpa aalnrlnkvl ttadlaylne qvdswrrlpa
      301 dvarnylksk gllpks
//
LOCUS       WP_457689131             224 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689131
VERSION     WP_457689131.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23465
     Region          7..218
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mntvsavwrw lttaanwsge ngvwhrleqh lvltfaclvi salialpval tlghlgrgga
       61 lavnlanigr avptfavlvl llltpigrhg qwptiialvl faipplltna yvgmrevdqn
      121 vvraargmgm tgtqlvwrve vplasplvlt giriaavqlv atatlaalvg ggglgriita
      181 gfnlastpqv vagavlvavf allmeaafel aqrwapgwvr grar
//
LOCUS       WP_457689134             275 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689134
VERSION     WP_457689134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29668
     Region          79..249
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(84..87,137..142,175,177..178,199,205..206,229,231)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(86..87,137,141,177..179,199,229,231)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mpkpisaarr tsiaglltat slvlalsgca tydvtapada radapaaeva kkdtalaase
       61 dgkaprgaag ddidcrkakc valtfdagps entdrlldil kkekvratff mlgenhvekr
      121 pagvkridae ghelanhtws hqilteispd aakremsrlq eavrkitgkt prlmrppqgr
      181 tdetvseisk dlglaqvlws vtakdyqtnd salitkrvle qterdgiill hdiyrgtvpa
      241 vpgilkelkk rgytvvtvsq llspakpepg mvyrp
//
LOCUS       WP_457689133             250 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689133
VERSION     WP_457689133.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26300
     Region          19..200
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtapppddcl ahndwicgdy lstrrqilld alaqhlqltl isvvlglvia vplallarrr
       61 rwtvgpvlgi ttvlytipsl amfslllply glsatlvvag lalysltllv rnllagldgv
      121 paeateaarg mgygpmrqll tvelplavpa amaglriatv savalttvga ivgygglgnl
      181 iysgmnaffk aqvltasvlc vliavvldll llgverlltp wrragrrvrv rtrvtagpkr
      241 pvaaapgqra
//
LOCUS       WP_457689136             432 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457689136
VERSION     WP_457689136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46337
     Region          105..377
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltsqsley tvivlavlcv aatvwlwprl arrgvgavlg rlgaivvtqv sivcalalav
       61 ntnfefygnw dellgntdea pasvsqgggq yasvgnlkgg lvqpagpqgl drvtglpkgp
      121 adrvgkvesv kiigrrsrai npgfvylppq yfqqqfrrqr fpvmvvisgy pggimnlaqh
      181 lqvpqnagrl iaqgkmqptv ivmvrptiap prdtecvdvp ggpqaetfft kdlpdamksa
      241 yrvgrdpsaw gafgyssggt cslqlamrnp kiytsavsls gdyaikddlt tgslfgpgpe
      301 garrerehdl lwrlknlpap qisalvassr kgeagygdtm kflraakspm tvdsiilpqg
      361 shqfttwrre vvpalqwqsq qltfpqdtea vpqrkpgvgk ggapgqrttp spapstsddk
      421 ghrrveaerp rg
//
LOCUS       WP_457689142             491 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689142
VERSION     WP_457689142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..491
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50194
     Region          3..467
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(10..11,14..15,18,50,100..101,103..105,108,129,
                     132..133,136,260,263..264,267..269,272,300,304,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mviaiaqlmv vldativnia lpsaqrdlgm sdanrqwvit aytlafggll llggriadlv
       61 grkrtfmigl vgfavasglg gaatgsgllf garalqgafg allapsalsl ltttftigke
      121 rskafgiyga iagggaaigl iaggllteyl dwrwclyvnv piavvafvga avflhdktep
      181 grvhldlpga vlgcgglvai vygcseaqpr gwgdglvigl lvggvvllgv fawwqtraph
      241 pllplhivrd rnrggafltm alaviamfgm flfmtyylqt vlgyspvrtg maflpmvaai
      301 vvgstqisar llhrvpprfl mvpgallaaa glftlrylta vpayvshvlp amllvglgmg
      361 lifmpvmata tsgvaphdsg vtsatvntaq qvggsigtal lntiatstsa vfiadhlada
      421 arkggglglt pavrnqivkd gvvhgfnvai gvasgimlla alvaglmvng rapkhgrtpa
      481 gdsaesadap v
//
LOCUS       WP_457689150             378 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Streptomyces nigrescens].
ACCESSION   WP_457689150
VERSION     WP_457689150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38714
     Region          38..370
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mrndseengr ggegerpqpp rpllpvqarr aaawclvall iaavvalgvw lcvelsaavt
       61 pvllallgsg llgplyrrlv amklnrslaa gltcavlvvv vggagyivvn alidtgdqii
      121 aslreaakdl srhlgaagts lddlasrske lvtkfggtaa sgllagvsvv gqvlaasila
      181 llltffflrd sdkavralrd wapgssapql ermarrgfhs iegfmrgttf ialidaicit
      241 vgllilqvpg aiglgalvfv gayipylgaf isgavailva ladrglvial walgvvlavq
      301 vleghvlqpm iqsrtvkmhp atvllaitag asvagilgml lsvpltaavt gvlhelrlhy
      361 aagsdsddsg paaspass
//
LOCUS       WP_457689151             317 aa            linear   BCT 27-JAN-2026
DEFINITION  pirin family protein [Streptomyces nigrescens].
ACCESSION   WP_457689151
VERSION     WP_457689151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33778
     Region          36..304
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mpavtvenpl tlprvaapva ahtrpvlava tapsgfegeg fpvrrafagi dykyldpfim
       61 mdqmgeveya pgepkgtpwh phrgfetvty lidgtfvhrd shggggvind gdtqwmtags
      121 gllhieappe slvmsgglfh glqlwvnlpk sdkmmapryq digggqvkll tsgdggallr
      181 liagdidghq gpgithtpit mmhvtvnpga eltlpwrkdf nalgyalagr gtagaegrpf
      241 hmgqavvfgt gdsitirade sqesrspnfe vvllgglpir epmrhygpfv mnthaelaqa
      301 fedfqagrlg tipadar
//
LOCUS       WP_457689152             608 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457689152
VERSION     WP_457689152.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10575288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..608
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66273
     Region          3..34
                     /region_name="AcylCoA_DH_N"
                     /note="Acyl-CoA dehydrogenase N terminal; pfam12418"
                     /db_xref="CDD:463571"
     Region          41..461
                     /region_name="ACAD_fadE5"
                     /note="Putative acyl-CoA dehydrogenases similar to fadE5;
                     cd01153"
                     /db_xref="CDD:173842"
     Site            order(162,164..165,170..171,196,198,440,447,449)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:173842"
     Site            order(171,224,445..446)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:173842"
     Site            445..446
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173842"
     Region          473..603
                     /region_name="Acyl-CoA_dh_C"
                     /note="Acetyl-CoA dehydrogenase C-terminal like;
                     pfam12806"
                     /db_xref="CDD:463716"
ORIGIN      
        1 mghyksnlrd iefnlfevlg rdsvygtgpf aemdvdtaks vlseiarlse nelaesfadt
       61 drnppvfdpd tntapvpdtf kksyqaymda ewwrlgipee lggttaprsl lwgfaetilg
      121 snpavwmyas gpafagvlye egteeqhria qlmvdkqwgs tmvltepdag sdvgagrtka
      181 vqqedgswhi egvkrfitsg ehdmsenivh fvlarpegag pgtkglslfi vpkydfdwet
      241 gelgerngay atnvehkmgl kasntcemtf ganhpakgwl lgekhdgirq mfkiiefarm
      301 mvgtkaiatl stgylnaley arervqgpdl aaftdktapr vtithhpdvr rslmtqkaya
      361 egmralvlyt atvqdeilvk eaagedasaa irlndlllpi vkgygseksy eqlaqslqtf
      421 ggsgylqeyp ieqyirdaki dtlyegttai qgqdfffrki vrdqgqalta lsdeikkfla
      481 dntggeeleq argelakaaa dleaivgtml tdlaatekdv ksiykvglnt trvlmasgdv
      541 vigylllkga avaaeklaga sakdkpfytg kiaaakffah nvlpgvsver glaesvdqsl
      601 meldeaaf
//
LOCUS       WP_457689161             300 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689161
VERSION     WP_457689161.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31771
     Region          36..82
                     /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"
ORIGIN      
        1 mrgvpgqqnh arvrrkplap lpdelsgpvr dfvaalrrmh gelgyslkql esrlpvsrss
       61 lsrylrgqsl pderllvqwc klsftgedrl palvellhrv qeaadagela aaerdaasdg
      121 epradaggpa ggagtgagaa ataglrrrrl vlaglgtaav llaaalavpa ltssngspdh
      181 ggdgrapdak saasatgsar itvhnverac qhrrtencal glardpyrly rrsnvvghvw
      241 hgdvlravcr iangitvtde vgghssmwfr vdhdgeqvwv pairiraeqv enttlpgcpd
//
LOCUS       WP_457689164             602 aa            linear   BCT 27-JAN-2026
DEFINITION  NHL domain-containing thioredoxin family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689164
VERSION     WP_457689164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10221921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..602
                     /product="NHL domain-containing thioredoxin family
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64240
     Region          10..135
                     /region_name="Thioredoxin_like"
                     /note="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold; cl00388"
                     /db_xref="CDD:469754"
     Region          <152..>263
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          177..214
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          212..524
                     /region_name="NHL-2_like"
                     /note="NHL repeat domain of NHL repeat-containing protein
                     2 and similar proteins; cd14951"
                     /db_xref="CDD:271321"
     Region          224..263
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          227..269
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          286..324
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          340..385
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          397..437
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          440..473
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
     Region          483..524
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271321"
ORIGIN      
        1 masrarvrap eltgkggwln tgnkdltlsd lrgrivvldf wtfccvnclh vldelrelee
       61 rhrdtvviig vhspkfvhea ehqavvdave rygvehpvld dpelatwkqy avrawptlvv
      121 idpegyvvaq hageghahai eklveeleae htakgtlrrg dgpyvppepv atdlrfpgka
      181 vrlpggsflv sdttrhqlve laadgeqvlr rigtgerglt adsfnepqgl allpdgrvav
      241 adtvnhairv fdpdsgalet vagtgkqwwq gsptsgpare vdlsspwdla wwqdrlwiam
      301 agvhqlwtyd paagtvgvaa gttneglvdg paaeawfaqp sglaaagdrl wvadsetsav
      361 rwvepadagd gyvirtavgt glfdfghrdg aagqallqhp lgvtalpdgs vavadtynha
      421 lrrfdpasge vttlakdlre psdavlvdgd ivvvesarhr ltrlrlpeea irvesvahrt
      481 qraatevapg alrlevvfqa pagqkldtry gpstrllvsa tppelladga gagtdltrdl
      541 vladgvtegv lhvsamaasc ddapdieypa chvhqqdwgv pleiaeggaa rlglvlagld
      601 ae
//
LOCUS       WP_457689166             274 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457689166
VERSION     WP_457689166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30115
     Region          13..244
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mtvhpslqss idawthsiea itelvtplve gewnratglp gwsvrdvvsh viglecemlg
       61 dprpihtlpr dlyhvrsesa rrmevqvdvr rhhtapemlg eleytvirrs rqlrnesrqp
      121 davvrsplge drslefvlqq rafdvwaheq dlrralgkpg nldspgahvt rdllvkvlpg
      181 ivakraqapa dsavvfdvsg pleflrtvri daegnatidg svslgptvtl aldwdtfhql
      241 acgrvrpaav aeqikidgda elaaaildhf avtp
//
LOCUS       WP_457689168             227 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689168
VERSION     WP_457689168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24449
     Region          11..223
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mpsastptap aresaakqpp aaervyahik davlerryeg gmlltegela eavgvsrtpv
       61 reallrleve gliklypkkg alvlpvsaqe iadvvetrll vekhaaakav pasqalvgel
      121 telletmreq aasgdlaavs vtdrafhaai vrsagnqild rlyeqlrdrq lrmgvavmha
      181 hpdriaknit ehaeilealr agdadaatdv vqrhvswvrn laqgevr
//
LOCUS       WP_457689176             497 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689176
VERSION     WP_457689176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..497
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51107
     Region          12..496
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mtastanaqr frefkmpdvg eglteaeilk wyvqpgdtvt dgqvvcevet akaavelpip
       61 ydgvvhelnf gegvtvdvgt viisvdtdpg agpatapape qapqeaakde eeaepqgrqa
      121 vlvgygaaps stkrrarkpq agvpaqpepv saalqaelng rtapapaapp apaapvapva
      181 pvangaaaga vgrplakppv rklakdlgid latiaptgpg gvitredvha aaapaavpap
      241 aevpgpapva eavapagtgv vdaaarerrv pvkgvrkata qamvasafta phvtefitvd
      301 vtrtmklvqe lkqdpdmagl rvnplllvak aflvairrhp evnaswdear qeivykdyvn
      361 lgiaaatprg livpnikdag vktlpqlaee lgdlvatare gktspaamtg gtvtltnvgv
      421 fgvdtgtpil npgesailaf gavklqpwvh kgkvkarqvt tlalsfdhrl idgelgskll
      481 advaavlerp krlitwg
//
LOCUS       WP_457689178             327 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Streptomyces
            nigrescens].
ACCESSION   WP_457689178
VERSION     WP_457689178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35467
     Region          5..327
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mavfekitia kaineslras meadpkvlvm gedvgklggv frvtdglqkd fgedrvidtp
       61 laesgivgta igmalrgyrp vveiqfdgfv fpaydqivtq lakmharalg kvkvpvviri
      121 pyaggigave hhsespealf ahvaglkivs psnssdaywm lqqaiagddp viyfepkrry
      181 hdksrldtes ipdplhkarv artgsdltla aygpmvkvcq dvanvaaeeg kslevidlrs
      241 lspidfdtvq ssvqktgrli vvheapvffg agaeiaarit ercfyhleap vlrvggfhsp
      301 yppsrledey lpgldrvlda vdralay
//
LOCUS       WP_457689191             379 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces nigrescens].
ACCESSION   WP_457689191
VERSION     WP_457689191.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..379
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41174
     Region          49..343
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mklpsqdaaa revpedrshr vllprrtpmp plrqvarrll mallvllstv fivwidrney
       61 hdnadgrvdl ldcfyyatvt lsttgygdiv pygdsarlln iliitplrvl fliilvgttl
      121 evltertreq wqlkrwrnal rdhtvivgfg tkgrsaaqtl catglnrdri vivdpsskvi
      181 daavadgfag vvgdatrsdv llwaevqrah qvviatqrdd tavlvsltar qlnrraniva
      241 avreeenapl lrqsgadavi tsasaagrll glsvhspsag tvmedliqqg sgldlvertv
      301 vkaevgksvr etddlvvsvl rghrllgydd peasplqitd rlitivraap teaadlsgkq
      361 sakptlpgtg vapmrrade
//
LOCUS       WP_457689197             553 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoamide acetyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689197
VERSION     WP_457689197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..553
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54543
     Region          4..550
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mavvreftlp dlgeglteat ivhwmvevge vvaidqpvve vetakamvev pcpyggvvta
       61 rfgeegaevp vgaplvtvav gavpddlaga gpgtgpgsga gaegsapdgg aaatnrdsgp
      121 tadgaadags gnvlvgygts aaaarrrrir pgpgagpmag vprppggaad gsagageaeg
      181 tpggsravaa gataigavgv tgaagasgad gsagtdgsag adgsagagav edgsrtvavi
      241 splvrrmare ngldlrqltg sgrdglilrt dverairarq erettgvaga aptvgagelt
      301 gagvtgvaga gavtavgsaa gamageerip lkgmlgaaae kfsrsrreip eatcwveada
      361 tellaarkam nvpgapkvsl lallaricta alarfpalns tvdtkaqeiv rlpavhlgfa
      421 aqtdrglvvp vvrdahartv eglsaeiarl tetaraggls laelthgtft lnnygvfgvd
      481 gstpiinhpe aamlgigria akpwvhegel avrqvvqlsl tfdhrvcdgg taggflrfva
      541 dcveqpalll rtl
//
LOCUS       WP_457689199             344 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Streptomyces
            nigrescens].
ACCESSION   WP_457689199
VERSION     WP_457689199.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36965
     Region          14..335
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mtttapatar kpatmaqalt ralrdamadd psvhvmgedv gtlggvfrvt dglakefged
       61 rctdtalaea gilgtavgma myglrpvvem qfdafaypaf eqlishvarm rnrtrgaltm
      121 pltirvpygg giggvehhsd sseayylatp glqvvtpatv edaygllraa iasddpvvfl
      181 epkrlywska dwlpdaptev aplgraairr pgssatlity gpslpvcmea aeaaraegwd
      241 levvdlrslm pfddetvcas vrrtgravvv hesngfggpg geiaariter cfhhleapvl
      301 rvagfdipyp ppmlerhhlp gvdrildtva rlqwesdwte grge
//
LOCUS       WP_457689233             120 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689233
VERSION     WP_457689233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..120
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13174
     Region          15..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 madhgeamcr qvdggmtrvf elfgkrwtgl ivatlmpgpv hfaelrrait gisermlsdr
       61 lmelaatglv vrevdagppl rvsyrlteag lamepalkel grwaetylad ggqcperfrk
//
LOCUS       WP_457689223             377 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689223
VERSION     WP_457689223.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39832
     Region          1..375
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdftfteeqq aaveaaravf sgvapdsvps paltpgavad dfdralwhkl adadllslpi
       61 apehggagld pialclvlre sakvlarvpl lesgaaaltl qrhatdelca evlprigage
      121 lvvtvaahgr tghepadlav eahqegaewv ldgvqtavpw arttdrillp ahtpeghtvl
      181 alvprshpdi tlddqvstsg eplaevrlds vrisaretit dpaawdslrn vlttgtcala
      241 lglgervlam tsdyagkreq fgfpvatfqa vacqaadrfi dlrameatlw qaawrittea
      301 tgplplagdv avaktwaseg vrrvvqtaqh lhggfgadtd yplhryhawa kqlelslgpa
      361 aaheeslgel laahplg
//
LOCUS       WP_457689235             216 aa            linear   BCT 27-JAN-2026
DEFINITION  FMN-dependent NADH-azoreductase [Streptomyces nigrescens].
ACCESSION   WP_457689235
VERSION     WP_457689235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase (NADP+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22745
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 matlllidss vfpeggsasr svtaafrkaw eeqhpdgtvi hrdlaadplp hldgagasaa
       61 fsdpashtpe qqaafalrvk laeeleqada ivigapmynf tipstlkawl dqviimgrta
      121 geqpsakgtp vtvvasrggs yapgtprepf eyvqnyleav lngglglevd fivpeltmap
      181 nnpamaelvp lyetsrdkah edaaakakal verlaa
//
LOCUS       WP_457689237             415 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689237
VERSION     WP_457689237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40139
     Region          33..400
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,236,239..240,243..245,248,276,280,331..332,
                     336,340,355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mtnieggaaa rgaevaaraa esgrkrgggl pavgalaaat ftvvtsemlp vglltpigre
       61 lrisdgtagl tltvtglvaa vsaplltmlv grrdrravlv almgtlaaan llaayapnvv
      121 vllvarvlvg lgmggvwaia aglavrlvpa rsvaaatsli fsgvaaasvl gvpagtflge
      181 lggrrtafga mavvcgavav alavllpplp eaaavrlngv lavlrgapvr tglvlvgllv
      241 tghfaaytyv rpvleqvaga gagqistlll afglaglagn flagagaars praallvicg
      301 vlagavllmp lagrgagvpg aalvvavwgl ayggvsvstq twlmaaapga reaasalfva
      361 vfngaialga laggraadgw gavgvmwlgg vlavgalvav gvgrapvrev pscpe
//
LOCUS       WP_457689238             308 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689238
VERSION     WP_457689238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32499
     Region          16..308
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 msgpsaatag lpgpglelre lecflvlsee lhfgrtgerl yvsqsrvsql lralesriga
       61 rlvdrtsrrv rltplgeefr tslrpaydal rttvesarsa argiegrlti gfqgtaddri
      121 mraidvfhrr hpgcateive iplcdpfgal rsgavdaavt llpvaepdlt lgpvfpaqqq
      181 tlavsvrhpl asratigaed lattplisaa gpapaywraa hapaatpqgr pipagpgvst
      241 lqegltlaaa grggmllcrp tadyhgrrdl vfvpvtglpg svlglvhhta rdtarvrafr
      301 tvvteiag
//
LOCUS       WP_457689244             460 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689244
VERSION     WP_457689244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48802
     Region          70..436
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mssttnttti gtigapsrrn telamlifav lipvfayvnv glakdgsvpa gvlgyslglg
       61 llagvahlvv rkwapyadpl mlpigtllng lglifiwrld qepslgkama pnqlmwstlg
      121 vafflailif lkdhrvlqry tyismvialv lliapmffpg vngakiwiti pglgslqpge
      181 fakiiiaiff agylmvkrda lalasrrfmg lylprgrdlg pilviwalsl milvfetdlg
      241 tsllffglfv vmlyvatert swivfgllls aggavavatf eshvqirvhn wlnplelqgg
      301 gvtetaqamy sfgsggilgs glgqgysrli qgiapksdyi latvgeeigl aglmailmly
      361 glliergirt alaardpfgk llaiglsgaf alqvfvvagg vtglipltgm tmpflaqggs
      421 svianwalia illrisdtar rpapapapst daemtqvvrp
//
LOCUS       WP_457689246             489 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689246
VERSION     WP_457689246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=52071
     Region          <75..489
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnkplrrvai fcgllvlall vrvnwvqfvq gdelkndphn rrvaierysi prgniivggk
       61 aitgssttds gdfkykrtyk ngkmwapvtg yasqafdanq leklndgilt gtddrlffsr
      121 tvdmftgskq kggnvvttld akaqkaafdg lgkqkgavaa inpetgaila lastpsydps
      181 tfagmsnkda eaynalqkks npdepmlnra lrqtyppgst fkvvtaaaal englyndvds
      241 strsplpytl pdtsgvelkn egnipcknas lrealrvscn tvfgkisadl gnkkmkaaae
      301 efgfndpgin tpvrasesif ptdnrpqnam agigqasnra tplqmamvas avanggklmk
      361 pymvdklvap nlnvvqqhtp kemsqplgpe naqkvqsmme tvvksgtgtn aqipnvtvgg
      421 ktgtaqhgen nkdnpyawfi syaktdkgtp vavavviegs dtlrddiagg klaapvakhv
      481 mqavlegek
//
LOCUS       WP_457689263             175 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Streptomyces nigrescens].
ACCESSION   WP_457689263
VERSION     WP_457689263.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=18815
     Region          1..175
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 maeqlyatlk tnqgdieirl lpnhapktvk nfvelanger ewthpatgkk stdrlydgtv
       61 fhrvisgfmi qggdplgngt ggpgyefgde fhpdlafnkp yllamanagp gtngsqffit
      121 vgatawltgk htifgevsne askkvvdaia gtqtnprtdr plqdvviesv aietr
//
LOCUS       WP_457689267             182 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689267
VERSION     WP_457689267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..182
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19145
     Region          12..>61
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mdsaqqeata rardlqrnwy geplgalfrr liddlglnqa rlagvlglsa pmlsqlmsgq
       61 rakignpavv qrvqalqdla gqvadgsvsa aeatdrmeei kktaggsvln ntaqqtsstg
      121 attvrrvvre iqsllrsvad agdiidaant lapahpelae flrvygagrt adavahyeah
      181 qs
//
LOCUS       WP_457689284             168 aa            linear   BCT 27-JAN-2026
DEFINITION  Jag family protein [Streptomyces nigrescens].
ACCESSION   WP_457689284
VERSION     WP_457689284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Winther,A.R., Kjos,M., Stamsas,G.A., Havarstein,L.S. and Straume,D.
  TITLE     Prevention of EloR/KhpA heterodimerization by introduction of
            site-specific amino acid substitutions renders the essential
            elongasome protein PBP2b redundant in Streptococcus pneumoniae
  JOURNAL   Sci Rep 9 (1), 3681 (2019)
   PUBMED   30842445
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Zheng,J.J., Perez,A.J., Tsui,H.T., Massidda,O. and Winkler,M.E.
  TITLE     Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins
            suppresses the requirement for PBP2b by overproduction of FtsA in
            Streptococcus pneumoniae D39
  JOURNAL   Mol Microbiol 106 (5), 793-814 (2017)
   PUBMED   28941257
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Errington,J., Appleby,L., Daniel,R.A., Goodfellow,H.,
            Partridge,S.R. and Yudkin,M.D.
  TITLE     Structure and function of the spoIIIJ gene of Bacillus subtilis: a
            vegetatively expressed gene that is essential for sigma G activity
            at an intermediate stage of sporulation
  JOURNAL   J Gen Microbiol 138 (12), 2609-2618 (1992)
   PUBMED   1487728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="Jag family protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=18110
     Region          25..168
                     /region_name="Jag"
                     /note="Predicted RNA-binding protein Jag
                     (SpoIIIJ-associated), conains KH and R3H domains [General
                     function prediction only]; COG1847"
                     /db_xref="CDD:441452"
ORIGIN      
        1 mtdttpateg tdtltrleqe geiaadyleg lldiadldgd idmdveadra avsiisdsts
       61 rdlqklvgrd gevlealqel trlavhretg drsrlmldia gfrarkreel selgakaaee
      121 akgtgepvkl dpmtpferkv vhdavaaagl rsesegeepq rrvvvlpa
//
LOCUS       WP_457689286             365 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Streptomyces nigrescens].
ACCESSION   WP_457689286
VERSION     WP_457689286.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38640
     Region          82..346
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mserrrglgr glgalipaap qstdhagpag qgatspssvp vlapergvaa akvtslpahg
       61 vsreteapag aeasaagvse vagahfaevp ldaikpnprq prevfdedal aelvtsikev
      121 gllqpvvvrq tgpgryelim gerrwracre aglekipaiv ratddeklll dallenlhra
      181 qlnpleeaaa ydqllkdfkc thdeladrig rsrpqvsntl rllklspsvq krlaagvlsa
      241 gharallsve dseeqdhlar rivaeglsvr sveeivtlmg sapkgaskat gpragarvsp
      301 altglasrls drfetrvkvd lgqkkgkivv efasmddler ilgtlapgeg rvlgqtlaee
      361 nneee
//
LOCUS       WP_457689301             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689301
VERSION     WP_457689301.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43699
     Region          16..415
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(26..27,30..31,34,69,123..124,126..128,131,149,
                     152..153,156,245,248..249,252..254,257,285,289,342..343,
                     347,351,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mhavralrvl lrlrdfrsll aarllsqaad gvfqvalatf vvfspekqas paaiasamai
       61 lllpysllgp ftgvlldrwr rrqvllygnl lrallamata tlivskapdw lfyasalsvt
      121 avnrfvlagl saalprvvdg eqqlvmansl tptagtlaat aggglafavr lagsdvdafv
      181 vllaaalyfc salttlrmap qllgpdpvrl qphlkealls tvrglgeglh hlaerrtpar
      241 aliamavirf cygaltvmvl mlcryswaet eseglallgi tvgvsgagff aaavvtpwav
      301 grltafgwia gcaalgavlv pslglfftpg pmlaaafvlg lstqgtkist dtivqstvdd
      361 afrgrsfaiy dvlfnvafvg aaavaalmlp pdgrsaallg mvtvlyalva aamvrsgrg
//
LOCUS       WP_457689305             226 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689305
VERSION     WP_457689305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 226)
  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 226)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25460
     Region          4..98
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msrrsgvlef avlgllresp mhgyelrkrl ntslgvfraf sygtlypclk alvasgwlie
       61 etdgapegvp aasltgrrak ivyrltsagk ehfeellahs gpdawedehf gvrfaffgqt
      121 srdvrmrvle grrsrleerl ermrtslars rerlddytle lqrhgmesve revrwlneli
      181 eseragrdqr ptgsaaqdkk nqsgdtgglp rhrggsrpdp sddttt
//
LOCUS       WP_457689307             885 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689307
VERSION     WP_457689307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..885
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=93549
     Region          121..785
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msehrrkppq pqsggraaar raaqqppgrr aapsrgsaag saahsepsgy eprqggrada
       61 rraaqrggrr rssdaamasg dgaggrgggg rrggggggpe ggrgrgrggg kpakkrlidy
      121 pranrvgwrr fvpswkqvtt lcvgfigliv gasgvalalv hvpsesdaak sqnnvylwsd
      181 gkvmardget nrqnvtinei plemqkaaia aenasfrtds gvdpmgiara lvnmakgget
      241 qggstitqqy vknamlsqeq tldrkfkelf iaikvgwsks kdqilqgyln tsyygrgayg
      301 iqaaaqayyg vdaeklnanq saflatvlkg adlydpaggt spgatraant krakarwswi
      361 ldrevennll skaerekyrg hfptpnlpkp vasksgqigy mmdtakkyvl knsglseaqf
      421 dkggytihtt fsskktnqle tavkqvnkry idpkkrakdk fvqfggasvv pgdgkivaly
      481 ggegydkghf snnadtfgvp vgstwkpfvl aaamkngtvk sngvpvrqds ryngddhlkv
      541 kdaqggyvkr rdgsyffqen esnhpwgyis ltkameqsvn tpfvqlgmdv gmdkvrdmae
      601 atgiskasfd knlnpsfalg tstpsairma dayatfaqsg tkvepysvtk vsykgrdldg
      661 fekprsatam epniannvtk vlenvidngt akeakrlnmp aagktgttde nksawfvgyt
      721 kqlstaitmf redagnprql smngvggfds ihggalptev wteymlqamk gvtpesfppa
      781 tpigqrldqe gvptptptpt psdtpsstps espsesvppt nspsptptds cspwdlecrn
      841 sggasngggn gngaggpggg pggtsptpdp tdatdsggwl ggpng
//
LOCUS       WP_457689309             493 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 87 protein [Streptomyces nigrescens].
ACCESSION   WP_457689309
VERSION     WP_457689309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Morita,Y.S., Sena,C.B., Waller,R.F., Kurokawa,K., Sernee,M.F.,
            Nakatani,F., Haites,R.E., Billman-Jacobe,H., McConville,M.J.,
            Maeda,Y. and Kinoshita,T.
  TITLE     PimE is a polyprenol-phosphate-mannose-dependent
            mannosyltransferase that transfers the fifth mannose of
            phosphatidylinositol mannoside in mycobacteria
  JOURNAL   J Biol Chem 281 (35), 25143-25155 (2006)
   PUBMED   16803893
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..493
                     /product="glycosyltransferase family 87 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54622
     Region          47..460
                     /region_name="COG5650"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444371"
ORIGIN      
        1 mtsvrrddpv rptkrdevaa agseliggpi grrallgthw ltpvriialv aigmfalgmv
       61 qklpcynggw ffgattqyth acysdiphly agrgfadgli pyfdrlpgdm eyleypvltg
      121 vfmevaswmt phaggiqhre qiywlvnagm lmicaaviav cvarthrrrp wdgllvalap
      181 afaltatinw dllaialtaa gmlmwsrsrp laagiligla taaklypvll lgpllvlcwr
      241 agawrayrra ltgtvaswlv vnlpvmithd aagfhiregw akfytfsqer pidfgsiwll
      301 isqrtgnple nantyatllm ivgcgaigll tlyaprrprf aqlaflvval filtnkvysp
      361 qyvlwltpla alarprwrdf liwqacevmy flgiwtylay tgsgdkhqgl ptegyqlaia
      421 lhllgtlylc alvvrdilmp erdvvrrdgd ddpsggvldr spdvfvlgra hhrprhavqf
      481 qaapqvrwga vrd
//
LOCUS       WP_457689317             281 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457689317
VERSION     WP_457689317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="trypsin-like serine 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=30035
     Region          73..279
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mlpltfvvmv aaavvgyate eadtnsssgg grssfgksge agqdpqdqdp aatapagdgn
       61 aytprrteqn arvgavfekd dsgdhfctas vvqspgrnml itaahcafds dgktpvndlv
      121 fapdyrdgde ptglwkvkkv ilddrweksn dedldvaflv ldkkkgkeiq dvlggntlgi
      181 drgyenevki tgyptsrdtp iscqnrttkf sdtqlrirct dfeggtsgsp wladydpksh
      241 tgtvigvlgg hegggdqddv syaayfdddi aalykraqde d
//
LOCUS       WP_457689319             445 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Streptomyces nigrescens].
ACCESSION   WP_457689319
VERSION     WP_457689319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..445
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45670
     Region          15..435
                     /region_name="MATE_DinF_like"
                     /note="DinF and similar proteins, a subfamily of the
                     multidrug and toxic compound extrusion (MATE)-like
                     proteins; cd13136"
                     /db_xref="CDD:240541"
ORIGIN      
        1 mtlapatprr tgrrhdreii alalpafgsl vaeplfvmvd savighlgtp qlaglgvaaa
       61 llttavsvfv flayattaav arrvgagdlp aairqgmdgi wlalllgaav iaavlptapw
      121 lveafgasgt aapyamtylr isalgipaml vvlaatgvlr glqdtktply vaiggfsana
      181 vlniglvyga glgiagsawg tviaqfgmaa vylvvvvrga rrhraslrpd aagirasaqa
      241 gvpllvrtls lravlmiata vaarlgdaei aahqivltlw sllafaldai aiagqaiigr
      301 ylgagdrdga raacrrmvqw giasglvlgv lvalarplfi plftadpavq gpllttllvv
      361 avtqpvsgiv fildgvlmga gdgpylawam vvtlalfapl alvvpllggg lvalwwamal
      421 mmtvrmltlw lrtrsgrwiv tgasr
//
LOCUS       WP_457689323             321 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457689323
VERSION     WP_457689323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33539
     Region          9..317
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(48..50,53,135,139,161..166,185..186,188,202,
                     221..222,243,246,265..267)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 msetgapqmr avsqdtaggp evlkvittdr pvpgpteilv rvhaagvnpa dwktraggrf
       61 ltgseppfil gfdvsgvvea vglgvtlfap gdkvfgmprf phpagayaey vtaparhfah
      121 lpagldhlqg aalplaslta wqalvdtaqv qpgarvliha aaggvghlav qiaksrgayv
      181 igtarrakhd flrglgadel idyterdfet avrdvdlvld tisgdygars lrtlrpggsl
      241 vsvlplddtf padrareaqv raafvlvepd rsglqavael vntgklqvnv dtvfplehaa
      301 kahalgetgr ttgkivltva p
//
LOCUS       WP_457689325             324 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689325
VERSION     WP_457689325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..324
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34540
     Region          2..321
                     /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 mhrvgvlald gvvpfelgip arifgaacsa ageplysvvt csldgrpvrt eadydiavse
       61 dasvlahvdt vvippshgla tfreggrlpd dlraalerir pgtrmvaict gsfvlaaagl
      121 ldhrpatthw reaaqlqrlf ttvrvdpnvl fvddgdvlts agaaagvdlc vhivrrdhgs
      181 avanevarlc vvppwrdggq aqfirqpvpe psaggtaatr awalerlgep ltltdlaaha
      241 rvsvrtltrr frdevgmspg qwlagqrier arhllettdw pidlvahhag fgtgtslrqh
      301 lhsavgvapl ayrrtfrsaa alta
//
LOCUS       WP_457689331             482 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689331
VERSION     WP_457689331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51848
     Region          29..353
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtiaqstefp rpepvgpgpg avgtpdefae llpqtrrall rrlavgqaeg rapsmtgavv
       61 rdgravwtga rgtvagevph gdvqyrigsl tktfvavlvl rlrdegllrl edpvgrhleg
      121 tpvpdatiaq llshsaglaa eprgpwwert tgelrpepad lfderpqrlp agrrhhysnv
      181 gyallgalve rlrggapwge vlrrevlepl gmdrttlrpe rpyasgwavh pwadallpep
      241 aedtglmgpa gqlwstlqnl crwaafllrg darvlgaasl aelrtpavpp esgtwdagyg
      301 lgvqllrreg rllvghqgsm pgflaalwad veedvagvvl tnctsgpaag alaadltgiv
      361 iaqepripep wrplpgpldp ellaltgpwy wganphalrl raergleltp lsgagrssrf
      421 raeedgtwtg ldgyytgetl rvrrdrdgvv shldlgtfvf trgpyepsap vpggvdpegw
      481 rv
//
LOCUS       WP_457689334             251 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689334
VERSION     WP_457689334.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26495
     Region          10..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdggvtpsr adarrnralv lqaarsafee qglevplgei arragvgagt vyrhfpskea
       61 lfrativdri elftdtardl aevadpgavf frflssvvrl avrnkalcda leaagagrfe
      121 pspgvgqdfd dalevllrra qeagavrqdv giadlrallv gclsmeravp gsgsgggapg
      181 rmtalmcdal rteravtavt eleaesvkrn esrcgvcgaa iaaartgrpa rycggacrqk
      241 ahrarertrq t
//
LOCUS       WP_457689338             175 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457689338
VERSION     WP_457689338.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18818
     Region          27..168
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtqqtrdkre tqktavpqpa aaepgcpsae ppglaqgwca lsalhgries hieralqtah
       61 dlsvrefsvl nvlseqhdgp gghlrmhqva dsvvlsqsat trlvtrledr gllsrylcpd
      121 drrgiytnvt sdglallvea rpthdgalre alkdaaqrpe laplvtavet lappe
//
LOCUS       WP_457689340             406 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689340
VERSION     WP_457689340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41195
     Region          10..372
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(15..16,19..20,23,55,105..106,108..110,113,133,
                     136..137,140,208,211..212,215..217,220,248,252,301..302,
                     306,310,325,328..329,332..333,336)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mplallalai gafgigttef avmgllpdma agfgvsipla gyattlyalg vvvgaplmta
       61 lgtrftrkqm lillmglfiv gnlltalapn fgimlagriv aafthgaffg igalvaadlv
      121 apqkratais lmfsgltvan vvgvpagtml sqqsdwrttf yaitalgvig llgivklipa
      181 qqakaaspig selavfrnpq vglamlmtil gfggvfaavt ylasmmtevt gfapssviwl
      241 taifglgmvg gnlvsgrftd rammpmlfvs ltglalslaa ftftahdkta atvtialigi
      301 fgfatvpplq krvmdqaasa ptlasagnia afnfgnalas wlggivisag lgytapnwvg
      361 almtvaalgv aifasvlerr qtsrgqvvaa grpgvvadep vpaahg
//
LOCUS       WP_457689341             145 aa            linear   BCT 27-JAN-2026
DEFINITION  GlcG/HbpS family heme-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689341
VERSION     WP_457689341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Ortiz de Orue Lucana,D., Bogel,G., Zou,P. and Groves,M.R.
  TITLE     The oligomeric assembly of the novel haem-degrading protein HbpS is
            essential for interaction with its cognate two-component sensor
            kinase
  JOURNAL   J Mol Biol 386 (4), 1108-1122 (2009)
   PUBMED   19244623
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Pellicer,M.T., Badia,J., Aguilar,J. and Baldoma,L.
  TITLE     glc locus of Escherichia coli: characterization of genes encoding
            the subunits of glycolate oxidase and the glc regulator protein
  JOURNAL   J Bacteriol 178 (7), 2051-2059 (1996)
   PUBMED   8606183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14822
     Region          9..140
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mstptvtptv rplptreada lieaavraad glgvrgsvtv ldaggqllgf rrddtavlis
       61 getstckayt alqldaptgd lvdlvrpdgl fhtlptaldr pllfiaggvp lhrdgrliga
      121 lgfgggapeq ddrivtaaia eadlv
//
LOCUS       WP_457689345             211 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457689345
VERSION     WP_457689345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22589
     Region          1..191
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msklhlfdmd gtllygsaaa ieisrqlgld reigelergf aagaltpvqf aqracelwaa
       61 eltelqvaaa fdgapwltgi revwadirar gercavisls paffverllp wgadaahgsr
      121 wpavpirqav epagiltsaa kvriadelcv qygltradcv aygdslsdte lfaavpqsva
      181 vnadhhvsdl asyayaggdl reayelvrtg r
//
LOCUS       WP_457689352             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689352
VERSION     WP_457689352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31391
     Region          1..295
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdlallrtlv tvhragsftr aaallglsqp avtsqirale rqlgrplflr yargvtptti
       61 gdelahkvap hldalteite agldrdsvtr tlhlagppef lteralpala plisqglsir
      121 tafgsaedml aglaaghhdl tvtttrprgg lltatplcde ehvliaaphw eaqlggpgvl
      181 qaggvrlldp vpivevhesl plitrywsav fdakptasaa vitgdlravl scvaagagla
      241 vlprylcada laggevltll dppvpplrty flavrtgtlg lphiarahew llrsavdw
//
LOCUS       WP_457689356             217 aa            linear   BCT 27-JAN-2026
DEFINITION  low molecular weight protein-tyrosine-phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457689356
VERSION     WP_457689356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   He,R., Wang,J., Yu,Z.H., Zhang,R.Y., Liu,S., Wu,L. and Zhang,Z.Y.
  TITLE     Inhibition of Low Molecular Weight Protein Tyrosine Phosphatase by
            an Induced-Fit Mechanism
  JOURNAL   J Med Chem 59 (19), 9094-9106 (2016)
   PUBMED   27676368
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Zhang,Z.Y.
  TITLE     Mechanistic studies on protein tyrosine phosphatases
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 171-220 (2003)
   PUBMED   12882518
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Wang,W.Q., Sun,J.P. and Zhang,Z.Y.
  TITLE     An overview of the protein tyrosine phosphatase superfamily
  JOURNAL   Curr Top Med Chem 3 (7), 739-748 (2003)
   PUBMED   12678841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="low molecular weight
                     protein-tyrosine-phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=22879
     Region          6..179
                     /region_name="LMWPTP"
                     /note="Low molecular weight protein tyrosine phosphatase;
                     cd16343"
                     /db_xref="CDD:319971"
     Site            order(11..18,49,155,157)
                     /site_type="active"
                     /db_xref="CDD:319971"
ORIGIN      
        1 mtapfricfv ctgnicrspm aesvfrarla eagldgrvev dsagtggwhe gdgadprtva
       61 vlraggyeha htarqfhasw fdrldlvial dsghlrelrr laptaqdaak vrllgsygtg
      121 aatgamadsg sgpvpvpasa lvsdpdlsad ldvpdpyygg fegfeeclem vetasegllt
      181 avraalpart vvtarapehd nrraarephq pqekesa
//
LOCUS       WP_457689358             269 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689358
VERSION     WP_457689358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28955
     Region          23..258
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mphcertwgl alaivngesa shptligsvq ralrlleavg ahpdgapakq lareaglplp
       61 ttyhllrtlt hegylrrvsg vfvlgaaaea igragarhrq rahisealav agrelgaavy
      121 favyregeve vvavtddpar ppvtewvdfr ttahahaigq cllaqldeaa rkehlarhpv
      181 qsitpfsmrt eddllhrldt vrrgqvayer qeyalgtvcs aipvqvgaaa atlavslpvg
      241 elrrlrsvtd rlrkmaeatl ttlafsisi
//
LOCUS       WP_457689369             366 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689369
VERSION     WP_457689369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  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   2  (residues 1 to 366)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38746
     Region          18..352
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtaagkhqvs rstgrrlgra girdvaaaag vsittvsdal ngkgrlpdat rshvrevadr
       61 lgyrpsaaar tlrtgksgll gltvttygde pftftefayf aemaraatsa alargyalvi
      121 lpatsrhdvw snvaldgtvv idpadgdpvv telvrhgipv vsdgrpggal pvtgwvdndh
      181 eaavlglldh ladagarrig lltgnttdty trlsttaylh wcervgqdpv yesypahdpc
      241 agavaadrll arpdrpdavy glfdpngtdl laaarryglr vpedlllvcc sestlyaate
      301 ppittlslkp rrigtaviqi lidaiegldn grpieqvipt dlivrassqr rsprttvspp
      361 rgptcd
//
LOCUS       WP_457689372             502 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome ubiquinol oxidase subunit I [Streptomyces nigrescens].
ACCESSION   WP_457689372
VERSION     WP_457689372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..502
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55722
     Region          7..476
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 melalapetl arwqfgittv yhflfvplti slaalvagle tawvrtgkek ylkatkfwgk
       61 lfliniamgv vtgivqefqf gmnwsdysrf vgdvfgapla fealiafffe stfiglwifg
      121 wdklpkkihc fcmwmvsigt ilsayfilaa nswmqhpvgy kynaangrae ltdfwkvltq
      181 dttlvvvfht ltaafltgaa fmvgiaafhl mrkkhikvmr tslrlglitl visgiltavs
      241 gdqlgkvmfk qqpmkmaaae alwetekpap fsvfaygdvd eghnkvaiev pgllsflahn
      301 dftspvpgin dvnrseqqkf gpgdyrpnip vaywgfrwmi gfgmssfaig laglwltrkk
      361 fwlapglrtg deepprlalt knrelgarls kwywslafvt lgfpllassw gwiftemgrq
      421 pwavygvlrt sdavspgvsq gevltsmivf ttlyailavv evkllvkyvk agppeltdsd
      481 lnpptkiggd stdadrpmaf sy
//
LOCUS       WP_457689380             299 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457689380
VERSION     WP_457689380.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32576
     Region          24..298
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mrlstlilpv rrwseggrev wqraeelgfh aaytydhlsw rsfrdrtwfg alptltaaas
       61 vtsrmrlgtl vtspnfrhpv tlakelisld disdgritlg vgaggngfda talgqepwap
      121 reradhfdef valldrllsq dvvshegahy sahevrnipg cvqrprlpfa vaatgprglk
      181 laarygqawv ttgdpkvsng ggspaesrea irgqlerlgk acadqgreva dlqkimltgf
      241 tpdrpldsvd afvdfagrha elgidelvlh wpiadslfet dvavferiat egaaqlaar
//
LOCUS       WP_457689390             351 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689390
VERSION     WP_457689390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36640
     Region          13..232
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 magtttvddv tvivteslsk rfprvtaldr lsvdiapgvt glvgangagk stlikillgl
       61 apategtahv lgldvtkdgg tirervgymp ehdclppdvs atefvvhmar msglpptaar
      121 ertadtlrhv glyeeryrpi ggystgmkqr vklaqalvhd pqlvfldept ngldpagrde
      181 mlgliqrvhs dfgisvlvts hllgelertc dhvvvidggk llrssstdef tqvtaslave
      241 vtdtdahpdg tealraalaa tgaavttraa gseglaasgh llyveaagee tydlvrdtva
      301 glglglvrme qrrhqiaevf rdadaaqaap atagapsapy atqdggahdv a
//
LOCUS       WP_457689396             423 aa            linear   BCT 27-JAN-2026
DEFINITION  CynX/NimT family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689396
VERSION     WP_457689396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43055
     Region          38..418
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(48..49,52..53,56,88,137..138,140..142,145,164,
                     167..168,171,249,252..253,256..258,261,288,292,341..342,
                     346,350,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 magprseapl idaeedlvaa ppvaaarrrl rahpalvmtg ivlaalnmra alagvspllg
       61 eigahfrlta tasslvttip lifmglgsia apklarrwgt etalcaalva lcggivlria
      121 ppvvalfagc avvgasiall nvlmpglikr dfperaagmt alystamilg atvsaasavp
      181 mehvlggwqg alvswallaa vaaviwipqt lmarrgtrhg aaaatplhla edgprlsrsp
      241 lawqvtlfmg sqsliayvsi awmptiftdh glgkgeaglv fafstlvqma gsfvvpmlag
      301 rmrrqrllav avtalmacgi tgllvapvag awlwatllgv gqggalglal tmmvlrsgda
      361 htaarlsgma qtggyllaaa gplvlgavhq atdgwtvplv lllavcagla llgmgagrdr
      421 rig
//
LOCUS       WP_457689389             288 aa            linear   BCT 27-JAN-2026
DEFINITION  M24 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457689389
VERSION     WP_457689389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lowther,W.T. and Matthews,B.W.
  TITLE     Metalloaminopeptidases: common functional themes in disparate
            structural surroundings
  JOURNAL   Chem Rev 102 (12), 4581-4608 (2002)
   PUBMED   12475202
REFERENCE   2  (residues 1 to 288)
  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 10099437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="M24 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32763
     Region          19..263
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cd01066"
                     /db_xref="CDD:238514"
     Site            order(87,104,115,203,241,254)
                     /site_type="active"
                     /db_xref="CDD:238514"
ORIGIN      
        1 masvtsatsp gageltaglr gfrevqrlay acaeavaaql kpgvteraaa rmqrewlrer
       61 gvrdwfhlpf awfgdrtaft nfrvplqffp threlepgma fildmapihn gytadigysg
      121 clglnpvhdr lladleahre lilrevrerr plreiyedvd rlmvrqgyan rhraypfgvi
      181 ahkvdrvrqr rwsptlfgfg tqslrglasd alhghrdgws plwspysfsd hppqpglwav
      241 ephlgfrgtg akfeeilvvt dsknpqesaf wldddlphvr rwqeekaa
//
LOCUS       WP_457689404             307 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689404
VERSION     WP_457689404.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32335
     Region          1..297
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mtlddlrafv avceagnlsa vardlgctqs avsqrikrve raagidller rprgvaptqa
       61 grilhraaad glsgldlalr rladlragdg gtvrvttgat tvrhfmsdav vafrarhphv
      121 nlefqtesss rrcfeavadg sselawitig ppergieqhp virlpwvlav raddpladre
      181 ciepgelagi rhirlpenst srmrldghlg hrdagpvppp sttsvadwdt alllaelgvg
      241 pavvpqlpgl pataqpalrl vpiaglppla tgwavrrwaa lspaavafae tvtaclggaa
      301 tegevvr
//
LOCUS       WP_457689406             528 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689406
VERSION     WP_457689406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..528
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52623
     Region          36..493
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,238,241..242,245..247,316,344,348,401..402,
                     406,410,426,429..430,433..434,437)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrsapergta vggrspgagg epgggpagkw wplaaitlgn vlllvdvtiv ntalpriadg
       61 lgatltslqw vldiyalala allmvagsta dlfgrrrlyv agltlfalas lvcglapdag
      121 vlvaaravqg vgaaamfatn tpllmaayqg rdrgvafgvw ggssgaaaai gpvlggllte
      181 yvdwraiflv nlpltavavw itvrrvpesh gdlprprths agrtplarid wlgaasftvc
      241 agaltyglmr ggeegwtepg tlaalggaal allvfivver rvqrplldlg llrrpafaal
      301 laaalllqaa afpyltfvgl wvqnilglsp vqaglaatpm alvsllvgal ggrllqrtap
      361 qlpvgigmll vgagvlleya llddgagwaa lvpglavsgl gvgaampvlv satlgaappq
      421 ragmasgavn tsqqlgyalg iavlgtvfad alhdvrpgas rtavaaahvs gltdillisg
      481 tvalvggllv lavvrrgagg dgdgdgdgdr paarvagapa ragapgga
//
LOCUS       WP_457689402             314 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689402
VERSION     WP_457689402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 314)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33038
     Region          2..110
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            40
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(51,54,58..59,68,82,86,92,96,99..100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          121..307
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mfsigdfaqy grvsarmlrh ydaigllrpa rtdpvsgyrf yeaaqlarln riialknlgf
       61 slqqvgailt eevsvpelrg mlrlrqaele aaltaagarl aqvearlrti esegrmsadd
      121 vvvkrtgtvl laelsgiaas ygpedigpvi tplyaelcrl letagvtpag tglayyedvp
      181 epgkgserpa ggndgkdaiv vhagmvitee alakagvtag vtagamaggt sgrpgapsat
      241 glgfdvvtlp gldsaatvvh rgpmsrilpt aqnlahwidd ngyrsagyar elylecppdp
      301 ekwvteiqep vvra
//
LOCUS       WP_457689408             352 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689408
VERSION     WP_457689408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37476
     Region          26..155
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          195..329
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mksdgkpeva drgkgtgdpg sptgfdtldh rlihalqldg rapfsriaav lgvsdqtvar
       61 rytrhrthgt lkvlglpdaq algevqwlvr vqctpdaava vaealarrpd tswvglmsgg
      121 teitavcrav ssdhsdvlll qklprtpsvi gvtahcrlhq fyggpqglis ksgaltdeqi
      181 arlspplpdp aaapvtltda drrlfdllar dgrtplaela aatgwspttv rrrfaelran
      241 gvlyydvdyd lrqfgygvmv alwlsvepar laaageamat hpevayacat tgpnnlfasv
      301 lcrnvgavyt ylttrvaalp gvrsmesapr irhikgpgpl fsaghaapgr rr
//
LOCUS       WP_457689411             276 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457689411
VERSION     WP_457689411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28738
     Region          13..273
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 msapapaagt plpfkliatd ldgtllrsde tvsertrqal aaataagaah ivvtgravpw
       61 trhildaldy rglavcgqgg qvyhagehrl ltsvtldrql aglalskiea evgplylaas
      121 rdglegevlv gpgyrvqegp lpnvlmddpg elwaapinkv yiqhptlddd alalvarqva
      181 gdlvgvtvag egivellplg lskatglsla arrlgltake tlafgdmpnd ipmfawaarg
      241 vamanahdel kavadeftas neddgvavvl erlyls
//
LOCUS       WP_457689419             788 aa            linear   BCT 27-JAN-2026
DEFINITION  copper resistance CopC/CopD family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689419
VERSION     WP_457689419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   van Sorge,N.M., Bonsor,D.A., Deng,L., Lindahl,E., Schmitt,V.,
            Lyndin,M., Schmidt,A., Nilsson,O.R., Brizuela,J., Boero,E.,
            Sundberg,E.J., van Strijp,J.A.G., Doran,K.S., Singer,B.B.,
            Lindahl,G. and McCarthy,A.J.
  TITLE     Bacterial protein domains with a novel Ig-like fold target human
            CEACAM receptors
  JOURNAL   EMBO J 40 (7), e106103 (2021)
   PUBMED   33522633
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Lawton,T.J., Kenney,G.E., Hurley,J.D. and Rosenzweig,A.C.
  TITLE     The CopC Family: Structural and Bioinformatic Insights into a
            Diverse Group of Periplasmic Copper Binding Proteins
  JOURNAL   Biochemistry 55 (15), 2278-2290 (2016)
   PUBMED   27010565
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Cooksey,D.A.
  TITLE     Molecular mechanisms of copper resistance and accumulation in
            bacteria
  JOURNAL   FEMS Microbiol Rev 14 (4), 381-386 (1994)
   PUBMED   7917425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18622140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..788
                     /product="copper resistance CopC/CopD family protein"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0046688 - response to copper ion [Evidence
                     IEA]"
                     /calculated_mol_wt=80614
     Region          <43..140
                     /region_name="CopC"
                     /note="Copper-binding protein CopC (methionine-rich)
                     [Inorganic ion transport and metabolism]; COG2372"
                     /db_xref="CDD:441939"
     Region          358..>494
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; COG1276"
                     /db_xref="CDD:440887"
     Region          <692..774
                     /region_name="FixH"
                     /note="cl46415"
                     /db_xref="CDD:480755"
ORIGIN      
        1 mvttglrprr savlrllvva lalagtligg lggaapasah aaltgstpaq gsvvdrapeq
       61 vtltfsegva lgddsirvld pqgkrvddkk lrnlssdrvv kygaglppgl rdgtytvawq
      121 avsadshpvs gaftfsvgap skttapvpqq eaggglvgtl ygiarylaya gfvllaggaa
      181 fvvvcrpaaa lvrsvqqlvv ygwallagtt vvmlllrtpy tgsgdladvf dlgglqqvli
      241 tkpgaalvsr llllaaaalf vavlfgayar ahepaevdgq gadgqgaaga rgesgaader
      301 gasdergald aadergasdg sgrgaadaee raeeqaddaa eqarrrkdlt fglgfggviv
      361 atglaatwam aehastglqp avampvdvlh llavaawlgg laalvvslyw gppversavr
      421 rfsrlafgsv vvlvatglyq swrqvgtwqa ltdttygrll lvkvalvvvl vgiawlsrqw
      481 tgrlaevpaa elrapedaeq gaeheagkea gkeagkeahk daekeaekat vgasaaaata
      541 gpastsgssp ksgssptrgp spksgsspas detpathdip taddgtstpd dtpvpdpara
      601 aqlarqqaal rtartkrqrd adperlglrr svlaeasvav vllvvttalt ateparteaa
      661 vkatsggqsa aagrpqvlti pfdtggphgk gtarvnlapg rsgsantlql risdpsgkam
      721 dvpevkvsft ektkklgpls vttrhtgkgq wrasgvqlpv pgkwqlslvv rtsdidqvte
      781 iknvkigs
//
LOCUS       WP_457689421             148 aa            linear   BCT 27-JAN-2026
DEFINITION  copper chaperone PCu(A)C [Streptomyces nigrescens].
ACCESSION   WP_457689421
VERSION     WP_457689421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Fisher,O.S., Sendzik,M.R., Ross,M.O., Lawton,T.J., Hoffman,B.M. and
            Rosenzweig,A.C.
  TITLE     PCuAC domains from methane-oxidizing bacteria use a histidine brace
            to bind copper
  JOURNAL   J Biol Chem 294 (44), 16351-16363 (2019)
   PUBMED   31527086
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Abriata,L.A., Banci,L., Bertini,I., Ciofi-Baffoni,S., Gkazonis,P.,
            Spyroulias,G.A., Vila,A.J. and Wang,S.
  TITLE     Mechanism of Cu(A) assembly
  JOURNAL   Nat Chem Biol 4 (10), 599-601 (2008)
   PUBMED   18758441
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Banci,L., Bertini,I., Ciofi-Baffoni,S., Katsari,E., Katsaros,N.,
            Kubicek,K. and Mangani,S.
  TITLE     A copper(I) protein possibly involved in the assembly of CuA center
            of bacterial cytochrome c oxidase
  JOURNAL   Proc Natl Acad Sci U S A 102 (11), 3994-3999 (2005)
   PUBMED   15753304
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..148
                     /product="copper chaperone PCu(A)C"
                     /GO_function="GO:0016531 - copper chaperone activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15582
     Region          1..142
                     /region_name="COG2847"
                     /note="Copper(I)-binding protein [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:442095"
ORIGIN      
        1 mnrhttlava ltltagltla gcggdgvpri evadpympqp vtqqmagayl tvknngdtae
       61 kltevtsnla ktitihktvg nkmeqveslp vpangtlrls hggnhlmfmg lkskpakgdv
      121 ftvtlhfaaa dpvrvqipvk aadyqpkh
//
LOCUS       WP_457689423             214 aa            linear   BCT 27-JAN-2026
DEFINITION  SCO family protein [Streptomyces nigrescens].
ACCESSION   WP_457689423
VERSION     WP_457689423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22578
     Region          52..184
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(84,88,174)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mrrttllasa ltaaaalslt acggddskpa aevsggtsak siitldspma kpdlvltdth
       61 gakydlpekt kghptliyfg ytncpdvcpl tmaniavavk qlpkaeqkdl rvvfvtsdpe
      121 rdtsaalkkw lgginkdftg ltgtfdtiqa garsvnigie kpvkkkngdv vsthgaqvll
      181 tspkddkvhw mamqkatsdd ytkalpkilk gqnp
//
LOCUS       WP_457689425             262 aa            linear   BCT 27-JAN-2026
DEFINITION  YcnI family copper-binding membrane protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689425
VERSION     WP_457689425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   de Oliveira Silva,Y.R., Zheng,D., Peters,S.C. and Fisher,O.S.
  TITLE     Stabilization of a Cu-binding site by a highly conserved tryptophan
            residue
  JOURNAL   J Inorg Biochem 253, 112501 (2024)
   PUBMED   38342077
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Chillappagari,S., Miethke,M., Trip,H., Kuipers,O.P. and
            Marahiel,M.A.
  TITLE     Copper acquisition is mediated by YcnJ and regulated by YcnK and
            CsoR in Bacillus subtilis
  JOURNAL   J Bacteriol 191 (7), 2362-2370 (2009)
   PUBMED   19168619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="YcnI family copper-binding membrane protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=27610
     Region          21..203
                     /region_name="YcnI"
                     /note="Uncharacterized conserved protein YcnI, contains
                     cohesin/reeler-like domain [Function unknown]; COG4549"
                     /db_xref="CDD:443613"
ORIGIN      
        1 mskiskmtqm pqqrpdlsrt rrlarrlplv gatavgsvvl laapafahvs vqpagaapkg
       61 gyatvnfkvp nerddastvk levtlptdrp lasvmpqpvp gwkvdvkksk lakpiemhge
      121 kineapskit wtaedkgvep gqfqqfpvsv gmlpedadqv vfkalqtydn kevvrwiept
      181 kdggpepenp apvlkltape edghgaaaan dksggkdhlk naaasedass sdttarvlga
      241 igivvgiigv gfgvfagrrr sa
//
LOCUS       WP_457689431             486 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces nigrescens].
ACCESSION   WP_457689431
VERSION     WP_457689431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Singh,R., Goyal,V.D., Kumar,A., Sabharwal,N.S. and Makde,R.D.
  TITLE     Crystal structures and biochemical analyses of intermediate
            cleavage peptidase: role of dynamics in enzymatic function
  JOURNAL   FEBS Lett 593 (4), 443-454 (2019)
   PUBMED   30582634
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wilk,P., Uehlein,M., Piwowarczyk,R., Dobbek,H., Mueller,U. and
            Weiss,M.S.
  TITLE     Structural basis for prolidase deficiency disease mechanisms
  JOURNAL   FEBS J 285 (18), 3422-3441 (2018)
   PUBMED   30066404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..486
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53790
     Region          68..191
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          222..467
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(285,302,314,397,428,452)
                     /site_type="active"
                     /db_xref="CDD:238520"
ORIGIN      
        1 mtdeltpetp dedeqpikqr knglypgvsd elaenmksgw adtelrdlqp veqapnaarr
       61 raalsarfpg erlvipagnl ktrsndteyq frasteyvyl tgdqtddsvl vlepkgdthk
      121 atihrlprsn redgefwlng mgelwvgrrh slreaeallg vpckdvrela dalkeatgpv
      181 rvvrghdagi eaaltdkvta erdeelrvfl searavkdef eigelqkavd stvrgfedvv
      241 kvldkaeats eryiegtffl rarvegndig ygsicaagph attlhwvrnn gevrsgdlll
      301 ldagvethtl ytaditrtlp ingrytdlqr kiydavyeaq eagiaavkpg aayrdfhdaa
      361 qrvlaeklve wglvegpver vlelglqrrw tlhgtghmlg ldvhdcaaar tehyvngtle
      421 pgmvltvepg lyfqaddltv peeyrgigvr ieddilvtdd gnrnlsaglp rrsdeveawm
      481 agllgk
//
LOCUS       WP_457689440             225 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689440
VERSION     WP_457689440.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..225
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23395
     Region          44..184
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mrhhvplgrf pvqsigafip wrgakevsgv almvaqevpt ssimavphgp vgvgmarrrm
       61 reellasgvq dtvvddavli lsellsnscr harpiyengs pgsataeakd gpsasirasw
      121 ridaqgrltv avtdgggptr plpatpsvta rggrglaiir slakdwgvhd svvgevtvwa
      181 alslqgafat rvdltpdlpp slttgagvst vrpltpgfpe fddlt
//
LOCUS       WP_457689444             489 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces nigrescens].
ACCESSION   WP_457689444
VERSION     WP_457689444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47738
     Region          200..485
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mstenegaav pseakpptgp qpdsapasas gaqapdapya ppppgfaptv gsapgaghpp
       61 qpgfghpgdd ptteqtaqip pypgaghgap gagggwgqqp pyggdpwgvt gspapkrrng
      121 gliaavlaaa lvaggvgggi gfwaagqnds asttvsasgd pgalnrkpts vsgiaqkalp
      181 svvtieaqga tgeggtgtgf iydkqghilt nnhvvagaag ggkltatfsn gkkydaevvg
      241 naqgydvavl klkntsgapl nplplgksgn vqvgdatiai gapfglsgtv ttgiisakdr
      301 pvassdgggt sasymsalqt dasinpgnsg gplmdaagnv iginsaiqsa gnggglgges
      361 qqsgsiglgf aipidqakrv aqdlirtgkp vypqigvqvg mrdtgdgati artgnngsea
      421 vtpngpadka glrpgdtitk lddtvvdsgp tliseiwqhk pgdevtltyk rggkehtahv
      481 tlgqrtgdk
//
LOCUS       WP_457689450             440 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689450
VERSION     WP_457689450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=46272
     Region          231..436
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(238,277,315,419,422)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(238,419,422)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(238,277,315)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mglfqfvpar rvvplvgmam vmalagtgga aggggaaada dgagrrsarw tetwgaavqq
       61 pvegdvddvp nwsekgfrhq svrqvvrvsa ggarvrirls nrfgkaplrv dgaviarsgg
      121 gaqawpgttr kvtfrhsgrh sgatvipagg eavgdavrls tsplenlvvt lyfagatgpa
      181 tfhraglvts yrasgnhlnd vpakayrqss qssyflsgvd vsgpfrerrn tvvalgdsat
      241 dgvgstpqah grytdglaer laaarrklgv vnagiagsml ltssscfgek gvtrfrrdvl
      301 drpgvrtviv elgandvgan watgpcfpss hkpvslrqit egyraliraa hgrgikviga
      361 tlvplrgypg ysakverlra qvnhwirtsg aydavvdfdk aladpahqdr prpgyvyedg
      421 lhpndagyqa ianafdvwgl
//
LOCUS       WP_457689452             159 aa            linear   BCT 27-JAN-2026
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689452
VERSION     WP_457689452.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 18525239
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..159
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17405
     Region          <3..54
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          72..148
                     /region_name="PG_bind_siph"
                     /note="peptidoglycan-binding domain; NF038080"
                     /db_xref="CDD:411663"
ORIGIN      
        1 mstqqttqdk hyiviagdtl sgiasrfhtt vkqlqiwnni sdpnvikvgq rlivakvstg
       61 epqpgdpsfv pfpggewfkt lptspiirmm glrlveegcg apygfsgpgp rwndkhrqay
      121 asfqralgys gsdadgwpgr kswdqlrvpf peedfgaae
//
LOCUS       WP_457689456             252 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689456
VERSION     WP_457689456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27843
     Region          53..140
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mtrsfeelva eaeavsvegw dfswlagrat eerpswgyqr amgerlaras aaldiqtggg
       61 evlagaaklp pvmvateswp pnvakatall hplgavvvad edepplpfad aafdlvtsrh
      121 pvtvwweeia rvlrpggtyf sqqvgpasvf elveyflgpq pehirrgrhp edarraaeaa
      181 glevvdlrae slrteffdig aviyflrkvv wmvpgftvaq yrdrlrelde lirtegpfva
      241 qttrfliear ka
//
LOCUS       WP_457689454             170 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689454
VERSION     WP_457689454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..170
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18420
     Region          9..163
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mggsrrgvvt irraegrdag rltrlvrssr ayegryssmv egyrvgpdyi eahrvfvave
       61 ergdgagage reservlgfy almvepaeld lmfvadqaqg ygigrrlveh mrgearragl
      121 dsvrvvshpp aegfyrsmga rpvgtvpanp pavmwdrpel aflvgpgges
//
LOCUS       WP_457689472             292 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689472
VERSION     WP_457689472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /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]"
                     /calculated_mol_wt=32069
     Region          68..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtdgpprtti sawrptvpgi aevfhahfte haypshthdt walmilndga vdftcdrhrh
       61 gaagsgtvvl lppgvahdgr tvtaagfrkr vlyldatvlp eeltgravdg pvfgdellrh
      121 rihqlhtslg hpgeghtaav hlddvrtgiv htgeafeaes rlsfirerll fhlatlrppr
      181 tpgreanrla aalrdlldar lptamslqea aavlhahpth lircfkqtyg lpphtyltgk
      241 rierarglll dgrrpaevaa tvgfhdqahl nrhftrhvgt tparyaatrr rs
//
LOCUS       WP_457689478             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689478
VERSION     WP_457689478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31342
     Region          25..81
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(31,35,60)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(34,59)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(41..42,53,56,60..61)
                     /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 msvdgadeas wdldpedeaq avveavgrql klwrkaaglr paqlgaligy genlvykver
       61 gvriprpefl dkadevlgad gkisamkkdl eqarypkkvr dlakleakav eigtygnhni
      121 sgllqtkeys raliqtwrpa ysqdevermv aarmarqslf erspaptltf vqeevtlsrp
      181 iggrmvlrrq lerllevaql rnveiqvmpt dcddhagmgg riqvlkfgdg savghdegqv
      241 tsrpisdpke irilelrygi iraqaltpre slvfiekllg et
//
LOCUS       WP_457689484             119 aa            linear   BCT 27-JAN-2026
DEFINITION  SH3 domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457689484
VERSION     WP_457689484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 119)
  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 119)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 119)
  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 707922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..119
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=12149
     Region          23..111
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mrawaktvas vsagalgllg laiapasavt ahsvsakaak cyayngtksa lnvhsgpgqr
       61 yttigtiakg gklpcgrngd ssitgqqyrd cgwksdrwgt vkingqdgwv ayecvafgi
//
LOCUS       WP_457689480             136 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689480
VERSION     WP_457689480.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  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 136)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13014796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=14954
     Region          47..130
                     /region_name="HATPase_RsbW-like"
                     /note="Histidine kinase-like ATPase domain of RsbW, an
                     anti sigma-B factor and serine-protein kinase involved in
                     regulating sigma-B during stress in Bacilli, and related
                     domains; cd16936"
                     /db_xref="CDD:340413"
     Site            order(50,54,57,81,83,84..85,101..104,116,118,123..124,126)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340413"
     Site            order(91,104)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340413"
ORIGIN      
        1 mnqeiaehkl hfhvqlsatr rgarlarllg teqlrswgmp fevpaqvlae laanaashgr
       61 vpgrdfrlvm ssdadtlrve vtdargerlp aqqamglres ghglilvdal adrwgtcrgp
      121 fpcktvwaef dlpmwg
//
LOCUS       WP_457689486             406 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689486
VERSION     WP_457689486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 406)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42448
     Region          1..400
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(1,27,95,395..396,399)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
     Site            13
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mrvllstygs rgdveplagl avrlrelgad vrvcappdqe fvdllagvgv plvpvgrsar
       61 elttaappps slpryaaevi asqldvvtea aegcdalvat galpaaagar svaeklgips
      121 vsvtfqqltl psphhpplay pgrpfppevt dnrvlwdlda qsinvlfrea lntnratigl
      181 ppvdhvrdyv igdrpwlatd pvldpwlkpa dldvvqtgaw ilpdvrplpa elmafldagt
      241 ppvfvgfgsm pmltstdaar vaieairaqg rrvlvrrgwa dlaliddrdd cfvvgevnqq
      301 alfgrvaavv hhggagtttt atragtpqvv vpqgvdqpyw agrvaelgig aahdgptptf
      361 eslsaglrta ltpetrarat avagmiradg atvaarllld avvpaa
//
LOCUS       WP_457689488             291 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Streptomyces nigrescens].
ACCESSION   WP_457689488
VERSION     WP_457689488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Rinaldo,S., Paiardini,A., Stelitano,V., Brunotti,P., Cervoni,L.,
            Fernicola,S., Protano,C., Vitali,M., Cutruzzola,F. and Giardina,G.
  TITLE     Structural basis of functional diversification of the HD-GYP domain
            revealed by the Pseudomonas aeruginosa PA4781 protein, which
            displays an unselective bimetallic binding site
  JOURNAL   J Bacteriol 197 (8), 1525-1535 (2015)
   PUBMED   25691523
REFERENCE   2  (residues 1 to 291)
  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 291)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="response regulator"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=30583
     Region          1..>145
                     /region_name="RpfG"
                     /note="Response regulator c-di-GMP phosphodiesterase, RpfG
                     family, contains REC and HD-GYP domains [Signal
                     transduction mechanisms]; COG3437"
                     /db_xref="CDD:442663"
ORIGIN      
        1 mtttpdtaps ilivddmeen lvaleavlgs ltqkvvrars geealkamlr eefavvlidv
       61 lmpgmngfet aanikgldqt kdvpiilltg asvdpnyayr gytvgaadfl ikpfdpwllr
      121 tkvnvflelh rknrqlaaqa eqlkrlltsd drpggegppp apttaapstv tgtdmgapst
      181 psapavttsa paappapkey pdpqqrpepr qraghpplpp egpgapapse pppqpappaa
      241 gdasrlaeia gqlaevelll rdakgsdker ladriaelea svgrlmvsrg t
//
LOCUS       WP_457689496             484 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689496
VERSION     WP_457689496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51491
     Region          27..372
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mskylkqeaa qagsplhgtg vdvpafdsar wrtrldella ahhvpgaala vvadgaihel
       61 asgvlhtgtr vavttdsvfq igsiskgyta tlvvqlahag kldldapvtd vlpdfavada
      121 eatktltprq llnhtsgieg dfvsdtgrgd dclaryvegv rnvgltnppg atmsysstay
      181 nllgrivevv tgrtwdealk kmlcvplgle htmtlpeevl rfraamghmg epgedpvptp
      241 lwnmlprsag pyggicataa dvarfarlfi dggrtpdgtq vlpaevveam lrrevempdq
      301 wslgahwglg wglfewdgvr gfghdgstfg qlaylralpe agiavalltn ggaaapkvfe
      361 tlcreltael agvgmpefgp paeepavdpa pfvgsyrreg flmtvadrpa gegmlrvkye
      421 gadglkdsfe plfwnlvpvs dtpsktvfag rrnekdgwip vvfyaladgs ryvhfgirat
      481 aksg
//
LOCUS       WP_457689498             247 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689498
VERSION     WP_457689498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26982
     Region          31..75
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          94..241
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mpvdkkqpip svwtrpqrrk reqpalsrsq ivaeavrlld eegidalslr rlgtrlnaga
       61 tsfyshvank delielvvde vygeievpda dgredwrsav agcadslraa mlrhpwmasv
      121 lggvgaaylg pnmmrisegm igmfraagfp gdeadaavst ltayvigmav seaawltlla
      181 rsgeseqdwv krllpaaeea arshphlqeq yaalwekdpr etrdakfayg lqrvldglav
      241 ridrtgg
//
LOCUS       WP_457689508              66 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689508
VERSION     WP_457689508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..66
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7338
     Region          11..57
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mrkvtrvpsa lltvdqvaar lrvsrwtvyn lirshelgsl tigrcrrise aaldayislr
       61 teqeaa
//
LOCUS       WP_457689528             266 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457689528
VERSION     WP_457689528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=29269
     Region          2..217
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mkvlwlfahp dqrslsgalk teglraldaq ghqhrvsdly amkwnpvvda adydhdpadr
       61 llvgeasera ytdghlapdi raeqhklawa dtlivqfplw wygmpailkg wfdrvfvkgf
      121 afgitdpatg rpqrygdgkl agkramvitt agarattlgp rgvngdlndl lfplqhgtlw
      181 ytgisvvppl lipgadrmtp tayataatrl rerlrtlptt eplpfrhqns sdyddelllh
      241 pdlaqlpppr tgpavhytap pppvhg
//
LOCUS       WP_457689530             366 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689530
VERSION     WP_457689530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38775
     Region          38..356
                     /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 maivckdram gvvesggghg gsggpgrvra vpgsggrhrv avlvrdgmlp ievgivhrif
       61 gearsadgep lyelvtcale pgevrtdtdf tvnvahgpea laeadtvvvp asgtdyalat
      121 ersagrlspa maealgrirp gvriasictg afvlaaagll dgrratthwr svddfrqlfp
      181 aveldadvly tdegevltaa gvasgidlcl hmvrcdhgaa vandvarrtv vpphreggqa
      241 qyirrpmpep qisstgvara walehldrpl slrelaares msvrtftrrf reevgisplq
      301 wltqqriera rqlleetelt vdriaaeagf gtaaslrqhl qsalgvspra yrstfrgsgg
      361 ggglva
//
LOCUS       WP_457689534             291 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689534
VERSION     WP_457689534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32054
     Region          54..290
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 madgdervga fwrelglpgl idvhthfmpe rvmakvwayf dsagplvgra wpityrfeed
       61 erlavlrgfg vraftsmiyp hkpgmaqwln gwaadfasrt pdclrtatff pedgaaeyvr
      121 aeltdgarvf kahvqvggyd padalldpvw galaeagvpv vihcgsgpap gkhtgpepig
      181 rllarhprlr liiahmgmpe yadfldlaqr ypgvhldttm sftdfaeria pfpwaergrl
      241 mdlgervlfg sdfpnipygy ahalevlagl elgedwlrav cygnaarlfg v
//
LOCUS       WP_457689536             180 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Streptomyces nigrescens].
ACCESSION   WP_457689536
VERSION     WP_457689536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..180
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18111
     Region          1..160
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mrllalsgsl rarssngavl rsaltfwdgp aatadigalp hfnpdldged atppapvaal
       61 rtavasadal lvvspeyahg vpgalknald wlvssgecvs kpvavitasp spaggdhana
      121 qlrevlrmmt gevvtaacre ipaigpkidp ttervtdeat ltdlgvalah laaaaapltp
//
LOCUS       WP_457689538             579 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457689538
VERSION     WP_457689538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  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 579)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..579
                     /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=59820
     Region          <187..499
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maspapaatp aprrrwslrt rlvvsavali avvgavigtv ttialhsymq rqldgkvhdf
       61 vvraqiprph epsltqdgld fvamggqplg avgarvgpgg tveagakldn ptgrlpeqrl
      121 aeltraqvaa lntvprdgrs htaelpglgs yrvesakdgs lvlglpldyv qktvgtlvli
      181 eacvtvaglv aagiagsamv gialrplrrv aatatrvsel plhqgevalh vrvpasesdg
      241 rtevgqvgaa lnrmlghvgs alaarqeset rvrrfvadas helrtplasi rgyaeltrrg
      301 reqpgpetrh algrieseae rmtglvedll llarldsgrp layactdlsp lvvdavsdar
      361 vagpehrwrl elpdepalvy gdagrlhqil vnllanarth tpegstvtar vraaagaaag
      421 regvvqleve ddgpgipagl lphvferfar gdasrsravg stglglaivq avvaahggtv
      481 rvgsvpgrtv ftvtlptaev tstaegistt aatsktwnaa rrqapvtgrg apaagrnapp
      541 agrdappagp papspaptkp qvtpsaadsq aghrlstpp
//
LOCUS       WP_457689542             424 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457689542
VERSION     WP_457689542.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 424)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /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=45467
     Region          152..418
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 midrfsawqr atrplvvdlt valacfllat plavafayid rapvgwsvva lavscvplia
       61 rnrwpitvva vtlaihlvqa allplarptp aatavalytv airtdrrraw rvgtlaavtl
      121 itaslvfppg alqlpqslar pqslaladkl psslaliawt lmavaigdav rsrrevlaaa
      181 eeraeraert keeearrrvt aerlriarel hdvvahhitl vnaqagvahh lmrtdpehvy
      241 ralerirdts rgaldelrat vgllrygedp veprepapgl dgldglldsf rhsgldvtle
      301 rtgppgelsp itdltayrii qealtnthkh agpasarvhl dfrtdvlrlt vdddgrgteg
      361 sgrgtgpvat glqgiqeagt ghgmigmrer aqsaggtlaa gprpdggfri eaelplragr
      421 kgrp
//
LOCUS       WP_457689549             174 aa            linear   BCT 27-JAN-2026
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689549
VERSION     WP_457689549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=17968
     Region          26..133
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mggggtpgpg efggsgrera rrrgqgqlea qvlaalheas gpataawvqe rldgdlaytt
       61 vmtilsrlha kqavtrersg rayvwtpaad eaglaalrmr rvldgepdrd avltsfvstl
      121 sahdeqllrt lldsttadas atadgpapad gpaaepgtap aprrhhpsde argg
//
LOCUS       WP_457689555             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689555
VERSION     WP_457689555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45200
     Region          9..398
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mpadppggrk amavwgigva vyfvaityrt slgvagldaa erfhinasal stfsilqllv
       61 yagmqipvgl lvdrlgpkkv ltlgvvlytv gqfgfalsss yamalgsral lgcgdamtfi
      121 svlrlgsrwf parrgpmiaq vaalvgmagn listlilarf lhsfgwtptf aasaaggivv
      181 livlllflkd hpegfepppa saeltgagfv rrqiadawre pgtrlgmwvh fttqfpamvf
      241 lllwglpflv eaqglsrgta gelltlvvls nmavglvygq iiarhhaart pltlgtvgat
      301 glmwaivlaw padhapmgll ivlctvlgac gpasmigfdf arpanpaerq gtasgivnmg
      361 gftasmttll avgvlldatg dnyriafasi fvlealgvsq ilrlrrraar rererlvvsr
      421 veavhvpa
//
LOCUS       WP_457689557             144 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457689557
VERSION     WP_457689557.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..144
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16343
     Region          <33..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mahredsvet iqqemtafar rarataarmh pelslvsytl lahlddqqgc ratdlaahyf
       61 ldkstvsrqi aaleklgfve rrvdpedhrv qvlhptgqga qvlanvtasr rqafherlad
      121 wdeedldrfa tylrrynaaq erlg
//
LOCUS       WP_457689567             378 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457689567
VERSION     WP_457689567.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Koper,K., Han,S.W., Kothadia,R., Salamon,H., Yoshikuni,Y. and
            Maeda,H.A.
  TITLE     Multisubstrate specificity shaped the complex evolution of the
            aminotransferase family across the tree of life
  JOURNAL   Proc Natl Acad Sci U S A 121 (26), e2405524121 (2024)
   PUBMED   38885378
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38654
     Region          1..302
                     /region_name="PucG"
                     /note="Archaeal aspartate aminotransferase or a related
                     aminotransferase, includes purine catabolism protein PucG
                     [Amino acid transport and metabolism, Nucleotide transport
                     and metabolism]; COG0075"
                     /db_xref="CDD:439845"
ORIGIN      
        1 msdptansaa pdlldlpplt aahfariedk vgalmrtrcd vvamqgeall pleacirsav
       61 rpgstalnii tgpygetfgg wlrscgaevv tltapftgav tpqqvaealr erpeidfvsl
      121 vhaeaatgnt npvaeigavv rehgallmld avasvgaesl ltdewgvdlc viggqkamag
      181 pagvsvvsvs araweriaan eqaprrsyls lldwkerwid ggrtalphap aqlemlaleq
      241 aadrldaegl eavltrhraa aaatragvqa lgglapyvvr eedaapvatt lrvpegvdar
      301 eivtaavavd aavpvqaaag alakemirvn hygraadrav vtaslaalag gllalgvsvd
      361 aegaakaaga awdavagc
//
LOCUS       WP_457689568             559 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing sensor histidine kinase [Streptomyces
            nigrescens].
ACCESSION   WP_457689568
VERSION     WP_457689568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   4  (residues 1 to 559)
  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   5  (residues 1 to 559)
  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 559)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12128685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..559
                     /product="GAF domain-containing 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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58898
     Region          36..176
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          206..326
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          347..537
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdaateatrs lrglsselta rvpqlleamr tvgagldlhv tldrivetaa eladaryaai
       61 giiddarvgl sdfvtygvta qqherigalp dghkgllgal ihdpkplrld dltkdarsag
      121 fppghppmrt flgvpirvqg difgnlylte krdggvfsee dlhmvrvlat eagiaignsr
      181 lhaatrqrer widgsvavtt ellagsdvdd alavvaeqar kladsaagiv llpdgeggle
      241 ivavsadepa gimgtqipsd spvveqllag epvfvddsat dprmvtdiaq rfgpsmmlpl
      301 ksggrvlgtl atprargarp ftgaertlat qfaaqaalal vladaqrdre rlavyedrdr
      361 iardlhdlvi qrlfatgmml esaqrrsvvp evaqgvgkav deldvtiqei rtaifalqqg
      421 paeapsglrt rvlreigtaa vplgfqpsag fvgpvdsrvg eltgknliaa lrealsnafr
      481 haqasrievv vdatirlpdg tdgvrltvad dgigipdngr rsglknlanr aeslggssty
      541 gpglgeggtg tmvqweapl
//
LOCUS       WP_457689570             303 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689570
VERSION     WP_457689570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33116
     Region          4..219
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttlhidhvs rwfgnvvavn ditmtigpgv tgllgpngag kstlinmmgg flapsngsvt
       61 ldgttiwrna giyrhigivp eregmydflt grefvlanae lhglgraeaa ralatvemey
      121 aqdrkistys kgmrqrvkma salvhdpsvl lldepfngmd prqrmqlmel lrrmgdegrt
      181 vlfsshilee veqlaahiev vvagrhaasg dfrkirrlmt drphrylvrs dndralagal
      241 iadpstagie vdlaegalrv qavdfgrfte llprvardhg irlltvspsd eslesvfsyl
      301 vaa
//
LOCUS       WP_457689574             236 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689574
VERSION     WP_457689574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..236
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25285
     Region          4..236
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 malqaagrqs lvdtvvdalr sqltagewkv gariptehal aeqlqvgrnt vreavrvlvh
       61 agmlrsrqge gtfvvstadp gdimrgiqra girdvlelri aleaeaarla alrhrpddle
      121 rmraaldaqa eladaegqpd sgslelyadh dvsfhkavve aahntaltat ydwfsssvre
      181 alvnalddqa mpkivhgdhr avmdaiaagd peaaeratra lldkpkqave allaar
//
LOCUS       WP_457689578             539 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457689578
VERSION     WP_457689578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=56007
     Region          80..476
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 magiepalpa pthtvdprlg ktpadpasdt ppgaprgtap daasgtapga apdvsvvdql
       61 aavqdrlagw isdlstlhdl teqlartrtl edalhellra gaslvgarrg lvvlapadgf
      121 gpettvglgl ghaeigtiet iprralsyar ildglpepga ggdgtrtgpl ddtrhearda
      181 grppgprgaa aagpcteise pdipgekdld prlrevaarl gyaasyavpl aaapigrtga
      241 avwlydepae pterqrhlig lyrahaaehl arllelhrsr qavrtlreel lphrlpripg
      301 vrlavrhhsg prgggdwyda lplpdgalgl aigsvtgsgp savaamgrlr aslrayavme
      361 gedpvavlsd lelllrltep arsatalfaf tepppgapgg ppappmpggi tdpfarkivl
      421 agaghcppli lgdlrtayve tslsaplgml acweapsvei epaggetlll ysdgllhrtg
      481 epmdrafarl haaaagvpqa arhdpeavvd hivrtmlpqg lddpsseedv vllaayfee
//
LOCUS       WP_457689589             202 aa            linear   BCT 27-JAN-2026
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689589
VERSION     WP_457689589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10471097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22301
     Region          14..175
                     /region_name="CDP-OH_P_transf"
                     /note="CDP-alcohol phosphatidyltransferase; pfam01066"
                     /db_xref="CDD:460049"
ORIGIN      
        1 mevqetrvqt drvltipnil smarllgvpl flwlilwpvf ggpkadgwal lvlalsgvsd
       61 yldgklarrw nqisslgril dpaadrlyil stlvgltwre ilpvwltaal larelmllia
      121 vgflgrhgyg ppqvnflgka atfnlmyafp llllsdgggw lhtpatvfgw afagwgtaly
      181 wwagilyvvq vrrliradtt ad
//
LOCUS       WP_457689602             128 aa            linear   BCT 27-JAN-2026
DEFINITION  PRC-barrel domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457689602
VERSION     WP_457689602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=13952
     Region          8..75
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mqtdidprsl igrkafdrng akigtidevy lddatgepew aavrtglfsr dafvplepsk
       61 mvgeglhipy drklikdapd fgvgrhlspe qelqlyhhyr ldissptsdp vspgsgdknf
      121 gkiagsdd
//
LOCUS       WP_457689612             269 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces
            nigrescens].
ACCESSION   WP_457689612
VERSION     WP_457689612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=28060
     Region          159..251
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 madadvpgqg pgdgiveeps rsilrsetwi vlalslgasg lsalisfigs vtkpgglkdq
       61 aatlngshap grpwldlawq lfgiatalvp vvlvahlllr eragglrvig fdrrrpgfdl
      121 srgavlaavi ggsgvllylg araagfnltv vpealpevww kipvliasav qnavleeviv
      181 vgyllrrlgq lgwsplaala assalrgsyh lyqgiggfvg nmvmgalfvl lyrrwgrvgp
      241 lvaahalidi vafvgyalla grvgwlptp
//
LOCUS       WP_457689614             273 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689614
VERSION     WP_457689614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28287
     Region          1..271
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mririvdafs erpfagnpag vvlldsgafp dtawlqrvat evnlsetafa hplppggdad
       61 walrwltpaa evnmcghatl atahvlhttg tatgtvrfrt rsgvltttad dhgaitmdfp
      121 tapltpvevp pvvagalgte irsaydtgpd vgdllvelad eksvralapd lkalaghggr
      181 gvittaraen pdggydfisr cffpgvgide dpvtgsahta lapfwsarlg raslvglqga
      241 artgfvrtel rgdrtlltgs avtvidgell vtg
//
LOCUS       WP_457689616             217 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689616
VERSION     WP_457689616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 217)
  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 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   5  (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 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23450
     Region          77..150
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 medvimrsqg hehghehghe hrhehcgpgr hggrgdfagg werrraafgp fgppfggppf
       61 gggrgrggpr grarrgdvra silallkdrp mhgyemiqei aersggawkp spgsvyptlq
      121 lledeglits aseggkklfs ltdagrtead sgsdapweea grgvdweamn eirkaggglv
      181 eafrqvwatg tpeqrekama vvnkarkely lilaeed
//
LOCUS       WP_457689622             386 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457689622
VERSION     WP_457689622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38254
     Region          47..343
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mhassgspag sstgsgqgis gslgdrqssp algglrrrap grrgaglgia llsalafggs
       61 gvaakplisa gleplqvtwl rvagaalvml pvawrhrdla rrrpallagy gllavagvqa
      121 cyfaalsrip vgvallieyl apalvlgwvr fvqkrpvtra aavgvvlavg glacvvevws
      181 glsfdvigla lalgaaccqv gyfvlsdhgs dgddavdplg viayglliga vlltviarpw
      241 gmdwavlggg admngtqvpa vlllawivli atvaayltgv vsirrlspqv agvvacleav
      301 iatvlawvll gehlsapqiv ggavvltgaf iaqsakpkat etvrvagagt gdgvaapggs
      361 gspeplaapa saprtgddls agscat
//
LOCUS       WP_457689624             327 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457689624
VERSION     WP_457689624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32044
     Region          <84..313
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mhatpssalp vgrgllyvtl aatawgtaga aaallyrgsg pgplaltfwr tfgglvllla
       61 vrallrrrsa taavpapape eplrrrltri vmtgialavf qaayfaavea tglavgtvvt
      121 mgagpvliai garvtmgerl gaggvlavag alaglavlvl ggdggatvrp agigyallsa
      181 agcaamtlit rrlgkgggsd pyastvsafa vgalcllpla ameglwplah dlgrslclla
      241 yiaavptala yglyfaglaa vraatasvis liepvsaaai avlflgerlt mataigtgvl
      301 ltavaalavt eargavtaar saapvag
//
LOCUS       WP_457689632             355 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457689632
VERSION     WP_457689632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36614
     Region          58..345
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mstatgapta sadtttspat tagptadgda attaatslrt atataaptar grargwqlrf
       61 allslvwgfs flfikvgtqg faplqvtlgr vafgalvlla vlavkrerlp rsartwahlt
      121 vaafflnalp fslfayaelt isstlagicn atsplwgmal svvalsedrp trrrvaglgl
      181 gflgvltvlg awqgftgtds tgtvmalgas lcyaigwiyv rrtlagvqhs hlsmssaqll
      241 latvqlavvt plfttaptsy pvipllavfa lgalgtglaf liqyglvaei gpttaqmvty
      301 fipviataag vallheqlsw ntpvgalivl agaaltqsrp rpsrptiprt gsttd
//
LOCUS       WP_457689628             221 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689628
VERSION     WP_457689628.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23468
     Region          25..172
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 maraesyept arttptrare raaydhetvh tildegcvch lgfvrdgspv vlptlygrvg
       61 drlylhgstg srplrmagaa pdpglevcvt vthvdglvla rsafhhsiny rcvvvhgtah
      121 qvtdeeekta aldalvdhvl pgraadsrpg nakelaatsv irldlreasa kirtggpnde
      181 pedlalpyws gvlpvapvyg apipsddlap gtpepaylsa r
//
LOCUS       WP_457689634             302 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689634
VERSION     WP_457689634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   3  (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   4  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32681
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..292
                     /region_name="PBP2_LTTR_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08423"
                     /db_xref="CDD:176115"
     Site            order(108..109,111..112,115,119,121..127,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176115"
ORIGIN      
        1 mlnldrlrtl savarhgsvs aaadglhvtt savsqqiakl eretgqqlla kngrgvrltd
       61 agrlladhat rilsqvelaq aeleahrgqa vgelrlgafp taarglfpaa lvtlraehpq
      121 lrarltemep desvrgvvrg didlavvldw ynrplslpdg lakapllddp advampsthp
      181 larrrsvele efaddewisw pqgefcsewl mftlrskgie prvahmaeeh gtqlaliaag
      241 lgvavaprlg rgpvpegvsv vpvrhtmrrh vyaiwradad rrpsiraavg alrtagkrlq
      301 gs
//
LOCUS       WP_457689638             154 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689638
VERSION     WP_457689638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..154
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17050
     Region          6..151
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 madtqrrgrr immtqgelda flaaqrtcrv atvggdgaph vgalwfvwdg talwlysitr
       61 srrwaqlrtd priavvvddg heygelrgae lagraecvge aprtgepcpe lgaperlfae
      121 kyfgmsamph dgrhawlrlt pesvvswdfr kipg
//
LOCUS       WP_457689642             242 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689642
VERSION     WP_457689642.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27085
     Region          10..224
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mnentthgra raqrtsegwa flvesirnhr tvgsiapsgk slanlladpl leragrisnv
       61 levgagtgsv trillpqipr gsrldivean ahfaahlrrl vrgypnllek qeqvrvhnaf
      121 veqlntdrry dvivsglpfa nfsprqvdei mgryfdllrp ggtltyfsyc gsrwvrtflt
      181 srpearrqre vkdllqqyhn qyaigcwtvw gnlppanvwq lrrpvdavnt ssvltaqpgi
      241 sg
//
LOCUS       WP_457689644             176 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457689644
VERSION     WP_457689644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..176
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18123
     Region          1..170
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mnalsnllsq ippapaytvl aaaiiaesil lvgaiiptla lmltagalar tgsmnlfcvi
       61 avaasavvig dalghrtghl lgkrlrtgkl grripasawq rvetlmnkra gqtllifrfv
      121 pvmrtlaphl agvvglpyrh iapysalasv awasveggag ytaafsiqhi saigap
//
LOCUS       WP_457689646             306 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457689646
VERSION     WP_457689646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="trypsin-like serine 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=31791
     Region          97..278
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mpetftsvir rlrgratgla vagtalalaa pipatalagq araasadpvs vmtytakerq
       61 ealaywtpar ikavgksvdl gptgpkakpw qgtamktvgr lffvnangad twctatavks
      121 anrsavmtaa hcvrrgssph ntniamvfvp gyskgkmpyg afavrtavtp rswetdstdd
      181 lstlvvdpdk sgrkltdvvd gqdiafnrpv ggtisafgys atrpqlgeel lrcigtakkk
      241 sglqaipcdm sggssggpwl adfnattgkg vlvsvnssld sltptemqge vlgatakkvy
      301 draqhg
//
LOCUS       WP_457689650             408 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457689650
VERSION     WP_457689650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 408)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45394
     Region          22..403
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(74,95,97..98,181..182,191..192,195,198..199,202,234,
                     237..238,241..243,246,289,291,292..293,317,393)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(96..97,104,108,115,160,163,238..239,242..243,
                     246..247,250,288..289,292,294,317,344..346,349..350,
                     352..354,357..358)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 msqtvpvphg lpmerdaspf dpprqitrlr earpvspmvf pdghegwlvt gydavrqlma
       61 dtrfssrqdi gvlhlpyetp gmpaptepsp qvpglfvamd ppdhtrlrrk ltgaftvkrm
      121 kqleehivdi aerqldelar ltppvdlvke falpvpslvi cellgvpyad renfqvnsak
      181 flekdvslde kmaayhamtt ylaelvtrkr aapgedilsd larqddltie eltgiaflll
      241 laghettanm lalgtfalle hpeqlaelra npdlmpgave ellrylsiad ifyryatedi
      301 elggetigkg stvvvsllaa nhdpqrfdnp dtldihrtar ghlsfghgih qclgqqlari
      361 emragfdgll rrfptlelai padevklrtd mniygvhelp vtwtetar
//
LOCUS       WP_457689657             470 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689657
VERSION     WP_457689657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=51303
     Region          12..468
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnakifapds vrtlsefehd alriaqvlge rgvgpgdrvm lkagnspawv atllglmhig
       61 asivlidqqe haeqtrriil rtgtklvlsd edspldssqe avhlyellvs aagrpitgep
      121 ltvdawselp dglimwtsgs tgtpkgvvks ggkflknler naaqvghred dvllpllpfa
      181 hqyglsmvli awlkrcslvi apyrrldral lmaeesgvtv idappssyrs mlnlvsrkps
      241 lrpglerarm fcvgaapldd plvgqytaef grplldsygs telgniafat penpvacgqa
      301 mdgiqvrvvd dtgrpvpage pgevevntpd alegylaedg tlqptpqgwq rtgdlgrlda
      361 dgnlfvlgrk yavhrmgytl ypeliersva aqgcsariva lpderrgaql vffveddqgq
      421 edaywrerlc gmlaayehpd rvvvldrfpl nrngkpdkrq leqlarargr
//
LOCUS       WP_457689662             632 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457689662
VERSION     WP_457689662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 632)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..632
                     /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=69439
     Region          378..628
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfgrhlwapl rglvlfglgl tagpmlaavg lgtlfgiqal aqwyrdplnv yrtlasrwcg
       61 vdipvpyqpp ppppepehdg wyryknrlyl tpkklsyerr wdwlvkdpat srdilwmlin
      121 pfvgsvtall pltlvvvgat spwswpghag itvpiavata lagfgfgpvl lhlhgrwtcq
      181 llasapdsgi rraliwigrg giatwrlalt aglavaelaa almhllamvp illwawptvl
      241 vagrqltswr rhqiqewtgi ridrpylpep alppprpdgt yqigrtlyrt pemalrslry
      301 rqnardlatw rdllwllldp vvgvllaalp vvvtgycffg liwswawasl lqlfvdfhtf
      361 drwpllihdi pvigdypiat apvigvigtl tgsllaipll rlhglwswll lgptksallg
      421 rrvdqltetr mearetlsse lrrierdlhd gaqaqwvamg mklgaieali erdpasakmm
      481 vgtareasak alielrhlir ginppvlaer giadairgla ldsplsvglr idlpgrperp
      541 vesaayfavs elltnvskha dadrvridvr ytaqhlrivi tdngaggadp akgsglrgvq
      601 rrlatfdgsl avhsplggpt tvtleipcvl ss
//
LOCUS       WP_457689664             303 aa            linear   BCT 27-JAN-2026
DEFINITION  ACP S-malonyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689664
VERSION     WP_457689664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33753
     Region          19..262
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mgrfdfasag rflvldryar drlatadevl gfsvlerfhd agadyseyaq lafliaslaa
       61 adraedrfgm rpdvcagasf gqkaaaayag sldfadvvrm taelarceke yfttehsdvv
      121 thsvyrvpde efhtlldemr argewfdisg elergfymvs lresrledfi ravrdlggys
      181 lytmrppvha gafgalrrka eaevfakyri raprlpvisd adgtvvdsae amrtmlldtf
      241 drairwpdmv tsmvglgvdt lyvtgaddmf hrlnctvrnf dvitvnpkna lrpgppklra
      301 raa
//
LOCUS       WP_457689680            1031 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457689680
VERSION     WP_457689680.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1031)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1031
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=110172
     Region          3..>1029
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mqpistplsr asqkeealwl ldklvpdsgv nnipaaiqvs grlrttalre aaarllrkhe
       61 vlrtvfhdeg aglrkailap edarldievs qstadgpadd ltalaarpfk fngrpmlric
      121 qveapegdvl cvvahhlvfd vasaqivmge ltrlydavla gedlsgeavv pvaavaadap
      181 rpesfrfwrd hlsgfdagsl dlwmdrqgsa ettlkgatva hdlsdeardv vrrlrrelra
      241 sepvillaay ylllaqhgag pdivigspad irgqqaagai gyyvnilalr vrtdpaqsfr
      301 alvrqardvf leavshvdvh vdlllpeipr vnsawsttlf rhmfnylpgg lsaettiggv
      361 paralmvrng ysrmnlefdi lsekdritve alygleshrr ddvalllqry dallvavgae
      421 pdrpvgelss wsqrdrtvia aanrtaadap apsvlrtvae raaaapdava vahgdrntty
      481 aelwqaasdt rallcasgvt agdvvavaar rgpelaaaal gvwlaggayl pvdpdhpadr
      541 isyqlsdsga ravlagdtvt lpegtprldm aglraaqggi aelpadpdpa scayliytsg
      601 stgrpkgtkv shgnlanlvr hfldeltpgp gevtlwmttf afdisalelf lplasggrla
      661 vapdearvng tllrellvrh dvgivqatpt twrtvidqvg dqlagrrvlc ggealpadla
      721 grlletagev rnvygptett iwstagklda gdgavhagtp lrnttafvld pagrelplgv
      781 hgelciagag vaigyhnrpe ltaerfgehp rygryyrtgd larwrdngtl evlgrvdrqi
      841 klrgnrlelg eieavllehp evtgaavvtv gelsadavlv afvvahpteg iverlwehar
      901 aklpssavph dfvvtdelpt nanekvdyph ltrlatarra aaghgaaaeh hedalvnall
      961 alfrellgre dvtadanffv lgghsllaal lvqriqesfg aemrlaeffa lptplglaaf
     1021 lrsrgvdpgt g
//
LOCUS       WP_457689684             429 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457689684
VERSION     WP_457689684.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 429)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47482
     Region          25..429
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(71,115,117..118,201..202,211..212,215,218..219,222,
                     258,261..262,265..267,270,313,316..319,343,419)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(116..117,124,128,135,180,183,262..263,266..267,
                     270..271,274,312..313,317..318,320,343,370..372,375..376,
                     378..380,383..384)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtdidssgsv qelrfpmarr cpfapppeyt glraesplvr vqlphggsaw vvtrhaeaqq
       61 lltdprvssd ashpgfpsvr ppeeppadea tgsgepltae qlnelaeiaq fhegqfinld
      121 pprhshyrrm lisefgarrm nqlrpevqri tdrliddmla qgspadlved lglplsslvi
      181 cqllgvpyed reyfqsatrt lvqldaepeq ikaameglid fldelvkaav rapgdnligr
      241 lineqvgsge ltraalvgma fllltaghea tanmlplgml tllehpeqla elrenpallp
      301 gaveellrfh svsdwaafdr valddieidg qkiragegif vlsasanrde raferpdtfd
      361 ihrkarhhia fgygvhqcig qnlaraelei glgtllrrvp slrldkpmde lpfkyqnlvf
      421 glhampvrw
//
LOCUS       WP_457689688             253 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces nigrescens].
ACCESSION   WP_457689688
VERSION     WP_457689688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27855
     Region          16..249
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mnahadedlw vrrfhpapea atrlvclpha ggsasfyfpv sralapaidv laiqypgrqd
       61 rrnepcldni adladevter llpwtdrpla mfghsmgatl afevalrleq reitlqalfa
      121 sgrrapsrhr eetahlhdda alvreikaln gtesqtldde emlravlpai rsdyraaety
      181 ryqpgpplnc pvyamvgesd pkvsidears wsdhtmghfd lqtypgghfy lnaqapriia
      241 aisqavsats gta
//
LOCUS       WP_457689690             541 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689690
VERSION     WP_457689690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..541
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60150
     Region          25..518
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mfvpdfpfay ddwlrhpagl gtvprhrhgt pvavigggms gmtaayelmr lglrpvvyea
       61 eqlggrmrsv pfpehpella emgamrfpvs attlfhyide lglrtspfpn plapctpatl
      121 vhlegrthra rsaadlpsef qevadawaka lqdraelssm qdairrrdip vlkaiwnqlv
      181 keyddqsfyg flatspafas frhreifgqv gfgtggwdtd fpnsiieilr vvctaadddq
      241 mtieggaqql prglwthrpd rlahwpsgts laglhggspr paavriarda egyevtdadg
      301 rrdrypavvf sphvwallnh vdsdpdllpa dlwsaverth ymgsskvfvl tdrpfwldtd
      361 phtgqmamgm tltdrmprsv ylfdsgpdrp gvmclsytwn ddslkfatls aeqrlelllt
      421 klgeiypgvd irshlisepl titweteprf mgafkanlpg hyryqrrlfs hfmqheldpr
      481 hrgfflcgdd iswtggfaeg avttglnavw gvvdhlggst ppenpgpgdv fheiapvrlp
      541 e
//
LOCUS       WP_457689692             350 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689692
VERSION     WP_457689692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38824
     Region          28..146
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          188..318
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mssetevprp eqldeddlll analqaapra twselgkvlg qdavtlarrw erlsskglaw
       61 vtpalgpgll yrtcrafvei hcepgsaaqv saelsrqphl ltiqhvagty dlfaiaftpd
      121 fpsmsdyllt slprqegvvr vrshlvtrnf rtgsqwrlgv lnqrqerall rtrpepqsae
      181 ataystwere livalsndgr irytdiatel gvtprtvqrr lnrllgnrdl llrcdvarpl
      241 agwptgallw lnvpderlee agrtlgafpe trscaalsga nnllvtvtlh svdalhdwav
      301 qlrqalpyad iadrsvvlrq dklcghllda wgrsqgvvpl diwrpsglsr
//
LOCUS       WP_457689706             190 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457689706
VERSION     WP_457689706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20300
     Region          22..66
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          77..182
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mspkamarpg grsarvqeav haavreleae qgrasltvpa vaaragvtps tiyrrwgdlh
       61 ellsdvaver lrpeeppadh gglhadlesw vrqfldemas psgrayirda llgdpdgsna
      121 gqcsayaadq ievildratg rgeavpdvea vmdhvvapmm yrilfrpgql tgsyadhlvr
      181 avltspvspd
//
LOCUS       WP_457689708             217 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457689708
VERSION     WP_457689708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 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]
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23004
     Region          4..113
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          153..210
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mikvlvtdde pliragirmi ltsaddidvv aeaangreav elaraqrvdv vlldiqmpvm
       61 dgltalaelr raapdarvli lttfgeqqnv lralaegsag fllkdsapae lmravraaaa
      121 gdaylspgat rhvvdslasg rsvlrseqar rrletlsdre levlallgeg lsnadagqri
      181 hmseatvkty vsrilaklgc enrvqaalla rdaglgt
//
LOCUS       WP_457689710             519 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457689710
VERSION     WP_457689710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53677
     Region          120..>349
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          416..514
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 msrfpalrtt sllsaslllt lgatacspdk ddagharsap sapaglpasl tsqklnwqlc
       61 papstaqggg aapgklpdgt awecanlkvp ldhakpagdt idlamiraka egggkrigsl
      121 vfnfggpgas gvatlpgyaq arplrshydl vsfdprgvgn sagvtclsdr eldeqraeth
      181 dlagtaeqnk qtaaacakks gkvlphvgte saardldlir qvlgdtklhy fgisygtelg
      241 gvyahlfpkr vgrtvldavv dptqdavqes lgqakgfqla ldnylahcvk tpgtcpyrsp
      301 edgrrrithl laktgkqplp tksgrrltke qavmgivatl yskeawpals vslsdaeqgs
      361 gdnllmladg ylgrddkghy nnmqsanaai ncadteqrat pkevqarlpe frkaspvfge
      421 ltatgllgct gwpvtgkgdt pqvsapgaap ivvignagdp atpvagarkm aeklgtgvgm
      481 lltvkgeghg tygvnqcatk avnghlldgk vpapgtvcs
//
LOCUS       WP_457689718             267 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689718
VERSION     WP_457689718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28483
     Region          10..261
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtsmtatpgl avralragys grtvvegaef aipagqvaai vgpngcgkst llrtiarlhr
       61 pesgevhaag tdiwqlsrrq aarriallpq sprapeavtv aglvrygrhp hqgllrqwsr
      121 edehavreal eatgttelaa erldrlsggq rqrcwlamvl aqhtpvvlld eptsaldlgh
      181 vvdvlelvre vaaagrtvim vqhdlaaaar yadtliamkd griiahgvpr dtvdealvkd
      241 lyaldadilr apgdaspvvv prtrtgn
//
LOCUS       WP_457689720             355 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689720
VERSION     WP_457689720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35244
     Region          11..352
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtasgthpal tppdstvlra gtlswlfprr salvaaflvp lilllialav masstgmpls
       61 qtlsgllgtg dpgtvmvvre frlprvgvgi mvgialgisg cltqtlagnr latpdligvn
      121 egataavvas aagsatgmvg gwwlgplgav aaavlvvlca ggagsrgyrl lvvgigvstf
      181 igagsdlims rendntaggv flwavgslng rdgsvgtpll tallflvpla liaghrlqll
      241 rfdddmaacl gvdlrrvrav alalavalag iavgvggpia fvalaapila qrlsgptrvp
      301 vlgsaltgaa liaaadalgr vaapvelpvg vvtsvlggpf llwvllrsdr ttgka
//
LOCUS       WP_457689722             361 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689722
VERSION     WP_457689722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..361
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36622
     Region          48..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msitkgdrle aervrphvrs pfrsrtavwa aaglvavllg fvllslligt gsssaarawd
       61 ylrgdpsara daqlrlavld vrlprtlaav lvgiclgtag cllqaatrnp laetgllgvn
      121 sgaafavvlg ltffgattts alllwallgg maasavvllf aasgrtagsp lrlvlagsal
      181 gatfhgltsy vllgtqstyd tyrywtigsl agvetsdllp llpvvavgll ialgcarpla
      241 alglgddsar slghhpgrvr llvaaavsll agcavavagp iaflgllapy aaralagarm
      301 aaqlalsali aadvmiladi larivirpwe tpvsvllafv ggpllvwiar ssrlstagas
      361 a
//
LOCUS       WP_457689746             157 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689746
VERSION     WP_457689746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16802
     Region          15..148
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mdarlnyfaa ptagkalkyv msagkalkds plsattqelv alrvsqingc aacidmhtkd
       61 saaagetsvr lnlvaawrea tvfteaeraa lelaeegtrv adaargvsde vwayaakhyd
      121 eeqlaalvil vsfmnmvnrl niitqqpagn yepgqfh
//
LOCUS       WP_457689748             128 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457689748
VERSION     WP_457689748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..128
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14187
     Region          2..126
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mmggseqelv dewhgllarh atvhnalehe lqaqhglsvs efealellas shhgkcrgqd
       61 lthavhlsqs aasrlvarle rgslvervmc dldrrgifvv ltdeghqryr dakpthrsvl
      121 artlrgdn
//
LOCUS       WP_457689750             491 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689750
VERSION     WP_457689750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..491
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50275
     Region          25..461
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,151,
                     154..155,158,281,284..285,288..290,293,321,325,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtssaalsas tstwnaklwg vlltvslvig ldaldvsmvg valpsiqadl glstsalqwi
       61 vsgyvlsygg llllggraad llgrrrvflt avavfaaasv lgglvddgtl liatrilkgm
      121 aaaftapaal sivtttfaeg parnkalgvf svfgasgysa glvlsglltq vgwrwtfflp
      181 vpiaviawia anrllpkdgp rssggydipg aitsvgamll lvytvveape agwaapntli
      241 qfaiaaalll aflvierrsa hplvrlgilr sgslaranlg isvffggyig fqfvvmlyfq
      301 svlqwsalqt algflpaaai vafgsprmdp liervgtsrt iaggviahli ayvlflvidr
      361 dapyvvgvlp smtllgigft lafasfniqa tagipdheqg laggllntst qvggaiglai
      421 vtavltagge gktgpdalla gftpalltit vlsaigllig lsgvlgrrki dkttvepaak
      481 padepelalv d
//
LOCUS       WP_457689752             738 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457689752
VERSION     WP_457689752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..738
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77517
     Region          32..712
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mstddagvvv rsvatgrirl tvpwvrarpg saglvderlt gmrgfralri fprtgsvviw
       61 mapdlldvdr lvtaldqapp psaplkptrs tpdsstgela rlvvggavla ftalrrllgr
      121 pritagssgl lgaitlftgl pffrgalrsl rgrshpgtdt lvtaatvisl vlrenvvalt
      181 vlwllnigef lqtltlrrtr raieelltig eervwlvree gadgvgriet evaleevapg
      241 dlvavyehhr ipvdgrvvtg ealvdqaait gealpvyara gaevyagtiv tsgsltvrat
      301 svgadttvgr iisrveeaqs drapiqtiat rftqrfvpvs falaaltyvv trdarramtm
      361 lliacpcaag latptaisaa igngarrgtl ikggthlegv grvtavvfdk tgtltfgrpl
      421 vtsvvtlsdr ytanevlsla asgelharhp laqaivahte eqhlrapihq acevvlgmgm
      481 raeldgtrll vgspallrqh gveltheaqg wteqlrtsge tviciahdde ligllgvsda
      541 vrsgagtviq qltalgvtrl alltgdapet aqavadalgi aevhahalpe gklqlirdlq
      601 aeghtvamvg dgtndapala ladvgiamga hsshvaleta dialpgddlr qvpavvelsr
      661 htlrlvrqny glaigvnllg lvagaggsin pvlaallhnt ssiavvansa rlvnhtphlp
      721 qttddllmaa pledrrlr
//
LOCUS       WP_457689754             296 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689754
VERSION     WP_457689754.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31545
     Region          25..264
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mdrteavrpl pepggatgrg redlpaepvi slrgaalayg grvlwrgldl dvrpgeflav
       61 vgpngsgkts llrvllgrqq lsegaltvlg haprrggrhi gyvpqqtfqp ahallrardl
      121 vrlgldghrw glplarravr rqvddlldsv gatpyadvpl grlsggeqqr iriaqalatd
      181 prillcdepl lsldlhhqrt ltglveerrr sagtavvfvt heinpvlglv drvlylargg
      241 hrvgppdevm ssttlselyg tqvdvvrvgg rivvagvtdf gtghthadga dggesp
//
LOCUS       WP_457689761             342 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine synthase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689761
VERSION     WP_457689761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10107527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="cysteine synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_process="GO:0006535 - cysteine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=36094
     Region          19..309
                     /region_name="CBS_like"
                     /note="This subgroup includes Cystathionine beta-synthase
                     (CBS) and Cysteine synthase. CBS is a unique
                     heme-containing enzyme that catalyzes a pyridoxal
                     5'-phosphate (PLP)-dependent condensation of serine and
                     homocysteine to give cystathionine. Deficiency of...;
                     cd01561"
                     /db_xref="CDD:107204"
     Site            order(23..25,36,42,44,86,89,105..106,109..110,113..114,
                     172..173,266..268,269..271,295,305,308)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:107204"
     Site            order(49,79,185..190,229,275,301..302)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107204"
     Site            49
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107204"
ORIGIN      
        1 mpgalprpsv vsrisdligh tpllelavse tgsrlllkle mfnptgtaki rmarqmilda
       61 eargalrpgg riiestsgnt glglaviaae rgytftavvd hhacadklra mkalgtelvh
      121 vrnngteela taareelaed larsqdntvf teqhnnpsng vgyfpvahel nealdgrlnv
      181 ligavgtgga lcgtarelrt lipsfstigv epkgsiafgg pahdyyqsgt gtpegaeiga
      241 lvdfdlideg vkvgdieafa tcravartgl liggsaggvv hvalsrlpsl ppgttmvali
      301 ndggekyldt vfndewmrar gllapqtere ieelltklrr nr
//
LOCUS       WP_457689771             514 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689771
VERSION     WP_457689771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 514)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..514
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55012
     Region          39..496
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 mnrrqvlwag gaigaaalla gcsgsggtsn epaaaggkpk rggtlrvgal grasavtrdp
       61 hgtqtnesdy liialvhdtl tapgaktntv prlasrwqas ddlktwrfti akgakfhdgs
      121 pvtagdvaws lrrlratpng asrlpgikae niqaegadtv vlvsdypnae lpqltrlttf
      181 vlkkgtkdke igkapgsgpf kldwfrsgna rlvrnedwyg gevlldaiev kifespqama
      241 nallggqidv asnvgavaar taeprkdvqi irrpddmamp vvmrttdgpf adakvrealr
      301 lavdreamvk qvlsgygava ndilgtgdpa yaasipqrtr dlsraksllk eagfdtskty
      361 kllttedvsg ltesatlfat qvreagvkid vvkqesatfw dktwlqgdly ttywgtndsv
      421 vffasktmfs esatnetgwk saefdaayrk aigtkdaakr atalkelqqi ehdtsgyllw
      481 gmadgidlaa apvrglptlp gygrvqlera wlar
//
LOCUS       WP_457689775             284 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689775
VERSION     WP_457689775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29126
     Region          14..272
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtaphptale qpirrrrsrg fvlrtlpall litaavtgpw lhphaidtpl tapyaepgeg
       61 aplggdhlgr dvltrllagg relivtsllv allvtvvaal lgalgalrpa vgriversad
      121 vlmllpavlg illltlswpg ggrfaviaaa vvmgvpyavr laagaaapva asgyieaaav
      181 ggerlwhlvv revlpnlrat llalfglrfv aavyvvatag flqvgpqppa adwalmiren
      241 aggivlnpwg vlapslaigl lamsvnlavs alvpqtgrka vtal
//
LOCUS       WP_457689777             508 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689777
VERSION     WP_457689777.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53374
     Region          17..507
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mnhtpgrype sqvpsaepav tvtdltiaap dgrllldggs levrpgrita ltgpsgcgkt
       61 tllravagvl ppgtrltagr ievlgrdvpa ldatelrtlr rhrlayvgqd pgsglnprmt
      121 vrrllaevaa drspqalrdl isevqlpteg gllgrrpgal sggqqrrval aralarrpaa
      181 llldeptagl dpelrneiae llrhladrhq laialschda dlvsrladdv vdlsrgapap
      241 pplpcttdrp lptgeptlvi sglhaafgrr grrtpvlhdi glavpagsst givgssgsgk
      301 ttlvravvgl hrptsgsltf dgvrlaptaq grtreqrrrl qlvpqdplgt lnpsrtigat
      361 igrplrlhrr atpdqaptrv lelleqvglp anfagryphe lsggqrqrvs iaralaadpd
      421 vlvcdevtsa ldagtassim dllddlrdrr glvlilishd lrlmasrtds llvlsagrav
      481 esgptpqift spahpvtaal vagaaqpa
//
LOCUS       WP_457689781             531 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457689781
VERSION     WP_457689781.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..531
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=57263
     Region          11..268
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,69,74,79..82,94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,77,93..96,100,102,139,141,
                     143..144,146,156..157,160,177..180)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,77,93..96,100,141,143..144,
                     146,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,100,102,139,141,143,160,177..180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,173..180)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msdegrliag ryrltehigr ggmgtvwrae dkilgrqval krlhtqphlp ddelatlyer
       61 trrearsaar ithpnvivvh dvveddgrpc ivmeyvpspt lsellkggrt igpeeaarig
      121 lgmvaalraa haagvlhrdv kpgnvllgmg ervvltdfgi amtagastlt ktgemvgsid
      181 ymaaervrgr kpgtasdlwa lgatlyqave grppfrrdta metayaiavd ppeptkragp
      241 lepliealls kepddrpsad qteqalrdvw sggptavwpp atgassladr ksvgrkdvsp
      301 dtepggqass dmsvppapta ptrttagrgp rrarkrlilv stavtvaava tagalyvtsh
      361 rstgapdaqk shqadspswa aspvpqgfhq vregklgvsf pvpdgwkasv rtaeqvtyie
      421 pvekveisvr tvapaganpv shfedkeant kvnypiyrrl rmqqttfrdq paavweytfq
      481 grkrgfrave lgfgreggre ydvsvsapea kwdtyrpvfd kvrdgfipag s
//
LOCUS       WP_457689785              77 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457689785
VERSION     WP_457689785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..77
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7881
     Region          9..69
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 msdpreplrl svdrdrcaga gmcaltapev fdqddeeglv vllhpapape hraaarmavg
       61 lcpagaialn spdstts
//
LOCUS       WP_457689799             238 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689799
VERSION     WP_457689799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26770
     Region          2..104
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(3..5,19,36..38)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
     Site            order(50,53,57..58,67,86,90,96,100,103..104)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mltigqlaar agvtvravrh yhqrgllaep erdasgyrry daqavvdlir iktladagvp
       61 larinellaa qpeefteait eidqalevki seltrhrrri telaagdrlf lpsevieild
      121 rqrtlgvser mvrierdswi mlvalapesv adwvagkeka ladpefrrly lacdeamdwe
      181 pddprlpdla tamatwdaqq sehkqpspet lslmnanvta aspawrrlmv llsrtrqr
//
LOCUS       WP_457689803             287 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces nigrescens].
ACCESSION   WP_457689803
VERSION     WP_457689803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31112
     Region          42..>247
                     /region_name="TrkA"
                     /note="Trk/Ktr K+ transport system regulatory component
                     TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG0569"
                     /db_xref="CDD:440335"
ORIGIN      
        1 mleevthhhr peppprdrrg ygawlrdrla hlpwkvflar evlavfgala tivlvlavat
       61 alaepgplwk svylplldif tmgdpatdes parrvlqlia gfvglavlpl vvaatmnate
      121 afrkasvghp paedlsdhiv lvglgkigtr vlaqlrttah qvvvierdph argvslarel
      181 gvpllledag apgvldrari rqsrsllvlt rddgenldiv maareinlrv rvvmrlyddd
      241 faatvsrtmr asypdattlp qalnyvrage tpiaasppsp hcpsrpp
//
LOCUS       WP_457689817             186 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457689817
VERSION     WP_457689817.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..186
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19542
     Region          20..157
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mnviqdeerg pmggpggrri vvgvsgslgs ltalhraaae arvteaelwa vlaweapgge
       61 svhrggpcpa amtawrrmad erllsaldea fgsagprvpl kclvirgkpg dalltaadha
      121 ddllvvgaga rgrlrramwp svarycvara ccpvlavpps plhnaldaih rrnawklpld
      181 arelad
//
LOCUS       WP_457689819             633 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457689819
VERSION     WP_457689819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..633
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=65988
     Region          51..456
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msmaegeqav saagsaavee ppdtgtqats grtatgakpa drhrltalqg laalsldama
       61 siaygpeaiv lvlaaagaqg lgftlpvtla iagllavlva syrqviaafp ngggsyavak
      121 shlgrrtslv aaaslvldyv lnvavsitag vaaltsafpa lygervwlcl avlvlvtain
      181 lrgvvdsaka flvptmlfvg ailalivvgl frdapvstas aaghasalsd nattvgalll
      241 lkafasgcsa ltgveavana vpsfrtpavr raqhtevalg allgvmligl svligrfhlq
      301 pvhgvtvlaq ladasfghna afyllqfatm vllalaants fgglpvlmsl lardnylphl
      361 falkadrqvh rhgvlalaaa saallifsgg ntnalvplfa igvfvgftic qtgmvrhwyr
      421 qrptywqaka alnglgallt giaavvvtgt kltdgawlvv valpllvlaf egihrtygri
      481 gerlelgrip qpphrarslv iapvsglsrl tsqaltaars lgdevlavtv ihnapedrqa
      541 aetlcrdwel wdpgvdliev psttrslgrp laayirnlsh hhdaqvtfli pevepahlwq
      601 rllqnqrgav vahavrrdtd avicrlrfrl aps
//
LOCUS       WP_457689839             441 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689839
VERSION     WP_457689839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..441
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=48307
     Region          39..413
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(52,80,266..267,292)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 mttnmstasi rlsdeavmpl rtldptgpld dlewldqaig darvvaiges ahyngeffql
       61 rhrllrylve rhgfsayame sgfvegqrid hwvrggegrl gqvmangtts lmglwtqmrt
      121 hlewmrqhhr tashsvgfyg idmpgsmasl lpgldavsay ladadpefri dpsiretaav
      181 faatsafsap aaipaygnva derrdaltag ladltarmts rrldylrltt adayeralra
      241 lnvtvtldam frelsrgnpq gmmlnreati adtvewilrr egrivlaahn ghvqrwpttl
      301 pgmppsttmg mhladrlgkd ylvigttsat gqtlntapdf ytgklftele pprsdsldal
      361 maashdgpfa tdlrrlspad attvravsqq rfgtyysdls pleafdvivh lphvtpagad
      421 raalahapre vqvafsqwkp a
//
LOCUS       WP_457689849             486 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689849
VERSION     WP_457689849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 486)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..486
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51590
     Region          6..481
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mdsshtppit vtdleirlsq gpallsatsl slqagkiaal tgpsgsgktt llraligdlp
       61 hgsevtsgtv qvlgedvftl apdalralrr nrtayvgqdp gsalnprmta sqliaevatd
      121 atpdavtalm aecrlpdala hhrpcalsgg qqrrlalara larkpdvlll deptagldsa
      181 lrdeivdllr hlatglgitv ilachdpyvv dacadtvitl sspaapipdp alretdhsqa
      241 teaaapttdg lratqlqvaf thrrhthqal qdarfhaptg tatgitgpsg sgkttllrtl
      301 aglqkpdsgt ltwnghplpa dvrkrsreqq rciqlvpqnp lgalnptrti gasltrplql
      361 hrtvskphrp arvrellndv glpadfadry phelsggqrq rasiaralat epdlllcdev
      421 tsaldpvtat avldlltrlr aerqltlvlv sheldlitpy tdsvhmlnqg risdsrdleq
      481 vgthsa
//
LOCUS       WP_457689850             281 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689850
VERSION     WP_457689850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28593
     Region          <61..263
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtatavldqr sarrpwpril lpvvpaillv llavlgplla ahpvdkpvta pygeagsdaa
       61 lggdqlgrdv lsrllhggsa ligsaltval avtllatllg cfavlsprlg rlveriadta
      121 illppvlgim llalawpggg rlaitlaaiv lgtpyavriv asaaaplasa gfieaaiasg
      181 egtarlalre ilpnlratvl alfglrfvda vyvismagfl qlgpqppead walmirengp
      241 gillnpwavv apglaiglla isvnlaanal apatarraal r
//
LOCUS       WP_457689852             514 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689852
VERSION     WP_457689852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 514)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..514
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55600
     Region          39..496
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 mtfnrrqvlw agsgigaaal laacgggnnp assdsggkpr kggtlrigal grssaitrdp
       61 hgnqgnesdy lvialvydtl tapglkdntv grlasswkps kdlktwrftl akgatfhdgt
      121 pvtaddmvws lrrlrntpag aarlpgikad nitaegkdtv vlvsdvanae lpmltrlstf
      181 imkkntpeke iakapgtgpf kldwyrggna rllrndkwhg gkvyldaiev tmfespqama
      241 nammsgqidv asnagavaar taatrkdikv irrpndmamp ivmrtssgpf adpkvreamk
      301 lvvdreamvk qvlsgygtva ndilgtadpd yaknipqrhr dltkakkllk eakfdfskty
      361 elittedisg laesatlfss qareagikvk vvkqesgafy ektwlkgdfy tnywgtndsv
      421 vffasktmtt dagqneadws dkdfdtayhk viataapkar taalrdvqqi ehdksgyllw
      481 gmadgidlaa pkvhglpklp gygrvqlenv wlap
//
LOCUS       WP_457689862             468 aa            linear   BCT 27-JAN-2026
DEFINITION  MATE family efflux transporter [Streptomyces nigrescens].
ACCESSION   WP_457689862
VERSION     WP_457689862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..468
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=48601
     Region          11..450
                     /region_name="MATE_NorM_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Vibrio cholerae
                     NorM; cd13131"
                     /db_xref="CDD:240536"
     Site            order(262,266,292,295,379,383,410,436,440)
                     /site_type="other"
                     /note="cation binding site [ion binding]"
                     /db_xref="CDD:240536"
ORIGIN      
        1 mqlttllrds ralatlavpl vltqlaqval tttdtvmmgm lgtadlaagg laivlfnqlr
       61 tmgvglvtsv gnqiagaaar getaqgtdap dsdrevrkiv raslavatla giagavlmll
      121 igqalvflgq eadvvaraqt mllalapgll pclwfqairq ftvgmrrpqa llqitvasva
      181 vnaginwvli hgtwglpklg lpgvgvatsl vyllsflaly lsakkdtvlg pllslniaka
      241 dratvrrlvq lgvpiaatyg seagffsvta lmagsfgsaa laahtavnql vyivfqvavg
      301 lshaasinvs relaldrpea alrikntala cagavmvvvg iiyitlpdlv lspffdtssa
      361 rdaqavsiat hlllvimvlq ffdcaqnigv gllrglddtk sgfritligy wavglpaawl
      421 lgyplgldtl giwlglltgl attailllrr ytaslatrya apepaaat
//
LOCUS       WP_457689869             178 aa            linear   BCT 27-JAN-2026
DEFINITION  Rieske (2Fe-2S) protein [Streptomyces nigrescens].
ACCESSION   WP_457689869
VERSION     WP_457689869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schneider,D. and Schmidt,C.L.
  TITLE     Multiple Rieske proteins in prokaryotes: where and why?
  JOURNAL   Biochim Biophys Acta 1710 (1), 1-12 (2005)
   PUBMED   16271700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16254
     Region          85..175
                     /region_name="Rieske"
                     /note="Rieske domain; a [2Fe-2S] cluster binding domain
                     commonly found in Rieske non-heme iron oxygenase (RO)
                     systems such as naphthalene and biphenyl dioxygenases, as
                     well as in plant/cyanobacterial chloroplast b6f and
                     mitochondrial cytochrome bc(1) complexes; cd03467"
                     /db_xref="CDD:239550"
     Site            order(123,125..126,140,142..143,145,147)
                     /site_type="other"
                     /note="iron-sulfur cluster [ion binding]"
                     /db_xref="CDD:239550"
     Site            order(123,125..126,140,143,145)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239550"
ORIGIN      
        1 mtateetgpa grgagrravv aavgaaglta alaacggdma dagsgsskaa gdhkaapgts
       61 gggdsgsggt ggsggdgaag gdggpalakt seipkgggki fkgekvvvtq pqdgeikafs
      121 aicthagcvv gevaggtinc mchgskfdit dgsvktgpat kglapakvtv kggsvtlg
//
LOCUS       WP_457689873             578 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457689873
VERSION     WP_457689873.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 578)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..578
                     /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=60102
     Region          118..401
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mwplgrivge lllsvvlgtl avgiesvrdg gavqivaval aaglllqlrr vlpgtvlllt
       61 ivggaafygl apltpvvgws agrriagvgr atgtfafayv lsfglgllqe lprvtpgilv
      121 vgalltlvat vvpglagryw sqrrtlldtl reynaqllre ramiagqarm rerqriaqdm
      181 hdslghqlal isvhtgalev dreltgrqre avgvlreasv gamhelrevv gllrdgthdp
      241 gdgatvsatt ggtptpalea mgeedvkapa rgvagierlv evsrsagtav elrrsgevrp
      301 laptadhaay riaqegltna hkhapgasit ielryepdsl vvevangpap gtaddgrsvv
      361 sggqgltglg erarlvggmv hvgptadggf rlagvlpyts seagatgssp rtatatfvdp
      421 tgdfrqqisa gslgeadpvi dgnglpkelt kamsrdkrss giaigcgaaa lialllvtgv
      481 vvggiflmse mdkamiepke yaavkvgqse aevrkrlpdg ssflaegldn gappvpegak
      541 clslnstelg sswekdpvfr fcfkdgklie kksfevkt
//
LOCUS       WP_457689875             309 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689875
VERSION     WP_457689875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31667
     Region          54..289
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mglgfrlltd ggedtsiwhq ifnfdnygel lglvqnslia gvllglvggl agvfvimrdl
       61 pfavhgisel sfagasaall lgvnivagsi agsllaaaai gvlgvrardr nsvigiimpf
      121 glglgvlfls lykgraankf giltgqiiav stpqmawlvg tsvvvlvala vvwkpltfag
      181 vdpevaearg vpvrtlsltf mlvlglaval cvqivgallv lallvtpaaa aaritaspvl
      241 lpvlsvvfal cameggilla lgstipispy vttlafviyl gcrlvearrt qraprtalgs
      301 pgdpvrtht
//
LOCUS       WP_457689895             327 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689895
VERSION     WP_457689895.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33664
     Region          24..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 magttrpgst adrasdaaav gfsgvtrsyd avravdgldl eiatggtval lgrngagkst
       61 tlnmllgllp pssgtvrlfg gtpesavrag rvgamlqdgk aiprvtvrel itfvaatyph
      121 pmdvtealel agleefggrr vdrlsggqaq rvrfavalag npellvldep taaldvearr
      181 afwrsmraya rrghtvlfst hyleeadeha drivvidrgr vaadgsgeai krraggsrvt
      241 fdlagaatgp lsglpgvsav eirgdrallr ttdsdatvla laelglvrgl qvtpasleda
      301 flaltsaeaa paapaltaga rsakesv
//
LOCUS       WP_457689897             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689897
VERSION     WP_457689897.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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 242)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25436
     Region          52..240
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mldylrlevr rtlrdrgfvi fgigmpvlmy llmtnigvgp ggaapewkia smvgmaayga
       61 lgaaigtgtg vaedkqlgwl rqlritplsp lrvvvgrglt gsvtvlpaia svllvgalvn
      121 gvrmpvwqwg alagllwigt apftllglgn gyrlsaqstg vvnmgcvlll siigglwfpp
      181 elfpgwlrsl slwtpgnrfa elgrsitegs apglgsvavl avwlalfggy avyayrraar
      241 tv
//
LOCUS       WP_457689900             482 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689900
VERSION     WP_457689900.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49063
     Region          32..470
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,158,
                     161..162,165,289,292..293,296..298,301,329,333,386..387,
                     391,395,411,414..415,418..419,422)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mvgmppiatp atltetarrr tappawlvml lvcsgqflvi ldvsvvnval pamraglgls
       61 elglqwivna yvitfagfml lggraadlfg rkrifvlgla lftvaslggg laqqpwqlia
      121 artvqgigaa vlspatltil ttsfpagpar traiatwtav gagggavggl vggmltefls
      181 wrwvllinvp vgalvlggav lwltesrqaa grrldvpgal lvtaglglva ygivqtetdg
      241 waslsallpl aaglvvivaf lavearakap lmplglfrlr svssangamv lagaamfsmw
      301 yflslyvqnv lgyrpleagl sfiphslsiv lgskiaprlm nrlgakplai agavlsacgm
      361 vwqgtmdvdg tylgtilgpg ilmalgaglt atpiasiats gadpadqglv sglmntsrqm
      421 ggalglsvls tvaasrieag dgpkaladgy glafqvgsvv llgsillmvv alpqrradaa
      481 hg
//
LOCUS       WP_457689904             753 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457689904
VERSION     WP_457689904.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..753
                     /product="acyl-CoA dehydrogenase"
                     /EC_number="1.3.8.-"
                     /GO_function="GO:0016627 - oxidoreductase activity, acting
                     on the CH-CH group of donors [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78589
     Region          1..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
     Region          379..742
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(464,494,496,528,530,724..726,728,730)
                     /site_type="active"
                     /db_xref="CDD:173838"
ORIGIN      
        1 mgigitqeqr dlaeaaggwa aravppeavr klldtaparp grpaywdqla aqgllglhlp
       61 eadgggdgel ldlavvleel graafpgpyl pttlaaallh rggapalvra latgarigav
      121 algtgsltav egpdgyvldg tappvlsgad adllvlaaev tgeaegtgga egaadgavrd
      181 ggggrraget vwlavdagtl avrvqesadp trptaevrah gvpvpaerrl tvdsdlvrdl
      241 agvlwaaesc gtaswalhta aeyaavreqf grpigqfqav khlcaemlvr yeqaaalvwd
      301 aaraldeppa vrglvaalat ataldaavsc akdciqilgg igftwehdah lhlrratvar
      361 qllgsgdthr lraarhaadg arrplhlelp agaedfrsaa rtvidgvrgl dpaavrrala
      421 ptgyaaphlp apyglgagpv qqlaiqqela aadvqisdlg iatwvvpsli ahgtpeqqer
      481 ylqpslrgdl lwcqlfsepe agsdlaslrt raertadggw ringqkvwts aaqwashgil
      541 lartdpdapk hqgltfflvd mkapgidirp lkeitgeslf nevyfdevll padavvgevd
      601 ngwkvarttl dnervhmadq ltfdtgltal ldraaeldgs vrarvgalaa eahalgcigl
      661 rttlqqvsgl epgagagirk lvqtphqqkv aelalellgp dgavregage ralhgflmsr
      721 cltiaggttq vqlnvvaerl lglprdpepr pli
//
LOCUS       WP_457689912             267 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457689912
VERSION     WP_457689912.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..267
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29137
     Region          15..240
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mtlegslshd aycthlleet tkfretvrda dlsatvptcp dwtladlarh vggahrwvga
       61 ivatrsatdi deadipesdg pekddaaald awlaagvdqa vaalreagpd tevwtwspvq
      121 rtgfwarrmt hetvihrada altagaafdv apevaadcle ewlqlcalpl vtahhaergg
      181 qlfgpgrtih lhatdtppel naewlldltg drlvhrrahe kaavalrgpl tdllgvmyrr
      241 lpadsdrvev lgeralldrw lewasfq
//
LOCUS       WP_457689906             219 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689906
VERSION     WP_457689906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  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 219)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23071
     Region          48..176
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mpaptaptap qpeilaafea akgfmpvdeg lalyaaaaea atlglplvev gtycgrstil
       61 ladaartagv lavtvdhhrg seeqqpgwey hdptvvdpev grmdtlptfr rtlhaaglee
      121 hvialvgrsp qaaavwqapv glvfidgght dehatadyeg waphlapdgl lvihdvfadp
      181 adggqapyri yrralesgaf teisahrslh vlrrtgpgi
//
LOCUS       WP_457689916             470 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457689916
VERSION     WP_457689916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49558
     Region          30..434
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtaeavqaaa prpaeaspas aptngerplr iamltykgnp fcggqgvyvr hlsrelarlg
       61 htvevigaqp ypvvddgvtl selpsldlyr qpdpfrtpkr geyrdwidal evgtmwtggf
      121 pepltfslra rrhlaarrgq fdvvhdnqtl gygllggpga lgaplvttih hpitvdrrld
      181 laaadgwkrr asvrrwygft rmqkrvarrl psvltvsgss rqeivddlgv sagrihvvhi
      241 gadtdlfspd asvpevpgri vttssadvpl kglihlveal akvrtenpda hlvvvgkrad
      301 dgpvaaaier lglsgaiefv kgisdpelvd lvrsaqiacv pslyegfslp aaeamatgtp
      361 llattggaip evagpdgetc lavppadaga laggllrllg detlrrrlga agrervlarf
      421 twrqaalgta eryreaialq rgrsgartlp raasggaagt tpapsaaghv
//
LOCUS       WP_457689918              77 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457689918
VERSION     WP_457689918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..77
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7744
     Region          7..63
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mgdrwqvvvd rrvcigsgmc aaaapdgfrl dsarqsqpva peadaaesvl aaaegcpvea
       61 itltvsgsge avfppee
//
LOCUS       WP_457689928             542 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689928
VERSION     WP_457689928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 542)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..542
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56541
     Region          1..508
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mirfeqvsvt ygdaaapavq gidltvpege lcllvgpsgv gkstvlnavc glvphftggt
       61 lrgrvtvdgr dtrthkprel advvgtvgqd plahfvtdtv edelaygmes lgltpevmrr
      121 rveetldllg laelrdrait tlsggqmqrv aigsvltthp kvlvldepts aldpaaaeev
      181 lavlqrlvhd lgttvllaeh rlervvqyad qvillpspga ppvmgtpadi mavspvhppv
      241 valgrlahws plplsvrdar rkaaplreql tavppqapgg saegtpaasd aaaevsglgv
      301 rrgrtealhg ldltvrgget ialmgrngag kstllttlvg mhqpssgtvr vggavphrts
      361 prallrhvgl vpqeprdlly adtvaaecta adqdagapag scralvarll pdvpesvhpr
      421 dlsegqrlal alavvltarp plllldeptr gldyaakarl ievlrtlaae ghaivlathd
      481 velaaelahr vviladgeiv adgptdevvv sspsfapqva kvlaplpwlt vpqvaralea
      541 la
//
LOCUS       WP_457689941             209 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457689941
VERSION     WP_457689941.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23437
     Region          5..167
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mstddafaea yrahywavsr fvarrldgqa leveevvaev fsiawrrrae lpeaplpwly
       61 gvarnclant vrgmgryrrl lhrlgnheaa hrrqtvdspd aerpgswvhe alarlspadq
      121 evlrltawee ltieelavtl gcgqsaaamr lhrargrlrt qiermrprst arpeappprp
      181 dappaprpat prplsphpvp traggrrhd
//
LOCUS       WP_457689945             178 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689945
VERSION     WP_457689945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19342
     Region          45..172
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 msdaatlrlp wtvaaepags pdaeallrey ytevadryfa lhedrrstpe eieeglaeyp
       61 tadlappggv llvarhgeev agcagvrlld artaelkqmf vrparrglgg agallgaaet
      121 aavrlgaerl rldtrldlve avalyrrhgf leidpyhddd pyaeiffekw ldggplrg
//
LOCUS       WP_457689947             692 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457689947
VERSION     WP_457689947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..692
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73342
     Region          37..432
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(38..39,42,73,123..124,126..128,131,151,154..155,158,
                     283,286..287,290..292,295,323,327,380..381,385,389,405,
                     408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 maqdtgapav pgedrsrrtv laaigalllg lliaaldqti iatalptivs dlgglnhlsw
       61 vvtayllast aatplwgklg dlygrkklfq taivifligs vlcgiaqnmg eliafralqg
      121 lgggglivls maivgdivpp rergkyqglf gavfgsssvl gpllgglfvd hlswrwvfyi
      181 nvpvgivala viaavlhipr rrtphridyl gtaaiaavaa cfvlmtsfgg vtypwaswqi
      241 vgcgvlgvvl lgaflvierr aaepvlplrl frlrtfslta vigfiigfam fgsmtylptf
      301 lqvvqgvspt msgvhmlpmv fgmllastgs gqivsrtghy kvfpiagtgv valgllllhr
      361 ldpgsgvvem sacffvfgfg lglvmqvlvl iaqnavpyrd lgvatsgatf frsiggsfgv
      421 slfgtifagn lgtriadala gqqlppgidp sriaedprtv aqlpagqrag vlnayavsit
      481 dvflyavpvv lvafalawfl keeplrssvt apdttevlss npverssrde varalstlgs
      541 regrkhvyek iaaragldlk paaawlilri hrygsvepgl laerstvplg visesvrqie
      601 erglatregl lllltgrgrd taerlsaarq qslaemlgdw wtrdrptdlt elvheltael
      661 cgsdaeephn gdarsplprt hppaphppdl ak
//
LOCUS       WP_457689952             193 aa            linear   BCT 27-JAN-2026
DEFINITION  TMEM165/GDT1 family protein [Streptomyces nigrescens].
ACCESSION   WP_457689952
VERSION     WP_457689952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20033
     Region          4..193
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 mfsftvaavv fgviflaelp dktalaglml gtryrasyvf agvaaaflvh valaiaagsv
       61 ltllphrlvq gvvgvlflag aavllfrkge deeevkkpad qsfwkvsgag fmmilvaefg
      121 dltqimtanl aaryddplsv gvgavlalwa vaglgilggr tlmkyvpiel itkvaagvml
      181 llagfslyea iag
//
LOCUS       WP_457689954             252 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457689954
VERSION     WP_457689954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25791
     Region          30..239
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mllpvnttlg ivlavlltaa vaiaalarlg haraiavagl raaaqlaavs yligwvvhal
       61 swllgflvlm favavrtagr ritrnrswww aaapitvgvv pvvglllltg lvpprglvli
      121 pvtgiligga ltatvlggrr aldeletrhg efeaglalgl pdrdarmeva rpaasdallp
      181 gldqtrtvgl vtlpgafvgm llggaspvqa gavqlfvlva llavqataca vvlelvargr
      241 lhrvpltaae ge
//
LOCUS       WP_457689958             574 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457689958
VERSION     WP_457689958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 574)
  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 574)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..574
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=63037
     Region          103..464
                     /region_name="MPP_PhoD"
                     /note="Bacillus subtilis PhoD and related proteins,
                     metallophosphatase domain; cd07389"
                     /db_xref="CDD:277335"
     Site            order(109,152,155,214..216,220..221,432,434)
                     /site_type="active"
                     /db_xref="CDD:277335"
     Site            order(109,152,155,214..215,220..221,432,434)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277335"
ORIGIN      
        1 maglrlgpll ryvdadsatv wvetdrpcmv hvrcddgaag aqhtwqvagh hyalvpvtgl
       61 tpgsqtpyrv llddaqevwp lpdsrfpast irtlpasahe plhfafgscr wsatpsnaah
      121 dpvgpdaldt laatlaagsg rqrpdvllll gdqvyadqts eataqvlagr rdlteppwkq
      181 vadyeeytyl yyeswldpev rwllstvpsc mifddhdvid dwntsaswla rmratpwwre
      241 rilgglmsyw vhqhlgnlsp aelaadelya qvrsvpdate lvrefaagad adaaharwsy
      301 rrdfgrvrlv midtratrvl desnramldk tegewlrqav ldgrgsydhl llgsslpwll
      361 phlihagegw nanlcagerg prwarrserl rqradlehwa afpgsftalt eliaeagsga
      421 hapatvcvls gdvhhayvae phwrgagphp tsrvlqltcs pvhnsipgsl qagfrfgwsr
      481 tgrwlgklla rhgrlprpav kwrrtggpwf gnqlmtltla graarlaldq trqekqggvr
      541 lvtvwraalt darvggksgg aggpaagter pksg
//
LOCUS       WP_457689962             152 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457689962
VERSION     WP_457689962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15766
     Region          6..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mspltsftqr stphalalfr ivigllfach gasslfgvlg gamgqggtvp tgswpgwyaa
       61 viqlaggllv mlglgtraaa fissgsmaya yfsahqgsal wpiqnggeas amycwaflll
      121 fftgpgswal drvffdrgqe aaptaqreps sv
//
LOCUS       WP_457689964             217 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457689964
VERSION     WP_457689964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22238
     Region          13..183
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mleslgslgg tpwvyvivsl sivldvfvpi lpsgilviaa attaagtgta adavggvevt
       61 atvhtgahla eifslvlcaa tasvlgdmva yrlarrggdr fdraigrsrr lttaqerlgt
      121 altrggggiv vlarfapagr svvslgagva hrtvreflpw salagfawaa ysvslgyfgg
      181 hwlgtswmst alsvvalfaa gsaaaflmrr pdrrtah
//
LOCUS       WP_457689966             193 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457689966
VERSION     WP_457689966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19959
     Region          31..174
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 msgthashga hetgdsgsgd pavapgpwrp rpetpadtaa vrrinlaafe taeeadlvda
       61 lrrdpsawlp glsyaadapd gtpaayallt rchvdevpav alapcavlpg yqkcgaggav
      121 iralleaara agertaivlg hppyyprfgf vpaarfgilp pqpwpdeafm alslddsapp
      181 rgtvryaeaf gid
//
LOCUS       WP_457689976             216 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457689976
VERSION     WP_457689976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23352
     Region          20..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msviegdage htggdgagep tttedllydv irrlwplhrt vvraverela dtgmtageha
       61 lldalhtegp rtvpqlaram gldrqpvqrw vnhaaelglv vtapnpahrr sslirltteg
      121 taairgiqqf eatelrqrla dlpaedvrta lhvldrlgee frhlangsrv qreetdsqgs
      181 rdsrgsegsn gsngnpeghd irpapaplmh kgrsge
//
LOCUS       WP_457689979             166 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457689979
VERSION     WP_457689979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17700
     Region          3..131
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 msvrrlnhav lnvrdvprsv afytealglt vdveipgraa flsapgslnd hdlglfavep
       61 dapgpgtgrv glyhlawevg tlgelvaart rltergalvg ssdhlvaksl yakdpdgnef
      121 evmwrvpred wpgpdrpdrl lpldlaaale rwgpdretga aagsat
//
LOCUS       WP_457689981             183 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457689981
VERSION     WP_457689981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18328
     Region          41..158
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtsplgtlas sriatptrha pslhgydagl lllrlalglt maahgaqklf gwfggpgldg
       61 tgqfftmsgy pagrtmavva gltetlgglg laaglltpla gaavvgtmin alavkwgggf
      121 fapkgveyel lltagaaalt ltgpgryaid rflpglrapr pvhgvvalll gvvmaagvll
      181 vrk
//
LOCUS       WP_457689983             265 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457689983
VERSION     WP_457689983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10158671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27293
     Region          15..199
                     /region_name="crotonase-like"
                     /note="Crotonase/Enoyl-Coenzyme A (CoA) hydratase
                     superfamily. This superfamily contains a diverse set of
                     enzymes including enoyl-CoA hydratase, napthoate synthase,
                     methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA
                     dehydratase, and dienoyl-CoA isomerase; cd06558"
                     /db_xref="CDD:119339"
     Site            order(30,32,64,68..72,111,113..115,137..138,141)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:119339"
     Site            order(70,115)
                     /site_type="active"
                     /note="oxyanion hole (OAH) forming residues [active]"
                     /db_xref="CDD:119339"
     Site            order(95,103,124..127,139..142,148,150..152,154..155,
                     160..161,163..164,166..167,170,181,184,199)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:119339"
ORIGIN      
        1 mtavpapdlt iatfrtgava qirigdgsrr nalpgeawvr larqvrelga crslrvlvis
       61 ghgdtfcags dmtdwvdads ayveesfahm eeafsaieec pvpvvaeirg vaagagcqla
      121 lacdlrlmad sarigmpiar lgilaspafa armvalagps varellytgr lvdartavel
      181 gladhqvpea qltdrtgrlt aavaaqppaa ihaaklavga vlgpqrqata vnprpavars
      241 hfgqaiaafl gqqpaaaapd ppfap
//
LOCUS       WP_457689985             408 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457689985
VERSION     WP_457689985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43615
     Region          15..406
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mrntphpqpw lvhdgaltgl kvldlsrils gpfctmmlad lgadvikved tvsgddtraw
       61 gppfqgedaa yfhsvnrnkr giavdlkdpd clrliqelat tadvivenfr pgtaarlglg
      121 yqdvrdrnpa vvyasisgyg qtgpyrnepg ydaiaqavsg vmsvtgeptg ppvrfgvspa
      181 dlaagmwaai gilaalrnre htgtgewvdv slldgqvawl syvaggyfas gnvpqrygsa
      241 hptivpyqaf ptadghlmva agndglwrrf ataiglaalv ddprfatnpd rvrhraellp
      301 lieralsarg akewavllte aeipvgpint vdealrhpqv vargmiaele htdagtlrti
      361 aspiklsdhp atvrtppprh gehtapvlta mgvdprqlad lrarkaak
//
LOCUS       WP_457689988             148 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457689988
VERSION     WP_457689988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..148
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15588
     Region          24..138
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mnatapseys gshamprrda eflfplphip eavglvrrra htvltgwnlp aptiedavlv
       61 iselvtnavt halppavlql srtvaeepra lrievtdagp avpvprpadg rypaehgrgn
      121 aivtalaarh gtrvdpggit rwadlpag
//
LOCUS       WP_457689990             299 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457689990
VERSION     WP_457689990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32278
     Region          6..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mlnspaleyf levvrtgsvn easrrllvag saisrqigkl eqeigvalfe rrprgmvpse
       61 agtllaayar raaletdqvl aeirgrgrlg tivrvassqg aaqeflpaam asfrkdhpgt
      121 tfqmpvvtps latqmvqdgs vdlavtfsla papdvrviha qrapiqalvr sdhplaqrde
      181 ihlhellpyp valteegttn rrlfdlccsi egiafepllv sssssalsaf vkeanavsli
      241 ghisvygrlr vdglksitil npemhlrtlq iqamagrqlp avvnefadhl ihqlgetev
//
LOCUS       WP_457689994             108 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457689994
VERSION     WP_457689994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..108
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=11653
     Region          7..104
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 mtdevfvdsa alrklaksfe thaydlqshl ksfsqktgee aigdgfgvlt eseeitssyv
       61 dyskdvsaam ekvhrhldai gaaleqvtrn tetsdddvsa lfgrkggh
//
LOCUS       WP_457689996             364 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457689996
VERSION     WP_457689996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=36547
     Region          25..108
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 msddesvaek vfevgieain pggrpdvlra aaagwrslas eaeemfskld gevkgtvget
       61 wrgpaaeafq nhwkqlksai ddttgefeec akgldeaaks ieeindeihg iyaeigisva
      121 vsaatslfsf glstaagaar vaqlasrava aagrlgvllq rvasvfrtly agrkgkiild
      181 alanwaggta ggvatsilsg kgpewrtnal gglggatlgt gagkvaeslm gnrvgktfvt
      241 gaaggavggv tgdaldaafd kekefdpass aitavtgaaa gggaaegvsf qrafdirpth
      301 agrdlaqdva mnsavpvfgg pagndakdgv ekvsgssdea qaaakkrtdg lgtsgtdrie
      361 dvfg
//
LOCUS       WP_457690004             233 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690004
VERSION     WP_457690004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..233
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25168
     Region          7..231
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 msrsghaass ghgahhgave alarrifkgt ygegdslvmp evlaeldvsq tvlresikvl
       61 ttkgllgtdr krgtfvrpre dwnlldtdvl rwklaagvss dfladvlelr rsiepaaaal
      121 aaerrtdedl aaldaalsam aaadndpvll vradasfhta mliasnnrfy aqmhrvivpv
      181 lvqrdrevla adgafeqpha mhaavveavr nrdvdgayma mlelldvsar ehp
//
LOCUS       WP_457690011             379 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690011
VERSION     WP_457690011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..379
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40307
     Region          170..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlgiarrglr latglvlgav iaaaelpfvl lsglsllcvf awprgrravl kpvtaaaral
       61 tethrrrlrv yvaadtsgay adhralqyly lrwglgllga lvlgaaligv aygiswifil
      121 lltdvshpgt lalssigglf llflsmqgtf gvagletrla qyylgpshhe elerrieqla
      181 asragvvaav nderrrierd lhdgvqqrlv algmllgral rsqdvqraeq llrqaheesg
      241 qaltelreva wrvyptvlde aglraaletv aersaipvcl dyelatepdt avatvayfvv
      301 seavtnavkh sgagrisvrv apgedavlvr ieddgpggad ssggglfgla rrvaaldgrf
      361 rvdspaggpt titaelpca
//
LOCUS       WP_457690007             206 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional 4-hydroxy-2-oxoglutarate
            aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Streptomyces
            nigrescens].
ACCESSION   WP_457690007
VERSION     WP_457690007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Fullerton,S.W., Griffiths,J.S., Merkel,A.B., Cheriyan,M.,
            Wymer,N.J., Hutchins,M.J., Fierke,C.A., Toone,E.J. and
            Naismith,J.H.
  TITLE     Mechanism of the Class I KDPG aldolase
  JOURNAL   Bioorg Med Chem 14 (9), 3002-3010 (2006)
   PUBMED   16403639
REFERENCE   2  (residues 1 to 206)
  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   3  (residues 1 to 206)
  AUTHORS   Gefflaut,T., Blonski,C., Perie,J. and Willson,M.
  TITLE     Class I aldolases: substrate specificity, mechanism, inhibitors and
            structural aspects
  JOURNAL   Prog Biophys Mol Biol 63 (3), 301-340 (1995)
   PUBMED   8599032
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Conway,T.
  TITLE     The Entner-Doudoroff pathway: history, physiology and molecular
            biology
  JOURNAL   FEMS Microbiol Rev 9 (1), 1-27 (1992)
   PUBMED   1389313
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="bifunctional 4-hydroxy-2-oxoglutarate
                     aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase"
                     /EC_number="4.1.2.14"
                     /EC_number="4.1.3.16"
                     /GO_function="GO:0008675 -
                     2-dehydro-3-deoxy-phosphogluconate aldolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008700 - (R,S)-4-hydroxy-2-oxoglutarate
                     aldolase activity [Evidence IEA]"
                     /calculated_mol_wt=20518
     Region          1..206
                     /region_name="Eda"
                     /note="2-keto-3-deoxy-6-phosphogluconate aldolase
                     [Carbohydrate transport and metabolism]; COG0800"
                     /db_xref="CDD:440563"
ORIGIN      
        1 mdfstalrte rliaiirgrd aeasfrtvmt lakaglplie vslsghdalt virraraelg
       61 daawlgagtv ltasdarraa eaganlivtp glgagleesv rqglstlagv ltpseviaad
      121 algvsalklf pasvggpgyl qalrapfpel sfvpvggvda aaapayfaag avavgvgspl
      181 vgdaadggdl dalrkraaef kaacaq
//
LOCUS       WP_457690009             219 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457690009
VERSION     WP_457690009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24128
     Region          3..130
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          153..200
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrvvladdst llreglvrll aeeghevaaa vgdadqliav leqageqgek pdavvvdvrm
       61 ppthtdeglr aavqirerwp digvlvlsqy verryatell tddsegvgyl lkdrvvqvde
      121 fldalervsr gqaafdpevv rqllmrsrrs dplgtltare qevlremaqg htnaaiavrl
      181 hisqsavekh inaifdkldl igtagysrrv lavlrylgt
//
LOCUS       WP_457690012             212 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457690012
VERSION     WP_457690012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22291
     Region          12..182
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 miesigstap gwitdlmdal gapgagvaia aenlfpplps evilplagfa aargsmhlas
       61 alawttlgsv tgalalygag allgrertva iasklplvkv sdiekterwf rrhgtkavff
      121 grmiplfrsf isipagierm svpvflaltt igsliwnaif vlagyllgdn weevtgyvdv
      181 yskvvlvata lavavfvvvr vsrrgpggrr rg
//
LOCUS       WP_457690014             273 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690014
VERSION     WP_457690014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 229399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="HAD family hydrolase"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29388
     Region          4..>116
                     /region_name="HAD_like"
                     /note="Haloacid Dehalogenase-like Hydrolases; cl21460"
                     /db_xref="CDD:473868"
ORIGIN      
        1 msaiiasdld rtliysaaal glampdaeap rllcvetyer kplsymteta agllaeladk
       61 ttfvptttrt reqygrihlp gpasefaica ngghllvrge sdpdwqrtva erlaaqcapl
      121 deirahlvrt adpawllker saedlfaylv verpllpdtw vkdlagwade rgwtvslqgr
      181 kiyavpkplt ksaavaevar rtgaseilaa gdslldadll laadrgwrpg hgeladsgwh
      241 aphvtalder gvaageeimr afirgavppg had
//
LOCUS       WP_457690021             247 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457690021
VERSION     WP_457690021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=27373
     Region          <26..244
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msflgnlwrg gsqkfdfdsg gasyvveltk rnpvvsltkq gaatghlrvn lhwqmrpsdl
       61 herggrgkgg llrhpgklfk pevvqaqgpa vvnvdldlac lyelkdgtrg vvqplgnflg
      121 dlngppfvkl sgddrfgsgs getlyinldh rdeikrmlif vyiydgtpaf drthavvtly
      181 pssgprvevk lderasqars cavfmlenvk geltvrrevk yvygfqaeld rlygwglqwg
      241 rgyktkv
//
LOCUS       WP_457690028             533 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690028
VERSION     WP_457690028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..533
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54954
     Region          34..471
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,159,
                     162..163,166,291,294..295,298..300,303,331,335,387..388,
                     392,396,412,415..416,419..420,423)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mssqtpvaea apelpvpdpp kglrghpwlt lfsvaigvmm valdgtivai anpaikqdlg
       61 asladvqwit ngymlalais litagklgdr fghrqtflig ilgfaaasaa igfsdevalv
      121 itfrvlqglf gallmpaalg llratfpaek lnmaigiwgm vigastaggp ivggllvehv
      181 nwqsvffinv pvgvlalvlg lvilkdhrae naprsfdipg ivllsgamfc liwplikage
      241 whwdsmktwg fliaavvlfv lfavleskvr epliplrmfr slpltagtvl mvlmafafmg
      301 glffvtfylq nvhgmtpvds glhllpltgm mivgsplagv litkfgprip lvggmvltav
      361 amygmsgldt dsgtglmslw fallglglap vmvgateviv gnaplelsgv agglqqaamq
      421 vggslgtavl gavmasrvds dlpdnwrsag lppvppatas qlsdavsagi apipkgtppe
      481 faqkitsaah dtfvsgmgqa ftvacgvavv aavvafftkr ganaeagagv ghi
//
LOCUS       WP_457690030             217 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690030
VERSION     WP_457690030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24054
     Region          15..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matptphaap aglrerkkqr trdaliraal elfteqgyea ttideiaeav dvsqrtyfry
       61 fankedvafa vqemvearfl deltarpaae apltalrsav mvawddigsa iesvipvelh
      121 mrsfrmiest palvaahlrr sseleeqiar liarregldv dadprprvlv aafsgvmrva
      181 grvwgegqdc svasirevtq syldqigpam eddwrar
//
LOCUS       WP_457690036             463 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690036
VERSION     WP_457690036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  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 463)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..463
                     /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=49141
     Region          190..439
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtgrsstpep epahgpgrep arqralravr qglrvlavel gtptepgtpl lgsvrspwlr
       61 rlpyvvafgf avsllpttin vlshdygldg glagalataq tvplllavtr plqawwvifa
      121 advigalalt gadgvadraw pwppmeivgy lalmlalslr errrtltavw lttgvaglls
      181 qvftpdgsns twvlmfvltg vvlmmgatlr ergdaqrkli eqetiseaer arrtlleera
      241 riarelhdvv ahhmsvitvq aasapyrisg ipreaedefg tiaataresl aemrrllgvl
      301 rseetvqhdg pektpqpgig mlpklvegtv ragvpvelal peetvalepa vdlsayrivq
      361 ealanvvrha pgartrvsvt laadgarltv lvvnsapsap saplettgtg hgligmrerv
      421 rlvdgsldtg plpdggfrva aqlplpppps pasplsakds hsv
//
LOCUS       WP_457690039             416 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690039
VERSION     WP_457690039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /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=43752
     Region          33..>263
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msrllttarr grrtligags avaladrtpa drdraldglr alallavptg hwliggftld
       61 aggalhnasl ltavgglapa swvlqllgif flvgghasvl slrratgrge strawlrgrl
      121 vrlgrpvlgv tavwavllpl lygvgvpeat lrtgatlviq plwfvgvyav italtpcclr
      181 aarwmgawaa aplaaavaav dflrygpyad amppwlslln llpgwmfayq lgvswgerrl
      241 ggraawslll ggaavfaall lffhyptsmv gvpgqdrtns hppsllvlal aaaqsgaavl
      301 lrdrlarllr rpalwapvai vnlsaltilc whqtamlsla vpasflgqvp gltvapdtlg
      361 wvlarlawlp vfaaalllig rttrrfeapw tgvnkvrraa tallaagfga falgla
//
LOCUS       WP_457690041             338 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457690041
VERSION     WP_457690041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 338)
  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 338)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=36337
     Region          7..315
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(26,209..212,215,266,288..292,295,298..299)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(56,61,86,130)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mgsekietve lgnggprvgv qglgcmgmsf aygptdtdea ratleralel gvtlfdtadm
       61 ygmgenekfi apfirahrde vvlatkfais ldpddpskri irndrayirq avegslrrlg
      121 vdeidlyymh rrdvnvpiee svgamaelva egkvkhlgls evtgselraa qavhpitalq
      181 sewslfsrdi eegvvqaave lgvglvpysp lgrgfltgaf vhadkelgad dfrrqqprft
      241 gdnaaanaal lepvravaea hgatpgqial awvqqqatar glavvpipgt rkrsrieent
      301 gatrirlteq dlaqlepiag qvagaryadm sftsagre
//
LOCUS       WP_457690043             160 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690043
VERSION     WP_457690043.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 160)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..160
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18010
     Region          39..150
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(40..42,56,73..75)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(87,90,94..95,104,122,126,132,136,139..140)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 mtvtqsgpaa sraigglptk vrdcgtapph prpagrdqyt isevaqhtgl sahtlrwyer
       61 iglmphvdrt htgqrrftnr dldwlslvtk lrltgmpvad mvryaelvra gectfaereq
      121 lltahredvr qriaelqstl dvldykieiy adarraserf
//
LOCUS       WP_457690045             273 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690045
VERSION     WP_457690045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28563
     Region          5..271
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqslrmienw pvptaaaavv radgsvagay gplehrfpla svtkplaaya allaveegav
       61 eldepagpeg stvrhllaht sglafdeprp maepgtrriy snagfealgd hiakatdipf
      121 pqylheavlv plgmtatelp gspakdgvst vadlirfaae lqaprllapq tlaaapqvvf
      181 pglsgvlpgy ghqkpndwgl gfeirdgksp hwtgassspr tfghfgqsgt flwvdpdara
      241 acvaladraf gpwaieawpp ltdavlaela qta
//
LOCUS       WP_457690048             313 aa            linear   BCT 27-JAN-2026
DEFINITION  ACP S-malonyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690048
VERSION     WP_457690048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32151
     Region          1..302
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mlvlvapgqg aqtpgfltpw ldlpgvedrl rawsdaidld lvhygtkade eeirdtavaq
       61 pllvasalls arqlfatadd vatqtgavag hsvgelaaaa lagtltdeaa mtlvrrrgqa
      121 maeaaavtet gmaallggde avviphleql gltpanvnga gqivaagtae qiaalvenkp
      181 egtrrvvplk vagafhthhm apavsalesa taqlavadph tryvsnkdga lvssgqelvq
      241 rlvgqvanpv rwdlcmetfk elgvttliea apggtltgla kralpgvrtl alktpddlda
      301 artliaeqsa pae
//
LOCUS       WP_457690055             304 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690055
VERSION     WP_457690055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=33529
     Region          65..296
                     /region_name="SGNH_hydrolase_like_1"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01832"
                     /db_xref="CDD:238870"
     Site            order(72,277,280)
                     /site_type="active"
                     /db_xref="CDD:238870"
     Site            order(72,277,280)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238870"
     Site            order(72,121,149)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238870"
ORIGIN      
        1 mtrtdrpfrp rrrrfrlras rtvaigsalv ialtgcsgdg saphsgaagk rkaakgpvwr
       61 thprsiaalg dsitvgfdac tvlsdcpqvs watgtdpkvd slarrlvkhp tthswnlart
      121 galmsdlpdq vtaaadrrpe lvtvligand acrrdvrtmt ptdafrvdfa rsmkylrral
      181 phtqvyvaav pdllrlwseg rknplgkqvw klgicgsmlr npddltqaah drrakvrgrv
      241 mayntalaev cgkdplcrfd ksvfdyrftg rqlstwdwfh pgtggqkela elafraitrp
      301 grra
//
LOCUS       WP_457690057             348 aa            linear   BCT 27-JAN-2026
DEFINITION  aldose epimerase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690057
VERSION     WP_457690057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Thoden,J.B., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     The catalytic mechanism of galactose mutarotase
  JOURNAL   Protein Sci 12 (5), 1051-1059 (2003)
   PUBMED   12717027
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="aldose epimerase family protein"
                     /EC_number="5.1.3.-"
                     /GO_function="GO:0016857 - racemase and epimerase
                     activity, acting on carbohydrates and derivatives
                     [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36320
     Region          21..338
                     /region_name="galactose_mutarotase_like"
                     /note="galactose mutarotase_like; cd09019"
                     /db_xref="CDD:185696"
     Site            order(74,85,110,180,182,240,280,306)
                     /site_type="active"
                     /db_xref="CDD:185696"
     Site            order(180,306)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185696"
ORIGIN      
        1 mktqvsrepf galddgtrvd rwtlesgpgg vrvrvltygg iiqtveapdr dgtrgqlalg
       61 fadlgsyvah ggshfgalvg ryanriagas frldgrnwal tpndggnslh ggprnfsrvv
      121 wearpvdggv qlhrvspdge egfpgaldvr vtytlspgga lrivscartd aptvvnltnh
      181 tylnlggdgs gsaaghelrl aasrytpcdd sgipvpgapa evtgtgfdfr taravggafd
      241 hnfaldggvr qaprtvaely dprsgralel attepglqly taghldgtlt gtsgvpygpa
      301 aglaletqhf pdspnrpdfp stvlrpggty rsetvygfsv rprsagnp
//
LOCUS       WP_457690071             307 aa            linear   BCT 27-JAN-2026
DEFINITION  ribokinase [Streptomyces nigrescens].
ACCESSION   WP_457690071
VERSION     WP_457690071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="ribokinase"
                     /EC_number="2.7.1.15"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30465
     Region          3..293
                     /region_name="ribokinase"
                     /note="Ribokinase catalyses the phosphorylation of ribose
                     to ribose-5-phosphate using ATP. This reaction is the
                     first step in the ribose metabolism. It traps ribose
                     within the cell after uptake and also prepares the sugar
                     for use in the synthesis of nucleotides...; cd01174"
                     /db_xref="CDD:238579"
     Site            order(11,13,38..40,43,95,97,107,109,140,247..248,251,287)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238579"
     Site            order(14,16,21..27,40,94,96..98,104..111,166)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238579"
     Site            order(186,219..221,224,237,243,246,249..250,253,275,
                     278..279,282)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238579"
ORIGIN      
        1 mydvlvvgsa nadltvrvdr rpgagetvlg tdlvesaggk ganqaaaaar iggrtallar
       61 vggdaygell lgaqraagtd vtpvivdgta rtgtamiivd pdgdnsivvs pganaaltpq
      121 dvaaakdtia asavvslqle ipmesvraaa aaaeqagtrv vlnpspapta dlapellsva
      181 dplvvnehea rqlsgltdgt paqwaqalrd rgarsvvvtl ggdgalvlda sgaenvpgvr
      241 vkavdttgag daftgalatr largdalpea arfavrvgaa avtkpgaqps yptraelevl
      301 apeqpqs
//
LOCUS       WP_457690063             238 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690063
VERSION     WP_457690063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25061
     Region          23..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtardqhgpg ggpaarragg gretqraerr aaileaamel iaergyrrts laavaeragl
       61 tqqgllhhfp tkelllvgvl etrdrwdlas aaaaagarht dtlaqlvdyn atrpglvqty
      121 tvlsadsvte dhparaffes rfravraamt evlrtecgdt lpggltpera aplmvavmdg
      181 lqlqwlldpe dvempaafrd flallgcger radgpgeepg geagaepgge agaepgeg
//
LOCUS       WP_457690073             530 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690073
VERSION     WP_457690073.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..530
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=56898
     Region          14..509
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mtgvnddepg grellrvegv tksfpgvral dgvdltlrtg evhvllgeng agkstlikml
       61 sgahrpdegr llvdgdeati rsaqdaerhg iatiyqefnl vpgltvaeni flgrqprtrl
      121 glvdrkamra raaellrrvr ldvspntpva elgiarlqmv eiakalslda rvlimdepta
      181 vltseevetl feivrelrdt gvgiifithh leeigalgdr vtvlrdgrsv aevpastded
      241 elirlmvgrd iaeqfprrrp depgapllrv rgltrngtpa gpvfegidfe vragevvgla
      301 glvgagrtev vraifgvdry dagtveidgk elargdvraa mraglglvpe drkgqglvld
      361 aslqdnltla rldrdtrggl vdrgaqrrea atvaaqlkvr msglgqsart lsggnqqkiv
      421 igkwlltdtr llildeptrg idvgakveiy qlineltasg ravlmissdl pevlgmsdrv
      481 lvmsqgrlag elsaeeatqd avmelalqsp ggtpentqhd esamegsdvh
//
LOCUS       WP_457690075             333 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690075
VERSION     WP_457690075.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  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   2  (residues 1 to 333)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35142
     Region          1..331
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 manikdvaer agvsvatvsr vlnghspvae trervlaavr elgyrpnnva ralrtartga
       61 lgliisdltn pffteladav edearslgys lvignagerp dqqddyirtl ldrridgllv
      121 ssagtgsaml sevvasgtpl vlldrtvpgv dapcvradgr taltelaahl aalgrrrpai
      181 ivapagtptg derlslfrta lggygltlpd ervgatpdlq htggrqvmsa fldlaeppda
      241 vlatdnlmal gamdelrarg lrvpddvalv vyddvpwfah tdppltaiaq ptrelgraav
      301 htllariedr pagsvllpar lvtrrscgel ptp
//
LOCUS       WP_457690079             339 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457690079
VERSION     WP_457690079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=36028
     Region          5..337
                     /region_name="CurA"
                     /note="NADPH-dependent curcumin reductase CurA [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG2130"
                     /db_xref="CDD:441733"
ORIGIN      
        1 msalpttsre whlvarphgw ptpedfalre aavpevgegq ilvrtqhfsv dpymrgrmnd
       61 vksyvppfrl dqpmeggavg eviasradsi avgdhvlhgl gwreyavlda kraakvdpsl
      121 apltaylgvl gmpgltayag llevasfkeg davfvsgaag avgsevgqia klkgasrvig
      181 sagsdekvkl lveeygfdaa fnykngdvrt qlkeaapdgi dvyfdnvggd hleaaissln
      241 vhgraaicgm ismynateps paprnlamvi gkrlrlqgll vsdhsalqpk fveevsawir
      301 sgelkysetk isgiengvea flgllrgent gkmivsleg
//
LOCUS       WP_457690081             143 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457690081
VERSION     WP_457690081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15684
     Region          1..138
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtpradpltv evvdligtvv aryyeeyeqa aaehsltgaq arvlsllsle plpmrkvaqr
       61 lkcepsnitg ivdrlesrgl verrpdpadr rvklaaptde gtrtaaalrt sldfareplg
      121 rltvaertll kellqrmlgv ape
//
LOCUS       WP_457690083             607 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690083
VERSION     WP_457690083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 607)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 607)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 607)
  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 607)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..607
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64411
     Region          16..584
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtvrhsfprt gpaprlrtlw sfalphkgal aaalllglva salglatpmv tkwvldalgt
       61 ssslqgpvva llvllvvgga vrfrqwtllg tvgervvlea reamvrrflr atvpavtrrp
      121 tgelvtrvts dtvllreaat galiglingt vmllgtlvlm gvldivllgt tmaavaltgv
      181 lfavlmpgia aaqqraqehl grlggvlagt lrairtvkvs raedrtaeri laeartsaey
      241 gihavrreal awtaslsgie latiailgvg awrvgegqme vssliaflly afglmepvte
      301 lsanvsalqa giaaaerire tadlatesta kpasstspas yrgqrhdvpv ltlrqvtaay
      361 gpdaepavrd idlavarrgh taivglsgag kttlfslflr fleptrgell ldghpyrdht
      421 heeirarlay veqdtpivpg tlrdnlllsr pdttdeelrr vlrdvrlaek idalddgldt
      481 plsdttvsgg erqrialara llrtpdvlll deataqldgl teaavhdcvr araatgavvt
      541 iahrlstvid adtivvmeag rirvqgshge llatdalyre lvkslrisad tapapeavpa
      601 parrtap
//
LOCUS       WP_457690089             410 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690089
VERSION     WP_457690089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45329
     Region          150..406
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvtavrsawr evppyqvrqf aalaleevpt laqdilreic reypqlplvp defgepralv
       61 girqslehfv ahltagpdrp hvhprvfqef grgegiqgrs ldvlqaiyrl gvrlawrrla
      121 eigqqvaipa pamyelaesg yeyldglvae svrgyaeaaa rqagerlrlq rrlmeqlftd
      181 pgrrrrgaga adgvppalae raarigwplp ervavavllr pareviapav apdvlldmes
      241 erprmvvpep dapgrrella raaagwsgai gpavplldaa kslrwagaav dltergllpa
      301 gellqcteht ealvllppee liedltrrrl apldscgpah grrlaetlla wletrggape
      361 vaarlgvhpq tvryrlrqir elwgteiddp drrfelelvl rarrlrgels
//
LOCUS       WP_457690097             241 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690097
VERSION     WP_457690097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26717
     Region          38..148
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mrdpslrrsy tlfraflrer tdpghcyrll ardaadqier yaplrgavva dvgggsgyft
       61 aefrrrgalg llfepdtael tahgpppega vvadgyllpl adgavdicfs snvlehvadp
      121 qtflsemirv trpggliyva ftnwfspwgg hetapwhylg aerararyrr rtgkaakhtl
      181 gvnlfavhig rtlrqvrard diglvtarsr yapflaeavp rlpgvrevat wnlllilrrl
      241 p
//
LOCUS       WP_457690095             391 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457690095
VERSION     WP_457690095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41593
     Region          35..353
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mpqhvrpspp laalapspsa sgpppgagpp pfprrivfla rrdlgnpaag gsellvdria
       61 eglaahghqv tllcggpqgg aptrgyrvvs aggdaghflr vprqlarrvg acdllvevcn
      121 gmpylaplwh rgptlclvnh vhtdlwrlrc pgpaarlgrr lehwalagah rrdlmvavsg
      181 stasalcglg vdpgrirlvy ngvaepgpla pkapeplfla mgrlveykri dlllrlwerv
      241 rpvtggrlvi vgdgperarl aaaagpgvtf tghvseerkh qllcsawlll hpslvegwgl
      301 vvmeaaarrt pavgfdipgl rdsvedgttg llargesafa ahwcslalsa rrrdalgraa
      361 erraarfrws htvqsfrava aeavldplsr r
//
LOCUS       WP_457690103             245 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690103
VERSION     WP_457690103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25977
     Region          41..147
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtrppaalrd fyenpavpva sgadrsrrqa rllahalgsv rrgapaatvl dvgcgdgsaa
       61 ataaqmlagh rlvgvdwsqd alrrartrip cavrgeltdg glpfasgsad avlfsevieh
      121 lvdpdaalde lrrvlrpggh lmlstpnlaa wynrglllag vqpvfsevsm rgihgrpgtq
      181 vvghlrlyta ralrgflaas gfevvriaga pyhdvprplr pfdraacrvp slasillaha
      241 rrgre
//
LOCUS       WP_457690113             198 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690113
VERSION     WP_457690113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21345
     Region          4..194
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 msdlllvrhg etewsrdgrh tswtdlplta tgeeqaralr pllsdrkigq vyaspmeral
       61 rtaelaglar pqidadlrew dyggyegiat aeihrsrpgw ylfsdgvaag teehpgespe
      121 qvgaradrvl arlapqlaad egdvalvaha hflrvlaarr lglppaaggl ftfetgavgv
      181 lgtehdrpav iawnarsl
//
LOCUS       WP_457690116             291 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457690116
VERSION     WP_457690116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32008
     Region          5..234
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mrhlrvgvai ltmgnrpael ralldsvakq dlqpahivvi gngsplpplp hgaigvelsd
       61 nlgvsggrnv aldelrklgd ldvvvdlddd gllispdvfs rlaelhagdp klgivsfria
      121 dergrtqrrh vprlragdpa rgglvttflg gghslsvpml eriggwpddf fyaheetdla
      181 wralddgwhi ryapelvlqh pytsptrhav yhrmvarnrv wlakrhlpav lvplylgvwa
      241 altavrspsp aglrawaagf aegvrtpcgr rrplrwrtvw rmtrlgrppv i
//
LOCUS       WP_457690128             421 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457690128
VERSION     WP_457690128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44765
     Region          22..419
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mvdahqtfvi vggglagaka aetlraegft grvilicder dhpyerppls kgyllgreer
       61 dsvfvhepaw yaraqielhl gqpavhldpg artvrlgdgt livydkllla tgaeprrldi
      121 pgtglagvhh lrrlahaerl rgvlaslgrd nghlviagag wiglevaaaa rsygaevtvv
      181 eaaptplhgi lgpelgglft dlhrehgvrf hfgarfteiv gqdgmvlavr tddgeehpah
      241 dvlaaigaap rtalaeqagl dlvdreaggg iavdaalrts dpyiyaagdv aaadhpllds
      301 rlrvehwana lnggpaaara mlgqdvsydr ipyffsdqyd vgmeysgyap pgsyeqvvcr
      361 gdvakrefia fwlgadsrll agmnvnvwdv aesiqqlirs gaslapeala dpevplasll
      421 p
//
LOCUS       WP_457690132             293 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces nigrescens].
ACCESSION   WP_457690132
VERSION     WP_457690132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=30020
     Region          46..272
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtapiphlps assaplgtgd laaeitaqls tqlcrvrlrg fhppetpapt lvavahgsrd
       61 pralptvral ldrvralrpg lavrlghiel nrplladtla elrgeavlvp llfghgyhvt
      121 hdlpaapaaa pqltgrvaap lgphpllaea lhgrlleagf pgapsqrtav vlaaagsrap
      181 rsardterta qllsnrlggt pvvpayasaa aptvadavrt ltarghdria vascftapgr
      241 fatqcaaaap gtaadplgdh palarlvlhr ydqallartg sdpesvraat vav
//
LOCUS       WP_457690136             146 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamylcyclotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690136
VERSION     WP_457690136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Oakley,A.J., Coggan,M. and Board,P.G.
  TITLE     Identification and characterization of gamma-glutamylamine
            cyclotransferase, an enzyme responsible for
            gamma-glutamyl-epsilon-lysine catabolism
  JOURNAL   J Biol Chem 285 (13), 9642-9648 (2010)
   PUBMED   20110353
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Oakley,A.J., Yamada,T., Liu,D., Coggan,M., Clark,A.G. and
            Board,P.G.
  TITLE     The identification and structural characterization of C7orf24 as
            gamma-glutamyl cyclotransferase. An essential enzyme in the
            gamma-glutamyl cycle
  JOURNAL   J Biol Chem 283 (32), 22031-22042 (2008)
   PUBMED   18515354
  REMARK    Erratum:[J Biol Chem. 2008 Nov 14;283(46):32152]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..146
                     /product="gamma-glutamylcyclotransferase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15538
     Region          10..138
                     /region_name="GGACT"
                     /note="Gamma-glutamyl cyclotransferase, AIG2-like;
                     pfam06094"
                     /db_xref="CDD:428763"
     Site            order(10,13,15..16,84..85,96)
                     /site_type="active"
                     /note="putative active site pocket [active]"
                     /db_xref="CDD:119400"
     Site            order(56..57,96..100,102,114)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119400"
     Site            85
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:119400"
ORIGIN      
        1 mtreperlpf fvygtlrpge anygrtlrgr taaeeparig gallydgpgy pyatagpada
       61 vvhgalirpr dpdydevctv ldrlegytpg dphnlyerva teavcpdgrt vrawvylaaa
      121 plaarlratg tpieggdwpa sraaag
//
LOCUS       WP_457690138             250 aa            linear   BCT 27-JAN-2026
DEFINITION  SanA/YdcF family protein [Streptomyces nigrescens].
ACCESSION   WP_457690138
VERSION     WP_457690138.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Chao,K.L., Lim,K., Lehmann,C., Doseeva,V., Howard,A.J.,
            Schwarz,F.P. and Herzberg,O.
  TITLE     The Escherichia coli YdcF binds S-adenosyl-L-methionine and adopts
            an alpha/beta-fold characteristic of nucleotide-utilizing enzymes
  JOURNAL   Proteins 72 (1), 506-509 (2008)
   PUBMED   18393394
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Rida,S., Caillet,J. and Alix,J.H.
  TITLE     Amplification of a novel gene, sanA, abolishes a
            vancomycin-sensitive defect in Escherichia coli
  JOURNAL   J Bacteriol 178 (1), 94-102 (1996)
   PUBMED   8550448
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="SanA/YdcF family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26601
     Region          43..242
                     /region_name="SanA"
                     /note="Uncharacterized periplasmic protein SanA, affects
                     membrane permeability for vancomycin [Cell
                     wall/membrane/envelope biogenesis]; COG2949"
                     /db_xref="CDD:442192"
ORIGIN      
        1 mrgpvpglvr rirsgvrrvg rvrtvppgha lrlprtrrgr rrafqavvav tvlalapatw
       61 mnatagprvh gvadapaapv aivfgaglwn gapspylahr ldaaaalyer gtvravlvtg
      121 dnsrhdydep damrsyllrh gvpghkivsd yagfdtwdsc srahrifgvn ravlvsqgfh
      181 irralalcta agvdsdgvav gakrdvtway ggvreifaag kaaadallrp dpqflgprek
      241 gvtealadsr
//
LOCUS       WP_457690140             347 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457690140
VERSION     WP_457690140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="trypsin-like serine 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=35911
     Region          139..308
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 merdttkhra ttrvdrarpt rkrwikaata vagvtvclat atvghavnda rsaapstgkp
       61 spapddpwts rdaaaywtad rmagaapags dtparpaapt pstattrsav pkgtaaaara
      121 grtarhfngv psvgvlfsvd gdakahhcta svvhsphgnl iltaghcnpg traafvpqyr
      181 sgaatqpygv waiertfayp grgttgagad ldfafatvap gedgdtiedv tggntlsptp
      241 gytndvtvig ypnvqndped ravrcatrts rltgtrelrm ecggfyggts gspwlsdfde
      301 esrtgrvigv igglngggpk gpdadrisys pyfgskilnl yaraaqk
//
LOCUS       WP_457690142             121 aa            linear   BCT 27-JAN-2026
DEFINITION  divalent-cation tolerance protein CutA [Streptomyces nigrescens].
ACCESSION   WP_457690142
VERSION     WP_457690142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003543
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..121
                     /gene="cutA"
     Protein         1..121
                     /product="divalent-cation tolerance protein CutA"
                     /GO_process="GO:0010038 - response to metal ion [Evidence
                     IEA]"
                     /calculated_mol_wt=13060
     Region          18..121
                     /region_name="CutA1"
                     /note="Divalent cation tolerance protein CutA [Inorganic
                     ion transport and metabolism]; COG1324"
                     /db_xref="CDD:440935"
ORIGIN      
        1 madptalndp pdptgrqagf ltvmttidse tkarklarga iegrlaacaq isapvtsvfr
       61 wedaveasqe wqvlfktaqa ryealeayll eahdydtpei iatpitrggt gylswvaeet
      121 s
//
LOCUS       WP_457690145             276 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690145
VERSION     WP_457690145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30630
     Region          31..242
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtsprtnprp kvhlteeket llatlygrav dsraeqpilg dtlaadtvqr ldydfskmrl
       61 spgnaagval rarqldvwta rflarheeat vvhlgcglds rvhrldpgpg vrwfdidype
      121 vialrrqlyp eragyttips svtdpawvtq ippdrptmiv aegllmylte adgtallrrl
      181 mdrvpsgela fdafsrfair vqwlnrvvvk agarlhwgtd tagiaalspe leivenisam
      241 eipgieklsa gnrlaarmsa klpavrdmar myrcrf
//
LOCUS       WP_457690147             262 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfite exporter TauE/SafE family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690147
VERSION     WP_457690147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26332
     Region          46..260
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mppdislftl tllclaalaa gwidavvggg gllllpallv glphtpvayv lgtnkstaiv
       61 gttaaavtyv rkapidvrta lriglaavag slagaffaag insavlrpli mavllavlvf
      121 illrpafgta papsgpvsrk rivaailiag lgigfydgli gpgtgaflvi alaavlhmdl
      181 vtasatskvv nvctnigalt mfaiqgtvlw qlgallalfn faggmvgarm alkrgagfvr
      241 gvlvvvvval lcklgydqwl aa
//
LOCUS       WP_457690153             243 aa            linear   BCT 27-JAN-2026
DEFINITION  bleomycin resistance protein [Streptomyces nigrescens].
ACCESSION   WP_457690153
VERSION     WP_457690153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=26017
     Region          6..125
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,38,45..47,49,64..69,74..75,78,123)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(29..30,38,49,51..52,66,105,112,114,118..120,122)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 maektipmlp cptiqpvldf ytalgfevtf qqkspnpfav vqrggvelqf fgvkqyepad
       61 slstcyvvtd dvdglhaafr aglkaaygki ptrglprigt lkdtsygmrq flmtdpggnc
      121 lrigqrtsad lhhrpapket faralhhasl qadskedlaa avkiidrals lderptpvql
      181 lgllvlradv agrlgddata atalaeatai pltaeeresa hdsltrleel rdsdappape
      241 ags
//
LOCUS       WP_457690169             686 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457690169
VERSION     WP_457690169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..686
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70541
     Region          93..522
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 makvsqpedr peerpdtarp aavtttrpgg sgsgsgsgsg sgsgsgvgsg tdsgtgigtg
       61 tgsgtghtta ngprgaavae pdarhrltal qglaalslda masvaygpes ivlvlaaagg
      121 hglgftlpvt laiaallavl vasyrqviaa fphgggsyav arahlgrrta lfaaasllld
      181 yvlnvavsvt agvaaltsaf palyddrvgi clavlalita lnlrgivdsa kaflvptavf
      241 vgavltmvav glfraapatt atadghasvl adnattvgal lllkafasgc saltgveava
      301 navpsfrapa arraqrteva lgvllgvmli glsvligrfh lqpvegvtvl aqladasfgh
      361 nvafyvvqfa tmvllalaan tsfgglpvlm gllardnylp hvfglkadrq vhrhgvlala
      421 avaaallffs ggdmntlvpl falgvfvgft vcqigmvrhw rrersprwrg kallnsvgal
      481 ltgvsavvvt atkftegawl ivvtlpllvl afeavhraya rigarlglgr lpepprrars
      541 lvvvpvshls rltgealnaa vslgdevvav tvthgapedr patealrrdw elwnpgvell
      601 elpsatrslg rpiaayvtgl atrhpgtrit vlipeaepah lwqrllqnqr gavvahavrr
      661 dtnavicrlr frlaapgshv vtarcr
//
LOCUS       WP_457690188             423 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690188
VERSION     WP_457690188.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45412
     Region          24..321
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 maelerrrll aagggvalaa glatacgsnt grggggsgpe isqwyhqyge pgteravkry
       61 aaayrkanvs vqwrpgdydr qtaaalltds gpdvfeingp lldqiqggqv adltevvepv
      121 kddfhqavla pkiwqdkiwg ipqvvdaqml yyrksllkea gvrppqtlde lvdgakklsd
      181 rktkglflgn dggvgmlggt plfaaglsli nedgkvgfdd paaaralgki rqlyadksll
      241 lgaptdwsdp aafiqgltam qwsglwalpq ikkalgddfg vlpfpkdgsg gkpsvpvgay
      301 gsavsarsrr kaaatafakw lwvdrtdfqq dfalsygfhi parislakka eqlregpaad
      361 avrfatdhgy aepllwttad rtayqdalsr iikdganpes elktvvrkvn aelqrvkkkv
      421 kkk
//
LOCUS       WP_457690193             315 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA dioxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690193
VERSION     WP_457690193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="TauD/TfdA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35682
     Region          45..314
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mttladsaaa rtpalrphri padglyegpr ilrrtpdgad drpyerfeav pqaatigaei
       61 rgldlsrpls gelhaelnra llewkvlffr gqrlssreqr efarnwgele tnpllargds
      121 kdvvrfdkaa gpvttfenvw htdvtfrerp amgavlqlre vppaggdtmw admaaaydnl
      181 ppeiraring aravhdylpg farfyspaql apfqeefppv ehpvvrrhpe tgrrmlfvna
      241 sftthivgla qeesdrllrl lfqqaqvpef qvrwrwqagd lafwdnratq hyavndygth
      301 rrvaervaia gdrpy
//
LOCUS       WP_457690190             278 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690190
VERSION     WP_457690190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 278)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30487
     Region          34..276
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mddaltrvgr alrvvllval allflvpffl lvrnglateq ditapdwtff prvlqwsnlt
       61 kvfqdpnlpl grallnstli avsttagtvl laslagygla ripyrhanvv fyailgtlmv
      121 paavtfvpsf vlvsslgwis tlrglviptl fsafacfifr qyflgfprel edaarvdglg
      181 ywrtywrivv pnarpvfaav gtivfigawn aflwplvigq dqeawtvqva lstfttaqnl
      241 nlhelfvaaa vsiaplvvvf lllqryivag versgidd
//
LOCUS       WP_457690194             281 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457690194
VERSION     WP_457690194.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 281)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30472
     Region          <204..260
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mngearllap lvptrgyfpd fltpaegllg mtdalaalre tpaarlgael arlstaarpf
       61 pswiramadg dtralgrlag ilqryyeaav apywprvqgr ieadraargr alldggadrl
      121 laslppmmrw rppvleadyp vdrdlhlngr gllllpsyfc rrtpvtfhnp eltpvlvypv
      181 ehpaprltpq vpperslgrl vgqtrsailq rigvgcttse larradvsla sasqhatvlr
      241 dagllitlrq gnavlhtltp lgaallrgar paeeaayerl r
//
LOCUS       WP_457690199             504 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690199
VERSION     WP_457690199.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..504
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51016
     Region          47..501
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,310,313..314,317..319,322,350,354,406..407,
                     411,416,432,435..436,439..440,443)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mseltqdrip epgrisavas adgvtrnapt aapkgkrpqh tgillvvlga vfmalldatv
       61 vnvatptirt dlettgsalq livsgytisy aallitgarl garhgfrtvf ltglatftla
      121 sfgcglapta gvliaarvvq gigaglmvpq iysliqltfe gpararalsl yatviavavv
      181 vgqaaggllv sadlfgtgwr pvflinvpvg lallvaavrl lpvgtprsak gldlpglvtl
      241 taallllvvp lvlgheqhwp lwttlclaaa apvfgvfvlv ergvarrgga plvpgrvlrs
      301 pdlvcgaaal ffgmagyagf lfsfsqhlqs glgesatrag lafaplalgv atgsltwqkl
      361 parwhlpvit aacalaaagy laigctmrag gqgglvlpal qllwglglgy ttsplltlal
      421 sridpadasd asgvlttvpq laqvvgvaay gsiflaladr pgaagasdas avasaqalya
      481 talpvaagtl lgalailpll rkrr
//
LOCUS       WP_457690201             303 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690201
VERSION     WP_457690201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32964
     Region          18..97
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(43,68)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(50..51,62,65,69..70)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          116..281
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 msststrsaa aaasrrgela aflrlrreri tpadvglpgg prrrtpglrr eevaqragvg
       61 vawytwleqg rainpsvqvl daiaralllg paerehlhrl agvpgaaact parqplpaea
      121 qtildalnpl paglvsagyd vlafndayaa ldprmvllpp adrnvlwrlf tadeesqplv
      181 dwerevsfmv gqlraefgrr lhdphwrayi rklseasplf vemwarhdvt apvthrkrfr
      241 tadgrevtit atgftttavp dakmwiytpa deeavrvlge llgryretga aglvatgagg
      301 pes
//
LOCUS       WP_457690203             190 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457690203
VERSION     WP_457690203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21081
     Region          34..160
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msghrsigdt ekavqaklgd tpvrhermaa vanlyraaaa vrqhfensvl rgveltwtsf
       61 vvlwvvwigg eretrqvaee agiskgtltg vartlqsrgl lerkdhptdg rlallaltpe
      121 gerliarvfp efnaeeafvt eglsddeald ladllrrive qietrgedrr lelldghepr
      181 prrsgrraka
//
LOCUS       WP_457690206             484 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690206
VERSION     WP_457690206.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50360
     Region          17..453
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpelsrrrrl lvlaiccmsl livsldatil nvalpsiqrd lhasvagmqw tidaytlvla
       61 allmlagsta drlgrrrifl vglvvfavgs llcslapgle wlvvfrmvqa vggsmlnpva
      121 msiitntfte preraraiga wggvvgisma agpviggllv qsvgwrsifw invpigalal
      181 fltlryvpes rapkprrvdp vgqllvigll gsltyaiiea pdagwtspei lafvlvalas
      241 lagligyerp rseplidlrf fhsapfsgat vvavcafaal agflfintly lqnirglsal
      301 daglymlpma gmtlifapvs grlvgsrgpr lslllagtam gasgllfaaf daqstnpllf
      361 tgyvlfgigf glvnapitnt avsgmpraqa gvaaavasts rqvgqslgva vigavlasga
      421 haaatadafl aagrpawwii agcgaavlll galttgrwar atadrtaalf edeargyrpa
      481 darp
//
LOCUS       WP_457690208             307 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690208
VERSION     WP_457690208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33964
     Region          35..114
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          132..296
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtpdpsllpq patgpggaap pygtaprdda arraelaafl rsrreritpe qvglprgarr
       61 rtpglrreev ahlgavgvtw ytwleqardi hvspqvldav arallldrae rshlfalaga
      121 vdpmpgrect gvtrelrqil qqltpfpavl qnsrfdilay nrtygrlmcd ldalpeedrn
      181 cmwlafthpe wrasvgdlea tmrvmaakfr asmaehlaep awkalvarlt easpefreiw
      241 aqhevirpvs svklfrhprv gvleltatsl wtgpnpgpkl lsytpvdets rerleqlaae
      301 paalaav
//
LOCUS       WP_457690210             511 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690210
VERSION     WP_457690210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..511
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51978
     Region          63..476
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(70..71,74..75,78,110,160..161,163..165,168,188,
                     191..192,195,326,329..330,333..335,338,366,370,425..426,
                     430,434,450,453..454,457..458,461)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdiraqttt peapagplga patapeaafp dapatpeapa apgpapqqqr tatvltplgl
       61 ltvllgaalp midffivnva lptidhdlha gpamlemvva gygvayamll vlggrlgdmv
      121 grrrlflwgl aafgltslac glapdawtlv aarvaqgaaa alllpqvlat iqatttgkrr
      181 akavslyggt ggvssalgqv lggllvavdl agtgwravfl vnvpiaaaaw llaartvpet
      241 rsphparvdg pgtallaatl ltlllplteg raagwplwsw vllavfpfaa tafvlcerra
      301 erlgrtplvp psllripsvn sgllmlvpft lgfggfmfvv avalqsglhf gpfaagmsla
      361 pmcaafflts lagprlvlrf grrvviagsl iqgtglalla ltvhagwpgi svaglapsma
      421 vlgigqgmvm pvlmrivlse lpvtqagvgg gvlvttqqsg lalgvatlgt lflsllptvg
      481 irdallaall tqlaivagtt llalrlprtv r
//
LOCUS       WP_457690198             579 aa            linear   BCT 27-JAN-2026
DEFINITION  PQQ-binding-like beta-propeller repeat protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457690198
VERSION     WP_457690198.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Matsushita,K., Toyama,H., Yamada,M. and Adachi,O.
  TITLE     Quinoproteins: structure, function, and biotechnological
            applications
  JOURNAL   Appl Microbiol Biotechnol 58 (1), 13-22 (2002)
   PUBMED   11831471
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Duine,J.A.
  TITLE     The PQQ story
  JOURNAL   J Biosci Bioeng 88 (3), 231-236 (1999)
   PUBMED   16232604
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Duine,J.A. and Jongejan,J.A.
  TITLE     Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor
  JOURNAL   Annu Rev Biochem 58, 403-426 (1989)
   PUBMED   2549854
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1004790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..579
                     /product="PQQ-binding-like beta-propeller repeat protein"
                     /GO_function="GO:0070968 - pyrroloquinoline quinone
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60116
     Region          179..417
                     /region_name="PQQ_2"
                     /note="PQQ-like domain; pfam13360"
                     /db_xref="CDD:433144"
ORIGIN      
        1 msqppgqppq gafgapqdpp ppgggfgppq qppaqgafga pqgmpplppq pphqpqpgyg
       61 ypqqpapgpy gtpgpygpqp gygypqqqpq ypggpgmppp pdgggrgpfk gkpalvvaaa
      121 vagllvvggt vyavtsggdg ggkpvarqsd dprasgtpvd pgdgsgdgga dpenlnagrr
      181 sgeakvlwyk sapdapasga dapgmwitak tavkaaykqv fayqvgngdp awapitfpqk
      241 icavtsqksa ddkvvvaymn gtsdrakcnq lqeidldtgr rgwtatvadg glfdsalsie
      301 ltisgktlmv grsqsgtayd lgsghklydk keygascfpt afaggtdrlv qvascaagaa
      361 aehdeisqld patgriewtr pvkkgwqver tysvdplvvy mtneekkawn isvldgkgaf
      421 rsevkvnekf apecgwalla rdlqgcqgva vdantlylpt dvsgganeiv aisltdgtak
      481 wrvksptdes mypveveggr lvayvrpsyd aggqvvsvpt tgashrttrl lqnprhtagi
      541 eggfydgavd wadgrfylss trltgsddak eklmmafgn
//
LOCUS       WP_457690218             154 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457690218
VERSION     WP_457690218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..154
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17016
     Region          10..153
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtstplhwkl vvdahdphaq adfwaaalgy evedhstlig klldlgaips eilldhhdrr
       61 awrdaaavrh pddpydaesg aglgrrllfn rvppsetkta knrlhidlhg pagerdseve
      121 rlralgagvq rqvreqggew vimtdpegne fcvh
//
LOCUS       WP_457690216             167 aa            linear   BCT 27-JAN-2026
DEFINITION  anthrone oxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690216
VERSION     WP_457690216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Lin,Z., Zachariah,M.M., Marett,L., Hughen,R.W., Teichert,R.W.,
            Concepcion,G.P., Haygood,M.G., Olivera,B.M., Light,A.R. and
            Schmidt,E.W.
  TITLE     Griseorhodins D-F, neuroactive intermediates and end products of
            post-PKS tailoring modification in Griseorhodin biosynthesis
  JOURNAL   J Nat Prod 77 (5), 1224-1230 (2014)
   PUBMED   24786728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="anthrone oxygenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17629
     Region          3..160
                     /region_name="COG5500"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444251"
ORIGIN      
        1 mralqtatll aatlgaglma glfaafayav mpglarsadr tfvqamqnin raiingwfll
       61 pfllpiplli latvlawngh grvalpwila alvlymagff vtsgvnvpln naldkadtgd
      121 ddrakaaraa fegrwvtwnl vrallhtaaf gvlawalflh gtaagta
//
LOCUS       WP_457690220             408 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690220
VERSION     WP_457690220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 408)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /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=43872
     Region          162..407
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtvpprlrra lvrmrrdlaf laagvplhlf pvllswwais lladtvngvs seapveliap
       61 ltllviagyg fteaqrwrfr aicgvelprl rftegkrqlg ynwligpllg vlellllall
      121 ltalvaalvl vwvwlvppqw rrghpgyttt gtyltvlglv alaavpglaa glvrleilvg
      181 ravlgvsrsd elarrvedlt vsragavdaa daerrrierd lhdgaqqrlv slalnlglak
      241 atltdlprev qevidaahre akdaieelnh lvrglhpavl delgldaals glvaraplpv
      301 rlrvdlpael pqrtapavea vayfvvseal tniakharea traevtvtrl geilrvviad
      361 dgmggadpsk gsglkglaqr vrsvdgtfrm sspvggptmm svelpcpm
//
LOCUS       WP_457690226             259 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690226
VERSION     WP_457690226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26884
     Region          5..236
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mnqpptqpvi dlcgaaaslg arpvlrgvdl tvrsgevval lgangsgkst avrsvigqvp
       61 ltggelalfg tefrrfkdwa rigyvpqrtt aaggvpatvr evvtagrlar tklgilrkad
      121 raavhralel vgmadrakds vdalsggqhq rvliaralag epellimdep magvdlasqe
      181 vlaaalreqv grgttvllvl helgplepli dravvlrdgc vvhdgpppea vgqhalpghd
      241 hvhphadaaa epirtglls
//
LOCUS       WP_457690228             299 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690228
VERSION     WP_457690228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30871
     Region          6..258
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 meilnyafmq raliaalivg vtapaigiyl vqrrqalmgd gighvaltgv glgfllntsp
       61 iwvatavaia gsvvmelirw ygktrgdlal amlfyggmag gvmlmnlsda gsnanlgtyl
      121 fgsittvspq dmttiyvlaa lvlaitiglr rqlfavcqde efarvtglpv rllnllvavt
      181 aavtvtvamr vvglllvsal mvipvaaaqq isrsfavtfs vavaigvavt ltgtttsyyv
      241 dvpsgativl faiglfvlft glaaplakkr araaaeaskg ctlevpgdrt vaddvsvtg
//
LOCUS       WP_457690225             320 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690225
VERSION     WP_457690225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Hantke,K.
  TITLE     Bacterial zinc transporters and regulators
  JOURNAL   Biometals 14 (3-4), 239-249 (2001)
   PUBMED   11831459
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Claverys,J.P.
  TITLE     A new family of high-affinity ABC manganese and zinc permeases
  JOURNAL   Res Microbiol 152 (3-4), 231-243 (2001)
   PUBMED   11421271
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435238
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="metal ABC transporter substrate-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34053
     Region          11..309
                     /region_name="ZnuA"
                     /note="ABC-type Zn uptake system ZnuABC, Zn-binding
                     component ZnuA [Inorganic ion transport and metabolism];
                     COG0803"
                     /db_xref="CDD:440566"
ORIGIN      
        1 mnirrpista tlagvsalgl lalsacspsg gartedgklk vtasfypmef larqiggkhv
       61 evtdltkpgv ephdlelspq qtaqlgesga ilylkglqpa vdeaveqsgv knvadaaslt
      121 sleehgtevd gdhhttgdhh shseseggkd phvwldpvky aevakgvnkt lakadpdhka
      181 dyqkntdalv kklegldkdf kdglkkrasd tfltthaafg ylaeryglte eaisgldpes
      241 epsakrirdl htlakdhhvs tvffetianp atakalagdl hlktdvldpl eginaksrgk
      301 dyfgvqqanl aalqkalgsk
//
LOCUS       WP_457690236             277 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690236
VERSION     WP_457690236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30781
     Region          14..67
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(18,22,47)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(21,46)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(28..29,40,43,47..48)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manasrqaaw efwgtelkrr redagltqea lgrlvfvsgg yigqfeqair kpqldvagri
       61 devlqtdgff ermwrklidd qryadyfaaa aeleplatki cefepmivpg llqtpsyaqs
      121 lllagnplat deyiddkvrg rldravilkd ssrpvywavl heaalrvpvg sqgvmaeqle
      181 hiarlarerk illqvlpfaa gahpmigksl rlmefedapp tayteglysg nllddpavvk
      241 rvqqdydllr aaalspeasr aliesaaedy rrcasst
//
LOCUS       WP_457690245             411 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457690245
VERSION     WP_457690245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 411)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44731
     Region          19..408
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,90..91,98,102,109,240..241,244,248..249,252,
                     285,290..291,294..295,297,321,349..351,354..355,357..359,
                     363)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,84,86,89,91..92,178..179,188,239..240,243..244,
                     248,291,294..296,398)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 maqqgqqpfv idpvgsdihg eaarlralgp vartelpggi eawsvtshtl lkqlltddrv
       61 sknprdhwpa wqreeirssw lqswigvtnm ftaygadhrr lrkliapaft arrtdamlpr
      121 vesitmalld elaahpagep ldlrerfnhp lpmqvicelf gfpegeqrae larlveaimd
      181 ttatpeqaga taagvhalls elvgskrenp addltsllvs arddegqkmt eqelldtlll
      241 vigaghettv dllgnavhal lthpeqlklv lsgqvpwtdv ieetlrwaps iaalplrfav
      301 edidipdgpt irkgeailpa yaaagrdaaf hgdtaadfdi rrtrqehlaf ghgvhhclga
      361 plarmearia lpalfarfpd lqlatpadel eptsgfisgg lrtlpvrltp a
//
LOCUS       WP_457690249             342 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690249
VERSION     WP_457690249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=35995
     Region          44..338
                     /region_name="SEST_like"
                     /note="A family of secreted SGNH-hydrolases similar to
                     Streptomyces scabies esterase (SEST), a causal agent of
                     the potato scab disease, which hydrolyzes a specific ester
                     bond in suberin, a plant lipid. The tertiary fold of this
                     enzyme is substantially different...; cd01823"
                     /db_xref="CDD:238861"
     Site            order(50,92,144,300,322)
                     /site_type="active"
                     /db_xref="CDD:238861"
     Site            order(50,300,322)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238861"
     Site            order(50,92,144)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238861"
ORIGIN      
        1 msrygmpais rlavaavasl avvasafapa asgaparaad rpeyvalgds ysagvfvrpw
       61 eehdgcgrsg rnyphqvagq lgfeltdvtc gaaevvdgvl apqpaskiyg pptipppggw
      121 sdlppqveal spgtdyvtvg iggnslgfga ivkkclelga tkplqlrpct nhysnggage
      181 dwleerftql dtdlarmmtv ihrrapharv avvgypaivp dnsgcsfwhw nqlgsvkkgd
      241 mpwldglelr lnallekhaa yhaasyvdty gpsaahgvce sgdakwmygi kdsltgdggq
      301 tdppneqcrs lpgageactf vhpnargldn qtrqvsralm ts
//
LOCUS       WP_457690247             333 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690247
VERSION     WP_457690247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36056
     Region          3..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mklnlhrlwv feqvvkcggf saaarklyms qpsvsqhvhk levslrttli drtgarprlt
       61 degevllqya qrisslaqev aaaidrvsdv psgrllvgst stygnhlllp llarfaerfp
      121 evechvkvgn tsdvigllad gevrlavlpg daagasrhyr rerilderil lvahpehpla
      181 gravtpsdle qqhflfreeg satrraqdda larwklspar cpqisgnetl khavlaglgi
      241 avlpqrcvar elregrlgpl rpdpelpaca ivlatsrets lstterefid llrtvqdawa
      301 vgedspvpdr gsgapgplvv paghaedpaa rag
//
LOCUS       WP_457690256             416 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690256
VERSION     WP_457690256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42728
     Region          61..409
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 msrpaapeal tepteragrr wtaalslang aiwvgwygpl qillalqaae lappgtakes
       61 vlawvtgaga avsmvanplf galsdrtasr fgrrapwila gvlggagalv llagagtvpa
      121 malgwclvql tlnaafaait aavpdrvphr qrgavggwlg aaqilgvvag tglatvaggv
      181 vagylacagf vvlgalpyvl lhrdpvlpaa rrpaltwrav lagfwisprr hpdlgwawlt
      241 rflinlgnal allyllyylr dvlhhpdpeg gvlvltavna vtllgtvvvg glwsdrvgrr
      301 qpfvlgagvl mtvatgllag wqtwpgalca aallgvgfgi ftsvdfalmt evlpaaahrg
      361 kdmglinian alpqvaapal aapivqhlgg yrvlygvaaa igllgallvr rirgva
//
LOCUS       WP_457690262             296 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690262
VERSION     WP_457690262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32595
     Region          40..95
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(41,66)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(48..49,60,63,67..68)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..278
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 masyaatrdt arrrqdlrdf lrsrrarvtp aeaglpdggr rrtpglrree vavlagvgas
       61 wyqwleqgrd itvspqvlds varvlrlsga errhlyalag lnpplrqdae elgrtdvcag
      121 lqrlidawmp ypahimdpyw ntvahndaah lvlghgrpgv spncliafft dpfyraraas
      181 weanapliva qyraawsarp gdegfdevvr easalseefa glwgrgdvqd ggqlhkemdh
      241 plvgallfet tqlrvpvrpd lnivlhnprp etdtaaklew ltspegrrgg mssvag
//
LOCUS       WP_457690267             381 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690267
VERSION     WP_457690267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39777
     Region          35..330
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mssrredppp agpaavpaal dplagvradg dprtdvyltg tvfldiiftg ldsapvrgte
       61 swargmgssp ggvanmatal arlglrtsla aafgddhyge ycwealeqge gidlalsrtv
      121 pgwhspvtvs mayegertmv shgheapppd fafdgkhapg cppptracia slvpgrregw
      181 lgcaagrgsr ifadvgwdds grwdpadlad lehceaflpn aeeamrytrt dcpraaarkl
      241 adlvplavvt lgsegayavd grtgesaevp aiavealdpt gagdvfvagf vtgtladwpl
      301 gdrlafaglc aalsvqefgg slsapgwaei aawwqqvrac eagapgvlrr qyafldevlp
      361 aayrpaplar avptigfrrp a
//
LOCUS       WP_457690269             446 aa            linear   BCT 27-JAN-2026
DEFINITION  6-phospho-beta-glucosidase [Streptomyces nigrescens].
ACCESSION   WP_457690269
VERSION     WP_457690269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Varrot,A., Yip,V.L., Li,Y., Rajan,S.S., Yang,X., Anderson,W.F.,
            Thompson,J., Withers,S.G. and Davies,G.J.
  TITLE     NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases:
            structural insight into specificity for phospho-beta-D-glucosides
  JOURNAL   J Mol Biol 346 (2), 423-435 (2005)
   PUBMED   15670594
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..446
                     /product="6-phospho-beta-glucosidase"
                     /EC_number="3.2.1.86"
                     /GO_function="GO:0008706 - 6-phospho-beta-glucosidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47564
     Region          1..440
                     /region_name="GH4_P_beta_glucosidase"
                     /note="Glycoside Hydrolases Family 4;
                     Phospho-beta-glucosidase; cd05296"
                     /db_xref="CDD:133432"
     Site            order(9..10,12,35..36,40,80..82,105,125,141,143,278,305,
                     332)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(89,105,143,165,200,249,270,305,328,332)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(164,200)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(189,192,208,211,346,358,377..378,380,382..385)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(235,237,240..242,254,256..257,390..391,398,402,409,
                     417,420..421,431..432,434,436)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mrltilgggg frvplvyral lddpgravse vvlhdtdprr vaviaevlar laqghpapvp
       61 vrvadgldda ltgagfvfsa irvggtagri rderiplseg vlgqetvgag gvlyglrtip
      121 valhiaeraa alapeawvin ftnpagmvte amsqvlgdrv vgicdspvgl vrraaraaga
      181 dpaaladpdr sgydyvglnh lgwlrsltld gtellpglla ddaalgsfee grlfggdwlr
      241 tlgalpneyl hyyyfrretl dsvretretr gefldqqqgg fferavaagg pdavyalwer
      301 trlereetym ahsreasggw qrdshdlegg gydrvalalm hailgnsgtr lilnvrngtt
      361 vpqlapdaiv etvcevsaqg arplpcaplr edqlglmlqv kaveratvea avfkdrgaal
      421 ralalhplvd spavaarile raakea
//
LOCUS       WP_457690271             209 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690271
VERSION     WP_457690271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21782
     Region          19..188
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(64,66,68..69,128..129,147,188)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 maaridhlvt sgtfsldggt wdvdnnvwiv gdddeaivid aahdadaiva alggrtlrai
       61 icthghddhi daapalasrt garihlhpad lplwkmthpg tppdaeladg qvltiagtdl
      121 tvlhtpghap gavclhapel gtvfsgdtlf qggpgatgrs fsdfptivas irdrlltlpp
      181 etevrtghgd pttigaeaph leewikrgh
//
LOCUS       WP_457690290             464 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces nigrescens].
ACCESSION   WP_457690290
VERSION     WP_457690290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..464
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45816
     Region          38..442
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(67..68,71,123,137,139,169,202,403,406,442)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(374,379,394,403..405,408,430,434)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtgqpaatgs edqrgaaaar pgaapgrtll pgqpgrpdvf tfgetmvalr gsgplklggt
       61 mnvsiagaes nvaiglarlg hdvrwagavg edeagqlvlr tlraegvgvs gasadsgapt
      121 glllfeprlp evtrvhyyra gsagsrigae viqrafsaap prvlhltgit palsptaraa
      181 arralqlare fgslvcldvn frarlwtaea aaevlrewip fvdvliasdd elplclpggg
      241 ggegspggae gigggmgaer adgglraegi gagmgaerad gglrtegiga gmgaeradgg
      301 lrtegigagm gaegadggla rggseqgeda avdaracgda vplppqevtg gpaatvarqa
      361 gllldqgvge vvvklgaega tafthggslh epakpvravd avgagdafva gylsalldge
      421 gpagrlerav ttgafavasp gdwegapnrs elgmlgappg tvvr
//
LOCUS       WP_457690294             425 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457690294
VERSION     WP_457690294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..425
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45742
     Region          3..421
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdevllrslt psvlailvrr gadfaaaeda vqdalveavr vwpaepprdp kgwlvtvawr
       61 kfldatraes arrrredlvy eepapgptpa vddtlqlyfl cahpsltpss avaltlravg
      121 glttrqiaqa ylvpeatmaq risrakrtvs gvgvspapga pagrkpgekp gargrferpg
      181 dvatvlrvly lvfnegysgd vdlaaeairl trqlaatidh pevagllalm llhharraar
      241 tapdgslvpl aeqdrgrwdt eaiaegveil qaalardrlg efqaqaaiaa lhadaptaee
      301 tdweqivewy delarltdsp vvrlnravav geadgpragl aalaalddss pssrllpqps
      361 agrrpqsrgy piprhtavaa ylherdgdla taarlyaeaa rkapnlaerd hltrqaarln
      421 arrsr
//
LOCUS       WP_457690258             332 aa            linear   BCT 27-JAN-2026
DEFINITION  GTPase Era [Streptomyces nigrescens].
ACCESSION   WP_457690258
VERSION     WP_457690258.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Tu,C., Zhou,X., Tropea,J.E., Austin,B.P., Waugh,D.S., Court,D.L.
            and Ji,X.
  TITLE     Structure of ERA in complex with the 3' end of 16S rRNA:
            implications for ribosome biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 106 (35), 14843-14848 (2009)
   PUBMED   19706445
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Meier,T.I., Peery,R.B., McAllister,K.A. and Zhao,G.
  TITLE     Era GTPase of Escherichia coli: binding to 16S rRNA and modulation
            of GTPase activity by RNA and carbohydrates
  JOURNAL   Microbiology (Reading) 146 (Pt 5), 1071-1083 (2000)
   PUBMED   10832634
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="GTPase Era"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0019843 - rRNA binding [Evidence IEA]"
                     /GO_function="GO:0043024 - ribosomal small subunit binding
                     [Evidence IEA]"
                     /GO_process="GO:0000028 - ribosomal small subunit assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=35754
     Region          14..332
                     /region_name="Era"
                     /note="GTPase Era, involved in 16S rRNA processing
                     [Translation, ribosomal structure and biogenesis];
                     COG1159"
                     /db_xref="CDD:440773"
ORIGIN      
        1 mgamsvrtes saahragfac fvgrpnagks tltnalvgtk vaitsnrpqt trhtvrgivh
       61 rpeaqlvlvd tpglhkprtl lgerlndvvr ttwsevdvig fclpadqkig pgdryiagel
      121 adikktpkva ivtktdlvds kalaaqliai dqlgkelgie waeiipvsav esegagrsps
      181 dkggggrgag qvslladllv pmlpespply pegdltdepe qvmvaelire aalegvrdel
      241 phsiavvvee mlpredrpad kplldihanv yierpsqkgi iigpkgkrlk evgmksrkhi
      301 eallgtpvfl dlhvkvakdw qrdpkqlrkl gf
//
LOCUS       WP_457690298             322 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690298
VERSION     WP_457690298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35355
     Region          26..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrgpapaapp aperpslgar llgpqrrnlw fwafvgpfal glglftyvpl awsvylsffd
       61 ahntvspsgs dfvgpgnyta mltneaflgs lgtfalftvf ivpatyalsl alalmvnrlr
      121 faqaffrsvf flptacsyvv aaviwklsif ngvrfglant vlgwfgadqt awlsttdppw
      181 ywlvivtvrl wlqagfymil flaglqrisp qlyeaaavdg arpgwqtfrh itfpqlrats
      241 vavvlllvin afqafdefyn llsdargypp yarpplvyly ytalgrdqnl glgsagavil
      301 aliiavatvv qarwfglgrk ee
//
LOCUS       WP_457690296             101 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457690296
VERSION     WP_457690296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 101)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..101
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=10906
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maevfaalad ptrrrildal aahgeatatv laaelpvsrq aivkhlgvld raglvaghre
       61 grearyrvip erlgvtarwm drvaaawdtr lsaikrlaes e
//
LOCUS       WP_457690308             760 aa            linear   BCT 27-JAN-2026
DEFINITION  ArnT family glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690308
VERSION     WP_457690308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   2  (residues 1 to 760)
  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   3  (residues 1 to 760)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..760
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76278
     Region          39..>223
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
ORIGIN      
        1 mlylwslsas gyanqfysaa vqagseswka fffgssdaan sitvdkppaa lwpmalsvrl
       61 fglsswailv pealmgvatv gllhgavrrr fgagagllag aalavtpvaa lmfrfnnpda
      121 llcllmvgav acvlraleeg rtkwlvlagv cfglgfltkt lqawlilppl avvyaccapv
      181 avrrrfgqll laglalvvsg gwwvaivelw paasrpyigg sqhnsflelt fgyngfgris
      241 gnetgsvggg ggrpggsggg wgetgitrlf ssdmggqiaw llpaalillv agvavlwrar
      301 rtvaaeeagq raeflvwgga llmtfttfsf msgifhqyyn ialapyiaal vgmgaallwr
      361 rggrsaalvl agtvavtagw sfvllnrspd wlpwlrwtva algllaalgl llpvragaaa
      421 rkeaaaegap gpegapgpgr apgpdgargp dgaaapgrap gpdgaaapgr aaapgraaas
      481 gggalrasrr vvvlaaglgv vtalagpvay tlntvntakg gsiitagpsv rggmggpggg
      541 fpggrmpgrm pgrmggapga gqggaagqal ppgqgvrgga pggnqgngqa rvgkqgqlps
      601 pgtqgrpgar rgfpggkggf geggagrmrg mggllngskv sdrakallek daddytwaaa
      661 aigsqnaasy qlatgkpvma iggfngsdps ptlarfkeyv adgkihyfla ggqggqggqg
      721 gqggpgggrg gssqitswva ktfqkvtvgs ttfydltrka
//
LOCUS       WP_457690311             256 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690311
VERSION     WP_457690311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28263
     Region          38..82
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          99..250
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maatdgrtgk rpnsvwlter pplkrkadqp aglgldkiva atvrlldaeg lskfsmrrla
       61 aelgvtamsv ywyvdtkddl lelaldrvmg emrlpdeadt grdwrdhlrs laneyrillt
      121 ghawaarllg tyinigphsi afsnasmrvm kesglslqqi tgglsavfqf vygfatiegl
      181 fndrcaeagl pvdeyfqqvm tavesrpefa etlenttkvm earggttvre mrdrdfafal
      241 dlqiagieam rgrpgd
//
LOCUS       WP_457690317             157 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457690317
VERSION     WP_457690317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17270
     Region          4..138
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maaqsqyeel arqlsaigav kremgrtlpq dcppasagvl tlldrhgemr msqlaellai
       61 dmsvtsrhva hvaergwier kpdpadkrsr llrltpsgta llaelaeryt atlarylddw
      121 tdadvghlie llarlrtsfg dcrtrahhds ttrtpag
//
LOCUS       WP_457690310             519 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690310
VERSION     WP_457690310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52436
     Region          28..492
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,284,287..288,291..293,296,324,330,381..382,
                     386,390,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mspvasdatt tlqppgrtaa rwlilavicl aqltvildnt vlnvaipslt edlgattadv
       61 qwminayslv qsgllltagn sadrygrkkm lavglvlfgv aslgaalaqs pgqliaarag
      121 mgvggallvt ttlavvmqif ddderpkaig iwssvnslgf aagpliggvl ldhfwwgslf
      181 lvnlpvavva lsavltlvpe sksragerpd llgallsmig mvgvvfaiis gpvtgwlsgr
      241 vlvsaaiglv glavfalwel rvpypmldmh ffrnrrfiga vsggilvafg mggsmflltq
      301 hlqlvlgygp ldaglrmapl avtvillnft glsarllprl gtpgmivsgm sllaaglaai
      361 sllggdsygg mltglivmgv gvalamptma naimsaippa kagvgagvng tlmefgqglg
      421 vavlgavlns rfvallplva agagslpaal artrtdaert avhdafaagi gtsqlvgaaa
      481 vflgglvaai llrraertgq dtaapatpsg aepaaasae
//
LOCUS       WP_457690315             862 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690315
VERSION     WP_457690315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..862
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88193
     Region          40..438
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(47..48,51..52,55,87,137..138,140..142,145,165,
                     168..169,172,300,303..304,307..309,312,340,344,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          556..>845
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 matttpagvr ggharhgggq hasdgapmth rqimealsgl llgmfvails stivsnalpe
       61 iihdldggqs aytwvvtasl lamtattplw gklsdlfskk llvqislviy vagsvvagls
      121 qntgmliacr vvqgigvggl salaqivmaa misprergry sgylgatfav atvggpllgg
      181 vitdtdwlgw rwcfyvgvpf avialivlqk tlklpvvkre gvkvdwagaf fisaavslll
      241 vwvtlagdky dwmswqtaam vggavvlgai fvfvetkake piiplrlfrn ktitlasvas
      301 lfvgiamfag tvffsqyfql argesptmsg vltipmiggl fvsstvsgqi itktgkwkaw
      361 lvaggvllta glgllgtiry dteywhiaiy malmglgigm mmqnlvlatq nqvapedlgs
      421 assvvtffrs lggavgvsal gavlahrvth yvkdgladlg pkaakaaahg agnsgggipd
      481 ldalpaplrt vmesayghgv advflyaapc allaflftlf ikevplktrg glaqssedap
      541 aaatpsaaas eavipaqaee repalvgaap vapddeahtp swarpavata tqplaayasa
      601 gggdsapags avhgfvrnae ghpvprsavt lislsgrqlg ravtqangsy alsapgagsy
      661 vliaaadghq pqastvvigd qphaydills gtsglggqvr saatgapvdg amvvvtdvrg
      721 evlatgktga eghfafdela pgtftvavna pdhrpaalpv eiggqgttri eiellsgarv
      781 qgivragahr rplpdarvtl vdaagnvvat sttgedgaya ftdldagdyt viasgyppva
      841 tglavdargv dgydvelahp gd
//
LOCUS       WP_457690327             183 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457690327
VERSION     WP_457690327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19713
     Region          32..163
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtappgprpd pvdalmdawh telpdvlrpt telskriaql araldqatrg vlpelgltva
       61 efdilvalrr agepyrmkpn elaralllss ggisnvvnhl tdcglvrrep spddgrstmi
      121 rltpdgvrta eravranada heavfaeasp tsvdaatral revdirhspa prpirtgrnp
      181 srs
//
LOCUS       WP_457690329             157 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457690329
VERSION     WP_457690329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17210
     Region          1..144
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mpkitpnlwf dtqgkeaaef ycsvfpnski kdvtyyneag prpagtvltv efeldgqeyl
       61 alnggpeftf seaislmitc adqdeidyyw aklseggeeg pcgwlkdkyg lswqvapggm
      121 temlndpdqe raaramkamf gmkkidiaal qaaadqa
//
LOCUS       WP_457690337             193 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Streptomyces nigrescens].
ACCESSION   WP_457690337
VERSION     WP_457690337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20010
     Region          25..193
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mtvppsaslp spgpdplrdp witpmrqalg eaarapgtgd vpvgavvlsa dgtvlgtghn
       61 ereatgdpta haevlalraa aetlreeasr wgspqtesgg dpgrggggrr agewrltgct
      121 lvvtlepctm cagaivlsri drvvygarda kagaagslwd virdrrlnhr pevitgvlea
      181 dcaalltaff rer
//
LOCUS       WP_457690344             510 aa            linear   BCT 27-JAN-2026
DEFINITION  apolipoprotein N-acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690344
VERSION     WP_457690344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Bork,P. and Koonin,E.V.
  TITLE     A new family of carbon-nitrogen hydrolases
  JOURNAL   Protein Sci 3 (8), 1344-1346 (1994)
   PUBMED   7987228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..510
                     /product="apolipoprotein N-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016410 - N-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54731
     Region          26..491
                     /region_name="Lnt"
                     /note="Apolipoprotein N-acyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0815"
                     /db_xref="CDD:440577"
ORIGIN      
        1 mrtrpagrwl wwagtvllvl avhsnwhlas aawlfpvfll ryarlrparh gllrvgyalg
       61 laqlvwllst gmvfvpsvla vfavlavvqt lpfaadrlva ahsgsvgatl vfpvvlvcge
      121 ylftqlagfg dygvlgftqh gflplvqlas vtgvygvsfv vawtasvahr swqrgfrwre
      181 irrgavvwag vsalvlgagg vrlvcfaptt etvrvagisa graaerager alhaagqelw
      241 rprnlvradp rrvsaalapv addlvaatdr earagarivv wpetqagvla dgqqrllgrv
      301 aeiarkrqvy vntafalytp qppyvrniaa lvtpegkaaw tydkahptpm epmtpgkgvv
      361 pvigspygrl atvicydadf pglmrqaagq dtalimvpan dwagleslha qravfrsvey
      421 gyamvrqsvh gvatavdhqg rtrgmadyft adrqtlvaev pvqprtdtly srtgdlfall
      481 caggtllvva lgvrgrrarv gvpgaagdrp
//
LOCUS       WP_457690350             128 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457690350
VERSION     WP_457690350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 128)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..128
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13792
     Region          1..>86
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mnseellall savghaqrlr vigeladgrl yvselarrle msrpllymhl drlekaglvv
       61 grlelsedgk alkyfelapf elklnvatvl aalqedrsga ppeetgdadg aaeppstkgp
      121 ndprgtrt
//
LOCUS       WP_457690352             351 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457690352
VERSION     WP_457690352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10143012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37062
     Region          18..347
                     /region_name="CAD1"
                     /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283"
                     /db_xref="CDD:176186"
     Site            order(43..45,48,163,167,187..192,210..211,215,230,
                     249..250,252,272..273,296..298)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(43,45,66,92,163,298)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(43,66,163)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(97,100,103,111)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(110,170,174,266,271..273,275,284,286..287,290..297)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176186"
ORIGIN      
        1 mthtsvsaya apapkapler itiprrelga hdilidikya gichsdihtv raewgdggaf
       61 pivpgheiag vvtevggevt ryragdrvgv gcfvdscrec ancraglqqy ctgelgnvgt
      121 ynatgrdget tyggysthiv vdenyalrip esipldaaap llcagitlys plahwkagpg
      181 kkvavvglgg lghmgvkiah amgaevtvls qslrkkddgl rlgadhyyat sdpatfeela
      241 gtfdlivntv sanldlnayl gllrtdgtlv qvgapesplp vapfalipqr ksiagsmigg
      301 ipetqemldf cgehglaadi evisadrine ayervmasdv ryrfvidtat i
//
LOCUS       WP_457690354             189 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690354
VERSION     WP_457690354.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 189)
  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 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   5  (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 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20933
     Region          1..85
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          92..180
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 malrhavlaa lldgeysgyq lakafdagva nfwhalpqql yaeltklead glvagrqviq
       61 etrpnkrlfh vteeglaele rfaattakps firddllvkv qavdridaap viqqldarar
      121 taaakveile qlavrlrger deaevlahga rigpyltclr glaferetrd wcersagilr
      181 arhegrqqp
//
LOCUS       WP_457690357              68 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457690357
VERSION     WP_457690357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..68
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7080
     Region          1..>50
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mrvhidqdkc cgagscvlsa pevfdqreed givllldaep paalheavhe aaaicpaaai
       61 tveqterv
//
LOCUS       WP_457690359             412 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457690359
VERSION     WP_457690359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 412)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=45168
     Region          36..412
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(82,103,105..106,189..190,199..200,203,206..207,210,
                     242,245..246,249..251,254,297,299..302,326,402)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(104..105,112,116,123,168,171,246..247,250..251,
                     254..255,258,296..297,300..301,303,326,353..355,358..359,
                     361..363,366..367)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mttaeriere qetgpgaglt pvavpaarat gcpfdpapel erahreeplt ratlwdgssc
       61 wlvtghqdvr evlgdprfsa datrpgfpfl tagarqfatg npsfirqddp eharlrrmlt
      121 adfmvkkmea mrpevqriad elldrmtegr haadlvaefa lplpslvicl llgvpygdhe
      181 ffqkhssvll nlrstaeevh iaqkelqdyl cglaeskrre pddgivsrlv argelddaai
      241 asmgrlllva ghettanmta lstltllrnp dqlarlraep slikgaveel lryltivhng
      301 lpriadedvt igghtirage gvlcalntan rdeeifpgga aldvgrdarr hvafgfgvhq
      361 clgqplarve lqialetllr rlpglrldip fedvpfrhdm giygvhalpv aw
//
LOCUS       WP_457690361             167 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457690361
VERSION     WP_457690361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18050
     Region          7..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpdpgrdqdp tvalqrvlat lsylltrsra herqaaeagv taarsdlwll maledsggis
       61 rvgdlaallm vepphvtrqi gqleaqdlve rtpdsldrra rkvaitphgk avlnrlqqts
      121 qaglhealag fddsdiaatv avlnhlvsya rqkftaeerq rgrgdvs
//
LOCUS       WP_457690377             232 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690377
VERSION     WP_457690377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=26178
     Region          16..>200
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtaavhesag dgharytyrl rvsstanavl eaewarcrwl wneccarskk ahaegekcgp
       61 arldrmltea rtamawlreg ssvpqqqlir dfaksrakal kdikarlpqr qrtgmprykk
      121 khqadpslny trrgfrlkdg rlhlaggivv tvvwsrevpe lpssarvyrd ilghwyvsfv
      181 vptmtealpe tgrvigidwg glcavrsenq artasfrenl clhrvrsrvp qg
//
LOCUS       WP_457690381             263 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690381
VERSION     WP_457690381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29361
     Region          1..58
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          77..254
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgstygdwlk qqreeagltq qqladaavmt rshiahieag rrvpsredar rldmalntgn
       61 vlssfrpkdd saiadyfeva rqleqqatmi refglsfvpg ilqtkryasa vlgsgfppws
      121 deerdrllrt rleraevled pvtpvvwvll desvlrrpvg speimaeqit hivrlaesqr
      181 vrvhvmplgl gyhpllqgmv slmwfedqpp avycegmymg kvhdapamve riqstydlal
      241 gdalpmkesl almratakgf gtp
//
LOCUS       WP_457690386             199 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690386
VERSION     WP_457690386.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21198
     Region          1..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdhdeartri ldaaerlfye rgiqsvgmde lrtaagvslk rlyqcfpakh dlveaylrrr
       61 dtrwrtalae yvdahadgpa arplavfdwl gdwfaedgfr gcaflnayge lgatsdrvgc
      121 larehkeall gyvaglvral pvaepellar qlvllidgai agaalmgeps aarqartaaa
      181 almeaagsaa asgvgrngg
//
LOCUS       WP_457690388             200 aa            linear   BCT 27-JAN-2026
DEFINITION  carbonic anhydrase [Streptomyces nigrescens].
ACCESSION   WP_457690388
VERSION     WP_457690388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21269
     Region          1..200
                     /region_name="CynT"
                     /note="Carbonic anhydrase [Inorganic ion transport and
                     metabolism]; COG0288"
                     /db_xref="CDD:440057"
ORIGIN      
        1 mqqltahars fenrcaerge efrrlgagqs pqalfvtcsd srvvpalitg aapgdlfelr
       61 tagnivpeyr terpageaat ieyavrvlgv ehivvcghsh cgavgalvrg edltgvpavr
      121 gwlesaapel sdgagadggt peladavqrh alaqaerlrs ypcvaeglda grlsldvwfy
      181 evhtgavrrh rpetgrfesl
//
LOCUS       WP_457690390             533 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces nigrescens].
ACCESSION   WP_457690390
VERSION     WP_457690390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..533
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53822
     Region          14..486
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mltalkrttg klptlspgtl rrdvlaslvv flvavplcvg vavasgvpae lglitgivgg
       61 lvvgclpgss fqvsgpaagl tvlvheavqq fglaslgaiv laagllqlal galrcgrwfr
      121 aisvavvqgm lagiglilil gqvyamadtd qpssgldkia glpglaagia srpeaftasa
      181 vgvgtlgllv lwprlpakvr qvpgplaaia vatlvtavca lpiskvevhg llasiqppgl
      241 gelgglaqls vlgtvlafal iasaeslfsa aavdrmtgar tdydkelmaq gagntvcgll
      301 galpmtaviv rsaanvqaga rtkasrvlhg awllvfaall paalrvvpla alaavlvhag
      361 aklvpvrqlp qlwrehrgea vilgvtagai vftnmfegvl lglllavvkt awetshvqid
      421 vreltggrtl valsgnatfl rlpkildale alprdkpvel dltelrhldh acrtaldgwt
      481 tqhnaaaaps padrpatgta grstamaast sastsasast saststdgsp hrg
//
LOCUS       WP_457690394             373 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457690394
VERSION     WP_457690394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  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..373
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..373
                     /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=38277
     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 yrhdgmplev ihqlrawdhq vdvvwpgrsl iriseaiqag shdawvlktv
       61 sggpgltlle aaasvglttv ndvrairgvr dkalaaviar gkglpvpvty aaarpeefae
      121 ipeaefplvv kpadgssgra vrlvatpdrl papvepggpd gpggpgggll iaqpyvpnsg
      181 tdlkvysvag elyatercsp lhpahavrer qvpltpevar itaeigavfg ldlygvdill
      241 gpdgpvivdi ndfpsfrqvp davarvsaav ldlarhgtrg raasvrevvr gtgpvsgqet
      301 gpapvptagq pearpvpvsg qpgaaapaat gqpgaaalpa tgrtgttaap appftmpsvl
      361 rptrpaasig ggr
//
LOCUS       WP_457690396             282 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457690396
VERSION     WP_457690396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  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 282)
  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 282)
  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..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /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=29094
     Region          <66..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 mricllsadp ghpllagvtg lltpehqvet ldpgaegpgp dlssladvyl lkartprala
       61 laalleehga pvlnsaaata rcqdrvemaa varaaglpfa gtrfvatlge laaagvpagp
      121 lviksrfsrr qdlvaradsa vrlrelaadw aeepvvvqef tvnsgwdhkl wvvdgqlfaa
      181 lrrselapeg rgptlplpvg elpaswtaaa lrvgevfgle vygvdlldag ggaplivdin
      241 afpgirgqag apealaalal rtavsgrtgs aaerkvpqvs ek
//
LOCUS       WP_457690404             230 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690404
VERSION     WP_457690404.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..230
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24436
     Region          22..225
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mgelgggvpv sagrtlrhfv gdavwrdllg qvyerrhsag svmlrqgesg thvlamlsgv
       61 akvlrrerng dltllafrgp gellgevavl dddvrsasve tissctvgvi gkaeflrfvv
      121 ehdlfpvlvr yaftrmresd eargggdtlt rlvatlvgla disgqtggrs geplelaltr
      181 helaqylgis rntisaslae lescdvqagr krivlgdlta lrrmvaapgs
//
LOCUS       WP_457690415             246 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690415
VERSION     WP_457690415.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25475
     Region          38..83
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          95..223
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 msaastpspp sppsppgarp aattgrgrpp kldqvrtvea alalldeagl daltmrrlae
       61 amdvragaly ryfatkhell tamaevllad clgrplssrd wserlaelar rmrtallgrr
      121 dgarvyagth atgahtlgfa daligvlrea gfaaddagra altlvnftlg htleeqaarq
      181 gaadegpadp dllraavtpg qyphltaalp vltstdftah fefglglllq glralgpgst
      241 ppgtgg
//
LOCUS       WP_457690417             266 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457690417
VERSION     WP_457690417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29333
     Region          2..258
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpdveaf rgilascaqg rlirrtevyd agvlhgvsar rlrreltgrr faeperrgkw
       61 llahtdgptv llhfgmtgel vcatsadaph ahdrvvftvg rerqlryrdq rklqglwlvd
      121 eagldrmlrd qgpdaatvtr ktfeavlagr rgslksvlmd qsalaglgnl lvdeilwrar
      181 lhparragal sadecgrlyt elrrtlrsav ragrvpprrs wltgrrdgpg aacphcgaal
      241 crkrlagrgt vwcprcqpap tgrdea
//
LOCUS       WP_457690419             285 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690419
VERSION     WP_457690419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30180
     Region          20..239
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mfrrrrgaat vtaereepvs daltlegvgr eyrhgavalh pvdlvvprgr flavmgssgs
       61 gkstllqcaa gldrptagtv riggtdlssl keaaltrlrr ervgfvfqah hlvpslsvae
      121 nvalplllgg magtervrqg ladvglgerg eaapselsgg qcqrvavara lvtgpdivfa
      181 deptgsldpa taqdvlallr ravdrdghtv vmvthdpvaa awtdealfla ggrvvgntar
      241 pevsevsrim rdlgraeree rdgeherrgr dgrgrregpd gewaa
//
LOCUS       WP_457690423             393 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690423
VERSION     WP_457690423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 393)
  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 393)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=41490
     Region          15..>127
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          142..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgetmrragr ataqlmtaag lallsylylg vllftavatv ivigagvlpe tvlllrrmag
       61 fkrrrvadwt gtavpeaypp ltgglfervr taladpgtyr dlrwlavhfg ygwllaylal
      121 plwavgllvd gvwcgllrqr avvlpligrl adldaawsha llrpspdsgh rarlaervee
      181 ltvtragava ahgaelrrie rdlhdgtqar lvalsmrvgl arraydkdpe aarrllddaq
      241 nqaeealtel rhvvrgihpp iltdrglvga vralaassgl evavgedgla egprapaave
      301 aaayfvvaea ltnaakhsga drarvelvrg pgrltlsvrd egrggaetgs agasggsgll
      361 girrrvaald gtvevtspvg gptvidvelp caw
//
LOCUS       WP_457690433             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690433
VERSION     WP_457690433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25333
     Region          3..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtppvielra atksypggvh alrgvdlrve rgelaaivgp sgsgkstlln llgtldrats
       61 gevrvagydv sklsdaqlsa lrarhigfvf qhfhlapgrs aqdnvadgll yggtglrerr
      121 arartaleev glghrighla hqlsggekqr vaiaralvgd pdllladept galdtasgem
      181 vmnlihelha agttvcvith dndiadslpr rirfrdgeiv ddsgaaaaap gslaepteev
      241 tr
//
LOCUS       WP_457690437             552 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457690437
VERSION     WP_457690437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57871
     Region          11..460
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mskpavagsd svgggrhlrr vlgfwglmfi clgsiigsgw llgalttavi agpasliswa
       61 lasvmlavla lahaelgaty piaggtarfp ffafgplagf sagwmswlrs vliapiqvea
      121 tlsymdrigw ihdrvhllha ngtltaagml igsglmlift iinilgvqll sginsvtavf
      181 ktavplltvv vlmtlafrps nftagggfap hgahgvfaal pagvvfallg feqaiqlage
      241 ardpqrdisr avivamaiat alylllqvaf iaalepaalt rgwdnpvgag nfgpyatlat
      301 avgaawlati lyvdavispa gtglvymaga arlsyamgre rvlpqplari grsrvpvvst
      361 flafvvgeia flpfpswqal vglvtsaaai myafapvslh alrvrdggrn rpyrmpsgpv
      421 laplgfvfan lifywsgyea dwklgtvall gfvflaltrr gipsgersgl rgksaawvwp
      481 wlggmiligy fgryggtgal pewwdlavvi vfslavhyta vrlamppeav daavqreevg
      541 esvppppaas ar
//
LOCUS       WP_457690435             398 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690435
VERSION     WP_457690435.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 398)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40947
     Region          15..395
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 msgpalraar lspadvlrvg aeglrsrrtr vvlsalgiai giatmvavig lstssradim
       61 srldrlgtnm ltaeagkdad gndaklprna vsmverigpv qhataigavd arvrrsdavp
      121 eemaagvtvq aarpdlldal nartsqgrwl nraserlptv vlgsvaadrl gmtepgakil
      181 lndrwfvvtg ilapvelvpn ldrtamvgyp saerylgfdg hptmlferst dvsveavqgv
      241 lartvnpgde gsvkvsrpsd alaakaatdk gltslmlglg avallvggvg vantmvisvl
      301 errqeiglrr algatrgsir fqflteslll salgglagaa lgaaatfafa haqgwtavvp
      361 pwalagglga tlaigvvagl ypavrasrlh ptvalsat
//
LOCUS       WP_457690443             213 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690443
VERSION     WP_457690443.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23181
     Region          1..205
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mslgtpmvyp ahrqllqqgd esrhvllltr gvakvvasse sgyemllair vagdlvgema
       61 afedqprsgt viacsevtar iiqvnalegf larhpdamra mlamlcarlr wanrrridfr
      121 aydsltrlar vlaelsqayg dhgpdssatr qvldvtlnqa elaslaglal pttekalasl
      181 sklglversy rkitvcdvpk llvfakvfae npy
//
LOCUS       WP_457690439             270 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690439
VERSION     WP_457690439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /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=29407
     Region          <20..>66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          93..259
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdvnqsprvg vllrewrrrr rlsqldlall adtstrhlsc vetgrsrpsr tmvlrladal
       61 dvplrerntl llaadyapay resglddagm aqiraaldmm ltahepypav vvdrwwnvvt
      121 gngamsvlma gippqvlvpq pnvfrltlhp dglatrlana gevralmler llrqvqatgd
      181 aqlralyeev rrypvpaeqe tapaggpaar pgpiqvplri rtpsgelsmf stmatfgapa
      241 dvtlselaie lfypldefta ealraaaagp
//
LOCUS       WP_457690461             982 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690461
VERSION     WP_457690461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 982)
  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 982)
  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   3  (residues 1 to 982)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 982)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..982
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=106293
     Region          8..259
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          135..976
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mdggshqrlr iavlgpvraw rdgtpldlgp vrrqavlaal mlrpgplvsq eqllvgvwgg
       61 qpprsgrrvl psyvyplrka ldaegagrtg svirsgrggy sfvgdgvrld vaelaervge
      121 aqrarasgdl atamdrftea ltlfrgepla glpgpfaqge rqrlsqrqrt lqrerleclv
      181 llgrsadald dlaavsalpe sdpydeslta lrmralygig rqvaalsaye dmrerlrdql
      241 gvdpgeelrr vhqavlrrdd eqllgpavar saappdrprp rravnelpgd agrligrere
      301 lalltasspp esvsivavdg tagvgktalv vhaagalrvh ypdgclfvdl rahsterqrq
      361 ppqrvlrrll rsvgaadsev pddldeltaa wraatsslrl llvlddvlsa qqirplvpag
      421 pgsmvlvagr rqlagldtdr rvtlepletg dglsllrhiv geeradrepe atrelvrlcd
      481 glplalriag arlqtrpawt laylvdrmag derrlgelsa gdrsveaafr lsydqlapaq
      541 qrgfrtlgls ptvefnplts aamlgcssrd aeqtleslvd asllqqtrpg ryrlhdlvrv
      601 harrlaeaap aeagaartav lrlyldagri tsdwgqggfp tgpqpagapf adwkdaggwl
      661 gaasgelvdv vghaaalgea dyacwiaeal sdyfvrrgry hecrtaleia lahadeatdr
      721 rmapalrncm gitdiyqgri lqghawftea lhlsrhradr reearalagl gaadlnsgra
      781 eraiprltea velaqrlddh wlaamglcvl gavhhsqrrc eealacfaaa rahaetngrp
      841 rmismasgna agvhldlgqy aeakilyrqa adlaqrvgdv lmhaivltrl gtaehgegnl
      901 saaaalhhqa lsqhrtlspl tepncdrlem diryrlgrty saagrvaear eqfrtalalp
      961 gadehpeera laiaglkeck dc
//
LOCUS       WP_457690462             334 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690462
VERSION     WP_457690462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36238
     Region          57..313
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 msehlstrrs vlkavggisa amalggagvl ataspasaas aaddgfglti kdrneadprm
       61 wyyrfatdav ewdpavnvll pddyhtsgrt ypvlylfhgg gtdqdfmtwd rlpeggiraw
      121 tagkpiivvm pdgghagwys npvnsntgpr nwetfhidql lrwidanfrt yaeydgravg
      181 gfsmggfgal kyaakyyghf asvsahsgpp slrrdlsava hwanvssaal dlgggtiyge
      241 pfdearvsad npmehiesyr nkrvfmvagt sptpvdpfdl lnetevlagq refragldqa
      301 giphewheep gghfvrpela irdidgiiar lrqa
//
LOCUS       WP_457690466             399 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690466
VERSION     WP_457690466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..399
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42256
     Region          61..399
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mraqtrqglr sstrqqggrr rravsaavav aigvmtlgal appgasasds aasaaaaarp
       61 davqqalnal vrddgmpsal asvqdrngri rsytagvgdl ttgskvprdg qvrigsntka
      121 ftavvvlqlv gegkigldat vdtylpglvr gkgidgrrit vrqllqhtsg lpeygihvdd
      181 deirnryfep relldialry kadaapgttw gysntnyvla glivqkvtgr plaeemdrri
      241 ikriglrhty fpapgemtir ephphgyhrn pantplrdft emdpsagwaa gqlistnsdl
      301 nrfftallag rllpaaqlae mrttvpagts glryglglts rplscggvyw ghggdiagye
      361 trggvtddgr aanvavtsvp tdeaatqhvk davdralcg
//
LOCUS       WP_457690464             413 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690464
VERSION     WP_457690464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 413)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /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=43322
     Region          159..412
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mirgirpllr gstyagvlfa ycgalaslpl lpfallpals wrsasesvqi vlvllvwavl
       61 vgvvglarpv rralvvsarr llrvplpnpv agrrpsgslg ldrwrtplwl vlhvavgwtg
      121 alasgvlfim glslpgnwlg gearaslfgt svrvsggwsw vvaavcilla vaicvlvtka
      181 lrwaaprllg psaaerlala aereqllaer nriahelhds ightltaati qaavageals
      241 adpataraam rsieestraa ledldyvlgv lreeqsgtap trtladlpel ldrlrhagav
      301 vepelsgdla qvqgtlsraa yrilqegltn alrhgaggpi varvaagpdg ldltvvnrtg
      361 vrtgpgpgtf ptsghglpgl aervrllhge fqagpdgtqh wrlavrlpar asa
//
LOCUS       WP_457690468             388 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690468
VERSION     WP_457690468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41368
     Region          34..388
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msgrtrqgpr spgrqqgtrr ralpaaaava igvmtlgala ppaasavrpd avqqslnalv
       61 rddgmpaala svqdrngrir sytagvgdlt tgskvprdgq vrigsntktf vavvvlqlva
      121 errvdldasv dtylpglvrg kgtdgrritv rqllqqtsgl pnysnhlgdd vryytprell
      181 atalqhpadf apgtswkysn tnyvlagliv qkvtgrplae eidrrvvrra glrhtyfpap
      241 gdasirephp hgyyresadv plrditeidp swgwaagqmv stgsdlnrff sallagrllp
      301 saqlaqmrst vpaeatfgpg aryglglvsr plpcgglswg hggsfpgyet rggatddgra
      361 tnvavtvqlt deagrrnler avdtalcr
//
LOCUS       WP_457690476             303 aa            linear   BCT 27-JAN-2026
DEFINITION  SURF1 family protein [Streptomyces nigrescens].
ACCESSION   WP_457690476
VERSION     WP_457690476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial respiratory chain
                     complex IV assembly [Evidence IEA]"
                     /calculated_mol_wt=32015
     Region          3..257
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 myrflltprw wginvfavla ipfcifmgsw qlsrfedrvd thqqqedrsa raktaaarpl
       61 erllpvdkvt sgrqasargr ydtghqllvp artlkdkhge rqgfyvlnll rtdggkalpv
      121 vrgwlpgdag akadtakvpa pprgevtvtg alqasenqgt dgvqagggla pgqlgmisaa
      181 slvnivpyev ydawitltdt qaplhavppa avegsgldlk afqnlgytge wfvfagfvvf
      241 mwfrlfrrdt eaakdaalgi vvgaeehgvg aedggvgpag gvvpeggavp gegegeaara
      301 gkv
//
LOCUS       WP_457690481             277 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690481
VERSION     WP_457690481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31023
     Region          56..163
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mrkitgpedw reanrarwde rvpihtasdy ydqdrfrrar dvlrdfeiae vgdvtgrsll
       61 hlqchfgqdt lswahrgaar vvgldfsepa ietaralaae lgygpdraaf vaadvydaae
      121 avpdaaydiv ytgigalnwl pdverwadta aslvapggfl ylaefhplcd alddetgsri
      181 vhdyfsrdaw vdelpgtytd fgaptvnnrs vewqhplgdv vsalaatglr idflhehdkt
      241 mfqrfsalrr dddgyhrfpg drpriplmys lragrps
//
LOCUS       WP_457690479             328 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Streptomyces
            nigrescens].
ACCESSION   WP_457690479
VERSION     WP_457690479.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34727
     Region          30..311
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mrhqlahlvt phshaamdkv daaletsreg lrtlwislgi lgltsliqlv ivalsgsval
       61 lgdtihngad altavplgia fllgrraanr rytygygrae dlagiaivlt iaassvwaay
      121 esvdrllhpr dvthlwavaa aavigfigne wvaryrirtg rkigsaalva dglhartdgf
      181 tslavllgag gaalgwrqad pligllitaa ilmvlrdaar evyrrlmdsv dpelidaaet
      241 alravdgvhg vgqvrmrwig htlraeadiv vdsrltvvqa halavaaeha lihavprlta
      301 atvhtdhtpd dtpegrnpha alahhmaa
//
LOCUS       WP_457690485             430 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457690485
VERSION     WP_457690485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 430)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47705
     Region          31..429
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(68,75,112..113,120,124,131,259..260,263,267..268,
                     271,304,309..310,313..314,316,339,370..372,375..376,
                     378..380,384)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(75,106,108,111,113..114,199..200,207,258..259,
                     262..263,267,310,313..315,419)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 msalssspfa ahvgkhpgep nvmdpalltd pfggygalre qgpvvrgrfv ddspvwlvtr
       61 feevrqvlrd qrflnnpaap slghsieesp tvrllemmgl pehfrpyllg silnndapdh
      121 trlrrlvsra ftarkitdlr prveqiadel larlpehaed gvvdlikhfa yplpitvice
      181 lvgiaeedrp qwrkwgadlv slqpdrlsts fpamiehihe lirerrgalt ddllselira
      241 hdddggrlsd vemvtmiltv vlaghettah ligngtaall thpdqlrllk ddpallprav
      301 hellrwcgpv hmtqlrfase dvdiagtqir kgdavqlilv sanfdprhyt gperldltrh
      361 paghaenhvg fghgmhyclg atlarqegev afaklfahyp evslgvapeq lertplpgsw
      421 rldslplrlg
//
LOCUS       WP_457690487             259 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690487
VERSION     WP_457690487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28865
     Region          3..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 merahradri ldaagellla wgygrvtide iarrakvgkg tvylhwktkd slllavvlra
       61 qfrmhqrqla rmredplell psrmmrrhfl efqaepvlra lytddadilg rltetakkef
      121 aelmvqgdrn lrrhlevlra hglvrhdtdv qhqqytllat stgfflseal ladrapdsle
      181 vraeilahtl rsalevpaga gsgpgpdlds gtapgsdsgp dttslriraa aaaaapeiia
      241 vyehftefca qemrrqird
//
LOCUS       WP_457690491             435 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457690491
VERSION     WP_457690491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=45957
     Region          157..430
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mtdwlegpld gnwrggeaqa ehistgqiwr paehppqihq arppnldapg aapqalvppp
       61 rsnghtghgr pavrtggtgp gggntghtgp gggnpgrgrr aadpprrrrr itralivlat
      121 vlglgsagty vwadtelnre vdlgkiadrp ssgggtnyli vgsdsrvgls drarknlhtg
      181 gsadagrrtd smillhtgeh gttmvslprd swvtipshir petgkhyrat knklnaafsf
      241 ggpdllvrti ehntgvhidh yteigfagfv givnavggvp mcldrdikde ksgadlkkgc
      301 hnldgrtala fvrqrhqeak gdlgrgenqq kflaalakka atpgvlldps tvyptmsagl
      361 gtlivdkdtg lpnltslfka mkavtagdgk rltvpvsnla lqtpkgsavk wdtrlaeqlf
      421 telnndrpvt vgake
//
LOCUS       WP_457690497             266 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690497
VERSION     WP_457690497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27605
     Region          70..255
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msrqaparsr reqsadavpg avrtfgrqlr ydllaqarnp aaaffslglp liflitftsi
       61 garrddtavy yapatmaiav vsgtlsniai tlvylreygl lkrlqllpvq raallgsrvg
      121 asgllssvgv lllaayaaav hgvvpeqpmt vmaavlmlam agsalglalt vvipgesaag
      181 pianalalpl lmvsggffpl daspewvrql asflpfgsgi daavagyega atvsdlgeta
      241 latgawtaaa ltlvatrfrw vprrrr
//
LOCUS       WP_457690507             252 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457690507
VERSION     WP_457690507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27325
     Region          16..210
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrrriiivta vhapsahflp eaykslcqqd lpdgwewhwv iqedgksndv aphvpdderv
       61 tfrqgrpggp gvartialah aegeyikvld addqltpgal ardlaalegd sgiswatsrv
      121 ldllpdgsta gfpgdpepgp iepgavldfw kangfraqvh patlcvrrdl llalggwmal
      181 pasedtglll alnatsrgwf ssevglhyrk wpgqatgqas htdtaerear mavveararq
      241 laqfkwrcpa md
//
LOCUS       WP_457690509             262 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690509
VERSION     WP_457690509.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29505
     Region          5..250
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mavayeriad elreairage lkpgdklpae sklaerfrrs vptirealra lrdegliekq
       61 hgrgnfvrrq rtsalrtnrr hqweknrare plaeraqtga tehdtgltvd dlvfhasyrk
      121 veadkglaea fglpegtall ertyrtryaa esapfslvts ylvhdlvarn pdlldesnep
      181 wpggsqsqly tvgieldrve ervtarpptp eeaaelelwp gtsvlalrkt sidindrvvd
      241 vsdvilpgdr temlfttple rw
//
LOCUS       WP_457690515             308 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Streptomyces nigrescens].
ACCESSION   WP_457690515
VERSION     WP_457690515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  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 308)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=33187
     Region          25..307
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrarygvplt ltavgaagla yaagfevrsf rlrrvtvpvl prgmrplrvl qvsdihmvgg
       61 qrkkqrwlqs laglrpdfvi ntgdnlsdpe gvpetldalg plmefpgayv fgsndyygpk
      121 lrnparylie raqgrhglng napavgvvhn pweelrdafd aagwvglsns rgrlklegfe
      181 ialtglddph ikrdryaeva ggpesgadls lavvhapylr sldaftadgy plvlaghthg
      241 gqlcipfyga lvtncdidtd rvkglsthta dgrtsylhvs agcgtnrytp vrfacppeat
      301 lltltard
//
LOCUS       WP_457690518             733 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690518
VERSION     WP_457690518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..733
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78002
     Region          52..676
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mpkkrdgggl sktqqaakfl gvsvlagavl aglalpaaga lgltakgsve gfddipanlk
       61 tpplsqrtri ldakggeiak vysrdrtvvg lkdmspyirq aivaiedarf yehgaidlkg
      121 ilravnknaq sggvsegast ltqqyvknvf veeagdnadk vaqatqqtlg rkvkelkyai
      181 qvekelgkrk ilqnylnitf fgqqaygvea aaqryfskha kdlnleesal lagivqsptr
      241 ydpvnapqea tkrrntvlqr madlkdvsqa qadaaakkpi klavsrpkng citaadgagf
      301 fcdyirkvfl ndknfgksrk vrlqrwnegg mtirttldpq sqksiqasls dhvyeddpva
      361 gaativepgt gkilgmgqsr pygfrenqtv inlsvdhdmg ggagyqpgst fkpviaaaal
      421 eqgtnpeqey pspyrmpyps pvqtcdgewq gtdmtqnenk eevgpyamke ataksvntyf
      481 vqlisdigic pavkmaqkmg ieradgkplq qvpsmtlgvq emspltmaag yaafanggey
      541 cspvaiesit dargralkvp qtscrsamsk rtadtintll kgvvedgtgk eaglqgrdsa
      601 gktgtsdsry aawfvgytpn aagavwvgdp qhkrkmydis iggvphdkvy gadtpgpiwr
      661 damsgaladr papglptvpi ddpakdrnhg degdkgggkh kpgrgghggd nkpgdgwdip
      721 gfpdllgggn ggw
//
LOCUS       WP_457690526             278 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690526
VERSION     WP_457690526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14427476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28973
     Region          23..208
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(87,89,91..92,142..143,161,204)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
     Region          239..276
                     /region_name="BLACT_WH"
                     /note="Beta-lactamase associated winged helix domain;
                     pfam17778"
                     /db_xref="CDD:407650"
ORIGIN      
        1 mtdaaalpgq prggvisgpa tararcvlap npspmtldgt ntwivaepds dlavvidpgp
       61 ldethlravi dtaeragkri altllthghp dhsdgaarfa eltgssvral dpalrlgdeg
      121 ldagevittg glelrvvptp ghtadslsfh lpadravltg dtilgrgttv vahpdgrlgd
      181 yldslrrlrs ltvddgvatv lpghgpvlnd aqgavefyla hrahrlaqve taveaghrtp
      241 aevvasvyad vdrslwpaae lsvraqldyl gehglied
//
LOCUS       WP_457690525             315 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690525
VERSION     WP_457690525.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 315)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33422
     Region          33..237
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mssttngqwy ppewpdrira langeltpae prraatvlll rdsdsggptv hmlrrrasma
       61 faggayaypg gavdprderp vawagpsraq wavrmgvdpa taqtivcaav retfeeagvl
      121 lagasadtvv adttgedwea draalvahel sfadflgrrg lvlrsdllga warwitpefe
      181 prrydtwffv aalpegqrtr nasteadrtv wirpaeaaag ydrgdllmmp ptiatlrglq
      241 pyataadala aaeaqdltpv lararlvgge ielswpghde ftkhitqtda dsgapsggep
      301 dgptdgagss ggtpt
//
LOCUS       WP_457690532             242 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690532
VERSION     WP_457690532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25927
     Region          61..220
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mrsareqqyg keadagepas greatvtaeg lpewldpvar vaatlkppql srylppesgg
       61 rqsavlilfg hgprgpelll meragtlrsh agqpsfpgga ldpedgdpeg pgpvraalre
      121 aqeetgldps gvqvfavlpr lyipvsgfvv tpvlgwwrrp spvgavdqae tarvftvpva
      181 dltnpahrvt trhpsghigp aflvqnalvw gftagvidri lhyagweipw drdkavpldw
      241 rs
//
LOCUS       WP_457690538             152 aa            linear   BCT 27-JAN-2026
DEFINITION  phage holin family protein [Streptomyces nigrescens].
ACCESSION   WP_457690538
VERSION     WP_457690538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Saier,M.H. Jr. and Reddy,B.L.
  TITLE     Holins in bacteria, eukaryotes, and archaea: multifunctional
            xenologues with potential biotechnological and biomedical
            applications
  JOURNAL   J Bacteriol 197 (1), 7-17 (2015)
   PUBMED   25157079
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Young,R.
  TITLE     Bacteriophage holins: deadly diversity
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 21-36 (2002)
   PUBMED   11763969
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Wang,I.N., Smith,D.L. and Young,R.
  TITLE     Holins: the protein clocks of bacteriophage infections
  JOURNAL   Annu Rev Microbiol 54, 799-825 (2000)
   PUBMED   11018145
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Young,R. and Blasi,U.
  TITLE     Holins: form and function in bacteriophage lysis
  JOURNAL   FEMS Microbiol Rev 17 (1-2), 191-205 (1995)
   PUBMED   7669346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10538267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="phage holin family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15722
     Region          16..>101
                     /region_name="Phage_holin_3_6"
                     /note="Putative Actinobacterial Holin-X, holin superfamily
                     III; pfam07332"
                     /db_xref="CDD:462148"
ORIGIN      
        1 msavhdgtdr slgqlvatat aemsalvhde ialakaefrr dakragigsa afmvagalal
       61 falpvlsfaa aygihnlglg lawsflivgg aflvlaglla liamakmkki kkpeksinsa
      121 ketaavlqra kphprvapve hpvlesvtrs sv
//
LOCUS       WP_457690545             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690545
VERSION     WP_457690545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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   2  (residues 1 to 328)
  AUTHORS   Lindahl,P.A.
  TITLE     The Ni-containing carbon monoxide dehydrogenase family: light at
            the end of the tunnel?
  JOURNAL   Biochemistry 41 (7), 2097-2105 (2002)
   PUBMED   11841199
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Ragsdale,S.W.
  TITLE     Nickel containing CO dehydrogenases and hydrogenases
  JOURNAL   Subcell Biochem 35, 487-518 (2000)
   PUBMED   11192731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35443
     Region          1..268
                     /region_name="CooC"
                     /note="CO dehydrogenase nickel-insertion accessory protein
                     CooC1 [Posttranslational modification, protein turnover,
                     chaperones]; COG3640"
                     /db_xref="CDD:442857"
ORIGIN      
        1 mkiafvgkgg sgkttlsslf irhlaasrvp viavdadinq hlgaalglde aeaaalpamg
       61 ahlplikdyl rgsnpripss esmikttppg egsrllrvge dnpvydacvr tvdldgaavr
      121 lmatgpftea dlgvacyhsk vgavelclnh lvdgreeyvv vdmtagsdsf asgmftrfdm
      181 tflvaeptrk gvavyrqyke yardfgvplk vvgnkvqgpe dlaflrdeag ddllttighs
      241 dwvramekgr parfdhleea nrhaletlhh tadaaygrrd werytrqmvh fhlknaeswg
      301 naktgvdlaa qvdpsfvlse gaatpqpa
//
LOCUS       WP_457690549             301 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690549
VERSION     WP_457690549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32681
     Region          18..241
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mvgayarpve nhsvphstpr taaffdldkt viaksstltf sksfyqggli nrravlrtay
       61 aqfvflagga dhdqmermre ylsslcrgwd vaqvreivae tlhdlidpii ydeaasliee
      121 hhaagrdvvi vstsgaevve pigellgadr vvatrmvvge dgrftgevey yaygptkaea
      181 vqelaasegy dlercyaysd satdvpmlta vghpfavnpd ralrreavar gwpvlsfnrp
      241 vplkqrlpal smpsrpvlaa maavgaamat atlvwyasrr kttkprllig rsggtarnar
      301 v
//
LOCUS       WP_457690554             306 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690554
VERSION     WP_457690554.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30797
     Region          92..301
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 msvaavalvv amlcagaalr sgggrpeevr rraralfggr geadpaggwr dwlrgegvre
       61 wcagrlvege agrrwsvgrr gdvgrevwcl paglvlgvlg gsvfpvvasv aavflvrrwl
      121 vargagrvrd rraaaviglc aavagelrag rqpaqallaa gapglgaegs avlaaarygg
      181 dvpqalraaa rqpgaagltg maacwqvate ggaglasgle rgaaglraqr dqrdelraql
      241 agpratalml allpaagllm gsalgadplr vllhtpagwg clvvggllew ggvawtariv
      301 aaaega
//
LOCUS       WP_457690580             529 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690580
VERSION     WP_457690580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..529
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55769
     Region          124..365
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          427..522
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 matsrllrts aavlaatall isgcssgsss pgseaspgrr teagaqrpae aatlaplpas
       61 tpsglrpyyd qklswhpcgv agfecatmka pldyakpsad tdlklavark katgpgsrig
      121 slqvnpggpg gsaidylqqy apqpasvrar ydlvamdprg varsepvecl tdkqmdrytq
      181 tdvtpdspae ankltsayrs fakgcasrag kllphvstie aardmdvlra vlgdqklnfv
      241 gasygtflga tyaglypsrv grmvldgamn paldsrtvnl nqttgfntaf safaadcikr
      301 kdcplgtksv edagrqlsal fkkldahpat tgeerkltes lattgviaam yderawpvlr
      361 eylaqaedgn grglltlsds yyerdpngty anqmyanpav ncldlasaft gpaqvraalp
      421 sfrkaspvfg enfawaalnc aywpvkptgt ahrieakgaa pilvvgttrd patpytwaka
      481 laaqlssatl ltyegdghta ygrgskcida aindyllkgt vppkgkrck
//
LOCUS       WP_457690607             259 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces nigrescens].
ACCESSION   WP_457690607
VERSION     WP_457690607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28842
     Region          24..258
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtvsraargp hraldqewfr rprpvtdprm rlvcfphagg aasffrdwpq wlpadielaa
       61 vcypgredri alpsvesmde lagriaeelv paldrplaff ghsmgasvah evamrierrr
      121 ggvlrrllvs srsapsrlrp tglsresdev lvrdvmelgg tfsaaldhpd lrelllpair
      181 sdyrliddyr padplprigv pvtallgdrd phvheadmra wsevtdgdfg lqvlsgdhfy
      241 lleqapylva evgrlltsr
//
LOCUS       WP_457690605             399 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457690605
VERSION     WP_457690605.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..399
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=44034
     Region          12..336
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mydvivvgar cagastamlf aragyqvlmv draefprdtl stlyihqpgv allrrwgvld
       61 kviatgcppl dravyriadi riegcsipvd ghraayaprr ylldeilada avasgvefrq
      121 gctvtevlsd degqaigvrc rtsdggtsee harlivgadg mrsrfatmvd srittehpaa
      181 tcayytyweg vtdrfelyea pgrwvgtvpt ndnatliaay fpqaefervr kdamgaylea
      241 vrttapelya kiesqtpler lhgtgdqrny freaaglgwa lvgdaghhkd sitargitda
      301 frqaqllvdc vgtglrdpek lldgleeyay qrdeiliday hstlsvaele vpehrlsmlr
      361 tvagdqelmd ryfatlagvi gveefftpel hareeltrq
//
LOCUS       WP_457690608             252 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690608
VERSION     WP_457690608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27791
     Region          12..233
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mttsvlpaag algvlggmgp lasaeflrtl yagewhgpeq srprvlldsd pafpdrteai
       61 rqgraremte rledrlsqll ergadqvvvv cftahhflpl vdpvlrgrvv slvettaael
      121 agatgrflml stegsrrari fesqpgwdav ahrvvrpded dqarvhrliy rmkrygplph
      181 ealpeverlm qrhdctgvvl gctefhlvsr dlterygpdr tvdalrtlav rfsaglpapq
      241 rlvsslptsa tr
//
LOCUS       WP_457690614             278 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690614
VERSION     WP_457690614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30952
     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          92..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnrnelnpda speaaygarl rslreargwt qedlaeraey ssvhvsaven grkpptlrfs
       61 rsvdrvfgle gtpdsferey reikhgslle gfpeyvgyeg raveirlyni giipgllqtp
      121 eyarvladsa vrrgaitpeq aderveflae rqavlersrp pmvfvtldes cirrpvggst
      181 vmdaqlarlv efadlpntll qvapydiger rtlnlpvniv tlpdrsliyy aesqaqgnld
      241 restsvvpvl tayhqlqaea lsqaasvdmi eqlrkgip
//
LOCUS       WP_457690618             252 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690618
VERSION     WP_457690618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26908
     Region          55..251
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msslvrhsla lsrrnlrksl aspgqvldta lmpvvlsvif iyafggaiag nsadyrqylm
       61 pgimalnhti vsrtagialn tdfssgvmdr yrsmpvarsa vligrvsads vrllisqlav
      121 fafalligfr adngllptia afgllllygi alcwvnafig laarsidtvq svstiamlpl
      181 qfgssvfvap dtmpswlrif vennpmtqvv dasrnlmigg pvaahaqgal lwiagliavf
      241 lplsvwkyra rv
//
LOCUS       WP_457690629             331 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA family dioxygenase [Streptomyces nigrescens].
ACCESSION   WP_457690629
VERSION     WP_457690629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Islam,M.S., Leissing,T.M., Chowdhury,R., Hopkinson,R.J. and
            Schofield,C.J.
  TITLE     2-Oxoglutarate-Dependent Oxygenases
  JOURNAL   Annu Rev Biochem 87, 585-620 (2018)
   PUBMED   29494239
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schofield,C.J. and Zhang,Z.
  TITLE     Structural and mechanistic studies on 2-oxoglutarate-dependent
            oxygenases and related enzymes
  JOURNAL   Curr Opin Struct Biol 9 (6), 722-731 (1999)
   PUBMED   10607676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="TauD/TfdA family dioxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35707
     Region          40..311
                     /region_name="TauD"
                     /note="Taurine catabolism dioxygenase TauD, TfdA family;
                     pfam02668"
                     /db_xref="CDD:367137"
     Site            order(83..84,111,113,118,169,314,316)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238154"
     Site            order(108,110,135,301,310)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(108,110,301)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
ORIGIN      
        1 mtatfdgtav petlgdgael ilgegrtpvl rvtgpdlpge tvralldrhg allvrglglt
       61 apadlgraaq algvtpmter egftgrtdfg dgvygasewp adepmcmhhe rsygdevpgi
      121 alfgcltapr tggatavada rtvlaklpad lverfardgw rlarnyrdig vswtesfgtq
      181 daaqvdaycr ahaldhewlp dgslrtvqhr aavvrhpatg erlwfnqiaf lneltmdpav
      241 reylvslygp dslpfttfhg dgepvpaqvv eainevytaa tvrepwqagd llvvdnlrma
      301 hsreayegdr eivalfgdpv rldghvrpsa t
//
LOCUS       WP_457690631             789 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457690631
VERSION     WP_457690631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..789
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=85759
     Region          3..785
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mglserqgls pdtlllaahv rvlaavtgds svvtgylpee gpeksalplw aalsegswae
       61 lvtevaqlad dvrrhapqal delraetgrt eplfdtvlva graaapedlt agtvlaagla
      121 rtgdrlelvl shrpdaldge qadrfagyll aalrelterp gadhqewspv sqreaaqqla
      181 dfagphrelp drrvhelfed qvrlrpddia avhgteswty relneranrv ahalrrgglr
      241 dedvvavvte rtlqwlvavl avfkaggvyl pvephfpadr isgmlvradc rrvlterdas
      301 pgltealagl pgvradhldt llaedhpvtd pgvpvstgqs ayiyftsgst gapkgavceh
      361 agflnhllak iddleitegr vvaqtapqcf dislwqlvaa lavggrtlii gqpdildtar
      421 fietldtggv evlqavpsyl evvltelers pralprlrhv satgealkke lverwfatfp
      481 dvalvnaygl tetsddtnhe vmrrvpeqas vplgkpvanv rihvvderlr lvplgspgei
      541 lfsgvcvgrg yvndeertra afmpdpllpg ermyrsgdfg rwlpdgrlef lgrrdaqvki
      601 rgfrieigev enqllrvdgv rdsavvvtge gesrqlvafh sgeelsddtl leslgaalps
      661 ymipsrfrrl dvlpltangk idrkaltrla gqeeaagdgv elrtdterrl aqlwsqvlkv
      721 pagrigrash ffdsggtsls mlrlaialdr vvtpvelqqh pvlaecaall drraaeapnp
      781 grqpvdshv
//
LOCUS       WP_457690633             460 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Streptomyces nigrescens].
ACCESSION   WP_457690633
VERSION     WP_457690633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47237
     Region          93..431
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mlkvvagvvl llgavglwwg rlgsggsste vdttarflla vmviillshl lgallgrlgq
       61 plvigeilgg lllgpsllgw vwpsgqawll saevvsalnt vaqlglivfm fllgcelrme
      121 tpkkavgslg vsvlgamglp fvaglalaaa apamlrgstp hdfgylcffg lamsvtalpv
      181 lariltdlrl drspvgqfal asaavgdgia wlaltvilaa tgsgdatdmg stialvvalv
      241 vftalvvrpl latvvqraee rpgkgtllpl llvgaisyav lthllglhav igaflfgtav
      301 prdstvthrm nqqlqgftlt vllplffagv glnvsvgalg rdpwhwlvla gvvvvatltk
      361 ivgaggaara mgyqpkeslr fgalmncrgv telvvagigw qrhlisttgl tvlvlmavgt
      421 tamtgpllkl lgtkppeppp getddpsvav pqgaqlrada
//
LOCUS       WP_457690634             192 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690634
VERSION     WP_457690634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20053
     Region          19..172
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 maslpppssa pdtatrpvpa ddfrslmgaf ptgvavitty gtddrprglt csslssvtta
       61 pptlavwltt rgetlgalre ygafavnllh drgqragevf ahpvadrfsq vgwrrspeag
      121 lpwladdafa vaecrvtklv eesdhtlvvg avtgvtqhag tpllygvrrf aswpggeapa
      181 aplaldtplt sc
//
LOCUS       WP_457690636             514 aa            linear   BCT 27-JAN-2026
DEFINITION  tryptophan halogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690636
VERSION     WP_457690636.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Zhu,X., De Laurentis,W., Leang,K., Herrmann,J., Ihlefeld,K., van
            Pee,K.H. and Naismith,J.H.
  TITLE     Structural insights into regioselectivity in the enzymatic
            chlorination of tryptophan
  JOURNAL   J Mol Biol 391 (1), 74-85 (2009)
   PUBMED   19501593
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Yeh,E., Blasiak,L.C., Koglin,A., Drennan,C.L. and Walsh,C.T.
  TITLE     Chlorination by a long-lived intermediate in the mechanism of
            flavin-dependent halogenases
  JOURNAL   Biochemistry 46 (5), 1284-1292 (2007)
   PUBMED   17260957
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10521725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..514
                     /product="tryptophan halogenase family protein"
                     /EC_number="1.14.19.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57797
     Region          5..481
                     /region_name="Trp_halogenase"
                     /note="Tryptophan halogenase; pfam04820"
                     /db_xref="CDD:398475"
ORIGIN      
        1 minsvvivgg gtagwmsasy lkaaygdrin vtlvesdrva tigvgeatfs tvrhffdylg
       61 lderewmpec sgsyklgirf enwrepghhf yhpferlrts dgytladwwl qegdrsqpfd
      121 rscfitpalc eakrsprlld gslfaggldg slgrstleeq raqfpyayhf daallakflt
      181 kygtdrgvrh vvddvthvgr dergwishva trehgdltgd lfidctgfkg mlinetldep
      241 fesfqdvlpn nravalrvpq adqattgmnp yttatamdag wiwniplfgr ngngyvysde
      301 fctpeeaert lrdhvapgqd dleanhirmr igrnrrswvn ncvaiglssa fveplestgi
      361 ffiqhgieql vknfpdenwd palvddynnr vaevldgvke flvlhykaal redtpywkea
      421 ktralpdgla erlaigsshl ldertiyqpy hgfeqyswit mmlglghepk rprpslahid
      481 ptnaraelar lkadadelva alpscyeyia sins
//
LOCUS       WP_457690640             989 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690640
VERSION     WP_457690640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 989)
  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 989)
  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   3  (residues 1 to 989)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 989)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..989
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=108488
     Region          10..257
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          139..989
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          807..835
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          847..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(848,851..852,855..856,858,888,891..892,895..896,
                     898..899,928,931..932,935..936,939)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          886..916
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          927..953
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msedrsipra ikysvlrpll vitgsgriig vhgprqrtil tmlilawgrv vsvdslvdav
       61 wgdeppatar tqvaicigal rksfkqagve gdviltthpg yrlettgsdl dalqftslvt
      121 eaaahvkqgr heqgrvlyrq aldlwkgpal agvtgrpved eatrlderry aayeawseve
      181 lalghhqdii seltsianss plheqlrynl mlaqyraglr aeategfrmw rrnfvdelgl
      241 epsvaikelh asilqddpgl tlpvqvkplv vpaqlppdvd lfqgrsaelg kldrllgers
      301 prmglitgva gvgktglivh wahnvagefp dgqlyadlsq ydgkqpefva gallgrflra
      361 lgvpgdqips dpaeraslyr svladrksli vldnvrtmsh itpllpgtgr scvlaasreq
      421 laadsgtvrv dlglmtples qtlitkiage gratsekaav nelcrlcdgl plalriaaar
      481 lvakqhwsvq hlvdrlrdeh rrldelstgg levrasfals yrglteqtar myrllglldv
      541 pdfpawvgga lldvspaeae dmierlvdah lltpigsdat gtmryrfhdl lrlyarerae
      601 sdeaedkrra alhrvfrtyl tlaeqghire yggdfaiihg stprrhldap lvgrllgspl
      661 dwfeaerssl vasilqacal rmeelawdla mssvvlfetr nyyddwravs ekaleanrna
      721 gnirgeaamc yelasvemfq qrfdsamplf trafqlfdsv revhgraltl rnmaitdrvq
      781 gglrsamsrl dearntfrvv gdasaeahtl nqmsqielew gnpdaavrls leavriatal
      841 getrgaaqal nrlaaayvkq grfdaakqsy dgvlrivrsk gdtrgeayal mgigetlvas
      901 gqhdeaesil adaleiaerv ddlfllakvh lalgscsqql nqltrasqhl liarntfhei
      961 gsvwgelqas adisrlsaet cggrplpgr
//
LOCUS       WP_457690644             431 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690644
VERSION     WP_457690644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /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=45167
     Region          55..>306
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtdlelrpps pvrqpplptg plrplparrt pwqalhtaal ridaatpadr dratdvlral
       61 aitgvvlghw lvsgvvlqag ghlagdsplg hlpglapvtw ilqplavffl vggrvgarsy
      121 eaalargigy rtwlaqrlar llrpatafal twglvwlglv lagtahetih tlmwlayspl
      181 wflgvyalli aatplvhkag ariavaaclv vaaldasrvl fadsgwvdtl rllnipagwl
      241 vpyclgavwa aggftrqrpa valllgggga maalilwggy pasmvgvpgs tlsnlspptl
      301 aavafglaqa gaalllrapl rravtapapt gpattprnra tpaqflwaav allnlsavtv
      361 flwhqtamlt ttviplglgh tfpglhtspd slvwiaarsg wiavfvvvll vlgtafrdre
      421 garanraitn q
//
LOCUS       WP_457690646             234 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690646
VERSION     WP_457690646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..234
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26533
     Region          63..164
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mstltlesis tlyekyaddl ravrdaqrkf lqdnkdtvka qlddyeaeit ylllrdlkpe
       61 vvvevgtfrg wsttwilsal rdngtghlys fdivdnvvkn vpaelsegrw tftkgdlrdn
      121 lakvptetdy lfidadhgar farwyidnlf pvvrpgtpts vhdvfhgrrp kpmsegsvvi
      181 kwlaaqnvey ftpsvakape vtarlaevkk elglsepvre srhnpmiyfn lpqs
//
LOCUS       WP_457690663             234 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457690663
VERSION     WP_457690663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..234
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=25723
     Region          79..233
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meysaaphha pvrfalpgpr palwrwllrt arpaaahret prsghsprps afgqpagsrp
       61 rlpdgtgaap pdppptisel yhahrltmvr lavllvddra taedvvqdaf aalykrhgeq
      121 ldevdnalay lrtavvnaar svlrrrrtar nytppyeada psaeerivld eehrevfaal
      181 sgltarrrev lvlrywgdlt eaqiattlgi srgsvkslas raldslekil ears
//
LOCUS       WP_457690665             749 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457690665
VERSION     WP_457690665.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..749
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=79456
     Region          22..741
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mrpveprpke krpvtvrvav wsarhpwral agwlafvvlc lgvglamgth katgedyrvg
       61 eagraetlaa earldrepve qvlisarsgp ltqaaaepav rdvtarmrkl pevarvappv
      121 rsadgralrv avimkgaead addhvaplaa qtaavqrshp elrvaetgsp svsvgvdtqr
      181 gddlalseai alpvtlltll avfgsalmva vplllaltsi vaamglsmvv shlqpdagvg
      241 nniilligma vgvdytlfyl kregeerara ggrlgpealv elaaatsgra ivvsglaviv
      301 statlylatd vvfsslatst vivvlaavls sltalpallv kiaqradrra arraqradrr
      361 aarraqrtgr rpaprersdg pgrlwrallr pasehpartl clsvllmlal aapalgmqlr
      421 vlnkdshsre ipalqtydrl ttafpdlrvq hqivvrapaa eaaevasalr elsgraqsdp
      481 lyakgvtplv ktsrdrrttt melstphkvs speaiasldr lrtdylpdtv gavpgaefav
      541 sgdvahdtdy lahqdgklpl vvgalllltf lmttlvfrsv vigligvaln llsaaaafgl
      601 vvvffqhgla gtlfgfdtaa tsaigsrvpl flfvilfgls mdyqifvvsr ireaalrgvp
      661 treavlhgvg asakvvtsaa vvmvtvfasf mflhlaemkq igfslavavl ldafvirvvi
      721 lpsaltllgr aswwpsrtmr raqstlpvp
//
LOCUS       WP_457690667             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690667
VERSION     WP_457690667.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21346
     Region          10..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpdikhfhpd lvldeaiqvf wrhglpttgi qalvtatgvs rsslyatfgs kdglyaaalg
       61 ryiaqhstpa fahlsqassg ltsieeffag lievrcsgpv agwgcmvtna hagpecadsg
      121 irtlledhhq mlqsamraal anaaelghlq pscdldasaa vlatlaygvn lrsragadaq
      181 altdtvtaal aplraplspq ehppq
//
LOCUS       WP_457690672             597 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690672
VERSION     WP_457690672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 597)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 597)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 597)
  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 597)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..597
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64919
     Region          3..577
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mgfkesvrrf wpltrgdrrw illvclsavl aafaetvail vfaeltdnal qkgsvsafwa
       61 paglwlgvav aggvvgylgn slaawtaerf vmrlrarvfa hlqtlpphff qrnrrgdlle
      121 rmtgdvdaie alvvsglvqa atavfgvify agaafwlrwd malvtfalap lfwiatkrft
      181 grvkevsrre raadgaitsv veeglvnvvl tqaynrqhde qerlgrearr wlrasvtsar
      241 lnelyeqive vletlcvlai iglgaweist grmtlgella faafvgylyp pirdlgqlgl
      301 tvteatagse rlleildsrp avtdpddavv vatpsravga veacrvdfry pgsqkevlqd
      361 fsfsavpgel vvitgpsgag kstlaalllr fydpdagsir ldgipvnrmp ldrlrrnitl
      421 lpqetlvlhd tveeniacgr dnvthgdvvr aaraadaemf iaalpdgydt viapgtsrls
      481 ggqlqrvaia ramlrdapvl ildepttgld tlatqrilap lrrlaegrtt ivithdldla
      541 mdadrilvld egrlaesgth aqllagsgly atlfhthppp rngspyplah ptgshwr
//
LOCUS       WP_457690676             608 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457690676
VERSION     WP_457690676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..608
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65246
     Region          28..183
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          364..604
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpdwekrfra prvglpewae dapdrslfvs natgtfelya wdretgkqrq atdrpngttd
       61 gtlspdgrwi wwfsdtdgde fgvwmrqpfe ggpdepatpg lapsypggla isrdgtavvg
      121 cstdeegstv hvvrpgeppv eiyrhresag vgdlshdgsl ialehtehgd amhsairvvr
      181 pdgstvaeld dtkggteelg lsvmgfapvd gdarllvghq rrgrwepmiw dpltgvetal
      241 dinlpgdvsa dwypdgsall veheyqarne lwryelgapg gkgtpagaga aaaaaggplt
      301 rvetpagsva gatarpdgtv eflwssaaqp pevrstsgev vldppgmkap gsvpvrdvwv
      361 egpggrihal vqqpagegpl ptvfdihggp twhdsdsfas spaawvdhgf avvrvnyrgs
      421 tgygrawtda lkhrvgliel ediaavrewa vssgladper lvlaggswgg yltllglgtq
      481 pdawavglaa vpvadyvtay ndemealkam drtllggtpe evperfeass pltyvdavra
      541 pvyisagvnd prcpiqqven yvqrlegrgh phevyrydag hgslvveeri kqvrleldfa
      601 qryviers
//
LOCUS       WP_457690681             405 aa            linear   BCT 27-JAN-2026
DEFINITION  prenyltransferase/squalene oxidase repeat-containing protein
            [Streptomyces sp. 900105755].
ACCESSION   WP_457690681
VERSION     WP_457690681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            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 693
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..405
                     /product="prenyltransferase/squalene oxidase
                     repeat-containing protein"
                     /EC_number="5.-.-.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40132
     Region          <63..196
                     /region_name="ISOPREN_C2_like"
                     /note="This group contains class II terpene cyclases,
                     protein prenyltransferases beta subunit, two broadly
                     specific proteinase inhibitors alpha2-macroglobulin (alpha
                     (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and
                     C5 components of vertebrate...; cl08267"
                     /db_xref="CDD:415487"
     Region          <114..154
                     /region_name="SqhC"
                     /note="Terpene cyclase SqhC [Lipid transport and
                     metabolism]; COG1657"
                     /db_xref="CDD:441263"
ORIGIN      
        1 mtvlrrtaga laatavigaa mpattalaag tmspspsass vlpsglyggs dpkfdgvwrq
       61 slallaqrav gvtpaakavd wlagqqcang afaafraapa aacdakvtvd tnstaaavqa
      121 lkavggrdaa atravswlks vqnkdggwgy tpgspsdtns tgvvvgalaa agasadrspy
      181 dllakwslpc gqdgggalay qpdkqgklaa nadataagvl galgkgfvtt agkarakdpa
      241 cagsgtartr eevarngaay ladamsksgh lvsalagaep qpdygntada vvalaaqgwt
      301 gqakkpyawl eahaapwaeq sgpaayaeli laahamgadp rdfggtnlvt alnatgpapr
      361 aagavakhae ekksgnsvww ivgtglvagv gigflfsgrr kqqql
//
LOCUS       WP_457690686             520 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457690686
VERSION     WP_457690686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56629
     Region          39..509
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 maiqrrqllr sglllgagaa lpaalasagp alaapalvrs grpalthgvq tgdvtahggv
       61 vwtradrpar mavevstrpd farsvtmpgp vltaetdftg kvklsglpag sdlhyrvrla
      121 dpgdaslvge patgrlrtap darddvrfvw sadlagqgwg inpdaggyri framaerdpd
      181 fflcsgdfwy adgvipetrt lpdgsiwrnl vtpekskvae tlaefrgqhk ynlmdenlra
      241 faaavpqinq wddhevlnnw ypgevltdtr yterrvdvla ararqalfey lpietgpsgd
      301 grvhrviryg plldvfvldm rtyrddnsan tgpatdsgil gakqvawler elaasratwk
      361 viaadmplal vvpdaaaqea iaqgdggtpl gregelarll sfihrrhian tvwltadvhy
      421 taahyydpdk aafqdftpfw efvsgplnai vanepnrldg tfgpevrfqa lapdtehnnp
      481 ayghqyfgev didgssevmt vrlrdidgkv lysvgidpqr
//
LOCUS       WP_457690690             275 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690690
VERSION     WP_457690690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29599
     Region          26..164
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpilpreqpe pspaephqar rmaasfgvda qrydqarpgy paalvtriva gspgpdvldv
       61 gcgtgiaarq fqaagcavlg vepdarmadf ararglqvev gtfeawqpag rtfdaviaaq
      121 swhwvdpvag avkaarvlrp ggrlvifghv yepptevaep faaayrravp dsplsgqpar
      181 rpldlyqaay akfadkiret eqlgdpeqwr ydweqsytrd qwldllpttg gltqlrpdql
      241 aeildavgga idslggrftm hyttlaatav ragps
//
LOCUS       WP_457690692             200 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690692
VERSION     WP_457690692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20998
     Region          8..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptgvhlrda rqqlfdaaer vllrdgpngl tsravtdeag cakgvlhrhf tdfdafladl
       61 vldraaqlet qasalresag tgtvasnlts alitlfgpip vaiiplitfr delrtrlrqa
      121 rpgggiaild qattaisayl aderelgria adadinsltl slvggghlvf adrdsgpptt
      181 avvkklvtav iadavqrrpa
//
LOCUS       WP_457690697             308 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Streptomyces nigrescens].
ACCESSION   WP_457690697
VERSION     WP_457690697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33593
     Region          1..264
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 mheyqmplpr lgsthelvig pdgnlwvsqq ledrvlrvst agrvvgitef pansrphgid
       61 kdrrghvwvt eedtnalvel satgkriary plplpgagph glrigcdght vwwtgkangt
      121 vgsfdprthr wnvhrlapds epiylargpr camffteltg srvgrvdang vvreyatptp
      181 dsrpiaiaag rhghmwftee agaayaeldp ltghitehrt dvegaklagl tfdcfgnlwv
      241 qynqpglidr vrpdlatsry tlpttapvgh riisgpdgsm wfselavdiv gsittgcptp
      301 hqrpepta
//
LOCUS       WP_457690700             122 aa            linear   BCT 27-JAN-2026
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690700
VERSION     WP_457690700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..122
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13414
     Region          15..95
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtaesqpvna pgssvtfini feisaghlda fiaqweqraa lmstksgfld srlhrarsse
       61 trfqlvnvsh wesreaweaa ttdpefrkrt qaaqddpqtq itssrglydv avefsgaage
      121 pr
//
LOCUS       WP_457690704             459 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457690704
VERSION     WP_457690704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49716
     Region          62..456
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 merndfdsla artegpvllp gqegfdeert gfnlavrhrp evivgaarae dvaaavvfaa
       61 ahdlpvavqs tghgfsvaae ggllvttrrm dgvrvdpetr sayvaagarf eqvipeaarh
      121 glaplngsap hvgvvsytlg gglallgrsh gwaadrvlam dvvtadgrlr hvtpdaepel
      181 ywallggrdn fgivtgmefg lvpvarlygg glffdveqtp glleayrqwt atvpeemnss
      241 valipfpddp qvpeplrarh vwhvriaftg saeagervve plrqagprll eslrdmpyeq
      301 sadihddppv pmpwaaddal ladldgdtvr tilehtgpga alpaivelrh lggalarrpa
      361 hpnavghrda rfmlavltpl tgdsaveaha flervfkdle pwtsgrflnf mghgetadee
      421 rtrtayttdd hrrltalkad ydprnifrln ynipprtar
//
LOCUS       WP_457690708             250 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690708
VERSION     WP_457690708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25883
     Region          2..205
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mqfsgvlfdm dgvlvdtdqa iadlwnglaa eygltisdrd faahvygcvp ehtvetvfap
       61 lapqdrakvl trvresepgl aftpvphase lvhdlagagv plalvtgasa tradralrtl
      121 gltglfgtmv twgesargkp apdcyllaar rlgippaecl vfedtsggvr aataagatcv
      181 avsrldpapl raggarhavp gfeavsfrrh aagavlnvad qedmqfsstt ghqpvtptta
      241 thteggspcr
//
LOCUS       WP_457690711             422 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457690711
VERSION     WP_457690711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43155
     Region          36..400
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mtvprrrgpt aprgtdnads sdpstlcdgp vfrrdrltal gytslaayay clyalapflt
       61 llrrdldfsy lvmslhsttf aagsvlsglf ftqalcrlgr hrlfwlsvig tacgvvllav
      121 gntvaftlaa tallgltgpm lqtsslalls vhhsshrdra lveanatasl aavlapavig
      181 slggtdsgwr aglalpvvaf vllyalgrsr plpgqgaaag plhqgrlpgr fwlrssalga
      241 aagiefgtvf ygapllvsrl dlsishaatl mtlfavgili grtagsrlvn dqgkaprllt
      301 gslllaaagl sifwsshalv lssvalliag agvanlfpls fshaiaaapd rsdhaaarnq
      361 lvvnsaimaa plalgglsdl vgvsaafavq avlivaalll vtvdraaasg gagrtplpad
      421 rd
//
LOCUS       WP_457690718             375 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690718
VERSION     WP_457690718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40711
     Region          8..323
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msltltgqdr pelqkalaei vdsgfagvql rvndergewv gsagvrklge sgkpptngrf
       61 rigsttktft atvvlqlvae gkigldspad dylprlgldr ritvrmllqh tsglfnytge
      121 yyddgtvapg ipwqgqeyvd nqfhtyqpee lvrlalskpa rcepgtdwsy sntnyvlakl
      181 lieevtgrsl aeemqrlilq plglsgtvvp gaspeipeph ahgyyryeha gqwkladvtr
      241 fnvswisaag dmisttedlh tffsalmsgk llpdsllaem rtphpklgyg lglfveetdg
      301 ggtifhhngg ffgwaalmys tpdgsktlta slttgdaeld faataaafqk ahqrlvkevf
      361 cggkaevadk akpaq
//
LOCUS       WP_457690729             266 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457690729
VERSION     WP_457690729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27611
     Region          13..254
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mkmnsehktq apvavvtgva qgigrevaev lagegyalvl adlkepvdtl aavrdagaea
       61 vavvgdiase tyvahlaeqv qerfgrvdvl vnnagvslla paedttveqw rrvlevnltg
      121 pfllsralgr qmlaagsgsi vniasiaglh giadraayna skhgmigltr tlaaewggrg
      181 vrvnavcpgw vktemdatdq asggytdsdi vdrvpmarfa apgdiaqaaa fladparsgf
      241 vngvalpvdg gwtadaswts lrlrkr
//
LOCUS       WP_457690735             499 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457690735
VERSION     WP_457690735.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..499
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=52523
     Region          14..266
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,37..38,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,75,91..94,98,100,137,139,
                     141..142,144,153..154,157,177..180)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,75,91..94,98,139,141..142,
                     144,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,98,100,137,139,141,157,177..180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(153..159,163..164,173..180)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mepleaadpr aagpyrligr lgsggmgrvf lgesgtgrrv avklvredla atpgfrdrfr
       61 reaklamrag gfwtapvvda dpdadmpwia sqyvdgpsla ervtqqgrld eeevrrlgsg
      121 laealasfhr gglvhrdlkp snvllvddgp rvidfgiskt letaggtdlt kagtvlgtpg
      181 fmspeqalgq pvgppsdvfs lgsllvyaat gagafgdgss hallfrvvye apdlsavpdg
      241 lrglvqdclh kspegrptad allahladvp ratvsdpria pkavrktvsd adapaatgpq
      301 pgsstattkp pmpaprrhrp vaeppalptf tvetwgpaaf lrrlrrpavs altitgfllf
      361 iavafngtra vlppvllstl lhllyglkvs lpllraralr veadglfvrh gphtltvpwr
      421 diasvtltgk rnrhsiavta alaegtdtrv psplragtgv lkctivsaak detstrldgl
      481 dsalrnfags ryhshpsap
//
LOCUS       WP_457690730             312 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457690730
VERSION     WP_457690730.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33038
     Region          6..303
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mnstsidprl lktllavvre gsmsgaaaal gyvpsavsqh iarlerqvgm ellsrrpggg
       61 vtptaagral adaaapvlaa tadfqrvadd iagagapelr igvyataagr llptalaelr
      121 gahpqvalym tetepvqglr alrtgeidll layrylpedp paaddlhvrg lgreplwlma
      181 aqgigpatld gcleahwaag hpgtpdrrlq qrwahrvglh psvryetddy htalaliaqn
      241 lavglvpasv vtgwhdparp ltrighlpqa qllerevltv trprsrhplv ddltdrlsaa
      301 vaavrqassr at
//
LOCUS       WP_457690749             395 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690749
VERSION     WP_457690749.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  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 395)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="glycosyltransferase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42087
     Region          3..369
                     /region_name="YjiC"
                     /note="UDP:flavonoid glycosyltransferase YjiC, YdhE family
                     [Carbohydrate transport and metabolism]; COG1819"
                     /db_xref="CDD:441424"
ORIGIN      
        1 msrflfvvpp lvghinptvg vaaelarrgh qvawagrpql veplvggrat vfpcasrqlg
       61 dpgllrpdsl rgptalkflw erffgplahd mapgvraave efrpdvliad qqavagalva
      121 ermgvpwats attsagftsl egmpkveewi agllhglrqq igapdgtadp rlsddlvllf
      181 stealvgqda slgeqvrcvg psisarptgs dfpwkrldhr rpkvlitlgt antevaprfl
      241 aecaeavrtr tdrlqaivvd psgtlpetgd svlvrrrvpq lpllervdav vchaghntvc
      301 etlwhglplv vapirddqpa vagqvtraga gvrvrfnras aahinaalda vlhdpdyraa
      361 aqrvgrsfre aggataaath leqlavrtag etrpr
//
LOCUS       WP_457690760             432 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690760
VERSION     WP_457690760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46707
     Region          64..>377
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhkdhqgser rsfatpsgga svgpgpgrka gnlptevtsf vgrrwevsea rrllartrll
       61 tltgagglgk trlalrvaae vrrsfpegaw vvdlapltdg allaqtvlta lgidhdlarp
      121 mlpvlsdhla dkrlllvldn cehlldscae ltrsllaaap hlqvlatsrq algvdgehll
      181 tvrplsapdp nrppaaaltq yeavrlfidr aaavvpgftv gddqgaavag ichrldgipl
      241 aielaaarlr vlspqqiler lhdrfallsr gssaeparqq tlraaidgsf elctpserrl
      301 waylsvfrgg fdleaaeevc tddglsqgei ldvvtglvdk siliredhrd hvrlrmleti
      361 rhygrslldq gagseeldsv vdqrtasdal hslrslrlgs clrpldaelh rkaegrpdtg
      421 cirtfrqrge vp
//
LOCUS       WP_457690752             107 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Streptomyces nigrescens].
ACCESSION   WP_457690752
VERSION     WP_457690752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 107)
  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 107)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..107
                     /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=11490
     Region          12..99
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mnsgqpttpa aaneeevfne vvgmlqavlg dygldeaeit mdtrfhedld lesidlvtlg
       61 ghlearygdt vnfaeylagl gleqiislsi gqlvehvaac lrdseeh
//
LOCUS       WP_457690763             194 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690763
VERSION     WP_457690763.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20872
     Region          2..189
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkltyfigt tidgyiaapd gdfdfftphv tedylpfltt efadalptpg raalgiadrp
       61 ntrfdtvvmg rgtydpglam gltspyaqlr qivfsgslat spdpavevtd edpltlvrkl
      121 kqedglgiwl cggadlagql lpeidelivk qypivagtgi plfradfspc tfrladsrvf
      181 eggnvvltya ktsd
//
LOCUS       WP_457690768             145 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690768
VERSION     WP_457690768.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  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 145)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=15153
     Region          11..>92
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 maeeyatrlh nelaekpldr allaclleqt epgaaiadlg cgpghvaawl aekgartvgi
       61 dlsagmieag rrrfaqvefr egdllelpak dafvapvesa aagapgrlrc atvrcrrrag
      121 sapdtaragp pcderrwtgp plvgg
//
LOCUS       WP_457690772             285 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690772
VERSION     WP_457690772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29587
     Region          37..285
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mpphstgtph disqigifms vtvpdvtrrg rpgepvffnl irsewvkart vgvtawclla
       61 ltalavgvaa lialkeqtqv prslpvlvnl sqlglsigql avvvlaatsi gseynsgmir
      121 tslvavprra rwllakafvv galalvtgmv lsvisfaivy asvpadlgtf adpqviravl
      181 gvglylgvla vlslavttiv rgtaggvvvm fvlicvvpvl vpgsalssme rflpvgmlpp
      241 naglaitqva pmfgglapwv gfavlcawtv aamaaalyrl vrrdv
//
LOCUS       WP_457690775             418 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690775
VERSION     WP_457690775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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 418)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..418
                     /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=44752
     Region          149..410
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrpdhqaspt dssrspsspa vlrpwadlpg crfrwasrrs mlfdivvalg catafvvvae
       61 fpegypfglp apvffalava aglaliwrrr wptvvclgiv aatpfqvtlf alpvslysla
      121 kygrsgrhlv alsagaglaa aiallesgla sllnrlpfmv llvtgpvllg myagarqmvv
      181 eglrekaerl ereqsllaqq trmeertria remhdvvahr vslmaihagt levdpansek
      241 tvqtaeligg igrqaleelr qvlgvlrtdd egdesaprap qptlddvpll veqsratgmr
      301 iqltqsgtvr pldtscerta yrlvqealtn vhkhapgast qvdlrytpgt lqvtvdneag
      361 ldtlptglps gghgliglre rvtvlggtfe ararpdggfr vaavlptksa attretap
//
LOCUS       WP_457690777             197 aa            linear   BCT 27-JAN-2026
DEFINITION  carbonic anhydrase [Streptomyces nigrescens].
ACCESSION   WP_457690777
VERSION     WP_457690777.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21100
     Region          1..197
                     /region_name="CynT"
                     /note="Carbonic anhydrase [Inorganic ion transport and
                     metabolism]; COG0288"
                     /db_xref="CDD:440057"
ORIGIN      
        1 mkslvdnars ftthvadrae efsaleagqs pevlfitcsd srvvpslitg arpgelfelr
       61 tagnivpeys nghptsetat ieyavrvlgv rdiivcghsh cgavnalvsg gdltdlpavq
      121 gwlehaatqp ettephspdv aeavqlhava qlerlhshpc iaerveegtl avhawyyevh
      181 tgavkqygpd dksflpl
//
LOCUS       WP_457690779             485 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces nigrescens].
ACCESSION   WP_457690779
VERSION     WP_457690779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..485
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50017
     Region          7..479
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mlstlkkpad lrrdvlaslv vflvalplcv gvavasgvpa elglitgivg gvvvgflpgs
       61 slqvsgpaag ltvlvfeavq efglgvlgai vlvaglvqla lgalrfgrff raitvavvqg
      121 mlagiglvli fgqlytmada kqprsgidki aglphlatei atsrdaltaf aigaatiavl
      181 vlwkklpaka qvvpaplagv alataatava gwtvprvevq gllsavqppg msdfaslgsl
      241 aglgtvlafa liasaeslfs aaavdrlhng prtdydkelm aqgvgntvcg vlgalpltav
      301 ivrsaanvqa gaetklsril hglwlvlfaa llpaaigiip laalagvlvh agcklipvkd
      361 llplwrehrg eavvlavtai aiittnmfeg vllgivlavi kcawetshih ldthettngr
      421 livtltgsat flrlprmlet lealphdrpv eldlselrhl dhacritlen waqqrgatvg
      481 mlakv
//
LOCUS       WP_457690794             191 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690794
VERSION     WP_457690794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..191
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20484
     Region          1..184
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mraefpdfrl gnvlatsftg tlserhgdav eriptphrlv dwlavnglav dscttaqldl
       61 arelresiht aataaasqda lpasavqlin dcsaqgraaa iltpegkrrw rlssascved
      121 alsviaadai siiagerdgk lalcasptcq aaffdtsrsr trkwcdmntc gnrqkkarfn
      181 anqrnnprsa e
//
LOCUS       WP_457690796             390 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690796
VERSION     WP_457690796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43760
     Region          <37..120
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          82..>244
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mprltsdvqa feahatdadl ddlrarlaaa rlpeaetvyr aapdprrweq gvpladlvdv
       61 vnywrtgynw rsfeerlnri gqfrttiddl gihflhrrsa radatplilt hgwpdsiarf
      121 idvvdeladp kdadapafhv vvpslpgfgy sdkpattgwg tekiaaawve lmgrlgyskf
      181 aahggdwggn ittvlggrfp ahvlgihttf aegppglttd gltaverqwa eetrdfwrhr
      241 aayakqqatr pqtigyslvd spvgllawil dkfaewsdte dspfetisrd rilddvtlyw
      301 ltrtgasaar iyyeshnsld pelrvdvpsa ltmyprdvek cprpwaqery rqivrwrtpe
      361 sgghfpalev peyfvkdlqe glaavlaahr
//
LOCUS       WP_457690804             259 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457690804
VERSION     WP_457690804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26730
     Region          11..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 misrsylsel fsldgrvavv tggssgigra iaralaraga svvivarkes elaatvdela
       61 adgcraawvs adlssrdgvr aaaeqaagvf gepdvlvnsa ginlrppmge leeevwdatm
      121 avnleapyll gqrfgpgmae rgfgrivhvt sqqahrafvq sgaygvskga leslarsqae
      181 awsphgvtcn tlvpgfvmtp lnarlssdpe kvealaartm vgrnglaedf agaavflasr
      241 assyvtgqai fvdgglsvh
//
LOCUS       WP_457690818             567 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457690818
VERSION     WP_457690818.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59131
     Region          5..564
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mgtyadlvfl ggrvvtvdaq fsvasalavt ggiisavggq ddvaplvgpg trvvdlrgat
       61 llpgindshl hgcafgmatp plsldlghpa vssladvaea vceavgrvsg gqwitghgwd
      121 tgyldecvsd psrlpsrrdl davspdhpvv lysfsghatw vnskalellg idrhtvappg
      181 gaivadeage ptgllhegaq alvqnalppl srqertdair stlatlarlg vtsytepglg
      241 pggdgimrga lgaetldiyr rlladgelta rlgvlllptg mastaaefar tltalgepgg
      301 adprrlaihg vkifadgivp nktawmhepy vgggcgslcv ggatdaeria eidamirhah
      361 aaghqlgvhv tgdraidtva dafaaamaeh prpdprhyvi hgdfltahsm kvlaahgfgv
      421 nmnptikwtv admeeefvgv graayawpyr daidagvrva sgsdapvtyp dwrqgvatmm
      481 lreskaagrv sgpeqrigla eairtytida awqdfaddwk gslepgkvad lcvldgdllt
      541 adphdipemp vvltvvdgqv vhnalrd
//
LOCUS       WP_457690822             129 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457690822
VERSION     WP_457690822.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..129
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13367
     Region          22..122
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtkntgtaaa gmvkcaafwg hdgktladfy aaalgwavtq tfgdsaamis dgatkyvfyt
       61 aesfkapdwp adelvfhldl afgdveaaek rliglgatkp ahqpggkhwt vlldpsgqpf
      121 cisaagksg
//
LOCUS       WP_457690824             128 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457690824
VERSION     WP_457690824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..128
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14471
     Region          9..120
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mkppaiapcl gvsdtqatvd fyeklgftap pagndpdddl rillfdgefa lmvyrdehlr
       61 swlpilkdtp vgafgmfyla vddfdayver irpwvtvqkd vmehhgdklf yftdpngyvi
      121 gvnqkrtr
//
LOCUS       WP_457690826             411 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457690826
VERSION     WP_457690826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15920060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="epoxide hydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45889
     Region          10..114
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          75..>246
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          100..395
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mttphpfple ptpihvsdkv lddlrarlal trppldegng dwsygvpdsy lrelvaywrd
       61 gydwrkaeaa invyehyqvs vagvpvhfmr kpgrgprpvp lilthgwpwt fwhwskvidp
      121 ladpaafggd padafdvivp slpgfgfpgp ltgfsdvnfw kvsdlwhtlm tetlgyekya
      181 aggcdiggiv ssqlghkyad elygihigsg lpldfftgpr awdfarnrpl tddqpadvra
      241 riieldhraa shlavhmldg atlahglsds pagllawlle rwnawsdngg dvesvftkdd
      301 llthatiywv nnsiatsmry yananrypwa pahdrtpvvq apvgltfvty enptgihtan
      361 ervrafktgp qadwfnhvnv nahdhgghfi pwenpdawvs dlrrtfhgrr p
//
LOCUS       WP_457690829             942 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457690829
VERSION     WP_457690829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..942
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=106866
     Region          26..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          568..936
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mpkdqdrqsp rdeepvpdvs vvvivyndad rlpravrsvl kqslrnlevi vvddcstdst
       61 savavqlkas dprirylrla qnsggcstpr nagiaiarap yvmlldsdde lprhscksll
      121 ltaertgadf vtgettrife ethtsglwyp elfdtvrliq gvreapeyfh dhlstnklyr
      181 aaflarnglr fpegihyedq lftakaltla rsfavvpwpv yiwrlaadpa tlsisssrhk
      241 lqnvrdriav armidsflee sgnadlrpak dekflrhdlr lylgdlpfrs rewteqfael
      301 mtpylgeita eavgalpreh ricqhllrsg rldeaiecar sldrpriapr qvtreagrmf
      361 wgssvpdsds tdaldisewr ldeqpfesap irhevatlap agpvvrlslr tydparllad
      421 pvevtaqlwl aatgeplkip frytpcpgea dvytaeidld lrriplgskg fkgrrhpvvt
      481 lkravvtrtd vvlatgdvpa lrahlplhgs laghvvrvgr egrgagrlef twtrsgalal
      541 aeglaprlkp vrrkarrvhr kltgraakvi ayhellrfpv dkelvlfeal eghgyadspr
      601 yiyealvrrg lplrpvwsys gdpssfpddv rlvergswdy vrtlaragyw vdshgfpsvy
      661 pkrpetrylq twhgqaikhm gfdvpelrfs sperqqqhrd misrwdvlis pseefvrtfv
      721 raneftgqll rcglprndvl vrwnepeqrg raaavrarlq ipdgrkllly aptfrdgerg
      781 tgrsirvdla elversgrew tvvvrphyye rfaiprelrh avrdgrpfcd indlllasda
      841 lvtdyssvmf dyanlarpil lftddyeeys nssrgmyysl pdiapgpmmt ttqqladalr
      901 dldrirkewa arydrfqsmf nthetghask tvvdlffggg nr
//
LOCUS       WP_457690845             300 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690845
VERSION     WP_457690845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32614
     Region          29..258
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(32,35..37,40,48,50,80,99..102,193,195,197..198,200,
                     210..211,214,229..230,233)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(32,36,40,48,50,80,99..102,193,197..198,200,210..211)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(35..37,193,195,198,211,214,229..230,233)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 mtnseieita dlvhellqeq hpdlaglair evaggwdnqq wrlgdelavr mprterapdl
       61 lrkecrwlpv laprlplpvp npvrigepsa rfpkpwtimt wvpgepldyt sisrddhaad
      121 tlagflralh veapedapis sdrgahpkkc tdgfdhffha vvpddladdv ravwddavaa
      181 pewegppvwv hgdlhpanvv vsdgtlsgvi dfgdtfagdp awdlaaawvv lpagaasrff
      241 dvyahadeat irrarglaal kslflmlmgq ngdrglpggk ptwgpagraa ldrvlrnglm
//
LOCUS       WP_457690849             400 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 1 protein [Streptomyces nigrescens].
ACCESSION   WP_457690849
VERSION     WP_457690849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Strazzulli,A., Perugino,G., Mazzone,M., Rossi,M., Withers,S.G. and
            Moracci,M.
  TITLE     Probing the role of an invariant active site His in family GH1
            beta-glycosidases
  JOURNAL   J Enzyme Inhib Med Chem 34 (1), 973-980 (2019)
   PUBMED   31072150
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="glycoside hydrolase family 1 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43840
     Region          4..385
                     /region_name="BglB"
                     /note="Beta-glucosidase/6-phospho-beta-glucosidase/beta-
                     galactosidase [Carbohydrate transport and metabolism];
                     COG2723"
                     /db_xref="CDD:442035"
ORIGIN      
        1 mtdtslrfpd gflwgastaa hqiegnnvns dwwrkehdpa akisepslda cdsyhrweqd
       61 mdllahlgft dyrfsiewar iepapgafsk aelahyrrmv dgalarglrp mvtlhhftvp
      121 qwfedrggwt adgavelfar yvencapiia dgvrhvctin epnmiavmag lakrgeqgfp
      181 paglptpdee tthaviaahh aavkavravn pdiqvgwtia nqvyqalpga eeitasyrhp
      241 redvfieaar gddfigvqsy trtkigpdgp vpapedaert ltqweyypaa vghalrhtad
      301 vigrdlpliv tengiatgdd trridyytga laavaaaied glnvqgylaw saldnyewgs
      361 ytptfgliav dpvtfertpk psagwlgalg rtrelprnas
//
LOCUS       WP_457690851             294 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690851
VERSION     WP_457690851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 294)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31517
     Region          27..294
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 msaptasaqt astpggrrre grvrrpalyv laslgllvma apflwmalsa fktrqdltas
       61 ppvwipsgwt lgnfsalldq ldmpryfvns lvvavlvtvc nllfcsmlgy alakldfsgr
      121 skvfgvvlaa lmvpgnllil plyvlmsgmg lidtyaglvl pfaasafgvf lmrqfmqsvp
      181 delleaarid gagewyifwr ivlplvkpal atltiftflg swnnfvwplv atndpgkytl
      241 pvalatfand pnrtvaggng mlmagsllvv lpvlaafvvl qrhftqgiat aglk
//
LOCUS       WP_457690853             329 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690853
VERSION     WP_457690853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35988
     Region          42..325
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mslvtgsadg aavsktrrag gakppdarsg qrggrrslsr rnlhgwlfst pflvlfgvfm
       61 lfpivatlwm sftdfgvrdv rrpleaqfvg ldnyvklfgd dtfltalfnt ayfvvfgvpl
      121 tivlgllval llnngidrar tffrvgfyap vvtsivavav vwrfvldpsd glvaglaael
      181 gtkapdflgs etwampslil mavwrnlgtv mvlfiaglqa iptevreaar ldgagawqel
      241 rritvpllrp tmlyatvitt igylnvfeep fvmtqggpsn atltvsldmy regfhffhmg
      301 yasamayvlf vvimgvtvlq lrllkdntr
//
LOCUS       WP_457690861             349 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457690861
VERSION     WP_457690861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..349
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37151
     Region          49..349
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mveradsdpt akvtaaaprw awrrsgwwap gedakrdarg psawtrgrvl aalavltagl
       61 lafhravpnt tgrlgsllea flpwlglvvv vllglallrr satalvalll pvaawtylfg
      121 glllpgtkps ahdlavvqhn agdentdpag taraladaep dlialeelvp qalpvyektl
      181 apdypyhtvq gtvglwskhp ltdarlldik praitepwsr glrtvvhtqh geiavyvahl
      241 psvrlrasgl asswrdesag llgkaiaaek lktvillgdv nstvddrgla pltsqmnaae
      301 rgfafsfpaa fplaridqvm arsatvghir tlpatgsdhl pvtaritld
//
LOCUS       WP_457690857             369 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690857
VERSION     WP_457690857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 369)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..369
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39074
     Region          7..357
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtvsgaaptv ydvaersgvs iatvsrvyrn pesvrsetre rvlaaardlg yvpsgnargl
       61 asrstgvlgl cfpdgsdpda daeaaeaadd daamlysdqi irgmeraarr hgyalliaas
      121 lkdgpeslva kvagrvdgfa vlartvptve ldvisrrqpv vmlagpregl dtadrldhie
      181 vanfdgqqel trhliqdhgv rrpayigase espdvearfr gflaacrdag veaggepvvr
      241 vgmmtqaega raaevlcera gerpdafvfa ndqmavgalh alerrgvkvp gdvvvtgfdg
      301 iplsrlvrps lttvhqpmlr mgeaavellv erlsgsrtgd pvsvmlpvtv vrrascgcgd
      361 eepvspder
//
LOCUS       WP_457690867             688 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457690867
VERSION     WP_457690867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..688
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74169
     Region          88..>306
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 magnnsglin tgeivtivsg ssrypdtlte nlhtltqrvl adlgqdqvqq qlrsghplpv
       61 hcraapeelt ggrngarets aaladaspld lagplkniaa vymeesrsql lvlgragsgk
      121 ttlirrfaqa rledadwtgk elvpvifslg swdptatslr dwlidrlerd hpflarrrry
      181 krtwateliv mghvlaildg fdemaedlyq palrhlgafn lpllltsrhe alrgikpseg
      241 lfpgieltdl tfddcsarld astgwapvld rlsshsgepa aarlatvltt plmltmaeaf
      301 hasggdpecl lklaesssqd alekrlldaf vprtydpvln lsvperrrws aeraghwlgy
      361 lathlkkqkt daqkpdahai gaqdiewwql gttmslparm lvsgglcglv sgtavalvha
      421 lmsdppaall smflnvlgig lafgilhgfa skievggafk psrmqirvrg esrrvrsrrv
      481 resllprvgg glagglvfgi vfgggfavya mllsypwplv alllgnwlva gpllglaagi
      541 vvalvawlet dakpeesvsp tdllrtnrti vlvqaavvgl vlglgygtav thfngfalgl
      601 pagigtglaa avggctltaw grwvvlvrlw lplsgrlpwr vnaflddara rgvlrqagav
      661 yqfrharlrd rlaeahrqhd qpteggsr
//
LOCUS       WP_457690876             152 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces nigrescens].
ACCESSION   WP_457690876
VERSION     WP_457690876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=15328
     Region          8..>98
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 msapgagpap dgpgqllvlh haggsagpyq rlvralaarg reavavdlps rgrsageppr
       61 rsvaeavdhl vevvtqdfep gcalfghsmg gllafetagt wnasagrwag waslaaappl
      121 rrpwlprrig tggattgsgg tsvssaaprr rp
//
LOCUS       WP_457690870             219 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent F420 reductase [Streptomyces nigrescens].
ACCESSION   WP_457690870
VERSION     WP_457690870.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23223
     Region          15..197
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkigiigagn iggnltrrlt alghevavan srgphtltsl aeetgatptt vaeairgaev
       61 vvvtvplkav phlpsglwde aaenvavidt gnyypkerdg riaaiedglt esrwteqhig
      121 hrvikafngt yaqdildkpr pagdperial pvsgddeaak hvvrelidel gfdtvdaggi
      181 dtswrqqpdt pvyglragve evtkalaeas perpeafra
//
LOCUS       WP_457690880             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690880
VERSION     WP_457690880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27699
     Region          23..237
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtahslaphe lrtttgiaaa ttdlskvygs gdtrvvaldr vsiafregef taimgpsgcg
       61 kstlmhcaag ldspssgsvr vgttelstld drqltalrrd rigfifqafn llptltalen
      121 itlpltiagr kpdqqwldrv vsmvglsqrl ghrpaqlsgg qqqrvavara lasrpaiifg
      181 deptgnldsr sgaevlgflr dsvrelgqtv vmvthdpvaa gyadrvvfla dgllvddmps
      241 ptpgrvldrm kdfdtrsrts
//
LOCUS       WP_457690878             841 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457690878
VERSION     WP_457690878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 841)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 841)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 841)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..841
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86647
     Region          2..832
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mfrtalrnvf ahkarllmta favmlgvtfi tgslvygdsl nqattakatd gyeriavnvd
       61 vsadpanrgr pggldartvt alaklpgvaa aagrvdgfaa vadrdgkplg ngqdarggnf
      121 apaadgkdpa yrftggsgpt gkdtialdea taaqggyrvg dtvrvgtnkg assytlsgif
      181 radgtklpgg gsltlfagat aqklfyepgr yqdieltatp gtdatqllsr vesvlpkgts
      241 avtgaqlaqm qahlatsrts tmsqilvgfa avalfvatfl iantftmlva rrtrelalmr
      301 avgatreqvr rilltesllv gaiasvagla vgtgvaallq tlfadtpapl vltpttvlis
      361 mlvgtllpmv aawlpirram aippvaalsa aehtaparpg slrtglsaal vltgsaavvy
      421 galttekdar tviglgaala ltgtiglipl lsrpvvtlfr plltrlapvh gdlairntvr
      481 dprrtgataa alaialtlas glsvlgasat qyldrattha lsadyvvksa ggqgmtptta
      541 aplkklagat ysplnqstey ylggsksvlt gvdpatigkl lrydviegsl dslakgqiav
      601 adfkaeqegw hvgqtlplkr qndqhgslti gaiyqadeqs dlmpsitapd slvarydstp
      661 stdrilvatd ggtsraarag vthalgdnpt lsvldqadir aqdsrgigdq lnvfyallsm
      721 alviaalgia ntlamsvler rkelgtlral gldragvtrm irlealllga lgatlgtvmg
      781 vflgwavgrt lqanvagyel vlpwgrlalt ilialtgsll aslwparraa rvdipaataa
      841 q
//
LOCUS       WP_457690883             432 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457690883
VERSION     WP_457690883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Wolanin,P.M., Thomason,P.A. and Stock,J.B.
  TITLE     Histidine protein kinases: key signal transducers outside the
            animal kingdom
  JOURNAL   Genome Biol 3 (10), REVIEWS3013 (2002)
   PUBMED   12372152
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   4  (residues 1 to 432)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45719
     Region          136..419
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrpfhrlrpd raslrwkiaa laaataclvv tavgvlvhlw tardirdraa mqafngvysa
       61 mdvyrrtgal vdgaeldpae lpavlrhpad gdrhtaydgg vegnvgpsvw aaqrtggpgs
      121 pvltlqvsmg pqlhdlrrld vtmavvsliv lsaatplavy gaallarrlr qvsetagris
      181 agdldartgp tkgrdevadi aatvdlmads lsrrlrterq ftadvahelr tpvggllaaa
      241 dlmppgeted llrarvrdlr glvedlleis rldagadepv rahvplgavv seavartgfd
      301 tevtvadpqr aeadrtvetd prrlerivsn lvvnahrhgd tpvqvtvegr tvvvrdhgpg
      361 fpadllrhgp rrfqtgater gkghglglti alaqaqllda elrldnapdg gavatlrlps
      421 rpsgsggtaa sa
//
LOCUS       WP_457690891             151 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457690891
VERSION     WP_457690891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..151
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16655
     Region          6..107
                     /region_name="Glyoxalase_4"
                     /note="Glyoxalase/Bleomycin resistance protein/Dioxygenase
                     superfamily; pfam13669"
                     /db_xref="CDD:463951"
ORIGIN      
        1 mtafyhvcfv vpnleramqd fqraagvews dpvadrlgew dyrivfttgg ppfieliegp
       61 sgspwdaskg arfdhigfwt sdvrqgsqrl eevgmpvdfs gcpygrpfvy hqmdsvgari
      121 elvdvgrqas flngwspggk pmpaidepsr s
//
LOCUS       WP_457690913              87 aa            linear   BCT 27-JAN-2026
DEFINITION  lamin tail domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457690913
VERSION     WP_457690913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Eldirany,S.A., Lomakin,I.B., Ho,M. and Bunick,C.G.
  TITLE     Recent insight into intermediate filament structure
  JOURNAL   Curr Opin Cell Biol 68, 132-143 (2021)
   PUBMED   33190098
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Dittmer,T.A. and Misteli,T.
  TITLE     The lamin protein family
  JOURNAL   Genome Biol 12 (5), 222 (2011)
   PUBMED   21639948
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Dhe-Paganon,S., Werner,E.D., Chi,Y.I. and Shoelson,S.E.
  TITLE     Structure of the globular tail of nuclear lamin
  JOURNAL   J Biol Chem 277 (20), 17381-17384 (2002)
   PUBMED   11901143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..87
                     /product="lamin tail domain-containing protein"
                     /GO_component="GO:0005882 - intermediate filament
                     [Evidence IEA]"
                     /calculated_mol_wt=9951
     Region          <2..82
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
ORIGIN      
        1 mkntgrlpvn ikgwtlsdks shsyrfgnlr lnghsqirvh tgighdnrrd vyqdrrayvw
       61 dntgdtatlr ndhrrvvdaa swgrrgh
//
LOCUS       WP_457690918             165 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457690918
VERSION     WP_457690918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17820
     Region          <43..154
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrfvelsstt mvallkddla qasaeagval teyfvtdtak wvwqyrvnql tsdrgcagwl
       61 tqivvaepag avvgyagfhg ppdeagmvel gysvipvyrr qgyasvmlta lvrravtear
      121 vrtvrvtisp dntaslatis gfgfvevgeq wdeedgleli fevpv
//
LOCUS       WP_457690968             208 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457690968
VERSION     WP_457690968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22476
     Region          5..131
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mglreskkqe trqlisdcat rlfieqgfeq ttiaeiaaaa rvskktvtny fprkedlald
       61 hheaftegla rtvaeresge epltalgrmf rtalqehspv vgftgpafar mvadsptlta
      121 rlrelhdqre ealaaaltaa apapdpaiap ragaaliaaa drllfrriqe ltlaghtddq
      181 ieatlipead hlrtllaaal gnhptgrr
//
LOCUS       WP_457690969             305 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457690969
VERSION     WP_457690969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32172
     Region          2..215
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mleargltka yggkravddl sftvrggqvt gflgpngagk sstmrmflgl dhpesgsalv
       61 ngrpfhelrh pmhevgamle akaahpgrsa yghllalays ngigrrrvse vleitglgtv
      121 agkriggfsl gmsqrlgiaa allgdpqvll fdepvngldp egvrwirdlm kglafegrtv
      181 fvsshlmsem eltadhlvvi gqgrliadag vqevigsgsr ravkvrtpqa nqlcaqlrqa
      241 ggevtvdgad tlvvagldaa risamafqcg aelhelseqh vsleaafmel tghsveyrtg
      301 tpdki
//
LOCUS       WP_457690976             302 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457690976
VERSION     WP_457690976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5) (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=31537
     Region          19..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          157..291
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mrdaiestgp vvvgvetesd taravvrhaa rqaelhgnpl hllhalegap pgrardedsg
       61 rtsadaqgaa vverlaawah sefpnvavta qtvpgraaee llarsaeaat lvlghrgtgg
      121 farlplgsvs wqvathaacp vvivrpgeta erpearvvvg vdindvseea vdtafaeaal
      181 rgarlemvha nlhlsempvg pgmaapnfea ldeaarqiln aeatqraery pgvevltrve
      241 rvrpstilae asrrasllvv gshgrtglrr lmlgsvsaea lhtaacpvmv vptvednrig
      301 aa
//
LOCUS       WP_457690981             501 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces nigrescens].
ACCESSION   WP_457690981
VERSION     WP_457690981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52206
     Region          22..493
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mstsalspaa rlrslrpdwl ndpkvwrtei lgglvvalal ipeaisfsii agvdpaiglf
       61 asftmavtis ivggrramis aatgavalvi aplnrehglg ylvaavilag vfqvilgalg
      121 vaklmrfvpr svmvgfvnal ailifmaqvp emhvvpwpvy pliaagltlm mffpkvtkvi
      181 paplvsivil tvitvaagia vptvgdkgel psslpvpglp dvpfttdtlt tiapyalama
      241 lvglmeslmt aklvdditdt hssktresig qgianivtgf fggmggcami gqtminvkvs
      301 gartrlstfl agsflmvlcv vfgpvvsdip maalvavmvm vsfatfnwhs iapktlkrmp
      361 ageiavmvit vacvvatdnl afgvvvgsvt amvifakrva hlanvtavtd pdgssvvysv
      421 tgelffassn dlvgqfnyat dpdkividlt aahiwdassv aaldaietky kqrgktveii
      481 glndpsaqih eklsgeltga h
//
LOCUS       WP_457690986             453 aa            linear   BCT 27-JAN-2026
DEFINITION  dicarboxylate/amino acid:cation symporter [Streptomyces
            nigrescens].
ACCESSION   WP_457690986
VERSION     WP_457690986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..453
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47403
     Region          52..429
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mstsaetaes sqapqspqss ripkipfwaq ilaglalgvl lgwiaksgdv gwltatlqhi
       61 gdlfvqllkl avaplvffai lvsitnlrqv nnaarlasrt llwfmvtsli avaiglaigl
      121 ltnpgagtgl tpkdgkapee agswidfltg ivptdiitpf telnvlqivf maaiagiaal
      181 qlgekaepvl kisrsvlell qkalwwvirl apigtvglig haiatygwnl igkyatftvd
      241 iyvgcalvlf gvyplllstv akvnplqffr gawpaiqlaf vsrssvgtmp vtqqvterlg
      301 vpreyasfav pfgsttkmdg casiypaiaa ifiaqifdvh lgigdyllia fvsvigsaat
      361 agltgatvml tltlstlglp legvgllmai dpvldmmrta tnvagqsvip ilvsarekil
      421 drdayngaqg igvetagaeg aeekvsvpvp saa
//
LOCUS       WP_457690989             559 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarate hydratase [Streptomyces nigrescens].
ACCESSION   WP_457690989
VERSION     WP_457690989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   van Vugt-Lussenburg,B.M., van der Weel,L., Hagen,W.R. and
            Hagedoorn,P.L.
  TITLE     Biochemical similarities and differences between the catalytic
            [4Fe-4S] cluster containing fumarases FumA and FumB from
            Escherichia coli
  JOURNAL   PLoS One 8 (2), e55549 (2013)
   PUBMED   23405168
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Flint,D.H.
  TITLE     Escherichia coli fumarase A catalyzes the isomerization of enol and
            keto oxalacetic acid
  JOURNAL   Biochemistry 32 (3), 799-805 (1993)
   PUBMED   8422384
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11487765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..559
                     /product="fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /calculated_mol_wt=60302
     Region          1..541
                     /region_name="PRK15389"
                     /note="fumarate hydratase; Provisional"
                     /db_xref="CDD:237955"
ORIGIN      
        1 mpefaytdll pvgedntpyr lvtsegvstf eadgrtflkv epealrklaa eamhdishyl
       61 rpahlaqlrk ilddpeasan drfvaldllk naniaaagvl pmcqdtgtai vmgkrgqnvl
      121 teggdgeals rgiydaytql nlrysqmapl tmwdekntgs nlpaqielya tdggaykflf
      181 makgggsank sflfqetkav lneasmmkfl eqkirslgta acppyhlaiv vggtsaeyam
      241 ktakyasahy ldelpaegsp tghgfrdkel eekvfeltqk igigaqfggk yfchdvrvvr
      301 lprhgascpv aiavscsadr qavakitaeg vfleqletdp arflpettde eltegagpdl
      361 davaidlnrp mddvlaeltk hpvktrlslt gtlvvardia hakikerlda geempeylkn
      421 hpvyyagpak tpegyasgsf gpttagrmda yveqfqaagg skimlakgnr sqqvtdacgt
      481 hggfylgsig gpaarlaqdc ikkvevleye elgmeavwki evedfpafiv vddkgndffq
      541 dpapaptfts ipvrgpgla
//
LOCUS       WP_457690996             496 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457690996
VERSION     WP_457690996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..496
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49713
     Region          26..483
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgtggtgeg gaadgaedgt aregadsgap galrrtltfr dllvygllfi apmapvgifg
       61 tlqatshgai tlvylaatva maftaysyaq mvrvaprags vytyarvglg egagfvagwm
      121 amldyllipa vaylfsgial halvpsvhpw vwtalavavt tllnlsgvrt aaragfvvla
      181 meivvlavfv vsavvelvvh gaprgwaepl tgeggfspga vlaavsvavl sylgfdaias
      241 faeeagggqg grgpggpdrv aravlsclvv agvlfavqty laallmpmsa aelaarpaeq
      301 gaafyatvds avgrwlqdlv avskavgaaf aalagqaaag rllfamardr rlpgamskvd
      361 agsgvprral lgaalvtlva avgaarrddg laqlssivnv galtafgllh asvigwfwir
      421 grrgrpllgr sgepgggtps vlrhavvpll glavvvavvv easataqlvg gvwlvaglvv
      481 lavqhggrar aggaqg
//
LOCUS       WP_457691012             249 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691012
VERSION     WP_457691012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..249
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26581
     Region          16..236
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 msaephlspm prdwqralav vahpddleyg aaaaiaewta agrqvsyllv trgeagidgl
       61 apaecaavre teqragaalv gvhtvefldh hhdgviesgp alrrdlaaai rrhrpellvt
      121 lnhhdtwggv qwnsadhrvv gravldaagd agnrwifpel agaqglapwn gvrwvavaas
      181 pypthaaevg pgidravdsl aahstyikgl ggagqdpray arsfieqtlr sggeryrgrp
      241 atlfqlfpr
//
LOCUS       WP_457691005             255 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457691005
VERSION     WP_457691005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26720
     Region          2..254
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 magpvqsier aaailrllas gprrlglgev aaslglakgt thgilrtlqn idfveqdpat
       61 gkyqlgaall hlgtsyldvn elrsrsinwa dalaarsgea vrlgaplegk vlivhhvfrp
      121 ddtfqtldvg allplhassl gkvllafgsv plepaveagl eaytrhtlvd perltralte
      181 vrelgwaaev qemitdeagv aapirghggl vvgaigasgt vericdsqgv pqpalvtqvr
      241 haaraisrdl gaarw
//
LOCUS       WP_457691007             140 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691007
VERSION     WP_457691007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..140
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14664
     Region          19..137
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtaqldavvr eadehvcplp hipeavsvvr rrartvladw niapdlteda llviselitn
       61 avvhalppav lrlsrvvdgs halrvevtda gaaaadgrpv vepdadehgr gldivtalaa
      121 ecgtrvhagg itwwakllaa
//
LOCUS       WP_457691014             250 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457691014
VERSION     WP_457691014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27040
     Region          4..250
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpfgeqpayl rvagdlrqki vegvlpphtr lpsqariree ygvsdtvale arkvlmaegl
       61 vegrsgsgty vreqpvprri arvgfhsagg ctpfrqeqtd ervrgtwesn seqeaagsvv
      121 aarlripqga kvmrtryvfr aegepsmlst sweplevtgr tpvmlpeegp lagrgvverm
      181 aaidvvvdnv veevgarpal aqeamtlggv pghavlvvsr tyfaggrpve tadvvtladr
      241 hrvayhlpvk
//
LOCUS       WP_457691016             567 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457691016
VERSION     WP_457691016.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60268
     Region          10..461
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msttktpsae qgshsnyrrs lgtialtatg lgsiigsgwl fgaeraaaia gpaailawvi
       61 galvaltial tytelgsmfp kaggmvrygq yshgslagyl aawanwiaiv svipgeatas
      121 vqymsswdfg wahalydgke ltgtgvglas vllifyffln wfaislfakt ntaitvfkvi
      181 vpamtagalm lahfdtdniv hhggftpngw ssvftavavs givwayngfq splnlaaear
      241 npgkslpkav vwsivialvi yvalqvaflm avpgdklaag ggwaglgfns pladlaiawg
      301 lnwlalllya dafvspsgtg miyaattsrm ihgvqenghl pgifgkvdkk tgvprpalll
      361 nlviaflfla vfrgwgslae ivsvatvisy itgpvavmsl rrvspdlkrp vklkamplia
      421 piamifgslv lywgrwpltg kvilimavgl pvwawyeigk pltqgrkpwa alrphlkaga
      481 wmvayllvma svsymggkdf ggkgylpegw dillvaaigl afyywgvrss wrnptliqae
      541 aeiraedear eadeareteg vkapvga
//
LOCUS       WP_457691019             140 aa            linear   BCT 27-JAN-2026
DEFINITION  (deoxy)nucleoside triphosphate pyrophosphohydrolase [Streptomyces
            nigrescens].
ACCESSION   WP_457691019
VERSION     WP_457691019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..140
                     /product="(deoxy)nucleoside triphosphate
                     pyrophosphohydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15283
     Region          5..124
                     /region_name="NUDIX_MutT_NudA_like"
                     /note="MutT pyrophosphohydrolase; cd03425"
                     /db_xref="CDD:467531"
ORIGIN      
        1 mttvrvvvgg avcergrlla arrsappala grwelpggkv eddetperal erelreelgv
       61 eaaaleripg ewvlrpgyvl qvwtarlvsg aprplqdhde lrwllpgeen qvdwldqdrp
      121 avaeamrrla apagatgvrp
//
LOCUS       WP_457691028             798 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter family substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691028
VERSION     WP_457691028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Lewis,K.M., Greene,C.L., Sattler,S.A., Youn,B., Xun,L. and Kang,C.
  TITLE     The Structural Basis of the Binding of Various
            Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA
            from Chelativorans sp. BNC1
  JOURNAL   Int J Mol Sci 21 (11) (2020)
   PUBMED   32486296
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Marland,Z., Beddoe,T., Zaker-Tabrizi,L., Lucet,I.S.,
            Brammananth,R., Whisstock,J.C., Wilce,M.C., Coppel,R.L.,
            Crellin,P.K. and Rossjohn,J.
  TITLE     Hijacking of a substrate-binding protein scaffold for use in
            mycobacterial cell wall biosynthesis
  JOURNAL   J Mol Biol 359 (4), 983-997 (2006)
   PUBMED   16698034
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..798
                     /product="ABC transporter family substrate-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83959
     Region          65..781
                     /region_name="PBP2_Lpqw"
                     /note="The substrate-binding domain of mycobacterial
                     lipoprotein Lpqw contains type 2 periplasmic binding fold;
                     cd08501"
                     /db_xref="CDD:173866"
ORIGIN      
        1 mtdhdhpagr ravcrrrrca aliaagvllp lpalagcsed dreasvaasq diapaprsal
       61 knggtlrwav dampgtlnaf qsdadattar iagavlpsmf tidasgrpqr nadfldaadi
      121 strdpkqvvt ykinpkarws ngtaitaadf vaqwtalrgk dnaywtarna gydrigkveq
      181 ganahevkvt farpyadwrs lftplypknv mgsanafndg arerlkvgag pflvqkrdak
      241 esrvilvrnp rwwgepaklk rivlqslpgd kraaalaegs vdvaavdqia akrvasarrp
      301 aspgsprtpa egnagpqssg dragartgak aaaaensllr gytirkalep aytqlalngs
      361 sgpladdrvr ravaraldrq aladtvlkpl dlpskplgsh llmagqygya dhsdalgeqd
      421 agaakallad agwksdgadr qqagqkagap apdgypdedg depsddrhag dryddesded
      481 lpdgdsddrn paragrvhag apgrgerpaa aeaplsftga vgsevqqsal lrqsasfykq
      541 aaasekadad gdtgsaayak ykrykkraae algaaeliet gqgpqlpgsg ghpgarhaav
      601 eraadaaaap qpadgktsrv aavkkngkpl tlrfvvpdga gseqlrtvgr riasmlgkig
      661 iqsslqrvsd asyfqdhiag gdydlalysw pgtaypatda rpiyakpqpa pdgsltveqn
      721 ytrvgtdhid qlfdqaasel degaahtlva qadariwaaa gsiplyqrpe lvatkkslan
      781 vgafgfatpr fqdigyqk
//
LOCUS       WP_457691032             539 aa            linear   BCT 27-JAN-2026
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691032
VERSION     WP_457691032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 539)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 539)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 539)
  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..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /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=58753
     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 mrratcakwg acavavalva tgcgggsgas rsgvvsaswg dpqnplepan tnevqggkvl
       61 emlfrglkry npktgaaenv iadrietkds qnftvtlkgg wtfsngekvt aksfvdawny
      121 gallsskqkn apffqyidgf akvhpdrgtp qaktlsglvv kddrtftvrl nqkfsswpdt
      181 lgysafmplp qaffrdhdaw iekpvgngpy tvdsyekgsv lrmrkwdayp gddparnggi
      241 dlrvytdnnt aytdlqagnl dlvddvpaaq lknvqadlgg ryinqpagii qtltfpmydk
      301 rwsrpgtekv rrglsmaidr dqitreifqk trtpatdwts pvlgadggyq agvcgeacef
      361 npakakqlik eggglpggri altynadtgs hkdwidalcn sinkslgddq acvgdpvgtf
      421 adfrnkitak rmsgpfragw qmdypliqnf lqplyytnas sndgkfsnas fdklvneana
      481 dtdpqqavrt fqdaekilaa qmpaiplwyq ngsggysdri snvslnpfsv pvyneikvn
//
LOCUS       WP_457691038             339 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691038
VERSION     WP_457691038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36580
     Region          15..333
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtnedarstg adtalldvrd lrvefrtrdg vakavngvsy rvapgqtlav lgesgsgksv
       61 taqavmgild sppgfvtgge ivfqgrdllt lrkderrrir gakmamifqd alsalnpvvs
      121 vgaqlgemfq vhegmsrkds rgravelmer vgipaarerv gdyphqfsgg mrqrimiama
      181 lalgpdliia depttaldvt vqaqvmdlla elqreltmgl ilithdlgvv advadtiavm
      241 yagrivetas vhqlyrapah pytrglldsi prldrkgrrl yaikglppnl taippgcpfh
      301 prcplaqdic rtdppplyea gpgrasachf wketldgar
//
LOCUS       WP_457691036             330 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691036
VERSION     WP_457691036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34194
     Region          52..326
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mpesyvpkea ighgdggsaa laigeaesle rrpgaappgg gppggvpvgk prslwsdawh
       61 dlcrnpvfvv salvivflvi iaiwpqliat gnpyradlak aqqgsqpghp fgfdtqgrdv
      121 ytrvvygara sitvgvcatt gaallgsllg glagffggwg dtllsrladi ffgipvilgg
      181 lvflsmvtgt tvwpvvgfiv llgwpqisri argsvvtakq ndyvqaaral gagnrrlllr
      241 hiapnavapv ivvatialgt fialeatlsy lgaglkppti swgidistas tyirsaphml
      301 lwpagalsit vlafillgda vrdaldpklr
//
LOCUS       WP_457691039             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691039
VERSION     WP_457691039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38763
     Region          11..351
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mahgddggpa agsgtpilev rdlvkhfplt rgvlfrkqvg avkavdgvsf dlhqgetlgi
       61 vgesgcgkst vakllvgler ptagriryrg edistlsara lkavrrniqm vfqdpytsln
      121 prmtvgdiig epyeihpeva pkgdrrqkvq ellevvglnp efihryphqf sggqrqrigi
      181 arglalrpei ivadepvsal dvsvqaqvvn lleqlqhefe lsyvfiahdl svvrhisdri
      241 avmylgrlae tgtdeqiyeh pthpytqall savpvpdpda rthrdrilla gevpspanpp
      301 sgcrfrtrcw kaqqlctdvv ppldvprefr etagpaghas achfaeerhv vpse
//
LOCUS       WP_457691041             379 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691041
VERSION     WP_457691041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..379
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41000
     Region          15..351
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 maenvtlpap rdaaptpgep lltaegltkh fpiyggfpfk rkvgavqavd gvdltvhage
       61 sfglvgesgc gksttgrllt rlmeptsgki tyagqditra grkdlapirs eiqmifqdpy
      121 aslnprqtvg tiiggpmein ginptggrek rvqelletvg lnpehynrfp hefsggqrqr
      181 igvaralale pklivadepv saldvsiqaq vvnllqklqr elgiaflfia hdlaivrhfs
      241 ervavmylgk ivevgtrdei yhrprhpyth allsavpeak lveseeedre rirlagdvps
      301 pvnppsgcrf rtrcwkaqdk cateepplvq iggneaghlt achfpeeptt aargediild
      361 palaaieeaa eaadtgkte
//
LOCUS       WP_457691042             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691042
VERSION     WP_457691042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38120
     Region          20..338
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttltktedt pvptgsdpfl svrdlhvrfs tedgivkavd glsfdlergq tlgivgesgs
       61 gksvtnlail glhnpkntel sgeitlegqe ltgarektle klrgnkmami fqdaltalsp
      121 yytvgrqiae pfikhtgask regrqraiem ltkvgipqpg lrvddyphqf sggmrqrami
      181 amslvcnpel liadepttal dvtvqaqild llkdlqqefg saiilithdl gvvantaddl
      241 lvmyagrave rgsvkeiltq pqhpytwgll ssmprltsdv heelhpipga ppslltppsg
      301 cgfhprcgft gevggarctd erpllelgra aachlsaeqk qtlfteqikp rlg
//
LOCUS       WP_457691048             344 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691048
VERSION     WP_457691048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37394
     Region          35..339
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtspsqtaat esdtpgldsk glkktkdgkd gelvgrspgq lmwrrfkrdr tgvicavvvl
       61 affvvaalap viaklygknp ytfygnedps lfdefgypmg pnggisgdfw fgiepalgrd
      121 lftsllygmr tslgisvavt ilvvitgtll gvtagylggr tdywlgrvid fllafpsqlt
      181 fvafmpvvva ffippgdetp tyvrvvalil vqwalgwmgl arllrgqvls lrerefveaa
      241 kitgaspwri irkellpnvv tpilvqatym lplfvtaeag lsflgvgime ptpdwgrlfh
      301 tagmvyendp tfllfpgaam vifvlcfnll gdsvrdafdp ksgr
//
LOCUS       WP_457691060             378 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457691060
VERSION     WP_457691060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=40991
     Region          2..361
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 maadrptqsr rlapvllila ilvvtvldst tgpelhisaf mgiaplyaal rcpfrqtllv
       61 aavfvvclty vdiftvpdwa pasrvvgifg vflvaafslv lcrtrlqrea lhartslvad
      121 tvqramlrel plsagpvday gfyvsaeega rvggdiyeas dtpyglrlmi gdvqgkgmpa
      181 igaglevlvs freaaqhqes lesvvermeq alaryntrsa eegtderfvt allmevrgtd
      241 gaaegrvlsc ghipyylvrh grvherrdge galplglgal sgeprhsvrv hpepcdwvvl
      301 ctdgvtearg kdgefyplae rlarwthlep aelartlrad lesftggrlk ddatvlvvrr
      361 rehpapdaql smaraaaa
//
LOCUS       WP_457691064             357 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457691064
VERSION     WP_457691064.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..357
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37385
     Region          <270..340
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(289..291,301..302)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 meflaggrae vritradvgk rvsvrrltgg gagvpaftda vgvltswdqg vlsitrrsge
       61 tvrieesalv aakvvpdrpa tarqgaarps sgeparrrgp aatalelqtv aargwpavet
      121 arlgewtlra sggftrrans vlplgdpgvp letalerigq wyderglppv ilvatgradt
      181 gerlaaelae rgwtderhtt vriaalapla dtgadlsrva lsrepgadwl alynrtgaae
      241 psaeaartal qvltggpsvw fatvhgadgg taaigrlvvd grwagfaale vapaarrqgl
      301 atlvmaalae raleegasaa ylqveadnag alafydrlgf tdhhgyhyrr alpggrr
//
LOCUS       WP_457691076             201 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase I [Streptomyces nigrescens].
ACCESSION   WP_457691076
VERSION     WP_457691076.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..201
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=21889
     Region          8..198
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 msgvvrepdg iprcpwgmes aqmadyrayh dtewglpvhg ddalfermsl eafqsglswi
       61 tilrrrpgfr aafagfhipk varftdadae rlltdpgiir nrakivatin nakiadglap
      121 gelddliwsy apdragrpvp rtvsdlqptt pestalskdl kkrgfrfvgp ttayammqac
      181 glvndhlaec hvraaveaaa g
//
LOCUS       WP_457691079             227 aa            linear   BCT 27-JAN-2026
DEFINITION  O-methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457691079
VERSION     WP_457691079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  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 227)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24056
     Region          75..227
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mrqlrgqera itgnrqtsla faeaygagti ddsaeaalhw srdrareagi rtvttgtgaa
       61 lrllaaavda kavaeigtgt gvsgiyllhg mrpdgvlttv dleperqtfa kqafraagfa
      121 gnrarfipgr aldvlprlad ggydlvycdg dlmecleyla eslrllrpgg lvcfegvfad
      181 grtvdsavqp aevlrlrell ravresttlv psllpvgdgl lcavkrg
//
LOCUS       WP_457691086             386 aa            linear   BCT 27-JAN-2026
DEFINITION  Mrp/NBP35 family ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691086
VERSION     WP_457691086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Bych,K., Netz,D.J., Vigani,G., Bill,E., Lill,R., Pierik,A.J. and
            Balk,J.
  TITLE     The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1
            partner in the green lineage
  JOURNAL   J Biol Chem 283 (51), 35797-35804 (2008)
   PUBMED   18957412
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Swartz,T.H., Ikewada,S., Ishikawa,O., Ito,M. and Krulwich,T.A.
  TITLE     The Mrp system: a giant among monovalent cation/proton antiporters?
  JOURNAL   Extremophiles 9 (5), 345-354 (2005)
   PUBMED   15980940
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Vitale,G., Fabre,E. and Hurt,E.C.
  TITLE     NBP35 encodes an essential and evolutionary conserved protein in
            Saccharomyces cerevisiae with homology to a superfamily of
            bacterial ATPases
  JOURNAL   Gene 178 (1-2), 97-106 (1996)
   PUBMED   8921898
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="Mrp/NBP35 family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0140663 - ATP-dependent FeS chaperone
                     activity [Evidence IEA]"
                     /calculated_mol_wt=39945
     Region          5..98
                     /region_name="PaaD"
                     /note="Metal-sulfur cluster biosynthetic enzyme
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2151"
                     /db_xref="CDD:441754"
     Region          120..366
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(129..136,261,263,288..289,331..333,336..337)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(129..131,160..161,163,166..167,207..208,238,240,243,
                     267,270,332,334..335,337)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
ORIGIN      
        1 matdtphgat psedavrdal atvndpeihr pitelgmvks vdiaadgava vvvyltvsgc
       61 pmretitnnv reavervegv ssvaveldvm sdeqrkelat slrggtaere vpfaqpgslt
      121 rvyavasgkg gvgkssvtvn laaamaadgl kvgvvdadiy ghsvprmlga ygkptqvenm
      181 imppsangvk visigmftpg napvvwrgpm lhralqqfla dvywgdldvl lldlppgtgd
      241 iaisvaqlvp naeilvvttp qqaaaevaer agsiavqthq kivgvvenms glpcphcdem
      301 vdvfgtggge rvaegltrtt gtqvpvlgai pidvrlregg degkpvvltd pdspagsair
      361 siagklggrq rglsgmslgi tprnkf
//
LOCUS       WP_457691097             194 aa            linear   BCT 27-JAN-2026
DEFINITION  suppressor of fused domain protein [Streptomyces nigrescens].
ACCESSION   WP_457691097
VERSION     WP_457691097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Das,D., Finn,R.D., Abdubek,P., Astakhova,T., Axelrod,H.L.,
            Bakolitsa,C., Cai,X., Carlton,D., Chen,C., Chiu,H.J., Chiu,M.,
            Clayton,T., Deller,M.C., Duan,L., Ellrott,K., Farr,C.L.,
            Feuerhelm,J., Grant,J.C., Grzechnik,A., Han,G.W., Jaroszewski,L.,
            Jin,K.K., Klock,H.E., Knuth,M.W., Kozbial,P., Krishna,S.S.,
            Kumar,A., Lam,W.W., Marciano,D., Miller,M.D., Morse,A.T.,
            Nigoghossian,E., Nopakun,A., Okach,L., Puckett,C., Reyes,R.,
            Tien,H.J., Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T.,
            Xu,Q., Yeh,A., Zhou,J., Hodgson,K.O., Wooley,J., Elsliger,M.A.,
            Deacon,A.M., Godzik,A., Lesley,S.A. and Wilson,I.A.
  TITLE     The crystal structure of a bacterial Sufu-like protein defines a
            novel group of bacterial proteins that are similar to the
            N-terminal domain of human Sufu
  JOURNAL   Protein Sci 19 (11), 2131-2140 (2010)
   PUBMED   20836087
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Merchant,M., Vajdos,F.F., Ultsch,M., Maun,H.R., Wendt,U.,
            Cannon,J., Desmarais,W., Lazarus,R.A., de Vos,A.M. and de
            Sauvage,F.J.
  TITLE     Suppressor of fused regulates Gli activity through a dual binding
            mechanism
  JOURNAL   Mol Cell Biol 24 (19), 8627-8641 (2004)
   PUBMED   15367681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="suppressor of fused domain protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /calculated_mol_wt=20542
     Region          29..189
                     /region_name="SUFU"
                     /note="Suppressor of fused protein (SUFU); pfam05076"
                     /db_xref="CDD:461543"
ORIGIN      
        1 msdvlelvea rlrttlgepd araavtflgt drievlrfvd sgvvryatlg msaqpmadpt
       61 avladplrgp raelvlsvrg gradtdkalr alavlaaspq vegvvvapga sldvgeplwp
      121 gaaftsvlva spgglvedle ldepmepvrf lpllpmtpne aawkrvhgae alekrwlehg
      181 tdlrdplrtg vpld
//
LOCUS       WP_457691099             284 aa            linear   BCT 27-JAN-2026
DEFINITION  PHP domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691099
VERSION     WP_457691099.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29919
     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 asdgtdtpte lvrnaaaagl dvvaltdhdt vgghaearaa lpegltlitg
       61 aelscridgv slhmlaylfd peepelarer elvrddrvpr aqgmvaklrd lgvpvtweqv
      121 ariagdgavg rphiatalvd lgvvptvsda ftsewlandg rayvqkheld pfdairlvka
      181 aggvtvfahp lavkrgscvp esaiaelaaa gldgievdhm dhdaptrarl rgmaaelgll
      241 ttgssdyhgs rktcrlgeyt tdpeiygeiv rratgafpvp gtgg
//
LOCUS       WP_457691100             308 aa            linear   BCT 27-JAN-2026
DEFINITION  NYN domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691100
VERSION     WP_457691100.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33754
     Region          41..204
                     /region_name="LabA"
                     /note="NYN domain, predicted PIN-related RNAse, tRNA/rRNA
                     maturation [General function prediction only]; COG1432"
                     /db_xref="CDD:441041"
ORIGIN      
        1 mndvqptgpt dlaalavgie rtnelltrvl aevattpsth aafvdagyvy aaagrlvagt
       61 edrkafdlda egiieafidk armifpdsrl lrvywydgar rrihtqeqqr iaelpdvkvr
      121 lgnlnannqq kgvdslirsd leslarhrai sdavliggde dlvsaveaaq gygarvhlwg
      181 ieasggrnqa epllwevdsa rtfdlefckp yvtrragvec sdqpvgegpa psredvrfvg
      241 aqvaaqwlse rgrewvagll pghpylpgav dqelltasea llrhslrgha dlrrvlrdgf
      301 wdhvqgqy
//
LOCUS       WP_457691101             160 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457691101
VERSION     WP_457691101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..160
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17533
     Region          19..159
                     /region_name="SRPBCC_CalC_Aha1-like"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of Micromonospora echinospora CalC, human Aha1, and
                     related proteins; cd07814"
                     /db_xref="CDD:176856"
     Site            order(19,21,23,32..34,36..37,42,57,65,67,69,71,80,82..83,
                     85,88,94,96..97,110,112,114,116,126,128,130,132,139..146,
                     148..150,153)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtenpatppa dteggphgia ltrtfdarre lvfeawttpe hfgywfggel avpvdrmtmd
       61 trpggvwslv mqtpdggelp fsgvyrevap perleftlkd asapdgiege ivrvtltdlg
      121 drtemafrql ggnltaeqyr qaeagwsgff drltellara
//
LOCUS       WP_457691105             794 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457691105
VERSION     WP_457691105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..794
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83992
     Region          45..423
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mperwqwsrp tgrlrpartn pyegavrpps pphaashrrg kilstfrdlg ifpetaeale
       61 avgiispfpi qeltlpvals gndvigqakt gtgktlgfgl pllervrvpa dveagraqpe
      121 elteapqalv vvptrelcqq vtndlltagk vrnvrvlaiy ggrayepqve alkkgvdvvv
      181 gtpgrlldla gqkklnlsqv kslvldeade mldlgflpdv ekiiqllpak rqtmlfsatm
      241 pgqvislarr ymsqpthira tapddegqtv rnttqhvfra hsmdkpelvs rilqaegrgl
      301 amvfcrtkrt aadiadqlar rgfasgavhg dlgqgareqa lrafrngkvd vlvctdvaar
      361 gidvegvthv inyqspedek tylhrigrtg ragakgtavt lvdwddiprw klinkaldlp
      421 fdepeetyst sphlyaqlni pdgtkgvlpr aertraglaa eevedlgetg grgrgprrga
      481 tveeerpprt rtprqrrrtr ggtpldgpag seaqatgspa aaestegtda agprqprrrr
      541 rtrsgpsgaa vtapvaeaaa paavvteaaa vvteapaepa kprrrrtraa rpvetesfqt
      601 vevaaralaa egaavaaesv avsepaeapa kprrrtrgaa kaaaetapav vtetvveaad
      661 pvveapakpk rtrktaaaka aeaavdtaeg aveapakpkr trktaaakaa eaavetaegt
      721 eaapakpkrt rkaaaatkat adapaaedap akpkrtrksa aakpaadape aaeakpvrrr
      781 trakaavaea tpes
//
LOCUS       WP_457691121            1005 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces nigrescens].
ACCESSION   WP_457691121
VERSION     WP_457691121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1005)
  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 1005)
  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..1005
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1005
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=107158
     Region          730..1002
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mirdqeetae qqgaapprea gapealavda agtapgpaav terperqqva qqgkhqrkpa
       61 tasatekast iekaerpgas qrpegpkepe pterhkeerd stqpeeeqvr hdqgeeqvsg
      121 varskprtgs hradlsadey gefhvdrvsg depllparvh rpsdllrlll giagialvlg
      181 latfahgttq glendigsga kaappllinl agltssvavl ivpvafaver likrdglria
      241 dgvlaavlah gvslatdlwv aeaappsird altqtldngs lsapvhsyla pviaymtavg
      301 marrprwrva mwcvllldsf avlvgryttp faivttvlig wtvaygtlya vgspnvrptg
      361 qnllaglrrv gfhpvsalra edaagaeqse hadrgrrylv tledgppidv tvvdreqqaq
      421 gffyrvwrrl slrginqrrs lqslrqaleq eallayaaia aganaprlia tselgpdavm
      481 lvyehiggrs fdaladeeit dalmhsawrq vealqsrria hrrlvgdall vdrsghivlt
      541 elrggeiaag dlvlrmdiaq llatcglrvg aeravaaave vlgpdavads lpllqpials
      601 rttratlrql arergkrere avleasqaak eareardaag pkdrktirae rhaeknaekr
      661 aldeateear eedllaqirr qvllirpaav iepaklerls priliswiag afavylllsq
      721 lthfnfsdli skaqwmwvlv avgfsaltyi aaamsllgfv tekvsfvktv iaqiagnfvk
      781 lvapaaiggv alntrflqra gvrpglavas vgasqlfglg shilllltfg yltgtertpt
      841 ispsrtviag lltvavlvlv vtavptlrkf vstrvrslfa gvvprmldil qrpgklvtgi
      901 ggmllltaan vmcldasira fgggdtisya siavaflagn algsaaptpg gvgavegalf
      961 galtvaglag dvafpavllf rlmvfwlpvl pgwlaftylt rkgei
//
LOCUS       WP_457691123             134 aa            linear   BCT 27-JAN-2026
DEFINITION  MGMT family protein [Streptomyces nigrescens].
ACCESSION   WP_457691123
VERSION     WP_457691123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..134
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..134
                     /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=14251
     Region          13..126
                     /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(34,74..75,77,99)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(34..35,50,57,59..60,62,65..66,68,74,79)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msgtgetaeg elpayaervl avaelipagr vmtygdvaew lrdeeppegl patggggprq
       61 vgrvmalygg avpwwrvvra dgrllpgsel ralahyraeg tplraaarea edhiprldmr
      121 rarwdgqqng gaap
//
LOCUS       WP_457691125            1174 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent helicase [Streptomyces nigrescens].
ACCESSION   WP_457691125
VERSION     WP_457691125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1174)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
REFERENCE   2  (residues 1 to 1174)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 1174)
  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 11415205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1174
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0032508 - obsolete DNA duplex unwinding
                     [Evidence IEA]"
                     /calculated_mol_wt=125623
     Region          40..889
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          909..1169
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 msssfsaapp tqphraarra aagayrlvrt ppgrvdppvl daaqravvdh rhgpllvlag
       61 pgtgktttlv esvarrvrag ddperilvlt fsrkaavelr drlaarlavl egqpdglpgt
      121 agggrragip qattfhsfcy alvrahqdad lfadplrlls gpeqdlvvre llegqaelag
      181 agralvswpd elraclttrg fadevravla rsrelglgpe algafarrtg rpdwsaaaaf
      241 laeyldvlda qgvldyaelv hravllaeht dvaaqlarsy davyvdeyqd tdvaqvrllr
      301 alagnhgatg tpgspgrtlv afgdpdqsiy afrgadvngi ldfpetfrrg dgtpapvavl
      361 gtsrrsgatl laatrlltrr mpltrlpark vrahrepapv rdggrvevyt yptpgaeldn
      421 iadilrrahl edgvpwrema vlvraggrsl pavrraltsa gvpldidgdd lplrhepava
      481 plltalraaa raalrqepvg aadgdagsga gesdadepgp depdadepap ddpgadgsvg
      541 aapataaprw ldaetaldll asplggmdsa dlrrlgralr eeeraagqpl prpsdeliaq
      601 alaepqrlva hdpayargaq rlglllrkar ellagggtae qalwelwdgt pwpqrleraa
      661 hrggaagrna drdldavval fetaaraeer tggrgalnfl eeldaqdiaa dtltrravrp
      721 davrlmtahr akglewrlvv vagvqeglwp dlrrrgslle adrigrdgla epltpgalla
      781 eerrlfyvaa trarerlvvt avkaaaddgd qpsrfltelg vtpqditgrp rrplsvaalv
      841 aelrattvdp aatpalreaa aqrlaklaal hdddhhplvp sahpdnwwgl hepthssvpl
      901 rdrdrpvvls gsaldqlant cslqwflgre vkadtpataa qgfgnvvhvl adevasgrtp
      961 adltvlmerl dsvwdalafd apwksrqekd qaraalerfl rwhvmeretr grdtvatehg
     1021 fdltlgagay evrirgsmdh vsqdtqgray vvdfktgkqk ptgpevarhp qlavyqlavr
     1081 egavddafdg rtpepggael vhlrlgapqk eggdalpavq aqqpldgewv gellataagr
     1141 vleerftptt gshcthctfr ascsaqpegr hive
//
LOCUS       WP_457691132             742 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase UvrD2 [Streptomyces nigrescens].
ACCESSION   WP_457691132
VERSION     WP_457691132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..742
                     /product="ATP-dependent DNA helicase UvrD2"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /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:0008094 - ATP-dependent activity, acting
                     on DNA [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0043138 - 3'-5' DNA helicase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000725 - recombinational repair [Evidence
                     IEA]"
                     /calculated_mol_wt=80470
     Region          21..628
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
     Region          652..719
                     /region_name="HRDC"
                     /note="HRDC domain; pfam00570"
                     /db_xref="CDD:425755"
ORIGIN      
        1 mtaatdsslf pqvpdsadgv ldgldpeqre vatalhgpvc vlagagtgkt raithriayg
       61 vragilqpas vlavtftara agemrgrlrq lgaggvqart fhsaalrqlq ffwpkavgge
      121 vprllerkiq lvaeaaarcr irldrnelrd vtaeiewskv tqtvpadypa avakagreap
      181 rdpaeigqiy gtyeqlkrdr gsidfedvll ltvgvlqdrh diaeqvraqy qhfvvdeyqd
      241 vsplqqrlle lwlgdrdnlc vvgdasqtiy sftgatpdhl lnfrtrhpna tvvklvrdyr
      301 sspqvvhlan gllsqaqgra aehrlelisq reagpepvyt eyadepaeae gtarrirdli
      361 asgvsageia vlfrinaqse vyeqaltdvg vpyqlrgaer fferpevrea gvklrgaarf
      421 gsndalldda vdlpsevrav lsdmgwtsrp pagsgavrdr weslaalvrl aedfaearpt
      481 atladlvael deranaqhap tvegvtlasl haakglewea vflvgltegm mpityaktde
      541 qieeerrlly vgvtrarlhl glswslarsp ggrasrrasr flsglrpgsg avagrrtpga
      601 vsggvqrgeg aaavarrpkh rsparcrvcn rtltdagemk lmrcedcpse ldealyerlc
      661 ewraeqaars rqpayciftd ktlmaiaeav pgteselavi sgvgrrkfdr ygsdvlaica
      721 geelagvlee gpggaaknss kk
//
LOCUS       WP_457691137             475 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC1 kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691137
VERSION     WP_457691137.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="ABC1 kinase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0004672 - protein kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51495
     Region          1..458
                     /region_name="AarF"
                     /note="Predicted protein kinase regulating ubiquinone
                     biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport
                     and metabolism, Signal transduction mechanisms]; COG0661"
                     /db_xref="CDD:440425"
ORIGIN      
        1 msdlprkavt rtaklaalpl gfagratwgl gkriggrsae ivgrelqqrt aeqlfkvlge
       61 lkggamkfgq alsvfesalp eevagpyraa ltklqeaapp mptstvhavl aeqlgedwqe
      121 lfeefedkpa aaasigqvhr gvwhdgreva vkvqypgagq allsdlsqls rfarllgpli
      181 pgmdikplit elrdrvseel dysleaeaqr ahaeefaddp dvvvpavvhq cdqvlvtewm
      241 agvplsevia dgteeqrdra gqllarflfs gpartgllha dphpgnfrll agdfpdgpve
      301 ewrlgvldfg tvdrlpeglp ptigtslrmt ldgeadavyq llceegfvke sieldpdsvl
      361 eyllpiiepa qvdeftftrg wmrnqaarvg dprspahqlg kqlnlppayl lihrvtlsti
      421 gvlcqlgatv rlrdeleawm pgfvpeeepa gsdladfgtv vgadiseeai eesta
//
LOCUS       WP_457691141             208 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691141
VERSION     WP_457691141.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 208)
  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 11574951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="M48 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22853
     Region          115..191
                     /region_name="M48_yhfN_like"
                     /note="Peptidase M48 YhfN-like, a novel minigluzincin;
                     cd07344"
                     /db_xref="CDD:320703"
     Site            order(159..160,163,169)
                     /site_type="active"
                     /db_xref="CDD:320703"
     Site            order(159,163,169)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320703"
ORIGIN      
        1 mpadpsahgp getplrraad tsrgaapspv aggsgtsave vrrssrrrrt vsayregdrt
       61 vvmiparmse aeerrwvtvm ldklaaqesk rmlgdgelae ragrlsgqyl dgrarpasvr
      121 wvtnqntrwg sctpaegsir lshrlqgmpe yvidyvllhe lahllvpghg prfwrllesy
      181 prterargyl egvvaadrlp hlpvarge
//
LOCUS       WP_457691147             176 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457691147
VERSION     WP_457691147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 176)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..176
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19095
     Region          47..158
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mslhegaarv lkewpapspe qeqlrltyld hlaahqggmw kpckdghlta salvidpagg
       61 rvlltlhrkl emwlqmgghc epedaslada alreareesg iaqgltllpg gpvrldrhqt
      121 pcawhldvqy aalapagava eisdesldlr wfaydevpgv adasvvrlme rtrall
//
LOCUS       WP_457691149             487 aa            linear   BCT 27-JAN-2026
DEFINITION  zinc-dependent metalloprotease [Streptomyces nigrescens].
ACCESSION   WP_457691149
VERSION     WP_457691149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Lenart,A., Dudkiewicz,M., Grynberg,M. and Pawlowski,K.
  TITLE     CLCAs - a family of metalloproteases of intriguing phylogenetic
            distribution and with cases of substituted catalytic sites
  JOURNAL   PLoS One 8 (5), e62272 (2013)
   PUBMED   23671590
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="zinc-dependent metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51147
     Region          65..440
                     /region_name="Zincin"
                     /note="Zn-dependent metallopeptidase, zincin/DUF2342
                     superfamily [Posttranslational modification, protein
                     turnover, chaperones]; COG5282"
                     /db_xref="CDD:444093"
ORIGIN      
        1 msdtpfgfgl ppeepedgdn gkkkggqggs qgpadpfgfg ggsggadnpf aalfggmggp
       61 ggemnpgdlg aafqklgqml syeggpvnwd makdiarqtv aqgaedgskd aslspgersa
      121 veeavrladl wldgvtslps gsgsvvawsr aewveetlpv wkdlvnplae rvgaamgdvl
      181 pgemqamagp llgmmrsmgg amfgtqigqa lgvlagevvg stdiglplgp agkaallpgn
      241 iatfgeglgv peeevrlyla lreaahqrlf ahvpwlrshl fgavegyarg ikvdttkled
      301 vvgqidpqhp eelqnalqqg mfqpedtpeq kaalarleta lalvegwvda vvhaaakphl
      361 pssdklretl rrrrasggpa eqtfstligl qlrprrlrda srlwasltda rglegrdglw
      421 ehpdmlptaa dlddpdgfvh heqpdfseld kmlgeaasgr kpdldkpare sdgpdetpge
      481 skgdsdk
//
LOCUS       WP_457691155             365 aa            linear   BCT 27-JAN-2026
DEFINITION  YlbL family protein [Streptomyces nigrescens].
ACCESSION   WP_457691155
VERSION     WP_457691155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ratner,S., Bollinger,K., Richardson,J. and Dawid,S.
  TITLE     The Outer Surface Protease, SepM, Is Required for blp Locus
            Activation in Three of the Four Most Common Pherotypes of
            Streptococcus pneumoniae
  JOURNAL   J Bacteriol 204 (11), e0019622 (2022)
   PUBMED   36286514
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Hossain,M.S. and Biswas,I.
  TITLE     An extracelluar protease, SepM, generates functional
            competence-stimulating peptide in Streptococcus mutans UA159
  JOURNAL   J Bacteriol 194 (21), 5886-5896 (2012)
   PUBMED   22923597
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Lee,I., Berdis,A.J. and Suzuki,C.K.
  TITLE     Recent developments in the mechanistic enzymology of the
            ATP-dependent Lon protease from Escherichia coli: highlights from
            kinetic studies
  JOURNAL   Mol Biosyst 2 (10), 477-483 (2006)
   PUBMED   17216028
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Vasilyeva,O.V., Kolygo,K.B., Leonova,Y.F., Potapenko,N.A. and
            Ovchinnikova,T.V.
  TITLE     Domain structure and ATP-induced conformational changes in
            Escherichia coli protease Lon revealed by limited proteolysis and
            autolysis
  JOURNAL   FEBS Lett 526 (1-3), 66-70 (2002)
   PUBMED   12208506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="YlbL family protein"
                     /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]"
                     /calculated_mol_wt=37967
     Region          3..359
                     /region_name="SdrC"
                     /note="Predicted secreted protein YlbL, contains PDZ
                     domain [Signal transduction mechanisms]; COG3480"
                     /db_xref="CDD:442703"
ORIGIN      
        1 mprrtatlla silmliallc agvlipvpys emspgptvnt lgdhdgepvl qisrrktypt
       61 tghlnmttvr vtgpdyrmnl feavygwldh dnavvphktl ypegqtaeqa dqenaeefsq
      121 sqesakaaal qqldlpiaaq tvvgsvvkgk padgrlhagd viravdgtav kqtgdvaklv
      181 trhkpgekvv fsiipakeaa aaekqgkkpq agteqvtitt qkaddgraiv giqagvdyif
      241 pfpidvklad vggpsaglmf algivdkltp gdmtggkfva gtgtiddkgk vgpiggismk
      301 tvgardkgae ffltpkdnca aaakdipqgl tlvkvgtigd avkalekirk gdtaglpscs
      361 pagrs
//
LOCUS       WP_457691159             933 aa            linear   BCT 27-JAN-2026
DEFINITION  UPF0182 family membrane protein [Streptomyces nigrescens].
ACCESSION   WP_457691159
VERSION     WP_457691159.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Keefe,B., Leestemaker-Palmer,A. and Bermudez,L.E.
  TITLE     The ability to detach from biofilms in the lung airways prior to
            transmission to another host is associated with the infectious
            phenotype of Mycobacterium abscessus
  JOURNAL   Front Immunol 16, 1508584 (2025)
   PUBMED   40124375
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Gannesen,A.V., Ziganshin,R.H., Zdorovenko,E.L., Klimko,A.I.,
            Ianutsevich,E.A., Danilova,O.A., Tereshina,V.M.,
            Gorbachevskii,M.V., Ovcharova,M.A., Nevolina,E.D., Martyanov,S.V.,
            Shashkov,A.S., Dmitrenok,A.S., Novikov,A.A., Zhurina,M.V.,
            Botchkova,E.A., Toukach,P.V. and Plakunov,V.K.
  TITLE     Epinephrine extensively changes the biofilm matrix composition in
            Micrococcus luteus C01 isolated from human skin
  JOURNAL   Front Microbiol 13, 1003942 (2022)
   PUBMED   36204611
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..933
                     /product="UPF0182 family membrane protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=102859
     Region          2..927
                     /region_name="COG1615"
                     /note="Uncharacterized membrane protein, UPF0182 family
                     [Function unknown]"
                     /db_xref="CDD:441223"
ORIGIN      
        1 mtlgvlavla mlfvmfagfw tdwlwyrsvk yssvftttlw tkiglffsfg vlmavavgvn
       61 iwlahrlrpp lsamsmeqqs ldryrmsiap fkkwaliait avigliagas asgewrtwlq
      121 wvngvpfgkk dpqfgmdvaf yafdlpwyrf llsfgfacav lclvaaalth ylygglrlts
      181 pgsrataaat ghlsvllgif vslkaiaywl dryglavkss glksadnwtg lryvdanayl
      241 paktilffia aicavlffat lwrrtwqlpv igfglmvlsa vligglypai vqkfqvqpne
      301 qakeapyikq nikatrdayd iqdsevtpyk gdyqptgkad sqrlrddadt tasmrlldpn
      361 vvspafqqqq qvrgyyqfps tldvdrykdk dgaeqdtvig lrelniagip ernwindhfk
      421 ythgygavaa kgteaaeggg pkytesdlpa kgqlgkyqqr vyygektsqy sivggpqkel
      481 dysddsgeks ysyqgksgvn lgnpinraay avafgepqil ysgaigdgsr ilynrtpker
      541 vesvapwlti dgdaypavid grikwivday ttsngypyas rttlgdstad sltdgqravv
      601 aqqnqvnyir nsvkatvday dgsvklyqwd ekdpvlktwm kafpdtvekk saispalkeh
      661 lrypqdlfkv qrqllttyhv tdpgtfytgs erwqipndpt tksgnavppy ylsmkmpdqk
      721 nrafsltttf tpnkrdnlga fmavdanats rdygkirllk lpsetpvpgp qlvqskfnsd
      781 pvianelnil kkfgdseiey gnlltvpldg gllyvepvyl rgantnypll kkvlvsygdn
      841 kpvledslkd aldvvfgkka pstgteeppg gdtgqppsdq tvqqaladaq kayeegekar
      901 tsgdwagyge aqkklkaald raakasekgk pgs
//
LOCUS       WP_457691165             139 aa            linear   BCT 27-JAN-2026
DEFINITION  Fur family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457691165
VERSION     WP_457691165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15312
     Region          1..137
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msdllerlrg rgwrltaqrr vvaevldgdh vhytadevha lasdrlpeis ratvyntlge
       61 lvslgeviev stdgrakryd pnahhdhqhl vcsqcgtird vhvqgdplsa lpeperygfq
      121 vsevtvtyrg icpncsaps
//
LOCUS       WP_457691167             487 aa            linear   BCT 27-JAN-2026
DEFINITION  catalase [Streptomyces nigrescens].
ACCESSION   WP_457691167
VERSION     WP_457691167.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54182
     Region          9..484
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 msvesitgpl ttesgapvgd nqnsetagig gpgliqdqll ieklahfnre riperivhar
       61 gagaygtftv tadvtkytra nflsevgkqt etflrfstva gslgsadavr dprgfalkfy
      121 teegnydlvg nntpvffikd amkfpdfiht qkrdpytgsq eadnvwdfwg lspeathqvt
      181 wlfgdrgipa syrhmngygs htfqwnneag evfwvkyhfk tdqgirnltt seaaetsgld
      241 pdshqrdlre siergdfpsw tvqvqimpaa eaanyrfnpf dltkvwphed yppieigkle
      301 lnrnpqnifa eveqsifsph hfvpgigpsp dkmlqgrlfa ygdahryrvg inadhlpvnr
      361 phatearths rdgvlydgrh agrknyepns fggpvetgrp lwqpaavtgp tgeqaapsha
      421 edddfvqagn lyrlmaedek erlidnlagf isqvsrddia qraienfrka dadygkrlea
      481 avqalrg
//
LOCUS       WP_457691169             243 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691169
VERSION     WP_457691169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24756
     Region          2..>80
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpaareslld aaytaltera wtavrmvdva aaagvsrqtl ynefgskegl aralvrretd
       61 hylagvaral sqgsaaagtr gdaagrvaaa aawtlrtara nplvravltg cwsdrlpaps
      121 paadaaplrv agpgipaqra assgdgplpg paeivgrfcd qavaalepdw peeqlpalga
      181 acetaarltl acvvapvtpg aapspgrvpa prsrgelete avsrlvrdaf arvpadaqpg
      241 erc
//
LOCUS       WP_457691171             107 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457691171
VERSION     WP_457691171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..107
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10912
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawllvvvag iletgfavcl klshgftrlf ptiafaafal gsfglltlal rrldvgpaya
       61 vwtgigaagt aiygmvflgd vvstlkivsi tmvivgvvgl qlsgaar
//
LOCUS       WP_457691179             277 aa            linear   BCT 27-JAN-2026
DEFINITION  SOS response-associated peptidase [Streptomyces nigrescens].
ACCESSION   WP_457691179
VERSION     WP_457691179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=30572
     Region          1..268
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgryaasrr pedlvgdfgv qqwepketla pswnvaptdq vhavlerplk gaaaehyppg
       61 spvrqlrplk wglvpswsks peaaakmina rsetvhekps frqafatrrc llpgdgyfew
      121 vtdaaerqle eqgrkkrprk qpyfvtpadg svmamaglye fwrdrtlpgd hplawwvtct
      181 vvtteaettp lagadgstgp qaladihprm plvlppdrwd awldpartdp devrallapp
      241 paglmraypv ptevsnvrnn gpelvteldg pevgtlf
//
LOCUS       WP_457691185             477 aa            linear   BCT 27-JAN-2026
DEFINITION  HD-GYP domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691185
VERSION     WP_457691185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50310
     Region          <217..425
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mrglpaaarg yigcavpaaa lcaapaaglg adapwssala latlyglcel lrrcplsggr
       61 vpygtvsgas ggfpagwasp vllagvfllp pplaalaavp gaviapvepr saatrrlwha
      121 aelalaccaa ahvfrtlghh plsapqfpvv llpaaaaaat fcavlaaldg gvlataerhp
      181 vrtawrglls rslgphlvhg laglmmavlw cssygppaal lvllpmylsc wvfdryhrer
      241 aahqatiral vqavdikdry trghservgr asvmiarelg maedriealr fagilhdvgk
      301 lgvptrllrk dgpltpqerr vielhpeygh eivrgigfle earaailhhh erldgrgypy
      361 glrghhipef arvvavadaf damtstrsyr rarpvpvava elrkcagaqf dprmvralva
      421 sldrygwhpe lvtaadpepg tgrfgrgnvt ppragggapa pvapvplper agrdgar
//
LOCUS       WP_457691181             215 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691181
VERSION     WP_457691181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Marchot,P. and Chatonnet,A.
  TITLE     Enzymatic activity and protein interactions in alpha/beta hydrolase
            fold proteins: moonlighting versus promiscuity
  JOURNAL   Protein Pept Lett 19 (2), 132-143 (2012)
   PUBMED   21933125
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Ollis,D.L., Cheah,E., Cygler,M., Dijkstra,B., Frolow,F.,
            Franken,S.M., Harel,M., Remington,S.J., Silman,I., Schrag,J. et al.
  TITLE     The alpha/beta hydrolase fold
  JOURNAL   Protein Eng 5 (3), 197-211 (1992)
   PUBMED   1409539
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007573
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22017
     Region          28..215
                     /region_name="COG3571"
                     /note="Predicted hydrolase of the alpha/beta-hydrolase
                     fold [General function prediction only]"
                     /db_xref="CDD:442792"
ORIGIN      
        1 mstgametek vatpagdari twyraakpar avvalshgag ggieardlra laaalpargy
       61 pvalveqpwr vagkklapap ktldtgwtal wpalekpglp vvaggrsaga rvacrtarel
      121 gaqavlalsf plhppgrpek sradeltgag vptlvvqggr dpfgrpeefp pgteitevah
      181 gdhgfavpkk agvgeaesma vitdavavwl dgmfg
//
LOCUS       WP_457691189             659 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691189
VERSION     WP_457691189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..659
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=70928
     Region          25..577
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mmgtkgrrrv rrrfldyprq grqgprrwlp swrqwlgvla lgilglagmf avvytkidip
       61 tentlagqea tvyywadgsp mvsvgavnrq nvsldkvads vensviaaen atfysdsgvs
      121 lkgigralvs mvsggdtqgg stitqqfvkn tylsqdqtvt rkvrefiial kvsnqkskqd
      181 ilrgylntsw fgrdsygiea aahayygvda kqlnpsqsal laavlkgseq ydpglskanh
      241 qraearwkwi ldrqvaigkm sekqrakyrt fpeprplskp tsqagqtgyl idvankfvka
      301 gtgltdkdla rggyrihttf ekqrtrrlek avnevrrkni dpkhrtadtf vefgaasvrp
      361 kdgalvavyg gadatkhfsn nadttavpag safkpfvlaa alqdgvydld esedatvspa
      421 dgpttgaeel realvkgqsp pfvqagqrig lerlrdvava sglrkesmar leqtfplgts
      481 apsairmasa yttfangglh aepyavsrmt ydgkklpgfe rpepeqvlda evaqevsnal
      541 eevgrrtvgl pegkpalpva agraepgdrk ksawfigsph aagrvvgpgg gtdaekwqwt
      601 rpgaapgagd gdgpttaitm frnkagapel lpmegvggtg selgttippk iwqayqqgs
//
LOCUS       WP_457691193             195 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457691193
VERSION     WP_457691193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  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 195)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21779
     Region          1..190
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 mtalvdrphl metghfeeva qilarlekga rlefidgkir skavpdgshg rimewltrrc
       61 vqarpelrly rdqglkvqay ragrahpdge lapsgafagl gewadpdpal mvvavtshda
      121 dtgqrdrvem prvyaetgip lyllvdresr qvsvhsepdg gryevmhsvs ygrrihlpdp
      181 vgitleteql knwvh
//
LOCUS       WP_457691199             330 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691199
VERSION     WP_457691199.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36604
     Region          55..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavqldgvvd qtaprtgkgg apptrrgggs rraargtpyl lllpallata vllgwpmvrn
       61 lllsfqnlnm keliqhltdw rgignyqeil greqfwrvtl rtivftavnv vlimvlgvli
      121 glllarlgkk mrltlslalv lawampviaa ttvfqwlfds rygvvnwvld klgghsmahy
      181 dwvgsqlstf fvitvlivwq slpfvalnly aatttipkel yeaarmdgag twqvftavtf
      241 pflkpfflat tfleiiwvfk afpqifaine ggpdrltetl piyaftegvg nlhfgmgaai
      301 slltivvlla mtayylrltv kqeqqeenel
//
LOCUS       WP_457691201             276 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691201
VERSION     WP_457691201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 276)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30174
     Region          2..276
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mkhslagriw pnataavlal gfvfpvywmf ntafkptqdi itedpvwfpv hgtlehfata
       61 vhapdfwila gnsvlvtvga vglslvialc gafaltrmrf rgrkgilltf mvaqmapwev
      121 mvisiylivr dadllnsllp ltffymlmvl pftlltlrgy vaavpkelee samvdgcsrr
      181 qaflkvvfpl lapglmatsl fgfitawnef plvlvlnkep amgtlplwls qfqtqfgddw
      241 gatmaaasif avpilvlflf lqrkavgglt sgavkg
//
LOCUS       WP_457691203             516 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces nigrescens].
ACCESSION   WP_457691203
VERSION     WP_457691203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..516
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53006
     Region          55..487
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mtplvrsvrs adtltrdala vlqpgftgtt apdwllrrlg eglvsvglfg rnvadpaqla
       61 altgrlraer eelivaidee ggdvtrlevr ggssfpgnha lgavddtalt revarelgrr
      121 ladcginlnw apsadvnsnp snpvigvrsf gadpqlvarh taayveglqs agvaactkhf
      181 pghgdtavds hhdlphiavd lptlqerelv pfraavaagt ravmsahill paldgehpat
      241 lspaalhgll rapategglg fdglivtdgm emqaisatyg iergsvlala agadaicvgg
      301 gladegivlr lrdalvravr dgelpeqrla daaarvrala grtrsadvge rpepapgigl
      361 taarralrvt atgpyaplae payvaaftpl aniavgdetp wgvaaelarl lpgtetatct
      421 ceaaavagta alvdglltaa agrrlvavvr dvhrhpwmad alhsllaarp dtaviemgvp
      481 qappqgaphi athgaarvca qaatealtgr rpspge
//
LOCUS       WP_457691209             209 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691209
VERSION     WP_457691209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22377
     Region          11..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matketkqrg rprsfdreta leqavrsfwe qgyeatsisd ltrtmgisap slyaafgdkr
       61 alfdevvaey grlyggflsr avaeeptarr gveralreaa aeytlpgrpr gclvisaaln
      121 ispasaevad slremrlsnv reiaaairad iasgelppdt dagalaayig aviqgmsqqa
      181 rdgaertele avaelalkaw prktsgasr
//
LOCUS       WP_457691211             327 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691211
VERSION     WP_457691211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34695
     Region          1..327
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrallvvnpa atttsartre vlthalasdl klevaqtqyr ghardlarqa teggetdlvv
       61 alggdgtvne vvngllangp dpdshprlav vpggstnvfa ralglpndvv eatgalldal
      121 rdgsertigl glaagtpgsv degvperwft fcagfgfdag vvgrveqqre rgkrsthaly
      181 vrqvvrqflv easrrrgalt lerpggtega aetvedlala iicntapwty lgnrpiypsp
      241 dasfdtaldl falnklspsa varyatqllt stpergphgk halslhdltn ftlhsqvplp
      301 fqmdgdhlgl rtsvtftgvr ralrviv
//
LOCUS       WP_457691221             317 aa            linear   BCT 27-JAN-2026
DEFINITION  1-aminocyclopropane-1-carboxylate deaminase/D-cysteine
            desulfhydrase [Streptomyces nigrescens].
ACCESSION   WP_457691221
VERSION     WP_457691221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Thibodeaux,C.J. and Liu,H.W.
  TITLE     Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase:
            characterization of an unusual pyridoxal 5'-phosphate-dependent
            reaction
  JOURNAL   Biochemistry 50 (11), 1950-1962 (2011)
   PUBMED   21244019
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Nagasawa,T., Ishii,T., Kumagai,H. and Yamada,H.
  TITLE     D-Cysteine desulfhydrase of Escherichia coli. Purification and
            characterization
  JOURNAL   Eur J Biochem 153 (3), 541-551 (1985)
   PUBMED   3908101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33769
     Region          46..315
                     /region_name="Acd"
                     /note="1-aminocyclopropane-1-carboxylate
                     deaminase/D-cysteine desulfhydrase, PLP-dependent ACC
                     family [Amino acid transport and metabolism]; COG2515"
                     /db_xref="CDD:442005"
ORIGIN      
        1 mnhpvdlaaa lrprppsplq eiederfarr gvrlllkrdd llhttlpwdt aalgpvelcp
       61 pgnkwrklap nlraaaaage ralltfggay snhlrataaa grllgfatig vvrgdelaga
      121 plnwslarca adgmrlyfid raryrrradp evlaelhdrf gafrlipegg snalatqgct
      181 elgrelrgaa dtvavacgtg gtlaglaagl gpgqralgfp vlkggrphfl qetveelqra
      241 afggprgdwr ledrfhcggy arrtpeldtf aaafedrhgl pleriyvakl lyglttlaee
      301 gafapgstva avitgap
//
LOCUS       WP_457691231             312 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-ACP synthase III [Streptomyces nigrescens].
ACCESSION   WP_457691231
VERSION     WP_457691231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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   3  (residues 1 to 312)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="beta-ketoacyl-ACP synthase III"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0033818 -
                     beta-ketoacyl-acyl-carrier-protein synthase III activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31907
     Region          1..312
                     /region_name="PRK09352"
                     /note="beta-ketoacyl-ACP synthase 3"
                     /db_xref="CDD:236475"
ORIGIN      
        1 mtgsrvlalg hyqpsgvltn ddlakivdtd dawirsrvgi rtrhvaapde tvdsmaaaaa
       61 akalaasgla pqdidlvlva tctahdrspn taarvaarlg ldapatmdln vvcsgfthal
      121 atadhairag sathalviga ekftdvvdwt drstcvlvgd gagaavvgaa pepgigpvlw
      181 gsvpqmggav riegeparfa qegqtvyrwa ttqlpaiark vcersgitpa dlagvvlhqa
      241 nlriiepvae rigavnavva kdvvdsgnts aasvplalsk lverreiasg apvllfafgg
      301 nlsyagqvih cp
//
LOCUS       WP_457691235             330 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691235
VERSION     WP_457691235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /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=35447
     Region          16..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msetsarlln llsllqtpre wpgselagrl gvttrtirrd idrlrelgyp vhatmgaegg
       61 yrlaagaamp pllldddeav aiavglrsaa gqtvegieea svralakleq vlpsrlrrrv
      121 gtlgtatvsl psgdhptvdp ehltvlaaai snqerlrfry ragagarskr lvephrlvas
      181 grrwylvayd ndredwrifr vdrlsepfpt gvrtpartlp aadagayvre rmqgrvathr
      241 avatvhapaa evaaklggpa agevepvdea scrwhstpds lewlavrlal lgheftvhep
      301 pelaaylram ggrvnraaga aageeegasp
//
LOCUS       WP_457691233             755 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457691233
VERSION     WP_457691233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..755
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77388
     Region          10..753
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mataigahgv eleiggmtca scaariekkl nrmegvtatv nyatekaqvt vaegsdvaaa
       61 dliatvertg ytaavpeppa aeppdgdagg padgrdgeah talrqrllvs laltvpvvlm
      121 amvpplqftn wqwlsltlaa pvvaygawpf hraawtnlrh gaatmdtlis mgtlaalgws
      181 lwalffgtag mpgmthpfel tlartdgsga iyleaaagvt tfilagrsfe arakrkagaa
      241 lrallelgak dvavlrdgre vripvgalsv gdrfvvrpge kiatdgkvve gasavdasml
      301 tgesvpvevs pgdtvtgatv naggrlvvea trvgadtqla rmarlvedaq ngkaaaqrla
      361 drisavfvpl vialalgtlg ywlgtghgav saftaavavl iiacpcalgl atptalmvgt
      421 grgaqlgill kgpevlestr rvdtvvldkt gtvttgvmtl tevhlaegvt epealrlaga
      481 lehasehpia ravatgaesr gaalpapedf envpglgvrg vveghtvlvg reqllnrwnq
      541 pltpelaaak aaaeargrta vtvgwdgaar avlvvsdavk ptsaeavrrl ralgltpvll
      601 tgdneavata vatevgidev iaevlpedkv avvarlqseg rsvamvgdgv ndaaalarad
      661 lglamgtgtd aaieagdltl vrgdlrtaad airlaratlg tirtnlfwaf gynvaalpla
      721 aagllnpmia gaamafssvf vvgnslrlrr fralp
//
LOCUS       WP_457691237             523 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457691237
VERSION     WP_457691237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54028
     Region          37..492
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(44..45,48..49,52,84,134..135,137..139,142,162,
                     165..166,169,237,302..303,306..308,311,340,344,400..401,
                     405,409,425,428..429,432..433,436)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtttvpaahe aavpaheaav papapagrrr wialavllta sfmdlvdati vniaipsiqr
       61 dtgasfsavq wvtagyalaf alglitggrl gdiygrkklf llgmggftla salcglatdp
      121 gmlvgarvlq gamaalmvpq vlaiihvsfp agergkvfgm fgaviglgav cgpligallt
      181 evdllglewr piflinlpvg iagillgrrf ltesratral rvdligtala tvgllmllyp
      241 ltqgresgwp lwgfvsmaas plvlalfvry erirarkdgs plvelslfsv rtfaagagvq
      301 ltfgvvsglf flvwtlhmql glgwgplhag ltgvpfslac saaagmsvqk lvprfgravl
      361 qagalimlsg allylweagh ygtalqswqm apamllmgag mglivapitd aaisevpaeh
      421 sgsasgifnt tgqlgmalgl glssvaffgv vggtgepgga gaaavlrpaf vdatthalww
      481 isgglvlifg llflmprrvp aqdapertah dgaeaeqqpv lvs
//
LOCUS       WP_457691239             288 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691239
VERSION     WP_457691239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=31264
     Region          4..258
                     /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 gvhdmysasi aaghyngffv sgfgfaasyy glpdigfiaw
       61 pdmaafverl rgafphhhll vdiddgyadp evtchvvqrl ertgasgvil edqqrprrcg
      121 hadgklvlpl edylekldlv lasrtdllvv artdateedd ilrraaalar teadvvlvdg
      181 vrrvdrirri rqvvgdkpll fnqiaggksp rlslteltal gvdvaiystp clfaahrame
      241 tamaelkyad grlpatgdtg gevgvkeate llarnisrhh pgrravpa
//
LOCUS       WP_457691241             145 aa            linear   BCT 27-JAN-2026
DEFINITION  fluoride efflux transporter FluC [Streptomyces nigrescens].
ACCESSION   WP_457691241
VERSION     WP_457691241.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   McIlwain,B.C., Ruprecht,M.T. and Stockbridge,R.B.
  TITLE     Membrane Exporters of Fluoride Ion
  JOURNAL   Annu Rev Biochem 90, 559-579 (2021)
   PUBMED   33492991
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Ji,C., Stockbridge,R.B. and Miller,C.
  TITLE     Bacterial fluoride resistance, Fluc channels, and the weak acid
            accumulation effect
  JOURNAL   J Gen Physiol 144 (3), 257-261 (2014)
   PUBMED   25156118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="fluoride efflux transporter FluC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14926
     Region          37..138
                     /region_name="CrcB"
                     /note="Fluoride ion exporter CrcB/FEX, affects chromosome
                     condensation [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism]; COG0239"
                     /db_xref="CDD:440009"
ORIGIN      
        1 mderprraap wqgqwpvigv vavggaigaa arygaallwp tgngsfpwtt lavnvvgcal
       61 mgvlmvmite vwparrllrp flgtgilggf ttfstyavdi qrlidgghpa aamaclagtv
      121 lgalaavgga vtgtrallel rrrtv
//
LOCUS       WP_457691251             421 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Streptomyces nigrescens].
ACCESSION   WP_457691251
VERSION     WP_457691251.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42910
     Region          58..>396
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mdgtlslvll llflwclcsr rmerfeltap aafvllglll gegtgvlgla lphetvkvla
       61 eitlvwvlft daarlsfral rpelglyvrl laiglplcvg lgallasvll pgvsgwsaly
      121 vgaalaptda algatmmvnp vvpakirrii nvesglndgi atplvvlala gvsaaehtdg
      181 pdatghalvq lavgaaygav vglaagwllr ttlrngwaae dfagagvlal sllgytsala
      241 iggngfvaaf vaglafgtth gapprvllyv eqsgallsvl vwlvfgavll pevfahvtwq
      301 avvyavlslt virmvpvalc lagsgldart vgfigwfgpr glasiifgll aveeltpaga
      361 rsvlpaiact vllsvlahgl tsaplanryg raaadrgigp agpaaeelrv rgmaaggphr
      421 g
//
LOCUS       WP_457691255             230 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD:protein FMN transferase [Streptomyces nigrescens].
ACCESSION   WP_457691255
VERSION     WP_457691255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..230
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=23949
     Region          11..220
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mrsghrlgdg qaqaraarvf styragsqis rlgrgelteq qcdpevaevl glcraaaras
       61 sgwfsatpgg rldpsavvkg waverasqll ydagarhhsv ngggdiqtrg eaapgrpwqi
      121 gvahplcpgd lttlvtgrdl avatsgtaer gphildphtg rratdlasit lvgrhltevd
      181 alataafamg daargwlrsl dgieafavta darawwtpgf aaygrvpaha
//
LOCUS       WP_457691259             209 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691259
VERSION     WP_457691259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23067
     Region          10..184
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 melayysdya vrlvnteqpe rgtdtltsve vvrelfgpaq qaarratdsd vtrlrtvrar
       61 lravfeaada gdevlavdll nalmmefpvs pqisghefrd dngrpdwhmh iadhaanata
      121 gftatacmgl afhltelgvd rlgicearpc rnvyldtstn rsrrycsdrc atranvaayr
      181 arkrlesera artgrtadta qdstpatdr
//
LOCUS       WP_457691261             253 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457691261
VERSION     WP_457691261.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28054
     Region          <9..>79
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          45..151
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtetvvgadw qawqnswdrq qewylpdree rfrvmldmve alvgpeprvl dlacgtgsis
       61 drllkrfpga esvgvdldpa llaiaegyfe geprvrfvra dlkdpqwtek lphdsydavl
      121 tatalhwlyt edlrglygql gtlvrdggvf mnadhmpdeg tprinaaera frharqdaak
      181 aagavdwaew wqlaaadprl aaptaerfei ygehadgdtp saawhtavlr dsgfaearpv
      241 wasptdalvl glk
//
LOCUS       WP_457691266             407 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent malic enzyme [Streptomyces nigrescens].
ACCESSION   WP_457691266
VERSION     WP_457691266.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Alvarez,C.E., Trajtenberg,F., Larrieux,N., Saigo,M., Golic,A.,
            Andreo,C.S., Hogenhout,S.A., Mussi,M.A., Drincovich,M.F. and
            Buschiazzo,A.
  TITLE     The crystal structure of the malic enzyme from Candidatus
            Phytoplasma reveals the minimal structural determinants for a malic
            enzyme
  JOURNAL   Acta Crystallogr D Struct Biol 74 (Pt 4), 332-340 (2018)
   PUBMED   29652260
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Tao,X., Yang,Z. and Tong,L.
  TITLE     Crystal structures of substrate complexes of malic enzyme and
            insights into the catalytic mechanism
  JOURNAL   Structure 11 (9), 1141-1150 (2003)
   PUBMED   12962632
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Xu,Y., Bhargava,G., Wu,H., Loeber,G. and Tong,L.
  TITLE     Crystal structure of human mitochondrial NAD(P)(+)-dependent malic
            enzyme: a new class of oxidative decarboxylases
  JOURNAL   Structure 7 (8), 877-889 (1999)
   PUBMED   10467136
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Goward,C.R. and Nicholls,D.J.
  TITLE     Malate dehydrogenase: a model for structure, evolution, and
            catalysis
  JOURNAL   Protein Sci 3 (10), 1883-1888 (1994)
   PUBMED   7849603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="NAD(P)-dependent malic enzyme"
                     /EC_number="1.1.1.40"
                     /GO_function="GO:0004471 - malate dehydrogenase
                     (decarboxylating) (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0004473 - malate dehydrogenase
                     (decarboxylating) (NADP+) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=42051
     Region          27..384
                     /region_name="SfcA"
                     /note="Malic enzyme [Energy production and conversion];
                     COG0281"
                     /db_xref="CDD:440050"
ORIGIN      
        1 maaeivnprs dsnsgadags apddafdpaf alhrggkmai qatvplrdkd dlslaytpgv
       61 akvcsaiaek pelvhdytwk sqvvavvtdg tavlglgdig peaslpvmeg kailfkqfgg
      121 vdavpialgt tdtdeivetv vrmapsfggv nledisaprc feierrlqer ldipvfhddq
      181 hgtavvtlaa lrnaakltdr slgqlravis gagaagvaia kilieagigd vavcdrkgvv
      241 stdrsdltdv krevagftnk grltgsleda ldgadvfigv sggtvpeeav akmakdslif
      301 amanptpeih pdvahkyaav vatgrsdfpn qinnvlafpg ifagamqvra sritegmkla
      361 aaealaavva delsadrvip spfdervapa vtaavaaaar aegvarr
//
LOCUS       WP_457691270             153 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691270
VERSION     WP_457691270.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15792
     Region          33..151
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 migvsdsaaa gvpesgsgsa rrrskavgsa taewsfpadp gavrtartvv rrvlddwgln
       61 gaadmavllv selvtnslrh asgpigvrmv llssdgllve vsdplpdppq erdaapddeg
      121 grglqlvacs srrwgtrrgk sgktvwfels vag
//
LOCUS       WP_457691272             890 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457691272
VERSION     WP_457691272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 890)
  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   3  (residues 1 to 890)
  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   4  (residues 1 to 890)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 890)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 890)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 890)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 890)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 890)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..890
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=95007
     Region          45..286
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          282..747
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          757..872
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mssggaepaq adgqggadsp gdpggrphvr dlqgppvwqs srpgsiydyi rvasfslgpd
       61 grieqwsera eqmlgipary algkdpveaf vprelretgh rkvseildgr ewtglvpyrr
      121 etsgeaagla eiyvmpsrne dgeraavclv vdvralrgie tdlaasqavf gqspmgftlf
      181 gtdlkllrvn erfasvfggp askyrgcgph dflprseaer mtaalrrvld tgepvaemql
      241 vglasgdedr rrwsvslyrl hgasgrpigv aalaadvtgr rraereaana rrnlallnea
      301 garignsldl ettartlldv avpqfcdlas vdlyqgllsg deappgmsdg saelrrvafa
      361 savsdaplat tpgvlgdtpd pvavgavhry pfnspcagal rtahaqiipg resddgpelg
      421 avvhstlavp mvardtvvgl vqfsrtkgse pfgerdtala velaaraavc idnarlyrre
      481 heralilqrs llppgdpeaa gldiacrylp gttatevggd wfdvielpgh rtalvvgdvm
      541 grglraavam gelrtavrtl alldlepaev lsaldeiarg lggdgdgrst arsargrsgt
      601 adgtpetnrs artadlsevy latcvyavyd pvtrrctfan aghlppvlve dgedallldv
      661 ppgmplgvgg epfeeievel pdgallalyt dglvesrhhp ldeglrafrt alsgadrple
      721 dacdhvlnal dtshgeddia llmarvhglp kdavgdwsla pearsvarar elardqltdw
      781 glqdlvdtte llvselvtna lrhghgeirv rllldrslvc evwdadlaqp rrrrardtde
      841 ggrglqlvgl lsegwgsrrt prgktvwfel alpdgestav dpaeallslf
//
LOCUS       WP_457691282             424 aa            linear   BCT 27-JAN-2026
DEFINITION  HD-GYP domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691282
VERSION     WP_457691282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43590
     Region          <234..418
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mvpgacgsav vaavyapaaa lacwslgrtl wdglaepgia lafgvlitvg elvgrgpapa
       61 agcarvpgar egaplaaaga layallgeag grptthgvpq tvtvvlaagl vgivpqlarg
      121 qgpvldhlar rvltagfaat cfqplyntgt lgswvasgpv ypffliglla ltalcdavlv
      181 aalarartgw pygpllrdel rallgigsai catgvvisla tavaglwalp vfclpllltq
      241 fafrrfaavr ttyrqtiasl arsteiagyt phgharrvaa lsravgrelg lnepeldvle
      301 haalmhdigq lslldpvpdg ataplppaeq rriallggav vrqtgvppev aviverqadp
      361 yreqpvtari vrtvnayddl sgesvgpggp lraleqlrls tardheprvv ealarvlacg
      421 grtv
//
LOCUS       WP_457691286             488 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457691286
VERSION     WP_457691286.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..488
                     /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=53698
     Region          1..486
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mndlvrqhta lsdtdlewlh llvsewqlls dlsfadlvlw vptldgtryv svaqmrpntg
       61 ptsyqddmvg hlvprgrrpm ldsaldegri vregdpewre evpvrvesip vrregrvlgv
      121 iarntnlltv rtpsrlelty lqsasdlaqm iaagsfpfpg qqvdmdaspr agdglirlda
      181 egvvqyaspn alsayhrlgl aadlvghhlg qataelapar gpvdealvkl asgwaprefe
      241 vegedgviql raiplkpkgt higslvllrd vtelrrrere litkdatire ihhrvknnlq
      301 tvaallrlqs rrmdseqgre alneavrrvg siaivhetls qtldervefd eiadrvlamv
      361 aeispgkvtt rrtgrfgild aevatplsmv ltevlqnale hafdqvergv vevgavrggs
      421 rteprllvtv qdngrglpeg fdphragnlg lqivrtlveg elggkfdmvr apergtqvil
      481 dvpvraek
//
LOCUS       WP_457691289             250 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691289
VERSION     WP_457691289.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27231
     Region          1..249
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mvkaegvhks fgaahilkgi dlevaprevf cligpsgsgk stflrcinhl ekvnagrlsv
       61 dgelvgyreh ngklfelrdr evaarrrdig mvfqrfnlfp hmtavenime apiqvkgesk
      121 aaarerattl ldrvgladka gnypsqlsgg qqqrvaiara lamepklmlf deptsaldpe
      181 lvgdvldvmk dlaadgmtmi vvthemgfar evgdslvfmd dgvvvesghp rdvlgnpqhe
      241 rtksflskvl
//
LOCUS       WP_457691291             850 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691291
VERSION     WP_457691291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 850)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 850)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 850)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 850)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 850)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 850)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..850
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88254
     Region          2..847
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mlrtalrnvl ahkarlmmta lavllgvafv agtlifsdtv geaikkasak nlsgvavsvq
       61 alsddnaplv gkdgkrstvl ddklvntvra lpgvqsvrrn vagtatlagp dgipigkgwq
      121 niatnfqpdk dgydaryplm rgrgpaagne ialdeataka aghklgdsvr fatdgpvltk
      181 klvgivtted pqvtaggsla lfdtataqkl ylhpgqfdel vvgaapgadq qaltakvrav
      241 lpkdraeaas gaelaaeqsr miaeqnksls qtllvfagia lfvgifiian tftmlisqrs
      301 reialmravg asrrqvvrsv laeacllglv ssvigfglga giavglravl dangagfpdg
      361 pviisptavl aslavgvvvt vlaawlpsrk aakiapveal ntveappvlr slvirnslga
      421 ivtglgvaim fyvttlkssd dlpiamagsm ltltgviila pllsrplvsl agvittrlfg
      481 iggklakena lrnprrtaat asalmigltl itgmtvvgns aqqaldemta nglkadykie
      541 tstfigldtk lsqkvadipg veamaplrns gvnvgdsyvn ligtdlaaig kvarldftsg
      601 slaaagangi aisqtaaker gwqtgetlda tfddkkkakl kiagiyadne vvgeaigats
      661 lvdphmaelk nqellvkaad gptealekqi rhalddspll kvqdhadlrk enagqietvl
      721 yivygllgma viiavvgvvn tlamsvfert reigmlraig ldrsgikqmv rlesvvislf
      781 gavlgigvgi flswaggnlv seglptyell lpwgrlglfl lialvvgvla alwparraar
      841 lnmleaigaq
//
LOCUS       WP_457691293             266 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691293
VERSION     WP_457691293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28242
     Region          29..243
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mshaaafpgf sgspaptrat aavaaratdl skvygqgetr vvaldsvsve fgkaqftaim
       61 gpsgsgkstl mhcmagldai ssgsarigdv elaslndkql trlrrdkigf ifqafnllpt
      121 ltalenitlp mdiagrkpdr ewvsrvietv glsgrlahrp aqlsggqqqr vavaralaaq
      181 peiifadept gnldsrsgae vlgflresvr amnqtvvmvt hdpvaagyad rvvfladgri
      241 veelyeptad tvldrmrlfd skgrts
//
LOCUS       WP_457691295             236 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691295
VERSION     WP_457691295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..236
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25091
     Region          21..80
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(21,25,56)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(31..32,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          87..134
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
ORIGIN      
        1 mpvnthagep rrppfnaeaa rrlrealgmt pahvaygiga afgmriapet vaswergesg
       61 pseaeltala galwctpgel lgtpgtlrey rlalglapvd valrigmeps ayerleaggk
      121 wrgndrqaaa laevlrlplp allrftgrde klaelltsaa ttrwqayvrp vgklvalpkq
      181 qiqgvlqelh geyqatmtat lnwggggsad esgragrafl ddivaefwar aggqdp
//
LOCUS       WP_457691297             277 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691297
VERSION     WP_457691297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 277)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29789
     Region          4..260
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mplprhrrhh rlaadagllv aavafavplv wlvlasldae atlrvrlpes ptlhnfsavl
       61 tdeitftpml nsllicggat lltvvcaala ayplsrfrsr larpylltvl fstclpitav
      121 mvpvyglfvq vdlidtrygt alflaaaqlp faiwlmknfm dgvpkvleea awtdgaswpq
      181 tllrvilplm gpgvgvvaiy tfimmwgnff vpfmlllspe qlpasvsifn ffgnygaiaf
      241 gelaafsily stpvvalyil isgrlgggfa lggavkg
//
LOCUS       WP_457691299             307 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691299
VERSION     WP_457691299.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33086
     Region          14..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtgavarnaa rartpgapsa gglrtrllrw splvpatvll llflvgpigy cvliaftdtq
       61 ltgqesasfv glanfrqafg dpafrnavvl tlvftvlssl vgqntlglal aglmrrasrp
      121 vrsltgamvi tawvlpeiva gfllytffer rgtlnallew lqlpaqnwlf tlpimavsfa
      181 nvwrgtafsm liysaalagi pqevtesaev dgagglrrlw hitlpmirrs igtnlmlntl
      241 qtlsvfgliw vmtrggpgnr sqtlpvfmyd qaflksligy gtavalmlll vgalfsvgcl
      301 rllreev
//
LOCUS       WP_457691304             553 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457691304
VERSION     WP_457691304.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
REFERENCE   7  (residues 1 to 553)
  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   8  (residues 1 to 553)
  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   9  (residues 1 to 553)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20761992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..553
                     /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=58267
     Region          66..181
                     /region_name="sCache_3_2"
                     /note="Single cache domain 3; pfam17203"
                     /db_xref="CDD:435783"
     Region          217..548
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mrlprprpsg rlrgprslag qlfamqvvlv avvvmgcavf ayvsagrqae etarrqataa
       61 atavadspav vaaartknpt aalqpyserl rrdagvdfvv vmapdgtrwt hpepsaigkk
      121 ylghtgpalr geifpethpg vlgpsvrvva pvrdprhggr italvssgit ietisaqlrd
      181 qvlalvgvaa aalalgglgt yvinarlrrh thgmnaqels rmhdyhqaal havregllml
      241 dgqrrvalin dggrellgls ddavgrgvte lglpepltet llasgprvde lqltservlv
      301 vnsapvsgge rrgsvvtlrd htelqalsge ldsvrgftea lrsqaheaan rlhtvvslie
      361 lgraeeavef ataelelaqa ltdqvvgava epvlaalllg kaaqanergv aliltpdsri
      421 ddgllppglp srdlvtvlgn lldnaldaaa ptqehdtdep prvwvtarah egelllrvad
      481 ngpgvaadaa eeifqrgwtt ktdtdtparg rglglalvqq avrrnggtvt ldrapeggar
      541 ftvrlplrag asr
//
LOCUS       WP_457691315             522 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457691315
VERSION     WP_457691315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 522)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..522
                     /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=56301
     Region          <3..486
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          164..382
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtpwkrpdar qlhawapglv lwllvcgppa lafgslshtq pwatavafpl lgvsvllrrr
       61 rpltalalpi apslvisldl ftvaycaala vfgylagvrm srarpalwff savaagglpl
      121 cavvgrtvwp wfsllltlll nvmlpwllgr yrrqyaelar tgwqlaerme reqqavadrt
      181 rlrerariag dmhdslghdl alialragal evdprldadh qaaagelraa agtaterlre
      241 iigvlrtdde saprvpades verlvdrara sgmtvtleqa dgtgatalpa mtghalhrvv
      301 qesltnaakh apgaavrvrt graagqvqvt vantarpagp aadpvsggsg lvgldervrl
      361 aggalragpt peggftvsar lptsggtppe pferpeptaa erelalaqrq vqrrlrqtva
      421 vplallaalv vlssiyhlvs pswtvlerer yevlrlgadr srmesllpff aldappdgtp
      481 ppphgwtcey ysvrpgsdta yelcftdddr lvkksvvhrr dr
//
LOCUS       WP_457691321             155 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457691321
VERSION     WP_457691321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 155)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..155
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17063
     Region          20..144
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 marhdyeddp sapeanslvp aastvvvdds grvllqrrad nnmwalpgga mnfgeslpec
       61 avretreesg ldveligivg tytnprhvfa yddgevrqef sicflarpvd gtltvssest
      121 dvrwftpqei dglpmvpsir krvddwrqgn tpalr
//
LOCUS       WP_457691323             543 aa            linear   BCT 27-JAN-2026
DEFINITION  M4 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457691323
VERSION     WP_457691323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  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 543)
  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 543)
  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 543)
  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..543
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..543
                     /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=56830
     Region          48..543
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtprisrktr vagtaiaaaa llaagitagt agaspasapt pdgsplklsa shraellrda
       61 satkaqtake lglsaqeklv vkdvikdadg tthtrydrty gglpvlggdl ivhtakggai
      121 ksttkstekp vkvasttaki aptaaaksaq gtavkslsak kadaqtpkkv vwaasgtpvl
      181 aydtvvkgvk kdgtpsrmhv itdansgkkl fqydeirtgk geseysgsve lgtskegngf
      241 tltdkergdh kttnlenges gdgkpftded dkwgtgkpdd pqtaavdahy gagvtwdyyk
      301 kvhgrsgikg dgkgafsrvh ygksyvnafw ddecfcmtyg dgegdkaplt aldvaahems
      361 hgvtsatanl tysgesggln egtsdifgts aefyaksekd pgdyligeki dingdgtplr
      421 ymdkpskdgq sqdnwdsstg gldphyssgv anhffyllse gsgpkeiggv kydsptadgk
      481 kvegigrdka ekiwfkalte ymtsntdyka areatvkaat dlykagsaev kgveaawtgv
      541 avk
//
LOCUS       WP_457691327             198 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691327
VERSION     WP_457691327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21258
     Region          1..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marrhltpqd wstaalrama rggvaavsvn alagelgttr gsfywhfkdr dalltaalem
       61 weqdtttali selgamtdpr qrltalftta lgqesingle paivahadlp avapvlrrvt
      121 errigyltdl ytdlglapap arrqavaaya aflgwlelrr sacdivpeva ttgttatval
      181 ehlitelars akhqaepe
//
LOCUS       WP_457691332             630 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691332
VERSION     WP_457691332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 630)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 630)
  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 630)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..630
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66889
     Region          54..625
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttttgrps dgpedrpgpr prpaphppes gapapdafah dalpapkgaa rsllasllap
       61 hrrrvgavav mlllqqaavq agpllvayal dravpalrag dhgpllavav agvlcavvsg
      121 glqfgfielc arvsqdvlld lrgrifrhgq alsldfhery tsgrlisrat tdveslrell
      181 deglqeliti vlstgcitvt lvwldwglga aalasagpla llvrsfrrrs hqvhsaksta
      241 maavivkfte tlngirpvqa frrerpndaa farlnhrher ingdtllema ryvvasrlva
      301 nfavaaivlw gayrvatggl algvlaaavl ylrrlydpid rlgmflnsye saaaslqkia
      361 gllarrpgvp epavsaalpp vaavrpgrev tfrgvrfayr tggevlprfd ltlaagttva
      421 vvgatgagks tlakllarfy dptegqvlld gvdlrelsta vlrrgvvmvt qeaflfsgtv
      481 adnialgrpd atraqieraa kaigahdfit alpdgydtdv rkrggrisag qrqlvgfara
      541 lladpavlll deatssldip geravqramd tvlegrtalv iahrlstvdi adrvlvmadg
      601 rivedgppde liaargrfaq lhqawrdsvg
//
LOCUS       WP_457691334             611 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691334
VERSION     WP_457691334.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 611)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 611)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 611)
  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 611)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..611
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64997
     Region          19..602
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 madtaqttpr ndrtdlpqrs avrsllrlwp farpvrarlf taafvavlas cvslviplvl
       61 kwlvdgpvae rdpggawlgg gyllllglae allfglrrwl varplagvea amrealyrhv
      121 qrlpvafhdr wssgqllsrg ttdlqllrmf lafpltfllv ngvtilvggv lllaqrwslg
      181 lvllapvlpl mvlcsvfeak ygraarraqd qlgdlttvve esvlgiriik gfgrhrsqaa
      241 afrkltralr tselrkarll awiwgcnttl pelaiggalv lgtlqvadga lsagtlvafl
      301 stalalrwpv esigfllams neaatatdry fevldepavd apardtaaqd aaaadapard
      361 apapaglvfs gvqfrypdap pdsppllqdi tlhirpgetm alvgatgsgk ttltalvprl
      421 ydptagrisl dgrdlaalgr eevralvava feeptlfsat aaenvlmgge gaqesdlrra
      481 levaqadgfv dalpeggatq vgeqglslsg gqrqrlalar avvgrprfli lddplsaldv
      541 htealveaal rqvlatttal vvahrpstvl ladrvallsg gritavgthh allrdhpeya
      601 tlmsgegegd r
//
LOCUS       WP_457691340             412 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Streptomyces nigrescens].
ACCESSION   WP_457691340
VERSION     WP_457691340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=43443
     Region          70..251
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          257..384
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvqpnsgep arrrrwphqg ggplavllaa vlllvtgcgg ddgdgkkagk aggdkdasqv
       61 avtiapkdga devatsgalk vtaqkgrlks vkvkdgkgne vdgkisgdgg vwkpsghlga
      121 stkytvdaia vdgqgreaae hsgfttlvpk ntfigqyspe ngqrvgvgmp vsirftrgit
      181 dpgavedaie vsaepsvpie ghwfgndrld frpekywapg tkvtlklnln gvegrpgvyg
      241 tqakevsfti grsqvstvda kskqmtvvrd gktvrtipit agapgtetyn gkmvisekhl
      301 vtrmngdtvg fggeydikdv phamrlstsg tflhgnywsg raafgtrnas hgcvglfdqr
      361 gggdgstpaa wffrnsvigd vvvvknshde tiqpdngfsg wnlswekwka dr
//
LOCUS       WP_457691342             255 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691342
VERSION     WP_457691342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26990
     Region          3..246
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtvnlevadg vgtirldrpp mnaldiatqd rlrelaeeat rrddvravvi wggekvfaag
       61 adikemqvmd haamvvrska lqdsftavar ipkpvvaait gyalgggcel alcadfriaa
      121 dnaklgqpei llglipgagg tqrlarlvgp skakdliftg rqvkadealt lglvdrvvpa
      181 aevheqahaw aarlaagpal alraakesvd agletdidtg ltiernwfag lfatedretg
      241 mrsfveegpg kakfr
//
LOCUS       WP_457691344             179 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691344
VERSION     WP_457691344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19596
     Region          56..176
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mmggmagleg meqprprsdp aaarrgipga drdrapaprr pvsaalepag dptlgevrlp
       61 srpqsagiar rltaavllkq wsltpqlaeh avllvselvg navrhtgart fglrmlrrrg
      121 wirievrdps rglpclmpvq emdlsgrglf lvdklserwg vdllprgktt wfemriadr
//
LOCUS       WP_457691346             256 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Streptomyces nigrescens].
ACCESSION   WP_457691346
VERSION     WP_457691346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27118
     Region          86..243
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mpvsasptrk laaigavial vvaviaigva vgtsvegdrd tgrpeaaasa apqedpaqqk
       61 mfddlakrts rradgdplai gkkdapvvlv eyadyqcsfc grftretqpg likkfvdagt
      121 lriefrnftv fgadseraar aswaagqqgk fwqlhdalya ktrkgaalae dklvdlarts
      181 gvddldkfra dlksadaera lkkdqdegyr lgvqstpsfl vngrpvagaq pyevfaqavq
      241 kaaeraghgp aakgak
//
LOCUS       WP_457691347             279 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c biogenesis CcdA family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691347
VERSION     WP_457691347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=28885
     Region          2..185
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mtdigylaaf lggalallsp csalllpaff ayslstpgrl vartgvfylg lattlvplga
       61 astaasrlfn ghrdlliavg gwvviamgla qilglgfasr raqaaaarit prsavstfll
      121 gcvyglagfc agpilgavlt vtavsgspvy gasmlavyal gmalplfvla llwdrcklgt
      181 rgwlrgreft lgklrlhsts llsgvffigi gvlflrfngt salpgildad tefraeewat
      241 rigngvpdvv liavaalvva gvlgrfalrp ekkqrdgse
//
LOCUS       WP_457691357             406 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457691357
VERSION     WP_457691357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 406)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44539
     Region          2..370
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(15,207..209,269,291)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 mkitlllhna yaiggtvrtt lnlaaaladr hdveivsmlr hrevprftvd prvrlvplvd
       61 trvgsedmad plfgepardf plaekrhrqy srlvdvraae llrgadadvl igtrpginvy
      121 larfgprral riaqehlrhd ahskrlrtel achyrtldav vttteadaav yrarmplpgv
      181 rvlavpnivp apagppsegt skviaaagrl vrgkrfdlli eafstvaakh pdwrlrihgg
      241 gsrraqlqgl idelglsgqa eltgprspie aefakasiva sasdaesfgm tlveamrcgv
      301 pvvstdcplg paeiihdgtd gllvppgdar altgalltli edpgrrrtma eraresshry
      361 dpepiaeryq vlfgelrstr grrawqriva rarararrll rralqr
//
LOCUS       WP_457691359             261 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457691359
VERSION     WP_457691359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  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 261)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28131
     Region          2..250
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mthsvllaed drpirtaler altlegyqvt avadgiqala aahrerpdvi lldvmmpgid
       61 glqvcqvlra eqdrtpilml tarvetadri agldagaddy vvkpfeveev farlrallrr
      121 ttagsagaed gggpgtgpdg vddpgeagad magayearva dsgvveaadl ridgpsrraw
      181 rgereleltr tefellella rnagivldhs tiydriwgyd fgpgsknlav yvgylrrkvd
      241 vpgsrpliht vrgvgyvlre d
//
LOCUS       WP_457691361             517 aa            linear   BCT 27-JAN-2026
DEFINITION  HAMP domain-containing sensor histidine kinase [Streptomyces
            nigrescens].
ACCESSION   WP_457691361
VERSION     WP_457691361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Dunin-Horkawicz,S. and Lupas,A.N.
  TITLE     Comprehensive analysis of HAMP domains: implications for
            transmembrane signal transduction
  JOURNAL   J Mol Biol 397 (5), 1156-1174 (2010)
   PUBMED   20184894
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Hulko,M., Berndt,F., Gruber,M., Linder,J.U., Truffault,V.,
            Schultz,A., Martin,J., Schultz,J.E., Lupas,A.N. and Coles,M.
  TITLE     The HAMP domain structure implies helix rotation in transmembrane
            signaling
  JOURNAL   Cell 126 (5), 929-940 (2006)
   PUBMED   16959572
REFERENCE   5  (residues 1 to 517)
  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   6  (residues 1 to 517)
  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   7  (residues 1 to 517)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20436615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..517
                     /product="HAMP domain-containing sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54478
     Region          <151..>298
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          227..278
                     /region_name="HAMP"
                     /note="HAMP domain; pfam00672"
                     /db_xref="CDD:459898"
     Region          277..489
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpgphdragt gpragrrslr vrlrarlrsw rrggsaawlr trrpaslrta favafaagaa
       61 avtvlvgfls ydaaarlvri deksvfsqvv rdlriqvqek pfgpadyata dpdhngprdd
      121 ltrpsrtevq ilgpggrive rgrpvlpagp aerriadder agehaeread igdeeyhvat
      181 valgggrgav qvaqkfsete dllsalqqrt allaaavial agaggwwlar ritgrlvrlt
      241 avaesvaehg rldvpvpvag rdevarlgra fddmlgrlas avqdqqrlvq daghelrtpl
      301 tslrtnisll krfdelpsda reelladlag earelsdlvn elvdlaagqr dddplaevsl
      361 aeaaekaaas arrrtgreit vrtvrpavve grpaalhral tnllenaakf daggtapiev
      421 vvtgarfevl drgpgiadad ltrvfdrfyr aaaarglpgs glglaivrei atahgghafa
      481 ihrpgggatl gftvgtgkgt gsgtgsggah aetgpgs
//
LOCUS       WP_457691365             252 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatase PAP2 family protein [Streptomyces nigrescens].
ACCESSION   WP_457691365
VERSION     WP_457691365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=25863
     Region          51..218
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(134,141,158..160,202,208,212)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mtaagpepgp gaegprpepv pqpgtrprpg taalltlaav caalfavtal tvslrngtpf
       61 aaeqaavrws tahqgepsrs magaltaags gllpylmvvl agllagrrar grlravccav
      121 vvlaagqair yglmellarp rppaadwtgh asgyafpsgh atasvlaagi lawgiarrar
      181 pavartwcvv lalwaagvgl triylgvhwp gdvlggwfla agllalalll epfalhrpdr
      241 srtrprgaps he
//
LOCUS       WP_457691368             564 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457691368
VERSION     WP_457691368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..564
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58949
     Region          2..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdmsagerkg lslfalimig igsifgsgwl fgagaaaqva gpaalvawvi gvvfigmiam
       61 syaevgsayp ipggmarygh lshgpvlgfl tgwavwiata slipiesiaa tqymtswsfg
      121 wakdlvdpat hqltlsgtam alvltlalwl tcfwsvqlla rantvltlvk faipvlavva
      181 ligsgfhtsn ftahggfapy gwpavltavt tcgvvfafng fqavvnlgga aknpgraipl
      241 alvgalalgl viylalqvsy lgsvppelle rsggwqgvnl nspfadlagl lmlhwvvtml
      301 qfgafispag snianvasaa ymvtnlaetg ffprklaavh prygtarpam wlnlgfsvll
      361 lltvgrswha lagvvsaamv isyligpvav gvlrrtrpdl prpfrlpaag vlcpvtfafa
      421 acalywskwp etgkitlltl vsapvaalvl wrrgeiakgg easgkggraa sllrqfaptw
      481 wmiaflvwta tvsalggref ggrgvlpgel gtaviavtap lfyfwavrsg vrahergltg
      541 tlspdettpa ptvtaddgrr mvsv
//
LOCUS       WP_457691370             419 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydroxymethyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457691370
VERSION     WP_457691370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Stover,P. and Schirch,V.
  TITLE     Serine hydroxymethyltransferase catalyzes the hydrolysis of
            5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate
  JOURNAL   J Biol Chem 265 (24), 14227-14233 (1990)
   PUBMED   2201683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..419
                     /gene="glyA"
     Protein         1..419
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0070905 - serine binding [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=45086
     Region          5..419
                     /region_name="glyA"
                     /note="serine hydroxymethyltransferase; Reviewed;
                     PRK00011"
                     /db_xref="CDD:234571"
     Site            order(12,14,21..22,31,36,54,72..73,81,96,103,138..139,263,
                     281)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(35,55,65,98..99,126,176,201,204,229..230,236,366)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(35,126,230,366)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(57,64,121,125,127,255,350)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 msllnsslhe ldpdvaaavd aelhrqqstl emiasenfap lavmeaqgsv ltnkyaegyp
       61 grryyggceh vdvveqiaid rikalfgaea anvqphsgaq anaaamfali kpgdtilgln
      121 lahgghlthg mkinfsgkly nvvpyhvdek tnlvdmeeve rlakehrpkl ivagwsaypr
      181 qldfaafrri adevgaylmv dmahfaglva aglhpspvph ahvvtttthk tlggprggvi
      241 lstqelakki nsavfpgqqg gplehviaak avsfkvaate dfkerqqrtl dgarilaerl
      301 vqddvrqhgv svlsggtdvh lvlvdlrdse ldgqqaedrl hevgitvnrn aipndprppm
      361 vtsglrigtp alatrgfqae dfrevadiia ealkpsydtd alkarvtala gkfplypsl
//
LOCUS       WP_457691383             371 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691383
VERSION     WP_457691383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40726
     Region          31..360
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtdssedkte tavagsaaat akeapqkaaf lqvkdlkvhf rtddglvksv dglnfslekg
       61 ktlgivgesg sgksvtslav mglhrasrqq rgkvdmsgei wldgkelvsa dpdevrrlrg
      121 remamifqdp lsalhpfysv gnqimeayrv hndvdkktar kravemldrv gipqpdkrvd
      181 dhphqfsggm rqramiamal vnnpelliad epttaldvtv qaqildlird lqkefgsavi
      241 iithdlgvva eladdllvmy ggrcvergpa ekvfyepqhp ytwgllgsmp ridreqtdrl
      301 ipvkgsppsl invpsgcafn prcpyadvpk dnltrtvrpd lreaggghss achmsqeere
      361 riwteeiapk l
//
LOCUS       WP_457691385             374 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691385
VERSION     WP_457691385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40434
     Region          25..353
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtettddqnk kiplqkgaet sadapsdaep llkvrglvrh fpitkgllkr qvgavqavdg
       61 idfdvrpget lgvvgesgcg kstmgrlitr ldeptggsie fqgqdithls pgrlrpmrrd
      121 vqmifqdpyg slnprhtigg ivstpfrlqg vepeggvkke vqrllelvgl spehynryph
      181 efsggqrqri giaralalkp klvvadepvs aldvsiqaqv vnlmddlqee lgltyviiah
      241 dlsvirhvsd riavmylgki veladrkaly etpmhpytka lmsavpvpdp krrtqrdril
      301 lkgdvpspin ppsgcrfrtr cwkatevctt tepplvapat ghqvachhpe napdqapaaa
      361 tasggpagqa ptgk
//
LOCUS       WP_457691387             469 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457691387
VERSION     WP_457691387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..469
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51352
     Region          52..458
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(164,166..167,298..302,317,320..321,324,339,343,398)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 malsrsarrt srwlalatav asvatlaaap gaspgapgvg dpyfprlgng gfdalhydlg
       61 vsyhpgsgrl dgrtkltara tqnlsafdld lqkltvdsvr vngrrahfar sgdeiavrpd
      121 fplrrgkkft vtlayhgvpk plggpiifgs pygwmktkdg vfvacepnaa stwfpssdhp
      181 gdkatydiri dapkgltgvs ngrlissgea hgrsyahwre qrpmatylat atigkfdvrt
      241 gttpggtpiy vatdptlptg kvdvygitae atdywsqvfg pypfeetgai vddmpqagfs
      301 levqskpvys avrnettivh elahqwfgds vsvkqwqhiw lnegfatyaq wlwaehrgtr
      361 tahdafraay kdlpaeddfw kqkiadpqrd tmfagavyqr gamtlqalre rigdkafftl
      421 lpvwttqhry gnaetsqfia laekisgqql ddlfdawlkt eskpplpar
//
LOCUS       WP_457691388             348 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457691388
VERSION     WP_457691388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20862280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..348
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38435
     Region          52..122
                     /region_name="ParB"
                     /note="ParB-like nuclease domain; smart00470"
                     /db_xref="CDD:214678"
     Region          58..231
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mvhheriqrs rtngsehted qseeqaedrt qkgvrhgghr vpltalntsv kvrldgpder
       61 htralaesge fppilvhrat maildgvhrf haarlrgetd iavrfcdepl etafvrsvre
      121 nvrhglplsr sdrtaaagri laahphwsdr svaraaglsp rtvadlrkda rsgtdpthrl
      181 grdgrlrptd aderrrraae ilrsqpdssl rrvgrlagis attvrdvkrr idsgqdpvpg
      241 srpehpevpp prngpptidp tdfpalvkrl cnepslrhsa dgrlllrlld lhlaaqrssa
      301 riasvvpahq iatvavvaar crqiwqemaa gfentrlgld ekavaenr
//
LOCUS       WP_457691389             211 aa            linear   BCT 27-JAN-2026
DEFINITION  trimeric intracellular cation channel family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691389
VERSION     WP_457691389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22075
     Region          1..199
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mlhvlylagv aafaasgvla ayranmdpfg glvlafaasi sggtlrdlil drqplywthd
       61 wvlltviicv gvgtmaylrf wqlphkallv vdaiglavvt vigaraaida gatplaviil
      121 avltgvagev irdvlcgefp plllredvya iaalaggccy lllhhlgtga tpaaaisagv
      181 vfglrmgavy lglhlprpqq lrdrrgrqes d
//
LOCUS       WP_457691391             282 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691391
VERSION     WP_457691391.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  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 12150045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="thioesterase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29598
     Region          29..276
                     /region_name="4HBT_3"
                     /note="Thioesterase-like superfamily; pfam13622"
                     /db_xref="CDD:463937"
ORIGIN      
        1 malvthgnse fdrdtavtrr apgvydahls agwtiiqavn ggyllalmgr algdalphpd
       61 pmsvtahylt asvpgpavir tevvrtgrtm stgtagliqf aedgseverl rvlaaygdlg
      121 alpddvrtta kppaippyeh clgtdsapdg rpaipgstai aerlalrldp atagwavgap
      181 sgkgemrawf gladgrepdp lsllltvdal pptafemgls gwvptvelta hirhrpapgp
      241 lrvaittrnl aggfleedae vwdsedrlva qsrqlaravl qg
//
LOCUS       WP_457691397             337 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457691397
VERSION     WP_457691397.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  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 337)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 337)
  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   5  (residues 1 to 337)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36950
     Region          50..>289
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtgqsaagah ddpgaepedw wvfrgpaqlp apppwrhlpa grgtaprapy llerneisvv
       61 naalhlhrpl lvtgrpgagk sslaravaee lglgemlrws vnsrstlqda lyrydavgrl
      121 reaslrrere aphgsarrpr arrataagdi gqylrlgplg salaagrprv llvdeldkad
      181 idlpndllvv leegefeipe larlpehqqe vqvllsgsre rvavhrgvvr cthfpvvimt
      241 sngerdfppa flrrcvrldl peptgdrlrk iiehnlgeqa vaaaedliev fhqraktqtl
      301 atdqllaavh lrisgadltk eellaavlhr ldesmsp
//
LOCUS       WP_457691402             389 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine desulfurase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691402
VERSION     WP_457691402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40131
     Region          1..387
                     /region_name="NifS"
                     /note="Cysteine desulfurase/Cysteine sulfinate desulfinase
                     IscS or related enzyme, NifS family [Amino acid transport
                     and metabolism]; COG1104"
                     /db_xref="CDD:440721"
ORIGIN      
        1 mvyldhaatt pmlpeavqam taqltvtgna sslhadgrra rrtveeares lavslgarps
       61 eivftaggte adnlavkgly warraadpar trvlaspveh havldavewl aehegahvew
      121 lpvdsygrvh aeglraaiar npadvalatv mwanneigti qpvreladia aefdiplhad
      181 avqavgqlev dfaasglaam tvsghkiggp ygigalllgr eyapvpvlhg ggqerhvrsg
      241 tldtpaiaaf aaagrhavah redfardiga lrddlvkavr aaapdavlgg dpdpagrlpa
      301 nahfsfpgce gdslllllda qgiacstgsa ctagvaqpsh vllatgmspd largtlrfsl
      361 ghtstaedva alaeaigpvv erarsagls
//
LOCUS       WP_457691404             242 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457691404
VERSION     WP_457691404.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /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=26738
     Region          70..225
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mqrmgkrdge kgggqeappg itrrralwig gggavaagta afagrdvlaq wwwrlpgndk
       61 prkagavdhr gaqwvaaspe nyrradrpad ygidrvvihv vqgsyatald vfqdpdheag
      121 ahyvvrkdgh iaqlireldv afhagnrgyn ersigieheg fvdrpesftd amyassarlt
      181 asicrrygfp adrehlvghv evpgtdhtdp gphwdwdryl rlvraelrkp vrpgesppvr
      241 kt
//
LOCUS       WP_457691417             702 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces nigrescens].
ACCESSION   WP_457691417
VERSION     WP_457691417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 702)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..702
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=74692
     Region          7..675
                     /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 mkptdsaapa srlrrlvvpa lpativtvag lalatgvivt lgegdalfpg gsvgwslail
       61 tgiivghlva lgrdrwwggt gsgaalalav lllygwmpav lvslsvvvlv gaarrhrwrq
      121 avvhgavdil glgtaalgla afgvvssvrh pwappawnla vlpevvvtaa gyllvsrgll
      181 wisltprtgq lpaiprtavv rqalvgiall gispliavca ihaplllplf avplialdst
      241 lwiararaee qlrdpltglp nrqwllertw salddaervg arsalvlidl drfrsvndtl
      301 ghlagdrlll qiadrlrhal prgaeaarlg gdefavllpt tdsltssqra arnlvaalgs
      361 pldldgltlv leasagvavf pdhaldaegl lrradvamyq akrdrsgvel yeakrdgntp
      421 drlgllgdlr raldagdvel hyqpkvgfdg hvaglealvr wvhpdrgrvp pdefiaiaes
      481 sglmprltey vletalaqva rwramglevp vavnvsprdv hspgfagava arlarhrvpp
      541 galqleiteh vlledpqraa dtlagltahg vkmslddfgt gysslvhlrr lpvselkidr
      601 sfvarlavdt edaeivrctl dlahslgllv vaegveddet werlrdlgcd avqgwlvaaa
      661 mppdettawl rargergwqr esetaalaae kaaerpsgqv ln
//
LOCUS       WP_457691426             334 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457691426
VERSION     WP_457691426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  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 334)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35902
     Region          2..310
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(21,209..212,215,265,283..287,290,293..294)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(51,56,85,129)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mkhrqlgtpg ptvstlglgc mgmstsygvp ddaeslrtld raaelgitll dtadaygrga
       61 neeflgrwlr srtasqrdel vlstkfglrh daatgrvnev dtsaawvrea chaslrrlgt
      121 dridlsymhr rdpavpieet vgamaelvaa gavrhlglse vspqtlrrah avhpisavql
      181 eyslftrevv egemlatcre lgigivaysp lgrgmltgal aarddltaed arrrwprfae
      241 enidrnlrlv qavrttaesl gctpaqavla wllaqgediv pipgtkrrsy leenaaaagi
      301 algpeqaarl raavpdgava geryplaale rlgh
//
LOCUS       WP_457691430             273 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691430
VERSION     WP_457691430.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30846
     Region          16..73
                     /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          90..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mqpankpkri tswhvigaql shfrraarit qpalaervgl hedtigsieq grrplkldla
       61 etldelldtk galavavakv pereklpafv qdlveheeea ltllsyqnqv vpgllqiepy
      121 arevfdclyp ppdpdeaaew istrldrqkl lerrkpqpml nfileevilh rpvggpdvlr
      181 eqirhlrqca elpflglqim ptkrashagl dgpmilletp qheylayieg qlvryliedp
      241 dqvstlqqky gmlrsqaysp neskgllddl lge
//
LOCUS       WP_457691432             137 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691432
VERSION     WP_457691432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15263
     Region          21..134
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mqkeiqtlca rtvryrrerr svplarefar taladwdler raddvllcvs elatnallhg
       61 vppgreyrlc lllgedgllr vevhdsgdge pripmpgygg agesgrglll vsaladkwgv
      121 gernpgkivw cewwpvw
//
LOCUS       WP_457691434             303 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691434
VERSION     WP_457691434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  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 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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18524816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /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=32512
     Region          8..221
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          <237..301
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mtsrqfqetl rylaamglvr psrdgalpvp vspetafall ldtaeqtmad rlvglrslra
       61 afsaladslp vppsgggqpa armevrvgaq riaesmdama asarrevlal rpndpaaper
      121 wdeagrrgvq vlargvslrt vhlhstpena aghahlcglr ragaevrlam tlpfrltlvd
      181 evralvtlgs dgeeatalei hgaamcrllr qvfehcwvya erltdagsgg aqqgsheavl
      241 tereqmvlrm faaglkdrai arnlgvsdrt lrrtitpllt klgaasrfqa gmmavergvl
      301 srv
//
LOCUS       WP_457691424             300 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457691424
VERSION     WP_457691424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31638
     Region          10..297
                     /region_name="F420_MSMEG_4141"
                     /note="probable F420-dependent oxidoreductase, MSMEG_4141
                     family; TIGR03620"
                     /db_xref="CDD:274681"
ORIGIN      
        1 mpqhalasri grigvwhggl gqvpgavarq taaeieqlgy galwfgetpa tesmslagll
       61 laateritva tgianiwvrd asaahaaaqt laeaydgrfv lglgashapl vdarghsyak
      121 pltavrayld amdeapydgp vadppparvl aalgpkmlel ardrtagahp yfvtpehtar
      181 areilgtgpl lapeqavlle sdpatarsla rehhtrfylq lpnytgnlrr lgfgdddfag
      241 ggsdrlvdai vawgdvdavr rrvqehldag adhvaiqpla tdrglgidql relapalids
//
LOCUS       WP_457691436             320 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457691436
VERSION     WP_457691436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32470
     Region          30..293
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mttvttrtar pgnrplwlid vpvvlvavvw gssylaakel atgttviall llrfvlatpv
       61 mavvagrgit rltgretaag avlgmllsgv lvletfgvvh tsatnaglli sltmiftpla
      121 eavatrtrpt ggfvgaaals vtgvalltqg sgftapssgd llmllaavar tvhvmamsrm
      181 kavrstdsga ltvvqfaaav vvfalaspfa avspvdaaaa yspqqwaall ylalmctlfa
      241 ffvqmwavrr tspsrvslll gteplwaavi gvalggdrpg algvagaalv ligttwgrqa
      301 tapppaaedr paatqpagav
//
LOCUS       WP_457691444             747 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457691444
VERSION     WP_457691444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..747
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77692
     Region          8..716
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mtalarwclr rrivvtvlwl aafagvavaa gvtgaaysnn yevpgtesgq atarmakafp
       61 grsgdsdtlv whtdsgtvrs gavqktmrht lekiaglpgv sevqgpygtp adgpgarqis
      121 kdghtayalv rfdrptddld vdrvqkvvdt aqtasrpglq ielggagial teapraqlae
      181 iiglcaaavv lflafgslaa tflpiitala avgtasagit llshamtvad fapmlgmlig
      241 lgvgidyalf ivtrhrkglr aglpvdeaat ravavsgrav vfagatvcia llgmlilrls
      301 flngvalaas ltvvltvaaa vtllpallgl igmralsrre rrrlaehgpr perptgiaar
      361 wsgfverhpk llgavaaavm lalalpafgl hlgtsdqgnn patsttrkay dllagdgpga
      421 grgsgfgpgf ngpltlvgtl dgakdriafd alpdrlrdtp gvarvsrpvf dgshstgvit
      481 vvptsspqsr qtsdlverlr tevlpeagga atlrvqvggi tasyddfasv ivgklplfig
      541 vvialgslll llafrsigip lkaalmnvaa vassfgivva ifqwgwgsel lglgsagpie
      601 pflpvimvsv lfglsmdyqv flvsrmyeew qlthnncrav rvglaetsrv insaavimia
      661 vfgafvlsgd riiamfgigl aaavaldafv lrtllvpalm hllgganwwl pswldrwlpr
      721 isiepppepg avrlpgpqdg ekplvgv
//
LOCUS       WP_457691451            1051 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691451
VERSION     WP_457691451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1051)
  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 1051)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Rosinski,J.A. 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 1051)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1051
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=113318
     Region          <8..943
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          985..1045
                     /region_name="GerE"
                     /note="Spore transcriptional regulator GerE (stand-alone
                     HTH domain) [Cell cycle control, cell division, chromosome
                     partitioning, Transcription]; COG5905"
                     /db_xref="CDD:444607"
ORIGIN      
        1 mlssvetrsv spvfvgraae lavlgdaldr iaasgepqal liggeagvgk trlieefges
       61 arargalval ggcieigseg lpfapfsail htlnwhlrde laaavagqeg elsrilpelg
      121 eapgeahdee tgrarlfelt arllerlaah rtlvivvedl hwadrstrel layllkalhd
      181 anvllvatyr sddihrrhpl rpflaeidrm rtvrrvelar fnreevrsqi agingsdpek
      241 dtvdrvykrs egnaffveel argladgclh glsdplrdll lvrvealped aqrvvrtaae
      301 ggstvehell aavcrmpedd liealraavg sntlvptqdg tgyrfrhala reavvddllp
      361 gertrlnrry aealeanpsl vraevcaarl asywykahda akalpavlaa svqarrrhay
      421 aeqlrlldra lelwddapte vrqgvrpvdy aeaypacgsd dgdalrfldl laeiavaarl
      481 sgdierafti tkralrslrh endpppssqh gssrgdplrk awflvqrsrl cqgtgrgngw
      541 edlgsaqelv rglppssvha evlaavaswe vlhepgpgtf ataeravela qlvgdehael
      601 nsrltlaglr idsgevdegl adfrmslera vdrgyfavig rgqvnlasal egvgrsreav
      661 dvtdqgielt tryglkdsts wvlgnraesl qslgrweear ravadarrla qnpraialaa
      721 crradlalde gdlakaerel avtqeyygth dpqpqnalvm arhalriaar qgrlldarsi
      781 lqqaldagfp pgtqryawpl lwaattaead arglpaaepg raailarird aakrlpqlcp
      841 vwsafglavd aelrraegre tpdawagava afeplerphe laracyrwae sllhgserat
      901 tglhgrppre aalllltqah taavtmgarp ladelellaq rariplpglt paaaagtagt
      961 aagtgraaae asapsgtapa eslgltprer evlrlvadgr snrqiadalf ispktasvhv
     1021 snilaklgvs grgeagavah rlrlfgeptp g
//
LOCUS       WP_457691461             972 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces nigrescens].
ACCESSION   WP_457691461
VERSION     WP_457691461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 972)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..972
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=103851
     Region          236..919
                     /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 msapgamlsr ppasagnpps avpqivlavv cggyaigaaf gwgspevaai mgdfglsfaa
       61 flaavscgly arkrrsrfrp awmlfaassg maglgngvwg wyeviegvtv pspsladfcf
      121 llfappaivg llvlakrpvt ragwvclgld swliagslvt lswslalaht ahfqgrsvaq
      181 salslaypll divlvsmvla lhfrrssvhr saintavaal altvlcdalf sspllrehyr
      241 sgqildagwf agsmllayap wvarrageec taeeakpaar rvqphgsrpi agslaaltpy
      301 laaavctlgi ltnvldgrri drvvlftgct vvlalvvrqg imlldnitlt qelaqkenhf
      361 rslvqgssdv imiaaptgvl ryvspaaagv ygrdaeelvg selaslihpe dlgrvvhevr
      421 rflaaapede pttriecrfr ageqrsggdg wlnvestvnr hhgglifnsr dvtervrlqa
      481 qlqhnashda ltdlpnralf tervtqavtg rrasdhdtav lyidldgfkq vndtighqag
      541 dellvqaarr ladsvrsgdi aarlggdefa alitgdgtrd raarefrihe iadrlrikls
      601 epyridgrdv rvaasigvaf adpgvspagl lrnadlamyr akqagkgrve lyapqmqnev
      661 adraelagkl rtalsdgafa llhqpvvela tgrvtavaah arwrsaqgil ftpaeflrvg
      721 drgrladdgd raaeldrwql eeaveqaaar hragypvpva vrlsarrlld halspkgves
      781 lltrhglpsr alvvelsesd priplddler rlvalrrlgv rialdgfgsg yaaisalrrl
      841 pvdvlrldrg lvdgvvesar lhkitagllr iagdlgmqsv adgvdlpeqv lalrsmgcth
      901 gmgtafsgpl dehrlrrslt hahypvpdla gqgravvltg sglparqggp vgpeslvhpp
      961 lrsnsetsvp pt
//
LOCUS       WP_457691468             208 aa            linear   BCT 27-JAN-2026
DEFINITION  PRC-barrel domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691468
VERSION     WP_457691468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  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..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /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=21599
     Region          11..>58
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnaplgdapq sltglhvvda dgskvgtvqq vyrddatnep ewitvrtglf gmketfipla
       61 garrtgdelh vphakatikd apridanghl dpseeeelyr hygmtrpgma apdptgptsr
      121 pdpratgdta ppaptggern kliegpmaga gagagagtrs gpgagdtars reqtpetgae
      181 ehergpgkre sgpdhgpggr regpdrpr
//
LOCUS       WP_457691107             213 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691107
VERSION     WP_457691107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22911
     Region          16..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msaieqteat rprgtrlprr arrnqllgaa qevfvaqgyh aaamddiaer agvskpvlyq
       61 hfpgkldlyl alldqhceal lhsvraalas tsdnkqrvaa tmdayfayve dpggafrlvf
      121 esdltndpav rervdkvsle caeaisavia edtglsqdes mllavglggv sqvvarywls
      181 sesqvprdta vqlltslawk giagfplqgg dth
//
LOCUS       WP_457691470             199 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691470
VERSION     WP_457691470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21004
     Region          4..192
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mghredlleg akrcllekgy arttardiva asganlasig yhygskdalm rqaiiassee
       61 wgagvaqvpa adeampdeag plerfaavwd lflqriater efiaaqvevl gllprdaalr
      121 eaigevlpeg geglvaifeg vpdtevdaea arvvgsfyqa lltglmvqsl ltpdampsgr
      181 dlatalrrvt agevlgkke
//
LOCUS       WP_457691473             456 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457691473
VERSION     WP_457691473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..456
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47138
     Region          <321..456
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrgdyqqlvd eisaalgapa tledrdfgli afgahegddd evmdpvrtrs ilqrrstaav
       61 rawfeafgia raktalripp dpaagvfrgr iclpvrhrgi vhgyvwlldd ghltdlelgs
      121 rgappdpria qametaarig alladearag selgdllrel viaqpdgqpa aaaalrdalr
      181 dslrftpgap ltlvavvpwd tsdtdaaplp slpgllaaca lpagggpadg pavaadetep
      241 aahpapgrtg ragpagllqp aapvpalaal vrlrasgasa pahtvaehll rsprasagpa
      301 egraarggar gggsghhppl rpaaagigvg treltdlpat wrealdaara ahaeprlgpi
      361 tqwdaigpyr mltalpgtap dpaigpllap ahaelartae vfldcagqas rtahalgihr
      421 qtlyyrlgrv ekltgldldd gehrlllhma lkaarl
//
LOCUS       WP_457691479             535 aa            linear   BCT 27-JAN-2026
DEFINITION  purple acid phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691479
VERSION     WP_457691479.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 535)
  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 535)
  AUTHORS   Klabunde,T., Strater,N., Frohlich,R., Witzel,H. and Krebs,B.
  TITLE     Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on
            crystal structures
  JOURNAL   J Mol Biol 259 (4), 737-748 (1996)
   PUBMED   8683579
REFERENCE   3  (residues 1 to 535)
  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 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..535
                     /product="purple acid phosphatase family protein"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=58268
     Region          90..195
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          200..505
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
     Site            order(210,212,237,280..281,372,408)
                     /site_type="active"
                     /db_xref="CDD:277317"
     Site            order(210,212,237,280,372,408)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277317"
ORIGIN      
        1 mtgnprgaap lpshtprvgi peqlaarmsm peqhdylrtk lsrrgllrts aatagvvags
       61 gllagsahgv aptllssptt aavdgslvap fgrhlafgad pksqmrvswq vplavkrpyl
      121 rvglqpwdlg rkieaevrel htpslsaklp avqqyylhaa ldglrpgtty yygvghegfd
      181 padprhfstv gtfrtaparp eafvftafgd qgvsyhalan dqlilgqnps fhlhagdicy
      241 adtdgdgseh daydarvwdq flaqtesvak svpwmvttgn hdmeawyspn gyggqnarwt
      301 lpgngpdakn apgvysftyg ntavvaldan disyeipanq gytdgrqtrw ldrrlgelra
      361 adgidflvvf fhhcafsttt shasdgavrd awlplfekhq vdlvvnghnh vyertdalks
      421 grvtkkmpig asvdttregi vyvtaggagr alydfpvpds yeghvkdldh vdtyhwskgq
      481 aktketvews rvrytgysfi avevtpgrqp rmkvtalaes geridhfevt rspaq
//
LOCUS       WP_457691489             564 aa            linear   BCT 27-JAN-2026
DEFINITION  urease subunit alpha [Streptomyces nigrescens].
ACCESSION   WP_457691489
VERSION     WP_457691489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Mobley,H.L.T.
  TITLE     Urease
  JOURNAL   (in) Mobley HLT, Mendz GL and Hazell SL (Eds.);
            HELICOBACTER PYLORI: PHYSIOLOGY AND GENETICS;
            (2001)
   PUBMED   21290719
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11486466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..564
                     /product="urease subunit alpha"
                     /EC_number="3.5.1.5"
                     /GO_function="GO:0009039 - urease activity [Evidence IEA]"
                     /GO_process="GO:0043419 - urea catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=58282
     Region          4..564
                     /region_name="ureC"
                     /note="urease subunit alpha; Reviewed; PRK13207"
                     /db_xref="CDD:237305"
ORIGIN      
        1 mtgsidphey asvhgpragd rvvlgdsglv vrvesdaqkp gdeflagfgk tardglllka
       61 aavretcdvv isnvlvidav qgirkmsigi regrihaigr agnpdtldgv dvvvgtgtsi
      121 vsgegmiata gavdthvhll sprvmeasla sgvttvigqe fgpvwgvgvn spwalghafs
      181 afdawpvnig flgrgsssgd aplvealaeg gacgfkvhed mgaharaldt alrvaedhdv
      241 qvalhsdgln ecltvedtlr vldgrtihaf hiegcggghv pnvlkmagvp nvigsstnpt
      301 lpfgrdavae hygmivsvhd lktdlpgdaa mardriragt mgaedvlhdl gaigitssda
      361 qgmgragetv rrtfamagkm kaelgpmqgd gahddnarvl ryiakltinp aiahglshei
      421 gsievgkmad vvlwkpqyfg akpqlvlksg fpaygvtgdp naatdtcepl vlgpqfgayg
      481 atpaeisvaf vagaaaeqgg dgmptrrrrv avrgtrgigp gslvhnsrvg qvqvdgssgl
      541 vtldgdpmrs epadtvslsr lyfl
//
LOCUS       WP_457691491             346 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691491
VERSION     WP_457691491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
REFERENCE   2  (residues 1 to 346)
  AUTHORS   McGraw,W.T., Potempa,J., Farley,D. and Travis,J.
  TITLE     Purification, characterization, and sequence analysis of a
            potential virulence factor from Porphyromonas gingivalis,
            peptidylarginine deiminase
  JOURNAL   Infect Immun 67 (7), 3248-3256 (1999)
   PUBMED   10377098
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006811
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0004668 - protein-arginine deiminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37657
     Region          12..345
                     /region_name="AguA"
                     /note="Agmatine/peptidylarginine deiminase [Amino acid
                     transport and metabolism]; COG2957"
                     /db_xref="CDD:442197"
ORIGIN      
        1 mntpvadgfr mppewarher twmawpgpgf tfgeergetl drarrawaav aravrrfepv
       61 tvvagtgqsa garallgadi eiverplnda wmrdigptfl tddtgqlaaa dwvfngwgaq
      121 ewarwdldek iaeqvcglag arryatplvn egggihidge gtvlltetvq ldpgrnpgrt
      181 qeeveaeiha hlgttkaiwl prglaadygq fgtrghvdiv aafarpgtvl vhtqpdpdhp
      241 dhaicseiak llrgstdagg relevievpa ptvleedgel vdysyinhyl cndgvvlcgf
      301 ddprdeeaaa ifrrlfpdrt vtlvdartif aagggihcit qqqpkv
//
LOCUS       WP_457691493             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691493
VERSION     WP_457691493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10451994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23203
     Region          <30..63
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          88..197
                     /region_name="TetR_C_6"
                     /note="BetI-type transcriptional repressor, C-terminal;
                     pfam13977"
                     /db_xref="CDD:433619"
ORIGIN      
        1 mpgparrprr rlnqpreqvl aaamatiaae gldrltmagl grevgmssgh ilyyfgtkde
       61 lllqtlqwse eqlgaerraa lsrrvparer ldalvdlylp eghrdprwtl wlevwnrsqn
      121 addetrerql elelawhrdl vallvegisk gefrpvdaer fatrtralld gfgsqlvvgl
      181 pgtereevrg hirefldesl saleg
//
LOCUS       WP_457691494             443 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457691494
VERSION     WP_457691494.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47444
     Region          12..416
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(19..20,23..24,27,65,123..124,126..128,131,151,
                     154..155,158,241,244..245,248..250,253,281,285,338..339,
                     343,347,363,366..367,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 mgreqwkkiw vgsagnmvew fdwfvyasfa vyfadsffpk gndtanlmnt mgifavgffm
       61 rpvggwvlgr vgdrkgrkaa ltltvtlmsa savliavapt ygvagyggva vllvarmlqg
      121 lsvggeyaas atylteasap grrgfassfq yvsmtagqll glglqivlqr tlsedalhsw
      181 awripfiiga lgaaivfylr rnmletevya eddsanadpa rgtikallah kreaflvial
      241 tmggtvayyt yttyltkyls gsaglpkpta slvsfcalfi fmciqplagk lsdrigrrpl
      301 litfavgstf ltvpimtllk hagsfwpalg lsllalvvvt gytsinacvk aelfptgira
      361 lgvalpyaia nalfggtaey valwfkeggi esgyywyvag caavslivyi tmretrsidl
      421 hrvgkqdegt gagrervgap vad
//
LOCUS       WP_457691509             197 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691509
VERSION     WP_457691509.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=20994
     Region          10..197
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mdfassdsgs dgntaratts akivvaggfg vgkttfvgav seinplrtea vmtsasagvd
       61 dlshvkdktt ttvamdfgri tldqdlilyl fgtpgqdrfw fmwddlvrga igavvlvdtr
      121 rladcfpavd yfensglpfv ialngfegyq phtpdevrea lqigpgtpiv atdarhrnea
      181 ksalitlveh almarlq
//
LOCUS       WP_457691508             308 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces sp. 900105755].
ACCESSION   WP_457691508
VERSION     WP_457691508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 308)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 15746489
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..308
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34016
     Region          <49..>88
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          79..308
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          227..304
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvetgqppvp ppvlergyrn ptrpglglel lpfadlrrrl pgdeyrrihr pdfhhltlvr
       61 rghgtamvdf vdrpcrpgtl lhirpgqvqr lptaadgtpa gldatlvlft pdfpprlpat
      121 arvtddpfgp aawqlrpadq drlgrafael aeeygaytad gadgadseit rellrqllsg
      181 vllrmarlpg gtdgpasrtp paaqepyrhf qhelersftt lrqahdyaar lgyslktlnr
      241 acrratghta kqlidarvtl eakrllahtd lpvaavshrl gfteptnfgk fftretgrtp
      301 gafrtgqr
//
LOCUS       WP_457691515             257 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691515
VERSION     WP_457691515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Hong,H., Seo,H., Park,W. and Kim,K.J.
  TITLE     Sequence, structure and function-based classification of the
            broadly conserved FAH superfamily reveals two distinct
            fumarylpyruvate hydrolase subfamilies
  JOURNAL   Environ Microbiol 22 (1), 270-285 (2020)
   PUBMED   31657110
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Ran,T., Gao,Y., Marsh,M., Zhu,W., Wang,M., Mao,X., Xu,L., Xu,D. and
            Wang,W.
  TITLE     Crystal structures of Cg1458 reveal a catalytic lid domain and a
            common catalytic mechanism for the FAH family
  JOURNAL   Biochem J 449 (1), 51-60 (2013)
   PUBMED   23046410
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12105251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="fumarylacetoacetate hydrolase family protein"
                     /EC_number="3.7.-.-"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27433
     Region          1..50
                     /region_name="DUF2437"
                     /note="Domain of unknown function (DUF2437); pfam10370"
                     /db_xref="CDD:463061"
     Region          49..254
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mriarfsidg nvgfgvlegd eldvikghpf aefersgqkv pldkvrllpp vlpnkvvgvg
       61 rnyaehaael gnavpdvpvv ffkpstsvig pgdpiaypsf sqevhheael avvigrmcre
      121 vprervkdvi lgytcandvt ardvqqrekq warakgfdss cplgpwvetg ldpadiaagl
      181 avqctvngeq rqlgrtsdmv rsvedlivhi teamtllpgd viltgtpagv gplnvgdeva
      241 vtiegigtlt nkvikrg
//
LOCUS       WP_457691518             241 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457691518
VERSION     WP_457691518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25934
     Region          4..228
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mplravlwdl ddtlfdytgs dragvlrhlr tegildtygg eeaalerwrt ametefarfl
       61 agevgfldhr rgrartflgt plsdteadaw fgryvahyea swvlfpdsap alaalaplvr
      121 qavlsnaata nqerklaalg irthfeavfc adelghakpa eeafkgacka lgltpgevlh
      181 igdkldidal gardagltav wldragtgee ppagvrrivs laelpellrg vigfgapsti
      241 r
//
LOCUS       WP_457691528             218 aa            linear   BCT 27-JAN-2026
DEFINITION  HU family DNA-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691528
VERSION     WP_457691528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=22328
     Region          1..91
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnkaqlveai adklggrqna adavdavlda ivrsvvsgdr vsvtgfgsfe kvdrparyar
       61 npqtgervrv kktsvprfra gqgfkdlvsg skklpkggev svkkapkgsl sgagaikkaa
      121 akkatakkaa akkaapakka aakkttaakk atakkttakk apatkaaakk tttakkatak
      181 kttakktapa kkatakkapa kkatarktta kkttarkr
//
LOCUS       WP_457691533             333 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Streptomyces
            nigrescens].
ACCESSION   WP_457691533
VERSION     WP_457691533.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=34595
     Region          2..329
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mtrcavygtg swgtafamvl adagcevtlw grrealvdai nngrtnpdyl pgvelpaavr
       61 attdpaeaar gaefavlavp aqtlrgnlae wapllpadtv lvslmkgvel gtakrmsevi
      121 eevakvpaer vavltgpnla kevaarqpat avvacadeav arrfqaacht syfrpytntd
      181 vvgcelggav knvialavgi atgmglgdna kaslitrgla ettrlglamg adahtfagla
      241 gmgdlvatcs splsrnntfg tnlgrgmtlq etiavtkqta egvkscesvl dlarrhgvdm
      301 pltetvveiv hegkppmval kdlmsrsaks erh
//
LOCUS       WP_457691531             288 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691531
VERSION     WP_457691531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31588
     Region          8..226
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msrrrigfwy rlaavickpp llvlfkrdwr gmehipadrg fitavnhnsy ldplsyahyq
       61 yntgrvprfl akaglfrsgf vglmmrgtgq ipvyrettda anafraavta idkgecvafy
      121 pegtltrdpe lwpmqgktga arvalltkap vipvaqwgan damppyakek klrlfprktl
      181 rvqagppvdl safydrepta evlraatdvi maaiteqlav vrgepapaep ydwrkaiare
      241 rraareaaka tqgagadrtp aepaaaaepa vgpqqarstq qaqedesk
//
LOCUS       WP_457691534             378 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanine--D-alanine ligase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691534
VERSION     WP_457691534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11479728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="D-alanine--D-alanine ligase family protein"
                     /EC_number="6.3.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008716 - D-alanine-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40851
     Region          9..372
                     /region_name="ddl"
                     /note="D-alanine--D-alanine ligase; PRK01966"
                     /db_xref="CDD:234993"
ORIGIN      
        1 mssetsshkp rvavvfggrs sehaisvlta gavlraidre kydvlpigit tdgrwaltad
       61 dpermaiadr qlpsvaelae steggvvlpv dptnrevvys epgsvpkalg evdvvfpvlh
      121 gpygedgtlq gllelsgvpy vgsgvlasav gqdkdymkrv fssfglpvgp yevirprewe
      181 kdpaaarrki vdfaaehgwp lfvkparags smgitkvddl ggldeaieea rrhdpkilve
      241 sllrgreiec gvlefedgpr asvpaeippv tahdfydfea kyidsadgiv papltaeqta
      301 kvqelaveaf eaasceglvr adfflqdnge fvineintlp gftpismypr mwqesgvsyp
      361 elidrllqaa lhrstglr
//
LOCUS       WP_457691555             141 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691555
VERSION     WP_457691555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..141
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15828
     Region          24..127
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mateptgeta eeptpgctdd laydvfardc psrdalrhit drwgsltlga lldgtfrfne
       61 lrrrvagvse kmlaqtlhal erdglvhrea qqtnpprvdy altplgdqva rqlrmlidlv
      121 edrmpqvlqa rehydtqrta e
//
LOCUS       WP_457691557             125 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457691557
VERSION     WP_457691557.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..125
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13820
     Region          1..123
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtelsrrlda hqrsriaeld ltptqakale elgepktare laavlccepp nvtyviskle
       61 kqgmvvrrph pldgrakqlv ltdagrelrl gllrrmgtas pldhlsheer aalrddllra
      121 lgrgd
//
LOCUS       WP_457691566             384 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691566
VERSION     WP_457691566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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 384)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40972
     Region          102..240
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 msgnslrttd gqihqtagtv peaaggealr phaedsfaae laalaaaddr prperwrlsp
       61 wavatyllgg tladgtvitp kyvgprrive vavttlatdr allllgvpgt aktwvsehla
      121 aavsgdstll vqgtagtpee airygwnyaq llahgpsrea lvpspvmram aqgmtarvee
      181 ltripadvqd tlitvlsekt lpipelgqev qavrgfnlia tandrdrgvn elssalrrrf
      241 ntvvlplpat pdeevdivsr rveqigrsld lpagpeglde irrvvtvfre lraglttdgr
      301 tklkspsgtl staeaisvvt nglalathfg dgvlrsgdva agilgavvrd paadrvvwqe
      361 yletvvrerd gwkdfyracr evsa
//
LOCUS       WP_457691601             623 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail sheath family protein [Streptomyces nigrescens].
ACCESSION   WP_457691601
VERSION     WP_457691601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Bock,D., Medeiros,J.M., Tsao,H.F., Penz,T., Weiss,G.L.,
            Aistleitner,K., Horn,M. and Pilhofer,M.
  TITLE     In situ architecture, function, and evolution of a contractile
            injection system
  JOURNAL   Science 357 (6352), 713-717 (2017)
   PUBMED   28818949
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Ge,P., Scholl,D., Leiman,P.G., Yu,X., Miller,J.F. and Zhou,Z.H.
  TITLE     Atomic structures of a bactericidal contractile nanotube in its
            pre- and postcontraction states
  JOURNAL   Nat Struct Mol Biol 22 (5), 377-382 (2015)
   PUBMED   25822993
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..623
                     /product="phage tail sheath family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=66720
     Region          338..620
                     /region_name="COG3497"
                     /note="Phage tail sheath protein FI [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442720"
ORIGIN      
        1 mpthttypgv yveelpssir sittvttsvt afvghtrrgp lnqpvqitsf adferrfggl
       61 tsqspvayav hqffgnggtv avivrvtkag sgkeaqvtle steghsqcpv levhakepgv
      121 wgsglrlavd hdtpaehasg hpspcetfnl qvldahgtar esfaglsmdp dhghyaetvi
      181 nagsslirvr vvgegrpdps gtvskafhhe lpdlnveltv kigevereft lydpdcdgep
      241 pctvaelall lehklralpd apgkhafaga evtafgrriq vvagstdpgd vvrfigecan
      301 dlgleasvnp pvfplcgged geppgprdli gsearksglq alrevpdvnl lalpelasye
      361 stedmvtvls aagrlcrerr ifllvdapaa wggvdaarag iaaftpvrsn hsglyfphlq
      421 ltdpltgrlr sfppsgavag viartdserg vwkapagtea rlagvhslsv kltdrengll
      481 nplgvnclrt lpmvgpviwg artlegsdal dsewkyvpvr rlalhveesl lrglqwvvfe
      541 pnteqlwqqi rlnasaylhs lfekgafkgs tprqayfvkc dkdtttdadi drgvvnvvvg
      601 iapvkpaefv ivkiqqmagq fdv
//
LOCUS       WP_457691604             294 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457691604
VERSION     WP_457691604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=31628
     Region          4..163
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtqreqaata fddlhtrhaa almqqayllt grawlarrav ergfrlawqr wpevavdpdp
       61 agwvraavye yaltpwhqlc pglrtargpr kpsraagpsd galpaallsl papyrralll
      121 hdgvglgpaa taaeieasap aaagrlthar eriaallpql gldgqpperq geilrarlsg
      181 plsaaevtpr aaahvrsgse rsarrttraa fgatglfalv tlvmmalapd hstpppkrpl
      241 ataphtrvsp arhhgadtre rrnaarerrn aareqgnaav rkklrearla pdlr
//
LOCUS       WP_457691612             264 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces sp.
            900105755].
ACCESSION   WP_457691612
VERSION     WP_457691612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  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 264)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1008156
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..264
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29032
     Region          42..145
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mntraasrpa gnvtrgttnp nrlrrmdrwi aathggvlrr aadpvavdlg ygaapwtave
       61 llgrlrtvap rarvvgveie parvaaarpy ereglafrhg gfeipvaarp lliraanvlr
      121 qydegevaev wrrlcgrlap dgllvegtcd eigrrhvwva lgaegprtvt fatrlgsler
      181 psdlaerlpk alihrnvpge pvhvflrdfd rawaaaapya sygarqrwir avrdltadwp
      241 vtdsaarwrq gevtltweal apra
//
LOCUS       WP_457691630             238 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457691630
VERSION     WP_457691630.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25555
     Region          <10..232
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mravsvqara rrsgvvedaa qafgswqger rvgatgvvtc fsfgpiknlt cglggaivpr
       61 tpleadicrr lrglgivesa aqraevttyt idgfgmrvqm splnaavglv qlvhfaeaet
      121 rrralwraya aaldgidgvs lvdadvdrtv palcavrvld grrdrvfhtl lergigvgvh
      181 yppnhtqpaf aawhrplpvt ehlggqimtl pfhqhlteaa aehitgelra alaaetdr
//
LOCUS       WP_457691632             144 aa            linear   BCT 27-JAN-2026
DEFINITION  low molecular weight protein-tyrosine-phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457691632
VERSION     WP_457691632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   He,R., Wang,J., Yu,Z.H., Zhang,R.Y., Liu,S., Wu,L. and Zhang,Z.Y.
  TITLE     Inhibition of Low Molecular Weight Protein Tyrosine Phosphatase by
            an Induced-Fit Mechanism
  JOURNAL   J Med Chem 59 (19), 9094-9106 (2016)
   PUBMED   27676368
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Zhang,Z.Y.
  TITLE     Mechanistic studies on protein tyrosine phosphatases
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 171-220 (2003)
   PUBMED   12882518
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Wang,W.Q., Sun,J.P. and Zhang,Z.Y.
  TITLE     An overview of the protein tyrosine phosphatase superfamily
  JOURNAL   Curr Top Med Chem 3 (7), 739-748 (2003)
   PUBMED   12678841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..144
                     /product="low molecular weight
                     protein-tyrosine-phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=15124
     Region          7..139
                     /region_name="LMWPTP"
                     /note="Low molecular weight protein tyrosine phosphatase;
                     cd16343"
                     /db_xref="CDD:319971"
     Site            order(13..20,46,119,121)
                     /site_type="active"
                     /db_xref="CDD:319971"
ORIGIN      
        1 mtgtrprrll tvclgnhcrs plaalilael ggpavevrsa gtrdkwvgrp ahpemvtaaa
       61 aagydltphr gvyisqalle wadavlamdt gnlaalrala deatapklal ylgdrdvpdp
      121 wgkvpedfaa vvalveegtv rhlp
//
LOCUS       WP_457691633             393 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Streptomyces nigrescens].
ACCESSION   WP_457691633
VERSION     WP_457691633.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 393)
  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 393)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - obsolete lipid glycosylation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=40163
     Region          25..393
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mttdaprtfr livtgggtgg gtgghtypal tairtvqarl aasggtldvl wigtpdglea
       61 riapaegihf ttvatgkirr snnplkmasp anirdmarvp lgvaqarkiv agfrpdvvla
      121 tggyvavpag iaarmckrpl vlheqtvrlg lanrklagsa triavssest lrllpeavrg
      181 aavvtgnpvr pevltghadk avtalglggf drqlptlyvt ggaqgaqqin qvvagalswl
      241 leraniihqc gpanvdalrq haaglpaela aryyltgfvd aelpdvlala dvvvsrsgag
      301 tlaeltalgk pavfiplass agneqahnar hlaesgaava llddvtagal rdtvgslltd
      361 parreamaea arahgrpdaa drlvdvllsa asg
//
LOCUS       WP_457691645             300 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Streptomyces nigrescens].
ACCESSION   WP_457691645
VERSION     WP_457691645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31499
     Region          38..192
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          135..282
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mgsasaaapl tsdgsgslge trllvserag dqrrtvemdp adgavthtva dgldglysps
       61 gsqiayiryg dtcvpqaegc tyrpdlvtat asganqrvla pgvesetgev yianpdwapn
      121 gkrvvfdtpr giesvnadgt gretltsagl ratfspdgsr iaylratsye gpegteygtd
      181 vyvmdlatre srqvstdhqa vstppdwspd grhlvfggts glktvdtetg eqsdlydsgt
      241 watsvtdvrt pvyspdgtri afsgwddata trrlylvdad gthlravadt ggtltdwigk
//
LOCUS       WP_457691647             192 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691647
VERSION     WP_457691647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21208
     Region          38..179
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 marisltprr tltlrlaewy srraygevmq palalghhpk llrsyfsfes kvarwkaldp
       61 klkllaemas avtigcswcv dfghwhadql glplekvgkv pdwraheesf telerlvmey
      121 aeamtatppa vtdelagslr rrlgdtafve lttmvavenl rsrmnsamgl hsqgfsdaca
      181 ippgrrtpgg aa
//
LOCUS       WP_457691649             190 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457691649
VERSION     WP_457691649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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 190)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21407
     Region          19..183
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(33,48,86,112..113,126)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mtieltdrte mansselddm feqmhipegy kaeivegtiy mapqrsthwe tiadiyeqlr
       61 tryprkrvls dvridlpgyl ngfasdvval aenatkndkg rpryqdiefv aevisestgk
      121 ndygpkktay alaevpvyvi adpylgrcrv ftdpqdgeyk idltvaygrp vdlthtvagi
      181 tlstdefprd
//
LOCUS       WP_457691653             513 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457691653
VERSION     WP_457691653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..513
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55892
     Region          1..503
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mpvydyvvvg ggtagsvias rltedpdvtv avieggpsdi dredvltlrk wlgllggdld
       61 yeyttteqpr gnshilhsra kvlggcsshn tlisfkplps dwdeweaaga agwgakemdp
      121 yfgklrnniv rvakkdqnqi atdwieatkt algvpevvgf ndkpfdegvg ffdlsyhpen
      181 nkrssasvay lhphmeagdr pnlhlmletw atkleldgtt akgvhvrtkd geevyveaar
      241 evlvcagavd tprllmhsgi gpkkdlealg lpcvldlpgv genlidhpes vivwetegpi
      301 pgnsamdsda glfvkrdpeh kgpdlmfhfy qipftdnper lgyerpehgv smtpnipksr
      361 srgrlyltsa dpeakpaldf ryfededdyd gktlvdgikl arkvaqaepf kkwlkrevfp
      421 gpevtddaei selvrkaaht vyhpagtckm gaaddqlavv dpelkirgla giriadasvf
      481 ptmpavnpml gvlmvgekca ellhkaptqg gda
//
LOCUS       WP_457691654             377 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691654
VERSION     WP_457691654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   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 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   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /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=41056
     Region          30..365
                     /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 mattsagase ipnartsedt tateasdgrd vvfsvrnlwk vfgpkaerip gdssvaelsa
       61 qelrektgct aavrdvsfdv hkgevfvvmg lsgsgkstlv rcltrliept sgelemdged
      121 vramdrtalr elrrrraamv fqhfgllphr tvvdnvaygl eiqgmskter rekandmvdk
      181 vglaglekrr pgqlsggqqq rvglaralav dpevllfdep fsaldplirr dmqeevcrlh
      241 reegrtmvfi thdlaealri gdrialmrdg kivqlgtpee ivgspaddyv rdfvrdvpre
      301 qvltvrramr paedgeadqg palspdtlis daieavarsg gaarvvdgkr clgivdhacl
      361 lnvvarldsp qhdevaa
//
LOCUS       WP_457691657             664 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691657
VERSION     WP_457691657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 664)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..664
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69071
     Region          55..310
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          377..653
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
ORIGIN      
        1 msavptqpts qryldtakpa pvqqllrrpg lskllllava aavivpllqa kfgaawpssl
       61 tvdvsgplgk tsdwiidnrd shplfvyflg hlsnavvisv rgvyllllal gwtgvtagvt
      121 liawrvagvr iaatalisfl vsgllgmwvp tmqtfalmvv avavsvvvga llglaaglsd
      181 rlfrilrpvl dtmqvlpafa yllpvvlvfg igvpaallat viyaappmar ltalglrgad
      241 pgvleavssl gatgrqrllt arlplarkel llgvnqtimm algmvviasm igaaglgdrv
      301 yqalasvdvg aalaaaipii llaivmdrtt aaagerlgad taatgpkwlr gwqawtgiav
      361 vtallalagr lsgslvwpga wavdiarpvn dfkewmvdhl ysgipviggt rdwaahftdw
      421 vlnplrdglt alpwygtlli vaalawligt wrtaltavla maaigvlgvw kpsmntlsqv
      481 iaalavtlvv gfgigilaag skrfeailrp vldvmqtmpq fvylipvval favgrapaaa
      541 aavvyalpav irittqglrq vdpaamesar slgatrwqml rqvqlplarp slllavnqgv
      601 vmvlavviig glvgggalgy dvvtglatgd lalglvagva ivclglmldr vtqpterrta
      661 gkga
//
LOCUS       WP_457691663             324 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691663
VERSION     WP_457691663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=33251
     Region          1..324
                     /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 mravefqeyg gpevlkvvea dlpepgpgqv sidvayagvn fadlkaraeg yrvaslpfrp
       61 glevsgrira vgaevtglrp gqevaaltdg gayaetvvaa aetvfplpeg vsprvaatlp
      121 tvvptahalv hevgrlrage tvlvqgaagg igtvvgqlak aagagavygv vstaakaeya
      181 rtygydevfv gpdfdaevrr atggrgvdla ldpvggdtfr rsmdalaifg rlvsfgnass
      241 aepwqvgqpe lyptgrtvsg fsilglagta pealrtlaeq afrtvaegtv elpvtaefpl
      301 aeaaeahrli gsrqstgkll lrvg
//
LOCUS       WP_457691666             386 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457691666
VERSION     WP_457691666.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="trypsin-like serine 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=40776
     Region          142..>317
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mpsirrstaa aaalvallag tatacgpgdd kaagssaadq kdqadggiel pedmptsldd
       61 lkkwkdggwq nwdkwardas dfanpiikdh wksdrlakak tspeigvkat gaggefdgtd
      121 pepqpvtaeq varpyhdhma pvgkiffdsp kgpmvcsgtv vedpahpgks nlvwtaghcv
      181 hsgkkggwmr nivfvpsynd ngvpmnqvnn tpsqqitpyg rfwadwitts gewinmgsea
      241 tgnggsaydf avlhvkpeng sgkslqetvg naarvwfnap aanqisslda fgypagppyd
      301 garmmncpar pgrlvmqqgt pamnrigctm tggtsgggwf vnrggklilv sntsissnah
      361 twlagphlgp eaqrvfadis qkfanq
//
LOCUS       WP_457691665             114 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457691665
VERSION     WP_457691665.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 114)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..114
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12461
     Region          14..104
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpdrsshrae avhthpddvp vetalaalad pvrlqlvrel agsaawthsc ssfrvpvgra
       61 alshhftvlr aaglveqrdq gpkrlnrlrr eefdarfpgl ldlvlreegq gpsn
//
LOCUS       WP_457691671             172 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691671
VERSION     WP_457691671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18598
     Region          51..164
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtneaqlnkv qldeangand aagrsprvnf akaapkafka ligfdaaare gldpalvelv
       61 qirssqlnkc ayclhmhttd arkageseer lhmvavwqea shfftpkeqa alalteavtl
      121 vaqggvpdev yqraathfde pelarllali ftintwnrla lstgkvagtd er
//
LOCUS       WP_457691673             245 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691673
VERSION     WP_457691673.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /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=25123
     Region          6..236
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtaavlralh hgpdlplvlp gpwdaagakv fadagfpala tpsagvaasl gyedgrtptd
       61 emfaaitria ravdipvsad veagyglsak elvarltdag avgcnledtd httgalrdaq
      121 eqadwlaqvr aeagdalvin aridtylhgv qgleetvrrg rlyaeagadc vypilappll
      181 ltdlatgigl pvnavvtpdg psprelgtlg aaritfgpgl qqramaavae makqlreelg
      241 agtea
//
LOCUS       WP_457691674             167 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691674
VERSION     WP_457691674.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17928
     Region          31..164
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtttptartt patapgtahg hgprlpwakl apevykamia ldaaakqgld ptlvelvkir
       61 asqlnhcafc idmhikdare ageteqriyl lnaweeaagh ytdkeqaala lteaitllte
      121 gfvpdavydr aaahfgdtel ahlialitti nawnrfgvst rmapgra
//
LOCUS       WP_457691685             281 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691685
VERSION     WP_457691685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31337
     Region          15..62
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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          111..274
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtssssiqqa realgkrlre irkdsgltar elaararwhe skcsriengr tgpsdddlrv
       61 walhcgaegq tadliatarn idgayiewrr mersglrraq esvlplwert rhfraysswl
      121 ipgpfqtray ieallraird rralpddlee avrvrvdkqr ilhegprrfa vileesalrh
      181 riggaatmag qlghllslaa lphislgvip lhadrtalwp vedfwifdea qvsvelvsaf
      241 ltitqpheis myahtfagla elavygapar tlitaaidsl g
//
LOCUS       WP_457691683             396 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathionylspermidine synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691683
VERSION     WP_457691683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Sui,L., Warren,J.C., Russell,J.P. and Stourman,N.V.
  TITLE     Comparison of the functions of glutathionylspermidine
            synthetase/amidase from E. coli and its predicted homologues YgiC
            and YjfC
  JOURNAL   Int J Biochem Mol Biol 3 (3), 302-312 (2012)
   PUBMED   23097746
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Pai,C.H., Chiang,B.Y., Ko,T.P., Chou,C.C., Chong,C.M., Yen,F.J.,
            Chen,S., Coward,J.K., Wang,A.H. and Lin,C.H.
  TITLE     Dual binding sites for translocation catalysis by Escherichia coli
            glutathionylspermidine synthetase
  JOURNAL   EMBO J 25 (24), 5970-5982 (2006)
   PUBMED   17124497
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Bollinger,J.M. Jr., Kwon,D.S., Huisman,G.W., Kolter,R. and
            Walsh,C.T.
  TITLE     Glutathionylspermidine metabolism in Escherichia coli.
            Purification, cloning, overproduction, and characterization of a
            bifunctional glutathionylspermidine synthetase/amidase
  JOURNAL   J Biol Chem 270 (23), 14031-14041 (1995)
   PUBMED   7775463
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="glutathionylspermidine synthase family protein"
                     /EC_number="6.3.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44447
     Region          1..396
                     /region_name="Gsp"
                     /note="Glutathionylspermidine synthase, CHAP domain [Amino
                     acid transport and metabolism]; COG0754"
                     /db_xref="CDD:440517"
ORIGIN      
        1 merhtidprp gwqqtveaqg liypltrypd dslrpywdes ayysftlpev ealeevveel
       61 hgmclaaaah ivdrdrfadl giedprlarl iaeswrrree lpslygrfdl hydgsgpakm
      121 leynadtpts lveaaspqwf wmeerfpgad qwnslherlv aawkrqapll ppgvplhfah
      181 sagdelgedl mtvayleeta qqagletvai smedigwdrl sgrfvdqrlr fmracfklyp
      241 wewlatddfg pyvldtldng ggtgstlwie pawkmllsnk allavlwely pghpnllpay
      301 ldgprelaht rgyvakpllg regagvtlhe pgaepvlrap gdpccyqela plpdfdgnrv
      361 vlgawvvede aaglgiresa gpvtdeyarf lphvir
//
LOCUS       WP_457691699             475 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457691699
VERSION     WP_457691699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 475)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=49758
     Region          91..473
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(120,127,155..156,163,167,174,305..306,309,313..314,
                     317,350,355..356,359..360,362,385,414..416,419..420,
                     422..424,428)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(127,149,151,154,156..157,243..244,253,304..305,
                     308..309,313,356,359..361,463)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtdgqpksdg rpktdgrpkt gpeqpmpdgg qpttgprqpt tagqpptdar ppapaplppp
       61 gaacpahsgg gaphrlapgg agraaadall reagavvpvl lpgevpavav trhavlrevl
      121 ahpevaknac hfaalhdgtv ppgwplttfa tvdgmttadg adhrrlrglv tkvftarrva
      181 alrprvvelt aglldglpga aaadgtvdlr rhfayplpms vicellgvda alrdrlhels
      241 nlivgttgta devqaanrei tavlgevaea rradpgddlt saliaaqeed gdrlsarelv
      301 gtlllmiiag hettlnlitn avralctdrg qlelvragra twddvveetl rhdspvahfp
      361 frypvrdlel ggtvvprgtp mlasysaagr dpeaygpdad rfdvtrrpat rhlsfghgph
      421 yclgaplarl eatvalealf trypaldlav pdaelpphqs fignsthvlp vrltg
//
LOCUS       WP_457691700             194 aa            linear   BCT 27-JAN-2026
DEFINITION  2'-5' RNA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691700
VERSION     WP_457691700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=20698
     Region          6..174
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mgtvtlgvsi avpepygsfl qrkregfgdp aapgipthit llpptevrte alpgierhla
       61 evaagcrpfp lrlegtgtfr plspvvyvkv tdgvagctal qariraasgp carelqfpyh
      121 phvtiahgit eeamdraqag lrdftatwti ggfalyeqgs devwrlerey pfgpqtagvp
      181 rqaadlsrpp apsc
//
LOCUS       WP_457691704             474 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691704
VERSION     WP_457691704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..474
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49045
     Region          118..400
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mgsgsirrsa galfrgvlsa srakagtftd vpttfcvsta ssdptapnas attgnagraa
       61 rhgfplrtva alassgllat pllagtahad pkapkapkpp akmsqiggdr lgtpgvqval
      121 kpgapklpgp dtltarswiv sdaesgkvla aknphwqlap astlkmlfad tvlpkfpkdq
      181 khtvrpadle gmgdgsslvg ikenlsytvh dlwlgvflrs gndavhtlsa mnggtkatva
      241 qmqrhakeln ahdthvvtpd gydapgqvss aydlslfars glqnpdfrey cstataqfpg
      301 ekgkdgkrat fgiqntnrll sgdydmkpyp giagvkngst tnagstftgv aqrgdrqllv
      361 timnpekkeh neaykeaakl ldwgfaaadk vepvgrlvgp rseddgtgae gakgkgdgae
      421 qstqaaldga ggssgawtav gltaaamall vvgafavhrr wplpelvrgr rpgk
//
LOCUS       WP_457691703             185 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 900105755].
ACCESSION   WP_457691703
VERSION     WP_457691703.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..185
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20484
     Region          5..164
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          93..171
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtsgdyvira iradewesvk rlrlvalrdp vadiaflety ddalkrpdsf yreraarsae
       61 epsgarqfia etadgewagt vtvlieeags tdwagflver rqghvvgvfv rpehrgsglv
      121 kalfdagvaw arergaqrvr llvhednpra qgayrkagfv psgvtvqlea dagkrefefv
      181 lewpa
//
LOCUS       WP_457691708             444 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase [Streptomyces nigrescens].
ACCESSION   WP_457691708
VERSION     WP_457691708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 444)
  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 444)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=47248
     Region          193..439
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mifalilvpv lglffgvhry lwcrlvrdtt tpgsrprrtg tvaafvlplt tlaallagrg
       61 gapfplqqvl awpgylwlal vlyltlalla gevvravwlr avrareraeq dpsssaahgs
      121 epgeqtpqpt ptpspdpsps pspapphtps pssaptllpp rtpalpplat pprrlflara
      181 vaagaslaat aavgygtatt lrgpvvkrvt iplaklprta hgfriavvsd ihlgpvlgra
      241 htrrivetin rtrpdlvaiv gdlvdgnvad lapaaeplre lqsrygtyfv tgnheyysga
      301 dqwvdhvrel gihplenart elpgfdlagi ndvagqtena gpdydqalsd rdparavvlm
      361 ahqpvtihdt vrhgvdlqls ghthggqmwp ftyiadatnp tiaglerygd tqlyvsrgag
      421 twgppvrlga ppdvtvvela slra
//
LOCUS       WP_457691720             381 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691720
VERSION     WP_457691720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40475
     Region          51..367
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mnrirrgaaa lllaatlplp laaagtavaa pappaahtts ptapdthtrl elprptgpya
       61 vgrdtlpltd thrkdpwvps agprelmasm yyparpgtgg arspymstee arlllegtrr
      121 tdalppeqla atrtharsga raiggkhplv gvvekgddig ttfrggrtlt cvacdtvgqa
      181 pektqrklma kvatgraadi sfvidtltaa pdrhhvpawr hsamidpkri gtaghsiggn
      241 saasamaadh riragvnmdg tffapvprsg ldgrpflmlg glnghapgde dtswlrdwrr
      301 ldgwkrwltv rdaghftfid lpvlgeqlgv tdpnaplsgk rsgeitrdyv taffdqqlrg
      361 iprplldgps aanpeavfqk p
//
LOCUS       WP_457691728             257 aa            linear   BCT 27-JAN-2026
DEFINITION  succinate dehydrogenase iron-sulfur subunit [Streptomyces
            nigrescens].
ACCESSION   WP_457691728
VERSION     WP_457691728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11481909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="succinate dehydrogenase iron-sulfur subunit"
                     /EC_number="1.3.5.1"
                     /GO_function="GO:0008177 - succinate dehydrogenase
                     (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29132
     Region          27..257
                     /region_name="sdhB"
                     /note="succinate dehydrogenase iron-sulfur subunit;
                     Reviewed; PRK05950"
                     /db_xref="CDD:235652"
ORIGIN      
        1 mstptldkhs aaldaaedga shlitvtfri rrfnpeised aswedfqlqi dpkervldal
       61 hkikweldgt ltfrrscahg icgsdamrin grnrlacktl ikdinpekpi tveaikgltv
      121 mkdlvvdmep ffqayrdvmp flittgnept rerrqsaedr erfddttkci lcaactsscp
      181 vfwndgqyfg paaivnahrf ifdsrdegge qrleilndkd gvwrcrttfn ctdacprgie
      241 vtkaiqevkr alitrrf
//
LOCUS       WP_457691732             572 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457691732
VERSION     WP_457691732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..572
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.52"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61827
     Region          79..212
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          217..555
                     /region_name="GH20_DspB_LnbB-like"
                     /note="Glycosyl hydrolase family 20 (GH20) catalytic
                     domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and
                     related proteins. Dispersin B is a soluble
                     beta-N-acetylglucosamidase found in bacteria that
                     hydrolyzes the beta-1,6-linkages of PGA
                     (poly-beta-(1,6)...; cd06564"
                     /db_xref="CDD:119334"
     Site            order(227,256,304,366..367,423,444,473,525,527)
                     /site_type="active"
                     /db_xref="CDD:119334"
ORIGIN      
        1 msnpmrppra prpsafphpv trpttgkgpa arsalpaaal agalllagcs daadteppgs
       61 tsakmnpaat ptwapvtgtp qvipavrdfr radgrgwrpt kgarvvvpag eksnvadeaq
      121 rmardlgglt vvygdqtvrp gdievkltge ngadqannvp vrgaadeayt ltadgtrltl
      181 taptdagify gtrtvkqavr aagglpegti qdrpgrpqrg msldnarkpf tqdwiearlr
      241 emadlklnqf qlhfsddqgf riqsdthpei vsadhltkaq irqivalars lhisvvpeld
      301 spghlgavla hypelqlrra sgsvvpgaid isnpkaapli dsllkemsel ftnpkgapay
      361 whlggdeyqa llsstpstty pqltraarqk ygpngtiadl atgwlndrqk tveakgknri
      421 eawndgffss prvsadknrm vdywtgkeag hrepaaflre grnvmnfnde ylyyvlgepn
      481 qfvyptgqri feswtplvir gtrpvavpas mtgpdripga rfaiwcdraq aqtpqqvaag
      541 irlplaalaq ktwdprtpal swtdfkalan rv
//
LOCUS       WP_457691736             279 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691736
VERSION     WP_457691736.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=29959
     Region          69..137
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          167..278
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maavlvvaal avgcrpvtvt gagspdskga ryapttpapp plghhpppap arhtarprpp
       61 rtahhapaap rplmatgsrg aqvrelqarl aqlglfdrap tgyyasvtat avrafqrrqg
      121 lprtgavqpa awralrsqtr rpshaelypp ttrpvgvpdp rcmrgrvici skrsntltwv
      181 vnsrivsamd vrfgsqytpt regtfhitfk srhhvstlyh tampyamffs ggqavhysad
      241 faahgyrgas hgcvnvrdkr kiaalfatvk ggtkvvvhh
//
LOCUS       WP_457691733             263 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457691733
VERSION     WP_457691733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=27811
     Region          8..188
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrgddiqpdd rrltvavqaa qdgdeaafrt vyravhprll gyvrtlvsep dvedvtseaw
       61 lqitrdlarf sgdadrfrgw aariarnral dhirmrgrrp aiggdesela dtpgasdtag
      121 ealealgtgh tmrliarlpq dqaeavvlrv vvgldaksaa evlgkragav rtaahrglrr
      181 laellgeepg agrdgrqdss qaggedgagr qegapsgrpa agprrgggtv sgvpaqgrrr
      241 rdgvaesyvp gvtetaartq kdm
//
LOCUS       WP_457691738             532 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA mutase large subunit family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691738
VERSION     WP_457691738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Banerjee,R. and Vlasie,M.
  TITLE     Controlling the reactivity of radical intermediates by coenzyme
            B(12)-dependent methylmalonyl-CoA mutase
  JOURNAL   Biochem Soc Trans 30 (4), 621-624 (2002)
   PUBMED   12196149
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Marsh,E.N.
  TITLE     Coenzyme B12 (cobalamin)-dependent enzymes
  JOURNAL   Essays Biochem 34, 139-154 (1999)
   PUBMED   10730193
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..532
                     /product="acyl-CoA mutase large subunit family protein"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0016866 - intramolecular transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_process="GO:0006637 - acyl-CoA metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58016
     Region          4..529
                     /region_name="Sbm"
                     /note="Methylmalonyl-CoA mutase, N-terminal domain/subunit
                     [Lipid transport and metabolism]; COG1884"
                     /db_xref="CDD:441488"
ORIGIN      
        1 mahesgsvry nesglpiepv ygpealdgwd perrlgapgg ypftrgvyps mytgrpwtmr
       61 qyagfgtare snaryrqlia hgttglsvaf dlptqmghds dtpiasgevg kvgvaidsve
      121 dmrvllggip ldkvstsmti napaalllll yqlvgeeegv aagqlngtiq ndvlkeyiar
      181 gtyifppqps lrltadifqy craeiprwnt isisgyhmae agaspaqeia ftlangiayv
      241 rtavaagmdv ddlaprlsff fvsrttllee vakfraarri warvmreefg aknpksmmlr
      301 fhtqtagvql taqqpevnla rvtvqglaav lggtqslhtn sfdeaialpt dksarlalrt
      361 qqvlayetdv tatvdpfags yavesmtddv eeaavalmrr vedmggavaa iergfqkeei
      421 ernayriaqe tdagervvvg vnrfqldeee pyeplrvdpe ieaqqverla tlrarrnrra
      481 vsaalgdlqk aaegtdnvly pmrealrara tvgevcealr gvwgtyvptd af
//
LOCUS       WP_457691740             402 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691740
VERSION     WP_457691740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..402
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=45153
     Region          17..397
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mataqgtate eagharytyr lrvsstdrca lmsewdrcrw vwnqcvaesr aaykagekcg
       61 palldkmltg wrtkhdwlre gasvpqqqii rdfaksraka lkditarlpv rqragmprfk
      121 kkgladptin ytrrgfrlqd grlylargia ltvvwsrgmp teptsvriyr dnlghwyasf
      181 ivkveaqpla rtgrcigidw gvketattts ddhdlphaqh gkkaaeklaq yqrmmarrkp
      241 grgqaaskgy rrvwrqaasm hkkiarrrqd darkwakrvv vdfdqiaved frpkflgqst
      301 markaadaai satkhelinm arkhqralhl vhpahttmdc ghcgartkqa lplsertytc
      361 iacgaesprd knsarvmlvr agltpsgaer vsldrspngr aa
//
LOCUS       WP_457691748             384 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691748
VERSION     WP_457691748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41731
     Region          30..384
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mtttqltaga ppaapdlvtt apqpairgrs rtgasrlral dglrllaalm vaayhyggrd
       61 geiaqawggs paqqfptaap lfaygclgvq iffvisgfvi clsgwgrtlr afiasrvsrl
      121 ypaywvavll vtavfalpwv afkalspsdv ltnltmlqqp lgadrvlgvc wtlwaemrfy
      181 alfalcvvlp gatrgrvvlf cagwtlaaal aqathepfld tvlmpeyapf figgiglyll
      241 hrygardpia waivlvswll gqhyavarlw hapsadgfsy rssagiiavv tlgfalvaav
      301 algklrwanw rwltvagalt ypfylvhehl gwvvvralhh gvglpsyatl mltvglmlll
      361 awvlhrfier pltpvlkrsi dprr
//
LOCUS       WP_457691751             325 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457691751
VERSION     WP_457691751.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..325
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36695
     Region          1..217
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvklsvivpf ynvqtyapdt lkslaanare dfefllvddc srdetpeila raerelpgar
       61 llrhsqnggl atarntglde argeyvtfld gddwlapgyy pellsvmeel gcdfvrtdhv
      121 qctararsvh rvphgrrgvv mdprevilpa drstsvdyaf awagmyhrrl lddgvlhfkd
      181 glrtaedrpw iwrlhreaks mavvgllgvf yrrgvasslt qigdvrqldf irafdqviee
      241 taqdraadll lpkavrtyca iishhlgsie rfepqvarkl rtmsaaamkr mpqdvlkeal
      301 dsmdvqrasr lrrlrrrpvp aevaa
//
LOCUS       WP_457691758             343 aa            linear   BCT 27-JAN-2026
DEFINITION  BMP family lipoprotein [Streptomyces nigrescens].
ACCESSION   WP_457691758
VERSION     WP_457691758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=35920
     Region          39..340
                     /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 mrrviriaaa atatavlalt atacgqsfae anrakhagvg lafdiggrdd hsfneaaarg
       61 aenaskklgv nvkmltakng eteadreqrl tsfaeagynp vigvgfaysq svqnvakdfp
      121 ettfgvvdav pegknvdamv faehegsyla gvaaalkskt hkvgfiggvn naliqkfqag
      181 feqgvrdtdp kakvtsqyly pnndkgfndp aaakakaggm ldsdidviyt aagqsgagti
      241 eavskvkgaw aigvdsdqyq qpglaryknr iltsvvknvd vavfdliksa edgkpltgih
      301 sydlkhsgvs latsggfikd iqpqidaark kiiegkvkvk etp
//
LOCUS       WP_457691760             518 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691760
VERSION     WP_457691760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 518)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55353
     Region          2..487
                     /region_name="NupO"
                     /note="ABC-type guanosine uptake system NupNOPQ, ATPase
                     component NupO [Nucleotide transport and metabolism];
                     COG3845"
                     /db_xref="CDD:443055"
ORIGIN      
        1 manhdihltv rrgtvhalcg engagkstlm kilygmqkpd egtialggeq vtlhtpadai
       61 argigmvhqh fmladnltvl entvlgaekl hgigagarak ikeisdaygl hirpdvlved
      121 lgvadrqrve ilkvlyrgar tlildeptav lvpqevdalf dnlrelkseg ltvifishkl
      181 gevlsvaddi tvirrgttva svepsgttpk qlaelmvgse lpspetrest vtdeemlrvs
      241 evhlsatdsd gvvrtvldgi sftihkgevl gvagvegngq aelveavmgt rrpdrgtltl
      301 dgkdlsgast rarreggigy ipedrhrhgl lleaplwenr ilghvterpn skgklldipg
      361 arrdtarive eydvrtpgie vtasslsggn qqklivgrem shhpklliaa hptrgvdvga
      421 qaqiweqire arreglavll isadldelig lsdtlrvmyr grlvadadpa vitpeelgsa
      481 mtgaarghls asedgapedg apedgashda geqegdeq
//
LOCUS       WP_457691763             426 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691763
VERSION     WP_457691763.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tomii,K. and Kanehisa,M.
  TITLE     A comparative analysis of ABC transporters in complete microbial
            genomes
  JOURNAL   Genome Res 8 (10), 1048-1059 (1998)
   PUBMED   9799792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..426
                     /product="ABC transporter permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=43830
     Region          53..424
                     /region_name="NupQ"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     subunit NupQ [Nucleotide transport and metabolism];
                     COG1079"
                     /db_xref="CDD:440697"
ORIGIN      
        1 mstdlktatk lavpgkggrr kltypwilli iagalvavsa lraltgtadl tstgqfgaal
       61 saavpiglag lgglwserag vvniglegmm mlgsfaagwv gwqhgpwaaa aagiiggalg
      121 glihaiatvt fgvdhivsgv avnilalgat qylatlwfgq edsaamaagg ndkqsppmpd
      181 mptftvpgls dwlnsleghh wflvsdvagi lgaavtsvsw ltlltialfi gtfyvlwrss
      241 fglrlrscge apisaetlgv nvysykyaav lvsgalaglg gaflsigvhf yqdgqtggrg
      301 yiglatmifg nwrpggvamg aglfgfmdam qlrsggptvh alllglaall avlalfrlra
      361 akrtqavvag iaaavlviwy aladtvplel veaspyiatl lvlalfsqrl rppkangkpy
      421 rrgqsa
//
LOCUS       WP_457691762             389 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691762
VERSION     WP_457691762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 389)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41076
     Region          19..366
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mststknpav daiaksatrd kvilaiaapv laivaaivis slvflasgen pfraygimad
       61 yghysdsqvw iinkavpyyl salavaigfr mnlfnigvdg qyrlaafaaa avggaialpg
      121 aiqiillivi amlvgaiwsg iagllkttrg vsevittiml naiaasiigy flqdgrlaik
      181 dgnllhtkfl pesshffsfp thpkpvygfv viailagaly wfginrtrfg fdlravgase
      241 paaeasgvsv krmvissmll sgaaaglvgm ptllgesfqy gtdfpagigf tgiaiallgr
      301 nhpvgmafga llwafldrtg srlefegyaq eivgviqgvi vlcvviayei vrryglslqq
      361 rkvgeelavl srtrttdksd kndkpevsa
//
LOCUS       WP_457691769             184 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457691769
VERSION     WP_457691769.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20594
     Region          98..184
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtvsekitve asdgpaaars epafrlvyae vfaeepyges pesveatfrr frsqvrkstf
       61 raaiartahg dpvgiaygyp lstktgwwdr litpvsdtlk redgqrtfgl mefavrapwr
      121 rlgvarrlhe tllaegneer vllnalpeae aaqaayrswg yrkvgeahpw egaprhdvlv
      181 rqlr
//
LOCUS       WP_457691772             409 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691772
VERSION     WP_457691772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44386
     Region          10..74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mdlsdelgtg erirvlresr gmtratlahl cgrgpdwlkk ietgerelrs htlllrlgaa
       61 lqvsdlsvlt gdsdgpaqlv plgrlnhpam pdiwtavmnr sltaaasdpl epallqgrvd
      121 qtwrlwhttd rnrtevgall pglirdgeaa vraldgdqrr aalvalsdvy rltgqatayv
      181 apaelawvva dralsaaqda dqpaaiaaaa wnmgnilret sypeealriv aeaadlirph
      241 lddapddwrg iygalqlhaa vtvaregreg dawrywdkgd qaakslpasy vhpstvfgra
      301 nvdfhaisva tdlrkaqkal gladdldpdv mpsrerrarl wvevarghlq rgdrtaalhv
      361 mqmahrigae tvtytpsarv vaadlwrsap ramrkdagrl aeavgvsia
//
LOCUS       WP_457691778             197 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457691778
VERSION     WP_457691778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  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 10156002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21246
     Region          34..183
                     /region_name="DUF820-like"
                     /note="Uncharacterized PDDEXK family nuclease; cd06260"
                     /db_xref="CDD:411709"
     Site            order(35,51,91,117..118,131)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mvaltaehfp qegrvwealv riwedteapa gcmveivdgi vtiapprdvr qnvivaelsr
       61 elyqqalpen rgayqklala vparnglyvp nlvvapdavv rgpghfipaa aaelvveits
      121 mtsavhdrlh kpagyasagv plyllidlws pdgptatlcg epdntryriq sptrlgeplh
      181 lpepfdmtid tsafhag
//
LOCUS       WP_457691779             177 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457691779
VERSION     WP_457691779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 177)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20402
     Region          36..158
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mqwkihgerp iyenkwvnlw ltdvetpdgh rwehhvvklr hlavaavvnd rrevlmmwrh
       61 rfitntwawe lpmglveege tpadaaarev veetgwrpdp vkpliyaepa ngitdsqhyv
      121 fradgatyeg ppteknesdr iewipladir gmidrreivs sgslvgllyv lmdeair
//
LOCUS       WP_457691783             372 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM protein [Streptomyces nigrescens].
ACCESSION   WP_457691783
VERSION     WP_457691783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Wang,S.C. and Frey,P.A.
  TITLE     S-adenosylmethionine as an oxidant: the radical SAM superfamily
  JOURNAL   Trends Biochem Sci 32 (3), 101-110 (2007)
   PUBMED   17291766
  REMARK    Erratum:[Trends Biochem Sci. 2007 May;32(5):209]
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Layer,G., Heinz,D.W., Jahn,D. and Schubert,W.D.
  TITLE     Structure and function of radical SAM enzymes
  JOURNAL   Curr Opin Chem Biol 8 (5), 468-476 (2004)
   PUBMED   15450488
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425241
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="radical SAM protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=40488
     Region          81..224
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
ORIGIN      
        1 mhqlivsphn gtflvarpga ragmqipram ygqlasiaes ssplpvwlld gartawgldl
       61 agvpmrdail vrpearlgyg ratyeinkgc nfncehcyla erkfeglpwe gkarllyllr
      121 dagvlwlqft ggeplidrdf mdayvlayrf gmlieiltng srlhrpevie mlrelpphkv
      181 tvslygatpd sfdsltrkkg afrlvekglv aareagiald laliitkhna heldamrala
      241 drygagrtey gtisptysgt peplaaqapg flgktsvfkg cpaghaffhv dphglatmck
      301 vgrenpidlm tqgldgllrl pgiadaqmlr tggcggcqls gtcrvcrpla kayqeakapl
      361 ntycrhgree aq
//
LOCUS       WP_457691788             438 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457691788
VERSION     WP_457691788.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44279
     Region          49..419
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(58..59,62..63,66,98,148..149,151..153,156,176,
                     179..180,183,257,260..261,264..266,269,297,301,349..350,
                     354,358,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mppadtgasv tdraaaspqs stdsssaaap dpeagklrpg gpgyrrmsfa lfaagvatfa
       61 llystqallp aisgdlgvsp dqaswtvsaa tfglalgvip lsavserfgr rtlmtvslsv
      121 aaliamlvpf apslgalial raiqgvalag lpasamafla eevraralva aiglfvagns
      181 iggmsgrivt gwvaqawgwr aalaavgvla vvcavtfrll vpkarhfapr svgpralart
      241 lgnhladpll rrlyaigglf mtvfgavytv igyrlvsepf nlpqgivgsv fvvylvgtvs
      301 saaagklvar mgrrgalyla vgttstglll sladsvaavl aglilitagf faghavasss
      361 vsrtaktara qasalyqcay yvgsslggal gaaafhavgw egtvllglaa mlgaasitly
      421 atrkavaerr llhlekaa
//
LOCUS       WP_457691798             265 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457691798
VERSION     WP_457691798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29406
     Region          100..252
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mntlhgttss avitrlhdvv rsgeksgagr gctrgtvrqr ppfmvaidat tvelnrghgg
       61 naahggengg ntggaeyrea trerrspaet aeaeaaftay vqerraslya tayhltgdry
      121 eaedllqsal fstyrawdri sdkaalggyl rrtmtnlhis awrrrklney pteelpetag
      181 dvdamrgtel ravlwqalvr lpetqrtmlv lryyegrtdp eiadilnisv gtvkssiwra
      241 lrrlredevl sfgrdeeesf gelva
//
LOCUS       WP_457691800             158 aa            linear   BCT 27-JAN-2026
DEFINITION  OsmC family protein [Streptomyces nigrescens].
ACCESSION   WP_457691800
VERSION     WP_457691800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16675
     Region          36..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mpgqhsyrtt vtwtgntgag tgtyrgygrd hevraeglpp llgtadpafr gtadrwnpeq
       61 lllaslaqch mltylalcal ggvvvtgyad dadgtmtedg sgggrfteav lhprvevasa
      121 ddvaraqelh aeahkkcfia nsvnfpvrhe pvvtvrga
//
LOCUS       WP_457691804             289 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691804
VERSION     WP_457691804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=30084
     Region          12..>257
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mseltgrlsv fktyklyvgg kfprsesgrv yevtdskgtw lanaplasrk dardavvaar
       61 kafggwsgat aynrgqilyr iaemlegrrd qfvaevaaae glskakataq vdaaidrwvw
      121 yagwsdkvaq iagganpvag pyfnlsapep tgvvavlapq dssflglvsv lapaivtgnt
      181 vvvaaaenap lpalslaevl atsdlpggvv nvlsgrtael aaplaahqdv naldlagadd
      241 alakdletaa adnlkrvlrp stvnwtadpg tgrlltflet ktvwhpmgv
//
LOCUS       WP_457691808             207 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691808
VERSION     WP_457691808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22383
     Region          71..>101
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 mtsqdrttpp qqqyaersyr spaalvggal llllglwlgg dallrgvvht kltalfalll
       61 gvplviaytl rplvragedr ltvrnpfrti tlpwgavedl raafsaevft sggkyqmwai
      121 pvslrqrkkv srqaargsap rprfglnada gpvpramadq aldelreike rathresaqg
      181 epvvrwsypi lapavlgvvg lavmval
//
LOCUS       WP_457691809             560 aa            linear   BCT 27-JAN-2026
DEFINITION  phospho-sugar mutase [Streptomyces nigrescens].
ACCESSION   WP_457691809
VERSION     WP_457691809.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Shackelford,G.S., Regni,C.A. and Beamer,L.J.
  TITLE     Evolutionary trace analysis of the alpha-D-phosphohexomutase
            superfamily
  JOURNAL   Protein Sci 13 (8), 2130-2138 (2004)
   PUBMED   15238632
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10146591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..560
                     /product="phospho-sugar mutase"
                     /EC_number="5.4.2.-"
                     /GO_function="GO:0016868 - intramolecular
                     phosphotransferase activity [Evidence IEA]"
                     /calculated_mol_wt=58556
     Region          47..552
                     /region_name="PGM2"
                     /note="This CD includes PGM2 (phosphoglucomutase 2) and
                     PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2
                     is thought to be a phosphopentomutase that catalyzes the
                     conversion of the nucleoside breakdown products,
                     ribose-1-phosphate and...; cd05799"
                     /db_xref="CDD:100092"
     Site            order(51,53,56,150..152,160,300,302,304..305,349,370..372,
                     386,388,390,512,514..516,521)
                     /site_type="active"
                     /db_xref="CDD:100092"
     Site            order(53,150,305,349,370,372,386,388,390,512,514..516,521)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100092"
     Site            order(150,300,302,304)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100092"
ORIGIN      
        1 matdpaelin raqawlaedp dpetrdelsk lieaedtdel aarfagtlqf gtaglrgelg
       61 agpmrmnrsv viraaaglaa ylkaqgdgsg lvvigydarh ksadfardta avmvgaglra
      121 avlprplptp vlafairhlg avagvevtas hnpprdngyk vylgdgsqiv ppadgeiate
      181 iaavrsladv prpeagwetl detvldayla rtdavltpgs prdtevvytp mhgvgrdtlv
      241 aafaragfpa ptvvaeqaep dpdfptvafp npeepgamdl afatardrsa sgvdiviand
      301 pdadrcavav papgtpdgwr mlrgdevgal laahlvnkqa sgtfattivs sqlmsriaaa
      361 aslpyeetlt gfkwlarvdg lryafeealg ycvdpegvrd kdgitaalli telaaelkqs
      421 grtltdlldd lalefglhat dqlsvrvedl sviadamgrl raqpptalag ltvtraddlt
      481 qgtetlpptd glryylsgsp eagiegarvv vrpsgtepkl kcylevvvpv asaetlpear
      541 tkaattlasv kadlseaagi
//
LOCUS       WP_457691815             328 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691815
VERSION     WP_457691815.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33792
     Region          1..259
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mfaaerrqli lemvrangav slrelarvvq tsevtvrrdv raleaeglld rrhggavlpg
       61 gftresgfpq kshlataekt aiadlaagfv eegeaivvga gtttqelarr larvpgltvv
      121 tnsllvaqal ahanrvevvm tggtlrgsny alvgsgaeqs lqglrvsraf lsgsgltaer
      181 glstsnmlsa svdralvqaa gevvvladht klgsdtmfqt vptdvitrlv tdeppghddr
      241 aatelqalad qgvqiavang sgvshgpgqp gmdggpgdrr gprrdvplpg qrrshapggg
      301 aggpqlrsap slseagggrv adlaprrr
//
LOCUS       WP_457691818             394 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457691818
VERSION     WP_457691818.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42352
     Region          <119..382
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltsrslly avaavavvcv gltlwlwprf agrgprallg rlgsvvatql tivaalglvv
       61 ntnfqfyasw hellglydda paavgkwgdq gsagpvgdps kglvqasgpe gldkvhglpk
      121 gapeqagkve tvrivgkrtr avnpayvylp pqyfqpqyar qrfpvivals gypggtfllg
      181 qhlrlpqtag gliragrmqp tvivmlrpti apprdtqcvd vpggpqaetf fardvpdalk
      241 shyrvghdpg gwgllgyssg gscalqltmr hdrtytaaaa lspdykvsnd attgnlfgeg
      301 rdrvrrrqeh dlmwrlqhlp aprvnvlvgt srtgeknypa akaflaavkp pmkaesvvln
      361 hgshnfatwr relpaalqwm grsltfpedv vgns
//
LOCUS       WP_457691819             166 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457691819
VERSION     WP_457691819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17934
     Region          1..131
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 madltpadqh lifrqyldav glhgmagaea vgltasewya lsqialegtl tsgelaartg
       61 lttgattrli drleragfvr raadpadrrk vivepvadsl driesvvgpa rrqiaevlar
      121 ytpdqravlf dyfthaapaf raateeirda aahrrrpkge gakrls
//
LOCUS       WP_457691816             211 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691816
VERSION     WP_457691816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22615
     Region          29..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matetagqpq ttgpaatapa rtpevrpmra darrnyerll teartafteh gtdtsledia
       61 rragvgigtl yrhfpnrtal mgavfqgevd allaharela dapqpcaalv ewlraiitha
      121 ttyrglsral mtasaddssg mrrcsvpmre agealltraq ragavrpdvs isdlmqltng
      181 ialaveespd dpkladrllt ltlrglkgen r
//
LOCUS       WP_457691821             589 aa            linear   BCT 27-JAN-2026
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces nigrescens].
ACCESSION   WP_457691821
VERSION     WP_457691821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..589
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61866
     Region          1..465
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          521..587
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(544,553..555,562)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            554
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvarac rdagigsvav yadpdrdalh vraadeayal ggdtpatsyl
       61 diakvlaaaa dsgadaihpg ygflsenaef aqavldaglt wigpppqair dlgdkvaarh
      121 iaqragaplv agtpdpvsgs eevvafakeh glpiaikaaf ggggrglkva rtleevpely
      181 dsavreavaa fgrgecfver yldrprhvet qcladkhgnv vvvstrdcsl qrrhqklvee
      241 apapfltqeq naelyraska ilkeagyega gtceflvgqd gtisflevnt rlqvehpvte
      301 evtgldlvre mfriadgekl gyddpevrgh sfefringed pgrnflpapg tvtkfdapag
      361 pgvrldagve sgsvigpawd sllaklivtg atraqalqra aralgeftve gmataipfhr
      421 tvvqdpafap eltgsadpft vhtrwietef vneitpfaap gadeaetdsr etvvvevggk
      481 rlevslpssl gmplaraava ggakpkrkaa kksggaasgd alaspmqgti vkvaveegqq
      541 vtegelvvvl eamkmeqpln ahrsgtvkgl taevgaalts gaviceikd
//
LOCUS       WP_457691826             276 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691826
VERSION     WP_457691826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29036
     Region          1..272
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 matvvelisy pvkgcagvpa aeaeltpagl phdrsflvvg pggvfrsqrt dprlavirpe
       61 vgadgthltl hapdrdplrl didlgtgsta rsdvemfgtp yravdqgdra agwlsealga
      121 esrlvrvppe hdrvtdgltp gtsgfadssp lhvlslatfd dlnrriaaag rppvpmdrfr
      181 pnlvvdgwda pqtedrarrv avgggvlgfa klavrcavtl vdqrtggkag peplrtlasy
      241 rrvpeggvaf gskfsvletg kvavgdafev tewgtd
//
LOCUS       WP_457691828             203 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside triphosphate pyrophosphatase [Streptomyces nigrescens].
ACCESSION   WP_457691828
VERSION     WP_457691828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A.,
            Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C.,
            Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D.,
            Murzin,A.G. and Yakunin,A.F.
  TITLE     Biochemical and structural studies of conserved Maf proteins
            revealed nucleotide pyrophosphatases with a preference for modified
            nucleotides
  JOURNAL   Chem Biol 20 (11), 1386-1398 (2013)
   PUBMED   24210219
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="nucleoside triphosphate pyrophosphatase"
                     /EC_number="3.6.1.9"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009117 - nucleotide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21011
     Region          10..181
                     /region_name="Maf"
                     /note="Nucleotide binding protein Maf. Maf has been
                     implicated in inhibition of septum formation in
                     eukaryotes, bacteria and archaea, but homologs in
                     B.subtilis and S.cerevisiae are nonessential for cell
                     division. Maf has been predicted to be a nucleotide-
                     or...; cd00555"
                     /db_xref="CDD:238310"
     Site            order(14,19,39,58,77,89)
                     /site_type="active"
                     /db_xref="CDD:238310"
     Site            order(52,123..128)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238310"
ORIGIN      
        1 mteesrprrl vlasqsparl allrqaglap evivsgvded altaatpgel arvlaeakae
       61 avaarpeaag alvvgcdsvl eldgralgkp adaedatarw ksmrgrsgvl qtghcvidta
      121 ngrrvtatas ttvrfgeptd eeiaayvesg eplfvagaft ldgrsapfid gidgdpgnvi
      181 glslpllrrl ladldvaite lwt
//
LOCUS       WP_457691830             494 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691830
VERSION     WP_457691830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..494
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=52458
     Region          1..494
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnrplrhiav fcgvlvlall vratwvqfvq geelandpnn rrvkieafsy prgniivggk
       61 pvtgseatsg dfkykrtykn gpmyapitgf asqaqgtsfl egiynkvlsg kddrlalkna
      121 kdiltgekpr ggdvittidp kaqkaaykgl tdlnakgavv aldprdgrvl alastpsydp
      181 svftgisnae grkfkeldad kskplsnral retyapgstf kiltaaaale hgvvsdinas
      241 tdaaapyqlp qsttkigndv asapcdkasl ktgmqwscnn vfldtalkvg kdkmretaek
      301 fgfnanvyde dlgdllatks lypskldkpq taltgmgqgs ltstpmqmam vaaglandgk
      361 vmmphlvdev rgsdlstvek iepkmmsqav sadtakkvqe mmeytvnegt ankaaidgvt
      421 vggktgtaqh ganvtderpy awfvsyakqs dgsspvavav fvdpkdmdip rseiaggklg
      481 gpiaksvmea vlkk
//
LOCUS       WP_457691833             720 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691833
VERSION     WP_457691833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..720
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76147
     Region          310..709
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mggdgssgrp dtawsvdtdg salatavgsv larldahaar ahatvrgnaa gddgaaaaga
       61 gstppdtagg tdradadrag tdradadrtd tgkadaagpr gadpaprpqe daalspghsl
      121 paldalascf glstferevv llaaaaeldp ttgarcaaas sdpghayptf slalaalgdp
      181 hwsaltpvap lrrwrlvela detrlttsrl rlderilhfl vgspyldarl hgllrrttap
      241 atlpasydaa adrvaagwad agpdaplrve lvggdlrtra diaataarra glglysmaad
      301 dvptdaaerd rlarlwqrea vllpaallve vgeldreqha aadafiagsa vplvvsgpdp
      361 rqtghprgqr vtvpkltdee qvglwtdafa dvpevtarev qalvaqfqlp phvvrsaaat
      421 vrrelsgpgg pdgpdaagla wqagltearm gldelgrrie pragwhdlvl agrqlrilee
      481 ivahvrqrst vyqdwgfaka lrsglgvtal faggsgtgkt laaevmakel gldlfiidls
      541 qvvskyiget eknlsrvfda aerggalllf deadalfgkr sevkdshdry anlevsyllm
      601 rmeayrglai lttnmkkald safmrrirfv vdfpfpgeke raeiwrrvlp aqaptkgidt
      661 sllaqltvag gsirnialsg aflaaeegdr lhmrhmlaaa rteylklers ltpsevhgwv
//
LOCUS       WP_457691836             174 aa            linear   BCT 27-JAN-2026
DEFINITION  2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
            [Streptomyces nigrescens].
ACCESSION   WP_457691836
VERSION     WP_457691836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Cendron,L., Berni,R., Folli,C., Ramazzina,I., Percudani,R. and
            Zanotti,G.
  TITLE     The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
            decarboxylase provides insights into the mechanism of uric acid
            degradation
  JOURNAL   J Biol Chem 282 (25), 18182-18189 (2007)
   PUBMED   17428786
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Ramazzina,I., Folli,C., Secchi,A., Berni,R. and Percudani,R.
  TITLE     Completing the uric acid degradation pathway through phylogenetic
            comparison of whole genomes
  JOURNAL   Nat Chem Biol 2 (3), 144-148 (2006)
   PUBMED   16462750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10014418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
                     decarboxylase"
                     /EC_number="4.1.1.97"
                     /GO_function="GO:0051997 -
                     2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
                     decarboxylase activity [Evidence IEA]"
                     /GO_process="GO:0019628 - urate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18959
     Region          12..157
                     /region_name="PRK13798"
                     /note="putative OHCU decarboxylase; Provisional"
                     /db_xref="CDD:184333"
ORIGIN      
        1 mssrvrgtlp rpraegigla rfnalpreea lasllsccgs rrwaervaah rpypdpesll
       61 aasdeacydl taaeldeala eeslssqplv gargpgtlaa htalraahae yerrfrhvfv
      121 icldgyrdee lldqvlsgir trlgnepdee ravaadelrr ltrgrltrlt asgp
//
LOCUS       WP_457691851             329 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene/squalene synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691851
VERSION     WP_457691851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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 329)
  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 329)
  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..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /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=35657
     Region          16..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtaheldaag vtdprlreay ahcrrlnarh gktyflatrl lpagrrpavh alygfarwad
       61 divddpatgh ttadrarald alqhclddgl rggestepvv ravahtaavy gidhrhftdf
      121 mtsmrsdltv tdyptyadlr rymhgsaavm glqmlpvlgt vvpqeeavph aaalgiafql
      181 tnflrdvged ldrgrvylpa dllaahgvdr allrwsrdtg lpdpritaal aaaaeltrgv
      241 yreaapglam ldpvsrpcir tafvlygail davrddgyav lhrravvsrr rraatalggl
      301 arlaatrvta rppgvrrggv phyaqeetp
//
LOCUS       WP_457691854             428 aa            linear   BCT 27-JAN-2026
DEFINITION  polyprenyl synthetase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691854
VERSION     WP_457691854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Wallrapp,F.H., Pan,J.J., Ramamoorthy,G., Almonacid,D.E.,
            Hillerich,B.S., Seidel,R., Patskovsky,Y., Babbitt,P.C., Almo,S.C.,
            Jacobson,M.P. and Poulter,C.D.
  TITLE     Prediction of function for the polyprenyl transferase subgroup in
            the isoprenoid synthase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), E1196-E1202 (2013)
   PUBMED   23493556
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Chen,A., Kroon,P.A. and Poulter,C.D.
  TITLE     Isoprenyl diphosphate synthases: protein sequence comparisons, a
            phylogenetic tree, and predictions of secondary structure
  JOURNAL   Protein Sci 3 (4), 600-607 (1994)
   PUBMED   8003978
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="polyprenyl synthetase 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=44353
     Region          90..378
                     /region_name="IspA"
                     /note="Geranylgeranyl pyrophosphate synthase [Coenzyme
                     transport and metabolism]; COG0142"
                     /db_xref="CDD:439912"
ORIGIN      
        1 mrrrtgatvp lalcdagppp sgcpsgkapp drgdtcsagl gpdtvdadvp aavgrmlvsv
       61 lgeqvaraae iegtfardva arvarftleg gkrtrsqflw wglrscedrp gacavepalr
      121 vsaaveliqt calihddamd rsplrrgrpa vhaefagqya tpgtaeaagr fgtsaavltg
      181 dlalawaddt vagaelgaet gprvrhiwra mrmemvagqy ldlygqiags rsaalavrta
      241 ylksarysve rplalgaala gadedttral caagrcagva fqfqddllgv fgdqdrtgkp
      301 sggdiregkl tyllavgrar alergdraal alldrcvgds eldaadlerv ravlvatgal
      361 glvelriqrl varsirhlaa aalepsaaar lrtlfasvag lrtatgrcpa pdgvaspvpa
      421 gvaergna
//
LOCUS       WP_457691855             409 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457691855
VERSION     WP_457691855.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 409)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=41570
     Region          6..409
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mpgqcrevav tglgvispag igaratwdal ltgrstaard pglvglpvdi scqvpdfdta
       61 rlvgrkaawr ldrfvamall aarhavadaa lspaewdasr vgvvmgtgtg smeryvtefa
      121 klaagrpldi splaitrsvp nmaaaeiald ltatgpnfav stacasgssa lgvardllra
      181 gtcdivlagg aesarhpipa acfhrmgals rrtedpagag rpfdaardgf vlsegaavlv
      241 lerpeharar gaspraqlvg ygascdafhy aapdpegrga aaaltaalad aglaprdidh
      301 inahgtgtrl ndlaesralh svfpeppavt slkgalghai gaagaieaav tvmslqqdti
      361 pptanyedpd ldidldivak aprqtllsaa astsfgfggq naalvfrsa
//
LOCUS       WP_457691857              87 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Streptomyces nigrescens].
ACCESSION   WP_457691857
VERSION     WP_457691857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 87)
  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 87)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..87
                     /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=9114
     Region          6..75
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mptsaelits tltetfdldp aevtpertfe dlgldslalv emglmlqert gislddvplq
       61 ttigelaalm dsstadkalt tvpnsts
//
LOCUS       WP_457691858             536 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457691858
VERSION     WP_457691858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..536
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54263
     Region          24..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,149,
                     152..153,156,280,283..284,287..289,292,320,324,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaaapartp vapvrraaaa avvclglfml gldltvlnva vpdlqsgldt staqvqwivd
       61 gyalvlggtv lavgaftdaw grrrsfvcgv avcagaslgg avaaepwqvi aarctmgaga
      121 allmpatlav ihhlfpeaql rsraiaawaa vggmgglcgp viggwlvehf swraafwinl
      181 plaaviivla lllvpeshar rragfdvpga alsaagllvl vwsitesphr gwtspaaltg
      241 faaaalllaa fvrrqlhapa pmlplsllrv paigvaaaal almsfamfga lfvltlylqg
      301 vlgfspwqag vrtlplpagl algavcavpv rarlggrvpv vgglslvtag failatttpe
      361 sdyphcaafq lvagigaglv aaaatesvmg svateraglg saindatrqv gsalgvavqg
      421 sllaavftsr lsasltdlha papvaaaarh smlsvpaqam rlpgplrssv lsaarraftd
      481 amtltaivag vvtlltaaaa arwlgrpdrp hgaspdgrar lrgpqpapre eerpal
//
LOCUS       WP_457691859             260 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase II family protein [Streptomyces nigrescens].
ACCESSION   WP_457691859
VERSION     WP_457691859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27511
     Region          16..253
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtvaasavpe rvvlaarpqa alrlycvppa gagpdcylrw apllppwiep csvalpgrgt
       61 raaepsltdp aylsarlaav lddwtdprpf avfghsagal layeatrhlr rthgrlpsll
      121 alsslsaphi daysaglppr ltaglegire lvgpipdqll adarlmaaac tplladclll
      181 lhyrhrpepp ldvplalygg ehdpvtsvqd lqawndlvtt partqlfpgg htylqtetka
      241 lvghlagtld aalnrpvata
//
LOCUS       WP_457691860             412 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457691860
VERSION     WP_457691860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42085
     Region          9..379
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,136,
                     139..140,143,214,217..218,221..223,226,254,258,307..308,
                     312,316,332,335..336,339..340,343)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 merslragrl atftffglng fvmgmwivhi psveqragig havlgwllll lgggafvgmq
       61 lvgrltdrfg arrvvpasav lcslavtlpg latdgwalga allvlgfgng cldvsmntha
      121 vqvergyrrp vmsafhavfs iggvfaalvg artlslgwsa aatlavtslf glvisafaap
      181 allppasara enpaaargaa prtppriwal aalammlmlc egvandwsvl dlrevldapp
      241 ataafaygaf atamtvgrll tdrvaarigp vavlrygasl aalgltavvl spwiplalcg
      301 wavfgaglsg cipqlfsaag hadqdaagan vsrvaglgyv gmlagptvig plthlvplnl
      361 tfllpvafca vaagmarlle prdatavgsa yghphreaga aprelegdad sr
//
LOCUS       WP_457691862             157 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457691862
VERSION     WP_457691862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16560
     Region          5..115
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 msfrlaayav ciedgrvlla chvppkgetn wtlpggrveh aedpfdavir evaeetgcda
       61 vverllgvds riipaaerti pggpehhnvg ifyqvritgg qprpepngei aesiwtpipd
      121 vaglrrsslv diglalaqal patghvapvt vggliqh
//
LOCUS       WP_457691878             352 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457691878
VERSION     WP_457691878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Yang,X., Kang,C.M., Brody,M.S. and Price,C.W.
  TITLE     Opposing pairs of serine protein kinases and phosphatases transmit
            signals of environmental stress to activate a bacterial
            transcription factor
  JOURNAL   Genes Dev 10 (18), 2265-2275 (1996)
   PUBMED   8824586
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537757
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=37444
     Region          144..337
                     /region_name="SpoIIE"
                     /note="Stage II sporulation protein E (SpoIIE); pfam07228"
                     /db_xref="CDD:462119"
ORIGIN      
        1 miltvviagl ayatppelaf srllpaapal aaamwpvlpt vllgtvclll miglgivfpd
       61 lgtwwtaagv vavtvaaayg shvrlrreqt lfevrlvadt aqqvvlspmp rrfggieiea
      121 lylaaaaeas iggdfyevvd teygvrllig dvrgkglpav gtaaamvncf reaaydeadl
      181 vniarrleas strynaafpp egmmerfata llaeiphggg sigilncghp pplllnhgei
      241 raleptapsp llnlaeligd hysidtfdfa pgdllllytd gvaeardhdg effplaawlh
      301 rqppgppgel intlhhdllh hsrgrldddi aalavrlcas pepldgqrnq pa
//
LOCUS       WP_457691877             376 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691877
VERSION     WP_457691877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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   4  (residues 1 to 376)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (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   6  (residues 1 to 376)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (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   8  (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   9  (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   10 (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
REFERENCE   11 (residues 1 to 376)
  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 10002138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..376
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39877
     Region          18..346
                     /region_name="LivK"
                     /note="ABC-type branched-chain amino acid transport
                     system, periplasmic component [Amino acid transport and
                     metabolism]; COG0683"
                     /db_xref="CDD:440447"
ORIGIN      
        1 mntppsppgp ertdgssvqi galvpltrpg wvaagqhlla glelavrevn daggvvgrpl
       61 elvvrdtaad pqqataavde larlgvaala geyhsvvara aagradalgl pflcssavld
      121 alteqptewv arlsppqshg wqiyadflls aghsriavaa qpsvywasgt rilrdylapr
      181 ggtvieldms altpaavcde lvgnratall llvghpepav pivksvrrdq rlaeimigap
      241 agqpefaewa tllgddsagv pflrylperl gplgarvekv lrerlgeaps fvafegydtv
      301 avladvlrsh gadrartaes wprvavegtr gqiqfsrtrg isvwqwasap vqvvdrdpae
      361 pgrfrirhag restev
//
LOCUS       WP_457691883             245 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457691883
VERSION     WP_457691883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26563
     Region          7..120
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
     Region          134..242
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtlqlvqvnf karddaalgq fwaealgwgv ssegpgvtnl epvgfdwpdp savcidlvrv
       61 pdpetvkcrv hielattsda hqaelvarlk elgatpadvg qgdapwtvma dpegnvfsvl
      121 eprelyrdtg piaavvvdca dpramvrfwg eaidwtvhel tddrallrsv kgvgpylefr
      181 rtpddevvwn rvhldvmsdp vedqarevar leglgairad vgqgdvswvv ladpagnefc
      241 vlgrg
//
LOCUS       WP_457691887             216 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457691887
VERSION     WP_457691887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22560
     Region          2..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 miglgaiagi avvelgmvlt pgpnmiylvs rsiaqgrrag ltslagvflg flvylfavsa
       61 giatvfalvp eiylaiklag agyllwlawk avrpggrsav ttqelaqdga rklflmgflt
      121 cllnpkvail yisllpqfvd perghvglqg lllgltqiav gvagnaffiv tagsvagffa
      181 rhplwqrlhr yavgtalagf avkiatertg avvalr
//
LOCUS       WP_457691908             196 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457691908
VERSION     WP_457691908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21235
     Region          1..188
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mkidfsdyal gagvatdlvn tsptvrssge ilaapaalar fltehgihpd avkhgrrpte
       61 edldqvrtlr qevrtilett teedvvhaan alvaraaigp slhrdatgrw qwyiatssnt
      121 sladelavli gtgllgalrt lshdrfrhct apacngmfvd tskagrrryc mpdicgnrrn
      181 vanyrarklt etegap
//
LOCUS       WP_457691919              86 aa            linear   BCT 27-JAN-2026
DEFINITION  HPr family phosphocarrier protein [Streptomyces nigrescens].
ACCESSION   WP_457691919
VERSION     WP_457691919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..86
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9159
     Region          1..83
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 maettvtias lsglrvrpvs rivqeaqgyi sdirflvdgk easakslfsl qmlemshgke
       61 vvivakgrde qtaveaiatl iesvvl
//
LOCUS       WP_457691921             169 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457691921
VERSION     WP_457691921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..169
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17952
     Region          33..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msrftsrsps reqasaaala asellevlwg hgqeaarsae vslsqlrall viekregtnl
       61 rtlaealasr psavsrlcdr leamglaerg psatsrreve lrltlrgrvl leeyraarsr
      121 evtatlerme psdvvklaag leafhaasar laadeggaat rdngvadsa
//
LOCUS       WP_457691923             389 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457691923
VERSION     WP_457691923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41867
     Region          4..383
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mterigvgaa lraslphall dtvrdhltta ygatsvhlfl tdyggtvlsp cdssgggegs
       61 lpianspegr algsqerreq qaphgeaidh hlpvtvrgdr igiltvrlpa grstpvvlde
      121 lrqvadqlgh eilvaerdtd vyqrvrrvsr ltvaaemqwq llparactaa qyavgaqlep
      181 ayavhgdnfd wasdgdeltl tvtngmgqgv easllthlav salrnarrag vsladqaala
      241 dqavydhyrg rshvstllvr velatgrmei idagspqmwr lrgksverig ldkqlplgmf
      301 eeshyaaesf tvepgdrllf vsdgvyeaps prgqkyaega laralhatrl lpaamapgav
      361 lrdvaeyraa etlddalvlc fdwfgndlr
//
LOCUS       WP_457691926             138 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457691926
VERSION     WP_457691926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..138
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14445
     Region          9..115
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 msapasggvp ilrlgdvlvt gllnelddkt avaftqeltd ritsdgargv lidisrleiv
       61 dsfvartlme lttmarllga rvivagmrpp vaitlvelgl qltgvetaln aeqgmaalgw
      121 rqnpqpsggg rsecrpeh
//
LOCUS       WP_457691932             433 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457691932
VERSION     WP_457691932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46067
     Region          12..425
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtphtfhnlp glrravreic aahrlpshng arlllsvsrt ataafdaggp vrlevieqsv
       61 pdgekllavt lhtgrtaasl smtdlplrgq atpdgtvawy lplgeaedsp rpaampapps
      121 aapaqghtre adgaeaseae iaalegdlsa alsrvdtltt elhalkdela etnsgvlaly
      181 vqleerdeql rrahgqilre ledalrpppi tvsglefavh yapadtdapt ggdfydwlll
      241 pdgtvhitvv dalghgvrst rsalnvthav rtlaleghpl esivarthdi lapfdpdima
      301 tvllaridpe tgalrlangs hppalvvrad gtadylevrg rgigfplpgs esvledtlhe
      361 gdllvlytdg ltesrrdpie gearlvksaw aharrpvhei pgavakdmht vilhpddtla
      421 lavrraenpq gsp
//
LOCUS       WP_457691934             136 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691934
VERSION     WP_457691934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14503
     Region          20..130
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mqhqlaiddh psqpaqrvch pdsaadardf vrgfvallcp tppartiqnl lllvselvan
       61 alrhagavta vhlradreri evlvedpsst hpqerrpdls gstggfgwpm vhslaldvmv
      121 rpgpcggktv qaalar
//
LOCUS       WP_457691936             385 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457691936
VERSION     WP_457691936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..385
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41434
     Region          1..354
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mdtlrevlae gygalsvell ladygatala pfgavgtaaa pvpvansaeg rafgsqqprq
       61 qdrhgevveh hlpvtvrger tgiltvrlpv ersdpetvdg lvqaarllgh elvvaerdtd
      121 vyqrarrisr ltlaaemqwq llparacsad eyaigahlep aydthgdnyd wasdadeltl
      181 avtdgmgtgv dasmlthlav nalrnarrag isiedqaala dqalyaqyrg aayvstlllc
      241 fdlatgrvqa vdagspqlwr lrrrtierie lepqmplgmf eethykaqef evlpgdrlli
      301 vsdgvyaahs pqgeayaera lartlhagrl lpaadvprav lrdlaayrda espdgslvlc
      361 vdwfgqrgdr pagpgqaand gdgar
//
LOCUS       WP_457691942             398 aa            linear   BCT 27-JAN-2026
DEFINITION  FUSC family protein [Streptomyces nigrescens].
ACCESSION   WP_457691942
VERSION     WP_457691942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Utsumi,R., Yagi,T., Katayama,S., Katsuragi,K., Tachibana,K.,
            Toyoda,H., Ouchi,S., Obata,K., Shibano,Y. and Noda,M.
  TITLE     Molecular cloning and characterization of the fusaric
            acid-resistance gene from Pseudomonas cepacia
  JOURNAL   Agric Biol Chem 55 (7), 1913-1918 (1991)
   PUBMED   1370369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43664
     Region          34..223
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 magsagrvep seagrfarig qwwsralgsd gyerhtalli gkstlaatia wvisanllha
       61 qspafapfsa vlitqvtvyq slvqslryvg avvagvavqv algfmvgpev vtfalvalva
      121 lvigrwpalg vqgsqvataa ffafstyasa tgypekitel gqivllvlig svvalvvnla
      181 lfppmrfrsa eysvralaha lcdllgdihp alstgeleee rtqqwrtraa qtgelisear
      241 agmrtaqesl yynprrlfrr hrghtgfeny gavldalera lyqvasltrs ldqwrdtets
      301 ynyrafvery gtflasiadn arllstlded hladqagelc rladraqryr rqvteqaerd
      361 glpladparp ygvlvveair lmeefqhtsd vlrryadk
//
LOCUS       WP_457691944             236 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457691944
VERSION     WP_457691944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  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
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Identification of a PD-(D/E)XK-like domain with a novel
            configuration of the endonuclease active site in the
            methyl-directed restriction enzyme Mrr and its homologs
  JOURNAL   Gene 267 (2), 183-191 (2001)
   PUBMED   11313145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..236
                     /product="restriction endonuclease"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24747
     Region          112..223
                     /region_name="Mrr"
                     /note="Restriction endonuclease Mrr [Defense mechanisms];
                     COG1715"
                     /db_xref="CDD:441321"
ORIGIN      
        1 makpirreha ttrrprfsmr qltivfglva sgvlgiglal ksmqgstlrp gavallglvl
       61 vatalavirg rnrggprgpg tsgaeapqaa pepglrseeg gpeavyladd aelgpdefer
      121 amallcerdg creirvvgga ndlgadvlav tpeglrlviq ckqycednkv gsedlqrfgg
      181 tcftihgadi aavvttstft epaveyaeqs gircfdhdml faweagtgpa pwqtag
//
LOCUS       WP_457691948             322 aa            linear   BCT 27-JAN-2026
DEFINITION  SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457691948
VERSION     WP_457691948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=36149
     Region          21..181
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mghkakkrss ykgtsskail hqydflgdfy rltlgpelvf sygmweegdt ldsaqtrkld
       61 yhaeaahavg aervldigcg ygsllhrlve ahhvqhavgi tmspgqaawa rdqhwpgcev
      121 raenwfdhep dgpydaiiai eviehcagnt mwrtqrvary reffqrchsw lrpagrlsvq
      181 anawnergwl aslvlppqql aphrgggare rlalkdilgg iknvreglha srkvypecfl
      241 ptrdelieas rglfgivear sdpddgvatv rswlekaean rvrgaelige savsdiireq
      301 ktalrflreg rftvvrmvfe ka
//
LOCUS       WP_457691950             546 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457691950
VERSION     WP_457691950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..546
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59691
     Region          10..494
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 mhtaprppsa svgpqldavi vgagfaglyq lyrlralglr trvleacddi ggtwyrnryp
       61 garcdiesta ysfsfspeld qewewserya tqpeilrylh hvadrfdlrk dvtlrtrvtg
      121 avyderghtw qvttdtgetv strfvvlatg cmsavkepdi pgagtfagra lhtaewphed
      181 vdltgrrvav igtgcsgiqa ipllaeqaae ltvfqrtpvy alparnrpls aaetaelkar
      241 ypefrtaqrr srggtvfelp trsalevdea erratyeegw dsgllsgllr tytdilvdra
      301 anetvaefvr skirsivtdp etaetlsprt fpfatkrpcl dtgyyatynk phvsvvdltr
      361 tpiveitprg irtsdrehav dviafatgfd altgsqvaid ivgkggttlr ekwaagprnh
      421 lgllsagfpn lftvigplsp svlsnavvai eqhvewitdc lahlrrkgit eidatpraee
      481 dwcthvagla aqtlypavas wytganvpgk prvflaytgg ldryraecda aaedgyrgfa
      541 lsggad
//
LOCUS       WP_457691952             866 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457691952
VERSION     WP_457691952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 866)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..866
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89227
     Region          2..863
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mlrtalrnvl ahiarlimta lavllgvafv sgtlvfadtt analrnasaq slkgvavsvr
       61 aeaatatdpa apesaggedg kpataldsal aqkirqlpgv asvrptvhge atlagkdgrp
      121 vnadtngqnl atnyhpgkdg kdsrfplkqg rgpaaegela ldttttekag yrigdtvrfa
      181 tdgpaltkkl vgivstddpq vtaggsltlf dtrtaqklfr hpgqfdeiav aagpgadeya
      241 ltdqvqallp kegvsatsgs elaaqqsaqi aentgyltkt llvfagialf vgvfliantf
      301 tmliaqrsre ialmravgas rrqvvrsvli eaallglvas aggfslglgi atglrpllnm
      361 tgaalpdgsl vitpaaplas lavgvlvtvl aawlpsrkaa kiapvaalss vdqapparal
      421 mlrnilgtll tgagvvvmly vatlktstes hlmtamlgat ltlggviala pllsrplitl
      481 agkvttrffg vggklaeqna lrnprrtaat asalmiglal itgltvgahs aqyamakeat
      541 qgltadykvn ystarglepa aatkiarapg vaaaapvvta qldaqgedav itgtdpkafg
      601 kaaqldfrtg slhdigpgki avsdefagrv glqvgatlda elgggmdsgr ahkkkltvvg
      661 iyaktrttde algtltdvlp ysvtkeldkv lvkaepgkaa gvdrkiraal gdspllkvrs
      721 qeqlikenne svttvlsmmy gllgmavvia ilgvvntlam svfertreig mlraigldra
      781 girqmvrles vvislfgavl gigtgiflaw aggglttssm reyetvlpwg rlgtflvlal
      841 migvlaaiwp arraarlnml qsiqps
//
LOCUS       WP_457691954             259 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457691954
VERSION     WP_457691954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27730
     Region          19..236
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mpqpataptr lrapsvaara teltkvygeg eirvvaldsv tvefgrgrft aimgpsgsgk
       61 stlmhcmagl daisggsari gdtelsglkd rqltrlrrek igfifqsfnl lptldaleni
      121 tlpmdiagrk pdqewleliv gtvglagrlr hrpsqlsggq qqrvavaral asrpeiifad
      181 eptgnldsrs gaevlgflrd svrelgqtvv mvthdpvaas yadrvvflad grvtdelpap
      241 tpgavldrmr rfdakgrts
//
LOCUS       WP_457691956             252 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457691956
VERSION     WP_457691956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25953
     Region          1..232
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mastdrlgqi tdavreagql svaelagltg asemtirrdl ellsgqgvle ryrggarsll
       61 lrgeeppftl raqegleakr rlaaevaeli adgesvvids gttclevara lahrrltvmp
      121 lslhavnalt ggphlqlllp ggaprpvela ltgplaeasl galrfdtavl gccglntang
      181 ltaydladaa vkraaiasar rviavaeaak ftrtalahvt gvsaldavvt eesapaeele
      241 alaaaqvtvr qv
//
LOCUS       WP_457691960             386 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691960
VERSION     WP_457691960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /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=40729
     Region          17..359
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrelirriaa atpdgrdrgv dalralailg vmlghwlvta lvadsgtvrv vsplhqlpql
       61 tpaswllqtl avfflvggqm aatswaaara rggtyrrwlg artvrlfrpv aavlvvwsvv
      121 agallvtgag lqtvrtlgkl alsplwfllv favltaatpl varlhplwpl avvlhidlir
      181 fglggpawlg wanvaagwlv pyclgaawar gglrggvtgw vlllggtvtt aglvlwagyp
      241 aamvgvpgag isnlnpptla avtfglaqcg aallllgplr rllrrpalwa avalmnlsam
      301 tlflwhqtam mavtavgllt ggflpglhtl pdgagwvlar lawlpvfala llvcwaafrt
      361 yeqgrcggtk vireerpvea ravrra
//
LOCUS       WP_457691962             454 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457691962
VERSION     WP_457691962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  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 454)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..454
                     /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=48299
     Region          197..444
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mhrvsqggwk sggprlwaav rglphtlred lwtvardplp rmrwlgrlph ahvvlftvlm
       61 gwlnadrykv dfgpsagttv lvlavlqsga avlalsrpvp awwlstialf lvrnadavsp
      121 halwswsipg ialhalvlfl lalrvrpria aealvlsfla gaatpvfaap apdpsllpgs
      181 vpldfaaadq rsltqdamaf tiavvlgtal rgrrvartql veqevltaee rarrtlleer
      241 nriarelhdv vahhmsvisi qaqvaphlvk dptdelkehl agirgnavea ltelrrvlgv
      301 lrsedaladg vrhtpqptlg rldelvgtvr gaglrvttei tgeprplspg velsafrivq
      361 ealsnairha pgaevrvaig yrtggltiri ansapdgpap psqgaghgll gmhertamlg
      421 gelatgptpd ggyevtailp aqaaqpddpg epap
//
LOCUS       WP_457691984             503 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces nigrescens].
ACCESSION   WP_457691984
VERSION     WP_457691984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54375
     Region          46..503
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mglfeaagar vidspagtak ldraperggk ggkggnqpte rrlrqlalav dtggvllpvg
       61 llcavthqpq plltavlaga swlavgaskn rysreelagd davmpvlrdw ltmlgvlavi
      121 cvaarvevsl kicvlallpc lalsvarrkl vhryllairr raqalrrvli vgeagavdav
      181 laelahrtdh eyvvvgsclv geettdsavp vparlasdgs tpeaeldget vlgcaaelda
      241 dlvfvapgrq lsaarvrrla walhdggrnl aifpglidvs qhrvrlakaa gltvmhidpa
      301 arrgmpvllk qvtdrlgall llvllspvfa lvaaairlts ngpvfywqir vgqdlmpfrm
      361 wkfrtmvvta drmraalepa nehdgamfki rrdprvtpvg rllrrfslde lpqlfnvlag
      421 hmslvgprpp lpeeverydg telrrlsvkp gltglwqvsg rsdltwdetv aldlsyvdnw
      481 sytrdigvlv rtvravvdgr gay
//
LOCUS       WP_457691978             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease H family protein [Streptomyces nigrescens].
ACCESSION   WP_457691978
VERSION     WP_457691978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=25229
     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 miapmaervi aacdgaskgn pgpagwgwvi gddagtvvrw eagplgtatn nvaeltaler
       61 lltatdpavp meirmdsqya mkavttwlpg wkrkgwktaa gkpvanqelv vsidalltgr
      121 svefryvpah qvdgdplndf adraasqaai vqeaagsalg spqpppapdt vrpaatrrrt
      181 sgpaaqkasa pqrrtsgkpt rtlnakfpgr crcgrsyaag epitknpegw ghpacrsgag
      241 dd
//
LOCUS       WP_457691986             314 aa            linear   BCT 27-JAN-2026
DEFINITION  GDP-L-fucose synthase family protein [Streptomyces nigrescens].
ACCESSION   WP_457691986
VERSION     WP_457691986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33683
     Region          10..305
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(15,17..20,40,43..46,66..68,70,90,109..111,140,144,
                     167..168,170)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(87,111,140,144)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(111,140,169,188,205,213)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mddllptpar vfvaghrglv gsavarrlsa rgydvltrtr aeldlrdaga taaylrsarp
       61 davvlaaakv ggimanstyp vqflednlsi qlsviagshq agvrrllflg ssciypkhaa
      121 qpitedalls gpleptneay aiakiaglvq irsyrrqyga sfisamptnl ygpgdnfdle
      181 tshvlpalir rfheakeqgl peltlwgtgt plreflhvdd laaacevllr rydgddtvnv
      241 gcgtdltiad lascvasavg yegriafdps rpdgtprkll diskmralgw sptiplaegi
      301 artyrawrae patv
//
LOCUS       WP_457691995             560 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide biosynthesis tyrosine autokinase [Streptomyces
            nigrescens].
ACCESSION   WP_457691995
VERSION     WP_457691995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 13405342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..560
                     /product="polysaccharide biosynthesis tyrosine autokinase"
                     /calculated_mol_wt=58944
     Region          49..381
                     /region_name="YveK"
                     /note="Capsular polysaccharide biosynthesis protein YveK
                     [Cell wall/membrane/envelope biogenesis]; COG3944"
                     /db_xref="CDD:443144"
     Region          310..498
                     /region_name="BY-kinase"
                     /note="bacterial tyrosine-kinase; cd05387"
                     /db_xref="CDD:349772"
     Site            order(310,313..314,316..318,338,366,368..369,419,422,
                     445..446,448..451,454..455,458,470..471,473,475..476,479,
                     483,486..487)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:349772"
     Site            order(339..344,366,371,443,497..498)
                     /site_type="active"
                     /db_xref="CDD:349772"
ORIGIN      
        1 msvfdepaee pdqirdqlrq lfryralvvl glvlgmlggg avsllggsty tatgevvvha
       61 istapfeagg vsvdkqismg terqiaqsas vaagaakalk ldsdpatlqr dlrvsnppet
      121 qtlmfeysad spdraaalvn afvqaylkyr qdaatqridk tvgklsaelk pleeqrkvld
      181 rriaggsggs gratdesers nlvseiadlq grisslksld ttpgdivrkg dppafpsspg
      241 lavlllagav vglvlgilaa wirsvleprv rsvadvqdnl rapvlgilpr rqggtellev
      301 grtgrgnrae ayrtiafrlv hdqrfagrgs llivsprena eavsvavnla gafaeigndi
      361 llveadlrtp qlaqrlplhp ghgrpvpgsw adgerlavda gvdgrfdllp grevpnpara
      421 lsspqfarll napsgpnenv vvvtgpllsh adglavakqa agvvvvcdln evrrddldrv
      481 welitgaggh ilgavldkgs rgtslrrltd ggpthrkrgr grprtaavap pprpgppppr
      541 tgpapqdgas ldadttslrr
//
LOCUS       WP_457692005             353 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692005
VERSION     WP_457692005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38010
     Region          22..341
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrspkdffrp lavgaptpvr evpfrpsrmi hffdpgnekm aakvpsiapt vdvllgnled
       61 avaadrkeaa rsglvkiaqa tdfgdtqlwt rinsldspwa lddlltlvge igdkldvimv
      121 pkvegaedih yvdrllaqle akaqirrpil vhailetatg vanveeiaga sprmqgislg
      181 padlaasrrm kttrvggghp gylvredphg pdgaapratf qqdlwhytla rmvdacaahg
      241 ilpyygpfgd ikdttacedq frnafllgcv gawslhpvqi aiakkvfspa padvawarrv
      301 ieamgdgtga vmidgkmqdd atykqcqvva eladalaard pelrdayaaa eke
//
LOCUS       WP_457692007             290 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692007
VERSION     WP_457692007.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30679
     Region          7..290
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msdailrprr svlympgane ralekakslp adalildled avapdakada rkrvaaaaas
       61 geygyrevti rvngpgtawh addlraaaea gpdavvvpkv dsadtvreve raleaagapd
      121 rtaiwamvet pramldarav aaaserltvl vmgtndlake lhaehvpgra plltglslal
      181 laardtgkai ldgvyndvkn aegfeaecvq grqfgfdgkt lihpsqvepc nrafapsadq
      241 vahaqkiida fdeatregrg vvtvdgrmie nlhvedarri lalaeaiagr
//
LOCUS       WP_457692013             457 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692013
VERSION     WP_457692013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=48162
     Region          60..338
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mskvlfvyak ggpplgyals rvaarsavhl lalsalpptv aasadrlcas vlrpaeserr
       61 dlvslivsra qavgadavvt fseyavvava eaceklglag aggscalard krmmrrtwqe
      121 rgisqprfrp vaterdlhda aaalrfplll kaawsagsta hrilrsaddv paawerarev
      181 maesaqlgya elhvagagad fiveeivpgt asewfdqegw gdyvsvegvv vdgdfrpvcl
      241 sgrmptvepf teragitpaa lphdaqrrvv alareavdal glqncgthte iklgaggqmw
      301 vietaarfgg amtvpqieev fgldligmlt dhllgrrvsw paevrtpqea hgaagslvvl
      361 avdgageawp dqrvwdfptv rdavplsags hlsvvaensl pdgtpvpvyd paagantmaa
      421 lcllsatdpe tvirdfralv dalprilpaa gptevra
//
LOCUS       WP_457692019             273 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692019
VERSION     WP_457692019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29219
     Region          47..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mrateagryg eglfrpeetg eagridlgal aydevsaarl aalgagpgwh cldvgagtgt
       61 varwllesag vtgvlavdrd trsldagrtp glstltadit apdfdpgrfq lvharfvlmh
      121 lrswrrmiak lcslvapggv lvlsdavdlt tagapatpyt tvmramwqgl resigtdisw
      181 vpdypyllre eglhrvaaei hvpplvpgsp lsrfwadtwd raqgamlatg qvdeaqiera
      241 rralssdeca glspgmltaw gwrteeagrd qql
//
LOCUS       WP_457692022             378 aa            linear   BCT 27-JAN-2026
DEFINITION  agmatine deiminase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692022
VERSION     WP_457692022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Shek,R., Dattmore,D.A., Stives,D.P., Jackson,A.L., Chatfield,C.H.,
            Hicks,K.A. and French,J.B.
  TITLE     Structural and Functional Basis for Targeting Campylobacter jejuni
            Agmatine Deiminase To Overcome Antibiotic Resistance
  JOURNAL   Biochemistry 56 (51), 6734-6742 (2017)
   PUBMED   29190068
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Shirai,H., Blundell,T.L. and Mizuguchi,K.
  TITLE     A novel superfamily of enzymes that catalyze the modification of
            guanidino groups
  JOURNAL   Trends Biochem Sci 26 (8), 465-468 (2001)
   PUBMED   11504612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="agmatine deiminase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016813 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear
                     amidines [Evidence IEA]"
                     /GO_process="GO:0009446 - putrescine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39868
     Region          51..374
                     /region_name="PAD_porph"
                     /note="Porphyromonas-type peptidyl-arginine deiminase;
                     pfam04371"
                     /db_xref="CDD:461280"
ORIGIN      
        1 meisrrqtlq aavvtalgga lsgcgtpdsr pgphgagaap aaartagggr lpdeahphea
       61 tymawpgrqv wgphtagvra diarlartia efepvrllag greakaaqra cgsgvevvpt
      121 pvddlwmrdt gpvfvlgpdg vagvdlnfng wgdkqehghd rrvarailad erlprikapl
      181 iseggavegd gqgtlmvaes slvndnrnpg rsradlergl kdvfgastvi wvkgvkgkdi
      241 tdyhidalar fsapgvvvls tpaknaprnd ftgayeqark vleravdarg krlevvelpe
      301 padigrrgeg flacyvnyyv angavimprf gdrkadskaa ailreqypgr eivplpvdni
      361 geggggihcs tqqlpkad
//
LOCUS       WP_457692024             435 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692024
VERSION     WP_457692024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44334
     Region          34..393
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(36,69,124..125,127..129,132,152,155..156,159,235,
                     238..239,242..244,247,271,275,331..332,336,340,356,
                     359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpaiprpaas gplrlrdfrl llagaaagql gaqvtlvalp lvavlelnap afqvglltaa
       61 etaafllvgl pagawvdrmr klplmiradv vravamasip laavadaltm vqlylvalvt
      121 gvatvffdva hqsflpqllp kdhlvsgnga letirssaqv agpglggglv qllgaslaiv
      181 adaagyvlsa lflwgikqpe slppriagss lrqdiaeglr fvcghrllrv iavttglanf
      241 ftatlmatqs vflvrvlgla pgvvglvlaa savggltgal cagrlaarlg qariiwlsal
      301 atgpfamlwp lsgrgagaal favgsgvvff gavvynvaqv sfrqalcppr llgrmnatlr
      361 flmwgtlplg alaggalada fgartalvwc aagflvvplp lllsplrrmr dlpvadaaed
      421 apagsadpae pasvg
//
LOCUS       WP_457692028            1064 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457692028
VERSION     WP_457692028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1064
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:1901576 - obsolete organic substance
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=113257
     Region          2..1064
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
ORIGIN      
        1 mlplsssqei vwlheqvqpg sraynftaal dlwgtldtea lrhgltatld rhaglrlelv
       61 avagampgqr vaeacaprlr tvdlsgaadp etafqellrt eaetpldtye apllrwtlvr
      121 laddrhrlih vehhlihdgh sfaillrdvf tvyrgrvlge pvelppapsy adhvrartgd
      181 rataerregl efwagalrem sydmplpgla rpgarrrhhg gqlrqsigad laerlrahar
      241 argltpfatl lglfaellrr hsgrsqmvig tavgnrprgf edavgmfvnt iplplrldpa
      301 apaeesmdev tdtliralph qevpiqeltr alglhtsgad nplfgvmfsa hdaelpdidv
      361 pglditlfeg fntgttrfdl dvvllpddrr gvgprhgaag mtlvwdydad mfgedvakll
      421 agrfldllra yldapgtala dlapppappa lpaaapqtpr hdpldpatah drslpallvg
      481 arritygdla drvaalaqrm laagvtagqp vaavlprgad svvtllaclr travycplsp
      541 sdpparlall lerlspalvl tsadaavpvp dglpsatvda avlpparaae svpgaaylih
      601 tsgstgipkp vavgraalen hltgaagrfg lgagdrvllf aqpsfdvale evlpslyaga
      661 clvaperevp tgtelaella aarvtvvnlp tsyflatrqe mrsalrdghw aprllvlgge
      721 rlpadalrtf ladtdstvln vygvteaais stvheitrdg lidgaeiplg telpgervhv
      781 ldahhrplpd gavgelaiag aglaegyvgn peatearfrr iealggervy ltgdrgyrgr
      841 dgllyflgrl dhqiklrgyr ieleeveaaa saalggrsca vvldreapgg prlvgflesa
      901 dedgpwdeqa lhtelsrrlp salvpgrwar ldvmprlagg kpdrtaltrs aaalepaapi
      961 apaaepgdgq paeaadpmta llvegwreal ghgrfdlssd ffrigghsll aaqlaswlep
     1021 rlgqrpplrl lfqnpvltdq aaalaavgta spvpaasttv tesr
//
LOCUS       WP_457692030             647 aa            linear   BCT 27-JAN-2026
DEFINITION  non-ribosomal peptide synthetase [Streptomyces nigrescens].
ACCESSION   WP_457692030
VERSION     WP_457692030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10147902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..647
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=67016
     Region          56..541
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(195,198..203,205..206)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(198..199,313..314,330..335,361,429,441,444,535)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          571..630
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mtqpmtarta apttaagagr htphpgtlsi thgarpagdg aagvlarfee wvrrspeapa
       61 vidgahswty rqigtaadev aqalrarvrp gdlvgvcldr saalvvtava larigavylp
      121 lgprpgerrt davtedlnvv cligdpgllp prhrtadrmd lmlpgegana tatvvaafaa
      181 pgatahsapa gafyavltsg stgrpkavav gepalgglld wyrattglgp gdrqslmigv
      241 afdphllelw agltsgaalv papdevrwds vvlagwwrta gvsvavaatp mveplldrpw
      301 pqdlrlrhll aggdrmrrrp gaevtatvhn aygpaeatvi attyamhgtd saagtdsapp
      361 iglpvpgvtv lvadpdgrpv ergtegelli ggsglalgyl dpeltarrft avpeglelpg
      421 vervyrtgdr vrmaadgrle flgrlddqvk isgvriepae veaafeqdpa vlsavvtapr
      481 tadgrarlva yvraaadsgl tadallptlr awlpeqavps dirivgsfpl dangkvdrae
      541 ltrraagsgt prpggaapdd gapagatpge rlvlsavrdl ldrpgtslad nfteaggtsv
      601 laarlltvie kesgirlrap ellrqpdlra vallvdqrca srqpaga
//
LOCUS       WP_457692038             167 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692038
VERSION     WP_457692038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18592
     Region          2..164
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrllllsdth lpkraktlpp qlldevprad vvvhagdwvd tatldlltar arrligvygn
       61 ndgpelrarl pevayaelag vrlgvvhetg paqgrerrca erfpeldvlv fghshipwds
      121 tagdrlrlln pgsptdrrrq pyctymtaei tagrltavel hrlprrq
//
LOCUS       WP_457692040             275 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692040
VERSION     WP_457692040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28320
     Region          30..272
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mrgtgeteqa atahqdaava gagadrkpla ggvalvtgas sgigaatala laregcslal
       61 varrtgrlee laeaigaqgg aslaltadla aaaevrrtvd qtvdhfgrld vlvnnagfga
      121 rgavadsdla dwdrmvdlnf kavlrmshaa lphllraahe gprgvadlvt vssvagrvpr
      181 kdnsvysatk havcsfseal rqevtgrqvr vglvepgmtt temtrggsqa asahglppes
      241 wlqaediars vvfmvtqpph vaineitvrp taqer
//
LOCUS       WP_457692044             131 aa            linear   BCT 27-JAN-2026
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692044
VERSION     WP_457692044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..131
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14182
     Region          1..123
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mrrqpvlvyd gdcafctssv qfaerrlrpr caaapwqftd laklgisrqr aehevlwvtp
       61 tgsvhggaqa vaklllsadr gwpvvgallt lppvrwvahg vyrmiarnrh rmpggtaaca
      121 lpssaaarkq l
//
LOCUS       WP_457692046             243 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692046
VERSION     WP_457692046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /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=26212
     Region          <61..103
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          130..237
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkrrlnlrip rsgagrrasa alavtaltvp ltvalgstaq aatassctas rgpyqkqaek
       61 flglrvdgrq saadcraira fqtshgitpn igyagpvtwg vmrvvaqqka aghnpnkagh
      121 cptnkgriac vdltrqlswi qdgrklvfgp vpvrtgrdgy etrtgakkiy wrhlhhvstl
      181 ydvpmpysqf fdggqafhsi sgsvwsapgs hgcvnmrsnd akkywsllkn gddvyvygrk
      241 sgt
//
LOCUS       WP_457692050             162 aa            linear   BCT 27-JAN-2026
DEFINITION  EF-hand domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692050
VERSION     WP_457692050.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Persechini,A., Moncrief,N.D. and Kretsinger,R.H.
  TITLE     The EF-hand family of calcium-modulated proteins
  JOURNAL   Trends Neurosci 12 (11), 462-467 (1989)
   PUBMED   2479149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11473824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..162
                     /product="EF-hand domain-containing protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16944
     Region          4..151
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mitdalraey ehrfsmydtd gdgyltaqdf tdrarvltda vgepadsaka ralgagmrht
       61 feqlaalaqv datgrlnreq fveafarage lgslgrvvgp siaatvalad adgdgvvsre
      121 dfaavhraag ysaaqaeeaf aaldrdgdgr llleawpgaa pe
//
LOCUS       WP_457692058             676 aa            linear   BCT 27-JAN-2026
DEFINITION  M3 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457692058
VERSION     WP_457692058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..676
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74314
     Region          1..676
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mtasnpffep sdlpyelppf arirndhflp aftrgmadql aevaaigaca gpatfentve
       61 alersgavlg rvrrvffnkv asdtdeeiqa leveltprla ahddmlllda alfdrldtlh
      121 eqreqlgldg eqlrllerhh trrvragarl apeqqqrlre lnaeiaalct efgqnlraat
      181 adaalvldra eelaglpadq iaaaaenaqa lghpgkfvlv lknfscqtel aaledpalre
      241 rllaaslgrg idsngpiavt larlraeraa llgypshaaw evadrtagtt daveellgrl
      301 vapavanaer egaalaetag vteiraadwq yyservrker ydldaaalrp yleletvlhd
      361 gvfhaaelvy gitftrrpdl vsyhpdahvy evhdadgspl glyigdfhar eskrggawmd
      421 slvpqshllg qrpvvvnnln vakppagepv lltwsevntl fhefghalhg lfsdvrypll
      481 agtqvprdfv efpsqvnevw adwpevlahy arhhltgepm paelparlre aenfgagfrm
      541 vehqaaavld wawhtlsadg dvpgedevea feaaaleryg lamaaippry rtgyfahifn
      601 ygyaagyygy rwaevldadt vrwfrengrs iresgeifrr ellgrggsvd plaafravvg
      661 rdaeigplla rhgltg
//
LOCUS       WP_457692060             205 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457692060
VERSION     WP_457692060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22163
     Region          6..187
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 mdikaaiaae rrelaalldg lpaeqwdapt lcagwrvrdv vahmsmgfry plpkmaaell
       61 raggnlhrmt drcarrdaaa astselagfl rehahhpwkp pvggiaaalg hdvvhgldit
      121 valgldrrvp edrvrlllek itpgtarffg adlrgiqlra ddldwsfgsg tplsgtaqdl
      181 llvaygrklp pgrlhgerhq hfvag
//
LOCUS       WP_457692062             333 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692062
VERSION     WP_457692062.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34409
     Region          1..301
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqlqyfv avveeanftr aaarlhlaqp gvsaqirqle relgqplldr sgrsvtvtev
       61 geavltyara alaaaegirq tvdqfsgllr grvriallsg agsnrfdmas lladfhdahp
      121 qveisltedt sermlialqr galdiavigl mdeepppgts cqvvvdeplv aavapddall
      181 tpdvertgip laalrdrali slprgtglrg vleracaeag frpriafeaa apqvlarlaa
      241 rglgvavvpa lpaeeaaaag lrtleitapr prgrvalawr tegpagpaar allgrlraal
      301 pavgtgggaa vtghaggarr aagaapdhqa vga
//
LOCUS       WP_457692066             890 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692066
VERSION     WP_457692066.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 890)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..890
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92369
     Region          33..444
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(40..41,44..45,48,79,129..130,132..134,137,157,
                     160..161,164,295,298..299,302..304,307,335,339,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          <646..>869
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mstttsppga gteeipgpgv lshrqiltil sglmlgmfla aldqtivsts irtisddlhg
       61 lsrqawatta ylitstiatp lygklsdlyg rkpyylaait ifvvgsvlct fstsmtelaa
      121 fravqglgag glmslalaii gdivpprera ryqgymlgtf atssvagpli ggalagqdql
      181 lgitgwrwvf lvnvpigiia lfvvakvlni phtrrdhrid wwgaltisvg vvplllvaeq
      241 grewgwdssr siacyvtgvv giiawifver wvgddalipm rlfrngtfsk tsvlsvligm
      301 gmfggllmip qylqivkgas pttsglqmlp lmagmmiasi asgqitaktg rykifpiigt
      361 almvaamllf hfrvqwdtpl wetmaymlvf glglggcmqt lvlavqnavp prdmgvatas
      421 stffrqmgat agtaiflsvl fstvgdkisa afkdaaster fqaalhdpav lhdpankpvl
      481 dmlkhpgnad ssgvlsdssf iqhldprlae pfkrgfadsm htvflmgaiv valafvlmwf
      541 ikevplrqis glqaraqada eadaaaksag gaadsadaaa dgaddasadg addaavmpep
      601 yessessdpa gapvvdpgpa lagasatlad rgigttgpei rgavrdgdgr pvtqaavtli
      661 svdgrqlgrt staadggyal pttgagtyvl igsagarqpq avtvvvggep vsfdltlgga
      721 aglsgevrae kgdapvpgal vvatdvtgev vasgvagqdg sfafgelvpg sytlavsaer
      781 hrpsalpvev tsgnrnwyev rltpgaqvrg tvrtvhgspv ddarvtlldp agnvvgtats
      841 gqdgayvftd ldsgeytlia sgyppvatpl rleaaghgaf dielghepvr
//
LOCUS       WP_457692070             217 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692070
VERSION     WP_457692070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23175
     Region          10..194
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          54..144
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mveqdalsat reaydaaapt yaqlfrdslr dspldrailg afvevvsasg dgqvadlgcg
       61 pghiaaylde lglavfgvda spamielarq aypglrfdvg smtaldiadg alggvlsrws
      121 iihtppqelp vilaefhrvl apgghllvgf sasddpshpt qafdhavtla yrwspdhlaa
      181 llrksgltev armvrepqpt drrqfqevql larktsh
//
LOCUS       WP_457692076             331 aa            linear   BCT 27-JAN-2026
DEFINITION  D-cysteine desulfhydrase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692076
VERSION     WP_457692076.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10012093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="D-cysteine desulfhydrase family protein"
                     /EC_number="4.4.1.-"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33201
     Region          10..318
                     /region_name="PRK03910"
                     /note="D-cysteine desulfhydrase; Validated"
                     /db_xref="CDD:179673"
     Site            order(52..53,81,190..194,275,304..305)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107202"
     Site            53
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
ORIGIN      
        1 mssdsgtprr aalatwptpl epaprlaral glgaedlwvk redltalggg gnkvrklewi
       61 cgaalaegat tlvttgaaqs nharltaaag arlgldvvlv lagaagssts gnlaldglfg
      121 atvvwagevg gkqlaaaaee vaqrlrerga vpaliplggs splgaygyae cgrellsqap
      181 dldtvvvalg sggtmaglvd tlgpgkvlgv dcgavrdpad tvtglvtals gtvhapetlr
      241 lrreqvgagy stlteesmda lslagrtegi aldpvytgra laglraavrd gsvapgrrtv
      301 llhsgglpgl fghsdavarc qealtvlpfh e
//
LOCUS       WP_457692084             256 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692084
VERSION     WP_457692084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 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   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28176
     Region          28..255
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mpaertrqht tpvaaarrrr lradrarqla dllrhqvlgg gfpggvlphe evigadygvs
       61 rntvrqaldl lraeqlverq pgvgtvvvcq kyphaldrlr glaetlhphg rvtnevrtis
      121 pvpapapvad rlripprsev lyverlrrld glplsldlty vpmhiglpll dadlenndvf
      181 rlieetagqp lgtakitlea vnadahsaav leaprgtavl mlerlthlad gapvdlefir
      241 frgdrltmrg llrrtl
//
LOCUS       WP_457692086              75 aa            linear   BCT 27-JAN-2026
DEFINITION  4Fe-4S dicluster domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692086
VERSION     WP_457692086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Fujii,T., Hata,Y., Wakagi,T., Tanaka,N. and Oshima,T.
  TITLE     Novel zinc-binding centre in thermoacidophilic archaeal ferredoxins
  JOURNAL   Nat Struct Biol 3 (10), 834-837 (1996)
   PUBMED   8836097
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Beinert,H.
  TITLE     Recent developments in the field of iron-sulfur proteins
  JOURNAL   FASEB J 4 (8), 2483-2491 (1990)
   PUBMED   2185975
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Bruschi,M. and Guerlesquin,F.
  TITLE     Structure, function and evolution of bacterial ferredoxins
  JOURNAL   FEMS Microbiol Rev 4 (2), 155-175 (1988)
   PUBMED   3078742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..75
                     /product="4Fe-4S dicluster domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=7990
     Region          10..68
                     /region_name="PreA"
                     /note="NAD-dependent dihydropyrimidine dehydrogenase, PreA
                     subunit [Nucleotide transport and metabolism]; COG1146"
                     /db_xref="CDD:440761"
ORIGIN      
        1 mplapqradv pvtidesqci dgctlcvdmc pldslaidpa snkaymhvde cwycgpcaar
       61 cptgavtvnm pyllr
//
LOCUS       WP_457692090             290 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692090
VERSION     WP_457692090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30141
     Region          64..289
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 maaahcarpg vvrgrpgpva dgpdgsrgav vtstetslaa psqapapglr ltlddavlgr
       61 pgapvldrld levaageilt vvgpsgcgks tllrtlagll pllggrltqd gepvrgpaad
      121 ralvfqedal lpwrslranv elplairgva rarrraragd wlarvglteh aarlphqvsg
      181 gqrqrtqlar alagrpravl mdepfgalda qtragmqqll vtalsgthat vvfvthdvde
      241 alflgdrval lgtgrvldvp rprmrgahtd patvalrrev lasldgrsgs
//
LOCUS       WP_457692092             374 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457692092
VERSION     WP_457692092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39506
     Region          7..358
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpslsprwpr yvefapsvlv agglvwdafs padywgdpml taasvtagal lslrhtlaig
       61 aaivggvfal tvkdgtagdi vgylelintl faalmgvgvn rviarhgrhl dvvrsvaeaa
      121 qlavlpappe rigplsiaar yqaaqseari ggdayavqrt pfgvrlliad vrgkglgavg
      181 avsvllgafr eaaeeepdla tladrmeral lresehtsee drlegfital lcevlpgaag
      241 lrllncghpa pylchddevr aleagdpglp lgmgtlgver tcpavrpfpv gstlllvtdg
      301 vteardrtgr fydpaaqlag hgpfrgpqdv idhlvrdvea wtggprdddm avlaltrqre
      361 grmriprsgs spdr
//
LOCUS       WP_457692094             109 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692094
VERSION     WP_457692094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..109
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=11841
     Region          <5..93
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrdlwepttv lrgglgsavr dlksapgndi vttgsitpvh aliaaglvde yrlfvhpvvl
       61 rhgrrlfada tgtaqlrlae trpfhsgial lryrtawhtk pspgvrrlp
//
LOCUS       WP_457692102             601 aa            linear   BCT 27-JAN-2026
DEFINITION  M4 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457692102
VERSION     WP_457692102.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 601)
  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 601)
  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 601)
  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 601)
  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..601
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..601
                     /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=62935
     Region          29..597
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrrphirrhr laiavavtta atltagvags asatppaspv aassatpalq kavdaardaa
       61 yahasatgvs kkdtleatda lvdpdgrqhv rfvrthrgmp vlggdlvvhl taksayegvt
      121 rafrhqvdms gtdpklsage artkaaaaak gragdaelvv darngrttla yqvqvadsrt
      181 aesggtrtiv ldaasgtvls nvaaddsfls palqrklrar gerlnpatgl ftpappatgk
      241 aakaagfpaa akgtgasffv gsvplsttqt akksftlkds trgntetrda gdkelekfss
      301 gkaftsttnr wgngttsnra taavdaqygi astldfykkt fgrkgikndg rgaralvhfg
      361 kkvgnafwsp dcgcmlygdg dgktfakplv vldvtghels hgvvdatanl qptrvdiegn
      421 qfgepgslne sladifgsav efstnnpknp pnyllgeklg ldqkflrrld kpsldklega
      481 vdywskasyd tevhagsgvs shayyllaeg sgkktiggva ynspthdgsk vtgigrnkat
      541 aifyraltry mvsttdfhda riatlraakd lygaksteyk tvnkawaavn vkasntpsak
      601 h
//
LOCUS       WP_457692104             399 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692104
VERSION     WP_457692104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..399
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40238
     Region          5..355
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 miidrtrgtr rlgypaaagv favgmagttl ptplyglyra qlgfselmvt vvfavyalgv
       61 itvlllaghv sdevgrrpvl lcalalsaas alcfvfeggl pmlllgrvls gfaaglfsga
      121 ataavlelag pgqeahagfa ataanmgglg cgpllsglla qyapwplvlp flvhlllvag
      181 aagvtwflpe tvghphrprk lrpqglrlpp evrgvftpsa vaafagfsll glftavapsf
      241 vgetlgvhnl avaglivftv flgstagqsl terigvrral pggclvlvvg lllvatslav
      301 tslpllviga vcggvgqgla fragltavgh aappehrggt isafflvayl gislpvvgvg
      361 altlvlglrg aglvfsgcvi vltvavglyv llhppaded
//
LOCUS       WP_457692112             166 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457692112
VERSION     WP_457692112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17999
     Region          16..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maenaadrgt qsggrparpd laamvvplgr almaaeqpvl dahgltmway svllhldetp
       61 irtqaalaea iradktriia vlddletrel irrqqdpedr rvrllsltte grrlrdaaqa
      121 aiqegeerll aqlpaadraa fvrslqtlsg lpeltarkpg rgspra
//
LOCUS       WP_457692116             440 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692116
VERSION     WP_457692116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47085
     Region          21..418
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,252,255..256,259..261,264,293,297,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mteagpqsip qsppsaipak rwayvipvaa imymlayldr nnvsvilpym hgdlelsnad
       61 kglvggiffv gyvflqipaa ilaqrwsark tvvllmvawg laasltglvq tksqfyvarf
      121 vlgffeggvw pavlillasw fplreraran alwmaclpls svfmaplsgw mldhaswrwv
      181 lvlqgvpplv wavvwwfava drpaqarwis raeadhvehs iaadeaakps agsgsyldav
      241 rqksvlvlig vyffwitgfy gfnlwlpsvi kelthdgsst evglltavpf tvalavmian
      301 aawsdrtgrr rqavavplvv giaalllgqa vdgalprmll lcvtaaavya pygpfwaipg
      361 qllrfevvav amglinalgn lggfagpylv gwltdvtgss vtgfavlsgf lavavalvtl
      421 glrpsarpvr plsgqaaegt
//
LOCUS       WP_457692120             432 aa            linear   BCT 27-JAN-2026
DEFINITION  four-carbon acid sugar kinase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692120
VERSION     WP_457692120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11465537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="four-carbon acid sugar kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /calculated_mol_wt=43341
     Region          3..419
                     /region_name="OtnK"
                     /note="D-threonate/D-erythronate kinase OtnK and related
                     C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate
                     transport and metabolism]; COG3395"
                     /db_xref="CDD:442622"
ORIGIN      
        1 maqvlvigdd ltgsnatgal yarlglravt vgdlaqvary adrvdvlvvn tasrhwtpar
       61 ayaavraaae tagevplvvk rvdttlrgnp gseldavvdv laarepaari ralavpafpd
      121 agrttvgglh lvdgvpltrt avagdpfdpv rhsrvaavlg tqsgrttgel aldvvergpd
      181 avaaalresp adivvcdate nahlgtvaaa aarlaaedri rwvaldsgpf gaalaaelgl
      241 rpeggapatv lavvgsvtdr trtqlartet algarwadld paapdpdrvl aalraaageg
      301 atvlgvrvap elpgaaagsa pvpdpgtaar ilralaeiar ravaelrpgg lyasggdvaa
      361 aatsalgadg faieaevlpl aiaghlvggp hdgllfatkg gliggpdaar dclehlraac
      421 trhtlgptls at
//
LOCUS       WP_457692121             294 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692121
VERSION     WP_457692121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31337
     Region          49..278
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mkratwkssl kdagrrqqae agsevtsger satrrrrerm vellgagdis vhdlaaefdv
       61 slstvrrdla tlaalgritr tyggavdhra verswhdkeh eqrgekdaia rtaaalvrsg
      121 dvvlldagtt varlahelrd radltvvtng lstlvelada evevvvlggr lrrpnesllg
      181 trteqalrrl tpdiaflgvd gldprrginc pdpeqaalke tmaecartsw vladhsklgg
      241 gggfpywaam pagtglisgg egrelaaftd agwsvhpaae gpedvvegap lhts
//
LOCUS       WP_457692128             484 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457692128
VERSION     WP_457692128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50342
     Region          24..458
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpytpvasaa perdtrsate gdasttpqlt rsigvvggtl ltlscltpas slfvivpdsf
       61 aglgtgtalt iavaallcig vaftyselgt lipssggeya mvgtlmgrla gwlvfilsli
      121 vvmivppiia lgtaeylapi vqldpqytaa gvmllatamg lldlranawi tgiflvlevv
      181 acavvaflgf thtqrsasvl vnpvidagng tstavtagli vtglatalfi lqgfstavyl
      241 aeemdnprrn vsrtvlwtla igaavvlipv vaitlgapdl ktlgagdvag mvqdwsnsgi
      301 gtfvslcial aiinaaivmv iqnsrvvfss ardaawptav nrifshvgrr fgspwaatla
      361 vgvpgaalcf vnldtlsevt gvavaamyvf valgalvsrr gehkhrpawr mplwpavpal
      421 lvvvlawvly qqstkslvit gvivavaaly wacylrprqe thwvisvped eqapvekpag
      481 slpv
//
LOCUS       WP_457692130             694 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457692130
VERSION     WP_457692130.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Levdikov,V.M., Blagova,E.V., Rawlings,A.E., Jameson,K., Tunaley,J.,
            Hart,D.J., Barak,I. and Wilkinson,A.J.
  TITLE     Structure of the phosphatase domain of the cell fate determinant
            SpoIIE from Bacillus subtilis
  JOURNAL   J Mol Biol 415 (2), 343-358 (2012)
   PUBMED   22115775
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..694
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74202
     Region          24..258
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          286..690
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mgatdafpeg aapvgatpgq pgglldvlgv aavmldadgr itlwspqaea lfgwsaeeal
       61 grpaaqllvg pehfdlvlgl fsqvmagges wagvfpvqhk dgstrlvefr nmrllderge
      121 syalgiatdq avlrrverdl alsvrlvaqs piglavldts lrfvmvnpal erindlpadq
      181 higrdvreal sfldtetias smrevldtgt plldqftvgr taadphaeqa wsvsyyrled
      241 ahgrvlglat svvdvteqhr aateaararr rlaviadasa tvgttldvdq taheladviv
      301 peladlaavd vldavldgrr ptslsrggpa rfralavsaa ysteavraad ptgqiasyea
      361 drlitrcvte arpvlvpqvs addlphiaad pqgaallgka glhsylavpl iargevlgal
      421 slyrvrnpvp fdeddavlav elaaraavci dnarsyqser rtaltlqrhl mnhrppqpta
      481 meiayryqpa qaasevggdw fdaipvagdk talvvgdvmg sginaaatmg qlrttarala
      541 dldldpaevl rhldhiavgl dpafatclya vydphrmecr iavaghlppv vvrpdrqpel
      601 ldlptgaplg vggvpfeqtt vplregdqlv lytdglietr dqpidtrldt llellvepqh
      661 dleglcdrll galrdehdhd dvalliarvh ahkd
//
LOCUS       WP_457692136             236 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692136
VERSION     WP_457692136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..236
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24967
     Region          10..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maaearspra ryreqnraei kaaalqqlae ggvqavaltr iakdmglsgp alyryfagrd
       61 dllselirda ydevaqavgr vgtapadear atlhaladay rgwavaqphr ylliqgtplp
      121 gyaappdtll raravlgpfl kvfaagvpaa alrpvveema awvrkeegva dwlaqhtgla
      181 phdeaagtal agtvlvwsql hgtvslevsg qyagmghraq tllaaqldtl adsfql
//
LOCUS       WP_457692142             191 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692142
VERSION     WP_457692142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20874
     Region          1..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpdrptqile aaarliarrg vrglrveevs aeaavstali yyhfkdragl lrrtlefisq
       61 ravrytdaal dasddprvql tgmlllelqd tpqvkensaa wgelratavf dpdlrellaa
      121 atrswvedla gllrraqeag pgeagtdpya aaerltalve glserwlsgt tslerahell
      181 rgavdtelrp l
//
LOCUS       WP_457692144             129 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692144
VERSION     WP_457692144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..129
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13777
     Region          <12..124
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mrktedqrsa daqwavvpad gggllgrasl rsvhlaegra ecaywtvpaa rgsgvavrav
       61 samvhwafge mgfhrlelah svanhascrv aaksgfameg trrsaqlhtd gwhdmhlhsr
      121 vredgppav
//
LOCUS       WP_457692149             381 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerate kinase [Streptomyces nigrescens].
ACCESSION   WP_457692149
VERSION     WP_457692149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37266
     Region          2..380
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mliaadkfkg sltavevaeh vtaglrravp glevsavpva dggdgtvaaa laagftrhea
       61 rvtgpmgapv tatfalrmga pavagggtav vemaeasglq hlpegvfapl tattygtgel
      121 llaaldagat sivfgvggsa ttdggagmla algarfldad gepvapgggp lrdlatadls
      181 gldprlarta ivlasdvdnp ltgpkgapav ygpqkgaseq dvatldaala hyagvlerav
      241 gpraaehala pgagaaggig ygalvglgad frpgidvmld vlgfapalak atfvitgegs
      301 ldeqtlhgka pagvaaaara aglevvavcg rlqlpqealt aagirrayal tdlesdparc
      361 maeagpller aaaqlardfl v
//
LOCUS       WP_457692153             269 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692153
VERSION     WP_457692153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  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 10004355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28583
     Region          2..>63
                     /region_name="MJ0604"
                     /note="Predicted nucleotidyltransferase, MJ0604 family
                     [General function prediction only]; COG1708"
                     /db_xref="CDD:441314"
ORIGIN      
        1 mdeiaakvaq vpgvvgvmlg gsrargthra dsdwdlgvyy rgepdlvale tlaaevtggp
       61 vevygpgswg awvnggawlv lpdgrhvdwi lrdvdrvrqv weecragrfe igvqaghplg
      121 fwspaypgea algrvladtd gelarlrhet qdypealrka ltrdgvwdag fsvamagksy
      181 aaldvlhval clsravgdlv qalhahhrvw clnekgalaa aaampetplg fgvrasallg
      241 elghteeelr rslteaeglv advravtgg
//
LOCUS       WP_457692155             181 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457692155
VERSION     WP_457692155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=19008
     Region          12..169
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtvhasdpaa pvthtvldgt pvgpltlvaa ggalsglymt dqrhrppqet fgdpadpdep
       61 pfaetiaqlq ayfrgelmnf dlplalrgtp fqrrvwaalc tipygetvsy gqlaerlgap
      121 sasravglan grnpvgiivp chrvvgangs ltgygggldr krrllafert edglfpaeac
      181 g
//
LOCUS       WP_457692168             473 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692168
VERSION     WP_457692168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50101
     Region          3..470
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mprmldavvi gagpngltaa velarrgmsv evfeargtig ggarteeltl pgfrhdpcsa
       61 vhptgigspa fsampldryg lewlhpdlpm ahpfpdgtaa vlahsvgeta mslgprdagt
      121 yrrlmapfvg kwdtmahdfl rtqwlglpqd pltyarfglv gmqpvsllnr rfqdakargl
      181 laglgahana plsgfgtsgm almfalaahh kgwpvprggs qaisdalagl lrahggvvht
      241 dfevkrlddl pparayvfdt sptalariag lgnayrevky gpsvfkidya lsapapwtak
      301 eahragtvhi gptqgeigaa lnaathgqdp svpflitaqp slidptrape gkhtfwaygh
      361 vphgwegdat daverqierf apgfrdlvla ravagppqia arnanyvggd tntgsaaglr
      421 llirpklarv pyetahpavf lcsqatppgp gvhgmsghya akavwrrlra nrr
//
LOCUS       WP_457692176             254 aa            linear   BCT 27-JAN-2026
DEFINITION  SIR2 family NAD-dependent protein deacylase [Streptomyces
            nigrescens].
ACCESSION   WP_457692176
VERSION     WP_457692176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   North,B.J. and Verdin,E.
  TITLE     Sirtuins: Sir2-related NAD-dependent protein deacetylases
  JOURNAL   Genome Biol 5 (5), 224 (2004)
   PUBMED   15128440
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Brachmann,C.B., Sherman,J.M., Devine,S.E., Cameron,E.E., Pillus,L.
            and Boeke,J.D.
  TITLE     The SIR2 gene family, conserved from bacteria to humans, functions
            in silencing, cell cycle progression, and chromosome stability
  JOURNAL   Genes Dev 9 (23), 2888-2902 (1995)
   PUBMED   7498786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="SIR2 family NAD-dependent protein deacylase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0017136 - histone deacetylase activity,
                     NAD-dependent [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27072
     Region          17..248
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mtgtvpspdq pprrplvail tgagvstdsg ipdyrgpngl wrrdpeaekl vtydtymgdp
       61 eirrrswrmr qespafraqp naaheavarl ersgtpvrvi tqnvdglhqr agmperkvle
      121 lhgtvrkvtc trcharssme ealarvaage pdpaclvcgg ilksatvmfg erldpqvlgt
      181 algvakaaei flavgttlqv qpaaslaava aehgarltiv naeptpydel aaevirepig
      241 salprllegl aarp
//
LOCUS       WP_457692178             355 aa            linear   BCT 27-JAN-2026
DEFINITION  lipoate--protein ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692178
VERSION     WP_457692178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kim,D.J., Kim,K.H., Lee,H.H., Lee,S.J., Ha,J.Y., Yoon,H.J. and
            Suh,S.W.
  TITLE     Crystal structure of lipoate-protein ligase A bound with the
            activated intermediate: insights into interaction with lipoyl
            domains
  JOURNAL   J Biol Chem 280 (45), 38081-38089 (2005)
   PUBMED   16141198
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Reche,P.A.
  TITLE     Lipoylating and biotinylating enzymes contain a homologous
            catalytic module
  JOURNAL   Protein Sci 9 (10), 1922-1929 (2000)
   PUBMED   11106165
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Morris,T.W., Reed,K.E. and Cronan,J.E. Jr.
  TITLE     Identification of the gene encoding lipoate-protein ligase A of
            Escherichia coli. Molecular cloning and characterization of the
            lplA gene and gene product
  JOURNAL   J Biol Chem 269 (23), 16091-16100 (1994)
   PUBMED   8206909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="lipoate--protein ligase family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="6.3.1.-"
                     /GO_process="GO:0009107 - lipoate biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /calculated_mol_wt=37610
     Region          106..354
                     /region_name="LplA"
                     /note="Lipoate-protein ligase A [Coenzyme transport and
                     metabolism]; COG0095"
                     /db_xref="CDD:439865"
ORIGIN      
        1 mqgrhhgeyk vpggklvvvd lavaggvlrg vrvagdffle pdealeaing alegapadag
       61 ardlaarida alpagaalfg fsseavgiav rravadaaew tdfdwqiiha gpqppalhma
      121 ldevltseva agrrpptlrv wewdrpavii gsfqslrnev deqgaarhgv tvvrrisggg
      181 amfvepgnti tyslsvpqsl vqglsfaesy aylddwvlta lgdmgikawy kplndiatda
      241 gkvagaaqkr lasgagavlh hvtmsydida gkmtevlrig keklsdkgit sarkrvdplr
      301 rqtglpraev iermiasfra ryggsdgvvs naelararel aagkfssvew lgrvp
//
LOCUS       WP_457692195             294 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692195
VERSION     WP_457692195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31169
     Region          63..258
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 meqstpwefs ddrgrlavag drplrivayi qagatlwdhg irpvglfgsq hdgaapdpak
       61 ggelplaeip ylgsggalhp dtllearpdl vvavtydgeq vygleqktal elethvpvat
      121 vavgpgrsla evrerfaala gslglgeplv rareldaaed tlrqatggav rprvlalspa
      181 gpervhlarp sswpdlralt ehgvgllqpa agagmnwstv gwaeaaamdp divlmdvran
      241 aarpeqlrsd ahwraiears qllpwnpeap csrrahtrff alvadtvrea agta
//
LOCUS       WP_457692207             643 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457692207
VERSION     WP_457692207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..643
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69177
     Region          82..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msqffrpkrm mvgrpldsar lgetllpkrl alpifcsdpl ssvayateei llvvglggia
       61 llqltwyaaa aivlvlvvvv asyrqtcyay psgggayrvs aqnlgrnaal taasallvdy
      121 vltvavsvvs gvaaitsaip slgghdvals vgfvallvlm nlrgvresgr vfavptygfv
      181 ffiylmfvfa avrmatgadi raesadlplh avspytglal vllgmrafas gctaltgvea
      241 isngvpafrr pksrnaattl lvmgffsvtm fggitvlaml ydvhvavqpt elglppdtpt
      301 stalaqiara tfgdldtlfy llqaftagvl ilaantafng fpmlasilae dgfvprqlhn
      361 rgdrlvfsng ivllalaaig liilfdaelt rliqlyiigv fvsftlsqtg mvrhwrtvla
      421 apglpsrera rhrrsqaina vgavltgvvl vivlitkflh gawivviamp llflgmrgih
      481 qhyrrlarel avapgarpwe pagnhvrvlv nslhaptlka lgyaramrps slealtvave
      541 pgdvrelreq wdahdidvpl qvlsspyrdf trpvidcild vcarypggav tvvipeyivg
      601 rwweqplhnq salrlkarll ftpgvtvvnv pyrlpsgkep ret
//
LOCUS       WP_457692209             291 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692209
VERSION     WP_457692209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30973
     Region          107..279
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(112..115,165..170,203,205..206,227,233..234,257,259)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(114..115,165,169,205..207,227,257,259)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mdsdkhtntr rkflqaavvv galsaarvlf ssdggapetg pqqpaptrpp qppataagpp
       61 ppaeyagpas apgpfrlrpm agetsrsgpg aspphanvaf rlsadhreif ltfddgphpa
      121 htpeilrilr rhdtratffv igenaiefpd llraladdgh avanhtwshp qlttlppgav
      181 rselgrtsdl iedilgtapd larapygdwd dpslsicnal gmspvgwavd sqdwtapgae
      241 tiaytvldem hpgaivlshd gggersqtve aldwylprll degyrpvrie p
//
LOCUS       WP_457692213             214 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692213
VERSION     WP_457692213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23004
     Region          6..121
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msfdhndhyh rlllrhlprd crtaldvgcg tgrfarrlag lgldvhavdp saevlaqara
       61 aageaadggg pprfehadit rlelpdghyg fisclaslhh mpfdtvtalr kalapggvlv
      121 vlgcyqersp adwiwglaaa pvnavirlav gaserlrtrp agtaplkppv appgmplpri
      181 rreaaallpg crirrllfwr yllvfrkeas ptga
//
LOCUS       WP_457692211             245 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692211
VERSION     WP_457692211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142575
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25195
     Region          5..239
                     /region_name="SDR_c"
                     /note="classical (c) SDRs; cd05233"
                     /db_xref="CDD:212491"
     Site            order(9,11..14,33..35,57..59,85..87,112,140..142,155,159,
                     185..188,190..191)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212491"
     Site            order(113,142,155,159)
                     /site_type="active"
                     /db_xref="CDD:212491"
ORIGIN      
        1 msravlvtga srgigravae ifaahgdrva lhyasrrasa eaafaglags ghvlvqgdvs
       61 tpegaaalvd aavdglggvd vlvnnaaanv ahpldrtsfd dwqnawrqvv dvnllgaahv
      121 sycaarnmie revegrivni gsrgafrgep dhpaygaska alhamgqsla vhlapygigv
      181 asvapgfvat ervadrlted vqqqspfgrv aaprdvasav hylaspealw ssgtvldvng
      241 asylr
//
LOCUS       WP_457692215             773 aa            linear   BCT 27-JAN-2026
DEFINITION  MMPL family transporter [Streptomyces nigrescens].
ACCESSION   WP_457692215
VERSION     WP_457692215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..773
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=80522
     Region          59..739
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mslprnpsva aapgasgdrg vlrrtgewca rhfvvvlvlw lvalaglqvl qrayggeysd
       61 dfalpgvqst qgrevlqehe pkaggyssqv vlhdtaeplt dfrseidrav salgklpdvl
      121 taqnplpspg appakpppgt pnvgplstdg rtayitvrfs vqpstlkpdy lhgvdaavrp
      181 lrsagvevey ggplgelarp epddrtsevi gfgvailvll agfgsvlaag vplltaliga
      241 icglaglgli aavfvfatvs ptlatmiglg vgidyalfli trhrqnlmdg adpvtaagra
      301 vatsgravlv sgctvivalm glwvsgvsfi gklgvaaait vvsavlgalt lvpallgltg
      361 rridrlrvrr piaetdagpg eaaqgswhry aqrverrpww ylaggvlvvv vlaipvfsiq
      421 lghigdgadp ksftdrrafd lmssafgpgs ngpltlvide savpqadrpm latqarkvlt
      481 dvpgaafitp lkatpdgavl tgtaysaqap qsadttglvn rlkhdllpea vrgtdargyv
      541 tgttagqvdf ldivagrlpl iiavvvalaf viilavfrgv lvavkaavln vlsiaasygv
      601 vvavfqwgwg gpalgvsgtv piesyvpmmm faivfglsmd yeifllsrvh eawlrtgdsk
      661 asvahaleit arvitcaali mvsvfaafii sdnivvkmlg lglamsvlid atvvrlllvp
      721 avmtllgpaa wwtprwldri lphvrtesee qlpargpprg daprsgarpg gga
//
LOCUS       WP_457692219             372 aa            linear   BCT 27-JAN-2026
DEFINITION  glutathione S-transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692219
VERSION     WP_457692219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41161
     Region          32..331
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mphpdagnng gptdgtsdaa tdgnvgygrk pfkrskshfa dritadgrdg wpveagryrl
       61 vvsracpwas ravisrrllg leeslslait dpiqddrswr ftldpdgrdp vlgirflsea
      121 ydaretdypg gvsvpalvdv psgqlvtndf qqitldfate wtalhragap dlypeplree
      181 idvvmagvyr dvnngvyrag fatgqseyda ayrdlfrrld llserlrdrr ylvgdtltea
      241 dirlfttlvr fdavyhghfk cnrfkltedp vlwayakdlf qtpgfgdtvd fhhikqhyyr
      301 vhtginptgi vpdgpdlsgw ltphhreelg grpfgdgtpp gpvppaeevp psghpehllt
      361 gsdprphpgg rt
//
LOCUS       WP_457692222             442 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692222
VERSION     WP_457692222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..442
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46483
     Region          4..436
                     /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 mddyraiade laaeiaagrl rpgdrlpplr rfardrrias staarvyrel srrgltvgev
       61 grgtfvriaa paaepalaep gearvdleln fpvlpgqpal lakslghllr pealagalrp
      121 vgavgtavar qaaaahlarg dwapdprqll fagngrqava aaiaalvpag erlgveslty
      181 pvvkgiaarl gvtlvplamd ehgltpealr aapplravyv qpalhnplgi tmparrrael
      241 aetlreldlq viedaiygfl rhdlsplaal apertvvids lskrlapgls lgfltvpegt
      301 tqdcatalrt gtwtasrfal daatrwmadg taaaveeekr adaaarqria aerlagfrvr
      361 adpqayhcww elpdpwradt fvaaaarhgi avtpsgafai gpahapnavr lalasppldv
      421 laealdvlag laqgapedtg ae
//
LOCUS       WP_457692226             405 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692226
VERSION     WP_457692226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42771
     Region          21..381
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maageevlvv gagvvgasva yhltrlgher vtvldsrgpd alpgstglap gfvgqlsatp
       61 elavlakdsv atyrelsaaa depafwqvgc levatteerl aqahqdvehg rglgiearvl
      121 daaeavalap alvdaeqalg alhipsdgaa dpvgltrllv aaaetagarf rwrtpvqale
      181 adrgrligvr tgttgellra drvvlatgiw gpvlaagvgv rlpmvdvqhp yfftaeqpel
      241 ddtpidmpiv rypdhavytr rhgrryglgs yahrplpwep attrdsaevp freadfgsal
      301 aeasrlvpaf rqaapgrrln gvfaltpdel plvgpvaavp glwvaeaswv thaagvgrql
      361 aamlletggp avdpvrlapg rfdhwsdrkv hetalghyrg iydah
//
LOCUS       WP_457692234             288 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692234
VERSION     WP_457692234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31518
     Region          61..261
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mttalydvpg prtrqrhrly glggtvvila liawiiyllf asgqfvaakw tpftytgiqe
       61 lllrglgntl kafvlaavls lalgavlatg rlseyrivrw vctllveffr ampvlvmiff
      121 iyvalkvepl palvagltly ngsvlaevfr sgvhsvdrgq reaayalgmr ktqvmthvlv
      181 pqavramlpa iisqlvvalk dtslgflity eeflhagkli asnldydlpf ipvvmiispi
      241 yigmcmllsw lanwvskrqk rnpkveavev aapepgtllp ggrpkppa
//
LOCUS       WP_457692236             214 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692236
VERSION     WP_457692236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22746
     Region          1..214
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mnvlldnlsl ygegllgtve ltvyasllal vlgflmaafr vapvgslrsf gtawvtvlrn
       61 tpltllffav vlglprfglv lpfklfaila lgcytsafic eavrsgintv pvgqgeaars
      121 lgmtfpqtlg divlpqafrs vippigstli alaknsaiag afsvvellgv ykplnemgys
      181 iiwtfvwiav gyllvtltis aifnvlekrf gvar
//
LOCUS       WP_457692240             247 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692240
VERSION     WP_457692240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27058
     Region          6..244
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 magdalielr gvnkhygklh vlrdidltvg rgevvvvigp sgsgkstlcr ainrletves
       61 gsikldgrpl peegralaql raevgmvfqs fnlfahktvl anvmlapikv rkkkkdeaar
      121 qarelldrvg lasqadkypa qlsggqqqrv aiaralamdp kallfdepts aldpeminev
      181 levmrqlard gmtmvvvthe mgfarsaanr vvfmddgciv edrtpeefft aprserakdf
      241 lskilkh
//
LOCUS       WP_457692244             605 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692244
VERSION     WP_457692244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=62125
     Region          392..599
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(399,440,486,579,582)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(399,579,582)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(399,440,486)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mrvrrwgpal tllltatalp atgprtataa pagpaqpshr plplarhfdn ravsdnsapg
       61 aadfdgagrs lsaqdlaaag wspgsvltld gtrlglprta pgapdnvvad gqavavrgrg
      121 ealtflvagt ggtasgtgtv ryrdgsrssy eltapdwrsg plstkavalp hlntpggpsd
      181 eparlyavtv plragrevas vvlptadgaa galhvfavav rdtgrrtgsw aastagyrav
      241 gpwtdrtlrl vvhsgaggpr arirlantfa atpvdigaas iavrgagaaa dggpvpltfg
      301 rghtgtriaa gaeafsdpvd ftvpagtdll vsihlpgtvt aapvhqeaaq lsylsaagsg
      361 drtadtggaa ypetlavwpf ltgveveggp gsivalgdsi tdgvkstsgt nrrwpdvlar
      421 rfqgqhalpr ygvlnhgisa nrivtdrypg dgvstdtggv saqhrlerdv laqpsartvv
      481 vfegindvrw gtsseeviag lralarrahe rglrvvvati apcegyrdct pdvearrqav
      541 nafvranaga vfdatldfda virdpqrpqr mlpaydsgdh lhpgdaglka lgdsvdlral
      601 vpgrs
//
LOCUS       WP_457692248             213 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692248
VERSION     WP_457692248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22843
     Region          1..177
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 meltkkthac vrlekdgrsl vidpgvfsea daavgadail vthehvdhfn eerlragmea
       61 npaaeiwtla svaeqlsaaf pgrvhtvgeg dtftaagfev evhgqlhavi hpdipritnv
      121 gylidggavf hpgdaltvpe grsvetlllp vhapwnkvae iidyvrevap qraidihdsl
      181 lqdharpiyd smidklggtd hgrlvpgtrt alg
//
LOCUS       WP_457692294             211 aa            linear   BCT 27-JAN-2026
DEFINITION  SMI1/KNR4 family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457692294
VERSION     WP_457692294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Brantl,S. and Muller,P.
  TITLE     ToxinAntitoxin Systems in Bacillus subtilis
  JOURNAL   Toxins (Basel) 11 (5) (2019)
   PUBMED   31075979
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Hong,Z., Mann,P., Brown,N.H., Tran,L.E., Shaw,K.J., Hare,R.S. and
            DiDomenico,B.
  TITLE     Cloning and characterization of KNR4, a yeast gene involved in
            (1,3)-beta-glucan synthesis
  JOURNAL   Mol Cell Biol 14 (2), 1017-1025 (1994)
   PUBMED   8289782
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 4183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..211
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=23227
     Region          29..130
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); cl01747"
                     /db_xref="CDD:445532"
ORIGIN      
        1 msvesslkpl lslvsnehga deqvdwvgaq ealgvglpsd ykafmsvyga gnigdlgvlg
       61 plpvdylqwd pgsivdsvpt frelwdsegg vpgieadgss vlpwgsgcna nelgwltldp
      121 npdkwpvvaw rlqirygdsr wklfdcrmvd flvkmmraef decplgdasl wgrsapfvhw
      181 reaqrrwlag ldpesgepdp lvqeflqwpa p
//
LOCUS       WP_457692285             568 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692285
VERSION     WP_457692285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..568
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=61989
     Region          275..564
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtttsgtagr sprtswgreh lanlyslfvl smimndapde sdvltralta vgtlgpcrae
       61 aayltldnrl trtpadwpha tahldaqvqr lggqdgpvtv pdrewgwsla lhstadaigh
      121 lvvsapsqpt ddeyfllrvl aqqtaaaltq atarrterdr eqqlrqlsed raatnarltt
      181 svselehqrs vhemlsdasa nddgvqgiag alhrltgypv aiedrfgnlw awagpgrpdp
      241 ypkpaatphe ellqdaarrl rsvrvaervi alawhrgevl gtvalidpev rtgeqeefal
      301 dhactvlale lahlrnlaev elrlrrelvd dlitgtddes ayaraaavgh dlhgphylaa
      361 vqwvgrpadd tfvqavgrsa aglrmrslla rrsgmavlvl qgrprataly eavgrelgsp
      421 tgsigvggrc dtpgeiprsf qealralevr qrsqsphgtt tfdelglyri lgpggsyrdv
      481 eqfvrewlgl lldydaahhs dlvrtlsqyf ecggnydgta aalaihrstl ryrlqrirev
      541 sgsdladids rlnlhvatrv wkvlggss
//
LOCUS       WP_457692256            1483 aa            linear   BCT 27-JAN-2026
DEFINITION  discoidin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692256
VERSION     WP_457692256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1483)
  AUTHORS   Shinya,S., Nishimura,S., Kitaoku,Y., Numata,T., Kimoto,H.,
            Kusaoke,H., Ohnuma,T. and Fukamizo,T.
  TITLE     Mechanism of chitosan recognition by CBM32 carbohydrate-binding
            modules from a Paenibacillus sp. IK-5 chitosanase/glucanase
  JOURNAL   Biochem J 473 (8), 1085-1095 (2016)
   PUBMED   26936968
REFERENCE   2  (residues 1 to 1483)
  AUTHORS   Kiedzierska,A., Smietana,K., Czepczynska,H. and Otlewski,J.
  TITLE     Structural similarities and functional diversity of eukaryotic
            discoidin-like domains
  JOURNAL   Biochim Biophys Acta 1774 (9), 1069-1078 (2007)
   PUBMED   17702679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1483
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1483
                     /product="discoidin domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=160429
     Region          268..375
                     /region_name="F5_F8_type_C"
                     /note="F5/8 type C domain; pfam00754"
                     /db_xref="CDD:459925"
     Region          1287..1397
                     /region_name="F5_F8_type_C"
                     /note="F5/8 type C domain; pfam00754"
                     /db_xref="CDD:459925"
ORIGIN      
        1 mnatgtteli vpvevhallv ndkvrsqpvh rykpsfdgml gtiegtgrga aepepfsggn
       61 vqmdegvhiq wqlpealteg vvdeatgqtt yplvpnrwlv vryaqvrgaa kpargwvvhs
      121 dylysddpdg wdgrtainsf lnprartpev dwlgnihslt dgpwrepegr elfltavgag
      181 lpsfaayqpy henvfsmhdd ledlkdrseg dsyppdatls ylvvgwysda tkdileqaar
      241 ipgllppdse gtraevihal gwtmagrsat ttlgttepha ldhvldrrpd tyylsaqppv
      301 dssritidlg seqqisairv hagdldgghl lpavrlrtsl dnadwpeahh qdfpaaspvi
      361 eyvpaapfaa ryvqlctlea geeqvavrdf eitaapagel rtvysgtalg lewqrgqape
      421 dpdrpvngaq lkialghstg eaaaalvgrq arssrtaqlf salyhgtldt fdgadgdldl
      481 eeithsswfs grdggsswqi vprpaqdpdd qptrrgaglt pawlttlnsd qsrydaalrq
      541 ltasqwrvws lywlnevlan lpahlrpdda pddfeatcaw qlnpandgaa kavqtqlael
      601 dalrselppp gddqdaidtw atgkglsehl rlkrlpkggf hkpadpvlli egtgggtvpl
      661 trdsdnplpc rlpatllkav kldgvmtpvp enpddpgipa lpasattllk efalleraar
      721 tgapgstalh dllenprana qgmpaeftgp wrqpwlpmfl mwqlnffptp yrtdegchwt
      781 frapeedtgl nsygyrwngt gtlpadsese gnvlhrlfrg rsylapttvy varaqlarym
      841 atypdadtrs laalreelek ldilsqtldg fndwllqldg gaqvptegaa arltgdqnhv
      901 pdgagpgqrr fqpvragqff ftdlrvldrf grtldlvtsg ddgnsydqyp vpgptvtpsk
      961 dlytepelin perffqlppr ilqdtrlaft pvpaapaavg hgspvagwll vnhldqtlgv
     1021 ygptgqalge vrvittvdgt kaadynplph spylrlddqr feddhpqlhg fltaltgres
     1081 sadafkalla tidtslgttv dpapeddhlp vrligrpval iradldfele gppltdpswa
     1141 tvldpppady pedtwairlg dpykladgli gyysaepnqa vdydllhahq pagnsagyig
     1201 pvsgedlalp arasgrftrh vtllahphlp vhattdvlpv hslrldadqv hqalaavras
     1261 frlnpllatt rsmrtaatti pgghgnstpe agpvglildg kpdtwyesgs aprngdtvtv
     1321 dlgtvqpvtg vqvllgepgg aripsvrqlk tstdgeewtd ltadtatpge lhwpadgtvp
     1381 ppltarfvrv dleasqgtvv frglqvtpdv dalvipplsv rygtwswaqp dategdaagw
     1441 deralipadh lthpddpnpt aragylqlhp atpgsgpept pqp
//
LOCUS       WP_457692259             446 aa            linear   BCT 27-JAN-2026
DEFINITION  discoidin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692259
VERSION     WP_457692259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Shinya,S., Nishimura,S., Kitaoku,Y., Numata,T., Kimoto,H.,
            Kusaoke,H., Ohnuma,T. and Fukamizo,T.
  TITLE     Mechanism of chitosan recognition by CBM32 carbohydrate-binding
            modules from a Paenibacillus sp. IK-5 chitosanase/glucanase
  JOURNAL   Biochem J 473 (8), 1085-1095 (2016)
   PUBMED   26936968
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Kiedzierska,A., Smietana,K., Czepczynska,H. and Otlewski,J.
  TITLE     Structural similarities and functional diversity of eukaryotic
            discoidin-like domains
  JOURNAL   Biochim Biophys Acta 1774 (9), 1069-1078 (2007)
   PUBMED   17702679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..446
                     /product="discoidin domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47621
     Region          173..286
                     /region_name="F5_F8_type_C"
                     /note="F5/8 type C domain; pfam00754"
                     /db_xref="CDD:459925"
ORIGIN      
        1 myltatqags llqavgesvp vqfsistate tkkgtlfltf rkpgsgpdvr craltvtlpv
       61 gpkatdlvaa tdaanaddid dyprdsagve wtierktnpp eptspsevta liftctpetp
      121 sadttfgagr eftlilssip ingtvgaarl tltettatgt vevpartfst tmtanpsypl
      181 snlagdgsse frtqgtpain stltldlgsv qpvtgyyllt gttgggnrsg tpvlessttg
      241 atnswqrrtf kssqsvnnht lttpvdaryl rlrlsttptg ffgmrhfsvs ttatwadrpi
      301 alppvekagn efyfrrfscq kprvahgtat vlqwegtprn teyylswddh apkklnppqv
      361 sglhtepthe lthtttfvln aqtknaanet vhhylsttvt vngpditakt ldvtdklevd
      421 atfaangrtk kttantttfd gsvtln
//
LOCUS       WP_457692303             215 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692303
VERSION     WP_457692303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22564
     Region          7..201
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 maahsptvgf dldmtlidsr pgikavyqel sartgtfida dlaasrlgpp leheirhwfp
       61 eervaetaal frelypqyav aatpampgar eaiaaihaag grvivvtaky epnaklhleh
      121 lgldvdalfg slwaagkaea lrkhyaqvyv gdhigdvvga htagalsvav atgpcdatel
      181 rnagaevvla dltefpswle ryvaegvdgg dgaat
//
LOCUS       WP_457692319             384 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692319
VERSION     WP_457692319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41242
     Region          67..360
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtengrlpvv lvgglhsear eqvvlrllht vrgsvalhhd lstaaegtvr rtvrdasgel
       61 ssgeaplvnd caccalredl vpelqrlads glhrlavvel wdsvepkama eviaahgget
      121 ltlshvitav dpalvlpyla ngddlaeagf aaaatdqrti gdtwarqley apvlvlvdsp
      181 eaddedrall aqlhptarhv pvtsrqlaev afagfdveaa aaaqhpacal lpqeadesgv
      241 atlvwhrrrp fhperlyqal edlacaaars rgrfwladrp dtllswdaag galcvenagp
      301 wlaslpdaaw dmvpamrraa aaldwhpehg dccqhlvfta pgldrdgler lldscllted
      361 efaagreawk rlpasfdtll dpvs
//
LOCUS       WP_457692350             241 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692350
VERSION     WP_457692350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25539
     Region          4..234
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mttvttrtve ypadgltmig hlalpagvdr rpavlvgpeg tglsdverrr adalaelgyi
       61 alafdlhggr ylgdpeemla rcmpllanpd rmrgighaal dvlraeprtd pgriaaigyg
      121 tggaiglelg rdgvnlraig tvnalttgrp geaarircpv wagvgsedpi mppaqwdaft
      181 aemqaagvdw rlvvyggalh afhhppvdht vrpgvgyhpr haqrawcdvv dllaeclpvt
      241 e
//
LOCUS       WP_457692353             243 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692353
VERSION     WP_457692353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25066
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkiaviggtg ligsqvvkkl naagheavph sqstgvdvit gqgveeavag adgvvnltns
       61 ptfddaspaf fqtsmdnlla aahkggvghf vilsivgadq vpdlayyrak vlqedilkag
      121 pipysivhat qfmefigavm swttegdtvr lpttplqpia aqdvsdtvae vaagtplngt
      181 ldvggpdvhp ldelgritln arpdgrtvvt ddtagmfaav dgdvlttkgd ariapthytd
      241 wlt
//
LOCUS       WP_457692366             153 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457692366
VERSION     WP_457692366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15204
     Region          24..141
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 magsgqtstg fdlaaaqqal aaqpfsslvq aritefggga atleidiree llqqhgfvhg
       61 gvlsyaadnt ltfaaatalg paivtggfsi qyvrpalgrt lrasaqvvqa grrqavcrce
      121 ltvldaegae svcavaqgta mplsgpaggg geg
//
LOCUS       WP_457692360             356 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692360
VERSION     WP_457692360.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..356
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37454
     Region          26..353
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mshpdapplq pagpfesggd erllhrslar rlmgrpelgs vvgaaavfvf fsvvaepflr
       61 asslstvlya sstigimavp vallmiggef dlsagvmvvs salissmfsy qmtantwvgv
      121 gvsllvtlai gafngtlltr tklpsfiitl gtffmltgln lgftklisgt vstktiadme
      181 gfesartlfa shltlgsvdi qvtilwwlal vavatwillr trvgnwifav ggnadaarav
      241 gvpvtktkig lymgvafaaw vsgqhllfsy daiqsgdgvg neflyiiaaa vggclmtggf
      301 gsaigaavga fifgmaskgi vyaqwnpdwy kfflgamlll atllnawvrk raeeka
//
LOCUS       WP_457692369             219 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional 4-hydroxy-2-oxoglutarate
            aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Streptomyces
            nigrescens].
ACCESSION   WP_457692369
VERSION     WP_457692369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Fullerton,S.W., Griffiths,J.S., Merkel,A.B., Cheriyan,M.,
            Wymer,N.J., Hutchins,M.J., Fierke,C.A., Toone,E.J. and
            Naismith,J.H.
  TITLE     Mechanism of the Class I KDPG aldolase
  JOURNAL   Bioorg Med Chem 14 (9), 3002-3010 (2006)
   PUBMED   16403639
REFERENCE   2  (residues 1 to 219)
  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   3  (residues 1 to 219)
  AUTHORS   Gefflaut,T., Blonski,C., Perie,J. and Willson,M.
  TITLE     Class I aldolases: substrate specificity, mechanism, inhibitors and
            structural aspects
  JOURNAL   Prog Biophys Mol Biol 63 (3), 301-340 (1995)
   PUBMED   8599032
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Conway,T.
  TITLE     The Entner-Doudoroff pathway: history, physiology and molecular
            biology
  JOURNAL   FEMS Microbiol Rev 9 (1), 1-27 (1992)
   PUBMED   1389313
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="bifunctional 4-hydroxy-2-oxoglutarate
                     aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase"
                     /EC_number="4.1.2.14"
                     /EC_number="4.1.3.16"
                     /GO_function="GO:0008675 -
                     2-dehydro-3-deoxy-phosphogluconate aldolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008700 - (R,S)-4-hydroxy-2-oxoglutarate
                     aldolase activity [Evidence IEA]"
                     /calculated_mol_wt=22816
     Region          3..206
                     /region_name="Eda"
                     /note="2-keto-3-deoxy-6-phosphogluconate aldolase
                     [Carbohydrate transport and metabolism]; COG0800"
                     /db_xref="CDD:440563"
ORIGIN      
        1 myrweitraa laqrvfaivr srtydeasat adtllsagit sleislttpf aleavttltr
       61 elgddaviga gtvldavsar mavdagarfl vspsldaevi rtghrygvpv fpgvstptem
      121 vrglelgada lklfpasahd pswltevraa lpqvpllptg gvtvdsapew iaagavavgm
      181 gaalsdgdrd tvgkraadll trleeaapdr pmirgtsdf
//
LOCUS       WP_457692373             208 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692373
VERSION     WP_457692373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14302692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /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=22299
     Region          18..87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          101..188
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(104,117,119,130,133,137,171,173,185)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mtelpdeptg gppdelstva prlrdlrrrs gltletaarl vglspahlsr letnqrqpsl
       61 pmllalarty gttvsellge taperdpivr agraeaseag gwtywtvgga gramqalrvr
      121 vpqraqgdlv rvhpgeewly vlkgrlrltl gaavqvlepg daahfdsltp hriaaaspgg
      181 vellfvhtll qsgaaelclv ddtrrrgl
//
LOCUS       WP_457692388             628 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457692388
VERSION     WP_457692388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..628
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=64427
     Region          24..271
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(24,47..48,77,82,87..90,102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(31..32,34..37,39,51,53,85,101..104,108,110,147,149,
                     151..152,154,163..164,167,184..187)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(31..32,34..37,39,51,53,85,101..104,108,149,151..152,
                     154,163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(35,108,110,147,149,151,167,184..187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(163..171,180..187)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mvnsaggtgi fqplegddpr aiagyrltar lgsggmgkvy lsytpggrpv aikvirpefs
       61 edaefrrrfk qevqsaqrvq glftapvids daegpspwla tayvpgpsla aavaghgklp
      121 vptvlllvag iaealqvihg agivhrdlkp snvllaadgp rvidfgiara adatsltssg
      181 vtvgtptfma peqaagstis patdvfalgq vaayaaigtp afgegtshgv lyrivheepd
      241 ltglpdelre lvtrclskea sdrpsvaevi alcgaasgqt qlrrpeewlp tavaadittr
      301 aaapapaqtp pppleaptaa apaqppnppa pspvqptqpp apptapvapv ptelshpqtp
      361 ppgfgpaafa ptvagtgapm atgptaavpt atvttatgpa vpgptaavpa pqppkkkrkg
      421 livslvlvcl lafagaggal vytvmkgdgq kkgnqatgds ktghkdssst ptgdptaspg
      481 dggsaapdap vkdptpvdyk tinlpddyhi slsdepvhpt dsdndtdidf sytdnsytdd
      541 evdtetgklv llnagqegtl atcraetrft dsiltkrlsk gaqmclttky ghvalitfkg
      601 yapktdpssy mtvdvrvwrn avepeqes
//
LOCUS       WP_457692393             307 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692393
VERSION     WP_457692393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32905
     Region          26..286
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mddrpgdhga ppaaggdaga gqelgmtvae rlrrvqgsls paelkiaral mahypaagle
       61 stsglagrag vspptvvrfv arlgfegyrq fqqslrdevq arraspltlr pvvsesspts
      121 dlveaaeevg rgalshtfaa lpeqefdrav elicdpakri vsfggrfsrl laeyldlhlr
      181 llrpgtqvhi papggdggfr vdlgrrevcv vfdfrryqrd tvelarfahe rgarvvlftd
      241 pwlspvaefa dvvlpvrvea pspfdsivap vavvetlvaa vhvrlgtaaa ermraaeeas
      301 gddrtma
//
LOCUS       WP_457692395             482 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457692395
VERSION     WP_457692395.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49560
     Region          1..452
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msnpprtrkl rlwealtlsv glmgptlamg lngagvattv gkavplvfll gllgvglvay
       61 gfwrltqhfn qagsvyalag atigpragff ggfallgtyl aflvctlaat gvfaqaflha
      121 lgirstgpwv avaflaalgv talnsrdgrt tartlliveg igilamlvla avimgrattg
      181 saprhqsldl svftaggtty savmtatvfa flswagfeac aslgeetdnp krnipralag
      241 svlltgclyv lmmfaqtigf gtdaqgisef gaaesalstl sgqyigtwfa lviaftavas
      301 afaaalsssa aaarmvqala rdgfgprala rthpvtgapt talrmcgava aaltavmygt
      361 gaaafdtyyw yatigvlcvl vvyavagvgv ivftlsgrgr ipryelvvpv aglgylgfvf
      421 lqqstgqsap ytyfpwiaaa wclagvavvl aapsltrrig arltsalvad ahptdpnrkv
      481 ps
//
LOCUS       WP_457692401             391 aa            linear   BCT 27-JAN-2026
DEFINITION  M20 metallopeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692401
VERSION     WP_457692401.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40545
     Region          9..367
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mslddtltal aaqlereldd avelrhqlha rpclsgdeaa arelvlaalp grhaaaevag
       61 tgavvrvggs gpaiavrgel dalavheetg vpwasqhpgv mhacghdvhl aalvalarav
      121 draggpapll avlqpreety psgaqdvted gilereqcra tigahvqpll aagtvactpg
      181 gvnasadeft vtvrgrggha ayphltrdpv vtlahvvval qslvsrgidp mssvvlsvtt
      241 laagtaanvv pgsaeargtl ramrtadrev iherlvetae lvaqaygcta dvritrgepv
      301 ldndatltaa trpllaslgl kvaadlrsag addfsyfser mpalmlfvgt hggteqlhsp
      361 tflppdervr dvahallagy laaaeqfipr h
//
LOCUS       WP_457692409             184 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692409
VERSION     WP_457692409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20162
     Region          1..184
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 marrreqvld agiqvlgseg arrltyqavd aaagvpsgtt snyfrnraal idgivdhlqa
       61 lerrdwenfa aaaapadage ladavtrflr yatgperart aarfalylea tarpelrptl
      121 trgretvvgw gaewlqrfds paphrhceil fdymdgvafh qlafpaedfd pgpgirellr
      181 gllg
//
LOCUS       WP_457692422             239 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692422
VERSION     WP_457692422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..239
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25866
     Region          4..235
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mdrsspvply fqlsqqleaa iehgrlapgs llgneielag rlglsrptvr qaiqslvdkg
       61 llvrrrgigt qvvhsqvkrp lelsslyddl eaagqkpatr vllntttead aevaaalgia
      121 egaevalver lrlahgepva hlrnhlpagl ieletaeleq tglyrlmrsa gitlhsarqa
      181 vgaraatvee gerldepega plltmqrttf ddtgravefg shvyrasrya fefqllvrp
//
LOCUS       WP_457692426             192 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692426
VERSION     WP_457692426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  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 10005267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="nucleotidyltransferase family protein"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19861
     Region          18..191
                     /region_name="MocA"
                     /note="CTP:molybdopterin cytidylyltransferase MocA
                     [Coenzyme transport and metabolism]; COG2068"
                     /db_xref="CDD:441671"
ORIGIN      
        1 maglllaagg grrlggrpka lldhrgrplv ehaaralrdg gchpvhivlg aaaaavrera
       61 elaaygisen pdwaqgmgss lrvglaalae sgadavvvsl vdqpgigaaa varvvaayeg
      121 raslvsaayd grrghpvlfg vdrwpdiaes aegdrgargy lqryadaltl vecsdiaepy
      181 didtpedlhr le
//
LOCUS       WP_457692428             483 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleobase:cation symporter-2 family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692428
VERSION     WP_457692428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..483
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49034
     Region          27..437
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mtgqksegdr khpvdetlpp lkmftsglqh vaamyagvva ppmivgpacg lsatetaflm
       61 gaslftagia tllqtlgfwk vgaklpfvng vsfagvtpmv aigkaqspgn alpiifgavi
      121 vagvlgflva pyfsklvrff ppvvtgtvit ligvsllpva fnwsqggngr apdygsltni
      181 gmaaltfliv lvlrrvlrgf lqqiaillgl iagtliaipv gitnfsaise asligfptpf
      241 hfgapqfdia aivsmcivml vcmtestadm lalgrivgrp adertieggl radtlgtals
      301 plfngfansa faqniglvam tkvrsrfvva tgglilivlg lcpvaasvis lvplpvlgga
      361 givlfgsvaa sgiqtlasaa mekgdnaliv aaavgiglip iaapdfyhhl pkdllvvlds
      421 gistgclvai vlnlafnhfg rkpadgdtad dpataahggp eappppapgt tdeagepaaa
      481 pah
//
LOCUS       WP_457692434             367 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692434
VERSION     WP_457692434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=38845
     Region          22..357
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mqtelsntlg aehavfgftp fpavaaaitr aggfgvlgav rytapdelar dldwmqehtd
       61 glpygldvvm pakkvagvse aeveamipeg hrrfvaelle khqvprlaeg easgwritgw
      121 meevartqld vafdypikll analgsppad vierahehgi lvaalagspr halhhkaagi
      181 divvaqgyea gghtgeiatm vltpevvaav dplpvlaagg igtgeqiaag lalgaqgvwl
      241 gslwltteea qlhsrrltak llaagpgdtv rsraltgkpa rqlrtawtda wddpsgpgpl
      301 pmplqgllva eansriqrhe vepllgtpvg qivgrmnser svqavfdelt rgferaidri
      361 nriagrv
//
LOCUS       WP_457692436             521 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692436
VERSION     WP_457692436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..521
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54967
     Region          5..465
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mpertsydav ivggghnglv aaaylaragr svlvlerldh tggaavstra fagvdarlsr
       61 ysylvsllpp kivqdlglrf avrkrtvssy tpavrdgrpt gllvgggear trtafaeltg
      121 sdreftawqg fygrtrrlae rvfptltepl ptraalragv dddalwhalf erplgevvee
      181 tftddlvrgv vltdaligtf agahdpslrq nrcflyhvig ggtgdwdvpi ggmgaltdal
      241 adaarqagae ivtdcavtgi atdghsaevt cdqgtvgarr vlvnaaprel arllgeappp
      301 paegaqlkvn mlltrlprlr dtrvdpreaf sgtfhiaegy rqledayqqa asgglpvspp
      361 seiychsltd psilgadlvr qgyqtltlfg lhaparlfta dndatrdrll aatlaeldth
      421 laeplagcla hdadgrpcie arspldldre lglpggnifh rdlafpyaep aedaaegtap
      481 arwgvatsqp nvllcgagav rgggvsgipg hnaamavlee g
//
LOCUS       WP_457692438             435 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 27 protein [Streptomyces nigrescens].
ACCESSION   WP_457692438
VERSION     WP_457692438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Naumov,D.G.
  TITLE     [Phylogenetic analysis of alpha-galactosidases of the GH27 family]
  JOURNAL   Mol Biol (Mosk) 38 (3), 463-476 (2004)
   PUBMED   15285616
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14423446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="glycoside hydrolase family 27 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47117
     Region          59..344
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(66,101..102,143,177,179,218,246,250)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          356..432
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
ORIGIN      
        1 mphpsvprig rtfagltava acsagllaap apasatpdpa rapgaprpgg typnlaprpp
       61 mgwnnwsyym cdldekivld naralvrtgl arkgyrtvtv ddcwmsrqrd angrlvadrk
      121 kfphgmghlg rqlhrmglkf giyadvgtlt cekfpgslgh fqqdaeqfar wkvdyvkadg
      181 cnvpvtpghs keatyrdlyr qmsralratg rpmtfsvsap ayfqfdgdsi whrvigwsae
      241 vgnlwrtgrd valetstpaa kwssivynfr ynsglaglqr pgrwndpdfl lagaagltrh
      301 emqsqmslwa mmaaplisst dlgklsptar kvlgnqqvia vdqdplglqg rvvaqdngss
      361 vlskplengd ravalfnsgg tprtlsvsar aaglaksgsy rlhnlvtgrr ahsegnivar
      421 evpphstvly rvtps
//
LOCUS       WP_457692440             305 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces nigrescens].
ACCESSION   WP_457692440
VERSION     WP_457692440.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10007665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33265
     Region          2..282
                     /region_name="COG3662"
                     /note="Uncharacterized conserved protein, DUF2236 family
                     [Function unknown]"
                     /db_xref="CDD:442879"
ORIGIN      
        1 magdpglfgp rsvtwqmhad pmmwiagvra lylqalhpra vrgvhqnsaa frmskqgsrd
       61 awgrlmrtah fvgtltygtt eaaeqagaav rgihrrlsat dpatgerygv depdlllwvh
      121 caevdsylhv lrrsgypvgd dradayldeq resarlvgld pagvpgsraa laayfarvrp
      181 elaltpeage vdgflrrppt paalvparal lwrqvaqlay galpayahql ygrpapppaa
      241 vtrrlratgr llraippsvr wrlpprhilr averlgpdtr papyklrrsa aildgqegtq
      301 gelrg
//
LOCUS       WP_457692448             381 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692448
VERSION     WP_457692448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40379
     Region          3..376
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mhpttpriai igagpggltc arvlqrsgvp vtvfahessv avdpqggtle lqmttgrtal
       61 raaglyeeft avarpageev rlldhtatvl lqdapapggp draevdragl rrlllaslpa
      121 gtvhwdrylr tlhpvgdgrh kaefddghte tfdlvigadg awsrvrpmlc ddtphysgvt
      181 fvetaiedad srhpdlarlv gngsmlalsa nkgliarrhs hghllvyagf rgsqdwalea
      241 gvkmtdteav ravlldgfag wddrllallr dndrgfvnrp lfalpvphpw phtpgltllg
      301 daahlmtpfa gggaglamld gcelaralve dgdpdaavra yesamlpraa raaehaaral
      361 ahafapdapr salrflsagr p
//
LOCUS       WP_457692450             336 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692450
VERSION     WP_457692450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34291
     Region          31..318
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mpdprpaanv lrrlplfvag lcaltvcaal slalgarsvp latvwdaltg aahgpdalvv
       61 mglrvprtvv alvvgaalgv agavvqgitr nplaspttlg inagasfavv taiyalhltr
      121 pvqylwfafa gaaaaalfaq alarragdld pvrlalggtv lqlvllswtw tvmlaskrsl
      181 dearfwlags laerpltvly pvlptlvigl vialaltpal nalalgddsa qalgvpvari
      241 rtvgglavvl laasavavag plafiglaap hlvrqllrts dhrvlvpgcl iagpllllta
      301 dilgrlvirp selqvgiisa flgapllall arkvar
//
LOCUS       WP_457692452             358 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692452
VERSION     WP_457692452.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=35545
     Region          24..350
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mndalrsrqp lgssslppap atgrragrgr tlllalaglv vlcalvtvsv angemplppv
       61 eaakglfgag dagtvlivqe fraprmaaai vagaglavgg allqrlfrnp laspdvmgvt
      121 ggasfgavam laagasqami plaalgggll aavllgafgw rsgtsvtrlv lvglavqagl
      181 saavsfmvvs fptelagsal qwttgslygr twtevwsagg avavglalaf alhrrlavld
      241 lgddsagtlg lnthtarlqv lviaivlasl aaaltgpvaf valavphmvr flagpptagt
      301 lalsalagav lllasdlvaq yllpvsglpv gvvtatlgap wllvlmirqs ssvnrsar
//
LOCUS       WP_457692454             337 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692454
VERSION     WP_457692454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     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   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 337)
  AUTHORS   Clarke,T.E., Tari,L.W. and Vogel,H.J.
  TITLE     Structural biology of bacterial iron uptake systems
  JOURNAL   Curr Top Med Chem 1 (1), 7-30 (2001)
   PUBMED   11895294
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   7  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35732
     Region          10..329
                     /region_name="FecB"
                     /note="ABC-type Fe3+-citrate transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4594"
                     /db_xref="CDD:443650"
ORIGIN      
        1 mftrtafpgs rrlsaallaa tvgtatltac gggtpttgde svkggtgfpr svksvlggsv
       61 kipakpkrvv vldtgelddv tmlgikpvga vsphmkndgg fpaylkgkig gvkdvgplle
      121 pnlekiamlk pdlilsskvr hekiydklna iaptvftett ggpwkanlkv hakalgleke
      181 adqrlkeyea rakalgeaik kkydgkmpsa svvrfvagpt rlyqkssysg vvlndigldr
      241 pksqsstdpv ktmldvspeq idkadadmvf vtvaddpdkt qqkdvtsnpv wkdlravkeh
      301 kvhnvsdetw msgigiqaae hvladvakat gvplpks
//
LOCUS       WP_457692456             397 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692456
VERSION     WP_457692456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=43037
     Region          52..307
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mrmyllalnp tdsvtegflp aaarlgldvt iltdqppahr dvapqtevle cdvhdfravi
       61 nriathhrad avftnsdhlq tqaalaadyf glpgkdwrta lrtknkgemr rhlavsgida
      121 vrsvelaagq dpsafaaaad lpypvvlkpr egvasedvil agdpeelvtr akeiqarrph
      181 aallaeefln gelytletig dgrvrhvlgg fhttvspppv fieerldfva appepviaqv
      241 taqldalgvg lgachteyvv hegrarliev nyrvigdqcd lllsqlldip lfehilrahl
      301 geplpadlga rrdgagrvds pladragtlt aapaatdrtv dgvrltyrpl ralgerhphy
      361 gtnrdylgll rvtgtdrsav drvadgflaa erweitp
//
LOCUS       WP_457692460             434 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692460
VERSION     WP_457692460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44544
     Region          20..370
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mrtttsrrve pavvetkdrp glarrqvhav agcyfvasfa alglppylte ilpefgdgaa
       61 rwagllyivp tifgaigapl wgrladrfgr krlllraqlg laaafllagw adsmstfvaa
      121 lvlqgilggt faasngylga alegnalsra ltlmqgsara alvfapivvg sltpwlsphr
      181 qyallavlpl taavmlaalp epprapaaaa kqaeavaetd avqtpetaag taaepagrtp
      241 vaslralyal efafvfstvi sfpylislik eripgtgpmv sgvlfalphm cylvaamavh
      301 avfrtrsrlg igigfgcial glaghglvds ltgfiavrlv lgagltlglv clsvlaadca
      361 rgrapgglfg sieffskaga vaagvaaavg ndwfgpaapv ltgtaialvt vlataapvll
      421 srlsptrrsp rclr
//
LOCUS       WP_457692466             256 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692466
VERSION     WP_457692466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Rea,D., Fulop,V., Bugg,T.D. and Roper,D.I.
  TITLE     Structure and mechanism of HpcH: a metal ion dependent class II
            aldolase from the homoprotocatechuate degradation pathway of
            Escherichia coli
  JOURNAL   J Mol Biol 373 (4), 866-876 (2007)
   PUBMED   17881002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="HpcH/HpaI aldolase family protein"
                     /EC_number="4.1.-.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27596
     Region          2..237
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mlrpnevrqk lgageevygl fstlpeptmv emigcagydf vildtehtlv dpqrlenlir
       61 aaettgltpf vrvpeadpga vlraldagam givvphvrgr adidatiraa ryapegmrsl
      121 nggrgpgfgl idpaeylrra naeimviall edaegveaid eilspggvdl vlpgpgdlsq
      181 sygvpwqvrh prvqeavrtl reacarhtvp fcamsttper raewradgvt afvvgedrdl
      241 taralrghla rtagre
//
LOCUS       WP_457692462             593 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457692462
VERSION     WP_457692462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..593
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63799
     Region          22..575
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mppltdspgt aaahaaptgl ptadqavaht llncllrevs gpehqtavdh grlllrlprr
       61 gvllrvalrr tslfgahrft gpvseqtadg waevgwrrla eyvhaelslr tgvhneefla
      121 qiasshqavs aalaarteqr paagepgagd wqtayvtseq slilghrfhp tpkartgdpt
      181 awqsyapetg aafpllllav reeliaeeaa eegaaaplda lhsevpdgyr llpvhpwqfe
      241 llrdhaglqe aldrddirvl gtggapfaat asvrtlydge aflkfslnvr itnclrknas
      301 yelsgavalt rllapaltdl atrfpgsavl repayrslal pgadgspdte llegfgvivr
      361 eglsqrllpg ttpllaaava deyptspahi srlldgsgpq aalewwaayl nlllppvlaa
      421 yfdhglvlep hlqnvlvcvd gdgmpaqvlf rdlegtklvp ehhaellasl peqiaapmty
      481 daqrgwdrvv ycllvnhvae mlaaladlhp dteaelwaqv rrtlqthadr ygcpprlaal
      541 lagvplpaka nlltrwerka dreagyvllp splaeavlsg avrvddttpw sar
//
LOCUS       WP_457692468             410 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692468
VERSION     WP_457692468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..410
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43688
     Region          21..408
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mdrntaflia gaglagakaa etlraegfdg plvllgdese rpyerpplsk gylmgtseke
       61 kvyvhpprwy adqdvelrlg qavtaldpaa hevtladgsr lgyaklllat gstprrlpvp
      121 gadldgvhyl rrladsdrlk evfrsasrvv vigagwigle ttaaaraaga evtvlesaal
      181 pllqvlgpev arifatlhtd hgvelrcgaq veeitgsggv vdgvrladgs rigaeavivg
      241 vgitpnsepa aaaglkvdng vvvderlcss hpdifaagdv anayhpvlgr hlrvehwana
      301 lhqpqtaara mlgqdvrydr lpyfftdqyd lgmeytgyag pesydrvvfr gdpearefla
      361 fwlsggrvla gmnvnvwdvt eeiralvasg qavdperlad pyvplagllp
//
LOCUS       WP_457692476             802 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoketolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692476
VERSION     WP_457692476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Suzuki,R., Katayama,T., Kim,B.J., Wakagi,T., Shoun,H., Ashida,H.,
            Yamamoto,K. and Fushinobu,S.
  TITLE     Crystal structures of phosphoketolase: thiamine
            diphosphate-dependent dehydration mechanism
  JOURNAL   J Biol Chem 285 (44), 34279-34287 (2010)
   PUBMED   20739284
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Jordan,F., Nemeria,N.S. and Sergienko,E.
  TITLE     Multiple modes of active center communication in thiamin
            diphosphate-dependent enzymes
  JOURNAL   Acc Chem Res 38 (9), 755-763 (2005)
   PUBMED   16171318
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467695
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..802
                     /product="phosphoketolase family protein"
                     /EC_number="4.1.2.-"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88364
     Region          17..802
                     /region_name="XFP"
                     /note="Phosphoketolase [Carbohydrate transport and
                     metabolism]; COG3957"
                     /db_xref="CDD:443157"
ORIGIN      
        1 mhdaetpags tgapattgpl dtaelqrlda hwraanylsv gqiylmanpl leaplrpehi
       61 kprllghwgt spglnlvhth lnrvikarel dalcvwgpgh ggpavvansw ldgtysetyp
      121 dvsrdgagma rlfrqfsfpg gvpshvapet pgsiheggel gyslthayga afdnpellva
      181 cvvgdgeaet gplaaswhat kfldpvhdga vlpvlhlngy kianptvlar ipqdeleall
      241 rgyghdpihv agddpatvhq alaaamdral driaaiqrra rtegaterpr wpmivlrtpk
      301 gwtgphevdg qpvegtwrsh qvplpgvrdn aehlrqledw lrsyrpdelf daggrprpev
      361 lasvpegsrr lgasphangg llvrdlplpp leryavevdk rgsalheptr vlggllaavm
      421 dataerrdfr vvgpdetasn rlealyeatg kawqaqtlgt dehlahdgrv mevlsehlcq
      481 gwlegylltg rhglfssyea fahivdsmvn qhikwlrtar rlpwrrpias lnylltshvw
      541 rqdhngfshq dpgfvdhiln kspevvrvyl ppdantllsv adhalrsrdy vnvivagkqp
      601 gfdwltldea rahcargaga wewagtedgs rdpdvvlaca gdvptqetla aaallrrhlp
      661 elavrvvnvv dmarllpsge hphgmpdpey dalftrdkpv vfayhgypwl ihrlcyrrag
      721 hgnlhvrgyk eegttttpfd mvvrndldry rlvmdvvdrv pglgvraval rqemadvrtr
      781 hhawirehgi dlpevadwtw ag
//
LOCUS       WP_457692490             362 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Streptomyces
            nigrescens].
ACCESSION   WP_457692490
VERSION     WP_457692490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39172
     Region          31..321
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mtrhadaaph stgrpdrhhg kdpedaktav tvfvalganl vialaklagg lfagspalls
       61 eaahsvadsl nelfllaslk rsnrapdsrh pfgygkeryf wsllaavgif vmggcfsffq
      121 giealrsdhs etrtgylvgl avlavalvae gssliralvq vrgqarqngr gmreavraad
      181 dpalrtvlae dstacfgvlv amagmglhmi tgevrweawa smiigallvf vayqlakasr
      241 gqiigeaadp alrrdlrrfl eeqpeidtvt tlltmrlgtr stliaartdl vggldseeve
      301 evlvrlksai reqwpiadqv fldvteaspk drerarrerr qldetvaagr eeyeatrqed
      361 ag
//
LOCUS       WP_457692500             501 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692500
VERSION     WP_457692500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54015
     Region          99..321
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          398..494
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 maavvallcv fggtpaatav ddpelaafyq qtlswepcgq dlqngaqsdg aspppgfrer
       61 lecarlevpr dyanptrstm qvqlirlkat gpgerlgslv inpggpgasg vnylidsgsa
      121 farpgqrydi vsfdprgtgh tepiscgskl ttgsddslaa kekrineacg rysgsllrwv
      181 gtpdvardmd vlraavhddk lnylgfsygt klgavyahef pdkvgrmvld svedptkntw
      241 qtalaqargf qralddfaad clqtadcplg tdksraqeql rtwyrqlser pmkvkgetve
      301 ettyvyalre alysrsdwpa lrqalaqlrr gdaagilrls esgggsatrt vpappvgqde
      361 lppqdqlalr aiacrdtser ydaddyprae reltkasplf gpdiaplmld cydwpvagdd
      421 ssrdvaapda pplllvattn dpatpyegaf nmarelgnss vvltfhgegh aayttqdpcv
      481 qryvdnflln gvlptartsc g
//
LOCUS       WP_457692508             322 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457692508
VERSION     WP_457692508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33538
     Region          9..276
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrvlpaapsi qgltavvtgg srglgllmar qllrrrcdvv llardeaela ravgklrqwg
       61 ggtvravvcd vrdraavqdr laeiarehdg ldivianagi iqvgpadalg sdgfeeamds
      121 vfngalntal aalphlrrsp aggrlalvgs vggllamphl lpyscaksav aalaeglhae
      181 eaphgvtvta vhpglmrtgs hvhalfggdr rreyawfsal agapllsmna eraaerivta
      241 lqrrrprivl tpaarlgata hglapvtttr lvsavarvlp rngahgtvdg stvaagekpp
      301 arrlrgvlga lneraadrfn qr
//
LOCUS       WP_457692514             254 aa            linear   BCT 27-JAN-2026
DEFINITION  PIG-L deacetylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692514
VERSION     WP_457692514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26735
     Region          41..>186
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mnsarqaaad aidapgtpea dwaswpalgl lpavplptgp vvvvaahpdd evlgfggtma
       61 alaahgtdvq vlsvtdgegs hphstrltaa rlaavrsael rdalgdlglp slrpqrlrip
      121 dtqvhrheta vrhqitarly avnaalcvap wtgdlhsdhe aagraaaaac rssgvplwmy
      181 pvwmwhwarp adprvpwdsa arlvlpagaa rrkaaalgrf vsqihplgdg dgdaailppa
      241 elahhtrpfe vvfr
//
LOCUS       WP_457692518             178 aa            linear   BCT 27-JAN-2026
DEFINITION  Dps family protein [Streptomyces nigrescens].
ACCESSION   WP_457692518
VERSION     WP_457692518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=18934
     Region          1..150
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mteseggevi grlrlrlhal ndlaltlkhv hwnvvgphfi avhemldpqv davramvdat
       61 aermatlggs ptgtpgalaa ertwedysvg raqaiehlga ldvvysgvir dhraavaatd
      121 gidpvtqdll iehlrslelf qwfvrahles aggtlstgsa nglseaghaa aeqarrqp
//
LOCUS       WP_457692522              82 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457692522
VERSION     WP_457692522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..82
                     /product="gas vesicle protein"
                     /GO_component="GO:0012506 - vesicle membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=8515
     Region          21..58
                     /region_name="Gas_vesicle"
                     /note="Gas vesicle protein; pfam00741"
                     /db_xref="CDD:459920"
ORIGIN      
        1 mrpaggppap tdeplpdrqi alidlldrll sggvvltgdv vlsiadidlv rislralivs
       61 iseqnpspws alapsvrddh dg
//
LOCUS       WP_457692524             271 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457692524
VERSION     WP_457692524.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=29173
     Region          7..259
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mtevisyaya vakdddgsla ealtglpgva eapvhlvrag drgevvvavs pvpeqdfqes
       61 alranledld wlesvarahh rviealaart tvlplrlatv ylddervrhm laarqeafag
      121 rladlaahte wgvkiyveap aptdrpaapp adeglspgra ylshrkaqrh arddayrdae
      181 evarrveaaa rghavdrvqh rvqqgelarg pgenvvnday lvplrdaesf raevtraaeg
      241 lsgvrvevtg pwapysfatp peaeplkgaa p
//
LOCUS       WP_457692528             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457692528
VERSION     WP_457692528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=25959
     Region          3..237
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 msvyvysiva tshpqrldgl hgvgnppsel rtvqskklsa vvsdspeelr pkrrdlgahq
       61 avqerlmadg tvlplqfgft ttddeavrav lkertdefte rlealagcae yhlkvaqded
      121 allrqiltes dqarelneqi rsgtaspdlp lalgelvage vqarqeqlaa avldalrgfa
      181 reertspptg ndfvsvsylv eqdneksfls aerdlakelg edfdlrllgp lpaysfv
//
LOCUS       WP_457692530             151 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle structural protein GvpA [Streptomyces nigrescens].
ACCESSION   WP_457692530
VERSION     WP_457692530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10013202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..151
                     /product="gas vesicle structural protein GvpA"
                     /calculated_mol_wt=15888
     Region          21..130
                     /region_name="PRK09368"
                     /note="gas vesicle structural protein GvpA"
                     /db_xref="CDD:236485"
ORIGIN      
        1 mtvvpqsggt vaagggggsg nlydildlil drglvidvfv rvslvgieil kidarivvas
       61 vdtylrfaea cnrldlesgr kapsqltdlv gevteggshg kakgalsgaa eavtdalrgg
      121 gdddeehetr hkesaerrer parrparrrk e
//
LOCUS       WP_457692532             136 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein GvpO [Streptomyces nigrescens].
ACCESSION   WP_457692532
VERSION     WP_457692532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Pfeifer,F.
  TITLE     Distribution, formation and regulation of gas vesicles
  JOURNAL   Nat Rev Microbiol 10 (10), 705-715 (2012)
   PUBMED   22941504
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="gas vesicle protein GvpO"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=14953
     Region          41..134
                     /region_name="GvpO"
                     /note="Gas vesicle synthesis protein GvpO; pfam05800"
                     /db_xref="CDD:399068"
ORIGIN      
        1 maageqdete rvrrpsskkt akktvkktat rassgragsg eseseaprag rrvsapramr
       61 yaaeqlkell grapesvsav kptedgwqad vevlelervp gttsvmatyr vmldkegelv
      121 ayertrrytr gqidrr
//
LOCUS       WP_457692536             545 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692536
VERSION     WP_457692536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..545
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56933
     Region          1..503
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mpdavvigag pnglvaanll adagwtvevl eqqdepggav rsdravhpdf vndlcssfyp
       61 lavaspvlaa ldlyeeglvw shapqvlahp ltdgrcallg rsttgtaagl etfgtgdgaa
      121 wqglcgiwdr vgsdlldalf tpfpplrala rlaarvrgsg glrlartmll pvrrlgeeef
      181 rgeagrllla gnalhadltp etagsggfgw lmsmlgqsyg fpvpaggaqs ltsalvrrlq
      241 rrggvlrcge rvdevvvrsg ravavrtsig eivpgrravv advsvpalyg rlvdsrhlpg
      301 rlpadlrrfq wdfatfkvdw alggpvpwta eaaatagtvh ladgmdeltr fsaqiaagqv
      361 pdrpfalfgq mttadatrsp pgteaawayt hvphrvrgda gedgiggawg qgdqeamadr
      421 leeqverfap gfrsrikarr ilapptfeam danlhggaln ggtaalhqql vfrplpglar
      481 petpvaglyl asagahpggg vhgapganaa raalrtrtps gvlsraqral hrggaplrap
      541 teggr
//
LOCUS       WP_457692543             394 aa            linear   BCT 27-JAN-2026
DEFINITION  zinc-dependent alcohol dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457692543
VERSION     WP_457692543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 394)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41904
     Region          1..394
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,255..257,295,312..314,337..339,380)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mraltwhgkr dvrvdtvpdp kieqptdviv ritstgicgs dlhlyevlgp yldpgdilgh
       61 epmgiveevg pevtavsvgd rvvvpfnvsc gtcwmcaqgl hsqcettqvk drgtgaalfg
      121 fsklygqvpg gqaellrvpf gntlpvkvph gppdqrfvyl sdvlptawqs vayadappgg
      181 tvtvlglgpi gdmaarialh kgaskvigvd lvperlarar drgvhtldln eygknvaeei
      241 rvltegrgtd avieavgmea hgaplvraaq nlagrlpdal gekvmgragv dsmtafntav
      301 davrrggtis ligvyggnvd pvpmltlfdk qiqlrmgqan vrrwvddimp llndadvlgv
      361 dgfathtlpl eegpqayktf qakedgmikt vltp
//
LOCUS       WP_457692548             775 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457692548
VERSION     WP_457692548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..775
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=88203
     Region          9..227
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          364..725
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mpetglrsap rfsiivpvyn vqgylracln sllaqdftdf eviavddcsp drsgeilaef
       61 aardprvihv rheenggiga arntgverar gdyllfldsd dtftpgalra madrlgasqd
      121 pdlllfdhvr tywwhavkps avrellaeag sevfkpaert eflhmfavvw nrafrrdffv
      181 dngfrytdgl yedalmvytt mltaeravcl dhacveyrqr rhgnsmktpg rkhftifdqy
      241 qrlfdfldgr pdldhlrplf fermvshflf tgaresrvlv qdrpeffrrs vamyrrhkpa
      301 gftpppevda lqfqaldrgs yrvfqalnlv srtrqrgqhr lrkaqramsk rastsfyrmq
      361 lkrpidqnla vfsaywnrtp scnplaiyek akelaphlhg vwvvredvvd tvpdgmdhvv
      421 vntrrywelm arakyfvnnv nfaddvvkrt gqvhiqthhg tplkrmgidq qkypaaakgm
      481 smrkllerad rwdlsvssnq htseqwervy pcsftsidag yprndvffrt gaqeileird
      541 rlgiapgsta vlyaptvrdy qvgyvpqldl ekitrelgpd ivllvrthyf ygqnpqlqel
      601 qeqgalidvs rhpsveelcl aadalitdys simfdyanld rpiinyaddw etyvrsrgvt
      661 fdllsgkpgd tpgivatted elieafrsgr wkgteaaelr aafrarfcmw ddghaaervv
      721 nraflgsqdl tpaplplser tvapspheaa rsaegvvlap gtdtssgrpe velts
//
LOCUS       WP_457692549             219 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457692549
VERSION     WP_457692549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23081
     Region          4..217
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 miamdalwtf almvglltlt pgldtalvlr taalghrrra wgvvlgiqsg tlawgvltsl
       61 gvtalltash layetlrwag aaylvwmggr llwatwrrsa decpkptgsg aatttgkgad
      121 dtllggwrqg matnllnpkm gafyvavlpq fipadasqla agvllaavhi llavmwagal
      181 itlaqvlrdr lqrpsarrvl dritgtviaa fglrlalge
//
LOCUS       WP_457692551             220 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692551
VERSION     WP_457692551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22302
     Region          9..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mgslptgtea vvfdcdgtlv ntevcwtvae taifaahgha fgpeqkalvi grtveaagea
       61 madyfgrpga gaelaaelle rvrkelahga aalpgaaelv racraavpia vasnsprell
      121 dtalgsagla gylthsfaad evpspkpapd lyltacealg vapkrsvafe dsatgissar
      181 aaglyvavvp slpgadldhd wlgagldepe llgwarelgc
//
LOCUS       WP_457692554             395 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692554
VERSION     WP_457692554.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  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 395)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42254
     Region          1..389
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(1,28,116,384..385,388)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
     Site            order(12..13,15,146,149..150,154,181,233,302,304,306..307,
                     310)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(12,233,302,304,306..307)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            13
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mrilitahai yshlaplvlp vaeraqeagh evavatgagv vqhieerglt altlpnvqsm
       61 gealqdgtlr lppdmeqags vtveltpeff aaafvghlae agtrdlleva rswqpdlilh
      121 esteyggyla aeslgiphga ldiapmapya hpvvteelnr qrgkfglapv sdawhtfraf
      181 ragvvpedfy ptdsrlpgar yyqvpaqaaq galdpdiaql stdrplvlat lgsnatrlpg
      241 gahtlletii etlgelpvtg vvalgadrdp rqwdgprpdn vhltsfvqqe lllrssdlfi
      301 thagfngtre alaagvpmva vplfaeqshn adrlqqlgvg tridvqdvtr dalsaavrna
      361 ledrsyrsra qglqrrahal pdldrlveda aalaa
//
LOCUS       WP_457692556             526 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692556
VERSION     WP_457692556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..526
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57231
     Region          91..>250
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          398..491
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrnrriapvl aasavaalvp altpatasaa enplsqhleq rpawhrcssa tpasfqcati
       61 kvpldysrpg gkkidlaisr iktstpaerr gvlllnpggp ggqgldmpqs lsaelpksvq
      121 rkydligfdp rgvgksspls cgltaeeenw qrpykaasfa kdvkwartva ekcdaeqgdk
      181 lrhittrnta rdmdviravl gekkisylgy sygtylgavy tqmfprrsdr ivldsavdpa
      241 riwrgmmqvw segsepaftr wskwtaqrna tyklgntpdk vrktfwalva ranrkpieln
      301 gtlisgddir arravffsvr eaadeivelk kaadgkgqsa tpdtgtterp appafgravp
      361 sdnysasfwa vvcsdtrawp rdpeqyrrea irdkakyply gdfashikpc afwkkngsep
      421 attidnkvka ltlqnewdsq tplssglgmh rvmkgsrmvt vaggvghgiy gskscadkta
      481 taylttgklp akdvtcqapa parerssasq lplpappgip gmpgrf
//
LOCUS       WP_457692564             214 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457692564
VERSION     WP_457692564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23484
     Region          46..205
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msadrdrplp acapahvraa elaplprcsl pdsapapfdr rlsitfeafl atharkwlty
       61 aylhtgseaa arevtraayg qlsrlwphal rqasveayaw svlkervvew lydhhqptal
      121 tetaafavvt hallrecqqq famlesqlgl yaaiarlper qcdvivlrhv igysdaqigs
      181 llgvdevtvr syasrgkrkl aaalgidqgn argn
//
LOCUS       WP_457692568             391 aa            linear   BCT 27-JAN-2026
DEFINITION  sialidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692568
VERSION     WP_457692568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41414
     Region          37..387
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
ORIGIN      
        1 mkaarpvtla tllavgagll tapaapavpp hrapgrpaly ettdlavsgq gahtyripal
       61 atlpdgtlva aydrrndsaa dlpgnvdvmv rrstdqgrtw saaqaavdyd ggvgagdpsl
      121 lvdrttgrvf lfhayapkgv gfgsagagna hdsrtvlhtd ysysdddgrs wrsrrithdl
      181 kdpswhgifa ssgagsqlag grllqqyafr kadgsmwaas aysddhgasw rmgtpvgplm
      241 denktvelad grvmlnsrts sttrrlvahs rdggltysap aaddelidpa nnasilrydp
      301 tapphrarah wllfsntast garenltvra scddggswpi arsvtpgpaa ystltrlkdg
      361 tfgllyesgp yrkitftrfd dvwlgmncpa g
//
LOCUS       WP_457692570             140 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692570
VERSION     WP_457692570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..140
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15040
     Region          17..109
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(27,29..31,37,60,62..64,66..68,71..72,94,98..99,101)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            63
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mssemrslav taivqaeeca vlrvsgeldl rteqtflaea rsvvsaghrf lvldltalrf
       61 cdsrglscll alewlcrrle grlllaslgv rmlrllvgtq slnvfscypt vghaltavpd
      121 asrpawppav dgpsaekdds
//
LOCUS       WP_457692572             253 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692572
VERSION     WP_457692572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27248
     Region          1..253
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mraeerqhri lalarqsgrv evaeaasefg varetvrrdl selerrglvr rthgaaypve
       61 sagfettlar retqqvdekr riaaaaaalv geaetvfvde gytpelvatl lptdrpltvi
      121 taslrtaslv aasesttvll aggrvrsgtq atvgswardm larfvidlaf lgangvsreh
      181 glttpdpava evkeqavrss rrrvlvgvhs kfgassfcrf aevrdfdtiv tdaglsapea
      241 hrysllgpqv lrv
//
LOCUS       WP_457692576             327 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692576
VERSION     WP_457692576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35660
     Region          34..299
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpirttepap aaevaaeprg gspaararrt eraknwarra pllpalvflv ivtqlpfvat
       61 vvisftrwna lapenrgfaa ldnyravftd pamrasvgtt vlltvtvvlv slllglglal
      121 lldrgfrgrg ivrtllitpf lvvpvasalv wkhalynasy gllngsltwi wrlfgsddpp
      181 qpdwmtdspl aavevsliwq wtpfmmlill aglqsratda ieaarmdgas afdifryltl
      241 phlrrylela allgtvyvvq nfdavftits gglgtanlpy tiyqtfyqah dygrasaqgv
      301 vvvlcsllva tfalrtvssl lreevtr
//
LOCUS       WP_457692574             471 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692574
VERSION     WP_457692574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50932
     Region          58..456
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(170,172,298,300,333..335,376)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mhvplvprkv ravrarppgp grgarslglt alavalalst agcyrgagda gndgrnsinv
       61 lmvnnpqmvd lqrltaehft ketgikvnft vlpeddlrdk msqdfssqag qydvasvsny
      121 etpiyarngw ltelgahaak drafdqddil apvrssltaa dgkiyaepfy gessflmyrk
      181 dllkeagltm parptwhqva tlaakldgfr kgmkgiclrg qpgwgqlaap lttvvntfgg
      241 twftkdwqpk vdspeftrat rfyvdlvrkh geagapqagy teclndmqqg kvamwydata
      301 gagslesags kvagkvgyap apvertrdag wlftwawgiq kasthqdaaw kfirwasgkg
      361 yerlvgrelg wsrvpggkra slyrdpayvk asgafagpte rairsarpgd pgvqqrpapg
      421 iqfvgipefa dlgtkvshei ssaiagkqsv sealkksrrp aqevsdaytd h
//
LOCUS       WP_457692578             291 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692578
VERSION     WP_457692578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 291)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30571
     Region          13..291
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mnrtplaprr pgspaarrrr rtgsllglaa wlcgigfflp vawmvltsfh setdaatnpp
       61 svgaglslhg yreffgagsg vspwpplvns ltasvvatll vlllavpaay alaikpvrkw
      121 sdvlffflst kmlplvagll piyliaqntg lldsiwllvl lytsmnlpia vwmmrsflae
      181 vpvemleaas idgagltttl trivapvamp giaatalisf ifswnellfa rvltgivagt
      241 spvfltglvt sqglflakvc aaatvislpv ivagfaaqdk lvqglslgav k
//
LOCUS       WP_457692582             337 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692582
VERSION     WP_457692582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 337)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10053807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36384
     Region          257..325
                     /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(258..259,263..265,277..279,288..291,293..294,
                     297..298,300..301,307..309,314..316)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(277,280,323)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mlrihfedrd iarvqiadap dplwetvlal hhvapaargv pvygawrara rreldarglt
       61 raarlisala padaryfpdf ltpdaardgl aaglaalrdt spvrltaesa raalpdrlpr
      121 wsaalvagsr epldelarai qevhraviap dwteaaatvd sdrgararal crggvdgmln
      181 slrpalrwep pvlyvdypqd rdlrlggrgl rlipshfcwr rpialadpgl ppvlvypveh
      241 stawapastr schpqalstl lgrtrarila aldaptttge larrlrvsap sasehvsalr
      301 eanlarsrrd ggsvihaltp lgtallhgdl apvrlph
//
LOCUS       WP_457692588             465 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692588
VERSION     WP_457692588.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..465
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49200
     Region          38..460
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mrprapavaa diegtltrrg dpgyedtrtg avwnevtprr fpdivvraat dadvvhaltw
       61 araqglrvsl rsgghnwsgs plrdggllld lsglrqcgit pahgtepata tvgpaatgqd
      121 lvaaltpqdl afpvghcptv avggfllsgg lgwnsrawga scadvreira vtadgrtvic
      181 seteypelfw aargagpgfc aavtgfrlal hphpasimtt gltfplaevt rvtewaepla
      241 rrlppyveta fvlassgppa dgaprgprit vaatafaate rearqalepf adcpfgacav
      301 trqppapvsf aalhdgaaai wppahryaad tlwspeshat qltriadava hapsgkslvl
      361 spvqpvsqdp allrnmafap lgesylvcya vwddpagdqd narwlrdama aadpqgdgch
      421 yiaetdlead pararrsyap atwdrlqeik aqwdpenlfh sylap
//
LOCUS       WP_457692595             192 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692595
VERSION     WP_457692595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20982
     Region          2..184
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkiivslsv sldgfiadpd ggidwhlvdd elhryfnewl rpmgafltgr vthelmagfw
       61 ptadadpana gpmaefagiw rdmpkyvfsr tlddaggyht tlmrdvvpee imalkarpgg
      121 dmvlggadla asfrqhdlid eyrlyvhpvl igrgkplfqa sdartglela gtrtfgtgvv
      181 llhyrrpgaa ag
//
LOCUS       WP_457692601             107 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457692601
VERSION     WP_457692601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..107
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12065
     Region          2..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mifivvkfpv kpeyaeewpq hvtsftdatr aepgnlwfew srsiedpnty vlveafkdda
       61 aeahvnsdhf ragieqmrpl lrrtpdivst tiegadgwsa mgeitid
//
LOCUS       WP_457692614             193 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692614
VERSION     WP_457692614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19988
     Region          32..174
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mslsaadssl qrgippsgqa svtagrlrrv aghyptgvvl vtgprpapgq pppamvvgtf
       61 tsvslhpalv gflpaksstt wpriraagrf cvnvlgadqq qvcrrfaaad phrwevphqe
      121 tatgspvlld alawfdceva geaeagdhwf vtgavrdlav grpgpplvfl rggyghcaed
      181 adaagsgrpa rpd
//
LOCUS       WP_457692604             403 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692604
VERSION     WP_457692604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43627
     Region          88..403
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mslsslsrra vvgaalsgav vaatagpara asrpapapsg ggparripsa pvpvpplnvp
       61 alraalsdle hpqltaaqlr vsgsagrwyg nagvadrvtg rgvherdtfr igsitkvfva
      121 tvvlqlaaer rlspelpvqr llpgllpakf ppitvlqlln htsglpdeqd ppydpssped
      181 iarhrydrwt peqlvarvth gpmkftpgte qeyrsinyil lallierltg crygeviarr
      241 ilrplglrht svpgndprmh gphvhgymrm tdgslldite fdqsaawggg emishtgdld
      301 rfltalfsge llpshelerm ftlppdevrm vdgsparyaa glqtitmngi tlwgktgery
      361 gycsamlatr dqqrravfsf nptrrdatqa qvsqrigeal tka
//
LOCUS       WP_457692634             454 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692634
VERSION     WP_457692634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Jansonius,J.N.
  TITLE     Structure, evolution and action of vitamin B6-dependent enzymes
  JOURNAL   Curr Opin Struct Biol 8 (6), 759-769 (1998)
   PUBMED   9914259
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Yoshimura,T., Jhee,K.H. and Soda,K.
  TITLE     Stereospecificity for the hydrogen transfer and molecular evolution
            of pyridoxal enzymes
  JOURNAL   Biosci Biotechnol Biochem 60 (2), 181-187 (1996)
   PUBMED   9063963
REFERENCE   3  (residues 1 to 454)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000675
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..454
                     /product="aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48387
     Region          12..447
                     /region_name="BioA"
                     /note="Adenosylmethionine-8-amino-7-oxononanoate
                     aminotransferase [Coenzyme transport and metabolism];
                     COG0161"
                     /db_xref="CDD:439931"
ORIGIN      
        1 mtsarpapsg asgaelaatd ratlihptlp ahrtdrtvlv sgsgsrvrda hgreyldasa
       61 vlgvsqvghg rqelaraaae qmtrldyfht wgtlsndrav elaarlagls peplrrvyft
      121 sggaegneia lrmarlyhhr rgepqrtwil srrmayhgig ygsggvsgfp vyhdgfgpsl
      181 pdvhfltpph pyrrelfsga evtdfclael rdtiertgpe riaamigepv mggggavipp
      241 adywprvael lcsygillis devvtaygrt ghwfaadhfs vvpdimvtak gltsgyvphg
      301 avltteevaa evtgdqgfpv gytytghpta cavalanldi iereglaana aavgdhlgrr
      361 laeladlpiv gevrqlglll avelvsdrds rrpltggtla ladalreqag illrtnrnal
      421 vinpplvfsr adadeladgl rsvlsrtgpd gqvh
//
LOCUS       WP_457692632             394 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457692632
VERSION     WP_457692632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44813
     Region          43..391
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mksilfylpt vgshaqilrg msgvnpqnyq nmlwqltrqa qaadelgywg lsftehhfhv
       61 egfevsnnpv mlglylgmqt khirvgqman ilpfhnplrl aedlamldhm trgrtfvgia
      121 rgfqkrwaei mgqvygvgst lsdagendrr nralfeehwe ilkkawttet fshsgdrwti
      181 pvkdlefpye avrrygrgld ddgvvqevgi apkpyqrphp pvfqpfsfse dtfrfcareg
      241 vvpilmntdd rvvrrlmdly qeeaeaaghg tlrrgervgv mkdvlvsrda deahhwaarg
      301 ggfifenwfg pmgftealrn egetgpigad ygtlvergle wvgtpddinr kieklvaqhd
      361 peyllqcqys gliphdvqmr slelwateia pnwl
//
LOCUS       WP_457692635             422 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692635
VERSION     WP_457692635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Pederick,J.L., Thompson,A.P., Bell,S.G. and Bruning,J.B.
  TITLE     d-Alanine-d-alanine ligase as a model for the activation of
            ATP-grasp enzymes by monovalent cations
  JOURNAL   J Biol Chem 295 (23), 7894-7904 (2020)
   PUBMED   32335509
REFERENCE   2  (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   3  (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   4  (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 18411733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="ATP-grasp domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45087
     Region          60..327
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
     Region          344..419
                     /region_name="LAL_C2"
                     /note="L-amino acid ligase C-terminal domain 2; pfam18603"
                     /db_xref="CDD:436613"
ORIGIN      
        1 mpqrpkillv gqlstfpwvf dsaeragidl vlvprgddsv aaarraksvv evlpldidgd
       61 pesalsaiva rfrrdpfdgi magnekvvpf varaarmlgl pglpeevaav vrdkrsmrrl
      121 lreaglgapg fvsldspdrw adaltlrfpv vvkpangyss lgvvrvdgkd qlvpavartw
      181 elcnselrqa ggpadevgvl veeyldgpev aaeslvhhgr vqvcaigwkg emtgpyfeet
      241 tvrapaqlpa dvlaaieaev igahhafgvt egtthtelrl vggvrpvlle maariggagv
      301 nhylthiagg idlaaealri hlgqepvcws qepvptghaa aysvpvgkgg rivrvhglda
      361 vradprvdhv vqtvgpgdll rpypdwagyp aivlshhesd aaavefrdhl artlhveyee
      421 es
//
LOCUS       WP_457692637             394 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692637
VERSION     WP_457692637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40684
     Region          16..360
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(25..26,29,32,65,115..116,118..120,123,143,146..147,
                     150,221,224..225,228..230,233,260,264,313..314,318,322,
                     338,341..342,345..346,349)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mkalrsslgg lprpfwwlwg etlitsaggf vlpflaiylt svrgysvsfa slaltvfgvg
       61 sgiaslaggv ladrlgrrav llasqvlavv gmlglgtart etmvlvgtlv vgvglnatrp
      121 araaavadlv aeegrprafs llywgtnlgs svaavsagva aehgffllfv vnacanlaag
      181 avvyryvpet rpepvprrgt kalpagavhr drpflvllgs vlllgilfqq plvalpltmt
      241 adgispagyg lammmnglvi vvfqipltrl agrlrpefal aaasaltgig lgctaavhsv
      301 pgyaatvvlw slgeiviwpt cmtlvaalap phqqgayqgw flsvwsvsva laplfssqli
      361 gafdgtavvw aaclalalla atahlllarl rrpa
//
LOCUS       WP_457692641             266 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457692641
VERSION     WP_457692641.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  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 266)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27629
     Region          26..266
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mskartrrgt lagavlagaa lvgssappaa avvggdraei kkypwtvalt sqdvkepdca
       61 gtlvaprkvl tashcvspat vegvrvvggr edlrdtrkgt vrkvaklwih pkadtegnga
      121 tyahdiavlt lnapmpyrtl platpaqqkl yeegtpnrvl gwgsttgrad drrvpplqta
      181 lipnrgdeqc itaygtrryq ksytmclgyp aggvsacegd sggpvvvqgr lvgvisgggs
      241 ctsrlypgva akaasyypll qsqiag
//
LOCUS       WP_457692642             305 aa            linear   BCT 27-JAN-2026
DEFINITION  AEC family transporter [Streptomyces nigrescens].
ACCESSION   WP_457692642
VERSION     WP_457692642.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31193
     Region          8..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mialtvkali pvvllialgy alkrsmitae gfwseaerls yhvllpalfl hslatadtdd
       61 lpvrslagtl vastvavavl viavrpmmrl kgdgftsvfq gsvrfnnyig vtiaaglygt
      121 qgvataavcn aaivptvnvl cvlvfarfgs vhlrltgivk qlvtnplila sgggillqal
      181 dlrlppgiep alqalgaasm plgllcigaa lrfgaarswa apiltsssvk fvlmpagtfl
      241 aaqmvglgsq aliiavlfqa lptasssyim arqlggdapl magitatqtl lgiaavplvl
      301 alvsa
//
LOCUS       WP_457692644             423 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692644
VERSION     WP_457692644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43730
     Region          3..372
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30,88..89,91..93,96,116,119..120,123,214,217..218,
                     221..223,226,254,258,310..311,315,319,335,338..339,
                     342..343,346)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msfpgsdplv gtllsfltya vgfaarpiga lvfghygdrl grkkllvlsl llmggatfai
       61 gllpthatvg tvapvlltal rlvqgfalgg ewggavllvs ehgdarrrgf waswpqtgap
      121 agqllatgvl samtallsda afvswgwrvp fllsgvlvvv glwvrlsvde spvfqaalvr
      181 aearragggv lekmplvavl rhhwrdvlva mgarmaenis yyvitafvlv yatshtglsq
      241 qtalnavlia salhfavipa wgalsdrigr rpvyllgavg vgvwafpffa lvdshrfgpl
      301 llavsvglvf hgamyapqaa ffaemfatrm rysgasigaq fssvaagapa pliatallad
      361 ydsptpvaly viaaalltll avgmaretrs rdlaavegsa vagegrtagp dggassavps
      421 gga
//
LOCUS       WP_457692639             268 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457692639
VERSION     WP_457692639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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 268)
  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 268)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28638
     Region          1..268
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mtrhrytrgl vlaclmvlvg agfavlpaqs aqaviggqkt staaapwtvt inlwrqtdty
       61 prsgqfcggt lvtprkvvta ahcvvdeapt dlgvvagrtd lrrhegrlrk vtkawihprf
      121 grhlendvav ltldkpmppq ytplpvataa dtgpyrpgtg arvygwglld nedreanvlr
      181 sanlrvlpdr tcqrlnpwgd fdptmhvcan dpvtgahhae gdsggplvag gkligivswl
      241 angnaatptp gvytrvaafs reiarqlg
//
LOCUS       WP_457692650             185 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692650
VERSION     WP_457692650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 185)
  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 185)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20377
     Region          1..84
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          90..164
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslrhavlgl laaqpasgyd llktfqssla nvwpatqsql ygelarlads glvavraegp
       61 rgrkeyaitd vgrrelrhwi levepervrr sdtllrvfll gsvepeqald flqgrvaafd
      121 erhaelgtla dstawsqgdl svygritlew glrfsamqre wadwaagqia aaapaveqkp
      181 rqprg
//
LOCUS       WP_457692648             322 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692648
VERSION     WP_457692648.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=34846
     Region          91..228
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(96,98,163..164,167)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            98
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(162,209..210,212..213,217)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(168,173..174,205,208..209,212..213,216,219)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(194..196,205..206,209..210,213,217,220,224)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(194,210,213,217,220,224)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(218,224..225)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mtdhqaalas eaddverhpc prcdvspgsp crsrsgavag tyhtgrftkv prlakllrvp
       61 tpadrgpgqp wrpgtpapap idpdtptadi rigyarcssl tqelqsqlda laghgiprdk
      121 ifaekvstrv rvrpqfeaal aaareikaha phcrviftvn emkrlgrdaa eltaladhlt
      181 ahglvlemla gplqgmydps gpgrllfgff aamaeteren ireatlegld taarkgnhgg
      241 rppvitddml htvlrrrakg etvediqpdl liptgrrkgq spslssiyra laehekaqay
      301 peavetahad faalqqrdrs pk
//
LOCUS       WP_457692661             167 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692661
VERSION     WP_457692661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 167)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18349
     Region          4..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpdfirdl rnsigrqllw lpgvsavvfd dqgrvllgrr vdtggwsvig gipepgeqpa
       61 etavrevyee tavrvvpegi vlvetmppth ypngdicqfm dvtlrcravg geaqvnddes
      121 levgwfdvda lpeleeyalt rikraleagp twfhgmeeep pgrhpea
//
LOCUS       WP_457692667             472 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457692667
VERSION     WP_457692667.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=48137
     Region          11..472
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msmlkgsnvp vpapavrvel gwqaapgapd vdasalllvs gkvrddgdfv fynqaahasg
       61 avrhegkrpa ggamtdclav dlaavepavd kvvlaasadg gsfggvpglh irvldaaggt
      121 elarfdsqda gtetafvlge lyrrqgawkf ravgqgydtg laglatdfgi sveepaapqp
      181 papapapaap appppamapa ppmapqspap appmapppta pappmptgqp aasippppgq
      241 pvpapapppv rltkvtltkd apavsltkqg gtsgamrvnl nwsggsagkr lgkklgrkam
      301 eamgargall ppsgeldldl calyqltdga agvihplgnn fgslhappyi qldgddrtga
      361 laagenmtin ldhqdrikrv lifvtvyaga rsfeglsatv tlqpqhgapv dftldactvp
      421 snvcalamit ntgselvvqr earylvpepg vspqrtvdqa ygwgldwspa rk
//
LOCUS       WP_457692669             274 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692669
VERSION     WP_457692669.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29634
     Region          4..274
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpkpalqsih lypvksiags gpgeavvepw glagdrrwll vdaegrqitq rqqptlalar
       61 aeglpgsalr ltapgreplt vavpgpgetv pvevwkdeve avpagpeaae wfrtylgvec
      121 rlvhldapek rrpidpaysa pgetvsfadg fpllltttss lnalnsliaq gdhadegplp
      181 mnrfrpnvvv dgtapwaedd wrrvrigevd ftvakpsarc vvtttdqrta ergkeplrtl
      241 arhrrfgdrl vfgqnliprg agtirigdpf eilg
//
LOCUS       WP_457692671             147 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692671
VERSION     WP_457692671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15371
     Region          28..124
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mvssgpaevp seesgrrllq rrftarllpq lrllveecaa reglceprrg efvlavdeia
       61 gnavehaggs grlelrqvgd elecrisdag pgfseevipe llpgldgatq grglwlarlv
      121 adrftvagga agtgatgavv tlavrlr
//
LOCUS       WP_457692665             279 aa            linear   BCT 27-JAN-2026
DEFINITION  glutamate racemase [Streptomyces nigrescens].
ACCESSION   WP_457692665
VERSION     WP_457692665.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10002726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="glutamate racemase"
                     /EC_number="5.1.1.3"
                     /GO_function="GO:0008881 - glutamate racemase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=27941
     Region          24..217
                     /region_name="MurI"
                     /note="Glutamate racemase [Cell wall/membrane/envelope
                     biogenesis]; COG0796"
                     /db_xref="CDD:440559"
ORIGIN      
        1 mkialmdsgt gllaaaaamr rlrpdadlvl ssdpdgmpwg prtpddviah alavaraaav
       61 hrpdalivac ntasvhalpa lraelepqip vigtvpaikp aaagggpvai watpattgsp
      121 yqrdlidrfg rgvdvtgvpc pgladavqta deaaidaaia aaahltprdv rtvvlgcthy
      181 elvaeriraa lqqpgaptlv lhgsaeavaa qalrrigaep apaaaptgal svilsgrpag
      241 lpaealayae grllarsrtd lapgdavpaa dgaaaaarr
//
LOCUS       WP_457692677             281 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692677
VERSION     WP_457692677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29090
     Region          8..273
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msdnqnllae qrralildev rrrggvrvne ltrklsvsdm tvrrdldala rqglvekvhg
       61 gavpvsepsa hepgfeaksg lelsakedia kaaaemaapg saialaggtt afalaqqlle
      121 vpdltvvtns vrvadvfyta qraaasggta pragaatvvl tggvrtpsdt lvgpvadaai
      181 rslhfdvlfl gvhgisveag lstpnlaeae tnrhfvrsar rvvvvadhtk wgtvglssfa
      241 tldqvdvlvt daglpagara efgelppelv vageqpedad i
//
LOCUS       WP_457692685             168 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692685
VERSION     WP_457692685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18314
     Region          10..128
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mirqpsrhct velqavpari ghvrrivsaq lrywrldali dpaalgvtel lanvhrharp
       61 skqctvelcv lldqltvsvh dedprlprir vaeswetcgr glaliaalse swgvrpdgsg
      121 kvvwftlpal ttapeeartv rgcgeplple dartaagshi rirgtkvg
//
LOCUS       WP_457692689             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692689
VERSION     WP_457692689.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20974
     Region          9..143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstqeppgtq erlvrstqel lwergyvgts pkaileragv gqgsmyhhfa gksdlalaai
       61 rrtaeelkqa aeeclgapgt aydrvaaylr rerrvlrgcp igrmtqdrdv vqsaelrrpl
      121 demfewlrgr itevltegqr rgelaaaldp aataatvaav vqggyvlara addsapfdaa
      181 vqgvlallaa qvttag
//
LOCUS       WP_457692693             322 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotriesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692693
VERSION     WP_457692693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chen-Goodspeed,M., Sogorb,M.A., Wu,F., Hong,S.B. and Raushel,F.M.
  TITLE     Structural determinants of the substrate and stereochemical
            specificity of phosphotriesterase
  JOURNAL   Biochemistry 40 (5), 1325-1331 (2001)
   PUBMED   11170459
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Shim,H. and Raushel,F.M.
  TITLE     Self-assembly of the binuclear metal center of phosphotriesterase
  JOURNAL   Biochemistry 39 (25), 7357-7364 (2000)
   PUBMED   10858282
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Kim,G.J. and Kim,H.S.
  TITLE     Identification of the structural similarity in the functionally
            related amidohydrolases acting on the cyclic amide ring
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 295-302 (1998)
   PUBMED   9537960
REFERENCE   4  (residues 1 to 322)
  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
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Tuovinen,K., Kaliste-Korhonen,E., Raushel,F.M. and Hanninen,O.
  TITLE     Phosphotriesterase--a promising candidate for use in detoxification
            of organophosphates
  JOURNAL   Fundam Appl Toxicol 23 (4), 578-584 (1994)
   PUBMED   7867909
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004443
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="phosphotriesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33063
     Region          17..312
                     /region_name="Php"
                     /note="Predicted metal-dependent hydrolase,
                     phosphotriesterase family [General function prediction
                     only]; COG1735"
                     /db_xref="CDD:441341"
ORIGIN      
        1 mngtpadgpa vraapavrtv lgdiapaglg icdahdhlfl rspqlpgqel ddaeaaaael
       61 safraaggaa viqwtpygmg rraaelprla resgvrivaa tglhqaahys pgllarvrpd
      121 laglfvaelt egiggtgpra gmikvaggfh gldrharhtm aaaaeaqrat gavvgvhlel
      181 gtgaldvldl lcgalavppd rvilghlnrs pdlvvhrtaa eagsylafdg psrahhttdw
      241 rlpealaala dagfgdrill ggdtttagar svdggpgmpy llrrhrerle lalgadlvtq
      301 fltanparaf aadwarapgg sr
//
LOCUS       WP_457692699             409 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692699
VERSION     WP_457692699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40340
     Region          28..381
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,155,
                     158..159,161,239,242..243,246..248,251,279,283,332..333,
                     337,341,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mptlnkirra ltkehgsvpt eprltrpria ltaffamdgf lfagwvvrip aikaqtgaga
       61 gtlglallgv sagavafmmi agrlcrrfgs htvtavsaaa lslsivlppl trsatalglv
      121 lllfgaayga lnvamnsaav alisalrrpv mpgfhaafsl ggmlgaglgg llagslsatv
      181 hllllaaigl lvtvvagral cgqpapevpe qlpaseesrp rsvragrarr lvlvfglial
      241 ctaygegama dwgalhlsqd lgagpgtaaa gyavfalamt vgrlsgtavv qrfgaarali
      301 aggttatagm llgalaptaw aacagfavag lglanifpia laragetggp dgvavastvg
      361 yggmllgppa igllaeavgl paalttvall aalaagiaya trgahtgrp
//
LOCUS       WP_457692701             253 aa            linear   BCT 27-JAN-2026
DEFINITION  maleylpyruvate isomerase family mycothiol-dependent enzyme
            [Streptomyces nigrescens].
ACCESSION   WP_457692701
VERSION     WP_457692701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wang,R., Yin,Y.J., Wang,F., Li,M., Feng,J., Zhang,H.M., Zhang,J.P.,
            Liu,S.J. and Chang,W.R.
  TITLE     Crystal structures and site-directed mutagenesis of a
            mycothiol-dependent enzyme reveal a novel folding and molecular
            basis for mycothiol-mediated maleylpyruvate isomerization
  JOURNAL   J Biol Chem 282 (22), 16288-16294 (2007)
   PUBMED   17428791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="maleylpyruvate isomerase family
                     mycothiol-dependent enzyme"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27538
     Region          17..229
                     /region_name="TIGR03083"
                     /note="uncharacterized Actinobacterial protein TIGR03083"
                     /db_xref="CDD:274422"
ORIGIN      
        1 meitefvetl rldggllada aqeagpdari pacpewqmrd lvthvgqvhr watefvtqgv
       61 qqpsrppeap dladdalvpw lreghhhlvl aldsapqdla awtflpapsp lafwarrqah
      121 etsvhrvdaq qaagasltpl psafaadgid elltgfhard rsrlrtdlpr tlrlratnap
      181 gadwtvhlsd apphtvrtap dadgpdagkp adctiegpae elylalwnrl pwdamtvtgd
      241 eslprlwqer ggv
//
LOCUS       WP_457692713             151 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457692713
VERSION     WP_457692713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..151
                     /product="gas vesicle protein"
                     /GO_component="GO:0012506 - vesicle membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16589
     Region          19..57
                     /region_name="Gas_vesicle"
                     /note="Gas vesicle protein; pfam00741"
                     /db_xref="CDD:459920"
ORIGIN      
        1 mgdypsragp yggqgssanl adilervldk giviagdiqi nlldiellti klrllvasvd
       61 kakemgidww ehdpslssra sdgyrslade nkrlraeiqa lregdelppa edeeededee
      121 errpaaarrp argartkrdg pgsrpkkrdt s
//
LOCUS       WP_457692717             188 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Streptomyces nigrescens].
ACCESSION   WP_457692717
VERSION     WP_457692717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=20929
     Region          1..164
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 medkellaea vrlatesven gwggpfgavl trngdilarg qnrvlltgdp tahaemetir
       61 kaiqvlnpea psiavehqne stleyvprpe gspdpvaera rmlqgcsiyi sgapcpmcms
      121 aiywsridav yyscdledta rigfddtfqy edfkrplder rikiaqiype lgahayaawt
      181 nrpdkhpy
//
LOCUS       WP_457692719             411 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692719
VERSION     WP_457692719.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45275
     Region          11..411
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mgngnnglse aglrrlrevl erhveskkip glvalvgrge ethveaigtm rhdggapmrr
       61 dtifrmastt kpvavaatmv lldecrlrld dpinqwlpel adrrvlkrpd splddtvsar
      121 rpiavrdllt stcglgldtt amgspmmsay feqrvygeng wmlpavepde wmrrlgtlpl
      181 myqpgerwly nvsddvlgvl varvtgqsfe aflrerifdp lgmkdtgfhv padkihrlpp
      241 lyapdpqtge ftvedqaegg hhskppafqs sgggldstvd dyhayfrmll nhgkhgteri
      301 lsrpavelmt tnrltpeqta alqawarsvv hlshgqgqtg gwgfgmtvrt yrgdyapigq
      361 fgwdggagtt tyadpdnqlv gilltqtgms tpdsaramqd fwttlyqaid d
//
LOCUS       WP_457692727             315 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692727
VERSION     WP_457692727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34183
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdliavrtfv tavdagqfqe aavnlsitpq avskriavle kdlgvqlfsr targarltid
       61 gqaflpyara llqaeeqaaa svrpgrralr vdvigrrlsv agllrdfhra ypetdldvvt
      121 lfdydaaiaa vrsgmidatf ravtmpgrql pdgieatpvf deplllftgp ahvfaaarai
      181 apaqlagrri wmpgnlpgte waayydefaa efgltidaig pnfgieplld tiadsstlat
      241 fvseqtplvw pvghdlrrip lhdptplyph sliwradnph paltalrnhl tsaypgrpds
      301 gtwtpkwtqh atpps
//
LOCUS       WP_457692733             180 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692733
VERSION     WP_457692733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Wozniak,K.J., Burby,P.E., Nandakumar,J. and Simmons,L.A.
  TITLE     Structure and kinase activity of bacterial cell cycle regulator
            CcrZ
  JOURNAL   PLoS Genet 18 (5), e1010196 (2022)
   PUBMED   35576203
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..180
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=19847
     Region          37..>109
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 mrpprswter dlllsaaepq fiaeslalle krpdligsad ldrarrewqv leplvrsrta
       61 ferafpgidl qpihgdsppa nifggvdgdl yadfelvtlg pvewdlaalg pvlesaynrg
      121 aqrtgmrpln edvlrfvnav gmlraiaslt lvpqlpslve ylqptvdqwq tmpfaggrte
//
LOCUS       WP_457692735             126 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692735
VERSION     WP_457692735.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14358
     Region          29..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtkqfsgsp deadltrads lareifsdia nkwalliiea lgertlrfse lrneiegish
       61 kmltqnlrml ernglvertv hptvpprvey tltepgqalr vtidgmcdwt hrylghieas
      121 rhrfdt
//
LOCUS       WP_457692739             138 aa            linear   BCT 27-JAN-2026
DEFINITION  Fur family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692739
VERSION     WP_457692739.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..138
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14886
     Region          1..137
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msdlldrlrg rgwrmtaqrr vvaevldgeh ihltadevla ratarlpeis ratvyntlge
       61 lvslgeviev atdgrakryd pnahhphhhl vcsgcgaird vhpggdplad lpaserfgft
      121 vsgaevtyrg lcpdcara
//
LOCUS       WP_457692747             452 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692747
VERSION     WP_457692747.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48702
     Region          22..451
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 meqvtanvcv vgagfaglaa arqlaeagre vvvleardrv ggrvwnrelp dgtvvsaggt
       61 wlgkgqermf qlcrelglev ypqydkgdhl vcvdgrnhrh rgipktgpaa laslglaflr
      121 lnlmarrlpa dapwearrar twdartlgqw lshplnvpsa aahtllrstm nllfcadpae
      181 vsllgalvla rggggagfgy ytdprktesh lvdggapela rrmaarlgta vhlsspvrri
      241 vqnttdvevi tdalavrarr vivatppvla grisfdpplp aahshlrqrv vpgaiirvht
      301 qypepfwrgq qlsgqtlapq spvpitidqt prsgepgvls syafgagalr lgslepkerq
      361 eiwldalaer fgpearrpta yletdwseqp wslggmvahf ppgaltnygs alrepvgrih
      421 wastesatlm hglmegavrs geraarevlt an
//
LOCUS       WP_457692749             757 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692749
VERSION     WP_457692749.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 757)
  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 757)
  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 757)
  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..757
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..757
                     /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=84143
     Region          2..757
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mpglkrpvrv tvdawgvphi fadnvgdlfq aqgfnvarer lfqidtwrrr glgrfsevlg
       61 ascveqdraa rlflyrgdma aewasygpea rdaatrfvag inayidwlgd hpdalpaefq
      121 klgyrparws pedvvrirth gignnlnsqv ararlmsvgg nkasayfhkl epdhtvqvae
      181 gldlslipad vlgvyslata pmvfadgklr rmsdglnvlr esatgsnvwa vaptrtatgr
      241 pilagdphre nytlpanryi ahlsapglni igagepwnpg ismghngmva fgltnlpadq
      301 adlyvyeldp ddhsryryrd rweklttvte eiavaggepr kaqlsftrhg pvvkideknh
      361 kayavrtvwt epgtspylgs lnyqrvkdsr efveaisrwk vpgsnlvyad tkgdigwvpg
      421 aiipkrrgrg ydgllpvpgd grfewdgfyd naqlptsrnp ragffvsane ynfppgyptp
      481 tydwlpayrk drihevlsqq rrtsiadtla lqsdvksgva kqflpyvtkl rstdpttaka
      541 lrllssydgv askdsagaal fetwmmrfly pawaqlllpk paadylvgis idvdlrimnd
      601 sfvrpddwfg adgarkrdel llstlpkayt evasklgade rawrwgamhi hvfmhplggp
      661 nvgpterggs fdtvcvsyfh ypdypyaevv gatfkmaldv gewdnsrvin apgqsgdqrs
      721 khyndlqdkw sageyfplly seqaierngg trillqp
//
LOCUS       WP_457692757             136 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692757
VERSION     WP_457692757.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101108
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14934
     Region          1..114
                     /region_name="HTH_MerR-like_sg3"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd01282"
                     /db_xref="CDD:133388"
     Site            order(2..4,18,34..36)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133388"
     Site            order(48,51,55..56,65,88,92,98,102,105..106)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133388"
ORIGIN      
        1 mrigelarrs gvserslryy etqgllraer tpggqrhyge wavdrviriq alyaaglnsk
       61 kigqllpcmr dadggpseia tprlvtelta erdridrmit dlirsrdvld eaittasadp
      121 pasatsradt sgshrr
//
LOCUS       WP_457692759             393 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces nigrescens].
ACCESSION   WP_457692759
VERSION     WP_457692759.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41517
     Region          10..343
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(29,31,62,104,230,303,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(29,31,62,104,106,113,178,181,183,230,237,303,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(31,106,178,181,183,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            183
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mthtpvisrl feparlgalr lpnrlvmapl trnragadgv pqpimttyya qrasagliia
       61 eaatpnavgq typhipaiyn erhvagwrrv teavraaggr mflqlqhggr vghpdnsglm
      121 pvapspvplp etihtpdgrq eavvpremtv ddirstvadf ataarnaida dfagvevhaa
      181 nghllhqfms qstnrrtday ggsvagrirf avevtqavae aigsdrvglr ispgntvngi
      241 degdteniyp aliealadtg paylhlvfad pdqplfhdlr kswpgtlian palgwgaplp
      301 adggmqager lltagadlia lgraflanpd lverlrigap lnpvrdqhmm yvggetgytd
      361 ypllapvqhr aetsdsaptp apkagpapap agp
//
LOCUS       WP_457692765             115 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457692765
VERSION     WP_457692765.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..115
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=11669
     Region          7..108
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 msttyvvvtl laaamagfsa asvflraqwv vqpladygip rswcpwlgaa kavgaagllv
       61 glalpvigvl agiglvlyfa gavvtvvrar ryshipfpll yaapvvgala lgfta
//
LOCUS       WP_457692761             253 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692761
VERSION     WP_457692761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28128
     Region          3..104
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,79,83,89,93,96..97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          148..247
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mawpiaevar msgvtartlr hydeigllpp awigtnghry yeerellrlq qilvlralgl
       61 glsetgrvla aqvdelealr shhrrllder drldalagtv artiteleqs rkdgrpmtsi
      121 nrpenlfegv epaqygeslr dfpelageie rrtsamseae ieaghrkrta qmirlaella
      181 agtpagaepv qaeieaqyra laelravsae eyraigrscv dnepwraaye aiapglaeyq
      241 rdaieayatt rls
//
LOCUS       WP_457692768             228 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692768
VERSION     WP_457692768.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24591
     Region          1..182
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mklltvnlgs praveyatdp sgttgifkep adgpvrvadp gppgrgasgv agdavcdltr
       61 hggsdqavya faredldfwe relgrplpng afgenlttsg ldingarige rwrigpevvl
      121 eatsgriscl tfqrrmgeeg wvrrftrhaa tgaylrvivp geiragdpie ivhrpdhrvt
      181 vamafravtl erqllpevla agealhtevq rvareyvaal kereqsgt
//
LOCUS       WP_457692773             209 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692773
VERSION     WP_457692773.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23136
     Region          2..192
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 msklivtafv tldgvmqapg gpsedvdegf ehggwqvpyv dddfmdlmqg vfertadhll
       61 lgrktydifa ahwprvtden dpiavklnam pkyvasrtrn slewnnshll kgeaaesvaq
      121 lkeqldgvim tqgssdlirt lqqhdlvdey rllvnplilg tgkrlfsega apsawtltes
      181 ratsvgvqyc tyeragkpey gsflldeqe
//
LOCUS       WP_457692774             416 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692774
VERSION     WP_457692774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45796
     Region          1..406
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 mpdpyplrpv tddefetwar viantygddr sdedlahera iieldrtiga fdgdrpvggt
       61 aaytrsltvp gtvlpvagvt wvgvapthrr rgiltalmrk qltdlheggr epiavlrpse
      121 ariygrygyg pssrgaqlrc ekrsmhfrps tdfgdgsirl lsrdearphl ekvyeqvrlg
      181 mvgwpdradr fwdgrlfdep qarggatalr yavhqdpdgq atgyalyrik serdifgvna
      241 savqvvelaa asqqayaalw rflagidlvp wieyegavde plphlltdpr aarsvevdrl
      301 wvrlvdvdra lagrryatpl dvvldvrdsf cpwntgrfrl qadgdtvdce rtgaspdlcl
      361 tsaelgaafl ggttlaslaa agrvqelrpg althasmafr gsrepfypgg wafpay
//
LOCUS       WP_457692776             423 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692776
VERSION     WP_457692776.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=46434
     Region          32..414
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(45,73,259..260,288)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 mlsewfrehs ttlttldpqq plddlealre ivgdarvvai gegahfveef srarqrvlrf
       61 laercgftvf amefgfseaf pldrwlqgeg ddsdlakvsr taaewgaadl mhwlrrhnrt
      121 sgyplrfagi dvpeaggalr ptlepvadyl revdpdalrl vdtalevsdr flkgagsgaa
      181 aaprwaglea aeqneltavl arlllrlraa eplyvsrssq rrfdiarrrv eaachtdymf
      241 qamnallsgr glaadlsvre iymaesvrwh ldhaepgari vlaahnshih kttlelgggl
      301 ttltmgrhlq rmlgqdyrtv afvhtadhvp emypdqsapv gftlaeaqlp paepgsveaa
      361 ltdagladri tltdlrdapr daqgvpllns irsqssalst pvpeafdavl avptvtrdrt
      421 vrf
//
LOCUS       WP_457692779             307 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692779
VERSION     WP_457692779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          7..307
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 mspskavevp qplaasyars fgeegrawia glpalaagfl erwelqrdga agageaslvl
       61 pvlrkdgtra vlklqmpree tiaaviglrt wdgegmvrll dhdpesstml lerldgartl
      121 asiedddvam gilaelqarl vrvpapqglr slgdiateml eqvpravtal adpadqqhlr
      181 gwasavaelv gepgdrmlhw dlhydnvlaa erepwlaidp eplsgdpgfd lwpaldsrwe
      241 dviakgdtlr mvrrrfdllt evlgldrara tgwtlgrllq nelwdieggt talapssvai
      301 aesllnr
//
LOCUS       WP_457692783             460 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692783
VERSION     WP_457692783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Sophos,N.A. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase gene superfamily: the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 5-22 (2003)
   PUBMED   12604184
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Hempel,J., Kuo,I., Perozich,J., Wang,B.C., Lindahl,R. and
            Nicholas,H.
  TITLE     Aldehyde dehydrogenase. Maintaining critical active site geometry
            at motif 8 in the class 3 enzyme
  JOURNAL   Eur J Biochem 268 (3), 722-726 (2001)
   PUBMED   11168411
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Perozich,J., Nicholas,H., Wang,B.C., Lindahl,R. and Hempel,J.
  TITLE     Relationships within the aldehyde dehydrogenase extended family
  JOURNAL   Protein Sci 8 (1), 137-146 (1999)
   PUBMED   10210192
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=46451
     Region          77..451
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mttavssvts rnpadpsdvl vsvpapgafa avaaveqgra aqpgwsagga aarsaalgav
       61 aaaieaaade laalavrevg kplteahaev artvaiwryy aqapyepvga vhetaagpgl
      121 lltrrrpygv aglitpwnfp faipswkaap alaagnavvl kpapeataca rrlaclveqt
      181 lpagvftvlp ggategnalv saadvvsftg sttvgravvh aatargvpvq aemgglnaal
      241 vlpdadieqa arhiaaaiag yagqkctats rviavgaald plrealteal ravavgdpad
      301 pstvcgplis epardqvssa wdglsvlagg tvpglpgwya aptlvekvpa ghqllreevf
      361 gpvaallpad dlahavritn svpyglvtsv hsagldpvlh gldrldtgmi rvnapstgvd
      421 fhlpfggake sghgpreqgr aalefytssr tytlspartm
//
LOCUS       WP_457692784             302 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692784
VERSION     WP_457692784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32395
     Region          11..299
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtaftwnsir pwrgimvata lplrddlsvd hdayarhvrw lieqgcdgvv pngslgeyqt
       61 ltdeerarvv rtaveaagdg arvmpgvaay gsaearrwae qagevgcgsv lllppnayra
      121 deravrahyt evaeagvpvv aynnpldtkv dltpgllarl hqdgsivavk efsgdvrray
      181 eiaelapeld lligaddvll elavagavgw iagypnafpa tcaelyhaav agdletalpl
      241 ykslhallrw dsktefvqci klsmdlvgrr ggptrpprsp ltgeieaevr aatekaraag
      301 hh
//
LOCUS       WP_457692787             384 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692787
VERSION     WP_457692787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39320
     Region          29..379
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mltrrtsdvi vvgagvvgaa cayyaaragl svtvldrgpv aggttgageg nllvsdkepg
       61 peldlallst glwrelaell ppqieyepkg glvvaageag mqalrdfaag qdkagvraee
      121 vpgdrlqele phltpglagg fhypqdaqvm palaaahllr aagdrvclrl geevtgllta
      181 adgsvrgvrt tagevqaphv vnaagtwgge farlagvelp vlprrgfvlv teplprvvrr
      241 kvyaadyvad vasgsaalqt savvegtaag pvligasrer vgfdrtlste vlrrlaaqat
      301 alfpvlagvr amrtyvgfrp ylpdhlpaig pdprvpgllh acghegagig lapatgllia
      361 rslgggappl dpgpfnparf eatv
//
LOCUS       WP_457692785             487 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692785
VERSION     WP_457692785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Blumer,C. and Haas,D.
  TITLE     Mechanism, regulation, and ecological role of bacterial cyanide
            biosynthesis
  JOURNAL   Arch Microbiol 173 (3), 170-177 (2000)
   PUBMED   10763748
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Castric,P.A.
  TITLE     Glycine metabolism by Pseudomonas aeruginosa: hydrogen cyanide
            biosynthesis
  JOURNAL   J Bacteriol 130 (2), 826-831 (1977)
   PUBMED   233722
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14289850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="FAD/NAD(P)-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50371
     Region          27..>321
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     Region          394..436
                     /region_name="GlpA-like_Fer2_BFD-like"
                     /note="bacterioferritin-associated ferredoxin (BFD)-like
                     [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate
                     dehydrogenase subunit A, hydrogen cyanide synthase subunit
                     B, and similar proteins; cd19946"
                     /db_xref="CDD:381079"
ORIGIN      
        1 mpasasdpyd lavigagcag lagavtaagh glsvalldas pqtggqfyrh paralgaarp
       61 evlhhdwqaf aglrrrlers dvrhlsghhv wavtkedgdl wavhavtgad gadkrsvqvr
      121 artvllatga yerqlpfpgw tlpgvvgagg aqamlksglv lpgrrivvag sgplllavas
      181 slatagaqvp avieasgylg yarrpralaa npqklaeaav hgaallrhrv rlrtrsavte
      241 vhgtdrvsav tvtrldrdwr pvrgsgrria cdalavghgl vpqielatal gcatrptadg
      301 tsalaldglq etsvrglwaa getggvggaq laraegelag laaaarlhgr pvhegrvrel
      361 rrrrdrmraf aeamavshap aagwtdwltd dtdvcrceev tagrireavt dlgardahtv
      421 klltragmgw cqgrmcgtaa aclaagggav eppaerrpfa vpvplsalas pdeptgsrpd
      481 aapavdd
//
LOCUS       WP_457692789             310 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457692789
VERSION     WP_457692789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32443
     Region          13..304
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mttatapvei pagsgpwqla raqlrrrtsv qvslvivalf vvmaaaapll sglggwspda
       61 fdksavdpyl ggqpigplgg ispdhwlgve pvtgrdlfar vvhgaqvsll iaftataivv
      121 vagtaagiaa gyfggrtdav lsrlmdltms fpslifmiam msvakdvnri vlmtaviglf
      181 gwpgiarvvr gqtlslkhre yvdaarvggs gpwriltrdi lpgvagpvia yttlivpgmi
      241 ateaalsylg vgvrpptpsw gqmiaesaaf ydtdpmyfvi pssclfltvl aftllgdalr
      301 dildprgsri
//
LOCUS       WP_457692791             335 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692791
VERSION     WP_457692791.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35936
     Region          8..331
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mttppqills vrdlsvtfat krgpvravds lsfdvhrgrt lgivgesgsg ksvtsmavlg
       61 lhtgaevtgs irldgqelvg rperewsrlr grraamifqd plsslhpyyt vgeqvaehhr
      121 vhfrsrrava rrravemlae vgipeperra geyphqfsgg mrqrvmiama lacepellia
      181 depttaldvt vqaqilelia rlqeerglav vmithdlgvv arvahdvlvm yggraaelap
      241 vdalfaspah pytrglldsl prlddaddap lrvipgspps llapapgcaf aprcaraaga
      301 spserlrcdt erplltgpag hpaachfpah egvts
//
LOCUS       WP_457692792             326 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692792
VERSION     WP_457692792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35147
     Region          3..326
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtgtdrplls vrdvtmafpg rrrgaapvra vdgisfdvaa getlglvges gcgksttgrm
       61 ivrllepttg sitydghdis hlsprglkpl rrelqmvfqd phsslnprqt variisdpll
      121 vqgssasdar kraaelmdlv glipehldry phefsggqaq rigiarslat nprlvvadep
      181 vsaldvsvqa qivnlmerlq qelglaylfi ahdlsvvkrv cdrvavmylg riveigdker
      241 vyaapahpyt rallsavplp dpaaerarer itllgdppsp aapppgctfh prcpkarsrc
      301 rteapllria apgeprevac hfpeaa
//
LOCUS       WP_457692795             506 aa            linear   BCT 27-JAN-2026
DEFINITION  PepSY-associated TM helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692795
VERSION     WP_457692795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Yeats,C., Rawlings,N.D. and Bateman,A.
  TITLE     The PepSY domain: a regulator of peptidase activity in the
            microbial environment?
  JOURNAL   Trends Biochem Sci 29 (4), 169-172 (2004)
   PUBMED   15124630
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..506
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=53797
     Region          33..437
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msteqrlass dspgspdpar sgeeravrrt gwaalrplvl rlhfyagvli apfllvaavt
       61 gllyacsfqa ekvayahelt vpvgteklpl sqqvadarka hpegklaavr papqpgdttr
      121 vllsdvpgvp ddhqlavfvd pytgnvrgal etygstgalp lrtwldalhr dlhlgeggrl
      181 yselaaswlw vvaagglalw igrkrknrtl ralalpdrta tgrrrtlswh gavglwaavg
      241 liflsatglt wsayaganig dlrealgqat ptvstavtek ragqgehdgh gdssgagemp
      301 dmpgmdgtkr npssgsapsd vgidkvlraa raqglsdpve vglpadegta yvvkqvqrsw
      361 pekqdaiavd patgkvtdvs rfadypvlak ltrygidlht gtlfgianqi alaalalalv
      421 flilwgyrmw wqrrptrdlt lsfgrpmprg awrqvplpvl vplvlavaav gwlvpllgis
      481 lvaflavdia lgalarrrrv stadgg
//
LOCUS       WP_457692799             578 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457692799
VERSION     WP_457692799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 578)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..578
                     /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=61939
     Region          355..578
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mspevagsat apaplpdrap pgpgplfrlp erpswwrpwg ataldvliam gcawfdaqfr
       61 stfleeqlhs plpqgwaigl tvvgalllvl rrrcpvvvta vitcglllgt gsvlatvvay
      121 yslarhtprl rtvfvaapvg lllvlgvavl hllqfdpphg rdvteepvvi alvgltavva
      181 pvltglyprt prqpwwwehr sammfdvllv llfplanpva lvsglnslen dpllvpapvf
      241 vllvmvqgva liwrrrypda laavavllip lvlpsfsilp vslyalakyg asrrnlllgs
      301 gtaavvlvaw tvvatefkad qfipysiflv vpsvvvpvlf gmyrgakrsl mvtlqdradr
      361 lereqhllas qarmeertri aremhdvvsh rvslmvvhag aleagaggtg vatdtgrlig
      421 dmgrqalnel rqvlgvlrld dgeqqvplsp qptpediatl veesraagmq iafdvigeps
      481 aadstvqptl yrviqegltn ahkhagnvpa rvevryqkda vrviveneap agpvptllps
      541 gghglvglge rvtvlggtfe agalenggfr itatvplr
//
LOCUS       WP_457692802             284 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457692802
VERSION     WP_457692802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  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 284)
  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 284)
  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 284)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29181
     Region          13..278
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrrgrrrrag avlgavmvgv alsvstagav hamsggtqlp qrgaapwlat lalkgdapll
       61 qrascggali apdrvltaah cldgqdtrra evhigssvls qdpgtvrdir svtthpryel
      121 lpspadpdnv alssaaydma eirlsapvrg vkplpvarhr plpgtpvsvf shgttaapdp
      181 sqpgkeirgd vlrrgdltvr thaqcaaqtp aivdeasvlc ardisdggtt mcfgdsgspl
      241 viwgrrgpel agvfsfaget agkvcgqaad gafadvpalm arvk
//
LOCUS       WP_457692804             219 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692804
VERSION     WP_457692804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23358
     Region          7..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrtidpakha arrqhivqaa salfatqgfe rtttaqicka agmssgnvfh yfpnkraifi
       61 allqddkddk terlaratas adpwaalldv vqflaapaae plapplvmea mlqahrdpel
      121 aellsqdstd eqsvitellt kaaaagqidp gldpgptasw vmaliasmyt saatepsfdp
      181 agqlptllli vqrflrgeps ehrrsattgk qrgdagevt
//
LOCUS       WP_457692812             520 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457692812
VERSION     WP_457692812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53595
     Region          62..442
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtadnselpg prpameaepa gqadrrrnst qddppraegg drgtsdlaap prwrellgpe
       61 hrgaavvlaa gvlvgavniy lassmlptav adiggesfya wnmtlylvam viatmlvsrf
      121 larwgnagay ligfalflvg slacaasltm pvllvgrclq glgagllsgl gfavirsalp
      181 rrlwtrgnal msamygvgnf vgpalgglfa qfgswrlafv lmagvaavcg aavprvlprs
      241 ersdlaapvp vvslvlvtaa taavsvagvl hdilaraagl avavllvvgf vaherrserr
      301 vfpgatyrag salkwiyltl gllafgvave sfvplfgqrl aglppvaagf fgaavslgws
      361 ltqigsssav rertvrrlrt igpvllalgf lvqgllqren apiwwvviwv pvlcvagsgi
      421 giayphlsva amtaaadpee grqaaaaiat vttmstafgt avagvlvslg gqsmlgsarw
      481 llfgfavlca igivtaraad rtsrsersaa vgrssvtqgs
//
LOCUS       WP_457692813             187 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692813
VERSION     WP_457692813.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20809
     Region          13..178
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mfaislgddg aelrplepwh ageffahmdr greyigqyva lpdrttdlas ataflqmyad
       61 kaaadsgrly giwsdgvlvg gvlfrtfdvt sgsceagcwl eesavgrgli trairvlidw
      121 aveergmhrv ewiaasantp sinvakrlgm vregvqresy phrgvrhdme vwsvlapewr
      181 rqretar
//
LOCUS       WP_457692814             288 aa            linear   BCT 27-JAN-2026
DEFINITION  ketopantoate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692814
VERSION     WP_457692814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29725
     Region          14..287
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mavlgpggvg gllaavlsra ghrvicvage attralrqdg irvrsgqfgd ftaaveadta
       61 lrepvdlcli avkhtalaaa lerippgvlg dgvvlpllng iehpamlrgr ygsacvapgi
      121 irvestrtap gviehgspft eidlagaher fapltamltd agvrtrvved etaalwakla
      181 flapfalltt rygrtigevr tqrreelval veeaaavsra cgapadaaka lalydafpag
      241 skssmqrdae agrpleldai ggallraaer hgvpvpvaar ltaelsad
//
LOCUS       WP_457692816             383 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692816
VERSION     WP_457692816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40536
     Region          4..382
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtnlhdilek hisdgpvpga vglvargdrt evqavgsadv dgtspmares ifriasltkp
       61 viaaavmmlv edgrialddp vghwlpelas psvvrtpggp vddvvpaarp itvadlltsr
      121 aghglpsdfs lpavgllfse lkqgppqpql vaapdtwmaa lsripllhqp gdgwlyntss
      181 diqgvliara sgrplpefla erlfeplgmv dtgfevppgk rdrftswyra dpedglelvd
      241 apdgqwsrpp afpsgagglv staddwhafa rmlladgsad grrsllspts vrqmttdqlt
      301 paqreagrvf legqgwgfgg svdieviepw nvpgrygwig gtgtaahlta stgtvtills
      361 qlelagptap almrdfwrya adv
//
LOCUS       WP_457692818             157 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692818
VERSION     WP_457692818.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17850
     Region          7..145
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtteffvrpa rpadartlae lrwtfkqedy egqppaparh peeaehwird rlsdghwlaw
       61 vaeadgelcg hvflclverm pepyednnpv gyvtnffvtp sqrnkgagsa llealkqhsh
      121 ragleglivw pserstplyq rfgfqppeel lelpldt
//
LOCUS       WP_457692821             205 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692821
VERSION     WP_457692821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=22874
     Region          1..99
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mtatvksspl altvlallhh rplhpygiqq llkrwgkvhv vnvgqragly rtierlqagg
       61 liavrqterd qlypertvye vtdegravtr dwleqmlavp kaefpvfpaa lsnmlmlspa
      121 evlpilerra arladrrael erqtadaeig lpritliene yllavlgaee rwlqgvmsdl
      181 rdgsltwsae mlaafqease pasde
//
LOCUS       WP_457692823             279 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457692823
VERSION     WP_457692823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  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 279)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30015
     Region          14..265
                     /region_name="AKR_AKR13B1"
                     /note="AKR13B family of aldo-keto reductase (AKR);
                     cd19088"
                     /db_xref="CDD:381314"
     Site            order(20..22,51,56,81,124..125,154..155,174,201..207,227,
                     244..249,252,255..256)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381314"
     Site            order(51,56,81,124)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381314"
ORIGIN      
        1 maatmfrigg dlgvrrlgfg amhlptepgp aretslavar ravelgvtli dtaylyggga
       61 neellaealh pypegllitt kvgiapsgps hewrldgrpa vlraqveqal rrlrveriel
      121 lqlhridpet pladqlgtlr dlqtegkidr iglsevtvde ldqargiidv asvqnrynll
      181 drehepvlaa ceaagiaflp wrpvawgesg aaaeiatvaa elgatptqva lawllghspv
      241 ilpipgtarm dhleenlaae dlalsrphrd rldrltapa
//
LOCUS       WP_457692829             143 aa            linear   BCT 27-JAN-2026
DEFINITION  protein-tyrosine phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692829
VERSION     WP_457692829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="protein-tyrosine phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=15729
     Region          <48..143
                     /region_name="CDC14"
                     /note="Protein-tyrosine phosphatase [Signal transduction
                     mechanisms]; COG2453"
                     /db_xref="CDD:441989"
ORIGIN      
        1 mtdtwnaada gilrlpsgrl irgrglrrpl pagptpayav yllgkqppev pwesqwlrwp
       61 dfrlpsshaq aqavlraawa raeaerveia caggrgrtgt alaclavldg vpageavdfv
      121 rreydprave tpwqkryvrr fad
//
LOCUS       WP_457692831             358 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457692831
VERSION     WP_457692831.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36505
     Region          104..155
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          171..354
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(203,228,263,266..270,272,280..284,287,291..294,296,
                     304,309..314,329..331,337,340)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(203,292,294,296,309..314,329..331)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mkhtrvptpr tvitgaalva ltaatltlqt adaapaknpd ppsasaagqr akgisstlga
       61 dgagayydae hhklivnvtt eaaaakaraa gaeprivkhs lasldaarat lkkqatipgt
      121 swgmdprank vvinadrtvq gdqleqlkrv aaslgdraav rqsadtlrpl iaggdaiwgt
      181 garcslgfnv trggqpyflt aghctnavrs wsatqggsei avteagtfpg ddfgivkyta
      241 adivhpsevd lyngsmqpia kagdpivgqr vqrsggsthv qegdvtalev tanyqqgtvd
      301 gliqttvcae agdsggslye gdtalgltsg grgdcatagv tyyqpvreal ektgaqig
//
LOCUS       WP_457692832             359 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692832
VERSION     WP_457692832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=38844
     Region          3..343
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 mssltglrfa aavgvlyths mlminphlae tlgpevwvgg savslffils gyvlthsarp
       61 ndtarafwrr raakifpnhl ltwclvvgal acagattlse gsgiaaslss lflvhtwvps
      121 hlfvsagnpv swslaaevff yflfpvmlpw ikrlsprgll igaataiavv wlwplfcala
      181 vspdgssfrr hwflymlpvt rlpefvlgml aariassglr iprigvlpaa lgvisaivmn
      241 paflpqpfly aastvaplvv lvyataeldl hdrtsllrar plvllgemsy amylvhflvl
      301 gllylgltdq gwsslsvvlv glpfvllasw llyagverpc vrrfstprar artraaaas
//
LOCUS       WP_457692833             352 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692833
VERSION     WP_457692833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=39738
     Region          111..267
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
     Site            order(129..135,153..154,177..179)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mnkrseqiaa hrpryqdela hglerffdpe rttcpwctsa rlrrrlrttn hpqrkpgkfv
       61 ldqcrncghv fqnprlsadg ldfyyrdcyd glgeatmarm aasplavkly rararamlpf
      121 srparwldvg tghghfcaea rrihprtefh gldwgegvei gvrngrlara yrgsfaglag
      181 qltcqydvvs myhylehtla prqelaaaht alrrgghlli evpdpqsaaa rllgrwwgpw
      241 lqpqhlhlip ldnlcaalte qgftvvatnr rephiptdlt saavnvlnsv lpgedlpwlp
      301 rrpgpvsrwv rrlsllatap allvlfgldi llapltrrtr lsnayrviar rd
//
LOCUS       WP_457692834             415 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692834
VERSION     WP_457692834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43964
     Region          1..412
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(1,27,110,406..407,410)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
     Site            order(12..13,15,168,171..172,176,201,259,320,322,324..325,
                     328)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(12,259,320,322,324..325)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            13
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mhiliatags hgdvapytgl garlrqaghr vvmatharsa emvrrsglgf rplpldryat
       61 sgagspqgdg sgngrsgarl skveqiqlar elapemadav aeacasgaev vllssslapl
      121 glvaaeglgl pslgvflqpl aptrefppvi fdmpsmgpft nraaarcaes llarafapgv
      181 rhlqrrlgvp saslerrrat wpvqhgfspv vvprpvdwrp gmevagywwp seipdwtpep
      241 rladflqsgp ppvyvgfgsm epsdperlgr lvaralklag vrgvvqaswa glsvddddvl
      301 tvgevphawl fprmsavvhh agagttaagl ragvpavpvp mmldqpfwas rltalrvspg
      361 kvpfrrlsae nladavrkav hdpryrhrar qvssligaed gagrvltave hlagr
//
LOCUS       WP_457692836             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692836
VERSION     WP_457692836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21650
     Region          2..201
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkrvdheer raqitealvr vagrrglhav gmrdvateag vslrlvqyyf etkeklllhg
       61 lqwltagiga riadrvraag dapgpreiie avllealptd eesrtfhlvy tayavlavtd
      121 etlaaqpfid gpnaaedlla dqlerartag ltppdldvrt eaisllalsa glgtsvlvgq
      181 rtpeaaapvl rhhldrifpg gg
//
LOCUS       WP_457692837             254 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692837
VERSION     WP_457692837.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26859
     Region          3..199
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          6..35
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          37..68
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          78..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(80..81,84..86,88..89,93,96,105,107,111,115..116,
                     119..121,123..124,128,131,139,141,143,147..148,151..153,
                     155..156,160,163,172)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          107..139
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          141..172
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtealtpqli saiyadeadk veallrqgas psapdadget plylaavsgq sdivrlllea
       61 gaspdtesrg qpgseglplc aaacwgheev vrallahgad pdlreddgtt ytplmwaasn
      121 ghhrtaqlll egqadpdagh rdrtplmaaa argsiavvra llrhgatpql tdaqgrtawh
      181 mareesgkdi erelrrkagv asdarcevrr sprpegtelv eltvrapdgt hageyhqetg
      241 haaivallee napd
//
LOCUS       WP_457692840             252 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692840
VERSION     WP_457692840.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27062
     Region          6..249
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgngegptli tsvqrafrlm eavgahegga pakqlaretg lplattyhll rtlahdgyir
       61 klddggfvlg eklatlhagg rgqalltrvr palaalrddl saaayltfye dgeirvveii
      121 dgpraprvdl wvgfedagha talgkcvlre ldgearddyl srhpladltp rtitgraell
      181 rrldttpltp avtdmeeyal gtfcvavpvy sgetlgslgv slradrvsri deirnrlipa
      241 asrvtrglsl ti
//
LOCUS       WP_457692842             139 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692842
VERSION     WP_457692842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15737
     Region          10..128
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mskpplpdaa vamlgkanpa vittlrsdgq pvstatwylw dhgrvlvnmd egrkrlthlr
       61 ndprvtvtvl degnwythls lighvaeird ddeltdidrl aqryldkpyp qrdrrrvsaw
      121 ieidrwhgwg glkdssqag
//
LOCUS       WP_457692844             297 aa            linear   BCT 27-JAN-2026
DEFINITION  Vgb family protein [Streptomyces nigrescens].
ACCESSION   WP_457692844
VERSION     WP_457692844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Korczynska,M., Mukhtar,T.A., Wright,G.D. and Berghuis,A.M.
  TITLE     Structural basis for streptogramin B resistance in Staphylococcus
            aureus by virginiamycin B lyase
  JOURNAL   Proc Natl Acad Sci U S A 104 (25), 10388-10393 (2007)
   PUBMED   17563376
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..297
                     /product="Vgb family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016835 - carbon-oxygen lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30955
     Region          2..266
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
ORIGIN      
        1 mprrapsfqq ipvsgaesgp yalttgpdga lwctlvhagq iarltpdgql drfaldsasc
       61 gpsvitsgpd galwftrnqd hrigritmtg eatsfplptp gsgpfgmvsa pdgalwftql
      121 hgdrigritt dgrvtefplp vsgafpsaia agpddalwft lnqahaigri sfdgeitlhp
      181 lpaensapvg itcggdgalw fveigagrig rittdgqide fplpdpasrp haivagpagd
      241 cwftewganr igsitpdgri eeydlpiass ephgltfgpd galyvaleig avvrlal
//
LOCUS       WP_457692850             304 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692850
VERSION     WP_457692850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32650
     Region          6..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mlkplhlltl kavvrsesfa laardlgyta saisqqisal eketglvlfe reahgirpta
       61 aahrlvdlst hvlaamddld hqvqelatga tgrlrlgsfp tadvrlvpsa lsalvethpr
      121 aqiqleeaep eelitalshg dldvalvyey glsprqwpag ltrhhllred llllrahgsg
      181 lgaqlsqlss arwitsredt agarsfvrlc aaagfeaava frsnnyavvr elvsaglgva
      241 vvpalghlps egveatrltq rsahrrvmal hrsensnpll pamlsclrra vpsgepylhp
      301 arad
//
LOCUS       WP_457692852             382 aa            linear   BCT 27-JAN-2026
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457692852
VERSION     WP_457692852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="Glu/Leu/Phe/Val family dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016639 - oxidoreductase activity, acting
                     on the CH-NH2 group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39656
     Region          13..377
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtdalslvde wgpektvvvs hrrtgmkgvl vidntargig kggtrmspgv tveevsrlar
       61 vmtwkwaavd lfyggakagi vadpaardke avlrafaral snevpreyvm gldmgltesd
      121 aaiiqdelgd rgaavgtpeh lggvaydklg vtgygvaeaa daaarhqglp lagsrvalqg
      181 fgavgsaaaq rfaelgativ avstahgvry dpsgldvgal ltardehgdh fvtrhsagta
      241 lpsgaeltvd cdilvpaalq dvitrgtahe ikaklivega nlptsadars ilaergitvl
      301 pdfvanaggv vaaafamdar ysgfrpgtsg ifesvsarlr antvtvldea rhqditphaa
      361 grrlaeervr tamqskgrip rg
//
LOCUS       WP_457692854             300 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692854
VERSION     WP_457692854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32066
     Region          33..263
                     /region_name="APH_ChoK_like_1"
                     /note="Uncharacterized bacterial proteins with similarity
                     to Aminoglycoside 3'-phosphotransferase and Choline
                     kinase; cd05155"
                     /db_xref="CDD:270704"
     Site            order(38,41..43,46,54,56,86,105..108,198,200,202..203,205,
                     215..216,219,234..235,238)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270704"
     Site            order(38,42,46,54,56,86,105..108,198,202..203,205,
                     215..216)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270704"
     Site            order(41..43,198,200,203,216,219,234..235,238)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270704"
ORIGIN      
        1 mcarkmhade adidvplvhr llaaqfprwa dlpvtvvdsa gtsnamfrlg tdmvvrlpri
       61 egaaqdvake hrwlprlaps lpaavpgplg kgtpaegypw pwsvyrwldg etpavghlaa
      121 prslaadlae fvsalhridp tdgppsyrse platrdgatr atvaaldgli dtdaaiagwe
      181 aalqapvwpg pavwihadlq pgnlltvrgr lgavidfgcl glgdpavdmi vawyllpada
      241 rgvfrtavga ddatwargrg walsialdel ryyretnpvm aaiarhviee vrteqahaaa
//
LOCUS       WP_457692861             318 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692861
VERSION     WP_457692861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  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 318)
  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 318)
  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..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /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=35013
     Region          <123..318
                     /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 mrhgmilavs fhddlhalav qhavrsrghd fhivecdtis grrslswrsh geeadgraga
       61 atvltsegvp vapeeaallw wrraradqei tgsagsther slvnndcrga lggilaatfh
      121 gdwisppaat dqaadklyql avaresgfrv prtlisqsrd dviaftrqvg rtivkpvvga
      181 rgpslytrrl ddpelipaps feicpatyqe yiegsrhirl ncfgdrmyaa liettaldwr
      241 pdlnvpispw pvpedlrrrv gtvlhqlglr mgivdlklsp egepvwlevn pqgqflflep
      301 ltgepltehf adfllsav
//
LOCUS       WP_457692862             519 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692862
VERSION     WP_457692862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56131
     Region          129..>315
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          406..503
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 msafrtprwp raalsgtaaa allsavlpta pparaadrsg apvparyahq qlnwqpctak
       61 pslecarmiv prdwhhpgtg adltvavsrh rateparrrg vlmmaaggpg asgltrpadf
      121 aarspavgav ydvvgfdqrg igsstpvrcq tdaefqdfya hdfrdrspaa lrgvidrsrq
      181 lvagclrrsg dlvpwltteq avrdmdlfra llgvrkisyy gpsyatwlga yyatefpqrv
      241 eravldsnld fsgtwqdveg gqprsfqrrf eqdflpwiar ydatyhygrt aaeakarwea
      301 rrralrdhpl tvgtltigpn qldnatlqni ydaqqqfpql asalsaldhw psatpaertl
      361 agkvfgsyls pgfaaaffsv tcndtpwrrd lghwirrsae dtaahplaga relayaatca
      421 swpvpaaprv rvtgkglptt lmlnsvhdpa tyyegalaah ralrgsrlvt vtgggdhgqy
      481 qngnacvdgi vnaylldgaa perdmacaag plpvpsgrg
//
LOCUS       WP_457692865             149 aa            linear   BCT 27-JAN-2026
DEFINITION  RrF2 family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692865
VERSION     WP_457692865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=15288
     Region          2..132
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrltkstdia lriamrlavl gdagdapttr evasavkvpy thaakvvskl qhlgavearr
       61 grggglalta agrtgslgrl vrelegvddv vgceddppcp lrggcrlrga lraaqeafya
      121 sldplsvael veaptgplll sltpapptd
//
LOCUS       WP_457692868             178 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692868
VERSION     WP_457692868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19037
     Region          <39..153
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtanlpstss avvrlarytr telseilgdg pdpfgvswag ltwlakeehf gikrdgrlva
       61 htglvtvpls igpletravg vggvavapdl rgqglarivm taaleharti gpqygllfcl
      121 phllplygrl gwqqlhedva veqpgdtttv mpletmwtpl cdgaqwpsgp vrlrslpm
//
LOCUS       WP_457692869             324 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692869
VERSION     WP_457692869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..324
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=34381
     Region          41..321
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mtpqttspag pnplphtaes pdalqspaal qspdalpspd rievlrysaf ttdpaggnpa
       61 gvvldaegld darmlavaae vgysetafvt ahdtaarryr lryfspraev afcghatiat
      121 avalasrtgt gellfetpag eirvgtsldg gllratltsv pahshpardt qvepvlralr
      181 wnrddldagl pphvafagnd hlvlavrsre qlaaldydfd alhaimrqhg wttvhlvhre
      241 aadrldfhar dpfpvggvve dpatgaaaaa fggylralgl vteplrvhir qgedmgrpsd
      301 lyvdlhpddp rvrvtgqavp lpap
//
LOCUS       WP_457692870             304 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692870
VERSION     WP_457692870.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32201
     Region          1..301
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdtrllrtfv tlaragsfta aaralhlaqs tvtvqirtle kelgtplfdr mpsgtvptra
       61 gqrlleeaed vldavarlra taaaatgqrd aeggtaegqv vvgsgdslcs arlpgviaal
      121 rqahpqldvq lhavstaaav dglrtgrldl alllepevae ndllarrias eplayvaapg
      181 hplagraagw delaqecffv heegcsysdr lvrtllglpg arpritrfgs idaarscvaa
      241 glgltllprv tverhlgegr ltvvegpeap pvpvqlvrhr rrwfapgari vaeemtrtfa
      301 atea
//
LOCUS       WP_457692875             226 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Streptomyces nigrescens].
ACCESSION   WP_457692875
VERSION     WP_457692875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24636
     Region          17..182
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mptdahpgrp nahpgplrvl vlgaslrags tnarlaslvg rmmtdadatv dlarmrefsm
       61 plydgdveet qglpdgalal rdrlewcdaf alsspeynas vpgvvknaid wvsrvrpqpf
      121 ktkhallvsa spslvggnrg lwalrvpleh lgtrvypdmf slaaahqgfs edgqltdsal
      181 qqrleetvta flrlveadar yvclqrrwye fpgdrtgapv tqraed
//
LOCUS       WP_457692876             749 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces nigrescens].
ACCESSION   WP_457692876
VERSION     WP_457692876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..749
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79940
     Region          1..749
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mttgatleav grpvdrvdgp akvtgrgrys aeitlpntay aalvgartas gritgirtda
       61 aeradgvlav lthqnlpkia grpsllpsla ghaapgesff plqddsvhyf gqpvamviad
      121 slerahfaar qlhvdydrsp svttldegrd qayepeaifa gflpartvrg dveagfkaat
      181 qrldatyhfa anhhnpieps attavwdgdr ltlydatqgi vatqstvaal lgippskvrv
      241 rasfvgggfg ckamiwphvt laalaarqvg rpvklaltre qmftscghre eqeqrielga
      301 tddgrltalr hhklsltspf dewaepslgm asqayacphy egiyrlirsn tmtptftrgp
      361 gettgmcale clmdelayqi gvdpvqlrlr nhaeadphtg hpwssdgaee cyrrgaarfd
      421 wqsrnpeprs qrdgnrligk gmatagypvl fpmqpqrara rlyadgtavv qagtqefgtg
      481 vgtamtqvaa dglgvalrnv rfeygdtdlp nvaaavgsag agmisaavyt aattlrdqmi
      541 eqaiadpgsp lhhadpatvv vregrmqlrd rpdngetysa lmqrhfmtdl dalgswsppp
      601 qnlpyglatf gaqfaevavd pdlgtvrvrr mvgafapgrv lnaktahsqa vggmlwglgq
      661 allegsvvdt rdgrwanasl geylvpvnad apdvavefve vpdtvvnplg vkglgevgmv
      721 gaaaaianav fhatgyrvre lpiriehll
//
LOCUS       WP_457692877             332 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692877
VERSION     WP_457692877.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35339
     Region          1..322
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mraisytrpt dvhsavaavt sdpgssflag gttevdllrl dvlrphrlvd inrlpltgve
       61 drsdggllig alarmsevae dravverfpm lsqalllgas aqlrhmasmg gnlmqrvrca
      121 yyrdpesacn krvpgsgcsa ldgvnrghai lgtsehciat hpsdlavalv aldavvhveg
      181 mdgtrtipvd dffllpgdtp erehpltpge litaievpal pmarrslylk vrdresyefa
      241 lasaaaalal engvirevrl alggvatkpw rarraedllv gqradedifv raaaaelspa
      301 vtrpmnafka elarrtlvra lrtaattggg ta
//
LOCUS       WP_457692878             178 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692878
VERSION     WP_457692878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18909
     Region          26..177
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 madkgapisv tqpstletrg pgsvnvaldv ngvsrvlnle prvslldalr eqmaltgskk
       61 gcdqgtcgac tvwvdgrrvl scltlaisce grdvttiegl aegdalhpmq raflehdafq
      121 cgyctpgqim savallnegh aetdgeiaew msgnicrcaa ypqirsaire mrdrktgq
//
LOCUS       WP_457692879             152 aa            linear   BCT 27-JAN-2026
DEFINITION  RrF2 family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692879
VERSION     WP_457692879.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=16120
     Region          2..141
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrisaradya vraalqlada rdagplkaea iaqaqdiphk flegilndmr rgglvqsrrg
       61 gnggyrlakp aeaisiadvi rvvdgplvsv rgvrppelsy tgparsllpl wialranvrq
      121 ildgvsladv asaelppqva eltenpdswt np
//
LOCUS       WP_457692883             236 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692883
VERSION     WP_457692883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..236
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24993
     Region          11..204
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mtteparttg pgsdgrrvph ralvvhrgpe tpraavlllh ggradgpgpp prlnlpalrm
       61 rpfgsamsre lrgrevllas vryrcrgwng pradaardar qaldelaarg adipvvlvgh
      121 smggraallt gghpavrgiv alapwcppde pvahlrdrtl vllhdaddrv tdaegswlla
      181 drarqagara htvamprggh tmlrgarhwh rltvdlvaal ldgtplpeaa ggirpg
//
LOCUS       WP_457692885             228 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692885
VERSION     WP_457692885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25232
     Region          11..214
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mghlkhrdln atrerlrdqv ahalraalis gelrpgevys apvlaedfgi satpvreaml
       61 dlareglvep vrnkgfrvte vnehdldqyt eiralieipm igritrsaar eelealrpva
      121 eeivraardh dligyleadr qfhlellgls gndrlvetvg elrkrsrlyg ltgldergel
      181 ipsaeehlel ldlmlagnak gaekcmakhl ghvrslwaks gttaksgk
//
LOCUS       WP_457692886             334 aa            linear   BCT 27-JAN-2026
DEFINITION  proline racemase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692886
VERSION     WP_457692886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Visser,W.F., Verhoeven-Duif,N.M. and de Koning,T.J.
  TITLE     Identification of a human trans-3-hydroxy-L-proline dehydratase,
            the first characterized member of a novel family of proline
            racemase-like enzymes
  JOURNAL   J Biol Chem 287 (26), 21654-21662 (2012)
   PUBMED   22528483
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Fisher,L.M., Albery,W.J. and Knowles,J.R.
  TITLE     Energetics of proline racemase: racemization of unlabeled proline
            in the unsaturated, saturated, and oversaturated regimes
  JOURNAL   Biochemistry 25 (9), 2529-2537 (1986)
   PUBMED   3755058
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="proline racemase family protein"
                     /GO_function="GO:0016855 - racemase and epimerase
                     activity, acting on amino acids and derivatives [Evidence
                     IEA]"
                     /calculated_mol_wt=35473
     Region          1..334
                     /region_name="PrdF"
                     /note="Proline racemase/hydroxyproline epimerase [Amino
                     acid transport and metabolism]; COG3938"
                     /db_xref="CDD:443139"
ORIGIN      
        1 mrtrhvfhav dshtegmptr vitggvgvip gatmaerrlh fiehldhlrt llmyeprghs
       61 amsgailqpp tradadfgvl yievsgllpm cghgtigvat vlvesgmvpv tepvtpvrld
      121 tpaglvavdv hvadgvaksv tltnvpafca aldrtvevpg ygrvtydlaf ggnfyafvel
      181 dalglpfdra rkddllaagl avmaainasp drpvhpeqpe iagvkhvyla apgsdahhsr
      241 hamaihpgwf drspcgtgts armaqlharg elpldrdfvn esfigtrftg rlvaetevgg
      301 lpavvptvtg rawitgtaqy fldpddpfpg gfll
//
LOCUS       WP_457692887             429 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457692887
VERSION     WP_457692887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46076
     Region          1..390
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mlgdliaash vvtmeqipdl vakhaakvgw ldvqiyladl qqvilcrlag yasgsgggve
       61 pasdvvrveg tlagrafqtg givagttset gqwwvpvldg terlgvlrat aapgtemdaq
      121 aaqdlrnlgg lvalmvvskr gvsdtyarlv rrrrmniaae mewrvmpprt fatdrvlisa
      181 vmepayevsg dvfdyaiaee tvhlalfdam ghdtaaglta nlalaasrnh rrqncgilei
      241 aeaveqalvk qfdanrfatg ilaelnaatg vltwtslghp lpviirrgrt tltlacspsp
      301 pmgtdlgvpp tlcrdqlepg drlllytdgi teardhkgee fglegftdfl iqhhadglpv
      361 petlrrlirr hlayhdgrle ddatvlllew sgptpyrpar vealaglpeh ttpatalpkp
      421 wmapgtetg
//
LOCUS       WP_457692889             389 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692889
VERSION     WP_457692889.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41074
     Region          24..375
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mssssrtvpp tadvvivggg vmgtsiafhl aeagvpnivv vergelgsgs sgkpiggvra
       61 qfsdplnial gsrslrawqd fprrpgadir ldsvgylfll tsdqqatdfe tgvhiqnsfg
      121 vpsrmigpre aqqlcpyvst dglvaaaysp idgharpgla vqgyaraaar agvvfaphta
      181 vtgidttgdr vtavhtdhgr iscstvicaa gawsarigem agvhlpvrpv rrqlafttpl
      241 appapripft idfastayfh nsddgllfgl adpaqadgfd ttwtpdwlel fraaarrrap
      301 aladmethdg waglyevtpd hnaligrsgt lsnflyatgf sghgflqapa vgeimrdihl
      361 drtpfvdvtp lsaerfttga etrpeahvv
//
LOCUS       WP_457692890             635 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 5 protein [Streptomyces nigrescens].
ACCESSION   WP_457692890
VERSION     WP_457692890.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Schroeder,H.R., Yeager,F.M., Boguslaski,R.C. and Vogelhut,P.O.
  TITLE     Immunoassay for serum thyroxine monitored by chemiluminescence
  JOURNAL   J Immunol Methods 25 (3), 275-282 (1979)
   PUBMED   762437
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..635
                     /product="glycoside hydrolase family 5 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=68548
     Region          101..423
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mclvltglav pganaapalp easapgpsaa gkaaeewtap lstrgryivd adgrrfrlks
       61 anwdgaqgsw ngsgdindpa ghhsgqnshg iplgldrvgi pallddfral glnsirlpfs
      121 nemirstarv pdaavaanpq lrgrtplqif davvaaltag gfavilnnht nttrwccgld
      181 gnerwnsrqs trqwaddwvf marryqhnsr vvgadlynev rrdilddpnw glgdrhdwqa
      241 aaqeaadril teanprlliv ieginwtglp vdglphgrpt ltpvrtlsht lvtsgklvys
      301 ahfygytgph hsgatgvget sdpryqdltr dqlrsvlhdq afyvsaetgr hftaplwise
      361 fgigseesgp aarawfgnlt dyladtdtdf aywplvgwst dgqgrpagdn wamlrydsag
      421 rrtgvldgdd wrapawhrlm tapqktgpvp ptpawhlltt dhrdfvqsln arslgdwdsg
      481 arkaacpdge rligishtrg rglctdapta rdlrapgsvp tvvrderyvp aggdwapghs
      541 klqcpdghfl tgyslrgekv saalctpart algtagstlw fdrgdnrppg dpggdfahgh
      601 fkgqcpshsy aaglaytsrl ghhgrpdall crplt
//
LOCUS       WP_457692892             254 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692892
VERSION     WP_457692892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27111
     Region          174..249
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mernlaehac hlhrsmtgaa vtetgdllva dsgldddtfn ivaaarftaa tapariteta
       61 rtlartgrrf swwtgpastp pdltarltaa glpasereta mwaelddtlp lpaaqgldiq
      121 mvatpeqlad yaavlaanwa ppadtvrrff aqavpqalaa hcpvrylvgy vegrpvcsae
      181 vfdhagvagi ynictlaahr rrgyggaitl galrtarehd hriavlqasa dgepvyrrlg
      241 frscgqfteh ainp
//
LOCUS       WP_457692893             563 aa            linear   BCT 27-JAN-2026
DEFINITION  BCCT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457692893
VERSION     WP_457692893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..563
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59643
     Region          15..522
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mtdlpdgpqe hgppqtdrvv fgvtalltla fiawgasste slknastsml nwvidnlgwa
       61 fvlsasafvi faiwlavsky gritlgkege epefrtvswv ammfsagmgi glmfygvsep
      121 lghfatpppg tdpqdaaqam dtamattlfh wtlhpwaiya vvglaiaysc frrgrrqtis
      181 avftpligtr rangwggrvi dilaifatlf gsaaslglga lqigsgikvl gwmdsvsttl
      241 lvgvitvlti afilsavsgi akgvqmlsni nmvlalilav fvfvvgptil ilnllptslg
      301 sfigelpqla grteagsgdd vggwlrswtv fywawwiswt pfvgmfiari srgrtirqfi
      361 ggvilvpsvv slvwfavfgg samklqeskq lsgsstpegq lfdvlhqypl atvtsvlvmi
      421 lvgiffvsga daasivmgtl sqkgtfeptr lvvifwgvvt gavaaimlli gggsgdaltg
      481 lqnltilvav pfmvvmiamc walmrdlrsd plivrgqkge eavelaviag heqydgdfef
      541 qigpggtgng dgedsgaevk sdg
//
LOCUS       WP_457692894             447 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457692894
VERSION     WP_457692894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 447)
  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 10154696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..447
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48307
     Region          103..327
                     /region_name="M14-like"
                     /note="Peptidase M14-like domain; uncharacterized
                     subgroup; cd06242"
                     /db_xref="CDD:349461"
     Site            order(113,116,163,172..173,202..203,208,294)
                     /site_type="active"
                     /db_xref="CDD:349461"
ORIGIN      
        1 miprsrrlav gplaigltat lganppaapa aptatpaprt gfetshgarw tgqaeeqdfl
       61 ravdrgsvrv ridrigttgq grpvqlvrig apapdrpakv rrgnsvllic sqhgdepsgr
      121 eaclttvrnl ayakdaatrr flahtsvlvv ptanpdgraa dtrgnadgtd inrdhialrt
      181 aegramaavi rdyhpdtiyd lheygptvpy ymkdvlslwp rnlntsdgvh reagslsqdf
      241 vrpavhragf stgvygiwtd petgdpvkqv agdgqerilr ntagvkgsvg llvetrvdal
      301 tdaekadppl nnrrrvdsql aaldgaftff drhrsrieaa ttaarlagya dhgpvylgga
      361 dnepatdaqi lahppcayrl derqfaqvre elvrhgvvwr rdrdgvvvpl rqplrklvpl
      421 lldqragyhl tvatplnvcr rvvggng
//
LOCUS       WP_457692895             495 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457692895
VERSION     WP_457692895.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..495
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53869
     Region          46..456
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(154,156..157,290..294,314,317..318,321,336,340,395)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mrhrllvpga aalslllaip asaadftpga pgvgdtyype sgnggydvsh ydlrlkyqpk
       61 tdllegtatl latttqdlsr fnldfglkvs eiringkkas ftssgkhele vtpaaplekg
      121 kqisvvvrya gkpselkidg ysawartpdg gvvaqepdaa vwwfpsndhp tdkatydisv
      181 avpdgtqals ngvlasqssk lgwtrynwrs dkpqatyltt lavgkfdltt dktanglpvi
      241 navskdlgan agsarasier tteitewles vfgpypfnav ggyvpnvpag yaletqtrpf
      301 ygkkafdrgt nvsvvvhela hqwygdnvsl kdwkdiwine gfatysqwlw sekegegttq
      361 eladwvysqh paddpfwtvk pgnpgaenqf dgavydrgal tlqalrnkvg dkvffgilks
      421 wqtenkygna svadfvkfae kksgkelagf fdtwlfqpsk ptagaarqal garqapvaep
      481 kswkqiaath dvhkh
//
LOCUS       WP_457692896             283 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces nigrescens].
ACCESSION   WP_457692896
VERSION     WP_457692896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10007665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32174
     Region          7..273
                     /region_name="COG3662"
                     /note="Uncharacterized conserved protein, DUF2236 family
                     [Function unknown]"
                     /db_xref="CDD:442879"
ORIGIN      
        1 mnavkndpkp ppvggvlwsl agdirmlltl ppalamqvah pavgagvddh svfrtdpwgr
       61 gersltslql wvyggeaaaa egrrlralhr tiqgtdahgr ayhaltpayy awvhatgypv
      121 frhaqhylgr pfteaqerql yaewlqvgrv lgihdrdmpq tieefwpyyq kvldneleet
      181 vvvkellatd pplpapdrgp rwlrlllrls wpwlrprfar vrrfvtiglm ppdarqaigl
      241 ewtdaqerrl rrlgrvvrav vpvlperlrf mpiarrarqa arg
//
LOCUS       WP_457692902             424 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457692902
VERSION     WP_457692902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 424)
  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 424)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=44932
     Region          48..197
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          175..415
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfdnpraags racvavgrcq laslhaiavs avgslvvlal llvpvgvgfr llppaaralr
       61 vlsdrsrara drwtgvrigp peplpgdrsl narkrsgaii adegfwrdla wawlepvvgg
      121 llvavplalv eygafgalvq pfiwrliddg nwyafvpvhs tatmcaalvl glafmavgll
      181 aapatlrlht rvsrpllsas rssrlaqrve rltdtraral daqaaelrri ernlhdgaqa
      241 rlvalgmtld ratrlmetdp aaarellldv rrtsegalqd lrelvhgihp pvladrglgd
      301 avrslaldsf ldvhvetrlp gqlpapvesa ayfavseala naakhsgare vgvalsyeng
      361 llratvtddg hggadpsrgt glagvrrrld tfdgtldlhs pqggpttvml eipcalsspk
      421 tsss
//
LOCUS       WP_457692903             275 aa            linear   BCT 27-JAN-2026
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptomyces
            nigrescens].
ACCESSION   WP_457692903
VERSION     WP_457692903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=28312
     Region          122..224
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 maagppggiv damrrksvdi ramalfltva flaagalgal qpatrisgev iqltqfgpal
       61 gvglaallwp grvrellagp vpgrsgrgvl llvtapaiia lsvlaytalt gdahptrpga
      121 pfvliavaql igacgeeigw rcflqpllrt rcgplaasvt vgvawgvwhv qifarhpvya
      181 gafimaavsm svvmgwaleg vrasrlllag gfhalinlgm llfmdeesga vlpmvlfgas
      241 claaaglwtw lslgrlrsag asapakippv mddvr
//
LOCUS       WP_457692910             130 aa            linear   BCT 27-JAN-2026
DEFINITION  MmcQ/YjbR family DNA-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692910
VERSION     WP_457692910.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..130
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13779
     Region          15..127
                     /region_name="MmcQ"
                     /note="Predicted DNA-binding protein with #double-wing#
                     structural motif, MmcQ/YjbR family [Transcription];
                     COG2315"
                     /db_xref="CDD:441889"
ORIGIN      
        1 meermakaag paavrervra falglpgave efpwgesvik vnkkvfvflg vddgsyplgv
       61 tmklkdpeah ahaltspgar pagyglgksg wvqvpleepd appaellcdw aeesyrviap
      121 kkliaeldga
//
LOCUS       WP_457692905             618 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457692905
VERSION     WP_457692905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..618
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66953
     Region          11..617
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mttllrmpge pdeltlpall lrnaedhgel palswrgtge grwrtlswae vrrrvaelaa
       61 gfrslgvrrg eivllmmgnr pehwlsdlal vhlgavpvtv ygtaapgqia hivrhsrarf
      121 avlegarelg rwepllddat trldklvive tdetdeadea hatgaagrhq tyaalagrga
      181 elydpaafee awrqvaaadt ltvvytsgtt gdpkgvvish rnvllnapal davvelpdhv
      241 ehlcylpfah iaermlgiyl pvfrashvyl cadpaavapt vrelrpaqff gvprvwekla
      301 aavragcaql peerraavda agetvrayia cqergerpsd eladacarar aevldpllap
      361 agfdrlvwta sasapmppdv vrfwaglgiv imdawgltet tgvcttngpg gfrlgsvgrp
      421 iggmevrtaa dgeievrgrt vcegylradg svepatdadg wfatgdlgrv dedgflwltd
      481 rkkemivtst gknvspalve ntlkehplvg qalvhgdgrs ylvallvlda epaaawaarh
      541 giegtmqela ghpdvraeve ravteankhl nrseqvkkfs llgeewspes geltpslklr
      601 rreihhkygq ildglytl
//
LOCUS       WP_457692909             395 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692909
VERSION     WP_457692909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40887
     Region          3..366
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 maepgngpls gvrvvelagi gpgpfaamll adlgadvvrv drpggaglgi dpayditnrn
       61 krsvlvdlks pdgvaqvlel veradvlveg yrpgvaerlg vgpekclarn prlvygrmtg
      121 wgqegpladt aghdigyiai tgalgmigpp dgppavpanl lgdyaggsly lvigvlaalq
      181 harteggkgq vvdaaivdgt ahltamihgm laaggwqdrr ganlldggtp fygayetadg
      241 gymavgalek rfygefirll giegeapsrd dlaawgelrt viaarfktrt reewtgvfee
      301 sdacvapvls lreaprhphl aargtfvehg gitqpapapr fshtpgavrr ppaspgadte
      361 eiardwqapg llapspaapa ppagpsrteq kdtag
//
LOCUS       WP_457692904             486 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457692904
VERSION     WP_457692904.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..486
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51569
     Region          19..474
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mstetvteta hrspdggrst qqdagdagys kglkgrhvnm iaiggaigtg lflgaggrlh
       61 sagpalaiay avcglfaffv vralgelvlh rpssgsfvsy areflgekga yvagwmyvvn
      121 wsttgiadit aialythyws lftdipqwvm alialavvlt vnlisvkifg elefwfaiik
      181 vaalvvfmfi gifllatqhp vgghtpgldl ltdhgglfpt gllpvvivlq gvvfaysave
      241 lvgvtagetd epekvvpkav nsimwrvgvf yvgsvillam llpwnkyvsg espfvtvlsn
      301 vgvpaagdvm nlvvltaams slnsglystg rilrsmsmag sapkfaglmn rnqvpyggim
      361 ltsavcvlgv glnyvmpgea feivlniaal giistwctim vchmvfvrrs keglvdrprf
      421 rlpgtpvtdi vtiafllgvi vlmwfdggvg rqtvllipvl aialvggwfa vrgrvsriaa
      481 erelsk
//
LOCUS       WP_457692911             395 aa            linear   BCT 27-JAN-2026
DEFINITION  saccharopine dehydrogenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692911
VERSION     WP_457692911.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41630
     Region          7..395
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mprqdtsgra ydlvlygatg ftgaltaayl aahapkgcrw alagrstarl eqlrdrlaks
       61 dpacadlpll radssdpgsl rglaadtrvl vttvgpylih geplvaacaa agtdyvdlsg
      121 esefidrmyv rhdatarasg arlvhacgfd svpydlgvry tvgllpegvp vridgfvrtn
      181 atfsggtlas altaasrpva maraarerqr veprpagrtv hapfgppirs getrtwgvpl
      241 ptldpqiiar savaldrygp dfryrhyagv rrlpvavgga lgagalcala qvpparrwls
      301 grlepgdgpg perrarswfk vrfvasggdt rlitevsggd pgydetakml aesalslafd
      361 dlpetagqvt tavamgealt arlqeagikf gvvre
//
LOCUS       WP_457692912             234 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease V [Streptomyces nigrescens].
ACCESSION   WP_457692912
VERSION     WP_457692912.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..234
                     /product="endonuclease V"
                     /EC_number="3.1.21.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003727 - single-stranded RNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=25012
     Region          16..234
                     /region_name="Nfi"
                     /note="Deoxyinosine 3'-endonuclease (endonuclease V)
                     [Replication, recombination and repair]; COG1515"
                     /db_xref="CDD:441124"
ORIGIN      
        1 mdtpgmiscd delrhwptde aqaravqdrl rpcvrldeag pepgfegtvv gvdvaydder
       61 dvvaaaaval dartravvdr atavgqisfp yvpgllafre iptvldalgr lartpdlvvc
      121 dgyglahprr fglashlgvl tglptigvak npftfryvpp gpergatspl ldgteevgra
      181 lrtqkgvkpv fvsvghrtdl dracahtlhl aadyrlpett raadtlcrra lada
//
LOCUS       WP_457692916             301 aa            linear   BCT 27-JAN-2026
DEFINITION  SIS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692916
VERSION     WP_457692916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32174
     Region          8..296
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 msetsymeqe lcsqpetwrq aarigaaagp lpkagqrvav vgcgtswfma qsyaalreaa
       61 gqgvtdpfaa seaflgsdrg ydavvaitrs gtttevlrvl davkgriptv tilgdpetpa
      121 valsdetvkl pfadeksvvq trfatsaltl lrahlgedts ravtdaeeal aapmekewvd
      181 aeqfsflgsg wtfglaneaa lkmreasqsw tesypameyr hgpiaiaapg rvtwlfgqap
      241 egleadvvrt garfvhhard pladlvlvqr valerararg ldpdnprslt rsvmletpaa
      301 s
//
LOCUS       WP_457692917             293 aa            linear   BCT 27-JAN-2026
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces nigrescens].
ACCESSION   WP_457692917
VERSION     WP_457692917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=30284
     Region          23..259
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplvptssiv daarearaga aafnvihlet aealvtaaer tgvplilqis enciryhgsl
       61 lpltratlal aedstariav hldhitdadl vhqgitagvg svmvdasalp yeenvattae
      121 laawchdrga yveaelgevg gkdgvhapgv rtdpdealaf vratgvdala vavgsshamh
      181 ertavldkdl iaalhttlpv plvlhgssgv pddelrraia agmtkinist hlvsvfthsi
      241 rqtlgadpal vdsrkyikpa reavaeeaar llgvlgtpat vpgqhaaqap arg
//
LOCUS       WP_457692918             267 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692918
VERSION     WP_457692918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..267
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28639
     Region          1..261
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mkrhermnal lellgdrgrv dveeaatale vsaatmrrdm dalaeqqllt rtrggavlss
       61 vaydlpiryk hahrsaekea vakaaaklve rgdvvglsgg ttttaiarvl atrpdfaeag
      121 pqphltivtn slnianelav rpqikivltg gvahsrsfel vgpfselvlq qisidiafig
      181 angmdpmmga tvhdeaearv nrlmaerarr avvvadsski gercfarvgd advfdtfitd
      241 ngakeatrre fadrglkvvt arpsade
//
LOCUS       WP_457692921             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692921
VERSION     WP_457692921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22809
     Region          14..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpaakkkttt asasperrre lltiaaevfa ahgynattvr riadeagmla gslyyhfesk
       61 esmldeilss fltelwdgyd avlaaglgpr etiealvtes freidrhraa vaiyqkeskh
      121 laaqprfgyl adsqhkfkka wlgtlergva dgafradldi rltyrfvrdt vwvaaswyrp
      181 ggqhspeeia rqylsmvldg iavra
//
LOCUS       WP_457692923             168 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457692923
VERSION     WP_457692923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18656
     Region          21..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtedivagvl rqwqqvhpgl dtgpmavigr lnrcsallqq asdaplrrag ltrpefdilg
       61 tlrrmdrelt pgrvaretfa sgaavtkrvr qleerglivr rpddrdrrvs hlsltdegrd
      121 tidrllpeql ryeaslldgi gdqrqeelst algellvvle grlgslld
//
LOCUS       WP_457692926             230 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692926
VERSION     WP_457692926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..230
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25002
     Region          2..200
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkkvdhear rqeisealwr iagsrglegt slrdvaaeag islgrlqhyf rtrdemllfa
       61 lqhinrlaad rireriaala eeptprevlr aclsgmlpld ersrvgllvg aayyaravhd
      121 ealraeakng ipqlraffad qlrlaadrge lpperatede amllismteg latyvlldvh
      181 gpetalrlld lylenffgae rsaeggaera agngagrate tpapsgpvap
//
LOCUS       WP_457692927             172 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692927
VERSION     WP_457692927.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18660
     Region          16..164
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 mpehaapllr pprhrvdpra rrwwtlqall tlsgpmllta ltmavlsllf fpgalpwlgp
       61 lllavlvlpa lgylivmprw ryavhawelg gqavyaaggw fwqkrriapl srvqtvdtvr
      121 gplqrrygla tvtvttasta gdikiaglsd adaeelarri geaaqdvpgd aa
//
LOCUS       WP_457692928             548 aa            linear   BCT 27-JAN-2026
DEFINITION  PH domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692928
VERSION     WP_457692928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..548
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58279
     Region          34..517
                     /region_name="YdbT"
                     /note="Uncharacterized membrane protein YdbT, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3428"
                     /db_xref="CDD:442654"
ORIGIN      
        1 mstprepgap dippgasags gpaappdapv eetpwrrldp rtllvhcgwm aapfgslalt
       61 alatggrint eswitlaait asfavvttlg lirwartdfr itvpqhrdgp gggasptfdv
      121 rtglltrrlr svplhrirtv dltatpvhrv lgvtvlragt agsgdgrsel slealtvpea
      181 erlraellay adaeavandp vvarinwrwl ryapltfwvi ggvfvvagga yraldgigie
      241 awklgfvqra faefgagalw ltipaallvi lalgsvgavv lyienwwnyc lewtdartlr
      301 vrrgllttra vtierarlrg vmlreplllr agggalvrav agglgnreen qkrsgllppa
      361 praqalrvag galrspfpgs aapaeltphp rvalrrrrvr gllfvvlpgt avlaglgaaf
      421 tpvllhcawi yavvttamsl wlardayrnl ghglhgpylv arsgtfsrdt valqrdaiaa
      481 wtfstspftr raglvtltaa vaagedgyri pdlpagdapa fattaapgil deflvhpgpe
      541 hlpgqrlr
//
LOCUS       WP_457692930             255 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692930
VERSION     WP_457692930.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27085
     Region          73..244
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(74..77,127..132,167,169..170,191,197..198,221,223)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(76..77,127,131,169..171,191,221,223)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 margfgkegg iigvaaaavv alaaagtlvf sgagtdssaa daakqpkkap rvvapvdpri
       61 ehasdrpgrs lnitiddgpd pvwtpkvlev lkqqdvkavf cmigpqakah pdlvkqvvaa
      121 ghklcdhtms hntgmdhesq syqkqqilda qkmiedaagg aqveyyrapg gaftpysrkl
      181 aadrgmrplg wnvdskdfeg gtvemieatv rgelangptv lfhdgggdrs rtvevlerll
      241 pwmkqqgygf gfpkr
//
LOCUS       WP_457692940             169 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457692940
VERSION     WP_457692940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..169
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17566
     Region          35..167
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtthpaetvh dalreepced awwapapdgf aacalsgsar tvpearrftr atlegwqvca
       61 gladdavlvv selvsnalrh glqgpgpgge gtaapapfcn awlaltrqat tvlcavsdag
      121 pgapvirtqd alaesgrglh ivdrlsdswg wtppdrsgkt vwatmslrg
//
LOCUS       WP_457692942             302 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692942
VERSION     WP_457692942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33472
     Region          30..90
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,39,64)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(38,63)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(45..46,57,60,64..65)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          116..296
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msaaqpssgp slrryldhpr ggptvlrivl gtqlrrlreg agitreaagd airgshakis
       61 rlelgrvsck erdvadlltl ynvtdeavra dflklarrts spgwwhqygd vlpgwfethi
      121 gleeaasvir tyevqfvpgl lqtpdyarav aqlghprsss eeierrvqlr vqrqelltip
      181 daprvwavid easlrrplgg pevmadqlrh llkmtelpnv tlqiapfslg glaaaggpit
      241 ilrflepdlp divyleqlts alyldkrddv dhylavmdrl saqsespres vailerllkq
      301 eg
//
LOCUS       WP_457692944             215 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692944
VERSION     WP_457692944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23564
     Region          16..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdtrrrrip rpvreqliid aaigvfakrg yhassvdeia elagiskpmv ylyldskegl
       61 flaclrreae rlvaafraaa gpapspelrl ragllafftf vtehpdswvv lhrqaselsp
      121 aiaaelaqtr ravltevsgl vricgaestg parpedeadf vaytlvgaad sltdwmvlhp
      181 depperitvr lmnmvwvgmr nvldgevwtt paeeg
//
LOCUS       WP_457692946             440 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692946
VERSION     WP_457692946.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46963
     Region          <297..435
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 metsttvpes aaalhagida ltdevidglr aqlpsyaavs agrlrprvma slrnglslvq
       61 rwaeerrtar gtgrddgpay gipathldev tslarslpve diisayrigt divwrrfgee
      121 mtarggtaed llpiaetlra wvdantlriv rscrvglqgd dpaadrrhaa mvralllgea
      181 rwdtspagfg gwgagftgeg padgyrterq addaeavdgs yehsalrlpf rarlpdaspp
      241 gapaatghag pgdrdfrrtv dllrpwlald eagrplvttv dgdvagllvg rpaglcrsli
      301 lglgapapas glateftrat qalraaagfg lvgaftreel glratvvalp avgeqlvrlr
      361 laplaerged gaqleeaaaa ylrqglrlea aartlyvhpn tlrnrlrrfe eitgtnlrdp
      421 adlaevwwal thrrfhgpts
//
LOCUS       WP_457692950             527 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457692950
VERSION     WP_457692950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..527
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55999
     Region          29..502
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mvrvtgpetp rpgtradgsh dddaiaelgy kpelkrtlgn fhtfaagisy isiltgtfql
       61 fyfgiahggp aywwswpmvf agqlmvalcf celaarypva gsvynwakkl ggphigwlgg
      121 wmmvtatmvs lsavalayqv tlpqisswfq figdgtgksa aenavllgtv litfttlvna
      181 fgvklmarin sagvaielia aivlilllaa hvtrgpgvvt dtfglgkges lgyfgaflta
      241 slasayvmyg fdtasslgee skdpgrnapr ailralvasf ligglillfa llavpnlqae
      301 qlkvdglqyv vlstlgstvg qivlwcvvia itvcelavht agirlafama rdnnlpaasl
      361 lakvsprfqt pvlpavvigl vavgilvinv nqpqifsvit siaiimiyla ylsvtlpmli
      421 qrlrgnwtpa kgkfslgrfg ipvnilavlw giamslnlaw praavynatg pqhwylrwga
      481 flfigvvaig gfayywfvqr krtgvlamha avhpgdgtpg dagtptp
//
LOCUS       WP_457692951             520 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692951
VERSION     WP_457692951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56685
     Region          8..518
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mpeeapvdef dyvvvgggta gavvaarlse dptvtvclle agpsdagden vlrldrwmgl
       61 lesgydwdyp vepqengnsf lrharakvlg gcsshnscia fwapaedlde waamgctgws
      121 aadcfplyqr lenndapgdh hgrngpvvlr tvppqdpcgv alleacaaag iptapfntgq
      181 tvirganwfq incrpdgtrs sasvsylhpv mgtrnnlevr tglqarrlnf dsvrhctgvd
      241 ylapdlihtr tvnarretvv scgsidspkl lmlsgigpat hlratgieai vdspgvgsnl
      301 qdhpegvimw dakqpmvrss tqwweigifa dtepgldrpd lmfhygqvpf dmntyrrgyp
      361 tsenafcltp nvtrarslgt vrlrtrdfrd kpkvdpryft dehdqrvmvh glrlareiis
      421 qspmadwagt elapgpsahs dtelleyirt thntvyhpsc tvrmgaaddq atpldpqlrv
      481 kgvtglrvad gsvmpflpav npcittmmig ekcadmmrsg
//
LOCUS       WP_457692957             147 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457692957
VERSION     WP_457692957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15785
     Region          18..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 madtpyapsr iralpswllg raaarghrlv adalaaegmr mmhhavlsav aelgavsqae
       61 lgrtlaidpk dmvaivndlq kdglvtrtpd pkdrrknave isadgrrrlr rtqqlgdqan
      121 aeltaaltpa ereqliallt rialpea
//
LOCUS       WP_457692945             290 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692945
VERSION     WP_457692945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31497
     Region          47..175
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtmnksevtp lpgipptaee mvlanqanwd artpihvase fygldgsrta edwfapfewt
       61 dlgeltgrdv lhlqchlgte taafaergaa htvgldfsaa avaearrlae eagrtmefvq
      121 advhrapeal garrfdvvyt gkgalcylpd ltawagivss llrpggtfyl vefhplldsl
      181 gpaggpdqqe lrlrndylgg rgplrsdtpc tytdgppvqg attsyewrhg lgevisavig
      241 agmtvelvre tellpwkrfd amvpgengww rlppsepivp llyalravkn
//
LOCUS       WP_457692958             314 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692958
VERSION     WP_457692958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  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 314)
  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..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /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=32095
     Region          1..314
                     /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 mrrvrfhsyg gpevlcieet aeepvpgpge llvrteaigv tlpcvrrvrg dgngggdplp
       61 ampggeiagt vvalgpdvtg fapgdrvtsl tltgsytela lapaflasri pegasaveav
      121 alvrsghval aalstaaprg aesvlitgaa sgtghlavql aklqgvprvv aavssaakae
      181 flrglgadev vtydqeswga pvdivldgvg gellpralaa aapggrliff nsgggtvpay
      241 ellagaktit gltmrhfstv hrelyeehra qlwelagsgr lraavhaelp ldeaakahqi
      301 iegranlgkv vlrp
//
LOCUS       WP_457692960             367 aa            linear   BCT 27-JAN-2026
DEFINITION  bile acid:sodium symporter family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692960
VERSION     WP_457692960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Claro da Silva,T., Polli,J.E. and Swaan,P.W.
  TITLE     The solute carrier family 10 (SLC10): beyond bile acid transport
  JOURNAL   Mol Aspects Med 34 (2-3), 252-269 (2013)
   PUBMED   23506869
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Doring,B., Lutteke,T., Geyer,J. and Petzinger,E.
  TITLE     The SLC10 carrier family: transport functions and molecular
            structure
  JOURNAL   Curr Top Membr 70, 105-168 (2012)
   PUBMED   23177985
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Hagenbuch,B., Stieger,B., Foguet,M., Lubbert,H. and Meier,P.J.
  TITLE     Functional expression cloning and characterization of the
            hepatocyte Na+/bile acid cotransport system
  JOURNAL   Proc Natl Acad Sci U S A 88 (23), 10629-10633 (1991)
   PUBMED   1961729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="bile acid:sodium symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=37302
     Region          19..321
                     /region_name="SBF_like"
                     /note="SBF-like CPA transporter family (DUF4137);
                     pfam13593"
                     /db_xref="CDD:433336"
ORIGIN      
        1 mrrpplpklp srlpvdgcil alvgtvalaa llpargpaat aaegastgav gllfflygar
       61 lstreamdgm rhwrlhltvl actfvvfpvl glaarglvpq vlpptlytgl lflclvpstv
      121 qssiaftsia rgnvaaaica gsfsslvgiv vtpllaglvl hgdgggfsag slvsivcqll
      181 lpflagqllr rwvgswlirh kkalgyvdrg silivvyaaf sagmvqgiwh qvsalrllcl
      241 lgveavllav mlsatwygsk klgfhradri aitfagskks lasglpmasv lfgaqaglaa
      301 lplmvfhqmq lmvcavlakr faasaasaas aasaasaape aavagttags gavtaaagdv
      361 vaggarr
//
LOCUS       WP_457692961             287 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692961
VERSION     WP_457692961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31532
     Region          6..279
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mfepaqlrtf lavaqtlsft qaahrlglrq stvsqhvrkl eeaagrrlfa rdthgvelte
       61 dgeamlgfar tileaneraa sffagtrlrg rlrfgasedf vltrmpevle efrrdhpevd
      121 leltvelsgt lhellaagrl dlvlakrrpe dsrgrlvwrd rlvwvgaerl rldpqrpvpl
      181 vvypppaltr aralealera grewriacts gslngliaat raglgvmaht rgmippglvr
      241 ippraglpel ggvdfvllyg qrdraargpa ealadailag gdrlqlp
//
LOCUS       WP_457692962             608 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457692962
VERSION     WP_457692962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..608
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66192
     Region          1..607
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mreftvppla taprvgglad avyehaeadp drvalarkdd agdwqnvtsg qfrdeviala
       61 kgllaqgvrf gdrvgimsrt ryewalfdfa lwsigvqsvp lyptssaeqv fwmlhnadvs
      121 aclvehedha mtvgsvidrl pqlrklwqld adpvaeltaa gahidddvvh rhrmavtpda
      181 tatiiytsgt tgrpkgclit hanfmaesdn ivlryesvfh skpgdeaatl lflplahvfg
      241 rmvqvaairg rvklahqpel aarallpdlq tfqptfilav pyifekvfaa arrraeadgk
      301 vgpfdkavev avryaeaqeh kafgtgsgps aslrmqhqff dkvvyskvra amggrvrham
      361 sggsamerrl glffagagvr ifegygltes taaatanppe rtrfgtvgtp vpgttvhiae
      421 dgeiwlyggq vfhgyhndpk atdavlhdgw fstgdlgald edgyltitgr kkeilvtsgg
      481 ktvspvglee rvrahplvaq civvgndrpf iaalvtldpe avahwlamrd kpempasdlv
      541 rdpdleteir ravvaantlv sqaesirtfr ilanqfseeh glltpslklk rkaietayta
      601 evdalyqt
//
LOCUS       WP_457692964             277 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457692964
VERSION     WP_457692964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29980
     Region          11..272
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mskvpsikln ngvampqlgf gvwqvedeqa fsavgqalda gyrsidtaai ygneegtgka
       61 laasgidrde lfvttklwns dqgydstlra fdtslaklgl eyvdlylihw plpsrdtyie
      121 tykaveklya dgrakaigvs nflpehlerl lgetsvvpav nqielhpqfq qaasravhar
      181 hnivteawsp lgqgkglled ptiaelaakh gktpaqvvlr whlqlgnvvi pksvtpsria
      241 enidvfdfel ddadltalag ldsgnrlgpd patfdmg
//
LOCUS       WP_457692966             298 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692966
VERSION     WP_457692966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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 298)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31692
     Region          58..162
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msnpdrpgpg hhhphdsahp dwealgpvle rgaelytply eqvaawlrep atgpggvrrv
       61 ldigsgpgvv scllarafpd aeviavdate allerardra grlglgdrvh thpaelpdgl
      121 dalggadliw sskalhhvgd qraavaalag hlrpggllai aegglaprfl prdlgigrpg
      181 lqsrldaage ewftemraal pdaadetedw pafladaglr tprtrsflld lpaplsadar
      241 ayvvatlsra rdmygdrfde ddlatlarlt dpedaagitr rpdafflsaq tvhtaraq
//
LOCUS       WP_457692967             459 aa            linear   BCT 27-JAN-2026
DEFINITION  cryptochrome/photolyase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692967
VERSION     WP_457692967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vechtomova,Y.L., Telegina,T.A. and Kritsky,M.S.
  TITLE     Evolution of Proteins of the DNA Photolyase/Cryptochrome Family
  JOURNAL   Biochemistry (Mosc) 85 (Suppl 1), S131-S153 (2020)
   PUBMED   32087057
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Kavakli,I.H., Ozturk,N. and Gul,S.
  TITLE     DNA repair by photolyases
  JOURNAL   Adv Protein Chem Struct Biol 115, 1-19 (2019)
   PUBMED   30798929
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Konig,S., Juhas,M., Jager,S., Kottke,T. and Buchel,C.
  TITLE     The cryptochrome-photolyase protein family in diatoms
  JOURNAL   J Plant Physiol 217, 15-19 (2017)
   PUBMED   28720252
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Hitomi,K., Okamoto,K., Daiyasu,H., Miyashita,H., Iwai,S., Toh,H.,
            Ishiura,M. and Todo,T.
  TITLE     Bacterial cryptochrome and photolyase: characterization of two
            photolyase-like genes of Synechocystis sp. PCC6803
  JOURNAL   Nucleic Acids Res 28 (12), 2353-2362 (2000)
   PUBMED   10871367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="cryptochrome/photolyase family protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003913 - DNA photolyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=49950
     Region          1..456
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mdvalclfss dlrlhdqpvl hgalraaaqv vplfvvdagi adagfmvpnr aafladalad
       61 ldaglrergg rlvirtgdvv tetcrvaaet gageahlaag vsgyalrrer rlgaelaaag
      121 rslvvhdavi talppgavlp sgpgkdhfav ftpyfrrwqa agrrsvlpap rsvqvpaevr
      181 sedlpsaqvl cpdgapspal peggeragrr rfgawqrsgm adyqdrqddl pgdatsrlsp
      241 ylhfgclspl elvhkasgrs dagaeafvrq lawrdfhhqv laarpdaara dyrtkgdhwr
      301 hdgaevtawk egrtgypvvd agmrqllheg wlhnrarmlv asfltktlyv dwrvgarhfl
      361 dllvdgdman nqlnwqwvag tgtdtrpnrv lnplvqarrf dpegayvrrw vpelaglaga
      421 avhqpwklsg persaydypd pvvdladalv rfkrargle
//
LOCUS       WP_457692968             314 aa            linear   BCT 27-JAN-2026
DEFINITION  YihY/virulence factor BrkB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692968
VERSION     WP_457692968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33391
     Region          25..304
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mggsgmrrel drtqldralg aagprqpaal ptwaqcrtal rrtplsvwhd dvtdwaaslt
       61 yysvlallps livtvsligl adppateqli hqisslapae agptvhralv gmaqqqtaaw
      121 vvvggalvsa lwsscsylav frralhamhr tkddrppwrk aprilctall lmallissav
      181 allvsgpiat algravglge ageatwnvlk wplllllatv lamvlfrsgp ptsrgvrraa
      241 pggvvavllw lissagfaly asyvgtfnrl ygslagpvvf liwlwfshls llsgaqfnve
      301 laragrvvrp rtgs
//
LOCUS       WP_457692971             145 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692971
VERSION     WP_457692971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 145)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15844
     Region          5..126
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04669"
                     /db_xref="CDD:467553"
ORIGIN      
        1 mnervravlv tadetmlvir rskpgvpvyw vlpgggveah desreaalhr eiheeiagka
       61 diicllhtle aederqlfyl ariatwsfed rtgpefsaeg rgeyaleevp ltvegidgid
      121 lkpeeiahvl rgaiadgtla dvtta
//
LOCUS       WP_457692972             263 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457692972
VERSION     WP_457692972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27744
     Region          14..262
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mplpllevpl qarplqgrta lvtggatgig aeigralaaa gavvainhlg qereaqalla
       61 afdrggslgv ainadltdpd avhamtdrvr aeagpidilv nnagayprvp wqdtdedawk
      121 ysldvnltah yrachavtpc mverrwgriv nigsvnarag rtnlvaysta kagllgltrs
      181 larelgrygv cvntvlpgai qveaetvipa rhranpkdqi nrqcvprrgr pedvaalvaf
      241 lvgptasfit gqsvhvdggw llh
//
LOCUS       WP_457692979             179 aa            linear   BCT 27-JAN-2026
DEFINITION  lamin tail domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457692979
VERSION     WP_457692979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Eldirany,S.A., Lomakin,I.B., Ho,M. and Bunick,C.G.
  TITLE     Recent insight into intermediate filament structure
  JOURNAL   Curr Opin Cell Biol 68, 132-143 (2021)
   PUBMED   33190098
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Dittmer,T.A. and Misteli,T.
  TITLE     The lamin protein family
  JOURNAL   Genome Biol 12 (5), 222 (2011)
   PUBMED   21639948
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Dhe-Paganon,S., Werner,E.D., Chi,Y.I. and Shoelson,S.E.
  TITLE     Structure of the globular tail of nuclear lamin
  JOURNAL   J Biol Chem 277 (20), 17381-17384 (2002)
   PUBMED   11901143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="lamin tail domain-containing protein"
                     /GO_component="GO:0005882 - intermediate filament
                     [Evidence IEA]"
                     /calculated_mol_wt=19635
     Region          46..162
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
ORIGIN      
        1 mqhefvklwr gsllrkrpvv aaaaavtagv lsflaaapaq aaeyhsalki rgvqydapgr
       61 dsnscssgnt hqeyltikny sssatinlkg yvvkdatgnr ftftashylq pgdyvnlrgg
      121 hgtdsdkynv vhrdncnfmw nndrdtiyly kpsgsrsdvh sytksgsdsd gngyiryhs
//
LOCUS       WP_457692981             349 aa            linear   BCT 27-JAN-2026
DEFINITION  fatty acid desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692981
VERSION     WP_457692981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..349
                     /product="fatty acid desaturase family protein"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38418
     Region          21..345
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mttslefsrs aagpaasags dfarlsrriv aagllrrrpg yyavrlalvt mafaggwvaf
       61 falgdswwqm avagflalvf aqvalvthdv ahrqvfrgrr psevggllfg nlgvgmsygw
      121 wmnkhtrhha npnheeldpd vapdilvwsr dqaraatglp rfigryqaql ffplltlegf
      181 nlrvssiral rsptmkhwgs eaalllthiv lylaalflvl spgkalafll vhqalfgvyl
      241 gctfapnhkg mptltggarp dflrrqvlts rnvrgglltd vllgglnyqi ehhlfpsmpt
      301 phlrraqtiv raycaelgvp yhetglirsy aealrhlrqv geplrgpra
//
LOCUS       WP_457692983             259 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457692983
VERSION     WP_457692983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27699
     Region          2..243
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 msvevtwwgh atvtvedsgv rvltdplfvh rlahlrrrrg alppaeaara dvvlvshlha
       61 dhlhpaslar lapgtrlvvp rgataavpgl rrvaaaralr vtelrageec aagaltvrav
      121 saahdgrrlp ygprrvpalg yvvrgavrty fagdtglfee maeevgpcev allpvggwgp
      181 flghghldar raaqaavrla pccavpvhyg tywpigmdav rphefhapgq eferqmalla
      241 pevtvhrlgh gesvrpkvv
//
LOCUS       WP_457692970             271 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692970
VERSION     WP_457692970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /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=29612
     Region          15..>72
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          99..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mttaaasspe tttgvgtllr ewrgrrrisq lelalradss arhisfietg rsrpsqemvl
       61 rlaehldvpv rernalliaa gyaptfpetp lddpsmaalr sgmerlltgy epfpalvvdg
      121 tyrvqaanrg itmllesvap sllqpplnam ritmhpdgla prirnyrewr ghllsqmerq
      181 lalmrsaplr alydevlayp lppgghetaa lgahapfalp mmiehhdtvl sfistiatfn
      241 tpmdvtvsel avetflpadp etagylrgvg v
//
LOCUS       WP_457692984             211 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457692984
VERSION     WP_457692984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22151
     Region          21..204
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mtlvgelvrs vppestqqvv gypslfllvv lgslvpvvpt gavvssaavv afhhtspfal
       61 ltvfvvassa afvgdvglys lgrrgshspy gsrwlarlra ratperldra qhklrehgvl
      121 vlvlsrlvpa gripvmlacl laamplrrfv rgdipaclaw aatyqlvgll sgslfsstwe
      181 gvlmavalal vislapalwr rvraaggegg a
//
LOCUS       WP_457692990             271 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457692990
VERSION     WP_457692990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29713
     Region          35..163
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpqesavyth ghhesvlrsh twrtaansag yllgalrphq qildigcgpg titadlaalv
       61 pdgqvtgley apdvleqara taaargvtnv rfavgdvhal dypddafcvv hahqvlqhvg
      121 dpvqalremr rvtrpggiva vrdsdyaamt wypesdgmte wlrlyqrvar gnggepdagr
      181 rlhawarqag fapdaitata atwlfrtpee rswwselwad rtvsssyari avdgghatee
      241 qldriaqawr twgadedgwf gilhgeilcr v
//
LOCUS       WP_457692992             396 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457692992
VERSION     WP_457692992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41489
     Region          50..390
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mldrsrpvpr vrvspasrrr vsamgavvaa alavggalps satqaqgsgd avrkgldrlv
       61 hedrypaala stvgrdgrth hftagvadvk tgakvpvdgq vragsntkaf tatvvlqlvg
      121 egkvaldapi erylpglvrg edidsrritv rqllqhtsgl pdytdfiadp tgkarhtyvr
      181 pralldtala hkavfapgtn waysntnyll aglliekvtg rpfagqltqr vigriglrht
      241 yfpgvgdegi reahpqgyfa akpgrpleni teldpswgwa agqvisspsd lnrffsallh
      301 gellepaqla qmrttvkvpe sagigpgvry glgvtsapls cggrswghgg dipgygtrtg
      361 vtddgravtv avtadgpptk qgpadalall dtvlca
//
LOCUS       WP_457692994             307 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457692994
VERSION     WP_457692994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31701
     Region          1..304
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,129,133,154..159,178..179,181,194,
                     217..218,239..240,252..254)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mkaiiansyg gpevleytdh pdpkvgpdsf lirvkaagvn pvdwkilagy ldpmmdghfp
       61 lipgwdvagv veavgadate yaigdevigy vrkdevqhgt faelvaapvr tlarkpasls
      121 wqqaaglpla gltayqalsr vgvtagetvl vhaaaggvgs lavqiavaqg arvigtageh
      181 nheflrslga epvtygdgld grvrelapeg vdaavdfvgg gvvdisqell kdrsrvasia
      241 dgevkakggh mvwvrpdtad ltalgalada gkltvpvaaa fplteaaeaf rqsmtgrtrg
      301 kivlevs
//
LOCUS       WP_457692995             248 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457692995
VERSION     WP_457692995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 248)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27127
     Region          15..104
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          163..245
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpksrhaprm ttglrplpag tgvdahrhde hqivyagrgv lsvttdagsw iapatravwi
       61 pagtvhehha hgdtdlhlmg lpvrdnplrl drpavlkvgp llrelilvyt erpagrsaer
      121 lrlravlldq lrhsaeqplh vpaatdprlv avcallrddp adnrtlaqlg atagvsdrtl
      181 trlcraelgm sfpqwrtqlr lhhalrllae dtpvtavahr cgwasssafi dvfrrafght
      241 pgahraqr
//
LOCUS       WP_457692997             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457692997
VERSION     WP_457692997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22938
     Region          31..74
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          89..185
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 maertesnqt appeqqparg rprdaerdra llaatlqvlq esgyggltta avakragvst
       61 atlyrrwrsk edlvvgtavs wasdlgpqpd tgslkgdlav llrdkaetle gpggrllhil
      121 igeaahneal arvldsaivq pvrdraaevv rravargdip pledahvlad lvvgsmvsrl
      181 fltpdvtyqg ttdgptsgea aisellpfll ralgaqpg
//
LOCUS       WP_457692998             442 aa            linear   BCT 27-JAN-2026
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457692998
VERSION     WP_457692998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   McLeish,M.J., Kneen,M.M., Gopalakrishna,K.N., Koo,C.W.,
            Babbitt,P.C., Gerlt,J.A. and Kenyon,G.L.
  TITLE     Identification and characterization of a mandelamide hydrolase and
            an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas
            putida ATCC 12633
  JOURNAL   J Bacteriol 185 (8), 2451-2456 (2003)
   PUBMED   12670968
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Vasiliou,V., Pappa,A. and Petersen,D.R.
  TITLE     Role of aldehyde dehydrogenases in endogenous and xenobiotic
            metabolism
  JOURNAL   Chem Biol Interact 129 (1-2), 1-19 (2000)
   PUBMED   11154732
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..442
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_process="GO:0006081 - aldehyde metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47019
     Region          13..438
                     /region_name="ALDH_F3-13-14_CALDH-like"
                     /note="ALDH subfamily: Coniferyl aldehyde dehydrogenase,
                     ALDH families 3, 13, and 14, and other related proteins;
                     cd07087"
                     /db_xref="CDD:143406"
     Site            order(121..123,149,178,196,295,297..298,301,342,344)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143406"
     Site            order(123,218,249,252)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143406"
ORIGIN      
        1 masqthttdl daaavvgrlr rtfstrrtas pewrrgqlaa lrtlltdhrd dllaalaedl
       61 gkgpeeayrt eigftvneid htlnrlddwl kprpaelper llpasaqtvr eplgvvlvia
      121 pwnyplqlal aplvgalaag ncavvkpsel apatsaalar llpryldsda vavvegavpe
      181 ttallvqrfd hifytgngtv grivlaaaap hltpvtlelg gkspvvldpg tdlaaaarrl
      241 vtgkflnagq tcvapdyvla igdtareiep hlaaavrety gadpagaeey grivserhfd
      301 rltalldsgr tviggahdra trylaptvla dvtpdapvmq eeifgpilpi vpvpdldaai
      361 afinerdkpl alyaftased tkrrllaets sgaltfglpv ahltapelpf ggvgesgmgr
      421 yhgeysmdtf shtkavldkp la
//
LOCUS       WP_457693000             301 aa            linear   BCT 27-JAN-2026
DEFINITION  arginase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693000
VERSION     WP_457693000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Dowling,D.P., Di Costanzo,L., Gennadios,H.A. and Christianson,D.W.
  TITLE     Evolution of the arginase fold and functional diversity
  JOURNAL   Cell Mol Life Sci 65 (13), 2039-2055 (2008)
   PUBMED   18360740
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Ash,D.E.
  TITLE     Structure and function of arginases
  JOURNAL   J Nutr 134 (10 Suppl), 2760S-2764S (2004)
   PUBMED   15465781
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Cederbaum,S.D., Yu,H., Grody,W.W., Kern,R.M., Yoo,P. and Iyer,R.K.
  TITLE     Arginases I and II: do their functions overlap?
  JOURNAL   Mol Genet Metab 81 Suppl 1, S38-S44 (2004)
   PUBMED   15050972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10177987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="arginase family protein"
                     /EC_number="3.5.3.-"
                     /GO_function="GO:0016813 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear
                     amidines [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31480
     Region          5..298
                     /region_name="Arginase-like_1"
                     /note="Arginase-like amidino hydrolase family; cd09999"
                     /db_xref="CDD:212523"
     Site            order(100,122,124,126,143,230,232,275)
                     /site_type="active"
                     /db_xref="CDD:212523"
ORIGIN      
        1 mrrtvlidap snlglrppsp gtvpgcykla galreqgllr rlgaleggvv vpprydlgew
       61 kegdgdfnaa alaaytgrla trieghvgsg dfpvvlggdc sillgavlal rrlgrygvay
      121 ldghgdfrhp dnsavsgpvg aaageglaqi tgrgqadltd ldglrpyird edvwalgird
      181 adedqeeltg lgishapvge irrrgpavva revlthfqrs pldgfwihld advldpsvmp
      241 avdspdpggl ltgelrallg plaasprcag invtiydpdr dpegtgavll adllesvfaq
      301 p
//
LOCUS       WP_457693002             183 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693002
VERSION     WP_457693002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20350
     Region          10..176
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mtsndrylvr gprvgirhft aadreeftal aresaelhrp wlfppttdaa ydsyllrlqe
       61 pqregflice ladgriagyl tvnnivhgaf rcgaigygaf ahaagrglms eglrlvlhha
      121 ftemglhrle vniqpanels ialvkragfr legfapdflf idgawrdher waitaemvsg
      181 qae
//
LOCUS       WP_457693004             212 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693004
VERSION     WP_457693004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22798
     Region          17..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdmaqqrvka prgsssrqrl taqdwadaal tamgegglaa vaveplaarl gttkgsfywh
       61 ftnrdaliea alerweevgt eavitelete pdpgrrlrrl lveattlaat dplevsllas
      121 atdprvaaal arvtdrrigy vaalfaalgf pedearhrgl laytaylgha qlghavpqsl
      181 pvdaardryl dgvidtlvqp rdggdraeld rt
//
LOCUS       WP_457693005             395 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457693005
VERSION     WP_457693005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 395)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..395
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43870
     Region          17..395
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(63,84,86..87,170..171,179..180,183,186..187,190,226,
                     229..230,233..235,238,281,282..285,309,385)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(85..86,93,97,104,149,152,230..231,234..235,238..239,
                     242,280..281,283..284,286,309,336..338,341..342,344..346,
                     349..350)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mteaipyfqd rtcpyhppag yqplreagpl tqvtfydgrt vwavtghtea rallsdqrls
       61 adrqnpafpi pverfeairr vrtpligidd pehntqrrml ipsfsvkria tlrpeihriv
      121 dglldrmldq gppaelvsaf alpvpsmvic sllgvpyadh effeeesrri lrgrtadeae
      181 darlkleeyf tgliaakekn pgdglldeli aerlrdgslt heelvglami llvaghetta
      241 nmislgtftl lehpeqldrl kaeeglmpaa ieellrflsi adgmlrvate dieiggqvir
      301 addgvlfpts linrddtayp apdeldldrs arhhvafgfg ihqclgqnla raemeialra
      361 lftripelrl avpaaeipfk agdtlqgmie lplaw
//
LOCUS       WP_457693006             310 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 peptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693006
VERSION     WP_457693006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=32578
     Region          7..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtvagairpp rlrpgdrvav vapsgpivae rldrgldvlr gwdldpvaah hargthptlg
       61 ylaasdeera rdlqeawcdp svkavfaarg gygaqrmvdl ldwdalraaa pkpligfsdv
      121 tvlheafavr agvstlhgpa vagevflkdd atrdhlrrtl fapetvrtvv spsarplvpg
      181 rargvtlggc lamlatelgt pwarqgaagg lllledvgep pyridraltq llragwldgv
      241 agivlgswar cgpydrvrev lvdrlaglgv pvaeefgfgh gdsaltvplg vpaeldatag
      301 tltfedpatv
//
LOCUS       WP_457693009             249 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693009
VERSION     WP_457693009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..249
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26983
     Region          <73..222
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mierggsqqv arliedvlrs ghplpekvra vmlrtdtdih lvasalgdcl vstpgeapgl
       61 lipaaladgk sgrarlkgvl rhraavvgha vppteaansv raasrlldla sahdgpdagv
      121 vfvddhlssl vllqdeslth tliarrlrpl agltpercer leatllawlg gmgapevaka
      181 lsihpqtvry rmrqleklfg arlrdprtrf eiemalrsrq lmaaarrrra aatrrpratt
      241 kprkalprp
//
LOCUS       WP_457693012             283 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693012
VERSION     WP_457693012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30738
     Region          26..258
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mpgrvkadlk gvpetalwtl yhraaeaarp dtvlpdprav qlrteiefpf rermgtarpw
       61 laqaialral gfdrvvrafl adcpdgtvva lgegletqfw rvdngraqwv tvdlngplal
      121 rkrvlphgar qrlvacdard srwmagidps rgvlvtaqgl lmylqpaqvt rliaacagaf
      181 pggtmvfdtv srrfsartht rakgpgghrl ppmpwgmdav drddlrqahp aisevsevpl
      241 pagrgflgyl apraaalpll rtdrplitrl rfgaapaslt gqp
//
LOCUS       WP_457693014             852 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693014
VERSION     WP_457693014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19094666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..852
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87079
     Region          73..458
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(74..75,78,109,159..160,162..164,167,187,190..191,
                     194,319,322..323,326..328,331,359,363,416..417,421,425,
                     441,444..445,448..449,452)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          547..>836
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mggttlserv ertdppvsga atataapmap lpapavggvp qepgpgapap vsprrlrlvl
       61 aglmltllla aldqtivata lpkivgelhg lgamswavts yllasaiglp lygklgdlfg
      121 rkpvflfall vftvgsalag wsrtmdelvv fraiqgvggg gliigvqaii advvpprarg
      181 rsagligaaf glaaaagpli ggfctdhasw rwcfylnvpi gvltllviac vlklprptrr
      241 gkpdiagall laafstclvl laswggttya wnsrvilglg agalgtallf laveyfatep
      301 llplrlfrds vfnvtgliga avglalfgaa gylptflqma dgatatesgl lmlpllggiv
      361 laslvsgrli srtghykvfp vlgcalaavg mwllsrpqqd tareafslwt gllglgigfv
      421 lpvlllavqn svrtadlgaa tsathyfrqi ggsvgaalfg tlladrlarr lgdrlpasaq
      481 lpdpesitpq llralpaslr dssvaayada vpgiffalvp vlvlglvlaf flkekplvsh
      541 ashapqaats pqmpygdpsd psvvpqaraa tdstavnsrd sgspytrahs yaptghtavm
      601 agvpvcgtvq hhdgsivpra altlidvagr qigrgatged gryalstpga gsyvliaaag
      661 ghqpqavtvt vgerpveldv vlggagrlag tvttadgtpv rdamvtltdv rgevvattrs
      721 greggyvige lvageytlas sapafrpaal pvtvqasret rqdielagga vlrgtvragg
      781 grpvedarvt lldaagnvvd tattgpdglf rfvdlsagey tviaagyppv atvlqvaggg
      841 rterdlqlgh ed
//
LOCUS       WP_457693018             246 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693018
VERSION     WP_457693018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25705
     Region          57..183
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 meeefheltd rvraelrspq dlvayerllg larkntpagr eelarmlvav erplwareia
       61 afvlgcagdk rafetlvlll nyrdpvrcat aahalgrlgd prtaraaaal atnplrtaya
      121 lhpvrllael rapqsvpali atlerlltph npywrvalac veglgalgdr ravpaltaav
      181 thprlaaaaa aslarlgvhe dvtaadgaaa tdgpddgeda raargagrvp gpergagpgg
      241 gqglsg
//
LOCUS       WP_457693019             606 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693019
VERSION     WP_457693019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..606
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=63470
     Region          20..297
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          327..603
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mgpqstpdls tpasslslst vaiiglgtmg tgiaevltra grevigidtd eaaarhavsa
       61 leaataravq rerltererq dalarfrtft dlqavadadl vievvpedye lkrqvfaeld
      121 avvrpdtila tgtnalsvtr laadsqrper vlgvhffnpa pamklvevvs svltaptava
      181 avtelardlg kdpiavgdrp gfvadgllfg ylnqaaamye skyatredid aamklgcglp
      241 mgplalldli gvdtartvle amytesqdrl hapapilgql aeagltgrka grgfytydap
      301 gsptvvpdae spaaaddlag grtvtgvgva gsgtmasgia evfakagfkv vlaarsleka
      361 ekakariaks lgrsvdkgrm saeardaala aitpagslda fadvdlavea vaedlavkqe
      421 lfktldkvck pgavlattts slpvvacara tsrpqdvigm hffnpapamk lvevvrtvlt
      481 addvhatvra vcakvrkhpv dcgdragfiv nallfpylnn aikmveehya tlddidaamk
      541 lgggypmgpf elldvvgldv slaiekvlha efrdpglapa pllehlvaag clgrktgrgf
      601 reyarr
//
LOCUS       WP_457693023             332 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693023
VERSION     WP_457693023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35876
     Region          17..323
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtqahpspat tpgegrnrlr prrsclavpg snprflekaq glpadqvfld ledacaplak
       61 egarhhivea lnegdwtgkt rvvrvndwtt hwtyrdvitv vegagpnldc imlpkvqdaq
      121 qivaldlllt qiektmgfev grigieaqie nakglvnvdg iagasprlet iifgpadfma
      181 sinmkslvvg eqppgygada yhyilmrilm aartydlqai dgpylqiknv dgyrevagra
      241 aalgfdgkwv lhpgqveaan evfspsqedy dhaelilday ewhtseagga kgsamlgdem
      301 ideasrkmal vvagkgraag mirtskfeap ea
//
LOCUS       WP_457693024             413 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693024
VERSION     WP_457693024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45089
     Region          10..410
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtrlaqtegl tdiqreilst vrdfvdkeil pvatelehrd eypsqivegl kelgvfglmi
       61 peeygglges lltyaltvee iargwmsvsg iinthfivay mlkqhgtqeq kdyflpkmaa
      121 geirgafsms epalgsdvsa isskgvrddg gtsrssgaes ggdfvltgqk mwltnggtst
      181 lvavlcrtde ghpegtaphk smttflveke agfgevrpgl tipgkidkmg ykgvdtteli
      241 mdglripadr vlggetgrgf yhmmdgvevg rvnvaargcg vaqrafelgv syaqqrhtfg
      301 kpiaqhqaiq fklaematkv eaahammvna arkkdsgqrn dleagmakyl aseyckevve
      361 dafrihggyg fskeyeierl yreapmllig egtaeiqkmi igrrlleeyr iqg
//
LOCUS       WP_457693026             638 aa            linear   BCT 27-JAN-2026
DEFINITION  Xaa-Pro dipeptidyl-peptidase [Streptomyces nigrescens].
ACCESSION   WP_457693026
VERSION     WP_457693026.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11480810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..638
                     /product="Xaa-Pro dipeptidyl-peptidase"
                     /EC_number="3.4.14.11"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008239 - dipeptidyl-peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67607
     Region          <22..600
                     /region_name="PRK05371"
                     /note="x-prolyl-dipeptidyl aminopeptidase; Provisional"
                     /db_xref="CDD:235435"
ORIGIN      
        1 maavaallsa liapaaaqaa pgesrpvysy drairesvwv dtrldgdadg rtdrvavdiv
       61 rpaepaqqgr ripvimdasp yysccgrgne sqkktyddrg rpvgfplyyd nyfvprgyat
      121 vlvdlagtnr sdgcvdvggr sdirsakavv dwlggrgray tartggepvt agwsngstgm
      181 igkswdatia ngvaatgvkg lktivpiagi sswydyyfak gaplydsgpd sladmvdspe
      241 arkrcaavqk kladgaprtg dwtglwserd yvrnarkvra svlmvhgmqd lnvrtrhagq
      301 wwdalarhgv erkiwlsqtg hvdpfdfrrg awvktlhhwf dhyllgydng iertpmadie
      361 rspgtwstdp qwpapgttpt tlrprggtap gvgvlgtrka pqgatetftd dpklseadwa
      421 aridaptaak agfrtgplra plrlsgsgtv tvnvtpstst ahlsavlvdl gpdtirnyaa
      481 dgegittldr rtcwgagttg dtgcfketaa dtrkvahtvf srgwadlgny adahkgrplt
      541 pgkpytltld laasdhvvpa ghrlalivag tdaglidppa stpkltldls rtsaelpltg
      601 gapafvrata gapahpdaaa pldgiappps isrlpavg
//
LOCUS       WP_457693029             320 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693029
VERSION     WP_457693029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34744
     Region          1..291
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdllslryfr avarrehisr aaeelrvaqp svsrtiarle aelgvplfdr hgrairlnry
       61 gaafltrver aldelddarr emadaagldd ggiavaaetl lpltellagf raahpgvtvr
      121 clqstpevmr ehlrarevdf ciasqplpgp glgavrllhe evlltvpagh plagrervtv
      181 eeiaeepfit trpghwqral lerlftaigr rpviscegde pgathfliaa glgiglmpsl
      241 aradlasvpl awlhldtpgc vrtlslvrre dsylstaaar frdlavahfa eraqrtlpag
      301 elpasrgsvl apyeggvldr
//
LOCUS       WP_457693034             235 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Streptomyces nigrescens].
ACCESSION   WP_457693034
VERSION     WP_457693034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  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 235)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         <1..235
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          1..232
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 allaerdrdr avagerarma relhdmvanh ltaiaihsta aqsiddpsat realaviren
       61 svqglaemrr ligllrgpkt aeggtepaat ptldgleali eqartsgrss gltfvlddar
      121 spagpgtgph qaapaelaay rivqesltna lkhaapgevl vrlahdrgga ltvavrspfa
      181 drpgprapgs gsglvgmrer aallggafea gpesgpagrv wlvqaalpaa geear
//
LOCUS       WP_457693039             447 aa            linear   BCT 27-JAN-2026
DEFINITION  MraY family glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693039
VERSION     WP_457693039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..447
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47447
     Region          42..322
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            101..102
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            227..230
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(298,312..315)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mgqpvreyll tlcvtaavty lltgpvrkfa iaagampeir ardvhreptp rlggiamfgg
       61 lcagllvash ltnlksvfen sneprallsg aaliwilgvl ddkwgvdalv klggqmiaag
      121 vmvlqgltil wipipgvgtv sltpmqgtll tvalvvitin avnfvdgldg lasgmvciaa
      181 aaffmyayrm wfgygieaaa patlfsvvlm gmclgflphn mhparifmgd sgsmliglvm
      241 aagavsvtgq vdpdllnlka gglreatham vpvyiplllp ltviavpvad lilaivrrtw
      301 kgqspfaadr ghlhhrllei ghshsravli myfwsaliaf gavaysanna smwivlgivl
      361 lsavglvlll lprftprtpl waewmvppry rrvapaaapa atapatddes avepeeerep
      421 vpagihgata igdrsrfvgr rkadshr
//
LOCUS       WP_457693044             375 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457693044
VERSION     WP_457693044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=39837
     Region          87..359
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 madsngtaqt aesrargira tgrrrkgptr rrravtitlc tltsaallgg aglgyvyfkl
       61 ngnlkgvdin galghdrpkn iddgsmnilv mgsdsragkn geygkdegaa rsdtamivhv
      121 ykghkkasvv svprdtmvkr pdcttkdgkd vpgaqramfn tafevggpac avktvesmsd
      181 vrmdhfvevd ftgfkklida lggvdittsk aidddhshlh lqpgqhnlng eqslglvrtr
      241 hgvpggdgsd lgriqlqqaf ikalmnqvkn vgvltnptkl ydiadtatka ittdtdlnsv
      301 seltglaksl gnigsenidm vtlpvtydpa npdrvvpltk kseqvwnalr vdkeipksai
      361 kgsagdqggt dkyvk
//
LOCUS       WP_457693048             430 aa            linear   BCT 27-JAN-2026
DEFINITION  homoserine dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457693048
VERSION     WP_457693048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Navratna,V., Reddy,G. and Gopal,B.
  TITLE     Structural basis for the catalytic mechanism of homoserine
            dehydrogenase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 5), 1216-1225 (2015)
   PUBMED   25945586
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Thomas,D., Barbey,R. and Surdin-Kerjan,Y.
  TITLE     Evolutionary relationships between yeast and bacterial homoserine
            dehydrogenases
  JOURNAL   FEBS Lett 323 (3), 289-293 (1993)
   PUBMED   8500624
REFERENCE   3  (residues 1 to 430)
  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 11482218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="homoserine dehydrogenase"
                     /EC_number="1.1.1.3"
                     /GO_function="GO:0004412 - homoserine dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006520 - amino acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43939
     Region          4..428
                     /region_name="PRK06349"
                     /note="homoserine dehydrogenase; Provisional"
                     /db_xref="CDD:235783"
ORIGIN      
        1 mmrtrplkva llgcgvvgse vtrimtthad dlaarigapv elagiavrrp dkvregvpae
       61 lvttdatalv krgdidvvie viggiepart littafehga svvsankalv aadgaalhaa
      121 aeangadlyy eaavagaipl vrplreslag dkvnrvlgiv ngttnfildk mdstgagyse
      181 aldeatalgy aeadptadve gfdaaakaai lagiafhtrv tiddvhregl tevtaadias
      241 akrmgctvkl laiceraadg asvtarvhpa miplthplas vreaynavfv eaeaagqlmf
      301 ygpgaggspt asavlgdlva vcrnklagat gpgesaytrl pvspmgavtt ryhisldvad
      361 kpgvlaqvat ifaehgvsid tvrqsgkdge aslvivthra adaalsstvg alreldtvrg
      421 vasimrvege
//
LOCUS       WP_457693051             174 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator [Streptomyces nigrescens].
ACCESSION   WP_457693051
VERSION     WP_457693051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=18043
     Region          1..119
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msgrilvvdd nkvirqlirv nlelegfevv taadgaecld vvhhvrpdvv tldvvmprln
       61 glhtaarlrs dprtwdipia ivsactqgev dngetvgvda flakpfepae lvrtvgmlvr
      121 egrqrqrqre rgpaggaeee dgesdgggga agraassggv aapggvgmvd agge
//
LOCUS       WP_457693053             428 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457693053
VERSION     WP_457693053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 428)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46778
     Region          48..424
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(95,112,114..115,201..202,211..212,215,218..219,222,
                     256,259..260,263..265,268,311,313..316,340,416)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(113..114,121,125,132,180,183,260..261,264..265,
                     268..269,272,310..311,314..315,317,340,367..369,372..373,
                     375..377,380..381)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mttlrsriia wagrmylart qkkgfdlsrm sflpesvlmp lrrdglnpvg dlaavrerep
       61 isklpvpiaa nvwlvtgyde vkavlgkana fssdftnlvg kagagaeqnp gglgfadppv
      121 htrlrrlltp eftmrrlgrl tpriheivee rldamekagk dgdpvdivhs falpipslvi
      181 cellgvpyed radferlsaa rfdlfsgana sfgaisesls yfrdivkkqr enpgdgllgm
      241 ivkehgdsvs deelagladg vltggfetta smlalgalvl lqdpkhfaal hdgddvvdry
      301 veellryltv vqvafprfar edleiggvqi asgdvvlcsl ngadrdgklg pemeqfdptr
      361 nvpshlafgy gihrcvgael armelraayp alvrrfpnmr laakpedlef rklsivygie
      421 slpvrlng
//
LOCUS       WP_457693058             368 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693058
VERSION     WP_457693058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 368)
  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 368)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..368
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42303
     Region          100..230
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(109,139,142,189,219,222)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mptrdlyvqd pgdpvwkvpa sgaarfswdy ddgrdrllal yqkgkdkqwd anlridwdle
       61 vdpqdplgtp desmslygtk ywdkmtekdr gdmrrhytsw qfsqflhgeq gamvcaariv
      121 esvpdldakf ysatqtmdea rhaeiysrfl qekigmlypv ndnlqallsd tlkdsrwdmp
      181 ylgmqvlieg lalaafgmir dtttkplpkq ilayvmqdea rhvafgrmal rdyykqlsda
      241 elrereefvi egcylmrdrl rglevlenfg iphkeaaeft erseflhlfr kllfsrivpc
      301 vkdiglwger lqrayvdmgv femgdsnldl lmaqdeelae kldaerfaae eeartaevaa
      361 aiaegaed
//
LOCUS       WP_457693059             315 aa            linear   BCT 27-JAN-2026
DEFINITION  AurF N-oxygenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693059
VERSION     WP_457693059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Choi,Y.S., Zhang,H., Brunzelle,J.S., Nair,S.K. and Zhao,H.
  TITLE     In vitro reconstitution and crystal structure of p-aminobenzoate
            N-oxygenase (AurF) involved in aureothin biosynthesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (19), 6858-6863 (2008)
   PUBMED   18458342
REFERENCE   2  (residues 1 to 315)
  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   3  (residues 1 to 315)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   4  (residues 1 to 315)
  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 10569062
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="AurF N-oxygenase family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35783
     Region          25..298
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mtsaptamte tdtdvlrdal gllkdreqva erlldssakh sfdpdteldw dapleegkwf
       61 wppelvslyd tplwrkmspa qqqdlsrhea aslaslgiwf eiilmqllvr hiydkpvtsa
      121 hvryalteia decrhskmfa rmiqkgdapa ypvsrlnhnl arilktvstt pgsfactllg
      181 eeildwmqrl tfpdervqti vrgvtrihvv eearhvryar eelrrqmvta prwereltri
      241 ssgeaarvfs vafvnpavya qvgldkreav aqvrasghrr evmqsgarrl tdfldeigvl
      301 rgvgrrlwrs sglla
//
LOCUS       WP_457693060             246 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693060
VERSION     WP_457693060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26717
     Region          21..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mngsgtapav prpayrrlsv eqrrsqllta aldlfaqrap edvslddval aagvsrplvy
       61 ryfpggkqql yeaalrsaad ilercfaepe sgpltqrlsr aldrylafvd ehdagfsall
      121 qggsvvettr ttaivdevrr aaadqilrhl gepepglrlr mtvrmwitav eaasliwlde
      181 dkqpaldelr dwlvdhfial ltataagdpq tarvtraalk letsdgpagd larrtlpvvs
      241 daahll
//
LOCUS       WP_457693063             205 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693063
VERSION     WP_457693063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=21904
     Region          19..201
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mgqagpaaaa adaglqswqt drsrapiatk ivvaggfgvg kttfvgsvse itplqteavm
       61 tqasadtddl tatpektttt vamdfgritl dqelvlylfg tpgqqrfwfm wddlvrgaig
      121 aivmadtrrl edcfpaldyf escglpyvva vnhfegteaf avehvrdalt vppqvpvvim
      181 darrrttvie sllalvghal ettpe
//
LOCUS       WP_457693074             377 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457693074
VERSION     WP_457693074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41033
     Region          9..370
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtrwpctplr elwqrvwegl rpldpyrsvk aalgalvsvs viittllvfv amhsatelrv
       61 itifsiiasl litqfvansl tapldemtdv trsmahgnys rrvrserrde fgalanafnr
      121 maadleavdt hrkelvanvs helrtpiaal ravlenvvdg vcepdpetmr talkqterlg
      181 rlvehlldls rldngvvplh arrfevwpyl sgvlkeanms rgaatlsgls gvagsgthtr
      241 tdvhlhldvs ppeltahada erlhqvvanl idnaikhspr hgrvtvharr gegpqslvve
      301 vqdegpgipe aeryrvferf nrggpapsgp gtdggtglgl aiarwavdlh ggrigvaesp
      361 rgcrirvtlp glesars
//
LOCUS       WP_457693080             452 aa            linear   BCT 27-JAN-2026
DEFINITION  vanadium-dependent haloperoxidase [Streptomyces nigrescens].
ACCESSION   WP_457693080
VERSION     WP_457693080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="vanadium-dependent haloperoxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140905 - haloperoxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48116
     Region          201..425
                     /region_name="PAP2_haloperoxidase"
                     /note="PAP2, haloperoxidase_like subfamily.
                     Haloperoxidases catalyze the oxidation of halides such as
                     bromide or chloride by hydrogen peroxide, which results in
                     subsequent halogenation of organic substrates, or
                     halide-assisted disproportionation of hydrogen...;
                     cd03398"
                     /db_xref="CDD:239492"
     Site            order(304,311,347..349,398,404,408)
                     /site_type="active"
                     /db_xref="CDD:239492"
ORIGIN      
        1 meisrsgrra algavtalll lvitavagpt ataeshpqpa adpaairdwn viatdtisan
       61 lgptrpsgqv viwhgfvsaa vynavvgiqr tyapykwrar gpstaspeaa avtaahrvll
      121 tyfpasqapl daayadslak ipdgrakrqg vafgeraadh lielreddgr fapveftaep
      181 apgvwrptpp ahlpfidpwl gklrplllts psqfrpggpp alssaryard vnevktmgar
      241 tgsartaqqt etalffggnl amqfqsafrd ysarhhldia dtarmfaagn asatdavvta
      301 wdaklhygfw rpitaiqlad tdgnpatdad ppwqpllvtp phpdylsght tvagavirtl
      361 tgllgtthld lnvpseitgt trhyaeagqf nedminarvw agihfrtadv vgcragtrig
      421 vwalthyfqp lrpagphavp paqqmcphgs as
//
LOCUS       WP_457693083             262 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693083
VERSION     WP_457693083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28531
     Region          14..261
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mastrsslae vdrrrqdvla hvvehgevri ddlarhfgvs latmhrdldq laerrllrke
       61 rgraapfpsl tmetatrfri gvnhpvkeal caavadeirp gstvvlddst tvfplaaria
      121 rteavtvvtn slgvarlfde tpgtdvtllg gryrgefgsc vgpdvlrglg riradlavms
      181 avsvlggrlf hpireyaeik eamlecaqrs lllvdhskfg ktathaygdi ghydrvvtdr
      241 gtpaeeltal rrkgvtvdvv ev
//
LOCUS       WP_457693085             752 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces nigrescens].
ACCESSION   WP_457693085
VERSION     WP_457693085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..752
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=81793
     Region          3..740
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msnaewqheq efidllydrl telrdlaeta vhtaalppeg nhaqmrlern vlvaersgll
       61 aafnagengl cfgrlafrdg rdhhigrigi rrddpdrtpl vidwraevar pfylatghtp
      121 mglrrrrhit tegrrvtalh deimdladav rtghegtdad avllaaldaa rtgrmhdivq
      181 tiqaeqdgii raphhgilvv eggpgtgktv valhraafll yahreqlarr avlivgpnpa
      241 flsyiaevlp slgetgvlla spgelfpgvt atgtdtpeaa eakggaamad alaafvrdrq
      301 dlpdsvivid hedgelrlda emarearrra retrlphnla rphfafriid altaqlvdri
      361 gadpfggpnf lgpddiaqlg kaiatsaevh haieelwpel tpeqlvadfl adpvhlpdae
      421 adairrvdgd wtpadiplld eaaellgedt saaraaaeae rqeridyaqg vldlsygsrt
      481 qefeerdded sevlaahdlv daelladrhe eadhrsaaer aaadrtwafg hiivdeaqel
      541 sammwrllmr rcptrsmtlv gdpaqtaepg scgsweaila pyvddrwdlv rlgvnyrtpt
      601 eimevaaqvp rstdpnftpp rsirstgvrp wahrtddlvr vvaeavaqes rqdgrlavia
      661 psarhealaa alpdvsagpa pdltsavvll gprqakglef dsvivvepae lgasdlyval
      721 tratqrlgvi htgplpdgle meprtdaapv gr
//
LOCUS       WP_457693086             184 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693086
VERSION     WP_457693086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20092
     Region          3..147
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mselrterll lrewresdlg swaamnadpe vrahfpevlt peqsaasvag fqadlahrgw
       61 gwwalevrat gefigftgld pvddhmpftg veagwrlars awghgyatea gkaalsfgft
      121 tlglpeilav ttatnlrsqa vmrrlgmdrn paddfddpdv pdgplrpsvl yrlsagawra
      181 verg
//
LOCUS       WP_457693087             293 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693087
VERSION     WP_457693087.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 293)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31765
     Region          12..293
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mttvngtpas rrragarpvk wlsrgviqvf llivglvwlt paaglflssl rteeanassg
       61 wwtalttpgq lslenytall kdsgivqafw ntvlisvptt lavvviaala gyafawmdfp
      121 grdwvflvvv amlvvpvqig llpvaklfga lglfgsipgv vlfhtayglp faifllrnyf
      181 aeipkemlea armdgggewr ifsqlvlplg rpaiaslaif qflwvwndml vallfadnqs
      241 qpltvalqsq mrqfgsnigv lapgaflsli vplivffvfq rhfvqgimag svk
//
LOCUS       WP_457693089             444 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693089
VERSION     WP_457693089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46535
     Region          1..389
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrrpsvrhtr aalsgaavlg lalsatacgg gvsagggkqe lsgesvtvag vwtgveqqnf
       61 kkvldafsek tgakvtfsst gdnvstvigs qveggnapdv vmvpqvgvlq qfakkgwlap
      121 lsaeigaeak knfaqvwkdy gtvdktyygl yfkashkstv wyspeafaqa gvkpaktyqe
      181 llksgrtlsd sgvpafsvag eagwpltdwf eniylsqagq ekydklaahk ipwtdpsvvk
      241 altalgklfs dknlvagggs galrtdfpes vqqvfgpepg aamvyegdfv salvtdelhk
      301 kvgkdakffp fpavddgkap vvsggdaavv lkagkhkkaa melvkylatp eassvwakag
      361 gyispnkkvp agtyhdevtr kaaqslteag nsvrfdmsdq apaafggtqg agewkllqdf
      421 lrdpsdpeat arkleaaaak aygk
//
LOCUS       WP_457693090             586 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces nigrescens].
ACCESSION   WP_457693090
VERSION     WP_457693090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   4  (residues 1 to 586)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10877734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..586
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64232
     Region          42..522
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(98,101,138,141,186,209,213,245,309,370..371)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(245,309,371)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          503..579
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mliatagngs sadstpspsl pgpasaalsp atgptsrnta qhwwrdaviy qvyvrsflds
       61 tgdgigdlag vrtglpylkk lgvdgiwlsp fypspqhdhg ydvadyrdvd pvygdlaefd
      121 llvadahrlg lkvlldivpn hcssehpwfr aaladgpgsp arslfhfadg rgengelppn
      181 nwramfggpa wsrvkeasgd egqwylhmft peqpdlnwrn pavgtdfdsv lrfwldrgvd
      241 gfridvaagl fkhpelpdsp dpsadertrd svnplawnqp evhqvwrdwr alceeytard
      301 grdrllvgev svrtpseqaa yvrpdelhqa fffhlltarw digtfrkvis ealtdiagtg
      361 stvtwvlnnh dqvrtvtrya tdprgtdrte sagalgpara raaallmlal pgaayvyqge
      421 elglpevvdl pdevltdpiy hrtgsrehir dgcrvplpws ghaspfgfts gtdaarpwlp
      481 qpdwfadhat draladtrsf whlyreglal rrslpqlgeg tlrwldsppq vlafvrgdgl
      541 vcavnfgtep vpapvpdvpl lasgdcpagt lpgstaawwm htpesr
//
LOCUS       WP_457693097             242 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693097
VERSION     WP_457693097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25872
     Region          4..232
                     /region_name="Abhydrolase_6"
                     /note="Alpha/beta hydrolase family; pfam12697"
                     /db_xref="CDD:463673"
ORIGIN      
        1 mttfvlipga acgswhwhll eaelrargra vvsvdlpced daagleqyae avvaavagrg
       61 rltlvahsfa gftaplvcar vpvevlvlla amvpvpgeap dewwaatghp daqvrragra
      121 aqqagdgtga egvpeaavpg saadpffqdl ppelaaeaav rwrrqsetpa arpwpmkawp
      181 dvatrfllcr qdrlfpapfl ravaterlgl vpdemegghf pmlsrpvela drlerysttt
      241 ar
//
LOCUS       WP_457693105             454 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693105
VERSION     WP_457693105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..454
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48089
     Region          9..399
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mrgeprdgri vivgaslagl raaetlrekg ftgsltlige epqlpydrpp lskqvllgrv
       61 padrtglpqr rdvnaqwklg vratgldpng krvlladgee vpfdrlliat gtrarpwpnp
      121 aeaaldgvft lrtsdearrl aerldagprr vlvigagftg seiasacrer glavtvaerg
      181 paplvgalgg tlgalaaklq rahgvdlrcg vtvtalegdg rltgaqfsdg tridadvavv
      241 algairntew laeselaagp rgvtcdagcr afdmygivtd difaagdiar fphplfeyql
      301 lslehwgnav aqaevaahnm vnpgprrlph ltvpafwssq fglniksvgv ptfsdqvvia
      361 qgslkdarlv avygyrgrvt aavsvnqars leyyqrliet aapfppapga adriespvpa
      421 psdvpdpkml shgptvaltg hlpdrrltvv qpar
//
LOCUS       WP_457693109             257 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family substrate-binding domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457693109
VERSION     WP_457693109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="LysR family substrate-binding domain-containing
                     protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27370
     Region          9..192
                     /region_name="PBP2_LTTR_aromatics_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators involved in the
                     catabolism of aromatic compounds and that of other related
                     regulators, contains type 2 periplasmic binding fold;
                     cd08414"
                     /db_xref="CDD:176106"
     Site            order(14,21,22,24..25,28,36,38,40,84,110..111,129..130,
                     135..136,138..139,158)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176106"
     Site            order(15,61,107..108)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176106"
ORIGIN      
        1 mtsseaspsf rlayvpgvtp tkwvriwner lpdvplnlia vpaaeacell rgggadvgfv
       61 rlpvdrtdla aiplytettv vvvpkdhlvt avdevaaedl adeivlhpld etldwehrpg
      121 rpanerpatt adaielvaag vgllvvpqsl arlhhrkdlt yrpladapas rvalswlqee
      181 ttdlvedfig ivrgrtvnst rgrsqapaqp kgkrpeagga rrkpaagkaa gkpagksprs
      241 gsggpkgsrr gkprrrs
//
LOCUS       WP_457693111             215 aa            linear   BCT 27-JAN-2026
DEFINITION  CatB-related O-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693111
VERSION     WP_457693111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23281
     Region          32..188
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(37,39,70,84..85,90,92,94,122,124,127,146,162,170)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(39,41,83..84,86,95..96,124,127,144..145,150,158,
                     160..161,163,167)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(39,41,83,95..96)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100040"
     Site            order(84,86,114,124,127,132,144..145,150,158,160..161,163,
                     167)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 mpavpadptv vhpmpeqprv vllkplvtsp lievgefsyy ddpddptafe trnvlyhygp
       61 eklvigkfca lgegvrfvmn ganhrmdgps tfpfpimggs waehfelitg lpgrgdtvvg
      121 ndvwfgyram vmpgvrighg aviasgavvv ddvpdygivg gnparlirrr fddadiarll
      181 alawwdwpve hltehlptim sgsvdaleav apgkk
//
LOCUS       WP_457693112             479 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693112
VERSION     WP_457693112.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..479
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50943
     Region          <169..>220
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          382..466
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrpdgrrrpa paappppalr fgacpdsvpa ppapeqvecg rlsvplgrsh pdgkhldiav
       61 srvrasgpas errgvllvnp ggpggsglpf avtkraklpe rvrrshdvig fdprgtgasa
      121 padcgpmggl fdspgqdpvp agrtaeqayl dglrrtaddc aqhvkdalph lsttetardm
      181 dairealger rigylgvsyg sylgaayaaq fpqrvgrmvl dsvvgpgewy dfdllqsral
      241 vrqravffaw aarhekrfgl gadgtavraa yqrvrdglae rpvdgfgaae fdravyralg
      301 rterwaglad glrtylrdgs tgplrpaepf dgpasrtfea anrtvkcadg papsparvia
      361 dirrmrrldp qpvltgmeas vcaywhhrpa hgtplgspda ppvlliaseh dpvtpiegar
      421 alqrrlpgsr lvslhddysh gvfasrgngc vdetaaaylt dgtvpradvh ctgpglptp
//
LOCUS       WP_457693116             263 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457693116
VERSION     WP_457693116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 263)
  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   3  (residues 1 to 263)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28849
     Region          12..168
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mnsenlltdn pelyearfpd aerlagrwae dclrrhrsgg rvldlgcgtg rdaaylhgag
       61 rtvvgadlsa amlahartqh pgpdyvqadl rdfdlhqgpf daivcldsal lychtnaeld
      121 gflaacrrgl apggllvaem rngafflgrt elldapavnd ftwrgtayts tttlyidraa
      181 qllrrtriwt tddgspqheq rsawrlifpq elryalaahg fevldlhdgp gprtdpawhe
      241 gagpgesadg drlhlvarlt rhd
//
LOCUS       WP_457693117             528 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693117
VERSION     WP_457693117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 528)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10170709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..528
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57359
     Region          57..508
                     /region_name="PBP2_NikA_DppA_OppA_like_17"
                     /note="The substrate-binding component of an
                     uncharacterized ABC-type
                     nickel/dipeptide/oligopeptide-like import system contains
                     the type 2 periplasmic binding fold; cd08503"
                     /db_xref="CDD:173868"
ORIGIN      
        1 myegpvndsr fpglrrrgfl aaaggvaglg alalagctgp skdaadgggk prrggklraa
       61 fagggasetl dphlanlfad aarakalfdk ladfgadlaa eprlaaswep naaldrwtvk
      121 lrkasfhngk pvtardvlys frriadpkka frakaslepl dlkasravde rtvefalkrp
      181 taefpnllaa fgayivpdga tdfdtkpvgs gpfrfvsftp grsavfrrnd dywdgapyld
      241 qleflvanee sarvnsllgg qveyahelsp ttarahegkg qieivrlrns amqgfamktd
      301 rapfddkrvr eafflladrk elvdgalsga geigndlfgk gyeyyaeglp qreqdldrar
      361 hllkkagadg lrvtldtsav aagftesaai frdqaakagv qvkvamgskd sywqdtldsg
      421 tlccyrsgam pieshfsqrl lsgsttnatk wqhkdfdaly qqaqstkdqk draavyarmq
      481 rrlyaeggfl iwgfadwilg tartvrgvah rapantldwa rfdkvwla
//
LOCUS       WP_457693119             303 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693119
VERSION     WP_457693119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31732
     Region          46..260
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 msprtasgrg rftfalliia vplllallgp lfagepgpra psftvgsghw agtdfvgrdv
       61 wrqvmlggrp vvlaalaata layavalplg ligalthrrw leellmrpld vllavpslli
      121 illvaavltp gavglallva lvnipdavra vraataeaaa rpavealrmq getwwrtavg
      181 yvgrsalrtl aadagvrltg vlylvataaf lgvgaepdaa dwavmvdrnr tgmfvqpwav
      241 vlpallimal tmgtnllfda altrrdrrpg rdrapqpvrt pappptdgtp pgpgrdeksd
      301 pci
//
LOCUS       WP_457693125             687 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693125
VERSION     WP_457693125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 687)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 687)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 687)
  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 687)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..687
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72547
     Region          33..617
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mpgegetgge elqfvdrtgs keragqqirl admarrlprl vrrsvalaws idrwaclgll
       61 vcqvasgamq algllavsgt iaallsggdi ygrllaawps lvmlagaaaa rallgitvaw
      121 lssrlgpqms reaelgllga vtevelsayd apgfnhrkea aergaevaqd lvtegqdlia
      181 slasliagag vltalhpall pllalagfpq avaqisaarv rylarlrsng dyrllsilrw
      241 hvgdryaadq iragtmssfl vgryrhiter inradrraad tgarmsviga lcggvasaav
      301 waavvwllat grmsvghagt avfalqtvgm alrglvvgga rimrtglymd dwsaflreag
      361 gyrmnrgatv pgppqqitvr dlvfryeesa ndavrgvsft lrrgevvalv gyngsgkttl
      421 akllsglylp atgsvtwdgv ptgeldpqam wshvalvpqd yarwpltare nmtlgqptag
      481 gdadihaaca rsgadevlte lrsgletvla rdwlggqels ggqwqrialt rafyrpagll
      541 vldeptaald plgehrifag lrklaatrav vlithrltnv acadrilvlh kgrivqqgtf
      601 pelvaepgpf rdlwayqhtr eaadpaggqs adgcapsaht apgvpvpaph pvphgdmapr
      661 tgnsteseta pvsmeaeaea eaeaeas
//
LOCUS       WP_457693126             407 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457693126
VERSION     WP_457693126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44642
     Region          4..406
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mpkataaevg rvfreeygra vavlvrvfgd idvaeeavqd afstaaerwp saglppspag
       61 wiittarnra vdrlrreasr ddrhaqaall haggepaeeg pvrddrlrli ftcchpalap
      121 aarvaltlrl lgglttaeia raflvteptm aqrlvrakgk irdaripyrl ptdadlpdrl
      181 ravlavvyli fnegytassg eslvredlcr eairlgrllt ellpdepeam gllalmllte
      241 srraartgpd gdlvlladqd rsrwdgtlva egqalvrrcl rrnqpgpyqi qaainavhsd
      301 aptaagtdwr qilelydqll aldpspvval nravavaeve gpeaalalvd slpldryhvf
      361 hairadllrr ldrnteaaea yekalartdn taerhflqrs rqalprd
//
LOCUS       WP_457693130             154 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693130
VERSION     WP_457693130.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..154
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16352
     Region          <47..95
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <65..>127
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mdksstpsgr sladklnhlf etvspagrgp ynseeaarll ttsgvpisgs yiwllrrgqr
       61 dnptlrhlea laklfgvppa yffddqvtae vdaqlgllta lhdsgvhsva lraaglspes
      121 lesirevier vreleglprd pdgvreggpg sgap
//
LOCUS       WP_457693131             364 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Streptomyces nigrescens].
ACCESSION   WP_457693131
VERSION     WP_457693131.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648940
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39180
     Region          41..122
                     /region_name="ParB"
                     /note="ParB-like nuclease domain; smart00470"
                     /db_xref="CDD:214678"
ORIGIN      
        1 merlpvaadg agheaggsgr dggaaglqgh rtwegqeptl valallrpsd sprtagedsr
       61 hvqmlaeset plppivvhrp tmrvidgmhr lrvaelrget hakvlffdgs epdafvlavr
      121 lnathglpls radraqaadr virshpqwsd rliaaatgva trtvsairkr stengrqlnt
      181 rigrdgrsrp lsaaegrrra gelmarrpea slreiseaag ialattrdvr erlrlgqdpv
      241 ppklraaelk qtspagagag ggrkagavtv rtvvpaaesp taarsesqpa ldilrrdpsl
      301 rftevgrrlm fllslhsina pewqrlvdav pahcsrsvaq varqcaeewl wfadriesng
      361 rmag
//
LOCUS       WP_457693133             250 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693133
VERSION     WP_457693133.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27256
     Region          7..133
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mqqsvnfspa adfydktrgg eqrgrriapa iaertdpgkl lldagmgtgv valalkesgr
       61 svvgidlsha mltkavtrig pavanasltq lpfgdatfdq vysvwvlhvv gdqrrglaev
      121 arvlrpggry vvvpgmilfd dqpvsrimee iqrrtseadd raekivpiae qvglkavevg
      181 eleaavheht paqiadgleq rmlfhlwavd davfdekvap lvrelralpe pdvpvvrrtr
      241 rqvvvfekqg
//
LOCUS       WP_457693134             215 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional 4-hydroxy-2-oxoglutarate
            aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Streptomyces
            nigrescens].
ACCESSION   WP_457693134
VERSION     WP_457693134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Fullerton,S.W., Griffiths,J.S., Merkel,A.B., Cheriyan,M.,
            Wymer,N.J., Hutchins,M.J., Fierke,C.A., Toone,E.J. and
            Naismith,J.H.
  TITLE     Mechanism of the Class I KDPG aldolase
  JOURNAL   Bioorg Med Chem 14 (9), 3002-3010 (2006)
   PUBMED   16403639
REFERENCE   2  (residues 1 to 215)
  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   3  (residues 1 to 215)
  AUTHORS   Gefflaut,T., Blonski,C., Perie,J. and Willson,M.
  TITLE     Class I aldolases: substrate specificity, mechanism, inhibitors and
            structural aspects
  JOURNAL   Prog Biophys Mol Biol 63 (3), 301-340 (1995)
   PUBMED   8599032
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Conway,T.
  TITLE     The Entner-Doudoroff pathway: history, physiology and molecular
            biology
  JOURNAL   FEMS Microbiol Rev 9 (1), 1-27 (1992)
   PUBMED   1389313
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="bifunctional 4-hydroxy-2-oxoglutarate
                     aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase"
                     /EC_number="4.1.2.14"
                     /EC_number="4.1.3.16"
                     /GO_function="GO:0008675 -
                     2-dehydro-3-deoxy-phosphogluconate aldolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008700 - (R,S)-4-hydroxy-2-oxoglutarate
                     aldolase activity [Evidence IEA]"
                     /calculated_mol_wt=21683
     Region          8..214
                     /region_name="Eda"
                     /note="2-keto-3-deoxy-6-phosphogluconate aldolase
                     [Carbohydrate transport and metabolism]; COG0800"
                     /db_xref="CDD:440563"
ORIGIN      
        1 maadepldla aelagtglia mitepdapvv pdvvrelgaa glraveltlt tptaldalar
       61 avatgatlvg agtvrdrata raavdagahy lltpgvlpev ldeagrmgvp vvcgafttte
      121 vmdawrlgaa lvklfparlg gpaytaslcm afpdipivpt ggitaadlpd hfragahaaa
      181 lgrpligdal hggdmaevrs rtaelldavr avrar
//
LOCUS       WP_457693135             416 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate aminotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693135
VERSION     WP_457693135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Kafala,B. and Sasarman,A.
  TITLE     Isolation of the Staphylococcus aureus hemCDBL gene cluster coding
            for early steps in heme biosynthesis
  JOURNAL   Gene 199 (1-2), 231-239 (1997)
   PUBMED   9358061
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..416
                     /product="aspartate aminotransferase family protein"
                     /EC_number="5.4.3.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45870
     Region          35..403
                     /region_name="HemL"
                     /note="Glutamate-1-semialdehyde aminotransferase [Coenzyme
                     transport and metabolism]; COG0001"
                     /db_xref="CDD:439772"
ORIGIN      
        1 mlldrsfela rkaeeidala akrknviasd qmiegeypif vdrtsgayfw dvdgnryldf
       61 flsygtvvlg hadrdvddqv iaeirkgfat glskpvqtel vsellevipg aemamlmktg
      121 sdatgaavrl srsftgrdrv arfgyngwhd wcaqwdhgip ratrdlvdtf ayndldslra
      181 lferhpgeia cvvmmpfeve ppapgflegv reltrahgal lildemrsgf rmalggaqey
      241 fgvtadlatf skafangyai saltgradvl rrldhvhiss tfyansdama aalatlrklr
      301 sgpyleriha lgsrlqeglr eltekyaapv evvghppmpf ldfrlgseee nqaakrsfyt
      361 etiragvffh pnhhwfvcaa tteedidtai eaaragfeal vrdgyagaar sgeaar
//
LOCUS       WP_457693138             347 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457693138
VERSION     WP_457693138.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36987
     Region          1..252
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkvaivgfgt aggarlsgyr svpgadvaai vepaperrrv aaeqlpygrv vasldellaq
       61 ggidvvdvct ppayhvplah raltagchvi cekpvavsla daqeligtar shgrllypsh
      121 nygtspmmrl lrqavdggig rlesarfqil rdrhargvrg frpdwrrsre lagggilldh
      181 gthcvymalr lfgelpakis ctvgrpegap davdeeaavr mdfgsavcdi elswraglra
      241 nhysvtgtdg flridddrvt aegpdgprtl dlaspsrdqt hldwfppmfa dfrqtladpg
      301 rwhvpadeia gtarvietay rsaaaggapl aldgdpsrpg lptespa
//
LOCUS       WP_457693142             100 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Streptomyces nigrescens].
ACCESSION   WP_457693142
VERSION     WP_457693142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 100)
  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 100)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..100
                     /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=10901
     Region          15..94
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 magadrtvvg qehldtvlee vrhvleeqce ipaeqanavt ptapmadlgl dsitlayvft
       61 yferkhdltf engdidptry ttvgelveai arrvhapagh
//
LOCUS       WP_457693144             348 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457693144
VERSION     WP_457693144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39955
     Region          5..245
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mdtvprvtai itsrerfsya eeslasffrh tsipcqlvyv dvnsphdrwn rikriadehg
       61 iiavrvnkyv spncarnigl ryaegeyvvf ldndveyten wleplvacad eekaamvgpl
      121 ylhgplheqt vhmaggdmef sgawgerefv qtqrhfmkpl aevpeqelrr qkcdiiefhc
      181 alvrreifde vggmdegllt trehldfsqr vldaggtvwf eprsvityrm pppfaltdlp
      241 yfmlrwsdew tkdtlrhfan kygikpsyve rvtknrkgrq yllfeqvkpl ltsvlgtsgt
      301 rvakkvfqav epvgnralve laalrepelr wetyrpatpa arktttss
//
LOCUS       WP_457693146              99 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Streptomyces nigrescens].
ACCESSION   WP_457693146
VERSION     WP_457693146.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 99)
  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 99)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..99
                     /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=10496
     Region          16..90
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mshaydgqpr ttapgieelv rrtlaervga elagaipate kfydlgidsl dlvvtlatle
       61 recgveriad gelwdiadsv gsltaylteh atvlpgear
//
LOCUS       WP_457693149             470 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693149
VERSION     WP_457693149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=49369
     Region          7..470
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mttstpyeal vrwaaehpdr pavvhehgsl syatlarkva garryhlgrg haagqrvglv
       61 vrndpesiva llglaatgae vvlhdarstr herdradqla gtrariapps lgaaheagag
      121 tepphvshat alslvtsgtg glpkvvrkdw aatcansaaf adtagitgsd rilcttplhh
      181 afafgaallp alhtgatlvl aphppapsal adalrttgat vvqsvpflyr sllsrgeals
      241 vpalricvsa gepldretar awrhatgrnl rdqygatelg qlafaddrpa gplrlvpgir
      301 aavrdddgli redtdaegel cfrhegppvv yrglpeltaq attdgwfrtg digvlpgdgt
      361 vqvrgragrr itvagrkvdp aevelalscl pgvreclvsa ppagtpgppd rfvafiaagp
      421 evteltvrrh lagllspyki ptrihltgrl prtgsgkvha arlwqeagqr
//
LOCUS       WP_457693150             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ACP S-malonyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693150
VERSION     WP_457693150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33284
     Region          9..317
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mtvqtigegr yvlafpgags qlpgmayrlv rdhpaarevl acadeatglp larlctdgtp
       61 aelrppelsh pavvatglac aaalrahlgt rwappalvgg hslghfaalv eagalglsda
      121 lrivaerarl mgeqarvrpa lmtsvtglpp dtvtgwcaec ppdlgqavia cyngprhlvv
      181 sgdadavrwv agraadtpdv rvtdvatgva shsplmapvq kqlrpalttv rlapptvpvl
      241 lnsdgrpadd vgalradllc qlevpvrwht alravvrtgn rllldtgpgq vmaraarrhp
      301 eltplalnam eplkavlplg
//
LOCUS       WP_457693152             498 aa            linear   BCT 27-JAN-2026
DEFINITION  peptide MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693152
VERSION     WP_457693152.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..498
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51529
     Region          5..498
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 msveestart tsrirhprgl palwgtemwe rfsyygmrai lvlhlvapas qgglglpptt
       61 aagvfgvygg lvnllavpgg wladrlwgah rtvlggglvi aaghcalalp laaagtylgl
      121 lliavgtgll kpnistmlgg lydvpgapda hstarrdagf slfylginig afaaplvtgw
      181 lgervdwhag fgaaavgmll glavylrgtr qlrpagpppr tpataaqlrr aaawagcalg
      241 avaavvavaa aaglgvlaga lyalsaltlv vpalyfvvmf rapgldavdr srlrayiwif
      301 laatvfwmia eqggslislf aqrhidralf gwqiptgwfq svgplygmll agvfaalwlr
      361 lghrqpstaa kfalglaglg vatllmagag laasggqpas plwllaaflv qvlaelclsp
      421 tglsvttrla phrfagqims lwflsvaags alsaqvvrls dtlpyevyfa vlgtaallca
      481 aavalartsl rrlmrgvs
//
LOCUS       WP_457693153             599 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693153
VERSION     WP_457693153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 599)
  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 599)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..599
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63430
     Region          44..587
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mkatvtpqls gpavlrravq vspelrqglg tvaglallaa agrvvvpiav qqtidqgfra
       61 qggarlghvl vtaavcaaav latawityam nhrlyrtver glatlrtkaf rrvhdlspas
      121 ldgerrgglv arvtgdvdqf stflqfagml visfgqllvg svvmfafswv lalmvwavfl
      181 plllvlprlq rrlshaygrv rdragdmlav tgeavvgatv ihayhaqeli geridtaver
      241 hrsaqsraqr lvavtlsgge vaaaaaiggv vvlgvllgvg ghltagelva flflvtlfig
      301 pmqmtnevln elqnalagwr rvlsvvdapv evrdpgergt dlpegpvsvr fekvsyaypd
      361 gprvlhgvsa evaprsrvav vgetgsgkst fvkllarlsd pssgqvllsg tpltavrfas
      421 lrrrvvmvpq dgflfdatva dnirfsrpda sdeevgrala dlglddwlas lpgglhtrvg
      481 qrgdalsage rqlvalaray ladpdllild eatsavdpat evrlqqales atrgrtsvsv
      541 ahrlstaqha dlvlvfdqgr ivqqgtheel vgrpgvyadl yaawvsatgg kgpahgarr
//
LOCUS       WP_457693154             613 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693154
VERSION     WP_457693154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 613)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 613)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 613)
  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 613)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..613
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65807
     Region          11..587
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mttdvtpatg sraslrrrgl hvlrvairee pwvfcgalaa sllyggapva tswtlgwvte
       61 dvvmpafreg rtgfaalaaa glaifgvaml rvigvigrrv gagimqfrlq atyrrkvahr
      121 ylrlplawhq rhpagqllsn inadveavwa pviplptavg vvamllaamg amltvdpyia
      181 lvsvgvfpav gllnvvyqrr lsplasraqa lraevseiah esfdgatvvk tlgkedaetr
      241 rfaeaaqrlr daniavgrtr gafdpvldal pnlgiltvla vgtarlaaga ltvgdivqva
      301 ylftmiafpv rafgwllael prsavgwqrv hdvldareel phgelqlads gpiglgvrev
      361 syaysgtdvl hgvsleaspg htvavvgptg sgkstlatll vrladpytgv vqmdgvdarh
      421 mrpgelasal afvpqqtllf ddtvrgnicl gldfrdeevw ealelaqaad vvralpeqld
      481 arvgergatl sggqrqrial aralvrrprl lilddatssv dpqvearilr glrearrpst
      541 vfvvayrrat ialadevvyv ergrvldrgr heemlvrcrg yrelvnayds rddgddgpra
      601 avtvadtteg qsa
//
LOCUS       WP_457693155             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693155
VERSION     WP_457693155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27855
     Region          1..249
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 miaalegvgv rryttgqvil gaidwtvrsg ehwallgang agkttllrlv galmfptvgt
       61 vevlghrlgs vdvrelravi glasgaqkvp qdatghtvvl tgatgtvqpl wrkydaatre
      121 rahellteld ckeladrpfg vcsggqrari liaralmaep rlllldepfn aldlpsredl
      181 idalhrlavg rpelatvtvt hhleelspai gnalllrdgr vqasgpvdev ltgermtacf
      241 grpievsrha grwlarsgkr
//
LOCUS       WP_457693156              69 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457693156
VERSION     WP_457693156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..69
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7225
     Region          1..58
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mnvvvdlnrc qgyaqcafla pgvftmhgee sllyhpvvpd gqlekvrrav aacpvqailm
       61 geeagagar
//
LOCUS       WP_457693157             297 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693157
VERSION     WP_457693157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..297
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32459
     Region          5..296
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 mglvidipee lvatqtrfng aagrdfiaal peraaefldr wglkptgpsl ngmsalvlpv
       61 eradgtpaal kmqlldeese gepvalriwg gegvvqlldh dvdtntllle rldekrhlst
      121 lndsreatri lagllarlsa vpapgglrql gdiarqmldt vpdavrkvaa paerallksc
      181 aaavrevvde pgdrllhwdl hydnilaadr epwlaidpkp lagdpgfelm palandfgps
      241 evryrfdlmt evlgldrqra aawtlgralq nllwniedee deldqeqlai arlllgq
//
LOCUS       WP_457693158             532 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693158
VERSION     WP_457693158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 532)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..532
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56862
     Region          11..526
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mnqpaevqdq aarvqdlrve idgralvdgv slrvppgrit aligasgsgk tttglallne
       61 yppgarvtge vhvpdtlvgy vpqhpatvln parpvaallq diartqvrhl prrarrpeir
      121 hrilralaqa qlhdgetllh ryphqlsggq qqrvvlaqal ltgartviad epttgqdavt
      181 kqqiadqlaa varegiavll lshdldvvra lahdvhvmra grivesgape qlwsrpghsw
      241 trelltsaas aepsdgtlap stdagtpage ttsgpaaaka vlqvrsltar hgrstvlhtp
      301 elflppgcsa vvgrsgsgkt tlarclaglh rsydgevlld gvalprslrd rtreqlaavq
      361 yvfqdaraaf dehrpvlgqv mrsavrlrrv prpealaeae rtlstlglsg dlvrrrpael
      421 sggelqraal arallarprv licdeitsgq dtvtrrnlrt lltdlvrthp emslvlithd
      481 rdtatlatri avldggrlve qgptgqlltt pqhpltaall qpapevgats vr
//
LOCUS       WP_457693161             315 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457693161
VERSION     WP_457693161.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  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 315)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 315)
  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 315)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=34013
     Region          3..302
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(21,203..206,209,259,277..281,284,287..288)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(53,58,83,124)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mhtvtlgshg pavgaiglgc mgmswaydps ardedtsagv lrqaldlgvn lidtadvygp
       61 ftneelvgka lagrreqavl atkvgfvage qrlrrdgrpe hiraavdasl rrlgtdhidl
      121 yqlhrvdpev plaetwgama etvragkvrm lglsdvtaeq vrtahevhpv tavqaelslw
      181 trdalaqllp ftersgiaci ayaplgrgfl tgrfrspqdv pegdwrrgnp rfedaafaan
      241 lpmvdriqgv aerhgasaaq ialawvmtrg ryvvpipgtk npgflkqnvr asqvrltped
      301 lrvldglpep vgarq
//
LOCUS       WP_457693168             306 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693168
VERSION     WP_457693168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34056
     Region          14..304
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msvphaaqpv ldrirvgsap dswgvwfpdd dqqvpwqrfl devaeagyew ielgpygylp
       61 tdptvlreei arrslqvsag tiftslhhgp svwdktwahv sevatltqam gaghlvvips
      121 fwrddktaee lepreltveq wkhlttgmer lgkrvrdefg ldivvhphad thidteehve
      181 rflhatdsgl vnlcldtghy aycggdsvkl irtygerigy lhlkqvdpdi lsevvakgtp
      241 fgpavkqgvm cepplgvpal ppvleaaqel nvdlfaiveq dmypcppdqp fpiadrtrrf
      301 lrscga
//
LOCUS       WP_457693169             339 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457693169
VERSION     WP_457693169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36245
     Region          5..330
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtshetlgva vigtgrmgad hvrrlnevis garvaavvdi daarvkhlad giegctpytd
       61 paaamddpgv davliaspgp aheatlldaf ardlpvlcek pltpdaasal rvleaeqalg
      121 hrrvqvgfmr rydadyrtlk slldqgtygr plmlhnkhrn agstpgftna mmindsvvhe
      181 idvtrwllee eitavrvlrp aptgnapegl sdpqlilfet aggqvvdtei fvncgfgyqv
      241 sceavceggt arigddhgvf sntaghwgga itpgfverfe eaydrqvqrw vnatrrgeve
      301 gpscwdgyaa aavceagvra qttgervave lierpalyg
//
LOCUS       WP_457693170             473 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar porter family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693170
VERSION     WP_457693170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49622
     Region          40..449
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(40,158,161,165,275..276,280..281,284..285,373,
                     377..378,382,405..406,409)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 maaptgqmas agpregartr harrfivgia aiaalggalf gydtgvisga lpfmeghfgl
       61 tslgegiits alligaafgs liggrmsdal grrnsllwag avfiggalav alspdvpfmt
      121 varfvlglav gsasvitply lsevapphir grlvsfnslm ivsgqllayl inaflaqwaa
      181 wrwmlglaal pavalfvglf flpdtprwyi skgrrdeaar vlrrtlpaed vpaelaridh
      241 arsleadarr ggrqqlrtpw irrlllvgig laavqqitgv navvyfapki lastglgtga
      301 sitatiaigv isvlatalgm slidrvgrrp llltglagmt vslallgaaf hlphspavsa
      361 lilglmvlym afmqatlntg vwlllaemfp lkvrglamga avfvmwlvnf avalvfplll
      421 davgagttfw ffgamcvlsl vfckryapet kglaledled elrkaagaap apd
//
LOCUS       WP_457693171             122 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693171
VERSION     WP_457693171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..122
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12921
     Region          59..120
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mntnalshav krtavltata glltaglltg pasadspagg radtlaacay yngnaltvyg
       61 qrgdrvrqvq cllanrrylp wgdvtgyfgp ktraavkkfq srhhltadgk vgkktwyaly
      121 ha
//
LOCUS       WP_457693173             373 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693173
VERSION     WP_457693173.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 373)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..373
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39698
     Region          28..371
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mersnkraeg rtagradgrt gtrpgadrpp tirgvaerag vskslvslvl qgsprvsdtk
       61 rqavldaiee lgyrpnaaar slvarrthtv gvllndmrnp wfvevldgln sllqahglrm
      121 lmadgrldrr agqdfartfq elrvdglvvv gtlpdtdgla evaerlptvi agnheprlph
      181 tdlvandder garlatehli glghrriahi agqglvgelr rrgfeaamra hglaasavva
      241 ggdgteeggy raavrlltpp pvppgpgagr paaqrptavf afndiagvga lsaaqelglr
      301 tpadlslvgy dntylarirh lwlnsvnnas hevgrraarc lldrmerpda pagqqlvape
      361 leirgstapp rpd
//
LOCUS       WP_457693172              64 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693172
VERSION     WP_457693172.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..64
                     /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=7440
     Region          1..61
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtdrklwsyk eiaahiqvqp dtvrsyrkhg llpepdlveg gkpywladtv rrwvaqrpgq
       61 rgrr
//
LOCUS       WP_457693175             216 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457693175
VERSION     WP_457693175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22533
     Region          23..186
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdvlalygll vlttlpplvp nsallvsvgv lasrgelflp lillivagsa llgdllmyla
       61 arrfggpvra wmrrkprrra llewtsdriq ryglpfviav rflpsgrivg alasgvlryp
      121 lrkyvlgagi aeatwatysv glgylgsatt grplhaaaig fgvscavatv gaaiqwaarr
      181 ralrepsegg gegesgsprk gdgeepggra ssvaat
//
LOCUS       WP_457693176              95 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy-metal-associated domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693176
VERSION     WP_457693176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..95
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9221
     Region          27..92
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 maensscctp egschsggtd vqvgtvttty kvtgmtcghc egavsaeige iagvssvqav
       61 aatglvtvts qapldeeavr aavdeagyel vgqaa
//
LOCUS       WP_457693179             286 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693179
VERSION     WP_457693179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30269
     Region          11..272
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mshgtpslld rlslnqetvr qwslpeladg caragvrgvg lwrapvqqyg aaaaarlird
       61 aglrvtslcr ggfftaldpg eraaalddnr aaldeaaalg tdtlvlvsgg lppgsrdlpg
      121 arervadalg elapyaaerg vrlaleplhp myaadrcvvs tlaqaldlae rfpadrvgvv
      181 vdtyhlwwdd tvgaqigrag gpdgaagsrl aafqladwvt plpegvllgr gqlgdgsvdl
      241 rwfrerveta gyrgpvevei fnpalwardg aevlaeivqr vrthvg
//
LOCUS       WP_457693181             383 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457693181
VERSION     WP_457693181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42443
     Region          4..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mthttvriam ngvtgrmghr qhlvrsvlal rdqgglalad gtrirpepvl vgrsahklra
       61 laerhgvehw scdldsvlgd gtigiyfdaq vtaareeavr kaiaagkhly vekptassld
      121 galelarlaq eagvkngvvq dklflpglrk lrrlvesgff grilsvrgef gywvfegdlq
      181 qaqrpswnyr aedgggiaad mfphweyvlh elfgpvrsvq ahltthiprr wdesgapyda
      241 taddaaygif elaggivaqi nsswavrvhr delvefqvdg tegsavaglr hcriqhragt
      301 prpvwnpdvp asepfreqwq evpdnaafdn gfkaqwelfl rhvvrdepwr wdlaagargv
      361 qlaelgrrss aegrrldvpe lsr
//
LOCUS       WP_457693182             327 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional helix-turn-helix transcriptional regulator/GNAT family
            N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693182
VERSION     WP_457693182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18570235
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="bifunctional helix-turn-helix transcriptional
                     regulator/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36356
     Region          <49..153
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          170..311
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mttgtasdtt sgaardatpd vrelrrfnrf ytnligaldy grhlytpftl tearvlyeva
       61 hhervdaadl raslsldagy lsrllgkfed relitrgrse qdprrqritl teggreaagl
      121 leersqdaag slleqlpagd rarlvdsmrt irallgedae qppedrgpkm tlrtarpgdl
      181 gwmvernaal ysteygfdls yealvariva eyaeafdprw drtwiaeldg rragavmcvr
      241 dgrpgvarlr lllvepdarg hgvgrqlvds cvefareagy gemvlwtnsv lgaarsiyqr
      301 agfelvtesa hhsfgqdlvg qdwrlvl
//
LOCUS       WP_457693183             300 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693183
VERSION     WP_457693183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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 11437618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31247
     Region          14..284
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mvstgnthgt tpamrfafst lgvtgmpvad vlrlaadtgy qgvelrahpe epvhpllgmr
       61 eraavrkqfa dagveilava gyarvaaard tageeelaqe lselvwlaad lgapyvrvfp
      121 gggerpaaea dadaarrlaa vaplaaergv rvllethdsh rtgaaaarvl gpvghrqiga
      181 lwdvlhswlg geepadthaa laphlgyvqv kdvasaedrt plplgagavp laaaldtlrq
      241 dpagaqgpvp apegiydqga ggwlcweyek rwypeaaglp allapgrvhl qrlldgpads
//
LOCUS       WP_457693184             613 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 3 protein [Streptomyces nigrescens].
ACCESSION   WP_457693184
VERSION     WP_457693184.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..613
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64220
     Region          57..559
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mhsrrtvltt aaaaaaaatg agagpahgta paighqptvp apsaatrarl rrlisrmtpe
       61 ekvgqlfvmr vyghsatdpd padaaanqke igvanaaeli akyhvggiiy fgwahntrdp
      121 hqiadlsngi qkaaaaqrlp vpvlistdqe hgivarvgap atlfpgamal gaggsrddar
      181 taariageel famgirqdya pdadvnvnpa npvigvrsfg adpqavarmv vaevkgyqga
      241 giascakhfp ghgdtdtdsh vglpyihhsa eewerldapp fraaiaagid simtahivvp
      301 afdpsedpat lsrpiltgil rerlgydgvv vtdslgmegv rvkygdarvp vlalkagvdq
      361 llnppdlsva hgavltalke gelterdldt klmrilllke rrglfkdpyt thqavdrvvg
      421 trghlatadr iadrtttllr ndtgilplsr rrerrvlvag vdaaapsgtg gppttvlara
      481 lielgftata lstgltptqq rideavaalg erdavvvaty nvtaasgqrk lvdallatgk
      541 pvvqlavrnp ydiaqlggvk aalasyswtd velraaarvi agqrdpagrl pvpimradap
      601 tralyqighg lty
//
LOCUS       WP_457693186            1318 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693186
VERSION     WP_457693186.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1318)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 1318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 1318)
  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 1318)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1318
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=140803
     Region          13..586
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
     Region          732..1313
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 magtdterag warrltrdcr qyrkdvllal gsslagmavl alvplvpkli idevivrher
       61 algpwaallv aaavvvyvlt yirrfyggrl aldvqhdlrt rmfgaiarld grrqdelstg
      121 qvvgratsdl qliqsllfml pmmignvllf vislvvmavl splltvvala vapalwfiaq
      181 rsrarlfpat wyaqgqaaav agvvdgavsg vrvvkgfgqe eqetgklrev srrlfagrlr
      241 tvrlnarytp alqavpalgq vamlalggwm atqgqvtlgt fvafstylaq lvgpvrmlam
      301 mltvgqqara gvervyelid tepsiaerpd ahelpadapa tvefdrvtfg yaplhggega
      361 gpapaaarpv ledfslriea getvavvgms gsgkstvsll lprfydvsag rvlvgghdvr
      421 eltleslraa iglvpessfl fsdsvrdnia yghpdatdaq vraaaraaqa dgfiselpeg
      481 ydtkvgeqgl tlsggqrqrv alarailtdp rllvlddats avdarvehei healrgvmag
      541 rttlliahra stlaladrva vldggrlvdl gtqeeleerc plyrrlltdp eelggverdp
      601 agelagafdg efaaggller dpapdtegpd gvrdgaagra gadgtitpel wvrreqeaea
      661 ggagmaaraa vaagpgigaa maglpsptlg saraggppsp ellaqvaalp patdtpdvde
      721 dravrpersy glrrllhgfg gplafalalv avdalaglll pvlirqgide gvrrgaligv
      781 wtaaaialvv vlaqwaaqig gnrmtgrige rvlyslrlki faqlqrlgld yyereltgki
      841 mtrmttdvda lstflqtglv talvsmltff gilvallaid lqlalvvfat lppliigtyf
      901 frkqsvkaye larerisvvn gdlqesvsgl rivqafrrer qgaerfaars dayrqarvrg
      961 qflisvyfpf vqllssvaaa lvlvvgagrv gsgtltagal vayllyidlf fapvqqlsqv
     1021 fdgyqqasvs lsriqellre ptfpqlstsf eqgrpqspav erprevpalr gditfdevhf
     1081 hygegedpal agialtipag qtvafvgetg agkstlvklv aryydpscga vrvdgtdlre
     1141 ldltgyrrrl gvvpqesylf tgtvrdaiay grpdatdaev eaaaravgah amiatldggy
     1201 lhevaergrn lsagqrqlla laraelvdpd vllldeatas ldlateavvn qatdrlvgrr
     1261 ttlvvahrlt taaradrvvv ldrgrivedg shaqllardg ryaelwrtft geeeelaa
//
LOCUS       WP_457693190             227 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693190
VERSION     WP_457693190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23975
     Region          23..185
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnvptvrrgg aghgtapgaa pgprrsstrr rifdaavili aeqgfsattv deiadragva
       61 kgtvyynfas knvlyeellr dgidlladsl rraadatadr ggtrvdalda miragldfia
      121 gspaliqlyv aelwrtnrtw ratltsvrgr aqavvedvlr davrtgelsa eldipltasa
      181 llgmvlvaal dwqsfqpdrs vedvhaalsr llqgrvgagg gpvraea
//
LOCUS       WP_457693194             127 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457693194
VERSION     WP_457693194.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..127
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=13557
     Region          6..107
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 magdglqadi pslksggrdf tnvgrryqsa vtklknaltg legkdtppwg ddeigekfgv
       61 vyeglrdgmy esmghlaakl qeiggalntm adnhqadedf ndslmkqhia naeaeskqiv
      121 alksphv
//
LOCUS       WP_457693202             309 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457693202
VERSION     WP_457693202.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  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 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33840
     Region          15..307
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mndalrslld llalerieqd ifrgesrasv vprvfggqva aqalvaagrt vpadrspssr
       61 lrssrgdpip hslhayflrp gdpgapivyt vdrirdgrsf ttrrvvavqh gqpvfhlsas
      121 fqapeegleh qepmppapdp lelptaaeml prhaerflap gvaerllear aaidlryvde
      181 ppyvtvgepr dprsqvwfrt qgkldddgei prplldiclv tyvsdmtlld svllahgrgg
      241 wavgdvvgas ldhamwfhrp lradewllyd qesptaqggr glgkgrifta dgqlavsviq
      301 egvirvprd
//
LOCUS       WP_457693208             385 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693208
VERSION     WP_457693208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41438
     Region          4..383
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msldhrlpae leelrrtvea fahdvvapki geyyeqhafp yeivqemgrm glfglpfpee
       61 yggmggdyla lgialeelar vdssvaitle agvslgampv yhfgteeqkr awlpklcsge
      121 mlgafgltep dggsdagatr ttavreggdw vingskcfit nsgtditglv tvtavtgrkd
      181 dgsplissii vpsgtpgftv gapyskvgws asdtrelsfs dvrvpaanll geegrgyaqf
      241 lrildegria iaalatglaq gcvdesvrya kerqafgrpi ganqaiqfkl admemrahts
      301 rlawrdaasr lvhgepfkke aalaklysse iavdnareat qihggygfmn eypvarmwrd
      361 akileigegt sevqrmliar elgvv
//
LOCUS       WP_457693211             173 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457693211
VERSION     WP_457693211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5) (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..173
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=18527
     Region          40..172
                     /region_name="USP-like"
                     /note="universal stress protein (USP) and similar
                     proteins; cd00293"
                     /db_xref="CDD:467483"
ORIGIN      
        1 magheipepa drkqvadpma dleaaektrh scdpafrhgv vvgfdgsmss eralayaigm
       61 arrlgsglii vhvanrlptt vwagceppvf vdvpdhrtev iglelacadh ltevpwilve
      121 rggdichele evgreyeada ivvgsthgiv grifgsvagr larraqrpvi vip
//
LOCUS       WP_457693212             426 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693212
VERSION     WP_457693212.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (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   3  (residues 1 to 426)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..426
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45593
     Region          24..329
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqdsaavpd aarklaarrr reivavllfs ggpifessip lsvfgidrqd agvpryrllv
       61 cagedaplrt tgglelsapy gleaisragt vvvpawrsit qapppaalda lrraheegar
      121 ivglctgafv laaaglldgr patthwmyap tlakrypsvh vdprelfvdd gdvltsagta
      181 agidlclhiv rtdhgadaan alarrlvvpp rrtasdmghq ryldrslpee igadplaevv
      241 awalehlheq fdvetlaara ymsrrtfdrr frsltgsapl qwlitqrvlq aqrlletsdy
      301 svdevagrcg frspvalrgh frrqlgaspa ayraayrarr pqnggsepal rperaerper
      361 eraalgagsg drysaaalag hglataeage agkpqsdaya srlpespvgr gagrpvlpgq
      421 rerpvg
//
LOCUS       WP_457693214             216 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693214
VERSION     WP_457693214.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22600
     Region          4..216
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mstialfgan gtigsrilhe alrrghrvta vvrdpakitt thehltvttg dildpasvaa
       61 vakgqdvlvs avgggdgpgh iatirpaaes lvaglrtlgd aaprlltvgg agslrtpdgk
      121 qvwdaeglpg fllqimhahg daldfyrsvp dvrwtnlspa atiepgertg gyrtatddlv
      181 tdaegrsris tedyavavld eierprhpge rftvgy
//
LOCUS       WP_457693215             303 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693215
VERSION     WP_457693215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /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]"
                     /calculated_mol_wt=32422
     Region          46..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvkkrqegge pvpeirevaf sapagrpagv evltlaelra radacrlstp hrpgfhhlll
       61 ldrgrlvhsv dfrehvlapg dllwsrpgqv qhfgdltgae grlvlfeagf ldpataaaar
      121 iedwygppvr hpegaaargv aealrqlhte fgalgglple ihldvlrhll avlvlraahp
      181 ggapgeesgg ggavnatylr frdavergft rsrrvadyar slgyaprtls rateasagvg
      241 akefidrrvv leakrllahg dqsaariadr lgfadatnfs kffqrqtgtt piafrvavrg
      301 gag
//
LOCUS       WP_457693218             230 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457693218
VERSION     WP_457693218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  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 230)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..230
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25126
     Region          1..218
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 masvlvvedd qfvrsalirh lteaahtvrs vgtalealre vahvgfdvvi ldlglpdldg
       61 gealkmlrgi tdvpviiata rddeadivrl lndgaddyli kpfsvehlsa rmtavlrrsr
      121 aaaagaepps rvirvgglsi dplrrqaeld gvtldltrre fdllaflagr pgvvvprrel
      181 laevwqqsyg ddqtidvhls wlrrklgeta anprylhtlr gvgvkleppr
//
LOCUS       WP_457693220             286 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase [Streptomyces nigrescens].
ACCESSION   WP_457693220
VERSION     WP_457693220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30402
     Region          33..230
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 maksrrgrgg pepvtetvdg glaelrpdrd rprgwtllid gapqshvdld dpahldfsyq
       61 rrlghladla gpagkplrvv hlgggaltla ryvaatrprs tqqvveidaa lvhlirrqlp
      121 wdsgwrirvr ggdaraglak ipdgwadlii advfagartp ahltstefva evhralrpgg
      181 fyaanladgp plrflraqia tvrtvfpelc ltadpavlrg rrfgnavlla adgelpvael
      241 trraatdpqs grvehgrall dftggaapvt datalpspap padvfd
//
LOCUS       WP_457693221             112 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457693221
VERSION     WP_457693221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..112
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=11574
     Region          60..111
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mkrfvttaam taascamvlg gagiasasgd hgrgrhdhhd nnyrhdnyrh dhrglynhrs
       61 ganasgfaag spgilsgnnv qvpinipini cgnslnlvaa lnpafgnacv nr
//
LOCUS       WP_457693223             499 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar transferase [Streptomyces nigrescens].
ACCESSION   WP_457693223
VERSION     WP_457693223.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11496317
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..499
                     /product="sugar transferase"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52967
     Region          132..498
                     /region_name="EPS_sugtrans"
                     /note="exopolysaccharide biosynthesis polyprenyl
                     glycosylphosphotransferase; TIGR03025"
                     /db_xref="CDD:274398"
ORIGIN      
        1 mttesadahr sarvpppsav prpaaavrpp rgpgretlpp prpgrgvrpr tvaplmaadt
       61 latvatalli lgtgtapttl glllvgllll hshaglyrpg papstlndlp tllgraavcw
      121 caaaavlaav rpgqalppal lvgavavqta licggrtavh rarraaarrr pratlivgtd
      181 paarrlaavl hthpeygmrp vgvvtppslp pagsgtppgp vgpplprigs aqditraviq
      241 htvrdvvftl ppygdphtta llrrfiaqgs avwlagaaaa regrtphadt dhlrgfacrp
      301 ldtapprhgh ggkrlldltl aasglvvtap vllgcalavr lavgpgvlfr qerigrggrs
      361 ftllkfrtwq pcdeheaatr wsladecrms rvgrllrrts ldelpqlwnv lrgemslvgp
      421 rperpffveq flgtcpeyga rhrmpagmtg laqvhglrgd tsvedrvrfd nlyidswslr
      481 qdllillrtv asvvrlegr
//
LOCUS       WP_457693225             419 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693225
VERSION     WP_457693225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 419)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11660203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44186
     Region          2..320
                     /region_name="Glycosyltransferase_GTB-type"
                     /note="glycosyltransferase family 1 and related proteins
                     with GTB topology; cl10013"
                     /db_xref="CDD:471961"
     Region          274..375
                     /region_name="RfaB"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0438"
                     /db_xref="CDD:440207"
ORIGIN      
        1 mkvlhvitdl dmggaeqqlr lllrrlpahc evltltgpgp vaegieadgt pvfhlgmtgt
       61 rdltalprla glirdggydl vhthlyracv ygrvaarlag vravvatehs lgdaviegrr
      121 ltrgvrtlyr aterlgtatv avsdtvaarl rrwgvpeqri hvvpngieah rfgfdpaara
      181 lvrtrlglpl dafvvggvgr lvpgkrfdvl vravtqlpgv hlllagagpe remlrrmaeq
      241 fgsgdrihll gvrdgavdaa adgrgaagpd ipgllsaidv lvspspdeaf glavlealas
      301 glhvlygscp avdelpadqa pgarhfslnv helgtalrdl rrqgpgrlpv ppvvrrydit
      361 rsaealmsvy eqalagppar rgspavvppp qgrpaalpaa svslpdpsrs pdpsplpnr
//
LOCUS       WP_457693230             197 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693230
VERSION     WP_457693230.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21752
     Region          5..193
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mapriflarh gqtewslsgr htgrtdvpll degrrgakll gerlhrapwd glpgvevrts
       61 plvraketce lagfgdraqq wdalmevdyg ayegltpaei ksarpgwliw rdgvpegetl
      121 aevtaradev idwarsaerd vlvfahghil rtlgarwlgl disfgarirl eptslsvlgw
      181 aygepaierw ndtghlg
//
LOCUS       WP_457693236             604 aa            linear   BCT 27-JAN-2026
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces nigrescens].
ACCESSION   WP_457693236
VERSION     WP_457693236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 604)
  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 11472025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="putative bifunctional diguanylate
                     cyclase/phosphodiesterase"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65233
     Region          33..600
                     /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 mterdettke saearpapsg rcddtaaslg dyratfyaar vamavlnrdg lvlaanpafg
       61 elvgadpael vaataadltd lgadprvwta yrevlcgrsd rlrctrrlkh peghsvwvev
      121 tvepltpepl sgeermllsv adisdrhdll arlrhlqmhd pvtrlpnral fferlssale
      181 tasfapsgtg riglcyldld gfkavndtlg hrvgdrllsa vaqrltrcae saadrgtgrg
      241 ghlvarlggd efallvedst gtdqlaelaq cvldalqrpf dlagqrlsvs asigvveraa
      301 tgttatglmq aadttlywak edgkarwtlf dpernahrmt rqalsstlrp avdrgeftle
      361 yqplvglgdg raqgvealvr wrhpqfgtls pnrfialaee ngaivelgrw vleracyqar
      421 awqlahpgep lfvsvnvavr qvwdsdlvad vagilaetgl ppellqlelt esavmgsagr
      481 plqalqalsd mgvriaiddf gtgysnlayl srlpvsvlkl dgsfvrgfrs qehpnpadem
      541 ivealvalah rlgltvtaec vesaeqaerl rrigcdtgqg wlysrpvapd rvaalldagr
      601 htga
//
LOCUS       WP_457693237             398 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457693237
VERSION     WP_457693237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41693
     Region          31..382
                     /region_name="oxido_grp_1"
                     /note="luciferase family oxidoreductase, group 1;
                     TIGR03558"
                     /db_xref="CDD:274646"
ORIGIN      
        1 msgedeeirs sgetaadgir gtapgtapvp lsvldlvtvg agstasaavr tsvdiartae
       61 rrgfhrywva ehhsmpgvas sspavllahl aahttrirlg sggvmlpnha plviaeqfgt
      121 leamapgrid lglgrapgtd gataaalrrt erlgegalgs pllersrelg defpqqlael
      181 trflddsfpd ghpyakihav pgpvqatspg gvqdphrppl wllgssgfsa rlagslglpf
      241 afahhfsaan tlpaldlyra sfrpsevlae pyaligvaal aaeseqearr qvmtgalsmv
      301 rlrtgrpglv pgpeeaeayr fnelernfvd swlgnvvhgt pdavrqgldd lakrtgadel
      361 mitanahgga arlrsyelia dayglpgqgv vrggcgrw
//
LOCUS       WP_457693245             252 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693245
VERSION     WP_457693245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27210
     Region          13..242
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 malkpeptap fhsvqyalrv letvsrhaeg vtdaqiaret glspaqlghm lamlrregyv
       61 eqgtdgayvi gesllllgsg gdrdqalrdk lqltldqlrd svgaavyisr yidgevkilh
      121 yadgplapkv newaefhrta hasaigkcll aqldhdgrkd hlsrhktarl tsrtitnekv
      181 lfhkldsqpp tvpvldlqey avgtvcaavp itagatvgcl alsmplehah rlrqaadtln
      241 rqaapvllsl ai
//
LOCUS       WP_457693246             197 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Streptomyces nigrescens].
ACCESSION   WP_457693246
VERSION     WP_457693246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /EC_number="1.14.99.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20551
     Region          1..>197
                     /region_name="COG3397"
                     /note="Predicted carbohydrate-binding protein, contains
                     CBM5 and CBM33 domains [General function prediction only]"
                     /db_xref="CDD:442624"
ORIGIN      
        1 mrkkisaavi glgvlgvsll stgsatshgy sdappsrqal cangtvkdcg aiqyepqsve
       61 apkgfpaagp adgnicsggh qsfaelddpr ggawpgtkls pgqgytftwr ltarhattdf
      121 ryfitkdgyd pgkpltradl epepfmtvpm ggaqpeatvq hqgtvptqks grhlilgvwn
      181 iadtgnafya csdvdls
//
LOCUS       WP_457693253             259 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD-IIA family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693253
VERSION     WP_457693253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28017
     Region          8..254
                     /region_name="HAD_Pase_UmpH-like"
                     /note="UmpH/NagD family phosphatase, similar to
                     Escherichia coli UmpH UMP phosphatase/NagD nucleotide
                     phosphatase and Mycobacterium tuberculosis Rv1692 glycerol
                     3-phosphate phosphatase; cd07530"
                     /db_xref="CDD:319832"
     Site            order(13..17,45..48,151,184,208..210,213..214)
                     /site_type="active"
                     /db_xref="CDD:319832"
ORIGIN      
        1 maerkpiesw ltdmdgvlmh egipvpgada fikrlresgk pflvltnnsi ytprdlharl
       61 nrigldvpwe siwtsalata qflddqrpcg tayvigeagl ttalhdigyv ltdhspdyvv
      121 lgetrtysfe altkairlin dgarfiatnp detgpspqga lpatgsvaal itkatgidpy
      181 fvgkpnplmm rhglnvigah setaamigdr mdtdvlagle agmetflvlt gltrpeeier
      241 hpfrpsrvvd siadlidlv
//
LOCUS       WP_457693256             260 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693256
VERSION     WP_457693256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 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   4  (residues 1 to 260)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28309
     Region          13..260
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtdvtgdstd tfdnrplher iaadlrdeim ngdlapgakl qstarlkerf aasnatvqka
       61 lgllkeerlv vgragsavtv rehrqrtmrp asymapadsg dryrwlteae klgaqarsrl
      121 lrvaevappa dvsavlglpe ggtallrqql llidhepvel vssfypleia rgtaiakrqk
      181 ikggtpvlla elgypprlsv drvsarvptq eqftalrlpg dlpvlrtlrv vrsdgglpie
      241 atvmvkaghl yelqyeftae
//
LOCUS       WP_457693258             265 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693258
VERSION     WP_457693258.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27918
     Region          26..265
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mlvhsrparr aihllflvlf lpvfalpllv ivaasfassw sgtlpsgatl khyqdiahge
       61 alhalltsvl talaaslaal tagtwaalaa eklgrrtrrl ldalfllpva vpsvvvglsl
      121 lvafsrppfl lngtpqivil ahtvlvtafa yqsvtaaltr ldpayeqsaa glgarpayvl
      181 wrvklplllp sltaavglcf tlsmgelsat mmlyppewlp lpvqifaatd rgalfagaal
      241 avtlmaatll vllgvsrirt kasyr
//
LOCUS       WP_457693260             401 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693260
VERSION     WP_457693260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42002
     Region          22..391
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msasaatapa rtagrsaapv psasgirfdq vsvaygkhge htvldsfdlt vepgevmall
       61 gpsgsgktta lravagfvrp vsgrvliggr dvtalpphkr gigmvvqqya lfphmkvaen
      121 vafglkaqkt praeipgrva ealemtgmaa yagrhprels ggqqqrvaia ralairpgvl
      181 lldeplsald arlrsgmlae larlhrelpd vsilyvthdq iealtladri avldrarlqd
      241 cgtpqqlyrr prteftasfv gtanllpvtv rrggdgrgdg vdfagrplav pigdevaega
      301 tatlcvrphl vglgespqtg gpgegpktng prntlrgtlt dvqwrgathr lyvtvdghri
      361 ladvrelrta papgdevtlh fapedavivp aglaeggapd a
//
LOCUS       WP_457693262             256 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693262
VERSION     WP_457693262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 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   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28075
     Region          21..250
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mefpygqdpg apirsgvpeh gripkyyaak veiaallael gegevlpter elalrfevsr
       61 etlrqalrel ilegrlrrlg rgtvvagpkm eqplslasyt egvrgqgrkp grhlvgldrf
      121 pcppalagdl gleagdavwh mervlladde rvglestyva vervpdlatg fepdssfyay
      181 lherlgigfg daderletvl atpreallig tpgalpmlli hrlsrdtegr plervrslyr
      241 gdrfsftthl gtaasr
//
LOCUS       WP_457693263             401 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693263
VERSION     WP_457693263.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=39554
     Region          66..>94
                     /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          115..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 mssddisqgr agaagtdgap gadggtpats gnpgatgnpg vnlpalrghn aalvlgllra
       61 ageqgvsrle laahtgltpq avskitarlr aeglaaeagr rastggkpat vlrlvpgarh
      121 avglhldrde liavladltg apvavrrapl afeagarevl dtagrevaal raeaggppvl
      181 gagvacpgpl dhisgvlhrv tgapqwdgfp lrdalaerlg lpvvldkdtn aaalglaqgm
      241 psgagsfgyl hlgtglgagl vlggslyrgp rtgagefghq tvqgdgprcs cgrrgcieal
      301 claavargdl pgaaevlgtg aanlvelldi drvllggrtv lenpdgfrtg vaealgaqar
      361 argrtavpva lapggarava dgaaelvlap lfgmrrpglv p
//
LOCUS       WP_457693265             398 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693265
VERSION     WP_457693265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44267
     Region          3..83
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mppsieehtg triaryrkqr gllqqglair anvsksllsk vecgqkpasp afvaacaral
       61 svstsdllgq pyadelrrdr mdeliqpire gmenwdipld wetapravpl iradvqrall
      121 qrrqaeytdm vrdlpglide svqavhtasg eeqrqayecl agtfrcvftv awkfgyidla
      181 tvaldrlawt aprtdepgla amysflraqt tlssgryeig mrvidgalrd legqgarrpa
      241 gieamrgmlh lraaviagra kdrdhadsrl aearalaret gelpdygvtw gptnvgvhav
      301 aiaseldefg ravelaedvr iprgwtrsra ghhwmdlara htwaghpaqa ldclqrarra
      361 apqqtryhpt vretvlalkr rerkrsadla qyaewigl
//
LOCUS       WP_457693267             285 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693267
VERSION     WP_457693267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30372
     Region          68..280
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkllrvgtvg aerpalldgt galrdlsglv pdidgtllad egklaqlrta aasgelprld
       61 paglrtgppv arigkivcig lnyhdharet gavtpaepil fmkapdtvvg pddtvlvprd
      121 svktdwevel avvigrtary latdaqalaa vagyavahdv serafqierg gqwdkgknce
      181 tfnplgpwlv tadevpdpqn lglrlwvnge lkqdgttaeq ifpvaevvry vsrfmtlypg
      241 dvintgtpag vamgrpdpkp ylragdvvel eidglgrqrq elkda
//
LOCUS       WP_457693268             385 aa            linear   BCT 27-JAN-2026
DEFINITION  YidC/Oxa1 family membrane protein insertase [Streptomyces
            nigrescens].
ACCESSION   WP_457693268
VERSION     WP_457693268.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Hennon,S.W., Soman,R., Zhu,L. and Dalbey,R.E.
  TITLE     YidC/Alb3/Oxa1 Family of Insertases
  JOURNAL   J Biol Chem 290 (24), 14866-14874 (2015)
   PUBMED   25947384
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Keil,M., Bareth,B., Woellhaf,M.W., Peleh,V., Prestele,M.,
            Rehling,P. and Herrmann,J.M.
  TITLE     Oxa1-ribosome complexes coordinate the assembly of cytochrome C
            oxidase in mitochondria
  JOURNAL   J Biol Chem 287 (41), 34484-34493 (2012)
   PUBMED   22904327
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Funes,S., Kauff,F., van der Sluis,E.O., Ott,M. and Herrmann,J.M.
  TITLE     Evolution of YidC/Oxa1/Alb3 insertases: three independent gene
            duplications followed by functional specialization in bacteria,
            mitochondria and chloroplasts
  JOURNAL   Biol Chem 392 (1-2), 13-19 (2011)
   PUBMED   21194367
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Ravaud,S., Stjepanovic,G., Wild,K. and Sinning,I.
  TITLE     The crystal structure of the periplasmic domain of the Escherichia
            coli membrane protein insertase YidC contains a substrate binding
            cleft
  JOURNAL   J Biol Chem 283 (14), 9350-9358 (2008)
   PUBMED   18234665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..385
                     /product="YidC/Oxa1 family membrane protein insertase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0032977 - membrane insertase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39211
     Region          3..234
                     /region_name="YidC"
                     /note="Membrane protein insertase Oxa1/YidC/SpoIIIJ [Cell
                     wall/membrane/envelope biogenesis]; COG0706"
                     /db_xref="CDD:440470"
ORIGIN      
        1 msmfgflgda lahgaqaiap lfgsaamaaa ivlftlgvra alhplaraaa rgekartala
       61 pqlaelqrkh kgnperlqka madlyaktgs splagclptl lqlpvffvmy hlfstgsggl
      121 ldhtllgapl gghwtealah ggvlgpqglv ylglfvliaa vatwnfrrar atmakapqpa
      181 agnpavpgma smakvmplls fgtlitvavv plaaglymvt tttwtacera llhrdrgrda
      241 qeagtagaag gaakgktgpa kgktgpakgk aapaaertsp dgapataaad gasgervprq
      301 rpaqqradrr tpksraarqr aararansqs hsqanaqahs qaransqara nsqaraasrn
      361 gsrpageags qsgggarehi gttpq
//
LOCUS       WP_457693270             633 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457693270
VERSION     WP_457693270.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..633
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68479
     Region          18..609
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrdisvpala aplrtgglad svfdtaahqp dfaqlarcdd rtpgswlevs aaefrdevia
       61 larglladgi rpgtrvalms rtryewtlfs yalwaigael vpvyptasae qlrcilagak
      121 vtaivvenea qamtvaeacd erarlrrlwq ldldcvrrlt eegtrltead vhrlrhavtp
      181 dtvaaivyts gttgrprgcv ithanlaagc dtlyagwggl laapgerpsl laflpfahiy
      241 glmvqvaclr ggvklahqpd vtsdellpal asfrptflfa vpyvfekica rarqaaeqag
      301 rrrtfdaamt vavryaeala aeaqgtgrgp dpflrarhal ydrlvysrir ellggrvrta
      361 vsggsplfre lgllfsgvgi tvydgyglte tsgaitvqpp grvrfgtvgl plpgsavhla
      421 ldgevwvrga vvfagyleed deapgsglyd gwlatgdlgh ldedgylvit grkkdiiits
      481 ngksvapqgl eqrlcahpli sqcvvvgdnr pyvtalitld pealdhwhkl reepgtdsga
      541 ptpeeqlqae vrravarana svsraesira frvlpgefsq esglvtpslk lrraaivrry
      601 aaeidalyaq gqreepetrq drrrwaaagl yar
//
LOCUS       WP_457693272             166 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693272
VERSION     WP_457693272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17375
     Region          7..146
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mpsgadllta rlvlrpwsdg elaavldgtp qphwaadfpa dgdrviagft agnpdargvy
       61 gqrqilerdg grvvgaiglf wpprdgslei gygivpsrrg rghaseaara lvafaftapg
      121 vhtvradvel snpasgrvle kaglvrwssd drlarfrlta peaaag
//
LOCUS       WP_457693281             317 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Streptomyces nigrescens].
ACCESSION   WP_457693281
VERSION     WP_457693281.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=31087
     Region          1..295
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mqtdlsaald iggtkiagal vdthgrlvvr avrptpadkd gatvmravae vvgelaagpd
       61 warvaavgig sagpvdaatg tvspvnisgw rdfplvagvr alvgerpvvl vgdgvamtaa
      121 ehwqgaargh analcmvvst gvggglvlng rlhpgptgna ghighisvdv egdpcpcgsr
      181 gcveriasgp niarralahg wqpgpdgdts aaavaaaaha gdpvalrsfe raaralaagi
      241 aatatlveid iavigggvag agevlfgplr aalrdyatls fvsglkvvpa qmgtdagvvg
      301 aaaaaqqsrl dafvpap
//
LOCUS       WP_457693282             346 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693282
VERSION     WP_457693282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  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   2  (residues 1 to 346)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36949
     Region          15..338
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtdtargtsr rygtrptmkd vaaragvglk tvsrvvngep gvtpdterrv qeaitalgfr
       61 rndsarilrk grtasiglvl edladpfygp lnraveevar shgallings saedpdreqe
      121 lvlalcarrv dglviipaad dhrylepeia agiatvfvdr pagridadvv lsdsfggaqd
      181 avahliahgh rrigfigdqp rihtaherlr gyrtamaaag lpvdeswvsl gptapervrs
      241 aatamlagpr pvtalfagnn rvtvtavrvl aerprpvalv gfddfeladl vdpaitvvaq
      301 daarlgrtat nllfrrldga ddaprrmeip trliprgsge ippses
//
LOCUS       WP_457693286             320 aa            linear   BCT 27-JAN-2026
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457693286
VERSION     WP_457693286.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32541
     Region          3..319
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 maevlvyvdh vdgavrkptl elltlarrig epvavhlgpn aeeaakvlae hgavkvlaad
       61 apefaeylva pkvdalqaay davspaavll pssaegkeig arlavrigsg iitdavdlea
      121 gdegpvatqs vfaasyttks rvskgtpvit vkpnsaapea apaagtveql avtvadsskg
      181 tkivsrtpre stgrpdltea aivvsggrgv ngaenfpvie aladslgaav gasraavdag
      241 wyphtnqvgq tgksvspqly iaagisgaiq hragmqtskt ivainkdaea pifdlvdygv
      301 vgdlfdvvpa ltdevktrkg
//
LOCUS       WP_457693287             168 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693287
VERSION     WP_457693287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17209
     Region          15..163
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mtalpglgtp rtaspellrs vfrqhaagva vitapgsrpa gftatsltsv aadppllsfg
       61 vgtgssswpa vseaehigvh ilgehqqela atfarsgadr fgpatswhtg pegvplldgv
      121 lawmvckvva rvpagdhclv laqpvvgdpa vpgrpllyhq grfnalrd
//
LOCUS       WP_457693288             139 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Streptomyces nigrescens].
ACCESSION   WP_457693288
VERSION     WP_457693288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14721
     Region          46..137
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtglmvciav laaasafgvw hqrrngrltv rerddtarlg aaeigaalge ratllqfssa
       61 fcqpcratrr tltevagmve gvahveidae dhldlvrqlh vlrtptvlvl dadgaivrra
      121 sgqprkadvi aalgaavrd
//
LOCUS       WP_457693290             238 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693290
VERSION     WP_457693290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25942
     Region          4..210
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 maelvyppvi gaartlfkal dlkfdiagtd hiprrggavl vsnhigyldf vfagltarpa
       61 krlvrfmake svfrhkvsgp lmramkhipv drgqgmhayk haltalrsge iigvfpeati
      121 sesftlktfk sgaarlaqea gvpllpvalw gtqrlwtkgh krdlgrnhfp itirvgeple
      181 adpaeqaeki tdrlrsrvqd lleaaqrayp vrpkgpedtw wipahlggta paapgsla
//
LOCUS       WP_457693291             241 aa            linear   BCT 27-JAN-2026
DEFINITION  B3/B4 domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693291
VERSION     WP_457693291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Roy,H., Ling,J., Irnov,M. and Ibba,M.
  TITLE     Post-transfer editing in vitro and in vivo by the beta subunit of
            phenylalanyl-tRNA synthetase
  JOURNAL   EMBO J 23 (23), 4639-4648 (2004)
   PUBMED   15526031
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Mosyak,L., Reshetnikova,L., Goldgur,Y., Delarue,M. and Safro,M.G.
  TITLE     Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
  JOURNAL   Nat Struct Biol 2 (7), 537-547 (1995)
   PUBMED   7664121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="B3/B4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=25651
     Region          14..211
                     /region_name="B3/B4"
                     /note="B3/B4 domain (DNA/RNA-binding domain of
                     Phe-tRNA-synthetase) [General function prediction only];
                     COG3382"
                     /db_xref="CDD:442609"
ORIGIN      
        1 mssssqvsdi acalhvsdev ralapgfacl aveahgltng psdeagaall ddatrrlver
       61 ldgrppqddp hiaawraayt afgakpsrtr nsaealarra ladgglprin rlvdlynals
      121 vahlipvgge dldriqggmr lvratgeepf vtaaggaetv eypdagevvw cddegvtcrr
      181 wnwrqgvrtr ltedsvsalf llermapmtl delaaagael aealhracpd arieigeira
      241 c
//
LOCUS       WP_457693293             356 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693293
VERSION     WP_457693293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..356
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38959
     Region          16..355
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtgaktdarq hhdpeirgfa sdnyagahpe vlaalalang ghqiaygedd ytahlqrvfr
       61 shfgqraeaf pvfngtganv valqavtdrw gaviaaesah ihvdecgape rvgglklltv
      121 ptedgkltpe lidrqaygwd dehrampqvv sitqstelgt vytpdeirai cehahergmv
      181 vhldgsrian aaasldvpmr aftnavgvdi lsfggtknga vfgeavvvln pdrvramkhl
      241 rklsmqlask mrfvsvqlea llakdlwlrn arhantmaqr laagvreigg veilypvqsn
      301 gvfarlphdv serlqkryrf yfwdesagvv rwmcafdtae edvdgflaal reelgr
//
LOCUS       WP_457693295             227 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces nigrescens].
ACCESSION   WP_457693295
VERSION     WP_457693295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24576
     Region          1..224
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 msfltighrg mmgvepentl rsfvraeheg ldvieldlhl skdgalvvmh dadvdrttdg
       61 agpiaertla elreldagqg eripvfeevl eavkaplqae ikdvaaaqal aevmrsrdlv
      121 grvdvisfhd ealaairtll pgvrtalvgs rygadvvdra lavgatmlsl nirrltlelv
      181 erahaaqlkv vawtvnthdq lrlarglgld gvvtdqpeiw ravrfta
//
LOCUS       WP_457693296             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693296
VERSION     WP_457693296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30605
     Region          56..281
                     /region_name="PBP2_peptides_like"
                     /note="Peptide-binding protein and related homologs; type
                     2 periplasmic binding protein fold; cd13530"
                     /db_xref="CDD:270248"
ORIGIN      
        1 mrlanrpfrl aacatvallv aavgcapqda spgagaagpg kqscdrgqlp tvadgkltvg
       61 tdkpayapwf hdddpadgkg fesavayava rqlgydkgav hwqtvpfnna fapgekkfdf
      121 dinqisisaa rkravafssg yydvrqavia lkgsraarak siadlrrvkl gaqvgstsld
      181 vlqdtvrptq ppavfqkndl aksalkngqv dailtdlpta fyitsaevkd aevvgqfaat
      241 gaaeeqfglv ldkesritgc vtaavdtlrk ngtlaalekk wltdavsvpv lk
//
LOCUS       WP_457693297             294 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693297
VERSION     WP_457693297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31567
     Region          <118..288
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mvktrtaqeg addgyvpspr rierervkra rarratsvaa lstlvtgavl flvitrspgw
       61 prtretffsl eyarmalpkv ldglllnlrl lvvcgaavlv lglllavart lrgpvffplr
      121 alaaaytdff rglpliicll mvvfgvpalr lqgvttdpvl lggsalvlty sayvaevfra
      181 giesvhpsqr aaarslglsg gqalrfvvlp qavrrvvppl lndlvslqkd tglvsiagav
      241 davyaaqiia gkdfnftpyv vaglvfvalt ipmtrctdwi tarmdrrraq gglv
//
LOCUS       WP_457693298             270 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693298
VERSION     WP_457693298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28989
     Region          25..264
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msttddtprp aveaagpaap dggpvlrles vrktygrgtv vlrdvdlevp phtvtaliga
       61 sgsgkstllr canlleeidd gaifldgaei tdpradvdav rrrigvvfqa ynlfphmtvl
      121 dnitlaprrv hgvpraeaea rarellerlg lggrageypd rlsggqqqrv aivralagrp
      181 rlllldeita aldpelvgev lgvvrelkee gmtmviathe mgfarevadq vcfldggvvl
      241 ergtsaqvfg apqhdrtrqf lqriiqagrl
//
LOCUS       WP_457693299             188 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693299
VERSION     WP_457693299.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20926
     Region          8..159
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mptseltfrt aldadvpglv gliesayrgd vsrsgwttea dllagqrtdp dgvtavvrhe
       61 tgrllvaerd geliaccqle hrgdhayfgm favrpelqgg glgkvilaea ertaqdiwga
      121 remrmtvirq rtelidwyer rgyrrtgert pfpygderfg ipqrpdlefe llvkplgqgl
      181 sdgawprp
//
LOCUS       WP_457693304             232 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693304
VERSION     WP_457693304.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24865
     Region          4..207
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mttikgvlfd fsgtllriep aeswlraala asgtamadae iapraaaler agalpggdpp
       61 gempaalaal wkirdrdarh hravytglar qvplpepely dalydrhmta aawqpypdaa
      121 evlaelhrrg trigvlsnig wdlrpvlrah gldryleacv lsyehgiqkp dpqlfavacr
      181 elgldpsavl mvgddrtadg gatalgcsfl pvdplpvdrr pdglrpvldl vg
//
LOCUS       WP_457693312             687 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693312
VERSION     WP_457693312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..687
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72344
     Region          280..677
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 msgatvaest ggallgrlag lrervaglve rrsaddptaa dplrglyvtp etarrlaaqa
       61 paegtgasyt adradtgepa dqapgpsdrs aalagrfgls aldlhillaa lapdvdrgfe
      121 plygylnddv grrratvala ldlagtgpye paararfhpg apllsggllv iededrplpg
      181 ralrvpervv ahllgddgld pelcgsevel lsaeqraagp tgsgartdda gfagrlaala
      241 serplavhlr errpgtaaep vtdglrragl pvlryrpdgd rddraglaga llrearlrra
      301 avvvgplper pdglvralag gdvpvvffgs epydpgwapd sglfaldapd dgasadevws
      361 telgsvgfdl aaavapyrlg aaqirraara atalaafdgt pvtaahiqhs arrqsaplld
      421 rharrvppav gfdglvlppe plsllhelvq rarhrekvlg twrlrtgggr grgvvalfag
      481 esgtgktlsa evvaselgld lyvvelssvv dkyigetekn lerifseadr tdavllfdea
      541 davfgkrsev ksshdryanl esayllqrle afdgiavltt nlranideaf trrldlvvdf
      601 pfpdaeqria lwrsclaatp caddlgldvc akefelsgga irsaavtagy laagrggpvt
      661 aadvragarr eyrkmgrlvp dasplwd
//
LOCUS       WP_457693314             970 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693314
VERSION     WP_457693314.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 970)
  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 970)
  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   3  (residues 1 to 970)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 970)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..970
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=102048
     Region          34..283
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          206..921
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 magrqgqgse gavrgdadel kgaegasgpd rgdrfrfqll gpvrawrgdr plnpgspqqr
       61 avlavlllha grpvsvpqlv dalwgeqppp ravgtlrtyv srlrgllepd rkprqhahll
      121 vssgggyalr vpgetldsag fetrlvtarr lreagdtaga yeqlrgalal pagvalaglp
      181 gpyaqrqrdr ltelcvtaqe elfdcvvelg ghaeaiaglr afaaehplre raqallmral
      241 hragrqaeal aayaatrhal htelgaepgr elralyeelr arpagsgpga rsgpgagpag
      301 drarpdryrd rtgdgrdrrp rpprpardts rigpppvpaq lppdiadfag raeavahlap
      361 alrgaagara pvvatlsglg gvgktalavh vahavrahfp dgqlyvdlqg pglapedssa
      421 vlthflralg vaesavpdgp aqkaalyrsl lagrevlvll dnardsaqvr pllpgapgca
      481 vlvtsrartl alpgadrvdv evmpegealg llgaivgaer vaaeptaare lvtacdglpl
      541 avriaaarla srpgrsmadl varlseerrl delrvgdvgv eatfrvgyea lgpglahafr
      601 alalcgmpsf crgaaaalld ttddeaeaav ealvdaglve lhgedryryh dlvglfarrl
      661 gerhdsswer saaqhrffdy vlatvltavr liephrvlpd llrrpdspgr tladadaare
      721 wlhdahprly aaveraldaa pgllgsavdl ltawshvlss tarhrdlepl vrravdtarr
      781 hdddaatala lcllgtphhg teryaraera lreslrpaha sagppvsart aapepaaapa
      841 amdrerpalv kvapdgisal grraegnrlf ahtarayvts grssevdeas tevlsaaqel
      901 rsegtlgrir ylsqaagrra rlgsgeperg pplpapappp gcgcgcgcan megavsvgra
      961 atlpgsckep
//
LOCUS       WP_457693317             525 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail sheath family protein [Streptomyces nigrescens].
ACCESSION   WP_457693317
VERSION     WP_457693317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Bock,D., Medeiros,J.M., Tsao,H.F., Penz,T., Weiss,G.L.,
            Aistleitner,K., Horn,M. and Pilhofer,M.
  TITLE     In situ architecture, function, and evolution of a contractile
            injection system
  JOURNAL   Science 357 (6352), 713-717 (2017)
   PUBMED   28818949
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Ge,P., Scholl,D., Leiman,P.G., Yu,X., Miller,J.F. and Zhou,Z.H.
  TITLE     Atomic structures of a bactericidal contractile nanotube in its
            pre- and postcontraction states
  JOURNAL   Nat Struct Mol Biol 22 (5), 377-382 (2015)
   PUBMED   25822993
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..525
                     /product="phage tail sheath family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=56046
     Region          241..515
                     /region_name="COG3497"
                     /note="Phage tail sheath protein FI [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442720"
ORIGIN      
        1 mptylspgvy veevasgsrp iegvgtsvaa fvglaptgpl neptlvtnws qyvaafgeft
       61 dgyylahsvy gffnnggtaa yvvrvggtge gepqaaaape apraltagep talgsfkvsa
      121 iaagsangga ltvevqdveg egsadrfklv vrdgdkvves fdvsakkssr nyvvaqvkqr
      181 skaiaieeav paaqvtkpda qnvtlappip apatpagtga veqlasgqfi gdsadrtgfg
      241 glealdevnm vavpdlmaay qqglvdleqv kavqlgliah celmgdrmav ldpppalnar
      301 dirkwrqeia gydsryaaly ypwikafdpa tgqtrtipps ghmagvwarn dsergvhkap
      361 aneivrgaid lelqitrgeq dllnpvgvnc irafpgrgir vwgartmasd pawrylnvrr
      421 yfnyleesil igtqwvvfep ndqalwarir rnisaflvne wrsgalfgqr pedafyvkcd
      481 aetnpvesvd vgrvvceigi apvkpaefvv frlaqfsggg gelee
//
LOCUS       WP_457693328             194 aa            linear   BCT 27-JAN-2026
DEFINITION  uridine kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693328
VERSION     WP_457693328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolution and classification of P-loop kinases and related proteins
  JOURNAL   J Mol Biol 333 (4), 781-815 (2003)
   PUBMED   14568537
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426306
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="uridine kinase family protein"
                     /EC_number="2.7.1.48"
                     /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=20717
     Region          16..187
                     /region_name="Udk"
                     /note="Uridine kinase [Nucleotide transport and
                     metabolism]; COG0572"
                     /db_xref="CDD:440337"
ORIGIN      
        1 mdrdlaslaa rlctappscg psrliavdgh agsgkstfag rlaeelggap vvhtddlath
       61 eelfawserf aaqilaplsr getarygvyd wvrgafteer alapaplvlv egvgagrral
      121 rpylacllwm elasehswer gqlrdgpgls afwsgwipae rahfaadpsr pyadflvhqg
      181 qmgyevamgp sgts
//
LOCUS       WP_457693336             260 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693336
VERSION     WP_457693336.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27337
     Region          3..208
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 matilvtggt gtlgrplvdr llddghdvrs lsrrphtgte rprprsyavd lrdgtglpea
       61 magvdtivhc attpaggdme aagqlvqaak aagiphlvyi sivgvdrvpl ryyrtklave
      121 rliedsglgw tvlrttqfhd lvlqvikaga rspvlpvptg vrvqpvevre vaarlaelta
      181 gnpagrvpdm ggpevlsare lvratleagg rrrllvplwl pgasaaalrr ggnltpehad
      241 gqrtyaefla eragvgvtgg
//
LOCUS       WP_457693337             425 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693337
VERSION     WP_457693337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=41648
     Region          22..97
                     /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(22..23,37..39,48..51,53..54,57..58,60..61,74..76,
                     81..83)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(37,40,90)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          86..407
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mhppraaaag rtaspatarl indrlalqll qfegpltagq lksltglsrp tvadlverlq
       61 eaglitvvge sgaqrrgpna rlygivadra hlvgldlrth svtvavadll grvraehtvp
      121 idpdgapdta vatalaavdk alaaagapap htiavgapgl vdpatgrlgg tdwvpswhvg
      181 lvgalrartg vpvllenevn laaiaeqrdg aahdrdtfvl lwlgqgtgaa vvldgtlrrg
      241 asggtgeigf lpvpgtgalp sasgcdggfh slagsaaict laaehglssg aaagpdgane
      301 pssgtgaptd appgesfvra avaagdagaa fldalaaria lgvaavcavl dpgcvvlgge
      361 ighgggaala drvaghlarl splrtdvrag avggravllg avraardaaq nelfgaagpg
      421 vsprp
//
LOCUS       WP_457693338             409 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693338
VERSION     WP_457693338.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40784
     Region          22..388
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,149,
                     152..153,156,224,227..228,231..233,236,264,268,317..318,
                     322,326,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 magngtpddt aplphtglrr arwsvavvfl ihgsvtgnfa tripwiqdht alspgqlgla
       61 lafpaigasl amplagrish rfgartalrg llalwtlslv lpalspglya lcpallmyga
      121 asgmsdvamn algvetedrl gkpimsglhg mwsagallgs aagtvaahag wdarlhlaga
      181 alvltllgal acrgvldlrs apeehppprf alpprsalvi gaigfcavfa egagldwsav
      241 ylrdvlgtda glaaasttaf actmtvarla gdkvvarfga vrtvraggvl aaagglliva
      301 arhpavamgg fglmglgiav vvplaftaag rsgpapsqai agvatityts gliapsaigg
      361 laqatslpvs fmlvttlacg lvagarvlrv psrtasgsap avtgdlers
//
LOCUS       WP_457693339             162 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457693339
VERSION     WP_457693339.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..162
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17927
     Region          17..150
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msveplqttt vpygelvpvt vhfddldalg mlhnsrypll aerawaeywh dqgfgfdgdw
       61 aaagdmcnvi kemhvtyers vtrpghyaah lwverlgrtg ltygfrlcsa dgaetyargh
      121 rvlvridaqt lrptpwsdra raiagrllrp easdagtead aa
//
LOCUS       WP_457693340             187 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693340
VERSION     WP_457693340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19834
     Region          5..175
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mansallvmd vqqdivdiad dgsaylprlr taidgartag ipviyvviel rsgqpevspr
       61 nrvltaavqa glftegapgt avhhavapqq gdivvtkrra safsgsdldl vlrardidsl
      121 vltgiatsgv vlhtlcqand rdfgltvlad acldtdpevh rvlterlfpq wsdvvavedw
      181 lkaiasq
//
LOCUS       WP_457693346             567 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693346
VERSION     WP_457693346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63141
     Region          48..543
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtstvptaaa hhadaqppit mfgpdfpyay ddflahpagl gqipatehgk evavigggls
       61 giitayelmk mglkpvvyea dqiggrlrtv gfdgtgaega gltaemgamr fppsstalqh
      121 yidlvdlktt pfpnplaadt pstvvdlkge shyartvddl pevyhqvmda wnacleegad
      181 fsdmnqaire rdvprireiw srlvekfdnq tfygylcdst afksfrhrei fgqvgfgtgg
      241 wdtdfpnsil eilrvvytea ddhhrgivgg sqqlplrlwe repakivhwa pgtslsslhd
      301 gtprpavtrl hrtagnritv tdahgdirty eaavftaqsw mllskiacdd slfpidhwta
      361 merthymess klfvpvdrpf wldkdeetgr dvmsmtltdr mtrgtylldn gpdepavicl
      421 sytwcddslk wlpleanerm evmlkslsei ypkvdirkhi ignpvtvswe nepyfmgafk
      481 anlpghyryq rrlfthfmqd rlpedkrglf lagddiswta gwaegavqta lnavwgvmhh
      541 fggatdatnp gpgdvydeia pvelped
//
LOCUS       WP_457693343             461 aa            linear   BCT 27-JAN-2026
DEFINITION  uracil-xanthine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457693343
VERSION     WP_457693343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47448
     Region          12..433
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 magfgwklhg dgrhlkpgev vrpgerltwg rtialgaqhv vsmigacfva pvlmgldpsl
       61 almasgvata lflvltrgri psylgsslsf vgvsvviagq ggdagtltga mlvvgaclag
      121 cgiaihvvga rvihavlppt vtgavvmlig fnlapvtast ywpqdqwtal atmlftglal
      181 vvlrgfwsri aiflglvfgy alswildrta gkihsvngag kltdhwridf sgvekadwig
      241 vptfhapnfs asavlvalpv lvaliaenag hikavgamtg dplddkmgma imadgtatvl
      301 stavggpatt tyaenigvma atrvystaay waaagfallf glcpkfgavv aaipggvlgg
      361 itvilygmig llgaqiwvrn kvdfsvplnl ipaaagiiia iggvslkfte hfelngialg
      421 tltvltgyhs lrwlsrvtgp rdtplldagt seykkpadge g
//
LOCUS       WP_457693349             179 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457693349
VERSION     WP_457693349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19356
     Region          <75..167
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mserervrmr everdgaadg aeaeiaaier amvalrrsaa rrtlarraar qggggpvpeg
       61 aafdvldvve aaeergepag vrevadalrv dqprasklva aavqaghlrr eadqtdgrrt
      121 llavtpdgre lleaahtfrr svvarvtrdw paaertafar lftrfmddfg avnepsged
//
LOCUS       WP_457693350             311 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693350
VERSION     WP_457693350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33387
     Region          10..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..298
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(106,108..109,113,170,207,274)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(107,110..111,114..115,118..119,121..122,125..126,
                     128..132,134,196,224..228,231..232,235..236,239,253)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 miarnahidl nlltaldall eeqsvtaaad rlglsgpams ralgrirrtt gdpvlvragr
       61 hmvptprale iraevrrlve aaqgvlapsa padpaqlarv ftinandlfv tavgprlvar
      121 vaqeapqvvl rflgesyvdl pllrdgaadl elgvidspep eivreelfvd rsvavvrdgh
      181 plttgtltar rfadashlnf srrgrltgpv daalaarglr rkviatvptf aaslmmvrds
      241 davgltgera gaatarglgl rtlpiplelp pmsmemawhp rqeadsghrw lrglvretvr
      301 eavqdvppde v
//
LOCUS       WP_457693357             477 aa            linear   BCT 27-JAN-2026
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457693357
VERSION     WP_457693357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  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 477)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=51211
     Region          28..477
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 msqqprrrps kpyrrpqkdp vrilafealr avderdayan lvlppllrka reggdfdard
       61 aalatelvyg slrrqgtyda iiaqcvdrpl revdppvldv ltlgahqllg tripthaavs
      121 asvelarvvl gdgrakfvna vlrkiaahdl dgwlervape ydedpedhlg ivhahprwiv
      181 salwdalggg ragiedllea dnerpevtlv arpgrsttee llaaageesa lpgrwspyav
      241 rlaeggepga ldpvregrag vqdegsqlva lalanapveg sdrvwldgca gpggkaalla
      301 alaaqrgaal lasekqphra rlvarslegn pgpyaviaad gtrpawqpga fdrvlvdvpc
      361 tglgalrrrp earwrrrped ldgfaplqre llrqalaavr iggvvgyatc sphpaetrav
      421 vddvlkgrgg epvevewida rplmpgvpal gdgpdvqlwp hlhgtdamyl allrrta
//
LOCUS       WP_457693333             217 aa            linear   BCT 27-JAN-2026
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457693333
VERSION     WP_457693333.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=23323
     Region          11..206
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 msvldtlnge aftalgqhvi wsdmigntig laalalgwrr siwtwpaqfl sgvilvaaya
       61 sahlsggvgk qllvigvalw gwrqwqrgrq qaqdgsiavr fagwrergll lggtavgtaa
      121 vgtlftlipq lswnpwpday ifvgtlaamv aqarglvefw fawllvdvvg vplafssgla
      181 fsglvyvvyl alvvwgmrdw wlrsrasgrp vlegaaa
//
LOCUS       WP_457693368             368 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces nigrescens].
ACCESSION   WP_457693368
VERSION     WP_457693368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10473666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..368
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.11.9"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38738
     Region          8..138
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; pfam01321"
                     /db_xref="CDD:460159"
     Region          144..350
                     /region_name="APP-like"
                     /note="Similar to Prolidase and Aminopeptidase P. The
                     members of this subfamily presumably catalyse hydrolysis
                     of Xaa-Pro dipeptides and/or release of any N-terminal
                     amino acid, including proline, that is linked with
                     proline; cd01092"
                     /db_xref="CDD:238525"
     Site            order(206,223,234,299,328,342)
                     /site_type="active"
                     /db_xref="CDD:238525"
ORIGIN      
        1 mselyaarrt rlrdrvagag saaalisrpa nvryltgcap pgaalllgpa ddvllcgnpl
       61 sgdpsegrpa edvrvsvlpt rggdpvvaga dlaakagadi laveehhltv trhralsqva
      121 prlrltdlac aveaqrlvkd ddeiaclria aeiadqalge llesilvgrt erhlaleler
      181 rlvdhgadgp afptsvatgp nagrpghlpt drrveegdfl svglganyrg yrceigrtfv
      241 igttpsdwqi elydlvfaaq ragrealapg vecrevdrva rhvldaagyg erlgpwtghg
      301 vgleidedpq lspaamgkld acvpvtvepg vhipgrggvr iddtlvvrpe adggpellti
      361 ttkellal
//
LOCUS       WP_457693372             185 aa            linear   BCT 27-JAN-2026
DEFINITION  shikimate kinase [Streptomyces nigrescens].
ACCESSION   WP_457693372
VERSION     WP_457693372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478131
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19736
     Region          1..168
                     /region_name="aroK"
                     /note="shikimate kinase; Reviewed; PRK00131"
                     /db_xref="CDD:234654"
     Site            order(13..18,111,118,155)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:238260"
     Site            order(17,33,35)
                     /site_type="other"
                     /note="magnesium binding site [ion binding]"
                     /db_xref="CDD:238260"
     Site            order(35,59,62,80..82,136)
                     /site_type="active"
                     /note="putative shikimate binding site [active]"
                     /db_xref="CDD:238260"
ORIGIN      
        1 mtspavvlig ppgagkstvg allaerlgvg yrdtdadive ttgrpiaeif idegepyfrd
       61 leraavrdal dghpgvlalg ggaildegtr klltglpvvf ldvqladavk rvgldaprpl
      121 lavnprkqwr elmehrrply tevaraviat gertpeqvve aildaldlrq avgdapqavh
      181 reeqa
//
LOCUS       WP_457693378             732 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693378
VERSION     WP_457693378.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..732
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=79453
     Region          2..697
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          492..520
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(493,496..497,500..501,503,527,530..531,536..537,
                     539..540,574,577..578,581..582,585)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          525..562
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          573..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrrltrpgpl srpsperlra pgrpgnlpae lnrfigrdde laalarqles arlvtltglg
       61 gvgksrlagh saailqdrfc dgawlvelss lrephlldht vaealapadh sgrpvraalc
      121 dhladrelll vldgyehlvd acaeltaell rrapglrvla agrrplgltg eqnvalapln
      181 tadatalfad raaavlggft vgaaneaavt elcerldgip lalelaagrl ralsvdqvlh
      241 rlddrfrllt gtargvlprh qtlrtaigws helctpeerl lwarlsvfag qfdleaveyv
      301 csgpelpage lldiiaelva qsvlvreeta agvryrmldt vraygagwla atpdgerlrr
      361 rhrdwylgla twceldwfss rqaeiaarid aelpnlrval eqslecpadt hlgqylagtl
      421 wfywvgcgrl segrhwlnra lelesdhdda rlkalwvagy vavlqgdtvg algalqecrd
      481 eaertgnata aayalhrtgc lalvcddmpr aeellrgalr ryreigelns nvllgqvela
      541 mavafrgepa davrlcedvl evcedhgerw trayaqfvla yaawsrgdae raralleesl
      601 avhhafhdll gvvlaiella mvtlgegdae eaavlqgaag riwpsvglpl fgsryfrrph
      661 alceeqarqr lgaehygral rtgerlglda tvarvlrpsv pvpgpqrtvr lvppgtnepa
      721 aspsasgget ag
//
LOCUS       WP_457693379             474 aa            linear   BCT 27-JAN-2026
DEFINITION  replication-associated recombination protein A [Streptomyces
            nigrescens].
ACCESSION   WP_457693379
VERSION     WP_457693379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..474
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=49986
     Region          10..455
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mepdlftaaa edrqekdpag splavrmrpr tldevvgqqh llkpgsplrr lvgddggggs
       61 ggpsgkgggg rragggpagp ssvflwgppg igkttlayvv sqatnkrfve lsaitagvke
      121 vravidgarr asggygketv lfldeihrfs kaqqdsllpa venrwvtlia attenpyfsv
      181 ispllsrsll ltlepltddd lrrllqralt darglagavt lpedteghll riaggdarra
      241 ltaleagags alakgekeit lqtleesvdr aavkydrdgd qhydvasali ksirgsdvda
      301 alhylarmie agedprfiar rlmisasedi gladpaalqt avaaaqavam igfpearitl
      361 sqatialala pksnaaylai daaladvrag qagavpphlr dshykgaqkl ghgqgyqyph
      421 dlpggiaaqq yapdevhgkr yyeptrhgae aryadvverv rvrlrsdsge saae
//
LOCUS       WP_457693383             276 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Streptomyces nigrescens].
ACCESSION   WP_457693383
VERSION     WP_457693383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=29242
     Region          99..275
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mvsrdqrrrq larekyerqq qrrsadrrkt krrnvviasa mavalaagva ayasaglags
       61 dqdsdraaap pspskapdpc gkpakgtpst ktwkkepams ldtsasysar lattcgtiel
      121 kldagkapht vnsfaflagq gyfdhskchr lvdqgiyvlq cgdpkgtgqg tpgytipden
      181 lkdsrlkggv ypagtvaman rydgrsdktr nsggsqfflv yqdsklppny tpfgtvtggm
      241 dvlkkiakag stpdpqtgnt apnatvvidk atvkks
//
LOCUS       WP_457693385             668 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457693385
VERSION     WP_457693385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..668
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=66622
     Region          9..283
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,75,91..94,98,100,137,139,
                     141..142,144,165..166,169,191..194)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,75,91..94,98,139,141..142,
                     144,165..166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,98,100,137,139,141,169,191..194)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(165..173,187..194)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtgrllggry rvtdrigrgg mgvvcravde vlgrevavkv lraytdasap eladlrtrmq
       61 rearaaarir hsgvitvhdv idedgrpviv melvdgpsld dvleqrgtld prevarigaq
      121 vmdaldaahe agvlhrdvkp gnvlldnwgh rpgrsgtggg rvvltdfgia sieapgdgat
      181 thltrsgelv gsldylpper aqgqgptpas diwslgmtly aavegggapf rrtsvwstlt
      241 aivtealpep rragpltpvl halmaknpad rpsaaearsl laavaegrep tplpapgtph
      301 sptvtdvraa aapdmhgehg pttgagelgg aaagpagptg pagptgpgpt gpvnagappa
      361 gwlsgpgtqg apatqptpls ppppppaptp ppapaghptp ppgtpgpnpa spaerdterv
      421 pargrrrvvp avaavlavla agggltyalv gggpgetvad rgrqsappag pgtrgaaegm
      481 aggedggkgn dkgsykgkgg gksaspsasd rpsegdgted pkpggaggsp ggqdgdsggt
      541 eggtdggsgs dggqggtsgg sggdsggggd eptqgsscep igggkancdv wrsaqsytas
      601 fqqvgtlnmg tnyfycqakl grretygkwt nvwwaktddd sgnsgvyisv vylkggandq
      661 pvpglptc
//
LOCUS       WP_457693389             683 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457693389
VERSION     WP_457693389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..683
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73893
     Region          23..501
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mskltdvpkr iligralrsd klgetllpkr ialpvfasdp lssvayapge vllvlsvagv
       61 saysfspwia vavvvlmftv vasyrqnvha ypsgggdyev antnlgpkag ltvasallvd
      121 yvltvavsis sgvenlgsai pfvvehktlc aiaiivlltl mnlrgvkesg klfaiptyvf
      181 vagvfimivw gvirgavmgd tmkaptadft ihaeqgglag lallflmlra fssgcaaltg
      241 veaisngvpa frkpksknaa ttlalmggla vtmfcgiigl amatnvrmae tpakdllyhg
      301 kpvgadytqn pvisqvaeav fgkgsflfvv laaatalvlf laantayngf pllgsilaqd
      361 rylprqlhtr gdrlafsngi vllagaaail vylygadstr liqlyivgvf vsftlsqigm
      421 vrhwnrhlvt ekdpakrrrm hrsrainafg afftglvlvv vlltkfthga wvallgmvif
      481 fvtmsairrh ydrvadeiaa eeapdddvvr psrvhslvlv skvhkptlra lnyaklmrsd
      541 sleavsvdvd qadtkalree werrgievpl kvlaspyrei trpiidyvks lrresprvav
      601 svyipeyvvg hwyehllhnq salrlkgrll ftpgvmvtsv pwqldsseaa kkrarkraew
      661 napgavrrgp vaqpkkekaa tkk
//
LOCUS       WP_457693390             442 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent RNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457693390
VERSION     WP_457693390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  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 442)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..442
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=47724
     Region          12..436
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mqaepkkslv geeyevevgp vahgghciar tdegqvlfvr halpgervia rvtdgeegar
       61 flrtdavsil easkdrveap cpfsgpgrcg gcdwqhaapg aqrrlkssvi aeqlerlagl
      121 speeagwdgt vepapgdkva kgevpawrtr vqyavdadgh aglrkhrshd iepvthcmia
      181 apgvselgie qrewpqiatv eaiaatgshd rqviltprpg grlpiveldk pvsvmrvgek
      241 dggvhrvhgr pfvreraadr twrvgnggfw qvhpkaadll veavmqglmp kkgdmaldly
      301 cgvglfagal aervgdkgav lgiesgkrav edarhnlqdl drvriehgkv dqilprtgit
      361 dvdlivldpp ragagkntvt hlasltprri ayvacdpaal ardlkyfaea gyvprrmraf
      421 dlfpvthhve cvvvlekatk da
//
LOCUS       WP_457693394             402 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457693394
VERSION     WP_457693394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..402
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=42896
     Region          7..398
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 migrtlppri gpylverrlg aggmgevyla ysvagepvav kvirpdrtdp htrarferea
       61 tiartisgtg rvarfidadp faeepwlamd yvpgrplsdl vkdqgplaap lvaslgalla
      121 eglaavhavg lvhrdlkaqn vilgdfgpvi idfglgaflg askgslsqag tvigtvrcmp
      181 peqalgevdm tqaadvyglg tvllyaateh ypydgarwea vaaqvvnpev dpdlsglpke
      241 lvpvvtpmla hkaddrpsle evtrqcadlm rllgtspara rraliqetta kdhptmvfpq
      301 pdapmldrld sldrllreel vsgerstpvp tvagqpgtdt vgeinveisl spepltalgs
      361 epgsgrpaep vpqpgrppas rrvadelrer yarrpalaws kr
//
LOCUS       WP_457693398             409 aa            linear   BCT 27-JAN-2026
DEFINITION  MinD/ParA family ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693398
VERSION     WP_457693398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Lutkenhaus,J.
  TITLE     The ParA/MinD family puts things in their place
  JOURNAL   Trends Microbiol 20 (9), 411-418 (2012)
   PUBMED   22672910
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Szardenings,F., Guymer,D. and Gerdes,K.
  TITLE     ParA ATPases can move and position DNA and subcellular structures
  JOURNAL   Curr Opin Microbiol 14 (6), 712-718 (2011)
   PUBMED   21963112
REFERENCE   3  (residues 1 to 409)
  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   4  (residues 1 to 409)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Surtees,J.A. and Funnell,B.E.
  TITLE     Plasmid and chromosome traffic control: how ParA and ParB drive
            partition
  JOURNAL   Curr Top Dev Biol 56, 145-180 (2003)
   PUBMED   14584729
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418836
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="MinD/ParA family ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43070
     Region          181..408
                     /region_name="FlhG"
                     /note="MinD-like ATPase FlhG/YlxH, activator of the
                     FlhF-type GTPase [Cell cycle control, cell division,
                     chromosome partitioning, Cell motility]; COG0455"
                     /db_xref="CDD:440223"
ORIGIN      
        1 mpngddwqgd vlrdlrggaq qgaqgpggqa yrapapgvgl ppqsaqvpdv apdsgaprqa
       61 ghpyqgqeqq agqqggrprq agyqgqrqqa paayapgpqp hsapgsrpva deglaravrr
      121 kpqhgesvaa ravralrrtl sssaarevae itrtaevlqr pvttgrqiav tsirggsgks
      181 tvaallgtty ahyrrdpvlf leadpalgsl plrlgaktlr wttsevadiv kpnmslldvt
      241 gylvqlpdna wllpasqgki gvmldsraye rtvvalrryf gvmvidcetl paevarvala
      301 aahgrvlttp atpegitsty svlqwmqglp rqviagtvvv ltesvphsgl dldaaarelk
      361 atgaavhllp ydrhlaaggp ihtellahpt rqaaarlaad vfhlsqksh
//
LOCUS       WP_457693407             130 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693407
VERSION     WP_457693407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..130
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13388
     Region          12..123
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtgtqqtpvn kaaeardsvq ellsahrprv delsmidall vtselvtnaq rhggglagfs
       61 aliaagllev tvadnsprhp ataiggekfg vggygwpmiq kltscvvivp aadgkaitvt
      121 vplrcdrtad
//
LOCUS       WP_457693408             119 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693408
VERSION     WP_457693408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..119
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12408
     Region          5..119
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mrgvpvraae arnfvhdllh kigspvddla lvdallvtte lvtnaqrhgg gltgftariv
       61 dgylevaved gsahcptass prepgatggy gwpliqrlar tvditatvtg ktirvtlpl
//
LOCUS       WP_457693410             137 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457693410
VERSION     WP_457693410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=13993
     Region          <58..135
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 meaavqtgks rntpacpaaa ghrssagaaa aqrcaarcrp havrhpvasv arrggavrlr
       61 vtsaghpapl vvrvdgwvee adtrgslvga lpevtsttap ldlapgescl lwtdgiteam
      121 ggpvgeelfg eerlrpr
//
LOCUS       WP_457693413             182 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693413
VERSION     WP_457693413.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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..182
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..182
                     /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=20456
     Region          33..175
                     /region_name="Bfr"
                     /note="Bacterioferritin (cytochrome b1) [Inorganic ion
                     transport and metabolism]; COG2193"
                     /db_xref="CDD:441796"
ORIGIN      
        1 madfltditt lrdrarreie kgpvteayga dlervlqvln ealateivct lrykrhyyta
       61 sgiysepvaa eflehaaqeq qhadkvaqri vqlggkpdfn petltqrsha gydasddlle
      121 mikedlvaer vaiasyteia kwlgdgdptt rrvfedllaq eeehaddlrg lleripqdkk
      181 ad
//
LOCUS       WP_457693421             315 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457693421
VERSION     WP_457693421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32349
     Region          38..310
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mispspplgs hersaprggv pdtaarptgr laelparval vavwssgfls gtlglryaap
       61 ytfaalrfav aglvllavag vrrqrlprgr rllhlavagv lvqavqfssi yagmdlgvps
      121 glaaliialy pltasllavp llhervsagq llglvlglgg valavaegiq lslgslpglg
      181 fltlgllgis agtvyqkrfc gqmepvsgna vqllaaslvv lvpallaegw dvhftaaywp
      241 vllwsalvns ivgvgllyrl lqrhgtsqvs slfqlvpmst aglgalllgq rlgpltlggl
      301 vlatagtlla hrvrd
//
LOCUS       WP_457693414             108 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693414
VERSION     WP_457693414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..108
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11592
     Region          1..100
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(17,19..21,27,50,52..54,56..58,61..62,85,89..90,92)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            53
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mthavedkaf vvrvsgsldh dsaplleeac alaedsgapr tvvdlsltdf adstvlhvll
       61 aaqrahhrrq rklivdgpfh evirrlfdvt gtagyftpad dmpgales
//
LOCUS       WP_457693423             320 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457693423
VERSION     WP_457693423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32171
     Region          24..312
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtlqekplsv rpdgsgkrra aggpvrpvva avagsacisa savfmklsgt nagtaaflrc
       61 alalvvlvpl avrevrrvgt rplrylamdl gagvllgvdm vfwaaavgtv gasvatvlln
      121 lqvvvfplla rlvsgtrlsg rfalmaplml vgvalasgai ghpapgsdpv agvtfgtaag
      181 vtyagylflm rlgggrehtv spvcvstaaa avaaavlggl wtgidlnpgw pawgwlsala
      241 lvgqvlawll ittalprlap htgaallllq pvlafalgva igerptptqa ggcalviaav
      301 whhsrasrgr apktaasras
//
LOCUS       WP_457693424             305 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693424
VERSION     WP_457693424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32220
     Region          16..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mfsidrlral aavaahgsia qaartlhmta sgvsqqlakl ereaghslle phgrsvrlth
       61 agrvlaghad rllvqlaaaq gdladlgeev lgplriggvg savrtllpda laalaaghpr
      121 ltptvvdgea vdlvprlihg eldllliesw aerpvsvpeg vtlrtlvsed vyvalserhp
      181 lsdrgtvdla dlrgmawacc ppgtapyeal vqvlrtcgae pdirylvaeh stqlalvarn
      241 ltaslvpams crpappgvrf latrpalrrd iraawltrae sppvracvaa veahrqaade
      301 vcpke
//
LOCUS       WP_457693425             401 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457693425
VERSION     WP_457693425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=43193
     Region          1..393
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mnrsgewile rvgrdrgpdr grtagrlaev vdnrgfevar ppawmrwlpv ayvvfvllle
       61 tvtptpwavs fllialpvia aytlgpfava aatvfavvle gvvagtpcct ghnihmlwen
      121 hhvaayvatg lvgalgvala ahrrrqerdl vrahsvaeal mrtllrpvph rvghllaagl
      181 yrsgevgtmv ggdlydirat psgeravigd vrgkglqavr tvadilgsfr eavhdqgdlp
      241 avatrmerrl areaeelldd elfvtavlie ydavahqvtv inhghiepvl isrgevtpli
      301 gppalplglg aladeepvay thpfnpgdvl llctdgliea rdhtgafypl ldrlrhrfag
      361 rtapgpadvi dflntdlprh trvfhddval lalaphdgsg a
//
LOCUS       WP_457693430             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693430
VERSION     WP_457693430.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20510
     Region          2..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marpkefdph aalavametf rrqgyegtsv qdlvaalgin rssmyaaygs khdlylkale
       61 rysaaeaara rdglagtgpa lpalraflls yveaaladpg gagcmvthgv lellpgdqea
      121 aarlraalgs leeaffalll rartngelap gtdvrsaarf lvtftqglrv mekaadrdcl
      181 tgaveqalra vsrdg
//
LOCUS       WP_457693431             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693431
VERSION     WP_457693431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37514
     Region          43..265
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttddeggrg rltgpagpde eprtpaapsp aapgpdgpvp davtcralry afgetkavdg
       61 vdlsvrtgev fgllgpngag kttvircitt llpvpagmvr vfghdaaker mavrrllgyv
      121 pqqlsadagl tgrenvalfa rvfdvarrer tarvtqalaa vgltdaagrl aktysggmir
      181 rlelaqalvs aprllmldep tigldpiart svwehinavr aatgmtvlvt thymdeadqy
      241 cdrlalmhqg riralgtpde lrsalrarrr aartpaaahp aphtpgtsap aaapdtsaat
      301 apasapatps apssapsrps dteptledvf rdvagsglde qsgdfrdvrs trrtanrvg
//
LOCUS       WP_457693432             285 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693432
VERSION     WP_457693432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 285)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30043
     Region          89..266
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mseapaapqt gsadtapggl dlllvpprar tgwrvltarv iamcvvelqk lrhdrtelyt
       61 ravqpalwll vfgetftrln aiptggtpyi dflapgiiaq samfiaifyg imiiwerdag
      121 iltkllvtpt prsaliagka faagvkaliq avvviviaal lgvamtwnpl rllavavavv
      181 lgsaffscls mtiagivltr drlmgigqai tmplffasna lypvaimpgw lqtvsmmnpl
      241 syqvdalrgl llgthahlal dytvlvaaaa lgiaaassll grlar
//
LOCUS       WP_457693434             295 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693434
VERSION     WP_457693434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31775
     Region          8..>156
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdlvaacrvf vqvgergsft lgaeavrvpq svasrrvaal eehfgerlfd rstrraaltp
       61 fgrdmlpsak rlvqlaeale yhaeqaklrp lglavpetcs vrhlamldaa ardtdtvldf
      121 rsagpaerae llrsrevraa lvavppadad wavplgvasp tdngtaplrl eslrpgraqr
      181 sfrriwiqpe ddvphirdrl eqtghrvalv paqiavaasl taavaatlra dgfllcsaaq
      241 aeelglwwrr lagtpvargy svsavtgdda ervragfwsq varalgtptd akera
//
LOCUS       WP_457693439             293 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693439
VERSION     WP_457693439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32239
     Region          7..293
                     /region_name="F420_MSMEG_2516"
                     /note="probable F420-dependent oxidoreductase, MSMEG_2516
                     family; TIGR03621"
                     /db_xref="CDD:200301"
ORIGIN      
        1 mplqrpfrfg vnmfvpgsrr ewsakcrrae elgfdvvgva dhlefsapfp amvlaaette
       61 rvrlstfvln tpfynpvlla rdvastdqfv dgrmelglga gyvkaefdta gipfpsggrr
      121 veqleqtvtt lrrlfedtty lprpaqpsgp plliagwgdr llrlaaahad iiafpggwas
      181 ttgdalhlag iaqteervay vrgllgdrad avelnmlvqq vippaeraav pdrfeplppd
      241 aehspeelps vligtpaema qqlkerrery gfsyftvmey nmenfapvia alr
//
LOCUS       WP_457693442             366 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693442
VERSION     WP_457693442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38216
     Region          6..361
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msqlpertds vvigggvign siacqlaeag vgtvllerga lgsgssgtta gvvrtyfpgn
       61 alisslaars laayhafter tgtdlglkri gllvlftdeh qvqdfrhtqa aqqaagvdve
      121 lvtaaeaarl nplvdertil aaawspeaya cdpaaivrgy aaaaqqagai lrtetpvtgi
      181 dpdgrvhtpa gsiradtivc aagpwagtva amadvripvt typvemlltd tpgsaprnal
      241 pmtmhpsslr irswgdrilv gmgrpapdet rqtwlqrvsh hlgttyptla gnglkngwsg
      301 dldvspdgma figrdrsrpf lyaagfsgqg lcqapaagei irnlvlgkes widtaglsta
      361 rcrrgr
//
LOCUS       WP_457693429             520 aa            linear   BCT 27-JAN-2026
DEFINITION  PTS ascorbate transporter subunit IIC [Streptomyces nigrescens].
ACCESSION   WP_457693429
VERSION     WP_457693429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   McCoy,J.G., Levin,E.J. and Zhou,M.
  TITLE     Structural insight into the PTS sugar transporter EIIC
  JOURNAL   Biochim Biophys Acta 1850 (3), 577-585 (2015)
   PUBMED   24657490
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Campos,E., Baldoma,L., Aguilar,J. and Badia,J.
  TITLE     Regulation of expression of the divergent ulaG and ulaABCDEF
            operons involved in LaAscorbate dissimilation in Escherichia coli
  JOURNAL   J Bacteriol 186 (6), 1720-1728 (2004)
   PUBMED   14996803
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..520
                     /product="PTS ascorbate transporter subunit IIC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=52815
     Region          6..435
                     /region_name="UlaA"
                     /note="Ascorbate-specific PTS system IIC component UlaA
                     [Carbohydrate transport and metabolism]; COG3037"
                     /db_xref="CDD:442271"
ORIGIN      
        1 mdwlislatf lvneilsqpa yliglitaag lialkktagq vvggalkatl gflligagag
       61 lvvsslaplg gmiqgatgaq gviptneaiv giaqdrfgar vawlmilgfa valvlarftp
      121 lryvfltghh mlfmatlltm vlatsgrssv svvvigglll gillvampaf ahpwtkritg
      181 nnsiaighfg tagyilsgaa gqlvgkrsrs tedmklpegl rflrdsmvat alsmvliyvi
      241 mslaylakag ratafkafaa eggsaatdlg nyvmqsvmqg lqfgiavavi lfgvrtilge
      301 lvpafqgiag klvpgavpsl dapivfpyaq navligflas flgglvslal lawvghpafg
      361 lalvlpglvp hfftggaagv ygnatggrrg avvgaflngv litflpalll kvlgafgken
      421 ttfgdadfgw fgtllgnaak agaaggsiam paigavllga ailfqkrvvd tgwdpgarrd
      481 allpreaptt agpatavvrt hakiapppga ptpppppegs
//
LOCUS       WP_457693446             129 aa            linear   BCT 27-JAN-2026
DEFINITION  cell division protein SepF [Streptomyces nigrescens].
ACCESSION   WP_457693446
VERSION     WP_457693446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Duman,R., Ishikawa,S., Celik,I., Strahl,H., Ogasawara,N., Troc,P.,
            Lowe,J. and Hamoen,L.W.
  TITLE     Structural and genetic analyses reveal the protein SepF as a new
            membrane anchor for the Z ring
  JOURNAL   Proc Natl Acad Sci U S A 110 (48), E4601-E4610 (2013)
   PUBMED   24218584
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Cendrowicz,E., van Kessel,S.P., van Bezouwen,L.S., Kumar,N.,
            Boekema,E.J. and Scheffers,D.J.
  TITLE     Bacillus subtilis SepF binds to the C-terminus of FtsZ
  JOURNAL   PLoS One 7 (8), e43293 (2012)
   PUBMED   22912848
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Hamoen,L.W., Meile,J.C., de Jong,W., Noirot,P. and Errington,J.
  TITLE     SepF, a novel FtsZ-interacting protein required for a late step in
            cell division
  JOURNAL   Mol Microbiol 59 (3), 989-999 (2006)
   PUBMED   16420366
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004532
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..129
                     /product="cell division protein SepF"
                     /GO_process="GO:0000917 - division septum assembly
                     [Evidence IEA]"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0090529 - cell septum assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13978
     Region          8..119
                     /region_name="SepF"
                     /note="Cell division protein SepF/YlmF, interacts with
                     FtsZ [Cell cycle control, cell division, chromosome
                     partitioning]; COG1799"
                     /db_xref="CDD:441404"
ORIGIN      
        1 mngpdatdeq weglaevvpl rsssewpswp dhralpedep teetrrfivi rvqtfadare
       61 vaeylmaqip vlldlssadt dvakrildfs sgvvfglgsg mhrvdtnvfl lapvgtevae
      121 talggvprs
//
LOCUS       WP_457693448             119 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide pyrophosphohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693448
VERSION     WP_457693448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Requena,C.E., Perez-Moreno,G., Ruiz-Perez,L.M., Vidal,A.E. and
            Gonzalez-Pacanowska,D.
  TITLE     The NTP pyrophosphatase DCTPP1 contributes to the homoeostasis and
            cleansing of the dNTP pool in human cells
  JOURNAL   Biochem J 459 (1), 171-180 (2014)
   PUBMED   24467396
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Galperin,M.Y., Moroz,O.V., Wilson,K.S. and Murzin,A.G.
  TITLE     House cleaning, a part of good housekeeping
  JOURNAL   Mol Microbiol 59 (1), 5-19 (2006)
   PUBMED   16359314
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Moroz,O.V., Murzin,A.G., Makarova,K.S., Koonin,E.V., Wilson,K.S.
            and Galperin,M.Y.
  TITLE     Dimeric dUTPases, HisE, and MazG belong to a new superfamily of
            all-alpha NTP pyrophosphohydrolases with potential 'house-cleaning'
            functions
  JOURNAL   J Mol Biol 347 (2), 243-255 (2005)
   PUBMED   15740738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..119
                     /product="nucleotide pyrophosphohydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0009143 - nucleoside triphosphate
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=13077
     Region          9..99
                     /region_name="NTP-PPase_RS21-C6_like"
                     /note="Nucleoside Triphosphate Pyrophosphohydrolase (EC
                     3.6.1.8) MazG-like domain found in mouse RS21-C6 protein
                     and its homologs; cd11537"
                     /db_xref="CDD:212144"
     Site            order(11..12,15,18..19,21,27..28,31..32,34..35,38,41..42,
                     45..46,66..68,70..72,74..75,77,80..81,83..84,86,88..89,
                     91..93,95..96,98..99)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:212144"
     Site            order(12,37,40,69,72,76)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:212144"
     Site            order(24,28..29,31..33,35..36,39..40,42,45..46,76)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:212144"
ORIGIN      
        1 msedlhalqr rlaefaaard wqqyhtpknl aaalsveaae lveifqwltp eesakvmsnp
       61 gkagrvedev advlayllqf cealgidala alaakierne srfpavrsar pdraregee
//
LOCUS       WP_457693449             307 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693449
VERSION     WP_457693449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33039
     Region          2..229
                     /region_name="F420_Rv1855c"
                     /note="probable F420-dependent oxidoreductase, Rv1855c
                     family; TIGR03560"
                     /db_xref="CDD:274648"
ORIGIN      
        1 mdlriftepq qgasydtllk vakatedlgf daffrsdhyl rmgnadglpg ptdawitlag
       61 laretrrirl gtlmtagtfr lpgvlaiqva qvdqmsggrv elglgagwfe eehkaygipf
      121 pkekfarlee qlaivtglwa tgtgeefsyd gtyyrlehsp alpkpaqgkv pvlvgghgat
      181 rtprlaaqya defnipfasl edserqfgrv raaagaagrk gdelvysnal vacvgkddae
      241 varraaaigr nvdelkangl agspaevvdk igryaaigas riylqmldld dldhlelisa
      301 qvqsqls
//
LOCUS       WP_457693458             341 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693458
VERSION     WP_457693458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  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 341)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..341
                     /product="MDR family NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35574
     Region          14..339
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(57,138,162..164,184..185,189,205,228..229,250..254,
                     256,283..285,328..329,331,333)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(58,256,286)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(61,65,244,249..252,255,273..274,277..284,287)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 msptvvpgip alhrevrlaa rvegeltahh fmiaevpvpe pepgqvlirn rvmavtaamr
       61 tqmtgirlpm asfvpgqalw gaavgevvaa pgggftpgel vhhpygwref aaveesrvrs
      121 laedplptpa ahlsqgataw galrlaaevr pgdtvfisga aggvgslagq larrlgagwv
      181 vgstgserka arlraelgyd dtvvrgagpi erqlrraapd gidvlldtvg geqltaalav
      241 arpdarfalv galssqlggs galapveldp gliimrrval rgfglhahpd lpqewtkefg
      301 qglregslvf phallkgiqq apralseltq grhigavlve l
//
LOCUS       WP_457693461             283 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaX family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693461
VERSION     WP_457693461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Ferrandez,A., Garcia,J.L. and Diaz,E.
  TITLE     Transcriptional regulation of the divergent paa catabolic operons
            for phenylacetic acid degradation in Escherichia coli
  JOURNAL   J Biol Chem 275 (16), 12214-12222 (2000)
   PUBMED   10766858
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="PaaX family transcriptional regulator"
                     /GO_process="GO:0006351 - DNA-templated transcription
                     [Evidence IEA]"
                     /calculated_mol_wt=30817
     Region          10..283
                     /region_name="PaaX"
                     /note="DNA-binding transcriptional regulator PaaX
                     (phenylacetic acid degradation) [Transcription]; COG3327"
                     /db_xref="CDD:442556"
ORIGIN      
        1 mndqqtqrtp rslivtfyga ygrggpdfag aaaapvpvaa lirllgalgv dppsvrsavs
       61 rlkrrgllvp artatgaaay glsdaarqll edgdrrifgr paarlsdgwv lavfsvpeee
      121 rhkrhllrsr larlgfgtaa pgvwiapaql yeetrhtler lqldpyvdlf tgthagfapt
      181 adavarwwdl davaaqhraf laeqepvlqr wsrrrsvppe aayrdyllal dawrhlpyad
      241 pglpspllpe dwpggraaev fgrlhttlra agaryaheam tga
//
LOCUS       WP_457693460             253 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693460
VERSION     WP_457693460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26283
     Region          22..237
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mrvateverp vrgvrgagge tiraavfdld gtlantlpai skllikvase qgcsvtarqa
       61 aaaigkppgp afgrllgkpe ddarvqaais ryrelfayev lclgpqllfp gvtaglsalr
      121 ahgvelavat skttrsaeal ldvmgirdlv gpvigqdmvr rgkphpemvl raagrlgvaa
      181 wqsayvgdtv gdmrmavtar mepvavtygv gtfgelaava gtrmcgsfkd vvsviaaarp
      241 rpgvavgaqq rrr
//
LOCUS       WP_457693463             377 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693463
VERSION     WP_457693463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39345
     Region          4..372
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtvfalgpde qewcaelral taerlsplae kgeegrvnrp lvaalgelgl lrrlfpaega
       61 lraldlcllr eslaqectea etalalqglg aypvvqsgta aqrdrwlpev aagravasfa
      121 lsepgagsda aalslaaepd gpggwrltge kcwisnapea dfatvfartg gaagargvta
      181 flvpadrpgl tgahldmlsp hpigtlvfdg tpvaradvlg evdggfavam atlnlfrpsv
      241 gafavgmaqa aldaalthag artafggplk dlqsvghqla ematrvesar llvyaaasay
      301 dtgapdlarr samakllate taqyvvdaav qihgaralrr ghllehlyre vrapriyega
      361 tevqrsiiak elyrarp
//
LOCUS       WP_457693471             362 aa            linear   BCT 27-JAN-2026
DEFINITION  caspase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693471
VERSION     WP_457693471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 362)
  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..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38979
     Region          9..245
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mpgspagcrd alliatgrye spalkplrsp rqdceglaav lrdpgigcfa veqlvdaksy
       61 evkraleqff rnrgredlll lhlschgikd deghlyfatq dtdkdlpast avpaaflhdq
      121 marcrartiv vlldccysga flpgakgddh vqvkeelagh grailtatnr teyawegdhl
      181 aasapqpsrf tgalieglrs gdadadqdgr ipvtelydyv yeylhhagar qrprmwadle
      241 yrvilartpa rtapgasagr papapapapa papapeapsp paasaprnap tavreqpapp
      301 qqglftrlkd alqrrrprhr pplhpaparp swpgrpdpdg vpadrdgagh gqghrgryrg
      361 gl
//
LOCUS       WP_457693486             509 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693486
VERSION     WP_457693486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Rosinski,J.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 18527136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56047
     Region          3..>69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          74..506
                     /region_name="MurA"
                     /note="UDP-N-acetylglucosamine enolpyruvyl transferase
                     [Cell wall/membrane/envelope biogenesis]; COG0766"
                     /db_xref="CDD:440529"
ORIGIN      
        1 maddylvrig rlirdarqhr gwtqtqlaea lgtsqsavnr iergnqnisl emiarigeal
       61 dseivslgya gpmhlrvvgg rrlsgsidvk tsknacvall catllnagrt tlrrvariee
      121 vyrilevlgs igvrtrwind gndleivppa eldlnsmdte aarrtrsvim flgpllhrmd
      181 hfklpyaggc dlgtrtvtph mtalrhfgle itatdgtyia evdrsvapkr aivltergdt
      241 vtenallaaa rhegvtvirn assnymvqdl cffleelgvr vdgigtttlt vhgvahierd
      301 vdfapsedpv eamsllaaav vteseltirr vpvefleiel avleemgldh ersteyaadn
      361 grtrlidltv rpsklqapld kihpmpfpgl nidnvpffaa iaasaqgqtl ihdwvydnra
      421 iyltdlnrlg aqvklldphr vlvdgptrwr saemmcppal rpavvvllam maaegtsvlr
      481 nvyvinrgye dlaerlnsig aqieifrdi
//
LOCUS       WP_457693490             119 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693490
VERSION     WP_457693490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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 119)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..119
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12332
     Region          3..110
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mlfrvdpgss vplgeqiaas vrgaiadgtv dtgerlpaar elaaslgvnv htvlrgyqrl
       61 keeglielrr grgavvigaa apararlget aerliaeark lglsdeeivt vvrvglagr
//
LOCUS       WP_457693492             439 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693492
VERSION     WP_457693492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44495
     Region          33..412
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(43..44,47..48,51,84,139..140,142..144,147,167,
                     170..171,174,247,250..251,254..256,259,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtatpepasa cpsppdatap ppadpplwrd rrfvllaaar tisvlgngfa rvalsfavla
       61 lpgagagqls lvlacqavpq lvfilaggvm adrmsrsrlm ivtdlvgaaa yaglaamvlt
      121 ghaplmalca laalagtata lfspamdgvi pllvpagrlq rangllrvgm nssmllglal
      181 sgvavavvga gwalalnaas fvvsallvrg lrlparvrtg ssgwadlrdg wrefagrqwl
      241 wvvvaqysvv vaalnanagv lgplvaenel ggarswsliv aaqalgtitg aglaarirvr
      301 rpvliavlst fplalpiall avrapvpwia lamfgsgiaa difgvlwatt iqrevpeaal
      361 srvssydwfg slafaplgll iagpvaarvg vgpalagcaa livlasaaal lspqvrgvra
      421 pgpaptgeer dehgaeqpr
//
LOCUS       WP_457693501             248 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693501
VERSION     WP_457693501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26210
     Region          1..242
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mptktlqipt adgqadafaa fpdhgerhpg vlmyadafgi rpvlremage laghgyyvlv
       61 pnffyrhgpa pvielpehig eearpavvaq lmplieahta erilsdaday lrfltaqpev
      121 dagpvavtgy ciggllamht aaahpgevaa vagfhgpvga dgpdslrrll stltaqvhlg
      181 haetdmtpea lgelnkalda agigytseiy pgtihgftms dtdafnpaal qrhwdrllpl
      241 ldrtlgng
//
LOCUS       WP_457693503             209 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693503
VERSION     WP_457693503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22959
     Region          6..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrqgmaekra aivegarkvf grdgytrtti dsiakeavvs trtiynhfpg gkvqlfravv
       61 vegsesvvea rldaidrrlh kvtaadleqd lvdfvrawva ashrfsdhfa vvrqmrvesa
      121 hvpeefltaw rrsgpqrasd avaerferla adgllatddp araarhllll tvaeineqgf
      181 hgalplseea egaiiesgvr aflqgyapr
//
LOCUS       WP_457693512             404 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693512
VERSION     WP_457693512.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40891
     Region          19..378
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(29..30,33..34,37,69,119..120,122..124,127,146,
                     149..150,152,233,236..237,240..242,245,273,277,326..327,
                     331,335,348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mdtgrrtpaa tpphmarlrr aislffaldg fvfagwvvri paikeqihas agalglallg
       61 lsvgsvatml ltgklcrryg nhpvtvvtaa llslsvalpa lthsalhlgl vlllfgaayg
      121 glnvafnaaa vdlaeavrrp ilpsfhaafs agglagaglg gllaphlspl whlllltatg
      181 lvvtayagrv llrtprpatg qgphrdgtda vpergrttvg rtrllvtvyg litlctayge
      241 galadwgslh lsadlhtgpg aaaagyavfa llmtvsrmsg twllerlgdt pvlvggglla
      301 avgmlvgals pqlwlvcvgy altglglanv fpvavggaga lggpqgvava stlgysgill
      361 gppsigflae ayglpraltt iavaaavaal lgrlvrrgrr rapc
//
LOCUS       WP_457693517             220 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693517
VERSION     WP_457693517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24048
     Region          5..124
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          39..64
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(56..57,60,63..64,87..88,91,94..95,98,120..121,126,
                     129,154..155,158,161..162,184..185,188)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          71..98
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          86..198
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          100..129
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          136..162
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mskqdtdtir alqglensss svrlqaalav gttpdprfid kliercasep efyvremltw
       61 altrhapsmt vpellhevrs eraqarsqal htlskigdrq awpaitrall tdaddevars
      121 awraavvlvp egeepelaav lstqlgrger etqlslsral ialgevmvpt lhaamkdpdp
      181 rvrahaiate rllrdpdagf efaideakrv valgrtsqeg
//
LOCUS       WP_457693523             194 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457693523
VERSION     WP_457693523.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20692
     Region          17..188
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 madatsssas saasptfdel fcgllprlyr ravmlagsrq saedvvheay lklaarpqrf
       61 lahpepyaya fttvlnvard ahrkdrrqvl vdgmegveea gagggagggl ggapggwdgg
      121 verrhaeiea vrllgrlshr qagivilvdl dgytldqaak imkvhrgtaa rhraraldrl
      181 raylvesehg qagr
//
LOCUS       WP_457693527             286 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693527
VERSION     WP_457693527.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29827
     Region          29..279
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtpspspgsv ppaepgepaa raepvdslvl httdngvwwl tlnrpdamna ltrdqrerli
       61 grladasadp dvravvltat grgfcagadl rgapaagerv agdvarlird gaqrlitavl
      121 dcekpviaav ngtaaglgah lalacdlvla aesarfievf vrrglvpdgg gayllprlig
      181 pqrakellff gdavpaaeae rlglvnrvvp dgelaktare waerlaagpt ralaltkqlv
      241 nasldtdrat afaaeataqe inmttadaqe gvasfvarrh ptfrgr
//
LOCUS       WP_457693529             751 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate--CoA ligase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693529
VERSION     WP_457693529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 751)
  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 751)
  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..751
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..751
                     /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=79485
     Region          61..747
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt thsrparvva cgeqpphtvh gmsephrdgg gqgdcpvdrd vsgrplhapv
       61 pdldrffrpe svavigasdr egrpntgitr qliawaervg arlhpvnpgr tevfgqpcha
      121 gvadlpeavd lavllvgdpl pvieqlaeak vkfavafasg faetgeqgaa aqarlaeava
      181 rsglrllgpn tnlnafekfr tdldgpaial itqsghqgrp vfslqelgir lshwaptgne
      241 adletadfls yfatrpevga iaayveglkd grsfllaadr aarnkvpvva vkvgrtetga
      301 rtaashtgkl tgadevvdaa mrqfgvirvd gldelqdtaa llararkpta egvavysisg
      361 gtgahfadla tsaglrlptl gaakqaelhq wipdylhvan pvdngghpvg dwrgrkilda
      421 iladpsigil icpitgpfpp msdklaqdlv daaeqtdklv cvvwgspvgt edayrrtllg
      481 ssrvatfrtf gncitavray ldhhrfvdgy rspfddapra lspsarkaha lmrpgqqlse
      541 haakqllray girvpreqlv tsaaaavraa slvgypvvmk asgpqlahkt elglvkvhlt
      601 sasqvrdayr eltdiaryed vpldgvlvcq miergvemvv gvtrdslfgp tvtvglggvl
      661 vevlqdiavg vppfgedqar amldelrgra lldgvrgapp adidalvevv lrvqrmalel
      721 gdelaeldin plvvlprgqg avaldalavc p
//
LOCUS       WP_457693533             151 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693533
VERSION     WP_457693533.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..151
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16388
     Region          24..149
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 margasrsaa rfdvpevdaf trpywdaaae grlllrrcra egcgaahhyp refcpycwse
       61 dvgwepatgr aalytwsvvh rndlppfggr vpyvaavvdl aegprmmtei idcpegelri
      121 gmplvvhfrg adegtdggeg aavtipvfrp a
//
LOCUS       WP_457693536             244 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxine/pyridoxamine 5'-phosphate oxidase [Streptomyces
            nigrescens].
ACCESSION   WP_457693536
VERSION     WP_457693536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liang,J., Han,Q., Tan,Y., Ding,H. and Li,J.
  TITLE     Current Advances on Structure-Function Relationships of Pyridoxal
            5'-Phosphate-Dependent Enzymes
  JOURNAL   Front Mol Biosci 6, 4 (2019)
   PUBMED   30891451
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Safo,M.K., Musayev,F.N. and Schirch,V.
  TITLE     Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a
            tetragonal crystal form: insights into the mechanistic pathway of
            the enzyme
  JOURNAL   Acta Crystallogr D Biol Crystallogr 61 (Pt 5), 599-604 (2005)
   PUBMED   15858270
REFERENCE   3  (residues 1 to 244)
  AUTHORS   di Salvo,M.L., Ko,T.P., Musayev,F.N., Raboni,S., Schirch,V. and
            Safo,M.K.
  TITLE     Active site structure and stereospecificity of Escherichia coli
            pyridoxine-5'-phosphate oxidase
  JOURNAL   J Mol Biol 315 (3), 385-397 (2002)
   PUBMED   11786019
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="pyridoxine/pyridoxamine 5'-phosphate oxidase"
                     /EC_number="1.4.3.5"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_component="GO:0032991 - protein-containing complex
                     [Evidence IEA]"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042301 - phosphate ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:1902444 - riboflavin binding [Evidence
                     IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0036001 - 'de novo' pyridoxal 5'-phosphate
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0042823 - pyridoxal phosphate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26875
     Region          42..244
                     /region_name="PdxH"
                     /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase
                     [Coenzyme transport and metabolism]; COG0259"
                     /db_xref="CDD:440029"
ORIGIN      
        1 mtdhpahqds pdaapadapa hhsddaesqa frellrglrv wdvalpsfdp atapaeplpl
       61 frqwlreaae agvpephtmt latadaagdp svrtlmlhda dergwhfash rgsrkgrela
      121 vrpraalgfy wpavgrqvrv sgpvtaagpe esaadlhrrs tgalaaalvg rqsevlgstq
      181 elarasdaaw erarrepeap vsswtlyvlh peeveffqgd aqrrhvrlny ryengrwvqe
      241 llwp
//
LOCUS       WP_457693547             460 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693547
VERSION     WP_457693547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46375
     Region          1..424
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdaafteeqh eirrtlrell lkrcgpdevk aavrtppgyd tqlwqqlagr lglpglalpt
       61 ayggvgcgpt elalaceetg ravlpsplia taalaaplil algserqraa llpalaagel
      121 tatlavpggr latalaltgp ndggwagggr aggiqarrvp qvceavpskn ggpaagggwr
      181 lygeagqvln ghtadvlvva ahtggfahsr tllflvraat ggadarsgte paapgllrtr
      241 qtaldetrpq arlelrevpa ellgegdgde aavagalaat gvtaaaalaa eavgaadaal
      301 artvahvqqr eqfgrpigsf qavqhrladl yvrlqaarsa ayyaawsagg gpsapegaag
      361 pygaaepgvg alalaqalet lravaaeavq lhggigftwe heahlyfkra acdelllgpv
      421 hrlraraaee aglfpdaage lggsgeqaga pgrvaaavev
//
LOCUS       WP_457693559             272 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693559
VERSION     WP_457693559.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28643
     Region          3..245
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtvrteiedg valvtldrpe rhnavdlata aelvgtwraf rfddtvravv ltgaggrafc
       61 tgidrsvdvp qpsspysldd pllrigpkan dlwkpvvaav egmacggafy llgeaeflva
      121 aenatffdph ttygmvsaye slymaqrmpy geaarlalmg taerlgapra yeiglvselt
      181 apgaaaevar hravvlaaqp teavqgtvra lwaakeaars qalaqapqli algslppdrq
      241 aalfaarkrh gdghggqddg qdggrsghpl vr
//
LOCUS       WP_457693566             526 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693566
VERSION     WP_457693566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..526
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55538
     Region          10..526
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mfepariqtl welveyrara scgmpmffdg dgrrvtfdgv rdealrvaag frelgigagt
       61 rvawqlptri gtvvaslala rlgavqtpvi plhrerevgf ilaqsaaefv lvpgvwrgfd
      121 htamvrklag dgvrvlpvgd rlptadpvgd glptadpagl paaapvgdga ttwiyytsgt
      181 tsdpkgveht dagliaggvg latalgmsad digsiafpya hiagpdyvva mlvsgfpavv
      241 ldtfepgraa avyrrlgvtm aggstafyqa fldesrryrr qlphagrlip slrllsggga
      301 pmppelyaaa grelgcaivh gygmtecpmi amgtpydsde qlsrtvgkpv vgaqvrivrp
      361 dgstagtget gevtlkgpml frgytdpalt eeaftadgyf rtgdlgrlrp dghlvltgrl
      421 kdiiirkgen isaqeiedll hthpavaeaa viglpdrerg ervcavvapa dpaappltla
      481 eltahlraag lmtqklpeql etvgalprgg plnkvlktvl reryte
//
LOCUS       WP_457693574             408 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693574
VERSION     WP_457693574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45403
     Region          106..397
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 metfpkiisv ddhtveppsv wrdrlpskyr digprivrap vkemtfvggk fapkmgdvgd
       61 dgpiadwwvy edlhrpltrl dtavgyardd iklegityeq mrpgsfsvpd rladmdvnhv
      121 qsalcfptfp rfcgqtftea kdrelgllgv rayndwmvee wcgpqaqgrl ipltlvplwd
      181 aelaaaevrr naargvravc fseipphlgl psihtdywdp flracdetgt vvamhigsss
      241 kmpstsadap pavgstitfa nccfsmvdwl msgkfdrfpn lkimyaegqi gwipyilera
      301 dvvweenrgw ggvadkvlrp pselftehvy gcffddafgl ksldaigvgn vlyetdyphs
      361 dstwpksrev gesqmghlea dvverivrgn aiellgltge glwvgegr
//
LOCUS       WP_457693583             261 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457693583
VERSION     WP_457693583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27059
     Region          1..256
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgkldgrvvv vtgaargqge qearlfvaeg arvvlgdvld eqgealakel gegaaryvhl
       61 dvtqeadwqa aavaakdafg kidglvnnag ilrfnelvst pleefqqvvq vnqvgcflgi
      121 rtvapeieaa gggtivntas ytaltgmafv gayaatkhav lgltrvaave laarkirvna
      181 vcpgavdtpm tnpaaldpsi daaeskravd elyqklvplg rigqpeevak lalflsceds
      241 syitgqpfvv dggwlagvsi v
//
LOCUS       WP_457693585             374 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457693585
VERSION     WP_457693585.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41841
     Region          36..355
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mefglfvqgy vgkraetdpl aehkalmeet eyviqadksg fkyawasehh fleeyshlsa
       61 ndvflgylah aterihlgsg ifnplaqvnh pvkvaekvam ldhlsegrfe fgsgrgagsh
      121 eilgflpgit dmnhtkeiwe etiaefpkmw lqeeyvgfqg khwqlpprki fpkpygashp
      181 amwyaagspt syamaakkgl gvlgfsvqkv sdmewvleqy ktairdaepi gdfvndnvmv
      241 tstaicaeth dkaveiavng glnylqslvf ryhdtfprpe gipewpellp dytaeiiell
      301 iaeelmicgd pdevlrqckr weqagadqls fglpigvsye dtmktvklig ehvipkidtd
      361 pvhrttrfrq aags
//
LOCUS       WP_457693586             579 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693586
VERSION     WP_457693586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..579
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=62135
     Region          1..573
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mldhlikgat vvdgtgtpsy tadvgirdgr iavvappgtv teearsseda tglvlapgfv
       61 dphthydaql fwdpyatpsl nhgvttvagg ncgftlapln perpadadyt rrmmskvegm
      121 slvaleegap wswssfgeyl dalegriavn agfmvghcal rryvmgedai ggqptpaqle
      181 rmlalfheam eagawgfstt qsathsdgdg qpvasrhaap aellalsrav gehegtqiea
      241 ivagcldqfs daeiellvgm saaagrplnw nvltidaavp ervprqlvag arareaggri
      301 valtmpiltp mnmslgtfca lnlipgwgdi lglpvperie klrdpgirae mlrradskea
      361 gvfrrlthfg ryvigdtysp anegltgrvv qdiaaergqe pfaclveica ndrlrtvlwp
      421 mptdndpdsw alraetwqhe dvllggsdag ahldrmcgap yttrflgdcl rgrklmgleq
      481 avkmltddpa qlfglrergr ieegwhadlv lfdperidag katlvhdlpg dsprldskai
      541 ginavwvngv etiredvvtg avpgtvlrsg rdtrtvstk
//
LOCUS       WP_457693606             526 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457693606
VERSION     WP_457693606.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 526)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   3  (residues 1 to 526)
  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 10183725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..526
                     /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=56500
     Region          4..487
                     /region_name="SLC5sbd_u1"
                     /note="Uncharacterized bacterial solute carrier 5
                     subfamily; putative solute-binding domain; cd11477"
                     /db_xref="CDD:271371"
     Site            order(51,54,328,331..332)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271371"
ORIGIN      
        1 mnsldwavlv gyfgvmiaig vwshkrvddv sdfftaggrm pwwlsgishh msgysavmft
       61 gyagiayryg itsyitwsfp iaigiaigaq lfagrlnrlr srlgvasple ylknrynlpt
      121 qqalawsgvl lkivdvgakw aaiatllsvf tgislnqgil ltgvitgvyc tvgglwadal
      181 telgqfviql lagvamlvtv mgelggvsal wtvwdklpdh htqptvgpyt ltfllaylfi
      241 ktfeysggmw nqaqrfmatr sarqaqrsar lsaalwflwp avlffpmwva pllvtaqkpd
      301 asdayallte rllphgllgl vivgffshtm amcssdanai savftrdiap alsakardws
      361 hragllaarl stvaflglsm aiatqvnspt fkdiitvvik wvaglvgpis ipfllgmlrl
      421 frrsgptaal gswaaglfaf wltnygldgv qlqiqivapv atslllfvll gsvrpeatpe
      481 rdavlarins dddgaartap vaipeqgdga aadgmrggag evprdr
//
LOCUS       WP_457693616             288 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693616
VERSION     WP_457693616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32587
     Region          15..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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          97..278
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 masnvnptvr rrrlgqelrr lrelkgmtae evaeallvsq skisrlengr rsisqrdvrd
       61 lcgvyevedh rivdslmqma kdsrqqgwwh afgdipysvy igleteaasl riyesllvpg
      121 llqtpgyaea vipgtvpela pdhlekriqv rmrrqervtd serplrlwvv ldesalrrvv
      181 gshlimreql dhlvemsqlp hvtvqvlpyd tgahagmsgt fsilefddaa dssvvyiegv
      241 tsdlylektn dvhkytimye hlraqalsae hsrefiadaa kshadamr
//
LOCUS       WP_457693612             407 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693612
VERSION     WP_457693612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42898
     Region          7..404
                     /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 mpdaiparaa tpvpglaara artgsspvrd ilaltarpev isfagglpap elfdtaglaa
       61 afqhvlaedp lralqystse gspalraaia arttarglat daddllvttg sqqgltllat
      121 allepgdvvl vedpcylaal qifsfagarv vpvptddegl dpvaldeita rerpkllyvv
      181 ptfqnptgrt lsaerraava evaarrglwi aeddpygelr fegepvpwva sfpgaedrta
      241 llgsfskvma pglrlgslra paalrracvi tkqaadlhts tvdqaaaary lavadldahl
      301 krvrdayrer rdalvdglaa alpegsrwnr paggmfvwat lpegydatal lpevvrhdva
      361 yvpgapffag ppdataarls fvthppeeir egldrlkkal ggarrhg
//
LOCUS       WP_457693618             253 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces nigrescens].
ACCESSION   WP_457693618
VERSION     WP_457693618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=26622
     Region          8..200
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mgrsrrtipe ellllaldpt tgttaqpqsl dlglagaqlv elalagriap dgdriavvma
       61 rptgdptlds alellrrrgs pvravhwigg prlglrqtyl thlercgmvh avagqmcgvl
      121 pttryqatet aisreirarl dnairtgvpp dprtaalaal ahavglgkhl ypgnegrssr
      181 srlrdlirhd pmgglvahav mdvqngaaaq prrqqaagag avrqpaarat adpagapvqs
      241 rhghsrmarv gar
//
LOCUS       WP_457693622             278 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693622
VERSION     WP_457693622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=28545
     Region          12..249
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mstspeyatf hfhalhhadq plllpnawdv isavalagag yaavgttslg vaaahgypdg
       61 rglaevrdat valalrlngr ltcpytvdve ggfggdpgqv gdlaaelaea gaaglnledg
      121 lpggeglqdp vrqaemisav kerapglfln aridthwrvd sppslsvtls raetylaaga
      181 dgvfvpgvva deeisvlaae ipaplnilfa pgrhtvsrla elgvrristg sllfrtalqa
      241 tltaadairt gqqpteaaga ggevlgyeev qrlvgeee
//
LOCUS       WP_457693627             147 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693627
VERSION     WP_457693627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12204063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16270
     Region          31..114
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtskaaaeqh lrdlarlrrv rdridreyaq pldvealarg vnmsaghlsr qfrraygesp
       61 ygylmtrrie ramallrrgd lsvtevcfev gcsslgtfss rftelvgvpp svyrreavra
      121 tagmpscvak qvtrpvrnre apapsgt
//
LOCUS       WP_457693639             220 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693639
VERSION     WP_457693639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23752
     Region          20..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maavaagaks gkqgqqprlr adalrnreri igaaretmve ygaevpldei arragvgnat
       61 lyrhfadrle lihhvtlsvm srtadraesa laeepdafqa lrrfvhaave erigalcpll
      121 sdgidrdhpd llaarerlea aveavmaaar nsgqlrtdia vgdlmvaitq ltrplpgssc
      181 pafdqfvhrh lqlfldglqa parselpgaa atlddlrrrs
//
LOCUS       WP_457693641             518 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693641
VERSION     WP_457693641.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53415
     Region          19..470
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,145,
                     148..149,152,277,280..281,284..286,289,317,321,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpetapsvdp rrwkalifia laqlmvvlda tivnialpsa qqdlgitdan rqwvitayal
       61 afgglllfgg rvadlwgrkr tfiiglvgfa vasalggaaa nqgvllgara lqgvfgalla
      121 paalsllavt fteakeraka fgifgaiagg ggavglilgg vlteymnwrw tffvnipfav
      181 vaatgaflvi repaegrnps rldipgvila tlglvslvyg ftraesdgwl agptlglfva
      241 aavlllafvl veskvrapll plrviaernr agvyaslgla vigmfglflf ltyylqivkg
      301 ytpvttglaf lpmivgmitg stqigarlmt rvrprllmap gftvaalgml vltqidldts
      361 ypalilpgfl lmglgmgtaf mpamslathg vqprdagvas amvntsqqvg gaigtallnt
      421 iaasattaya tshaagarsa dllklqsmvh gyttaiwwav gilalagvia ytfintgrpg
      481 agspvassad gestvlgsse gegegegege vqvpvmvh
//
LOCUS       WP_457693652             333 aa            linear   BCT 27-JAN-2026
DEFINITION  sigma-70 family RNA polymerase sigma factor [Streptomyces
            nigrescens].
ACCESSION   WP_457693652
VERSION     WP_457693652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="sigma-70 family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36682
     Region          37..322
                     /region_name="RpoD"
                     /note="DNA-directed RNA polymerase, sigma subunit
                     (sigma70/sigma32) [Transcription]; COG0568"
                     /db_xref="CDD:440334"
ORIGIN      
        1 matravarrq esssgsdgat gvravggeia drdlvgmyld eiartpllda akevelsqti
       61 eagvyaqqil dgevadgnaa gagreelerl veegakakdi firsnlrlvv avarryprag
      121 lplldliqeg naglvravek fdyakgfkfs tyatwwirqa itrsiadqsr tirlpvhlve
      181 elgrirrvqr efnrengrdp epaevagelg stparvtdvl dwardpvsln msvdddgdtq
      241 fgdlledtsa aspeqsvltl lrseeledli drldhrtasi ikarygiedg rertltevgk
      301 qhgltrerir qiekhallel krmahdtgfd aaa
//
LOCUS       WP_457693660             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693660
VERSION     WP_457693660.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31623
     Region          20..79
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          93..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpprravtgr sqeprqryve elrllraqkg dtlrqlgdvl gwdwslfgkm esgqtlgspe
       61 vvqaldqhyg tpgllltlwe lavadptqfk eryrrymtle aealslwhya vsalpgllqt
      121 eayahdllta ggisgeeltr qvearigrrq lldgdnaarf rsvlseavlr tpledaqqwr
      181 kqlehlldms errniviqvv rqevglhalt nthtmflrls dgrtvawvet gysgelveet
      241 aaaerlqlsy dlvrdlaltp vasrkfirqm leeascepst
//
LOCUS       WP_457693664             302 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693664
VERSION     WP_457693664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30908
     Region          14..299
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mrneagvrfv ttvkksvavl glgsmgaala galleaghev tvwnrtpgra eglvargarg
       61 agsvaeavta geivlvcild ygdigplleq qgggraalqg rvvvnvtngs peearamaer
      121 vtalgasyld ggimavpeii aspevfvlys gsreafeahr gvldafarsv ylgedpglap
      181 lhdlallsgm ygmfggflha aalvrsaggp vaeftttllq pwlramaggl pamaaqidsg
      241 dytvtgspla mqvahdsige vsraqgvspe lfaplfalme rrvadghgse glagvvelvh
      301 pr
//
LOCUS       WP_457693666             260 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693666
VERSION     WP_457693666.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28458
     Region          39..>136
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          105..257
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maskksadae drqpsgsaae apdpaevslw erldrpapap ratltpqkia aaavqiadtd
       61 gidavtmrrl atelgvapma ayryvsgkgd vldlmtdavy adlqlpdele nwrevmraha
      121 lrtreivlrh pwliqisspq alraltpnrm aeaeralssl dglgldidam mavvgtvtsy
      181 vhgavsaeca qhslmreqgw dspddlrtal gpqmrylmst gryptyhryl reavhkddpq
      241 wrfeagldsv ldgiaarldi
//
LOCUS       WP_457693670             197 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Streptomyces nigrescens].
ACCESSION   WP_457693670
VERSION     WP_457693670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21063
     Region          9..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mdsekrlqva vivgstrdgr fgptvaawva eriaqrgdma vevidlvetp aptvfpafgq
       61 ppapgtgell aeisprlaaa damvivtpey nhsfpaplkn vidwhhaewq akpvgfvsyg
      121 glsgglrave qlrvvlaeln amtvrhtvsf hnygdkfdae grptdpaaeg aakvmldqlg
      181 wwaralvdak avrpyaa
//
LOCUS       WP_457693673             448 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Streptomyces nigrescens].
ACCESSION   WP_457693673
VERSION     WP_457693673.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=46997
     Region          100..281
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          287..418
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 meqlvttpdn laparsrtph qllpsveqpa sgaprrnrrm rrtlavtalf aagaltlsac
       61 ggdasaggnd dgkngqagad aaaaknasdv kikvssddga tnasindtgv katggkltev
      121 klteadsgkv vagaissdgt swkpgvqler gtkyrivaka kdakgraate nasfttvssa
      181 nsfigsytpd ngktvgvgmp vsfnfdkait nkkdvqshit vtsssgqkvv ghwfgtqrld
      241 frpedywkag skvtmkidld gvkggqgitg vqsktvsfti grsqvstvdm ntqhmtvkrd
      301 gktlkdipis ggspenptyn gqmvisekfe qtrmdgstvg fkkkdgkgey dipdvphamr
      361 lsasgtflhg nywgspsifg qagtshgcvg lrdnkggggd tpgkwffnes ligdvvvvkn
      421 sddqtikpdn glngwnmswa ewqqgsav
//
LOCUS       WP_457693680             238 aa            linear   BCT 27-JAN-2026
DEFINITION  VIT1/CCC1 transporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457693680
VERSION     WP_457693680.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10116192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="VIT1/CCC1 transporter family protein"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /calculated_mol_wt=24034
     Region          16..233
                     /region_name="Nodulin-21_like_1"
                     /note="Nodulin-21 and CCC1-related protein family;
                     cd02432"
                     /db_xref="CDD:153123"
ORIGIN      
        1 mtsqtpdhde ahggglgsrl nwlraavlga ndgivstagl vvgvagatde rgtlltagla
       61 gllagslsma ageyvsvstq rdsekaalaq ekrelatepq aelielteml egkgldvqla
      121 revaeqlteh dalrahaeve lgidpdeltn pwhaagasfl aftagallpl lamvlppaad
      181 rlwitvgavv valglcgwgs arlgfapvgr amvrnvgggv vamgvtyaag svlgavgv
//
LOCUS       WP_457693682             366 aa            linear   BCT 27-JAN-2026
DEFINITION  P1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457693682
VERSION     WP_457693682.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Bompard-Gilles,C., Villeret,V., Davies,G.J., Fanuel,L., Joris,B.,
            Frere,J.M. and Van Beeumen,J.
  TITLE     A new variant of the Ntn hydrolase fold revealed by the crystal
            structure of L-aminopeptidase D-ala-esterase/amidase from
            Ochrobactrum anthropi
  JOURNAL   Structure 8 (2), 153-162 (2000)
   PUBMED   10673442
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="P1 family peptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36458
     Region          2..353
                     /region_name="DmpA"
                     /note="L-aminopeptidase/D-esterase [Amino acid transport
                     and metabolism]; COG3191"
                     /db_xref="CDD:442424"
ORIGIN      
        1 mphppgpqda ltdvlglrvg haqhigdgyl tgttvvlape ggavaavdvr gggpgtretd
       61 aldprnlvqr vealvltggs afgldaasgv aawledqgrg frvgpdpaqv vpvvpaaalf
      121 dlgrggnwra rpdaalgraa adaaagtepg apvargntga gtgavagglk ggigtasavl
      181 psgatvaala avnaagsvid prtgalyghl yedptalpap evhaaalrrl aearetsltr
      241 saasvrppln ttlavvatda tltraqahkl agtahdglar airpvhllsd gdtvfalsta
      301 trpltpdepr tdpafgihte agalnellst gadvltraiv naarsaetvr gpggifpsyr
      361 dlygtt
//
LOCUS       WP_457693697             266 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693697
VERSION     WP_457693697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29680
     Region          18..249
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mttepphgah gprpldrrsp lplwaqlsad lrrrmeagaf reefpaehrl tgeyevsrht
       61 vrealrrlra dglviaergr tsrldtrriq qplgslyslf relegqgveq rsevlrlert
      121 adgtiagqlg lvpeaplvvl erlrladgep lahdtaylpa evaeplldad fghtslygel
      181 trrcgvkvtg greriqpflp dirqtwllgl adreaafaie rlgqagerpv ewretvvrgd
      241 rftflaewsd dsravalapr ascpss
//
LOCUS       WP_457693701             567 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693701
VERSION     WP_457693701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58322
     Region          27..435
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,275,278..279,282..284,287,315,319,367..368,
                     372,376,392,395..396,399..400,403)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpklephthl dphthldpqa rwalaalatg afcvqldsfa lnlalpvvrd alhgsataap
       61 wvvssyllaa gslmpvagrl gdlygrrrml taglalfgvt avlcalapsl pllvtarvlq
      121 gaggalimpa glallanaap pgrgrramgr alglaglatv cgpflggvla rsvswravfw
      181 ltvplalaaa lcarraaesr dpdagqslds vgaiaatgla aclarwleha adwgwavgav
      241 lfgalfvrae rrsaaplvdl alfrnhpyva ltvagavans atvallyvvp wtlqqaegws
      301 vleagvvfaa pagalavggp lagrvrpgaa vpvmalclaa aaaalaattr gtgtpsllma
      361 ataaaaalgv agglaltgtq avvrrerage asgvtkavmt atagvglalt gagtgvgtrp
      421 slvlpaavcl vtaaalvtta rvlrlprvrg lplvcglpvi rglalvrrpa lirrpalirr
      481 palirrpalv lgralvlvra llpvrrrpdr rrasqrrtsq rrsdrrgecr rqtdrsaagq
      541 hqtdrrrsdg rgagrhrsar rqatrce
//
LOCUS       WP_457693705             160 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693705
VERSION     WP_457693705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17681
     Region          7..144
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtstlrlekv tpdnveaacr lkvrpdqerl vapvvrslae ayaqpevawp rlifegeqlv
       61 gfvmgfflvr fdpdnpedrl rsgiwrlnia aghqgrgygr favesvceev rrrgqsrvtv
      121 swvpgehgpe rfylglgfrp tgemsgeqvv gelvltggaa
//
LOCUS       WP_457693714             111 aa            linear   BCT 27-JAN-2026
DEFINITION  FmdB family zinc ribbon protein [Streptomyces nigrescens].
ACCESSION   WP_457693714
VERSION     WP_457693714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..111
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10878
     Region          1..>56
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mptyqyqcte cgegleavqk ftddaltecp acngrlkkvf savgivfkgs gfyrndsrgs
       61 ssssspakss ssgttsssdg sssssgssds kpstpaasss agstsgtssa a
//
LOCUS       WP_457693718             907 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693718
VERSION     WP_457693718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 907)
  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 907)
  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 907)
  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..907
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..907
                     /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=99991
     Region          19..907
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mpanksgpvp rkkkgrrgrl vaitvvlllv agigfgafwg vstvrasfpq ttgslklpgl
       61 tnpvdvtrda ngipqiyadt dedlfraqgy vqaqdrfwem dvrrhmtagr lsemfgksev
      121 kadaflrtlg wrevaqkeyd tklspstkky lqsysagvna ylkdhegsal sleyaaldfg
      181 ndykpekwtp vdsvawlkam awdlrgnmqe eidrslmtsr ftpaqiaqly paypykrnkp
      241 vvdggavdpa skefepggsa naapaapggv taglqsqlss lsktldkvpa llgpngngig
      301 snswvvsgah tttgkpllan dphlapqmps lwyqmglhcr ttspkcnyda sgftfsgmpg
      361 vvighnqnvs wgmtnlgadv tdlylekvna dgyfydnkqr pfitrketik vaggesreit
      421 vrstrngpiv sdrddeladv gkdapvgnaa pdrgdgyavs lrwtaldpgk smdavfelnr
      481 akdwndfrka aahfevpsqn liyadtkgni gyqapgripv rgkgdgqfdg typapgwnpk
      541 yqwtgyipqk alpyeynpqr gyivtanqav tdekypyllt kdwgygsrsq rindlieski
      601 kdggkvstdd mqafqkdnss eiarlltpyl tkidikdkyv rdaqqllegw dfsqepdsaa
      661 aayfnavwrn tlklafgnkm pkelrpdgqc ltvrpadetg padendkyir ecgeragdsa
      721 qpdggdrwye vvrtllddpd nawwktedrp nrpgdknrdq llahamkdar feltsklgkn
      781 idnwswgrlh qmflknqtlg tdgpgilqgl fnrgpwnvgg geaavdatgw naaggykvtw
      841 apsmrmvvnl gdldksrwin ltgasghayd ahyydqtdkw akgdllpway seeavkkagk
      901 dtltlsp
//
LOCUS       WP_457693720             202 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693720
VERSION     WP_457693720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20661
     Region          44..199
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 maatvvrylr svgapttaaq sspatalprp alravreder apldpaefrs vlghfasgvt
       61 vitapgepgp agfacqsfas lsldpplvtf mvartsttwp riaragvfcv nilgagqgel
      121 crgfavsggd kfagvpykaa patgsprlad vpawidctvq avhtggdhll vvgrvealgt
      181 dpsaagngpl lfhrgtfgqf rp
//
LOCUS       WP_457693722             160 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693722
VERSION     WP_457693722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..160
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17436
     Region          31..155
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtpivapatd nrpdngadll lpvpdedgap fweyaargel riqacadcde lrfpprpccp
       61 hcqsfaarwq rmsgrgriws yvlphppllp ayaeqpgyna ivvelaeapr irlvgnlvta
      121 adaplnsvdp arlrigapvk avfhtmpggv tvprwllerp
//
LOCUS       WP_457693724             303 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693724
VERSION     WP_457693724.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32622
     Region          26..271
                     /region_name="F420_Rv2161c"
                     /note="probable F420-dependent oxidoreductase, Rv2161c
                     family; TIGR03619"
                     /db_xref="CDD:274680"
ORIGIN      
        1 mqlpvqsqsa lyaesweaaa gpgdlveiar vadrcgfayv accehlaipr rlaeamstvw
       61 ydpvatlahl aavtervrll shvavvglrh plitakqyat ldrlsggrli lgvgaghvpe
      121 efealgvdfg qrgavldetv ealkvalgpe efpkfagerf afeglgqapr pvqtprppiw
      181 vggsspaavr raaergdgwl pqgdrreqlp gqitrlrrlr eaagieepvv igtiaeplyv
      241 gepgwevgrr tlsgaaeria dslreyramg vqqiqvrfrs rspaeltdqm vafgaevapl
      301 lng
//
LOCUS       WP_457693726             472 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 39 protein [Streptomyces nigrescens].
ACCESSION   WP_457693726
VERSION     WP_457693726.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 472)
  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 472)
  AUTHORS   Ernst,J.F. and Prill,S.K.
  TITLE     O-glycosylation
  JOURNAL   Med Mycol 39 Suppl 1, 67-74 (2001)
   PUBMED   11800270
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 472)
  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 472)
  AUTHORS   Gentzsch,M. and Tanner,W.
  TITLE     The PMT gene family: protein O-glycosylation in Saccharomyces
            cerevisiae is vital
  JOURNAL   EMBO J 15 (21), 5752-5759 (1996)
   PUBMED   8918452
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474915
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="glycosyltransferase family 39 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51120
     Region          22..>237
                     /region_name="COG5305"
                     /note="Uncharacterized membrane protein PF0508, contains
                     N-terminal glycosyltransferase domain of PMT family
                     [General function prediction only]"
                     /db_xref="CDD:444104"
ORIGIN      
        1 mlllgawgir rqdaiwrdea vtydmahrsl adlwstllhv dvvhglyyal mhvwfagyda
       61 tlrgafgdav glrlpsvaam tvaaagvall gqrlvgrrag llagvtfali pvvqqyaqeg
      121 rsyamvcalv vwatyvlvla aarprrglwf gytalmlaac llhefaalal pahgaavvla
      181 rlprrvlrsw llasatvlag laplavfstr qsaqiswlmw pdplqlltfa ilavlgiacs
      241 rvrirsrgpi glralgvpvl llptllllll shvepayvdr yvlyyvvgfa llagaalarl
      301 lrpagergqt rgrrlrrama vvalpavllp vnvhlrspds rvddvtavah avrevsepgy
      361 gllfmpsrrr iwratlprdf rglhdlalae splashtlyg tersgdvird rmlaarrivv
      421 agdpdgqpad dndqeiakrs tlraafevcs srevrgakit vygrpgacgg gr
//
LOCUS       WP_457693728             260 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693728
VERSION     WP_457693728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27479
     Region          1..260
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 myaperqqei lrlareggrv dvlslaeefq vtaetvrrdl kaldraglvr rvhggaipag
       61 rldfepdlae rdavaadekl riaraalael pggeggvgss gsvildagtt aarlaaeipl
      121 eaeltvvthg lpvaarladh pgltlhlvgg rirhrtraav ddwalrayre inadvlflat
      181 ngfspdgglt tpdlaeaavk rtliaaarrv vlladsakfg qqhfarfgel sdvdllitdt
      241 glspddalai eragtevvra
//
LOCUS       WP_457693734             477 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457693734
VERSION     WP_457693734.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 477)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=49236
     Region          19..472
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 mpvppagtal aggtngpral rplldtvlda lttgaedrag plppggpetv artvrdachp
       61 llpdhgtgph aalrtlvhtl aagaadpadp hcaahlhcpp lalataadla aaalnpsmds
      121 wdqapaasal ealtgrelaa lvypqatdpd alvttggtes nqlalllare staadgtatd
      181 phrparplri vcganahhsi hrsawllglp epltlptpdg iltpdtvhsc lanlagrtgp
      241 vllvatagtt dsgaidplpa ladlaeqhga rfhidaaygg allfsdthra alhglaraht
      301 valdlhklgw qpvaagllav pgpttltpla hqadylnadd dteaglpdll srslrttrrp
      361 dilkiavtlk algrhglgel vdrtlaaaqt ladlieahpr yelhsrptls tvlfrptgad
      421 httlatirrt lltdgqavlg rattptglwl katllnphtq pgdlttllkl veghtpr
//
LOCUS       WP_457693736             476 aa            linear   BCT 27-JAN-2026
DEFINITION  lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457693736
VERSION     WP_457693736.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Visca,P., Ciervo,A. and Orsi,N.
  TITLE     Cloning and nucleotide sequence of the pvdA gene encoding the
            pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in
            Pseudomonas aeruginosa
  JOURNAL   J Bacteriol 176 (4), 1128-1140 (1994)
   PUBMED   8106324
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790239
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..476
                     /product="lysine N(6)-hydroxylase/L-ornithine
                     N(5)-oxygenase family protein"
                     /EC_number="1.14.13.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52765
     Region          15..463
                     /region_name="IucD"
                     /note="Lysine/ornithine N-monooxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3486"
                     /db_xref="CDD:442709"
ORIGIN      
        1 msstpeaplt tdttspdepl dlagigvgpf nlslaalahp ltqlrtafyd qrpafhwhpg
       61 llidgatlqv pfladlvtlv dpaspwtfln ylktrerlfp fyfaerfhih raeydaycrw
      121 vseklptlhf ghqidavrwn perelfevdf tqldtdgeae algrtyarnl vlgigttphi
      181 pvplrplaea pavpvihsad yldhrehlla adhltvigag qsgaeifldq lrarpagreg
      241 lhwlartpaf apmeysklgl ehftpdytry fhalpervrd dlvpgqwqlh kgidhatlaa
      301 lhdelyrrtl dggwpdttlt pgvcvrtagr vgttkvelhl dhiqqgtrsr lttdavilat
      361 gyrerrmdtl laaldpyvrr dsgarprida hhrmvldpai tgsvyvqnae ththgvgapd
      421 lglaawrsat ilnsltgntp yplptrtaft sfglpqpstg rtgtvprqgs tlvprr
//
LOCUS       WP_457693738             605 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            nigrescens].
ACCESSION   WP_457693738
VERSION     WP_457693738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  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 605)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65406
     Region          50..581
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 msldrrkflg ssvvtgagva lagaapaaea vevreqggrg hgprreryaf tvmgttdlhg
       61 nvfnwdyamd aefddaahnd vglakistlv tqvrqekgrh ntllidagdt iqgtqlayyy
      121 akvdpitdpd gpvhpmaram navgydaaal gnhefnygip vlrkfeescd fpllganavd
      181 arslrpafrp yvlkrlrsph grvvtvavlg ltnpgiaiwd kahvqgklaf pglveqaakw
      241 vpklrsmgad vvfvaahsgm sgtssygdql pyvenaavlv aeqvpgidav lvghahveip
      301 errvrnkqsg revvlseplk wgqrltlfdv vvewrrgrwe vgsvgsrvln snavaedari
      361 tgllraehrk vvayvnrvig rskaemtaae apvkdtpild fiawvqaevv rkalagsafa
      421 slpvlsqasc fsrtarvpeg dvtirsmaal ypfdntlear vltgaqlray lefsvryyvr
      481 tpagggpvdp skvtnadgip dynydvvygv syevdiakpa gqrigkltfe gkplddaarl
      541 vlavnnyras gggnfphvaa aeqvwstsde irnlligwvq etgeidpaaf asvewkvtrd
      601 gvpvf
//
LOCUS       WP_457693744             221 aa            linear   BCT 27-JAN-2026
DEFINITION  ANTAR domain-containing response regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693744
VERSION     WP_457693744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=24512
     Region          28..216
                     /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 mrspvsaaep eqpvadddqs hvpplttrvv iaedealirl dlkemleeeg ytvvgeagdg
       61 qtavelareh rpdlvildvk mpvldgisaa ekiaeesiap vlmltafsqr elverardag
      121 amaylvkpfs ksdvvpaiem avsrftelkt lekevadltq rletrklvdr aksilqtqyg
      181 ltepaafrwi qktsmdrrls mqqvaeavie daeekkqqkd q
//
LOCUS       WP_457693745             318 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693745
VERSION     WP_457693745.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33538
     Region          15..269
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 mttpdtlapa tgtgtdtvlk adgvtmrfgg ltavrgvdlt vgageivgli gpngagkttf
       61 fncltglyvp tegtvsyrgt rlsrkphlvt qtgvartfqn irlfanmtvl envlvgrhtr
      121 tkeglwsall rgpgfkkaer gseqramell eftglahkrd hlarnlpyge qrkleiaral
      181 asepglllld eptagmnpqe trttqelvla iraqgiavlv iehdmrfifn mcdrvavlvq
      241 gqklvegtae vvqadervia aylgtpvedv aapdqatdpa aapdpaepga pdtaaepdaa
      301 dgaapadrpa qgqtgdtp
//
LOCUS       WP_457693747             599 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter permease [Streptomyces
            nigrescens].
ACCESSION   WP_457693747
VERSION     WP_457693747.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..599
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=62635
     Region          264..568
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mttktttttp argliplper tarlitaaga lattattgla wtwssdfpgd ltyyfspagl
       61 qvvtlvggvl tllfalaalg irglqwltpa grhaptllaa latfaatwft liaiavhlng
      121 linlepggal aavtslitla galalppdqa adkqpgtpwq rftaslaasp lrrrtrelps
      181 waeiliiaaa faagllafty gidtddgapf vgylifmvla ipalnragli arltaltrth
      241 rgvalgaafi aaacfpftqd tdqytiigan ilifatvalg lnvvvglagl ldlgyvaflg
      301 vgayaaalvs gspesafglr fpfwaalltg aaaslifgvl igaptlrlrg dylaivtlgf
      361 geifriamln lngttgpdvt ngamgipnip nleifgfnfg ephdilgvpi atygnyyllm
      421 ilvtafivlv frraaasrig rawiairede taaiamgins frlrllafal gaalaglagt
      481 vhahvvttat peqfqfagpq ppnsafllaa vilggmgtls gplvgaallf lipakldflq
      541 dyqlllfgia lvllmrfrpe glipdrrkql efhetgqldv pdqrlpdada tlgatkaka
//
LOCUS       WP_457693749             157 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457693749
VERSION     WP_457693749.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16573
     Region          23..149
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mgersttkfp qeildqwtgl gldlpsffsa ghlgermsvq vteaaperiv gtmpvegntq
       61 pygllhggas avlaetlgsv gamlhggptk lavgvdlnct hhrgvrsglv tgvatpvhrg
      121 rstatyeivv tdeqdkrvct arltcmlrev dtdayrg
//
LOCUS       WP_457693761             273 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693761
VERSION     WP_457693761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29913
     Region          56..176
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mnqdhepeat rrdasdaess rasrgwwdrn adeyqsehga flgddrfiwg pegldeaeaa
       61 llgpaaelkg rrileigaga aqcsrwlaaq galpvaldls hrqlqhalri aggsaddape
      121 lveadagalp frdhsfdlac saygalpfva dpvrvlrevr rvlrpggrfv fsvshplrwa
      181 fpdepgpegl svsasyfdrt pyveqdesgr avyvehhrtv gdrvrdvvaa gfrledlvep
      241 ewpewntqew ggwsplrghl ipgtaifvct aqa
//
LOCUS       WP_457693764             317 aa            linear   BCT 27-JAN-2026
DEFINITION  PAC2 family protein [Streptomyces nigrescens].
ACCESSION   WP_457693764
VERSION     WP_457693764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Ramos,P.C. and Dohmen,R.J.
  TITLE     PACemakers of proteasome core particle assembly
  JOURNAL   Structure 16 (9), 1296-1304 (2008)
   PUBMED   18786393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10561008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="PAC2 family protein"
                     /GO_process="GO:0043248 - proteasome assembly [Evidence
                     IEA]"
                     /GO_process="GO:0051131 - chaperone-mediated protein
                     complex assembly [Evidence IEA]"
                     /calculated_mol_wt=34283
     Region          34..254
                     /region_name="PAC2"
                     /note="PAC2 family; pfam09754"
                     /db_xref="CDD:462883"
ORIGIN      
        1 mldpqglyew epsglaevea lasrdsaglv llyhfdgyid agetgdqive rlldglpnev
       61 varfdhdrlv dyrarrpllt fersrwtaye tpsielrlvr dttdapflll sgpepdvewe
      121 rfagavkeiv erlgvrlsvn fhgipmgvph trpvgitphg nrtdlmpghg gffdeaqvpg
      181 saealiefrl aeaghdvlgv aahvphyiar saypdaalta leavtaatgl vlpgaahslr
      241 tealrtqeei erqisegdee lvalvsgleh qydavagaes rgnlvaepve lpsadeigre
      301 ferflaereg dggagga
//
LOCUS       WP_457693767             153 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457693767
VERSION     WP_457693767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15777
     Region          49..151
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtaasgldan tpdiepalaa esgsgsaads psagdpapas fvvnipgiad ddlepepldp
       61 sqilsgepvv tgkvlweapd gqqirgiwqi tpgvvtdtea nelfvvvsgr atievedgpv
      121 levgpgdacv lregdrtrwt vhetlrkayh isl
//
LOCUS       WP_457693772             980 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457693772
VERSION     WP_457693772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 980)
  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 980)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..980
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103956
     Region          283..956
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 marrwdaaag etrpsdgpat ampggagegs gtgdaalagc aavflpaqpp ragkialwrp
       61 dggplpdlgt gggeegasdq dgaaepgqlt varrhgngar srtvpavllp pamavplllr
      121 arhdptahpa aacwgaatlh alhlaargrl lpgltledtd awragpldpe diahlraiaa
      181 ampadahavp ipgsrplqvt dpavlvrlyv davvdalprt paakmvagap yaasapqhlp
      241 garewaaeva agvdagvrls lrldlaphkl fdtaeesgag gteersaaaa vlqvhsltdp
      301 tlvadardlw egegpdhfgp rsrvdtllal rraariwapl grllerpvpd vlplgedely
      361 ellgeaaprl gaagvavhwp kelargltaa avlrpapgsa adgfgffdtr ellqfrwqma
      421 mdgvplteae mdalaeahrp vvrlrdqwvl vdpglvrkar krelgylepv dalaatlngt
      481 aevdgeevev vpqgalaalr grltaevrpl pqppglratl rdyqlrgmaw ldtmtslglg
      541 gcladdmglg ktitvialhl hrrpsapvlv vcpasllgnw qreierfapg tpvrrfhgag
      601 rsldgldggf vlttygtmrs sathlagrsw awvvadeaqh vknprsstak alrsikapar
      661 ialtgtpven nlselwalld wttpgllgpl ktfralhare veggedpaaa erlarlvrpf
      721 ilrrkksdpg iapelppkte tdhpvalgre qaalyqavvr etltrietae giarrglvmk
      781 lltalkqicn hpaqylkeaa pglaarsgkl elldelldti laeggatlif tqyvgmarll
      841 erhlatrgip aqllhggtpv aerekmvdrf qsghapvfll slkaagtgln ltraghvihy
      901 drwwnpavee qatdrayrig qtqpvqvhrl iaegtvedni aqllsakral adavlsgget
      961 altelsdael adlvslrrpg
//
LOCUS       WP_457693778             314 aa            linear   BCT 27-JAN-2026
DEFINITION  quinone oxidoreductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693778
VERSION     WP_457693778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  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 314)
  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..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /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=32513
     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 mraivmrefg gpdvlrledl pepaprgghs lvdvalagin yadvhvrgds ylapvelpyv
       61 pgnevvgtvd ggrrvvglcr gggyaertll hrrvtwdvpd aisdeqaval alqgnsawhl
      121 lftslrltag etvvvpaaag gvgslavqla ahagakvial agspekrkla gelgahavvd
      181 staedlteri ldaaggpvaa alemtggvtf ertlaavapr grlavygfag gelasvptre
      241 lmersitvsg fwlpqlyadr talptsmral fdavaegtlk pltgavyglg eaarahhela
      301 artptgklal dvtr
//
LOCUS       WP_457693789             295 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces nigrescens].
ACCESSION   WP_457693789
VERSION     WP_457693789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Hejazian,S.M., Pirmoradi,S., Zununi Vahed,S., Kumar Roy,R. and
            Hosseiniyan Khatibi,S.M.
  TITLE     An update on Glycerophosphodiester Phosphodiesterases; From
            Bacteria to Human
  JOURNAL   Protein J 43 (2), 187-199 (2024)
   PUBMED   38491249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32310
     Region          34..290
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mrirpvatvv agalmglstl alspaaaqaa paghtpltva hrgassyape ntlaaidaad
       61 rlgiewvend vqrtkdgelv ilhdnslart tdveqvfpgr spwnvsdftl neiekldags
      121 wfgpkfrger vptledymda vehndqsllm elkspelypg ielqtltelr rtgwmdkghv
      181 khrliiqsfn adaiktvhml rsdiktgflg npsvadlpkf akycdqinpv htavtreyva
      241 avhglrgphr rtldlytwtv ddpavavkva nlgvdgiitn kpdvvrdale dhddd
//
LOCUS       WP_457693787             197 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457693787
VERSION     WP_457693787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20478
     Region          27..195
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtyaeqdsgp atppdaapea aarrdwawrr latpigplll aatreglvqv afhaderttr
       61 raltrleqff ggppltgiph lttataelta yfagelrsft vpldwslssg fnarvlhala
      121 dgvpygsvvg yqdladrvge pgaaravgaa mgsnplpvvv pchrvvasdg giggfgggle
      181 tkrlllaleg vlpaplf
//
LOCUS       WP_457693793             192 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457693793
VERSION     WP_457693793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=20308
     Region          1..187
                     /region_name="TerZ"
                     /note="Stress response protein SCP2 [Signal transduction
                     mechanisms]; COG2310"
                     /db_xref="CDD:441884"
     Site            order(47,49,94)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 msvnlskgqg islqksdgga ltavrmglgw rsaprrglfg rrtseidlda savlfadkkp
       61 idvvffqhlv sddgavrhtg dnlvggagqg gddeailvdl arvpvhidqi vftvnsftgq
      121 tfaevqdafc rlvdentgee larytltggg nytaqvmskv hrvgggwqmt aigepsvgrt
      181 fqdlvpaiap hl
//
LOCUS       WP_457693794             697 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457693794
VERSION     WP_457693794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10161385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..697
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=71948
     Region          13..165
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cd06974"
                     /db_xref="CDD:132992"
     Site            order(27,29,68)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mtaelvrgqn hpldrtrvei rvaaggpvva gvtlgdeqgr lsgveavahp gvprrtgiev
       61 prqaaaehri avdldalsat vhrvsvllal ptgiggltaf gaaaapsvtv tgldgtgiar
      121 ytitglgaes avvavelyrr qdiwkvravg qgyadglpam lrdqglpqaa elaaeieeav
      181 grgqaravpa paplaagrse rpgagpaaap aqdrpspapa taadgpapsg agagagsaag
      241 tgtgagakaa agakagdlpp apadggpidy rhprrrstpa paapapsagt ppsaaaptap
      301 dgsplpvagd aagwsmderl ynqvwgmfed larsvaayrs aadfaesrle qeldraladp
      361 rsrlgtagea vratardkha tlvtqaraal drdlaqlmae sevvepalpp afarwdnpvw
      421 qgyhvpqerp malrlgdlhl pevldlripm lvrlplergl widsgpdsya hggsgperdi
      481 grrelpgalt dgppdesalr glamesavai aarllaihpa gdfavqvidp ggtaapalap
      541 lvesgalpaf plpgakgvaa vlegltrrve lvqmavrhra adalpadldt aeqllivhdf
      601 phgfddralt qlryladegp avgvhlmlva draqsreygp vldplwrsll ritpvpdahl
      661 adpwvghawt yepplapkgs qvvrqvldrl aaarras
//
LOCUS       WP_457693796             355 aa            linear   BCT 27-JAN-2026
DEFINITION  S66 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457693796
VERSION     WP_457693796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Nocek,B., Tikhonov,A., Babnigg,G., Gu,M., Zhou,M., Makarova,K.S.,
            Vondenhoff,G., Van Aerschot,A., Kwon,K., Anderson,W.F.,
            Severinov,K. and Joachimiak,A.
  TITLE     Structural and functional characterization of microcin C resistance
            peptidase MccF from Bacillus anthracis
  JOURNAL   J Mol Biol 420 (4-5), 366-383 (2012)
   PUBMED   22516613
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Korza,H.J. and Bochtler,M.
  TITLE     Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with
            a Ser-His-Glu triad and a nucleophilic elbow
  JOURNAL   J Biol Chem 280 (49), 40802-40812 (2005)
   PUBMED   16162494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="S66 family peptidase"
                     /EC_number="3.4.-.-"
                     /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=38655
     Region          21..344
                     /region_name="Peptidase_S66_mccF_like"
                     /note="Microcin C7 self-immunity protein determines
                     resistance to exogenous microcin C7; cd07062"
                     /db_xref="CDD:132883"
     Site            order(97..98,224..225,227..228,257..258,260..261,264..265,
                     312..313)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:132883"
     Site            order(119,248,329)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:132883"
ORIGIN      
        1 mpisspsasa lrhppkprpg drvavlspss glpqrfpvpy elglarlekd fglipveypt
       61 trkwgagaqe raadlhaafa dpditavfas iggddqltvl phldrelfra hpkpffgysd
      121 ntnllaylwn tgivgfhgat vmcelgrpga mhpltadslr aalftpgpye lrpaercgde
      181 ngdwddpvtf aaepalwpgg gwrwhgperv vegpswggci evlswmlmad reiqedpaay
      241 dgcvlflets eelpgadevy fvlrsmgerg llrrfpallm grpkawslsr plsgeakasy
      301 vreqraavlr alaayapdtv avfdvdlght dpqlvvpygg tirvdgvarr itvty
//
LOCUS       WP_457693798             218 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693798
VERSION     WP_457693798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10865880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23236
     Region          25..197
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cd06262"
                     /db_xref="CDD:293792"
     Site            order(74,76,78..79,133..134,155,197)
                     /site_type="active"
                     /db_xref="CDD:293792"
ORIGIN      
        1 mgysgavkvg gpadvheltd lmiskvavgp mnnnayvlrc ratdeqllid aaaephtlla
       61 ligdsgiasv vtthrhgdhw galrevvdtt gartyagryd aegipvptdv pvkdgdtltv
      121 grveltarhl vghtpgsial vyddphgaph lftgdclfpg gvgntfgsae nfarliddve
      181 rklfgelpde twvypghgnd ttlgaerphl aqwrergw
//
LOCUS       WP_457693799             264 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Streptomyces sp. 900105755].
ACCESSION   WP_457693799
VERSION     WP_457693799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            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 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..264
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27381
     Region          1..255
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 maddpfvlgg ttfssrlimg tggapslevl eralvasgte lttvamrrvd pgvrgsvlsv
       61 ldrlgirvlp ntagcytage avltarlare algtdlikle viadertllp dpvelldaae
      121 tlvddgftvl pytnddpvva rkledvgcaa vmplgspigs glgirnphnf qliveharvp
      181 vildagagta sdvalamelg cagvmlasav traqdperma hamragveag rlarlagrip
      241 rrylaeassp aeglavldpe rpaf
//
LOCUS       WP_457693801             212 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693801
VERSION     WP_457693801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23311
     Region          10..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meegrltlre rkklrtrqri sgeatllfir rgfdhvtvae varaaevstm tvfnyfprke
       61 dlfldripea relivravre rgadeaplaa lrrlvlglla erhplagvge gfeyfwrtvl
      121 dspalrargr eaveemedtl aallaeaagg tdrpghdarl gaalvvaavr vayveaaarq
      181 lggdpvdeva veqaevlrrt fealeralpg fa
//
LOCUS       WP_457693805             336 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457693805
VERSION     WP_457693805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33761
     Region          1..326
                     /region_name="bac_FRK"
                     /note="Fructokinases (FRKs) mainly from bacteria and
                     plants are enzymes with high specificity for fructose, as
                     are all FRKs, but they catalyzes the conversion of
                     fructose to fructose-6-phosphate, which is an entry point
                     into glycolysis via conversion into...; cd01167"
                     /db_xref="CDD:238572"
     Site            order(49,274,277)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(201,244,272,275..276,279)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mivvageali dlvpspqnpl pashggspsp apdgplpall prrgggpynt avalgrlgsp
       61 aafcsristd afgealldgl rgggvdtslv qrgsepttla vadispdgsa gygfyadgta
      121 drlftlppal pdavralslg tcslvlepga sayesllrre arrgvftald pnirpglipd
      181 pdayrarfra wlpdvallkl seedalwlag sgegpggavg ggrdavlaaa kewlaagpaa
      241 ivlthggdgl tvltpgggal tvpgervtvv dtigagdtvn aallhrldah dalsrtavaa
      301 lgaedwqdil rfaaraaavt csragaeppf aaelaa
//
LOCUS       WP_457693806             352 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693806
VERSION     WP_457693806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  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   2  (residues 1 to 352)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37642
     Region          1..331
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mttmvdvarr agvsvatvsh vlnetrpvrp gtraavlgai delgythntl arslvtartr
       61 siglavsais npyfteilqg veagalaagy slliadphdd prherkvvrl lherrvdgmi
      121 vapsaepaem veylgrrkvp tvfldrlvgd ghdqvcaest gpmrqlvehl adlghsrigl
      181 vaglpglstt tervegyreg lrarglpfep allaggnsea agaqdatrql ltaagpptai
      241 vtannamtig alralrelgr evprdtalac fddfswaelf tprltaiaqp skdlgaaavr
      301 lllerlaepd rpprtlrlpc tfvhrtscgc aepappmrpa dhraaqernr tp
//
LOCUS       WP_457693808             137 aa            linear   BCT 27-JAN-2026
DEFINITION  Rieske (2Fe-2S) protein [Streptomyces nigrescens].
ACCESSION   WP_457693808
VERSION     WP_457693808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Schneider,D. and Schmidt,C.L.
  TITLE     Multiple Rieske proteins in prokaryotes: where and why?
  JOURNAL   Biochim Biophys Acta 1710 (1), 1-12 (2005)
   PUBMED   16271700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10131027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13638
     Region          43..135
                     /region_name="Rieske"
                     /note="Rieske domain; a [2Fe-2S] cluster binding domain
                     commonly found in Rieske non-heme iron oxygenase (RO)
                     systems such as naphthalene and biphenyl dioxygenases, as
                     well as in plant/cyanobacterial chloroplast b6f and
                     mitochondrial cytochrome bc(1) complexes; cd03467"
                     /db_xref="CDD:239550"
     Site            order(82,84..85,99,101..102,104,106)
                     /site_type="other"
                     /note="iron-sulfur cluster [ion binding]"
                     /db_xref="CDD:239550"
     Site            order(82,84..85,99,102,104)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239550"
ORIGIN      
        1 msqspdrrtv lrgaalagaa gfglaacssg dsganasavp depvdlgaaa evpvggakly
       61 redrlvvsqp akgtykcfsa kcthagcilt dvekeegscp chgsrfdvtt gkvlqgpase
      121 plpevpvkak ggkliag
//
LOCUS       WP_457693816             353 aa            linear   BCT 27-JAN-2026
DEFINITION  gluconeogenesis factor YvcK family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693816
VERSION     WP_457693816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /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=37592
     Region          20..341
                     /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 msgrtprlrr vrrfvpsgrm tkgatpkvva lgggmglsas ltalrritgd ltavvtvadd
       61 ggssgrlrde lgvlppgdlr kalaalcgdd dwgqtwsrvi qhrfqsegel hdhavgnlli
      121 valweqlgdh vqaldlvgkl lgahgrvlpm savplelqaq vrghdqdrpd eittvrgqat
      181 valtrgevqs vhvvpedppa vpeaacavrd adwvvlgpgs wfssviphll vpelrealee
      241 tkarkvlsln lapqpgetdg fspqrhlevl arhapklafd vvladkaavp diegltvaak
      301 qlvgsevela avaaqgddtr ssaggapdrh dpellaaayd rifrmhgrig pwr
//
LOCUS       WP_457693818             400 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoglycerate kinase [Streptomyces nigrescens].
ACCESSION   WP_457693818
VERSION     WP_457693818.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41541
     Region          3..400
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mktiddlqva gqrvfvradl nvpldgttit ddgriravap tiaklverga rvivashlgr
       61 pkgapdpdfs lapaaarlgd ilgqdvafat dtvgesarsv vagladgqva vlenlrfnag
      121 etskddaerg afadqlaala dlyvgdgfga vhrkhasvfd lpkrlphaag dliatevavl
      181 kkltedvkrp yvvalggakv sdklavidql iekadrilvg ggmaytflka kghevgisll
      241 qedqvpacle ylaraekrgv efvlpvdvlv saefpdlktk apahpgtvaa daipadkegl
      301 digpktrely aakvadagtv fwngpmgvfe hpdyadgtka vaqalldspa ftvvgggdsa
      361 aavrllgfde tafghistgg gasleylegk tlpglaaled
//
LOCUS       WP_457693823             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457693823
VERSION     WP_457693823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42935
     Region          25..388
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(35..36,39..40,43,75,130..131,133..135,138,158,
                     161..162,166,242,245..246,249..251,254,278,282,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 madsgtgada graagagalv rrggfgrlwg aaaisrfgda lrgtalplla yaltdsplli
       61 slvtacgfvp wlffgllggs iadrvdqrra mwtvdvlrgl lmagfalava fdragiglll
      121 alsfalttlq tlfdnaatal lpavvpkeal aaanarlmtg qelagrfvgg plapvliglg
      181 aalpfladaa tyfvaaalva slrtgpparr ptaagctvrr eiaegirqlw rdrvlrafcv
      241 svalgnvgig aliatlvvvi kgrlgagdfg yavvttgygi gmvlggllad rtiaaaggkg
      301 rtlllagvlq avtlvgfgtl rtvwvaavll glfgfagmvw nvlettavqq rspagmlgri
      361 ssafrtvsva gtplgalcgg aaatafgpna pallaaalla lgaaalipvl qtadgassds
      421 gqiphtar
//
LOCUS       WP_457693839             334 aa            linear   BCT 27-JAN-2026
DEFINITION  COX15/CtaA family protein [Streptomyces nigrescens].
ACCESSION   WP_457693839
VERSION     WP_457693839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=35773
     Region          39..302
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mpntlnplel iarrwqpsaa fvrraalaav vmaviivvtg gavrlsqsgl gcstwpkctp
       61 dsltptaamg ingliefgnr mltyvlcavv glfiiaarar hprrrsltrl gwaqfwlvmt
      121 navvggitvl tglnpyivss hflaatallt vavlswkras egdeeprdlv arparqlawl
      181 lvaatgaltv igtvvtgtgp hagdakkvhr ipldwqeitq lhvdfvyivv glsvalwftl
      241 ravkapaapr rmllelfaci aaqgvigyvq yfmglpeivi glhmlgsalv wicvlrfcls
      301 lrdrgplqae dpgepapsge heapepqgas alsr
//
LOCUS       WP_457693841             268 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693841
VERSION     WP_457693841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27675
     Region          77..268
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttteagrva gtfsprpgaa plprmiraqa aletrmllrn geqllltvii ptlllvlfsa
       61 vdivavptet aggtgrsvdf lapgilalav lstaftgqai atgferrygv lkrlavsplp
      121 rwglmtaktc avlvtellqi alltavalal gwsphgspla valllllgta afsglgllma
      181 gtlkaeatla aanlvfllll vgggvivple kfpeaaqsvl gllpitalsd glrevlqhda
      241 gipwpdlgil avwavlglga aarffrwe
//
LOCUS       WP_457693842             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457693842
VERSION     WP_457693842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33463
     Region          19..245
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mpstspggdp rppgrepave itglvkrygt ktavdgldlt valgavtavl gpngagkttt
       61 vetcegyrrp dagrvrvlgl dpvadaaalr prigvmlqsg gvyagakaee mlrhtatlha
      121 hpldvgtlid rlglgscgrt pyrrlsggqq qrlalamavv grpelvflde ptagldpqar
      181 hatwdlvrel radgvstvlt thfmdeaeql addvaiidgg rviaqgspde lcrggaensl
      241 rftgrpgldl asllkalpad saaaepvsgv yrvhgkvnpq llatvaswca qngvmpdaia
      301 verhtledvf leltgkelra
//
LOCUS       WP_457693851             106 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457693851
VERSION     WP_457693851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..106
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10660
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mayltlaaai lsevlattam kytegfsrlw psvgtalgyl lafallaqtl ksmsvgtaya
       61 iwsgagtavi aaigmvflge satalkvlgv llviagvvvl nldgah
//
LOCUS       WP_457693844             285 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693844
VERSION     WP_457693844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /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=29855
     Region          34..259
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mkyasedqeg paveqtegpa asapeqterr gpaphaaaph deqqgtrnrv arsildhgps
       61 taaelalrle ltqaavrrhl dalaaegvve prekrvygtr grgrparafa ltdcgrdafd
      121 qaydqlatea lrwiaqsagg gekgeaavaa fararlaaqa egyreaveaa epdarteala
      181 kaltadgyaa tarsapnpql geqlcqhhcp vahvaeqypq lceaetevfs rllgthvqrl
      241 atiahgdgvc ttfipkagag kaahstartt ktttasasta grnpa
//
LOCUS       WP_457693853             179 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693853
VERSION     WP_457693853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19407
     Region          1..179
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 marrydpdrr qriidaaitv vgergiagls hravaaaadv plgsttyhfa tlddllvaal
       61 rqsnvmcldd farwvdgidp aaplaeevar lvedtltgdr rrmeleyely laalrheavr
      121 piaaecvdem vrllgqrigd lrtartvval tdglvlqhll tgqpfdpeav raglagvla
//
LOCUS       WP_457693863             292 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693863
VERSION     WP_457693863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31217
     Region          66..195
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtqqpppagp agppdgpapp dlpdrvarvy geldlstvpa faggfinfgy wtglpgpadr
       61 eltradrvrs eedlyrlvlg tfdrpqgrta ldvgcgrglg calalrefgl gtvigldahp
      121 dqiararean aellttsada pgrlefllga aqdiplpdgs vdclfsveaa qhfrdlpgfa
      181 reaarvlrpa grlalttffa rtraaaralp ellppyadgl dvphvvdeva gtltaaglre
      241 vrvraigdgv wepydrymaq qpelgddewp rryltayetg lldyyvltaa ag
//
LOCUS       WP_457693865             414 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457693865
VERSION     WP_457693865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10993447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=42093
     Region          1..160
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cl18957"
                     /db_xref="CDD:473128"
     Site            order(26,28,67)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
     Region          232..396
                     /region_name="TerZ"
                     /note="Stress response protein SCP2 [Signal transduction
                     mechanisms]; COG2310"
                     /db_xref="CDD:441884"
     Site            order(269,271,315)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mtamtpgsnl plsavrvavd vtapvrldvs glllaadgkv rsdddfvfyn qpagpgvths
       61 aaagggdtit vdtaavpdgi ekivvtasld tpgatfagte ptgtvrnadd gsvlasftpp
      121 qlgpetalvv veiyrrgdaw kvravgqgya nglagiatdf gvsveepaap atapqappap
      181 papaapaapa gqwgpptgap apaappaapp apaaapaapa apgkinldkg rvslqknqtv
      241 slvkggrpll ssvrmglgwe pafrsksidl dasviaygpd rkkvdncffg klmilggaiq
      301 hsgdnltgeg agddeaitvh lgglppevtg lvfvvnsfsg qkfsdvakay crlldaqsge
      361 elvrfdlths eprtgvmmak lirqfsgewe mtalgeyvda rtvrgmvkpa gkal
//
LOCUS       WP_457693869             269 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693869
VERSION     WP_457693869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="NAD-dependent epimerase/dehydratase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28614
     Region          6..229
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtaprtvllt gaagglgtlm rellppygyl lrlfdqrpva gepdaitael adaealraav
       61 hgvdaivhla gisleapfek ilraniegty rlyeaaraag vrrvvfassn havgftprpa
      121 dgsaaipvdt prrpdtyygl skgfgedlas lywdlhgiet vsvrigscfp eptsvrmlsi
      181 wlspadcarl ldaaltapgv ghtvvygssa ntrlwwdlst aralgytpqd dsepyaaeli
      241 aaqgaldpen pahdrlggaf ctdpprwph
//
LOCUS       WP_457693874             236 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457693874
VERSION     WP_457693874.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  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 236)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..236
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25282
     Region          22..139
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          171..227
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtttqdddrr tgdgeaptrl rivladdeqm vrsalraild aegdmevvge aatgaeavpl
       61 iralrpdivl mdvrmpeidg irateqvlag mdrppriivv ttfendayvy dalragasgf
      121 llkrsgaedl vqavrlvsrs dsllfpaavr qlaarhager aaddavralr arlsererav
      181 lrlmtagmtn aeiadrlgvg patvkthvag vlaklgvrdr tqaviaayec gfvrpg
//
LOCUS       WP_457693878             418 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693878
VERSION     WP_457693878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..418
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=46745
     Region          1..382
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqlrynyrvy pdvsqrrala nafgcarvvw ndclrdrnea haarlpyvks aelsrrritq
       61 akrteerawl advsavvlqq slrdldtayk hffdslngtr kgrrvappry kskkdtrqsi
      121 rltttafslq engtvyvakv gnikvkwsrs lpvaptsltv tkdssgryfm sfvvnterdi
      181 lpdldtevgi dlglstfavl sdgtristpk flrraekklk rlqkglsrkt egsknrakar
      241 ikvarqharv adrrrdwhhk astqiirdnq avyvedlavs glartrlaks vhdagwsafv
      301 smleykavkh gryfgkidrf eptsqvcsac gtkdgpkplr vrqwtcqecg avhdrddnas
      361 knalaagrad rlnasqsagk tktkvpaqrv eagshrdgrt taagipgpqa gehvnlcr
//
LOCUS       WP_457693876             425 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457693876
VERSION     WP_457693876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  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 425)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..425
                     /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=43596
     Region          <203..409
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrltgrrwih lvlggallmp ffllaavvlp lvadgadplr hvgwqfvafg calplgalaa
       61 llfpllrple vaavrslcgv paerlaegpa vswaarrrta lwfvahlltg givsgmtlsa
      121 ppaavlllll pfsdplqhaa pglpdtfqgv lgplaglall alvagtswaa gtllgrvapv
      181 llgptpadrl aaaerraadl asrnrlarel hdavghalsa vtlqagaarr vldtdpefar
      241 ralaaieett rdavaeldtv lgllreedgg dpaapaptld gleallgrtr aagvpveatv
      301 egrctglapv vsreayrivq eglsnalrha gpvpvrlhlg vregelqirv enpvagpvag
      361 vatgsadpaa rpgggrglrg iaerarllgg aataaerdgv wrltarlpla gtatgtgtgt
      421 gteqr
//
LOCUS       WP_457693879             256 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457693879
VERSION     WP_457693879.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28016
     Region          7..252
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msaadtggsq vksavrtvel leyfagrpgm hslasvqeav gypksslyml lrtlvdlgwv
       61 etdatgtryg igvrallvgt syidgdevva aarptldrls ddttetihla rldgtnvvyl
      121 atrqsqhylr pftrvgrrlp ahstslgkal latytdeqvr allpptlaql tehtltdreq
      181 lieelhtvre qgfavdreen tlglrcfgva ipyrsparda iscsvpvarl tpgheqmikd
      241 alfdardrla latrrl
//
LOCUS       WP_457693885             229 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693885
VERSION     WP_457693885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24399
     Region          27..137
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtssqgflgf wettgsaktf thpldpalld ayvprsarvl dygcgygrlt aelaglgyra
       61 vrgvdvsaal iargqrehpg lellrcpglp lpfedgafda allfavltcv prdadqtaiv
      121 gelgrlvrpg gvlylsdvpl qgdalnrery arfaerhgty gvfetpdggv frhhpperlr
      181 glvreagfsv lkeragsaat ldgrtaerlq iiarrepaap apspgpvpg
//
LOCUS       WP_457693887             388 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693887
VERSION     WP_457693887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42493
     Region          1..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mssagqnvkt vrkrrgltqr eladasgvsl stirkleqgd regarletlr klaialhvpt
       61 mrlagapred ggpqttdrwe avksalerth waagvedepp tvtgvhsalq kalplftgdr
      121 ltelsvllps llrdtdalgp qgrtvrmrll qlsgwlmvqt rqfaaaetal eralehaadg
      181 ldkaatisiv cwlrlrqgrl deafalavgw adeieprmsr atpaelstwg wlllrasaaa
      241 irngqptead daiklamaaa vvmgrehape ndflrmfgpt tvklkaaena svtdrpdmvl
      301 rmaqripmag lrptsnnrnr hlldvadala ktgqyadafe kleqikadsp ewlpnqryar
      361 dilskliksr rtlttdmram adavglpl
//
LOCUS       WP_457693889             220 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693889
VERSION     WP_457693889.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23796
     Region          45..151
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mparhdiaae relwdtfaes trgkvfdsep vlcwtqytgh gpgpeilgtp ttaleigcgt
       61 gralahlaqq gvkvtgvdls pvmvehtter wgplgaqfvc aevleylrdr tdtydavysi
      121 fgavwftdpa kllplvaqrl npggvfafsh ppaipgaygp qgmykggfag kamytyrysy
      181 tprkwtsflh kagftgldvq ildaptpghi gtliaraikp
//
LOCUS       WP_457693892             282 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693892
VERSION     WP_457693892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30985
     Region          17..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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          108..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mavspsssaq qarqalakrl adlcrdaglt gldlaercgw srskssrimn aktppsaddv
       61 rawcraceae dqtedliasl rsaegmwvnw rrmeraglrq aqearlplyr ktrrfrsyss
      121 wlvpgmiqtq pyttaalqai qrrrglvddv adavaarmlr qrvlcegdrr faflveesvl
      181 rtgiggaevm sgqlghlvsv aslphvslgv vpmtpdrerw ptegfwiyda aqvnvelvsg
      241 yltitqpsev alyaetfael aalavygpaa ralitsamna lr
//
LOCUS       WP_457693903             355 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces nigrescens].
ACCESSION   WP_457693903
VERSION     WP_457693903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..355
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37624
     Region          5..336
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,226,290,310,312..314)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,174,177,179,226,233,290,310,
                     312..313)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,174,177,179,313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mttafdpidl agtplanrlv mapmtrnrat aegvptpsmv ryytqrasag liiaeaaqte
       61 ivgrgypltp glhtpeqvag wrrvtdsvha agskifaqlw hggrighpvl lpdglvpvap
      121 savaaagqgf tqdgptdfvt preltgeeih rtiegfaaaa rnaleagfdg veihggngyl
      181 ihqflapnsn rrtdewggsd eararfaiev vkavaaeaga hrtglrlspg npfndidepa
      241 peatystlve alaplglayl htcdvrdlel larlrkrfgg tfllnpateg rptgpeelsl
      301 veegeadlla ygalflanpd lprrlalggp fntpdrasfy ggddsgyldy palea
//
LOCUS       WP_457693905             406 aa            linear   BCT 27-JAN-2026
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Streptomyces nigrescens].
ACCESSION   WP_457693905
VERSION     WP_457693905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=43314
     Region          35..387
                     /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..133,192,244,268)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mlilttavta galtlsacgs rgddksgdgs kttvviglda pttgelsalg lgirnsaqla
       61 idnankagev kgvtfkleal ddkalpnvgq qnttklagde dvlgivgpln sgvaqsmqqv
      121 skqnnltlis panttpdltq gpdwrkdkrv rqfptyfrta ttdevqgafd gqyayekmkv
      181 kkayiiddqk tygvglassf kdqfsklggk ivgtehvspd drdfkavvsk vksakpdlvf
      241 yggeypasgp lsqqlkdggv tvplmggdgm ysgdyiklnk kaqgdyassv gkpveelpsa
      301 kkfiadykaa gfkesyeayg gstydstwal iqavkkvved ndgklpedar kkvvdamnkv
      361 tfdgvtgpia fdkygdttnt mitayqvdkg kwasrfsaef kkfdks
//
LOCUS       WP_457693923             210 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693923
VERSION     WP_457693923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23096
     Region          14..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maaargrpsl tehrrlqtrl eiaeaaatlf adrgydtttv ediasaagis lrtfyrycpa
       61 kedaltplfa ssvgqlvdvl aehpveepls aaieasfgta taerrledaa rarrlirvlg
      121 tvpvlkmrwl aagremqerl apalasrada pldslevrll ttavldaltv tmehwawqde
      181 peefvdlmrr alaflrldel qttpepsvdk
//
LOCUS       WP_457693928             440 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457693928
VERSION     WP_457693928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46192
     Region          2..431
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mdwdglrrrm rgallrpgda gfenarklfn plnddlvpaa vaqcesvadv reavtaaanr
       61 vplaarsggh syvgysaphg gltldlrrls tvqvqpdgta tigagatlqg vytalgqanr
      121 clpggscftv giagvalggg igvlqrkfgl tcdhlvsaev vtadgrtlta satqhpnlfw
      181 alrgggggnf gvvtqftfat dpapsltvfr ldfpagkatk vltawqpwit aaprelwanf
      241 nvsggtnprc kvagcfvgps sacnpllndl vsranvspel rrvedrdyfk amrffsgssd
      301 rqsfvassrv lashaanpga lvtllkdrpg mdlildplgg avadvdvqqt afphrkafat
      361 aqiyasataa seaavtrsvg qvvaglaaqg ikggyvnyid palpdwakay ygpnldrlrt
      421 vaydydpdqv fdfpqavaht
//
LOCUS       WP_457693932             512 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457693932
VERSION     WP_457693932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..512
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=54285
     Region          18..511
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 mhdapdrppp prhgpeplvr irglskrfgg tlaldavdld ihsgsilall gpngagkstl
       61 ikvlagvhha degevtvagh plgteaaart msfihqdlgl vewmtvaeni algtgyprra
      121 gllswrltre rcaealsiva ahldprtvla dlpraerslv aiaralstra elivldepta
      181 slpaadcarl fevlhtlrdq ghalvyvthr ldevykvaee favlrdgrli sqgplaghsp
      241 arlvhdivgh epvgfrlapa agpavlsldg vrtentapvs lelrtgeilg mvgltgaghm
      301 elgralagar pvvggrvrln grpytpgtvt aavdsgvglv tsnrqeegca aeltvrenfl
      361 anpradglpa fhwisprrer aeatalterf svfprdseap iatlsggnqq kvmvgrwlri
      421 hrsllileep tagvdigakt avyrllqdal aeglavllis tdfeevaqvc hralvfvrga
      481 vteelsgkal tvaglarass amaaltgetr rp
//
LOCUS       WP_457693934             346 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457693934
VERSION     WP_457693934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36219
     Region          39..328
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtpsphsppv rrlghlvgay gllaltallf lafslalpdt fptldnisei lsnqsipail
       61 algamipivt akfdlsigyg lglahvmtmq lianaswpwp laclvvilgg avigtfngvv
      121 vefakinsfi atlgtgsily altgwitnga rivpgpqglp aaftdlydsr flglpvsacy
      181 vlaltavlwl llerlplgry lyvigsnpra adllgipsrr yviyafagsg livgiagvll
      241 aaqqrignps vgldyllpaf vgallgstai kpgrpnalgt lvavvilaig lagigqfgaq
      301 fwvtplfngt tlllavgmag yaarrqlrhr raepprthkd lpkvts
//
LOCUS       WP_457693937             261 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457693937
VERSION     WP_457693937.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26394
     Region          16..260
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mpapaqtsdd gpqtgrlrdr valvtggasg igascarrla aegavvvvad ldedgatrva
       61 rqitaasgta lprridvtdp dsvtrvvtea atlrdglqia vnsagingpl splaelppad
      121 fdtvmrvnly gvfhamrcql pamaatggvi vnlasiaahs gfrghaayaa akqgvlaltr
      181 taareyaghg irvvsvspgi vdtpmvtslp pgatdgllta vplrrtaqpa evaaliaflv
      241 sddasyvtgs dhvvdggyla k
//
LOCUS       WP_457693944             481 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693944
VERSION     WP_457693944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..481
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51314
     Region          106..318
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          392..472
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 malgvvaatv plavpttasa apgdaalsay fdqrldwrsc ddggaaecad vevpldysrp
       61 dgktiriavs rikagqpser hgalftnpgg pggggltlpa kmlkkgvipd svsrrfdlig
      121 fdprgvgrsa pvncglteqe lslngpvyrp etfdkdvsra rtmaekcqdk nsgvlphitt
      181 rntardmdvi rgalgekkis ylgisygtyl gavftqmfpe radrfvldsa ldpgrvwrgs
      241 fqdrtqdaer aftrwtqwta krhatyglgd tpdkvrerfw alfnrpapnp vhdfvsgfps
      301 vfydvekaak siaglnttag ptapatgtsk easagpsaas gasdnfhsay wsvmcadsds
      361 wprdpeqyrr daaldkqnnp lsagsasnin acafwpkate pttvvdntag alivnnewds
      421 qtplagatgl qkamkgsrmv tvqdrvghgv ygtnpcadda vntylatgrl paknlncrst
      481 g
//
LOCUS       WP_457693964             320 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457693964
VERSION     WP_457693964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /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=34888
     Region          3..312
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrvlallel lqthpgltga qladrlgtdv rtvrryasrl relgipvqsd rgrfggyrla
       61 rgyrmpplml tneealvvml gllagerlgm sttapagaga lakiervlpd plraplaamr
      121 dtlsftantv laqapeagvl ltlaqacrsg htvglryrsw hqehterdvd pygvvfhsgc
      181 wylvghdhlr dslrtfridr iasatpraat ftapddfdpv thltaslart papwqvevli
      241 egpiediarr lprtiatlta tptgvlmraq aaqldsvarl laslewpftv hspdqlrqsl
      301 kdlaqrltaa aerppegtpk
//
LOCUS       WP_457693966             247 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457693966
VERSION     WP_457693966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26849
     Region          3..>103
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          4..244
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 matfvlvpga wlgawawett aqalrerghe alpvtltglg ersalatpev gldthiddit
       61 afvlerdlrd vtlvahsyaa vpvtgaagrl gprlerlvyl dsapfaegtc lldvmpddsv
      121 dqlhqqvaeh gdgwrlplpp fellstfstl egldedqldl mrtratpqpf ptfaqrltrp
      181 gelgpdvdrv vvacrdakal ldagmptlaf lnqspwrhfh lptghwpmls tpvelaetld
      241 avdssgy
//
LOCUS       WP_457693969              98 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein K [Streptomyces nigrescens].
ACCESSION   WP_457693969
VERSION     WP_457693969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Pfeifer,F.
  TITLE     Distribution, formation and regulation of gas vesicles
  JOURNAL   Nat Rev Microbiol 10 (10), 705-715 (2012)
   PUBMED   22941504
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523950
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..98
                     /product="gas vesicle protein K"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=11102
     Region          11..91
                     /region_name="GvpK"
                     /note="Gas vesicle protein K; pfam05121"
                     /db_xref="CDD:428319"
ORIGIN      
        1 mtgrtgtpes ridldreqmg rdlvslvltv vellrqlmer qairrveqgd lsdeqvehig
       61 etlmhlearm telceqhdlr ledlnldlgp lgsllprt
//
LOCUS       WP_457693971              76 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457693971
VERSION     WP_457693971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..76
                     /product="gas vesicle protein"
                     /GO_component="GO:0012506 - vesicle membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=7698
     Region          23..60
                     /region_name="Gas_vesicle"
                     /note="Gas vesicle protein; pfam00741"
                     /db_xref="CDD:459920"
ORIGIN      
        1 msarepvpwd tpgplagpig vplvdlldrv lstgvvvsgd lviaiadvpl irlslhalls
       61 svservpapw sdggpl
//
LOCUS       WP_457693973             270 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457693973
VERSION     WP_457693973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=28936
     Region          16..267
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mtteqlgtse satatatyvy avsrpldpva lsglaglaeg fpvrtlplgp ltavvqhvpa
       61 aeftqdawqq rlsdraeler carahhevvt aaaacgptvp lalatlyrgd eraqqalgad
      121 rdrfatalar ieghaewgvk vslpaaapep prtrspgsgg gpsggagray lerkrglhqa
      181 rerhhdralq taedidaals rlatatrrlr phtqemtger hrlqvlnaay lvttvrekel
      241 ldavetlrhr tgaevevsgp wvpysfvgev
//
LOCUS       WP_457693977             248 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457693977
VERSION     WP_457693977.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=26690
     Region          5..236
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mtddgiyvyg ivrtdrplps hvggvgdppg vvekivegrv aavvsqappk lrarrrdlla
       61 hqelllalse ggpvlpmrfg mvapdetvir rqladaeerh laaleslagr veinvkampa
      121 ndslaalvkg datirglrde vrrrpsyean mrlgeavata larraaeagq eivrelkpwa
      181 hevcpgpevs gcqvnvsflv drsdsaefaa eaerlaedrr ervelrvagp lpcysflepq
      241 vlagragg
//
LOCUS       WP_457693980             106 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein GvpO [Streptomyces nigrescens].
ACCESSION   WP_457693980
VERSION     WP_457693980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Pfeifer,F.
  TITLE     Distribution, formation and regulation of gas vesicles
  JOURNAL   Nat Rev Microbiol 10 (10), 705-715 (2012)
   PUBMED   22941504
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..106
                     /product="gas vesicle protein GvpO"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=11962
     Region          6..105
                     /region_name="GvpO"
                     /note="Gas vesicle synthesis protein GvpO; pfam05800"
                     /db_xref="CDD:399068"
ORIGIN      
        1 maeqsrtrvr sstaarkrks tpentpaeva hraaellqnv ishrtegvsa vrrtddgwrv
       61 vvdvlelari pdttsllaty evrlddegel leyyrthryr rgaadq
//
LOCUS       WP_457693982             366 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457693982
VERSION     WP_457693982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=38285
     Region          <11..360
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mkglqptlak vpwilaalal lvgvllnlfa pepymglpll aaaplvagat ltfrsalavv
       61 cvtcvlsval dierrrpatp lfvdlavvgl igvlalgvnr livrqgrdla lardvaeavq
      121 ravlpdppkr agplavaagy taaqaearig gdfyavqetp fgvrmiigdv rgkgmqavaa
      181 vsialgafrq eaeyaptldt lgrrmdeala raaalsgpvi ssegfttavl aevsadgevl
      241 slvnrghppp ylvhdgqlvr ldpalpqlpl gvglgditpa asapvdvvpl pvgaslllit
      301 dgvteardkr gtfydpvfsn rlgrrfmdpe alvealtkdv grwtegdhed dmailavtrr
      361 rpphaa
//
LOCUS       WP_457693986             166 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457693986
VERSION     WP_457693986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18166
     Region          1..119
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtedptldpt gkslwrplrl lqasmdadia riyaderiag lkpsfvmell rlhargpmti
       61 telagsvgrt hsalsqkvaa mraagwvetv agddarskkv alterargiv grlaaewrat
      121 eaalaeieae ipypltrvva dieqvlarrs fhdrivekla edpawe
//
LOCUS       WP_457693988             695 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457693988
VERSION     WP_457693988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Levdikov,V.M., Blagova,E.V., Rawlings,A.E., Jameson,K., Tunaley,J.,
            Hart,D.J., Barak,I. and Wilkinson,A.J.
  TITLE     Structure of the phosphatase domain of the cell fate determinant
            SpoIIE from Bacillus subtilis
  JOURNAL   J Mol Biol 415 (2), 343-358 (2012)
   PUBMED   22115775
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..695
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75233
     Region          24..259
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          273..685
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 msaadgrpag agqpevkppq psglmdllgv aavlldadgr ivlwspqaed lygytaeeal
       61 gryaapllvh qehwdlvigk ftgvmetgrs wsgtfpvrhk dgtvrlvelr nmrlmddrgd
      121 fyalglatds stlreverdv alstrlisqs piglamldte lryvavnpal ermhgipakd
      181 hlgrhyreim taakfevpea amrqvlktgt pmvdqatvvg rtpsdpdheh awsislyrle
      241 dphgrvlgva dlvvdvtdry qaareaaear qrlaliadgs arigttlevg qtarelaevt
      301 vpeladvvtv dvldsvldeh rptpddgpal fralavkaay pteavraadp pghiaaydtd
      361 rlatqcvrtg rpilvshada hdlariardd haatllarag vhsymlaplt arghilgvlg
      421 liralnsppf deddlalaae lasraavcid narshqsvrn aaetlqrsll pdhpphrpgl
      481 qlasryrpaq atyeiggdwy dvlpldgdkt alvvgdvmgs gidaaatmgr lrtatcafad
      541 ldldpaqvlq hldkitsgle hyiatcvyat ydphrsvfhi anaghlppal vrsgkhpefl
      601 nlptgtplgv ggvpfetttf gldpgeqlvl ytdglvetrh hslderldtl lrlldapdrs
      661 leetcdrllr elrrpddpdd valliagtep ftpds
//
LOCUS       WP_457693994             695 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457693994
VERSION     WP_457693994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Levdikov,V.M., Blagova,E.V., Rawlings,A.E., Jameson,K., Tunaley,J.,
            Hart,D.J., Barak,I. and Wilkinson,A.J.
  TITLE     Structure of the phosphatase domain of the cell fate determinant
            SpoIIE from Bacillus subtilis
  JOURNAL   J Mol Biol 415 (2), 343-358 (2012)
   PUBMED   22115775
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..695
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74931
     Region          20..257
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          276..688
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mgtagpfgpa gaqpppgapq rsglldllsv aavlldaegr ivlwspqaek lfgytaqeal
       61 gqyagrllvh eqhldlvirl ftevmatges wagafpvrhk dggtrlvefr nmrllddrgd
      121 fyalgiatde eilrqverdv alstrlvsqs piglavldtd lrylavnpal ermngvpaed
      181 hlgrsvrevl pfletdtiea alrqvldsgt plvdvhtvgr tpadpdneha wsvsyyrled
      241 pggrvlgvaa lavdvtdrhr aateaararr rlamiadgta rigttleveq tareladvav
      301 peladvaavd ildsvlegrp pqtpgarhal fralavtaay pteavraadp pghltsygad
      361 rlvtrcvrtg rpiliphvee rdlariardp eaaallarag ihtyltmpli argevlgalg
      421 ltrarnplpf deddlalaae ladraavcid narlyqsqrn aaitlqrsll pdhpphqkgl
      481 eiatryqpag ttsevggdwf dviplradkt alvvgdvmgs gidaattmgr lrtatstlad
      541 ldipptevlq hidkitegle qyatcayavy dphhavchia vaghlppvlm rtgrppelld
      601 lpigvplgvg gvpfeeatfg mrpgdqlvly tdglvetrhd piderlslll hlldspdrsl
      661 eetcdrllda lrdpddpddv avliararhq grdsp
//
LOCUS       WP_457693998             688 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457693998
VERSION     WP_457693998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Levdikov,V.M., Blagova,E.V., Rawlings,A.E., Jameson,K., Tunaley,J.,
            Hart,D.J., Barak,I. and Wilkinson,A.J.
  TITLE     Structure of the phosphatase domain of the cell fate determinant
            SpoIIE from Bacillus subtilis
  JOURNAL   J Mol Biol 415 (2), 343-358 (2012)
   PUBMED   22115775
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11451444
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..688
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=74079
     Region          21..260
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          257..684
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpsdrpsdeq argplwsepg sllehvavav fgidddnric ywgpgaqhlf gyraaemlak
       61 pgallfpaap adgsdacarl aergrtegyw rgrllathld gsvfdcgfrv fpvagvagrs
      121 vvmalasrgd eldrvktnla fldalfetcp iglvmldeel ryahlnqgla dinglpieeh
      181 lgrriteimi tadggeyerm lrgvaeegkp vagvrvgmrt rghpdrdkvl svsffplsra
      241 ggtrpgvggl lvdvtdreqa iveatatrqr lalldqastr igttldvqvt aqelvdavlp
      301 vfadaavvel vewlderesf dpalpvitrr lahgtvlppp atelvsgveg vhyppgsaih
      361 rmlrtgrpis vvvnqefilr tvmdeararv ladsgltcll lapliargtv qgiaifgrsa
      421 arpafteqdl slaaelasra alcldnarly srernialtf qrallpsslg tcpslhlahr
      481 ylpgshvtev ggdwydvial pdqrvalvvg dvmghgvsaa asmgrlrita kalarhdqep
      541 eellteldhc aqeagielat clyirydpvt grtriasagh pppllrypdg rtelidevlg
      601 vplgvggcpf rsteiglpdd ttlvlytdgl iearghdide gltalrtels rlpdsleaaa
      661 dhilarlvps spaddtvlll arvhrlrl
//
LOCUS       WP_457694000             518 aa            linear   BCT 27-JAN-2026
DEFINITION  GMC family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694000
VERSION     WP_457694000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56240
     Region          1..513
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mydyiivgag sagcvlaarl tedestrvll veagpvddaq eihvpaafsk lfqtkydwsy
       61 lsdcepgldg rrrflprgrm lggsssmnam iyirgnrrdy dawaatgaeq wgwddvlpyf
      121 lraedfrget spwhatggpl tvsegrsrhp lmaayvaaaq eaghpytadf ngpeqdgvgy
      181 yhltqrdgmr cstavaylrp alerpnlevl tgaqctrvlf dgaratgvel erggellqrr
      241 aerevllsag aynspqllml sgigvadelt argitprvdl pvgenlqdhp higlcyltdt
      301 eslltaetpd nvrmletegr gplssnvgev ggfhrtregl dapdvqvhat pvmfheegis
      361 pvtdhafmfg avllaptsrg kvslrsaips akphilhnyl tteedratav ralrmlldia
      421 dqpslrkhrr adfrvpratd dagllefarr elqtlyhpas tcaigpvvds rlavhgvsgl
      481 rvvdasvmpt vvrgntnapt imiaekaadl irglpapa
//
LOCUS       WP_457694002             577 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457694002
VERSION     WP_457694002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..577
                     /product="trypsin-like serine 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=61771
     Region          88..291
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkpskgvtqe eirkaqeler ywtperirta vpvdavrage kgqgpqgapd avgrsalfap
       61 shqvasgvat vgvflirsed gsatphqfcs agavtsptks lvltaahclk ggkpyrnvaf
      121 vpgyrggasq agrpgerpyg lfpmepgkvw iderylsssp sddvdfavlr vgpnsqgqll
      181 edaigrgntl tavpaanlar revtlmgypg gqktplqctn atrafqgrfm eiscagfrtg
      241 vsggpflegf dgsrgnlvga iggyktgglq ddisyssqfd ndvfrlyqqa vtdaapdtvn
      301 plgdattwqh attvltgrfh sdsvrnntgd livrwsdgev slypgnrayg lgkdiqlakk
      361 grlgkqakav tageftgnst ddllvrwadg kltlykdvne tnkltqaiql kgpngtwkha
      421 eaitagrfgg gntrrddlmv rwsdaemtly tnvdgrglha ekqlakrknt twahardsva
      481 gnfaaaagdq dlfvrwsdge vtvyenvaak gfkaehrlrp aksawryssl vtagafgggt
      541 rqddllalwp ggklvmygdt takalgrerl lvparis
//
LOCUS       WP_457694004             248 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694004
VERSION     WP_457694004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  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 248)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26851
     Region          39..141
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mdaavvfsda daaalydlln pwdpercpsd gfyhelvmaa gsvldvgcgt gamlhlarer
       61 ghpgrlvgld pdraalarar rrtdiewves taaaarwdaa fdlatmtsha fqclvtdael
      121 rasltavhta lrsggrfafe trhpqarawe ewnpskasdl vdaagralrv whetesvigd
      181 vvtftgttaa adgtvlrvdr trlrfldval ldaflvdagf tiearygtwd ggpvtgtsre
      241 iitiarrr
//
LOCUS       WP_457693996             256 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457693996
VERSION     WP_457693996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27539
     Region          168..240
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mqattlpprt adlfrqgler qagaallrfg aarrrsadri swsgdgaaaw lddarghlws
       61 vgeavpaagl vlraahelpd svreftgplg taalvgrhla vtevvewvfr wtleepplqr
      121 aeervielde thhgellafl nehspahstg pgssgvslwt girdtdgrlv acgalsslrd
      181 sgaplmasva tdgrlrgqgl gaaltswltr yavrrhgfct lwqladntpa erlytrlgyr
      241 nedpcvsari aapgrp
//
LOCUS       WP_457694008             264 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694008
VERSION     WP_457694008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27830
     Region          1..263
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mrafivdaft drpfagnpag vclldkpada twmqrvaael nlpetafvhr taentyglrw
       61 ftptvevdlc ghatlatthv lhttqgaapd aalhfdtlsg altarrhsqg visldfptdt
      121 ptatpvpphl aealraepkw tgrarhdllv elpdaatvrd lapdiaalad fsgravivta
      181 sapdgadhdf vsrvfapaag ipedpvtgaa hcvlaphwag rlgrttlngv qlsprggrvg
      241 velrgdrvtl lgqavtvfdg elra
//
LOCUS       WP_457694014             287 aa            linear   BCT 27-JAN-2026
DEFINITION  metal ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694014
VERSION     WP_457694014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29021
     Region          31..271
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 msafgqvgdl lqlipvqrag aglllaslgl pvvgvvivgl dimpvrfamm hvallgiavg
       61 qllgldpvlc allacalaga gvaplartad glsgamgllm slaiaaallm lalsgvnang
      121 afallwgsil avrpvdlavl galavalpal fvwrrrelsl llhdrelalc sgvavqrltv
      181 lllvlvavav agairltgal lvdaltllpa laarrlgrsl vsitlwaigi glvvnvvgfl
      241 aslawdlppg pvlvltagav alaahliper rtsswrepas ssvpspr
//
LOCUS       WP_457694018             552 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694018
VERSION     WP_457694018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57467
     Region          28..547
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mthrihdlvp gtlrrawaae grcpdldlya lfrahrmrdp lrtavidaqg etsyaeldte
       61 arclaaglae agirpgdvvg vqlpnsraav atdlalaalg aialpfpvgr ggreavsllg
      121 rsgaraviat tvfrgtehar elaeragalp alhtviaagp gpvpagcrsl adltgdertg
      181 ftperpdpds aarilvssgs eaepkmvays hnalaggrgn flasllvdds pprclflvpl
      241 asafgsngta vtlarhggtl vlldhftped alaalrthrp thvlgvptmv rmmvercgte
      301 grtadgpral vlggsaldaa thdeaarvfg cpvvnlygsa dgvnchsgmt qrpplpddgp
      361 givvgrpdpa vceirivpph gaasdgtgei largpmtplc yvgapelnmr yrtadgwvrt
      421 gdlgmlaadg tlrvvgrlkd ivirgganis paevegelss hpdvrdvicv gvpdplmger
      481 laacvvprag reitlqslca hldtrglerr khpehllpvt galpltpagk pdraalrkrl
      541 aaglpdepar tg
//
LOCUS       WP_457694021             415 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694021
VERSION     WP_457694021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43436
     Region          25..404
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnagqqlsat dpplgsaglg qpgcppeida lraqvmafvr ervmpcepvl daggaaarte
       61 lrrlqaeakr eglwalplpe ewggqglglp lyshiaeaeg asdhgpaalg saplldvlml
      121 arhaddtvke rflrriadge vrtcyamtep gtpgtdpglt atravsdtag gwvlhgrkwf
      181 tsgagdadli tvlarvddeg pgtdslslfl vpasaagftv vrelpvlgag gqweieldgv
      241 avppghavga pgqalriage rlvlgrvlrc lrwlgqaera fdlmclrars rsqsagplad
      301 rqlvqqmvfd sllairstrp lvheavarla aggdarletg lakvaaarml qqvadaaiqv
      361 hgaaglgpdt alpglfrtgr tarlldgpde lhitavarrv lrgypvtsrt dpsgr
//
LOCUS       WP_457694023             613 aa            linear   BCT 27-JAN-2026
DEFINITION  peroxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694023
VERSION     WP_457694023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Zamocky,M., Janecek,S. and Koller,F.
  TITLE     Common phylogeny of catalase-peroxidases and ascorbate peroxidases
  JOURNAL   Gene 256 (1-2), 169-182 (2000)
   PUBMED   11054546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..613
                     /product="peroxidase family protein"
                     /EC_number="1.11.-.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=69422
     Region          90..611
                     /region_name="PIOX_like"
                     /note="Animal heme oxidases similar to plant
                     pathogen-inducible oxygenases; cd09818"
                     /db_xref="CDD:188650"
     Site            order(271..272,386,389..392,395,419,469,472,476)
                     /site_type="other"
                     /note="putative heme binding site [chemical binding]"
                     /db_xref="CDD:188650"
     Site            order(321,389,555..556)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:188650"
     Site            order(322,325..326,330,385,389,391,541,545,549..550,
                     553..554,557)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:188650"
ORIGIN      
        1 mstaprgsar rsdprhagda pspflalynr lmlavdhrig wqnlpkplgl ltllglrnil
       61 rrqnlfdtsg ypaqdlpdtg ppaarhrter tadgtyndld nprmgmarsr fgrnvppaat
      121 fpepepeils pspreisral ltrhtfipae svnalvaawl qfmirdwvsh gqgsmdrpwq
      181 ieladddpwp aspmpvartl pdptrpasgd glpptyvnen shwwdasqly gndpaaqqal
      241 rsgtdgklrv phngslfpde perdpahtpg fwlglammhl lflqehnaic drlrheypgw
      301 sdeqlfqrar linaaliaki htvewtpavi shpttiaalr anwfgilger vhkllgritg
      361 sevlsgivgg rtdhfgvpys lteefvavyr mhplipddws frsaadnsll qeatfrelsg
      421 pyaydilrkh alpdlfysfg tshpglvtlh nypkflqefr rpddqlmdla avdilrirel
      481 gvprynefrr rlhlkpakdf asltddpswa eelrrmyddd iervdlmvgm faeprpkgfa
      541 fsdtafrifi lmasrrlnsd rfltrdytpq vytltgldwi ennsmttvll rhfpelrssl
      601 rsvdnafapw kas
//
LOCUS       WP_457694025             419 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457694025
VERSION     WP_457694025.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45536
     Region          1..418
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mgrervrrpe ldhaalfaat psaclvldpe lvivdvnqay lhatgrtrdd llgqyvfdaf
       61 pdnpadpdae gvqnlhpsll rvlstgepdt mavqrydipv tdqpglfeer wwstintpvp
      121 gpdgrvawii hrvedvtafv hsrrtrpvpg gqlsereeam eaelyvrara lqhlneelrr
      181 aharerqvav tlqeamlhsp dlaghrdiav rylpaigsln vcgdwydivd lpedgfalsv
      241 gdvvghglea aavmgmlrsa lsaaarsveg paqalkvlgl yarsvdkala ttavqalidt
      301 agrqvtyssa ghpppvllha dgthelldra tdpplgahpe qvprpqahlp yvpgdtlvly
      361 tdglierrde didtglarlt dtlarysrls perladalla rlgvsagard dialvivrl
//
LOCUS       WP_457694032             285 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457694032
VERSION     WP_457694032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5) (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=29522
     Region          1..136
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          146..282
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 magpvvvgld gagnsvpavl wgaeeaaarg lplhllyswg tpsapvppaa seaagperha
       61 aemlrtaadl ahtghpgvpv tteqvgerpa dalversara amvvlgsrgh gaiagfllgw
      121 vslqvlgrae cpvvtvreda afprreivvg vqyagpedea lldftftaae ahharvravr
      181 awgpaatvgp vraapdrspd etgignaekq tlaetlrpwr akfpavdvvp hvergraaav
      241 llaacshagl lvvgrrlqrs pmllgpvvha alhhancpvs vvpqr
//
LOCUS       WP_457694044             428 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694044
VERSION     WP_457694044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46863
     Region          16..379
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mspwrvrnld eddldqvvri weesrdtvre pavslaevvs alrgrmpavv avvgdrvvga
       61 avssvaqera wvlrlaiarq wrrhgigsal laaleerlae agvrrigall pegevgeqaf
      121 qnsgytgrpd lsyfekllsa dsaeaalldq lggvvpeagl wdgiagmtge kalierrlvl
      181 plenpavagr yqlvppravv lfgppgtgkt tfaravasrl rwpfievfpy qlaedahgva
      241 aalrrlfarv ehldevvlff deaeeiaser qdptslahrv tnellklipq frrgerrlli
      301 catnavrsld paflrpgrfd ylipvgppda earraiwtry igpdrvagid ldalvgasgr
      361 ftpadiefaa rtaaqsafer hlaadpqqag dlgqltddyl qaiahtrttl teedirafdr
      421 dlraaarv
//
LOCUS       WP_457694046             498 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457694046
VERSION     WP_457694046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..498
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52641
     Region          60..442
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnrtsrpndr fsrtrsagsg rgghrsqpan rsggkrrrpa pqgefalpvt htpalppaes
       61 faeldmpsal laslaaegvt apfpiqaatl pnslagrdvl grgrtgsgkt lafglallar
      121 tagqraepgk plalvlvptr elaqqvtdal tpyaralslr latvvggmsi grqagalrgg
      181 aevvvatpgr lkdligrgdc rlnqvgitvl deadqmadmg fmpqvtalld qvrpegqrml
      241 fsatldrnvd llvrryltdp vvhsvdpsag avttmehhll hvrdadkhat tteiaaregr
      301 simfldtkra vdkltkhlln sgvraaalhg gksqpqrtrt ldqfktghvt vlvatnvaar
      361 gihvdnldlv vnvdpptdhk dylhrggrta ragesgsvvt lvlpsqrrem drlmadagit
      421 pqstqvrsge aeltritgaq apsgvpvtia apvverakrs gsstrgrrsr ssqarrssga
      481 prtasgtsqr rpaagkts
//
LOCUS       WP_457694056             134 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457694056
VERSION     WP_457694056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..134
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14371
     Region          9..120
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 maiaktsvlv ldcaepaala dfyaqflgge vrigtspdyi evvesdtvhl airrdrgaap
       61 pswprpddsq qahlhflvpq gnmdeaerea vslgarplqt renrgpydar ryadpaghpf
      121 vlaaseghal gqan
//
LOCUS       WP_457694058             244 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694058
VERSION     WP_457694058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25389
     Region          1..241
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtehekvili tgassgigea aarrlaadgh rvflgarrtd rletlshdin kgggtaafrr
       61 ldvtsaedmr sfvaagcaef grvdvlvnna gvmplsplea lrveewdrml dvnvrgvlhg
      121 iaaalpvmra qgaghvvnia sigayevvpt aavycatkfa vraiseglrq esaggirvsv
      181 vspgvtesel adsitdptar damtayrava lpaaavadai afavgqppev dvnelvvrpv
      241 arar
//
LOCUS       WP_457694060             289 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694060
VERSION     WP_457694060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31139
     Region          5..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..266
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtnnelgafl rahrsqvlpe dvgmpshgrr rvaglrreev avlagmnady yarleqgrer
       61 hpspqvldal srallldedg rthlyrlagv vpddrpasyg qetvgpalrq lidgyphtpa
      121 fvlnpaldil aanslaealf spfvhadnla rmvfldpaar qfhtrwnraa qatvanlrqa
      181 vgrdpdaprp aalvrsltaa saafaelwns htvrgkshea kefshpevga lsltyqafdv
      241 rsapglqlvi yhaepgspsa ealsllgtlh atgrqgsdgt vrapgtrgh
//
LOCUS       WP_457694067             102 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein GvpO [Streptomyces nigrescens].
ACCESSION   WP_457694067
VERSION     WP_457694067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Pfeifer,F.
  TITLE     Distribution, formation and regulation of gas vesicles
  JOURNAL   Nat Rev Microbiol 10 (10), 705-715 (2012)
   PUBMED   22941504
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10530706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..102
                     /product="gas vesicle protein GvpO"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=11120
     Region          8..101
                     /region_name="GvpO"
                     /note="Gas vesicle synthesis protein GvpO; pfam05800"
                     /db_xref="CDD:399068"
ORIGIN      
        1 mateentere kahdggpksi savtvmrhas gqlaqllqce pgsvsalkpt ddgwlanvev
       61 veiervpdta svmasyrvhl deqgqlvgye rtrrygrgqi dr
//
LOCUS       WP_457694069             146 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle structural protein GvpA [Streptomyces nigrescens].
ACCESSION   WP_457694069
VERSION     WP_457694069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10013202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..146
                     /product="gas vesicle structural protein GvpA"
                     /calculated_mol_wt=15533
     Region          1..145
                     /region_name="PRK09368"
                     /note="gas vesicle structural protein GvpA"
                     /db_xref="CDD:236485"
ORIGIN      
        1 mtaiqqsnat tsgsgsgnly dvlelildrg lvidafvrvs lvgieilkid vrvvvasvdt
       61 ylrfaeacnr ldlesgrkap sqltdlvgea tesgakgksk galtgaveaf sesfqkgqed
      121 saeeeerpar kssaasnrrt arrred
//
LOCUS       WP_457694071             237 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457694071
VERSION     WP_457694071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=26194
     Region          2..237
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mgtylyaita aghplrlsgi sgvgepaaql rtvrtkdlca vvsdappelr akrrdvaahq
       61 dvqdrlladg aalpmrfglv gtddaqvatv leqdresylq rleevdgcre yhlkvarded
      121 dllreimres eevrrlndrt renpgayddk valgelisqe vqarqerars divarlagaa
      181 vrtadveptk rhflsvsflv erekaaafse avhkeagqrg dtydfslhgp lppysfv
//
LOCUS       WP_457694079             141 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457694079
VERSION     WP_457694079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..141
                     /product="gas vesicle protein"
                     /GO_component="GO:0012506 - vesicle membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15044
     Region          26..64
                     /region_name="Gas_vesicle"
                     /note="Gas vesicle protein; pfam00741"
                     /db_xref="CDD:459920"
ORIGIN      
        1 msdslagrmg pssgpspygr qgssanladi lervldkgvv iagdiqinll dielltiklr
       61 llvasvdkak emgidwwehd pslssrarps qqvptgrppe tgrnalaeen qqlraelael
      121 raaigssrgs gghradheee q
//
LOCUS       WP_457694081             291 aa            linear   BCT 27-JAN-2026
DEFINITION  GvpL/GvpF family gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457694081
VERSION     WP_457694081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Xu,B.Y., Dai,Y.N., Zhou,K., Liu,Y.T., Sun,Q., Ren,Y.M., Chen,Y. and
            Zhou,C.Z.
  TITLE     Structure of the gas vesicle protein GvpF from the cyanobacterium
            Microcystis aeruginosa
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 11), 3013-3022 (2014)
   PUBMED   25372690
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Li,N. and Cannon,M.C.
  TITLE     Gas vesicle genes identified in Bacillus megaterium and functional
            expression in Escherichia coli
  JOURNAL   J Bacteriol 180 (9), 2450-2458 (1998)
   PUBMED   9573198
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="GvpL/GvpF family gas vesicle protein"
                     /GO_component="GO:0031411 - gas vesicle [Evidence IEA]"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=31142
     Region          30..283
                     /region_name="GvpL_GvpF"
                     /note="Gas vesicle synthesis protein GvpL/GvpF; pfam06386"
                     /db_xref="CDD:461891"
ORIGIN      
        1 mnshlqaeap rqplrrpteq restplwsay vyaigragag ldtaaaqltg lrdgrlrtvt
       61 agrltalvss vpadafsaeg mkaqlenlte leeiarthht vveaahtgtt vlpmrlatvy
      121 ldddrvrsml qergaefdal lsrleghael gvkvyadpra aaaepppapd gpdaaaspvs
      181 pgraylqqrr aqrrtqrday raagaladdv rgrvaplard rvahrpqqge lasgegenia
      241 neaylvptdr irefhralag ladgvpgvrv evtgpwapys fatppaesrs a
//
LOCUS       WP_457694085             135 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein K [Streptomyces nigrescens].
ACCESSION   WP_457694085
VERSION     WP_457694085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Pfeifer,F.
  TITLE     Distribution, formation and regulation of gas vesicles
  JOURNAL   Nat Rev Microbiol 10 (10), 705-715 (2012)
   PUBMED   22941504
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523950
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..135
                     /product="gas vesicle protein K"
                     /GO_process="GO:0031412 - gas vesicle organization
                     [Evidence IEA]"
                     /calculated_mol_wt=14869
     Region          45..125
                     /region_name="GvpK"
                     /note="Gas vesicle protein K; pfam05121"
                     /db_xref="CDD:428319"
ORIGIN      
        1 mtnetaapve pafaevaqaa arafdlvpar adeppqgqgs alaqrlrtdp etverdlikl
       61 vltivellrq lmertalhrv dqenlseeqe erigltlmil qdrmaelcer ygltmedlnl
      121 dlgplgsllp rhdag
//
LOCUS       WP_457694090             591 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694090
VERSION     WP_457694090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 591)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 591)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 591)
  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 591)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..591
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60570
     Region          32..581
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mprtpgpssp psppaaprgp dtgvrsvltg afrhspvrav avclfsvasa gaavalpavl
       61 ghtldlvlga rpglhgalvl cavlliaevl ldalvaltgg vttarstawl rrrgidhlls
      121 laphrvadrf tpgdlvtrlt gnaadagtap taaatglaal itpvgalial altdiwlaav
      181 flaglplltr llrafahgss esvrryqrvq adiatrlvea lggartiaaa gtagrerarv
      241 laplpelgaq grqmwqiygr avvsssilvp llttavlavg girlaygsls vgellaasry
      301 aaltaglggv vgqlnalvrs raaahrtgel lalptpahgv tplpadgrgr lelravtvvr
      361 ggapalrgvd lvvpggttma vvghsgagks llaavagrlt dpdsgqvlld gvplheadpa
      421 qlrreigyaf erpalfgatv gaaigfgphe ppahaieaas raagadsfvr llpdgyatpl
      481 araplsggev qrlglarafa hagrllvldd atssldsvte lhvrralvhd vrtgsrllia
      541 hrvssaarad lvawmengrl ravaphdrlw adpdyravfa htddedtrta s
//
LOCUS       WP_457694094             369 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694094
VERSION     WP_457694094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  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 369)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..369
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=39413
     Region          6..353
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mggdlltlfl cgdvmlgrgv dqilpypgdp vlregyvrda rayvelaaar ngpipcpsgf
       61 swpwgdalea ldeaapaarv lnletsitqy agfapekeih yrmnpanlpc laaahpdvcv
      121 lannhvldfg rqglaetlgt lagaglrtag agadpdaarr pamvpvadgr rilvfsfgmp
      181 ssgiprdwaa aggrsgvdfv arpspaaage iigrvrqvkr pgdlavasvh wganwgyhvt
      241 hneaafahal leggvdvvhg hsshhprale ayrgklvihg cgdfiddyeg itgyeayrdd
      301 lrllflvtvd pdtgglhevr ivplqarrmr lrhaspqdsr wlqglldris sgfrpcaaep
      361 egtlilrps
//
LOCUS       WP_457694095             341 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457694095
VERSION     WP_457694095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..341
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34387
     Region          19..304
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mrrstqglll peaarggppa rsgrltgvam mcgsglanqt gaatgalafp aigpagvvav
       61 rqwvaglvll avgrprlrsf twrqwwpvlc lamvfatmnl slytaidrig lglavtlefl
      121 gplavalaas rrlvdllcal vagaavvvlt rpqpttdyag ialglvaavc wasyillnrl
      181 vgarlpgaeg saaaagvsal lylpigitvl ahhppsasal gyaatagils savpfladll
      241 alrrvparff gifmsvnpvl aalvglvvld qtlqgiewla vsaivvansv silaagprpa
      301 ppsavrgsta lpdpvalpap aadsttphgs sagaparcea c
//
LOCUS       WP_457694097             283 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694097
VERSION     WP_457694097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31277
     Region          1..273
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrhlrclv aivdaggftd aaielgisqa avsrtlgsle dslgvrllhr tsrsviptta
       61 gvqvlarark vlaeadnlir eattghtrlr ighawsamgr htaeyqrrwa arypdielhl
      121 vrtnsatggl aeglcdlavv rttfddarfa savvgherry camaaddpwa krraipladi
      181 hartllidrr tgtttadlwp pdtrpvieyt qdiddwlavi atgrsvgitp estvnqyrrd
      241 givfrrirda apvavhliwr rhdphpatha avalltdlyr qrt
//
LOCUS       WP_457694083              82 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457694083
VERSION     WP_457694083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..82
                     /product="gas vesicle protein"
                     /GO_component="GO:0012506 - vesicle membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=8405
     Region          34..71
                     /region_name="Gas_vesicle"
                     /note="Gas vesicle protein; pfam00741"
                     /db_xref="CDD:459920"
ORIGIN      
        1 megdaheaag aevsylgdlg drsaeeslag rqialidlld rllnggavlt gdvvlsiadv
       61 dlvhinlrav irsitsdgpa pw
//
LOCUS       WP_457694098             271 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457694098
VERSION     WP_457694098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11999121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..271
                     /product="potassium channel family protein"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29247
     Region          40..205
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          <150..204
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 merqsaqtrw eqatqrplla lavafavaya lpivdgsagh vltavctvae wvvwgsfavd
       61 ylirlalapr rkefvrthwt dlcavvlpll qplrllrlva tlmlvgrrar masqirltty
      121 vvgavvgllm fgslavlsve rdspngnirt lgdalwwsft tmttvgygdh apttglgrmi
      181 avglmlsgia llgvvtania twfiarfekd dveerrqtea igvlteevra lraevaalse
      241 rvgardggrs papagcrcah pcrpscttah s
//
LOCUS       WP_457694108             272 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694108
VERSION     WP_457694108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28242
     Region          21..267
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msesvapgag rtpgggssge raagaldrgl ailthvagnr gvstpeiaqa lgltrstayr
       61 lvdrleeqgw lthapaagqw qlgptavrla saavastnlr dtaapalrkl aeltqetvsl
      121 gvpngltmvf vhrergtrpa vvtaelgasr plhssslgra ylaalpqqkl edtlielvrd
      181 pmspvsaatv sdvhaevert rergwsqdlr dfdesscccg aavydhtgmp vacisvagva
      241 ermeplvpay gpvvaqvcre lssslgylap gs
//
LOCUS       WP_457694110             291 aa            linear   BCT 27-JAN-2026
DEFINITION  fumarylacetoacetate hydrolase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694110
VERSION     WP_457694110.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31343
     Region          60..271
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mylatvthqg rdrlagrlap qdpwrlapps fslaevisgg alpwswgqlp tgadlvpvlp
       61 frpgalygvg mnyrdaieer ggerpaeprl fpklsssvig sgeavvidpe ltqrvdwete
      121 lavvigtear qvseadalry vfgytvandi sardlqerdg qwlrgkgldt fcpfgpvlvt
      181 adevpdpqrl rirtrvnget vqdgstadmv fgvpaliayl srfftlrpgd vvltgtpagc
      241 gdfmrpprgl rpgdllesev egigrlanpv rsskrdgage rvavpqepga k
//
LOCUS       WP_457694114             300 aa            linear   BCT 27-JAN-2026
DEFINITION  PhzF family phenazine biosynthesis protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694114
VERSION     WP_457694114.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..300
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=31015
     Region          6..298
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 maagtpftlv dvftdqpleg nplalvpdad plpegllpri arefhqaett fllrpdrsga
       61 twrlrsftaa gvevfgaghn algawwwlaa agrlgpglgt grwsqqlgte vlpveitade
      121 hglievtmeq raaaygdelt draalaealg vddrelgaaa glpvaqvvst gaahlmvglr
      181 drgvvdaarp daarlrallp dvggqgvyly aldpaepgad vharfvnpva gitedpatgs
      241 aagplacllg rhgragdevt lvqghalgrp shlrvtvidg iprltgraal aatgelhlpg
//
LOCUS       WP_457694117             110 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694117
VERSION     WP_457694117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..110
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=11655
     Region          2..103
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mpheqiraqr saliatgqlt egerlptvrq lapdlglapg tvarayrele aaklirtrrg
       61 agsrvaalps epkhpdpaql arlawdftsa aralgadtea iltavreald
//
LOCUS       WP_457694121             119 aa            linear   BCT 27-JAN-2026
DEFINITION  gas vesicle protein [Streptomyces nigrescens].
ACCESSION   WP_457694121
VERSION     WP_457694121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Walsby,A.E. and Hayes,P.K.
  TITLE     Gas vesicle proteins
  JOURNAL   Biochem J 264 (2), 313-322 (1989)
   PUBMED   2513809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10465145
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..119
                     /product="gas vesicle protein"
                     /GO_component="GO:0012506 - vesicle membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12890
     Region          20..58
                     /region_name="Gas_vesicle"
                     /note="Gas vesicle protein; pfam00741"
                     /db_xref="CDD:459920"
ORIGIN      
        1 mtdvdyrqaa ppangpstan ladilerild kgiviagdik idlldiellt irlrlfvasv
       61 etarkagidw wetdpalssk aarselreen drlrerleal esgddgdasa srtkdeaas
//
LOCUS       WP_457694126             360 aa            linear   BCT 27-JAN-2026
DEFINITION  type III polyketide synthase [Streptomyces nigrescens].
ACCESSION   WP_457694126
VERSION     WP_457694126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..360
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38940
     Region          7..353
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mqgahpmavl ckpaiavpey vitqddtlel arrlhkdhsq lrlvlrlieh tgvrkrhliq
       61 pidkvlkhpg ldarsavyeq eskarvpavv rqaldqaele pqqidlivyv sctgfmmpsl
      121 tawlintlgf rsetrqmpia qlgcaaggaa inrahdfcta ypdanvliva cefcslcyqp
      181 tdlgvgslls nglfgdavaa avvrgnggtg vrlernssyl ipntedwisy avratgfhfq
      241 ldkrvpgtme plapalraia eqhqwdagel dfyivhaggp rilddlchfl evppeafrfs
      301 ratlteygni asgvvldala rmfdeasavd gqrgllagfg pgitaemalg twastpdiaa
//
LOCUS       WP_457694140             232 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694140
VERSION     WP_457694140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25243
     Region          13..>111
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvvlaeqdsg kaarilaaar elvlkrgvkg vtvaevaeka hvakgtvyly wdtkedllvg
       61 lfardflsav dnhidalthd pdlvrphqlf prlvlnalel pfiralqigd adllgvltnh
      121 prtkelldgl giarvmslvl pvwrryhlar tdwpldeqvy vlqalldgfv aavapthplr
      181 satvdepdkv iaaavttllg peqasqadir avadealqll raqresllas lv
//
LOCUS       WP_457694145             219 aa            linear   BCT 27-JAN-2026
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694145
VERSION     WP_457694145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  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..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /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=23909
     Region          13..216
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 midkllpapv rtaeafqdap vsemfpeewa qvanavpkrq refgtvrgca rralaelgfa
       61 papllpgpnr epqwpagvvg amthcagyra vavarssevr tigldaepnl plndpgvvdl
      121 vtlpeeraql rrlaalqpev cwdrlvfsak esvykawypl trrwldfeea rltldptnat
      181 ftaqllvpgp vvdgreltef ggrwlvgsgl vvtaivemv
//
LOCUS       WP_457694147             312 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694147
VERSION     WP_457694147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /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=34174
     Region          28..272
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtyeirtltp gaagpaaags ahgggrgrlv avsdlhvryk enrdiveglr pesdddwllv
       61 agdvgefvsd irwalsllss rfskvvwvpg nhelwtpaqd pvqlrgvary ehlvdicrel
      121 gvltpedpyp vwegaggpvv iaplfllydy tfrqpgttsk kdalaraeka gvvctdehfl
      181 hpdpyptrea wcqarvaate arlaavpeel ptvlvnhwpv vreptrplwy pdfalwcgte
      241 atadwprrfr aaavvyghlh iprllmldgv phqevslgyp rewqrraaap grpvqilptp
      301 aavgsgttgg pa
//
LOCUS       WP_457694149             537 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694149
VERSION     WP_457694149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..537
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56197
     Region          7..128
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          269..518
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mplhisdlla rpdldlsvty evpprllart ieaatvsdlp apgkwlqgge llmtiglllp
       61 kepaacrayv rdvaeggaac lalglgqglp yqeapeplvt aaeeaglpll tvpdevpfia
      121 vtkavfdara eeqrallqra fatqrrltaa atgdglrpml aewtaatgvg aavfdplgrl
      181 laagerahrt ppaqahdlie rvaarglrgs asstaagqql evqplgarrl rglllltgrp
      241 ddaarsvvpg lvsllslele rrhlrdeper rrrsallsel ladedptaer ardilrsagl
      301 taervrgvvv aagggadgrt asaapdagtg aadgaaqema adlalampgg lvrvvdgapg
      361 avieavvged ldirdvlarf aprrpagigp atapeavrvs lrqatgllav srssgepaea
      421 rqsqasrlll dlgdrrtlhg yadtvlgpld ladngeelta tlaawletgg awdatsrrlg
      481 vhrhtvrnrl dkamdltgrr lddpddrfdl wlatrirrgg asatgadgrp aapppgr
//
LOCUS       WP_457694160             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694160
VERSION     WP_457694160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32311
     Region          1..285
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          <167..>241
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
ORIGIN      
        1 mslrqmeylv avveqesftr aaealhvtqs alshqikale rtvggpller mtrgvrltam
       61 grayfphaql avrsarqarr aalaaggaes gelhiatvha qavgvlpevc arwararpgv
      121 rlvlheyatt eeldeqmarg vadlalgprp kdwpgpvtvv gqermvlvvp hgdplaares
      181 vrlaeladrl wvrcslepvv egrrwldrec ervgftprta vrtqhsstav rmasagvgvl
      241 ltaahelrgl dcaavptdpp whreitvfsr veptgaaaef tellrtvgst easpdart
//
LOCUS       WP_457694164             437 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457694164
VERSION     WP_457694164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 999995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43093
     Region          23..413
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(26..27,30..31,34,66,121..122,124..126,129,153,
                     156..157,160,251,254..255,258..260,263,285,289,342..343,
                     347,351,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
ORIGIN      
        1 mtaataafrr vlalggpmlp vlsflgrlpt amcqfgslll vaetsgslat aglvggalaa
       61 gqtaggpllg rladrhgqrp vvlaacwfda lavtalvsaa lartgalpla liallagagv
      121 pqigplartr lvalarrara ddrlvhtals fegtldevsf vlgpalvgls atvahpaval
      181 alaalllavc gsafalhpta aavrptgaps gpvpvpsgaa pvpdgrsgrr saarpararm
      241 pravhamras malqgalfga cqagitalta dlhrpaqagl vyaamgvmsa vaglslalvp
      301 ariglparwr aaavalivls vpllfvrslg alylavvvlg aafaphlitl fglterlvpa
      361 grlaesmafl tsaivggqal slavsgrlae aqgpsaafav avgaavlilg lalatrgtdr
      421 psaaltpaaa apagsar
//
LOCUS       WP_457694171            1120 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694171
VERSION     WP_457694171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1120)
  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 1120)
  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   3  (residues 1 to 1120)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1120)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1120
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=118529
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          137..1088
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrfrvlapld vrsaegrpap vpetkvrall aallahhgrp vssdrlvahl wgprpparpt
       61 aslqskvsql rraldtaepg arklvtatpp gyrldvaada ldagrftalt argraaagpr
      121 qraellgaal elwhgpafag fadsdlirpv aesleeqrlt aleeraaarl elgehaplta
      181 elaglaarhp lrerlralql talyragrqs dalaaydeir arladelgvd pgpeltavhr
      241 ailrqepwrp pddgtrhdgg atrpegrata apgtappagp rprtnlptpl tallgrqdav
      301 rrveallaat rlvtltgpgg vgktrlalet agrlagsfpd gvwlvelaal srpdapgrda
      361 gskctaavva eavlavlgir egasagpvae rlvgavrgkr lllvldnceh lveaaaevta
      421 ellgaapdlr vlvtgqeslg ltgetlwpvp plepdgavel ftarasaadp dfvldadata
      481 avaeicrrld giplalelaa trvralgvre lsarlddrfr llasgrrgap prqqtlrami
      541 dwswellpaa ertvlrrlav hadgctleaa etvcagdgvr rdevldllar lvdrslvtva
      601 rtpygpryrl letvaaycle rlreagelta vrrnhhrhyt elaehaapll ygpdqhkwle
      661 rldqeaanlr dtldgavreg aadralrlvn alawywflrg rlaeagrslt aalaayeagr
      721 ataaegrdpa aegrrlraaa wqvgmaslag ddadpverat avlrqygthd dpggrawaqw
      781 flgfaqvglg dpavarerva dslaafrtlg dgwgiaaals sraqgsvggd lrarlrdaee
      841 saalfrelgd rwgqlqaada lgalaeitgd ydraarlhrd glriaeelgl wiqasyklsg
      901 lgrialltgd laaardfher gmrlaaeqsh lrgemfaecg lalgarregr lddaeahllp
      961 wlewclgrdg dpgtafvlge lgfvaelrgd aetarrhhld gfeaaratad pravalaleg
     1021 lagavaltgr cavaarllgc aaaaraaaga pqpaaergdv arsaatarrs lgdaafeaay
     1081 asgageapev lvkeatgsag getygvpvip pstrssiplt
//
LOCUS       WP_457694172             263 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457694172
VERSION     WP_457694172.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..263
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26893
     Region          4..260
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlrlaghga lvtgsssgig atiaetlade gcdvlvhgrn agaaaavaeq vaargvraev
       61 vlgdltepgv aeqvaltard fgaqilvnna gpfaehdwes srpsdwrtaf egnvlptvrv
      121 sqtllpslra hgwgrvitig sravrtplph mvaysaakaa vvnmttslar hlagtgvtan
      181 cvspgviatp smyrmfeera aaedgprggp deadlvaeya pnpsgrlgrp adiaaavayl
      241 aspladyvng ielrvdggit gtp
//
LOCUS       WP_457694176             296 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694176
VERSION     WP_457694176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /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=31815
     Region          37..245
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtepspaaft earardvlaa aghpeaaada allslgenav falgdngpvv rvgrsaelle
       61 raerelgvaq wlaaegvpav raaepvatla dghpvtywqr lpeavrpagp ddlatllklv
      121 halpeppfal prrellggve rwlrlagdav sapdaeylrg rrdafaaaat alephlprgp
      181 vhgdalarnv hvgpdgpvlv dletfssdlr ehdlvvmals rdryglspda ydtfvsvygw
      241 dvrdwegcav lrgsretasc awvsqhapgn paalrefrrr iaslrdkdat vrwypf
//
LOCUS       WP_457694178             313 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694178
VERSION     WP_457694178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33956
     Region          27..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtlattprrs tepaadraar prrdlgawfl vlpallpilv lsvgpllygi glaftdaqsg
       61 rtqatrfvgl lnfsdlfqds lfwdsfrigl iwafgvtvpq fllalglall lhldlrlrwl
      121 aralaiipwa mpevvvgimw rlvyhpdagi lnetlrglgl sgagdgrdwl sglatalpav
      181 ivvgvwagmp qttvtllagl qnvprelhea asmdgagawr rfrtvtwpal rpialavtal
      241 nfiwnfnsfa lvfvltdggp ggrtrlpmlf ayeeafrygq fgyaatmgla mvavisvlla
      301 vylagrlkgd ddr
//
LOCUS       WP_457694180             316 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694180
VERSION     WP_457694180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 316)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33918
     Region          51..315
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtamestggs krrnaprgar sapiprrtpr rpttprrpat prrtaaragq yaallgylaf
       61 lafpflwlls tafkpprelg smhptwipea ptlenfrqaf aqqplpaaag nsllaaavsa
      121 llaillatpm ayvlarfrnr lsraatgwvv isqafplvlv iiplflilkg lhlvdsrigl
      181 imvyvvwslp falwmltgyv ravpreleea aavdgagrfr tlvsvtapll apgivatalf
      241 afitawneff falvllkspe kqtlpvvlth flgtegvadl gplaaaalla tlpslllfaa
      301 iqrritggml agavkn
//
LOCUS       WP_457694186             194 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694186
VERSION     WP_457694186.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21076
     Region          9..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdqeaglra rlvqvgidll teegvqalsl reiarragvs hgaprrhfpt hlsllsaiar
       61 qgfadlaqkv aaevddhgad prdrlmalgr gyldfalthr gmfelmfrhd llesnhlglr
      121 etslplfqvl vglvarvqpq sdvparvvag alwsnlhgia qlwrwgslql atgaddvepl
      181 lraaldahlg pegr
//
LOCUS       WP_457694188             510 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457694188
VERSION     WP_457694188.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..510
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51157
     Region          17..457
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtarrrqrlv ltgsitgavi valdgtvltv aqpalqrdlh asfgqvqwts tgyliavasl
       61 lvfagrlgdr yghqrifalg ilgfgatsag iglapgvgwv iglrvaqgif gallqpatlg
      121 mlratypsdr lgmplalrts aiglaaaagp vlggalvahw gwraafflnv vpagligvla
      181 lavrvptpgp ratagattgg tttaggtrtp arldlpgagl lalalvclvh tlvalpetgw
      241 tmattlggaa aaiacgafir hehrtasplv plsvvrsttv aaalavllsa saalfgalfv
      301 styflqdvla ldpmqsglrv lplavlmvls apasavlqrr ygprrttmaa mtlltvgila
      361 lsqldrtssv paisggflll gagfgtvmvt atavivrhvs adhagvaggl qqtamnigpa
      421 lgvatatmlv tltaptatgd rpsggphwtg eaflsamgpa lltlaavaat galaavklpr
      481 rtadgdspqp patagrdrdp aeatavtsgd
//
LOCUS       WP_457694190             363 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457694190
VERSION     WP_457694190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  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 363)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 363)
  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 363)
  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 10157591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..363
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39888
     Region          6..178
                     /region_name="CESA_like"
                     /note="CESA_like is the cellulose synthase superfamily;
                     cd06423"
                     /db_xref="CDD:133045"
     Site            86..88
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133045"
ORIGIN      
        1 mrtitvivpa hneeeglpat leslasqtvr pdrvlvvdda stdhtgevaa shgvtvlrpp
       61 hnlgskakaq nyalpqcttd lvlavdadtv lapdyietvl pvfddpgvsv aagtvrtrht
      121 rtlwergrst eylfgfhwhr piqaranspm vcsgccsvfr rddlmafggf pertivedmd
      181 ytwsqqiagr ravyvsdava laadpedlty lrkqvwrwma gfcqnvrlhl grlilhkpll
      241 avwvllalle iltaplwwat plllaattdq ppalafawwa gaelllttpp llyaarrrkl
      301 plstvllnip cvyatkavnl vyawkalive lllvplhlar gltvyekgra dsrptraala
      361 gag
//
LOCUS       WP_457694196             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694196
VERSION     WP_457694196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22674
     Region          2..204
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkivdpvar rravaqavls vaarqgleha slrnvaeeag laigsvrhyf adhdelmtft
       61 mrelsrrigd rirphaerll tpddrtdrra ateellaell pldearrqea alwlaftaaa
      121 hthpelrpca aemqadlhtl msrvlheaqs agglpdgmdv dlestrlaal ldgltlqatl
      181 lpdryppkll rqvlrrhldt lrags
//
LOCUS       WP_457694205             111 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457694205
VERSION     WP_457694205.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Chen,X., Hu,Y., Yang,B., Gong,X., Zhang,N., Niu,L., Wu,Y. and Ge,H.
  TITLE     Structure of lpg0406, a carboxymuconolactone decarboxylase family
            protein possibly involved in antioxidative response from Legionella
            pneumophila
  JOURNAL   Protein Sci 24 (12), 2070-2075 (2015)
   PUBMED   26402328
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Ito,K., Arai,R., Fusatomi,E., Kamo-Uchikubo,T., Kawaguchi,S.,
            Akasaka,R., Terada,T., Kuramitsu,S., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the conserved protein TTHA0727 from Thermus
            thermophilus HB8 at 1.9 A resolution: A CMD family member distinct
            from carboxymuconolactone decarboxylase (CMD) and AhpD
  JOURNAL   Protein Sci 15 (5), 1187-1192 (2006)
   PUBMED   16597838
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..111
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11955
     Region          1..101
                     /region_name="YurZ"
                     /note="Uncharacterized conserved protein YurZ,
                     alkylhydroperoxidase/carboxymuconolactone decarboxylase
                     family [General function prediction only]; COG0599"
                     /db_xref="CDD:440364"
ORIGIN      
        1 mtdeknehrp agprqqfgdi apalagysed vlfgqvwenp dlaardrslv tvaslitsgs
       61 teqlafhlrr ardngvseke lietithlaf yagwpkamsa ltaardafaa a
//
LOCUS       WP_457694208             383 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694208
VERSION     WP_457694208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41874
     Region          7..112
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          74..>203
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mdqstailpf hldipqadld elrhrltrtr wpdelpaagw dygvalpylk dlvaywaday
       61 dwrahearln alpqftttid gqhvhflhvr spepeatpli vthgwpstvh dflgiigplt
      121 dprahgadpa dafhvvapsv pgfaysgptr dkgwgtnria hawaelmrrl gydrygaqgg
      181 dfgalvspel grvapgnvlg vhvnalvnaa tpvspdeldh lseaereraq enelwwyghs
      241 gyatqmatrp qtvayalnds pagqlawnle wfvdhdptqt rqtpvdrdav ltnvsalwlt
      301 stagsaarly leagadgwgv rpapsgvptg vanflgdhal rglaslshhl thwseyatgg
      361 hfaalqapdt lvadirtffr tlr
//
LOCUS       WP_457694214             286 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694214
VERSION     WP_457694214.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29881
     Region          27..>173
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 madhdltgfd rgtfthdgtt rrilrrgtgp avivlaeipg itpkvlgfae rvaalgctav
       61 lpvlfgtpgr dadpahigrl kaglymassi gkvcvsreft vlatgksspv vtwlralaah
      121 ehqrcggpgv gavgmcltgg falamaader llapvlsqps lplaltksra gnidisaedl
      181 atvrgrcere glrvvglrfr gdrlvpgdrf aflrrelgea ftavelddsa anpdavpsph
      241 svltehlida pnqptraald evldlfrtrl laqgriadts aaggga
//
LOCUS       WP_457694210             315 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694210
VERSION     WP_457694210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34053
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvailale dvaafdltip cqvfamahgp dgspayelrv cagrtvtata gkqpsfrits
       61 pyglddarda dtvivpgvrp drapspravr lirevaargg rvasictgaf vlataglldg
      121 hratthwmfa dqlaqrfpdv evdpsvlfvd ngqiltsagv aagldlclhm vrrdlgaaaa
      181 artarmivma pqrtggqaqf idhraplsnt ehlgptlewm qenldkpltv adiarraams
      241 srslsrrfra qtgttplqwl lnrrlqrare llettdltme rvaraagfgs tetlrhhfsr
      301 hvgttptayr atfqg
//
LOCUS       WP_457694216             289 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694216
VERSION     WP_457694216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31220
     Region          6..268
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mlqrdievkl lrtlvavvde kgfaraaqtl hvtqptvsqq iqrlesiiqa plfqrakrpl
       61 rltpagrevv aharrvilln nevlsklsal hsqksfsmgc svhfadglrn mlsqlaverp
      121 hlrcamatgl savladklaq geleaalllg tetprcemlg rlrlawfgev plvpgdrfpv
      181 alvsersals mrivdtlaer nvpwrsvpwc sdplsvrasv qaglaytalp adthhnhpsl
      241 rpaspgvlgp apeplpvyla fsssapepvv daaravarat lkdlplspp
//
LOCUS       WP_457694221             202 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457694221
VERSION     WP_457694221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22694
     Region          21..155
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mataspsagp rtgqpglrld gvdhlafvtw rprathafyt qalgmplvha itatgwvted
       61 ypdfvhfffd mgrgnriaff yyfglpeeep psdlmhrsrh vafhvdteee llawrdrlka
      121 hgvrvtrplg heliesiyfd dpngiqleit rplremsaid ardaeltlha ltdvaesphp
      181 saqalwqrka elirkdaevs gp
//
LOCUS       WP_457694223             473 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457694223
VERSION     WP_457694223.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47658
     Region          29..460
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,155,
                     158..159,162,287,290..291,294..296,299,327,331,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 matqaepqra svadtarsgk psrtlligls lgyfmvlldm tivsvalpai srdlhvglsg
       61 lqwvtngyti tfaallltag wlsdryggrr vflwglvafg vlsgvsaaat tldalvvlrl
      121 algvagalll paslavitna ytdpaerara vgswaaitga alaagplvgg vltdtvgwrt
      181 iflinvplal vslvitvrla petarkqrsg ldltgqlsgv lalaalvyal iegpdkgwta
      241 agvpaafavt vvaavvfvva elragdaaml plrmfrsrgf saalasglla nfglsgllfv
      301 lslffqesrg yssfsaglaf lpltlptafn piftgrlvgr igprrpatig fvlmgvgall
      361 qapftgnsag alvatvvgll afgfgvsfal palvagmags vpaelagiga galnsarqvg
      421 aslgvavlgv vlnlassnag gtrwalvvgg lalligalia gtglrghtps par
//
LOCUS       WP_457694225             306 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694225
VERSION     WP_457694225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32903
     Region          17..306
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mtsaqpmghq lggglvelrh lrtfetvart lsvtqaarel hyaqssvsdq iqalerelgv
       61 elldrsqrri rltpqgsvls eytnrilkll eearwavsrp gselavgale tvglhllpdv
      121 lahyrslypq arvrvgqdnr gelykavrrg dldlcltfgd ppadaglcfe tlaeeplvvi
      181 vppghhlaar gragleelar esflatergc gfremydgsf gaapskepia evsgigtlga
      241 cvaagmgcal lplisvrgqa argevavvev gdtdlrttvt mtwldrnsan pnltgfqtvl
      301 rnqlgs
//
LOCUS       WP_457694226             599 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694226
VERSION     WP_457694226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..599
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=62731
     Region          15..530
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mharhpestt tfltfteale raaarrtgpa vwdglrwrsw rdcllqaert agalhlqglr
       61 agevlaaqlp ncwelvvlha atarlgalll plhsaygahe vqslvaqaga aalvardtyr
      121 grdrvgeila lrercgslrr vwvsdggsag tgaarperag lpssaellag apdpvtdlpe
      181 rpqdpraplv llassgttsr rpklcvhshg gllgnaaava adgglgpadt ivsasplsha
      241 fgllsvhlal vvgggvglfd gwdpqrflda lhaasataaf avpaqlrdlt tllegepagr
      301 apvglrevrt ggapvprela egvrrtlgar iivqwgmtei gagtftrpgd ppeaaftigr
      361 pvsggevrvr grdggpagpg etgelqyrsp ymfsgylrap eltraaltad gwlrsgdlaa
      421 lhpdgsvsyr gradelinrg glkfsaleve ellndlpqla qhavvgrpdp rlgqrsclla
      481 alragtgltl aevtghlsrk glatyklpeq lvivdqlptt vtgkiararl vtiplppapr
      541 ssdaqppvpq ssdpqsrdpq ppdppssdap qplsqrpvaq prqpvplaps apepqaveq
//
LOCUS       WP_457694230             232 aa            linear   BCT 27-JAN-2026
DEFINITION  O-methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694230
VERSION     WP_457694230.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25141
     Region          55..226
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mlrndtlgpr nltltpelht yllaqgrmtp dpvlaelieh trtavpdqah mtvapeegal
       61 ltflvrllga rrivevgtft gysalclarg lpadgslitc dvsaewtala rdfwarggva
      121 drielrlgpa ldtlralppe phldlafida dkpgyidywe elvprlrpga llladntlfs
      181 gqvidadpge kpaairafna haredervql vmlpvadglt marklpsges pi
//
LOCUS       WP_457694232             110 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457694232
VERSION     WP_457694232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..110
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12267
     Region          13..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 msetvirtdd gtiaminvfe vepehqkela evlsegaekf irhrpgcvsv nifpstdgkr
       61 lvyyaqwrsk adikatmadp nvqvyrdkaa elakpdphay tvfavhhpes
//
LOCUS       WP_457694234             419 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457694234
VERSION     WP_457694234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45763
     Region          42..394
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mldksyvvpw gkrgsmstda eaavlaelvh estpppagar rerfersfae avgsrhaisv
       61 nsgavalhma irmldlapgd eviatpqthr ttvqplldhd vrvrfcdidp ttlnldpval
      121 ealitprtra lllvhyggcp vemdtvmala rrhgflvled cvhalgaryr grspgsladi
      181 aafslrnakt stvlgeggli tcdrddwaer lhllrahdme trtahprpar ltepavlpga
      241 tyttplqrgc vrrpgsdatm peavaalgqa qlagvetaaa krralagrld evlmrypflt
      301 pqsapahsth ayhlytcfag hqelrdrlvl aldrrgveiq lryfpqhllp qwrhrghlrg
      361 ecpvaerswf eqhlnlpcha lltptqqdyl vealdgslae lnggapvpaa msatvcgqr
//
LOCUS       WP_457694237             348 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694237
VERSION     WP_457694237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  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   2  (residues 1 to 348)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36803
     Region          8..340
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mssaqseatm advahragvs vstvsrtlrg lstvsdttra rveaaarels faitrsassl
       61 vtgrtgrvav llphleswfl saalagmapa lreagldllv ysvadvrera dffdrlparr
      121 nadallvvsf altpaerarl ddlgmplvfv sqhapgrpsv yvddadaalr gtrhlinlgh
      181 rriaflqtvd atgfhwsskn rlaghlrald eaglehddal tmsvpgwkgs gmgaavgrll
      241 slqdpptalf tetddmafrl laalreanvp vpgrvsvmgf ddhvmagvlg lttlaqpaae
      301 igrtavrlar sviddsdgah qrhivlptdl vprgstappp aarqglsp
//
LOCUS       WP_457694241             327 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694241
VERSION     WP_457694241.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34877
     Region          40..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtssatvsrs papqpagprt gpaprgggpa rmsrrrrart gwffaspalt viaavtvfpv
       61 lfslllsfad vrleyggfrl lsltgdhyaa vlsspewrya lvftfgftav tvllelvlgt
      121 vaalvlerlg aargwvlavl llpwalinvv aaqlwgylfn gtyggltwlf eqilgrqpdi
      181 lgqpasamga mvvvdvwktt pfvaivvlag lmlipgdvye aaeidgagaw ttfwkvtlpq
      241 lrpimaiavl frilqafgif dlpfvltqgg pgtateslam lgyktlfqnl digrgaavat
      301 ttaviviscc llflrvfktq adeggrv
//
LOCUS       WP_457694243             282 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694243
VERSION     WP_457694243.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 282)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29660
     Region          1..282
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mnrrapasgi rrylnavnlg glaivvlstl plywmiassf kgpgeisaap pspvpeaatf
       61 gnyaeafvrn gigryllnsv lvatlstaav lglsffagya lartplrgrg gimtallmls
      121 vfppialvvp lfllerqlgl lnsyaglivp yvalnlpfai wimrnylvgi preleeaatv
      181 dgagplrtal tviaplarpg lftagiftft atwaefllal tfnsedghrt vpvgialfts
      241 qytvpygtlf agavaatvpi gvlvmifrrs ivsgmtsgav kg
//
LOCUS       WP_457694245             555 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces nigrescens].
ACCESSION   WP_457694245
VERSION     WP_457694245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 555)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61581
     Region          14..493
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(70,73,110,113,158,176,180,212,276,336..337)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(212,276,337)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          474..551
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 mtaqhldpar dttdwwrqav vyqvyprsfa dsdgdgigdl pgvtsrlpyl aslgvdavwl
       61 spfypselad ggydvadyrd vdprlgtldd fdamvaeahr lglkvmvdiv pnhsshqhvw
      121 fqealsaapg saareryvfr egkgehgelp ptdwiscfgg pawsrlpdgw wylhlfapeq
      181 pdfnwdnpev radfrhtlrf wsdrgvdgfr vdvahglakd latplrdigt ignyrpedlp
      241 edgshpfwdr devhdifrew rkvfneydpp rvavaeawvr nsrrtayatp qelgqafnfd
      301 flkasldaae lrdsidtala daraagatat wvlsnhdvir hasryglpdg rdeeawllsd
      361 gqepalegef glrralaatl lmlalpgsay vyqgeelglp evadlsrdsl qdpvwtrsgg
      421 alkgrdgcrv plpwrregss ygfgsggswl pqppgwgals veaqqgvasa plelyrtala
      481 trrrlvadea lewaddmsat drgtlhfrrs ggwecvanls deprplpage lllssapvtg
      541 dqlppwttvw lhttr
//
LOCUS       WP_457694247             256 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces nigrescens].
ACCESSION   WP_457694247
VERSION     WP_457694247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27099
     Region          3..240
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mdtrptllvi ahgsrdprha atvsalcarv ralrlglrve vgyldfnapr vpqvlerlsa
       61 egtrdvvalp llltrafhak sdipavlrea avrlplltir qadvlgpssl ltaalerrle
      121 eaglrpgdrr stgvvlasag ssdpeasavi aeiarewwrt agwcavrpaf asaslprtad
      181 avralraegv rrvavapyvi apgflpdria agarearadl lapvlgpape larlllrryd
      241 gaalahargd ltalsa
//
LOCUS       WP_457694249             302 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694249
VERSION     WP_457694249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31725
     Region          43..296
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mastetkaps taeagdssgd iagleaglda lesrvvdrqp wlrtatskal ppliaiaivl
       61 glwqlayhfe lkphyllpsp vevghslqqk wlegtllsfv wtsvsrgalg flasvaigtv
      121 lglivarvka vraaigpils glqslpsvaw vpaaiiwfgl sdatiytvvl lgavpsiang
      181 lvagvdqisp lylragrtig atgfagvrhv llpaslpgyi aglkqgwafs wrslmaaeli
      241 vnapdlgtgl gqlleqgrel qdmswvlsai llilivgigi ellifapver rvlrsrgllv
      301 ks
//
LOCUS       WP_457694253             451 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfate adenylyltransferase subunit 1 [Streptomyces nigrescens].
ACCESSION   WP_457694253
VERSION     WP_457694253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11458414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..451
                     /product="sulfate adenylyltransferase subunit 1"
                     /EC_number="2.7.7.4"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0004781 - sulfate adenylyltransferase
                     (ATP) activity [Evidence IEA]"
                     /GO_process="GO:0006790 - sulfur compound metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47555
     Region          1..426
                     /region_name="CysN"
                     /note="Sulfate adenylyltransferase subunit 1, EFTu-like
                     GTPase family [Inorganic ion transport and metabolism];
                     COG2895"
                     /db_xref="CDD:442140"
ORIGIN      
        1 mstttsaida vdagatsllr fatagsvddg kstlvgrllh dsksvladql eavehasrnr
       61 gqeapdlall tdglraereq gitidvayry fatprrrfil adtpghvqyt rnmvtgasta
      121 elavvlvdar ngvveqtrrh aavaallrvp hvvlavnkmd lvdyaepvfa aiaeqfttya
      181 aslgvpeita ipisalagdn vvtpsahmdw yggptvlehl etvavvadps ddpgrfpvqy
      241 virpqtaehp dyrgyagqia sgvlrvgdav tvlpsgrtst ieaidvlgqa vdvawapqsv
      301 tvrltddldi srgdliapts gapgvsqdie atichvadrp ltvgqrvllk httrivkaiv
      361 kdipsrltld dlsqhpapge lvandigriv lrtaeplald ayadsrrtgs fllidpadgt
      421 tltagmagta faeaaeeaap adaaddegwd f
//
LOCUS       WP_457694260             565 aa            linear   BCT 27-JAN-2026
DEFINITION  nitrite/sulfite reductase [Streptomyces nigrescens].
ACCESSION   WP_457694260
VERSION     WP_457694260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Lu,Z.J., Cao,Y.Q., Long,W.J., Long,Z.D., Chen,G., Ma,Q.S. and Wu,B.
  TITLE     Isolation and characterization of an operon involved in sulfate and
            sulfite metabolism in Sinorhizobium fredii
  JOURNAL   FEMS Microbiol Lett 282 (1), 89-99 (2008)
   PUBMED   18336549
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Schnell,R., Sandalova,T., Hellman,U., Lindqvist,Y. and Schneider,G.
  TITLE     Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium
            tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in
            the active site
  JOURNAL   J Biol Chem 280 (29), 27319-27328 (2005)
   PUBMED   15917234
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Zeghouf,M., Fontecave,M. and Coves,J.
  TITLE     A simplifed functional version of the Escherichia coli sulfite
            reductase
  JOURNAL   J Biol Chem 275 (48), 37651-37656 (2000)
   PUBMED   10984484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414977
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..565
                     /product="nitrite/sulfite reductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050311 - sulfite reductase (ferredoxin)
                     activity [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62427
     Region          34..565
                     /region_name="CysI"
                     /note="Sulfite reductase, beta subunit (hemoprotein)
                     [Inorganic ion transport and metabolism]; COG0155"
                     /db_xref="CDD:439925"
ORIGIN      
        1 maansevpaa atprrkagrh rgegqwavgh ftplngneqf kkdddglnvr trietiyska
       61 gfdsidpndl rgrmrwwgly tqrkpgidgg ktailepeel ddkhfmlrvr vdggrlsvaq
      121 lraigevsee yargtaditd rqniqlhwir iedvpaiwek leavglstte acgdcprvii
      181 gspvagiaad eiidgtpavd eihdryigsk efsnlprkfk tavsgspvqd vvheindvaf
      241 vgvvhpehgp gfdlwvgggl stnpklaqrl gtwvpldeva dvwagvvgif rdygyrrlrt
      301 rarlkflmad wgpekfrqvl edeylqrklt dgpapeqpts kwrdhvgvhq qqdgrfyvgf
      361 aprvgrvdgt tltkiaelaa thgsdrlrtt veqkmiildv tqdqvdslva glealdfqvs
      421 pspfrrgtma ctgiefckla ivetkgrgas lidelerrmp dfqepvtinl ngcpnacari
      481 qvadiglkgq lvldndgnqv egyqvhlgga lglepgfgrk vrglkvtade lpdyvervlr
      541 nfeaertdge rfaqwaarae egalk
//
LOCUS       WP_457694262             199 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694262
VERSION     WP_457694262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..199
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21777
     Region          52..186
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 msisvttwhl eqtspadlsp aqappaeqgv rivrsevpsp efsrflytav ggdviwtdrl
       61 twpyaqwtef lgrpgvetwv ayergtpagf ielageadgs veiayfglip afrgrriggh
      121 llaygieraw dladrwpgrv ptkrvwlhtc skdgphaman yqrrgfrlyd ttvaeedgip
      181 apgpwpgagp lttdspage
//
LOCUS       WP_457694273             362 aa            linear   BCT 27-JAN-2026
DEFINITION  YihY/virulence factor BrkB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694273
VERSION     WP_457694273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38365
     Region          <85..306
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mqpanepter pagrltkara lyrnvskrrl awlllkdtvn scmkyrvtgl aaeaafwsll
       61 slpplilgll gvlgytdawi ghdtidsvrq rildgagtvl sdkgvnqiar pllndvftgr
      121 rpdvisfgfa ialwsgsram nvfvdtitim ygldgrrgiv ktrllafaly laalvvgava
      181 lplmvagpdt vvswlpaseh iiralywpvv lllsvafltt lyhasvpvrs pwpedipgav
      241 valgmwllgs fllrlyltst vegptiygsl aapvavllwi gvsafavlvg aamnasldrv
      301 wpsvataaar eeiarraaar tgaeratgda dgaaangegg ddgrggdgrr geghdaggtr
      361 de
//
LOCUS       WP_457694285             183 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457694285
VERSION     WP_457694285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..183
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18715
     Region          26..164
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mghdahrvpr pagaagaags gddaldheve eviaavltas rmlvgvsara lgrtaasltl
       61 pqlralvvld grgpvklaal adalgvnpst alrmvdrlea agsvtrqanp gnrrevvlsl
      121 tdrgrglvaq vladrhaeia tivsrlpadr ragliealra ltdaadeprv aprpspppep
      181 sgl
//
LOCUS       WP_457694286             397 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694286
VERSION     WP_457694286.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42165
     Region          17..390
                     /region_name="Beta-lactamase"
                     /note="pfam00144"
                     /db_xref="CDD:395092"
ORIGIN      
        1 mepatvnghc apeftgvrda fernfsehge vgaavtvtvd geavvdlwgg hadaagtrpw
       61 erdtlvnvys tskgmtalca hllvdrgeld ldapvtrywp efgqagkqdi pvrwllshra
      121 gliapreplp aghaydwdrv cavlaatppw wepgtaqgyh avtfgylvge vvrritgqsl
      181 gaflrseitg plgarvfigt paeeharcad mvgqldevrl aeqfpgapkp pfrsladhpl
      241 aivmlaltyi ptgdvnsaay rsaeipagna hagahglatv ygalaggtlv rpgtleamrr
      301 sqslpgerdl tidalapagy ehrwglgfml nhqgqagpnp rafghggagg sfafadpenr
      361 lsyaytmnky gggttgqdpr naglvravyq alaqqrs
//
LOCUS       WP_457694289             272 aa            linear   BCT 27-JAN-2026
DEFINITION  lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694289
VERSION     WP_457694289.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wong,H. and Schotz,M.C.
  TITLE     The lipase gene family
  JOURNAL   J Lipid Res 43 (7), 993-999 (2002)
   PUBMED   12091482
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Cygler,M. and Schrag,J.D.
  TITLE     Structure as basis for understanding interfacial properties of
            lipases
  JOURNAL   Methods Enzymol 284, 3-27 (1997)
   PUBMED   9379943
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087743
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=30288
     Region          21..221
                     /region_name="Lipase_3"
                     /note="Lipase (class 3). Lipases are esterases that can
                     hydrolyze long-chain acyl-triglycerides into di- and
                     monoglycerides, glycerol, and free fatty acids at a
                     water/lipid interface. A typical feature of lipases is
                     'interfacial activation,' the process of...; cd00519"
                     /db_xref="CDD:238287"
     Site            order(81..82,84..85,88..94)
                     /site_type="active"
                     /note="active site flap/lid [active]"
                     /db_xref="CDD:238287"
     Site            140..144
                     /site_type="active"
                     /note="nucleophilic elbow [active]"
                     /db_xref="CDD:238287"
ORIGIN      
        1 mtsatidqka tgytvrhalc maraselayk deqtieatar qwgfdrvrhh httfrppfpl
       61 edtqaytlgg hsmiitsfrg tepvklrdwl sdattppwpg pggkgyvhyg fgealeavwp
      121 qvraaidafr dnrqtvwftg hslggalaml agarlhfeep hvtangvytf gqprtcdrhl
      181 skefntafsd rmyrfvnnnd ivpqlppepa fhhvsalryi daqgalhhtm plisglidra
      241 qgftadafap asdgvrdhfm dayihalekn qn
//
LOCUS       WP_457694292             188 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694292
VERSION     WP_457694292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19764
     Region          25..187
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 meptqhpadt gsapsadgrr sslvlhingv vqtltvdhrt tvldllrerl gltgakkgcd
       61 hgqcgactvl vdgrranscl lpavaqdgrq ittveglaeg erlhplqqaf lerdalqcgy
      121 ctpgqicsav gmlaevadgf pshvtpptad paapveltdd eirermsgnl crcgaypriv
      181 eavreaas
//
LOCUS       WP_457694294             331 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457694294
VERSION     WP_457694294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34849
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpfgylrat sveeavraaa gqpgarflgg gtnlvdlmkl gvetpgllid vtrlpldrie
       61 elpdgglrig amvrnsdlaa avpvrdrypa lsqallagas gqlrniattg gnllqrtrcl
      121 yfqditkpcn krdpgtgcpa regvhrdlav lghsehcvat qpsdlavala aldaevhlhg
      181 pdgertvpvt efhrlpgdsp erdtvirpge litavqlppa apgarsryrk ardrasfafa
      241 lvsvaavlev rdgavrraal afgglahrpw raraaeevlh gapatedtfa raadaelaaa
      301 rplrdngfkv tlarnlavgv laglaapsdd h
//
LOCUS       WP_457694295             717 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces nigrescens].
ACCESSION   WP_457694295
VERSION     WP_457694295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..717
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=75692
     Region          17..706
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mspdsfplgp ppyplgaplv rregrekvtg taryaaehtp pgcayawpvp atvacgrvta
       61 vdvaaalalp gvyavltqen aprlaatddp tlavlqddrv phrgwyvala vadsleaara
      121 aaravrvsye taahdvrlta ghpglydaet anggypgtre rgdfegafaa apvtldatyt
      181 vpplhnhpme phastawwsd ghltvhdssq gatkvceela alfrldrsei tvisehvggg
      241 fgskgtprpq vvlatmaarh tgrpvklslp rrempavvgh raptvqrvrl gagddgvlta
      301 laheaathts tvtefveqaa vpgrimytsp nsrtvhrvvp ldvptpswmr apgeapgmya
      361 lesavdelav lldidpvdlr mrnepdtepd sdrafssrhl vgclregaer fgwrprdprp
      421 gvrregdlll gtgvaaatyp vfaapssaea haaadgsyri rvnatdigtg artvlaqiaa
      481 gvlavpeerv rieigssdlp pavlaggsag tgswgwavhk actelrhrlr dhvgplpadg
      541 ltaavdtrqe taerspyarh sfgatfaevq vdtvtgevrv rrllgvyaag rilnsrtars
      601 qfiggmtmgl gmalmegsgl dpafgdfaec dlasyhvpvc advplieahw leeedphlnp
      661 mgskgigeig ivgtaaalan avrhatgvrl rdlpltpdkv lpglpdrpge dragglh
//
LOCUS       WP_457694297             185 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694297
VERSION     WP_457694297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19577
     Region          10..124
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtlpgdrhyt velhasaerv pqirrilaah lrywdlelhi ppvcrgvael ltnvhrhigp
       61 dapcvvelrw tgrhltasva dqgprlpkll sagggglsrv aalsdswgtc gtpdgkviwf
      121 trrveaarks pltsrtplrs vpdakgqpav ppavpveplv epardaaaet aaeatpaass
      181 avslv
//
LOCUS       WP_457694307             299 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694307
VERSION     WP_457694307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31853
     Region          48..171
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mdrdndrrad gdearppdev aagnaaqaea wngddgqywv rqrehqeary rrltprlmaa
       61 agiradsrvl digcgsggts leaaraaaeg avlgvdlsgp mldearkqaa aaglpqvtfa
      121 qgdaqvhrfe daafdvvisr fgvmffadpe aalrniaqal rpggrlaflc wrdlaqnayl
      181 tvpfealapy vrlpefgapg epgpfslagp driralldga gfdeisvgav depmwmgtde
      241 ddavasltam plartmldea gekprraala alretmaahr gpegvtlgsa awlvtarrr
//
LOCUS       WP_457694313             558 aa            linear   BCT 27-JAN-2026
DEFINITION  CocE/NonD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457694313
VERSION     WP_457694313.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..558
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60401
     Region          51..554
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mtphthdvvp rsgwaapsgk pplssrmmra twrglpaeqh dvgwepglva paadgsplrt
       61 dhyfprtkgd fptllvrspy grglpwsply gilfaeqgfh vvlqscrgtg gsggrfdlwr
      121 neaadgqaav swlreqpwft gtlgtigpsy lgyvqwalal dpppelkamv vqvglhdpha
      181 lfyeggalll etalavgagm tyqhrglmpf vratlrlqrr lreitgarpl rgayrsalge
      241 vpwldevmth pdaddpywrg asvaaaaera avptsvitgw hdaladqnlq qfarlrraga
      301 essllvgpwt htsalqqgwp evfaeslawl rahlcddrag lrptpvrvhv ggedawrdld
      361 dwppapatta wfpaadgkls rqapvesgpl asfrhdpadp tpsvggplls rsagprdnst
      421 learedvltf tgplltepvd ilgpvsarlr iatdtghadv farlcdvddr nrstnvcdgl
      481 vrlrttgqtp aevtvamrtm ahrfaaghri rlqisggahp ryarnpgtge psaeatrflp
      541 vhltlhtgsa ltlpqqtp
//
LOCUS       WP_457694318             345 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457694318
VERSION     WP_457694318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Yang,X., Kang,C.M., Brody,M.S. and Price,C.W.
  TITLE     Opposing pairs of serine protein kinases and phosphatases transmit
            signals of environmental stress to activate a bacterial
            transcription factor
  JOURNAL   Genes Dev 10 (18), 2265-2275 (1996)
   PUBMED   8824586
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537757
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..345
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=35919
     Region          141..331
                     /region_name="SpoIIE"
                     /note="Stage II sporulation protein E (SpoIIE); pfam07228"
                     /db_xref="CDD:462119"
ORIGIN      
        1 mavvttvdlt agpgvgflpl vslgpafagl vggwrrtavv gltasvlclg lgvynglfes
       61 rrgltallsv agvtaagvva avmrqrreae lasvrsiaev aqrvllrpvp rgagplriav
      121 sytsavaear iggdlyevvt spagvriivg dvqgkgleav esaavvlgaf reaahdepdl
      181 pavgervera lnrhlsgerf vtavlaeiga gpqatllnfg hpaplvvrpd gtvdfaappd
      241 ralplgltlh gtvaplpyev pftpgdqllf ytdgvteard aadrfyplde raallkdpdp
      301 eaalrsvred lvehvegplh ddaamllvry rqepvngpqv sgspv
//
LOCUS       WP_457694329             923 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA translocase FtsK [Streptomyces nigrescens].
ACCESSION   WP_457694329
VERSION     WP_457694329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..923
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=96584
     Region          406..913
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 masrtsgkgt qstagpskqr agrtagaakk taakkapakp aakkaaaakk apakrapakk
       61 aapkpapspt ggvyrlarvc wlglahgiga mfrgmgrgak nldpahrkdg lallllglal
      121 viaagtwsnl sgpvgdlvel lvtgafgrld lvvpillggi avrlirhpek peangrivig
      181 lsalvvgvlg qvamacgspg rddglaavqd aggylgwvas kpliftvgqt lavallallt
      241 lfgllvvtat pvnaipqrlr algiklgvvh pvadeadhde vedyaeewre qparrprrsa
      301 aapaandpda ieeaalakrr rprrasaqpa pdrpmdavdv aaaaaaaldg avlhgvqpsp
      361 lvaglsssis gerrghdged sagesgtvpp argaepeppa tehtpavpdf tkappepsge
      421 lparaeqlql sgdityslps ldllsrggpg ktrsaandai vtslttvfqe fkvdaavtgf
      481 trgptvtrye velgpavkve kitalaknia yavaspdvri ispipgksav gieipntdre
      541 mvnlgdvlrl adaagdehpm lvalgkdveg gyvmanmtkm phvlvagatg sgksscincl
      601 itsvmvratp edvrmvlvdp krveltayeg iphlitpiit npkraaealq wvvremdlry
      661 ddlaaygfrh iddfneavrs gkvsspegse relapypyll vivdeladlm mvaprdveds
      721 ivritqlara agihlvlatq rpsvdvvtgl ikanvpsrla fatssladsr vildqpgaek
      781 ligkgdglfl pmgankpvrm qgafvteaev aavvqhckdq mapvfrddvt vgtarkkeid
      841 edigddldll cqaaelvvst qfgstsmlqr klrvgfakag rlmdlmesrn ivgpsegska
      901 rdvlvkpdel dgvlavirge ate
//
LOCUS       WP_457694337             855 aa            linear   BCT 27-JAN-2026
DEFINITION  ComEC/Rec2 family competence protein [Streptomyces sp. 900105755].
ACCESSION   WP_457694337
VERSION     WP_457694337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Ogura,M., Liu,L., Lacelle,M., Nakano,M.M. and Zuber,P.
  TITLE     Mutational analysis of ComS: evidence for the interaction of ComS
            and MecA in the regulation of competence development in Bacillus
            subtilis
  JOURNAL   Mol Microbiol 32 (4), 799-812 (1999)
   PUBMED   10361283
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..855
                     /product="ComEC/Rec2 family competence protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=87510
     Region          282..851
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC, N-terminal domain
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0658"
                     /db_xref="CDD:440423"
     Region          602..845
                     /region_name="ComEC"
                     /note="DNA uptake channel protein ComEC C-terminal domain,
                     metallo-beta-lactamase superfamily [Intracellular
                     trafficking, secretion, and vesicular transport]; COG2333"
                     /db_xref="CDD:441904"
ORIGIN      
        1 msratdgaap gpaaadrsvr agpgrrtgtv parqdaradl rlvppasaaw ataalaldap
       61 pgwtaavavv clvagaillg lgrartrvvt esadatsalp sdwrrasaga lllcvagaaa
      121 saglhgadvr rgpvpglara yatvtaevel tgdpwaarpr vrgdhatpaa vlvrgevrrv
      181 eqgdgtvvtt rspvlmavdt gvaapggggr erwlgllpst rlrvsgrlap ataggdrvaa
      241 llrvrerpvp vvvgepsgpq rlagrlragl reatdglped arallpglvv gdtsritpel
      301 deafeatdla htlavsgsnl tillalligp pglaqqterr glaprlglsl ratalfasal
      361 tlgfvvvcrp dpsvlraaac gavallalat grrrslvpal atavlllvly dpwlarsygf
      421 llsvlatgsl lllapgwaea lrrrgvperl aeglaaaaaa qavcgpvvav lsarvslvav
      481 pcnllaeiav apatvlgfga laaapvampa akvlawcagw pagwiaaiar tgaglpgagv
      541 dwpgswagal llagvtvavv plgrrllrhp wwcgvlgall vllvvrpapl arvvtgwppp
      601 gwrlamcdvg qgdatvlaag agtgvvvdag pdpalvdhcl relgitripl lvlthfhadh
      661 vaglpgvlrg revaqiettg feepadqaef vrrqaaeyrv pltravager rrtgpldwrv
      721 lwpppgqape pdgpndasva llvrsaglrm lllgdleppa qqellrspaa admghvdvlk
      781 vahhgsayqn pqllrlaapr valiscgvdn pyghpapgtv aelravgavv lrtdrdgala
      841 vtgggtdgdl rvard
//
LOCUS       WP_457694340             269 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457694340
VERSION     WP_457694340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29645
     Region          2..260
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpegdtvwrl aqrlhdaltg gpltrcdlrv prlatvdltg revldviprg khlltrfegg
       61 ltlhshlrmd gawkiyapae rwrggpahqi railgtadht avgyrlpvld llrtsdesrv
      121 vghlgpdllg pdwdpaealr rllttperpl gealldqrnl agignvykce lcfllgaspw
      181 lplgalprpe rvpalakkll eankrrpari ttpsarpdrr lwvygragrp clrcgtevrt
      241 adqdptaeer vtywcptcqp dppgshpag
//
LOCUS       WP_457694338             156 aa            linear   BCT 27-JAN-2026
DEFINITION  Dps family protein [Streptomyces nigrescens].
ACCESSION   WP_457694338
VERSION     WP_457694338.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..156
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=16530
     Region          8..153
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 msvvkstlsd edlgivgnal qgalvdlvdl slvakqvhwn vigprfrsvh lqldevvasg
       61 rqhadtvaer aaaigvspdg ravtvaktsg igevkdgwik dgdvvramvd alsavigrmr
      121 eritatadpd pvsqdiligl tadlekhrwm fqaeaq
//
LOCUS       WP_457694347             412 aa            linear   BCT 27-JAN-2026
DEFINITION  AI-2E family transporter [Streptomyces nigrescens].
ACCESSION   WP_457694347
VERSION     WP_457694347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44979
     Region          23..368
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpesdeitsn dvprpedrpd armprwlpra mvlalalvac fqlatwgfhq lislllnvli
       61 afflalavep avdwmaargm rrglatglvf lsilgaavgf ftllgsmlag qianmveefp
      121 qyldsviswi nstlhthlsr vevqnnllks dwlqkyvtds annvlavsat vlgslfnllt
      181 valfsfyfaa dgprlrrtlc svlpphrqte vlraweiava ktggylysrg lmalisgiah
      241 yvlleilgvp yapalgmwvg lvsqfiptig tylagalpil iaftvdpwya lwvfgfvvty
      301 qqfenyvlqp ritaktvdih pavafgsvva gtalmgavga liaipatatl qaflgayvkr
      361 yevtddlrvh grrgrgvral armrrnlhda qpsapledrk aggtqaegee vr
//
LOCUS       WP_457694349             157 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694349
VERSION     WP_457694349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16542
     Region          15..148
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mnarldafss ptvgkvfkhi iaagkvleds tlptatqelv klrasqingc gfctdmhskd
       61 aaaagetsvr lhlvaawrea tvfteaeraa lelteqgtri adaaggvtde awanaakhfd
      121 eeqlaalvca valinafnra nvmiqqpagd yqpgqfa
//
LOCUS       WP_457694357             311 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694357
VERSION     WP_457694357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=33106
     Region          66..278
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 msgasvlydv pgpkakarnl vysvagslav laliafvvmr lntqgqlape vwnifnnagv
       61 rtnirdgvlt tlevfavaav lslvlgvlla varlsdhkpv rwlatgfiel fravplliti
      121 yalwvlllsn reaigltgdq pqfwalvigl tvyngsvqae vlraginsvp tgqreaayal
      181 gmsktqvmtt vlipqavram lptiisqlvv tlkdtslgyi itfeellfta rqmstniivn
      241 gndtyvpfii vtgtiyvamc lalsalanwi errgrraktg igvatagepv aatdamevsd
      301 pvpdgpvgtk d
//
LOCUS       WP_457694359             215 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694359
VERSION     WP_457694359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23036
     Region          1..215
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mnvlldylpe frdgflgtla itassallal vlgvliagfr vspipplraf gtawvtvlrn
       61 tpltllflva ffvvpqvlfq gaspyvlatl algfytssfv ceavrsgint vplgqaeaar
      121 slgmtfsqtl gqivlpqatr tvlpplssif ialtknsaia gafgfgelfn vskllndkgy
      181 aiawiflwta laylvitftl salfrllerr mgvar
//
LOCUS       WP_457694362             261 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694362
VERSION     WP_457694362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28341
     Region          20..258
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msevsvtkna egpapagdql vvldnvnkhf galhvlqdid ltinrgevvv vigpsgsgks
       61 tlcrtinrle tvdsgsitid gkplpqegre larlradvgm vfqsfnlfah ktvlenvmlg
      121 qtkvrktdka eaakkarall drvgvgtqad kypaqlsggq qqrvaiaral amdpkvmlfd
      181 eptsaldpem inevldvmqq lardgmtmvv vthemgfars aanrvvfmad griveeaepn
      241 qffnnprsdr akdflskilh h
//
LOCUS       WP_457694364             246 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457694364
VERSION     WP_457694364.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  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 246)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26243
     Region          1..221
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mrlllveddd hvaaalsavl akhglavvha rngedalkal lpddaepfav vlldlglpdq
       61 dgfevcgrir kfcatpvimv tarsdvrsri hglnlgaddy vvkpydtgel larihavsrr
      121 tapgsaeqpa eegtadealr lgavtvelst rqvsvdgaav pltrkefdll allaqrpgvv
      181 frreqiisev wrtswegtgr tlevhiaslr aklrmpalie tvrgvgyrlv vpaagpgvrt
      241 saapas
//
LOCUS       WP_457694367             180 aa            linear   BCT 27-JAN-2026
DEFINITION  DoxX family protein [Streptomyces nigrescens].
ACCESSION   WP_457694367
VERSION     WP_457694367.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..180
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17913
     Region          36..151
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkpptelrph trarseavrp ppvaadagll llrltvglil aghgaqklfg lfggpgldat
       61 gkgfeafgyr pgaffaglag asevlgglgl aaglltplaa aaligvmina malaapkglw
      121 aetggfeypl iiavvaltva atgpgrfald rpfrwghggw rsaafalvag gigaavvlal
//
LOCUS       WP_457694375             731 aa            linear   BCT 27-JAN-2026
DEFINITION  RelA/SpoT family protein [Streptomyces nigrescens].
ACCESSION   WP_457694375
VERSION     WP_457694375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Ahmad,S., Gordon,I.J., Tsang,K.K., Alexei,A.G., Sychantha,D.,
            Colautti,J., Trilesky,S.L., Kim,Y., Wang,B. and Whitney,J.C.
  TITLE     Identification of a broadly conserved family of enzymes that
            hydrolyze (p)ppApp
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2213771120 (2023)
   PUBMED   36989297
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ronneau,S. and Hallez,R.
  TITLE     Make and break the alarmone: regulation of (p)ppGpp
            synthetase/hydrolase enzymes in bacteria
  JOURNAL   FEMS Microbiol Rev 43 (4), 389-400 (2019)
   PUBMED   30980074
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   4  (residues 1 to 731)
  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
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416884
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..731
                     /product="RelA/SpoT family protein"
                     /EC_number="2.7.6.5"
                     /GO_function="GO:0008728 - GTP diphosphokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008893 -
                     guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015970 - guanosine tetraphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=77869
     Region          41..719
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msaeatnpgn sgaagrkrgr rrlelrglrr igraallgpa prdglphale hvakvhrghh
       61 pdadldtltk ayllaesshr gqlrksgepy ithplavtli laelgaettt ltasllhdtv
      121 edtevtldqv rdlfgdevcy lvdgvtklek vdygaaaepe tfrkmlvatg ndvrvmsikl
      181 adrlhnmrtl gvmrpekqar iakvtrdvli plaerlgvqa lkaeledlvf ailhpeeyat
      241 tralvmeyaa rpdplavlaq rvrsvldeag idaevlvrpr hfvsvhrvrl arreptgadl
      301 grllvlvaed adcyavlgel htcftpvise fkdfiaapkf nlyqslhtav tgpsgevaet
      361 lirthqmhrv aeagvialgn pyaptdgvda pegeradptr pgwlsrllew qrttpdpdtf
      421 wtslrddlaq dreitvfctd appdgpsggt ggviglpaga scvdaayerh geaahcciga
      481 rvngrlatls tvlhdgdslq llmapdsaag pspewldhar tpaarlaiar wlagpresca
      541 rpagpgdgls aappadrraa ghdrpggdpv apasvlvvad lpgaavrlag cctpvppdav
      601 tgfavrggtv tvhralcpvv armaatgrqp vgvrwrgagq gghgcrvtll aeafsrphll
      661 adlteaiasq gaavvsaave ppheqrvrht ytlhlpnaag lpslmramrq vpgvfdvlra
      721 grarqpaalr p
//
LOCUS       WP_457694377             542 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457694377
VERSION     WP_457694377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..542
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58779
     Region          71..488
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(177,179..180,310..314,339,342..343,346,361,365,427)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mslplrrpsr dpdrpvpalp rgpsgrgrrt glraaalgla alttlgvaep pavgpqglgd
       61 rlfptlgntg ydvtsydvsl dysghndrpm natteitara tseldhlnld fargavrsvk
      121 iggmaarheq hgedlvlipp fhisrgqelk isiehtsdpr ikndggwirt sdglamanqa
      181 daahrvfpcn dhpsdkalft fhitapqqlt avanglplrp gtrgarrtwt yrtthpmate
      241 laqvsigkss vvlrhgphgl plrdvvptad raalarwlak tpghvawmer rigpfpfeay
      301 gvlianaktg feletqtlsl fekalfttdq lpawyvesvm vhelahqwfg dsvsprrwsd
      361 vwlneahatw yealyaqekg drrasldarm rhayeqsdgw raeggppaap kipspgqkis
      421 ifrpivydgs alvlyalrqk igpaafdrie rewvtrhrdg vadtgdfvel askisgenlt
      481 affqgwlygd rtppmpgrpq wqprkgadkp gakgavpgpg akgtapapgg pkgaagkpgk
      541 pa
//
LOCUS       WP_457694379             396 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457694379
VERSION     WP_457694379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="trypsin-like serine 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=42447
     Region          149..360
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrsirrpvla aaaltavlal tatgcgpegd nadakptqga gqdttgggdf eipqdiqdkl
       61 kehgvdldkw kngewknwdr dkwlreagef inpiikdfwd kdkidkvkpp qdpskpedis
      121 edqgktdpep aavpaqpvkt pytstapgvg lllfstpkge srcsatvvkd pahpgksnlv
      181 wtaahcvhag ksggwyrnmm fvpnfnktgg sagqlknkpf edrvpsgkww addmatsqqw
      241 ikaggavpgv pmapydyalm hvkpeqstgg ksleemagga ykvdfnapam akipsltaqg
      301 ypaeppfdga aqqqctdkpt rlsmdakkpt myrigctmtg gssggpwfvk gadgkpvlvs
      361 nmsmgprpar wsagphlgpe akslfdnmsk kwaskq
//
LOCUS       WP_457694381             674 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457694381
VERSION     WP_457694381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..674
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73013
     Region          88..674
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnerpgpdgg qpaervpahq gagtiesvpr qqrrapdeac hqqlheppdr avphgapgph
       61 drartgdhdp ldhpdpavaa daagiehllr cwlresgphh paegrlrlpl qsaasaliip
      121 vrywsptgwh rlgaptldga pagaapldav tlaallrrea ahgdrrvsdg gehrvadgee
      181 rpepagapqq apdgdgaelv grvansvrnv avfltdrrar paddhgalfl eaeqslllgh
      241 plhptpksre glseaetray spelrgafpl hwiavhhsvl aadsawterg kpvpaeqltr
      301 gfagsgcrlp ddtvplplhp wqareladrp diaalreagl lhdlgahgpl whptssvrtv
      361 yrpdadamlk lslglritns rrenlrkela rgvevhrllr tglakqwqtv hpgfdivrdp
      421 aylavdgpdg apvqgldvvi rhnpfsttdd avciagltsp rpwpgrsgvr srledlvgtl
      481 sartgrtlsa vatewflryl eavvrpvlwl dgtagivlea hqqntvvlld pdgwpvggry
      541 rdnqgyyfrt srraelerrl pgigaasdtf vaddvtderf ayylginnvl gligafgsqr
      601 lvreeillaa frrfladaaa apqahrsplp eqllaartlr ckanlatrlh gmdelvgpve
      661 tqsvyvtlps plap
//
LOCUS       WP_457694383             227 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694383
VERSION     WP_457694383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24142
     Region          64..209
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mpptdpglss adtldrqlpp ecsalsddgq rppapaagpl ldnlagwgaa dtpdgpfalv
       61 pvrpdrdldr itgwmndpav aaywelagpp ettaahlrgq ldgdgrsvpc lgvlagvpms
      121 yweiyradld plarhyparp qdtgvhllig gagdrgrglg stllratadl vldhrpqcar
      181 viaepdlrnt asvaaflgag fryadeielp ekraalmvrd rarrhll
//
LOCUS       WP_457694385             588 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457694385
VERSION     WP_457694385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..588
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65939
     Region          10..586
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mspepqpshr awqhaarrlf aktlaefaye evltpepdgt apdgtpqyrl pvtdtlvyrf
       61 rarrgayghw rvdpdsitpd tdpfhffaha hdtvlglsgd ttghlirelt atlaadtrld
      121 agalsaadla dldyaslegh qtghpwlvan kgrlgfsatd aatwapears arrlpwlaah
      181 hsiahyrgip tlatpdrlyg eelapatrha fartisdegl dpadylylpv hpwqwdetia
      241 plfapqladr siialptdnd lrlpqqsirt flnlsrpear tvklplsiln tlvwrglpte
      301 rtlaapavtr wvhglrdtdp ylrdetrvil lgetasvtve hplydrlpgv pyqfkellgc
      361 iwrepltghl dpgerartla allqtdprgr altaelvrrs glaprawlar lfaallppll
      421 hflyrygtvf sphgenaivv fdehdvptrl avkdfvddvn tssrplpehd smpddvravl
      481 lteppafltq fihsglfvgv frylaplcad qlgvpeaefw slvraeilrh herfpalker
      541 hetfdlltpr ierlclnrnr lhvdgyrdrt drphaavhgt vpnplhmp
//
LOCUS       WP_457694386             678 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent DNA helicase [Streptomyces nigrescens].
ACCESSION   WP_457694386
VERSION     WP_457694386.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..678
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72649
     Region          18..647
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtkpslpdll haavtavggt erpgqvamae avaeavdeqs hllvqagtgt gkslgylvpa
       61 lahgmgappa rgsegrgrvv vatatlalqr qlverdlprt vetlhpllrr rpefamlkgr
      121 snylclhrlh egvpqeeedg lfdvfeqatp tsklgkdllr lrdwadetet gdrdaltpgv
      181 sdkawgqvsv ssreclgask caygaecfae aareraklad vvvtnhalla idaiegapvl
      241 pqhevliide ahelvsrvtg vatgeltpgq vnravrraak lvnekaadql qtasetferl
      301 melalpgrle eipedlgycl malrdaartv isalgstrdk svqdedavrk qalaavenvh
      361 avaeriangs eydvvwyerh drfgaslrva plsvsgllre klfddrsvtl tsatlklggd
      421 fngvaaslgl apegtegedv ppwkgldvgs pfdyskqgil yvakhlaqpg regsrtdmld
      481 eltelieaag grtlglfssm raaqaaaeel rgrldlpill qgeetlgeli rtfaedartc
      541 lfgtlslwqg vdvpgpncql vvmdrvpfpr pddplmsarq kaveeaggng fmavaathaa
      601 llmaqgagrl vratgdrgvv avldprvera rygsflrksm pefwyttdrn qvrrslaaid
      661 aaataaespq aaeakpea
//
LOCUS       WP_457694390             173 aa            linear   BCT 27-JAN-2026
DEFINITION  TerD family protein [Streptomyces nigrescens].
ACCESSION   WP_457694390
VERSION     WP_457694390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Taylor,D.E.
  TITLE     Bacterial tellurite resistance
  JOURNAL   Trends Microbiol 7 (3), 111-115 (1999)
   PUBMED   10203839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..173
                     /product="TerD family protein"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=18812
     Region          5..168
                     /region_name="TerZ"
                     /note="Stress response protein SCP2 [Signal transduction
                     mechanisms]; COG2310"
                     /db_xref="CDD:441884"
     Site            order(28,30,76)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
ORIGIN      
        1 mstlnkgiek vevtlkwdps ptgtpdndld ivaatytada phgepaylvh fdsrspdgti
       61 tlnrdsrtgq gfgfdeimtl eldrlaenyt rvivgvaiqq gegrkvfgdi antavrireg
      121 yadltehdft evagataatv aeftrdeagq wrfrpalrgf dtdpnafase mgr
//
LOCUS       WP_457694392             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694392
VERSION     WP_457694392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20793
     Region          2..193
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkqvdhesr rrqiaeavcr ladesglegv tlrdvaarak vsmgavqrcf gtkeemlvfa
       61 lghigervtt rvsarlaasp aqsartalgh aatevsllqe ehraearvwl afvaqaavsp
      121 plagilrtny aglqtvfaql iaeasgtadp draartllal adgltthvlv ghlspadald
      181 vlddqlnrlw dertn
//
LOCUS       WP_457694399             539 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457694399
VERSION     WP_457694399.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58087
     Region          7..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mptqislhdi tksygdrlll dgvslsvrpg ervgivgeng agkstllril agaerpdegh
       61 valradggvg ylgqtpdlpp drtvqdaida aladlreter rlrslesgld ratatgleey
      121 gdlltvfelr ggyeagarvd ralhalglaq lgherrlgsl sggeqarlgi acliaaapei
      181 mlldeptnhl dataldwleg allahrgtvl tvshdrlflq riatalvevd adrrglvryg
      241 ggystfiaak daarrrweqd harwceqitq ltdfaggaar svaqgrpmkd gnkmaydrdk
      301 grvqasvssr vrnaqerlrr lrenpvprpp dplrfraapd vgeaegtlvr ldgvrvggrl
      361 avdsltvaag erllihgang agkttllrvl aglttpdsgt vlrrgrigfl aqeipvsrpa
      421 epllsvfrrg lagdveelta lllsfglfre rdlqvpvgal sagqrrrlal arllarpadl
      481 llldeptnhl alglveelea alsawpgalv vvshdrllrr rfsgrsyeir dgrpalsap
//
LOCUS       WP_457694401             219 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694401
VERSION     WP_457694401.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25567
     Region          7..198
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 marprrivli rhgesegnvd dtvyerepdh alaltrdglr qaadaggavr emfgdervsa
       61 yvspyrrthq tfrelrldpa kvrvreeprl reqdwgnwqd redvrrqkay rdayghffyr
      121 faqgesgadv ydrvgafles lwrsfedphh ppnvlivthg ltmrlfcmrw fhwtvadfes
      181 lsnpgnaewr tlllgpdgry tldrpferwc epvpygatg
//
LOCUS       WP_457694417             254 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457694417
VERSION     WP_457694417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 254)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27132
     Region          45..238
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mppydpsafp pfavtvdlvv ltvrrhalca lavrrgeppf qgrwalpggf vradedlega
       61 aarelaeetg lhaqspagss pvygahleql atygdpkrdp rmrvvsvahl vlapdlpapk
      121 aggdahsarw apvetlleqd dtlaregela aplafdhari lgdgverars kieysslata
      181 fcppeftvge lrrvyeavwg valdprnfhr kvtgtpgflv ptggtttrqg grpaqlfrag
      241 gatllnppml rpev
//
LOCUS       WP_457694419             334 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694419
VERSION     WP_457694419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35524
     Region          92..311
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mlftkdlkgv qgvadkrcvs tlahtmmtaa rpgdtglagp geldrypyan aaanaanann
       61 aagqdraerv sqvwdgsead igrvgrraag srgrglhgql vqqlgqmivs gdlgadrplv
      121 peeigqrfev srtvvreslr vleakglvsa rpnvgtrvrp vsdwnlldpd iiewraygpq
      181 rddqrrelce lrwtieplaa rlaaghgred vqqrladmve imghsaaqgd tmtfsradae
      241 fhslllqlag nrmlehlsgi vsaalhvsgg pgggcerpve tsvgqhmrvv daigsgdata
      301 aesamrqlla ahseivgqgs gtpvdhvvpa preh
//
LOCUS       WP_457694423             269 aa            linear   BCT 27-JAN-2026
DEFINITION  serine protease [Streptomyces nigrescens].
ACCESSION   WP_457694423
VERSION     WP_457694423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Page,M.J. and Di Cera,E.
  TITLE     Serine peptidases: classification, structure and function
  JOURNAL   Cell Mol Life Sci 65 (7-8), 1220-1236 (2008)
   PUBMED   18259688
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10076129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="serine protease"
                     /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=27395
     Region          28..261
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            28
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(75,128,224)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(218,239,241)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
ORIGIN      
        1 mrptahaalg alalalalpa paaadesvig gkpaplshsp wavalasher fgaqrsgqfc
       61 ggvlvghstv vtaahclske vlgvpwrqvr dlrivvgrdn laggggrelk pakvwvnpry
      121 nswtndgdma vltldkplpn rpipiagrrd sayepgnaat vygwgdttgg gsyasrlraa
      181 hvnvlrdavc araypgsadg ryraqsmlca gepaggrdac qgdsggplvv rgrlvglvsw
      241 gtgcgqagsp gvytrasall pavsahgag
//
LOCUS       WP_457694425             706 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces nigrescens].
ACCESSION   WP_457694425
VERSION     WP_457694425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=77200
     Region          21..700
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaemsvpst avltgadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg gycdhievil hddgsvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrsskthsi sfrrgvpgif tesgpdapfd
      181 pgngllkgkr iaktktgtrv rywadrqifl kdaklsletl hararqtafl vpgltlvvrd
      241 ergidgagkt eetfrydggi sefceylaqd kavcdvlrlt gqgtfketvp vlddrghmtp
      301 tevtrelgvd valrwgtgyd atvksfvnii atpkggthvs gfersvaktv nevlrsskll
      361 rvaeddvvkd damegltavv tvrlaepqfe gqtkevlgts aasrivaqvv skelksflts
      421 tkrddkqqar svmekivaaa rtriaarqhk eaqrrktale ssslpaklad crsddvdrse
      481 lfivegdsal gtaklarnse fqallpirgk ilnvqkssvs dmlknaecga iiqvigagsg
      541 rtfdidtary gkvifladad vdgahircll ltlfqrymrp mveqgrvfsa vpplhrvelt
      601 npkkgqekyi ytysdnelrq tllelqrkkv rykdsiqryk glgemdadql aettmdprhr
      661 tlrrinisdl eaaekafdll mgnevaprke fitnsastld rsridt
//
LOCUS       WP_457694432             534 aa            linear   BCT 27-JAN-2026
DEFINITION  solute symporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457694432
VERSION     WP_457694432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10008332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..534
                     /product="solute symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015123 - acetate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55113
     Region          2..534
                     /region_name="ActP"
                     /note="Na+(or H+)/acetate symporter ActP [Energy
                     production and conversion]; COG4147"
                     /db_xref="CDD:443318"
ORIGIN      
        1 mtgdhqtlal llfsvfiavt laittwvsrr rrgsteefya ggrlfspmen gfaiagdyms
       61 aasflgisgl ialfgydgll ysvgflvawl ivlflvaelv rncgrftlad vvaarmrerp
      121 vriaagaasv tvsvlylvaq mvgagslval lvgsagqqar twmvigvgal mvvyvafggm
      181 rattwiqvvk avllmggava ltvlvlvrfh gdinelltta aersghgrdf lapglkyggd
      241 wtsrldfisl gialvlgtag lphilsrfyt vptaraarrs vvwsigligg fylmtivlgf
      301 gaaavlgsda vrasntagnt avpllaldlg ggagstggtv lfavvaavaf atilavvagi
      361 tlassasvah dlyaslrrpr gtaqdaqrae vavariaava vgavaiglal laqdlnvafl
      421 vglafavaas anlpvllytl fwrrfttrga vwsvygglvp aitlvvlspv vsgspeslfp
      481 gldfavfpld npgvvsiplg flmgwlgtvl speaadearh aetevraltg agaa
//
LOCUS       WP_457694441             380 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694441
VERSION     WP_457694441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41174
     Region          3..352
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 matqqipvvv lagflgsgkt tllnhllgtg dgtrigaivn dfgsieidam tvagqvdsmv
       61 slgngclcca vdtseldtyl erlarpsari dvivieasgl aepqelirmi lasdndrivy
      121 gglievvdaa efddtrvrhp eldrhvgiad ivvlnkadrl gdaarqslmd tlaglapgrp
      181 victaygrvd pelffdrgpg edhdaavrql sfedllreaa angaaayeah dahdaddrcg
      241 hpgdcddpgh thhaghlhaa yesveftsae pmhprrlmdf ldsrpaglyr ikgfvhfdvp
      301 enrqkftvha vgdflrfypa pwpkgeerct qlvmigsgid apalrkelen cresapsead
      361 pnsmwgvlry vaareeaede
//
LOCUS       WP_457694443             815 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA gyrase/topoisomerase IV subunit A [Streptomyces nigrescens].
ACCESSION   WP_457694443
VERSION     WP_457694443.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Nollmann,M., Crisona,N.J. and Arimondo,P.B.
  TITLE     Thirty years of Escherichia coli DNA gyrase: from in vivo function
            to single-molecule mechanism
  JOURNAL   Biochimie 89 (4), 490-499 (2007)
   PUBMED   17397985
REFERENCE   2  (residues 1 to 815)
  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 815)
  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 815)
  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 815)
  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 11415135
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..815
                     /product="DNA gyrase/topoisomerase IV subunit A"
                     /EC_number="5.6.2.2"
                     /GO_component="GO:0009330 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) complex [Evidence
                     IEA]"
                     /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=88608
     Region          12..804
                     /region_name="GyrA"
                     /note="DNA gyrase/topoisomerase IV, subunit A
                     [Replication, recombination and repair]; COG0188"
                     /db_xref="CDD:439958"
     Region          560..616
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          622..663
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          667..714
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          717..774
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
ORIGIN      
        1 marrstktpp pddfeerild idvvdemqgs fleyaysviy sralpdardg lkpvhrrily
       61 qmnemglrpd rgyvkcarvv gevmgklhph gdasiydalv rmaqpfsmrl plvdghgnfg
      121 slgnddppaa mrytecrmas atslmtesid edtvdfspny dgqeqepaal paaypnllvn
      181 gasgiavgma tnmpphnlge viaaarhlik hpsadldtlm rfvpgpdlpt ggrivglggv
      241 rdayekgrgt fkiratvtve nvsarrkgli vtelpfmvgp ekviskikdl vgskklqgia
      301 dvkdltdreh glrlvievkn gfnpeavleq lykltpmees fginnvalvd gqpltlglke
      361 llevyvdhrf nvvrrrsefr rtkrrdrlhl veglltalld idevirlirs sensaqaker
      421 liehfslsdi qtqyildtpl rrltkfdrie leserdrlqd eiekltrile sdtelrklvs
      481 gelaavakky gtdrrtvlle sagtsvgavp levsddpcrv llsstgllar tvtgdvpfda
      541 dakrvkhdvi vsavpattrg evgavtslgr llrisvidlp qlpetaaapn lsggaqlsef
      601 ltledgeelv clttldessp glalgteqgv vkrvvpdypa nkeelevitl kegdrivgav
      661 elrtgeedlv fitneaqllr ypasqvrpqg rpaggmtgvk lgegakvisf aavdpaadam
      721 vftvagshgt lddsvatakl tpfdqyprkg ratggvrcqr flkgedcltq awtvpapvra
      781 adakgspvel pevdprrdgs gvpltkpvta lagpv
//
LOCUS       WP_457694445             266 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457694445
VERSION     WP_457694445.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27174
     Region          66..260
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mafiratgkh rrasrpvrtt rnvagiatla aggvvasvas palaatdear lhdtglqqav
       61 vlgdelanrv eaqadaqqad aeaaaakaka eavakkqade akrraeaakk kakaaheakv
      121 raardaerkr lnafvapigd syvstaykas sglwssgsht gidfhaasgt svhavgsgtv
      181 veagwggsyg nnvvikmndg tytqyghlss lgvsvgqqvt pgqqiglsga tgnvtgphlh
      241 feartgadyg sdidpiaylr ghgvnv
//
LOCUS       WP_457694446             229 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694446
VERSION     WP_457694446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24870
     Region          7..202
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrghisahav ctairddivs galapgsrli eeilaarygv srvpvrealr tlqsegfvtt
       61 rhhagacvae pteqeaadll dvralleplg aaraavrrsp ahlkvlrglv rlgrerarhg
      121 npadlrqldg wfhetlaqaa gspsltallt qlrrkiewmy avelpprage swdehgavld
      181 avargdaera ralmaahveh slpvyrlqlp vkaevrdpkp pvntarvrp
//
LOCUS       WP_457694447             999 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional acetate--CoA ligase family protein/GNAT family
            N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694447
VERSION     WP_457694447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Sanchez,L.B., Morrison,H.G., Sogin,M.L. and Muller,M.
  TITLE     Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming)
            gene from the amitochondriate protist, Giardia lamblia
  JOURNAL   Gene 233 (1-2), 225-231 (1999)
   PUBMED   10375639
REFERENCE   4  (residues 1 to 999)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
REFERENCE   5  (residues 1 to 999)
  AUTHORS   Mai,X. and Adams,M.W.
  TITLE     Purification and characterization of two reversible and
            ADP-dependent acetyl coenzyme A synthetases from the
            hyperthermophilic archaeon Pyrococcus furiosus
  JOURNAL   J Bacteriol 178 (20), 5897-5903 (1996)
   PUBMED   8830684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18515002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..999
                     /product="bifunctional acetate--CoA ligase family
                     protein/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.2.1.13"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0046356 - acetyl-CoA catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=105730
     Region          26..175
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          203..990
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mqtppehayp thweadvvlr dggtarirpi tpddaerlvs fyeqvsdesk yyrffapypr
       61 lsdrdvhrft hhdyidrvgl aatiggefig tvrydrindq glpaknpedd qaevaflvqd
      121 ahqgrgvasa llehiaavar ergirrfaae vlpanskmik vftdagythq rtfedgvvrl
      181 efdlepteqs mavmrgreqr aearsvqrll apgsvavigt grapggvgrt alrslldsgf
      241 tgrvhavnha fpenlhrldp edvptvrtlr eitdpvdlav iavpadsvpd virdcgehgv
      301 qgvlvlssgy aeagpegrer qrallrqars ygmrligpna fglintapdv rlnaslapqm
      361 pgaghiglft qsgaigiall sglhargpgd ggiagisafv sagnradvsg ndllqywyed
      421 pdtdvvilyl esignprkfa rlarrtaavk pvvvakgarh ngtappghav ptvrvpdstv
      481 aalmrqagvi rvdtvtelid aglllasqpl pagpriailg nseslallay daclteglrp
      541 qrprvlasaa tpddfraala ealsadgcda vvvtaipwvg egaavspggs egaaladalr
      601 taaaaqpekp vtvvhlamdd laqtlaapap aqptesaapa rdeaarpepa arpanpapap
      661 ppvppapsrs prplaptgpp ptlaarqatp ardaeaatpr rprreplrip aypaaeravr
      721 slaeavryaa wrreaadpgr vpeyddiqea aagadiegll drlgpdvptg rsvpvppqda
      781 eallarygih tlpvlpapdp dtavraaarl gypvalktta phlrhrpdlg gvrldiagea
      841 elrrtyaelt dylgspeelr pvvqsmvprg vdtvvraaid paagavlsfg lagapsqllg
      901 diahrlipat drevaeqirs iraapllfgw rgsqpvdtaa laelllrvsr lvddhpevvg
      961 vdlepvvvaa qglsvlgatv rlarppattd lgprrlpvy
//
LOCUS       WP_457694449             396 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694449
VERSION     WP_457694449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42570
     Region          35..392
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mvhtapawpe pepldplsap vprygtasla dllptiaagl gipglagame lapadracvf
       61 lidglgwell rahpeeapfl tsllgtsfng sgrpltagfp sttatslasv gtglppgahg
      121 lpgytcedpa agalmnqlrw spwtdpyvwq pyptvfqlad tagihtcqvs apnfqhtplt
      181 kvalsggtfh grlsgeermd laaeqlaagd rslvytyyse vdgkghrygv nsdawrgqlm
      241 yvdrlaqrla eqlpprsaly itadhgmidi pfdpesridf dedwelragv rllggegrar
      301 hvyahqgaaa dvlavwrevv geqmwvasre eaiaagwfgp rvddrvrari gdvvaaahad
      361 mviiaterep resemvgmhg smtpveqlvp llevrt
//
LOCUS       WP_457694455             279 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase [Streptomyces nigrescens].
ACCESSION   WP_457694455
VERSION     WP_457694455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28667
     Region          10..273
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mnaiitatel aselarptpp vlldvryqlg gppgrpeyaa ghvpgavyvd ldselasppg
       61 pagrhplpdl dvfaramraa gvradrpvvv ydggqgwaaa rawwllrwtg hpdvrvldgg
      121 lavwkasgga lsveqpappa gdfrplpgav plltaddaaa larrgvllda raaeryrgev
      181 epidrvaghi pgavsaptte nvvegdtvfr daadlakrfa slgatadvev gvycgsgvsa
      241 ahqvlalava gvpaalyvgs wsewtadpsr pvatgpqpg
//
LOCUS       WP_457694457             296 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694457
VERSION     WP_457694457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 296)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 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 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31766
     Region          33..148
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          204..286
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvsgehpadg gpgaaavpra rdewarhwry dglpgldllr aryvrhsfpr hahdgyvvca
       61 vtsgieevgl rqgtvraghg giimlnpeva htaragapeg wayatlypsy evvaeiaeet
      121 talrgtagfd rtvaedpqlg gvitdihraa eagnalaads llriavarll rryggplpar
      181 tprtagarta araravleer maappslerl aqelgtspfa llrafkgvyg mpphtwltda
      241 rvrrarrlle agrtpadtav avgftdqphl nrhftrivgv ppgayrrers aqgrav
//
LOCUS       WP_457694459             272 aa            linear   BCT 27-JAN-2026
DEFINITION  AzlC family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694459
VERSION     WP_457694459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27387
     Region          18..237
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 meraappppa ppaktdaavi rdalgvgvav glsgfafgvt sagvglsllq tcalsllvft
       61 gasqfalvga laaggnplta aagafflgar nafyglrlsa vlgyrstvkp faahwvidet
      121 savtlaqpdr rtarlgftvt gltlyvlwnl ttfvgalgae algdteawgl daagpavfla
      181 llapmlketv ervaaglavv lvmvtlpllp tgvpvlvsal aapavlvvqg rrerakevgt
      241 aqepgagrgt agpparpdgt pesrrateed qa
//
LOCUS       WP_457694462             551 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457694462
VERSION     WP_457694462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
REFERENCE   7  (residues 1 to 551)
  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   8  (residues 1 to 551)
  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   9  (residues 1 to 551)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20761992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..551
                     /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=58742
     Region          <53..160
                     /region_name="sCache_3_2"
                     /note="Single cache domain 3; pfam17203"
                     /db_xref="CDD:435783"
     Region          183..508
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mvqlaiatgv talatglfla plsaqlddqa mrralaiaqt aaaesrldda lessrptrhg
       61 pvqneaerir aatgaeyvvi mdkrgvrwsh tdpdeigrhv stdpsaalsg qdvmqidegt
      121 lgrsargkvp lrgedgkivg avsvgiayes vqerllstvp qllayaggal avgalaaylv
      181 srrlqrrthd lafsdisall aereamlhgi regflaldkh grirlmndea qrlldlried
      241 tghhleaalp pgrttdvlag rvsgpdlltv sgqrvlvanr mptddggavv tlrdrteler
      301 lgreldgtrg lidalraqdh ehanrlhtll gllelglhee avefvtqavg vhrataeqvt
      361 erihdplvaa llvgkatvat ergvslsisp ethlpdrlvd ppslvtilgn lvdnaldats
      421 gerdaqleae vradgrtaiv rvsdngpgvp eerraeifte gwttkeppah gqrgiglalv
      481 rrlaeryggn aevaerlggg avftvtvpda lsdelseira aapqkaitdt httrraavgt
      541 hrphgateag r
//
LOCUS       WP_457694464             445 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457694464
VERSION     WP_457694464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..445
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48470
     Region          5..435
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mghtateqag sggltatehr langlrvvls edhltpvaav clwydvgsrh evkgrtglah
       61 lfehlmfqgs aqvkgnghfe lvqgaggsln gttsfertny fetmpahele lalwleadrm
      121 gslltaldde slenqrdvvk nerrqrydnv pygtafeklt amaypeghpy hhtpigsmad
      181 ldaasledar affrtyyapn navlsvvgdi dpertlawie kyfgsipshd gkqpprdgsl
      241 pvviggelre vveedvpsra lmaayrlphd gtreadaadl altvlggges srlynrlvrr
      301 drsavaagfg llrlagapsl gwldvktsgg vevpdierav deelarfaae gptpeemera
      361 qaqlerewld rlatvsgrad elcrfavlfg dpqlalsavq rvlditseev qaaakarlrp
      421 dnravlvyep tepsdadtee geadq
//
LOCUS       WP_457694466             460 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457694466
VERSION     WP_457694466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48181
     Region          6..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mdfhpqpqgg apkpwafpap ersqlpnglt lltshrpgqq vvaveinlva pldaepegld
       61 gvatimaral segtdthdae efaaelercg atldahadhp gvrvslevpa srltralgll
      121 adalrapafp eseverlvrn rldeiphela nparraamal skelfpatar msrprqgtee
      181 tvaridaaav rafydahvrp atatavivgd ftgvdlgaal adtlgawsgs taeplkaspi
      241 vaddtgrvvi vdrpgavqtq mllgrigadr hdrvwpaqvl gayclggtlt srldrvlree
      301 kgytygvraf gqvlrstapt spegstgaal laisgsvdtg stvpaledlw kvlrtlaaeg
      361 ltdeerdvav qnlvgvaplk yetaaavagt ladqveqqlp ddfqaqlyar laetgtveat
      421 aaavnafpvd rlvtvlvgda aqiaepvkal gigevtvvsg
//
LOCUS       WP_457694470             529 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces nigrescens].
ACCESSION   WP_457694470
VERSION     WP_457694470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..529
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57268
     Region          10..527
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 msepeaniht tagkladlqr rveeathags aravekqhak gkltarerid llldegsfve
       61 ldefarhrst nfgieknrpy gdgvvtgygt vdgrpvcvys qdftifggsl gevygekivk
      121 vmdfalkngc pvvgindggg ariqegvval glfaeifrrn vhasgvvpqi slivgpcagg
      181 avyspaitdf tvmvdqtshm fitgpdvikt vtgedvgfee lggarthntt sgvahhmagd
      241 ekdaidyvkg llsylpsnnl seppafpeea dletsdvdre ldvlipdsan qpydmhvaie
      301 hvlddhefle tqalfapnil tgfgrveghs vgivanqpmq fagcldinas ekaarfvrtc
      361 daynipvitf vdvpgflpgt dqeyegiirr gakliyayae atvplitvit rkafggaydv
      421 mgskhlgadl nlawptaqia vmgaqgavni lhrrtlaaie dpaaqderrq eliqeyedtl
      481 lnpyvaaerg yvdavimpse trrhivrglr tlrnkrealp pkkhgnipl
//
LOCUS       WP_457694474             268 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694474
VERSION     WP_457694474.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28191
     Region          14..261
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mqrqrqrfga dgwvaierhg fvaelimdrp kamnavstam adslaqacae laadrsvrav
       61 vlsstheraf cvgadlkern sftdadlmrq rphtraaytg vlelpvptia avhgfalggg
      121 felalacdli vadgtavvgl pevsvgvipg gggtqllprr vgaaraaelv ftarrvpape
      181 aaelglvdql aadgqdraea lelaariarn spvglraakr amrlghgldl raglevedga
      241 wrsvafsgdr aegvaafnek rdpewpge
//
LOCUS       WP_457694479             421 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Streptomyces nigrescens].
ACCESSION   WP_457694479
VERSION     WP_457694479.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=44447
     Region          71..253
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          259..390
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtdskrrkgl iasaallggv ltlaacggss aadrghggad airhensrqv daaaakdasd
       61 aritilpedg atdtglnsda nvtvsdgelt dvtmtsvesk eavdgtlaad gsswkpdqpl
      121 arstkykvta havdsqgrka venssfttva pansfignft pedgstvgvg mpvsinfdkp
      181 vknkadvesa invasssnqk vvghwfndkr ldfrpqkywk ansevtmelg ldgveaspgv
      241 kgiqnktvsf hvgrsqistv dakahtmtvv rdgrtlktip isagsdenat yngkmviser
      301 fkqtrmngst vgfkkhngkg eydipdvpha mrltssgtfi hgnywgkgif gkantshgci
      361 glkdakgakd sktdgawffd hsqtgdvvdv inspdksvkp dnglngwnmd wsqwvagsav
      421 q
//
LOCUS       WP_457694483             302 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694483
VERSION     WP_457694483.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31470
     Region          13..294
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mnnktdtpvk tdtpvsvigl glmgqalaga flkaghpttv wnrtaskadq lvaegarlap
       61 tvgdalkpgs ltiicvtdyq amhellgasd ieldgtmlin ltsgdsaqar eaahwaeqrg
      121 aryldgaima ipsaigtaea vilhsgpqsd feshkstlda lgtvtylgad hglaslydva
      181 glammwsvln awlqgtallr tagvdaatya pfarqiaagv aewlpghaeq idsgsfpaev
      241 asletharsm dhlieeseav gvnaelpkli kamadrsiaa ghggeqypvl ieefgkprra
      301 vp
//
LOCUS       WP_457694489             189 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694489
VERSION     WP_457694489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  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 189)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21156
     Region          39..131
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
     Region          <78..189
                     /region_name="COG2521"
                     /note="Predicted archaeal methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:442011"
ORIGIN      
        1 mtmnryhqwl cnsrmwarav erdllpwale dvqlgaetle igpgygattr vlerraggrl
       61 svlevdggsa erlraeygdr idvvhgdgca mplpdgrfda vvcftmlhhv psprqqdqlf
      121 aeafrvlrpg gvfagcdgra grgfrlihlw dtyvpvppgt lpdrlraagf rtpdislrhd
      181 yfrfravrp
//
LOCUS       WP_457694487             296 aa            linear   BCT 27-JAN-2026
DEFINITION  AraC family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694487
VERSION     WP_457694487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 296)
  AUTHORS   Khuri,S., Bakker,F.T. and Dunwell,J.M.
  TITLE     Phylogeny, function, and evolution of the cupins, a structurally
            conserved, functionally diverse superfamily of proteins
  JOURNAL   Mol Biol Evol 18 (4), 593-605 (2001)
   PUBMED   11264412
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   8  (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 14398393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31291
     Region          67..154
                     /region_name="cupin_NimR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to NimR, N-terminal cupin domain; cd06124"
                     /db_xref="CDD:380379"
     Region          73..296
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtttqqgdml yrrtdsgerr pdareqpggh qesdareqpn aheqpggqva ppgppagaav
       61 vvgsfamgrg qwfarhrheh hqlawarqgv lavratgttw vlppsmalwi pagtphatga
      121 agpalfrsly flpdrcpvgw saptvvgvsp llrelisyls dgtldpaare raeavvldql
      181 rpvsvatvqa pmphdprarr vaealranps dgrtlaewga rvgasgrtla rafvtdtgmp
      241 ygqwrtrvrl qaampllagg atvaavaarv gyaspsafva afrravgvpp gayfaa
//
LOCUS       WP_457694485             135 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694485
VERSION     WP_457694485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101108
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..135
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14845
     Region          1..112
                     /region_name="HTH_MerR-like_sg3"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd01282"
                     /db_xref="CDD:133388"
     Site            order(2..4,18,34..36)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133388"
     Site            order(48,51,55..56,65,86,90,96,100,103..104)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133388"
ORIGIN      
        1 mrigelsrrt gvnahqlryy eaqglleadr gangyreyde davlrvkqir hllgaglsse
       61 diayllpcaa geapelpgcp ellaamrsrl qrlddqmdrl aqsrdalavy idaaermgne
      121 syppfddadl epvpa
//
LOCUS       WP_457694493             455 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457694493
VERSION     WP_457694493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  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 455)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..455
                     /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=48152
     Region          142..429
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtrearrape arvrwfglwd syfvicylvt tglvftsavp qtgrvtaiga ltlivpwyag
       61 igrplmlrhe gdrrngvfag glfvlfglat avdltsafal faivpmlmms latrpavvag
      121 vlgnlvpvtm lwlqggatap lmlfvllasl lgialsvllg lwikrvvrqn kehaelieel
      181 rqnrdqvarl shragisaer erlareihdt laqsltsiis lvqaadaeve sapavarkhl
      241 alagrmates laearafvad rtpaslqess laqalrrqad glaaqtglla rfavegderp
      301 lpmavnvvll raaqeagtnv rkhadaravd lvlrygegqv glrvtddgkg fdaaeaerev
      361 aeheatehea tdreateagp ggsgsgdeds gfglrgmaar vaeiggvmsv vsrrgagtav
      421 evkvpldgav grpagpsapr peptgrltea ahdgr
//
LOCUS       WP_457694501             245 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694501
VERSION     WP_457694501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26201
     Region          49..>135
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          94..243
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mprtgsagrs agvdpeqlws qaerprrgrp pthsraaita aavaiadaeg laavtmrava
       61 arigagtmsl ysyvpnketl lelmidqvsg dhrlpaepsg nwrddlrqfa heqrtimrrh
      121 pwlpaalslr qtfgpnalaa leyalaalap agleaaarle tfslltgfvs shvsyelaqe
      181 raveaggrts gelldaqdry lrsvaaegry thlaqaltvp shdsapdavf drlldrmlng
      241 ltaav
//
LOCUS       WP_457694503             294 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694503
VERSION     WP_457694503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30374
     Region          8..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mhsdrpavtv iglgsmgsal aavalerghr ttvwnrsprr aqplvergar laatpeeaia
       61 aspltiacvl dyevlhavld paagslagkv lvnltsgspe qahqaaawar shaadyldga
      121 imttppgvgs pemmflysgs pavfeahrpt laslgdplhl gtdpglasly daallglmws
      181 tmtgwlhgta lvgaektpat aftpvairwl tavagfltty apqvdagryp gddatvdvqi
      241 aaidhlihaa aargidnalp ellksamert kaaghgsdsy asvievlknp aadk
//
LOCUS       WP_457694507             245 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694507
VERSION     WP_457694507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25508
     Region          5..243
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msgikgkvva itgagsgige atalllaerg arlvlgarrs erlaelvari ekaggaavqi
       61 rtdvtrrddl halvalager fgrldvlvgn agvgtispld dlrveewdhm vdvnvkgvlh
      121 giaaalpvfr aqgtghfvtt astaafrvvp amavyagtkf avralceglr qeagdslrvt
      181 tvspgatatd faeastnsrv raeitkmrdd laippdaiar aiafaieqpa tvdvneivvr
      241 ptaqr
//
LOCUS       WP_457694510             137 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457694510
VERSION     WP_457694510.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14660
     Region          <9..112
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mglhgmagae avglsasewy alsqitlegt lssgelaart glttgattrl idrleragfv
       61 rraadpddrr kvvvepvada ldrienvvgp arrqisevls rytpdqravl fdyfahaapa
      121 fraategird aaahrrt
//
LOCUS       WP_457694512             181 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694512
VERSION     WP_457694512.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19831
     Region          1..84
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          90..169
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslrhavlgl laaqpasgyd llktfqssla nvwpatqsql ygelarlads glvavrtegp
       61 rgrkeyaitd agcrelrhwi levepervrr sdtllrafll gsvepehald flqgrataad
      121 erhaelrala astpwgqgdl svygritlew glrfsamqre wadwaagqia aaspavqqkp
      181 r
//
LOCUS       WP_457694515             270 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694515
VERSION     WP_457694515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30704
     Region          10..89
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          118..260
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mplqpdqrrq lgaflrsrra rltpdevglp qtarrrtpgl creelallag isatwytyle
       61 qgreiraseq vltalaealr ldrherahlr qlaghapade pgerdpltpe aaavplllqp
      121 npayiiggny dvlshnpaaa alfprltdne tkqpanflrw vflepvardi vvdwepeara
      181 llarlrtqaa rhpadprytr lideltdhsp eartwwhqye vqprhsghkh lrhpqrgpve
      241 yaytafhlae qreqtlvvyv eeamarqdap
//
LOCUS       WP_457694519              74 aa            linear   BCT 27-JAN-2026
DEFINITION  cold-shock protein [Streptomyces nigrescens].
ACCESSION   WP_457694519
VERSION     WP_457694519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..74
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8047
     Region          1..>48
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mvtatvrewr deegwgvlds petpggcfgh fsdiqtagfr tlspgqqvdl tweapgfkqd
       61 gydyravsiv prsa
//
LOCUS       WP_457694531             166 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457694531
VERSION     WP_457694531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..166
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17725
     Region          7..151
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpttsdmtth tdpalldalq hqvavfarra eqsrlggvgq arnsmdraay lllnrldqeg
       61 pmgvkalaag mgidsstvtr qvaplvdsgl vsrathpedg ravvlqlser grarldevrt
      121 srralmalit eqwseeerta fttlltrfna sladitaslt pagpas
//
LOCUS       WP_457694535             292 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694535
VERSION     WP_457694535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31117
     Region          82..288
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttvtetagg apvrtpqprg gfsrsvrdsl vvakrnlirm iripevvifg liqpimfvvl
       61 ftyvfggsin ipgapvgdaq ayreflmagi faqtvtfata gagagiaddm hkglidrfrs
      121 lpmsrgavlt grtladlvqt altlvvlavv alligwrthe slaevlagfa lllllgyafs
      181 wigaliglsv rtpeaatsgg liwlfpltfi snafvpvngm paflqhvaew npfsatvaaa
      241 relfgntier vpksvtgawp mehpvvasii wslliiavfr tlavrkyrsa aa
//
LOCUS       WP_457694549             208 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694549
VERSION     WP_457694549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22781
     Region          21..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvsartsatt ppgtpkiglr erkkiqtrqa irraayrlfe eqgydatpid qiaeaadvsp
       61 stvfryfptk edivltdeyd avletglrar padepmvesm rrvtvealre iaaadrgelv
      121 qrirlirevp airgrtaent ardaalisav laertgrpad dlelrvisaa ilaalqeaml
      181 nwveggqsae lealinqtmd vlargltl
//
LOCUS       WP_457694545             335 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694545
VERSION     WP_457694545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  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 335)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="MDR family NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35325
     Region          5..333
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(50,132,156..158,178..179,183,199,222..223,244..248,
                     250,277..279,322..323,325,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(51,250,280)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(54,58,238,243..246,249,267..268,271..278,281)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 mthrthrevr ltarpqgpvt ddlfeivevp vpepgpgqvl vrntvmgvaa vmrtlmdets
       61 vvpvpsyevg eplngpalge vvaapgtdft pgdlvehrlg wreyalldad gvhrrdpglm
      121 pdpaaylsqg ptawmgivrg aevragdtvf vtgaaggvgs lagqiarlrg aarvigstgs
      181 qekadrlike fgydavvirg agpieeqlra aapegidalf dnvggeqlva alavanagar
      241 lalvgalssq lsedgkphtt eidtlsllar nitlrgvalh ahidlvpewn qrfgeglrdg
      301 tltfphtrlh gieqapralr eltegrhlga vlvel
//
LOCUS       WP_457694566             259 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694566
VERSION     WP_457694566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28163
     Region          1..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msqtvdrals ilpllaegpa dlgqvadrlg vhkstalrll rtlhehgfvy rqsdqryrlg
       61 arlfalaqqa vesldvreia hphlvelnek cghtvhlavh eenevlyidk vesrypvrmy
      121 srigkpvait vaavakllla dlpeperral aekldyplyt srstpnapaf laelakvreq
      181 gwatdlgghe esincvaapv rgadgrlvaa msvsapnvvv saeellrllp lvrrtadais
      241 reysgtaipp sptgpvqea
//
LOCUS       WP_457694568             493 aa            linear   BCT 27-JAN-2026
DEFINITION  GntP family permease [Streptomyces nigrescens].
ACCESSION   WP_457694568
VERSION     WP_457694568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Peekhaus,N., Tong,S., Reizer,J., Saier,M.H. Jr., Murray,E. and
            Conway,T.
  TITLE     Characterization of a novel transporter family that includes
            multiple Escherichia coli gluconate transporters and their
            homologues
  JOURNAL   FEMS Microbiol Lett 147 (2), 233-238 (1997)
   PUBMED   9119199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..493
                     /product="GntP family permease"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50402
     Region          31..493
                     /region_name="GntT"
                     /note="H+/gluconate symporter GntT or related permease,
                     GntP/DsdX family [Carbohydrate transport and metabolism];
                     COG2610"
                     /db_xref="CDD:442022"
ORIGIN      
        1 mylaattaap appppphtgg llalipgtag lltvaalgia lllvliikvr lqpfvalltv
       61 siavglaagl svtelfgtvq ksdavsliet gmggilghva iiiglgtmlg ailevsggae
      121 vlstrllrlf gekreplamg ltglifgipv ffdvgifvla pivyaaakrs gksillycmp
      181 llaglsmtha flpphpgpva aaglfkvdlg wvilmgiicg ipavlaawgy aawigkrlfv
      241 dvpqdmveaa eearaavsae kaaagitare epvslgtvlt iigtplllil latfssiala
      301 pspgrsvief fghpfvalsi allmsyyllg trrgwsrksl etvstaslkp vgniilvvga
      361 ggvfgavlkg sgvatalsdt fhhvglpviv layllslvlr vaqgsatvai vttagivvpl
      421 vegqgmppah laliimaisa gsifashvnd ggfwmvskyf giserdtlks wtvlesvlsv
      481 agfgvaavvs lvv
//
LOCUS       WP_457694560             544 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694560
VERSION     WP_457694560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Lai,W.L., Chou,L.Y., Ting,C.Y., Kirby,R., Tsai,Y.C., Wang,A.H. and
            Liaw,S.H.
  TITLE     The functional role of the binuclear metal center in
            D-aminoacylase: one-metal activation and second-metal attenuation
  JOURNAL   J Biol Chem 279 (14), 13962-13967 (2004)
   PUBMED   14736882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..544
                     /product="N-acyl-D-amino-acid deacylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0047420 - N-acyl-D-amino-acid deacylase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58422
     Region          1..542
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdtvfrdvrv idgsgspshr advalsggri aeihhesdsg prpgaarvve gqglalspgf
       61 idmhahsdla llrdpaheak aaqgvtlevl gqdglsyapv dertlaevra qiagwnggap
      121 gdtsldfswr tvggyldrld hgfdgqgiav naaylvpqgt vrmlavgwdd raatadelar
      181 mrqlvaegle qgavglssgl tytpgmyasd aeltelcrvv arydgyycph hrsygagalq
      241 ayeemvaltr eagcalhlah atmnfgvneg rapellalld raldadadlt ldtypytpgc
      301 ttlvamlpsw aseggpeail arlrddttaa rirqvmeveg adgchgvpia wdtieisgvs
      361 dpalahyvgk tvarsaaerg eepwrtarrl liedhlgsti lqhvghednv rrimrhrvht
      421 ggsdgilqgd kphpraygtf pqylgryvre lgvlsleecv ahltgrpaar lrlpdrglvr
      481 egyradlvlf dpetvaagst fdaprtlptg iphvlidgrf vmeegrrtdv lagravrrtk
      541 pgrg
//
LOCUS       WP_457694564             383 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar kinase [Streptomyces nigrescens].
ACCESSION   WP_457694564
VERSION     WP_457694564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40546
     Region          32..337
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(63..64,67,119,135,137,166,198,297,300,336)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(253,258,288,297..299,302,324,328)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mhrsegaepi viqppdvsgt tgpdgapvpv vdvvclgesm vtflprlpgr ladvpsfdra
       61 iggaesnvac tlartghttr wisrvgtdgf gdhlltaiad cgvdvahvrr dplrptgvyf
      121 rtagdratdt hevayyrags aasamtadgl dpaalragri lhlsgitaal sadclgllre
      181 lttrrpgrpl lsfdvnyrpg lwrdtaqarv lldlargadl vfvgddeard awglhgprai
      241 sralpkpqll vvkqgkagat vfrrtgepdf repdgrhdda tttfvpalnv dpvaatgagd
      301 afaagflsat lrglpdrdrl rhghlwaaaa ltvpgdlatp psrpyadrla alddtawerl
      361 hlgpgwtdad vsgrradeev ptq
//
LOCUS       WP_457694557             403 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457694557
VERSION     WP_457694557.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Amadasi,A., Bertoldi,M., Contestabile,R., Bettati,S., Cellini,B.,
            di Salvo,M.L., Borri-Voltattorni,C., Bossa,F. and Mozzarelli,A.
  TITLE     Pyridoxal 5'-phosphate enzymes as targets for therapeutic agents
  JOURNAL   Curr Med Chem 14 (12), 1291-1324 (2007)
   PUBMED   17504214
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   3  (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   4  (residues 1 to 403)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44114
     Region          1..402
                     /region_name="PRK09265"
                     /note="aminotransferase AlaT; Validated"
                     /db_xref="CDD:181738"
ORIGIN      
        1 mqviqstkla nvcyeirgpv leeamrleaa ghrilklntg npaafgfecp peiledilrs
       61 vgtahgygda kgllsarrav mqhyqtkgid lsvddiylgn gvseliqmsm qallddgdev
      121 lvpapdyplw tasvslsggt avhyrcdeqa dwmpdladie rkvtdrtkai vvinpnnptg
      181 avyddellrg iaeiarrhnl ivcadeiydk ilydgvthtp faslapdllt ltfnglsksy
      241 rvagyrsgwm avcgpkahas syiegltila nmrlcanmpa qhavatalgg rqsindlvlp
      301 ggrlleqrdt ayelltqipg vscvkpkgal yafprldpkv ykvkddrqmv ldllraekim
      361 ivhgtgfnwp epdhfrlvtl pskddltdav trigsfldgy gqy
//
LOCUS       WP_457694578             272 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694578
VERSION     WP_457694578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29038
     Region          72..266
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttapieavg trpltviths afltgrllra lwrmptflvi glvqpviwll lfgqlfrsvv
       61 hlpgfaygsg gfltfltpgv vmmtalfasa wagttylqdi drgvmdrllt spvsrgammc
      121 atmahqaiqt viqsliivvi aliagarfpg gvagvgltvl aavlltlvfs alsnavallt
      181 rqqatliais qfttlplmfl ssavmdlhla pawvrniary npvewavvaa rqamsadtdw
      241 savwarlgll avavlvmgvl atrafrayrk st
//
LOCUS       WP_457694580             449 aa            linear   BCT 27-JAN-2026
DEFINITION  M14 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457694580
VERSION     WP_457694580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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 10133673
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..449
                     /product="M14 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_function="GO:0004181 - metallocarboxypeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49093
     Region          128..425
                     /region_name="M14_CPT"
                     /note="Peptidase M14 Carboxypeptidase T subfamily;
                     cd03859"
                     /db_xref="CDD:349432"
     Site            order(188,191,248,265..266,323..324,330,374,396)
                     /site_type="active"
                     /db_xref="CDD:349432"
ORIGIN      
        1 mrprirggrt tvlaallslt laapiaaaqa qdapppgpta gaaqkaelph qyevtgpatr
       61 aertallatg vsidevhtra vvitatraqa ttvrelgytl rklpappgis atphkprikd
      121 fpagyanyhn ydeatkeida lvakypeils kqvigtsheg rnilalklsk nvtkdeqepe
      181 vlftahqhar ehltvemsly llneftskyg sdshvtkmld sreiwiipdl npdggeydia
      241 sgefqswrkn rqpnagssev gtdlnrnwdf kwgccngssd dpgdetyrgp saasapevqv
      301 vtkfvqgrkv ggkqqikaai dfhtyselvl wpfgftdddt gpgmtqddhd afatigknma
      361 atngytpeqs sdlyitdgsi ddwlwgdqki faytfemfps sfgsggfypk dsvipketsr
      421 nreavlqlle tadcvyraig keeqycsgn
//
LOCUS       WP_457694584             352 aa            linear   BCT 27-JAN-2026
DEFINITION  chitinase [Streptomyces nigrescens].
ACCESSION   WP_457694584
VERSION     WP_457694584.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Bourne,Y. and Henrissat,B.
  TITLE     Glycoside hydrolases and glycosyltransferases: families and
            functional modules
  JOURNAL   Curr Opin Struct Biol 11 (5), 593-600 (2001)
   PUBMED   11785761
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Fukamizo,T.
  TITLE     Chitinolytic enzymes: catalysis, substrate binding, and their
            application
  JOURNAL   Curr Protein Pept Sci 1 (1), 105-124 (2000)
   PUBMED   12369923
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Aronson,N.N., Blanchard,C.J. and Madura,J.D.
  TITLE     Homology modeling of glycosyl hydrolase family 18 enzymes and
            proteins
  JOURNAL   J Chem Inf Comput Sci 37 (6), 999-1005 (1997)
   PUBMED   9392855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007435
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="chitinase"
                     /EC_number="3.2.1.14"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008061 - chitin binding [Evidence IEA]"
                     /GO_process="GO:0006032 - chitin catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35970
     Region          <26..349
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
ORIGIN      
        1 mvrarsgrpk trprtglpar llagltaavl tsagivgtgt aqasgihsaa saaapaapaa
       61 vprhavtgyw qnfdngatvq klkdvddayd iiavsfadat gqpgavtfrl dpavgygstd
      121 efkadikakq aagksvilsv ggekgavsvn daasaqnfad svsalmdeyg fngvdidlen
      181 glnstymtqa lksvhdrhgd vvvtmapqti dmqspqneyf ktalgikdfl tavnmqyyns
      241 gsmngcdgkv yaqgtvdflt alaciqlegg ldpsqvgigv pasaraaggg hvapsvvnaa
      301 ldcltrgsnc gsfkpsrtyp glrgamtwst nwdaaggnaf asqvgahvhg lp
//
LOCUS       WP_457694595             446 aa            linear   BCT 27-JAN-2026
DEFINITION  CpaF family protein [Streptomyces nigrescens].
ACCESSION   WP_457694595
VERSION     WP_457694595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..446
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48888
     Region          40..407
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mslkarivap epageareds hmvavyrakl leeidlaems slaaaerrsr lervlghiis
       61 regpvlstae raqlirrvvd ealglgvlep lledasitei mvngpdqvyv eragrvellp
      121 vrfasheqlm qtierivstv nrrvdesnpm vdarlpsger vnviipplal ngatltirrf
      181 praytlaeli gmgtldeqml mllaglvrak fnvvvsgatg agkttllnal sglipdgeri
      241 itvedaaelq lqqshvirle srppnvegkg ritirdlvrn slrmrpdrii vgevrggetl
      301 dmlqamstgh dgslatvhan saedalmrlq tlasmsdvki pfealrdqin savdclvqlt
      361 rhadgsrris eiaildsrgh edyriatvcr fdaepmgadr vvhgrfryfp lprrvaerlf
      421 maseptppaf gvathdaqla trkals
//
LOCUS       WP_457694597             314 aa            linear   BCT 27-JAN-2026
DEFINITION  type II secretion system F family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694597
VERSION     WP_457694597.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33799
     Region          98..311
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mtggndlall aigatllcgl laiagartya agraqrqaiv drladerglp vtgrrrfpsv
       61 dralrgtrfg rrlelrltat gldvtpgefv vymlgtvlal wlvaqatlap ffgpiaalva
      121 iwaafaflnw qrqkriekfi nqlpelsril anatqaglal rtalgmaaee leapageela
      181 kvsdklsvgh sidealgela erlpsrelvv lvttlvlanr aggtvvgslr nltktleerk
      241 etrrevrtql sqvqvtayvv pllgigtlll mnriapgaid rmtssflgql avvvafalyg
      301 lgfffirrls kidv
//
LOCUS       WP_457694603             211 aa            linear   BCT 27-JAN-2026
DEFINITION  OmpA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694603
VERSION     WP_457694603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22569
     Region          105..207
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(109..110,143..144,147,151..152,155,197,201)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mtatqmprgr rvrraprsaa taavalllta altvpvahad ppgvtedssp pvhidpqdpd
       61 lrmvqggkla pskvlniksi veaddgserr qdtndnvtfa lqaevlfgkd saeltpeals
      121 ristigteik kqnatrlrvf gftdnlgsas hglvlskkra navqqelakd lgssvsfqir
      181 gygeqypiad nsteagrkkn rrvevsfpra s
//
LOCUS       WP_457694610             440 aa            linear   BCT 27-JAN-2026
DEFINITION  PhoH family protein [Streptomyces nigrescens].
ACCESSION   WP_457694610
VERSION     WP_457694610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Clissold,P.M. and Ponting,C.P.
  TITLE     PIN domains in nonsense-mediated mRNA decay and RNAi
  JOURNAL   Curr Biol 10 (24), R888-R890 (2000)
   PUBMED   11137022
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Kim,S.K., Makino,K., Amemura,M., Shinagawa,H. and Nakata,A.
  TITLE     Molecular analysis of the phoH gene, belonging to the phosphate
            regulon in Escherichia coli
  JOURNAL   J Bacteriol 175 (5), 1316-1324 (1993)
   PUBMED   8444794
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47885
     Region          10..435
                     /region_name="YlaK"
                     /note="Predicted ribonuclease YlaK, contains NYN-type
                     RNase and PhoH-family ATPase domains [General function
                     prediction only]; COG1875"
                     /db_xref="CDD:441479"
ORIGIN      
        1 mvnikqrren drrtyvldts vlladpgama rfdehevvlp vvvvteleak rhhpelgyfa
       61 rqalrlldey rvqfgrldap ipigglggsl rvelnhsdpg ilpagfrlgd ndsrilavar
      121 nlqaegydvt vvskdlplri kassvgllae eyraelaitd sgwtgmaelt isadqvdelf
      181 aaetaqvpev selpvhtglv lqsergkalg rvtsdgavrl vrgdrevfgi hgrsaeqria
      241 ldllldpdvg ivsmggragt gksalalcag leavlerrqh rkvmvfrply avggqelgyl
      301 pgseaekmsp waqavfdtls avttkdviee vvgrgmlevl plthirgrsl hdafvivdea
      361 qslernvllt vlsrigansr vvlthdvaqr dnlrvgrydg vvavveklkg hplfahvtln
      421 rserspiaal vtemleegri
//
LOCUS       WP_457694617             209 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457694617
VERSION     WP_457694617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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 209)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22701
     Region          31..186
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(36,52,94,122..123,135)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 msaaaaegpy agehrpltll eqadqlmkql pghrveilgg vltvtpppdp ahakglsrlr
       61 rpfvaagldg geteileglg lwlpdgpenf avpdlcvvda diedriiqye ccdpaafrmv
      121 leitsgnysn dlrtkvtayg sarvpvyviv drkherlhvl tepmedgyav hrihvagekv
      181 tlpesigaev tldvaqtldd arrrtpqrp
//
LOCUS       WP_457694618             199 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrofolate reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694618
VERSION     WP_457694618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..199
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21448
     Region          2..193
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrrlvycias tldgfiagpd gadptspdgf wpiaddyvkh laaelpevlp vqarsalgit
       61 degtrfdtvl egrrtyeigl ragltdayph lrhlvfsrtm aespdpavel vatdpvakvr
      121 elkdadgkdi wllggselag alypeidqli vklspltlgs giplfsrdta fdprtwelte
      181 htvlqsgaaf ltytrgava
//
LOCUS       WP_457694624             229 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694624
VERSION     WP_457694624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..229
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24316
     Region          1..221
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtpegsllaa eglykaygat paldgaefsi hpgevvavmg psgsgkstll hclagiispd
       61 agtvrygpht ltglsdaqrs alrrtdfgfv fqfgqlvpel talenvalpl rlngtkrkea
      121 erqarewler leveavhdrr pgeisggqgq riavaralat rprvifadep tgaldslnge
      181 rvltlltnaa resnaavvlv thearvaays dreivvrdgk vkdmlagli
//
LOCUS       WP_457694632             753 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694632
VERSION     WP_457694632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..753
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=80038
     Region          17..657
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mgraearrar qgsarrakpk etksgirrff twkkllgafl gvcllgilgf iglylyvdip
       61 kgnsaaklqs nvykysdgkv marvgdvnre svpidripkp vqrtfvaaen ktfyddsgvd
      121 lkgtlrgvln tlrgqgkqgg stitqqyvkn yylsqeqtvs rklqeivisl kvdnkfsken
      181 ilagyintsy ygrgaygiqa aaqayygvdv ekltvsqgay lasllqapsq ydwtsatkag
      241 qkrvkerway tldnmvemkw lpaadrakqk fdvpqapkpl pgvsgqtsyl vkqakqelfa
      301 qgvdetefea ggwtvtlgid kkkqqaleks vkrkltddld pkerkvdgda qlgatsvdpk
      361 tghivamygg dgypkhytnn atrsdyqpas tfkplilasa mennavtqdr lpinpntiyd
      421 grnrrpvvgg niafappned ekqygkisvq tatndsvnav faqmgadvgl eeikktavdl
      481 gmdgskidak pamtlgtmga splqmagaya tldnhgkkvt ptlvkkavhp vngvqtdvpl
      541 kdpigdqvls rrtadtltsv ltgvvndgta sdavrntaye aagktgtsdd nksawfvgyt
      601 pklvtavgmf gespkggtqv slkgtggggr vngggyparv wadytesalg gstgaefdle
      661 tdlgagvppt ptptpsktps tspspsetps ktpsqtpssp sgrpsdstsg kpsdpatptd
      721 pssspppgge dggdtggrpt ggkpdddslt gfr
//
LOCUS       WP_457694626             174 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694626
VERSION     WP_457694626.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=19423
     Region          1..88
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msightllgl lesgprhgyd lkrafdehfg qdrplhygqv ystmsrllkn glvevdavea
       61 gagperkrya itdagitdva qwlarpekpe pylqstlytk vvlalltgrd aaelldsqra
      121 ehlrlmrglt erkrtgdlad qlicdhalfh leadlrwlel taarldklae avrp
//
LOCUS       WP_457694634             487 aa            linear   BCT 27-JAN-2026
DEFINITION  catalase [Streptomyces nigrescens].
ACCESSION   WP_457694634
VERSION     WP_457694634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55036
     Region          9..481
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mtstahnvpr ttnnagvpve sdehsltvsp dgpillqdhy liekmaqfnr ervpervvha
       61 kgagaygffq vtndvsqftk adlfqpgktt emlarfstva geqgspdtwr dprgfalkfy
      121 tqdgnydlvg nntpvffvrd tikfqdfirs qkrrpdngmr dndmqwdfwt lspesahqvt
      181 wlmgdrgipk tyrnmngygs htymwvnagg erfwikyhfk tdqgidfltq adadriaged
      241 gdyhrrdlfe aidggnapsw tlyvqvmpfa dapdyrfnpf dltkvwphgd yplievgrmt
      301 lnknpedyfi hieqaafeps nmvpgvgpsp dkmllgrlfs yadthryrig pnyaqlppnr
      361 phvpvhsyak dgpmrsepsr aarpyapnsy ggpaadtlry gepagwetgg emvreaytlr
      421 rddddfgqpg tmvrqvldda ardrlvsnvs ghllngvsrp vldralqywr nidknvgdri
      481 ahqvngg
//
LOCUS       WP_457694640             470 aa            linear   BCT 27-JAN-2026
DEFINITION  class II fumarate hydratase [Streptomyces nigrescens].
ACCESSION   WP_457694640
VERSION     WP_457694640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Woods,S.A., Schwartzbach,S.D. and Guest,J.R.
  TITLE     Two biochemically distinct classes of fumarase in Escherichia coli
  JOURNAL   Biochim Biophys Acta 954 (1), 14-26 (1988)
   PUBMED   3282546
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="class II fumarate hydratase"
                     /EC_number="4.2.1.2"
                     /GO_component="GO:0045239 - tricarboxylic acid cycle
                     heteromeric enzyme complex [Evidence IEA]"
                     /GO_function="GO:0004333 - fumarate hydratase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /GO_process="GO:0006106 - fumarate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49959
     Region          10..469
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msdnsafgds dgfrtehdsm gevrvpahak wraqtqrave nfpisgqrle rahiaalari
       61 kgaaalvnge lgvldkeiae avqeaaaeva egrwdehfpi dvfqtgsgts snmntnevia
      121 tlaserlgre vhpndhvnas qssndvfpss ihiaatsavl ddlipalehl aeslerkaee
      181 faevvksgrt hlmdatpvtl gqefggyaaq vrygverlra slprlaelpl ggtavgtgin
      241 tppgfsaavi aevarvtglp ltearnhfea qgardaivet sgqlrtvgvg ltkiandlrw
      301 masgprtgla eialpdlqpg ssimpgkvnp vipeavlmva aqvtgndatv aaagaagnfe
      361 lnvmlpviar nvlesmrlia nvsrlladrt vdgitanter areyaessps vvtplnkylg
      421 yeeaakvakr slaerktire vvleggyver gllseeqlde aldvlrmthp
//
LOCUS       WP_457694642             314 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694642
VERSION     WP_457694642.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35107
     Region          15..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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          90..266
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 makeidpsvs vaalfatrlr rlrlnagltq aqlgrqahth strinqiert tgarptlelt
       61 raldeavgad dllvdlwpyi qqevfpywsr avlerlerat dirqyagstm pgllqtegya
      121 rallslgrtl esaaqleerv aarlgrqvrl yqadgpqlwa lldesvllrp igdrdglhdq
      181 ltrlleaanh pritlqvlpf ssgghsligr sltlarlpng sesayvevad fgqlfdepde
      241 vtaysvtydr lralslppsm sldlirsvme gthhaerips rserrrlaqv qlqqsggrrv
      301 rrgqrrpprp rprp
//
LOCUS       WP_457694659             219 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694659
VERSION     WP_457694659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22768
     Region          2..170
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msadtrtkll agalrtlteq glaktsarsi attagvnqal vfyhfgsvde llaaacgyga
       61 eqrvahyrer farvgslael lelgrelhae eraaghvavl aqllagaqtq prlvpataag
      121 lalwieeieq vlarvlagtp iaafvdvtgl sralaagfvg lelyegvdpe gaqgaldale
      181 qlsgligvle dlgpvaqrav rarirrstgr rgaaapear
//
LOCUS       WP_457694661             365 aa            linear   BCT 27-JAN-2026
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694661
VERSION     WP_457694661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Linder,J.U.
  TITLE     Class III adenylyl cyclases: molecular mechanisms of catalysis and
            regulation
  JOURNAL   Cell Mol Life Sci 63 (15), 1736-1751 (2006)
   PUBMED   16786220
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Linder,J.U. and Schultz,J.E.
  TITLE     The class III adenylyl cyclases: multi-purpose signalling modules
  JOURNAL   Cell Signal 15 (12), 1081-1089 (2003)
   PUBMED   14575863
REFERENCE   5  (residues 1 to 365)
  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 11450078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=39389
     Region          21..308
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Region          178..311
                     /region_name="CHD"
                     /note="cyclase homology domain; cd07302"
                     /db_xref="CDD:143636"
     Site            order(183,185..190,225,227..229,232,276..278,282..283,
                     286..287)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(185,229)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(190,202,205..206,209,213,225..226,271,274,277..280,
                     283)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
ORIGIN      
        1 mrdvpvsdpp gagdegdenn iavrleqlil gadrrytpfq aargagvsmd laarfwramg
       61 fadigqvkal teadvlalrr laglveagll seamaiqvar stgqttarla dwqidsfleg
      121 ltepqdsglt rteityplve lllpeleefl vyvwrrqlaa atgrvvraqd daemvdrrla
      181 vgfadlvgft rltrrleeee lgelveafet tcsdlvaahg grliktlgde vlfaaddagi
      241 aaeiglrlie tmahdetmpe lrvgiafgtv ttrmgdvfgt tvnlasrlts iapkdtvlvd
      301 qafaeelgri gdapvseada aaaekaaeeg tgappptyrf alqpmwqrpv rglgvvepwl
      361 lsrrd
//
LOCUS       WP_457694666             352 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694666
VERSION     WP_457694666.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38137
     Region          14..319
                     /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 mvvtedigvp swdlyelsip ctvfgkpqpd ladpwydlrl cttgkrqqds satgtglslr
       61 tryglddlvg adtvivpsvp dpcvdegrpl ptalitalrq aydagarmvs lctgafalae
      121 aglldgrrat ahwmhtaqla erypkvqvdd svlyvddgdv ltsagltagl dlclhlvrrd
      181 lgahvanqla rrmvvpahrp ggqaqfidls vpttddgslg pvldwarahl dqpltvedla
      241 rraamsprtl hrrlqaatgt tplqwllnqr lgraqnlles tdlpiekvge lsglgtannl
      301 rhhflkqigv spsnyrrafp rtmpepsppr wragpraera dggltaahpm pr
//
LOCUS       WP_457694670             160 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Streptomyces nigrescens].
ACCESSION   WP_457694670
VERSION     WP_457694670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..160
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17211
     Region          5..157
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mvvneaelrh lrrcvelate aleagdepfg svlvaadgtv laedhnrvas gdrtrhpefe
       61 larwaaanmp peeraaatvy tsgehcpmca aahgwvglgr ivyvssseql tawlaelevp
      121 appvrtlpir divpglvveg pipglaeqvr dlhrrfygas
//
LOCUS       WP_457694677             276 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694677
VERSION     WP_457694677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30578
     Region          5..66
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(11,15,40)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,39)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,33,36,40..41)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnrgelgaal ralrqasgke akavarsavm sasklskiet akaapsvldv eriltaigvs
       61 devkeeylea vraaateata wrlirrmgvh kaqqqtrale aqmavlrlfq palvpgllqt
      121 peyirailsr hdlgedvlak tisarierqq vlydstkglh fvitepvlrw rivtdsrmae
      181 qidriaslsr lphmdirivp lsarqhdman hafavrddrt vsvetvhaev vvtdprdval
      241 yvrkfedfaa malsgdears llesirdgfl heqets
//
LOCUS       WP_457694679             228 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694679
VERSION     WP_457694679.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25132
     Region          12..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttgtrrrmg veerreqlia valdlfshrs pedvsideva eaagisrplv yhyfpgkqql
       61 yeaalrraae eltarfveph egplgarllr vmerffdfva ehgpgfsalm rggpaigstr
      121 tgamidgvrq aayeqilahl gipdpaprle lvvrswvsla ettallwldg rrvpraeler
      181 qlvhdfaala avsaayderm advvrqilad epadgmfadl vvrlgkfs
//
LOCUS       WP_457694681             304 aa            linear   BCT 27-JAN-2026
DEFINITION  metal-dependent hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457694681
VERSION     WP_457694681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10562449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="metal-dependent hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34084
     Region          20..278
                     /region_name="Metal_hydrol"
                     /note="Predicted metal-dependent hydrolase; pfam10118"
                     /db_xref="CDD:431068"
ORIGIN      
        1 myntaslrpq paasehtplk prnvafdwad tplhwipgdp fsthtinvlh lllpagerwf
       61 vhvykqvlpy irdprlredv igfigqeamh sqahdevlph lkeqgldpap ytaqvdwlfe
      121 kllgdrtlpp grarrwwlle rvaliaaieh ytaflgdwvl naraldakga dptmldllrw
      181 hgaeevehrs vafdlfvhld ggyrrrvrtw ataftalvfl wqrgtrffmt ndpsladgka
      241 sfpefvragr rgvlpttgam arsipqylsr tyhpsqhgnt eqavaylags paataaeart
      301 tgga
//
LOCUS       WP_457694680             364 aa            linear   BCT 27-JAN-2026
DEFINITION  PDR/VanB family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694680
VERSION     WP_457694680.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38643
     Region          59..267
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(97..98,100,114..116,122,124..125,165,266)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(97,99..100)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(122,125,128,135)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(157,161..164,166)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(162..163,186..188,240..241)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          282..364
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mprtprvrtv vlvaaaalaa rralrrrvqa splwplpale ppvsgqgrka aetrqltvve
       61 rteeaagvvr lrlageglpa wepgahldlv lpsgtvrqys lcgepaspgs ytiaarlied
      121 grggsrevhe rlhegttvev rgprnrfplr dspayvflag gigitpilpm vrqaeragvp
      181 wqllycgrsr asmpflaelg elagaggdrl tvlaededgr pdlaavlsga psqaavyccg
      241 peplmdavaa llpavteglt lhterftaaa pspaggnapf evelhrtgrt vavpadtsvl
      301 rairdqalpd lpyscergfc gtcqqrvlsg evdhrddllt daerndslli cvsrahggrl
      361 vldl
//
LOCUS       WP_457694683             211 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694683
VERSION     WP_457694683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23576
     Region          6..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprrrldpa errsqlldtg aqlfaakpyd evfmeevaer agisrallyr yfpnkrdlfa
       61 avyqqaadrl ltrtefdpar pvgeqlragl dahidyfian rhtvlaanrv lagdpviqnv
      121 itdeltelrr rlldstglgd gpgelvpaal mgwlvfvrtl cvdwlthqtf srtelremcv
      181 gallgalrpv mdldrvltgd eehpadsrpa p
//
LOCUS       WP_457694685             458 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105755].
ACCESSION   WP_457694685
VERSION     WP_457694685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 458)
  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   4  (residues 1 to 458)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19948164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..458
                     /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=48124
     Region          10..439
                     /region_name="cztS_silS_copS"
                     /note="heavy metal sensor kinase; TIGR01386"
                     /db_xref="CDD:273593"
     Region          229..457
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnglalrlap rtlrgrlslv avttaallmt vltvafntvm drhlqhqada elgsraaava
       61 ttvdtsgsra rvletvndrl ldanvwiytg trllekppsa aaggtlteaa arlaldadga
      121 cttvtagepr svrlcarsva grrstatvvt aldlapyrns adavllgslv ldsvmlacty
      181 altrlavgra lrpvrtmtdq atewsavgsd erfgaagqpa elarlgasld alldrirtvl
      241 rherqltgel shelrtpltr iivelewwrs rprsgaetra theviaeaaq amrticdtll
      301 ddareearta gtapgvtavl pvlhrlvdrl gtparvtavv daagpdaaad vrpalveriv
      361 spllenalry ahstvtvsaw pvpggvrisv tddgpgvpeg fvgdlfqpgr radpgdghdg
      421 aglglplarr larsvggevt hdpaytpgar fladlpag
//
LOCUS       WP_457694692             266 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694692
VERSION     WP_457694692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10601953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28448
     Region          49..147
                     /region_name="Acetyltransf_5"
                     /note="Acetyltransferase (GNAT) domain; pfam13444"
                     /db_xref="CDD:463880"
ORIGIN      
        1 msmastasta vphpapttap aaapaapadp gytaeiadtr aqiraaqrlr hqvfagemga
       61 tlhsplaghd idavdeladh livthtatgd vvgtyrllpp grsprlysdg efdlgalael
      121 rpslieagrs cvhpdhrsga vmtqmwaala rytllsghry lagcasvpla dggtaathaw
      181 elgrtryaap pelqvtphhp whttlpvper pslaqlppll rgylrigavi cgapahdpef
      241 evadffvvld merlgdryrr yflger
//
LOCUS       WP_457694693             304 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694693
VERSION     WP_457694693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31465
     Region          30..238
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mngpwdvrsd ctpdcaahal prvpaahiar rgaafarsvr raltdgerma epgrlrthar
       61 alldalgihv egadsltvgd gpgtlvvvnh iswldilall avepvtllak revggwpvvg
      121 glarragthf idrthprrlp htvrevsell gagrsvavfp qattwctaea gtfrratfqa
      181 aidagapvrp vtlgytqqgl pstvaafcge dtfagslrrv laaraltvrv tahpaltpwd
      241 ggldrrelaa laaraalggr pvtaatgsga vtaargsgaa rpaaalrpav pvphapsrda
      301 pahv
//
LOCUS       WP_457694695             237 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694695
VERSION     WP_457694695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24152
     Region          20..>154
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mfeqldqlta plqgmlgspw lwlvvllvsg ldallpfmps ettvvlvavl igpdlsllal
       61 lagvaaagal agdclgyavg ryagprasar llrgergrar hlrararver haalliiagr
      121 flpggrvvaa lstgslrfpl rrfvvldavg agiwalgsaa lgglggaalt dspakgmllv
      181 sgiglvaacc agclhrrggp adrgaprrcg pragaasgrg gerrparpgl rqrqegv
//
LOCUS       WP_457694697             209 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694697
VERSION     WP_457694697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 209)
  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 209)
  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 209)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 209)
  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..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /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=21909
     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 mtnlrtltag sataplpaap aphahrhrlr avtpdealps patapaggta hqsaasvael
       61 lnsgatwlpa pqhslpalpg qppmvgylvl vpaeqatata pppaagpeap aptgdalvri
      121 dpeqrtaqiq grpldltyle fellahlvah phrvhtrdql vttvwgyghv gdgrtvdvhv
      181 arlrrklgta hrssivtvrr vgykyvpsi
//
LOCUS       WP_457694708             302 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694708
VERSION     WP_457694708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30673
     Region          1..292
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mttlrigllg tgpwarsvha palaahpgve ltgiwgrrpe aaaalaqvhg trpydapdel
       61 fgacdavaia lppsvqapla vraaeagrhl lldkpvatsv pearaltdaa dragvasvvf
      121 ftarfgeqeg awiaaqaaag gwftahadwl gsvfaddsss pyadspwrra kgglwdvgph
      181 alsvllpvlg daeavtaarg padtvlltmr hssgaastat vglaapataa gvevtlrgta
      241 gittlprrlg gpepayhrav dallaaagtg lpnacdvhfg lrvteilaaa eetlnplmpq
      301 ea
//
LOCUS       WP_457694712             188 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694712
VERSION     WP_457694712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 188)
  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 188)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20873
     Region          1..83
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          92..172
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslphailta llekpssgla ltrrfdrsig yfwsathqqi yrelgkleqa gyiralpseq
       61 psrgqkkefe vlpagraelt rwaggeqdsk pirdalllrm rasavvgrtg ldaelrrhlt
      121 lhrrqlaeyq eiedrdfgaa adpedrlrrl vlragiglet fwvewlaeal aevtdldaat
      181 apgdgtdg
//
LOCUS       WP_457694717             604 aa            linear   BCT 27-JAN-2026
DEFINITION  choline/carnitine O-acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694717
VERSION     WP_457694717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   van der Hoek,M.D., Madsen,O., Keijer,J. and van der Leij,F.R.
  TITLE     Evolutionary analysis of the carnitine- and choline
            acyltransferases suggests distinct evolution of CPT2 versus CPT1
            and related variants
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (8), 909-918 (2018)
   PUBMED   29730527
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10466051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..604
                     /product="choline/carnitine O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65754
     Region          14..588
                     /region_name="Carn_acyltransf"
                     /note="Choline/Carnitine o-acyltransferase; pfam00755"
                     /db_xref="CDD:459926"
ORIGIN      
        1 mttfaqedsl prvplptlea scerflawca plltaderaa teaevaaylr pggpgrvlqt
       61 aleeydateg vhswldtfwp yrylgrrdri alnanffflf qdpdpgqpqs qveraaglia
      121 gavgykrrld qeliapvvqr gvpqsmvqnk ylfsatripg aeqdtvrspy tdawpgpsea
      181 rhivvfhrgn mfrmevlgtd gvphslddle aglcavqkag aepaaagtsv ghlttmarak
      241 waaareslra rhprnadald dietalfcvc ledfapadtq eacdqllygd rgnrwfdkav
      301 slivfadgra ginvehceld gttilsftda llstpaeehs rrsgarsqgl palepvvfel
      361 ddalraqvrs aadafaeyga statrtvsfd dfgsttakal gaspdafvql ayqlahqrak
      421 ghlgatyesi atrqwrhgrt eamrvvtpei qafvaamedp aasadarraa fraaagkhva
      481 rakecqagqa peqhlwelel iqrrrgaelg vteqpalyrt pgwltmrddy lstssapsan
      541 iqyfgfgsts srcigvayvl lpdrfhvyls tplavagqmh afadrlreav aelrellasg
      601 pstd
//
LOCUS       WP_457694719             288 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457694719
VERSION     WP_457694719.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=31072
     Region          2..272
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpevesl arfladhlag rtvdrvypva vhalktydpp vtalergafe gvtrhgkfld
       61 lrvgalhlvl hlaragwvrw sdklpavppr pgkgplalrv rlagpdgagf dvteagsqkh
      121 lavyvvrdpr evpgvarlgp dplsadftpa afralleger rqikgvlrdq svlagignay
      181 sdeilhaarm spfklaakls eeeadrlyaa igatlqeave rshglalkdl kaekksglrv
      241 hgrkgepcpv cgdtirevsf sdsalqycpt cqtggkplad rrlsrllk
//
LOCUS       WP_457694727             168 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457694727
VERSION     WP_457694727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18735
     Region          2..161
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mgqlradafd rfvatrwsal lhlahlltgg drhraedllq ealvklwfaw prvaeqapea
       61 yvrrvlaraa arsarrrwwg erpverlpel peagdvaaav eertrleaal allpvrqraa
      121 vvlryyqdls evqvsealgc pvgtarslts rgvtrlrqll gdaiepvk
//
LOCUS       WP_457694742             317 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694742
VERSION     WP_457694742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33499
     Region          21..317
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mktesdvvvv vgdgvvlldv agpvqvlhgt gyrvrlasps gravvsdtgi plgvelaled
       61 vsetvdtvmv pgypplnghg hppelvahvr rlgtgarrtt sactgaylla eaglldgrra
      121 tthwaecetl arrfprvrve pdaiyvrdgp vitsagvtag idlalalvee dhgpeaarta
      181 akhlvvflqr pggqsqfsvr savtpprnag lrrvldavva dpggnhtlaa maerlavser
      241 hltrlfrrev ggtpgqyver vrveaaqaml escdagvnti artcgfgtde tmrrvflrvl
      301 gappaayrar fratssa
//
LOCUS       WP_457694746             102 aa            linear   BCT 27-JAN-2026
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694746
VERSION     WP_457694746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..102
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11068
     Region          6..100
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtdqavtfin vieisadqvd efieqwrerv almstalgfr dvrlhrallp darfqlvnia
       61 hwdsveacea aganptvlas vsqaeriasa spglyqvvae cp
//
LOCUS       WP_457694752             274 aa            linear   BCT 27-JAN-2026
DEFINITION  site-specific integrase [Streptomyces nigrescens].
ACCESSION   WP_457694752
VERSION     WP_457694752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471963
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="site-specific integrase"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=31666
     Region          83..>247
                     /region_name="XerC"
                     /note="Site-specific recombinase XerC [Replication,
                     recombination and repair]; COG4973"
                     /db_xref="CDD:443998"
ORIGIN      
        1 maepydrwhk krpesseekc rphgkvpsre hgrgkrwlar wrdpdgqqqs esferyedar
       61 rhltrmlgtv ddgtyiapkk gdtplkavak qwlenqtfdn prtyhqyesr vrnhiieplg
      121 dlklrqikps tiqtwikrrl qvldettvgl lfthlssila mavdddlipk npcetgsvkr
      181 vkprrskksa kevplsweqt ddlrkhlseq yqatvdcgrg lgmrqgeifg fspddvdwse
      241 ddktvhicrq ithhrgtlvf appkggtkdd pkdr
//
LOCUS       WP_457694754              73 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694754
VERSION     WP_457694754.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..73
                     /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=8479
     Region          19..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mkhteprqdv gkhrralasp qeisdylgip vrtlyqwkyr gigpkvhkvg khlryrwtev
       61 dawlqtqsld lva
//
LOCUS       WP_457694759             417 aa            linear   BCT 27-JAN-2026
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457694759
VERSION     WP_457694759.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001360
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..417
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45328
     Region          51..406
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtsplallgg tpavtdagph ftwppiddit rmkvvsqlds avslpdrsgi vadledalqd
       61 yfdvrhaitt ssgtaalhav ywaarirpgn evivpawtfh atasplfqlg avpvlcetrp
      121 dgnidpgrva elitprtrai mvthlwgkpa emtdlatlar drgldlledg shahgagygg
      181 qrvgtfglag afslnapkpl sggeggfvlt ddddtyyrvl tfahhnkrar neipeghpla
      241 ryavtgaglk lrihplaaal ahnqlsrlda ylagreeiaa ylirelgqip glevspmpeg
      301 vksswyalta tyrpdqlggl pldrfhaalv aegatefdrp gstrplnqlp lyqhpsplfp
      361 gypytrsryr egdfpiaeka hthtiklpvw hrekdlklae qyvsaarkas ehhkell
//
LOCUS       WP_457694757             336 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694757
VERSION     WP_457694757.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36332
     Region          45..259
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkrkenahet tccdhrpwpp grrgsparpa rlqpgrtrrg lrqqpghlap asdtlgvpgf
       61 tragdlldet apdfvvvavp hhagravtee caargvhvlk ekpfatsvee arelagichk
      121 grvelmvtlq rrfnpiyssv agmldqigtp flvgghysfh tpnpgagwrg dlkqagggci
      181 ldmgyhlidl llwyfglpsr viaefsttal peggydaedt avvqlgydsg lygslvlsrw
      241 mapktefmrv vgtagsvvlt kgavqrlald gtvveeltrp hapsvataqi dyfcrvldge
      301 rpnvsgpdqh lshaafiasc yqsktagryi dpkeml
//
LOCUS       WP_457694760             145 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457694760
VERSION     WP_457694760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 145)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15415
     Region          20..143
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mtvtsdlart laeeaeaegi ttfvaaaavt dgdlillvrr kpddfmgglw eipsghvdag
       61 esildaarre tleetgltva svdrylghfd yensrgtttr qfnfavtvse tgpviltehd
      121 lhqwaalagd lpgvtdgvre vlaca
//
LOCUS       WP_457694777             335 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694777
VERSION     WP_457694777.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36544
     Region          1..334
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mraarlikmv lllqarpsmt gaelarelev sertvardvl slseagvpvy adrgraggyr
       61 liggyrtrlt glgrseaeal flsgvpsalr emgladaasa arlkvsaall pelrdaatgv
      121 aqrfhldapa wyqepetptl lpeiadavwd drritaryrr kdteverele pyglvlkagv
      181 wylaartegd yrvyrvdrft avalkerdrv sgaedsgerf trdasfelpa fwaeraaqfa
      241 rsilreevvl rlstrgvlql pyvteraaar eaiaraqtag gpdeqgrltv tlavesadva
      301 yaqllalgpe geilappglr aqfasaaqrt aalyt
//
LOCUS       WP_457694781             207 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457694781
VERSION     WP_457694781.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23017
     Region          1..207
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtppvvhslr eqirehileg ivsgrwqpge riverriave levsqtpvre alreleslql
       61 iesapnkgvr vrnltaddlk esypvragle qvaaelaagr laedtvaler evaalrqadl
      121 agdgeaqvrh tvafhreivr aagnavllht weslgievwt tlsirwfspe prshaqdhqe
      181 ivdafrrrdp kigallkahv lscaprv
//
LOCUS       WP_457694787             264 aa            linear   BCT 27-JAN-2026
DEFINITION  adenosylcobinamide-GDP ribazoletransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457694787
VERSION     WP_457694787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cameron,B., Blanche,F., Rouyez,M.C., Bisch,D., Famechon,A.,
            Couder,M., Cauchois,L., Thibaut,D., Debussche,L. and Crouzet,J.
  TITLE     Genetic analysis, nucleotide sequence, and products of two
            Pseudomonas denitrificans cob genes encoding nicotinate-nucleotide:
            dimethylbenzimidazole phosphoribosyltransferase and cobalamin
            (5'-phosphate) synthase
  JOURNAL   J Bacteriol 173 (19), 6066-6073 (1991)
   PUBMED   1917841
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001250
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="adenosylcobinamide-GDP ribazoletransferase"
                     /EC_number="2.7.8.26"
                     /GO_function="GO:0008818 - cobalamin 5'-phosphate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0051073 - adenosylcobinamide-GDP
                     ribazoletransferase activity [Evidence IEA]"
                     /GO_process="GO:0009236 - cobalamin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25551
     Region          12..263
                     /region_name="CobS"
                     /note="Cobalamin synthase CobS (adenosylcobinamide-GDP
                     ribazoletransferase) [Coenzyme transport and metabolism];
                     COG0368"
                     /db_xref="CDD:440137"
ORIGIN      
        1 mtetptppap sdalrfafgt ltvlpvrvtr wdraaarggm lcaplaglvv glgaaavgga
       61 llvlgggpll aavgsaavpa vltrglhldg ladtadglgs gkpaedalri mkqsdigpfg
      121 vitllftlla qvaalyelya dswahgalaa avaaviarca ltlasrtgvp aarpeglgaa
      181 vagtvpvpaa llcaalvaag caaagagfgp ygalhtglaa lcglglgelv lrhcrrrfgg
      241 vtgdvfgala esaglaalva ltlg
//
LOCUS       WP_457694796             241 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694796
VERSION     WP_457694796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25559
     Region          25..229
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtdserteta apdgwgagpl repgargrrf daavrgylar hpeatvvalg eglgtgfwrl
       61 dngrlnwltv vapetaavrr mllpdgarrr tvaravtdhr wldavrepqr gvivtapgvm
      121 vrlsppavra llavcaerfp ggalvfdalp rpamalarra agpgggrwpg pvrwgldrae
      181 lprvagahpg ivavrevgpv raphgpagwl rrrmpvlgal tplvcevrft aagspggprq
      241 r
//
LOCUS       WP_457694800            1042 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-N-acetylglucosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457694800
VERSION     WP_457694800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 20657218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1042
                     /product="alpha-N-acetylglucosaminidase"
                     /EC_number="3.2.1.50"
                     /GO_function="GO:0004561 - alpha-N-acetylglucosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0030200 - heparan sulfate proteoglycan
                     catabolic process [Evidence IEA]"
                     /calculated_mol_wt=111904
     Region          53..114
                     /region_name="NAGLU_N"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) N-terminal
                     domain; pfam12971"
                     /db_xref="CDD:463762"
     Region          135..455
                     /region_name="NAGLU"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel
                     domain; pfam05089"
                     /db_xref="CDD:461545"
     Region          463..723
                     /region_name="NAGLU_C"
                     /note="Alpha-N-acetylglucosaminidase (NAGLU) C-terminal
                     domain; pfam12972"
                     /db_xref="CDD:463763"
     Region          <731..1013
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mlgtagaiga gaafggaapa aasgapaarr qerapaydta paraalarll prhadqfalv
       61 plapdgdgdr frvtgrpgri tvsgttpavl ltgvnwylky tcrahlswag dqvelparlp
      121 apaapverat slphrfalnd thdgytapya dwprwerlid alalrgvnev lvtpgteavy
      181 hrlltgfgys daeargwlpa pshqpwwllq nmsgyggpts peliakrael grritgrlre
      241 lgmhpvlpgy fgtvpdgfaa rnpgartvpq gtwaglkrpd wldprtdvft avaaafyrhq
      301 qqllgpadhf kmdllheggd pgdvpvpdaa ravekalrta rpgatwvilg wqdnprrell
      361 davdhdrmli vdglsdldtv tdrerdwggv pyafgsipnf ggrttlgakt hiwaerftaw
      421 rdkpdsrlvg taympeaaer dpaafelfge lawrerpvdr tawfdgyadl rygapddhar
      481 aafaalrtst yaisskdgrp hdsvfaarpn laarsgtvya thtpafdpaa fdtafaalla
      541 vrpalrgsda yrhdltdaar qalanrswql igqlqdayrr kdkdtfrals elwlrlmrls
      601 eevtgahrhf llgpwladar amatgpeeea rlehsarali ttwadratad ggslanyanr
      661 dwhgligevh lpqwqaylde ladalaadrp pktfdwyate epwtrartsh plrptadayr
      721 tarrvhdtla kapyqgtltv tadpaalppg gratltaalr nvnglratgr vdfaltgfea
      781 tasgpvslps vppggtgrah wrvtappgpl ktplhplpyd ltadygpkga prvrttrhgt
      841 lfvagpldpa lrtvttnaav fgqlddrfai hgagadlwka taefgavyrp dsltaggavt
      901 vevtaqdptg pwaragivvr nrltasapgs adalgflnls vtpangvvls ydangdgtld
      961 tyrrltgvta pvllrltrgk dtagsgtytg acstddgatw reiatvtvpg aaarqdtglh
     1021 qsaansatgd ggtaafrrwk la
//
LOCUS       WP_457694806             250 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694806
VERSION     WP_457694806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26627
     Region          <2..243
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvalfvtci ndlllprtgq avvallerlg vevgfpaeqs ccgqpqfntg yrhateplvr
       61 rfdrafrdye yvvtpsgsca amvrdnypri gakaaakgrg reladaaala vpktyeltef
      121 lvdvlkvtdv gayyphtvty hptchglrll glgdrprrll eqvkglelre lpgaeeccgf
      181 ggtfavknaa vsaamgadkv rnvlgtgaea vctvdnscll higgtlarqg savrpvhiae
      241 ilastegsvl
//
LOCUS       WP_457694810             219 aa            linear   BCT 27-JAN-2026
DEFINITION  LutC/YkgG family protein [Streptomyces nigrescens].
ACCESSION   WP_457694810
VERSION     WP_457694810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23456
     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 mssrdvvlar vrraladvpr gegpddppva rdyrrvhgsr taaqdvdlla enladyralv
       61 hrstaeelps lirrllaqrr artvlvppgl daswtagagv trvedrasgt preldavdsv
      121 ltgcavaiae tgtlvldggp dqgrrritlv pdhhlcvvrv pdqvvgsvpe alprlaperp
      181 ltwisgpsat sdieldrveg vhgprtlevi lvdaprtpd
//
LOCUS       WP_457694814              92 aa            linear   BCT 27-JAN-2026
DEFINITION  FmdB family zinc ribbon protein [Streptomyces nigrescens].
ACCESSION   WP_457694814
VERSION     WP_457694814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..92
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9925
     Region          1..>47
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 matyeylcsr cgsfdvklai gtapktygcp vcadaarrvy sspgltltsh avaalhdree
       61 qareapavvs evpprrrvpr rphpalsrlp rp
//
LOCUS       WP_457694824             194 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457694824
VERSION     WP_457694824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 194)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21200
     Region          1..133
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mhqiaadtyl aaavvvhhar vlivrrsyre rflpgawgvp cgkldrgesa esgalrelke
       61 etgllgtiva htgstsflsd yqgrrvhnhq enfvvrpltl dvvlpsadqa yrwalpaela
      121 eagvdaynlt virqalggrl dtaglramta rfghpgpppf sspktlperr vrqgrrpaaa
      181 eswavdprvr rgrl
//
LOCUS       WP_457694828             392 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694828
VERSION     WP_457694828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..392
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=41662
     Region          184..391
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(191,230,268,371,374)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(191,371,374)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(191,230,268)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mneaskslsw nagwsaavqr psegfhknwa qegfadqtvr qivrvtgsgt aariklshry
       61 gtaplelaga tialtdkgaa eragsvrplt fsgarsvrip aggeiysdaa evhvapfesl
      121 tvslyfarpt gpasfhaqay attyraagdq ldaadpavfg ettvswyhla aveladggpa
      181 rddtvvvfgd sltdgfastv dgnrrysdal aerladqgtp rpvlnqgigg nlllndsawf
      241 gdragdrfrr hvldqpgvrs vvvlvglndi gfseielpty rpnpdqppae liagycelir
      301 qahaagvrit gatimpfkga eyhtptaeak rrevnawirt sgefdavadf ataladpsdp
      361 eallpaydsg dhkhpndegy ramaaaidlt al
//
LOCUS       WP_457694830             605 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694830
VERSION     WP_457694830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 605)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 605)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 605)
  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 605)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65488
     Region          21..591
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mrsdepqwtp ppkdpekpvq lrrilalfrp yrarlalvgl lvgasslvsv aspfllreil
       61 dvaipgrrtg lltllalgmi vtavttsvfg vlqtllsttv gqrvmhdlrt avyaklqrmp
      121 lafftrtrtg evqsriandi ggmqatvtst atslvsnlts viatvcamla ldwrltvvsl
      181 lllplfvwis rrvgnerkki ttqrqkqmaa msamvtesls vsgillgrtm gradsltrtf
      241 ageserlvdl evranmagrw rmatigivma ampaliywaa glvlqlggpv fslgtlvafv
      301 slqqgllrpt vsllstgvqm qtslalfqri feyldlpvai tepaepvria aprgevrfen
      361 vtfrydpeaa ptldgidltv paggslavvg etgsgkstls clvprlydvt ggritldgtd
      421 vrdldfdtla rsvgvvsqet ylfhasvadn lrfakpdatd aeiqraaraa qihdhiaalp
      481 dgydtlvger gyrfsggekq rlalartilr dppvlvldea tsaldtrteh avqqaidels
      541 egrttltiah rlstvrdadq ivvldagria ergthdella aegryaalvr rdayltpvdd
      601 qvmap
//
LOCUS       WP_457694834             456 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-amylase [Streptomyces nigrescens].
ACCESSION   WP_457694834
VERSION     WP_457694834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 456)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..456
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48227
     Region          37..368
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(81..82,85..86,121,124,173..176,206,208..209,
                     211..212,234,236,241,295..296,301)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(123,178)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(208,234,296)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          374..453
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mqqrsrvlgg alagvlaaag latfapwssq atppgektvt atlfewkyad vakactdelg
       61 pagygyvevs pasehiqgdq wwtsyqpvsy kiagrlgdrt afasmvsach tagvkviada
      121 vinhmaagsg tgtggtrytk ydypgtyqdq dfhgcrksis dygdrndvqt celvgladld
      181 tgrdyvrtti atylddlrsl gvdgfrvdaa khisaadlaa ikstmrdpgy wvqevihgag
      241 eavqpeeytg ngdvdefryg shlksafqgg hldrlksiad gklgsdqart fvdnwdtern
      301 gstltykdga aytlanvfml aspygspnvy sgyewsdkda gppggsggwt rqhakqaitg
      361 mvgfrnavgs aeltdwwdng gsalafgrgd kgfvalnngd aelkqtftts lpagtycnvv
      421 aaapsacdgh tvtvgddgka qlsvpakgav alhrtr
//
LOCUS       WP_457694836             471 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694836
VERSION     WP_457694836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51940
     Region          70..354
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mneapsqhhd pneagpsrrs vlwtagaaga glglgglsag paaaagpaaa aaspratgrt
       61 migvpferrs tvrvgiiglg nrggsmidlf lavpgvrvva lcdpvkekta kaakkvtdag
      121 qpapavythg ehdfenlckr gdidfvyvat pwdrhfdmak tamlngkhvg vecplalrld
      181 qlwqlvdlse rtrrhcmqle nccygknemr vlrmahaglf gdllhgagay nhdlrglmfd
      241 peyyegpwrr lwhtrlrgdl ypnhgfgpva nymdvnrgdr avrissfgtp alglaayrke
      301 hmpandpswk esyiesdrti slvqtakgrv irlehdvstp hpysrinslg gtkgvfedyp
      361 eriylepdqs ndewgdfsty aewdhwlwke hanppgghgg mdymlvfrlm qcmrlglvpd
      421 fdvydgatwt apvplsdlsi kakgapqeip dftrglwkka rpgmdskkpe e
//
LOCUS       WP_457694844             593 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694844
VERSION     WP_457694844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 593)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 593)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 593)
  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 593)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..593
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63298
     Region          24..593
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 miglappdhd pdapqtlttl pvgspatvrs yvgglirrhr raftvliavn taaviasmag
       61 pyllggvvek lsagardlql ertiavfava laaqtlfvrm vrlrgamlge rmladlredf
      121 lvrsvalppg vleragtgdl lsrittdidr lssamreavp qlaigvvwva lllggltvta
      181 pplalavvia lpllivgcrw yfkrapsayr seaagyaavs avltesvdag rtveahrlga
      241 rrialserri rewtqweryt lflrsvlfpv idlthvlllg avlllggafv lqgwmspgql
      301 ttgallaqmm ieplgmilrw ydelqvaqvs iarlvgvrei apeatdpdrr pdgrdvhade
      361 vsfgyragvd vlrevslrvr pgtrlalvgp sgagkstlgr llagvygprv gsvtlggaal
      421 sampaerire hvalvnqehh vfvgslrdnl llartgaada elwaalgavd addwaralhk
      481 gldtevgsgg htltpaqaqq ialarlvlad phtlvldeat slldpraarh lerslgrvld
      541 grtvvaiahr lhtahdadvi avvedgrise lgshddlvaa dgayaalwrs whg
//
LOCUS       WP_457694850             837 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457694850
VERSION     WP_457694850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 837)
  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 837)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..837
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93017
     Region          10..832
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtlidhlpnd aepdalfeaf sgwaeqqgis lypaqeeali evvsganvil stptgsgksl
       61 vaagahftal andqvtfyta pikalvsekf fdlckmfgte nvgmltgdas vnadapvicc
      121 taevlasial rdgkdadigq vvmdefhfya epdrgwawqi pllelpqaqf ilmsatlgdm
      181 srfegdltrr tgkptsvvrs atrpvplsye yrttaltetl telletrqsp vyivhftqaa
      241 averaqalms inmctraekd eiaqlignfr fttkfgrnls ryvrhgigvh hagmlpkyrr
      301 lveklaqagl lkvicgtdtl gvgvnvpirt vlftaltkyd gsrvrtlrar efhqiagrag
      361 ragfdtagfv vaqapehvve nekalakagd dpkkrrkvvr kkapegfvnw gentfeklia
      421 sdpeplnsrf rvthamllsv iarpgnafea mrkllednhe prknqirhir raiaiyrslv
      481 dggiverlae pdtegrivrl tvdlqqdfal nqplstfala afdlldpesp syaldmvsvv
      541 estlddprqi laaqqnkarg eavaqmkadg veyedrmerl mdveypkple ellfhaygly
      601 rkshpwvgdh plspksvird myeramtfte ftsfyelart egivlrylas afkaldhtvp
      661 ddlksedfqd iiawlgemvr qvdsslldew eqlanpevet aeqaaeradq vrpvtsnara
      721 frvlvrnamf rrvelaaldk veelgemdae sgwdvdawge amdaywdeyd elgtgpdarg
      781 pkllqieeda ahglwkvrqt fadpngdhdw gisaevdlaa sdeegravvr vtdvgql
//
LOCUS       WP_457694852             289 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457694852
VERSION     WP_457694852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  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 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32692
     Region          4..287
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtnpaeklvd lldleqievn ifrgrspqes lqrvfggqva gqalvaagrt tdgdrpvhsl
       61 hayflrpgrp gvpivyqver vrdgrsfttr rvvavqqgrt ifnltasfhk pepgfdhqlp
      121 mrrtvpdped lptvadevre hlrelpegle rmarrmpfei ryvdrlrwtp deiegaeprs
      181 pvwmravgpl gddplvhtca ltyasdmtll davripiepl wgprgfdmas ldhamwfhrp
      241 fradewflyd qespiatggr glargriydq egrllvsvvq eglfrklgg
//
LOCUS       WP_457694858             204 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694858
VERSION     WP_457694858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=21766
     Region          17..199
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mnaaqgapeg aapgldaelt lkilvaggfg vgkttlvgsv seihplrtee rlseagetvd
       61 dtggvdlkgt ttvamdfgrv tirqglslyl fgtpgqdrfw flwddlsega lgavvladtr
      121 rlqdcfpavd yferrsipfl vavncfaesr sygadevara ldldrgtpvv lcdardrdsg
      181 kevlvrlveh agrrhsarvl dsvg
//
LOCUS       WP_457694856             142 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457694856
VERSION     WP_457694856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15478
     Region          12..134
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mahkmtkdew qrflsegtrt gklatvrddg gphvapvwfl mdgdelvfnt geetvkgrnl
       61 ardgrvalcv dddrppfsfv vvqgaaeisn eladvrhwaa riaarymgee qaeeygarng
      121 vpgelvvrvk idkvialadv ag
//
LOCUS       WP_457694860             203 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694860
VERSION     WP_457694860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21303
     Region          16..147
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtdhhadhph evraffasra atwdtkfpdd gpayaagvae lglqageqvl dagcgtgral
       61 palraavgpr gtvlgadltp emlqaavrag rdrdtalllt dvarlplpda aldavfaagl
      121 lshlpdsagg ltelartvrp ggrlalfhpi graalaarkg rpitpddlra epnlrplltd
      181 cgwdlvryed edarylalav rqg
//
LOCUS       WP_457694862             298 aa            linear   BCT 27-JAN-2026
DEFINITION  oxygenase MpaB family protein [Streptomyces nigrescens].
ACCESSION   WP_457694862
VERSION     WP_457694862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10561995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="oxygenase MpaB family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34265
     Region          42..226
                     /region_name="MPAB_Lcp_cat"
                     /note="ER-bound oxygenase mpaB/B'/Rubber oxygenase,
                     catalytic domain; pfam09995"
                     /db_xref="CDD:462938"
ORIGIN      
        1 mrrydwlrei rrldperdfl riyriiathe fpwdltrale lalyrtyavp sigrllaeta
       61 eltdrtqkry ddtallldav vehgfdsddg rtairrinqm hrsydisned mryvlctfvv
      121 vpkrwldeyg wrrltaheqh avatyyrtlg rhmgitelpq tyedfeqcld ayeaahfgwd
      181 egarrvsdat ldlmagwygp lapvvrgasm allddsllda fryerpkpav qkavrtalkl
      241 rakavrllpp rrtphyarqn peikgypngf rvaelgtfpa srrtggcpvp hgegpaas
//
LOCUS       WP_457694878             261 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457694878
VERSION     WP_457694878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=28297
     Region          40..261
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mpvskrqrar itrgvqygvl vaavavfali adwhqlrmaf fdvevakalf peiittalvn
       61 tvlytllgfg fglalglvla lmrlssvppy rwlavtyief frgipcllvf ialgfgvpla
      121 fevaldmnit vmlslglvga aymaetirag iqavpkgqte aarslgmsqg ramasivipq
      181 afrivlpplt nelilltkds slvyllglsl tqfelanfgr dalnehkslt piliagllyl
      241 vitlplgqlv rrleartaka r
//
LOCUS       WP_457694880             279 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694880
VERSION     WP_457694880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29957
     Region          19..256
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msgvttdqaa petvdakaid vqglrkafge levlrgidfs vargevvcvi gpsgsgkstl
       61 lrcvnlleep sagrvvvagt evtdpdvdid rvrrrigmvf qsfnlfphlt alenltisqr
      121 rvlrrdrtea eriaranler vglsdkaaay paqlsggqqq rvaiaralsm dpqlmlfdep
      181 tsaldpelvg dvlavmrsla qegmtmlvvt hemsfareva drvvfmdggv iveqgtpeqv
      241 vgapqhertr tflarvldpa aaevgevadt gaagkrvdr
//
LOCUS       WP_457694881             304 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces sp.
            900105755].
ACCESSION   WP_457694881
VERSION     WP_457694881.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   di Salvo,M.L., Safo,M.K., Musayev,F.N., Bossa,F. and Schirch,V.
  TITLE     Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate
            oxidase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 76-82 (2003)
   PUBMED   12686112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1562906
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..304
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004733 - pyridoxamine phosphate oxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33000
     Region          9..112
                     /region_name="YzzA"
                     /note="General stress protein 26 (function unknown)
                     [Function unknown]; COG3871"
                     /db_xref="CDD:443080"
ORIGIN      
        1 malldsapld vldayrtcef atlgrdgtpl awptavrrrp dgtlllstsl afaqkalnir
       61 rdgrvallfs dptgsgleqp pqifvggrae cpdeimtgpq gaedywrmlf erqphsrsyv
      121 tapmrlvmdw yylrllitvt pqqvlvrspl prsaapaapp gelvgaaqla rfptavlaar
      181 dasgapvlar arpvptgegf avdvpadcpa tagpaallvh rhderlnhmh nalvrgelra
      241 agtgwvlvpa kvvepmgsgr vsdavsvlrs trqatdrylr rrglprprvr waefralaqd
      301 arrs
//
LOCUS       WP_457694884             321 aa            linear   BCT 27-JAN-2026
DEFINITION  acetylxylan esterase [Streptomyces nigrescens].
ACCESSION   WP_457694884
VERSION     WP_457694884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11465865
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="acetylxylan esterase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0045493 - xylan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34525
     Region          1..320
                     /region_name="Axe1"
                     /note="Cephalosporin-C deacetylase or related acetyl
                     esterase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG3458"
                     /db_xref="CDD:442681"
ORIGIN      
        1 mftdlpldal htycpprpep agfdafwrrt lvearthdld arftevdtgl tllrthdvtf
       61 agfgghpirg wfllpratar plpcvvqylg ygggrllphd wllwpsagya tlvmdtrgqs
      121 gpnrpgdtpd pvasgnpgvp gkltqglldp dgyyyrrlft davraveaar ghhavdadri
      181 vvaghsqgga aalamtglvp glagalidap flthirrave itdvgpygel tryfagardr
      241 idtalhtldh fdglnfaara tapalfgtal rdevvppstg faafhhyaga kelkvwrfna
      301 hesgggeqra aeiaflrglf g
//
LOCUS       WP_457694894             212 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457694894
VERSION     WP_457694894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /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=23453
     Region          49..204
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mepaprrpar rrlltgaaal aasaaltplt aatagaaahr rtppggaypp vewipaspan
       61 fttadrptqy sietvvvhvt qetyadtlkl fqdpahkaaa hyvvrsadgh iarcvrerhv
      121 awhagnwdyn trsigieheg widdptwftd plyeqsallt aaicdryrip kdrehiighv
      181 evpgtdhtdp gefwdwaryl qlvnevswqh ag
//
LOCUS       WP_457694896             393 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457694896
VERSION     WP_457694896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Goddard,A.D., Bali,S., Mavridou,D.A., Luque-Almagro,V.M.,
            Gates,A.J., Dolores Roldan,M., Newstead,S., Richardson,D.J. and
            Ferguson,S.J.
  TITLE     The Paracoccus denitrificans NarK-like nitrate and nitrite
            transporters-probing nitrate uptake and nitrate/nitrite exchange
            mechanisms
  JOURNAL   Mol Microbiol 103 (1), 117-133 (2017)
   PUBMED   27696579
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Jia,W., Tovell,N., Clegg,S., Trimmer,M. and Cole,J.
  TITLE     A single channel for nitrate uptake, nitrite export and nitrite
            uptake by Escherichia coli NarU and a role for NirC in nitrite
            export and uptake
  JOURNAL   Biochem J 417 (1), 297-304 (2009)
   PUBMED   18691156
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="MFS transporter"
                     /GO_function="GO:0015112 - nitrate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39560
     Region          5..391
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mtvaayrnli lattgcavtf wawnllsplg htfrtglnlt gteaaalvaa pllagslggv
       61 pvgaltdryg arvmfplvsg ltivpvllli pakgsyavll aagcllglgg ttfaigiplv
      121 ngwfpprrrg lalgilgtgt agialsgylt prihrydenl pylvvatala lfallgalmi
      181 sdhpdgplpr tslatrpgrt grrrgtwepa alyaiafggi vaagvylpvy letwyhlgvt
      241 eagtgaagcv lvaavfrplg gwcadrvhpa vvtawslgaa alcaviqafd palnpvgtvd
      301 llviaaglga aagavvalva rvtpqdrigg vagvigaagg lggflpalvl gavhrskgty
      361 slgflllsdl alaggvyalv rmrtadaapa ggp
//
LOCUS       WP_457694917             208 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457694917
VERSION     WP_457694917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22564
     Region          1..197
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mtdfilvrhg etvwhaenry agrtdvaltd hgrdqaaala twaataglta iwssplsrar
       61 qtaapaaeac gltpgvderl yevdfgqgeg ltrdemrrrf peqlaaflad pvehhlpgge
      121 hprhaaeraa dclaelaraq phgrillvah stlvrvllch llgipladyr rvfprldnga
      181 rteiriengq tallsfnapa partaalh
//
LOCUS       WP_457694919             502 aa            linear   BCT 27-JAN-2026
DEFINITION  FGGY-family carbohydrate kinase [Streptomyces nigrescens].
ACCESSION   WP_457694919
VERSION     WP_457694919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..502
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52592
     Region          16..443
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 msdprhngaa paldgiwfgl dlgtqsarcv avdgtgqvla taarpltgrr dgnrheqdpe
       61 ewwraigaac realdgidtr rirglaidgt sgtilladhr gtprtpglmy ddgraaapaa
      121 avnaagekvw qelgyrsmqp swalpklval leddpglrtg srllhqvdli twrlagrqla
      181 sdashalktg yhlveerwpq evmaelgvpe gmlpdvvrpg sllgtvcapa aeatgipegt
      241 tivagmtdgc aaqigagala pgawnsvlgt tlvlkgssph lvrdpagvvy chrgpggtwl
      301 pggasssgag ilsqrfpgad ldaltaqaaa ldpdavaypl vagggerfpf rapgaepfll
      361 geaptraaef hacllgvacl erlcfdyldh lgapvdgplt ftgggarnay wcrlradvlg
      421 rpvrlpqqae galgmavlaa tssgtglqea aaamvrtare itprpartar ylpvhlrfid
      481 eltrrgwldr svadharrra ap
//
LOCUS       WP_457694924             261 aa            linear   BCT 27-JAN-2026
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694924
VERSION     WP_457694924.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27927
     Region          7..257
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mdrveaqeer rrrmrdtvia rgfvrtadla eefgvslmta hrdldalqaq gwlrkvrgga
       61 tglpsaqfhg svaermatma qtkqqlaraa atllvpgqtv llddsttcll lahqlsghtp
      121 ltvitnslpa lttlakepgv alitpggayf paydafmgph taeavrafra dvlfmsttav
      181 tngrcyhtsp etvqvkramm esagrrvlva dhtkftkggl yalapltdfd llivddglaa
      241 eqvravragg tevmvvpgqg r
//
LOCUS       WP_457694926             145 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457694926
VERSION     WP_457694926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15856
     Region          18..138
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 miaphpnpae vvlhedvldy tprpksiala rnraarliae wghdqladda kvlvselatn
       61 alrhahvrgr lfrvrlthtd salriavtdt rgeslpcvge ppphashgrg llivrtlsar
      121 wgvhvlgvgk tvwcelelkq nfqvg
//
LOCUS       WP_457694928             444 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457694928
VERSION     WP_457694928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46880
     Region          25..438
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 msnaghiakd rapggarpps rlrqlaaasi gnavewydwy aysflavyfa gqvfpegagn
       61 slvpllstfa vfavgffmrp vggllmgaia drrgrrtalt ltillmgggs llvaltptya
      121 ttgvlaplvl viarlvqgls vggefaastt flvesagpgr rglfssfqyv sttagqllas
      181 gtaallatll teqqmgqwgw rvaflfgall sllglwirrg aqetlpqalh sgetpgakqq
      241 aadrpglfea lrrhprqsll icgitaggti ayytwttylp tyaqvnagfd kgdsltvgtl
      301 slvffallqp lggmlsdrig rkplllgfsl gfavlavpll hlvtdafvsl llvqcagmvl
      361 ltgytsvaaa vnaevfparv raagigfpys ltvalfggta pyvgtwfkqa ghaalfpwyv
      421 aalclvsffv yltlpetarq kldk
//
LOCUS       WP_457694936             425 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457694936
VERSION     WP_457694936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  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 425)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448560
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..425
                     /product="glycosyltransferase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44454
     Region          2..387
                     /region_name="YjiC"
                     /note="UDP:flavonoid glycosyltransferase YjiC, YdhE family
                     [Carbohydrate transport and metabolism]; COG1819"
                     /db_xref="CDD:441424"
ORIGIN      
        1 mlfvvpplag hvnptlavaa elaarghqva wtgptaalap llptgsllyp agdrdtadgh
       61 dlggarwrdl rgiaalrflw aealiplara mlpgvhtave afrpdvlvad qqalagplva
      121 rrhglpwats attsaeiirp fddfpkvgew vtqriaallt ecgapgdwdp rfsphlvlvf
      181 stpaligdgp eralasaqda aggpggvggr ypphyafvgp afgarppagd fpwrrldpgr
      241 arvlvslgtl nraagarfyp avlraadala draqlilaap adlagdipph mlhqeyvpql
      301 qllphldavl chgghntvce alayglplvv apvrddqpiv arqvaeagag vrvrfgrart
      361 delhqaltav ldnpahrrea rriqasfaaa ggaavaadrl eklppgprpg psapgtaptr
      421 nekgp
//
LOCUS       WP_457694934             404 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphodiester glycosidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457694934
VERSION     WP_457694934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gorelik,A., Illes,K. and Nagar,B.
  TITLE     Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme
  JOURNAL   Structure 28 (4), 426-436 (2020)
   PUBMED   32109365
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Das,D., Lee,W.S., Grant,J.C., Chiu,H.J., Farr,C.L., Vance,J.,
            Klock,H.E., Knuth,M.W., Miller,M.D., Elsliger,M.A., Deacon,A.M.,
            Godzik,A., Lesley,S.A., Kornfeld,S. and Wilson,I.A.
  TITLE     Structure and function of the DUF2233 domain in bacteria and in the
            human mannose 6-phosphate uncovering enzyme
  JOURNAL   J Biol Chem 288 (23), 16789-16799 (2013)
   PUBMED   23572527
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468539
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..404
                     /product="phosphodiester glycosidase family protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40432
     Region          <294..402
                     /region_name="NAGPA"
                     /note="Sugar-P-sugar glycosidase (uncovering enzyme, UCE),
                     NAGPA superfamily [Carbohydrate transport and metabolism];
                     COG4632"
                     /db_xref="CDD:443670"
ORIGIN      
        1 mravltvlma wgvlagggva ggapataada glrrsgavsv apgvaygefr mtvprgtvhg
       61 hlltvdladp rvsvdllypg avgarspvsq laaerravga vngdffnite tqhpgvqatg
      121 asvgpavasg rqlkgavpdg qrfgpvmppg attedvigvg ydrrarldrl tlrgavltge
      181 galplrglnq yalpvggiga ytpqwgpasr vratcgtdtd raapctteta evtvrhgrvt
      241 avgevpgagg vavgsmvlvg reegarqlrt lhigepvgvs sylvgqghgr lrcavggfpv
      301 vrdgapvagl dtvavavrts agigaggrvl ylmaldgapg qtgltvrela dlmaqlgard
      361 amdldgggss tlvtgdeyga tvrnhpsgga erpvpnalgv fsag
//
LOCUS       WP_457694950             429 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457694950
VERSION     WP_457694950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45220
     Region          36..412
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(46..47,50..51,54,86,141..142,144..146,149,169,
                     172..173,176,249,252..253,256..258,261,285,289,342..343,
                     347,351,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mlycrvpatt tsekgdiplr srifadltpl rtspdyrrlw cgntiswmgq qmtalavslq
       61 vyslthstfs vglvglcslv plvvfglygg aiadtvdrrt lglysamgat vmslilataa
      121 lagyhrvwll ytvvacqavc famnsparss miprllpteq lpaanalnsl tsnlglmggp
      181 mlggvivglw gyqtaylidv vafsgslyam wrlpsmrpdq gegprrrasv ldglrflatr
      241 pnlrmtffsd laamvlaqpr alfpaiavlw fagdaktvgl lvaapavgav lgglfsgwlg
      301 girrhglail iavaswgaai acfglsrhlw lglfflavag cadtvsmvfr stmlqaatpd
      361 emrgrlqgvf ivvvaggprl gdflagsaad ltspatavig gglacvlavt alglgrrafa
      421 rydardpqp
//
LOCUS       WP_457694958             233 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457694958
VERSION     WP_457694958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 233)
  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   3  (residues 1 to 233)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..233
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25230
     Region          28..204
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 msrgfveady esdeagpedi rldrvgqaea fdaigdryde afpykkgqla aaewvigslp
       61 agsrvldlgc gtglptarql vaagcevvgv dlsrgmvtla reyvpgatfh rvdiadlgpd
      121 gphdlgrfda vvaffsllml praeipgalr tvhdllvpgg lfslsmvead vdyfeipflg
      181 nairvsgylr edlrkvieea dfevveessy tyapeisdvp peeqlflnct rrg
//
LOCUS       WP_457694961             104 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457694961
VERSION     WP_457694961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..104
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11564
     Region          <57..102
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mvgrlqghsv rtctyrikgs arqrnwrrri pgpahgwsvr asypcrdgta raakfpfdfa
       61 vddldqaetl llewgavkpd sqpgggrwrv fidpaghpfc ltrs
//
LOCUS       WP_457694959             576 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding SpoIIE family protein phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457694959
VERSION     WP_457694959.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 576)
  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 576)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18599219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..576
                     /product="ATP-binding SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=61828
     Region          11..439
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          451..561
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 megprgsaap apetqtddrl rflevasqri argvdldetl relrqaaipa fadamlvhlr
       61 hplptgegea aeplvlrlhs vaqgpegavt aappgaaelm qltvtgrfva fllarqpafg
      121 dapeiapava ellepvasmp tppspgrrli ivplygrrhl mgtvallrga drpaftsddl
      181 fvasqlatya asgvdetmly ghdasvadel qltmlpsslp ettgvrlasr ylpaagttqv
      241 ggdwydaipl pgnrvalvvg dvmghsltsa aimgqlrttv qtlarldlpp eevlyhldeq
      301 aqrlgsehma tclyaiydpi sqrlqvadag hpppvllhad gsgevlqvpp gapigvggvp
      361 fetvempapt gatlllytdg lvesrnmdvw tgvellrtrl eaaallaspp letlcdavlt
      421 lldpdarddd valiaarfdg fpprnvaywf lspqpqtagr arqltrralh rwglgpmlda
      481 telmvsevvt navryasrpi alrllrtevl rcevgddspq lprmrraqag deggrglflv
      541 dqlsqrwgat mlstgkvvwf eqqipeeyrq ngpdap
//
LOCUS       WP_457694976             469 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457694976
VERSION     WP_457694976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..469
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49928
     Region          12..463
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mstgtvrddn ttrdgapaap gglqrglkrr hmqlialggv igaglfvgsg vvirstgpaa
       61 vlsflaagvl tvlimrmlae mtvarpalgs fyahvrealg lragftvgwl ywyffvivva
      121 veavaggriv qlwlpdvplw avslvlmtll tatnmvsars ygefeywfss vkilaivvfl
      181 flgalfvlgl wpdapgglgn ltahggfape gvgavlaavv pcigfftgae ivtiaaaesv
      241 eperavadai rsivlrvvaf yvlsvflvvt vvpwtskaie vspyaavldr lavpaagtvm
      301 nalvliavls clnsalytss rmlfaltrng daprgftkvs asgvprrall agtsagylsv
      361 iaawispdvv frflinsyga valfvylaia vaqvrmrrkl erteperltl kmwlfpwlsr
      421 ltialmavvi gamawlpdsr sqfwlslltv avvpagyelr rrkgpadav
//
LOCUS       WP_457694982             474 aa            linear   BCT 27-JAN-2026
DEFINITION  lipase maturation factor family protein [Streptomyces nigrescens].
ACCESSION   WP_457694982
VERSION     WP_457694982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Doolittle,M.H. and Peterfy,M.
  TITLE     Mechanisms of lipase maturation
  JOURNAL   Clin Lipidol 5 (1), 71-85 (2010)
   PUBMED   20543905
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10535984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..474
                     /product="lipase maturation factor family protein"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          121..463
                     /region_name="LMF1"
                     /note="Lipase maturation factor; pfam06762"
                     /db_xref="CDD:462004"
ORIGIN      
        1 mawfsdsgyw lgrlvfqrml avlyvvafla avrqfralig argmlpvpay vamvpfraap
       61 svfhwhysdr ffalwswggv llaaavaaga adavplwasm amwavlwvmy lsivnvgqtw
      121 ygfgweslll eagslavflg naetappvpv mwllrwllfr vefgaglikm rgdrcwrdlt
      181 clyyhhetqp mpgplswffh hlpkplhrae vaanhvaqla vpvllftpqp iagwaavaml
      241 vtqlwlvvsg nfawlnwvti alavsaaapl waqpsaplpa ppvwfevlal latagvlals
      301 yrparnllar qqlmntsyes lhlvnsygaf gsitrvrrei vvegtadavt gpdttwlaye
      361 fhgkpgevrr lprqfapyhl rldwlmwfaa lspayarawf vpfvarllen drdtlrllrg
      421 npfpdlppar irarvfryrf ttwrelrdtg awwhrteere flppvarsal rgrr
//
LOCUS       WP_457694998             389 aa            linear   BCT 27-JAN-2026
DEFINITION  CapA family protein [Streptomyces nigrescens].
ACCESSION   WP_457694998
VERSION     WP_457694998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  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 389)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..389
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=40713
     Region          54..371
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 msaytryaaa allaalavgc tsphpvprpa prptpeptpr ahagapvtkd aggqpftlva
       61 agdvlpsdpe vlatarrdap hdgydyrpil kgvrpvisaa dlalchldap lgplggpftg
      121 hpvlqappqi atalkatgyd scatashhal drgvpgvqrt lealdtvglr htgsardaae
      181 garpallrap ggarvaqlay tygtgggrrp ayapwtvnll dekriikdar aarragadvv
      241 vvspywgtey rtapdarqig laraltaset agrpdidliv gtgahtpqpy ekvngtwvvy
      301 glgdqlsgvm kkphgnwgsi arfrfapphr agegwrvtta eylpqlvqqg arvrvrnlat
      361 tgkhdrirkt igkavlsrga aadglttgr
//
LOCUS       WP_457695001             406 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457695001
VERSION     WP_457695001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 406)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=44714
     Region          22..406
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(68,90..91,178..179,188..189,192,195..196,199,235,
                     238..239,242..244,247,290,292..295,319,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(89..90,97,101,108,157,160,239..240,243..244,
                     247..248,251,289..290,293..294,296,319,347..349,352..353,
                     355..357,360..361)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtlstapapl pveppsgcpf dppvefgtlr tqqpiskial pdgswawlat rysdirtilg
       61 dtrfssdttv hgyplsgmtg ggstenrgfi rrdppehtrl rrmvtrefmv krvealrpei
      121 qriteelcdl meraergahg gvdlvealal pvpslvisll lgvpyddhdv fqrltgtlls
      181 rtvpederea arlelrdyld rlvtakeadp gddilgrliv eqqrtgeigh devaafaall
      241 liaghettan miglsaltlm rdaetaeqlr qepglirgav eellrfhsii rngprrvata
      301 dieidghlir agegvvvavp sanrdesvfp dadrldvrrp naqhhvafgy gihqclgqal
      361 arvelqvvig tllrrfptmr pavpldeipf rtdmaiygch alpvtw
//
LOCUS       WP_457694999             205 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457694999
VERSION     WP_457694999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=22966
     Region          13..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          97..205
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mseqaavrar nprgqgerlr eellraterl leevgsedal slravaraag vaapsiyrhf
       61 sdktelvwat levsyerlae amagaaekaa ddpverlraq lraycryava hpatyrllye
      121 trqtpvdper laghpagllv rswqqaltac edagwrvrgs rseapyvlws avhgrvtlwq
      181 vmpsqkdtgr ldrfvdemlq lller
//
LOCUS       WP_457695003              64 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457695003
VERSION     WP_457695003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..64
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6495
     Region          1..62
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mkitldadkc caagqcvlia pevfdqrded gvvvlldaep pagqhaavre aaaicpaavi
       61 evha
//
LOCUS       WP_457695004             473 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457695004
VERSION     WP_457695004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..473
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47700
     Region          23..461
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtarpiavvg asaaglaaae alrrggwrgp ltligdephl pydrpplskq llhgawepdr
       61 lllrteeqla plgldlrlgt ratgldvatr tltldgrekl gcagviiatg vaahtlpgad
      121 riagvhtlrt ldealalrgg langgtpage gvasggppgg ggvasggppg sggvaagggg
      181 ggrrlvivgn gvlgceaaav arelghevtl vgieatpmaa avgtevgell aeehrargvr
      241 lltgavdgfe tapaapagtd pqvtavrlan gaagggggss lpadlvllai gsrpavewla
      301 dpaldttdgl rcdaycaaap giyaagdvar wdhpvhgrpv rfehrmnate qgmaaarnll
      361 aeltatadat gaaenapape rrpfapvpyf wsdqydlklq aygltagadr veatvldrae
      421 rrilalygrd ghavgvlaag ipprqlralr avvatplpwe earerigaat aag
//
LOCUS       WP_457695008              70 aa            linear   BCT 27-JAN-2026
DEFINITION  EF-hand domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695008
VERSION     WP_457695008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Kawasaki,H., Nakayama,S. and Kretsinger,R.H.
  TITLE     Classification and evolution of EF-hand proteins
  JOURNAL   Biometals 11 (4), 277-295 (1998)
   PUBMED   10191494
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Persechini,A., Moncrief,N.D. and Kretsinger,R.H.
  TITLE     The EF-hand family of calcium-modulated proteins
  JOURNAL   Trends Neurosci 12 (11), 462-467 (1989)
   PUBMED   2479149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10040236
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..70
                     /product="EF-hand domain-containing protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7659
     Region          6..64
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(15,17,19,26,52,54,56,63)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
ORIGIN      
        1 madmekaraa fdrfdadgdg qvtpeefkha maemgdayvt gpvaeavina rdtdsdgrms
       61 fdefwqalqr
//
LOCUS       WP_457695010             320 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695010
VERSION     WP_457695010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33852
     Region          5..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..301
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,238..243,
                     249..250,252..253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 midprlqtlr vlhergtvta taealhltps tvsqqlrqls arlglellep agrtirltpa
       61 alalvehada lfarweeara dlaghadgva grlritgvat aiagviapaa arlreelprl
      121 aveigedpge nrfelllagr adiavvipap ggpppssrlr ssrevppsdd arfvqqplle
      181 epqdllvpag hrfagraaqg valaeadges wiragdpadq hqllltacat agftprvrhd
      241 avdwyavaal vahgfgiclv prlapvperc pvvrvplcge plpvrrflaa vrrgserqpp
      301 iarglaalra aagereakgv
//
LOCUS       WP_457695014             794 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457695014
VERSION     WP_457695014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..794
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86470
     Region          10..783
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mpwlsrtrlr tagavlaaal igsvlavpta qaeppggplt dlvnpfigsq ndgntypgaa
       61 vpfgmvqlsp dtghftgygy gydhirgfsa vhlsgvgcgl ggdlpvlptt gditetdyak
      121 yasgyrhdde sarpgyyrvg ltsyggitae ltatartgkq rytfpatdka nvllntgqsl
      181 hktvstrvev ldsrtvrtai tgrgfcqdtq pytvytitrf drpftsygtw dgdkvtagsk
      241 estaggrhga yarfdtrtdr tveattalsy vdaagaarnl haeggssfdr akaaadaawe
      301 rrlglvktqg gdrtlrrtfy sslyrsflap nigsdvdgry tgwdrkthra kgftyyqnws
      361 lwdtyrtqaq llallapges rdmalsvlri dkesgwlpkw gygtvetnim tgdpvtpflt
      421 nayrqgllrg heeeayaalk knadgvppdg spavgreana pylkdgfapy ikgrphtkpg
      481 dsdfdhgasa tleyalsdam laqmardlgh dkdadryaar aqnyrkifds stgffrarda
      541 qgaftgpadp aksegfhegt swqyqwlvpq dlpgmlrlig gkdkaderld sffayrkllk
      601 dpektarevw vngpydyyna dkynpqnepd liapytylst grpwkttdvv haaltlftda
      661 ptgmtgnddl gtmsawmvls sigvfpvqpg tdtwglstpv fdrveltldr ryypsgrftv
      721 tapgtsaahr yvqsvrldga dhdrtylttg dlrsgrelaf tvgtepsrwg tgehaapppv
      781 gtgsaaqqqs grqr
//
LOCUS       WP_457695022             120 aa            linear   BCT 27-JAN-2026
DEFINITION  recombinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695022
VERSION     WP_457695022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..120
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=13479
     Region          14..>97
                     /region_name="Ser_Recombinase"
                     /note="Serine Recombinase family, catalytic domain; a DNA
                     binding domain may be present either N- or C-terminal to
                     the catalytic domain. These enzymes perform site-specific
                     recombination of DNA molecules by a concerted, four-strand
                     cleavage and rejoining...; cl02788"
                     /db_xref="CDD:445923"
ORIGIN      
        1 mafiydrcas rsyrqlemrm tgcdgytdrm gwvpagrwid lgedaltaqr pkfgalleam
       61 qeraaerevl clvhnwgrls adgperlafq trivkaggws ettfgesdrh grallvgrrt
//
LOCUS       WP_457695026             296 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695026
VERSION     WP_457695026.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31471
     Region          3..296
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mtlnlpqlra flavvdtggf saaaaelgms qsavshavas lereltapll iratpvrttv
       61 lgeqvlphar malsavrsve qlaaeatgtm tgtvrlastp tvcqglvpgl lrhwredqpr
      121 vtvrvfegds gevaawledg tadaavlidp ppatagrcpr sgpgielatd eyrallpreh
      181 pladeprvdi rdleddpfli spngcearvr tihslaglrf spthrvrdla tlismvqagl
      241 gvtvlsevsr slippdlvll plqpqtsrrl vltgpqtrpw hpalrtlaes aaghla
//
LOCUS       WP_457695028             245 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457695028
VERSION     WP_457695028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27021
     Region          53..171
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mdrnirtvdd ilrlldglfa peadrwtsga aswwdgfyad rgravpffva kpdenlvsyl
       61 ergliapgra ldlgcgpgrn alhlaslgfe vdavdlspaa vawaedrare agaeigfhcg
      121 dafdlagtal ggpydlihds gcfhhlpphr risylalldr vlapgghlal tcfaagemgs
      181 elpdrdfyrq srlhgglayt peslrwifsd ltevelrrmq deppespyfg epflwtalfr
      241 rdprp
//
LOCUS       WP_457695034             153 aa            linear   BCT 27-JAN-2026
DEFINITION  universal stress protein [Streptomyces nigrescens].
ACCESSION   WP_457695034
VERSION     WP_457695034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16259
     Region          17..152
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 meenpaaqfe rgtdgpkviv vgidgsdssw raaayaagla rrqasklvlv yvqpvlpaga
       61 amgapvmdat nevaeelmae irraterlqg iyqvrwefht lrgdpyngmv qmaddlkada
      121 vvvgasesag hrimgsvavr lvkagrwpvt vvp
//
LOCUS       WP_457695047             374 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457695047
VERSION     WP_457695047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..374
                     /product="trypsin-like serine 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=38070
     Region          142..348
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 metsergtvp adsagraaed agapapevcp gpggptctgr grdgvplrvt lalgaltvvm
       61 gstvlalgsp srdpflapgd tatgsytatr adgdqaaaav lagpykerpg ppvaarhsgv
      121 maaplsasrp llaapaapsp aigalfspdd dgnpahhcta svvqspagdl ivtaahcvhd
      181 dgfrtrlvfa pglhdgvapy glwvptrihv dprwirdrdp dhdvaflrmr ragraggria
      241 dltgaerirf dtpagrpaql tgypedrdtp vscrhtadaq gaaqlrficp gfpngtsggp
      301 mltdvnpatg tgaligvigg rdeggddlvs yssrfgkdva alyrrataep gprppqpgsr
      361 adasgvrppa aprs
//
LOCUS       WP_457695058             403 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457695058
VERSION     WP_457695058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Amadasi,A., Bertoldi,M., Contestabile,R., Bettati,S., Cellini,B.,
            di Salvo,M.L., Borri-Voltattorni,C., Bossa,F. and Mozzarelli,A.
  TITLE     Pyridoxal 5'-phosphate enzymes as targets for therapeutic agents
  JOURNAL   Curr Med Chem 14 (12), 1291-1324 (2007)
   PUBMED   17504214
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   3  (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   4  (residues 1 to 403)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..403
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=44226
     Region          1..403
                     /region_name="PRK09265"
                     /note="aminotransferase AlaT; Validated"
                     /db_xref="CDD:181738"
ORIGIN      
        1 mqfkqsskma dvcyeirgpv iehadaleea ghsvlrlntg npalfgfecp deilqdvmrn
       61 lsrahgytes rgilsarrav aqhyqqsgmp dvgvddiylg ngvselvsma vqallddgde
      121 ilipapdfpl wtavtslagg kpvhylcdes adwlpdladl askitdrtra mviinpnnpt
      181 gavyprelld gmldlarrhg lmvfadeiyd rilyddavhh haavlapdlv cltfsglsks
      241 srvagfrsgw lvvsgpkqha adyleglgtl aamrlcpnap aqyaiqaalg gqqsiqdlvl
      301 pggrlheqrd rawerlneip gvscvkpkga lyafprldpa vhkihddekf vldlllreki
      361 qvvqgtgfnw prpdhfrilt lpraddldaa isrigrflag yrq
//
LOCUS       WP_457695060             224 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695060
VERSION     WP_457695060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24153
     Region          2..87
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mprrsydqyc avaraldavg drwtllivre llggprrytd lhadlpgvst dmlasrlkdm
       61 erdglatrrr lappgaafvy eltarghall palsaladwg apalderrpt davrahwfav
      121 plmarlarhf tdgidvigia ldegefhvvl gsdgpesgdp dggagyadgp aerpdvrlrm
      181 dtatcaaiay drlslaqgie sgrivvtlpe gsgerqrrkr ttta
//
LOCUS       WP_457695066             298 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695066
VERSION     WP_457695066.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32886
     Region          11..91
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(37,62)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(44..45,56,59,63..64)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..282
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdtpamdspa elgnflrtrr arlqpedvgl vrygnrrrvp glrreelaql agvsvayytr
       61 leqgqshqas egvldalara lrltaderah lralarpgaa prrpavrhdr arpgvrqlla
      121 avadvpalal gprfeilawn rlghaltagh ldfdspgrpq drpnaqrllf ldphtrelyp
      181 drdeetrrav salrvtagqr pddqqlaali gelsmkstef sslwarhvvh nctfgtkrfh
      241 hplvgdleld femmqtpdgs gqgvlmytaa qgspseaalq llaaergpev rvleperp
//
LOCUS       WP_457695045             344 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidylinositol-specific phospholipase C domain-containing
            protein [Streptomyces nigrescens].
ACCESSION   WP_457695045
VERSION     WP_457695045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Katan,M.
  TITLE     Families of phosphoinositide-specific phospholipase C: structure
            and function
  JOURNAL   Biochim Biophys Acta 1436 (1-2), 5-17 (1998)
   PUBMED   9838022
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171188
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="phosphatidylinositol-specific phospholipase C
                     domain-containing protein"
                     /EC_number="3.1.4.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36531
     Region          25..314
                     /region_name="PI-PLCc_SaPLC1_like"
                     /note="Catalytic domain of Streptomyces antibioticus
                     phosphatidylinositol-specific phospholipase C1-like
                     proteins; cd08589"
                     /db_xref="CDD:176531"
     Site            order(42,67,134,199,208,210,240,242)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176531"
     Site            order(42,81)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176531"
     Site            order(43,65,67,134)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:176531"
ORIGIN      
        1 mngkrcvgtv avaaaaviav tgpagaepag ttygtstsvg vhnayekeky pyfadaldsg
       61 aalleldlwt nglgrsfrvs hsnplgnnsn cegaanasel rtkdrnqdfa gcladvkawh
      121 dahpghrpil fkiemkdgfn akggrgpaef dalvreklgd avygpgdlia ghatpdeavr
      181 aggwpsradl agkflielip gtveeknpfd klwtdveyag hlkdlaargq lgrstafpav
      241 hgaapgdpre rytdpalrpw fvvfdgdaat ylngsidtaw ydtrhyllim tdahnvppvm
      301 dgtrpteaea larvkqlaaa hasfatadwy plpsvlktvv prga
//
LOCUS       WP_457695068             332 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH:quinone oxidoreductase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695068
VERSION     WP_457695068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34047
     Region          1..324
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(41..42,124,128,149,152..154,173..174,178,193,217,
                     239..240,242..243,264..266,316,318,320)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkawrvhang epravmrlee vpdpqpgpgq lllrvraanv nfpdallcrg hyqvrpplpf
       61 tpgveicgev lavgegaage sgarvlaqpp lpdggfaerv vvdaatvrpa pealddaeaa
      121 alhigyqtgw fglhrrarlq agetllvhaa aggvgsaavq lgkaagatvi gvvggadkar
      181 varelgcdvv ldrrtddlva avkeatggrg advvydpvgg eayaksvkci afegrivvvg
      241 faggaiptpa lnhalvknya ilglhwglyn tkdpaavdac heeltklaaq gaikpliggr
      301 fplaeaadav qqvadgtsvg rlvvvpgaee ar
//
LOCUS       WP_457695072             384 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695072
VERSION     WP_457695072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..384
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38800
     Region          13..380
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mndgttlpga dpdllysede dalraavrsl ltdrsdpatv laglesdvay dtglwhalat
       61 eigtagllvp eklggagasa reaavvleet grsvapvpyl tsaviavtal lgcdhgradv
      121 aaplaalaeg rtvgvlavpl ptapgglpep asvradasga ltgrvtsvad aaaaelllvp
      181 aqgpdghaly aveasadgvc tdtvtsldlt rplghltfdg ahgrllatgd raratvdral
      241 ltgagllase qlgvaewclt etvrhtaert qfgrpvgsfq alkhrmaalw levasaraaa
      301 rnaadalasg spdapvavav aqaycapvav raaqecvqlh ggigmtwehp ahlflkraks
      361 delalgspgr hrdalaglvg iaap
//
LOCUS       WP_457695079             409 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457695079
VERSION     WP_457695079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41955
     Region          126..177
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          204..401
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(238,266,303,306..310,312,320..324,327,331..334,336,
                     344,349..354,372..374,381,385)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(238,332,334,336,349..354,372..374)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 merrfrkaal wgatvaavla avgpfspahg vprpdptpqp sprgmldamr rdlgltavqv
       61 rtrlaqetda hraaaavrrt lstppagmwf drttgklvva vtgaadaqrv raagavpktv
      121 phsratltal vgqitsragd gvagvtgwgv derangvvvr idrtrhtart agfektvrel
      181 aargkipvtv ersdqtprqq ggtvvggerw mpgsegicsi gfsvtgpgdf qgfltaghct
      241 ltadqaafgk dgsrmgtsne ggghsvngre gdfglvevdq pdwtvsadva gqggapvtvt
      301 gaqeglvgms mchsgqssgw hcgeitrvdq avdygntvie glsftnacsa pgdsggsyvt
      361 qpnapkalgv hsgggaagcg nfggatltif qpvgealekw nlrlktgsp
//
LOCUS       WP_457695080             155 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457695080
VERSION     WP_457695080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..155
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16681
     Region          16..146
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mteatesavg pdaagpftva itvrgyetdt qghlnqsvyl qyaeharwsl lqasgirqst
       61 mvdrrvgpvt vettirylre lragdevevs cafvwgegkt frieqtvrta dgtvaaevsa
      121 vgglldlter kllkdpraaf rdladkpsll gladg
//
LOCUS       WP_457695084             383 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457695084
VERSION     WP_457695084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=40690
     Region          23..336
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mspapaydvv vagggpagca aaltlvhagr tvlladagtg ppkagealvs mgrllladlg
       61 vaepvlgsgh lpchgnlsaw gsaelhavdf lhdpyghgwh ldrplfdrrl raaaraagae
      121 vaehtavrsp srqsdgtwrl alrdraggag ertvrcrwvv datgrgaaia vrsgarrrtg
      181 dqltalhltl gpapqtptdg rslvesdqdg wwytallpsr hrlvayftdp dlpvaaarga
      241 erfrqrllat rhisrragph glttlrpprr apahsahldr vhgdgwtaag daaaafdpls
      301 sqgiltalyt glsagqavda rlhgdraala dyaakvttar tayqhghrav haqetrwtdr
      361 pfwarrqrnl hhnpppmkge tsp
//
LOCUS       WP_457695090             188 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695090
VERSION     WP_457695090.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21369
     Region          8..137
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mavartprhk wideglrala tggpeavqie alakalgvsk ggfygyfsdr ralleemldr
       61 wereitddve arvekeggda karlrhlfai vdtgdgldtd vttdlairdw arhdpavaer
      121 lrrvdnrhmd ylrslfrtfc adedevearc litfslyiad qfmfadngdr sradvheltt
      181 rwlldspr
//
LOCUS       WP_457695092             152 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457695092
VERSION     WP_457695092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 152)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16456
     Region          7..140
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04663"
                     /db_xref="CDD:467548"
ORIGIN      
        1 mtpprirvaa yvirhravpe vlvfdhlgmp eagtqvpagg vtsvegleea vlrevaeetg
       61 lltatvvrqv avedkphpdt gqprrtsfff lqapadtada wdhyvhgdgd dagltfacrf
      121 lplplkqpla daqdawlgri dpcwttvtcd sr
//
LOCUS       WP_457695103             322 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695103
VERSION     WP_457695103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          5..296
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 madwdlkklr ilrtlhelgt vtataealhm tpsavsqqlt glakalgvtl leahgrrvrl
       61 tdaaqlvlrh aeavfaqler adaellgylq geagqvrvga fstaipalvv pavqelrrsh
      121 pglsvavrea eaeaayella egsvdlalsl aahaptprdp kfsrisllad pldvalpagh
      181 plaaepglrl adlagepwif gssgpwsqit ttacenagfv peqahaaadw saiwamvaag
      241 mgvalvprma raggvgagre grrepgsdgv alrvlhadqp rrhviaaarr gsegapgpar
      301 vlaalrqaaa aqppgeetvq ss
//
LOCUS       WP_457695116             362 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695116
VERSION     WP_457695116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37948
     Region          33..315
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfwsaspvaa ahlsaaipgs sgptslddat edatnaagwv qenwgtwlts glqivlilvi
       61 avvlrhvirr titkliermn rtaaaaqgsa lggllvnaer rrqrseaigs vlrsvasfvi
      121 mgtaaltvls vlkinlapll asagvagvai gfgarnlvtd flsgvfmile dqygvgdeid
      181 agvatgtvie vglrvtklrg pngaiwyirn gevkrignls qgwstaavdv miaanqdlqr
      241 ardtittage emskaepwne qlwepvevlg lsevhldtvt isvsaktmpg kalgverelr
      301 wrikhaldta gvhlaprplp edaqaeatdp aagmaapsal nnplspqsla tnpiaspskl
      361 gk
//
LOCUS       WP_457695117             329 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces nigrescens].
ACCESSION   WP_457695117
VERSION     WP_457695117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33494
     Region          8..314
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mgltdtalav dagnsktdva lvavdgrvla targggfrpp vvgtgravdv laplvesvla
       61 qagaaagpvd hlsaflanad lpveearlta eiagrgwart vtvrndtfal lraglpddge
      121 pvgvavvcga gincaglgrd gatarfpalg risgdwgggs cladealwca araedgrgaa
      181 telaralpah fglttmreli ealhlhdipg hrrhelppvl favaasgdri artlvtrqae
      241 evvllagval erlgllgept pvilgggila arhpllhdql tqlltdrapk aaphvvtapp
      301 vlgaaldtld ragaeagayg rvrgwgwge
//
LOCUS       WP_457695121             230 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695121
VERSION     WP_457695121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..230
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24378
     Region          8..230
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mqsvrkgrvs lvetatdeir gqivngtwpv gsrippesal setlgvsras vreavrslvh
       61 sglleprqgd gtfvisddds avalrrrler aelshvtqvr qgldvvaarq aathrtdaql
      121 agieaalarr raalaahdse aftaadaefh vlvaeasdnp vladiyrsls aalreelrra
      181 acldtataap tdphsrltda iraqdpqaav daavlllagh vrdlalpldd
//
LOCUS       WP_457695135             601 aa            linear   BCT 27-JAN-2026
DEFINITION  FHA domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695135
VERSION     WP_457695135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..601
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=60075
     Region          502..601
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mptcpsghqs vaedwcevcg qrmagavppp pslpagflnt ppsqptgqpg pppgqpgppq
       61 gqpgppqgqp gpppgqpgpp pggpgpgfgg pggpdsqggq ggygfpppqp gpgapgpgtq
      121 ggqdgygfpp pqpgpgtqgg ygfpppqpgp gapgpgtqgg qdgygfpppq pqqggpgpsg
      181 qpetcpqcgt preamapfce gcrynfltns ptsyapppgq qpgpppgapg pgtqggqggy
      241 gfpppapgpq ggpqqggqgg ygfpppqpqq pqppqqqgmp pggpgpggfp dqpgpggpgp
      301 ggfpdqpgpg gfpdqpgpga fpdqpgpggf qpgpppgmpg pgpqggpppq qqggddwtln
      361 ppsaqaappp mapappgpgp qapyeqqppp apfppqqqpg pyeqqppfeq qqppyeqqhq
      421 qppyeqqpgp yeqqqmpqqq pgpdqqwngg pgqgpaappq gpppvvgagw vvavapdrey
      481 fmammgrsgp eaaglnlpsy speqvlplan gqiavgrrrn stgespdidl gsapedpgvs
      541 hqhallvqqq dgswavvdqn stngttinlg edpiqpyvpv plhegdrvhv gawttltvrr
      601 g
//
LOCUS       WP_457695142             365 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695142
VERSION     WP_457695142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38402
     Region          49..276
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttrpdgtpp dapvpgaapa spprpaatsl aelerraasr rgrpayghda liacdrlvrv
       61 fatdgvevqa lqgldllvae gelmalvgas gsgkstlmni lagldvptag aatvagrdll
      121 tmdakarlgy rrevvgfvwq qtarnllpyl talqnvmlpm qlrggrrraa rakaaeells
      181 mlsldrcrdr rphqlsggeq qrtaiavala ntpsvllade ptgeldshta eqvftafrta
      241 neelgttivi vthdqavase vrrtvairdg rtssevlrrt erdaatgqes lvareyamld
      301 ragrlqlpae ytsslgmahr vllelesdhi gvwpdhtadg aargrggdag egggvggseg
      361 tgegg
//
LOCUS       WP_457695147             152 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457695147
VERSION     WP_457695147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 152)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16656
     Region          15..122
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mllymsssqp qtrstplhsv svagvvvred grvltirrad ngtweppggv leldespeeg
       61 vrrevyeetg lkvtadrltg vyknmtrgiv alvfrchvdg gheqlsaest avewltsdev
      121 sermgdvyav rvldalddvp hvrshdgrkl ia
//
LOCUS       WP_457695149             259 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695149
VERSION     WP_457695149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 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   4  (residues 1 to 259)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..259
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27750
     Region          8..258
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 massgtassg kpkylqiadd laeqiragsl apgaavpset elmerysvas gtvrkavael
       61 rttqliethh grgsfvrarp pvqrkssdrf rrahrkagka aylaeaeqsg gipsvtvlhi
      121 gpteaspeia drlgvapgak vlarrrryfr dgtpteeats ylpwgivkdi petfaenpgp
      181 ggiyarleeh gymlaeftet vrarlatkae taalalspgs pvihlvrnaa tadgrvvevc
      241 dtlmaadqfv ldyrfpard
//
LOCUS       WP_457695168             360 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457695168
VERSION     WP_457695168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..360
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=37963
     Region          1..345
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtkavvldlf agpggwsegl rhlgtadvgi eldpaacatr aaaghltira dvaayptahl
       61 tgrvsgligs apcqpysaag pgtgrddmpl chqalddlah gndtrrilht gcsdprslll
      121 veplryalal rpewialeev paaeplfvht arhlrtvgys twvgvlnaad ygvpqtrrra
      181 fllasrtrav appepthara aepdslfgpg rqrwvsmaea lgwgatdrpv ptvtagggks
      241 ggaepfptra raalqasrdr gdwvlrngnr skattrsadq pastmafgnn sariewvdgp
      301 nsvritvpea aalqtfrsny pfrgsktkqf eqvgnavppl laaavlapvl vpsnhlevaa
//
LOCUS       WP_457695172              64 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695172
VERSION     WP_457695172.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..64
                     /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=7415
     Region          1..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mkrplperyl tpvdladllg ipvetvyqwr rkhsgprgfr vgrhlrydpe dvrtwvagrm
       61 eeaa
//
LOCUS       WP_457695174             420 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457695174
VERSION     WP_457695174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..420
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46505
     Region          82..403
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maghiqdrwy kvepgpggkp iklrtdrygs glryraryig pdgteksksf pdkqkrraet
       61 wlinieadma rgqyldpqaa rttfreyaer wlaaltidls sraavegrlr lhalpylgar
      121 pigsfqpehi rdwsrqleea vpsasyrrli fdavssvlna avddrlltsn pcrvrsvkap
      181 rpvptrvqpw sasrvfavra glpkryqama dvgggcglrq geifglavdn igelgwlyvr
      241 qqvkkvrgsl vfappkrgkl rdvpldpevs aaltehmkrf ppvevtlpwq tptgpkvthr
      301 lvftsgvgta lwsnafndqt wkpalasagi isvpekgqry aparehgmha lrhfyasvll
      361 dagenvkals lylghsdpgf tlrvythlmp ssetrtrkai samykaagra hdgpetaqaa
//
LOCUS       WP_457695184             490 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457695184
VERSION     WP_457695184.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..490
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51708
     Region          14..468
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtstqvgtnp gddngasgaa peegyerglg srqvqmiaig gaigvglflg aganiakagp
       61 slilmyalag vivffimral gelllyrpvs gsfseyaref lgpffgfvtg wtywlmwvvt
      121 gmaeltaaai yvhfwfpqip qwvtalvflv vlfaanlisv kifgeiefwf smvkvtalig
      181 mivigigvvt fgfsqagdaa avsniwahdg ifpkgigssl mtlqgvmfay lavelvgvta
      241 gesenpektl pkaintlpwr iivfyvgals vilmvvkwte fepgvspfva afakigipag
      301 aaivnfvvlt aalsscnsgm ystgrmlrdl aanteapkal grlsstktpa vaitlsaalm
      361 gigvilnyvv pekafgyvts vataagiwtw lmilishily rravvagrlp assfpapggt
      421 vcswiavafl lmvtvliaid pdsrvslyvg agwavclavg wavlksrnph itakgtsqdk
      481 qlqttgrprg
//
LOCUS       WP_457695190             174 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695190
VERSION     WP_457695190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19011
     Region          42..164
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mlpttmhsae vmvtarhiag wpqernslvp adcwgsaqqv vlqlpalkra vpvcrslars
       61 wldgqrihde dtrylvllvl selftnaiqy sagtritcri srsenllhie vhdrggtpsv
      121 prmrhpgqgq ehgrglelva ksssqwgrrv eadsgctvwa avplaagvrh svap
//
LOCUS       WP_457695197             318 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457695197
VERSION     WP_457695197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=35117
     Region          18..290
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mhgletltms pylagwrlrv vpsighvlvr kvtrrvvnra lhcwiadecg lstvknslav
       61 lvrvleqavr dgvldanpar vagwqqeyqr aqaertaprs lalpdadale rlaatlvqrs
      121 sdgyegwgdi vrfaawtgtr fsevsalqaq didvstwtwq vqhftvsepe glhdrpcrgr
      181 hhrvvplrpa arelaagrle rarhtpparl ftgphrsrft aavlrdatcw ddvvdelghe
      241 hlrrqdlrht gltwmadagl plpllcgaag rppqdtrryl ppdghrlsae shgeppassa
      301 partsgggrt vflhppte
//
LOCUS       WP_457695201             240 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695201
VERSION     WP_457695201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26171
     Region          9..240
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 maspktftki adhfrerils gdlepgakvp tnreisgqwq vaaatvsral qalqvegyir
       61 ttprgtyvad dpvwtlsard rlarvqrvks llaegetsrv taaelvtppl yigelfdldt
      121 gdqvvrrewl agrgktrtvf avtwypaafa alvpdllnta pgrnhgvsak vleitgrtit
      181 harddmharp adareasalg lpvgspilag ahrwsdaegv ieygewclpp rftigyeyqp
//
LOCUS       WP_457695211             339 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457695211
VERSION     WP_457695211.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36515
     Region          8..330
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mhkalfrpvi alialtvlva tagcgtsasq aspvrfggpq sgaalhtgpp ggrslvqwpt
       61 rpisfevesr vggagentpi gvttlhgpks gvtgkvwvwa ppeyyekrna hkgfpvmeal
      121 pgsygypvny wigadlklqe nlarwskngs slpfivvmpv lnpddkqyyd gsdipgrpki
      181 gtwlsqdvpd lvrqnfrtlk trdawavmgs ssggfaalkn vlqhpdtfkv aipngpdivp
      241 dsplwqghaq akrdnnpevl arrlmarggp evylafqdgs rehtvlpkvr kflaryghgp
      301 vhtrlqivpg gthsaatyvr glgegtmrwv sahmqgpta
//
LOCUS       WP_457695215             178 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase, partial [Streptomyces nigrescens].
ACCESSION   WP_457695215
VERSION     WP_457695215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         <1..178
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <7..178
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 tllatnerse qlveglllla rsenkvvdkr pvdlsevaaq avdqsreeah akgvelrgvr
       61 hqvlvqgngv llerialnlv qnavrynvpe ggwvevvtep qpgcavlvva ntgpvvpaye
      121 venlfepfrr lrtertgsde gvglglsivr svvrahdgsi tarpregggl vmrvvlpr
//
LOCUS       WP_457695217             378 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695217
VERSION     WP_457695217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=38657
     Region          2..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"
     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"
     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 mndraaldll vsqgpltrtr igeltglskp tasqllarle aaglvrttgn vtgrpgpnaq
       61 lyeinpaaah laalavdqlg itaavaditg qvlgeervgt daiaedapnr tvqlvaqavd
      121 gglakaglgr tqlhgavigt pgaldpqtgr lryaphlpdw haralkeela evlglpvtle
      181 ndvnlaavae qhdgaaqdvd dfvlvwadeg vgaalvlggq llrgatggag eigymplpga
      241 plsrggersa aradagggfq rlvgapsvie lareygapdv rtvtealahd avraeiarrl
      301 atglaavmav vdpqlivlsg evaqaggeal ralveeeftg lalprpvlrl sriegnpill
      361 galqtaladt rdavfhtg
//
LOCUS       WP_457695219             427 aa            linear   BCT 27-JAN-2026
DEFINITION  6-phospho-beta-glucosidase [Streptomyces nigrescens].
ACCESSION   WP_457695219
VERSION     WP_457695219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Varrot,A., Yip,V.L., Li,Y., Rajan,S.S., Yang,X., Anderson,W.F.,
            Thompson,J., Withers,S.G. and Davies,G.J.
  TITLE     NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases:
            structural insight into specificity for phospho-beta-D-glucosides
  JOURNAL   J Mol Biol 346 (2), 423-435 (2005)
   PUBMED   15670594
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..427
                     /product="6-phospho-beta-glucosidase"
                     /EC_number="3.2.1.86"
                     /GO_function="GO:0008706 - 6-phospho-beta-glucosidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45836
     Region          1..424
                     /region_name="GH4_P_beta_glucosidase"
                     /note="Glycoside Hydrolases Family 4;
                     Phospho-beta-glucosidase; cd05296"
                     /db_xref="CDD:133432"
     Site            order(9..10,12,36..37,41,81..83,106,126,142,144,269,291,
                     296)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(90,106,144,165,194,241,261,291..292,296)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:133432"
     Site            order(164,194)
                     /site_type="other"
                     /note="divalent metal binding site [ion binding]"
                     /db_xref="CDD:133432"
     Site            order(183,186,202,205,310,322,341..342,344,346..349)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133432"
     Site            order(227,229,232..234,246,248..249,354..355,362,366,373,
                     391,394..395,405..406,408,410)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133432"
ORIGIN      
        1 mklavvgggs tytpelidgf arlrdllple elvlidpdte rlelvgglar rifarqghpg
       61 riswtgdlda gtdgadavll qlriggqaar nqdetwplec gcvgqettga gglakalrtv
      121 pvvldiaerv rrrnpaawiv dftnpvgivt rallthghka vglcnvaigf qrtfaallgv
      181 apeqvelehi glnhltwers vriagedvlp ellaahgdal agklrmpral ldhlgaipsy
      241 ylryyyqhda vvrelrskps raaevaaier qlltlygdpa ldekpellsr rggafyseaa
      301 valtssllgd tgdvqivnar ndgtlpflpd davievpatv gstgaaplpv rplepryagl
      361 vahvtayeql aleaallgsn grttdrtdgr davfsallah pligqldqad rltdeliahn
      421 rehltwa
//
LOCUS       WP_457695238             616 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 35 protein [Streptomyces nigrescens].
ACCESSION   WP_457695238
VERSION     WP_457695238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..616
                     /product="glycoside hydrolase family 35 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68290
     Region          46..360
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mtqfsrrrfl saaivggasv gvalgsgrtt faqadsprgl tirgneflld gepfrilsga
       61 fhyfrthpkd wrdrllrmra mglntvetyv awnfhqpyee kadfsgwrdv aafvrtadea
      121 glkvivrpgp yicaewdfgg lpawllkdkd aplrrsdpay eravdawfae llprfvdlqa
      181 trggpiiamq veneygsydd dhahlehlrd smraqgvdsl lfcsngatqe mlkagslpdl
      241 lstvnfagdp tgpfaelrtf qpdkplfcte fwdgwfdhwg eqhhttdpaq taadveklle
      301 agasinfyma vggtnfgwsa ganlsgtayq ptvtsydyds pisesgelte kfhkvrdvla
      361 kyttlpstpl patprrmpaq rvavresvpl mdaldalstp vrhttpvhme algqpyglih
      421 yrtrvrgpqg tkglritglg dralvfgdgr rigtfdrnqp dhtvdftvad asstldllvd
      481 ptgrinfgqs fndpkgisgk vllddeelsd weirrlpldn lsalkfgsgd tptgpafhra
      541 rvhvdtpadg flafpgwdkg mvwlngfalg rywslgpqvt lyapshlwrr grnelvvlem
      601 ertgdrievr sepdig
//
LOCUS       WP_457695234             820 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457695234
VERSION     WP_457695234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 820)
  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   3  (residues 1 to 820)
  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   4  (residues 1 to 820)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..820
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=88894
     Region          25..247
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          263..678
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          689..800
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mdtpvttfse apddpfavhr sasavlddng rvvgwserae allgyapedv lgrpardvll
       61 dprdedvvma avaacmsagg wfgiipvrdr ggtrvelgcr vravaradsg iewflvggta
      121 eqviqwetdr svldgmfrrs piglavlapd lsllrvnrai arfggiptay yrglrigdfv
      181 igrdaetvea rlrrvletge plifteqpcr lrhdpdrelv vsvsafrmqd ptgrilgvtq
      241 mvedvtdryr arrrlallnd vgarigttld vertarelae vavpdladcv svdlpepvtr
      301 geepgqeala pmvrtavrsi speasrvmyp vghtmhpppg apqtrclaer rpvlepvlef
      361 spgwssldpd kvervqelgv hslivvplva rglvlgvvsl wrwrrpepfe eddltlaeef
      421 aaraavcidn arrytqqhqa alalqrsllp sevpehpave idhrylpada tagvggdwfd
      481 viplsglrva lvvgdvvghg ihaaatmgrl rtavhtlanl dlppdevlsh lddlvdrlaa
      541 eqeatderap qvvgatclya vydpvsgrca laraghpppa vvtpdgrvef pdlpagpplg
      601 lgglpfeaae lelpegslla lytdgllagr rrdvdegrel lrgalsdpar sledickave
      661 dallpdrpgd dialltartr claahkvatw elsaeptaaa egrtlavaql ndwglaemaf
      721 ttelivseli tnayrysagp vtlrlirdrh licevsdpss tsphlrhaat tdeggrglfl
      781 vaqlterwgt ryvrngktiw teqpvpsmpg evspnafcgk
//
LOCUS       WP_457695240             249 aa            linear   BCT 27-JAN-2026
DEFINITION  SOS response-associated peptidase [Streptomyces nigrescens].
ACCESSION   WP_457695240
VERSION     WP_457695240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..249
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=27530
     Region          1..242
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrfvstrr pqdlvdlfev trwdpgqald pswnvaptdd vwsvlerver dtgeitrrlr
       61 plrwglvpsw akslsvgakm inarvetvae kpayrrafak rrcllpadgf yewqtvaate
      121 takarkqpyf ispedgqama laglyefwra pdvsdddapg awwttctiit teatdaagrv
      181 hprmpltiap gdwsawldpa hqdpaelral ltapaaghld sravstdvnn vrnngphlld
      241 eiteapsdg
//
LOCUS       WP_457695244             519 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457695244
VERSION     WP_457695244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..519
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54542
     Region          131..>306
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          414..512
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 msltvgvlat tslvvtgcgv sgaaasqpdd akgmntsapv lparftqqkv qwtacgedvt
       61 peavsgaecg wvkvpvdyaa pdgetvklrv srvpakdhsr rlgsllfnpg gpgaggasdv
      121 aggnwqaggq ararydlvgf dprgiagsgq ikcpdgvaeg penpprteae aektftdatr
      181 rakackkasg avlahmdsvs vardldvlrt vlgdaklnyt gvsygtfigq qymklfpgkv
      241 grmvldgvvn patdmqqvar rdvktsedal rryaqdlvar gddrlgatag eilrsltefa
      301 krleqeplrg adgeevtdat lstyldmavm deeswkpltt alvaamdgdg taferfeaat
      361 agesggeelt pqeeqaeene sasmpavlcl dspsapkspk emldtadafa kqsplfgryy
      421 awqmidcatw piaptgaaep ikasgaapvl lvsytddsht plgnaqavhr qldnssllvr
      481 kgrghgayas edpstctdra vdrylvggkl pdkaancpr
//
LOCUS       WP_457695246             126 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457695246
VERSION     WP_457695246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  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 10002786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14201
     Region          3..126
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkvtisprfs evdvlghvtn savpvwfehg rlpifrlfsk ernmrdlali lrryeidftr
       61 qifasvdvii etkvakignt siaieqiatq dgaevargtc imvhfdyere tttsipdhlr
      121 aelsal
//
LOCUS       WP_457695248             508 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695248
VERSION     WP_457695248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56576
     Region          8..378
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msrnplvdld spefldnfrr sidefdsarl pheplsresl rklvdlglyl paiprayggr
       61 eshqemcevi eimsernlpm gmytmivtvl flrnvaasgd dalkeevfdd fannpviggl
      121 aftepgsgsn larmqttyhd dggayritgt khwqafseqa dwwiicakhp erkefayfah
      181 krsdggfvtt evydslglkn lgyglntldl rvprhyrltk treglgdaae ilcasrfska
      241 amasgflrrl steslrqvst rkigdgtlhd idyvrykvnr ikqnyvvcna lyqqlmlaen
      301 yytdledsmf aslatkvlas elmlesaidy qqlcggegyr kgapdniaay alldarvytv
      361 fdgtndllcq hlanlflrqf qqsglrsale figrfgyled affhltdinl shiadapsqd
      421 kivilgrils riygistlqk ssrsaapsar lavddadhpk aiavlkneiv glvneyelaa
      481 qlagtqavsg amrprtavis fdskvgmh
//
LOCUS       WP_457695250             314 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457695250
VERSION     WP_457695250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33437
     Region          7..296
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtggtknvkv slialtfvil ygsgfvggry glpyaepfyy lairfgatav ilfalilcfr
       61 vgwprsgcvh livsgillqg vfsvgvfyal yhgmtpavsa liialqpilv wlmvsvvtar
      121 rvrllsvlal iggllgvait vyrglesssg ltltnvafgf lglvglstgq fyyqmknpga
      181 hllingflqs gssavvmlig glifeegvir wtpelllsel wmsvgvsiga lsllfvlmrs
      241 esadrvasyf ygvpiaagli awpvlnqrpt vseiigfavi mlsiivfnrs srpprahhap
      301 avavdssvpa tdrp
//
LOCUS       WP_457695252             283 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695252
VERSION     WP_457695252.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31205
     Region          28..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          102..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdrrelagfl rsrreritpa dvglpagarr rtpglrreev aqlafistey ysrleqarap
       61 hpsrevlaql aralrlsdae rdhlhhlags ppgpppgpsr evrqsiadll hrlpeaaaiv
      121 msatyeviaw ndlaaalmed fsalsrrdrn lirrtflgpy rhgrrlygvs dadefartsa
      181 qhlraaaary phdpevtglv eellagseef arlwaahdvt arptlcktfe hplvgpvsvn
      241 cdvldiadrd qrvviytaap gspseealrl lsvvgtqrmg vpg
//
LOCUS       WP_457695253             274 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457695253
VERSION     WP_457695253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28131
     Region          26..274
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msgraghrlf gmnntsitst ttsgllagkv afitgagrgi gaasarlfar egarvllaar
       61 tepqleavte eirtaggtae yvvcdladpa svraavdrsv elygrldvaf nngatgqppg
      121 pmdqlseadf dhicavnlkg pwlamtaeia airatakhga ivntssvgsl mgnpalpayg
      181 askravnslt asaaatygpe girvnaiapg ttltemlhew dekapgtieq lnaqtplgra
      241 adpdeiaqaa awllsdrssy vtgtvlrvdg gmra
//
LOCUS       WP_457695256             618 aa            linear   BCT 27-JAN-2026
DEFINITION  class I adenylate-forming enzyme family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695256
VERSION     WP_457695256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..618
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=66629
     Region          7..421
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mirtesgala elpagarvvi rlpngpalad vllacfdlhl vavplhprat dravaeiaer
       61 vsatalvdih glhrtalpdv hkapddlafi mftsgstgpq kgvmlsrrav lgnaaktaal
      121 hgltperphg tclplyhcna lvmsllgthl tgtpliqqaa fdpagyfaal gaagartasl
      181 vpalladlle vgpdwpdgle ylitaaaplt sdlarrfhrr ygprlrqgyg lteavnfsft
      241 mprlddaefr dqylehlppv gvplpdtelr lesgevwirt pdlmtgywqd grttaatvtd
      301 dgwlrtgdlg elrdgllvlr gragerinrg gekhypldie hdwrraglsg rfaavavdep
      361 slgqdiglia teqpvsavre lyeraplrpa alqfggllat stgkpqrkam srvlaarrla
      421 paryerllry aaatahdllh sgvdhpglra laaqaedrph aheeavfgaf dflrehwhhe
      481 ddaelsraka hwrttlltew plavhgelaa evaarhgfeg ppvpfgtear fdggtllvlp
      541 hgpaadgpvw plgpllsfld gspedggadr wtrltrlrdr gfltigcsvl ragrhdlggv
      601 lwarqpdsgp nehagatg
//
LOCUS       WP_457695264             471 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457695264
VERSION     WP_457695264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50045
     Region          29..443
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mnhpdrlgts hgnlarpvtl tpavspvasf adlelpaevl rtltelgvhe pfpiqaatlp
       61 nalagrdvlg rgrtgsgktl afglpllart agrraepkqp lalilaptre laqqvteala
      121 pyadalrlrm atvvggmsig rqaaalrdga evvvatpgrl hdlierracr lgrvritvld
      181 eadqmcdmgf lpqvtevldq vhpdgqrmlf satldhdvdh lvrrylhdpv vhsvdpsaga
      241 vttmdhhvlv vhgpdryavt teiaardgrv llfldtkhav dqltrhlras gvhaaalhsg
      301 ksqpqrtrtl aqfkngqitv lvatnvaarg lhiddldlvv nvdpptdakd yvhragrtar
      361 agesggvvtl vlssqrrems rlmagagiep titkvrsgea elsritgaka psgtpldggp
      421 aaprakntna pfrglgtskd asrgtggksr kasearklae arkaarvrrg n
//
LOCUS       WP_457695265             377 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457695265
VERSION     WP_457695265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=39856
     Region          1..345
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mhtpvtiiga glggltlarv lhvhgipvtv yeaesaptar kqggmldihd hngqlalkaa
       61 glmdefhaiv iegrqtmrlv eqdgtvlhem addgtggrpe vqrgelrril ldslpadtvr
      121 wghkvsgara lgegrhevtl adggtvitsl lvgadgawsr irpllsdatp eyvgtsfvet
      181 ylfdadtrht gsakvvgggs miapspgkei fahresggtl hayvalsrpq dwfaaidftd
      241 aaaatariar efngwapelt alitdaditp vlrphhalpa ehrwdrvpgv tllgdaahlt
      301 apngeganla mldgaelgnt laaypddiea alaeyeqamf argtepvtfe gtevvqgids
      361 enntaqamlk mitaqgq
//
LOCUS       WP_457695283             282 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695283
VERSION     WP_457695283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30291
     Region          1..281
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 metrelryfi avaeelhfgk aaqrlgiaqp plsraihqle rrlgaaller tsrtvtltea
       61 gsvllreara aldavaaaer rtrraalaat ghagvvlatk agassellak lldayaaepd
      121 avtvdlllcg paeqerllrd gradvallhr pfdttagfdt eelcterqvv ilptghplts
      181 rphvqmaevt elpglpmprw pgrdgtypdg pgpqvrdhaq llqlialgra cwiapescra
      241 qlrddlaavp vlnaptvttv iawpphsrsr avaalvrtat rl
//
LOCUS       WP_457695290             347 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent alcohol dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457695290
VERSION     WP_457695290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10143012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="NAD(P)-dependent alcohol dehydrogenase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36854
     Region          6..342
                     /region_name="CAD1"
                     /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283"
                     /db_xref="CDD:176186"
     Site            order(41..43,46,159,163,183..188,206..207,211,226,
                     245..246,248,268..269,291..293)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(41,43,63,89,159,293)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(41,63,159)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(94,97,100,108)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(107,166,170,262,267..269,279,281..282,285..292)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176186"
ORIGIN      
        1 mrntigwqve gpsttlrrtp lerrdlrpdd lavrvdycgv chtdvhavst rdgegdqplv
       61 pgheftgvvt etgpavtrft vgdpvavgni vdscgecamc radqenfcha fptltydgvd
      121 rrdgsatlgg ysreyvvrdr fayrlpagld paaaapllca gitvweplha lgvgpgtrva
      181 vaglgglghl avkiavalga dtsvisrspd kaddarrlga hglivstdpe qmadardrfd
      241 vvidtisaph dlgpylrlva mdgtlshlgh lgpitvettd llvgrkrlss agsggrlata
      301 amldfcgehg itadiellps arvnealdrl rrndvryrfv ldmsdlg
//
LOCUS       WP_457695285             305 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695285
VERSION     WP_457695285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33079
     Region          1..274
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 meirllryvv tlaeelhfgr aaarhhisqq pfgqyirrle revgaslfer tsrrvtptpa
       61 gvrlvaearv lldavdqlae harsegagrd ertlrlgvlg fgagqrwddl raalnaqvpg
      121 lridyvdldw atqyravldh tvdagimwha gpmhglrsdv vlssprvavv parslladat
      181 sltmddvadg pwlatpplsp vmrewlgpav epgpnapvvr qpaaiptava tsgyialahe
      241 vardfyprad vrfvplagaa peiavvtran derptiaalr raarfargga vpplpvaekd
      301 rrrng
//
LOCUS       WP_457695297             206 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695297
VERSION     WP_457695297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22002
     Region          16..166
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mrtdfdpaam srnefyrllt avvvprpiaw istigpdggs tnlaphsfft iasvappvvq
       61 fssvgrkdtl rnveatgqfv vnlapeglfe qindtgtdfp hgvsefeaag igsepslrvk
      121 pprvaaspva lecevhttlg igdatvvfgr vvhavvaqda lvdghpeisr mkplsrlgkd
      181 ewgtvgdvre isrirhadwr gpagdr
//
LOCUS       WP_457695298             284 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695298
VERSION     WP_457695298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31343
     Region          30..282
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(35,70,162,196,198,247,274..275)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(70,274)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(162,198,275)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 maaaaavagp aaavygpgta yaadggralr vmtfnlryas dirphswaer rpvmrallrh
       61 eaphllgtqe glygqlrdia edlgprydwv gtgrgggskd efaavfydar rfapveydhf
      121 wlsdtpylig satwgntvvr mvtwvrfrdm raggefyaln thldhanqys rersagline
      181 rlggldpslp rvvtgdfnva ahknsvyeam ldggslvdsw dtaderstqy atfhgyrplv
      241 pdgdrvdwil tspgvrtrra tintysahgq fpsdhlpvqa lldw
//
LOCUS       WP_457695302             272 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457695302
VERSION     WP_457695302.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Guengerich,F.P.
  TITLE     Introduction: Metals in Biology: alpha-Ketoglutarate/Iron-Dependent
            Dioxygenases
  JOURNAL   J Biol Chem 290 (34), 20700-20701 (2015)
   PUBMED   26152720
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="alpha-ketoglutarate-dependent dioxygenase AlkB
                     family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016706 - 2-oxoglutarate-dependent
                     dioxygenase activity [Evidence IEA]"
                     /calculated_mol_wt=28529
     Region          62..270
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mstplpgfeg fgepvgaegp grpvvsgepg gsdgsggage sggsgglhsp vgdrsrartg
       61 srqeiapggv hvpgwltmaq qrelvtacrd wargpapirh tklprggvms vqtvcigwhw
      121 qpyaytrtad dvngarvaef pdwmvelgrr alvdayqdsa agngytpdta linfyddqak
      181 lgmhqdkeer ssapvvslsi gdtcvfrfgn tetrtkpytd ielasgdlfv fggpsrfayh
      241 gvpkvrpgtg dpasgltggr lnitmrvtgl dg
//
LOCUS       WP_457695305             178 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457695305
VERSION     WP_457695305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..178
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18947
     Region          16..176
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mispetttvt tgyttfdspl gelllvgees atapggtalt slsmpeqrgv tvqphwrrgp
       61 gpfaeavrql rayfageltr felafrtggt dfqervwral eaipygtttt ygrladvvgv
      121 prgdvralga aiganpllil rpchrvigad gtmrgyaagv erkvallrhe galqptli
//
LOCUS       WP_457695308             130 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457695308
VERSION     WP_457695308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14228
     Region          16..128
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mvgpmmagrp rislatvvld cpdahvladf yrqllgwevk cnepdwvllg cpdggtrlsf
       61 qsepgyqapv wperpeeqqk mlhldlrvdd ldgaeayava agatraafqp qddvrvlldp
      121 aghpfclflp
//
LOCUS       WP_457695310             438 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695310
VERSION     WP_457695310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46757
     Region          56..405
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpvasthrrr mrlagtataa lltltiptaa saaaapstpa gnaatagatd rsgidraale
       61 ktlkafhdag mygaysavrs gtaewqgasg vadvdtgrpt tpqmehrigs itktftavgv
      121 lqqvskrhie ldapigrylp dlvpgergra itvrmllnht sgigdyagai fatadsiegn
      181 rfhqfdprel arlglkeepl gkpgqayhys ntnfvlagll lqkvtgkspe ayitehvirk
      241 aglrhtyfpr sayvtgphak myeaayggfn pprdfsvynl swggtagalv stmpdlnrfy
      301 rallggella paqlrqmktt vptedsklry glglftvhlp cgefwghngl vlgaetwsms
      361 sadgqrqmsl gfnltryqkl dgnghpetgp idaamkahia qalcgtsdsp rlpgltdanp
      421 phslpvapqe rplpaprr
//
LOCUS       WP_457695315             232 aa            linear   BCT 27-JAN-2026
DEFINITION  aspartate/glutamate racemase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695315
VERSION     WP_457695315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Liu,L., Iwata,K., Yohda,M. and Miki,K.
  TITLE     Structural insight into gene duplication, gene fusion and domain
            swapping in the evolution of PLP-independent amino acid racemases
  JOURNAL   FEBS Lett 528 (1-3), 114-118 (2002)
   PUBMED   12297289
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="aspartate/glutamate racemase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0047661 - amino-acid racemase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24905
     Region          1..227
                     /region_name="RacX"
                     /note="Amino acid racemase YgeA [Cell
                     wall/membrane/envelope biogenesis]; COG1794"
                     /db_xref="CDD:441399"
ORIGIN      
        1 mktigllggm swestaeyyr llneltrerl gglhsarcvl ysvdfaeier lqaegrwera
       61 gevladaaka lesagadmll ictntmhkva dqvaaavtvp llhladttad avrasglrri
      121 gllgtaftme qdfyrgrles hgldvivpda agrgtvhrvi yeelclgivh eesrqsfmav
      181 irdlvaagae givlgcteie lligaehspv pvfpttrlha eaavtralsd ap
//
LOCUS       WP_457695317             253 aa            linear   BCT 27-JAN-2026
DEFINITION  chitinase [Streptomyces nigrescens].
ACCESSION   WP_457695317
VERSION     WP_457695317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Flach,J., Pilet,P.E. and Jolles,P.
  TITLE     What's new in chitinase research?
  JOURNAL   Experientia 48 (8), 701-716 (1992)
   PUBMED   1516675
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="chitinase"
                     /EC_number="3.2.1.14"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26420
     Region          52..253
                     /region_name="chitinase_GH19"
                     /note="Glycoside hydrolase family 19, chitinase domain;
                     cd00325"
                     /db_xref="CDD:381595"
     Site            order(105..106,112,114..116,146..150,152..153,186,
                     215..216,220,228,232)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:381595"
ORIGIN      
        1 mrsriaalls aatvavgval vvptmpaaat tgcshcaaap agadaraegf vvseaqfnqm
       61 fpnrnafyty sgltaalsay pefantgsda vkrqeaaafl anvshetggl vhvveqntgn
      121 yphycdasqp ygcpagqaay ygrgpiqlsw nfnykaagda lgidllnnpy lveqdaavaw
      181 ktalwywntq tgpgtmtphh amvsgagfge tirsingsle cnggnpgqvq srinnyksfv
      241 qilgttpgdn lsc
//
LOCUS       WP_457695323             429 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695323
VERSION     WP_457695323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46056
     Region          40..406
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
ORIGIN      
        1 mnwlihdyre ndlaevvhli dstaelgqes vfslaecisa ltsrqpavva vhqgapigaa
       61 lacvagergw vmriaissaw rgrglasall velerrliaa rvsriayvlp eedmlgegll
      121 nagytrqpav ayfektephh gpaaglledl ggrflptdlw akvagmeaek dlierrvvlp
      181 laeperaarh gvrppraial fgppgtgktt faraiaarlg wpfvellpsr ladegnlaaa
      241 lrsafariae lervlvfide veeiapvrhe paqpgglhgv tnellklipg frerderllv
      301 catnslrsld paflrpgrfd ylipigtpdp aarsaiwsry tdgradvdva alvaaselft
      361 padiehaarv aaqasferdl eaigvgagah grlgastddy laaiaqcrpt vtpamidefg
      421 aditaharc
//
LOCUS       WP_457695321             397 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457695321
VERSION     WP_457695321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 397)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43382
     Region          18..395
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,83..84,91,95,102,230..231,234,238..239,242,
                     275,280..281,284..285,287,310,337..339,342..343,345..347,
                     351)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,77,79,82,84..85,169..170,178,229..230,233..234,
                     238,281,284..286,385)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 madivdlgay gedftadpyp yyaklraqgp vhrvrlpyvp eawlvvghqa vraalsdprl
       61 nknwreaglq sdggdesalf tnmldadppq htrlrklvak eftsrrveal rprvqqitde
      121 lldtmlaape gradlveala fplpmtvice llgvpamdrd afrawsneiv aptseeaaqe
      181 avvamsgylv dlietmrnap gdgllsalir tsdedgdqls rdelvgtafl llvaghettv
      241 sllangvral lqhpaqlaal radyslldna veemlrydgp vematwrfta epveiggtli
      301 pagqtvmial asasrdrehf aaaddfditr darghtafgh gihfclgapl arlearvalr
      361 sllercpgla mdadfddltw rtgmlrgieh lpvrwkg
//
LOCUS       WP_457695335             314 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695335
VERSION     WP_457695335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34248
     Region          <17..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..301
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,232..237,
                     243..244,246..247)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mfdlhrlrll relkhrgtla avaaalsysp ssvsqqlsql etevgvplle pvgrrvrltq
       61 qaeilvthte avlerlerae aeiatsltdl tgtlrvasfq taalalvppa ltllrashpr
      121 lrvhvtqmep eralpgllar dfdlviaeey pgnpnprpae leqeelcrdp lrlahphpvg
      181 nggvaeaada sgpmarlral aehpwvlepe gtaarhwamt lcrsagfepd vrfestdlll
      241 hlrlveqgha aallpdlvwd grpatvplqq lphgrqarrl ftairrgrgr hpaiqacrra
      301 lreavgasgp pggr
//
LOCUS       WP_457695342             810 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695342
VERSION     WP_457695342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..810
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=85869
     Region          24..810
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          558..586
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(559,562..563,566..567,569,593,602..603,606..607,
                     609..610,638,641..642,645..646,649)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          591..627
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          637..660
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgrerelsrl rtllrssrll tltgpggvgk trlalelagr vrggrtghaq wvaldslqds
       61 ellpqalaaa lgvrerggra gvealvhalg trtmlivldn cehlaeacar laatllarcp
      121 rlrllatsre plrvpgevvf rvgelslspa gedhdtaall rseavrlfla rartsdaafe
      181 sgpgeartva eicrrldglp laielaagrv gslslpgilh glddqlsllt dgsrtgpgrh
      241 relgaaidws hrlldplerv vfrrlsvlgg gfdaegaaav cangeghevr dryrdgdryg
      301 ggevrgegva dgggtrrgdg vhrsvcpqgp hslvrpeqll rvvcaleaks livrvrgdep
      361 ggparfrqls airaygmdrl aeagelpdtw nralgwlagk aagavtpgvf ldtvegplar
      421 eqenlaaalt ysaarsdhrh vplavalarl qyqqeqltaa rtllsgvler vqgpedrsaa
      481 walaarsacl qddhaaalaf aqeavaagrt grhpgglana ldalaaarlc rgefsdavav
      541 faecldvvrt lgcpldlalc rhhlawallq agrtaeaeql mqeclpelet sappgqltaa
      601 lhtagairla lgdvdaaerr faevllkapp gesfhglypl eglaivaaer gdlqrslrly
      661 aaaaamrrri dtepeahwwg qveavvarvs ervhpsgvra amaagrrlrg arlvayalrg
      721 tqvrsvgqes vqaaspdrvd eagqppltgr esavaelvae gmtnqqiash lglakstvag
      781 hldrvrdklg vrsrtqiavr vagriadgel
//
LOCUS       WP_457695350             114 aa            linear   BCT 27-JAN-2026
DEFINITION  MmcQ/YjbR family DNA-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695350
VERSION     WP_457695350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..114
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12900
     Region          1..112
                     /region_name="COG3801"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443014"
ORIGIN      
        1 midsadvrri alslpetvek eawqmptfrv agkmfvtipd detsfavrcp iherkeliaa
       61 epekfwvpph easshwvrvr laeledmtel rdilvdswkq aaptrlvdaf pgss
//
LOCUS       WP_457695351             165 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces nigrescens].
ACCESSION   WP_457695351
VERSION     WP_457695351.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=17960
     Region          32..113
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mvpsflvsvl nrlfrneawr rlhaqaalwv tvvmtavlla gaalvvvaes gaphanitsy
       61 pkalwwsiet attvgygdfy pvtlwgrvia sllmlsaita fgvitaalat wfvghaeqdm
      121 lrlskavgsh aredaealrs elhtlherfd hvenlirdkg thsas
//
LOCUS       WP_457695353             326 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457695353
VERSION     WP_457695353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="trypsin-like serine 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=34737
     Region          102..305
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 msrpiavrgr falllttlll glsftlapap pahaakppng hgpglhlaaa sadtywtsqr
       61 mqaaqpaaar kstaaprpat aatppshpfd glpqvgtffw tdgsntgrfc ggtvvrsphr
      121 dlvvsaahcl rspdpkrhls fvpqyhdglk phgiypvers yldqryydlg tnagarwdya
      181 vvrlgaredg aeveevtggf dllpypgydh rkvrligypg nkdtthpkpl dctssthryt
      241 stdpsapgdf leiacagyig gtsggpflvr dftgyaligv iggyhtggdf pdvsyssyft
      301 adtlalylha vhgdppatpr qgvsar
//
LOCUS       WP_457695355             408 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695355
VERSION     WP_457695355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44102
     Region          42..>309
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mnrrtvtksg alaatmllag ggiaqaqpgk tpttkdltvr lpaptgphpi gvttlylvdr
       61 arrdpweplp vrevmatvfy partvrgypv apqmtrgaae rlpfieplfh eglpakgvnw
      121 aatkthahtg apaqgvrrpv llyspgggdp rtvgtgiaee lasrgyvvvt ldhpgdgsev
      181 efpharagrk kvresvfrgd pradpkmfrt vidtriadtr fvlnqleala agrnpdaegr
      241 plprhlgral dlrrvgiygh saggttaaea myedrrlhaa inlegfldhp pespgqegkl
      301 fpiarygtdr pllllgtdgf ryqkelersw samlahphgc tgrrqldhta hgvftdyaai
      361 apqlqaaglm taahriklvg aidpavsvpl vrhhvvsffa rhlpacrp
//
LOCUS       WP_457695356             328 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457695356
VERSION     WP_457695356.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 328)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35468
     Region          <255..310
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mirihftaad faqvrfaprp aplqelnval mkmcspddal lfgrwrrrll qslppavqpl
       61 gdlvpaevap hfldvfsdtl kegldtvras ppelvraeie rvyarqpspa plwlrdlyrg
      121 dggawhllrr aqhaafdtal rpvwplvqdl hqaeftrhal avaehgigaa ltelvpgarl
      181 henvwaveap yeddialggr gvlllptfhw tgrplvsdlp erpvavtypa gpglplspag
      241 aagsdealag vlgrtrcdil lllgeehtts elarrlnvsn atasahtaal rgaglittar
      301 agravlhrrt algsllvqrr srltghge
//
LOCUS       WP_457695432             107 aa            linear   BCT 27-JAN-2026
DEFINITION  putative quinol monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457695432
VERSION     WP_457695432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..107
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12133
     Region          5..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mtggyalvvr fttrdadaar efdalvtrta egirtepgtl vyvthipede plvrvfyely
       61 adreafqehe nqphtkhflk ereqhltste vtflneltgk rpavegt
//
LOCUS       WP_457695429             142 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457695429
VERSION     WP_457695429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15301
     Region          45..111
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mniaaplgpi dprlideieg alanertrsh raviqqiaes hnvkrkfing srtvrkkati
       61 akrdgarcay cqepfpdlsv atldhvipyc lvrtnanwnl vlscspcnng kgcaipdvml
      121 pmlaslivtl gqlgkqqtgg ar
//
LOCUS       WP_457695460             185 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457695460
VERSION     WP_457695460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  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 185)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20096
     Region          27..185
                     /region_name="Uma2"
                     /note="Endonuclease, Uma2 family (restriction endonuclease
                     fold) [General function prediction only]; COG4636"
                     /db_xref="CDD:443674"
ORIGIN      
        1 msiesadynh gveperalky aiqhirgdra eivegviepv sptwdheata etirdqirar
       61 areldcvtgs gnldlpgssn wyvpdiavvp aaaakgagal lpadtllvve vtsesnaetd
      121 rvvkrkryae ygaplyllvd rqersvtlys epgqlgytra dgphpygvvv ripepfglel
      181 dtsel
//
LOCUS       WP_457695486             350 aa            linear   BCT 27-JAN-2026
DEFINITION  type III polyketide synthase [Streptomyces nigrescens].
ACCESSION   WP_457695486
VERSION     WP_457695486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37476
     Region          12..349
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mpahvtwptv khpdnwvttd eicdnvqthh pehprlgvvl rvirntgvqr rafaypldsd
       61 tvsgqtglvd rnakawtaac tlaedaaeqa lenaglqprd vdavitshst swavpqldvh
      121 linalglrpt vrrtalttlg caggatalsk aadhvaarpg srvlvvvaea istiyhhadd
      181 tiegmiykal fgdsagaciv tseplqpglr iddtweyvlp gsrdnsywgr idelgfhfds
      241 areavngpaq vmphlrdwlk qhdaldpdfv vihaggpail navqqgldlt aeqlahswas
      301 laevgnlgcv slfdaqrrth dappadgdrg vmlaygpgfa italtgtwvs
//
LOCUS       WP_457695502             176 aa            linear   BCT 27-JAN-2026
DEFINITION  nuclease-related domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695502
VERSION     WP_457695502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 176)
  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
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Grynberg,M. and Godzik,A.
  TITLE     NERD: a DNA processing-related domain present in the anthrax
            virulence plasmid, pXO1
  JOURNAL   Trends Biochem Sci 29 (3), 106-110 (2004)
   PUBMED   15055202
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..176
                     /product="nuclease-related domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19176
     Region          13..121
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
ORIGIN      
        1 maeaqrnaar wqagaegerr taqllapllr agwyvlydla vgkranvdal lvgpdgqvft
       61 ldtklwaard garrpmmvhv vrgrlthgvr drdrqvdtal wetgevskal gvpvtplivv
      121 hnapvdgggf hvrgvavfpa drmlgllrhn tngrpdprea qrlaqlaear lpayvk
//
LOCUS       WP_457695508             106 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457695508
VERSION     WP_457695508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..106
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11358
     Region          <27..92
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mtapvqvgps ptsggptpaa grrksqtvli mtprrieilv laangntnad iarklwlsee
       61 tikthmrkih evlgardrsn avalgiirgf vrpdqidlhp akrhaa
//
LOCUS       WP_457695523             247 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695523
VERSION     WP_457695523.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28059
     Region          141..186
                     /region_name="HNH_3"
                     /note="HNH endonuclease; pfam13392"
                     /db_xref="CDD:433169"
ORIGIN      
        1 mdsiesyplh skrgpkictv pdcetkvcar glcnmhykrw kahgnpltfl pkryegclvs
       61 ecegthksng yclkhykrwr rhgnpnmkrp ttpaeerfws rvnksgpmpa qgvvqglcwq
      121 wtagktakgy gslslpgghh vlthrfswal hrgpipdglv idhlcrnrac vnpdhlevvt
      181 laentrrgfs vstwnrlkth cpkghpysae ntyihpkgsr icrqcarerd rqphrlisnr
      241 rakkaaa
//
LOCUS       WP_457695529             158 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695529
VERSION     WP_457695529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17553
     Region          18..80
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 mnpthmhrat prvtasnwte yracadtdpd vftdddkrvq afakdicalc pvrsfclqfa
       61 idtntqhgvy ggldpderde llgkrrlpgh ghqgnpepmw qqilrvperr eklldlharg
      121 wsagriagal htnvqtinrv fsaldeqaql aaslaeva
//
LOCUS       WP_457695531             262 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457695531
VERSION     WP_457695531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28868
     Region          <194..237
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtthaphtpr hkkgrarsat ngdhplaakw lrmrfnaamr akgipakacs rcrvikdlea
       61 fsayrsasdg lssycricka aahaekmatd pnyvarrraa aiaynvanta arrayrvqrd
      121 ivvraanrak hadrvqdpav lkicvgrcqr llpetafrld rgnsdglrer crdcaarvar
      181 rlcedaygep kgqtcylcge aiasstdaha dhlipqsqgg edtasnlrwt hgacnvrrga
      241 spitpeqwqr mrlldssket sq
//
LOCUS       WP_457695563             359 aa            linear   BCT 27-JAN-2026
DEFINITION  ParB/RepB/Spo0J family partition protein [Streptomyces nigrescens].
ACCESSION   WP_457695563
VERSION     WP_457695563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38452
     Region          39..>226
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mskademges aafgrvgnrl sargrskdqa fnndgptvla lhllshnpdn predigdvte
       61 lsnslrdhkq kqplaimtrg ayleanpgre geleanaeyv vidgnrrlaa ardaglkslk
      121 vmlddeglgk dgneilesal vanvfnqkle pldeakalkt lleihgtqda laarlhrsqg
      181 wisqrlslld lkpdlqerlk agkesashlr rvgkkpseeq daalaaikak earekeeraa
      241 rarakaqake qaaakpkgep pnpsdrepad gamngeggha deargdgkdh ygvikessdd
      301 sttrikegas atgsagggqa vapslpfhdv samariiseg meledvrrlv ktlwathgd
//
LOCUS       WP_457695565             382 aa            linear   BCT 27-JAN-2026
DEFINITION  ParA family protein [Streptomyces nigrescens].
ACCESSION   WP_457695565
VERSION     WP_457695565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41424
     Region          118..381
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 maspypdger ekvasklpsa lrqqlkvraa elsidiqdav ttaihewqak ttplpavdta
       61 gadsfstwlp tglydqfktt cstrdvsytq glaqsirgwl dgqagetpad tdiperkvvg
      121 nqkggvgkta vsagiaeaaa eagktvllvd fdpqghlsdq lgveqigpgd dslvthmnae
      181 grgdirdllv tiegerfgkr lqvlpacfdg flldaklatn rvirhketal eralepiesd
      241 fdvviidcpp slgmamdaai yygrrrener rgvsgivipv laedssatay tmlsqqiesi
      301 vedcnidvey lglvvnlyds rrgyvatssl kawrdlqdpp vlavigdlke qreavrkvkp
      361 lldyaplseq aeamrqiwsa is
//
LOCUS       WP_457695571             405 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695571
VERSION     WP_457695571.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44341
     Region          32..>83
                     /region_name="HTH_ARSR"
                     /note="helix_turn_helix, Arsenical Resistance Operon
                     Repressor; smart00418"
                     /db_xref="CDD:197713"
ORIGIN      
        1 mmavhwaadp kakryvpsrs hgprgmnhtt lricqeianl kacrpgvayl mrklklsert
       61 veyhlgmlre agllvyrskg tnvagvggqa svferviptq fddahgirtt gegvqrrpvg
      121 askehqsilg klskkaarki rrprqkkass gegrctlmkg gtsgsstagt styppeskla
      181 sgtsdcptpk ipkqrarral nrvgrrhqla relvaqvpwl gganpariaw varevadagw
      241 saveiaayld qfgigdhegi rrpsgvlarr lkgatrllrs pqarqecvqa wrdsrqaarg
      301 ehdraqyetf gpgpsspsiq rlaqeafrrv adaqrteetv myeitahtta mtledltpae
      361 vidlrataak dpdviglaid lmgedkarrl ytnaavnryk etsra
//
LOCUS       WP_457695578             292 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695578
VERSION     WP_457695578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31466
     Region          <53..106
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 mssrnayftl idhryyryrg caadpdqpaq aqgdtavpvn awlpftddgg elpsvrnarq
       61 aaaqrvcgdc pvlaqcraya lsvdsdgrla epegvwggml plerhrdlva rrtaktpaaa
      121 aaaidekqla ecrtdqkqav lrslaahvde elvaygasmd vrtanwhrsl lcgllgldke
      181 ratrqqllaa arahgvlpag arvvpdgdvp iaaapntdgs rqrrlarghr lqptrpiqli
      241 lpgyeqllrv prprrtharg gpalrvvrvt aepltldvll ppvpapalep aa
//
LOCUS       WP_457695602             299 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Streptomyces nigrescens].
ACCESSION   WP_457695602
VERSION     WP_457695602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31627
     Region          91..256
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msqknhegkk tarerlqeqr erekararrg rqaivagavv vvlavaggia vwassssdkp
       61 aandnevavp kqasgggrpa vpvgaadaps tltvwedfrc pacrqfetaf rpviheleds
      121 grlkseyhlv tiidgnaggq gsrnaanaal caqdagkfra yhdvlfshqp pepqdkfadk
      181 kyllqlagkv kglvtpaftk cvndgtydrf vkksndsfat sgyrgtptvl lngkdlskek
      241 ggqfspadfk kmvlaahkak qpgkkstaph pgaspqdkhp grsaapqgal tgrsaapap
//
LOCUS       WP_457695624             396 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces sp. 900105755].
ACCESSION   WP_457695624
VERSION     WP_457695624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 999995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..396
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40135
     Region          13..371
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(23..24,27..28,31,63,114..115,117..119,122,142,
                     145..146,149,223,226..227,230..232,235,252,256,309..310,
                     314,318,333,336..337,340..341,344)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
ORIGIN      
        1 mpsyrslfrt peftplflga aaqnaagtvg glalgtlvyr ttgspllsal smfgpslaqv
       61 lgatfllsga drlpprttla aisltfaavt agmalpglpa galltavlll glvsalgggv
      121 rwgllneilt kdgylpgrsl fnmmsglvqi tgyatggall aavsprtcll laaalylasa
      181 ltlrlglsnr pprtagrpsa aatwrtnall wssrprrlty lglwlpnglv vgceslyvsy
      241 apdaagtlfa caalgmlagd vtagrllpsa vraraatpll lllatpylvf flqpplvlaa
      301 vcatvasvgf gaslvqqerl msltpdalsg halglhsagm ltmqgvgatl agsvaqvtsp
      361 ahamtlvaaa slavtlalat aarrertapl pvpsar
//
LOCUS       WP_457695646             430 aa            linear   BCT 27-JAN-2026
DEFINITION  NYN domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695646
VERSION     WP_457695646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="NYN domain-containing protein"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45503
     Region          2..172
                     /region_name="LabA"
                     /note="NYN domain, predicted PIN-related RNAse, tRNA/rRNA
                     maturation [General function prediction only]; COG1432"
                     /db_xref="CDD:441041"
ORIGIN      
        1 mdrcvvlvda gyllgaaasl lageparsri tvdhaaliqg lrqraeaete rpllriywfd
       61 gapdrvpqpe hrrlrvmprv tvrlgaltrs dgrwaqkgvd aamhaeltel arnracsdiv
      121 lvtgdgdllp glmsakehgv avhlwavqaa dgdynqsedl vaeaderrvl drtwitravr
      181 akelggpcap ppvprpeiaa ilsaplpesa vaaaaaaaag pesaehtheh ngangvsrps
      241 agtengaaag gepgaagskv vptpkdlagl grahaagqqp agtggpapaa gatlrwssdk
      301 gwverggpag epdgtaalpt laqltsaeqr wadreedita vsgdpfevgq vfarrwtdrl
      361 sdaahlqqls teypriphri dgellryaar fgllahkddq idehdryair agfwrevdlr
      421 taaehapagd
//
LOCUS       WP_457695658             547 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457695658
VERSION     WP_457695658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..547
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59473
     Region          7..511
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtdhdqisrr tavtavaata allpfagaat ahaqeapdra pffqhgvasg dplpdgvllw
       61 trvtptpaat pgsgrgpate vswqvatdkd fasvvargsl tssaatdhtv kadvrglqpa
      121 tryyyrftvd gqhspvgrtr tapahdtaag nirfgvvsca nwesgyfspy rhlaarsdld
      181 avlhlgdyly eyksgeypef kyvirphspa helltladyr irhgvhktdp dalamhathp
      241 viaiwddhef adnawkggat nhtpdsegsw sarmaaakqa yfewmpvrps iagttyrrlr
      301 fgtladlhll dlrtfrdeqa kpgsgavddp srtltgraql dwlkaglers dtawrlvgts
      361 vmisqvafga ipakllgpla eilgipkegl aintdqwdgy tddrrellsh lsdrgidntv
      421 fltgdihmaw anevplqaat ypadqpvate fvvtsvtsdn vddflhvaph tvslagvaal
      481 kaanrhvkwl dmdshgygvl dvsaertqmd yfgisdrtdp qatsallrsy rtrsgtqqme
      541 radqpvg
//
LOCUS       WP_457695664             262 aa            linear   BCT 27-JAN-2026
DEFINITION  TraR/DksA family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695664
VERSION     WP_457695664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27026
     Region          144..262
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvakktaaek sttpadeava kqpaakrtap kkaaakktad gtatpekata kkaapkraaa
       61 kktaakktaa kktvvkktaa kkaakkapak taavpakktg aktvvakkta aasatahgnd
      121 savpmarvaa apdelavrpg edpwtpaeva aartelmeet grlrleivsa edaiaglmrd
      181 sgdgagddea dtgsknitre helalasnar emlhqteral grldagtygl cencgnpigk
      241 armqafprat lcveckqqqe rr
//
LOCUS       WP_457695690             186 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-class carbonic anhydrase [Streptomyces nigrescens].
ACCESSION   WP_457695690
VERSION     WP_457695690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10130171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..186
                     /product="beta-class carbonic anhydrase"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20035
     Region          48..182
                     /region_name="beta_CA_cladeD"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd03379"
                     /db_xref="CDD:239474"
     Site            order(48,50,57,59..61,73,76,95,100,110,113,172)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(57,59,110,113)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(58..61,67..68,73..75,77,79,90..91,94..95,172,
                     174..175,177,179)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 mpipasqplp psadgaavrt gdtvtdslve ankryaaafs dpgmdarpvr kvavvacmda
       61 ridlhaalgl elgdchtirn aggvvtddii rsltisqral gtrsvvlihh tgcgllslte
      121 dfrhdlaaev gqrptwavea fkdldedvrq smqrvrtspf lphtddvrgf vfdvttgllr
      181 eidpqr
//
LOCUS       WP_457695680             482 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Streptomyces nigrescens].
ACCESSION   WP_457695680
VERSION     WP_457695680.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49576
     Region          2..467
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mislslaeia sivggqqhdi pddgrrvtgp vvadsravgp galfvafagd rvdghdfapg
       61 aveagavavl aarplgvpai vvddvvaalg alaravvarl gttvvgltgs agktstkdli
      121 aqllqrhgpt vwpegnlnne iglpltalra dettrhlvle mgargvghir ylagltppri
      181 gvvlnvgsah igefggreqi alakgelies lpsaedggia vlnaddpyvr amaprtrart
      241 ilfgeaaeaa vraenvrlte lgqpaftlht psgcsdvtmr lygehhvsna laaaavahel
      301 gmpvdeiata lseagtlsrw rmevteradg vrvvndayna npesmraalr alvamgaagk
      361 atgartwavl gemaelgees laehdavgrl avrlnvsklv avggreaawl dmgaknegsw
      421 geesvhvsda raavdllrse lrpgdvvlvk asrsvglerv aaalldegmr gaagaeggaa
      481 tr
//
LOCUS       WP_457695684             664 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695684
VERSION     WP_457695684.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..664
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=70134
     Region          57..647
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mteprdprrv prpaqrggra gsgagrppaa krpaprpgsr pgpprparlr sgtpvlrlgs
       61 prprlrlvsl gltlimlvfv vrlfqvqavd agafaakane nryvpvklaa ergaitdrng
      121 vdlattvday ditadpslla pektkiddap qraaallapi lgedkatlak kldrpearya
      181 llarqqtpqv wkkikdlrkt ldakaaaapk gaprpdvlvg ifadkhskrl ypnknlaagv
      241 lgfvngagkg ggglearldk qlagkdgklv yaqsggrrvp tadtqehpav pgsdveltld
      301 rdiqwaaqqa iteqvaksra drgyvvvqdt rtgeilalan apgfdpnevs kadpealgna
      361 alsdafepgs tskvmsmaav leegvatpat rvtvpnrlhr gdrlfaddvd hetwhltlng
      421 vlakssnigt ilatgqlgrt qpeanqvlys ylrkfgigrp tglgfpgetd gilakpqdwn
      481 tsqqftipfg qglslnavqa asvystiang geriapslvr gstgpdghya papkpaknrv
      541 ispktaatla tmlesvvdde egtgakakid gyrvggktgt snrvdprtgr yhgytasfag
      601 fapadkprit vycavqnptt gsyfggqvcg piyqqvmafa lktlqvpptg akpprlpvtf
      661 tpgq
//
LOCUS       WP_457695692             339 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457695692
VERSION     WP_457695692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37156
     Region          16..307
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mttyderasl sdltttaerv hrsveevieg kpevvrlalt vllaeghlli edvpgvgktm
       61 lakalarsid csvrriqftp dllpsditgv sifdqqqrdf efkpgaifsq ivigdeinra
      121 spktqsalle smeerqvtmd gqtyelpdpf mvvatqnpve megtyplpea qrdrfmarvs
      181 igypspaael qmldvhggas plddlqpvah aheivklidt vrtvhvaeav rrytvdlvva
      241 trshpelrlg aspratlhll raakasaalq greytlpddv qslaaavlah rllptaqaql
      301 nrrtaeqivl eilqrvpvpe psaqpwrtpg qqppgvrgf
//
LOCUS       WP_457695706             505 aa            linear   BCT 27-JAN-2026
DEFINITION  phytoene desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695706
VERSION     WP_457695706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..505
                     /product="phytoene desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016116 - carotenoid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016117 - carotenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53169
     Region          25..495
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag mgamaaaarl avaghrvavf erdathggav rrlardgftf dtgpgllhlp
       61 avyrdlflkt greplescle lsqvdpaarh vfadgtavsl pnasragvla aldealgaga
      121 gerwselvgr areawdatrr plleeplwkd wrvlgrdpyp avrrrglfgr gkgpttatla
      181 evarreladp rliallesha laygfdprsa pasavvlpym eqtfgswypr ggmraladal
      241 yercvarkve fsfgaavtgi vekdgraagv eladgrvsea efvvagvdpv rlvelcrgre
      301 pwgaddvrpa lgpgdratgr ltvclalrga rpgdaahrtv vhaadrtael agvfgvgfgl
      361 rtpcdrptvt vlrpddpstr pddaheavtl tstvaphgpv dwqdgaavaa gaermveiae
      421 aavpglrerv lwrevlpptd dalvpgpala gqegrflrpg nrtripglya vggwshpggg
      481 pahagmsgai vaglivngdd whgst
//
LOCUS       WP_457695713             413 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457695713
VERSION     WP_457695713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43081
     Region          14..412
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mseqskssqa pdrtprvviv gagiagvqta valreqgwrg aitllgdeph qpydrpplsk
       61 avllgkaegs tfdvdfaald ielhlgrpvt allpdahvve tadgpvsydy avlatgadpi
      121 vlpgsegmpg vhllrtldda erlrpvlaaq heivvvgagw igaefataar eagcsvtvve
      181 aadrplagal paevaahmtg wytdagaelr tgarvasvta gavtladgtt lpadavvvgi
      241 garpatawla gsgvevspqd gavladdqlr tsvpdvyavg dcasfpsary gtrllihhwd
      301 nalqgprtva eniargdaeg lvydpvpyfw seqfgrfvqy aghhgdadel vwrgdpagaa
      361 wsviwlrdgr lvallavgrp rdlaqgrkli ergvvldrer aanasvplka aav
//
LOCUS       WP_457695717             264 aa            linear   BCT 27-JAN-2026
DEFINITION  thiazole synthase [Streptomyces nigrescens].
ACCESSION   WP_457695717
VERSION     WP_457695717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18578739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="thiazole synthase"
                     /EC_number="2.8.1.10"
                     /GO_function="GO:1990107 - thiazole synthase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27610
     Region          1..256
                     /region_name="ThiG"
                     /note="Thiazole synthase ThiGH, ThiG subunit (thiamin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG2022"
                     /db_xref="CDD:441625"
ORIGIN      
        1 maddpltlag ttfdsrlimg tggapsldvl erallasgte lttvamrrld ptvqgsvlsv
       61 lerhrirvlp ntagcftage avltarlare algtdwvkle vvadertllp dpielldaae
      121 tlvddgftvl pytnddpvla rkledagcaa implgspigs glgirnphnf qliteragvp
      181 vildagagta sdvalamelg caavmlasav traqepelma tamrhavasg rlayragrip
      241 rrhfalassp tegvpdldpe rpaf
//
LOCUS       WP_457695723             310 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695723
VERSION     WP_457695723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32786
     Region          13..232
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mrgrrgaaqa pavrandgit ldvhrgeifg llgpngagks tlvrqltgll rpdsggisvl
       61 ghdlvrhper aarllgylgq estaldemtv alavettgrl rglgareara erdavidelg
      121 ladltgralk klsggqrrla cfataliger pllvldeptt gmdpvarrav waavdrrrae
      181 rgvtvvlvth nvleaesvld rvavidrgrv iacdtpgglk emvsdevrle lvwrdrppld
      241 vpevaalqaa ahasgrrwtl rlpadrarsa vaavtagpaf aalddftlat psledvylal
      301 ggraeglvka
//
LOCUS       WP_457695725             203 aa            linear   BCT 27-JAN-2026
DEFINITION  dienelactone hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695725
VERSION     WP_457695725.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21608
     Region          17..201
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msvpastess tsglstivlf hsvcglrpav haaadrlraa ghevivpdlf dgrtaesvpd
       61 gilikdeigk eellkraita vapysdrglv yagfsfggsv aqnlalgdek trgllllhgt
      121 sdiaedtaad dlpvqlhvad pdpyephdwl nawylqmrra gadvevfrya gaghlftdpe
      181 lpdydaeaae rawkvalgfl agl
//
LOCUS       WP_457695727             363 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695727
VERSION     WP_457695727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..363
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39575
     Region          80..331
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 meavlrpivv iggsivltli lvwltdrvlr ridaahpetp lwgllrrcri plevalctal
       61 lrgsydetgl kiaedheagi graltlvlia aaawlvvraa aaivessysr yaasgrdaar
      121 vrrvrtqvtl iqrvvtavvi vvaaasmllt fpemravgts mlasagllgi vagiaaqstl
      181 gnlfaglqia fgdmvrigdt vvvdsewgtv eeitltaltv rtwderritm pvsyftgkpf
      241 enwsrggaqm tgtvffhldh sapvekmrqq lleilqecad wdgrswnlvv tdttpstivv
      301 ralvtardad tlwtvrcevr ermlewlrte hayalprist apappgvpea rhgeepgarl
      361 pkd
//
LOCUS       WP_457695729             483 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457695729
VERSION     WP_457695729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..483
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50785
     Region          20..452
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mgahpptttk tvpitgepgs gstggpsqdg lqaglknrhl smiaiggvig aglfvgsgag
       61 iaaagpgill syaltgllvv lvmrmlgema aasptsgsfs ayadralgrw agftigwlyw
      121 ffwsvvlave ataaaailtg wvpavpqwaw allvmivltg tnlvsvgsfg efefwfagik
      181 vvaivifivv galaifglpp ggdpvgvshl tgdggflpng pgailsgmll vvfsfmgsei
      241 vtlaasespn pvqavrkavn sviwrialfy igsitvivtl lpwndpavak spyvavlksl
      301 eipyagivmd ivvltavlsc lnsglytasr mafslgqrgd apksfatvnk ggvpavaiya
      361 svafgfiati fsytskdtvf qfllnssgav alfvwlvicl sqlrmrriie retperltvr
      421 mwlypwltya tiglivfvig ymfydpdgre qmvlsvvaav vvlavglild rrrprerdav
      481 ega
//
LOCUS       WP_457695733             409 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457695733
VERSION     WP_457695733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Green,K.D., Pricer,R.E., Stewart,M.N. and Garneau-Tsodikova,S.
  TITLE     Comparative Study of Eis-like Enzymes from Pathogenic and
            Nonpathogenic Bacteria
  JOURNAL   ACS Infect Dis 1 (6), 272-283 (2015)
   PUBMED   27622743
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kim,K.H., An,D.R., Yoon,H.J., Yang,J.K. and Suh,S.W.
  TITLE     Structure of Mycobacterium smegmatis Eis in complex with
            paromomycin
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 9), 1173-1179 (2014)
   PUBMED   25195887
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Houghton,J.L., Biswas,T., Chen,W., Tsodikov,O.V. and
            Garneau-Tsodikova,S.
  TITLE     Chemical and structural insights into the regioversatility of the
            aminoglycoside acetyltransferase Eis
  JOURNAL   Chembiochem 14 (16), 2127-2135 (2013)
   PUBMED   24106131
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Wei,J., Dahl,J.L., Moulder,J.W., Roberts,E.A., O'Gaora,P.,
            Young,D.B. and Friedman,R.L.
  TITLE     Identification of a Mycobacterium tuberculosis gene that enhances
            mycobacterial survival in macrophages
  JOURNAL   J Bacteriol 182 (2), 377-384 (2000)
   PUBMED   10629183
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479597
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44046
     Region          1..409
                     /region_name="PRK01346"
                     /note="enhanced intracellular survival protein Eis"
                     /db_xref="CDD:234945"
ORIGIN      
        1 matelrmlrd vewdtwsdtl nrafgeppps peqravrrev tetdrsfgvw dgadcvatag
       61 afsfgltvpg gaevpaagvt mvsvqpthrr rgllrammrh qladvrerge plavltasep
      121 aiygrfgygp aaqdmqltvd tvrlaapelp gvdevrlrlv dpaaaladce rvyaqlvpar
      181 pgmlarrpgw armavldppg eregagelqc vvaevdgevr gyvryavkpv wenagpagvv
      241 lvrhiealdp vvyaalwrfl fgidltssvs vrtrpvddpl phlvgdmrrc rpglreslfv
      301 rpvevgaala artyrtpvdv vlevtdpfcp wnegrwwltg detgascart tdpaglalsv
      361 relgsaylgg faltalaaag rvrelrpgal aaasvafgsd vapwlphgf
//
LOCUS       WP_457695731             273 aa            linear   BCT 27-JAN-2026
DEFINITION  Fpg/Nei family DNA glycosylase [Streptomyces nigrescens].
ACCESSION   WP_457695731
VERSION     WP_457695731.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Le Bihan,Y.V., Angeles Izquierdo,M., Coste,F., Aller,P., Culard,F.,
            Gehrke,T.H., Essalhi,K., Carell,T. and Castaing,B.
  TITLE     5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA
            glycosylases
  JOURNAL   Nucleic Acids Res 39 (14), 6277-6290 (2011)
   PUBMED   21486746
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Zaika,E.I., Perlow,R.A., Matz,E., Broyde,S., Gilboa,R.,
            Grollman,A.P. and Zharkov,D.O.
  TITLE     Substrate discrimination by formamidopyrimidine-DNA glycosylase: a
            mutational analysis
  JOURNAL   J Biol Chem 279 (6), 4849-4861 (2004)
   PUBMED   14607836
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="Fpg/Nei family DNA glycosylase"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.-"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008534 - oxidized purine nucleobase
                     lesion DNA N-glycosylase activity [Evidence IEA]"
                     /GO_function="GO:0140078 - class I DNA-(apurinic or
                     apyrimidinic site) endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=29818
     Region          2..268
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtihrl aldhrsrfeg ervrvsspqg kftggaalid gqvmtgaeah gkhlflgfgp
       61 drwvhvhlgl fgklgfgaap appptdtvrl rlanpsgyad lrgpttceli tdaekhaihd
      121 rlgpdplrpg ddgtrawqri srsrttiaal lldqkviagv gnvyraevlf rhhidpyrag
      181 rdltraewda vwadlvflma egvrhnridt vrpehlpeam grpprvddhg gevyvyrrah
      241 mgchicgsev rtaglaarnl fwcpgcqpat ggg
//
LOCUS       WP_457695746             484 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695746
VERSION     WP_457695746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Shalaby,M.W., Dokla,E.M.E., Serya,R.A.T. and Abouzid,K.A.M.
  TITLE     Penicillin binding protein 2a: An overview and a medicinal
            chemistry perspective
  JOURNAL   Eur J Med Chem 199, 112312 (2020)
   PUBMED   32442851
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Shaku,M., Ealand,C., Matlhabe,O., Lala,R. and Kana,B.D.
  TITLE     Peptidoglycan biosynthesis and remodeling revisited
  JOURNAL   Adv Appl Microbiol 112, 67-103 (2020)
   PUBMED   32762868
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="peptidoglycan D,D-transpeptidase FtsI family
                     protein"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=50441
     Region          <74..484
                     /region_name="FtsI"
                     /note="Cell division protein FtsI, peptidoglycan
                     transpeptidase (Penicillin-binding protein 2) [Cell cycle
                     control, cell division, chromosome partitioning, Cell
                     wall/membrane/envelope biogenesis]; COG0768"
                     /db_xref="CDD:440531"
ORIGIN      
        1 mnkplrraav fclalivalm gwttwlqgak ageykedphn prvtigkysa plgnilvdgq
       61 pvtgsaatss slkykrtykd gplyapvtgf tsqifgsnql eslngdlldg tdsrlqsptd
      121 altrkrakgg dvvttidakv qkagyraldg kkgaavamdp atgrilgmvs tpsydpgtfa
      181 gsagadqkaw rkmsgdadhp evnralrqpl ppgsafklvv aaaalengly tsvdeptdsp
      241 dpytlphtrt eltnengaap cknadirtal qyscntvfak mavdlgkdkv kaqaekfgfn
      301 dgevdtpvra gksvypgnmd qaqtalsgig qfddqatplq mamvtsaian ggelktpqlv
      361 dkltdgggnt vedngpktyg dgktmsarsa qqlqsamqtv vdkgtgsaak idgltvggkt
      421 gtaqhgvdns gtpyawfvsn aedgngrrva vavmvedgha arnevsgngl aapiarammk
      481 aalp
//
LOCUS       WP_457695760             148 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695760
VERSION     WP_457695760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..148
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16026
     Region          24..146
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mhpqtapvtr tpirvragar phlltapstp lapktardfv ravlrrtpla plldtavllt
       61 seavtsshlr tprsadillr mlttghglri svhdeapvri prpatlageq eadhgllltg
      121 hladdwgttp ygglprstsf wfelhlkh
//
LOCUS       WP_457695762             559 aa            linear   BCT 27-JAN-2026
DEFINITION  CYTH and CHAD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695762
VERSION     WP_457695762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Lorenzo-Orts,L., Hohmann,U., Zhu,J. and Hothorn,M.
  TITLE     Molecular characterization of CHAD domains as inorganic
            polyphosphate-binding modules
  JOURNAL   Life Sci Alliance 2 (3) (2019)
   PUBMED   31133615
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Tumlirsch,T. and Jendrossek,D.
  TITLE     Proteins with CHADs (Conserved Histidine alpha-Helical Domains) Are
            Attached to Polyphosphate Granules In Vivo and Constitute a Novel
            Family of Polyphosphate-Associated Proteins (Phosins)
  JOURNAL   Appl Environ Microbiol 83 (7) (2017)
   PUBMED   28130300
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Martinez,J., Truffault,V. and Hothorn,M.
  TITLE     Structural Determinants for Substrate Binding and Catalysis in
            Triphosphate Tunnel Metalloenzymes
  JOURNAL   J Biol Chem 290 (38), 23348-23360 (2015)
   PUBMED   26221030
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Bettendorff,L. and Wins,P.
  TITLE     Thiamine triphosphatase and the CYTH superfamily of proteins
  JOURNAL   FEBS J 280 (24), 6443-6455 (2013)
   PUBMED   24021036
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Kohn,G., Delvaux,D., Lakaye,B., Servais,A.C., Scholer,G.,
            Fillet,M., Elias,B., Derochette,J.M., Crommen,J., Wins,P. and
            Bettendorff,L.
  TITLE     High inorganic triphosphatase activities in bacteria and mammalian
            cells: identification of the enzymes involved
  JOURNAL   PLoS One 7 (9), e43879 (2012)
   PUBMED   22984449
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The catalytic domains of thiamine triphosphatase and CyaB-like
            adenylyl cyclase define a novel superfamily of domains that bind
            organic phosphates
  JOURNAL   BMC Genomics 3 (1), 33 (2002)
   PUBMED   12456267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18995808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..559
                     /product="CYTH and CHAD domain-containing protein"
                     /EC_number="3.6.1.25"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050355 - inorganic triphosphate
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=59854
     Region          7..188
                     /region_name="CYTH-like_Pase"
                     /note="CYTH-like (also known as triphosphate tunnel
                     metalloenzyme (TTM)-like) Phosphatases; cd07374"
                     /db_xref="CDD:143620"
     Site            order(7,9,11,44,58,60,62,73,83,117,119,138,167,169)
                     /site_type="other"
                     /note="putative active site"
                     /db_xref="CDD:143620"
     Site            order(7,9,136,167,169)
                     /site_type="other"
                     /note="putative metal binding residues [ion binding]"
                     /db_xref="CDD:143620"
     Site            order(7,9,11)
                     /site_type="active"
                     /note="signature motif [active]"
                     /db_xref="CDD:143620"
     Site            order(9,11,44,58,62,73,83,119,167)
                     /site_type="other"
                     /note="putative triphosphate binding site [ion binding]"
                     /db_xref="CDD:143620"
     Region          266..553
                     /region_name="CHAD"
                     /note="CHAD domain, binds inorganic polyphosphates
                     [Function unknown]; COG5607"
                     /db_xref="CDD:444338"
ORIGIN      
        1 madtvreier kyeadddtgl pdlagvgria avaeagtedl dalyydttgl rlaadgitlr
       61 rrtggkdagw hlklpvapgv rdevraplse epppeltalv rsrvldrelv pvvrlrtrrt
      121 vrvlkdtaga plaevaedav rawpaagaag ageggagrag arwreievel lgegdtglld
      181 eigralaaag vrpasaaskl eralaetgqg gdgsaphtag pderrtdgsg kaaakakska
      241 kgsastqgka aakgaakgkg agkkgqtagd vvlryareqv rviieldpav rrdlpdavhr
      301 mrvatrrlrs afrsyskvld ravtrpigve lkwlaaelgv erdrevltgr lrealdgapg
      361 tlrlgpvdar lriwserrra gareqllavl dgprhlsllk tlhafleepp lrkaagrpap
      421 evvagavlkd yrrlarrtea alaapagrer dealhgarka akrtryaaea arpalgrpak
      481 kfarrtkrvq qllgdhqdsv varaalrela tqaqqagegg ftfgllygre ealaadrera
      541 lpelwrkvsr rkhraalrp
//
LOCUS       WP_457695785             365 aa            linear   BCT 27-JAN-2026
DEFINITION  M48 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457695785
VERSION     WP_457695785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 365)
  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 11574352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39787
     Region          66..269
                     /region_name="M48_Ste24p_like"
                     /note="M48 Ste24 endopeptidase-like, integral membrane
                     metallopeptidase; cd07325"
                     /db_xref="CDD:320684"
     Site            order(140..141,144,191,195,257)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320684"
     Site            order(140,144,191,257)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320684"
ORIGIN      
        1 mtespggsan vpsrdrrrfp gissrsyehp adrsalvalr klsgfdtvfk tlsgllpers
       61 lrllflsdsv rvsdqqfahl nhmlrdacyi ldlekvppmy vnqdpqpnam cigldepiiv
      121 vttglvelld eeemravvgh evghalsgha vyrtillflt nlamkvawip lgnvaimaiv
      181 talrewfrks elsadragll vgqdlqasmr glmklaggnh lhemnvdafl kqadeyesgg
      241 dlrdsvlkil nllprshpft tvraaelkkw aasrdyqrim dghyprrded kdtsvsdsfr
      301 dsaahyadsv rnskdplmgl vrdiaggagd lggklrdtvf rggprpdssg gangsggagg
      361 pddrs
//
LOCUS       WP_457695795             971 aa            linear   BCT 27-JAN-2026
DEFINITION  leucine--tRNA ligase [Streptomyces nigrescens].
ACCESSION   WP_457695795
VERSION     WP_457695795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   ALLEN,E.H., GLASSMAN,E. and SCHWEET,R.S.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes
  JOURNAL   J Biol Chem 235, 1061-1067 (1960)
   PUBMED   13792726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..971
                     /product="leucine--tRNA ligase"
                     /EC_number="6.1.1.4"
                     /GO_function="GO:0002161 - aminoacyl-tRNA deacylase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004823 - leucine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006429 - leucyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=106812
     Region          25..971
                     /region_name="LeuS"
                     /note="Leucyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0495"
                     /db_xref="CDD:440261"
ORIGIN      
        1 msettnspvv esvggaatet aaphrytaal aadiearwqd fweangtyea pnpkgdlagd
       61 aepvarpkkf imdmfpypsg aglhvghplg fiatdvyarh qrmtghnvlh tlgfdafglp
      121 aeqyavqtgt hprvsteani vnmrrqlrrl glghdqrrsi etidpayykw tqwiflqifn
      181 swydpeadaa rpidtlaaqf eagtrptpdg rawselspie ranvlgeyrl ayasdapvnw
      241 cpglgtvlan eevtadgrse rgnypvfkak lrqwnmrita yadrllndld aldwpeaikl
      301 qqrnwigrse garvdfpvgd dkitvfttrq dtlfgatymv lapehplvag sdngtgslvp
      361 dawpegthdv wtgghatpgd avaayrkqaa sksdverqae akdktgvftg afatnpvsge
      421 qvpvfiadyv lmgygtgaim avpahdsrdf afarafelpm rcvvepsdgr gtdpsawdda
      481 fasydakivn ssgatvsldg lgvteakaki tewladqgig egtvnfrlrd wlfsrqrywg
      541 epfpivyded gvahalpesm lplelpeved ysprtfdpdd adtqpetpls rnedwvnvdl
      601 dlgdgikryr retntmpnwa gscwyemryl dphnsdalvd peieqywmgp regqpaggvd
      661 lyvggaehav lhllyarfws kvlhdlghvs ssepfhklyn qgmiqafvyr dsrgiavpaa
      721 eveerdggyy yqgekvsrvl gkmgkslkna vtpdeicaey gadtlrlyem amgpldvsrp
      781 wdtravvgqy rllqrlwrnv vdeatgevtv vdtepdettl ralhkaidgv tqdmanlrfn
      841 taiakvteln nhltkagtpv prtvaerlvl liaplaphia eelwrklght dsvvhadfpv
      901 adpayvvdet vtcvvqikgk vkarlevaps isdadleaaa laepavvaal dgagirkviv
      961 rapklvnivp a
//
LOCUS       WP_457695801             161 aa            linear   BCT 27-JAN-2026
DEFINITION  RrF2 family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457695801
VERSION     WP_457695801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Schwartz,C.J., Giel,J.L., Patschkowski,T., Luther,C., Ruzicka,F.J.,
            Beinert,H. and Kiley,P.J.
  TITLE     IscR, an Fe-S cluster-containing transcription factor, represses
            expression of Escherichia coli genes encoding Fe-S cluster assembly
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 98 (26), 14895-14900 (2001)
   PUBMED   11742080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449279
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..161
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=17242
     Region          2..149
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrmsegvewg lhccvtlawl egdgpvstar laasfelpaa ylnkrlqalv ragvlsstpg
       61 arggfqlarp peritlmdvv aaiegtddvf rcteirrkga gavasgrefg rpcgistamr
      121 kaelawrrel aaqtladvma gtpasaaert rrwfaaerth t
//
LOCUS       WP_457695811             642 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457695811
VERSION     WP_457695811.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..642
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69349
     Region          1..639
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtdthtlien rppsvahlfl ervaatpdie ayrypvppsp klsasleqgg aptgqgpddw
       61 kviswsqaae rvyavaagli algvhpeerv alaantrvew iladlgvlcs gaatttvyps
      121 tnaeetayil adsgsrvlia edagqlakar aqraelpela hvvvideaga epaegdpegw
      181 vltlaelekr gtayleehpe cvkervaalr adqlatliyt sgttgrpkgv rlphdcwsym
      241 araiqatglv heddvqylwl plahvfgkvl tagqiatgqv iavdgrvdki ienlpvvrpt
      301 ymaavprife kvyngvaaka raggaaryki fqwaaevare yakvsqdnfr rtgsasvpfa
      361 lgakhkvada lvytklreaf ggqlraavsg saalspeigy ffsgagihil egygltessa
      421 asfvnpgeay rtgtvgkplp gtevriaedg eillrgpgim egyhglpdkt aevleedgwf
      481 htgdigelsp dgylritdrk kdliktsggk yiapaevegq fkavcpfvsn vlvhganrnf
      541 ctalialdep timtwaqehg lggksyaevv atgqvrelid gyvervnegl qrwqqirkfr
      601 llprdldieh gevtpslkik rpvvertfkd lldemyagar ea
//
LOCUS       WP_457695803             269 aa            linear   BCT 27-JAN-2026
DEFINITION  arylamine N-acetyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695803
VERSION     WP_457695803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Zhou,X., Ma,Z., Dong,D. and Wu,B.
  TITLE     Arylamine N-acetyltransferases: a structural perspective
  JOURNAL   Br J Pharmacol 169 (4), 748-760 (2013)
   PUBMED   23517104
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Sim,E., Walters,K. and Boukouvala,S.
  TITLE     Arylamine N-acetyltransferases: from structure to function
  JOURNAL   Drug Metab Rev 40 (3), 479-510 (2008)
   PUBMED   18642144
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Sim,E., Westwood,I. and Fullam,E.
  TITLE     Arylamine N-acetyltransferases
  JOURNAL   Expert Opin Drug Metab Toxicol 3 (2), 169-184 (2007)
   PUBMED   17428149
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Sinclair,J.C., Sandy,J., Delgoda,R., Sim,E. and Noble,M.E.
  TITLE     Structure of arylamine N-acetyltransferase reveals a catalytic
            triad
  JOURNAL   Nat Struct Biol 7 (7), 560-564 (2000)
   PUBMED   10876241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29340
     Region          7..251
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mdtaatdayl erigagrpas pdadalralh lshlrtvpfe nlsihlgeei vlaeqpvldk
       61 ivgarrggfc yelngafaml lgalgyevel laarvfgaeg rlgipydhla lrvqtpdgpw
      121 ladvgfgrhs hfplrwdsra eqtdpggvfr ieetergdld vlrdgsaqyr leqrprayad
      181 fevgcwwnqt sptshftqsl vcsrltetgr itlsgrtlvt tavdgareer qvgadevlaa
      241 yheyfgivld repvvgevpp pgvgghgrp
//
LOCUS       WP_457695816             192 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457695816
VERSION     WP_457695816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Knizewski,L., Kinch,L.N., Grishin,N.V., Rychlewski,L. and
            Ginalski,K.
  TITLE     Realm of PD-(D/E)XK nuclease superfamily revisited: detection of
            novel families with modified transitive meta profile searches
  JOURNAL   BMC Struct Biol 7, 40 (2007)
   PUBMED   17584917
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21249
     Region          11..176
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(25,41,77,103..104,117)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mtavderrmt elfenlevpe gvkiellrge ivmmagpdlv hneiveavqd qiprkrwrrl
       61 qtqdiailse ssepqpdlav lergvgpdsg rllpsemitm lvevvsknsv drdygikrsi
      121 yaagkvpgyl iidpivahcv lltepvgggd eadytvqrit kfgdpvplel lgmeldtsef
      181 gtlpnvrphr rp
//
LOCUS       WP_457695820             244 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457695820
VERSION     WP_457695820.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25590
     Region          24..230
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(72,74,76..77,156..157,179,219)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(72,74,76,156,179,219)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mhtaweeagw eqlgdgvarr rmpgwdetig viagatgvmi vdtgatlrdg adlrrairgv
       61 lgrgvthval thphfdhvlg taafagvevf gaaglgellr rgkdvlrhda mrhgvdrdaa
      121 aeaadllvap hhhvhdqltv elgdrqvlla nvgpghtahd lavlvpgrgg dpeivfcgdl
      181 veesgepqag pdalpqrwpg aldrllalgg edaryvpghg avvdarfvra qrdalaarfg
      241 vaps
//
LOCUS       WP_457695828             376 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695828
VERSION     WP_457695828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..376
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..376
                     /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=41887
     Region          35..304
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mpparkaagt drtgptaqps gaaegaaapa pktggrnpff dnakylaivl vamghvwepl
       61 tdgsraaeaf ymtvytfhmp afiiisgyfs rsfdmrkdrl qrlvtgvavp yilfetayaf
      121 fkrwadddpg hpislldpwf ltwflvalfi wrlttplwqi vrwpiplava iavlasvspd
      181 igddldlqrv lqflpffvlg lllrpehfkl vqrravrias lpifaaalvm aywaaprmss
      241 awfyhrdsaq elgttwwvga vmtpalfgcs ivlvacffaw vptrqtwftv lgagtlygyl
      301 lhgflakgsr fwgwfddyaw lhtplgeiav tliaggivta lctppvrrvf rfameptmaw
      361 afrkdpaeta rarvsg
//
LOCUS       WP_457695832             168 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457695832
VERSION     WP_457695832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..168
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18316
     Region          24..157
                     /region_name="COG3981"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443180"
ORIGIN      
        1 mdeflaegad saphsgmahe lrtwrgrwgt vdgfaeyvgm vggvmdherv dgvvplstrw
       61 wvdgdtylgr vafrhrltps llawgghigy gvrpgarrrg hatamlraav pvarhelgid
      121 pvlvtcddtn tasrkvieac ggifedqrdd klrywihaaa atagqqpq
//
LOCUS       WP_457695834             217 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695834
VERSION     WP_457695834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23407
     Region          12..204
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mnatksgqgr rivlwrhgqt awnlerrfqg stdielteag vgqarraarl laalgpdaii
       61 asdlqraaat arelaeltrl evthdaalre tyagswqglt hdeilaqyge qytawkrgep
      121 vrrgggelet evadraapvv lnhadklpen gtlvvvshgg tirttigrll gleahhwegl
      181 gglsnccwsv lgkgargwrl mehnagtlpe pvlgddd
//
LOCUS       WP_457695837             257 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695837
VERSION     WP_457695837.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27548
     Region          3..250
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 meltldglsv vtdgkslvrd lslevasgqv vglvgpngsg kstalrcvyr alrpssgtvr
       61 vgeddlsrls mrrsaqviaa mtqdgavdld ftveevislg raphlqgnqa lsrrerdlce
      121 ramdrldird larrgvltls ggerqrvlla ralvqepkil vldeptnhld vrhqvellsl
      181 lrdsgltvlv vlhdlnlaaa acdrlgvlsq grlvtagtpe evlttelvde vfgvkasiis
      241 hpltgdpqll ysltpsp
//
LOCUS       WP_457695842             264 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695842
VERSION     WP_457695842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 264)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
REFERENCE   5  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28891
     Region          7..100
                     /region_name="SoxR"
                     /note="DNA-binding transcriptional regulator, MerR family
                     [Transcription]; COG0789"
                     /db_xref="CDD:440552"
ORIGIN      
        1 mawstreiae lagtslravr hyhevgllde perrvngykq ytvahlvrll rikrlvdlgf
       61 slsqiaemgd addhpeealr aldaelaati erlqrarmel gfilrksapt dlppqfataa
      121 adtpmseadr lfvtvmsrvl gpqgmaawag lmkdplvdpa gaafdqlpad adehtradla
      181 erlvafvhal yrqhpglstl padarrgeef pkktvgsalq diyndaqvdv lrrlgillaa
      241 areagserrs epstqqrdad ghsa
//
LOCUS       WP_457695852             297 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457695852
VERSION     WP_457695852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..297
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30588
     Region          1..295
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,121,125,146..151,170..171,173,186,
                     207..208,229..230)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mkrvsfaefg gpdvlqlvda eephaspgri riavraagvn pvdwriregq iltahpielp
       61 agvgldaagv vdevgegveg vevgdhvfge gsstyaefav lsawarmpeg ltfeeaagyp
      121 svaetalrvi revgvrsgqt llvsgasggv gsavlqiard rgitvigtag aanqdylrsl
      181 gavattygeg wvervrqlgp vdaaldlags gvirelvelt gdpqkvisia dlaapelgvr
      241 fsgvagsvpe alveavglis rgklhipvqk sytlaeaaaa hidsqaghtr grrvliv
//
LOCUS       WP_457695854             202 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695854
VERSION     WP_457695854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22163
     Region          9..142
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtvptgrrer kkaatrqkia dtalrlfler gydavgirdv aaeadvavtt lfshfaskea
       61 lvfeqdedfe qrltqavtgr apheplipal rreihalvrh ctadsaapiw rlidgspvlr
      121 eyeesmrlrh aeslataiaa dpylsqttta crtiarfvid ayslareaad peaavdeifr
      181 mieaawevac psrnsttgta gp
//
LOCUS       WP_457695859             644 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457695859
VERSION     WP_457695859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..644
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=68171
     Region          28..269
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(37..38,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(98,100,138,140,142,158,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(154..162,175..182)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mnllnpddpr aigpyrllgl lgeggmgrvy larseggrtv avkvvraefa rqddfqqrfa
       61 revdaarrvg gdwtapvldf dtsaatpwva tgyvpgpdlq tvvaddygpl perslrplan
      121 rlalalgaih daglvhrdlk psnvlvtvdg prvidfgiar alhaasgngf rtrtgvvigs
      181 pgfmspeqar glevgpqsdv fslgavlaya atgrppfgsp siglhaqlfr vaeeepdleg
      241 vpedvlglvr qclekapeer ptpaelvart aagqvrpwlp gevleqlgrh aawlldldpq
      301 grtsvvpvdt qpdvsveapl daradvqpdi pvdaymevqs dvpvvvsvgt ptsggrptqp
      361 sapparsrfk rarflgavvg vlvlsvgvpi aanswdgnga dpggsggtng gaggsdeptp
      421 aavavpknfl gawegvplsd trvrvefkkd aqhrtvarsf fltgtslcvv nkepkkaske
      481 svslgdarne nafsggkckf lpsytlkark dgnldfatdn grykvilska rageapvpek
      541 yvgqwvpkge agdpkaqvti eqaktgeffv rgwdnshqkh ctwrevlvfv ndtglvsrpv
      601 yrrgsadpcg maptgargya ladsgvlsmg hgaqklefvr kpga
//
LOCUS       WP_457695871             207 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695871
VERSION     WP_457695871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22058
     Region          6..207
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mnvrsgrapa paprheliad aaldllaerg mrglthravd qaaglpqgst snlartraal
       61 letavrrlae reaavltpre mpqppaegag pdgmtaavad alslalhryl srhrelliar
      121 yelaleatrr pelravydra grafrepvta mlaaagstap erhalsmiaw cdgvlfscia
      181 gqfhtavptr talrtscael ldgmlrg
//
LOCUS       WP_457695875             302 aa            linear   BCT 27-JAN-2026
DEFINITION  Gfo/Idh/MocA family protein [Streptomyces nigrescens].
ACCESSION   WP_457695875
VERSION     WP_457695875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32984
     Region          1..292
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkvgciglgd iaqkaylpvl gtqpglelhl htrtpatlqr agathrlpaa qlhpeldsll
       61 atgldaafvh aatsahpeiv trlieagvpt yvdkpiayel atsqrivtla edrgvgltvg
      121 fnrrfapayt qcrehardli lmqknriglp edprtlvldd fihvvdtlrf lvpgevdhid
      181 vrarirdglm qhvvlqlsgd gftavgtmnr lsgsteeild vsgqdtkrqv vnlaevidhk
      241 gqpsirrrgd wvpvarqrgi eqivlafldd vragrqpsar dalrthelce rvvtdalaqt
      301 ac
//
LOCUS       WP_457695880             647 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695880
VERSION     WP_457695880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 647)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 647)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 647)
  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 647)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..647
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69491
     Region          22..620
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mdmevtawha lhssmtaqqg rrrfsrgtlr ritafarphr rhlvwflvls tvtamlavat
       61 pllagrvvda ivggdspslv vslsvliavi avaeaglgll trwlsasige glildlrttv
      121 ydhvqrmpia fftrtrtgal vsrlnndvig aqrafsdtls gvvsnivtll ltlgvmltls
      181 wqitlialvl lpvfvlparr vgrrladlrr egadhnaemg tqmterfsap gatlvklmgr
      241 pahesaefat rarrvrdigv rsamvqtyfv taltlvsala lavvyglggf lalrgqleag
      301 aivslalllt rlyapltals gahievmsal vsfervfevl dlkplitekp daravpegpv
      361 svefdsvrfg ypsadkvsla sleevatldt rggeevlhgi sfraepgqmv alvgssgagk
      421 stvaqllprl ydtdagavrl agvdvrdlta aslrdvlgmv tqdghlfhas irenlllakp
      481 eateaelwda lrrarleeli aglpdgldtv vgergyrlsg gerqrltiar lllahprvvi
      541 ldeatahldn tseaavqeal tealdgrtal viahrlstvr aadqilvveg grivergthe
      601 tllaaegrya elyrtqftds edrhaaavea grpdsgpdll pesalvn
//
LOCUS       WP_457695882             268 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695882
VERSION     WP_457695882.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10637359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27419
     Region          9..110
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
ORIGIN      
        1 mvavgsdhdl rraldriaet aasltgarra avgihdedgr pgdlithgas peaeppigas
       61 lkvpirvqge lfgtlhlagk ddgeefgdgd lhlvrvlate agialsnarl hsaarqrrrw
      121 idgaasvtta lpaglgtrst atnaltvvae qgrelaeatt gavllphaeg gmevvaistv
      181 lsesvqfvgp vdarvddrsg relvtalgev latvgasaps qparvsvvvd atatlpdgra
      241 gvrltvscpd gshptltwer plkgrsgs
//
LOCUS       WP_457695883             177 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695883
VERSION     WP_457695883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19326
     Region          2..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtrtplsdva csiaratdlf cdawtalimr dvltgigrfd elahdlgisr kvltarlsrl
       61 veegvlarer yqerpprehy vatrkgrely pvllalmhwg drwyagedgp parihhlgcd
      121 rdttmvavcg hcgepltadn trqlpgpggr tgpgtqvigp liasraphsd tapeple
//
LOCUS       WP_457695885             257 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457695885
VERSION     WP_457695885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26856
     Region          39..148
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mgsapliald sadpdavdgr qiraaafqgv rlaytsgvle rhgrprsgha lvvgsgrgll
       61 arglaglgfq vtavdpsesa salaraaaer dgltiehrta paerpavpea sfdlvyladt
      121 leitadpdrv veqaaralap dgvlvydtvt rtpvsrlvyl vafqrlpmtr ivpagryaas
      181 rlrtpsevaa llarhgltdg gvcdfkphsv rsliagvrar ragrvsddal eavagfafap
      241 gskplvtylg harkgrl
//
LOCUS       WP_457695887             129 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695887
VERSION     WP_457695887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..129
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13057
     Region          8..102
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(18,20..22,28,51,53..55,57..59,62..63,87,91..92,94)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            54
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mgpsraaggt tvlelrgeld ilavsvlsdr lddltgvqgt dllldvravt fidcaglsll
       61 sraryrtrqr ggrlrltgvt rggsvgrllr mtgltgafei vsdeegaeep aaggagsaev
      121 tdgagtava
//
LOCUS       WP_457695894             422 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457695894
VERSION     WP_457695894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 422)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=44189
     Region          3..416
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mtrrvavtgv givapggvgv pafwdllssg rtatrgitlf npegfrsria aecdfdpvah
       61 glseeqvars dryiqfamva anealrsagl dteaedpwri gvslgtavgg ttrlehdyva
      121 vsshgarwdv dhrpagrhle rafspsslas avaeqigahg pvqtvstgct sgldaigyaf
      181 htieegrvdv ciagasdspi spitvacfda ikatsanndd pahasrpfda hrdgfvmgeg
      241 gavlvleele harargatih ceirgyatfg nayhmtgltq eglemaeain salgharida
      301 tqvdyvnahg sgtqqndrhe taavkrslga hahrvpmssi ksmvghslga igaieivacv
      361 lalthqvvpp tanyetpdpe cdldyvpkta relplrsvls vgsgfggfqs avvltrqggr
      421 as
//
LOCUS       WP_457695902             266 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457695902
VERSION     WP_457695902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29077
     Region          34..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          97..260
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mvvfagqgda rrsmallwra egsagtrtrr wpgpkpalsv aaivdagvav adadgmaals
       61 mravgerlgr tamalytyvp gkselvdlmy dqvlaelpad ydltpgwraa vtswaedtwe
      121 fylrhpwvlq vsqarpvlgp neyrametll rllyatelss tvlrrvvgal fhfirgaaqt
      181 vtesrlaaas tgvsdeewwq arsgmltemv pdfaerypll vrletegaap dpgdsvpyme
      241 rearstfdig ltvildgiea airqgr
//
LOCUS       WP_457695908             124 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457695908
VERSION     WP_457695908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..124
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13000
     Region          7..115
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mtslvrhitv dctdayrlas fwaevldgsl aeddlpgdpe atvtaaggal lfitvpeaka
       61 gknrvhldlq pqdggrdaev erllalgatl vadhrradgt gwatladieg nefcversaa
      121 erag
//
LOCUS       WP_457695906             287 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457695906
VERSION     WP_457695906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31369
     Region          1..264
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtavpvaliq vtdvrritph mvrvtfagdg lddfptwpdq qlkllfprpg rraprlpdva
       61 adgdamswyq aflalpeder pwmrsytvrs ydpvrhriti dfvlhgttet agpatrwaas
      121 aavgdllary gpaaayakpl pldradwlll agdatalpai gslvealpag tralacievt
      181 gaaeeqhftt radltvqwvh adgrhdalpa avraltfppg svfawlagea gavralrrhl
      241 veergidkrq idfsgywrrt ltqddaptee dlaeaqerla aarplqd
//
LOCUS       WP_457695909             132 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457695909
VERSION     WP_457695909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 132)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..132
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13644
     Region          13..87
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(16..17,19,22,25..26,29..30,33,63,83,85..87,89..91)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(17..18,22..24,37..39,48..51,53..54,57..58,60..61,
                     67..69,74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mngawfpvcq akadffrmlg hpvrirvlel lqsglmpvsg llsaigveps alsqqlavlr
       61 rsglvtatrs gstvvyelag gevtellraa rraltevltg qhalltelrq adararptag
      121 gvpatggvga vs
//
LOCUS       WP_457695914             247 aa            linear   BCT 27-JAN-2026
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695914
VERSION     WP_457695914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25790
     Region          48..217
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mgvqllvlea lrrvaglstt gwltgcafal atwvvltlal rrswtpsfgm anrvtlarti
       61 lvggvtalva dsferpapvv vlvtlaaval vldavdgqva rrtgtvtplg arfdmevdaf
      121 lilvlcvhla mplgpwvlai glmryvfvaa swlwpwlrga lphsmarktv aalqgvvlvv
      181 agagvlpras aatavsgala llvwsfgrdv awlwrvrglt sgpaavsgpa ragtgprams
      241 rragpdr
//
LOCUS       WP_457695918             372 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457695918
VERSION     WP_457695918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=38515
     Region          24..362
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mtrtgataae rvvhfvlpgd vddpaapsgg niydrrvcrd lpsagwqvrp yalpgswprp
       61 datacaglaq rlaalpdgav vlldglvacg vpevlapeaa rlrlavlvhl pladetgldp
      121 alaaeldare hrtlhaveav vatsdwaarr lvthhglaaa rvhaalpgad paplapgtdg
      181 aagllcvaav tprkghrrli dalatvtelp wscacvgald rdpgyvaqlr gavatfglgd
      241 ritftgpqag adleasynaa dllvltsyae tygmvvteal argipvlata vdgvpeavgq
      301 apdgsvpgll vppgrpaala dalrgwlgdp qlrdrvrssa rgrramlegw emtshslagv
      361 leqlrhkprs tr
//
LOCUS       WP_457695922             383 aa            linear   BCT 27-JAN-2026
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces nigrescens].
ACCESSION   WP_457695922
VERSION     WP_457695922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=38849
     Region          35..306
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkrsgwvawl rllaglgilv alvwhlgsha flaglrrida atllaalgig vlttvcsawr
       61 wclvarglgl rlplgravad yyralflnaa lpggvlgdvh ravhhgrssg dlgrgvrava
      121 lertagqvvl lvtgavvllv rpspvlapva rfltspaval svaaagllvl avtvrlrrrr
      181 gasrgeralr tvvaearqgl largvwpgva lssaavlagy lgmfvlaarv agvtaptael
      241 vplvvlalla malplnvggw gpregvaawa fgaaglgaaq glttaviyga lafvaslpga
      301 vvllarvspl saarpaasga vplgiripsk eptrsgterk aerpplaaat gmirqraaev
      361 psavaggarp qapqataarg dts
//
LOCUS       WP_457695923             279 aa            linear   BCT 27-JAN-2026
DEFINITION  RibD family protein [Streptomyces nigrescens].
ACCESSION   WP_457695923
VERSION     WP_457695923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Stenmark,P., Moche,M., Gurmu,D. and Nordlund,P.
  TITLE     The crystal structure of the bifunctional deaminase/reductase RibD
            of the riboflavin biosynthetic pathway in Escherichia coli:
            implications for the reductive mechanism
  JOURNAL   J Mol Biol 373 (1), 48-64 (2007)
   PUBMED   17765262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="RibD family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29350
     Region          66..268
                     /region_name="RibD"
                     /note="Pyrimidine reductase, riboflavin biosynthesis
                     [Coenzyme transport and metabolism]; COG1985"
                     /db_xref="CDD:441588"
ORIGIN      
        1 mtelldaaaa wdrlrrirtt deaiaagmva dgdgglrwer patpeamela grylplclag
       61 prfafaqlgq sldgfiatrt gdadyvtgae drchlhrlra lsdavvvgag tavaddpqlt
      121 vracagdnpv rvvldprgrv prdigvftdg aaptlwvvgp evtptapgtg tevlvlpdaa
      181 afaperllta larrglgrvl iegggvtvsr flqeralhrl yvtvapvllg dgipglrfpg
      241 tpvmrealrp plrrallged tlfelelrpg ggpfggtad
//
LOCUS       WP_457695930             190 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457695930
VERSION     WP_457695930.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20088
     Region          2..181
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mttrvmlvsp aageaqrevr fdddgplsea glrrvraaag alpaadrtfa spsarcrrta
       61 eelglsvlpa gelagcamgg wrgrtlteva daepvavstw lsdpdftghg geslrqlcdr
      121 iagwltrmal esgrvlavve pdvvraaavc alrvspdafw rldvppltvt elsgrggrwn
      181 lglgrelgrr
//
LOCUS       WP_457695938             608 aa            linear   BCT 27-JAN-2026
DEFINITION  alkyl/aryl-sulfatase [Streptomyces nigrescens].
ACCESSION   WP_457695938
VERSION     WP_457695938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Diene,S.M., Pontarotti,P., Azza,S., Armstrong,N., Pinault,L.,
            Chabriere,E., Colson,P., Rolain,J.M. and Raoult,D.
  TITLE     Origin, Diversity, and Multiple Roles of Enzymes with
            Metallo-beta-Lactamase Fold from Different Organisms
  JOURNAL   Cells 12 (13) (2023)
   PUBMED   37443786
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Hagelueken,G., Adams,T.M., Wiehlmann,L., Widow,U., Kolmar,H.,
            Tummler,B., Heinz,D.W. and Schubert,W.D.
  TITLE     The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas
            aeruginosa, defines a third class of sulfatases
  JOURNAL   Proc Natl Acad Sci U S A 103 (20), 7631-7636 (2006)
   PUBMED   16684886
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10824]
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..608
                     /product="alkyl/aryl-sulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0008484 - sulfuric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046983 - protein dimerization activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65848
     Region          5..606
                     /region_name="BDS1"
                     /note="Alkyl sulfatase BDS1 and related hydrolases,
                     metallo-beta-lactamase superfamily [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2015"
                     /db_xref="CDD:441618"
ORIGIN      
        1 mtavpvddhe dfadadrgfi aaldppqvta ddgrviwdae aygflagncp dtaneslwrq
       61 grlvsrqgly evtdgiyqar gldlshmtlv egdhgvivid pllsietaaa alelyrkyrg
      121 drpvtgliyt hshgahfggg rgvlppghhp vpvlapagfl ehavsegiya rtamtrravy
      181 mygselpkgp dgqigcglga ahstgtvtli pptvditrtg qeeivdgiri vfqltpgtea
      241 paemnfcfpa hqalclaena thtmhniltl rggavrdara wshhlgeala lfgdeaevaf
      301 ashhwptwgk drvkallahq rdlyaylhdq tlrllneglt gaeiaeelrl ppglervwah
      361 hgyygslshn vkgiyqrylg wfdgnpahlw ehppaeqarr yvdtlggvea tvdagkryaa
      421 egdlrfaatl lnhavfaapq nlrarrelal vyerlgygce ngtwrnvylt gamelrgsla
      481 eavpgtvhpd iamaltvdql idslairidg prawstaltl dlylpeedrt wqltlshgal
      541 tyisapgvpt psedrtpdlt ltltksqllg lltgqgpgda aqhgetgalh qllgllstph
      601 ptfpvvtp
//
LOCUS       WP_457695940             677 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457695940
VERSION     WP_457695940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..677
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72488
     Region          6..677
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 masnipeest sfvgrqaelr riddeltehr litltgpggv gktriamraa raaaarfpdg
       61 vcwadlwplq gdgllvasvc davgladhta rtpvaalcew ladkrlllvl dscehlvdac
      121 rdllgdllta apavtvlvts rqpldivgew tteigplpyt gdndaltlft qragaaapgl
      181 rlttplhaea aavicrrleg iplalelaga qlahssveri aerltsrfda ldpadgpvrl
      241 prhrtlrcai gwshelcapl erllwarlsv frgtfdeesa savcaggplt gpgvrstlaa
      301 laaksvltre gtrfrmldtl reygrmwlae lgegtaladr haahfadfgr raelgwlgpe
      361 qvswyrrvad ahvdlctald hllvtdpvra qelsasiglf wsccghlhea rnyvaralaa
      421 qpdpspartr alwalgvavl lqgdlalada lglecaraar asddaeavla agylmslthl
      481 iagrpmsaht vaeqvlgppp ddpfdspgrl rchlvqifal tglgelarar aeatalrrgc
      541 vergeywtrs ytdyqlslis lfqgrpeesa dharamlaak qgigdkfgia lgldllaaav
      601 aaqgdgaaaa rvygsghaiw rtvghpqrgt pelravreec eqraraaigd eayselfhra
      661 seerpgtsla rilagdl
//
LOCUS       WP_457695942             346 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457695942
VERSION     WP_457695942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37115
     Region          9..343
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mspdrpgpal adrladavtl idapdivlav trrgrrtvmt ggsamapptp rhalryelgs
       61 lsktftvlll aelarsgvls ledplaahlp dlplphpysr ritlrhlath tsglpripad
      121 liagalvhpy sngyarydte rllqtfartr prnepgtrwr ysnfglallg pamsraagag
      181 ypalltdrll splkltdttl gpgttgtdai ghrtngvtpv gsadmgafia agsvratpgd
      241 lltyleahls pedtplagpl rdvqvpqlrr gwrkrnthtl twyqhpaarg pllfhvgatf
      301 gqqaflgyhp ashtglvala trrgrtchmi ntayellytl agdpsp
//
LOCUS       WP_457695949             412 aa            linear   BCT 27-JAN-2026
DEFINITION  M4 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457695949
VERSION     WP_457695949.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  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 412)
  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..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /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=43365
     Region          <86..412
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrqklalgva vsaaavlgaa vqsvpasagt snnasapggr sgaesvssar eeaaqrvegs
       61 tasegatsva kattsagaet saesrtgtgk gvyvgkvkit trlrngkyel tdptrgglst
      121 vdfgnranrd essgkrftds dnvwgngtvs srqsaavdvy faagktwdyy kktfgrkgmr
      181 dngngpstiv hygkgvasae hdndlwfgdg kddknpltel divahefthg vtfstagfag
      241 tsessglnea tcdifgtmve fdasiaadtp dyligekvnf hgdgkpmrym dkpskdgrsp
      301 dywkpgidrl ddphhaagva nhffyllaeg sgkkvingva ydsptydgsk vtgigrekaa
      361 kiwykalttq fasdtdyksa ragtlktaaa lygktsseyr tvqkawtavn vk
//
LOCUS       WP_457695951             135 aa            linear   BCT 27-JAN-2026
DEFINITION  TOBE domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695951
VERSION     WP_457695951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..135
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14279
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mptysigqaa gllgvsaetv rrwadggqlr merdgtgnrv fdgvslaafa kqraaglhpv
       61 pgevltsvrn sfagivtrvt ldeviaqvei qsgphrlvsv vsreaveelg ievgvtatar
      121 vksthvhidl pddrr
//
LOCUS       WP_457695955             139 aa            linear   BCT 27-JAN-2026
DEFINITION  TOBE domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457695955
VERSION     WP_457695955.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13738
     Region          1..137
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mslsirnqip gtvasvtpge vmatvkvrld ggqeitaait reavrelglt egsavrtlik
       61 stevalatga veglsirnri pgtvtevatg gamagvkvav aggeltaait rdavedlgla
      121 agsevtalik steialaas
//
LOCUS       WP_457695962             489 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457695962
VERSION     WP_457695962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50665
     Region          14..434
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstqpatsaa psprtartlg rnaigtgdlv ffvvaaaapl tvmagaapva igmagqaapl
       61 gyllsgllmi vfaagftams rhvrnagafy ayigrglgra vgvgaayvav lsynaievgl
      121 lavfgwftes gfqdltgvqv pwwvwatagl vaigvlgclk vtlsakvlav alalevlill
      181 vfeaavyahg ggpdgprfga lspahlgtag aggmfvlsvg afigfeatav yaeearrper
      241 svpratylav gflalfytft vwtvlnayga drartvanga agtdmvfaat arfagawaad
      301 amqllivtsa faatlafhng atryfyalgr erllprrlgt vtarhrspaa avvlqsaial
      361 vvvlatlltg qdpyavtflw sngtgilgim llqalaalav ygffrrdrrg lpawrvvaap
      421 ltagaglvvl ivlvcrnfgl lteastavnl allaplplvf algpavalri rhrapraytr
      481 lttvdverg
//
LOCUS       WP_457695964             484 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces nigrescens].
ACCESSION   WP_457695964
VERSION     WP_457695964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..484
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49638
     Region          3..483
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mkrfpsfrad ftaslvvflv avplcvgvav asgvpaelgl vtgvvggllt gllpgsslqv
       61 sgpaagltvl vfeavkeygl galgalvlaa gvlqlamgal klgrwfrais vavvqgmlag
      121 iglvliagql yaltdakapg sglanigglp dlvtstvrsg salaalaiga gtiavlvlwp
      181 rwrraarvlp aplaavalat tavwaldmpv arvevsglld aiqppglddl gqlgsvgvig
      241 tvlafalias aeslfsaaav drlhdgprtd ydkelmaqga gnavcgvlga lpmtavivrs
      301 aanvqagakt kasrvlhgfw llvfaaafpa algvvpvaal agvlvhagck liplrdlrpl
      361 wrehrgeavv llvtaiaivt vsmfegvlig llmavaktaw etshihldvq ipedtaepvq
      421 vraignatfl rlpklldqle tlpadrdvel dlsglrhldh acgaaltnwa eqhrrsarev
      481 elvs
//
LOCUS       WP_457695978             339 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457695978
VERSION     WP_457695978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34434
     Region          18..333
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtacaalvlv llasivvaig lgsavitpgd tawylwsals ggriaadevt tyqiiwqirt
       61 prvllaalvg aglsaigaai qamvrnalad pfvlgvssga svgavgvtvt gglaalgiya
      121 vsagaflgal vasllvyvas ssrgalsplr lvltgvalsl gfqavmsvii yfapdseats
      181 mvlywtmgsf gaatwgalpv vsvavilgla vlyrygrald ilalgdetaa slginpdrhr
      241 kgllvlvslv tgvmvavsga iafvglvmph lvrmvagath arvlavapla gaifmvwvdl
      301 vsrtlvapre lplgvitalv gvpvfivlmr rkgymfggr
//
LOCUS       WP_457695985             440 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase [Streptomyces nigrescens].
ACCESSION   WP_457695985
VERSION     WP_457695985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /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=46234
     Region          95..276
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          282..410
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 meqlvappht pasdrprpph llphsveqqv pdaprrsrrt rrmpavtvll aagalalsac
       61 gagpsaggnd dgknngaaav nssdakiklp skdgatdagi ndvsvkvtgg kltevkltea
      121 dsgkvvagai ssdgaswkpg vqlergtkyr ivakakdakg raatenasff tvssansfig
      181 sytpdngktv gvgmpvsfkf dkaitnkkdv qshitvtsss gqkvvghwfg tqrldfrped
      241 ywkagskvtm kidldgvkgg qgitgvqskt vsfaigrsqv stvdmntqtm tvkrdgktlk
      301 nvpisggspe nptyngqmvi sekleqtrmd gstvgfdkqn tydipdvpha mrlsdsgtfl
      361 hgnywgspsi fgnsgtshgc vglqdnqggg gdtpgkwffn esligdvvvv knsdeqtikp
      421 dnglngwnls wtdwqagsaa
//
LOCUS       WP_457695982             544 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457695982
VERSION     WP_457695982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12021846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..544
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=58526
     Region          8..365
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mnptaedrvp vlivggslvg lsaslflgrl gvrhllvekh sdtsrhprgr gnnvrtmely
       61 rvagaeqrir eaastladnh gilqarsltg ddqewlfkei dpggglarfs psawclcsqn
      121 dlepvlvrca rehggdlrfs telssfeqda qgvtavlrnr etgeqstvha dyliaadgpr
      181 spvrerlgig qtgpgdlfhn vsitfrapal adavgdrrfi acyltnpead gallpvdnra
      241 ewvfhapwhp drgetledft dercidhirr atgvpdmave itgkapwhaa ervaerygag
      301 rvflagdsah emsptgafgs ntgiqdahnl awklatvlng sagpgllasy eaerqpvare
      361 tsarasarsa ehshpgyapa pgtgggrqrg vltvalgycy pqgavvgtdp elpvvpeqmr
      421 ltgepgtrap hmwlqaager rstldlyeks fvlltgsdge mwrtaakgan eefslglqcy
      481 migtgpnddm apeedadwae khgttpegav lvrpdgfvaw raegrvadpe aalrevlasl
      541 lcrs
//
LOCUS       WP_457695995             296 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces nigrescens].
ACCESSION   WP_457695995
VERSION     WP_457695995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=30115
     Region          2..259
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mttppallia ghgtrdegga dalralvrll gerhpevpva ggffgvpasp lplddaidgl
       61 vgkgatqlav iplltaptgp vpealpavle ragerhpglg hvcgaglgph pklldvlerr
      121 ldealgsgar rpadrarttv llvgrgaadp yanaevvraa rllwegrgfa gvetafvsqa
      181 apdvpagldr cralaaaagt ggpgrivvlp yflfaggpve rlwmqaegwa aahpdtevya
      241 aqvigpeaev advvmeryrt avagascgcr aaaedarpvh gaaresapla agtger
//
LOCUS       WP_457695998             188 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces sp. 900105755].
ACCESSION   WP_457695998
VERSION     WP_457695998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20686
     Region          8..167
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          96..174
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mspmtsgdyv irairadewe avkrlrlval qdpvadvafl etyddalgrp dsfyreraar
       61 saeeasgarq fiaetadgew agtvtvliee agstdwagfp verrqghvvg vfvrpehrgs
      121 glvkalfdag vtwarergaq rvrllvhedn praqgayrka gfvpsgvtvr leadagkref
      181 efvlewpa
//
LOCUS       WP_457696021             375 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696021
VERSION     WP_457696021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39876
     Region          148..371
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrlgtaaava aitvigagaa avavgryasd ialkpspdqp fpgdsrltvh sateerialt
       61 rslaslrpgt ygltgsgcha vigdvihgvp hpadavvrrl vrvthgtlgp gnrmlltpqv
      121 hignprdalg ldcadvdipg elgplpawfv pgvrdtwvit ahglgttreh pmvvmpflhr
      181 hrlpvlalsy rndlgaprta dginhlgdte wrdldaairy alrygaqdvv lhgwstgatm
      241 alraathsal rdrisgivld spvldrnatv ralaaarrip rallplvvra aegstglpld
      301 hpayavdpde leiptllfhg pddqiapwta srsfaarrad lvtlqpvpha phaamwnadp
      361 sgyeealrrf ltplm
//
LOCUS       WP_457696024             532 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457696024
VERSION     WP_457696024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..532
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57414
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mitasglelr agariliesa sfriakgdri glvgrngagk ttltkvlage gipasgtvtr
       61 ggqvgylpqd prtgdldvla rdrilsardl dtvlrkmren edrmangkga trdkamkkye
      121 rletefltkg gyaaeaeaat iaaslglpdr ilgqplhtls ggqrrrvela rilfsdsdtl
      181 lldeptnhld adsivwlrdy lktyrggfiv ishdvdlvet vvnkvfylda nrsqidvynm
      241 gwklyqqqre adekrrkrer anaekkaaal ntqadkmrak atktvaaqnm akradkllag
      301 leavrasdkv aklrfpdpap cgktpltaeg lsksygslei ftdvdlaidk gsrvvilgln
      361 gagkttllrl lagvetpdtg avrpghglkl gyyaqehetl dpdrtvlenm rsaapdmdlv
      421 airktlgsfl fsgddvdkpa gvlsggektr lalatlvvss anvllldept nnldpasree
      481 ilgalhtftg avvlvthdeg avdalqperi illpdgvedl wgqdyadlva la
//
LOCUS       WP_457696035             197 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696035
VERSION     WP_457696035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21098
     Region          2..187
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mrigvylahp rpgsfnhavf davveelggr gcqviahdly aegftpllsa detetvgaas
       61 ptqdsqvmlh rtevatldgm vfvhpnwwgm ppavltgwvq rvlapgvayk lgtaegepig
      121 lmkagralvl ntsdtpadre esefgdplqs iwascvlpyv gvsdvrravf rtvtgsadet
      181 radwlqqarr eaaalla
//
LOCUS       WP_457696044             210 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696044
VERSION     WP_457696044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22577
     Region          1..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrtaltgee vltaaarlvr adgpgaltmr rlatelgtav tsiywhvgnr eslldalver
       61 tvremgeihp sgetphariv svahalhsal rerpqliamv hergltermf lpaqqalvhe
      121 mhaaglrget aaealravqf qvvgfvlver nrerspeqhp segelwdspt aehdpalara
      181 lagpvdtgrl ftvslealvt sllspaasas
//
LOCUS       WP_457696051             411 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696051
VERSION     WP_457696051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44552
     Region          57..369
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mtddrytvis adchagadll dyrpylesry hedfdawaaa yvnphedlla dtadrnwnsa
       61 rrlaeleadg ivaevvfpnt ippffpsasl mapaptrtes eqrwaglrah nrwladfcae
      121 apgrragvaq illndvdeav revrrtreag ltggvmlpgt ppgsglpelh saaydplwav
      181 caelgvpvnh hggsaspplg depaaravfm vettwfshra lwhlifggaf rrhpglrlvl
      241 teqgsgwipg vldmldyyhg rlvasasasr aataeakfgv glgeamgdsp agiwrdhcfv
      301 gasfmrphev plrhrigldk imwgsdyphd egthphsrea lrlayagvpd detaamlgtn
      361 aarvygfdla rlaplaarvg pritdlaepl eeippnatsp afarggavrv w
//
LOCUS       WP_457696052             303 aa            linear   BCT 27-JAN-2026
DEFINITION  sterol desaturase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696052
VERSION     WP_457696052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34188
     Region          91..238
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mphlpdvvlw svpafvlltv vemvsyrlhp dedaagyeak daatsvgmgl gslvfdalwk
       61 ipivaiyaai yeltplrvpv lwwtlllmll aqdffyywsh rghhvirvlw achvvhhssk
      121 kfnlttalrq pwttwtvwpf yvpmvalgvh paviaftsgv nlvyqfwvht ervdklprpf
      181 efvlntpshh rvhhasqggy ldrnfggili iwdrmfgsfv aeterpvygl tkniesfnpl
      241 rvatheyaai ardiraadsw reragrvfrg pgwqpaeria aeearkagls gdragasvee
      301 paa
//
LOCUS       WP_457696061             545 aa            linear   BCT 27-JAN-2026
DEFINITION  solute symporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457696061
VERSION     WP_457696061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10008332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..545
                     /product="solute symporter family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015123 - acetate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56360
     Region          12..544
                     /region_name="ActP"
                     /note="Na+(or H+)/acetate symporter ActP [Energy
                     production and conversion]; COG4147"
                     /db_xref="CDD:443318"
ORIGIN      
        1 mnltqqplvq qlaaggageh raliitlfav fvvatlaitv wagrqtkgae dfyaggrqfs
       61 gfqnglaisg dymsaasflg iagaialfgy dgflysigfl vawlvalllv aeplrnsgrf
      121 tmgdvlayrm rqrpvrtaag tstivvsify llaqmagaga lvtlllgits eagkilvvvl
      181 vgivmilyvt iggmkgttwv qmvkavllia gtllitflva lkfnfnlssl lgaaaensgq
      241 gaaflepglk ygvsatskid fislglalvl gtaglphili rfytvptaka arksvnwaig
      301 iigvfylmti algfgaaali kpetitasnk agntaaplla eaigggpgst ggaillavis
      361 avafatilav vagltlasss sfahdlyvnv frkgkateke evgaarwatv gigavaivlg
      421 vfarglnvag lvalafavaa sanlptllys lfwkrfttqg alwsiyggla ssvflvlfsp
      481 vvsgketsmf paadfaffpl enpglisipl gfllgwlgsl lskeepdaqk yaelevrslt
      541 gtgah
//
LOCUS       WP_457696073             398 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696073
VERSION     WP_457696073.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42119
     Region          52..322
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mpgpaaadgp hgiddlraga haaepaepae padfesrldr rgvqflprpd vpeppevsal
       61 swmvtdmadg kvlaakdahr plppastlkt lfaltvlpkf sqgavhtvsl edlagiesgs
      121 slaglkedmp yqvvdlwhgv flssgsdavh tlasmnggwh ktiddmqeta rrlgardtrv
      181 gsadgfdtpg qvssaydlsl fgqagltdpd fahfastkwa elpqdggpda ftlqntnrll
      241 vgshgvrpyd gligvkngyt thagntliaa arrdgrtllv tlmnpqsggr navyeetrdl
      301 ldwgfeaapr aaavgvlpgv apeertgepq pvahrprpvp lhkagvavqp dgerltryrw
      361 flsaagavgi iavvglgtal wrrrrtscec rsgesesg
//
LOCUS       WP_457696069             208 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457696069
VERSION     WP_457696069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22415
     Region          5..128
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mprpdaapdp ywnhnvhyhr lvldavpdgc graldigcgd gllvrklagr irevtgvdrs
       61 aamvrlarer saqvpnaafa eadfmtpgga psggfdflta vavvhhldft aavhrmagll
      121 vpggrlvlvg larnrtpldw iisgagvpaa rflarrhggk sgppempvld pamawgevrr
      181 aargclpgsr frrhllwrys lvwdkprs
//
LOCUS       WP_457696075             341 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696075
VERSION     WP_457696075.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36200
     Region          38..317
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mkrpyavala lalaasssll agcsdagkpv dfnaggkgdg aarvrpvddd tlmptgpksd
       61 fritrtlddg thiaratlrg qksgvtgsvw vwapkeygdp kyaksgfpvl ialpgglgsp
      121 kepggvtnyw vggdielqen lsqwtaegks lpflvvmpml npdtryhdas dipgsqkmgt
      181 wltedvvqlt ranfrtfksr dgwafmgsss ggfaglksvl khpdkfkaai asgpdlvpds
      241 plwaghqaek dannpeklaq rllqkggpdv ylafqagske psavtapiqr fqrtygkgpi
      301 htalqiipgg rhnawdyqkg maagsikfis drmkapvpsg s
//
LOCUS       WP_457696081             429 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase 5 family protein [Streptomyces nigrescens].
ACCESSION   WP_457696081
VERSION     WP_457696081.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Sharma,K., Dhillon,A. and Goyal,A.
  TITLE     Insights into Structure and Reaction Mechanism of &#946;-Mannanases
  JOURNAL   Curr Protein Pept Sci 19 (1), 34-47 (2018)
   PUBMED   27739373
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Ketudat Cairns,J.R. and Esen,A.
  TITLE     beta-Glucosidases
  JOURNAL   Cell Mol Life Sci 67 (20), 3389-3405 (2010)
   PUBMED   20490603
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="glycoside hydrolase 5 family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47132
     Region          1..334
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mrfgvnytpt hgwfhhwldf dldsvradld siaglgldhi rvfplwplfq pnrtlirpra
       61 veqlvqlada aaergldvnv dglqghlssf dflpawtrtw hrrnlftdpe vlsgqeeylr
      121 tlaaaladrp aflgmtlgne inqfsdrphp dpdrisreqa gawlermlaa ceqgapgrmh
      181 lhaaydaawy qdghpftpaq aarlgavtav hswvfngtaq rhgptgtate hhaayliels
      241 kawatdphrp vwlqevgapa phipetraar fteatvtaal dcpdlwgitw wcshdvprsl
      301 adfpdleygl gllgsdrtvk pagralaalv aewhgrthrp pvrstaltvd tggaeaaprr
      361 svcapggpvf eawaeltaqg vrpalvlsel aadeahlrsr citevctpdd vgriprrpsp
      421 avphrrsts
//
LOCUS       WP_457696083             294 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696083
VERSION     WP_457696083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 294)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32068
     Region          41..294
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 msatvqrgpd rragwaragr riprwqlllr yllllavlal tigpflwqls tslkgpgedi
       61 yryppsllph rftldnyagv aetipvwdfa lnslkvavtn vltncagaal agyalarmrf
      121 tgrksalvvf imamlvpves imiaqfvtmr elqlnntllg vvlpgcigam nvllmrnafa
      181 alpyeveeaa fvdganawqr fvrialpsvr gtlavvaifa fmgawddflw plivlsdqsk
      241 ftltiglnfl hgtfadnqrl vaagtviavl plivlfaclq rsffrgvgeg aikg
//
LOCUS       WP_457696085             430 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696085
VERSION     WP_457696085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46268
     Region          14..430
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mripcraaat tatlvtsvla ltacgssggs ggsdsasgkv egrvtfqtwn lkanfkkyfe
       61 gviadfenny pdteirwvdq paegypekls adaaggtlpd vvnvspdiay plakaglald
      121 lektagkyrg eyldgawesh rmpgmtgvya fpwylntgpm fynkelftka gldperppts
      181 ydqlfkdavt marksgrkia mlagspsied fgrygvrlmn apgteftfne pkgvellehy
      241 kklyaagald sqaltaqaes agrkfqqqsv amnpgsaldl enfkkeapgl yrhigitdav
      301 nntgkanmyv qglmvnaqsk vkpaavafah fvtdkknqma fakqvtifps tkgslddpyf
      361 tkedgtdatr vrvasakslk tavnytpvll sdqmktvlrn avakalqgkq tpeaaldgav
      421 aecnrllkta
//
LOCUS       WP_457696086             371 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696086
VERSION     WP_457696086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 371)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39446
     Region          13..369
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtapgeaarr kparrptikd iarragvses avsfalndrp gvsqdtrarv rrvaeelgwq
       61 ansaaralsg eragamglvl arpaqtlgve sfflqlvsgi qevlsarqia llfqvvedld
      121 tecalyrrww aerrvdgvlv vdprtadprp ellaalglpa vvvggpatpg pdpsepatae
      181 ssaapahpll stvwaddaka marildhlyg lghrrivhia glpglahtar riqslrnead
      241 rrgldrrqvh svttdysdae gaeatrrlld aarpptaivy dndvmavaga svaagrgipv
      301 pgalsivawd dsalcrvthp rltalvrdtp gfgrlaaqel lavldggplr tvqgelphle
      361 arestgtpph r
//
LOCUS       WP_457696101             114 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457696101
VERSION     WP_457696101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 114)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..114
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13020
     Region          5..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtlpfdvlae psrrkildll lerprlvgel teqlglsqpg tskhlrvlre aglvqvrqda
       61 qrrwyelrpe plaeldawla hyrhlwtgsl dappanagrc pqerhldame ddpr
//
LOCUS       WP_457696104             412 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457696104
VERSION     WP_457696104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 412)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=42510
     Region          11..412
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mtarqepfsa avtglglvta agvgakatwh svtqetlpgg vshqeeladl pcdfmytiad
       61 ldttellgva tqrlmdrfsq laviaareal adagldpesw dssrvavvig sahgglpfyd
      121 qqhvamarrg arrvspklap ltvvnsaass vcmdigaqgp smgvatacss gtvalgtahq
      181 llragvcdia laggaesvls rlliasacqm kavstrrddp atacrpfdvg rdgfvvgega
      241 gllvlerpeh asarrapvra hirgygassd ayaavapdpe gngieralri aladaqvqgr
      301 dvghvnahgt stivndrvea tvlrrvlgdh plvtstkamt ghalgaaggi etaltvlale
      361 qqlvpptanl evpdpripid ivrkearqaa fdcavktslg fgghnaalvl tr
//
LOCUS       WP_457696106              77 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Streptomyces nigrescens].
ACCESSION   WP_457696106
VERSION     WP_457696106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 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 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=8251
     Region          5..76
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mnaaevvntl lvqrfgvspa diteetplrs lrldslalee lrvlieerld idldevsltp
       61 rntvgqlvaa vdgnvpa
//
LOCUS       WP_457696116             317 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696116
VERSION     WP_457696116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33661
     Region          37..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtprarvata dtpavtpppa parrpargtr tqlpsspwlf lapgllivaa fslypflstv
       61 ahsftdartl tagqfvggan yrelihdamf wtglrnslly vlgvvpllvm lplllamlvq
      121 rhlpgitffr aafytpvvas vvvvgliwvw llddrglina lleglgfgkv gflsdpwlll
      181 lsamavtvwk glgyymiiyl aalanvprel heacavdgag avrrfltvtv pavrstmvlv
      241 aalssvgafk vfsevylmag ptggpggadt tlvmlvqqvg tglsgrvgya salsvvvfvl
      301 tlglmllvlr anrkeda
//
LOCUS       WP_457696118             313 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457696118
VERSION     WP_457696118.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  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 10172349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=33448
     Region          61..184
                     /region_name="SRPBCC_CalC_Aha1-like_6"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of an uncharacterized subgroup of CalC- and Aha1-like
                     proteins; cd08899"
                     /db_xref="CDD:176908"
     Site            order(61..63,65..66,71,79,87,89,91,93,100,102..103,105,
                     108,114,116..117,125,127,137,139,141,143,147..155,
                     157..159,162)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176908"
     Region          192..310
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
     Site            order(204,206,208,217..219,221..222,228,236,237,245,247,
                     249,256,258,265..266,268,270,280,282,284,286,292..296,298,
                     301..303,306)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176908"
ORIGIN      
        1 mcgpgawtlp qltlggaprn gtstpwrttp depalrhphh rrrphrttyg aqarpsarkg
       61 lwsaitdpah lgqwfpseat velrpggamt fampgvsgia mtgtvtdaee prlfaftwge
      121 dhprweitpd gdgsllvlvh tfgdrfggag fasgwhlclt alsqlldgds tpvdrdagel
      181 heayleqfdl grgavedtae gprvhferql vrpagavwaa ltsgdepatg apapegftsr
      241 qapagpvtev tapavpayrw hpegtvrwel gqgtghgprl vliqtgpqgf dadaaldawh
      301 erieqlaarl lan
//
LOCUS       WP_457696121             217 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces nigrescens].
ACCESSION   WP_457696121
VERSION     WP_457696121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..217
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=23702
     Region          21..204
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtgtpltlpe ellllalepe rgrflnnaty lryglagaal adleeagrit vgggdrltvt
       61 nplplgdpvl dgalaalpgp dkrgrgikae rwvrragrpv qelcvrrleq rgalrretrr
      121 alglfpyerf pagavdlvgp ardrfaaald agfpdrrgrl maalasatdl drrlllsrgy
      181 rpvrremkrf arefwmahav qravrqdeea ganagsa
//
LOCUS       WP_457696125             337 aa            linear   BCT 27-JAN-2026
DEFINITION  polyprenyl synthetase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696125
VERSION     WP_457696125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wallrapp,F.H., Pan,J.J., Ramamoorthy,G., Almonacid,D.E.,
            Hillerich,B.S., Seidel,R., Patskovsky,Y., Babbitt,P.C., Almo,S.C.,
            Jacobson,M.P. and Poulter,C.D.
  TITLE     Prediction of function for the polyprenyl transferase subgroup in
            the isoprenoid synthase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), E1196-E1202 (2013)
   PUBMED   23493556
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Chen,A., Kroon,P.A. and Poulter,C.D.
  TITLE     Isoprenyl diphosphate synthases: protein sequence comparisons, a
            phylogenetic tree, and predictions of secondary structure
  JOURNAL   Protein Sci 3 (4), 600-607 (1994)
   PUBMED   8003978
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="polyprenyl synthetase 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=35489
     Region          14..335
                     /region_name="IspA"
                     /note="Geranylgeranyl pyrophosphate synthase [Coenzyme
                     transport and metabolism]; COG0142"
                     /db_xref="CDD:439912"
ORIGIN      
        1 mtvvgpfgls vrdqaleadv qaglaaveeg lleatksdvp fiteaaqhlv raggkrfrpl
       61 lvtlaaqfgd pyspgvvpsa vvvelthlat lyhddvmdea dvrrgvasan arwgnsvavl
      121 tgdflfaras hiladlgpea vriqaeafer lvtgqileta gprdgrdpid hyldvlagkt
      181 gslvavacrf gammsgaees tvniltqyge rlgtafqlad dvldiasdsh esgktpgtdl
      241 regiptlpvl rlraraesaa gtpedralce llagdltdda rhaealaglr ahpaleearr
      301 dtvryaeear amlaplpscm aksaleglcd avvhrag
//
LOCUS       WP_457696130             288 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696130
VERSION     WP_457696130.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30017
     Region          19..225
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 msqaeavrrt prplwslgll rseiamtfrr wrtlallavl agvpvlvgia vkietgdggp
       61 gggaggpafl sqvthnglfl vfaslavtlp fflpmsvgvi agdslageah ggtlryllva
      121 pagrtrlllv kyataltfcl agalvvalsa latgallfpl gevtllsgts vsfgeglwra
      181 laiavavals ltglaavglf vstltssgia amattvglli tvqildtipq lhaiqpylfp
      241 hywlsfadll rdpvywdqlq knfglqalya vvfgsaawar fttrdita
//
LOCUS       WP_457696134             292 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696134
VERSION     WP_457696134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10142960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="SDR family oxidoreductase"
                     /EC_number="1.6.5.2"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=30325
     Region          5..274
                     /region_name="TMR_SDR_a"
                     /note="triphenylmethane reductase (TMR)-like proteins,
                     NMRa-like, atypical (a) SDRs; cd05269"
                     /db_xref="CDD:187578"
     Site            order(7,9..12,34..35,38,52..55,73..76,139..141,172)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187578"
ORIGIN      
        1 msfvvtgatg algrlvieel lrrtapgeiv alardrakaa dlaargveik hadysrpetl
       61 qgtfaagdrv lfisgneagq rltqhrtvid aareagvgll aytsvlggpt atfsiaeehl
      121 ateqallasg vpycllrngw yhenytgala ttlktgavvg sagegrvata arrdyaeaaa
      181 vvltgsgqen tvyelsgdta wtmaeyaaev srqtgrripy rdlrpeqyva llveagvpal
      241 gaqlvadada giargelsat pgelsrligr pttpiaeaia ealkglkglp tg
//
LOCUS       WP_457696136             364 aa            linear   BCT 27-JAN-2026
DEFINITION  2-oxoacid:ferredoxin oxidoreductase subunit beta [Streptomyces
            nigrescens].
ACCESSION   WP_457696136
VERSION     WP_457696136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Chen,P.Y., Li,B., Drennan,C.L. and Elliott,S.J.
  TITLE     A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes
            C-C bonds from CO2
  JOURNAL   Joule 3 (2), 595-611 (2019)
   PUBMED   31080943
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Yan,Z., Fushinobu,S. and Wakagi,T.
  TITLE     Four Cys residues in heterodimeric 2-oxoacid:ferredoxin
            oxidoreductase are required for CoA-dependent oxidative
            decarboxylation but not for a non-oxidative decarboxylation
  JOURNAL   Biochim Biophys Acta 1844 (4), 736-743 (2014)
   PUBMED   24491525
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Fukuda,E. and Wakagi,T.
  TITLE     Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from
            Sulfolobus sp. strain 7
  JOURNAL   Biochim Biophys Acta 1597 (1), 74-80 (2002)
   PUBMED   12009405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="2-oxoacid:ferredoxin oxidoreductase subunit
                     beta"
                     /EC_number="1.2.7.-"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38922
     Region          20..362
                     /region_name="PRK11867"
                     /note="2-oxoglutarate ferredoxin oxidoreductase subunit
                     beta; Reviewed"
                     /db_xref="CDD:237006"
ORIGIN      
        1 mtetiserss qiealslvpk adakqsmkdf ksdqevrwcp gcgdyavlaa vqgfmpelgl
       61 akenivfvsg igcssrfpyy mntygmhsih grapaiatgl assrrdlsvw vvtgdgdals
      121 iggnhlihal rrnvnlkill fnnriygltk gqysptsevg kitkstpmgs ldapfnpvsl
      181 algaeasfva rtvdsdrkhl tsvlreaaah pgtalveiyq ncnifndgaf evlkdkekae
      241 eavirlehgq pirfgalapd gfgskgvvrd patgdlkvid vreegtggvl vhdahnpspt
      301 tafalsrlad pdtlhhtpig vlrsvdrpvy dtlmsdqlda aieqkgkgdl aalltgndtw
      361 tvvg
//
LOCUS       WP_457696140             437 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457696140
VERSION     WP_457696140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 437)
  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 437)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46428
     Region          32..221
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          229..437
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdtayaphpr gsrvpvglsa pfsgrtwref lylclsfpms vlmfvyaitv islgagllvt
       61 flgipvlagg lagsralggl erararallg ldvadpepar askpglmgwv gavlksgvsw
      121 rhlvysvlhm pwavfsfvfs vtfwsvgwgl layplwrwtf layldqpglq mwgdgrghgi
      181 yldtpadigf tsgfglllvl agpwvihglt qvdrvmvhgl lgpsslatrv sqlesdrgvv
      241 vdtaaadlrr ierdlhdgaq arlvalsmdl glakeklaed peaaarmvde ahgevkialq
      301 elrdlargih pailtdrglg palsalsarc tvpvtvtvdl dhrpaaaieg iayfttsell
      361 qnvsrharas satldvwrta drlmvlvadn grggahtgsg tglaglaerl davdgllivd
      421 sptggptcit aelpwrg
//
LOCUS       WP_457696142             443 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457696142
VERSION     WP_457696142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 443)
  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 443)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12155181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="sensor histidine kinase"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46934
     Region          36..174
                     /region_name="Sensor"
                     /note="Putative sensor; pfam13796"
                     /db_xref="CDD:433485"
     Region          181..412
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtessrpsaa edaldgaspp pprpplsgtt wreiayllan fplglvafav lmvwvllglg
       61 lsvivitlpl latglmacrq ygrlerarar allgvrveep srlrarypgf lpwlwtglkd
      121 pvawrhalft firlpwaalt ftvvfvllfl gwpalpwvar wlsnvdramv rgllspsdel
      181 erriaelesd rvtvtdtaaa dlrrierdlh dgaqarlval amglglakek llegqadasv
      241 aamvdeahge vklalqelrd largihpail tdrglgpalt slagrctvpv ttavdlaerp
      301 apaiegiayf tvsellqnvs khsaarqasv evwrvkgggp agpsdkgggg rragdrlliq
      361 vtddgkggar ldggsgmtgl aerlrsvdgl fvldsptggp trvtaelpwr trtgaesrtg
      421 aesrtgaesr tgtgtgagig aag
//
LOCUS       WP_457696152             322 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 1/NuoH family protein [Streptomyces nigrescens].
ACCESSION   WP_457696152
VERSION     WP_457696152.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   3  (residues 1 to 322)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="complex I subunit 1/NuoH family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=34506
     Region          3..320
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 msdtldivlr llavfavflv fplvigqteh kvmahmqgrl gpmyaggfhg waqlvadgvk
       61 faqkedivpa gadrrifqla pavallpyll vlvaipigph navgqtldag iffvlavmgv
      121 gvlgslmagw asankfsllg glrtaaqlla yelpmlltaa svamaagtls lpgiieafhw
      181 wwvpwqivgg vvfftaglae lqrppfdmpv adseiifgay teytglrfal fllaeyagiv
      241 vlcaltsvlf lggwhgpfga dglgwlwtll ktvilafgvi wlrvtyprlr edqlqklawt
      301 vliplalaqi altgvvkvvi ss
//
LOCUS       WP_457696148             220 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit B [Streptomyces nigrescens].
ACCESSION   WP_457696148
VERSION     WP_457696148.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Grigorieff,N.
  TITLE     Structure of the respiratory NADH:ubiquinone oxidoreductase
            (complex I)
  JOURNAL   Curr Opin Struct Biol 9 (4), 476-483 (1999)
   PUBMED   10449365
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Friedrich,T. and Weiss,H.
  TITLE     Modular evolution of the respiratory NADH:ubiquinone oxidoreductase
            and the origin of its modules
  JOURNAL   J Theor Biol 187 (4), 529-540 (1997)
   PUBMED   9299297
REFERENCE   4  (residues 1 to 220)
  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 10001254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="NADH-quinone oxidoreductase subunit B"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /calculated_mol_wt=23365
     Region          42..186
                     /region_name="NuoB"
                     /note="NADH:ubiquinone oxidoreductase 20 kD subunit (chain
                     B) or related Fe-S oxidoreductase [Energy production and
                     conversion]; COG0377"
                     /db_xref="CDD:440146"
ORIGIN      
        1 mdvtpastss aaaaegaape flpeprrlgt larlapepmk vvlnwgrrys lwvfnfglac
       61 caiefiaasm arhdfirlgv ipfapgprqa dlmvvsgtvt dkmapavkrl yeqmpepkyv
      121 isfgacsncg gpywdsysvt kgvdqiipvd vyvpgcpprp eallqgilkl qekiareslg
      181 eryakggtar psaaalrsgl vtppaptpad apkpageear
//
LOCUS       WP_457696154             194 aa            linear   BCT 27-JAN-2026
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696154
VERSION     WP_457696154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Yu,H., Schut,G.J., Haja,D.K., Adams,M.W.W. and Li,H.
  TITLE     Evolution of complex I-like respiratory complexes
  JOURNAL   J Biol Chem 296, 100740 (2021)
   PUBMED   33957129
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="NuoI/complex I 23 kDa subunit family protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21315
     Region          1..157
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 msfpgsglak glavtlrtmt krsvtaqypd vqpdlpprtr gviglfeenc tvcmlcarec
       61 pdwciyidsh ketvppaapg grersrnvld rfaidfalcm ycgicievcp fdalfwspef
      121 eyaetdirdl therdklrew mwtvpeppal dpaaeepkel aaarkaadkl aaqqaaaeae
      181 asapdrpdtp gegk
//
LOCUS       WP_457696156             204 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit J family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696156
VERSION     WP_457696156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kravchuk,V., Petrova,O., Kampjut,D., Wojciechowska-Bason,A.,
            Breese,Z. and Sazanov,L.
  TITLE     A universal coupling mechanism of respiratory complex I
  JOURNAL   Nature 609 (7928), 808-814 (2022)
   PUBMED   36104567
  REMARK    Erratum:[Nature. 2022 Nov;611(7936):E9. doi:
            10.1038/s41586-022-05457-8. PMID: 36316422]
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
REFERENCE   4  (residues 1 to 204)
  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   5  (residues 1 to 204)
  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 10002877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="NADH-quinone oxidoreductase subunit J family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=20956
     Region          19..178
                     /region_name="NuoJ"
                     /note="NADH:ubiquinone oxidoreductase subunit 6 (chain J)
                     [Energy production and conversion]; COG0839"
                     /db_xref="CDD:440601"
ORIGIN      
        1 mtlaataagh gflsptgvev afllvgiatl gaavitvttr qlvhaalwlv valggiaiey
       61 llltaefiaw vqvliyvgsv vvlllfglml tkapigrspd adsgnrwaal avalasagcl
      121 vwvvvdafra twisfegaaq gsteasgrsl fqywvlpfea lsvlllaalv gaivlsrrtg
      181 egkaaaadlk tgasrapapr eeqg
//
LOCUS       WP_457696158             680 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit 5 family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696158
VERSION     WP_457696158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Desmarais,J.J., Flamholz,A.I., Blikstad,C., Dugan,E.J.,
            Laughlin,T.G., Oltrogge,L.M., Chen,A.W., Wetmore,K., Diamond,S.,
            Wang,J.Y. and Savage,D.F.
  TITLE     DABs are inorganic carbon pumps found throughout prokaryotic phyla
  JOURNAL   Nat Microbiol 4 (12), 2204-2215 (2019)
   PUBMED   31406332
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Efremov,R.G. and Sazanov,L.A.
  TITLE     Structure of the membrane domain of respiratory complex I
  JOURNAL   Nature 476 (7361), 414-420 (2011)
   PUBMED   21822288
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Nakamaru-Ogiso,E., Kao,M.C., Chen,H., Sinha,S.C., Yagi,T. and
            Ohnishi,T.
  TITLE     The membrane subunit NuoL(ND5) is involved in the indirect proton
            pumping mechanism of Escherichia coli complex I
  JOURNAL   J Biol Chem 285 (50), 39070-39078 (2010)
   PUBMED   20826797
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Brandt,U.
  TITLE     Energy converting NADH:quinone oxidoreductase (complex I)
  JOURNAL   Annu Rev Biochem 75, 69-92 (2006)
   PUBMED   16756485
REFERENCE   5  (residues 1 to 680)
  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 11436849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..680
                     /product="NADH-quinone oxidoreductase subunit 5 family
                     protein"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=69390
     Region          4..663
                     /region_name="NuoL"
                     /note="Membrane H+-translocase/NADH:ubiquinone
                     oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+
                     antiporter, MnhA subunit [Energy production and
                     conversion]; COG1009"
                     /db_xref="CDD:440633"
ORIGIN      
        1 mtltttavlv pllpflgava glllgrppvs rrrpeerraa lhapgfvrpl avlptlaaaa
       61 lavtvaigqg tgpatdvatq ltptgsipid lalhidgfaa liavlvgiva scvqlystsy
      121 lrddpryasy aalvslftsa mllvvytgdl mvllvgwevm gicsyflvgh yweteaaraa
      181 slkaflvtkl gdvpflfgif alaadagtfr itgilgsvtg ggldhptlia llllagvagk
      241 saqfplhtwl pdamagptpv salihaatmv aagiyvvarl lpvfaasaaa lvvmavmaai
      301 tmvgsglaal aqddikrvla ystvgqlgym lgalavgdrg aavfhlishg afkallflga
      361 gviihaagtn slaamsrmsg larripdayw tvtvallala aippfagffs keavlgaaeh
      421 taigaahgip gaagwtvlvs glltalltaa yatrlwllaf rgkgveapdh gpqpvvmnav
      481 lwvlfvptva lglaapllpd wfdgrslapt lttsvlgtgi aligglvtya awrhttalaa
      541 rtpigavvtd pdaspglaee taiathapvy gsvagapdpa dpgrlllgpl qphaavgfhl
      601 davysalfvr pvraaatlvr fldrevvdty vrgagtaprw lgaavrraqt gnvqtylgal
      661 lagslvlava avlvatgtga
//
LOCUS       WP_457696160             544 aa            linear   BCT 27-JAN-2026
DEFINITION  complex I subunit 4 family protein [Streptomyces nigrescens].
ACCESSION   WP_457696160
VERSION     WP_457696160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  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 544)
  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 544)
  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 544)
  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..544
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..544
                     /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=56095
     Region          9..542
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mnhtalqlll aavvvlplvg alaalfpapp glrgknpdqa vlrhgvtvtg vvlaaavgla
       61 agfdhdhaar mqattdiswi paldirihlg idgislplvv ltalltflca lysyfhmptg
      121 pspkafvall ltleagtlat favldlmlff lafemvlipm yfliarwgga gkqaaawkfi
      181 lytllgsvvm llgllliglk sgtfdmvala tdngpnaqls htvqvlavla igiglavksp
      241 lwplhswlpd ahtaaptvgs vllagvllkm gtygfvrial pitpegmqtf apylaalaav
      301 giiygslacl alvrkgakgd lkrliayssv ghmgfvllgi asmtptgvng alfaniahgl
      361 itgllfflvg alkdrygstd ldafagstga alygraprfg gllafgavas lgipglagfw
      421 gemlamfgaf qpaaglsrpa fltfmvmagf gtlltaayll lvvrrvcmgg tphlaptapl
      481 gtadpagedp sgqpaqvpav pdiaryeyaa wtplavltvl aglwpaallg ltdpavqqll
      541 gggk
//
LOCUS       WP_457696162             524 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit N [Streptomyces nigrescens].
ACCESSION   WP_457696162
VERSION     WP_457696162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..524
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=53948
     Region          10..523
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mssitplvqs vdwlavappt ltaavalvvl vadlflpaar kpllgwiata glalaalfll
       61 pllgggrrtf clpahpdvcs yvadpftlvi qflvlggall tallsidtik dqdlpageyw
      121 flllssaaga allpasrdla tlvialevas lpafalvglr rgdrlsseaa lkfflssvaa
      181 tavmllgvsf lyaatgslyl srvadaltgl pdprlatlas agvaltlvgf afktaaapfh
      241 fwvpdtyvga plpiagylsv vgkavgfsgl ilvtvqgfps yadvwgpala vlaaltmtvg
      301 nvaalrqdpr rahsavrlla wssvgqagyl lvpiaaagya qdpahaigst vayalmyaav
      361 nlgafavaal vartrpanri sdyrglyhqr pivalalgff llclaglppg iiglfakvtv
      421 fsvavdagla wlavimavnv vialyyylqw ttvlfreaea aeapeaaeap eaaeapetap
      481 aeqpparari paplataial atvlgialsg apqlvlrfas gall
//
LOCUS       WP_457696169             147 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457696169
VERSION     WP_457696169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15917
     Region          3..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 menevgheia dalglllrrt trtqlhkqlt egmgeavdel typvlsalar tgprsaadla
       61 pdvgvdrsgv trrasrleaa glirreadpa drrahllvlt eqgrhavael rarlaahima
      121 slsswppgea eafarhlrrf tvegpft
//
LOCUS       WP_457696181             411 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457696181
VERSION     WP_457696181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43748
     Region          14..411
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(112..114,138,188,219,248,250..251,259)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(115,148,212,257..259,288,291)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            251
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 msaatppass ptdrrvsarv gaisesatla vdakakalka agrpvigfga gepdfptpdy
       61 iveaaieacr npkyhrytpa gglpelktai vaktlrdsgy eieaanvlvt nggkqaiyea
      121 faaildpgde vivpapywtt ypesirlagg vpvdvvadet tgyrvtveql eaartdrtkv
      181 llfvspsnpt gavysreqve avgrwaaehg lwvltdeiye hlvygdaafs slpvvvpelr
      241 dkciivngva ktyamtgwrv gwaigpkdvi kaaanlqsha tsnvsnvaqa aaiaavagdl
      301 taveemkvaf drrrrtivrm lneidgvlcp epegafyayp svkellgkei rgkrpqtsve
      361 laelileeae vavvpgeafg tpgylrlsya lgdedlvegv sriqkllaea t
//
LOCUS       WP_457696217             541 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457696217
VERSION     WP_457696217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..541
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60035
     Region          16..526
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mghleaghle yylpdgrvll gdvsfrvgeg asvalvgang agkttllrli agelqphgga
       61 vtvsgglgvm pqfvgsvrde rtvrdllvsv aqprireaaa avdaaelaim taedddeaaq
      121 mayaqalsdw aeargyeaet awdictsaal gmpyekaqwr qvrtlsggeq krlvleallr
      181 gpdevlllde pdnyldvpgk rwleeqlret rktvlfvshd rellaraaek ivsvepgpag
      241 sdvwvhgggf gtyhearrer farfeelrrr wdekhaqlkq lvnmlknkaa fndglasryq
      301 aaqtrlrkfe eagppqeppr eqdirmrlrg grtgvralta knleltglmk pfslevfyge
      361 rvavlgsngs gkshflrlla gddvrhtgew klgarvvpgh faqthahpel egrtlvdilw
      421 kehakdrgga msvlrryele kqaeqrfdrl sggqqarlqi lllelsgtta llldeptdnl
      481 dlesaealqe gleayegtvv avthdrwfar sfdrflvfgs dglvretaep vwderrvers
      541 r
//
LOCUS       WP_457696233             272 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696233
VERSION     WP_457696233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27912
     Region          78..272
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mstsvretgv pehagtaget gaaarllslg raeltllgrn ktalttalli pvalafamkg
       61 avsgmdlsgt glsvgtvllp aalgyvlifa vysnltgayv arreelvlkr lrtgelrdle
      121 iltgtalpsv lmglvqcall vvlgglvlda glptaphlli agvvlgtaav vgfaaassvl
      181 aksaeaaqla vlpfmmvsla gsgmvvpldi lpervasvle llplspamel iragwtgggd
      241 lketlgqvit glawtglalf avqrwfrwep rr
//
LOCUS       WP_457696229             299 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696229
VERSION     WP_457696229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32281
     Region          1..>169
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          93..285
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,221..226,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlrrlssfl avveeghfgr aatrlflspa avtghiqqle refgtpller spvaptpagr
       61 rlvshartll aaanaamddv advaqgaapr rplrvgvmgh gsaevtpaav safrrarpev
      121 plslvqltft ehcsalredr vdvafvrpgf qsegitvdvl tteqrivvvs aassladaar
      181 egvrradiid lpylrlppht prpftdylyf degerrspdc altphdclts vvagrgagsa
      241 lksfaryypw pgtvyipvld apwahsvlat rekdpdpevr ifraltvala relgpaaar
//
LOCUS       WP_457696235             354 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696235
VERSION     WP_457696235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37570
     Region          26..270
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnigeknigg tgrggarsag sgdgvievtg lrrsygavgr rtsgqrergg rngpsgpsgp
       61 sgprsfeavr gidfsverge lfallgtnga gktstlelle glalptagqv rvlghdpfre
      121 rrkvrprvgv mlqeggfpse ltpaetvrmw agctsgarpv dealgsvgle rrrnvrvkql
      181 sggerrrldl alallgrpev lfldepttgl dtearhatwe lvrelrdsgt tivltthyle
      241 eaeeladrla ilhngriaaa ghvadvvaah pshisfelpt gfhlgdlppl gelgvighet
      301 dgrtvrlrtd elqraatgvl lwaqdkgial gnldvrsasl eeaflhiakg lena
//
LOCUS       WP_457696238             170 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457696238
VERSION     WP_457696238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 170)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..170
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18539
     Region          83..167
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdleqrvsel errlavleqa adrpapsper epddalwalr glkdqlaelg adnggvlftg
       61 avrtpagqry ewqyglvtdt vlerdwadaa esfaalgqpv rlrllreilg grctaaelte
      121 ldgtgttgqi yhhlrqltaa gwlhttargr yevptervvp llvmltaagp
//
LOCUS       WP_457696240             289 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457696240
VERSION     WP_457696240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30718
     Region          47..244
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mpstsirklt alvarifllt ffgmvvtnff vdyfaywltw tplalwalie fginrrrpgt
       61 kaeratgsap epvviaapvt grwtalnspa dkvpshgtrt ygqayaidiv aepapgarpg
      121 fgwwplargn adfpafgapl lavadatvvh tddrqrdhls rtswlavgyf ffvegavral
      181 ggarrvvgnh vildlgggty alyahvrrgs ltvrpgdrvr agqqlgqcgn sgnstephvh
      241 fqlmdaadpe aadglpftwq gigvpanget feaapatvah aegavsgpa
//
LOCUS       WP_457696250             372 aa            linear   BCT 27-JAN-2026
DEFINITION  Leu/Phe/Val dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457696250
VERSION     WP_457696250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Brunhuber,N.M. and Blanchard,J.S.
  TITLE     The biochemistry and enzymology of amino acid dehydrogenases
  JOURNAL   Crit Rev Biochem Mol Biol 29 (6), 415-467 (1994)
   PUBMED   7705101
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10500541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="Leu/Phe/Val dehydrogenase"
                     /EC_number="1.4.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38728
     Region          32..149
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          166..368
                     /region_name="NAD_bind_Leu_Phe_Val_DH"
                     /note="NAD(P) binding domain of leucine dehydrogenase,
                     phenylalanine dehydrogenase, and valine dehydrogenase;
                     cd01075"
                     /db_xref="CDD:133444"
     Site            order(200,202..204,223..224,228,260..261,282,284)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            314
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mgvttvtdvr pasagtdggf lhtlfrseqg gheqvvlcqd rasglkavia ihstalgpal
       61 ggtrfhayas eeeavldaln lsrgmsykna lagldhgggk aviigdpdli ktdelllayg
      121 rfvaslggry vtacdvgtyv admdvvartn kwttgrspdn ggagdssvlt aygvfqgmra
      181 saqhawgdpt lrgrkvgiag vgkvghllve hllqdgaevv itdvraesve rvrakfpqvt
      241 avadtealir tegldvyapc alggalsdes vpvltakvvc gaannqlahp gvekdlsdrg
      301 ilyapdyvvn aggviqvade lhgfdfdrck tkaakifdtt laifarakad gippaaaadr
      361 laeqrmaear ha
//
LOCUS       WP_457696259             557 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696259
VERSION     WP_457696259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 557)
  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 557)
  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..557
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..557
                     /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=58749
     Region          279..456
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 maraarsrtp npdtpqsplh rllhtglhgv ralpaavrra yrsrrtapaa glvepphpla
       61 rslgliavtv vgawlgllli gsirvpvgpm dtsmalrpsl tggtridvap lgdlelsshh
      121 apvrldvdvd rldpvrsqal vdhperfagl qaevthdvtr galglalhsc vavasgatal
      181 glavyrrprr alaagglalt llaasagtay atwnpqsvle pkfsglltsa psvvgnarni
      241 vsefhvyqke larlvtnvtr lydatstlpa yqpdpttirv lhvsdihlnp gawriiaslv
      301 kqyrinvivd tgdtmdhgsa aenhfldpvs tlgapyvwvr gnhdsrgtqk yltgrrhvtv
      361 ldhgkvtqva gvriagvgdp qftpdrsvva agdpaertag grladalrtq rlagtpvdia
      421 lahnptavte adglaplala ghvhhrentl lpqgtrlmve gstgggglra vqnkkpepvl
      481 asvlyldrtt krlqawdeit lgglglsrae vsrhlprenq pgatpapsgs ppsadpssrp
      541 ssgsssrpar spsehpr
//
LOCUS       WP_457696267             390 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457696267
VERSION     WP_457696267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="cupin domain-containing protein"
                     /EC_number="1.14.11.47"
                     /GO_process="GO:0043687 - post-translational protein
                     modification [Evidence IEA]"
                     /calculated_mol_wt=42637
     Region          15..274
                     /region_name="RoxA"
                     /note="Ribosomal protein L16 Arg81 hydroxylase, contains
                     JmjC domain [Translation, ribosomal structure and
                     biogenesis]; COG2850"
                     /db_xref="CDD:442098"
ORIGIN      
        1 mtaissavrs lggdfpaeaf grtyrlwprv gdfsdlftwd dlnqiiarhr lepprlrlfn
       61 dgsqipqhsy ahpvvskrht vwhriepanl hhqlkdgasl vldavdalhp gvedlatale
      121 rhfrtdvqvn lyaswtpkeg fgvhwddhdv vvvqlegakr wkiygatrid plrvdteape
      181 pptgapvaev vlqagdmlyl prgwwhavaa tegrslhltc glkpttgadl lswladqlrv
      241 sntvranlpy fappdersay lqalrkefad alhegvieef inargstdpg rpmpslpfvd
      301 gipadrslsv rltaagawyg vdeighvvfs aggqewtfsr pvlaviklll ngttatlgel
      361 svssglpvgh vaalvselve agvaavsrrr
//
LOCUS       WP_457696273             437 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696273
VERSION     WP_457696273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46364
     Region          1..82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 magseltlgk tiakarrrkg wpqrdlaami drseswvsqv erdvipvnsl dalrqisdvl
       61 dislsallva appgptpvst rrraasarvd rnlgpeegdd pvrrrellaa aavvfttpla
      121 gaspaeastl apledhllyg tatvprrgev spagvaaevk asreefraar ydtlarnlpg
      181 riaqaqglep aelsatavad lyniatrlci klgedglvai tadraltsar iggdaltiae
      241 ahrmvssawr rqghlaratd iavraaqdvr gdrstpetar lsvsvsllat aaytaakmgd
      301 rptahglige aaeaaeigrt spetrtdtgt qqvllhqlsv hyllgdagqa idlartinpa
      361 alptaerqgr fftdvarcfd qwgkpeqcyr allaaeraap qeirrgsvks lasgllrhdr
      421 tfpgvrafag ragvavn
//
LOCUS       WP_457696275             338 aa            linear   BCT 27-JAN-2026
DEFINITION  ice-binding family protein, partial [Streptomyces nigrescens].
ACCESSION   WP_457696275
VERSION     WP_457696275.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vance,T.D.R., Bayer-Giraldi,M., Davies,P.L. and Mangiagalli,M.
  TITLE     Ice-binding proteins and the 'domain of unknown function' 3494
            family
  JOURNAL   FEBS J 286 (5), 855-873 (2019)
   PUBMED   30680879
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10572153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..>338
                     /product="ice-binding family protein"
                     /GO_function="GO:0050825 - ice binding [Evidence IEA]"
     Region          17..202
                     /region_name="Ice_binding"
                     /note="Ice-binding-like; pfam11999"
                     /db_xref="CDD:432251"
ORIGIN      
        1 matlvplgaa atygvlanta itntgltvva gdlgvspaga vsgfppgtvt gtihvndaaa
       61 aqaqadllig ygnallqpvt atvptelggt tlfpgvynsa sgtfslngpl tldaqgdpna
      121 vfifktnttl itgaagtvnl aglaqsshvf wqvgssatlg ggstlrgsil antsitavtg
      181 aivdgrllal gaavtldtnt vtvpalatcq vvvqpvvgpv vvgqptpvsa vvtcnglpvs
      241 gasvtfngga vpvtvttnva gvatgsltfn tagtatvtat vtaagtacsc tgvvsapitv
      301 tvtpqtscqv vvqpvvgpvv vgqptpvsav vtcnglpv
//
LOCUS       WP_457696279             137 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696279
VERSION     WP_457696279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14301
     Region          21..137
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mngmkitsap hpvptvvrge sldsihrare atraftdslt papgpervdt fllvvselat
       61 nalrhgggry tlqlfagpdt ltaavsdlss aaprertpdl ngggggfgwh mvrhltshla
      121 iapapgtgkt iyaqlpr
//
LOCUS       WP_457696289             372 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457696289
VERSION     WP_457696289.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37961
     Region          <222..366
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 masnrpapes psayelddrg afpgpgaddg dgpweewnpt eestrsvrgk hrvakqrggg
       61 farsgtvlgv gviaavgagg masaedrppv pismpdiggm addlsenlpd akslpgigel
      121 isdedsaaas aaaadaapaa sgpltratqt sadtgggtga gealrsrilq qadaqqgaae
      181 qearetaqqa avqqaateaa ahqesaekaa aakkaaemea krkaeeaarq kaeaerlakl
      241 aksfvapvss ytltasfgqa gdrwaadhtg qdfaaptgtp vkalhsgtit qagwagsygy
      301 rivltlddgt evwfchlssm vktsgkvntg dvigrvgatg nvtgphlhle vrpdagdpvd
      361 pmpwlrdhgi nv
//
LOCUS       WP_457696301             607 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457696301
VERSION     WP_457696301.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 607)
  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 607)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..607
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66181
     Region          22..572
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mgsaangttl hlgfdashtk avlrtteeyr adlvqlaarf rtggqlgpla vlvdiedlla
       61 nlnsisswpd hqgvewapql kelvvssled setvkkqlaa sagreqlash dvssligevw
      121 tapltgfqkr diakllslrh ganfsvpgag ktrvglavys amkargdvrr llvvspksay
      181 eswlyesgyc fsqglrpmll esardewael lianyerldr slaflaswle eapsmiilde
      241 ahrmklgvrg tygaacmalg plarrrlilt gtpapngakd lenllgfvwp gygqrtvaqa
      301 vaggdlahas svlrplftrt tkhelglppv sahiqrvrmt elheeiyral vgdlsaraea
      361 saddftalgr salrllmaat npallvegss rdepveyrlp plelpqggsl yellkdlpsy
      421 elspkygeaa kivaanaarg rktlvwstfv rsltsiakll enfqpavvhg gtpdreeqlr
      481 rfredpdcmv lvsnpatlge gislhqvchd avyvdrdfma grylqsldri hrlglaadte
      541 trvtvlaaea tidevvevrl rekldfmarv lddpsvqqla dlqeapavlg gldaadiral
      601 lrhidkt
//
LOCUS       WP_457696303             429 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA cytosine methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457696303
VERSION     WP_457696303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..429
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=47301
     Region          9..374
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mgassrdesq pltsieicag aggqalglhg agfrhlalve idknahatlk enigthvdwg
       61 dcealnedlv hefnarrema alggrplaeg eldllaggvp cppfsvagkq lgrdderdlf
      121 prmialidel kpraimienv rgimdakfde ycdsiikdie gmgywfcgwh llearnygvp
      181 qlrprsifva irdaerqkag ldrddfpwpv svlghkknvf ealedsmrdr rdrlvkefpd
      241 hsanieqayl dwcqradkpn vvaptlvggs kkhggadlgp srakaawrel gvnavgvadd
      301 lddvkridve khlgreflrp dgpmltvqqa aliqkfpehw kfqggktaqy rqvgnafppp
      361 vaeavgrais svlqpelrdk hlkglqterl garrgrrvyr qseiaevldv svaaaeapld
      421 drngdlvra
//
LOCUS       WP_457696306             438 aa            linear   BCT 27-JAN-2026
DEFINITION  PrsW family intramembrane metalloprotease [Streptomyces
            nigrescens].
ACCESSION   WP_457696306
VERSION     WP_457696306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Ho,T.D. and Ellermeier,C.D.
  TITLE     PrsW is required for colonization, resistance to antimicrobial
            peptides, and expression of extracytoplasmic function sigma factors
            in Clostridium difficile
  JOURNAL   Infect Immun 79 (8), 3229-3238 (2011)
   PUBMED   21628514
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006386
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="PrsW family intramembrane metalloprotease"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47412
     Region          47..314
                     /region_name="PrsW"
                     /note="Membrane proteinase PrsW, cleaves anti-sigma factor
                     RsiW, M82 family [Signal transduction mechanisms];
                     COG2339"
                     /db_xref="CDD:441909"
ORIGIN      
        1 mypsqppphp phapappsyt phtyepsaaa arrrtapwrs ktlravalvs llalsgviiv
       61 gmvrqetgte gflvglglav fpvpllvaaf cwldrvepep wrnlafaftw gacaatlval
      121 langfatdwl aaniastsps eaeawgatvi apvveevvkg aavlllyrfr rrdfdgitdg
      181 iviagitatg faftenvlyl gnafgedqsl ghsgldslta gtfflriivs pfahplftil
      241 tglavgitat ryprrraari alallgllta vllhaiwnga sslgdlgfli vyglfmvpvl
      301 ialtwlavwa rtqellslrg ylapyitagw lapteptals slktralard larhtqgpaa
      361 aravteyatv atslsfhrrr ahlngtdpnf twreqhllqh lryyqrwgrd altealatve
      421 eprqqpqgtg pcsrrrgr
//
LOCUS       WP_457696305             152 aa            linear   BCT 27-JAN-2026
DEFINITION  very short patch repair endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457696305
VERSION     WP_457696305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Tsutakawa,S.E. and Morikawa,K.
  TITLE     The structural basis of damaged DNA recognition and endonucleolytic
            cleavage for very short patch repair endonuclease
  JOURNAL   Nucleic Acids Res 29 (18), 3775-3783 (2001)
   PUBMED   11557809
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Tsutakawa,S.E., Jingami,H. and Morikawa,K.
  TITLE     Recognition of a TG mismatch: the crystal structure of very short
            patch repair endonuclease in complex with a DNA duplex
  JOURNAL   Cell 99 (6), 615-623 (1999)
   PUBMED   10612397
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Tsutakawa,S.E., Muto,T., Kawate,T., Jingami,H., Kunishima,N.,
            Ariyoshi,M., Kohda,D., Nakagawa,M. and Morikawa,K.
  TITLE     Crystallographic and functional studies of very short patch repair
            endonuclease
  JOURNAL   Mol Cell 3 (5), 621-628 (1999)
   PUBMED   10360178
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790390
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="very short patch repair endonuclease"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0006298 - mismatch repair [Evidence IEA]"
                     /calculated_mol_wt=17301
     Region          14..145
                     /region_name="Vsr"
                     /note="G:T-mismatch repair DNA endonuclease Vsr, very
                     short patch repair protein [Replication, recombination and
                     repair]; COG3727"
                     /db_xref="CDD:442941"
ORIGIN      
        1 mpddndwtap egswassaar rrnmqairsr dtkpeqrirr lvhaqglryr vsarplpglr
       61 rtadmvfrpa kvavfidgcy whgcpehyva pktnsgywse kvtrnvtrdr dtdeqlasag
      121 wlvlrfwehe paklcadkia vtviqrrlsg gn
//
LOCUS       WP_457696317             296 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696317
VERSION     WP_457696317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30619
     Region          55..>143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhiqgsqwpa tvavahaadg agsssennrp hsngtavtng agtgtggrst plrvdaqrnl
       61 ehvlraarev fgelgygapm edvarrarvg vgtvyrrfps kdvlvrriae eetsrltdqa
      121 rtalgqeddp wsalsrflrt svasgagrll ppgilrvsad adrsagptae gaeghrvpdg
      181 lsearvpqqr tapgtdgaaa dlrpaarrdt qegepagaap aaaeeangad alldvvgrlv
      241 erakaagelr advtvsdill viatgaptlp dpgqqqaasa rlleillegl rsrpar
//
LOCUS       WP_457696318             605 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding SpoIIE family protein phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457696318
VERSION     WP_457696318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  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 605)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
REFERENCE   6  (residues 1 to 605)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18599219
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="ATP-binding SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=63166
     Region          66..468
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          484..602
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 miftrwsakl pgtqrraaar sdraaprpap gtpavppaaa papsaepata dgapsaptaa
       61 ttgsvpaara ehtdpapsqd rapatlpptv dalsvheilg tipalvavvy gpehrlayvn
      121 gayasvfgpr pagrtareal peldalgllp lmdqvlrsgk prtvksrkvp ggaggdrtrd
      181 gyytftctpi evaasgpapd pevacvaphk gvlvfgaevt dqiesaerlr asearqreaa
      241 vtlqrsllpq eleqpddlcv aatyqpggtd aavggdwydv itlgagrtal vigdvmgrgv
      301 raaavmgqlr tavrayarld lpphevlqll dglaaeidas qiatcvyavh dpnegrlvya
      361 saghlpilvr dpdgtvrraa eptgpplgtg gwlhtsgsvp lgpgssavly tdglverrdk
      421 didhgveale rafagaagap divcdrllrs lgitathddd vailvlqhpa rtghdaelfh
      481 naalelhggt eaaprarafa sgvlaswrfs pelhdlgvla aselvanslq hgtppmrlrl
      541 rrtdrrlive vtdgddhlpr rrraepadea grgisivati asswgsrrtp gggkavwcef
      601 alprg
//
LOCUS       WP_457696320             186 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457696320
VERSION     WP_457696320.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..186
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20746
     Region          31..170
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpepsdaaae aaepsleeqi aayqrefqdl dpqveqvvsa lqrlnrrmnv aygrqtatlg
       61 lsnaewevlk alvvsgapyq lgpgelakrl gltpaamthr idrmaneglv trerdetnrv
      121 rviveltreg rekwleamrl asvfeedllq dlsgeerqll gqvltrllrr vedaqpdadg
      181 rlsdld
//
LOCUS       WP_457696327             459 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696327
VERSION     WP_457696327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=49499
     Region          7..421
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msskdvtril vvgggyvgmy talrlqrklk qelrqgtvev ivvdpepymt yqpflpeaaa
       61 gsisprhvvv plrrvlpqck vvigevtaid hdarratltt laaeetgnga ievaydelvl
      121 apgsvsrtlp vpgladvgig fktveeaigl rnhvlgqldi asstrdpair daaltfvfvg
      181 ggyagveala eledmaryav ryyhnikped mkwilveatn rilpevgpdm ggyavrelra
      241 rnidvrletr lescekhvaq lsdgssfptr tlvwtagvkp hpilaatklp lnahgrlkct
      301 palqvdgveh awsagdaaav pdltaeppae pdapralcap naqhavrqsk vlaeniaaav
      361 rggpivdyah kyagsvaslg lhkgvahvyg rklkgypawf mhrayhlsrv ptfnrkarvl
      421 aewtlaglfk reivslgsle npraefelaa gtgrhneas
//
LOCUS       WP_457696325             380 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457696325
VERSION     WP_457696325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39832
     Region          1..376
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mlrgeappeg dgergerrsr rslfgrllvr rlpailivgg vvfdmgtpas ytaapffsaa
       61 plvaaplssl rgtaltalaa llgeiwvvty rsagqnyses vteiatvlvv allalginrv
      121 lrtadarlas vrdvseaaqr avlpmpparl ggltlaaryv garadarigg dlyavqdtph
      181 gvrlivgdvr gkgleaveta vivigafrea aeqestlgav agrleralqr eggrrkgveq
      241 aegfttavla eipadgksvl rvlnrghpsp llltpdgglr elapaapalp lglgemasrp
      301 drpdetffpa gallffftdg vteardllgr fynpssklrg crfpgpdvll dtvvedvarh
      361 tggapaddma llavqrpmga
//
LOCUS       WP_457696333            1272 aa            linear   BCT 27-JAN-2026
DEFINITION  chromosome segregation SMC family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696333
VERSION     WP_457696333.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1272)
  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 1272)
  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 1272)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1272
                     /product="chromosome segregation SMC family protein"
                     /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=135916
     Region          1..1271
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mhlksltlrg fksfasattl rfepgitcvv gpngsgksnv vdalswvmge qgakslrggk
       61 medvifagtt grpplgraev sltidnsdga lpieyaevtl trimfrnggs eyqingdtcr
      121 lldiqellsd sgigremhvi vgqgqldsvl hadpmgrraf ieeaagvlkh rkrkekalrk
      181 leamkanlar vqdltdelrr qlkplgrqaa varraaviqa dlrdarlrll addlvtlrra
      241 lraeiadeaa lkerkqaaed rlrtaqqrea aleeevrtlt prvqraqqtw yelsqlaerv
      301 rgtislaear vksataappe erhgrdpedm ereaarireq eaeltaalea asraledtve
      361 hraglerqla deerrlrdva raiadrregl arlsgqvtaa rgraasaqae igrlaearda
      421 arrradtaqe eyeqlkaevd gldaddeeia erheaarrel aetetaltaa realtaaerk
      481 raataarhda lalglrrkdg tgallaaadr ltgllgpaae lltvtpgfev pvaaalgaaa
      541 davavtgpat aaeairllrk qdagraamvl ggsggrsrtg avpaparaae ategggaaea
      601 vgafgvvdaa gvpagsgaag aarsqgadav rgtgggegfa gaaegavvdv cegaagapgv
      661 pghrvpgprs epvpaaelvr gpgdltaava rllrdvvvvg tledaeelva arpelmavtg
      721 agdllgahfa qggsagapsl levqasvdea aaeleelaar ceelaeaqra aaerrtagaa
      781 lveelaerrr aadrekskva gdlgrlggqa raaageaerc daaaakaeea llrateeaee
      841 laerlavaee epgvgdeepd tsvrdrlaad ganarqteme arlqarthee rvkalagrad
      901 sldrgaraer eararaerrr arlrheaava gavaagarql lahvevsavr aeeergaaer
      961 akaereqalv aernqgrelk seldkltdsm hrgevlgaek rlrieqletk aleelgvepa
     1021 glmaeygpeq lvppsppaeg evlpddpehp rnqpvryvra eqekrlkaae rayqqlgkvn
     1081 plaleefaal eerhqflseq ledlkktrad lmqvvkevde rveqvfteay hdtarefegv
     1141 farlfpggeg rlvltdpndm lstgvdvear ppgkkvkrls llsggerslt avallvsifk
     1201 arpspfyvmd eveaalddtn lqrlirimee lqessqlivi thqkrtmeva dalygvsmqg
     1261 dgvskvisqr lh
//
LOCUS       WP_457696335             472 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar porter family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457696335
VERSION     WP_457696335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50120
     Region          25..462
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(37,155,158,162,284..285,289..290,293..294,387,
                     391..392,396,419..420,423)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mtstaqptgs egrkahpehl ghvifitaaa amggflfgyd ssvingavea irsrydvgsa
       61 vlaqviaval igcaigaata griadrigri rvmqiasvlf tisavgsalp fslwdlafwr
      121 iiggfaigma svigpayiae vspsayrgrl gsfqqaaivi giavsqlvnw gilnladgnq
      181 rgtlagleaw qwmlgvmvvp avlygllsfa ipesprylis vgkvsrakev laeveghtvn
      241 ldtrvteiqd amrrehkssf kdllgskmgf lpivwvgigl svfqqlvgin vafyyssalw
      301 qsvgidpsas ffysfttsii niigtviamv fvdkigrrpl aligsagmal slaleawafs
      361 aktaagtlpp tegtvaliaa hvfvlffals wgvvvwvflg emfpnriraa algvaacaqw
      421 ianwaitasf pslsdwnlsg tyviytifal lsipfvlkfv ketkgkalee mg
//
LOCUS       WP_457696337             309 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696337
VERSION     WP_457696337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33133
     Region          14..301
                     /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 mtgvgtrrpg lpahydfrvc tphpgpvrtt sgydmlvtag laalaaadtv vipgwtpada
       61 pltpavrral rrahargarl vsicsgafal aqtglldgrr atthwslaaa lterfprvev
      121 dpdvlyidhg dlatsagaaa gvdlclhlvr sdhgaahaar iarhmvmpph reggqaqyat
      181 pppadrlapa lamdqslapl lewvdgrlye pvsvedmagr lrissrtlar rfaeqlgtsp
      241 gqwllgrrit aartlleetd lpveaialrv glssatnfrr rfrdalhttp aayrrafrir
      301 rtgqgagrp
//
LOCUS       WP_457696341             327 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457696341
VERSION     WP_457696341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..327
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35760
     Region          33..327
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mmsvlrinlv dpaptpatls aryraavema afaddrgftm vqteehhatt ngwmpspltf
       61 agavfgatrr igvtvsalit plhdplrlae dlasldligg grlvtvaglg yrpeeyaahg
      121 kdwpgrgrlq devletllsa wtgepftyqg rtvqvtprpy tqphplllig gssraaarra
      181 arlglpffps arlpgleayy heqraafgte gwvmqppert allhlsedpd rawaeygghl
      241 lhearmyasw qsagirsavr ssaqdvgalr eegvyrivtp ddclrlarrt gdrgalilhp
      301 lcggmpvdeg wrslhlfaeq vlprlkd
//
LOCUS       WP_457696343             494 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457696343
VERSION     WP_457696343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..494
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51664
     Region          4..469
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mgttsstsap apegavetrg iepvpdnerq grvrelfptw vatnisvlll tmgaslvvan
       61 glnfwqvllv saiaaavafg mvgvlsvsgk wggapgamls raafgvrgny fpgailwvar
      121 fgwetinavt gayavltvlh lllgvesntv lvvvtllafv avtylvsglg rkalnvcnky
      181 stylfalfsi mvlvylvatm dwdavfakka gttamviagi gtiaaggisw vptgpdfary
      241 lphsasgkki vgvtvsgaal alvpmvlmgg vmavsdpkla grntdpmsfv gsilpgwlav
      301 pylitalvgm vlinslsmys agftaqtmgv klpralavsv navislvggl fmmlvakdfi
      361 gqfiafltll avsfsawigv ygidmarrhk lavrydadsl mntgrtsryw yvggfcwqam
      421 tawgvalvag lcftkvqwft gplattwige nglgwaatia isalvfavlp tpvesapaar
      481 adeaaearqp vevg
//
LOCUS       WP_457696345             407 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696345
VERSION     WP_457696345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=42207
     Region          1..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mfdvlvlggg faglwsaaaa trllraegsa hsvalltphp dlvirprlyq adparmrvpl
       61 drvlgpvgvr riaatatavd tgrrrvtalm sdgsrtevay rslvlatgsa vvrpelpgsa
      121 llhdidtlpa avrleehlqg lpeapagpgr wtavvvgagf tgleiatelv grlraqaapy
      181 gaadevrvvl veraavvgag lgaaarpvit raldtlgier rlgttvtgld arsvhlsdgs
      241 tvpartavwt agmrasaltt qipaprdelg rlavdrglrv rgveglyaag dtaaalaedd
      301 hpvlqscqha iplgkvaghn aaagllglpp vdfapdpyrt cldlgpagav atagwnrtlr
      361 egpegfakel krainetwis ppaddpqell rraghrvgtr pdsassa
//
LOCUS       WP_457696352             446 aa            linear   BCT 27-JAN-2026
DEFINITION  ammonium transporter [Streptomyces nigrescens].
ACCESSION   WP_457696352
VERSION     WP_457696352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, 57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..446
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46046
     Region          10..420
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mppgiltlaa dkatlspant gfmlicsalv mvmtpglaff yggmvrvksv lnmlmmsfis
       61 lgivtilwvl ygfglafgtd kggfigwdgh faglsgiglt elwgattipv yvfavfqlmf
      121 aiitpalisg aladrvkfta walfialwvt ivyfpvahwv wgeggwlfel qvidfaggta
      181 vhinagaaal gvllvvgkri gfkkdpmrph slplvmlgag llwfgwfgfn agswlgnddg
      241 igavafvntq vataaamlgw layekirhgs fttlgaasga vaglvaitpa cgavsplgai
      301 avgviagvlc amavnlkykf gyddsldvig vhlvggvags llvglfatgg vqseakglfy
      361 gggfdqlgrq avgvvcvlly slvvsyvlak aidlvmgfri gedeevagid qaahaetayd
      421 ftgagggtvg rkgpalgeal tkkvda
//
LOCUS       WP_457696353             112 aa            linear   BCT 27-JAN-2026
DEFINITION  P-II family nitrogen regulator [Streptomyces nigrescens].
ACCESSION   WP_457696353
VERSION     WP_457696353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Huergo,L.F., Chandra,G. and Merrick,M.
  TITLE     P(II) signal transduction proteins: nitrogen regulation and beyond
  JOURNAL   FEMS Microbiol Rev 37 (2), 251-283 (2013)
   PUBMED   22861350
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..112
                     /product="P-II family nitrogen regulator"
                     /GO_function="GO:0030234 - enzyme regulator activity
                     [Evidence IEA]"
                     /GO_process="GO:0006808 - regulation of nitrogen
                     utilization [Evidence IEA]"
                     /calculated_mol_wt=12090
     Region          1..112
                     /region_name="GlnK"
                     /note="Nitrogen regulatory protein PII [Signal
                     transduction mechanisms, Amino acid transport and
                     metabolism]; COG0347"
                     /db_xref="CDD:440116"
ORIGIN      
        1 mklitavikp hrldevkdal qafgvhglti teasgygrqr ghtevyrgae ytvdlvpkir
       61 ievlvedada deltdvivka artgkigdgk vwsipvddav rvrtgergpd al
//
LOCUS       WP_457696371             426 aa            linear   BCT 27-JAN-2026
DEFINITION  murein hydrolase activator EnvC family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696371
VERSION     WP_457696371.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Weiss,D.S.
  TITLE     Bacterial cell division and the septal ring
  JOURNAL   Mol Microbiol 54 (3), 588-597 (2004)
   PUBMED   15491352
REFERENCE   2  (residues 1 to 426)
  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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..426
                     /product="murein hydrolase activator EnvC family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44082
     Region          <198..328
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mrrntrrncg ptrafhaftg lrgrlprpvd rrqprprprp rsqpgrgpgp lppprlrsps
       61 rphsrfrspa pltpaprrkp ngygpscffp ahaagallap taaavltlft palanaaaas
      121 svsaatghgv argveggaer glgavagrpl grgidrvvsr aagraagrev dvergemagr
      181 aeggapaara appaedrswp vggaagvqpt vvrgwepppa pwaaghrgvd laasagavvr
      241 aaapgrvaya gtvagrgvlt levsrsgrpp lrtsyepvrs tvrkgqrvta gqpvavlqhg
      301 gpfhcrepcl hwglrrgkty ldplsllpps mlgggpsrll pifgvpvpag ghtaprppep
      361 peptaqasss aptaaaltea vglaavtiwa lgrlpaarsa vsdegtprrr wrgwgwrrrv
      421 lgrgge
//
LOCUS       WP_457696377             388 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatidate cytidylyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457696377
VERSION     WP_457696377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10471701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..388
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016772 - transferase activity,
                     transferring phosphorus-containing groups [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40785
     Region          125..375
                     /region_name="CTP_transf_1"
                     /note="Cytidylyltransferase family; pfam01148"
                     /db_xref="CDD:426080"
ORIGIN      
        1 mnesswgapp gagqwgppdh gpasslrgva ppapagpvyd wgdaaqtrpm pfvpgqggyq
       61 ddnrehrdir dnrdhlddrg aarrsgplfr dekpqepmpt slsgsdnspd sekpkkksag
      121 rnlpaaigvg vglgviivas lfvykpvfig viaiavvvgl weltsrlaer kdikvplvpl
      181 avggtamvva gyvrgaegaw vamaltalav lvwrmteape nylrdvtagv faafyvpfla
      241 tfvalmlaae adgplrvltf llltvvsdtg ayavgwrfgk hklaprispg ktreglvgav
      301 lfamaagalc meflithgaw wqglllglav aasatlgdlg esmikrdlgi kdmgtllpgh
      361 ggimdrldsl lptapvvwll fvvfvgag
//
LOCUS       WP_457696387             358 aa            linear   BCT 27-JAN-2026
DEFINITION  thiamine ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696387
VERSION     WP_457696387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   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 358)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Domain dislocation: a change of core structure in periplasmic
            binding proteins in their evolutionary history
  JOURNAL   J Mol Biol 286 (1), 279-290 (1999)
   PUBMED   9931266
REFERENCE   6  (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   7  (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 10008329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="thiamine 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=38279
     Region          1..358
                     /region_name="TbpA"
                     /note="ABC-type thiamine transport system, periplasmic
                     component TbpA [Coenzyme transport and metabolism];
                     COG4143"
                     /db_xref="CDD:443315"
ORIGIN      
        1 msttsritat avvaavgmta lagcggsggg sadaktvtlv shdsfhvsks vlaafekesg
       61 ykvkmlkggd agkavnqail skgnpqgdvf fgidntllsr gldedlfspy qakglqsvpa
      121 glqldkgehr vtpldygdic vnydrgyfdr hkiappktfd dlikprykgl lvtensatss
      181 pglafqlgti akygekgwpd ywkklkangv evvdgwdqay ydrfsgsaag kgkgdkplvv
      241 syassppaev lgkkpapkea ptgvatgtcf rqiefggllk gaknekggka lldfllskef
      301 qedvplqmfv nparkdaevp elftkygtti dkpttlapet itknreqwik qwsslvlk
//
LOCUS       WP_457696388             581 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696388
VERSION     WP_457696388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 581)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..581
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61870
     Region          22..572
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mvlarsevtp sdvtgvrrgr pargtavrlg lmavplaffa lffaypvvai vgrglkdggq
       61 wqlsrfgavl sdpdvvhvlw ftvwqaaast gltllialpg ayvfarfdfp gkqllravva
      121 vpfvlptvvv gsaflalvgr ggllddlwgv rldtsvwail lahvffnyav vvrtvgglwg
      181 qldprqeeaa rvlgagrfea wrrvtlpalg pavaaaalmv flftftsfgv vqilggptfs
      241 tleveiyrqt adfldlptaa vltmiqfaav lgvlalhawt vrrresalrl vdasqtarrp
      301 rgrgqwallw gtlaviavll lvplvvlver sfagpdgyga vfyaslgsaa sadstfavap
      361 ldalwnslay gaaatvialv vgglaaaalt lprlrrgpsg rtpvvsrfvr gfdvllmlpl
      421 gvsavtvgfg flitldeppl dlraswwlvp laqalvgvpf vvrtmlpvlr avdgrlreaa
      481 avlgaspwrv wrevdlpmvr ralliaagfa favslgefga tvfiarpdqp tlpvavarll
      541 gragelnygq amalstilmv vcaaallvle rlrpidrsge f
//
LOCUS       WP_457696390             357 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696390
VERSION     WP_457696390.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37644
     Region          9..352
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtaragstaq ellrlggvtv rfdargrpal davdlevaah eivcvlgpsg sgkstllrvv
       61 aglqqadagq vllegrdqsg vpthrrgvgl mfqdhqlfpq rdvagnvafg lrmrrssrgd
      121 qertvaelld lvglpgaqrr avaslsggeq qrvalarala prprllmlde plgqldrglr
      181 erlvvelrrl fhelgttvla vthdqgeafa ladrvvvmqd griaqtgtpl evwqrpatef
      241 varflgfdnv veatvqgeaa atpwgkvpvp aatpdgpcrl lvrpagvrlt aapeglpctv
      301 aartfrgthv alllqpsggp qveaacalrd apevgervgi afqaqdvvvl dasaaag
//
LOCUS       WP_457696393             386 aa            linear   BCT 27-JAN-2026
DEFINITION  LOG family protein [Streptomyces nigrescens].
ACCESSION   WP_457696393
VERSION     WP_457696393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41294
     Region          166..379
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mtdvqsnsqp paprrthddn ddreieslee fdrvvasgsl aghrvqsvdl tdrtfallsa
       61 dttesvflgc vmepdaaaki raggalvfpp vpglpfdpyr gglygpdelf egladagfda
      121 tpdartyrwy qetksdgdif asmlrsihdd avsdaldehl agaqvvgimg ghalergsaa
      181 yagaarlgrr ltrdgltvat gggpgameaa nlgaysapfe demldsalel laktphftps
      241 vtdwaqaafe irrsrpgggt svgiptwfyg heppnafath iakyfvnavr edgllarsha
      301 gvvflpgaag tvqeifdnat pnyyqsrgep tpmvlvnreh wteklptwpl lqalaadrpm
      361 aarialvdsv deapdalarl rtqafs
//
LOCUS       WP_457696399             246 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696399
VERSION     WP_457696399.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26043
     Region          7..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mvappdndvl warglhhtyg gtsalagvsv gvregeilav tgprgsgktt llkclsgqlv
       61 paegevwfns apvhtlssps rerlrldrfg widtephlva eltawenaal plllrgtgtr
      121 sakhtaiewl drldvgmcas rrpaqldqsq rqriaiaral attpqvlfad eptaplhhad
      181 gtqvlrtltt aarshqitvv lathdpdvat ladrslvlld ghqasgapdg tgssdeesra
      241 acslsv
//
LOCUS       WP_457696403             164 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696403
VERSION     WP_457696403.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..164
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18005
     Region          17..152
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mngvaasrns hdrtgtptid svslaiieql qedgrrpyaa igkavglsea avrqrvqkll
       61 dqgvmqivav tdpltvgfrr qamvginveg dldpvadalt tmeeveyvvm tagsfdliie
      121 ivcedddhll eminkrirtl pgvrstesfv ylklrkqtyt wgtr
//
LOCUS       WP_457696407             393 aa            linear   BCT 27-JAN-2026
DEFINITION  polyamine ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696407
VERSION     WP_457696407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Igarashi,K. and Kashiwagi,K.
  TITLE     Polyamine transport in bacteria and yeast
  JOURNAL   Biochem J 344 Pt 3 (Pt 3), 633-642 (1999)
   PUBMED   10585849
REFERENCE   5  (residues 1 to 393)
  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 10194417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="polyamine ABC transporter substrate-binding
                     protein"
                     /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=44154
     Region          52..387
                     /region_name="PBP2_PotD_PotF_like"
                     /note="The periplasmic-binding component of ABC
                     transporters involved in uptake of polyamines; possess the
                     type 2 periplasmic binding fold; cd13590"
                     /db_xref="CDD:270308"
     Site            order(57,267,270,293,295,331)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270308"
ORIGIN      
        1 madlarrall rgmgglgvtg alaamtgcgv ppayveaadr ggpdrsardr klvfanwply
       61 idvddrhkqr rptldaferr tgisvtytee indndeffgk ispalmnhqs tgrdlivisd
      121 wmcarfvrlg wvqemdraaq phvarhldpl lrrphfdrgr khsvpwqsgi tgiaynrkkl
      181 greiqhtadl wkddlrgrvt llsgldesfa mllqgngvdi trwtaddfhr mtdqirrlvs
      241 kghirrftgn dyikdldsgd vlaaqaysgd viqlqadnpd iefvvpqega elwaesllip
      301 nlaehkrsae rlidyyyrpe vaadlaawvn yvcpvpaare vlasskdker aalaedplif
      361 pddamrkrla iarditseer tafakewnai vgl
//
LOCUS       WP_457696410             207 aa            linear   BCT 27-JAN-2026
DEFINITION  NADAR family protein [Streptomyces nigrescens].
ACCESSION   WP_457696410
VERSION     WP_457696410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11179911
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="NADAR family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /calculated_mol_wt=22872
     Region          41..200
                     /region_name="NADAR"
                     /note="NADAR domain; pfam08719"
                     /db_xref="CDD:462576"
ORIGIN      
        1 mmhegtgitt gdtagraadg prsveelqra aargkhvkyv yfwghsprrd gslgascfsq
       61 wwpapftvdg vryataehwm magkarlfhd aeaerraiaa vhpkqakdag rrvrgfdeet
      121 wqrhrfdlvv egsvqkfgqd aalreyllgt nsrvlveasp ldriwgigla adderaadpa
      181 rwrglnllgf almaarqrlr eeagats
//
LOCUS       WP_457696415             390 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696415
VERSION     WP_457696415.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41859
     Region          13..371
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mthtatpqss ggdvrlqgis kiygpftavh pldltvpags ffallgasgc gktttlrmia
       61 gleepttgtv elsgqdvtvl ppykrqvntv fqnyalfphl diyenvafgl rrrgiksvkk
      121 qveemldlvq lgpmarrkpq qlsggqqqrv avaralinhp qvllldeplg aldlklrrqm
      181 qlelkriqte vgitfvhvth dqeeamtmad tvavmnggrv eqlgapadly enpattfvan
      241 flgtsnliea evveagdrqh gelllkaada tlrlpaarcs asarkgekvl agvrpekvsl
      301 thaddagsit dgrnrlpgri kdasfigvst qyvvvvpglg elavyeqnve rdgrlvpgad
      361 ivlhwspaht fgldaaqdiq agadldeeaa
//
LOCUS       WP_457696414             415 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696414
VERSION     WP_457696414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=45490
     Region          29..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mehheqpepl spaelaavrr sltdgrlamt rrsllrasga maaavgglga lsacgippag
       61 rtdagrsedh ssaekrisfs nwteymdvsd dgkhrptler ftkrtgiavk ytedindnde
      121 ffgkiqaqla agqdtgrdli vltdwmcarm islgwiesld panlphayan lspqfrspaw
      181 dpgrahsypw qgipaiiayn kkatggrkvd sisqlledpe lkgrvgflse mrdsvgltll
      241 dmgkrpedct addfdaaiar iqkgvdskqi rrftgndytt dldkgdlaac vawagdvvql
      301 qndnpdigfa ipkagymtss dnlmvpnkar hkqnaerlid yfyepkvaak iaayinyvcp
      361 vegvreelak idkkaadnpl iipdkemaer shsfralsak enkaftqkfs dltga
//
LOCUS       WP_457696417             312 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696417
VERSION     WP_457696417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34031
     Region          23..312
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtttetpapp dggaqaaple vrktparkrl vpywlllpgi lwlivffaap lvyqastsiq
       61 tgsleegfkv twhfatylda lgeywpqfvr svgyaatata lclllgypla yliafkagrw
      121 rnlvmilvia pfftsflirt lawktiladg gpvvgllnsl hvldvtswlg ltegqrvlat
      181 plavvcglty nflpfmvlpl ytsleridpr lheaagdlya rpattfrrvt fplsmpgvva
      241 gtlltfipaa gdyinaellg stdqkmignv iqsqflrvld yptaaalsfi lmaailamvt
      301 iyirksgted lv
//
LOCUS       WP_457696418             281 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696418
VERSION     WP_457696418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30409
     Region          20..280
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mavhgtteat avrtpnrglr wlrrniitia glctlgylil pnivvmvfsf nkpngrfnyq
       61 wqrfstdaws dpcgvadlcg slglslqial watvgatvlg tmiafalary rfrarsgvnt
      121 liflpmampe vvmaaslatl flnmgiqfgf wtiliahimf clsfvvtavk arvmsmdprl
      181 eqaaqdlyas plqtflrvtl piaapgiaag allsfalsfd dfiitnfnag stvtfpmfvw
      241 gsaqrgtpvq invigtamfl vavlcvvvgq lagarkrskr s
//
LOCUS       WP_457696420             472 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696420
VERSION     WP_457696420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51711
     Region          40..415
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 maraamtpsa ahaladaept pfwladpgrp aarpalvgde tcdllvvggg ysglwttlia
       61 kerdperevv lvegaeigwa asgrnggfca aslthglgng larwpgelat leelgirnld
      121 aieeavaryg idcafertge idiatephqi aelrefaeda atigldrhtf ldedelraqv
      181 dsptfraglw drngvamlnp arlawglkqa cldlgvriye rtratdlasd gtgmavrtpy
      241 grvfarhval gtnafpslvk rvrpyivpvy dhalmtepls deqlaaigwk nrqglsdsnn
      301 hfhyfritad nrilwggydi vyrygggvra eydhhpatye klarhffrcf pqleglrfth
      361 swggaidtcs rfsaffgtah agrvayaagy tglgvgstrf gaevmldlls gertertele
      421 mvrskplpfp peplrwagig itqwsmtqad trggrrnlwl kamdkvglgf ds
//
LOCUS       WP_457696428             548 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696428
VERSION     WP_457696428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..548
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=56778
     Region          17..118
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          228..541
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mphtlaslvn htalkltvla geerlevpvr wahaselidp vpymeggell litalkldae
       61 dpeatrryvr rvaeagvvgl gfavgvnyeg vpqalveaar eqglpllgvp rrtpfiaisk
      121 avsaavaadq yravtagfea qreltraals aegpaellar laahldgwaa lydasgavva
      181 aapdwaarra arlsddvgrl rerpapassv vsdtdgddrv elqslgtgrr argvlavgtg
      241 aplgtaerya vhsavalltl ttersralqd aeqrlgaavl kmllagepdh aravagrlyg
      301 glldapfrvv vaepvageep ssgvaagaga vgvldglada mdsaaartge avlavpdagr
      361 livlvadgga aadacaayaa eaearagaqp rargragrte aahgegvavg lsaptgpiaa
      421 anayrqaeqa lsvarrrgra lvehedvaag svlplladda vrafadgllr alrehdatgr
      481 gdlvaslraw larhgqwdaa aadlgvhrht lryrmrrvee ilgrslddad vrmelwlalk
      541 atsapqge
//
LOCUS       WP_457696434             158 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696434
VERSION     WP_457696434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 158)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18089
     Region          5..138
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mrqvsrivll dpddrilllh gfepdrptdt wwftpgggle gtesreeaar relaeetgit
       61 dvvlgpvlwk rrcafpfdgr rweqdewyyl grtdrtatht ggqtdlerrs vsglrwwtse
      121 elsashetvy ptrlaellrt llddgppdap vlleterv
//
LOCUS       WP_457696436             179 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696436
VERSION     WP_457696436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18941
     Region          3..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqrgalldaa rtllseggte altfpalaer tglarssvye yfrsraavve elcavdfpvw
       61 aaeveaamqr vdtpedkvea yvrrqlalvg drrhravvai sageldagar ekiraahggl
      121 iamivealat lgheqprlaa mllqgvvdaa vrrielgaae dpgeiteaav amalrgvrg
//
LOCUS       WP_457696445             394 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696445
VERSION     WP_457696445.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42386
     Region          9..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maveahtgvg kriayqrria rltqqqlada aqihlgtlrk iergargagd avlesiaaal
       61 gvdpsvllpr ydraedrvnq ampvlsavla tydmpddgpv rsladlhtav seaetwrlga
      121 eyvrisrelp allaelsrgl hcspdgergt vagllvsacr tadavafkyg aldlsarlid
      181 vmrwaapqae dplvdasvay vrtetffaar thhaglrale ravdavpatg rtaalasrga
      241 lhmraaviag ragqadaaht hldlartlgd rvpesvyrgt afgpdsvrih evsvavslgd
      301 shaqraleva aawqppltlp aerrsgfyie lgraqlwagr pdhafaslkr arsiapqhar
      361 ehqwvrqdaa tlrrlkrtda eslthfadwc hatg
//
LOCUS       WP_457696447             212 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696447
VERSION     WP_457696447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22561
     Region          2..210
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mieavvfdvg etltsddryw aawadwldvp rhtlsalvga vvaqgrdnad avrllkpgid
       61 laaeyaaree agrgetldes dlypdvrpal aslraagfrv lvagnqtvra gellrslnlp
      121 vdalatsgdw gvakptpeff ervvrlaata pdrivyvgdh pandiapaaa aglrtahlrr
      181 gpwghlwads peaaaadwri eglddllplv sg
//
LOCUS       WP_457696454             432 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457696454
VERSION     WP_457696454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43555
     Region          26..391
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(36..37,40..41,44,76,126,128..130,133,153,156..157,
                     160,233,236..237,240..242,245,273,277,331..332,336,340,
                     355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 metehipepv agdapgtrpg lgrgtlllms vaaglsvagn yfaqplldii grdlhlpaat
       61 aalvvtvaqv gyglgllllv plgdllerrr lavtltaata vfltvtasap naallltgta
      121 ltglasvaaq vvvpyaatla apaergrtvg tvmtglllgi llartaagll aelggwrtvy
      181 wvnaalmllm avllrlrlpa lrttaglgyp allrstlalf gqepvlrwrg algaltfagf
      241 svlwtalafl msgpsygwqe saigllglvg aagslaasvg grladrglah rvtgaaafll
      301 lgswgllalg gaggawslaa llagvivldl saqavhvsnq nlvyavrpea rnrlnsaymt
      361 syfvggavgs altsvawaaa gwggvcvlga glaavvvalw aaermrrras dggrtgrgqa
      421 aaaeapapsl ts
//
LOCUS       WP_457696456             291 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696456
VERSION     WP_457696456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444074
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001217 - DNA-binding transcription
                     repressor activity [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30919
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_LTTR_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08436"
                     /db_xref="CDD:176127"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176127"
ORIGIN      
        1 melqqmryvv avaetggftr aaerchvvqs alshqiarle kelgarlfdr tsrsvrltaa
       61 geafvpvarq aleaadrara evaaatgevr grlavgaist vaavdlarel gafrtrcpqv
      121 rislqtamsd qlleqvrqgv ldvafvglvp aartvgvrek elargelvav vppvhplagr
      181 ewttlsrmar etfvdftags aarrqredaf raagltaeva fevttvefla klvraglgvg
      241 mvpeaiasel tglhivrvrp apertervvw sglgpspaav afltglgvdp a
//
LOCUS       WP_457696457             435 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457696457
VERSION     WP_457696457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 435)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47759
     Region          34..430
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(71,78,107..108,115,119,126,259..260,263,267..268,
                     271,309,314..315,318..319,321,344,371..373,376..377,
                     379..381,385)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(78,101,103,106,108..109,191..192,202,258..259,
                     262..263,267,315,318..320,420)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mhdkphttaa dapagcpaag papalftwef asdpypayaw lrehapvhrt elpsgveawl
       61 vtrytearqa ladgrlsknp vhhseaahgk gkvgipgers anlmthllni dppdhtrlrr
      121 lvskaftprr vaafaprvqe ltdhlidqfa akgeadlihe fafplpiyai cdllgvpred
      181 qddfrdwagm mirhgggprg gvarsvkkmr gylaelihrk reslgetaea dedlisalir
      241 asdhgehlte neaaamafil lfagfettvn ligngtyall rhpaqrellq ksiaagdtdl
      301 lttgieellr ydgpvelatw rfatqeltlg gqriaegdpv lvvlaaadrd parftepdvl
      361 dltrrdnqhl gyghgihycl gaplarlegq talatlltrl pdirlatepd dlrwrgglim
      421 rglrslpvef tperp
//
LOCUS       WP_457696462             150 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsB family cell division protein [Streptomyces nigrescens].
ACCESSION   WP_457696462
VERSION     WP_457696462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Villanelo,F., Ordenes,A., Brunet,J., Lagos,R. and Monasterio,O.
  TITLE     A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
            complex
  JOURNAL   BMC Struct Biol 11, 28 (2011)
   PUBMED   21672257
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Noirclerc-Savoye,M., Le Gouellec,A., Morlot,C., Dideberg,O.,
            Vernet,T. and Zapun,A.
  TITLE     In vitro reconstitution of a trimeric complex of DivIB, DivIC and
            FtsL, and their transient co-localization at the division site in
            Streptococcus pneumoniae
  JOURNAL   Mol Microbiol 55 (2), 413-424 (2005)
   PUBMED   15659160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=16640
     Region          36..118
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mpadrfstat rlkalgeqaa arvyrarppr rnrltgraal lalvmcslvv alaypirqyv
       61 sqrsdiadqr rkaqeagaal drlreqkarw qdpayvrqqa rrhlhyvmpg eagyivpdgs
      121 gtgsapkgaq aaqrpwyenl wdavdaadkr
//
LOCUS       WP_457696468             463 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696468
VERSION     WP_457696468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..463
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=50240
     Region          6..413
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mstterpril vvgggyvgly aarrilkqmr ygeatvtvvd prsymtyqpf lpeaaagsis
       61 prhvvvplrr vlpkaevltg rvttidqdrk vatiaplvge ayelpfdylv iamgavsrtf
      121 pipglaecgi gmkgveeaig lrnhvleqld kadsttdedv rrkaltfvfv gggfagaeti
      181 gevedmarda akyynnvkre dmrfllvdva dkilpevgpk lgaygkehle grgvevylkt
      241 gmdscvdghv klnnglevds ntivwtagvk pnpalarfgl plgprghvdt gttlqvqgtd
      301 yiwaagdnaq vpdlvgrkng nenawcppna qhalrqakil gdnvlsgmrg fpqkeyshan
      361 kgavaglglh kgvamivmgk mkiklkgrla wymhrayhgm amptfnrkir vfadwtlamf
      421 lkrevvslga menpreefye aakpapappt aaeagdktka kas
//
LOCUS       WP_457696472             852 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696472
VERSION     WP_457696472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 852)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 852)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..852
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88455
     Region          2..852
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mfrtalrnvl ahkarllmtv lavmlgvafv sgtlvftsti sdafrtssek sfdnvdvslt
       61 ppssdgppgt rakeprldgk aldtvsrlpg aasvtgtvng ftgigdkdgk ligsgesrgs
      121 nyfpgkdgkd arypmkqgta ptradqfald agtaakggyh vgdtvrisad gpvrqqkltg
      181 ifttddgrva aggslalfdt rtaqqllgls ggysqidvka aagtsqaalq qaigkalpkd
      241 satsftgkel adleakmidh dmqgmktall afaavalfvg ifliantftm lvaqrtkela
      301 lmravgasrr qvtrsvliea flvgaiagvs glvagigiaa vlrevlngfv akfpegplvv
      361 spstavaalg igtvitvlaa wlparrgakv ppvaamnsvh avattksllv rntlgalvag
      421 igtasviiat svydgddisk imlggggmll lvgvfiltpl lsrplialat pvlrafgvsg
      481 rlarqnalrn prrtattasa lmigltlitg mtviagstqk gidklavdal kadytvsmqg
      541 ntqlpttaeq kvrdvpgvta ltplregmat igtssaarqp tqltgvdgaq fgslvrldis
      601 egslgtlrgd rvlvdentat nkgwragtrl svtfedgkka tltvsgvykg nemlngvlld
      661 nralaphqkd isdkqllvkm adgatdankd dlvealgknp avtvadkkdv snaiasmftl
      721 llnmlyglla mavivavlgv intlamsvfe rsqeigmlra igldrrgikr mvrleslvis
      781 lfggvlgigl gvfmgwavgq listhlatye lvlpwarmgl flglaalvgv laalwpafra
      841 aklnmlaaik ae
//
LOCUS       WP_457696474             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696474
VERSION     WP_457696474.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27777
     Region          23..237
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttthsgvft atrataaaar atdltkvygq getqvvalda vsvefrqaqf taimgpsgsg
       61 kstlmhcmag ldsisggsar igdieltglk dkkltqlrrd kigfifqafn llptltalen
      121 itlpmdiagr kpdrawldrv vetvgladrl khrpsqlsgg qqqrvavara lasrpeiifa
      181 deptgnldsr sgaevlgflr nsvrelgqtv vmvthdpvaa syadrvvfla dgrivddmpg
      241 ptadtvlerm kgfdalhrts
//
LOCUS       WP_457696480             295 aa            linear   BCT 27-JAN-2026
DEFINITION  Bax inhibitor-1/YccA family protein [Streptomyces nigrescens].
ACCESSION   WP_457696480
VERSION     WP_457696480.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Guo,G., Xu,M., Chang,Y., Luyten,T., Seitaj,B., Liu,W., Zhu,P.,
            Bultynck,G., Shi,L., Quick,M. and Liu,Q.
  TITLE     Ion and pH Sensitivity of a TMBIM Ca2+ Channel
  JOURNAL   Structure 27 (6), 1013-1021 (2019)
   PUBMED   30930064
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Watanabe,N. and Lam,E.
  TITLE     Bax Inhibitor-1, a conserved cell death suppressor, is a key
            molecular switch downstream from a variety of biotic and abiotic
            stress signals in plants
  JOURNAL   Int J Mol Sci 10 (7), 3149-3167 (2009)
   PUBMED   19742129
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Zhou,J., Zhu,T., Hu,C., Li,H., Chen,G., Xu,G., Wang,S., Zhou,J. and
            Ma,D.
  TITLE     Comparative genomics and function analysis on BI1 family
  JOURNAL   Comput Biol Chem 32 (3), 159-162 (2008)
   PUBMED   18440869
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Reimers,K., Choi,C.Y., Bucan,V. and Vogt,P.M.
  TITLE     The Bax Inhibitor-1 (BI-1) family in apoptosis and tumorigenesis
  JOURNAL   Curr Mol Med 8 (2), 148-156 (2008)
   PUBMED   18336295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="Bax inhibitor-1/YccA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31126
     Region          58..295
                     /region_name="COG4760"
                     /note="Uncharacterized membrane protein, YccA/Bax
                     inhibitor family [Function unknown]"
                     /db_xref="CDD:443793"
ORIGIN      
        1 mrssnpvfsr rgfsrdtgya gfnappqagg paanpyagan pyaqggnpya qdatnpyaqg
       61 qqdvtqappq ytpqtrpmtm ddvvartgmt lgtvvagatv gwlfltenlg faigaglvam
      121 vlalvqsfkr kpspalilay aaleglflga lsgfindlpk mngapmqavl gtmavfvaml
      181 vayktrivrv tarftrfvmi aamgfvllsl vnvmfmvfgg geglgfrsgg lgilfgvvgv
      241 vlgalflald fkqvedgiay gapreeswla afgltltlvw iymemlrlis ilrgd
//
LOCUS       WP_457696488             337 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696488
VERSION     WP_457696488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=35121
     Region          72..269
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(82,121,152,247,250)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(82,247,250)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(82,103,152)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mpmtmsrarv arriataaaf ggggvgllgv atvgvlltev rlarrtvggs sdippcadgr
       61 ygaafghrtd rpplrlgflg dstaagqgvh rasqtpgall asglaavsel pvdfrnvalp
      121 gaqsddlerq velmlaagte vpdvcvimig andvthrmpp aqsvrhlsea vralrtagce
      181 vvvgtcpdlg svepvyqplr wvarrlsrql aaaqtigvie sggrtvslgd llgpefearp
      241 relfgpdnyh psaegyataa mavlptlcas lglwpeeerp epargegilp veqaaaeaas
      301 eggtevtasr apwallkhrr rrqlptaett dpssvtp
//
LOCUS       WP_457696491             490 aa            linear   BCT 27-JAN-2026
DEFINITION  sialidase family protein [Streptomyces sp. 900105755].
ACCESSION   WP_457696491
VERSION     WP_457696491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..490
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52342
     Region          <140..239
                     /region_name="BNR_2"
                     /note="BNR repeat-like domain; pfam13088"
                     /db_xref="CDD:463781"
     Region          215..>394
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          250..303
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          329..373
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrvflpltav taaalllgta tgatpaaavr dpdgtplvkv shgdpyarct igarspdsvv
       61 ypgtevepyl svdprdpghv vtvfqqdrwn dggarglaag wstdgrtfhp stlpfslcap
      121 ggadyeratd pwvstgpdgt vyaggegvdf tkstrtalla vtsrdggrtw qnlttthvde
      181 qpffndkpsl tadpirkgta yqvwnrldnd ppgpssldgp gyisltrdgg rtwsrarrfv
      241 vtstvpntqt ighqivadrr tgtlydffdr ityaddlttv vearyemvts tdageswsap
      301 vtvardtsvp evdpndpatp lragstlpsp avdpgtgtly mayegadfag gkvdsvqlvr
      361 stdggrtwgt pelispegvp afspsiavde rgtvaltyyd lrflepgntt tlptayqlat
      421 lrhgdpklrt errisrifdw lqapfaggyf lgdyqglaad gkgvravlte ansgapqnrt
      481 dvytgtlrid
//
LOCUS       WP_457696493             470 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457696493
VERSION     WP_457696493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49459
     Region          2..456
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 magvveqrsi dvvpdderhg savsqftlwl ganlqitavi tgalavvfga nafwsligll
       61 lgnllggavm alhsaqgprl glpqmitsra qfgvrgavvp lalvivmyig ffasgsvlag
      121 qavgelthlg etpgivifaa vtavaaavgy rlihtlgkia glvcalafvy lgirllqrvd
      181 lgtlladhrf elpvfllavs lsaswqlafg pyvadysryl prhtsaratf wwtlsgsvlg
      241 sqwsmtfgal aaaaapaafv ghevsyivgl ggagliasfl yfvialgklt inilntyggf
      301 mslvtsvsgf rgqrtlsprg raayiagimv agtavallgk dsfltsfkdf llflltfftp
      361 wsainlvdyy liskerydip alsdpagryg awnvraltvy vlgvlaqlpf lvthfytgpl
      421 vaplggadis wlvglavpav lywfaarhdt artaepgtld gdrspaglgg
//
LOCUS       WP_457696495             185 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine dioxygenase [Streptomyces nigrescens].
ACCESSION   WP_457696495
VERSION     WP_457696495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Chen,M., Zhu,J.Y., Mu,W.J. and Guo,L.
  TITLE     Cysteine dioxygenase type 1 (CDO1): Its functional role in
            physiological and pathophysiological processes
  JOURNAL   Genes Dis 10 (3), 877-890 (2022)
   PUBMED   37396540
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Joseph,C.A. and Maroney,M.J.
  TITLE     Cysteine dioxygenase: structure and mechanism
  JOURNAL   Chem Commun (Camb) (32), 3338-3349 (2007)
   PUBMED   18019494
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14410663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="cysteine dioxygenase"
                     /EC_number="1.13.11.20"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0017172 - cysteine dioxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20292
     Region          64..151
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mtdtasqadt arevpdgaqp ftalpernld krelqalvde laarpdlwre qvafsdterh
       61 yaslhrdefv dvwllcwtrq ndtgwhdhdl ssgavhvvqg vltesnprig gehlatavga
      121 gssfcfgpdh ihrltgatdd avsvhayspp lwrlgqydit gdglmrrvsv syadelrpmd
      181 attaa
//
LOCUS       WP_457696498             347 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696498
VERSION     WP_457696498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  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   2  (residues 1 to 347)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36907
     Region          5..341
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 marpnkrttl revaeatgls taavsyalrg khvsketeer vrkaaaelgy eadpiarala
       61 sgrtstvgvl agdlqdlwqq qlmaaigrel lagdryalil daggdperel alakqlrdqr
      121 vdgllvspvd psaegwskia davpvvsigd alsrartage vlfdnragid avleylrglg
      181 hrrvtvltpt gpstpdrpad vyvreaadrl gievevlpcp qeldaatama rrvlanspdg
      241 rrpagalapp tavfcfsdsi aygvyaaaae asltvgrdls vvgfddhpvs rvltpplttv
      301 dwgltdiake aarlavaaie grrvrrkril caprlsergs avelrre
//
LOCUS       WP_457696502             308 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696502
VERSION     WP_457696502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 308)
  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 10194457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32500
     Region          45..303
                     /region_name="PBP2_ProX_like"
                     /note="Bacterial substrate-binding protein ProX of
                     ABC-type osmoregulated transporter and its related
                     proteins; the type 2 periplasmic-binding protein fold;
                     cd13606"
                     /db_xref="CDD:270324"
     Site            order(50,52,99..100,103,142,144,225,249)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270324"
ORIGIN      
        1 mnrrtvlttl lagasaplla acssgitslk gdgvggdsgs ssggltigta nftenqilgy
       61 lyagvlnaag vkttvkpnlg sreivvpalr sgdidllpey qgslllyldq kateteagam
      121 qnalatvlpn glevlpyaaa edrdsfavtr etadryglkt ladlrkvngk lvfgaaaemk
      181 krvvgvvglk eqygvefkef kaldssgplv kgalkkgdid ianvfttdvd taengwvllg
      241 dpknlipaqh ivpliasrka dskvrkalar lgntlttpql telnrlvdke krdpdrvaea
      301 wlkkqklg
//
LOCUS       WP_457696504             405 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696504
VERSION     WP_457696504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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 405)
  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..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /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=42536
     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 vggrdilead aaelrrgigy viqqsglfph rtildniatv plllgwgrrk araraaelle
      121 lvglpadagk ryphqlsggq qqrvgvaral aadppvllmd epfgavdpvv rtqlqnellr
      181 lqeelrktvv fvthdideav rlgdriavfr tggrlvqcaa paellarpad dfvadflgae
      241 rglkllsltt ladvpyapgr eiradepvga lsrdgdrwrl vtsprgeplg wldtdalpag
      301 gtageaplea vrplrdtdsl lsalneavss pasavarvta dgvltgltsr daiheragrs
      361 haeagrtaat tepapeppva kdgkngkdae dtaplksaaa pepsa
//
LOCUS       WP_457696506             344 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696506
VERSION     WP_457696506.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 344)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35360
     Region          73..341
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msgdgdnggg iggaagdgpr dragttqsar aaagpdtgad vgmdtgtdtg agvgtdtgav
       61 vgadvgmdtg taarlqklfe ghrltptqrr iahcmvrraa dapflssvel aelagvsqps
      121 vtrfavalgf dgypalrrhl revaptdkpg dtgsyneyqq avqaeidnlr hlaasladps
      181 pvieagrlfa asrplpvlgl raataqaagf syfarkvhpd vrlldeggtm ltdridaavr
      241 agasallcfa lprhprevvd aleyartagl tvvtvadsaf apvahhtdll lpapvgtgla
      301 fdtacapmll grvlleamcd alpdaqarle efdaraaarg lfve
//
LOCUS       WP_457696512             329 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696512
VERSION     WP_457696512.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..329
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34253
     Region          105..308
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrgtevtsat aatdtteggi ttdttgttgt vrttdaapre aaaphprrry wragvlrggi
       61 elrhllrnpk elsghlvnvv valalagyin dkvpgtqvpm ahltlsgfaa yllfqiglvn
      121 lpqilvtere egallrlrat pggipaylva ksllvvamaf gtlvlllgta allvdgplph
      181 gpagwltllw vsalgllavv plgaaigavl pnprealali mlpvmallit sgamfplasl
      241 pavvqkiasv fplkwmaqgl rsallpdaar aaepagswel ptvaliltaw avlgfllavp
      301 llrraarres gsrlterhrk aglsggrag
//
LOCUS       WP_457696514             333 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696514
VERSION     WP_457696514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36274
     Region          29..246
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtttdhqpva paatapapts sstprqpvir vrdlrmsygs ahvlhgidld ihrgeifall
       61 gpngagkttt veilegfrqr sagevgvlgt dpargddswr ariglvlqsw rdhrrwqvae
      121 llthfatyyp rprdpaella lvglteqagq qvdrlsggqr rrldvalaiv grpellflde
      181 pttgfdpear rhfhdlverl ardegvtill tthdlaeaer ladriamlvn griraygtps
      241 elarraaaqa evrwtapdgt srrertedps qlvwelhqet ggpvadlevr rptledtylh
      301 mvhrdagdag dgadagttga seagasdgek raa
//
LOCUS       WP_457696528             167 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696528
VERSION     WP_457696528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17163
     Region          37..163
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 msttrpyppg dlgpesggag asaaapaaai pagqirrlrl agtrgavarg rdfarqalhd
       61 wgwlpaagad qraaaedvll vvselvtnac lhaegpeelr lrctakvlrl evsdlgagsp
      121 aprsphrpgr pgghgmfivq rlcldwgvvr nadgagktvw aelaaps
//
LOCUS       WP_457696532             330 aa            linear   BCT 27-JAN-2026
DEFINITION  COG1470 family protein [Streptomyces nigrescens].
ACCESSION   WP_457696532
VERSION     WP_457696532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11444751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="COG1470 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32700
     Region          <60..>288
                     /region_name="COG1470"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441079"
ORIGIN      
        1 mpfrprtavs gailataavl lcpaaaaarp aaapappgws aapapgdgat psaqdrpsfy
       61 legapgtvmn drlslhnptg ravavrlrgs gawiafaakk vtvpprtrat vpftvtvphd
      121 aapgdhpatl vatagdpgsg aaerdavpvh lrvsgpvlaa ltvenvsvrg rgdaaviryt
      181 lvnrgntvlt prlavradgl fgpvlrrglr tlpgrlspgq saeltepwag ppgldavevr
      241 ltvtadggah gsatasytal pwgvvagtaf llvagagglv vvrrrrraqg pggvggggpv
      301 rsaaggarps egqaadpaae lastgsgars
//
LOCUS       WP_457696538             169 aa            linear   BCT 27-JAN-2026
DEFINITION  GtrA family protein [Streptomyces nigrescens].
ACCESSION   WP_457696538
VERSION     WP_457696538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8) (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..169
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18998
     Region          9..141
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 msersalwsr lealtrevvk fgavggagvv vnfavfnlvr qltevpvvra siiatvvatg
       61 tnylgyryft yrdrdkrgrt keltlfllfs alglviengl lyvatygfhw dsplqsnifk
      121 flgigvatlf rfwsyrtwvf rtlpareaie taesfladgs rrprsasrk
//
LOCUS       WP_457696543             391 aa            linear   BCT 27-JAN-2026
DEFINITION  dipeptidase [Streptomyces nigrescens].
ACCESSION   WP_457696543
VERSION     WP_457696543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42409
     Region          12..375
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 msssqgaard llarwpvvdg hndlpwalre qvrydldrrd iaadqsahlh tdlprlragg
       61 vgaqfwsvyv radyagdkav satleqidvv relvarypda lrlaltaddm eaaraegria
      121 slmgaegghs innslatlra lhqlgvrymt lthndtidwa dsatdeprhh glsafgeevv
      181 remnrcgmlv dlshvsadtm rdalrvstap vifshssara vcdhprnipd dvlerlsang
      241 gvamatfvpk fvlpaavewt lradenmrah glhhldttea gmtvqrafea anprpkataa
      301 tvadhldhmr evagvdhigi ggdfdgtaft pdgladvagy pnliaelldr ewseadlakl
      361 twrnavralr aaedvaraer avrgpshvtl g
//
LOCUS       WP_457696534             501 aa            linear   BCT 27-JAN-2026
DEFINITION  peptide MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457696534
VERSION     WP_457696534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53604
     Region          14..501
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 massltkdaa qqgnpanggk tffghprgla tlfmtemwer fsfygmkall plyliapggm
       61 hmqattatai ysvymamvyl lampggwmad rfwgprktva igaaiviagh itlalptaas
      121 ffaglvlval gsgllkanis tmvghlydgp edprrdggft lfyiginiga flapltigtv
      181 genvnwhlgf tlaavgmalg laqfmlgtrh lsaessvvaq patpqekssv lrkgliwltv
      241 aavfytllgv tgnfadwalm pitiaglvip iavlfrmkrd kelseleqsk lsgyiwffav
      301 aavfwmiydq ngstlsifge hsttnnllgf hfptswyqsl npifimalap vvasawlwln
      361 rrekepstav kfasslalig isfavflipl idtaanggkv spmwlvaiyf iqtvselcls
      421 pvglsvttkm apakyssqmm gvwflavtag dsvaglltsp qlnvdlntag avtveavfav
      481 iagvgiwtsr krikelmggv n
//
LOCUS       WP_457696547             948 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457696547
VERSION     WP_457696547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..948
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=108930
     Region          1..206
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          569..942
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mpdvsvvviv yndadrlpta vqsvldqtlr dvevvivddc stdrsfevaq rlaadhpgrv
       61 rafqlpensg aggeprnvgi qhtegryvmf ldsddvlein acrnmleaae esgsdivsgl
      121 cvrlhkdtrn qkrdewyawl ysttrtlesv telpdlfvwd tlstnkcyrr dfliennlrf
      181 pkgmfyedlm fiadaylaag ritlipnqvy fwhvyeraav ksvtnrrhem tnythrldih
      241 rridallaer gleelklakd vkflkhdlvl hlrdlpfrde syrrefsels reylesiape
      301 aydrvqpiqa icayllqqgd wdnlipavdt linrdkvssp ltehdgriyw cdghlddpfg
      361 revldvtdig yhekpvnqlf lrnqltrfss sgravslagr itnplgvvpp garlkgelef
      421 sarrrslqsf rfpvhelrhe gdalhweaaa dltaklrplg ivdtiwdvrl rldvdgvrtt
      481 trltvadtgl seplpvrprl trmvadhlep hvsakghlaf rlvseghsae rvqelitrgv
      541 rgkpgtlakt gyrkakalrk kvtsgdnklr ayhevfcrlp vkkrtvvfes hlgkqysdsp
      601 ralyeemrrq gldfeaiwsy sgspkdfpkd vtlvrrwslp ylkalaqaef wvdnqsyplk
      661 ltkrpettyl qtwhgsalkn mgfdqpalka qtrgqqaeqq rsldrfdrfl vrsehdvrtl
      721 akafrlkekt llragyprnd alvharqrea ergvrergpl aaelgipedr tvllyaptfr
      781 kaggrhgrfe lpfdverfad qfgdryvllv rshylnhvvl pptvqgrvid vsarhdvtpl
      841 leladglitd yssvmfdyal ldrplvffty dydayvhegr gtyfdlleha pgpvvrtedd
      901 fhetiksfes qtleyaqrrk efvakfgeyd rgdaartivd qffaqwsr
//
LOCUS       WP_457696549             494 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic amino acid ammonia-lyase [Streptomyces nigrescens].
ACCESSION   WP_457696549
VERSION     WP_457696549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..494
                     /product="aromatic amino acid ammonia-lyase"
                     /EC_number="4.3.1.-"
                     /GO_function="GO:0016841 - ammonia-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009072 - aromatic amino acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=50975
     Region          19..461
                     /region_name="Lyase_aromatic"
                     /note="Aromatic amino acid lyase; pfam00221"
                     /db_xref="CDD:459718"
ORIGIN      
        1 mldngprtgr ritldgsalh ptdiaalaer tahpsapdpk afaraeeswe tarrlaatgr
       61 vygrstgvga nrtedvgaad adhglrllrs hagaigdplp arevramlav ranqllagga
      121 glnpavitsl laaldagahp vvnehgavgt gdlaalaqtg lalagehpwh cppggrapap
      181 ialdnndala lissnaltlg qsalaldelr rllaaslpva alsllavggs wepfaepvll
      241 arphpgsaaa aarlrtlsgi pprptpplgr iqdpygfrci pqihgpalda adtldgvlti
      301 evnaaaenpl isiedqaayh hgnfyaahaa laldtfrlav lqtarlstar laalsepdft
      361 rlrpflgdaa passgvmile yaagaalgem ravshpaslg havlsrgvee qasfaslgar
      421 qtlractyyr qilacelvaa vralrmrsle pdpglplata ftlaaealdp rmedrpltdd
      481 vavatglldg lael
//
LOCUS       WP_457696559             254 aa            linear   BCT 27-JAN-2026
DEFINITION  MHYT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457696559
VERSION     WP_457696559.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Galperin,M.Y., Gaidenko,T.A., Mulkidjanian,A.Y., Nakano,M. and
            Price,C.W.
  TITLE     MHYT, a new integral membrane sensor domain
  JOURNAL   FEMS Microbiol Lett 205 (1), 17-23 (2001)
   PUBMED   11728710
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="MHYT domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25741
     Region          3..>246
                     /region_name="MHYT"
                     /note="MHYT domain, NO-binding membrane sensor [Signal
                     transduction mechanisms]; COG3300"
                     /db_xref="CDD:442529"
ORIGIN      
        1 mghlhhfsag wispvlayam acvgsalglr ctvraraaeg rsrrnwllta svaigsgiwt
       61 mhfiamlgfg vtgspvhydv pltvlsllia mvvvgaglft vgygapglrs lllgglgtgv
      121 gvaamhylgm aamrlhgrvg fdpglvalsv viaagaataa lwaalsvrga vgaavaslvm
      181 glavssmhyt gmaavhielt psrapltgvt amefifplav algsflflta afvalsptar
      241 eraaaasvds lheh
//
LOCUS       WP_457696565             197 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696565
VERSION     WP_457696565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=21306
     Region          1..192
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mdsarsdsfm alkilvaggf gvgkttlvgs vseirplnte erlteagrpv drldgvqqkt
       61 tttvamdfgr itihddlaly lfgtpgqdrf wflwdelaqg algavvladt rrladsfaai
      121 dyfehrsipf vvavncfdga rahraqevar aldldpetpv llcdareras ckevliglve
      181 haasayearl pansvsp
//
LOCUS       WP_457696573             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696573
VERSION     WP_457696573.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29312
     Region          21..257
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 matdvhgtvt gtatgkgprs apsgaavqva glvrafgdra viddlqltvq pgefvallgr
       61 sgcgkstllr vlagldreie gevlvprrka vafqaprlmp wkrvwrnvll glpgraeres
      121 avraldevgl ghradawpkt lsggeaqras laralvrepd lllldepfga ldaltrikaq
      181 rlvaelwrer gcavllvthd veeallladr alvmeggria yettvdlprp rdisdprfga
      241 lrarlldrlg vagstddgag rterteatdd gsaaaa
//
LOCUS       WP_457696591             204 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696591
VERSION     WP_457696591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=21479
     Region          13..204
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mvsvpspthg thsvtaveqp pvpvklviag gfgvgkttav gsiseirplt teaaitevaa
       61 gvddlthtpg kttttvamdf gcitidptlk lylfgtpgqd rfgfmwddvv egalgglviv
      121 dtrrlddcya avdyfehkgi pfavavnafd gevhhdldev rwaldvsdhv plvvfdartt
      181 gsvrdallvv levalsraeh taas
//
LOCUS       WP_457696575             307 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696575
VERSION     WP_457696575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32269
     Region          52..301
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mtldqavpgh appdtsaeaa rpslskggka raesdspagg peldrvvpvs grrrsvprwl
       61 rravgpvall vlwqvfsasg aleedilasp gtiaatagdl lsdgtlpsam lvslqrvavg
      121 lllggvtgvv lalasglsrl gedlvdatmq mlrsipwvgv iplfiiwlgi geapkialis
      181 lgvafhlyln vyagirgvda qlveagtslg lsrwglirhv vlpgalpgam tglryslata
      241 wlalvfgeqv naddglgflm nqareffrtd vivvclvvya ilglladflv rtlerlllqw
      301 rptftgq
//
LOCUS       WP_457696583             153 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457696583
VERSION     WP_457696583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16386
     Region          10..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mlenvsaeps hptkdvtqhv gyllkrtqaa lrgamdkvlr ehgltvpqya tlellalhpg
       61 msnadlarat fvtrqsgnvv lrglqeagli trpatadhgr arpahltekg narlaavqaa
      121 vyaieqrmve aipaqrlavl ladldrmaaa lee
//
LOCUS       WP_457696597             165 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457696597
VERSION     WP_457696597.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17721
     Region          12..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maergaltra mddvdavtra vltasrllva vsarslgeae ervtlpqlrm lvvlstrgat
       61 klvalaellq vapstamrmv drlitaglah rqanpdnrre tllqltdegr rtveevtarr
      121 raevsaiver lapeqrasli ealtafneag geppvdapee thplg
//
LOCUS       WP_457696601             423 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457696601
VERSION     WP_457696601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  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 423)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /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=44726
     Region          171..422
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrqvvswvas acvgfaracv vvavsmlvpa vwaaavavai wwgpgnpwsw vpgcvlgsvg
       61 tlalsrpvcr mfrflvaqwt atdipagyrr aepvvrmstg ywwngfsyer trrdalldqr
      121 wrlrwsdpat wrdlrftgia pitagvigav ppagvavavl gfsqpalsah lvgvlglvaa
      181 vagapyawrs aepvavrflp aspakvladr vaeltaqrad ttvaqaaeir rierdlhdga
      241 qarlvglgls lataeklmet dpdqakalmr earagaatsl telrelvmgi nppvlnergl
      301 idavralald splevavsae vplrldppie savyfgiael vtnaikhaqa trvrislard
      361 gtgtgtgivv dvedngrgga daraggglag lrrrlavfdg tleisspagg ptrvrmmvpc
      421 esl
//
LOCUS       WP_457696602             215 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457696602
VERSION     WP_457696602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Galperin,M.Y.
  TITLE     Structural classification of bacterial response regulators:
            diversity of output domains and domain combinations
  JOURNAL   J Bacteriol 188 (12), 4169-4182 (2006)
   PUBMED   16740923
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Galperin,M.Y., Nikolskaya,A.N. and Koonin,E.V.
  TITLE     Novel domains of the prokaryotic two-component signal transduction
            systems
  JOURNAL   FEMS Microbiol Lett 203 (1), 11-21 (2001)
   PUBMED   11557134
  REMARK    Erratum:[FEMS Microbiol Lett 2001 Oct 16;204(1):213-4]
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23041
     Region          3..125
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          148..209
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrivvaedly llregmvrli eayghqvvat aatgpetlda lltwrpdvav vdirmpptqs
       61 deglrvalaa rselpglpil ilsqhvvqly arelladgag gigyflkenv fdadqfidal
      121 ervagggtam dpaviaklls sgsshrrleg lterehsvlg lmaeglsnqa igqrlflsds
      181 aiskyttslf gklgitddgt snrrvlavlt ylnep
//
LOCUS       WP_457696604             205 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696604
VERSION     WP_457696604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22156
     Region          1..167
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mritkythsc vrlerpgggt lvidpgiwse aralhgadai lvthehvdhv dvlrlkglga
       61 pvyapkgadf gglldvieve pgeefsaagf avtahggrha riygdfpdca nlgyllderl
      121 yhpgdsfhvp dkpvetlfvp vqaswlrase aidfvravkp eraygihdaq inerglhsvn
      181 gwldeeaggc yswvppgals pcser
//
LOCUS       WP_457696607              94 aa            linear   BCT 27-JAN-2026
DEFINITION  acylphosphatase [Streptomyces nigrescens].
ACCESSION   WP_457696607
VERSION     WP_457696607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Stefani,M., Taddei,N. and Ramponi,G.
  TITLE     Insights into acylphosphatase structure and catalytic mechanism
  JOURNAL   Cell Mol Life Sci 53 (2), 141-151 (1997)
   PUBMED   9118002
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..94
                     /product="acylphosphatase"
                     /EC_number="3.6.1.7"
                     /GO_function="GO:0003998 - acylphosphatase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10237
     Region          1..88
                     /region_name="AcyP"
                     /note="Acylphosphatase [Energy production and conversion];
                     COG1254"
                     /db_xref="CDD:440866"
ORIGIN      
        1 mirrrvvvsg evhgvffrdt crrtadqfgv agwvrnvpdg tveavfegep ervqklvdwa
       61 hqgpplatvd avavreeepe gltgfeirst sggf
//
LOCUS       WP_457696615             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457696615
VERSION     WP_457696615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45292
     Region          8..395
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,140,
                     143..144,147,234,237..238,241..243,246,274,278,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 meprgrtrwa iggllaggiv vnfldrtais vasssiadef gldlqqlgvv lsaftwsycl
       61 vqlpagmlvd ilgvsrltri asalwavagl ltavaggvgp iilarlllgv aegpsmvgas
      121 kataawfpvs ergmatalfd gatklanmva fpvlafvmse wgwragflfs avvsllftvv
      181 wwwgyrdpse yrslrpaere filrggardt drgglrqfrs alrsgrvwtv acgfacygyt
      241 inivltwmpe flqrefhvrl lqsgfysmvp waiatvaela vggwlvdrli rrgrnpwavr
      301 rtvltcglal ggtigaagsa gspviavgwm svslaglaia apvawalpgl lappgavgav
      361 sglmnflnta ataggvlltg wlaqvtgsfd apflfavavl avgvalywra lrpapvrdqa
      421 parqldrv
//
LOCUS       WP_457696619             359 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696619
VERSION     WP_457696619.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  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 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   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   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   6  (residues 1 to 359)
  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 359)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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   9  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..359
                     /product="sugar ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37900
     Region          34..338
                     /region_name="XylF"
                     /note="ABC-type xylose transport system, periplasmic
                     component [Carbohydrate transport and metabolism];
                     COG4213"
                     /db_xref="CDD:443359"
ORIGIN      
        1 mnaimrralt gavalslaap laacgsdqkd agagkdsigl llpenkaary ekfdrriiss
       61 riaslcleck vdyhnaeqqv daqrrqfdgl vkkgvkviil dpvdaaasks wvdsaakkgv
      121 kviaydrlae gdvaayvsyd nekigrlqaq gilaalgsqa aasdvvmmng sptdpnapay
      181 kkgahdvldg kvhkivyekd ipdwsaatak kemtdvinaq gaegfdavys andgmaggia
      241 aalksagikn vpvggqdael palqrlvagt qyftiykevr peaetaaeia frllrgksik
      301 slttttadsk sksgipaqlf kaqivtkknl kntvvrdgav rtdllcedfa dacksvgle
//
LOCUS       WP_457696621             252 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696621
VERSION     WP_457696621.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26313
     Region          17..216
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msaspaspvt svppapvifd ldgtlvdsep nyyeagrrll adhgvpdfsw ehhtrfigig
       61 tretletlrr efgldaplee llagknrtyl elarahtevf pemrvfverl saaghpmava
      121 sgssraaiea vlagtgldal lttvvsaeev ahgkpepdvf leaarrlgvd ptdcvvleda
      181 apgalaahra gmrciavpyv agtaddpafa gagllfqggq geftaqaayd wlrrggtaav
      241 eegpgrggrv gg
//
LOCUS       WP_457696623             159 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696623
VERSION     WP_457696623.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17088
     Region          1..137
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mavdsldaki lrllleqprt svreyarllg vargtvqarl drlerdgvit aysprlspaa
       61 lghpvlafvh ievtqghlee vadalaevpq iieafsttgg gdlltrvvar daahledviq
      121 qlislpgvvr trtemalrer vphrmlplve avggaagpr
//
LOCUS       WP_457696609             467 aa            linear   BCT 27-JAN-2026
DEFINITION  lanthionine synthetase C family protein [Streptomyces nigrescens].
ACCESSION   WP_457696609
VERSION     WP_457696609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Zhang,Q., Yu,Y., Velasquez,J.E. and van der Donk,W.A.
  TITLE     Evolution of lanthipeptide synthetases
  JOURNAL   Proc Natl Acad Sci U S A 109 (45), 18361-18366 (2012)
   PUBMED   23071302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..467
                     /product="lanthionine synthetase C family protein"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0031179 - peptide modification [Evidence
                     IEA]"
                     /calculated_mol_wt=49225
     Region          52..463
                     /region_name="LanC"
                     /note="Cyclases involved in the biosynthesis of
                     lantibiotics; cd04793"
                     /db_xref="CDD:271201"
ORIGIN      
        1 mtapltlcda asdlahrvad llsspeqvag taheafaalp pellqpawqp aslllghpgi
       61 allhtrcarn daryaavgha hlaaavaatt dagpaavgdl llparlhaqe hggyarllar
      121 saevhatyvr ahvarlvarr qehgpglaag dydaisglag egrglllaad hgdercaqal
      181 rdvldflvgm thplpspagd gsqmpgwwca pdrylvprdr aefpggdfnv gvahgicgpl
      241 almslayrag hqvpgmpdal rrmadwvvsv gypdelgmrw pgrvahpeaa gepshpslqr
      301 rqsgetgars rsgwcygtsg iawtlylagr alddrrltdl aedavsglvq rpydaavsad
      361 pgfchgragi lhtvsrmala tgrtewwaaa delarelvae cdartpfgyr qvlppsplse
      421 ptphrvhnpg lldgaagial vladyadarr gvaldevngw daaflmg
//
LOCUS       WP_457696630             317 aa            linear   BCT 27-JAN-2026
DEFINITION  sirohydrochlorin chelatase [Streptomyces nigrescens].
ACCESSION   WP_457696630
VERSION     WP_457696630.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=31622
     Region          52..263
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mssptgpapg spdfdaasps pgaapglpvr mprrqsgrhr kpeplaapeg apalvlavpg
       61 spsaasrsla eevssiarse lpgldarigy vdggddefps leavlaraaa ehkdrvgadg
      121 qpdpgpaavv vpllagpdsa llrrirqamm nsgsgaeltd vlgphpllae alhvrlseag
      181 laradrarlf tvataadgii latvggeeav qaagitgmll sarlavpvla aaldqegais
      241 rtaeqlresg sqqlalapyl igpeitdgll gaaaaeagca saealgaygt vgrlvlsnya
      301 aavgitlptq tqgvpvr
//
LOCUS       WP_457696632             342 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylglucosamine kinase [Streptomyces nigrescens].
ACCESSION   WP_457696632
VERSION     WP_457696632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Reith,J., Berking,A. and Mayer,C.
  TITLE     Characterization of an N-acetylmuramic acid/N-acetylglucosamine
            kinase of Clostridium acetobutylicum
  JOURNAL   J Bacteriol 193 (19), 5386-5392 (2011)
   PUBMED   21784936
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006823
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="N-acetylglucosamine kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0045127 - N-acetylglucosamine kinase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=33530
     Region          17..322
                     /region_name="BadF"
                     /note="BadF-type ATPase, related to human
                     N-acetylglucosamine kinase [Carbohydrate transport and
                     metabolism]; COG2971"
                     /db_xref="CDD:442210"
ORIGIN      
        1 mgepagrgpd tpvaghvlgv dsggsglria varagdagar plavrasdep vrtgpagiea
       61 ehmlsqllpa aaelaretga dgfaavcvga agmatlgeel rtrlpaalat afgvrrlalt
      121 adavtayaga lgqrpgavia agtgmialgt dltpaggwrr adgwghllgd cgggawigra
      181 gleaalrayd grpggsaall araeavfgpv tglpgalypr pdrpavlasf apevarcaae
      241 ddtvalgvlr aaaghiadaa aavcppdagt tvactgglfg mgepllaplr talaerlpda
      301 rtaaaagtpl dgsltiaaal agdrltlptd rkllqitwpa pg
//
LOCUS       WP_457696640             123 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457696640
VERSION     WP_457696640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..123
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13384
     Region          22..107
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mptdttsprt psgsrslehp aredirladv lhaladpmrl rivralaaae selncadiel
       61 pvskstcthh frvlrehgvi qqlyrgtakl nglrradlde lfpglidgvl rgadlqagrl
      121 gee
//
LOCUS       WP_457696647             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696647
VERSION     WP_457696647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23726
     Region          22..183
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msprsasvne elrrrsrerl lqatvelvge rgyeattlad iarragvarg lvsyyfpgkr
       61 qllqsavhrl mhrtlqaale raprpsgpda gqelmaraid ailglahdhp llmrthmagi
      121 ltaegfiqcp eqqrlaqllr etvvaygssd pdadypllra llmgsvvaml lpgaampqar
      181 lraellqryg lewergvppd eaapggtrtp gpvrggqr
//
LOCUS       WP_457696650             203 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces nigrescens].
ACCESSION   WP_457696650
VERSION     WP_457696650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=22054
     Region          4..180
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mttprdlliv amdvesgrpl ergdlslala gaelidllga ravrldgdqi vpgyrptipd
       61 rlldqaassl vqetpyesvd dwlwrrgegl agaylaaled egqvtrqhrr wrpfrtggtv
      121 lvdsparrqa adrwtsqetv ltvlasaagi ngtrtgdepg vaddavstvl aavhdavrel
      181 eterqrrsle kaafdniwrg dgd
//
LOCUS       WP_457696652             470 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457696652
VERSION     WP_457696652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..470
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49179
     Region          12..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 msrtitrspq dspeagqnse svlshglkqr hlsmialggv igaglfvgsg vgiaaagpai
       61 vllfmgtgal vmlimrmlge msaarpstgs fsvhaeeeig swagttsgwm ywlmlcagva
      121 aeataagtim hswvsfipay gwvalfmvff casnltavkn fgefefwfsa vkvaaivafl
      181 vlgvlgilgv fgsapgtshl tghggffptg aaglaagllt tisgfaglet vtiaaaesdn
      241 psrnvaravr tavwriavfy igsmavvvtl vpwndpkvak egpyvtvldq lgipaagtim
      301 qivvlvalls amnaniygss rmayslvnrg qgprflgkvt rgvpaaavla scvfgfvavi
      361 agivwpdtvf awllniagcs vlvvwsivcl tqlkmrrrle retpellsvr mwgfpyltwl
      421 tlaailgvfa vmasnadgrh qligtavvva vlagaghlkq rrdrraaesa
//
LOCUS       WP_457696660             336 aa            linear   BCT 27-JAN-2026
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696660
VERSION     WP_457696660.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35233
     Region          21..>240
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 msgqlterag gagpqafpal rivapeiegp edvvadadgs lyagaadgti wrlrlpapda
       61 agratavaht ggrplglqpl pggellvcda rrgllridpr hgtvrvlade adgaplrfcs
      121 nvtsaadgtv yftvssrryg ldewlgdfle htgtgqllrl rpdgtpevll eglqfangva
      181 lapdesflvv aesgayrlsr ywltgpragt adilagdlpg ypdnisrgpd gafwvalagt
      241 rsagvellhs mprrvrrtaw evlkrlrfsl ppdptarvla vrpdggpagd lravrspyrm
      301 vtsvcrtehl lamgsiaerg iavcalpgad gaasah
//
LOCUS       WP_457696656             210 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457696656
VERSION     WP_457696656.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..210
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22592
     Region          6..142
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mthdvtvpde efwdaryaes driwsgrpna alvreagdla pgraldlgcg egadalwlae
       61 rgwevtavdi srvaldraag haaattvgdr itwqhcdlgt afpagtfdlv taqflhshsd
      121 mpredilrka agavapggvl livghtgipa wepgsdvplp tpdevvaalg lpdgqwdllr
      181 ceehpsfrtr hdgepdprtd ntvklrrrtv
//
LOCUS       WP_457696664             440 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457696664
VERSION     WP_457696664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=47335
     Region          5..400
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mnrrrprivi vgagfagyec artlsrqakg aaeivlinph dyflyvpllp evaagilepr
       61 risvsltgtl pgvrlvlgev hdvdfdarrv dytdpedrdg sltydrlvlt vgsvnkllpi
      121 pgvaehahgf rgmpealylr dhitrqmela gaaedpaera arttfvvvga gytgtevtaq
      181 gvrftdslvr qntglrdgpr prwllldiad rllpelderl srtadrvlra rgvevrtrts
      241 ikeatmdgvl lddgefvssr sliwcvgvrp dplvascglp tdkgrlcvde flavpgqpgv
      301 facgdaaavp dltrpgettp mtaqhaqrqg kvaahnlaas cgqgtpraye hhdlgfmvdl
      361 ggsqaaanpl hiplsgplag avtrsyhlla mpgnrirvaa dwlldavlpr qavqlglvrs
      421 wsvpldaetp evarvpggrp
//
LOCUS       WP_457696683             407 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696683
VERSION     WP_457696683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44755
     Region          131..404
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtlfkdpafn fnglfalggs gygasevgev ltavntinka glsaqtytet fknlgdqlrk
       61 ppssgepgte ttrfralraa qyyaqalffv lgsdtpgsee elykagrrsw dafcercdpv
      121 pvtaripygk tplpvwffrp dssgerrrtv iltngsdgqn vdmwtygvaa alqrgwnalv
      181 ydgpgqgqll fvdqvvftpr wetvvtpivd wltarpdvds rkialtglsm agdlapraaa
      241 fehriaalva mpgvlspwlg fppevreilt pdkektnniw nkevvpelpa saaatmkkri
      301 epfsvpamla aragkmftdf ytpatlvksl ditdvvdrik mptlvldydf eqfypgqprq
      361 lfdkltapkd yvkltaatga qlhcspmapq qhcevvfdwl qeklsgs
//
LOCUS       WP_457696686             231 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696686
VERSION     WP_457696686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..231
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25501
     Region          18..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mseidrsraa raeartriee vaarlfaerg fagttigeia aeaglskpml yrhfdskqel
       61 hlallerhrd elaaapvrel lygegdldqr mtamydawfg yveshpytwr mmfrdttgda
      121 evqafhrelq rrqretdmal lrefvpgipe aeleplgeai rsalyglalw wldrpdhpre
      181 llvatmtrit rglistvedp naetpgassp gtpgapgpsg aapsdapggt d
//
LOCUS       WP_457696688             352 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696688
VERSION     WP_457696688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37315
     Region          112..322
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msvqpemqlr ttmrvhpelv pafealphfp dpyediegtr egfhkmlaaf padrtgvsse
       61 rfeipradgs altvevyrpe ggavtgaeed tgpgqdtqga apegagralp avlhfhgggy
      121 algrslpgqd raaialcrel pavvltveyr lapehrypag vedcyralew aaeraaglgi
      181 dparialtgk saggglsaav almardrggp aivhqslcvp dlddrvgade vasdaegave
      241 arvttardiq rawrhylpeg mavaetyaaa aragdlsglp payvlvcdld plreaglaya
      301 rrlmdagvpv tvrnvpgawh gfelfapdsr vakemtahwt gqlrealypv eg
//
LOCUS       WP_457696693              81 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457696693
VERSION     WP_457696693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..81
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=7631
     Region          <39..80
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mkfvskaavl saatgiavvg gagmasahgg agaagvaqns pgvlsgnliq vpidlpvnvc
       61 gntlnfiall npafgntcln v
//
LOCUS       WP_457696712             382 aa            linear   BCT 27-JAN-2026
DEFINITION  CobW family GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696712
VERSION     WP_457696712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Edmonds,K.A., Jordan,M.R. and Giedroc,D.P.
  TITLE     COG0523 proteins: a functionally diverse family of transition
            metal-regulated G3E P-loop GTP hydrolases from bacteria to man
  JOURNAL   Metallomics 13 (8) (2021)
   PUBMED   34302342
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..382
                     /product="CobW family GTP-binding protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40226
     Region          64..358
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 merlnvvlvg glhaearqaa verllrtvpg svalhhdlas aadgtvrrtv rdaggtldtg
       61 daplvndcac calredlvpe lerlaagrtc rlaivelwds vepkamaevv tacgsenlal
      121 tgvltavdpa lllpylgcgd dlaeaglaaa asdqrtvadt warqleyapv laiatgeepa
      181 epadlalldq lhpmahqisv esgelaaaat agfdvaaaad rqhpacallp qeadadgvst
      241 lvwrhsrpfh perlyaaled ltcaaarsrg rfwladrpdt llswdaagga lcventgpwl
      301 aslpdaawem vpptrraaaa ldwhpehgdr tqhlvftspg ldreglrsll dsclltdaey
      361 aggppawksl ppafdalldp vs
//
LOCUS       WP_457696716             287 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696716
VERSION     WP_457696716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32064
     Region          16..78
                     /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          102..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msasessgsv vrrillgsql rrlresrgit reaagysira seskisrmel grvsfkardv
       61 edlltlygvg daqerealls lareanvagw whsysdvlpg wfqtyvgleg atsllrvyev
      121 qfvhgllqte syaqavvrrg mpdagpaeie rrvalrmerq kllvaersaq fhcvldeaal
      181 rrpygeravm reqvkhliev serpnvrlqv mpfslgghag esgaftmlgf qesglpdvvy
      241 leqltsalyv dkpeevaqya rvmdrlqeeg pnpaetrdll rgllqlm
//
LOCUS       WP_457696721             228 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696721
VERSION     WP_457696721.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 228)
  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 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   5  (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 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24169
     Region          1..90
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 msairllvlg avrqhgrahg yqvrndleyw gahewsnakp gsiyhalkqm akqgllrahd
       61 iapstvggpp rteyeltaag eaeffallra alsqhdqkvd mlsagigfvv dlpraeaval
      121 lkervralqe wrgtvtgyyt peggteqlgh igeimnmwvh sadsgaewtq glieriegga
      181 yvfagegepf vgvladgqen pyattdaedp dgggsggagd ggaatear
//
LOCUS       WP_457696729             252 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696729
VERSION     WP_457696729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 252)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28676
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          131..247
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 msysvgqvaa fagvtvrtlh hydeigllqp gernhaghrr ygdddldrlq qilfyrelgf
       61 pldevaalld dphvdpqqhl rrqhdlltar idqlqkmaaa vehamearrm nvrltpeekf
      121 evfgdfdpde haaeveerwg hteaykesqr rtaaytkedw krvtaeldai hramadllar
      181 gesadsaaam dvaeehrqfi cgayydcahe lhtclgemyv tderftatye airpglavym
      241 rdaivanaar hq
//
LOCUS       WP_457696732             235 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457696732
VERSION     WP_457696732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..235
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=25612
     Region          14..209
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mntlalgpqw ldpdyliatf gligvlvivf aesglligff lpgdsllftt gllvttnkld
       61 rplwmvcsli vlaavlgdqa gylfgrkvgp slfkrpdsrl fkqenvekah effekhgpks
      121 lilarfvpiv rtftpiiagv srmnyrsfit fnviggalwg agvtllgasl gkvefvhkhi
      181 elilvaivli svvpiaiefl rarskskkaq aapphpadrp hgaptdtrrg rhakr
//
LOCUS       WP_457696740             371 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696740
VERSION     WP_457696740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..371
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41175
     Region          <108..368
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltskkvll lavfvavalf vltiwlwprl skknwravlg rigllvatql slfatiglsa
       61 nnsfgfyasw adllgqeqep gvvtdyqtgp ngtklrmlgt qrvsvqngar ptaggridkv
      121 lirgehsqia spayvylppq yfqkkyahqk fpaalvltgy pgtaealykk lhfpqtqhel
      181 lkrhkmrptv lvmmrptvap pqdtecmdip ngpqtetfft kdlradisdh yrigreaksw
      241 gvigdstggy calkmtmrhp esyssavals gaykaprdat tgdlfggnqq lerennllwr
      301 qrnlpappvn llvtsskqge gnyretlefi qqtkspsris siildsgghn fntwrreipa
      361 alewlgnhlr a
//
LOCUS       WP_457696751             412 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696751
VERSION     WP_457696751.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43616
     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"
     Region          254..371
                     /region_name="CBS_pair_SF"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains superfamily; cl15354"
                     /db_xref="CDD:449531"
     Region          256..330
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341358"
     Site            order(282,294,299..300,303,335,357..359)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341358"
     Region          335..371
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341358"
ORIGIN      
        1 mirfehvtks ypdgttavdd ltfevaegel vtlvgpsgcg ktttmkmvnr lieptsgril
       61 ldgedisald pvqlrrrigy viqqvglfph ktvldntatv phllgrprre araraaelld
      121 lvgldpatyg drypeqlsgg qrqrvgvara laadppvllm depfgavdpv vrehlqnefl
      181 rlqttlrktv lfvthdleea vrlgdriavy gagrieqfdt patvlgapat pytaefvgad
      241 rglkrlsvtp vepgdlerpp vvrlddpaar aagrisadga swavvldadg alhgwvpaaa
      301 ltgapeapad gagpglkkht pqgatvreha rrmdarlplg aplrqalstm lqhdagwvav
      361 qdggrflgvl tparlhtalr rattadaanv prgevsldtv pgpgapapgp ag
//
LOCUS       WP_457696753             244 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696753
VERSION     WP_457696753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 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   5  (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   6  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25217
     Region          20..224
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mrgsaagpsc letndwicge ylrtrsqelv datvqhlgit avsvaiglli afplalvarr
       61 wrgaagpvlg lttvlytips lamfalltpv fgvsaavvvt glvlysltil vrnilaglqa
      121 vpaevreaar gmgygparll cevelplalp alvaglriat vstvamttig svvgygglgn
      181 liadgmagff kaevltasvl cvllalladl llmglqrqlt pwtraqgrat ararrgtrva
      241 kavg
//
LOCUS       WP_457696755             250 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696755
VERSION     WP_457696755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25519
     Region          8..217
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mgaiagawqw lttaanwage kgvwhrlteh lwlsglclvl sclialpval wlghlgkgga
       61 lavnlsnvgr aiptfavlvl ltigplgtqg dwptlialvl favpplltna ylgmreadrd
      121 vveaargmgm sgpqlllrve iplayplimt glrsaavqvv atatlaalag ggglgriita
      181 gfgnydtaqv vagallvavl alavegvlvl aerfldpmrg rrraarrasp pakgagpgat
      241 raapasapap
//
LOCUS       WP_457696760             380 aa            linear   BCT 27-JAN-2026
DEFINITION  NADH-quinone oxidoreductase subunit D [Streptomyces nigrescens].
ACCESSION   WP_457696760
VERSION     WP_457696760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="NADH-quinone oxidoreductase subunit D"
                     /EC_number="7.1.1.-"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=42027
     Region          11..380
                     /region_name="NuoD"
                     /note="NADH:ubiquinone oxidoreductase 49 kD subunit (chain
                     D) [Energy production and conversion]; COG0649"
                     /db_xref="CDD:440414"
ORIGIN      
        1 mtettvgigg aaestdmvln igpqhpsthg vlrlrlvldg eriqhaepvi gymhrgaekl
       61 feardyrqii mlanrhdwls afsnelgvvm avermlgmev peravwtrtl laelnrvlnh
      121 lmflgsyple lggitpvfha frereelqtv meeisggrmh ymfnrvgglk edlpagwlgr
      181 arhavadvrs rmdvfdnlvl gneifrgrtr gvgvlapetv haygvsgpia rasgvdfdlr
      241 rdepylayge lqstlrvvtr eegdclarfe cllaqshnal dladacldri aelppgpinq
      301 rlpkvlkape gatyawtenp lgingyylvs kgdktpyrlk lrsasfnniq alvellpgtl
      361 vadmvailgs lffvvgdidk
//
LOCUS       WP_457696757             320 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696757
VERSION     WP_457696757.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 320)
  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 10194457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33537
     Region          46..313
                     /region_name="PBP2_ProX_like"
                     /note="Bacterial substrate-binding protein ProX of
                     ABC-type osmoregulated transporter and its related
                     proteins; the type 2 periplasmic-binding protein fold;
                     cd13606"
                     /db_xref="CDD:270324"
     Site            order(51,53,99..100,103,151,153,234,258)
                     /site_type="other"
                     /note="putative chemical substrate binding site [chemical
                     binding]"
                     /db_xref="CDD:270324"
ORIGIN      
        1 msstsrvart avaagtvitl aaglaacggk sleekgggkg ggkgelvigs agfteskvla
       61 eiysrvlada gyrtrvqtla nrelyepale kgqidvvpey astlaeflna kkngskakpv
      121 assdldktvt aleklasprg lkvlpagrat dqnafavske faaenklktl sdlgkskqki
      181 klasgeecet rvfcklglek tygiditgld pkgvgtpqak qavkdgtdql vlttttdatl
      241 dnfglvllkd dkklqnadnv lpvvnaesag dkeietalgk ltralttedl itlnrkvdae
      301 rlkpadvaqa ylesrglakk
//
LOCUS       WP_457696764             401 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457696764
VERSION     WP_457696764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..401
                     /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=43409
     Region          138..400
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mqrlydflrr hptgvdtfwa iplfgitslw vasrtdgpqq liaaiftigl clvvalrrka
       61 pvkmllltaa igvgqlvfri etnpgdaamf aitytvasgp tvprwasrca lagavfgpal
      121 sfwrfrdeag gqtmgeslfv tvlltvpfvl awvlgdsmrt rraywaqlee raarlekere
      181 aqsriavaae rariarelhd vvahnvsvmv vqadgaayvl daapeqtrqa letisgtgrq
      241 alaemrrllg vlrtgeqpeg geyvpqpgve qltdlmdqvr saglpvdfrt egeprelpss
      301 valtvyrivq ealtntrkhg gpdvgatvrl syrdddldll veddgrgaqr elyedggadg
      361 lghgligmre rvgmvggtlt agprpgggfr vsavlplkpa r
//
LOCUS       WP_457696769             320 aa            linear   BCT 27-JAN-2026
DEFINITION  threonine aldolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696769
VERSION     WP_457696769.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="threonine aldolase family protein"
                     /GO_function="GO:0004793 - threonine aldolase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - L-threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34210
     Region          43..>263
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mraafrgarr vlpehvrret vrerldrlva dapaaydldg wtdvygnddg iigelerrta
       61 galgteaaaf fptgtmaqqv alrcwagrtg natvaghpls hmevherdaw avvsglrmvh
      121 ptnaprppta aeiydlpepf galalelplr dagfvlptwd eltaaveaar dreavvhfdg
      181 arlwecgphf grtlpeiaal adsvyvsyyk slggisgaal agteefveea rtwrhryggq
      241 lfqqwpaala alagldrelp rwavtpprts ppsppqtsap smpqtspprp ppppppggas
      301 prllsgrrgg ggpaggrrgp
//
LOCUS       WP_457696771             330 aa            linear   BCT 27-JAN-2026
DEFINITION  Rossmann-like and DUF2520 domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696771
VERSION     WP_457696771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="Rossmann-like and DUF2520 domain-containing
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=33190
     Region          38..295
                     /region_name="COG5495"
                     /note="Predicted oxidoreductase, contains short-chain
                     dehydrogenase (SDR) and DUF2520 domains [General function
                     prediction only]"
                     /db_xref="CDD:444246"
ORIGIN      
        1 mnaippleaq erparltvgv vgagrvgpal aaalqlaghr pvavsgvsda svrraaellp
       61 dvplvtpaev laradlvllt vpddaladlv sglaetgavr pgqllvhtsg rfgtavldpa
      121 tragalplal hpamtftgts vdvqrlagcs fgvtspdelr maaealviem ggepewiaes
      181 arplyhaala iganhlvtlv aqsmellhda gvqapdrmlg pllgaaldna lrsgdaaltg
      241 pvargdagtv aahiaelrrh apqsvagyva marttadral ahgllkpela edlldvlads
      301 ddgpgtapga pdasgpdpda pghgpeggdr
//
LOCUS       WP_457696784            1080 aa            linear   BCT 27-JAN-2026
DEFINITION  NACHT domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457696784
VERSION     WP_457696784.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     The NACHT family - a new group of predicted NTPases implicated in
            apoptosis and MHC transcription activation
  JOURNAL   Trends Biochem Sci 25 (5), 223-224 (2000)
   PUBMED   10782090
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475721
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1080
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=117421
     Region          273..1047
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mdpsavgvrl asgvvaplvk klfvkegpga glvakpvris glvsfkgerr tltdkglrkl
       61 aaelvdravr sagpgerpla adeeqavada lattlrglgd ldmddvqavr lgatalaerl
      121 eaasphavrg lsrdaellha tllgtaclhi vhfftqrsaf vartlvqqsr sldslitlid
      181 aflerhpspr aadaafergy layiarkhgr ltiygidlah spdrwpldaa ymsleatapa
      241 araltgvspf veetgprggp papvpvpadq alagrdrvll rgvagsgkst lvqwlavsct
      301 kapaetalph lygripfvlp lrtlardgap lptpdrflas vgcpvsgsqp egwadrvlas
      361 gralllidgl deipdrerel trrwlrdltd afpdnlwlvt srpsavrddw laadgfgelt
      421 lsamsraeva afigrwhdaa rcdaedperl dayeqsllaa vhtkqdlarl atnplmcgli
      481 calhrdrrgy lptgrkelyd aalgmllsrr drerdmaapt gielsdgpqi qllqrlaywl
      541 irngrseldr eraerilgea lpavpaaaeq gdataifrhl llrsgllrep apgsvdfvhr
      601 tfqdylgaka avedgdfgll vahaedsqwe dvirmavaha rpreraeilr gligrgdgie
      661 drrarlrvhl lamaclehat eidprvrdev heragailpp rsreesnlla gvgplvlell
      721 pgpegladde aqevvataal igsdaalevm krfrehpatg aqhqlalswp hfdtdtytre
      781 ilqhldsfvt ftakspaelh alralgqprv svsgpftaae llgalplgri eslsimenpe
      841 isdlaflref pslewlslwd cpavesvapl adlplhslsi sgppeknvpi prglhrlrht
      901 rtlvlhctlp peglaalpad aplihltlsr pvgteftgvt rwprirdiql lrlthdfgad
      961 qwsalaslse lehfsfgpae egvtlhlptg lrlpqvktls iintarlpvp gmshllasal
     1021 pafpgvrklq lygvidgsid lsptsvlpel qevylsylrp epdyslpphi klsryprprt
//
LOCUS       WP_457696788             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696788
VERSION     WP_457696788.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23029
     Region          4..>116
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstqarrgnt rqriqdvale lfseqgydkt slreiaekle vtkaalyyhf ktkedivisl
       61 fqdlgrpcde liawaegqpr tletkqevlr rysealrsae plfrfmqenq aavrdlsige
      121 tfksrmltlf dllkepesel tdqvrcital fsmhagtfam qnvegdpeek rkailevate
      181 lvtaanpphr rparpdsaqt vsp
//
LOCUS       WP_457696786             222 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457696786
VERSION     WP_457696786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..222
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21988
     Region          14..217
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mskftalrns kkfalrnrva vvaagvgvta algagiataa daglqnltsg vgstvsaqad
       61 aqaksavdak aaakakkaav kkadawvtpv dkytlgstfg lagnmwsssh sgqdfvvpsg
      121 vavkaahsgt vvkagpnggg dgpaygnaiv vkhgngmytq yahlsqinvs vgqqvgtgek
      181 iglsgstgns sgphlhfevr tgpnygsgie ptgflrahgd tv
//
LOCUS       WP_457696790             547 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457696790
VERSION     WP_457696790.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..547
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57024
     Region          44..439
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(51..52,55..56,59,90,140..141,143..145,148,168,
                     171..172,175,300,303..304,307..309,312,340,344,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mgksqhatpt gdgqtsavkg rppaapapgq ekqpagvrtv lfalmiamll amldnmivgt
       61 amptivgelg glehlswvvt aytlataast piwgklgdmy grkgvfltsi vifligsals
      121 gmaqdmgqli gfravqglga gglmvgvmai igdlipprer gkyqgmmagv mavamiggpl
      181 vggtitdhlg wrwsfyinlp lgaialimvt avlhlpkkrs qtridyvgaa lltvgitalv
      241 littwggtey dwlsgqiigl gvlgvlalal fvlverkvse pvlplhifrn gnfslvtlig
      301 flvgfvmfgs mtflplfqqt vqgasatnsg llllpmllam mvvslfagrv ttrtgkykif
      361 vvvggglitl gltllslmdt dttrftsgvy mavlgagmgf lmqttmliaq nsvemkdmgv
      421 gsssatlfrt iggsfgvail gaifthqvqa tmverigkag ekmtsggaqm dpkglaqlpp
      481 mikdayshav atgthhvflw gaalsiagfa aawflkevpl rggpatpaes pqngdapadr
      541 iavaetv
//
LOCUS       WP_457696798             159 aa            linear   BCT 27-JAN-2026
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696798
VERSION     WP_457696798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..159
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=17309
     Region          1..103
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mtrvwewnrp vtvrevledl qkersiaytt vmtvldnlhq kgwvrreaeg rayryeavst
       61 raayaaalmn eawsasdnpa aalvaffgmm speqrqalrd avrmvqidep aedpeqqaee
      121 aeetapaeer taeaaaeaag eagpaegdep gasatgkgr
//
LOCUS       WP_457696802             224 aa            linear   BCT 27-JAN-2026
DEFINITION  urease accessory protein UreF [Streptomyces nigrescens].
ACCESSION   WP_457696802
VERSION     WP_457696802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22538
     Region          2..224
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 msraalfvla dgrfpaggha hsggaepava agritdaasl esfcrgrlht aglvaaalaa
       61 aaaaghdple ldaaadartp vpalrttark lgrqmmraar rtwpsaelda laaarprgah
      121 qpvvlglaar saglgpldaa avvayenvsg pataavrlls ldpfdatavl arlaheidri
      181 attattaaar ishegtnalp aasaplldit aqqhagwpvr lfas
//
LOCUS       WP_457696810             201 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696810
VERSION     WP_457696810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21438
     Region          14..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttrreqtsh esselilraa aelfaakgyr qttfadvaer sgisrgsipw hfgseeglll
       61 avlersvdli raglvegpae lagpegveag fdrltagada lfaqpttklf vtllvealep
      121 gspihgryve ihntlrdhcr rwlerlplpp glsaetlavt iigagigihq qwllapdrvd
      181 peqalaalrt lvagavlpag d
//
LOCUS       WP_457696808              92 aa            linear   BCT 27-JAN-2026
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696808
VERSION     WP_457696808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Qin,Z., Devine,R., Hutchings,M.I. and Wilkinson,B.
  TITLE     A role for antibiotic biosynthesis monooxygenase domain proteins in
            fidelity control during aromatic polyketide biosynthesis
  JOURNAL   Nat Commun 10 (1), 3611 (2019)
   PUBMED   31399587
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..92
                     /product="antibiotic biosynthesis monooxygenase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10112
     Region          11..>59
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mkvgmvashy phaayreefi srvhqvrevf lrtpgclsae cwvsadavvs ivqwesqeas
       61 atsfatveaa gldlaydere srpreivrla ac
//
LOCUS       WP_457696825             197 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457696825
VERSION     WP_457696825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Chapman,E., Best,M.D., Hanson,S.R. and Wong,C.H.
  TITLE     Sulfotransferases: structure, mechanism, biological activity,
            inhibition, and synthetic utility
  JOURNAL   Angew Chem Int Ed Engl 43 (27), 3526-3548 (2004)
   PUBMED   15293241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16049904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21799
     Region          10..189
                     /region_name="Sulfotransfer_4"
                     /note="Sulfotransferase domain; pfam17784"
                     /db_xref="CDD:465504"
ORIGIN      
        1 maedrparpk vfglglsrtg trslttalrt lgfdvahypc dpgtyqalvd gtarfpllae
       61 rdgitditva pyyeeldlaw pgakfiltvr eeqswlrsca hhwerpitsk aapgsvyvrv
      121 qrflraavyg cqefnaarfa rvhrrhveqv rrhfagrdgd llvldivggq gyerlapflg
      181 vpvpdepfps fcgasat
//
LOCUS       WP_457696828             380 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457696828
VERSION     WP_457696828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41725
     Region          2..368
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mriaylhsgs ipsvyangvh vmrmcdaftd aghevvlhal pgtapaddiy ayygtrnrfe
       61 vrtlgqpavp gagkwirarq vradlrrrgv pdllygrdpf sllacsglap lvyethllwp
      121 srsiravers lfrrpdlrrv vcvsqaladd yraafpelta lstidlvtah dcadpvpadg
      181 qvaplpgrar alrigyvghl ypgrgtdvil glaeqlpdad fhlvggttad ralwqsrcrq
      241 phvyfhghrp paelapfyra fdivlapyqr raycaggvge isrwvspmkl feymsygkav
      301 iasdlpvlre vltdgvncll rppgsvadwa qavtqlaedt alraalgnea rrqlterytw
      361 raradrvlpa vpaaagpesr
//
LOCUS       WP_457696833             248 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457696833
VERSION     WP_457696833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26490
     Region          10..>143
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mttvpryagd fadryddwft psagstrdtv dllvrlaraa ppgpllelgi gtgrvalpla
       61 grghqvhgid aaptmvdqlr akpggeeltv sigdfsevdh dgafamvyva ngtffelpsq
      121 qdqlrcfara aqrllpgglf vldghlpevl aahsggggaq svastngdpm lrtrrlqpas
      181 qrytsdylvl degtfrhvrv vfryaapgel dlmaaaaglr lrerfgawsg apfndssrgh
      241 isvyelpa
//
LOCUS       WP_457696835             279 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457696835
VERSION     WP_457696835.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  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 279)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30765
     Region          58..160
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mtapsgsrdp qtyirenhem wqrwtplkaa saqydlagfr aggsrmrale caevgevrgr
       61 sllhlqchvg ldtlswarlg aqvtgvdfca egvatarsla advapsavfv eadalglpsr
      121 ldgtfdivyt shgvlgwlpd lyrwaevaah ftapggfvyv feshpaawml dnkvdrpelr
      181 lrysyfgeae plafeyrspi avpeaelpgw eyawghslge vvsalaaagl rveflhewpf
      241 vgwrmvpfmt qdqdgwwrlp eglpslplsf slragkpsd
//
LOCUS       WP_457696844             145 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457696844
VERSION     WP_457696844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15664
     Region          3..144
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mvdeldvsav gsalqvslgl fvrrlrqplp geltlpevsa lsrleraesa ttselaraeq
       61 itpqalgmtl agleerglvr rrpdpadgrr vvmsvtedgq relrnrrsvr aeqlaealva
      121 ggftraelet lraaaplier lgenl
//
LOCUS       WP_457696850             347 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional class I SAM-dependent methyltransferase/NUDIX
            hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457696850
VERSION     WP_457696850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 347)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
REFERENCE   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18603225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="bifunctional class I SAM-dependent
                     methyltransferase/NUDIX hydrolase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37108
     Region          28..143
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          205..328
                     /region_name="NUDIX_MTH2_Nudt15"
                     /note="MutT homolog 2; cd04678"
                     /db_xref="CDD:467561"
ORIGIN      
        1 mgnvtqdawd ahygegrsfr plddaeltll relvpaprgg ghaldvgcgl gdlarhlaat
       61 gytvdaidya asalstaeqt ppasgtvkfv rcdiekdpld glrssydlia frlsyafigd
      121 rtrvmhrlre rlspggaivv itpvvegvpa drraialdee eiallsagwh tverrdaegl
      181 afivlrdpaa gpvayrgkgr psphaltgag vvvtdeagrv llgrsrrgtw elpggkndgv
      241 esfveaavre leeetglrak eadarllail mdavhgiprv taavrvvdfs gkpavrepdl
      301 ihrwewhdva dlpalgaalf tpsahvldvv wpgvlpglpp vhrypla
//
LOCUS       WP_457696865             567 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457696865
VERSION     WP_457696865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  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 567)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..567
                     /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=59456
     Region          196..409
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mssstpsvae nrptrsffag pkeqgrwllw raageaflaa alvllahegv stidgrlega
       61 apalgligip lvlvrrrfpv acvvglaalm gvvsavallt avaaytaarq lrtprrrvgv
      121 llgagaltml tcaafapgln vgsrlfglal gavfagttiv vpglvgtagg qqdrllralr
      181 eraaaaeear rladsesrmr ersriaaemh dlvghrlslv slhagglema lqkeapelrd
      241 eaavvrratr damqelreal gvlgplgsdt gtgaltdatg tradiealve esrsggipva
      301 fswdgpdlda rpaqvrravh rvvresltnv hryaagahvt vevrhtderv avrvrngvpp
      361 trpaavtglg sgrgltglre rvallggsle vgrtpgggfa vaagipatpg pgaetadaaa
      421 ddsgsapvde srsrlsvlqr rvagavigll glagvgmmml fgillvdrsr ydlayqspek
      481 prlgmtreqv eravaaddda sraaaagrep prpasatdcm ypysdtklkg grmqivrycf
      541 rsdtliaidr ftvpivtepp resrthd
//
LOCUS       WP_457696875              74 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696875
VERSION     WP_457696875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7766
     Region          2..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 maiivdldvq lakrglsvge fadavgitpa niavlkngra kavrfttlda icrtldcqpg
       61 dvlrwvpddn sdda
//
LOCUS       WP_457696885             149 aa            linear   BCT 27-JAN-2026
DEFINITION  SRPBCC family protein [Streptomyces nigrescens].
ACCESSION   WP_457696885
VERSION     WP_457696885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790656
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16633
     Region          1..145
                     /region_name="SRPBCC"
                     /note="Ligand-binding SRPBCC domain [General function
                     prediction only]; COG4276"
                     /db_xref="CDD:443417"
ORIGIN      
        1 mpnfevvtai aappdqvfav cldvqahtrs maasseravd grtrgelslg dtvtfqarhf
       61 gltwrlkari taydrprrfv deqesgpfkr wrhahhfepd gaggtvmrdv idfasplgpv
      121 grivdrills rymphlirtr naylagtfd
//
LOCUS       WP_457696888             253 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457696888
VERSION     WP_457696888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27310
     Region          23..159
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mervtnlpes laqpadpaqa nhydsfaeay saetesnlln ayyerpamla lagdvagrri
       61 ldagcgsgpl stalrdrgav vtgidasagl lalarrrlgd daalhvvdls erlpfadgaf
      121 ddvvaslvlh yledwgptla emrrvlrpgg rliasvqhpf vdyaiqdprp dysattsytc
      181 emtfngqsvp msfwrrplha mtdafttagf rlavisepqp dpsarelfpd dfhalstkig
      241 flffvlegsa sts
//
LOCUS       WP_457696893             631 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696893
VERSION     WP_457696893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 631)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 631)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 631)
  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 631)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..631
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68000
     Region          9..605
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtrlkfgqma aalprmvgmv lrtgwevdrr alagvvaaqf gqgvtaawgl vavnrvltql
       61 fadgptadkl hqalpslvvl avvsvgsall aawstamsgr lepqveravs aryyaavtrv
      121 eveaterpev qrvleagrfg tdsarsmlrl svgvgsvlig mvaaavvlvs lhwillpmll
      181 aiafpkgwga vrsarreyts rlnwvdhrra issllayltr phaageirvh aagetllrgy
      241 eemsrqaeae qrrlaraqah tdlvaggfag laslacygll wwllsagglp lavggtavia
      301 irnsterlts lvqqvnrlye ellfltdtrh atelaaehai prtgtplphp travhvenvs
      361 ftypgadspa lkgvslsvrr gtvtalvgan gsgkttltki laglllptdg svwwegepgr
      421 rvelreadrt evfdtvgllg qdfphwemta atniaigvgd rprdmdrvke aaqaadvhal
      481 iaglphgyds ivfkgyergv qlsggqwqkl gtarsryrna pfflvdepts aldphaeiaa
      541 feglwslaer dhavvlvthr laatakadhi yvlddgrvve egthdqlmsv ndglyrgmfa
      601 aqaaqygltq ppgdtlpapr rdsaprreet l
//
LOCUS       WP_457696897             306 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696897
VERSION     WP_457696897.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31488
     Region          <5..277
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mtgthplhgp ahrpvhdgtp vlvaeglakt yplpgggrhr aadrisftlp rggsigivge
       61 sgsgkttvar mlvglvrpda gtvtvdghar tprtprgraa rlarardiqm vfqdpyvsld
      121 prltarqclh talrlhgaap rhaelratel lglvglgtre adarphglsg gqrqrlaiar
      181 alavdpkvlv ldeavaaldv siqaqilqll aeirrdtgva lvfvshdlav vrhltdetlv
      241 mrrgqtveqg pteqvlaapa apytrallaa vphpgwdpat ataaaavaga gsgsgagsga
      301 gsgvta
//
LOCUS       WP_457696898             353 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696898
VERSION     WP_457696898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37133
     Region          22..330
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpnptthpap vpsapppdaa plldidrltl qlpgtarpvl aevslrvgpg evvglvgesg
       61 sgksttakaa lrllpedara egtvrvsgtd vlslsgaalr ahragsvamv hqdprsalnp
      121 vrrigdflte rlarsgldrp amraralell dtvglsdpeh rirqrphels ggmlqrvvia
      181 galaaapqll ladeatsald vttqaeilal lrtlrdehgm gllfithdlq laaaycervy
      241 vmyagrvvee qpagalfsap rhpytrglle cspdlaeapr vlrpipgrpp sladafpgcp
      301 fharcahadd dcavwtpapa alptggsasc rklpdapvpt dsptpssyek rqp
//
LOCUS       WP_457696900             289 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457696900
VERSION     WP_457696900.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29516
     Region          21..285
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mtslnpamgp gptvtavprp rtrrpvapta aagflalvvl aalcapllap yapdaidlss
       61 slegtgrehl lgtdasgqdl lsrvlygart sliaplllla laavlgvtlg tvaawrggwv
      121 dtlvsritdv myafpgllfv vliiavfgsg ittsvialgl afaptiakyt rsialaerak
      181 pyvdaylvqg mggarlcvrh lipnlgrsla gylvvlfgea lmslatlsyl gfgtqppssd
      241 wglmvqegqa aivqgallpa mvpgcavaav vvafniagvr aadrlsakg
//
LOCUS       WP_457696908             308 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696908
VERSION     WP_457696908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32610
     Region          15..263
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 meipagagvg egtgmtrlra avrdawdels tseravaqyl vgaepeqllf agaqelgtas
       61 gtsnatvvra lqrigyaglp alkrdlttdf tttvapevrl rqriahvgkd ltgiwddvfd
      121 eaaerighar rltdaesfqr avaalaqage vfcygvaase laarhlalml artgrrarfl
      181 gatgfafada llplgrgdav vvfqparplt eftvlverar avgakvvfvt delgdtfegr
      241 veavltapht ptgitaeslt glviadalll alttldetra vetshqltal reqllppsvr
      301 trgrkdas
//
LOCUS       WP_457696904             561 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696904
VERSION     WP_457696904.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 561)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 561)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 561)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..561
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59157
     Region          71..545
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mkrtfrptap llaasvvtla lgtagcsgat ntlgggkaln aadlrltptt aeatgrldtv
       61 nwlledepds ldldtqgtsa grvvltnvce rlyqlqpdms vrpflarkat rpdpttlvls
      121 lrddvtfhdg akmtaddvlw slkrhadpdm eqadefgnvk kmaktgphei titfkepdal
      181 ftkalagdag lvyhrsqvqa agaefgtpgr gdacsgpyel tswksgdslt irradsywgs
      241 kpltrqivfr wasdsafvna lttgaadggy aespntaaal agrkgltqhy gpstaslali
      301 ptergglkdp airralslal dragiaasgy gglvqpwatp vgsgawgyak paftaaqrkl
      361 naaaparpda aalarakklv qsagaptepv iigtdasqgr tvianavraa lqriglvgqi
      421 ktvptaqfee fyssaqarse idvlvgdwyi sksdpmgfyd nalsdspnnw vgfksrtyds
      481 kvhqalrtld dgararlaig vqkefadaav wipvaqvpav lvlkdgltgp pasqahlyyp
      541 waaelgtapg aapahqpqkk d
//
LOCUS       WP_457696924             430 aa            linear   BCT 27-JAN-2026
DEFINITION  diacylglycerol/lipid kinase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457696924
VERSION     WP_457696924.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="diacylglycerol/lipid kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0001727 - lipid kinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45001
     Region          103..396
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mlvllvfagl rsivlvgvgl aglavtaagl wwvlartgvi rvlafilait tpvvvlvlya
       61 vagllwvvlv slalwtlavf tgrtalvpqk tdparlperp vappsrpfli mnprsgggkv
      121 grfqladrar algaevveld pgqpqdvaql arravddgad llgvaggdgt qalvagvaaa
      181 rgvpfvvica gtrnhfamdl gldredpsac lealtdgvel rvdlgfidvg qpvaegrgri
      241 fvnnasfgay atvvqspayr ddkarttlqm lpdllthhsg prlkvragdv tvdapqavlv
      301 snnpylmedp aglgrrerld sgvlgvlgvt vdnavqaasm lrgshgpglt sltvqevvvd
      361 adapvipvgv dgealtvptp vrcwiepgal rvrlprhrpg tprakppmnw rrvhslaltv
      421 grtaagrdtg
//
LOCUS       WP_457696926             136 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457696926
VERSION     WP_457696926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14748
     Region          7..118
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 msvslravvi espdpvalga fwsavlessi dsgtdgvvir fgqhreqlly ivegsgrpsr
       61 gpepfmcvaa adatldeevd rlvklgavvi krkwnvdeel hvgfalmtdp egncfqvlss
      121 deevqaaerm lesesw
//
LOCUS       WP_457696925             123 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696925
VERSION     WP_457696925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101108
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..123
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13895
     Region          1..115
                     /region_name="HTH_MerR-like_sg3"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd01282"
                     /db_xref="CDD:133388"
     Site            order(2..4,18,34..36)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133388"
     Site            order(48,51,55..56,65,89,93,99,103,106..107)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133388"
ORIGIN      
        1 mligelsrrt gvkarllryy eaqglldarr eqngyryyde davvtvrqvr alldaglste
       61 virsvlpcvr geaqeapefd wcadlrailq gemtamdehi dhlrrtrstl adylaqspvs
      121 ptr
//
LOCUS       WP_457696934             167 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457696934
VERSION     WP_457696934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18431
     Region          19..161
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdrpdlsyaa yardrlagmp spaapeafal ayhllhlsyl vvadleshih rprgwtlpgf
       61 rlmfklwllg ptqparlavi samsrsavtn aintlerdgl verrpvpddr ravaagltat
      121 genavreafa eqsrreqqwf atldaeerat ltdlltrvla arpedad
//
LOCUS       WP_457696950             764 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457696950
VERSION     WP_457696950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..764
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=82258
     Region          7..763
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          591..619
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(592,595..596,599..600,602,632,635..636,639..640,
                     642..643,672,675..676,679..680,683)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          630..660
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          671..697
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          711..739
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mllgtdlrtr rrqlglsqed larragidvk tvrsiergra aprpstvrql adalgltgtd
       61 regfcaaaap gpidppiqpv srppqnphrt vpaqlppdvr gftgraahld aldaiaaagg
      121 qqpttvvvta idgsagvgkt tlavhwahrv adrfddgqly vnlrgfaptg apmppaeair
      181 afldafhvpp qripagldaq aalyrsllag krmlivldna rdvdqvrpll pgapgclvlv
      241 tsrnqltglv aaegahplgl dpltpreacd llthrlgaqr vtaepepaea iiaacgrfpl
      301 alaivaaraa trphlplhtl adelsgtatg ldalstgepa tdiravfsws yhalspdaaq
      361 lfrllglhpg pdtsapaaas laalpvaqvr pllaelaran liaehtpgry alhdllraya
      421 tdlahhvdpd ehrhaathrl ldhylhtaht adrllvrard litltppqpg atvdhptdqq
      481 qalawftaer rallaavgha aaagfdthtw qlawilwtfl erqghwhdla aagrtavaaa
      541 rrladptvqt rahlvlasvs tryldrldda hahlqqalel stqdgdqvwq ahthfnlsll
      601 rerqghhtea ldhaqqalnl lraaghrrgq arainrvgwc qallgdhqqa ltacrqslcl
      661 hqelddplgq akswdtlgya hhqlghhaqa vscyqhahtl frdlgdryhe adilthlgdt
      721 hhaagnasaa hdawqhalai ltdldhpdad tvhaklaphr dhav
//
LOCUS       WP_457696957             466 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457696957
VERSION     WP_457696957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..466
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51464
     Region          23..439
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(133,135..136,273..277,298,301..302,305,320,324,377)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 mnpqqvstpg tdpyfpdhgd tryrvhryel dldyrpvsnr lsgsarisal agpapleeia
       61 ldlaafrihr vlvdsrtarh thragklrir ppealapgta ftvevrytgn ptpmrspwgg
      121 lgweeltdga lvasqpigap swypcndrpa dkasyrvait tpspytaiag grlltrttra
      181 ssttwvyeqp aptstylvtv slgkytavpl tsavpaegrh ppvpqtaylp arllpefted
      241 fdrqtrmmqf fqdmfgpypf geytvvvade eldvpveaqg matfgtnhld gartserlia
      301 helahqwfgn svsvtdwqhi wlnegfakya ewlwsehtgg rtaaahaaaa hqlltalpqd
      361 lvpadpgkkl mfddrlyerg gltvhalrca lgedaaffhm lkdwtrrhrh gtvstadfta
      421 haqqyaaasl dglfdawlre pslpplphps ephrpanlqv kplsqg
//
LOCUS       WP_457696968             276 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457696968
VERSION     WP_457696968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29737
     Region          29..266
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mnsshdgngt heehsrirgh rpahgeplld rafrmlacfg pdtpvlslta laaradlpka
       61 talriarqlt eqgalertds ghytiglrll eiatvaprgh glrtialpyl qdlwhatrqh
      121 vqlvvregle gvlverlsar daprvmyrvg grlplhattp glvllafapt qvqedfltad
      181 hpadddspsa tadalrpkla airrdryavf srpqwdtpmt gvaapildrn httvaaisvi
      241 tpseqsqpaa hipavvavar aitramttdt agdplp
//
LOCUS       WP_457696962             126 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696962
VERSION     WP_457696962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14418
     Region          29..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtkqfsnsp edadlrrads lareifsdva nkwalliies lgertlrfse lrneiegvsh
       61 kmltqnlrml erdsliertv hpvvpprvey tlteagqalr vtidglcdwt hqylghieas
      121 rrrfda
//
LOCUS       WP_457696970             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696970
VERSION     WP_457696970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20775
     Region          16..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mndsddgagr aappkradar rnketlldaa aaifvtsgve apvrdiaaka gvgtatiyrh
       61 fptradliia vyrhqvdaca eagpallatg ptphaalgqw inlfvdflvt khglaavlqs
      121 dnpgfdtlha yfldrlvpvc tqlleaavva geirsdlday almrgvgnlc igadsdpryd
      181 arrlvellia glrrph
//
LOCUS       WP_457696977            1013 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457696977
VERSION     WP_457696977.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1013)
  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 1013)
  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   3  (residues 1 to 1013)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1013)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1013
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=107576
     Region          19..268
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          162..1013
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          805..839
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          885..913
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(886,889..890,893..894,896,926,929..930,933..934,
                     936..937,966,969..970,973..974,977)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          924..954
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          965..993
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpshrpetas dhvssappal ffrvlgplrl rvggqesdvr ppqsaallat lllrhgrrgs
       61 tqalidavwg dnvpsrapgs lrahvarlrg mleplrppra parilvsrpn gyalrlepda
      121 ldltvfdrqv gsaeralrag rakdalalyd taldlwygep lagvpgpfaa aqrsalrerr
      181 laavearsaa elalgghtlv veelralaee hpqrerlqel lmtalhetgr qtealsvytr
      241 trqvlnengr tgagaglerv rrrilagpga weagshgsgr pahhrrpdgs tdrdvsagtv
      301 srpatpasam lrlpaditdl vgrdavvarl rnalensrvv algaisgmgg vgktavavrv
      361 ahaarslfpd gsffvdlrgl dhrpaephqv lgdvlralgv apahlpdett eraalyrsll
      421 adrkvllvld nardldqvrd llpagpgcgv lvtsrirlag lsgailvdld elpdraavdl
      481 laslvgarrv raeeeasrel vvgcgrlpla irivaarlaa rpartvaeta raladerrrl
      541 telggdtaav eptlrlgtgl lapeqlrafr llalpdvpel srsaaaalld rpdrdaeclc
      601 edlvdasllq spapgryryh dllrlfarvs aaegvpaper daalvrllra yapvardafr
      661 latgdafptd etpvkptrpg tglrslaplv sqeqatvwll deqasllalt eqaagvtgvp
      721 asacaellla adplgrngtr tqnleraaga vleaakrsgd vtaegvahcm lggarairfe
      781 maaalphlra aagifrregr rtllahalna lggcalarrd faaalehlme alpltreprs
      841 psseavslgy lglallasgr peegvrsgre avalarssgd sggqanalra lgqillyagq
      901 edealeclhs slelwrstgs afreslvlgg laeaynllgr hdeavahage ardiatrhgh
      961 ayfqaralmq lgnafgaqgr pdqaafsyqp alrifrqlgm peaadaearl dgr
//
LOCUS       WP_457696985             150 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system RatA family toxin [Streptomyces
            nigrescens].
ACCESSION   WP_457696985
VERSION     WP_457696985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10789869
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /product="type II toxin-antitoxin system RatA family
                     toxin"
                     /GO_function="GO:0043023 - ribosomal large subunit binding
                     [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0045333 - cellular respiration [Evidence
                     IEA]"
                     /GO_process="GO:0045947 - negative regulation of
                     translational initiation [Evidence IEA]"
                     /calculated_mol_wt=16387
     Region          1..143
                     /region_name="PasT"
                     /note="Ribosome association toxin PasT (RatA) of the RatAB
                     toxin-antitoxin module [Translation, ribosomal structure
                     and biogenesis]; COG2867"
                     /db_xref="CDD:442114"
ORIGIN      
        1 mplvhveihi aappedswna vvdvesypac mdsvqsvtvv ersgedrrtt awsvhlkgsv
       61 lewveaeqld haarrfdfhq vsgdlahfig hwavqpcddg gslvsltvef eigipllaem
      121 lnpvaatalr dnaqqmlhal errltktvga
//
LOCUS       WP_457696987             414 aa            linear   BCT 27-JAN-2026
DEFINITION  class-III pyridoxal-phosphate-dependent aminotransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457696987
VERSION     WP_457696987.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..414
                     /product="class-III pyridoxal-phosphate-dependent
                     aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42972
     Region          36..405
                     /region_name="OAT_like"
                     /note="Acetyl ornithine aminotransferase family. This
                     family belongs to pyridoxal phosphate (PLP)-dependent
                     aspartate aminotransferase superfamily (fold I). The major
                     groups in this CD correspond to ornithine
                     aminotransferase, acetylornithine aminotransferase;
                     cd00610"
                     /db_xref="CDD:99735"
     Site            order(115..117,143..144,146,196,229,231..232,258)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(116..117,143..144,196,229,232,258)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            258
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mtgphtagev fdqlrrhqsp klaltgkfag qgavessalg srvtlsdgrs aldfgsyava
       61 llghrhprvv aavgrqlgvm ptstrslanp vaaeaaahla dylggrlpki yfglngadav
      121 evsvklarla tgrdrvlavt ggyhgktlga lalthspmfr aglrgcvvdv vhldpddpha
      181 vreqlsagpv aavifepvqg engavplrta vlrqwcedah ahgafaiade iqcglrrcge
      241 rsvaladrlp vdavlvgkpl gggvmplsav actqelyrpl dtdpflhsat fgghplscaa
      301 lpaaleavee laehgrtlsg rltdglralg erhprvmsgf hgrgllwgid fttpaaagev
      361 vvslanngll vspclgrptt vrllpplvtt eaeldealdi ldtaldaagt gidd
//
LOCUS       WP_457696989             105 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl carrier protein [Streptomyces nigrescens].
ACCESSION   WP_457696989
VERSION     WP_457696989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 105)
  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 105)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..105
                     /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=10579
     Region          24..102
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mthttptetp ttpsagvpap adppgadlat vvretvaevl gttpdaivas tdlraeygid
       61 slelmaigaq leralnvqis aedlmgadtv gqavellaqr kagqa
//
LOCUS       WP_457696990             422 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457696990
VERSION     WP_457696990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Bukhari,H.S.T., Jakob,R.P. and Maier,T.
  TITLE     Evolutionary origins of the multienzyme architecture of giant
            fungal fatty acid synthase
  JOURNAL   Structure 22 (12), 1775-1785 (2014)
   PUBMED   25456814
REFERENCE   2  (residues 1 to 422)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="beta-ketoacyl-[acyl-carrier-protein] synthase
                     family protein"
                     /EC_number="2.3.1.-"
                     /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=43537
     Region          19..418
                     /region_name="FabB"
                     /note="3-oxoacyl-(acyl-carrier-protein) synthase [Lipid
                     transport and metabolism, Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0304"
                     /db_xref="CDD:440073"
ORIGIN      
        1 mtgrshhsgt hrwpserprv vvtgigvksp agltldevme tvlaadstaa phkelveqgs
       61 pvhfacrvpe fdvdpyvtrr errqidrpte lalcaaadav eqaalsglpp arvgvhlgtg
      121 igglptmesi vrdhdahptg mpvhsvprtm ansaaarvam ryglhgscvt ystacasgat
      181 algeatrriq ygeldaavag gfdsavttfm lsgfsrmqal srrndapqla srpfdaqrdg
      241 fvmgegaavl vlerresalr rgahilgeva gyatnadahh ivaphadgav aaacmadava
      301 dagllpsdig qinahgtstq andsaeatai hrcfngqapp vtavkgvtgh liggsgalea
      361 aislvcaerr ivppvanlmv aseadridvv agsprsvdca pvlsnsfgfg gqnvclvllp
      421 at
//
LOCUS       WP_457696993             182 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Streptomyces nigrescens].
ACCESSION   WP_457696993
VERSION     WP_457696993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..182
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18538
     Region          1..151
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mhallingsp rarsataala avvegalrar gatvstvdla tdagrspdar pamllgdsap
       61 rfdavvlasp vhhasysgll kltldglpgd wladtavgll ahgggprsgs vvcehlrtva
      121 kslggwvvpt qvaacpddfv rladgtaapd epllrrchvl atelhrcatm lrhsaptaav
      181 lp
//
LOCUS       WP_457697003             317 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697003
VERSION     WP_457697003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..317
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32347
     Region          4..315
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mavsvrigts evgysdlgra lggrlglpve plprlldsli wdlraprvlm aavvgaslav
       61 cgaalqsitr naladpyllg vssgasagav vvvllgvgan tlgitggafg gslvsfgllm
      121 lllrrsglds vkivltgvvv gqlftaltsl vliaagdadt traitywllg smasarweav
      181 iicaivavtg lavvwvcaaa ldgfafgtdt amslginvrm trivllvvta lmtsvavasv
      241 gaigfvgliv phgvrflvgp rhrvllpfta lagavflvwt dalarvafap qevpvgvfta
      301 llgvplflli lrkrgel
//
LOCUS       WP_457697004             258 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697004
VERSION     WP_457697004.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27826
     Region          5..234
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 madetiirdv nveiqpgetv gligpngsgk ssllrcvagl raptagviry dghdirgwna
       61 rrlaqhvafv eqasdadsdl rvadvvalgr tpfrdrwrgl drtdravida alarvgltdl
      121 rarawqtlsg gerqrahiar alaqqpwgil ldeptnhldv khqlelmdll satdqtvlvv
      181 lhdlslaarf cdrlillhqg avvgsgkpqe vltpdrlkdv fevdaevghd gldnlavsyr
      241 gvapaggrnd ahtagesm
//
LOCUS       WP_457697006             279 aa            linear   BCT 27-JAN-2026
DEFINITION  Fur family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697006
VERSION     WP_457697006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31888
     Region          141..263
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mhptgppppl rymqmktilv ysawlthvav grdrrcalhe pasrwlavrp srrhavlvhr
       61 vrnqrtaaev rlrarrdprl tlsqgidcra tsperrtcve lpverpsege emakeqvvap
      121 srqlharrsa dqadgrrpsp rstwqreavl raleeldafa saqelhrllr gqgnrvsltt
      181 vyrtiailer ldlvdvvrdd kgersyrrrd apehqhylvc rqcghsvpvp seafetwlta
      241 vqqahgftev qhmldlvglc recwtgeqtd shsseprha
//
LOCUS       WP_457697008             297 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697008
VERSION     WP_457697008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..297
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31425
     Region          10..159
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mkprdltagf angaesfdrl faalwspiga atvkaaglrp gahvldaccg sgasaipaad
       61 rvaphgtvda vdlaepllhl graraaargl gtvrfapgdv ldwpaprggy davvcslgif
      121 ffpdmaagte rlsrllrpgg rltatiwarg aveplpelif rsvlperpel aeasrpanpl
      181 epigtaesfr dwltarslsf veveryplal prdpdllwsl vlgtafrgll dglpaaaver
      241 vrerftasll eggrdpidfs tlvgtgalrr vaprrhaggt rrfptaiepi gpmphis
//
LOCUS       WP_457697016             202 aa            linear   BCT 27-JAN-2026
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase [Streptomyces
            nigrescens].
ACCESSION   WP_457697016
VERSION     WP_457697016.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Ju,T., Goldsmith,R.B., Chai,S.C., Maroney,M.J., Pochapsky,S.S. and
            Pochapsky,T.C.
  TITLE     One protein, two enzymes revisited: a structural entropy switch
            interconverts the two isoforms of acireductone dioxygenase
  JOURNAL   J Mol Biol 363 (4), 823-834 (2006)
   PUBMED   16989860
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Dai,Y., Wensink,P.C. and Abeles,R.H.
  TITLE     One protein, two enzymes
  JOURNAL   J Biol Chem 274 (3), 1193-1195 (1999)
   PUBMED   9880484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="1,2-dihydroxy-3-keto-5-methylthiopentene
                     dioxygenase"
                     /EC_number="1.13.11.53"
                     /EC_number="1.13.11.54"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0010308 - acireductone dioxygenase
                     (Ni2+-requiring) activity [Evidence IEA]"
                     /GO_function="GO:0010309 - acireductone dioxygenase
                     [iron(II)-requiring] activity [Evidence IEA]"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0019509 - L-methionine salvage from
                     methylthioadenosine [Evidence IEA]"
                     /calculated_mol_wt=22198
     Region          1..186
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 mtllqvmped apdnvllrtr nheriaealr gcsvafsrwp lhgtitpgts qaevlshyra
       61 evdelcareg lglvdvaqlh peeghewear aakarsafle ehrhaedevr ffahgtgcfy
      121 lhlagrvyav vceagdllsv pagtrhwfdm gpcpefaair ffekedgwvg dftgdpiaqr
      181 fprldallas gaatdaetet at
//
LOCUS       WP_457697029             428 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697029
VERSION     WP_457697029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43559
     Region          26..371
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 msidvkdstm dreaaeveep lpgdlrmara lwpvllasav gllpftifst ylvpiadeag
       61 ssvaamgglr glgglaallv gtalapfidr vrkewaaaag lvalgasaal gasgdfilla
      121 vfcllvgast svlnpaltaa aadrfgtgka agraatlvta vqsmtamlaa pvvalpallw
      181 gwegdlvavt aasvllavvf flrgrnkaae digseqrlsy lasfkalgas rgvvplllis
      241 llrtavfmgy laylaayydd rfqldpglfa fvwtlsgasy fvsnlltgri tnsaeprirt
      301 ermlviglva alvsvvgfyf thwlplalal tslhaashav vaacavsllv rrcgplrgsa
      361 lsvnaagqsl gvflgaalgg aglglagypg iavafgalvi valgaaflvs rpgageqeqd
      421 tndapasg
//
LOCUS       WP_457697034             243 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease, partial [Streptomyces nigrescens].
ACCESSION   WP_457697034
VERSION     WP_457697034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 243)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..>243
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          46..>239
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mpqtlappap aparasapda sgdpelrala erhgltvsga rpslpeylrq lwhrrhfisa
       61 fagakmtaqy sqaklgqvwq vatpllnalv yylifgllig trngvpdfvp flvtgvfift
      121 ftqssvmagt ksisgnlglv ralhfpracl pisfclmqlq qlffsmgvlv lillgfgqlp
      181 twswllvipa lalqfvfntg lamvmarlgs ktpdlaqlmp fimrtwmyas gvmfsidlil
      241 kgk
//
LOCUS       WP_457697036             211 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697036
VERSION     WP_457697036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21882
     Region          31..77
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          89..196
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 makdgsgsep aaarrapaga avlredktea iraavfeela aagfarmsie giarragvgk
       61 tavyrrwrsk lhlvldvisa vavagmptpd tgslsgdvrm llevaaralr hpmasqiipd
      121 llaeaarspe laqalkaalh dsqegvaaav varavergel pqdvdarlal dlltgplywr
      181 llvvrdelpk gyldalsgsv vaalgaalgp e
//
LOCUS       WP_457697038             781 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457697038
VERSION     WP_457697038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11421729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..781
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=88017
     Region          10..222
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          365..726
                     /region_name="Glyphos_transf"
                     /note="CDP-Glycerol:Poly(glycerophosphate)
                     glycerophosphotransferase; pfam04464"
                     /db_xref="CDD:398259"
ORIGIN      
        1 mseigldagp rfsiivpvfr vqgflrecmd svltqeftdf eliaiddcsp drsgaildey
       61 aahddrvqvl hlpanvglgp arnaglaqar gdyllfldsd dtlvpgalga laerltated
      121 peilifdyar tywdgstrrn alsalldesg apffplaerp qlldllqivw nkayrrdfve
      181 ehdfafpegy yedapwtfct litaqriavl drvclhyrqr rqggnilrtt srkhfdvfdq
      241 yarvfdhlda hpelsrwrph mfrkmvdhyl tvldkpgrlp hhaqaeffhr aardyrlrlp
      301 agfvrpsgva ggkyallard aypalaglkv vgkvrrtvrk hagkrvrqak rkamdlryqa
      361 llrqpldenl avysaywnrl pscnplavye kakelapdvh gvwvvkkhla dsvpagidhv
      421 vlnsprywev varakylvnn vnfadnvvkr egqihlqthh gtplksmgtd qkrypaaakg
      481 msfrkllara drwdfslsan rhtteqwerv ypcdfasvda gyprndvyyr ataqdvldir
      541 erlgiapgrt avlyaptmrd yqvgyvprld leklsrelge nfvllvrthy fydrdpglqk
      601 lqergalidv sghpvveelc laadalvtdy ssimfdyanl drpiinyadd wdtyvrsrgv
      661 tfdllsglpg dtpgvittte delieafrsg rwdderatgl raafrarfcq wddghaaerv
      721 vrrvllgqea tpeplpqeer tvapspraaa aaagllklpa prtaahddva psgtsdvela
      781 g
//
LOCUS       WP_457697040             651 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457697040
VERSION     WP_457697040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..651
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70675
     Region          19..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpvpddlaaa aptgpdapap tvsvivpvhn trryldrslg svfaqtldrr hieviavddg
       61 stdgsaewla eqarrhpqlt vlrqeasgga gkprnaglar atgdyvffld sddrlapeal
      121 fwltrtarry gsdivhgria gadgraapvd lrttsahvsv fdspvywsla ayklfrrsfl
      181 erhrlrfveg rllgedlpfg stallraevv svfaertcyy lhgrddnsna srqdtdwcey
      241 lgyigtvldg vaaavppgan rdklmvrhfh geilmpfgap ylardpagrt amaaaarplv
      301 erhltdrvra alpprlrlra hclragldde ltavvradte trpdpphldd dgrvyagypy
      361 frdprralpd acydltdrvv lrqrlirqrw aggvlhlqgt aalpwlggdt veillrrgdt
      421 thrvparsad gawraavdpa taadgaplad gvwgfkiavt ahgpggaagp avrreawlvp
      481 eddrededds gfaprivgrg pagpavaalf lsrphghlhl dldrdgvrrp lggdlhgaae
      541 ctrsgratlt arltlpgcpv daelrlilyd atrtvalrtt veraagdryt vrsllrsgpp
      601 gtwrvalrvt agtlrrelpv rtagrgaggr tpltltvpdg sparllrrar r
//
LOCUS       WP_457697047             550 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457697047
VERSION     WP_457697047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..550
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59643
     Region          19..223
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkealeplpg ptitpsaqvs ivviafndag hvgdavrsal aqgapgetvt eviavndast
       61 dgtgaaldal ahteprlrvi hrdtnsggcg tprndglraa tgrfvmflds ddvlppgaar
      121 allaaalehd apvvagacvr relpahrdvp wqpglyrepa vysspeagpq lvrdtlcvnk
      181 lyerafldkh aitfpegrft yedfvftarv laaapriati pdrvyvwhvr rsaarqsisl
      241 drkdvanwqa riaahrasvq ifqeaghkal ahaastkfld hdlrmyvrel htrgadyrge
      301 wwrltrdyla gfdeadlraa raparwlarv vlaspaprdl grltqlaarp grllppyaea
      361 ggravwspdl peveldaigt kpmhrlpvti daepavsspg vlrlrvhdly grlaaagpes
      421 idielrrrrd drrgpvhtaa ltpapaaggs eacwtaeivl dlgalvergg ryradpepwd
      481 lmaqvscadg agfraalrai gpglrrrvlp srrhvlllvq pyattggals lrvasglrsv
      541 wriaarrlrr
//
LOCUS       WP_457697049            1210 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional glycosyltransferase/CDP-glycerol:glycerophosphate
            glycerophosphotransferase [Streptomyces nigrescens].
ACCESSION   WP_457697049
VERSION     WP_457697049.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18420642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1210
                     /product="bifunctional
                     glycosyltransferase/CDP-glycerol:glycerophosphate
                     glycerophosphotransferase"
                     /EC_number="2.7.8.-"
                     /GO_function="GO:0047355 - CDP-glycerol
                     glycerophosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0019350 - teichoic acid biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=130987
     Region          2..>192
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
     Region          834..1208
                     /region_name="TagB"
                     /note="CDP-glycerol glycerophosphotransferase, TagB/SpsB
                     family [Cell wall/membrane/envelope biogenesis, Lipid
                     transport and metabolism]; COG1887"
                     /db_xref="CDD:441491"
ORIGIN      
        1 mkprltvvvp vhriegsern veeclesvaa qtlteldvvl vdgppaagre dataaesapa
       61 alarrfaard prfrivhhpg dgpapgcgav rntgarhayp htdylaflda dedvllpray
      121 edlvglldrs gsdlatgnvy rlgaagrsqs ahhpagreta lrtrigddlt llsdhvarnk
      181 vfrrtfwdrh gfafpegewc hdaavtlpaf flaeavdvlh ehvcyrrlpe gpgrhrrlda
      241 rgvrdrfaav agirrfladp ardglsghrr dydraqlteg lldlvealpg aapecrtafl
      301 dcardflsgv dprlfptlpv elrmrwylir agrladllal lthearnpag ftvagpplrk
      361 ravlplappl elppgvtrld radfpvvarv reavwrggvl vlrgyvylrn ldaaarhryl
      421 rtavlscgrr rillplrpva mpeataesgq elhcydwsgf elrldparlr rgghweegdw
      481 tvgvllasag vvragalqap dtgsgaapsa rdvadggage glritpwyag grlrlsvhrr
      541 trrlaghraa aagdldltvt apgpspaalr lthqgtgtvv sfpvetalpe eagpgepgev
      601 segahgapps ehtfrirlda laaarpardg apravppaht eswapelvlp gggtdpiaca
      661 pgltpapypl phgrelvvaa taaghlvlhd ripqayldrl mwradgtlll sgglpaaaph
      721 atelvlkhga hatelafptt hdegrfhgtl plgalpslag tlplregrwt lhlrergavg
      781 slldapvrca psvldglpas rtvrgkpltl drhrqdealv vagpalpatd rgpyrrrmlr
      841 eqhyslhrsr plrdtvlyss fggraygdsp ravheelvrr gmevehlwav rdaqtavpet
      901 aravlvgsae whgalahsrw vvtnthlprw ftrrggqrii qtwhgtplkr igadlagtlc
      961 aglahlaprp rvsrqwsvll spnahstpvl rsalgysgrl letglprtda lfapdrelta
     1021 aavrerlgie pgrkvvlyap tprddrayda ghhrlhlpld lelarqelae dhvllvrshp
     1081 lvadrlpahh apfaldvsah pdatelllaa dvlvtdyssl aadfantgrp mlfltpdlph
     1141 yrdtlrgftl dfearvpgpl lsstgelida lgdltaitaa gadayadfre tfchrddgga
     1201 agrvadlmer
//
LOCUS       WP_457697052             318 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697052
VERSION     WP_457697052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35068
     Region          51..172
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mtapiadqsa eqlprptrls evkgwffaad qllfdwflkr qqersepgdl lelgaymgks
       61 aiflgarrra gerftvcdlf dspaedvsns qemkksyatl trrafeanyl afhdelptiv
      121 qglssivgdh vdedsvrfah idashlyehv hgdilavrrl ltghgvvvmd dyraehcpgv
      181 aaatwqavan eglrpicitg tkfygtwgdp epfqealvdw ikargdiwhe vqyvndaplv
      241 rlsakgakep ahpvsrhssr garapqgpta qaptasaarp gprpplpars tlrrvaldvl
      301 ppvvtravvn arrrartr
//
LOCUS       WP_457697051             228 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697051
VERSION     WP_457697051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23877
     Region          71..167
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 mpgrtdssaa tdspdagppg sdvrtarpap aagtapsast arlpaerrrg gparllpars
       61 pfrsqlrrig ggrvleigcg tgdtladcat gsvgvdhdpq svarcrqrgl taytadtfla
      121 spharpgafd alltahvleh lddeqvedll rayvpyvrpg ggvllitaqe aghragpapv
      181 rftdfpllra faesaglrvr rtyshplprp agmllrsnvf vlvgqvpr
//
LOCUS       WP_457697054             304 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697054
VERSION     WP_457697054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 304)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..304
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32492
     Region          20..304
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mttvegvvpa grpdaaggvr arrplaariv artgggamrv flvlvalfwl mpsvglllss
       61 lrspeqiaes gwwqvfsepa qitwdnysql lsndkvmgsl lttaaitvpa tvlvvvigsl
      121 agyafawmdf pgrdgwflvv vgllvvpvqv alipvaklfg avglfettag vvlfhtafgl
      181 pfavfllrnf faeiprelle aarldgagel rlftrvvlpl ggpaiaslgi fqflwvwndm
      241 lialifadsg hppvtvalqq evrqfgnnid vlapgaflsm vvplivffaf qrqfvsgvma
      301 gavk
//
LOCUS       WP_457697055             453 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697055
VERSION     WP_457697055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..453
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47805
     Region          52..429
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdaevsrag errrgraggg grgrgrvlgt rpwlaavfll pallllgalv vypivfsvyr
       61 slfdasgdgf vgldnygamf sdegirtalr nnvvwvvvap tvstalglif avlterirwg
      121 tafklivfmp maismlaagi ifrlvydqap ergvanavwv gvhdtfadpa pfpgakprpr
      181 adlkpsggga fttgsavrag spvllplvav rpgdlrgaqr aaaarpqpgr itgtawldft
      241 rggggrpnav dggekalagl rveavrggrv vasattaadg sfalpadrae garlrlpaan
      301 faeayhgvdw lgpalvtpai igsyvwmwag famvliaagl aavprellea arvdgagewq
      361 vfrritvpll apvlvvvlvt lminvlkifd lvyiiapgss irsanvlalq lfqssfgtdv
      421 deglgsaiav fllllvlpvm yvnlrrlrke rrr
//
LOCUS       WP_457697057             464 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697057
VERSION     WP_457697057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 464)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..464
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48162
     Region          62..405
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrrrldrtag rattavaata vlalalaacg sgggsgsgsg gtkdegsggg kggstaptvq
       61 lpslkgqklq vtavwtgper enfgkvldef ekrtgatvdf vpsgddmagf igskvagggp
      121 pdiamlqqvg vlnefakkgw lkplgasaka qlaknyakgw qdlgahkgtp ygvyfkasnk
      181 slvwynaqaf ddagahepkt wpdfvkaaei iaesgvepvs vggsdgwtlt dwfeniylsq
      241 agpekydqla qhrikwtdpt vkqalttlgq lfgrkdllag gnsgalqtdf ptsvtqtfsg
      301 gdtpkaamvs sadfaaanit qtkakvgtda kvfpfpavga kspvvtggdv avalrdtksa
      361 qalltflast daakiwaqag gfispnkeld qaayadevmr eiakalvaag ddfrfdmsdq
      421 apasfggkpg qgewkdlqdf lknpkdiagt qaqlekdaaa sfgr
//
LOCUS       WP_457697059             555 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457697059
VERSION     WP_457697059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..555
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=59528
     Region          7..277
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(7,42..43,72,77,82..85,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,46,48,80,96..99,103,105,142,144,
                     146..147,149,164..165,168,185..188)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,46,48,80,96..99,103,144,146..147,
                     149,164..165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(18,103,105,142,144,146,168,185..188)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(164..172,181..188)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mrpvgskyll eeplgrgatg tvwrarqret agaeaavage pgetvaikvl keelahdadv
       61 vmrflrersv llrlthpniv rtrdlvvegd llalvmdlvd gpdlhrylrd sgpfspvaaa
      121 lltaqiadal aashadgvvh rdlkpanvll agsdgsgemh pmltdfgiar ladspgltrt
      181 hefvgtpayv apesaegrpq tsavdiygag illyelvtgr ppfagstale vlhrhlseep
      241 qrpgtlpepl wtvierclrk rpeerpsaes laralrtvaa gigvharpae aeaalgvaal
      301 lapdpapatv pgtgadggqa tggdadptqv lpsgagsydp aaatsvlpst ggpggpagqg
      361 dptramppmp mgapaggpqg pdgphpwesq mraardrneq tqvqyldpse dplrrrpqrq
      421 aapqqppqrp qqpqyrqqpa pvpyaqqqpp qqqrqpqapq rrqepppqry epqrppapep
      481 rprreprqrs anpmkipglg clkgclftli llfvaawliw eltplqewig ttrgffaqlg
      541 eifqsvqnfv qklgr
//
LOCUS       WP_457697061             436 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457697061
VERSION     WP_457697061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..436
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=45446
     Region          8..281
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32,60,65,70..73,85)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,34,36,68,84..87,91,93,130,132,
                     134..135,137,155..156,159,189..192)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,34,36,68,84..87,91,132,134..135,
                     137,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,91,93,130,132,134,159,189..192)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(155..163,185..192)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 markigsryt ahqilgrgsa gtvwlgegpe gavaikllre elasdqelvg rfvqeraall
       61 gldhphvvgv rdlvvdgndl alvmelvrgt dlrtrlerer rlapeaavai aadvadglaa
      121 ahaarivhrd vkpenvllnm qgplgpggah palltdfgia rlvdsprrtl pqtpsggtpt
      181 slrstkvigt pdylapeiie glpprasvdv yalatvlyel lagftpfggg hpgavlrrhv
      241 tesvaplpgi pdelwqlllq clakapasrl rapelaarlr ellpglagip pldidepddd
      301 epegeqeaaa gsreeafyps aapaeatppr gavplvqgav pdsnrethts mrvpgpdela
      361 ggahgtarap raagerrags arhraspeav rrrriklgaa aaaalvaagl ggwlasgdde
      421 pgdatpgvhq pepdtp
//
LOCUS       WP_457697070             405 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457697070
VERSION     WP_457697070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41622
     Region          68..386
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 msgpcsydrp rrirrgaalt lflasvlatg vvtgtwsdaa egavgrtapd rmssgahtre
       61 sladraaver aaseavedgk sgaqaaaevv srsgdrwsti ytpgeyedfq eqlgggyvgv
      121 glwvrqasgg rivvsrvqpg gpaeragiav gdrlraidgq ttrdapvtdv varlrgnapg
      181 gsrgpaaaag tavtldlqrg drrwtetlhr trvkarnvvv drpagdhgpt rvkiaaftkg
      241 tgdavrravr qaspddgmll dlrgntgglv teavatasaf ldgglvatyd vrgsqrvlya
      301 erggnthvpl vvlvdggtms aaellagalq drgravvvgs ptfgkgavqm pselpdgsva
      361 eltvghyrtp sgrtvddtgl tpdlvvgnga ekrartvlsg lgggs
//
LOCUS       WP_457697074             324 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697074
VERSION     WP_457697074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35134
     Region          5..299
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mpydidprll raftavaeel hftraaarly vaqqalsrdi rrlerelgat lfvrstrrva
       61 ltadgerllp yaqrvlaaqd elaaafraap erpllvdvsv pigtahavle aardrvpdsc
      121 elvarfhsgl tgaaaemaag rldvsfgria alpadiragl dhqpvrlepm avllrddhpl
      181 aarpavplae lagetlyaaa gnpqtvewtd laerlfagrg iataepfpei egsqefirvv
      241 rkrgwsvlas vefmdvpgmv lrplvdpvpl spvslvwrrg lrhagldalr aaareqaerh
      301 awlappgsaw wlpeadaram gvhg
//
LOCUS       WP_457697080             275 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697080
VERSION     WP_457697080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30529
     Region          18..75
                     /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          93..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mqprkkprnr hsaameviga qlamfrinag ltqralgert taseetiasi eqgrralmph
       61 latefdqllr tggalatgve klppkdkypi waeefigyeq qalalswyey gvlpgllqte
      121 dyaratfrsk iplldeetve rrvagrlerq qilhrakpvi asfviseaiv asnlggrevm
      181 raqishlrsc adlngvsvqi lplsrehhag ldgqfvvlet adhqhlayte aqrsselisd
      241 pdevsilaqk ygmlrmqaln aeetvglldr llger
//
LOCUS       WP_457697082             482 aa            linear   BCT 27-JAN-2026
DEFINITION  nitrate/nitrite transporter [Streptomyces nigrescens].
ACCESSION   WP_457697082
VERSION     WP_457697082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Fukuda,M., Takeda,H., Kato,H.E., Doki,S., Ito,K., Maturana,A.D.,
            Ishitani,R. and Nureki,O.
  TITLE     Structural basis for dynamic mechanism of nitrate/nitrite antiport
            by NarK
  JOURNAL   Nat Commun 6, 7097 (2015)
   PUBMED   25959928
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Yan,H., Huang,W., Yan,C., Gong,X., Jiang,S., Zhao,Y., Wang,J. and
            Shi,Y.
  TITLE     Structure and mechanism of a nitrate transporter
  JOURNAL   Cell Rep 3 (3), 716-723 (2013)
   PUBMED   23523348
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..482
                     /product="nitrate/nitrite transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50560
     Region          56..450
                     /region_name="MFS_NRT2_like"
                     /note="Plant Nitrate transporter NRT2 family and Bacterial
                     Nitrate/Nitrite transporters of the Major Facilitator
                     Superfamily; cd17341"
                     /db_xref="CDD:340899"
     Site            order(66..67,70..71,74,106,160..161,163..165,168,187,
                     190..191,194,264,267..268,271..273,276,304,308,360..361,
                     365,369,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mtaaaaetrs espdetpagr rgesrprrgg rwiehwdped egfwresger varrnlvfsv
       61 lsehigfsiw tlwsvmvlfm gpeygidpas kfflvamptv vgavlrvpyt favarfggrn
      121 wtvisaamll vptaaaavvm epgtsyttfl lvaalagvgg gnfassmtni nsfyplrkkg
      181 walglnaggg nigvpviqll gllvigtaga thprivlavy vplivvaavc aalfmdnlap
      241 vtndtgaald aarephtwvm sllyigtfgs figysfafgl vlqnqfartp lqaasltfig
      301 pllgslirpv ggrladrfgg aritlgnfga mglatgvviy asaerslpvf lvgfialfvl
      361 tglgngstyk mipgifqaqa lrrglageea aaygrrlsga amgligavga lgglainlaf
      421 rqsflvagsg tpafvsflgc yvvcgavtwt vylrpaarar rtaqaaeaap adegrrpvya
      481 ev
//
LOCUS       WP_457697084             258 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697084
VERSION     WP_457697084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  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 258)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29432
     Region          98..199
                     /region_name="Methyltransf_12"
                     /note="Methyltransferase domain; pfam08242"
                     /db_xref="CDD:400515"
     Site            order(100..106,124..125,153..155,171)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 msrkslltnr aslthklgya lrhpdritpy vkrtardtwl rlkhpghvay yravmasdag
       61 rnpeaavgsr sherwlalge mqfdylaehg lkpghrmldi gcgnlragwr fiayldagny
      121 ygidispdil isakqtltty elqdklphlt itqdlkldfl psahfdvvha hsvfshspld
      181 videclahvg rilapggffd ftfdrtegae hqvlredfyy rtetllqlar khglearfmd
      241 dwetrkhgqs kirvnnpq
//
LOCUS       WP_457697086             213 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697086
VERSION     WP_457697086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22605
     Region          2..177
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 maapcelrfd cgricldlaa tadgaaaerl tgpdqlrawl tgaglvphgt pldgvdgrwv
       61 grfrglrell lrvvhdelrg gaaeadltll nsaaaagqpp apcavrapdg tlaralprpp
      121 ecagllaava rdaivlltda aaraqlrqce gesctlvyld tsrgrrrrwc ssevcgnrer
      181 varhrrrttv rrkqsggava dpvtraenfs pgr
//
LOCUS       WP_457697088             246 aa            linear   BCT 27-JAN-2026
DEFINITION  anti-sigma factor family protein [Streptomyces nigrescens].
ACCESSION   WP_457697088
VERSION     WP_457697088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Devkota,S.R., Kwon,E., Ha,S.C., Chang,H.W. and Kim,D.Y.
  TITLE     Structural insights into the regulation of Bacillus subtilis SigW
            activity by anti-sigma RsiW
  JOURNAL   PLoS One 12 (3), e0174284 (2017)
   PUBMED   28319136
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="anti-sigma factor family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25645
     Region          5..>109
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mipptqpdrh sdvgayalgv ldaadaerfe ahlvgcdrca aeleelmalt pvlaefhqsa
       61 ptpqtitavp gprvldglld evhatrrgrs rrrlflvaaa vvlivggpla tfslkgegdk
      121 apapplanav raqyaagekv tstdpdtkvs agvsmaartw gtqvvlelan vkgplscdlv
      181 avgkdgkrqt vttwavpkgg ygipgsaaqw nreplyaagg aalnrgdidh feintldgkr
      241 latvka
//
LOCUS       WP_457697089             876 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces nigrescens].
ACCESSION   WP_457697089
VERSION     WP_457697089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 876)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 876)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..876
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=93411
     Region          16..861
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 maahnathap dhasdsvrdr eieaeqthld rvyrrleeki heaeflmdda akrgqvgtpg
       61 alaerdaqvf qagvhlhrln seyedflfgr idlllgkdgk kgpdgaftsv epadgaiedg
      121 ratiaetlhi grlgvldady splvidwrap aaapfyratp vapgrvvrrr virskgrkvl
      181 gveddlmrpe vtatldgqel paigdgalma algrarshtm rdivasiqae qdkvirapaa
      241 svteveggpg tgktavalhr aayllyqdrr ryaggilivs ptpllvayte gvlpslgeeg
      301 qvairalgsl vdgaeassgg gpegldegrr sgdggaydpp avarikgssr mqkllrkaar
      361 galelaaaps aphtgreaat aaangggapd ggaqlsledl fgaagvdtgr daaangsrrr
      421 rtraprpgpt ppaagpptql rvvafggrie lgadelrair qsalggtapv nllrprarrl
      481 ildalwtksg aarrytdpel aaearegfde dittepdfqe fldawwpelt prgvlaamad
      541 erllgrwarr llnprevrql arslqrldgs ghgplsvhdv alldelqmvl gapmrparpr
      601 eadpldhltg leeltthadr mgggrsrrer leeertdyah vivdeaqdlt pmqwrmvgrr
      661 grhatwtvvg dpaqsswsdp deaavardea lgtrprrrft ltvnyrnpae iaelaarvla
      721 lampgmaspk avrstglepr falvadgngn gngngngqar sgddaalaqa taaeaerllg
      781 evdgtvgvvv amnrraqarr wlaplgdrvv algsleakgl eydatlvvsp aeiadespag
      841 lrvlyvaltr atqqltvlsa erdepdaagv pdllrd
//
LOCUS       WP_457697093             417 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697093
VERSION     WP_457697093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..417
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44329
     Region          47..384
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msitprrmar rtaavlsaal lttllpagta gtaaaaadrt srlqrdadal rdagvtgvsa
       61 rlatphglrt vrsgvgdlrt grpvpadgyl rigsttktfv atvllqlage grlslsdtvd
      121 twlpgvvrgq gndgrritlr qllrhtsglp dyikdvvpep gaagyrhhrw taytpeqrva
      181 lalrhrpafp pgarweysnt nyvlagmvik avtghsweqe vrdrilrplr lahtltpgnr
      241 pflpgpharn yqqfepdgpm tdttiaylpf dgdadgsmvs taadtgrffs alvqgkllap
      301 aqlaemqrtv dvpddhgapq gtraglglvw tplscgggyw ghggtgfgyv vwpavtpdgr
      361 ttltvsahsr pgdndtavrq irgvteladh alcaaqdgrd gpwggrgpgr ppvrpag
//
LOCUS       WP_457697103             298 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697103
VERSION     WP_457697103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30106
     Region          15..298
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mtthaphash tvtlpaslde avaaltampa avpvaggtdl maavnagllr paalvglgri
       61 seirgwqyld ghallgaglt larmgrpdfa alipglaaaa raagppqvrn agtlggnivt
      121 saptgdtlpv laaleatvii agpegsrrei pvshllagre mlspgelvgf vrvpllhapq
      181 tflkatgrtg pgratasval vldparrgvr cavgavaamp lrpleaeqwv aslidwdger
      241 glvpealtaf gdyvaaacip dpappedgse patlppaalh lrrtvaalar ralgrals
//
LOCUS       WP_457697101             577 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces nigrescens].
ACCESSION   WP_457697101
VERSION     WP_457697101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..577
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63023
     Region          15..556
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mpetdttpta pggglvpapl sidgpyrsav rlgedtalaa gpgtedtarw lratlgaafg
       61 lplppgsgkt tdtlalvldp dlppegyrla adarwgvrit ggspagvfwg aqtlrqllgp
      121 hafrraplap ecaavlpqqt iedgprfawr gmlldvarhf lpkdgvlrcl dllaahklnv
      181 lhlhltddqg wrieirrypk ltevgawrer tklghraspl wderphggyy tqddireiva
      241 yaaqrhitvv peidipghsq aaiaaypelg ntdvidttsl kvwdtwgvnp nvlaptdntl
      301 rfyehvleev lglfpspfvh iggdecpkdq wrasataqar iaelslaged elqswfirhf
      361 drwlaargrr ligwdeileg glaegsrpsp atalpdappd svrgdphsaa pfavsswrgy
      421 aggiaaaksg hdvvmcpeqq vyldhrqhps pdepvpigfv rtledvyrfe pvppeltade
      481 aahvlgtqan awteamdsqq rldyqvfprl aafaevawsr lpapadrdyq dftrrmaahy
      541 trldalgvgy rppggplpwq krpgvlgrpi dgappnv
//
LOCUS       WP_457697106             776 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces nigrescens].
ACCESSION   WP_457697106
VERSION     WP_457697106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..776
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80760
     Region          29..733
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msgtsdgaga vtatpaagvq ipaepplhgl gvslppadap aktegtfpya adlwaegllw
       61 aavlrsphpr arilsidtkh avempgvrvv vthedvpgda ghgrgtadrp vfakdevrhh
      121 gepiaavaae hpdtarlaaa aiaveyevld avtdpqlafe aeplhpdgnl irhiplrfgd
      181 aeamgevmve glyrigrqdp apigaeagla vprpdggvei ytastdphtd rdlaaasfgl
      241 epeqvkvvvt gvpgatadre dpgiqlslgl lalrtgcpvk laatreesfl shahrhptll
      301 ryrhhadadg klvkveaqil mdagayadts adalaaavsf scgpyvvpha ivdgwavrtn
      361 nppsghvrge gamqvcaaye gqmdklaarl glepdeirlr nvmatgdllp tgqtvtcpap
      421 vaellhavke aplpelpkda peaewllpgg pegagepgav rrgvgyglgm vhmlgaegtd
      481 evstatvkvs gsvatvicaa vetgsgfstl arqivqetlg veevhvagvd tdqppagpac
      541 hgrhtwvsgg averaakmvr tqllqplahk fgmstellqi ndgkitsydg vlsttvaeal
      601 dgkelwataq crphptepld eggqgdafvg lafcaircva dvdielgtir vvemtvaqdv
      661 grvlnprqlr arieagvtqg mgaalmenlr ttrgqvrhpd ltgyalptal dapeirivkl
      721 veerdvvapf gakpasavpv vtapaavasa vraatgrpig rlpirpqaav aqvvtq
//
LOCUS       WP_457697111             509 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697111
VERSION     WP_457697111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 509)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   3  (residues 1 to 509)
  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 509)
  AUTHORS   ter Beek,J., 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 509)
  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   6  (residues 1 to 509)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   7  (residues 1 to 509)
  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   8  (residues 1 to 509)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   9  (residues 1 to 509)
  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   10 (residues 1 to 509)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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   11 (residues 1 to 509)
  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 10002138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54521
     Region          90..488
                     /region_name="LivK"
                     /note="ABC-type branched-chain amino acid transport
                     system, periplasmic component [Amino acid transport and
                     metabolism]; COG0683"
                     /db_xref="CDD:440447"
ORIGIN      
        1 msarifeppr pprrwglwii svlvaaavvv aavvqivetn grcgegvrev aggecvgvtd
       61 gayafgnmks lsdriraend kvaksgersv avayleamag gsadrgpeat rqavsgayla
      121 qralnaerst lpkirlllan tgrgdrhwrq vvdqliamkd kerlvavagf gqsndrtmra
      181 vqrlraaglp mvgatvaadg lssrtagfyr vsfpnrdqtv aaagylkeqq rkhpgyrvqv
      241 irdgnekdny ntslyedfsa aarragldvd devipfrsge deeatagnal slvadkvcgd
      301 pkppdavyfa grgrelrrli eaageggrhc rttvlsgssa lgvyfdtggd rhraelatla
      361 erwkdsqltv yytafthpai skevyggagn gpftdferay gkevggpttd lasgqamlgh
      421 datytigkaa rnavgvygtr qvtarmvlam leqtngrsrv rgisgyiafd pdtgepvdrp
      481 lalvelrrpt dtgeagdiyr fvaglsagr
//
LOCUS       WP_457697123             149 aa            linear   BCT 27-JAN-2026
DEFINITION  PTS sugar transporter subunit IIA [Streptomyces nigrescens].
ACCESSION   WP_457697123
VERSION     WP_457697123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Peterkofsky,A., Wang,G., Garrett,D.S., Lee,B.R., Seok,Y.J. and
            Clore,G.M.
  TITLE     Three-dimensional structures of protein-protein complexes in the E.
            coli PTS
  JOURNAL   J Mol Microbiol Biotechnol 3 (3), 347-354 (2001)
   PUBMED   11361064
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Robillard,G.T. and Broos,J.
  TITLE     Structure/function studies on the bacterial carbohydrate
            transporters, enzymes II, of the phosphoenolpyruvate-dependent
            phosphotransferase system
  JOURNAL   Biochim Biophys Acta 1422 (2), 73-104 (1999)
   PUBMED   10393270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="PTS sugar transporter subunit IIA"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=15155
     Region          1..149
                     /region_name="NagE"
                     /note="Phosphotransferase system IIA component
                     [Carbohydrate transport and metabolism]; COG2190"
                     /db_xref="CDD:441793"
ORIGIN      
        1 mttvtsplag raiglaavpd pvfsgamvgp gtaidpvrep saavspvdgv lvslhphafv
       61 vvdseghgvl thlgidtvql ngegfellvn kgdtvtrgqe vvrwnpaave qagkspvcpv
      121 valeatadsl gdvredgdvk agdqlfswq
//
LOCUS       WP_457697139             205 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697139
VERSION     WP_457697139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..205
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=22528
     Region          17..192
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mafgrsdrrr rsaavepvtl kilvaggfgv gkttlvgavs eikplrteer lteagrpvdd
       61 ldgveakttt tvamdfgrit vheelvlylf gtpgqdrfwf lwdelargal gavvladtrr
      121 ladsfaaidy ferrglpftv avncfdgadr yppqavrdal dldpqvpvml cdarlkdsar
      181 dvlisvveha mrtgeknrrr epalp
//
LOCUS       WP_457697131             801 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 31 protein [Streptomyces nigrescens].
ACCESSION   WP_457697131
VERSION     WP_457697131.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 801)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..801
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=86636
     Region          174..301
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            212
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          301..639
                     /region_name="GH31_glucosidase_II_MalA"
                     /note="Alpha-glucosidase II-like; cd06604"
                     /db_xref="CDD:269890"
     Site            order(318,346..347,383,420,454,456..457,519,532,535,537,
                     568,593)
                     /site_type="active"
                     /db_xref="CDD:269890"
ORIGIN      
        1 mdgrdlvrsv rmvravgpaq glrsvrsawr awradaralp rrgaerarvp gpalraepqp
       61 ggglihfars slrvrvaagg avfcgwdgae pepsyalaga cpevdaravl epdteggwrv
      121 vservlvvvs rhgavevrtp ggavlrrelp prwwdrtgdg gadahngrpe gcgvsrwvqr
      181 sevaadgrff glggrahgpr lrdgayrlwn tdpggafapg ddplsltmpv qlvvadagth
      241 lvfhdnswdg rvtlregaeg agsghdrpgt celrmdggpl rywvlagspa rvlqvwtalt
      301 gapalppqwa lgyqharwgf ggedevrrvl agykerqlpl savhldidhy drhrvftvdr
      361 qrypdlpgla relrtdgvrl vsivdpavka epgdvvyegg aaadafvrda rgrevrgvvw
      421 pgesvypdft darvrkwwga lyaerlaqgf sgvwhdmnep ssfaafgert lprsarhale
      481 grggdhreah niyglamara gfeglcelrp aerpflfsrs gwagmqrygg swsgdvatgw
      541 pglraslslv lglglcgvpy sgpdiggfsg apcpelylrw fqlgaymplf rthsargagr
      601 repweygsev lahartalhe rqrllpyfgt lgqlarltga pyvrplwwsa prdralrdce
      661 dafllgdall vapalaagvt rrpvrlprgr wydtatgray dgpgqvwvea plsripvlar
      721 agavlpvaga dggtelevwa pvagrggsgl vvpdagdgwq rptverftsr rsggrvvver
      781 rdggavgypv rvrglddgae g
//
LOCUS       WP_457697135             255 aa            linear   BCT 27-JAN-2026
DEFINITION  MIP/aquaporin family protein [Streptomyces nigrescens].
ACCESSION   WP_457697135
VERSION     WP_457697135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25664
     Region          3..255
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mysngdivvg evigtailil fgagvcaavt lhhskakgag wvviafgwgm avlagaytaa
       61 plsgghlnpa vtlgsavagg tewskvplyi laqmagavig avlawalyya qfaanaeqsk
      121 tqptlgifst apeirkpaan lvteiiatig lvlpllcfgq nkgigigqvp geqagiygsg
      181 invllvallv vgiglslggp tgyainpard lgprlvhall pipnkgssdw syswipvagp
      241 ligavlsglv ynaaf
//
LOCUS       WP_457697140             203 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697140
VERSION     WP_457697140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22349
     Region          11..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msgkrttrlt pdqrreqlvg iglemladrs ldelstdeva rragisrgll fhyfdskrdf
       61 yravvraacd rftaatepdg tlepvawmra fiagfvayvl ehrqvylalv rgaagshpav
      121 tdivgatret larrvgdgqr rlgmpdaprl elasrawmaf aeeavinwpa eepgaqdelc
      181 afiessfvsm lglldrpgvl tpr
//
LOCUS       WP_457697152             268 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697152
VERSION     WP_457697152.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28122
     Region          18..268
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msktsetadd rseerrggag svqsvdravs vleilaklge agvteiseel gvhkstafri
       61 lgvlenrglv eqekdrgkyy lgagvlrlag aaairldisq egqpvcrala edtgetania
      121 vldgdaavni mqargsaavt aynwlgrrtp lhatasgkvl lahlpaprre tlvtrklprf
      181 tertlttaag lreqltaale dgfactseel eiglnavaap vrahdgavig aigvsgpayr
      241 merqllpela eraakaaadl srlmgyag
//
LOCUS       WP_457697166             260 aa            linear   BCT 27-JAN-2026
DEFINITION  LamB/YcsF family protein [Streptomyces nigrescens].
ACCESSION   WP_457697166
VERSION     WP_457697166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Oke,M., Oni,O., Bello,R., Samuel-Omoyajowo,K. and Senbadejo,T.
  TITLE     Structure-function relationships of the 5-oxoprolinase subunit A:
            Guiding biological sciences students down the path less traveled
  JOURNAL   Biochem Mol Biol Educ 47 (6), 620-631 (2019)
   PUBMED   31520514
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="LamB/YcsF family protein"
                     /EC_number="3.5.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0017168 - 5-oxoprolinase
                     (ATP-hydrolyzing) activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27274
     Region          12..259
                     /region_name="PxpA"
                     /note="5-oxoprolinase subunit A [Amino acid transport and
                     metabolism]; COG1540"
                     /db_xref="CDD:441149"
ORIGIN      
        1 mserspvppp vidlnadlge gfgrwqltdd eallsvvtsa nvacgfhagd patmrrvcel
       61 aaergvviga qvsyrdlagf grramdvppd elaaeiayqi galevfaraa garvgyvkph
      121 galynrcvhd aeqagavidg irtaggglpv lglpgsrlhe aarearlpvv geafadrayt
      181 pegtlvprre pgavihdpde vvkralgmar dhavtardgr rvgisarslc lhgdtpgaad
      241 larrvrselt aagvhvrsfv
//
LOCUS       WP_457697170             287 aa            linear   BCT 27-JAN-2026
DEFINITION  5-oxoprolinase subunit C family protein [Streptomyces nigrescens].
ACCESSION   WP_457697170
VERSION     WP_457697170.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Niehaus,T.D., Elbadawi-Sidhu,M., de Crecy-Lagard,V., Fiehn,O. and
            Hanson,A.D.
  TITLE     Discovery of a widespread prokaryotic 5-oxoprolinase that was
            hiding in plain sight
  JOURNAL   J Biol Chem 292 (39), 16360-16367 (2017)
   PUBMED   28830929
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="5-oxoprolinase subunit C family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29249
     Region          5..283
                     /region_name="PxpC"
                     /note="5-oxoprolinase subunit C/Allophanate hydrolase
                     subunit 2 [Amino acid transport and metabolism]; COG1984"
                     /db_xref="CDD:441587"
ORIGIN      
        1 mtdrafsvvr agalttvqdl grpghahlgv pragaldapa hrlanrlvgn pgsaatlett
       61 ltgcalrvrt attvavtgap cpvtvdgrpa pwgapvrvpa gavvdagpat hglrsylafa
      121 ggidtepvld sraadllsgl gpdpltdgav lplgdphgpp agadavphrg plpelllpfl
      181 pgprdawftd aglhtlttgr frvspasnri glrtegpple rartgelpse gmplgalqvp
      241 pnglpvlflh dhpttggypv igvvpercla paaqavpgtp vrflrmr
//
LOCUS       WP_457697175             375 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457697175
VERSION     WP_457697175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 375)
  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 375)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133585
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..375
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39768
     Region          2..364
                     /region_name="GT4-like"
                     /note="glycosyltransferase family 4 proteins; cd03814"
                     /db_xref="CDD:340842"
ORIGIN      
        1 mrvvlvtesf ppdvngvshc alqtarhlvr rghdplviap lggasadtgt despcpvvrv
       61 psmplpgypq vrialpgrrl saaldghrpd lvhlaspfvl gargmaaaar rqvpaiavyq
      121 tdlgryarty lgggaatawr riravhaaad rtlapssaal ldltehgvpr vhlwprgvds
      181 erfhpgrrda vlrssltagr ellvgyvgrl apekdvrlla etsrlpgvrt vvigegpsaa
      241 glrtalpevr flgrrtgdel arlyasldif vhtgpyetfc qtvqeamasg vpvvapragg
      301 pldlvdhgrt gllvtpgdgg afrdavrfla dsaevrerfg aaarravadr tweavgdqll
      361 ghyeavlsdr tavaa
//
LOCUS       WP_457697177             472 aa            linear   BCT 27-JAN-2026
DEFINITION  HEAT repeat domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697177
VERSION     WP_457697177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51009
     Region          <236..315
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mfdpdiapsg tllgllqrgr gdgtlhalaa praealaaln dsvlrdprrd wqvenrslyy
       61 arlymqldgg leqierhlfh pddlvdtgee rtglalavlg hlaaygrdaa rlllrsyaaa
      121 gsnwrwalde lalrdddagl mtlapavlar fpeteegeae laaairdafe prpwrlwted
      181 prygarlaaa geqgsfdrwq rqlqprgprp gwsvtevlew aqqglelepa eqrhhaaarc
      241 lgavagpedr pellraahsa pdaaraavih hlaergdpgt ldlieaavad pfsseqlvsa
      301 alaaftrmrs vaaverarlw asrtdrlgaa aagvlarrgg rrdaelvlaa lrstvreegp
      361 daeglwelvd gtgrlgvgca apvlrhiyre tssshlrgra agalaatdpg faagfavecl
      421 wdceettrel aarhaatgdd rvveqlrrla adpaeedevq tavrsrigpe gs
//
LOCUS       WP_457697179             488 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457697179
VERSION     WP_457697179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..488
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=52295
     Region          47..486
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpsplfadhs adrpperetv ealitqarrl rggldavrre stvdtdlvad pqlrwqralc
       61 dlavhhlddl gghldqlreg lpaesadapa peaelppapp epephergal lrrvgsaewn
      121 lltdevswsd elfamfgrap sdgpltldel pslvhtedqd glatmvtdcl vdsrpidgef
      181 rivrpdeslr tvhmvgepvl dadgstacmw avlrdvselr rsqqavretr dslhrerqia
      241 qtehrlavel qeavlppwrg slrfphggpv aldlagrylp sgtrdliggd wydalqlpdg
      301 stllsvgdlt ghgvtatsgm amvlgalrgm avaghrpgpl mgflnqllds aaqpalgsav
      361 cgrfdpaart lewaqaghpa pllfrggtgr aldppegvll gatsgasytq hteqlepgdl
      421 lvlhtdglvp rraqgadaah egaerllala prfaatrsaq dsvrivveef gtaereddac
      481 vliarvgg
//
LOCUS       WP_457697183             377 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697183
VERSION     WP_457697183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  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 377)
  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..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /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=40730
     Region          91..306
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 myaassavtv ptrphrphpt gggpyldpsp sagavtglpg grtrrvqgtg aqplsgrldl
       61 sgpqgaqlra avasvhricp efnpvqvlrr sgrsvllvgt tgrmtavakc lldqspawae
      121 rfrqeisayr afvrhrppvr vprlvaadpd nctlimermp grvaaltrhp seappradvr
      181 aalgaicrin lwrppsglfd tpldyagrig ryhdlglltd rdlgdlqklm hglshtqgqf
      241 chgnallnnv llspagpvll dwddagwylp gydlatlwsv lgdapvarrh isqlaqnagp
      301 asrdaflvnl mlvltreirr yetavqrtmr eptptgtpgp gqpgvpaage eqrlllrrlh
      361 ddcqmarrav raavgtr
//
LOCUS       WP_457697185             668 aa            linear   BCT 27-JAN-2026
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces nigrescens].
ACCESSION   WP_457697185
VERSION     WP_457697185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..668
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..668
                     /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=71501
     Region          291..447
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mqgsapedek rvprpalrrs atavaaavll lplsgapsaq agqprtdalq qafteaaarf
       61 hvprsvllgv sylesrwddh ggapsvsggy gpmhltdart altrtpefse gdedargdeg
      121 rarkrvpaga aqraalptel parlrtlpta akltgipaek lrsdpaanvl ggaallaaeq
      181 rklgtpagsd parwytavar yggqdsarsg kafadevyav mrqgqarttd agqrvalaaa
      241 pglapdaaqq krlstpaaka stapaarkpe cpwnvacesv papyeefgda dygnhdkadr
      301 padqrvstiv ihdtegswet tlklikdpay vswnytirss dgliaqhvpt kdvawhagnw
      361 yinshsvgie hegflaapda wyteamyras arlvkylsrk ydvpldrqhi lghdnvpgtt
      421 tatipgmhtd pgpywdwahy ftllgkpfka tagprgglvt irpdydenqp aytgcakagd
      481 tcaphgstav rlysapdeda plvkdvglhp dgsasttgvn dtgarattgq rfavagrsgd
      541 wtaiwylgqk awfhnphdep vavpakglia vpksgrdeip vygraypeke aypagvpyqa
      601 vsplpyklaa gqkyavgdrm tgdyfyaptf dlskhaivrg kdvyyeiqlg hrvgyvraad
      661 vevrrsgs
//
LOCUS       WP_457697189             202 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697189
VERSION     WP_457697189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..202
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21674
     Region          5..187
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mtatrlaldl avtirhdghg gvaddlagpd rladwvrera alldcaeqpv tvdealhtav
       61 rdlraalrsl faravrpgpp ssadahrllp eaeaidrlna aaalvptvpr lswksdagpt
      121 lrlqpagspp aadrivaala raalafldgp drallracpa prcvryfvkd harqewctps
      181 cgnrarvarh herrreargd ap
//
LOCUS       WP_457697201             318 aa            linear   BCT 27-JAN-2026
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697201
VERSION     WP_457697201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34447
     Region          26..127
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
     Region          186..295
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mpevltaplv vefpftrslg pvqsafltgl rertvlgvta sdgrvvvppt eydpvtaeei
       61 relvevgshg tvttwawnps prrgqplatp fawvlvrldg adtallhald apgpdavrtg
      121 mrvrvrwaaq rtgaitdiac fepddspagd sepaphsgef adavtgittp arldytyspg
      181 raqsryiqal sdhktigerc pscrkvyvpp rgacptcgva tdtqvevgpr gtvttfcivn
      241 ikarhsanld ievpyvyahi aldgadlalh ariggipydr vrmglrvepv wtehgrfpdh
      301 yrptgepdad ydsykeli
//
LOCUS       WP_457697219             247 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697219
VERSION     WP_457697219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26783
     Region          22..243
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maggvakndq grltevsgle rdrpllgrss taervadilr dritegyfpp garlseesig
       61 galgvsrntl reafrllthe rllvhelnrg vfvrvvtved lediyrvrtl vecaavrglg
      121 qgpygagate aiavieaavq ageaasadre wqalstanir fhqgivalag sprtdelmrg
      181 vlaelrlvfh vmadprrfha pyltrnrqiv ealqagdaae aerlllsyle dsrsqlsgay
      241 aqriaeg
//
LOCUS       WP_457697221             310 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697221
VERSION     WP_457697221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=31450
     Region          17..204
                     /region_name="SGNH_hydrolase_like_1"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01832"
                     /db_xref="CDD:238870"
     Site            order(23,185,188)
                     /site_type="active"
                     /db_xref="CDD:238870"
     Site            order(23,185,188)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238870"
     Site            order(23,64,93)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238870"
ORIGIN      
        1 mvipapgggr saapdcfval gdslteglgd pvpgggwrgw aallaealge rpgsvplvnl
       61 aqsgalaadv aerqlpaara lgprfasllv gandtlraaf aiervaaald rahgalsadg
      121 avvltaclpd pgrmlglpap larplgrrmr avntvvhavs aryegvhlhl adhpwvadrt
      181 swsvdrlhps erghrllarg fhtaltavgl pagpppaltl dgppptrags alwmatrgtr
      241 wvadrctdll pgllglalqe crhglagsgr lldaaadrat rsalaalgrt dgvgggkdps
      301 makgaatmag
//
LOCUS       WP_457697226             292 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697226
VERSION     WP_457697226.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=31932
     Region          35..236
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtttsltpqg aaqracivwg lsargisplr thatsvyllp hadavvrvsr veqrasiqra
       61 ialtrwlagq glevtepldv sqpldvhgyv itvwrhypqp egpppgperl gnllsqlhrl
      121 peppielpay rphlalravv gssttlapsd rewilgrsde lldsyahldf plsqglvhgd
      181 aypgntlwdg saarlgdwde aaigpreadl antfqgvrfg rtaaqlrafs daygydlagw
      241 pglsvltelr dlhtlgsfir ranrgdleaa sqlafrldtl krddhttswv ih
//
LOCUS       WP_457697267             258 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697267
VERSION     WP_457697267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28422
     Region          10..149
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 merrdvqghy erlaaeydeh wvygphhitw msariaetlr lssadriadi gcgtgmfare
       61 varivnpeha ilcvdpsvam lgqigtpppa gltpivasae diaagrsqlp ygqldaiwlk
      121 esvhhvadpa atlyglaarl apggrllvim lptsieyplf qaaldhfael qpdpalivgh
      181 lreaglqthl rhveyelrld rekyvgmvra rymsmlstft dseiekgide mraahpepvl
      241 afpdcfafll gvkpeegr
//
LOCUS       WP_457697272             597 aa            linear   BCT 27-JAN-2026
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457697272
VERSION     WP_457697272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..597
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62761
     Region          169..565
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mqsprtttps tttgtdllly llialaglgv gggslawlfg nlanavadtd pwaayqptta
       61 llqpeqvwph laqptvitgc yvlpslvlla aavlaakvwl rfrhnpsgla aarelapllp
      121 kqvaakaidl rpslkgskpe dvapedrgvl lgtlkpgrte vrsswedvil aimaprsgkt
      181 sclaipailh apgpvvltsn kaardaytat ldaraqlgtv wtldpqqiah aprtmwwdil
      241 adardlagar rlaghfvtas vdessagdfw staaantlta lflaaaqdgr pitdvlawla
      301 spadrtpidl lqdagldava aqlqgtvaga vetrdgifet arqyasclld ptiaawvtpp
      361 nafekvrkfk pkdfatskdt lfllskdggg sasaiiaaaa davmraaviq aerdggrlda
      421 pllaildeaa nvckisdlpd lyshlgsrgv ipmtilqsyq qgvrvwgqag mdalfsaati
      481 kligsgidda dfadklsrla gdhdvrtvsv stsesgksts vsmrqervlp pdairalpkg
      541 tayllatgir ptlldlkpwy kepdadqlsa asakataait dralakplhq ddfgpaa
//
LOCUS       WP_457697278             154 aa            linear   BCT 27-JAN-2026
DEFINITION  restriction endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457697278
VERSION     WP_457697278.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 154)
  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 154)
  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 154)
  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
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Identification of a PD-(D/E)XK-like domain with a novel
            configuration of the endonuclease active site in the
            methyl-directed restriction enzyme Mrr and its homologs
  JOURNAL   Gene 267 (2), 183-191 (2001)
   PUBMED   11313145
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Bujnicki,J.M.
  TITLE     Phylogeny of the restriction endonuclease-like superfamily inferred
            from comparison of protein structures
  JOURNAL   J Mol Evol 50 (1), 39-44 (2000)
   PUBMED   10654258
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10517218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..154
                     /product="restriction endonuclease"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=17253
     Region          13..122
                     /region_name="Mrr_cat"
                     /note="Restriction endonuclease; pfam04471"
                     /db_xref="CDD:461322"
ORIGIN      
        1 msvisesspt addevnwraf eelvakhvad ldpkarvthd arlkgrlsgi drqvdvlarg
       61 slagsmitia feckrykrsv giatveefig klhdlavdrg vlcvfgdite pafwrlahan
      121 hpqvdlyvwr rpkptgweid indmgeeflt pvyy
//
LOCUS       WP_457697291             372 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457697291
VERSION     WP_457697291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38118
     Region          154..371
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkvaaiags vvlapmllia piavalagas naqaactdgg adavdakava kqvesilkgg
       61 gkgsvsvpgl ddpkeqipna ktiqatgvam kvpargqiva latalqesgl rnldygdrds
      121 lglfqqrpsq gwgtaaqvrd pvhastkfye gllkvsgwqs mtiaqaaqav qesgfpdaya
      181 kweplatalq kaiakdlpnk sgsgrdakpe vpaggcgrgg dgsgfgpipa gsvpkgykip
      241 tdapksvrta irwglgqlgt pyqwgghcta prgqdpmgrc dcsslmqasy kaggvsvsrt
      301 tysqvkegka vsvdalkpgd llftrgtaav pehvgmfigq glilqapktg dvvkistlas
      361 wrpdilaarr vv
//
LOCUS       WP_457697296             347 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457697296
VERSION     WP_457697296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=39232
     Region          39..325
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 measrdlaal svplvgelva mddpwdpyrl inptgepveg adaflrdlqg agrsattars
       61 ygmdllrwfr flwavevswd rasrieargf srwlqiagqp rrphwrrpse agrwsaggkp
      121 yapsvrahse tvlrtfydfh rdigtgpvln pfpldrsrhg rrahahrnpm dpprnersgl
      181 yrprvpkrvp rsvpdeefne ifarlpshrd ralvafyist garasellst wqagvdpgrq
      241 lisvvrkgtr evqelpastd afvwlrlyqv emddaipcgr rlplwwtlrs psrpltyhav
      301 hrmferanak agtsatlhal rhtaayrmae dpslpspmsn sssvmls
//
LOCUS       WP_457697299             834 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457697299
VERSION     WP_457697299.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..834
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=93425
     Region          <487..687
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtatlsarad rapalgvspg rtralaaqqr fpartvpesw pgtersrvaa arllsrppyt
       61 lnnagselhh khgivmvldw ledqpgqtwq erwqasgieq agaawrpvik qwlherglka
      121 awrmpvvgra lttvisaell rpsvdwlaag asrqgvlvrs mahsrdprgf erlrelgsqa
      181 qgvrpgavst tlcrsalila akggtladit igdvlelldi qavvlkrama gtevfyrllh
      241 qfgafgedap pnlravrnlg qrtpeelidr yglicrpvrd llvdylrerq paldhnslks
      301 lsyhlgkcfw qdiehhhpga dslrlapdvi gqwkqrirtk dktvtdpdgr rtstkverln
      361 hrdtltqvra fyldiaqwal edpgrwgpwv apspvradel enrkhqrrrk armdartrer
      421 lpvlpvlvrs vdqrrrdaaa vleaarhtrp gevftaagqq lvravvphgt agriwaedpd
      481 tgkrrdlgle derafwtwaa vevlrstgir veellelshh slvqyrlptt gelvpllqiv
      541 psktdterll lvspeladvl saiicrards tgavllvrsw drrecewqap apllfqrris
      601 gedraftdet vrtmldqali atgltdatgd plrytphdfr rlfitdailn glpphiaqvi
      661 aghqdinitl gykavypeea vqahmsflar rrslrpseey rvptddewhe flghferrkv
      721 sigacgrafg tpcihehacv rcpmlwpdpa qrdrlveird nlvariaeae regwlgeveg
      781 lqvslagaqq klaqvdqlta qrttvdlgmp ttihtaaats patvtpgwdp rdhr
//
LOCUS       WP_457697323             268 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697323
VERSION     WP_457697323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=26994
     Region          38..266
                     /region_name="SEST_like"
                     /note="A family of secreted SGNH-hydrolases similar to
                     Streptomyces scabies esterase (SEST), a causal agent of
                     the potato scab disease, which hydrolyzes a specific ester
                     bond in suberin, a plant lipid. The tertiary fold of this
                     enzyme is substantially different...; cd01823"
                     /db_xref="CDD:238861"
     Site            order(44,88,116,247,250)
                     /site_type="active"
                     /db_xref="CDD:238861"
     Site            order(44,247,250)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238861"
     Site            order(44,88,116)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238861"
ORIGIN      
        1 mrlsrfaalt saffvttala ltgasaaasa qlptatgyva lgdsyssgvg agsydsasgs
       61 ckrstkaypa lwaaahspss fqftacsgar tgdvlssqla plnsstglvs itiggndagf
      121 adtmttcalq gesaclarva qartyiantl pgrldgvyna isqkapaaqv vvlgyprfyk
      181 iggsciagls eksrsainaa addingvtak raadhgftfa dvnatfsghe lcsgsawlhs
      241 vtfpvlesyh ptatgqsggy lpvfasaa
//
LOCUS       WP_457697328             463 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697328
VERSION     WP_457697328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..463
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49861
     Region          38..450
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,166,
                     169..170,173,286,289..290,293..295,298,325,329,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mtdttsstpe rrggtpigar aaarldrlpp srwhrritli vgigaffdly eiflggvlaa
       61 alaeqwhlgh takswviaag flgmfvganv lsvladrfgr rrmflvnlga yaffsllcaa
      121 apdlswllvl rflsglglga elvlvdtyla eflpravrgr yiawaytigf lgvpvaallg
      181 arlvaahrlf giegwrwllv agalgaaflq vmrrqlpesp rwltvhgrge eaerivagle
      241 ervarecggs lpsvpeaetv perkvplaem frgeqrrrtv mwwifqvlqt vgyygfgsla
      301 pvvltakght vtesllyaal sfcgypigsa lslplidrie rrtliiasal giagcglafg
      361 fatatwavvt fgflltvcsn vfsnafhvyq telfptglrs saigiaysls rltsavlpfv
      421 alsvltdlga aavftgsagl mvllcldval lgprstgrsl eri
//
LOCUS       WP_457697330             232 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent F420 reductase [Streptomyces nigrescens].
ACCESSION   WP_457697330
VERSION     WP_457697330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24552
     Region          22..223
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mtgrlrsspp ryrkehhhmt sigilgagrv gtnladklsa aghhvtlggr spedtaarta
       61 glapriafad qrttarttdv vinatpgdss ldrltglrte lagkilidvs natrddgdgl
      121 pgdlcypgss laeklqaalp dthvvktlnt mlfmvmtape alaapptayl sgndehakrt
      181 vtgllgdlgw qperiedlgd ittarateam ilvvphilrr hgfkpfavsl ar
//
LOCUS       WP_457697351             294 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697351
VERSION     WP_457697351.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30453
     Region          42..279
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 manepehide rgasappqrt taasaggpas apgggaagpp avriqglwkk fgeqiavngi
       61 dltlpagrfi glvgpngagk tttlsmvtgl lrpdaglvei gghdvwrdpv svksrigvlp
      121 eglrlferls grellgyigr lrglpgdevd kraaqlldvl dlagsqhklv vdystgmrkk
      181 iglasallhn pevlfldepf egvdpvsaqt irgvleryta sgatvifssh vmelveslcd
      241 wvaviaagri radgplaevr gaapslqdaf lelvgandrg agadldwlgg ggar
//
LOCUS       WP_457697367             405 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697367
VERSION     WP_457697367.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43824
     Region          10..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 melfheepgi geriarlrar rkltqeglae raglcvdivr kleqgvrrta rlttlnalar
       61 aldvepsalv gqpatfevrs egdqpsvlal rqaispvsdl lgddpdpedp pgiaalrasl
      121 rsterirrdg rmgeigvllp qlirdakaaa ragsgaeaaa ahsvlaeayq vaattltalg
      181 kedaaftale rsmaaaakgd dphlqtvgfs slawiltkqg rladaerval naaeriepgf
      241 rspppelalw gilllraata avrlerhdtv rdllnlasaa aarigtdrld yatpfgptnv
      301 gvakvnflle meqsaealra srtvpelqal pptwrarfhv dralafadlh kddgalrall
      361 taertapewm ryhstsrrlv adlrhrerrr tsplteladr lgldg
//
LOCUS       WP_457697361             234 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457697361
VERSION     WP_457697361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..234
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=25730
     Region          10..161
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mghdapprwd rrmqqrlahg eaaalgelyd rfaslvhsla hrvlddedaa drltrevfty
       61 iwehpdsydp kqgplrswia gvtrhqavqr lrqteaasar dcgdgapapa eieqkirdas
      121 taaradyivt smpaplraal elayfqrrdy rqtaadlgvt edearrrlrl glqllstahh
      181 hqalppghra sytsraprss ptaphaprgp ltphtqhtgp gtsappgpgh grsr
//
LOCUS       WP_457697369             185 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697369
VERSION     WP_457697369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20014
     Region          7..158
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          85..181
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 msperhivyr eaqpadteqi daiddsfttd tvyevvagde gfalrpavvd pplvkvfpdd
       61 eeneddeaad dmhvevavdd gtvcgfiavg veewhrrlvi hqiavasthr ghgvgaalmq
      121 racaygsrlg artawletsn vnvpairayr rmgftfcgld ttlyrgtpse getalfmskt
      181 lgadg
//
LOCUS       WP_457697375             655 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457697375
VERSION     WP_457697375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..655
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=67653
     Region          14..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,72,77,82..85,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,80,96..99,103,105,142,144,
                     146..147,149,160..161,164,181..184)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,80,96..99,103,144,146..147,
                     149,160..161)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,103,105,142,144,146,164,181..184)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(160..168,177..184)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgifggegrl iggryrlgir lgrggmgtvw raidevlgrq vavkelhlde gtaepearvq
       61 reramreart vaqikhpnvi vvhdvveqdg rpwivmelve gpsladrlqs ggpvapreaa
      121 rigiallgal raahtrgvlh rdikpanvlm esgtgrvvlt dfgiaqvpgv ttltdaggfv
      181 gspeytaper magrgtgpea dlwslgvllc aalsgaspfh rdslggvlha vvydeielpe
      241 sarplhavvh gllereperr lgvaeterll rgylqsgrap ergpgghpgh gpgrghgghg
      301 ghgghgghga ggggaaglaa eavagaggpg epfpggpdtp rhpgpdvhap lydvpggglp
      361 gehppnehph sedapvagtp ppgpatpart pagggagrpg grtggrtpgm pirealddra
      421 laaaarphtg rartallval aavviggvga giavllmnqs gteggtgtgg rpsrsqqasd
      481 tgppqsggpg takptvtppp asggtgkipa gyrlvrdpeg falavpegft rsyenervyy
      541 ysqgkrfrig iqlqqqvpeg plgamrtaha kgpadyrgyr qgqvtetthn glqaglwefv
      601 wdgstqdggs rytydlswde ggrmidvwis spvasrteak rhfdtaldaf rlsga
//
LOCUS       WP_457697385             214 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697385
VERSION     WP_457697385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Stuffle,E.C., Johnson,M.S. and Watts,K.J.
  TITLE     PAS domains in bacterial signal transduction
  JOURNAL   Curr Opin Microbiol 61, 8-15 (2021)
   PUBMED   33647528
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Henry,J.T. and Crosson,S.
  TITLE     Ligand-binding PAS domains in a genomic, cellular, and structural
            context
  JOURNAL   Annu Rev Microbiol 65, 261-286 (2011)
   PUBMED   21663441
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 214)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   5  (residues 1 to 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   6  (residues 1 to 214)
  AUTHORS   Taylor,B.L. and Zhulin,I.B.
  TITLE     PAS domains: internal sensors of oxygen, redox potential, and light
  JOURNAL   Microbiol Mol Biol Rev 63 (2), 479-506 (1999)
   PUBMED   10357859
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   8  (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
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459460
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /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_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0140110 - transcription regulator
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=23344
     Region          9..209
                     /region_name="YheO"
                     /note="Predicted transcriptional regulator YheO, contains
                     PAS and DNA-binding HTH domains [Transcription]; COG2964"
                     /db_xref="CDD:442204"
ORIGIN      
        1 mgtaeeapdp rvrmwapacq avarllgpya evvlhdpdtd rvleiwnpms srgpgdpsll
       61 geldelepsp qgvygpyekl ladgrrlssv savlrdahdr psavlcinld rtpleqaaev
      121 lsafgaptvq rpeplfeqdw seriqhivgs hvretgrpve rmtrqdrlav lgrldearvf
      181 avrraapvva galrvsrstv ygllaelras sakd
//
LOCUS       WP_457697402             480 aa            linear   BCT 27-JAN-2026
DEFINITION  PspC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697402
VERSION     WP_457697402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Joly,N., Engl,C., Jovanovic,G., Huvet,M., Toni,T., Sheng,X.,
            Stumpf,M.P. and Buck,M.
  TITLE     Managing membrane stress: the phage shock protein (Psp) response,
            from molecular mechanisms to physiology
  JOURNAL   FEMS Microbiol Rev 34 (5), 797-827 (2010)
   PUBMED   20636484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..480
                     /product="PspC domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49276
     Region          23..83
                     /region_name="PspC"
                     /note="Phage shock protein PspC (stress-responsive
                     transcriptional regulator) [Transcription, Signal
                     transduction mechanisms]; COG1983"
                     /db_xref="CDD:441586"
ORIGIN      
        1 mndaahvees apadpagsap shpplrrsrr hkviggvcgg lgrqwdldpv ifrivlavls
       61 vgglgliayg fawllipldg edenegrrll sgrvegpalt allfalvgcg lflttlakgs
      121 mmsfaimltl avagsaywsr rrrlveaegp esmdtataqa vadappetka ppvptspsww
      181 raqrgeaagp gylwgpdttp lpldityrae hgaaaatapy rqdgwsdagr ppgapvppgg
      241 appapapsrg rrsgrpiggw tfllallagc gtalavsrhd glvpalqagl acalvvfglg
      301 lvlsawfgrt gggtvfmvvl talllagatt lpdnltahwq kstwspttls avrpqyelgs
      361 gegeldltgl plkadstvht gaevgagrlq vtlphgvtar lhislglgdv qlpgesphdv
      421 dltaggqrtv tlpadglkkg ekprgsveln lelvagqvav traapapaap aaptsqgapr
//
LOCUS       WP_457697407             373 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697407
VERSION     WP_457697407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..373
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40157
     Region          37..370
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 msltgtpffl tsltllivav vlpfalwgri agpplvrgla rllmllfaqv taitvvfvlv
       61 nnanslydtw gdllgtdshv eaardlgpdg mggrqikhep kqlqqfrpad dpkvgagvrm
      121 telrgrisgv rgevyvwlpp qyndpayrnk kfpvvellpg ypgsakswlg slhaaeqlmp
      181 lmqngtvkpa ilvaprtnll pgadtgcvni pgkvnadswl tvdvrkmiid nfragdkpds
      241 walagysaga hcaaklalah pdryraavam sgyndpaler dslagkdpkl riesnplhil
      301 ksanaagkpp rtalyvsgaa rdgyqaglgl rqfaqspttv tlrqippgag httvvwkqqv
      361 peifrwlgtq lra
//
LOCUS       WP_457697408             254 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697408
VERSION     WP_457697408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26052
     Region          191..>242
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mthtaaapdt glhsavhawv dgwarargtd apqavpggfr ievrrpghla rhvlseaapa
       61 vlrdlvdtlt tpgqwikvca prevvepllt adwevsepqy lmttaalapp rsgaglppgy
      121 rleivdesee vfearvhavg gtgnglgpgp gsgsgraega gpvlaasgra alttgapgss
      181 papyapsvvf dmigtepahq rrglgravmt alagraverg arqgvlvasp dgralyeamg
      241 wrsrsmvtaa grmg
//
LOCUS       WP_457697418             423 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces sp. 900105755].
ACCESSION   WP_457697418
VERSION     WP_457697418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  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 423)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..423
                     /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=44980
     Region          77..>152
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          106..129
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          193..419
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstvsgdisi rtfegrrwlf psavihgldp eagpagrrpr rtardwlvdl scfllavllg
       61 aaaantmrqd pnvphglava dqlmgglaca avwlrrrwpt glaiamipvs fasdtaggas
      121 mvalftlavh rpfrhvawit aanlvlvplf ywlrpdpdlp ylavvilvvl ltllvvslgm
      181 fvrskrqlmv slrdrarrae teaglraera qrlareaiar emhdvlahrl tllsvhagal
      241 efrpdapree varaagvire sahealqdlr eiigvlraad gedaggrpqp tlaaleslva
      301 esrgagmkvv ldnhvgdpaa vpasvgrtay riaqegltna rkhapgaevt vrvtgapgdg
      361 lditvhnpap atetphvpgs gqgliglaer atlaggrleh rpvgdggfev rawlpwaaas
      421 pat
//
LOCUS       WP_457697419             310 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697419
VERSION     WP_457697419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33270
     Region          100..202
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mqalpflsap lllarlvstp lrcarllptr assfplrstv vdlavlaghl vlyptgisqe
       61 rplprpaphp aaepaegfma aeapqpapga ptmlptegra hppilllhgf idnrsvflll
      121 rrslhrhgwr hvealnyspl tcdlrkaael lsrhveeics rtghrrvdiv ghslggliar
      181 yyvqrlggdt rvrtvvtlgt phsgtriapl msahplvrqm rpdseviael srpapncrtq
      241 fvafwseedq vmvpattari shpdliaynv hvagvghlal pvngavaagi realvsaeta
      301 egaadaisva
//
LOCUS       WP_457697424             223 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional DNA primase/polymerase [Streptomyces nigrescens].
ACCESSION   WP_457697424
VERSION     WP_457697424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Iyer,L.M., Koonin,E.V., Leipe,D.D. and Aravind,L.
  TITLE     Origin and evolution of the archaeo-eukaryotic primase superfamily
            and related palm-domain proteins: structural insights and new
            members
  JOURNAL   Nucleic Acids Res 33 (12), 3875-3896 (2005)
   PUBMED   16027112
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Lipps,G., Weinzierl,A.O., von Scheven,G., Buchen,C. and Cramer,P.
  TITLE     Structure of a bifunctional DNA primase-polymerase
  JOURNAL   Nat Struct Mol Biol 11 (2), 157-162 (2004)
   PUBMED   14730355
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Lipps,G., Rother,S., Hart,C. and Krauss,G.
  TITLE     A novel type of replicative enzyme harbouring ATPase, primase and
            DNA polymerase activity
  JOURNAL   EMBO J 22 (10), 2516-2525 (2003)
   PUBMED   12743045
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Koonin,E.V., Wolf,Y.I., Kondrashov,A.S. and Aravind,L.
  TITLE     Bacterial homologs of the small subunit of eukaryotic DNA primase
  JOURNAL   J Mol Microbiol Biotechnol 2 (4), 509-512 (2000)
   PUBMED   11075926
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..223
                     /product="bifunctional DNA primase/polymerase"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /calculated_mol_wt=23863
     Region          25..201
                     /region_name="Prim-Pol"
                     /note="Bifunctional DNA primase/polymerase, N-terminal;
                     smart00943"
                     /db_xref="CDD:214927"
     Site            order(94,105,131,134..135,137,163,172)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:238291"
ORIGIN      
        1 meetigvtga sqiplqrgeq lletavryae erhwdvfpga wlehdgetpr cscdaddcaa
       61 pgahptvpgw agqasgtata vrrmwskqpr asillptgrt fealdvpeta gclalarmer
      121 mglalgpvtr tpdrrmlflv lpgasvkvpa lvrtlgwapa aldlicrgeg eyiaapptrv
      181 gahgsvqwar rptpanrwlp daeelispla yacardavav rgr
//
LOCUS       WP_457697427             428 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457697427
VERSION     WP_457697427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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 428)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /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=45523
     Region          159..427
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvargeakar allrgalgrr lrslaavavp vllaiadaml vngleldlev gvsmlaaaal
       61 vlrrrfpllv flctlpglyi gyiwfapmig lctlavrrpg rarlglcavl liaahifpyp
      121 msdfvltdyr entqvlidac vtsatpialg llmrtrqela srvedltrsl rredrlladr
      181 vktterarla remhdvvahq vslislqaga vqvstedaea ragartirel svrtleelrh
      241 mvgvlradgg egaeahglap qpdleelprl iemsaldvty eggvvagasg tktveraafr
      301 tvqealtnvr khapgarvrv rvdpvdavrv dpvdavrseg sgrgegagra etsgraeaae
      361 esraahglrv eirngppdat atvpalpggg hglvglrera qslggtlear htsdggfvvr
      421 aefpygag
//
LOCUS       WP_457697441             215 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697441
VERSION     WP_457697441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22452
     Region          7..201
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 maahsltvgf dldmtlidsr pgiraayhel sartgtfvda dlavsrlgpp leqeisrwfp
       61 eervaetadl yralypahav tattalpgar ealdavrsag grtivvtaky epnaklhlah
      121 lgldvdalfg slwaegkaea lrkhdaqiyv gdhigdiaga htagalavav atgpcdatel
      181 raagaevvld dltefpswle ryvaegadgg vaaat
//
LOCUS       WP_457697451             218 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 25 protein [Streptomyces nigrescens].
ACCESSION   WP_457697451
VERSION     WP_457697451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Martinez-Fleites,C., Korczynska,J.E., Davies,G.J., Cope,M.J.,
            Turkenburg,J.P. and Taylor,E.J.
  TITLE     The crystal structure of a family GH25 lysozyme from Bacillus
            anthracis implies a neighboring-group catalytic mechanism with
            retention of anomeric configuration
  JOURNAL   Carbohydr Res 344 (13), 1753-1757 (2009)
   PUBMED   19595298
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Monterroso,B., Lopez-Zumel,C., Garcia,J.L., Saiz,J.L., Garcia,P.,
            Campillo,N.E. and Menendez,M.
  TITLE     Unravelling the structure of the pneumococcal autolytic lysozyme
  JOURNAL   Biochem J 391 (Pt 1), 41-49 (2005)
   PUBMED   15943581
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Fastrez,J.
  TITLE     Phage lysozymes
  JOURNAL   EXS 75, 35-64 (1996)
   PUBMED   8765293
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="glycoside hydrolase family 25 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24223
     Region          1..217
                     /region_name="Acm"
                     /note="Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25
                     family [Cell wall/membrane/envelope biogenesis]; COG3757"
                     /db_xref="CDD:442971"
ORIGIN      
        1 mdtshhshgr gekeridwtr vartnsfafl kasqgtgykd pwftrdhaav artsllrapy
       61 hffdprstgd gaaqarhfia taraagyhgn rtgelppvld vekvrrnhre vcprelrpgq
      121 ltvflqevrk afkvtpivyt rasfvkecmg gqgrvfaghp lwlarygsgt hepqpvpgag
      181 rswtfwqhte hgrtpgipgt gdrnvfrgsl gqlrgmas
//
LOCUS       WP_457697461             728 aa            linear   BCT 27-JAN-2026
DEFINITION  HelD family protein [Streptomyces nigrescens].
ACCESSION   WP_457697461
VERSION     WP_457697461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Larsen,J.S., Miller,M., Oakley,A.J., Dixon,N.E. and Lewis,P.J.
  TITLE     Multiple classes and isoforms of the RNA polymerase recycling motor
            protein HelD
  JOURNAL   Microbiologyopen 10 (6), e1251 (2021)
   PUBMED   34964291
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..728
                     /product="HelD family protein"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78294
     Region          24..727
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpshahhptt kprtessrpr pgsddplqre kshlaasrsa lramradaea lniadvtanw
       61 vnaevlqsev darikaladl shtplffgrl dylqapgldl aegasrgaap cgsprtesgg
      121 asgkggggrr egenfyigrr hvhdadgdpm vidwrapvsq pfyraskkdp mdlklrrrfg
      181 ytggeltaye dehltdptea artsallqse ierprvgpmr divatiqpeq deivragigg
      241 svcvqgapgt gktavglhrv ayllyahrer larsgtlvig pnrsflhyie qvlpalgele
      301 vkqatvddlv ghvevrgade aaaatvkgda rmaevlrrav rshitmpqep cvvvrgsrrw
      361 rvpayeleei vrelrdreir ygaarealpq riahtvlvrm eqageapddr vqdavarnaa
      421 vkaavkavwp pvdpaklvlr llgdaeflae qaegiltpee qktilwtrpa rsvksakwss
      481 adavlideam dlvartpslg hvvldeaqdl spmqyravgr rcstgsatil gdiaqgttpw
      541 atdtweealt hlgkpgsave eltqgfrvpr eviayasrll paiapdltea tsiresagdf
      601 tirtvgpadl taatltacdd alakegsigl iaaearipal rtaleaagvt clapgeetsa
      661 earltlvpat lakgleydyv vldepaaivd gepdertglr rlyvcltrpv sgltvvhaaa
      721 lpeqlagr
//
LOCUS       WP_457697465             240 aa            linear   BCT 27-JAN-2026
DEFINITION  copper homeostasis protein CutC [Streptomyces nigrescens].
ACCESSION   WP_457697465
VERSION     WP_457697465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..240
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24190
     Region          4..233
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mskrallevi algpqdavaa eaggadrlel vtdmaadglt psrgtfaavr aavglplrvm
       61 lraadgfaag dvaalceeaa alraegaeef vlgfltpdgr pdlaavaala evidgcrwtf
      121 hraldraadr dalrkelaga agtagldtyl tagsaqgvdg glstllaeqa rtaagepgya
      181 prilvggglg lghlpvlraa gldafhigga arpagwsapv eaaavrewre aldlpvaqrv
//
LOCUS       WP_457697467             227 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697467
VERSION     WP_457697467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..227
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24956
     Region          17..225
                     /region_name="COG4339"
                     /note="Predicted metal-dependent phosphohydrolase, HD
                     superfamily [General function prediction only]"
                     /db_xref="CDD:443480"
ORIGIN      
        1 mtsvprtadi tdpapelrqr wadtvtaarg tknptapdpa pyadnllsrw repqrryhtv
       61 dhlaavlyri delaahaddl ptvqlaawfh davyrpdrse neersaalae ralpelgvga
      121 artaevarlv rltvthdpap ddpdgevlcd adlavlagsp dqyaayaaav rdeyafvpdp
      181 dftagrsavl tqllslprlf rtprgydlwe htarrnlste ldllrga
//
LOCUS       WP_457697470             180 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697470
VERSION     WP_457697470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..180
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19117
     Region          37..167
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 msaseqggqp atdldpnyss egatatawpa avggmteaei fwlttvrpdg rphvtpllav
       61 wsdgalhfct gpgerkaknl asnahcvltt staggndlha gldvvvegda vrvhdeptlr
      121 rladlyveky gsdwhfdvrd gafhgegnra vvfrvepvta fgfgrgetys qtrwsfdgga
//
LOCUS       WP_457697476             315 aa            linear   BCT 27-JAN-2026
DEFINITION  MurR/RpiR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697476
VERSION     WP_457697476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32651
     Region          31..308
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msssvketfk dvavetrpap appapaalaa kvrtlaptmt rsmqrvaetv asdpagcaal
       61 tvtglaertg tseatvvrts rllgypgyrd lrlalaalaa qqaaggapav tadiavddsl
      121 vdvvaklaqe eqqcladtaa aldvtqleaa vtalsgarri dvygigasnl vgqdlvqkll
      181 rigliahaha dphlavtnav qmrtgdvaia ithsgrttdv ieplrvafdh gattiaitgr
      241 pdgeiasyad hilttstare selrpaamss rtsqllvvdc lfigvaqrty etaapalsas
      301 yealahrhsp rnnqh
//
LOCUS       WP_457697463             711 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457697463
VERSION     WP_457697463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..711
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75474
     Region          20..270
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(26..27,29..32,34,47,49,81,97..100,104,106,143,145,
                     147..148,150,159..160,163,177..180)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(26..27,29..32,34,47,49,81,97..100,104,145,147..148,
                     150,159..160)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(30,104,106,143,145,147,163,177..180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(43..44,73,78,83..86,98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(159..166,173..180)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtgmgvrpls gddpqrlgvy rmlgrlgsgg mgriylarst vdgslaavkt llaegvvsdt
       61 drrrfarevt larridsayt arvrdadpda elpwmaieyi papalselvr sagrlpgsav
      121 rwiaagtaqa lvvlhdegiv hrdvkpqnil lplagprlid fgishandit rtsltlgtva
      181 ftspeqarae psttasdvys lgatlfylav grppypetdd tirlltlvqr galdltglpr
      241 elaplirpcl aagpderpep adllrqfled ldrmptsrrg erwlpprwta ligkyeaygr
      301 slrkaggaqa ptadewtqqv pppeptrvyt eeraarrkqe eraarqkqee raraererea
      361 rkarerkeae drkraqarar ataqaaekqr reraererqk radnarreqr graasaqtaa
      421 sapsktspap qpansssggg cfwavllcia fvvflwkpwn aedtagsssg tssgsssgss
      481 sgsyssggtg sgissgtyss ggtgsgtssg tytsggtssg astsgsgtss sgtsssggtg
      541 srpttaasrt pspvdaafaa vrpgdclday qngygswsrs apvrvgcgaa saylrvlrva
      601 rtgscpsggg rggwwhsgtg ssstnlcver qfrrgqcfla kaqggrpgpa nlltawncsa
      661 drvprefsyi mqvtavlqas agtgacpgep gryryswnvy dgrtmicakv a
//
LOCUS       WP_457697490             251 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697490
VERSION     WP_457697490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27100
     Region          5..251
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 maaqesslpk yrriadalkr siaagefrpg drlpgendlm drhgvarmta rqalgvltse
       61 glaearkgag vfvrdfqpir rrgvprlare qwgegrsvwa advpdrdlvv devsvdeepa
      121 aetvaarlgi apgdaviarr rrfvldgkpv llstsylpaa lvagsaitqp dtgaggtyar
      181 laelgaapar freevrsrmp apeevdrlrl pagtpvilis rmartedgra vevnemilds
      241 sayvleydfd a
//
LOCUS       WP_457697494             487 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces nigrescens].
ACCESSION   WP_457697494
VERSION     WP_457697494.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=52351
     Region          11..486
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mvsersaapa gaevlvasnr gpvsyalgeg gtltakrggg glvsglsaig sdtdavwvca
       61 algggdreav rrtggaldpg dtggqrvrml dipvevytaa yngiansalw fvhhmlyqtp
      121 lepvydtefr aqwasyesyn rafaqalade aaegaavlvq dyhlalvpgm lrtlrpdvri
      181 ahfshtpwap peyfrmlpdd iaqqllagml gadrlgfltr rwadafaacc aavvggtgdt
      241 qigvyglgad agflrersqq edvaerlsal reqigtgpdg tarktvvrvd rtelsknivr
      301 gllayrqlla dhpswrervv hvafaypsrq dlavyreyte evgrvaesin saygtadwqp
      361 vvlhvkddfa rslaayrlad valvnpirdg mnlvakeipv vsdqgcvlvl sreagaheel
      421 gqdaltvnpy dvsgtaralh ealsmdager sertarlaaa atalppaqwf lkqlralqev
      481 tpradar
//
LOCUS       WP_457697502             421 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697502
VERSION     WP_457697502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..421
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45558
     Region          8..336
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mqrrylslaa aiattmtltl tgcgsgsgsd dvtlkliaad ygdsrsngsq hywdelaraf
       61 ekknpgikvd vevyswtdvd kkvedlvkdg hapdlaqiga yadyaakgql ysadqllsip
      121 tqadftpsla eageykrvqy gmpfgastrr lfynkklfte agitsppenw ddiahdaqll
      181 kakgvklpfa lplgpeetqa etmqwmlsgg ggytdgigky tidspenvkt fkwlkenlvg
      241 kgltgtdpae lnredaferf adgevgmlng hptlmkqaaa kgidygtvel pgshgkakat
      301 mgvadwmmaf kqgghrtqvg kfldfvyskk nvekfsgeyg llpvttsasq tmladdkyak
      361 fhgflkqldh aefypankts wplisktvka kmgaavgprg npagvltdiq ntadatdqta
      421 e
//
LOCUS       WP_457697504             318 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family protein [Streptomyces nigrescens].
ACCESSION   WP_457697504
VERSION     WP_457697504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=31747
     Region          1..310
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mrhvialdvg gtgmkaalvg vdtassagtp pvllyearrp tgrehgpdav veailgfaae
       61 lrdlgtaryg apaaaagvav pgivdehsgt avyaanlgwr dvpmrallse rlggvpvalg
      121 hdvrtgglae grigagrdad rflfvplgtg iagaigiggr ieagahgsag eighivvrpg
      181 grecgcgqrg cletlasaaa vgrdwaaacg dphanaadaa kavasgdara qpvwqravda
      241 ladglviglt lldpqtliig gglaeagdtl ftplreavrr rvtfqrlpsi vpaalgdaag
      301 clgagllawd llstevta
//
LOCUS       WP_457697508             311 aa            linear   BCT 27-JAN-2026
DEFINITION  1-phosphofructokinase family hexose kinase [Streptomyces
            nigrescens].
ACCESSION   WP_457697508
VERSION     WP_457697508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31844
     Region          2..300
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 miltvtlnaa ldityrvprl hphttnrite vserpggkgl nvarvlaalg hrtvatgfag
       61 ggtgaalrtl laetevtdal vpvggatrrt vavvdaatgd ttqlnepgpv vspaewdtfl
      121 gtyrellgea ravalcgslp pgvpvdvyar ltraargagv pvlldtsgep lrrglaarpd
      181 lakpnadela altgsteplr aardarrrga havaaslgpd gmlavtadga wqaapprria
      241 gnptgagdsa vagllsglve elpwpdrltr avalsaatvr apaagefdva tyeellrtvr
      301 aapspeirss k
//
LOCUS       WP_457697514             204 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697514
VERSION     WP_457697514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21329
     Region          41..202
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mftktpadaa asgpvarpvp avalasvpgd apiphsvgvs ddefraalsr laagvvlita
       61 hdpdsgphge dagmtatafl svsldpplvm vsvrndsrmd dllelqpdwa vsvlsghqrq
      121 iagrfamkgr isdrllfedi pfvrgeasga pliggalatl ecrteqrvva gdhtlviarv
      181 latsipnedd gpltyfrgky rqlg
//
LOCUS       WP_457697518              89 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697518
VERSION     WP_457697518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..89
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9019
     Region          15..>73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrtpltpre rergerlgal lrtargersm vevaaaagls aetlrkietg raptpaffti
       61 aalagalgls ldevaalatp peapaaava
//
LOCUS       WP_457697526             399 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457697526
VERSION     WP_457697526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 399)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..399
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016712 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, reduced flavin or flavoprotein as one
                     donor, and incorporation of one atom of oxygen [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43580
     Region          21..399
                     /region_name="CYP105-like"
                     /note="cytochrome P450 family 105 and similar cytochrome
                     P450s; cd11030"
                     /db_xref="CDD:410656"
     Site            order(67,89,91..92,175..176,185..186,189,192..193,196,228,
                     231..232,235..237,240,283,285..288,312,389)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410656"
     Site            order(90..91,98,102,109,154,157,232..233,236..237,
                     240..241,244,282..283,286..287,289,312,340..342,345..346,
                     348..350,353..354)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410656"
ORIGIN      
        1 mtgaqpttrt qptertcpfs ppegyrtlre edpitpltfp dgakgwlvsr yadvravlad
       61 prfganrrrv rpgdptpada plpppppgmf immdppehtr frrlltgqft vrrmqklapa
      121 veqivaeqld amaaaegpvd lvqafalpip slvicellgv pyadreefqe nsgmllrlda
      181 sheeiqqaht amnqyihqla vakrahptdd ilsglvqser ltdeelagvg sllllaghet
      241 tanmialgtm cllgnpeqla alradpalmd gaveellryl tivqyglrrv aledveldgh
      301 rieagatvla slasgnrdat qfsgdpdald vrrpysphla fghgvhqcig qqlarvemka
      361 alsalldrfp slrlavpadq vpmrddmliy gvhelpvtw
//
LOCUS       WP_457697529             477 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457697529
VERSION     WP_457697529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50882
     Region          121..477
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 magdwrgslr arlmvgvvll aavgmvavna vslvglrlnl vdvadttltk tretvqhrvh
       61 srrapidedd lnslipdgay ialvddrgrv vaqtpardld grarsrpdlp tplpdgfaeq
      121 ivtvsaqgmp vpryrtlsfp lghsatirpt pgappqrfsr vvaakslqpa edvvywliga
      181 daaatlavlg givllsrgvl gvglrplrdm attataiadg didqrievar phsevgevgt
      241 alnrafderq rseeqlrqfv anashelrtp lttirgwaql hlhglaqdpa lieramlrie
      301 geaarmhsmv eellllarld qgrpiahapv nlgaladdtv tdarvvapgr pitveapdev
      361 facgdedrlr qvlqnllsna lrhtppdtpv tvtarslptg taeltvtdqg pgmppataer
      421 iferfyrgde srnptsggtg lglsivksia eahngtatvh ttpgkgstft vtlptah
//
LOCUS       WP_457697535             367 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces nigrescens].
ACCESSION   WP_457697535
VERSION     WP_457697535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10473666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.11.9"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39516
     Region          24..141
                     /region_name="Creatinase_N"
                     /note="Creatinase/Prolidase N-terminal domain; pfam01321"
                     /db_xref="CDD:460159"
     Region          160..352
                     /region_name="APP-like"
                     /note="Similar to Prolidase and Aminopeptidase P. The
                     members of this subfamily presumably catalyse hydrolysis
                     of Xaa-Pro dipeptides and/or release of any N-terminal
                     amino acid, including proline, that is linked with
                     proline; cd01092"
                     /db_xref="CDD:238525"
     Site            order(208,225,236,300,329,343)
                     /site_type="active"
                     /db_xref="CDD:238525"
ORIGIN      
        1 mtqvdyerrm aragraaada glaglivtpg pdltwlcgyr ptavterlta lviepgrrsr
       61 llvpvleypd aeyspgawam evsgwtdgsd pyaevakwmd pqgrygmsds twamhllglq
      121 rsvpgsgyaa ltevlpmlra vkdaqevell aaagaaadat yeeiltvrfg grresevaad
      181 lvrlltehgh sqvdftivgs gpnganphhe agdrviedgd mvvldfgglk dgygsdttrt
      241 vhvgepgaee rkvhgivrea qqaafeavrp giacqdvdrv arkvikaagy geyfihrtgh
      301 gigvtthepp ylvegehlpl vpgmcfsiep giylpgrfgv riedivtcte sggrrlnqta
      361 remavvr
//
LOCUS       WP_457697537             393 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457697537
VERSION     WP_457697537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..393
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41455
     Region          1..390
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mdrivlvgas aagltaadal rregftgslt lvgeelwapy drpplskqvl aggwepertv
       61 lrqeadlrrl qldlrlgcra tgldpaartv tladgdrlry dglllatglr prrlpfghdl
      121 agvhvlrtld daltlraqlg agprvvviga gflgseiaat arglgldvtl vdteptplar
      181 qvgtwvgglv adlhrdhgvr lhlgrgvtdv tgargrvtav llddgtrlpa dvvvvaigsv
      241 pavdwlagsg lplgdgvrcd shcraapgvy aagdvanwpd patggrirle qrmnateqar
      301 taarnllagp gdtapyapvp fgwtdqydak iqfhgrcpad aqvecvegdp rartfvalyr
      361 lhgrvvgalg wnsaralrey rghigttgpv ktg
//
LOCUS       WP_457697539             242 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457697539
VERSION     WP_457697539.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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 242)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26427
     Region          19..228
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mlsasptsga plprgsgqrl lvvdddprma ellettlsla gyevatagcg gealrsyade
       61 ppdllvldvl lpdldgftic rrlvesgaql pvlfltards vedrvtgfam gaddyltkpf
      121 slpellarvh allrragrsa epgpllcfad ltvdersrrv rrgdrqials pteykllryl
      181 linadqvmsk eqimdhvwqh hfgegvvekl vsrlrakvda hapalihtmr gfgyslrlpe
      241 gg
//
LOCUS       WP_457697543             852 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Streptomyces
            nigrescens].
ACCESSION   WP_457697543
VERSION     WP_457697543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..852
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92052
     Region          52..840
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 msngfmgpeg ygpdpfgdfl srffgsaksg ggeqgqpvpr qadiarmmsa pardlvtsaa
       61 ayaaehgspe lgtehllraa laaeptrsml qhagadpdal aaeidraags gpkqasvavt
      121 pavkrallsa helardngas yigpehvlda laanpdsaag rilnlahfep qaapqggpga
      181 ahpgsehgaa pkhdtptldk ysrdltdlar agridpvigr eeeieqtiev lsrrgknnpv
      241 lvgdagvgkt aiveglaqrl adgdvpetla grrvvaldlt avvagtryrg dfeermnaii
      301 eevrahsesl ivfidelhtv vgagggsgdg gsleasnmlk palargelhv igattleeyr
      361 rhiekdaala rrfqpilvpe psvsdtveil rglqdryeah hqvrytkeal laavelsdry
      421 iahrflpdka idlidqagar vrlrsgakat dvrdlereve qlvrdkdqav aseqyerate
      481 lrdriadlta rieagqaepp sdchivqvta ediaeivsrq tgvpvssltq eekerllgla
      541 erlhtrvigq ddavtavsda ilrsraglad pdrpigsflf lgptgvgkte laralaealf
      601 gseermvrld mseyqerhtv srlvgappgy vghedagqlt eavrhhpysl llldevekah
      661 pdvfnmllqv lddghltdsq grtvdfkntv ivmtsnlgsd alsggrgvlg fgpdisgaea
      721 gdgarerals slrehfrpef lnrldeiivf rrltddqlrq itgllldgtr rrlhaqdisv
      781 dfspgavdwl thrghqpeyg arplrrtiqr eidnmlsrll ldgalssgde vrvevennel
      841 afrtgkrere sr
//
LOCUS       WP_457697547             204 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697547
VERSION     WP_457697547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (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   3  (residues 1 to 204)
  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 204)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23477
     Region          28..110
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhvtekrag atdtgdaerp alpatswavl gllsfgeels gydlkkwsdw slrlfywsps
       61 fsqiygelkr lekvgyvtsr mvaqetgnrd krvyvitdag maavrhware apveppvlkh
      121 gvmlrmwlgh lletdrmrev lgrhreyaet mrqraevdvd dacgeeaway palvlkwser
      181 yyaserdlad amladlderd rrrl
//
LOCUS       WP_457697555             358 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457697555
VERSION     WP_457697555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Fraaije,M.W. and Mattevi,A.
  TITLE     Flavoenzymes: diverse catalysts with recurrent features
  JOURNAL   Trends Biochem Sci 25 (3), 126-132 (2000)
   PUBMED   10694883
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="NAD(P)H-dependent flavin oxidoreductase"
                     /EC_number="1.13.12.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016703 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of one atom of oxygen (internal
                     monooxygenases or internal mixed function oxidases)
                     [Evidence IEA]"
                     /calculated_mol_wt=36923
     Region          16..349
                     /region_name="YrpB"
                     /note="NAD(P)H-dependent flavin oxidoreductase YrpB,
                     nitropropane dioxygenase family [General function
                     prediction only]; COG2070"
                     /db_xref="CDD:441673"
ORIGIN      
        1 mtattgietp ltrlvgvrhp lvqtgmgwva gprlvsatan agalgilasa tmtveqlraa
       61 vhevksrtda pfgvnlrada gdaaervrli vaegvrvasf alapsrelia rlkdagvvvi
      121 psvgarrhae kvagwgadav iiqggegggh tgnvattvll pqvvdavdip viaaggffdg
      181 rglvaalayg aagvamgtrf lltsdstvpp avqarylaaa akditvttkv dglphrmlrs
      241 elvatlerag rgtallravr haasfrklsg lswaqmvrdg lamrhgrdls wsqvllaant
      301 pmllkasmve grtdlgvmas gqvagviedl pscaelvdri maearetlaa lpptatpr
//
LOCUS       WP_457697566             480 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697566
VERSION     WP_457697566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49822
     Region          30..465
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,246,249..250,253..255,298,326,330,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mrprvapqve tadaggsfsh rdraviaaaa lsmlvvqmdw faldlmlpvi ardfgtsstd
       61 lqwlvsgyml aigalmivgg rtadvhgrrr vivigllvfa vlsvvcsaaq napwlvgarv
      121 vqgvgaalif pvsvavvtsy frddrqgpav gtvlafssig talgpfvggv faehvswrav
      181 fllnvplcla amllvlrfvp esrdahatrh ldlpgaaava lglaclmlav dqgqgwgwas
      241 aptlvtlalg vaflvlfvav errapeplie lslfrnvkfd vitlagslsn vvycliavla
      301 alylqqargl spfhagvifl alscgvgaas ywagqlalrw raellmacgm ltsgagllal
      361 twvqplgwya alfvvcglgi glgwaltnva tqahvpaert gaasglvlts lvlfgavsvt
      421 iaatvletvs gspttaasdg paieavlrgt svlaflgafa lfavcrprlr arglavedtg
//
LOCUS       WP_457697572             461 aa            linear   BCT 27-JAN-2026
DEFINITION  aminopeptidase P family protein [Streptomyces nigrescens].
ACCESSION   WP_457697572
VERSION     WP_457697572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Are,V.N., Kumar,A., Goyal,V.D., Gotad,S.S., Ghosh,B., Gadre,R.,
            Jamdar,S.N. and Makde,R.D.
  TITLE     Structures and activities of widely conserved small prokaryotic
            aminopeptidases-P clarify classification of M24B peptidases
  JOURNAL   Proteins 87 (3), 212-225 (2019)
   PUBMED   30536999
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Graham,S.C., Bond,C.S., Freeman,H.C. and Guss,J.M.
  TITLE     Structural and functional implications of metal ion selection in
            aminopeptidase P, a metalloprotease with a dinuclear metal center
  JOURNAL   Biochemistry 44 (42), 13820-13836 (2005)
   PUBMED   16229471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659804
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="aminopeptidase P family protein"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070006 - metalloaminopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49831
     Region          57..160
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          193..440
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cl00279"
                     /db_xref="CDD:469704"
     Site            order(256,273,285,370,401,425)
                     /site_type="active"
                     /db_xref="CDD:238514"
ORIGIN      
        1 mtsrtaplht gshdlpvsda ladfmtgqwa atplpagsrv pgfalfagrr arlaarfpga
       61 rllvpagelt vrsndcdhrf rphsayawlt gltgedqpgh vlvlepdgea vlylrprspr
      121 dgggefyrdr kygefwvgrr pdlaeagrlt gircahlddl vrhaadrdas rdpelacals
      181 elrlvkdawe vgqlqqavdh tvtgfgdvvr slpaalrhpr gerwiegifq lraraegngt
      241 gyetiaaaga hacvlhwirn dgpldpdqll lldagvetds lytaditrtl plsgrfspvq
      301 rrvyelvlaa qdagiaalkp gasfrdfhra cmgvlaegla dwgvlpvpaa ealapdsgly
      361 rrytlcssgh mlgldvhdcg raraeqyldg vltegqvltv epglylqpdd etlprelrgi
      421 girieddlvi tadgarlmss alprtadgve ewmagllage a
//
LOCUS       WP_457697570             238 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697570
VERSION     WP_457697570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26236
     Region          7..219
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mgelkhrsli taqerlrdqv ahqlraalva gelrpgsvys apglaadfgv satpvreaml
       61 dlareglvep vrnkgfrite vserdldqyt eiralievpv vgqvtrtagr aelealrpaa
      121 leivaaarah dligyleadr rfhlellgls gndrlvetvg elrkrsrlyg ltrldernql
      181 lpsaeehvel levmltgdae aaescmarhl ghvrslwaeg rdeplvprpq rragaqrv
//
LOCUS       WP_457697576             137 aa            linear   BCT 27-JAN-2026
DEFINITION  STAS domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697576
VERSION     WP_457697576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14502
     Region          14..105
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(25,27..29,35,58,60..62,64..66,69..70,92,96..97,99)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            61
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mrrqsttprr glprgapivv elfgeldfps aartnsrldp vtagnrphmv ldltqvdfld
       61 cggigvlcra rrrtrahggr lslvitdprf lrildavglt gsfdildapp dtarlsddgp
      121 ctagrdgsvt aaaaprs
//
LOCUS       WP_457697578             800 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 65 protein [Streptomyces nigrescens].
ACCESSION   WP_457697578
VERSION     WP_457697578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 800)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..800
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89697
     Region          3..798
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mthawtwsye gydpdterlr etlctlgngy fatrgaasev lsgpahypgt yaagcynrll
       61 stvagrpven edmvnlpnwl plryricpad aapgpwlspd hahltehrqt ldlrhgtltr
      121 wsvyedeagr rltveqcrlv hmgephlaal rtcfasqgwt gaveveagid gavrnagvar
      181 yrgladqhlt gwetgteqpd tvwlscrtld sdirialaar trvpgghggv praqltalra
      241 fhtlilpltp dspavvdktv alytsrdpai esplhtavda valaphfrql raahrrawen
      301 lwrqaklevp geagrilrlh lfhllqtlsp htaeldvgvp arglhgeayr ghvfwdelfv
      361 lpflnlhlpq vsralldyry rrlpaachaa reagragamy pwqsagdgre etqqlhlnpr
      421 sgrwlpdysr lqhhvgsaia ynvwqygqas gdteflhtrg aemlleiarf waaaadwdpt
      481 lgryrirgvv gpdeyhdgyp gaaepgvddn aytnvtaawv lmraldlcrt lpephqrqlf
      541 eqlqlspeep erwddiahrl hvpyhrgvis qfagygdlae ldwhgyrqry gdirrldril
      601 eaegdtvnhy qaskqadvlm lgylfsptel aavfrglgyp ldedtwhatv dyylhrtshg
      661 stlsalvhaw vlarvhrpda wtyceealtg dvadvqggtt aegihlgama gtldfvqrgm
      721 tgletrdqal wldpaplrel skfgvriryr rhwdidlrir aeqvriavpa senavvrvnl
      781 rdrsfalapg tsrrldlpee
//
LOCUS       WP_457697580             254 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697580
VERSION     WP_457697580.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26411
     Region          14..247
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtgapslaac lhslravifd tdgvitdsap vhaaawkgaf daclaavggq rpfdpvddyl
       61 ryvdgrarqd gaaaflhsrd ldlplgapdd apgtdtvrav aarkdelfse slrtrpiatw
      121 pgtvrllhal rhhglpcaav sasrhatell saaevyplfq avvdgneanr lqlpgkpdpa
      181 lfveaarrlg vpprdsavve dalagveagr rggfglvvgv drtagpysat alrrrgadvv
      241 vtdpgellms gegg
//
LOCUS       WP_457697585             574 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457697585
VERSION     WP_457697585.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 574)
  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 574)
  AUTHORS   Martinez,S.E., Beavo,J.A. and Hol,W.G.
  TITLE     GAF domains: two-billion-year-old molecular switches that bind
            cyclic nucleotides
  JOURNAL   Mol Interv 2 (5), 317-323 (2002)
   PUBMED   14993386
REFERENCE   3  (residues 1 to 574)
  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   4  (residues 1 to 574)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12187228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..574
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=61617
     Region          54..201
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
     Region          228..361
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          349..574
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvgdhgsgrr dtarrrldal pdelqqrlda lrqgpgdpan llleavlsvg reldlpqvlr
       61 riveaavvlv daeygalgvv segtrlsqfl pvgvteeqqe eigrlpeghg llgelirhpr
      121 plrlselsrh pssygfpphh ppmrsflgvp irvrdevfgn lyltekrggg efdaedetvl
      181 salavaagva ienarlyeea ryrqrwqean gaivaslllp gademaalrl ivdqareilt
      241 adlgviavpe hdgtalhval asgvdaeehr glllplqgsf mgaaldlrep listdverdp
      301 ritagpprwr glgpavavpm itggrprgvl lvarvrerap fteletgpll tfagqaalam
      361 eladqrrsae rltllqdrdr iardlhdlai qrlfatgmtl qsavrfvdhp easerllrav
      421 ddldetikii rstifglrth tsgrashglr vrtvtaveqa aralgftpsl rmqglidtdv
      481 paeiaedvva vlgealsnaa rhahatavev slavgggals lsvtdngvgl prngrrsgls
      541 nlakraesvg gemtletpaq ggtrlvwqap lass
//
LOCUS       WP_457697595             422 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697595
VERSION     WP_457697595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44000
     Region          40..418
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 msrtwalrkn kaagtsvtaa drrrlapefg tqnplellkr rfhsgelgsv pvalglivvw
       61 iifeslnenf lsprnlsnls vdivgigmis vgvvfvlllg eidlsvgsvs glaaaafavl
      121 nvnhgmpegl alliavlggt aigafqgffl akvgvpafvv tlagllgwng lmlyilgsng
      181 tiniddkgll amltgfyfhn vaaayglaal gtagyfltsy hdarrrraag vpartlseil
      241 lrtgvlaaia masafvlnqf lglplallif lvmlvgldfv lrrtrygrmi falggsveas
      301 rrtglnvdlv risvfmmsgt maavgglfla srvtsasqts gaglllmdvi aaaviggtsl
      361 fggrgrtwsa llgvlviqsi asgvalmgiq tavqfmitgg vllvavvids lsrraqrahg
      421 rv
//
LOCUS       WP_457697598             366 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697598
VERSION     WP_457697598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  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 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   3  (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   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   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   6  (residues 1 to 366)
  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 366)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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   9  (residues 1 to 366)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 11467991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="sugar ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38046
     Region          40..350
                     /region_name="XylF"
                     /note="ABC-type xylose transport system, periplasmic
                     component [Carbohydrate transport and metabolism];
                     COG4213"
                     /db_xref="CDD:443359"
ORIGIN      
        1 mnarlrgaaa llagvcmvag paacgeagga restgsapgg apkigvllpd ntsrlyhfdk
       61 pliekkihql cpectvetvs aqhdvatqqq qvdamitkqv qvlildavds kslrssvesa
      121 rragipvvay drlvegpvsa yvsfngetvg rlqgeallka lgpkardaqi vmmngastdp
      181 nsawfkqgal aalkgkvkig kayetgdwrp enanrnmsaa isalgaehid gvysandgla
      241 agiisalraa kvaplppitg qdaelaaiqr lvkgdqimtv ykpfapeagt aaamavalgr
      301 geklkgitth tansptnrgi pavlltpiav nvhnikntvv kdgmytidqi ctpkfesack
      361 kagllr
//
LOCUS       WP_457697618             487 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457697618
VERSION     WP_457697618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50964
     Region          18..446
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mttsppspva appappgngq gpqqsglqsg lknrhlsmia vggvigaglf vgsasgitaa
       61 gpgillsyal vgalvvfvmr mlgemaaanp tsgsfsayad ralgrwagfs igwlywffwv
      121 vvlaveatag aailtswvpa vpqwawaliv mvvltatnla svasfgefef wfagikvvai
      181 aafiaiggla ifgvlpgsdn aatgfanlts hggflpngps ailtgvlmvv fsfmgseivt
      241 laagesedpq ravtkatksv iwrvgifylg silvvvsllp wndpsiakkg syvaaldsig
      301 iphagqimnv ivltavlscl nsglytasrm afslgqrgda pkafartngr gvpqaailas
      361 vlfgfiavgf nylwpdtvfq fllnssgava lfvwlvicfs qlrmrgiilr enpdklivrm
      421 wlfpyltwvt iasisfvlvy mltddseggg rvqvllsvll avlvvgvslv rdrlgrgtae
      481 keavtsr
//
LOCUS       WP_457697622             825 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457697622
VERSION     WP_457697622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 825)
  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   3  (residues 1 to 825)
  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   4  (residues 1 to 825)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..825
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=88433
     Region          17..253
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          246..687
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          698..809
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mmsaenalpg dsdracdiak aatadlngqg riiawtraae rllgypagev lhrpaaella
       61 ipgdevrvas varwcragng wggsvaarhr dgrevqlalq vtpvldgtgh erwsvlamee
      121 wrvpgggvnq lmlepflaha pvgmavldtd lryvwvndvl erlipleqrl gkqvnevlpr
      181 leaaafedrm rrvlgtgspv mdyefrspty adphqersys asffglsdpq grriglwymv
      241 idvterwraq erlallndas arigstldvt rtaqeladva vpaladfvav dlldsvlrge
      301 epvpgpvdst ptmrrcgqqs vhegcpeagl avgetvqrsp sspiarcllk geslvepvld
      361 fatsawvted pvraaviref gfrsvmvapv qargitlgaa tffrsrrlgp fvaddvrlae
      421 elvaraavcv dnarrftrer taarvmqqnl lpheltggsa levaswyfpa dapsgvggdw
      481 fdviplsgar valvvgdvvg hginaaatmg rlrtavrtla nldlppdell arlddlvigl
      541 vkthradpaa daanpsvast fmgatclyav ydpvsrrcsv araghlppli vgpdgavdcp
      601 dlpagpplgl galpfeavel epaegslial ytnglietrd rdievglsrl sdalavpget
      661 lkdiganvvk alltgppsdd aalllartha ldaqqvaswe ltcdpavvgt arglagrqla
      721 ewgmddllft telivselvt nairhatapi tlrlirqdal icevsdasst sprlrhartt
      781 deggrglfiv aqltrrwgtr ytptgkiiwt eqsmpseaga ddead
//
LOCUS       WP_457697629             428 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457697629
VERSION     WP_457697629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..428
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45242
     Region          56..413
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 msnrdgaead rdaddarvla rlhtveeaae wigttldeqt tcaelarflc rhlcdaaave
       61 lltepgtgar tpspaaltrv ataglvkvle aqfpdegpgr pedaspslra ldeerlvtma
      121 avlpggrsae avaapllayg hrygvllalr aggsfaehet atvhylarlt atrlaharry
      181 aavqrtamdl qrallaepgr phpnlelatr ylpsgtsalv ggdwfetvrl hygrtllvmg
      241 dvmghgldaa vdmnayrshl ryvastdlpp hrvlrqldaa vaeeearrpa tcllarvdpa
      301 rglaafasag hlppavigpe gatalidvpv gpplgtgvgg yelvtravtp aetllmftdg
      361 lierrgedid aslsrlakmr lpagagveqv ldevllrldg lhaeddvail aarmrhhpga
      421 apagpves
//
LOCUS       WP_457697635             391 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697635
VERSION     WP_457697635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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..391
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..391
                     /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=43317
     Region          41..312
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mpaprssaqq gtdqlapagp patparhpav tsgepappap akqrdaffdn akylaivlva
       61 ighawepyyh gsrsaaslyl fvyafhmpaf tvisgyfsrs fdmrrdrlqr lvtgvavpfv
      121 vfqvtfalfr ywggdtesft lsmldpwflt wflaalfiwr ltaplwrivr wpvplalaia
      181 vgasaspdig teldlqrvlq flpffvlgmc lkaehfslvr rwpvriaavp vlagalvfty
      241 wavprmnnaw fyhtdsaekl gapwwigalm qpamfgcslv ltacflawvp grrmwctalg
      301 agtlygyllh gflakgsrww gwydagwvht pwgaavvtfl ggavvtllct ppvqrvfrfa
      361 mepkmrwafr aaeprtraaa astgkqpsap p
//
LOCUS       WP_457697637             254 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697637
VERSION     WP_457697637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27840
     Region          12..254
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mttfapdsla lnrklplwyq vsqslrasil grspeaplrl ptedslaahy gvsvltmrqa
       61 lkeletegli srhrrrgtfi epsgpggrrn ggvapvrllg svdaivaqqs gmstellehg
      121 ptavpselse yfpdlaevag frrlrsdeet geptnhacny vrpevaaaid padllrwpmt
      181 kvlrdavgvr isritdtvea rladpetarl lqvpllspil hytgvtyded grtvdvarih
      241 yrgdrfsftv tmda
//
LOCUS       WP_457697644             481 aa            linear   BCT 27-JAN-2026
DEFINITION  CitMHS family transporter [Streptomyces nigrescens].
ACCESSION   WP_457697644
VERSION     WP_457697644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Korithoski,B., Krastel,K. and Cvitkovitch,D.G.
  TITLE     Transport and metabolism of citrate by Streptococcus mutans
  JOURNAL   J Bacteriol 187 (13), 4451-4456 (2005)
   PUBMED   15968054
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Krom,B.P., Warner,J.B., Konings,W.N. and Lolkema,J.S.
  TITLE     Complementary metal ion specificity of the metal-citrate
            transporters CitM and CitH of Bacillus subtilis
  JOURNAL   J Bacteriol 182 (22), 6374-6381 (2000)
   PUBMED   11053381
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Boorsma,A., van der Rest,M.E., Lolkema,J.S. and Konings,W.N.
  TITLE     Secondary transporters for citrate and the Mg(2+)-citrate complex
            in Bacillus subtilis are homologous proteins
  JOURNAL   J Bacteriol 178 (21), 6216-6222 (1996)
   PUBMED   8892821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..481
                     /product="CitMHS family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0046942 - carboxylic acid transport
                     [Evidence IEA]"
                     /GO_process="GO:1905039 - carboxylic acid transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=50032
     Region          1..481
                     /region_name="CitM"
                     /note="Mg2+/citrate symporter [Energy production and
                     conversion]; COG2851"
                     /db_xref="CDD:442099"
ORIGIN      
        1 mltilgfvmi aaflvlimmk kmspmaalvl ipalfcvlvg qgahlgdyvl kgigdlapta
       61 amlmfaiiyf gvmidvglfd pivrgilkfc kadpvrvvvg tallaaivsl dgdgsttfmi
      121 tvsalyplyk rlkmslvvmt gvaatangvm ntlpwggpta raatalklda gdifvpmipa
      181 lavglvavfa layvlgrrer krlglltldd trpvtetlpe keteqvlvga gtggtggtpa
      241 gtprttggag tgsddepadg sgaqaddglq vldpqratlr pklywfnaal tlalltllil
      301 qtlpipvlfl lgaalaltin fphmkdqkar vaahaenvln vsgmvfaaav ftgvltgtgm
      361 vehmarwlvs gvpdalgphm givtgvlsip ltyfmsndgf yfgivpilae agaahgvapi
      421 eiaraslvgq alhmssplvp avyvlvgmak vefgdhtrft vkwaaltslv vlcagvlfgi
      481 i
//
LOCUS       WP_457697652             459 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697652
VERSION     WP_457697652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47735
     Region          22..435
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,265,268..269,272..274,277,305,309,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mdtapsaphg ntgtppsars rrrvataaal asavewydyf vfgiaaalvl gpaffpsgse
       61 aagvlasfat favgflarpv ggviagqlgd rhgrkpmlvl altvmglatt aigllpsydt
      121 iglaapillv vlrllqgiav gaqwggamlm ateyapegkr glygslvqlg vplgvmtans
      181 vfllagaftd ersfstwgwr lpflvgvlvl llaryihthv eetpefraae eklataeqaa
      241 aarrsplrei lrhhlgtvll aggsfavnta tfyilitgvl dyatrelemr rtsvlavsll
      301 vsltqlvlip aaaalsdrig rlrvyaagav glllwavpmf llidtaslvw lavgtfvgsc
      361 flsimygpqa alfaelftae mrytgaslgy qisailgggl apflmvllle asgtsmavsg
      421 yimalsvial vsiwllirra asasapgggg epgatkaqg
//
LOCUS       WP_457697654             215 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697654
VERSION     WP_457697654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22931
     Region          5..128
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          74..205
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 marprkplls rerivstala lidseglpal strrlaaelg vsgpslynhf ttkdeildav
       61 adtviakvdv stfetgtdwr tglldwarsy raalaahphi vpflaqgpgr rpaglkmada
      121 afgamveagw ppaqatrvca mvryfvagsa lgsfargfvd dpsaydpady phlgqahlla
      181 ehqrqvdega fetglralvd glalqhpdlv ppegr
//
LOCUS       WP_457697666             953 aa            linear   BCT 27-JAN-2026
DEFINITION  penicillin acylase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697666
VERSION     WP_457697666.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 953)
  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 12026968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..953
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=102619
     Region          136..942
                     /region_name="Penicil_amidase"
                     /note="Penicillin amidase; pfam01804"
                     /db_xref="CDD:460338"
ORIGIN      
        1 mrrrtgrlrt aaaaalfalg atllapppta aaaaapsptl dfaraggapi andycqgqcg
       61 dilppgatgn atlmeilgnk lfgthpehst dqlapygala sgyqsltddt lgtffndasf
      121 gvpadqvgkv ttprndvtit rdkktgvphi kgttrygtef gagyaagqdr lwlmdlfrhi
      181 grgeltsfag galanqgleq qfwpqapyte adlqaqvdri rdtngergel amqdaqayvd
      241 ginayreqsk ngryfpgeyv ltghvdaitn ageiqpfklt dlialasvvg glfgngggge
      301 vpsalallsa qqkygiekgt evwesfrern dpeaaktlhd gssfpyavkp drakgmalpd
      361 rgsvtpeplv fdrtgaatvk sgtpprdpvk apkkykkleg lfkdgvlpeg sfdptrrrgm
      421 snallvsgkh tasghpvavf gpqtgyfapq llmlqeiqgp gisargasfa gvgmyvqlgr
      481 gqdyswsats agqditdtfa velcnadgsa pakdstsyry rgacvpmekl ertnswkpti
      541 adptaagsyr mqvfrtkygt vthratldgk pvaytaqrst yrheadsiig fqmfndpsyv
      601 rdaksfqkaa ehigyafnwf yadsrdiayy nsglnpvrnp dvdpslpvka ddayewkgyd
      661 patnaaeytp saqhpqsvnq dyyiswnnkq akdydsagyg ngsvhrgnll ddrvraltkd
      721 ggvtrasltr amseaavtdl rgedvlpell rvvnskpvtd prlktavqql eawrkdgaqr
      781 retaagshty thpdavrlmd awwplmteav fkpglggdly dalranlgid espssghgpt
      841 gahagsafqy gwwsyadkdl ravlgdkvag plgrqycgng elsacrdtll atlqqasgkt
      901 aeqvypgdds ckagdqwcad aiihrtvggl thaaiswqnr ptyqqvvefp ahr
//
LOCUS       WP_457697672             425 aa            linear   BCT 27-JAN-2026
DEFINITION  exo-beta-N-acetylmuramidase NamZ family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697672
VERSION     WP_457697672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Muller,M., Calvert,M., Hottmann,I., Kluj,R.M., Teufel,T.,
            Balbuchta,K., Engelbrecht,A., Selim,K.A., Xu,Q., Borisova,M.,
            Titz,A. and Mayer,C.
  TITLE     The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the
            founding member of a family of exo-lytic peptidoglycan
            hexosaminidases
  JOURNAL   J Biol Chem 296, 100519 (2021)
   PUBMED   33684445
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..425
                     /product="exo-beta-N-acetylmuramidase NamZ family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0033922 - peptidoglycan
                     beta-N-acetylmuramidase activity [Evidence IEA]"
                     /calculated_mol_wt=46030
     Region          41..425
                     /region_name="YbbC"
                     /note="Uncharacterized conserved protein YbbC, DUF1343
                     family [Function unknown]; COG3876"
                     /db_xref="CDD:443084"
ORIGIN      
        1 malsrrvllg rlaatgaaga alaagagpar teqpahgggr rvhtgfdrla adgyrlldgr
       61 rvgivtnptg vtqelrhivd vmhaddrvrl tavfgpehgf rgtaqaggse gryddpatgl
      121 pvydtynksg kaltdiftas gvdtvvfdiq dvgarfytyi wtlydcmvaa vlagkrfvvl
      181 drpnpvtgrs atgpvldkay asfigrepia qahgmtvael allfngefvp qaagrpvele
      241 tvrmtgwhra dfydttrlpw vppspnmptp dtalvyagtc lfegtnlseg rgttrpfell
      301 gaddidrhwa aaateldlpg vhfreayfap tfskfqgkti ggvqlhlhdr aafdpvrtgi
      361 gllvtakrvw pgftwrpdhg idrltgsstv rtmidagagp deivaawqer lkgfrtvrrr
      421 ylryp
//
LOCUS       WP_457697656             383 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697656
VERSION     WP_457697656.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40218
     Region          1..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnlelsaeqt avrqlakdft dreitpyata wdraeqvdrg ivkklgdlgf lgltvpeeyg
       61 gsggdhlsyv lvteelgrgd ssvrgivsvs lglvaktvaa wgdeeqkraw lprltsgeav
      121 gcfgltepgt gsdaanlatr avrdgdtyvi dgakmfitng twadvvllfa rtgdapghqg
      181 isaflvpads pglerreihg klglrgqata elvldgvrvp agamlgpegk gfsvamsala
      241 kgrmsvaagc vgiaqaalda algyagereq fgkpiarhql vqelisdiav dvaaarlltw
      301 rvadlidrge pfvtaasqak lfaseaavra annalqvfgg ygyideypvg kllrdarvmt
      361 lyegtsqiqk lligraltgv saf
//
LOCUS       WP_457697670             443 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697670
VERSION     WP_457697670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46214
     Region          28..432
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(41..42,45..46,49,88,146..147,149..151,154,174,
                     177..178,181,264,267..268,271..273,276,304,308,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mssdataaqt tagvpaktdg tsggeslrrv avasfigtai efydfyiygt aaalvlnqaf
       61 fptldpvnat lasfstyava faarplgsvi fghfgdrvgr ksvlvaslll mglstafvgl
      121 lpgygtwgiw aplllialrf lqgiglggew ggaallaveh aprkrrglya afpqlgpsvg
      181 flaatgvfwl lssvlddaaf rswgwrvpfl lsfllvgvgl fvrlkisetp vftkvldaqe
      241 askvptvevl rrhprelllg aggmivaygl fytattycls yatgtlgisr ntmlglslva
      301 clflaagtwl aatrsdgagr rtlvlagcvl aavwglvlfp lldtgqpvli algiggalfc
      361 mgvvygpmga ylpelfsarv rysgaslayn lggvlggava plaatrlqsa ygsasvgwyv
      421 samavvsllc vlalpetrer dlv
//
LOCUS       WP_457697646             298 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457697646
VERSION     WP_457697646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30408
     Region          8..288
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msnaddprtp vtvlglgamg salagafvra ghpttvwnrt pgkadalvar gavradtvte
       61 avaasplviv cvvdyavahe ilepagpqls grvlvnltsd tperarsaaa waagqgidyl
      121 dgsvmvptpd vgqpgatlly sgsrqafety eetlkvlggr aaylgddham aavydlalla
      181 ffysamaglv hafalagaeg vpakefvpft eaiadilppl aagmaqdldl gvlrgdqdni
      241 vmeaagmahi ieasvdrgin tdvlaavkgl adrtiaagdg kagflsiige mrkpsakg
//
LOCUS       WP_457697673             256 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457697673
VERSION     WP_457697673.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26556
     Region          24..210
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maavrdktvv vtgagggiga alarrfaaeg arvvvndlde akakrtadei gavavagdas
       61 tvvpaareal gggidifcan agvgtgggpe apeedwalaw dvnvmahvra arelvpewle
      121 rgsgrfistv saaglltmva aapysvtkhg ayafaewlsl tyrhrgidvh aicpqgvrtd
      181 mlaatgtagd lvltptavep edvaealfaa maegrflvlp hpevadyyta raaepdrwig
      241 gmnhlqrkle qaegrs
//
LOCUS       WP_457697677             192 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697677
VERSION     WP_457697677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20424
     Region          1..182
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mgaiapsgpr lgraltryvi pspgsaravl evgpgtgavt rhiagslgql dtldlveanp
       61 rfvdllqgay ggdprlqfrt glvqdhdldt ydtiicglpf anfdapttad ifdrllgalk
      121 pggtlsffgy vggarmrrtf tgraarehvl dgqntlrhil nrhtfrtelv lgnlpparvh
      181 hlapvstpvq av
//
LOCUS       WP_457697681             350 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697681
VERSION     WP_457697681.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37807
     Region          40..290
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(45,48..50,53,64,66,98,117..120,218,220,222..223,225,
                     236..237,240,255..256,259)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(45,49,53,64,66,98,117..120,218,222..223,225,
                     236..237)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(48..50,218,220,223,237,240,255..256,259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mskgtpppqa qdredppgld ltrlrehldr erpglaggpl raqlieggrs nltyrvtdga
       61 aswvvrrppl ghvlatahdm qrehrvisal hetpvpvpet lllcadesvi gapfyvmelv
      121 egtpyrtagq ltplgpertr avvlslvdtl velhavdpea vglgdfgrpd gflerqlrrw
      181 gkqltasknr elpgidelhe alsralpasp apavvhgdyr ldnvligadd tlkavldwem
      241 stlgdpltdl gllamystdl nlpgspvstt sgapghpapa elieryaars grdtsaiawy
      301 tafawfklav ilegihyrft lgqtvgagfd rigelvpvfi drglttlkeg
//
LOCUS       WP_457697683             352 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697683
VERSION     WP_457697683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36640
     Region          63..266
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(122,124,126..127,200..201,219,256)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(122,124,126,200,219,256)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 mddataprra artsaapsaa rttgpgvtgp dameppgagt pagpppaagp pvpepyltel
       61 aagvhafiqp dggwclnnag fvtdgdatlv vdtaaterra rllrqriaes gapaprtvvn
      121 thhhgdhtyg ngvfapeatv ighascrrel laaghqlhav wpeveygdir ltppevtytd
      181 eltlhvgdie vrlihpgvah ttgdtlvwlp rerivfagdl vfhggtpflf mgsltgslra
      241 lrtlraldav tvvpghgpvt gpevydgier ylrfvgrlaq egraagrtpl etaqeadlgp
      301 faglaeserl vanlhrayae lagaapgvpl dpmagfgdma vmnggvpmac ha
//
LOCUS       WP_457697688             177 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697688
VERSION     WP_457697688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 177)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20218
     Region          14..170
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04697"
                     /db_xref="CDD:467578"
ORIGIN      
        1 mtdqqplntd evldvvdend qvvgqaprge tyarrmrtrc afvlvrdaee rifvhrrtpr
       61 klvfpghydm fvggvvgtge tydqaalrea eeelgvqgla ppeplfkfly etaehawwsa
      121 vyqvrctlpv apqeseidws aflpeeelir rldewpwtpd glaayrqvla rreagei
//
LOCUS       WP_457697700             433 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697700
VERSION     WP_457697700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44144
     Region          11..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(21..22,25..26,29,62,117..118,120..122,125,145,
                     148..149,152,230,233..234,237..239,242,266,270,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msgllrrhrd frllwcgeta gkfgaavsnv amplvavstl hastfavgli sacswlpwll
       61 iglpvgvwvd rlrrrplmlt aaalsmvlfa avpvlarygg ldlglltava lltgaaavlf
      121 qtaysaylpt llapadqaeg naklhgsasa aqiagqgasg liaqlagavn glfahaatfl
      181 vallcllgir yreprpaare gtprsltgev aeglrlvagd rwfrtltlfg atsnlalmgy
      241 qsltavflvr evglapgavg gllalagtgg iagafvvrrt agrlgtaram llfelcvpca
      301 allipltspg agtllyvags fgvsagvvag nilkvsfqqs ycpppllgrl vasssflnyg
      361 tlplgallgg algsalgvrt amwiltagvp laalillfsp vrtvrdlpvh paegergepg
      421 pgaaerdgas arg
//
LOCUS       WP_457697702             381 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457697702
VERSION     WP_457697702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /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=38757
     Region          136..369
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtdflvival aalgaalagl laapavralr rrsvalslfa vaalavaama agtvavaqam
       61 flsghdlgvv mavvavsgvv slaaallfgr riaagsrela rsartvgseg gfvapaeppt
      121 aelaalsral eetsgrlaea rereraldas rreliagish dlrtplaglr amaealedgv
      181 aedtaryhar mrievdrlaa mvddlfelsr iqagalaltl srvsvydlvd ealagagpla
      241 rasgvrlvdg gvvplpvrvd aqqitrvlgn llvnairatp adgtvavsar paegrvvlav
      301 edgcggippe dlarvfdtgw rggaartpra dgkggaglgl aivrgiveah egratvrntg
      361 agcrfevelp aaeapaeppt a
//
LOCUS       WP_457697704             265 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457697704
VERSION     WP_457697704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 265)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28441
     Region          20..229
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mhpatppsvp ppapshgppr rvlvveddpt vaevvtgyls ragyttahaa dgfaaldraa
       61 dfrphlvvld lmlpgidgle vcrrlrrgdg pavpvvmlta rgeeadrilg lelgaddyvt
      121 kpfsprelvl rigsvlrrae sappaaaraa vlragelsad pggrradrag ralsltaref
      181 dllvflmrhp grvfsreell hrvwgweigd lstvtvhvrr lrekieadpa aprlvttvwg
      241 agyrfdpvgd eppeddplpg ggpls
//
LOCUS       WP_457697710             541 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457697710
VERSION     WP_457697710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..541
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58765
     Region          27..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msmtptpasa asivctglgf awpdgspvle dfplvvgpgr tglvglngag kstllklmag
       61 elaptagsvk vagevgylpq hapldtalrv dqalgiaaar aalhaieggd aseehftaig
      121 ddwdveerar atldqlglpg idldrtigev sggesvllrl aalllrrpdv llldeptnnl
      181 draarqrlyt avtgwsgvlv vvshdrelle rvdriadlrd gevhwyggnf sayeralave
      241 qeaaermlrv aeadvqrqkr elsdahikla rrfrygnkmn ankrepkivm nerkreaqvs
      301 agkhrimhte rlkeardrld eaaeavrddd eiridlphta vppgravltl ralqarygvh
      361 ahlevrgper ialtghngsg kttllrtvag eippvagtae thvpyrflpq rlevldpalt
      421 vvenvarfap datnnrirar larflfkgar adqragtlsg gerfraslaa lmlaepapql
      481 llldeptnnl dlasvrrlvt alefyegall vvshdltflr dlgitrwlst eggeltdiap
      541 l
//
LOCUS       WP_457697712             141 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697712
VERSION     WP_457697712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 141)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..141
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=14890
     Region          1..121
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mttrgpkvsc vfvchdgagr vllarrsaga rdepgtwdcg agalefgetf eaavarevhe
       61 eygvrplgie qigvrnvlrg dpvdshwvav vfavrvapde vtigephkfd aldwfapdal
      121 pvplhsqcge tlglfgagar g
//
LOCUS       WP_457697714             224 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697714
VERSION     WP_457697714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12008676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24675
     Region          2..185
                     /region_name="Hydrolase"
                     /note="haloacid dehalogenase-like hydrolase; pfam00702"
                     /db_xref="CDD:459910"
     Region          96..205
                     /region_name="HAD_like"
                     /note="Haloacid Dehalogenase-like Hydrolases; cl21460"
                     /db_xref="CDD:473868"
ORIGIN      
        1 mlifdaddtl wennviferv ideflewmth pgldragvra vldgieaana ltlgygskvf
       61 lhslgecvar lrgraataee sariagwaaa fagdrvelip gvaetlaelg rrhelllltk
      121 gdteeqerkv aasgltrhfr gvhivaekni atyeelkray dlvpdstwmi gnspksdilp
      181 arsaglnavf iphdhtwvle hseldpaddk vlrlsafgdl lrhf
//
LOCUS       WP_457697698             648 aa            linear   BCT 27-JAN-2026
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Streptomyces sp. 900105755].
ACCESSION   WP_457697698
VERSION     WP_457697698.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Jenkins,J., Mayans,O. and Pickersgill,R.
  TITLE     Structure and evolution of parallel beta-helix proteins
  JOURNAL   J Struct Biol 122 (1-2), 236-246 (1998)
   PUBMED   9724625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 1002750
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..648
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=69384
     Region          <363..579
                     /region_name="NosD"
                     /note="Nitrous oxide reductase accessory protein NosD,
                     contains tandem CASH domains [Inorganic ion transport and
                     metabolism]; COG3420"
                     /db_xref="CDD:442646"
ORIGIN      
        1 mrtargsaaa alavaaalas tagapaphhp pttelyvapw gddhgpgtld hpfatparaq
       61 ravravaprm tsdvtvnlra gtyrltsplr ltsadsgrng hrvvyqaygy gtaqqepvtl
      121 sggrpvtgwr hapgrpgvwq advgsletrq fyvdghrapr aslgaplpge ltptatgytt
      181 tsrlplswhr padlevvyry dyaegrcgvk avsesattpa rttitmdqpc wrlarslyga
      241 dalarthdve napdfltrag twyldrsrpg hhtllyrpra gedmtrteai tptlqtllsg
      301 tgtapsrplh dltlrgltfa hatwlapnep agfaaawsmy mrpgrggdit artvpgnvtf
      361 ryadritltg nrfvhlgaqg laltagtsht tvtgnvltdi sdggitlgvl ppatrgtnag
      421 nritdnwihh igaeyraasa vwnsatqdtl iahnqvdhvp ytgilsgpse dlrgltrrtr
      481 ilgnrvfatn rlladgggiy lrgdqgpsya dgalvarnav tdspgavwni giytddtsnr
      541 vtvrdnvvhd yvasiggcse nwgnrpvrni rytgnfwddk vpswlarrpy pgawppapdc
      601 gdpqhlhfts ntlltpttpc pthptctait aaagprppyr ghlgpgpr
//
LOCUS       WP_457697716             253 aa            linear   BCT 27-JAN-2026
DEFINITION  Bax inhibitor-1/YccA family protein [Streptomyces nigrescens].
ACCESSION   WP_457697716
VERSION     WP_457697716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Guo,G., Xu,M., Chang,Y., Luyten,T., Seitaj,B., Liu,W., Zhu,P.,
            Bultynck,G., Shi,L., Quick,M. and Liu,Q.
  TITLE     Ion and pH Sensitivity of a TMBIM Ca2+ Channel
  JOURNAL   Structure 27 (6), 1013-1021 (2019)
   PUBMED   30930064
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Watanabe,N. and Lam,E.
  TITLE     Bax Inhibitor-1, a conserved cell death suppressor, is a key
            molecular switch downstream from a variety of biotic and abiotic
            stress signals in plants
  JOURNAL   Int J Mol Sci 10 (7), 3149-3167 (2009)
   PUBMED   19742129
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Zhou,J., Zhu,T., Hu,C., Li,H., Chen,G., Xu,G., Wang,S., Zhou,J. and
            Ma,D.
  TITLE     Comparative genomics and function analysis on BI1 family
  JOURNAL   Comput Biol Chem 32 (3), 159-162 (2008)
   PUBMED   18440869
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Reimers,K., Choi,C.Y., Bucan,V. and Vogt,P.M.
  TITLE     The Bax Inhibitor-1 (BI-1) family in apoptosis and tumorigenesis
  JOURNAL   Curr Mol Med 8 (2), 148-156 (2008)
   PUBMED   18336295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="Bax inhibitor-1/YccA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26277
     Region          4..251
                     /region_name="COG4760"
                     /note="Uncharacterized membrane protein, YccA/Bax
                     inhibitor family [Function unknown]"
                     /db_xref="CDD:443793"
ORIGIN      
        1 mpttsnpair nlltldgavs pagpagsgga spaaatdrpi tlddivvktl avfavlvasa
       61 fltlflelgf lalpalfagl glgiflslrp rpsaapallf aavqgivlge atqffdalhp
      121 gvgtqavlgt gcifagtlaa yhtrvvrvsa kvtrwavgag lgllvlllae lvaswgfgad
      181 lglrdggpla lavsvvaiaa asfffllefe aanrflqsga shrwawyvaf glamtlvwly
      241 leilrllsyl rww
//
LOCUS       WP_457697726             175 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697726
VERSION     WP_457697726.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18232
     Region          47..>127
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mlvhsppqeg lipgqeppyg seiplagtta pgipglerls avalcalpte eraaakarsf
       61 traqlctwgv gedvtyeaci lvselvtnal lhsgadgfcv glarsgrqlc ievtdngsgr
      121 spprlppttw rnaavaspwr tlsprasgct apppepapgr csrpwtarsq pdlcl
//
LOCUS       WP_457697730              77 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457697730
VERSION     WP_457697730.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..77
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=7024
     Region          26..76
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mikkvvaaaa vaggvvlaga glavadsgaq gaalnspgav sgnsiqvpvq vpvnacsnti
       61 svigllnpaf gagcvnk
//
LOCUS       WP_457697737             396 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697737
VERSION     WP_457697737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..396
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43753
     Region          6..387
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
ORIGIN      
        1 msstdaapar grasaidgfr glaalstvaf hvwqqyfryd tqgshppvdn pvlgaafsle
       61 vidlffvlsa ylltlsyara aldgrsirpa rlflfrrair ilplyflavl vvwasrnptl
      121 pgnwrdlveh ltfthvfdqq rifytlgptw slslevlfyl vlvalgplav racrplrrrr
      181 trvavcaagc lflyaaplaw iavahyrfgv phtdwvvyfg pqarfggfaa gmglavltaa
      241 lgdrgrlgpr talplaglal aglfalslds apenftftfy hpiasalwvv lifstlhvrq
      301 qtfwqgmlra rwltavglvs yslfiwhepv mlqlhnagll pagqsgfpla llivflvavp
      361 vaaasywlie ypasllgrlk dhrgsprefy pepatr
//
LOCUS       WP_457697739             242 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697739
VERSION     WP_457697739.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26703
     Region          41..237
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mcrtalppag rgrpalycsr scqakayrrr kqppvpaaer pavgdpsgkr lriaealwri
       61 aaerglhaas lrevaaeagv slrsvqyhfe skhrllvdal qllhaeneri arsrvrfdat
      121 eprgllravl eeflpvdaqr atalrvfaay yarsltdpal akvflpaeqp leqlvaelia
      181 aaqadgrtap gldpwreadl lvagavglgg dvlhdrrtld evrrtldyhl dkifagdrrt
      241 rr
//
LOCUS       WP_457697764             186 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697764
VERSION     WP_457697764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..186
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20785
     Region          14..>155
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mhdrrpqphg idtytirpae pqdcdgarsv mldtfyrefd ygyvpawhpd vidiqgtyld
       61 nprhqlival adgevvattg llsrgpahpp hprwlaerya saaqlvrvyv rpehrrhgla
      121 ramvrracef aaatagydcv ylhtnvnipg aqdfwnsiak evfdarttge hgagfstvhf
      181 eiplpd
//
LOCUS       WP_457697768             251 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697768
VERSION     WP_457697768.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26530
     Region          107..237
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mriaadaata iakalagrpd tsyvhllsgg teiscsvqtp tadesaalll hklprtsrit
       61 svsahlllgh yalpnnwagp arltpeqaal ltppptddsd islgpadrsl fdllsqdgra
      121 sytelaaatg wsestvrrrl thlrqagvlt flvdispavl gfrsearlwm avrpsrltav
      181 aaamahhpev slvaqttgpt nllaavncrs sldlarylte riasldaiht ietapvlrtv
      241 kragsllplg r
//
LOCUS       WP_457697774             231 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697774
VERSION     WP_457697774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..231
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24577
     Region          20..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meqgtteqep varawvpaqp gpaaprrhsv rgqvlaalrh alvggeltpg evysapalae
       61 rygvsatpvr eamqqlageg avevvpnrgf rvaecssrdl aelaevraml evpaiirlar
      121 alaperweel rplaaagvaa aargdrvgya eadhafhval msltgnrrlt evagdllrra
      181 qwpaggsrlr tadlladase htalldalva qeyavveria rehvsaarhp h
//
LOCUS       WP_457697778             559 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457697778
VERSION     WP_457697778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..559
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=59782
     Region          6..121
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          257..558
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrlralldtp slglrllgge deldrtvrgv mttdlrdpsr ylsggelvlt glawrraped
       61 serfvrilaa agvaglaage aelgsvpddl vaacvrhrlp lfsvvedvsf asitehvvrq
      121 vsgeragdla avvdrhrrlm tsgptgggpe vvldllgsdl dlrawvlspt grqiagstla
      181 gagpelsagt aarlagehla aarsgrrgph rvtieaagap agatfslfpi rhegrdlrqt
      241 llsdwllave adagdwpeer ldllhgvtql iaverdrrda artvrrrlaq evlelvqtga
      301 ppaeiaarlr vaapvllpgl gtaphwqivv arvewedgdv pggpvaqsll eemlvdpgaf
      361 gpepsdriav ahtgdeaval vplpvpdepg dasaaglhad ellsvvqepl grgladdgrl
      421 tvgvsasvhs aeglrgalee arharrvaaa rpgrvcaagh eelashvlll pfvpddvrra
      481 ftarlldplr dydrrhrael iptleafldc dgswtrcagr lhlhvntlry rvgrieqltg
      541 rdlsrledkl dfflalrms
//
LOCUS       WP_457697780             295 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD binding domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697780
VERSION     WP_457697780.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /product="FAD binding domain-containing protein"
                     /EC_number="1.-.-.-"
                     /GO_component="GO:1990204 - oxidoreductase complex
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31565
     Region          1..283
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mdflrpaswe ealaakaehp tavpiaggtd vmveinfdhr rpeylldlnr igdlsewevg
       61 eetvrlgasv pytqimehlr aelpglalas htvaspqirn rggvggnlgt aspagdahpa
      121 llasggevev esvrgrrmip vddfyvgvkr namepdelir svhlpkadgp qqfskvgtrn
      181 amviavcafg ialhpgsrtv rtgigsaapt pvrareaeef ltaaldeggf wesgspipps
      241 vakqfaqlas gacnpiddvr gsaryrrhav gimarrtlgw twesyrgner saqca
//
LOCUS       WP_457697781             195 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697781
VERSION     WP_457697781.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=20382
     Region          1..188
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mrvtftvngr rqeaddvweg esllyvlrer mglpgsknac eqgecgsctv rldgvpvcsc
       61 lvaagqvegr evvtveglad fakqraeggc asgacgtslq aaqqwqakgt dsqtgeggel
      121 spiqqafida gavqcgfctp gllvaademl ehnpqptdad irealsgnlc rctgyekild
      181 avrlaaarqg qeeav
//
LOCUS       WP_457697783             793 aa            linear   BCT 27-JAN-2026
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Streptomyces nigrescens].
ACCESSION   WP_457697783
VERSION     WP_457697783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..793
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=84154
     Region          15..790
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mgttgtptki tqgsqtkggi gestlrpdgt lkvtgefays sdmwhedmlw gftlrstvah
       61 aeivsidtse alaqsgvyav ltyddlptsi knygleiqdt pvlahgkvrh hgepvalvaa
      121 dhpetarraa akikieyrel pvvtdeasat adgapllheg rddhhaghva hpnivhrqpi
      181 vrgdagraak kadvivsgey vfgmqdqafl gpesglavpa edggvdlyia tqwlhsdlrq
      241 iapvlglpee kvrmtlsgvg gafggredls mqihacllal rtnkpvkivy nrfesffghv
      301 hrhpaklwye hgatkdgkit hmkcrivldg gayasaspav vgnaaslavg pyviddveie
      361 avalytnnpp cgamrgfgav qacfayeaqm dklaaklgld pvelrqlnam eqgtimptgq
      421 pvdspapvae ilrrvksrpl pperqwesse gadvrqlpgg lsntthgegv vrgvgyavgi
      481 knvgfsegfd dystakvrme vvggepvatv htamaevgqg gvtvhaqiar telgvtqvti
      541 hpadtqvgsa gstsasrqty vtggavkhsc elvrekvlei grrkmgtyhp awataellle
      601 ggkvvtdgge vladlvdvle geaveieaew rhrpteafdl vtgqgnghvq ysfaahravv
      661 evdtelglvk vielavaqdv gkalnplsvv gqiqggttqg lgvavmeeil vdpktakvrn
      721 psftdylipt ildtptipvd vleladehap yglrgigeap tlsstpavla airnatglel
      781 nktpvrpehl tgt
//
LOCUS       WP_457697785             485 aa            linear   BCT 27-JAN-2026
DEFINITION  NCS2 family permease [Streptomyces nigrescens].
ACCESSION   WP_457697785
VERSION     WP_457697785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..485
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49926
     Region          25..478
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mtqqsteprt taedagdgsr qpagrswldr yfhisdrgst vaqevrggit tfmamcyill
       61 lnplilstpd vekhtlahag vvtatalaaa vstllmgfig kvplalaagl nvsaaltaqv
      121 vpnmtwpqam gmcvvygvvi cvlvvtglre mimnaiplal khaitmgigm fvallglvka
      181 gfvgkgeggp vtlglngqls gwpvlffcvt lllifmlqar kvpgailigi vagsvlsiav
      241 triggltakd wggtppelng gavampdfgl fghvefggwg sigalsvgmi vftlvlagff
      301 damatiigvg teakladdkg rmpglskalf vdgaggaigg vtgssgqtvf iesasgvgeg
      361 artglssvit glffaaclff tpltqlvpaq vasaalvvig smmmsaaghv dwrdrsvsip
      421 vfltvalmpf tysitagvga gviayaaika aqgkwrevgg fmwvltavfv vyfslhpieq
      481 wlgvk
//
LOCUS       WP_457697789              97 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697789
VERSION     WP_457697789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..97
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10458
     Region          11..>77
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 midatalsek pvltgarirl aplsirhaaa fhtacqdpdt rrltgthydf tlaelqtwca
       61 gsagsadrld laiedrerlr agqrpgrpap plsrspr
//
LOCUS       WP_457697791             291 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697791
VERSION     WP_457697791.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 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   Rosinski,J.A. 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 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 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /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=30387
     Region          103..279
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          227..279
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrldpganet vdvraalsrl rragglpvaf ggllagagry rinelagtet avlrgldivq
       61 gnglggkava lsrplavtdy sassvishey daavaaeglr svlavpvivr rrvrgvlyga
      121 lrrpvrlgdr plsaameaar eleqalllqd eaarllsval pqalheqgga pstagdparw
      181 eevreahgel rglaqrvadp llrqelltac grlaaassrr pgtegaapvl sprevdvlac
      241 vasgatnaev aerlglrpet vksylrsamr klgahtrlqa vvaarragal p
//
LOCUS       WP_457697797             126 aa            linear   BCT 27-JAN-2026
DEFINITION  MmcQ/YjbR family DNA-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697797
VERSION     WP_457697797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Singarapu,K.K., Liu,G., Xiao,R., Bertonati,C., Honig,B.,
            Montelione,G.T. and Szyperski,T.
  TITLE     NMR structure of protein yjbR from Escherichia coli reveals
            'double-wing' DNA binding motif
  JOURNAL   Proteins 67 (2), 501-504 (2007)
   PUBMED   17266124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="MmcQ/YjbR family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13842
     Region          3..115
                     /region_name="MmcQ"
                     /note="Predicted DNA-binding protein with #double-wing#
                     structural motif, MmcQ/YjbR family [Transcription];
                     COG2315"
                     /db_xref="CDD:441889"
ORIGIN      
        1 midaqalrav cldfngaaee fpfprhpdvs afkvggkifa lttltdaplt vslkcepela
       61 erlraahpev vpgyhlnkrh wntvslggdl pdrlvldmie dsydlvvasl pkaqrllldw
      121 pgerra
//
LOCUS       WP_457697799             192 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457697799
VERSION     WP_457697799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20807
     Region          14..151
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 madetnnarg tagyllemgm lkrakrsgww iagvkdpesi aehsfrvgii gavlammega
       61 dpakvalmcl fhdtqetrlg diphigrryl eaasnekvta dqvsaahpav asgvqrvvee
      121 yengdsmevv vahdadklec lvqaieyreq gcsivqnwid tslaslktas aqalaeaaln
      181 mssiewqqty lr
//
LOCUS       WP_457697817             367 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697817
VERSION     WP_457697817.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..367
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39919
     Region          1..>67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maigdlirdl rrarglsqgg ladaindayr ttltreyvsk wernkvaptr vylarlssvl
       61 dvplavlege vnrrrfltdv aataiapvva sdllttgfaa rlrggpstdd weeklatygt
      121 dymslganni qrrvagelvv vqqqldeprl wsvasrlmtl yaktfpgsdg skavgwyrma
      181 aqaadesgde earvwvrgra aialgyegas lgiadiladq amsisrrpsl gllnaimgka
      241 haaairgdha tarkllndgr rvfdsaasye qtsdyavpyw rmnvftslla arlgdektav
      301 daqdaarrel paelprfath lemhrglmla rsgdkvggva yaraamealp pekhsltlrm
      361 lmneiea
//
LOCUS       WP_457697823             293 aa            linear   BCT 27-JAN-2026
DEFINITION  radical SAM/SPASM domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697823
VERSION     WP_457697823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Grell,T.A., Goldman,P.J. and Drennan,C.L.
  TITLE     SPASM and twitch domains in S-adenosylmethionine (SAM) radical
            enzymes
  JOURNAL   J Biol Chem 290 (7), 3964-3971 (2015)
   PUBMED   25477505
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Frey,P.A., Hegeman,A.D. and Ruzicka,F.J.
  TITLE     The Radical SAM Superfamily
  JOURNAL   Crit Rev Biochem Mol Biol 43 (1), 63-88 (2008)
   PUBMED   18307109
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Booker,S.J., Cicchillo,R.M. and Grove,T.L.
  TITLE     Self-sacrifice in radical S-adenosylmethionine proteins
  JOURNAL   Curr Opin Chem Biol 11 (5), 543-552 (2007)
   PUBMED   17936058
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Sofia,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and
            Miller,N.E.
  TITLE     Radical SAM, a novel protein superfamily linking unresolved steps
            in familiar biosynthetic pathways with radical mechanisms:
            functional characterization using new analysis and information
            visualization methods
  JOURNAL   Nucleic Acids Res 29 (5), 1097-1106 (2001)
   PUBMED   11222759
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15182508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="radical SAM/SPASM domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30939
     Region          20..163
                     /region_name="SkfB"
                     /note="Radical SAM superfamily maturase, SkfB/NifB/PqqE
                     family [Cell cycle control, cell division, chromosome
                     partitioning, Coenzyme transport and metabolism]; COG0535"
                     /db_xref="CDD:440301"
     Region          211..>247
                     /region_name="SPASM"
                     /note="Iron-sulfur cluster-binding SPASM domain; cl41754"
                     /db_xref="CDD:477760"
ORIGIN      
        1 mstissesal ptaqqtttkl lwldltrkcq lackqcyngs gpdgphgtmt redwlnvldq
       61 aaacgvkkiq figgeptmhp dfavlvdhal nvglhvevys nlvhvsnecw dvfqrnglsl
      121 atsyysdqaa qhnevtgrps hartrtnier avglgiplrv giidggegqr vaearsdleg
      181 lgvtrigvdh vrpfgrgaqe qapdmanlcg rcgtgraais ptgdvspcvf sgwmgvgnvk
      241 ttplatilsg admkrantsi raatmsggdd dddggnddec spgfpgsect prn
//
LOCUS       WP_457697829             125 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697829
VERSION     WP_457697829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..125
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13349
     Region          8..120
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mqrkvrhadl kavgevrrel rqllsrwtvp gggelaevat lltselvtna lvhaeggavv
       61 tarvsdrlrv evrdfvpgrp eprapttdgt sgrglmlvrs ladawgirte slgksvwfel
      121 gggpa
//
LOCUS       WP_457697832             485 aa            linear   BCT 27-JAN-2026
DEFINITION  catalase [Streptomyces nigrescens].
ACCESSION   WP_457697832
VERSION     WP_457697832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..485
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54113
     Region          2..480
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mtarflttea gapvadnqns atagvggpiv lqdqhllekl arfnreripe rvvhargsga
       61 ygyfevtddv tgfthagfld tvgkrtetfi rfstvadnlg gpdaardprg falkfhteeg
      121 nydlvgnntp vffikdpikf pdfihsqkrd pftgkqepdn vwdfwahape athqitwlmg
      181 drgipasyrh mngygshtyq wtnaegeaff vkyhfktnqg ircldaeqga elsgkdpnsh
      241 qtdllqsier gvypswtlyv qimpaaeaan yrfnpfdltk vwphsdyplq rvgrlvldrn
      301 pdnvfaeveq safspnnfvp gigpspdkml qgrlfayada hryrlgvnht qlpvnapkat
      361 taanygrdgl matngydrya knyepnsysg pvqtgrplsa plpvnghvgt heapahtkdd
      421 dffqagelyr lmsqdekkrl vnniagglsq vsrddviekn lahfhaadpd ygkrvearvr
      481 elred
//
LOCUS       WP_457697839             525 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457697839
VERSION     WP_457697839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 525)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  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 525)
  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 525)
  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..525
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..525
                     /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=54732
     Region          8..498
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnaavstgif ggfmvltvvl gllavrgkga gggldgwsvg grslgpvfiw vlmagesyts
       61 fsylgaagwg ynfgapvlyv laymscgyal gyvvgpmlwa yarrhglvgi tdmiahryra
      121 pwlgaavall atvcllpyiq lqitgmgvvv stisygaisi nwayflgfav ttgfvvisgl
      181 rgsawvsvlk dvlvigtlgf laiyvplhyf dgygpfldki vaekpqwltf pghasgglgq
      241 vwfvtttlvn sltvvifptt vagylgarna ealrsnalyl pfynvllfvp mllgmaalfv
      301 vpgltgadsn lalfkmvvds lpawavglvg vaaalssivp mavfmlvigt mwgrsvlgai
      361 prlhkgaaga asgdgggeat ggrqklwsql vvvvagalal lltytapdtl vrlslisyeg
      421 maqlvpmlll glvwrrltlh aavsglvagf tlvcvlvfgg hdpvrgmnag ivglavnvav
      481 alvvtwlgpr atderpdaev lalddefprd gvpsqggris ppvss
//
LOCUS       WP_457697845             436 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457697845
VERSION     WP_457697845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..436
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=45508
     Region          223..427
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(230,271,313,407,410)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(230,407,410)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(230,271,313)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mkksvgysll aglaavvvli staifvgfgg esggpgsssh kprdpaapav sgqwvgtwsa
       61 aaaaaepgtl ngyagmsirn vvhtsvggsg vriqlsnlyg trplvvshas lalaaapsnp
      121 taatgtmrrl afggkpavti paggavtsdp trlkvpgdad llvttyspsp sgpatyhpya
      181 rqtsylargd raedatgaay teqspywryl tgvdvwstea rgavvaigds itdgitstag
      241 anhrwtdfla arlrnepgap rygvlnqgis gnrllvngsr fspnngpsvl srlerdalsr
      301 tgvkavivei glndlfkspr qldpqkivag mreivreaha rglrvtgstl tpfgghrgys
      361 tllnsvreqv nriirsgtvy devvdfdkal rdpsapvrlr paydsgdhlh psdegframa
      421 navnlahlkq sapaal
//
LOCUS       WP_457697848             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457697848
VERSION     WP_457697848.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 342)
  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 342)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=37274
     Region          12..325
                     /region_name="COG4586"
                     /note="ABC-type uncharacterized transport system, ATPase
                     component [General function prediction only]"
                     /db_xref="CDD:443643"
ORIGIN      
        1 mvsgaaaaeq lievdgvekv fsvrrkagrl rrvrqevrav dgisfrvprg emvgyigpng
       61 agksttikml tgilvpsggr lrvagidpar ertrlarrig vvfgqrttlw wdlplkdsye
      121 lvrrmyrvpd sayranlerc velldlgpll tvpvrqlslg qrmrgdiaaa llhdpevlyl
      181 deptigldvi skakvreflr evnaergttv lltthdltdi eqlcrrvmvi dhghlvydgg
      241 ldglraagdg ertlvvdlar elppiegvpg artvrvdgpr qwlafpasqs aaplvaavae
      301 ryplvdlsvr epdietliae lyasggkrwd vagnggkagd al
//
LOCUS       WP_457697852             732 aa            linear   BCT 27-JAN-2026
DEFINITION  transglycosylase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697852
VERSION     WP_457697852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..732
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=78046
     Region          1..676
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msgqrtgwrr viptwrtvlg tvllflllvv ggmiagyllv gippansaak aqsniylysd
       61 gselahdgei nrqnvtlsqi prpvqqavla aedrdfyses avdpsamvra awntltgkgk
      121 qsgstitqqy vknyylgqeq tltrkakeff iaikldrevs kdnilegyln ssyygrnayg
      181 iqaaarsyyg rdaealttaq gaylasllna psayditahp enrqrvlarw nyvldgmvtk
      241 kwldpaerae lefpttkpak pspglsgqrg ylveavknyl tghhildedt lrgggyritt
      301 tigkkhqnaf vkavntrvmd rlddsrkvdr yvraggasid pasgrvvaly ggidyakqyv
      361 ngatrndyqv gstfkpivfa savqhrsttq dgtritpntv ydgtnkrmtv shgrstgfap
      421 aneddrsygp itvteatdks vnavyaqmgi dvgpakvkat avalgipadt pslassqgav
      481 slgtatpsvl nmaqayatla dhgtrrpytl vdkvtksdee ielpereeta avprtaadtt
      541 tailrgvvdg gtgtaargag rpaagktgta eedkaawfag ytpelatvva vlgqnpetaa
      601 qeplygaggl srvnggdypa qiwadytaaa lngrpvrgfd lrleagaeps spepsgsdsl
      661 spgasgtptt gptgsptvpv pptvaptrpt vepptptlpt epgpttpptn dfptvqpqsd
      721 elerqmqwrw dg
//
LOCUS       WP_457697850             265 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697850
VERSION     WP_457697850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28106
     Region          2..265
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mvyaavaags frryatyria tvagvftntv fgfivaytyi alwderphlg gydqaqaltf
       61 vwtaqallat aalmggggld elqerirtgd iavdlyrpad lqlwwlatdl graglqligr
      121 gvvpmavgal afplalpgda ltwgcfllsv lfgvlvsfal rylvalasfw lldgsglali
      181 sglacmfftg mvlplrvfpg gfgevvqllp waailqvpad vlmgvrsgde lvrglvfqav
      241 wavallalgr lvqsaatrkv vvhgg
//
LOCUS       WP_457697854             106 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457697854
VERSION     WP_457697854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..106
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=10751
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawilivvag llevgwsigm kftdgftrlw psvftgagiv asmlllsyaa rtlpigtayg
       61 vwvgigaaga avvgmtvlge pataariffi clllvavvgl katsgh
//
LOCUS       WP_457697859             435 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457697859
VERSION     WP_457697859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   3  (residues 1 to 435)
  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   4  (residues 1 to 435)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19835644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /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=45334
     Region          6..382
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          195..395
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mgirgriala iscmtalavv vlgfavhhia dverersara yqddrlssal qiyerdgtla
       61 lgaqlddatl psplrdavfr nqsgtyisgg edprvwaatg vgggdgsaps rslsvsaayp
      121 dddpsqvsld ralliagcgt vtlmagvswf vaqrlsrrlr lsaaaarria agaapdadal
      181 asngrdevae lgrsvhhmat slaaqaqaer eftadvahel rtpvaglvaa aellpqprav
      241 elvrdraqam rrlvedllev srldagvera dldacelpsl vrgivkraar qrgvdevsvs
      301 vegeprivet drrrvervlv nllanaakhg kppievvvag srivvrdhgp gypaelcaeg
      361 prrfrtaape rgtghglglt iaagqaevlg arldfgaaae ggaeavlelp dhtatapgig
      421 iplaatdngs cpgpp
//
LOCUS       WP_457697865             220 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697865
VERSION     WP_457697865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24911
     Region          154..199
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(174,176..178,180,189..190,194..195,198)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mpvspytrer leeaaassrt lsealrtlgv dpkgtsrryl hdrmrsmgvd tshferegtr
       61 wtkevledav alstnmcevl rrlgldpvgg qhthisrriq nlgidtshfs pvgrrktkar
      121 rryspeellv heenpgrrmp shrlkaalla lgadercavc rsgpvwrnrp lplevdhidg
      181 nwrnncrenl rflcpnchsv tdtyrgrnkg vcprdtgapq
//
LOCUS       WP_457697863             512 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457697863
VERSION     WP_457697863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55054
     Region          54..482
                     /region_name="MFS_ProP"
                     /note="Proline/betaine transporter of the Major
                     Facilitator Superfamily of transporters; cd17366"
                     /db_xref="CDD:340924"
     Site            order(64..65,68..69,72,110,168..169,171..173,176,196,
                     199..200,203,306,309..310,313..315,318,346,350,402..403,
                     407,411,427,430..431,434..435,438)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340924"
ORIGIN      
        1 mptgsteada apeqdrealk rhrvlfrava rrknpklrrt ditvtdervv kravkaaalg
       61 namewfdfgi ysylavtigk vffpggndtt sllssfatfa vaflvrplgg ayfgplgdri
      121 grkkvlaltm immavgtlci glipsyaaig fwspvllilf rlvqgfstgg eyggastfia
      181 eyapdkkrgf fgsflemgtl igytgaagiv lllnttlgde amlswgwrlp fliagplglv
      241 glylrvklde tpafqkfeat qthggsnsav eteaefshls enapkkkise ifsqqwptli
      301 lcialvgayn itdymllsym ptyltdtlhy eeshgllill gtmavlmcli stvgklndry
      361 grkpllmtgm lgffvlaipa flfvkqgsip avcagmgllg lslvcllgtm saalpalfpt
      421 nvrygslsig ynlavslfgg ttplvitalm dvfdknvmvp ayytmgaalv gviavacmke
      481 taqqplegsp psvatkeeav elieaqspep rf
//
LOCUS       WP_457697874             250 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457697874
VERSION     WP_457697874.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26926
     Region          1..250
                     /region_name="ElaC"
                     /note="Ribonuclease BN, tRNA processing enzyme
                     [Translation, ribosomal structure and biogenesis];
                     COG1234"
                     /db_xref="CDD:440847"
ORIGIN      
        1 mkltvvgcsg sfpsmesacs sylleadgfr llldmgngal gelqrhsgly dldavllshl
       61 hadhcidlcg yfvvryyrpd ggrcapmpvy gpagterrlt vahadvphdg amsevfgfrt
      121 lapgtftigp ftirtervrh pveafgfrie hggrtltysg dtgpceales laegadfflc
      181 easftygked ipdlhlngre agesarragv grlvlthipp wtdadisird aqkvydgpve
      241 aakagavyei
//
LOCUS       WP_457697881             487 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457697881
VERSION     WP_457697881.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..487
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51866
     Region          13..466
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtsvqvdkqh dgneapgqap eegyqrglgn rqiqmiaigg aigtglflga gkaismagps
       61 iilayaivgl viffimralg ellmyrpvsg sfseygrefl gpfigfvtgw tywlfwvvtg
      121 itevtaaaty vqywnkgipq waaalvftca lfginlisvk ifgelefwfs mvkvtaiigm
      181 iliglgvitl gfsdagdtas fsllwsdggf fpkgiggtlm tlqivmfafl avelvgvtag
      241 eatdpkkvlp kaintvpwri glfyigalii ilsvvswtaf kpgvspfvaa fqqiglpaga
      301 givnfvvlta alssansgmy stgrmlrdla lngqgpkfft rlsknglptw gtgvsvgmml
      361 fgvyinyqwp geafnyvvsf atisgmwawi vilasqlryr akanrgelpq sefkapgspf
      421 tsvfalafig mvivmmgvdk daraalyaap vwalvlavgy lcikrrdaai laaggapkda
      481 aakdtks
//
LOCUS       WP_457697900             492 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrolipoyl dehydrogenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697900
VERSION     WP_457697900.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Yan,L.J. and Wang,Y.
  TITLE     Roles of Dihydrolipoamide Dehydrogenase in Health and Disease
  JOURNAL   Antioxid Redox Signal 39 (10-12), 794-806 (2023)
   PUBMED   37276180
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Fleminger,G. and Dayan,A.
  TITLE     The moonlighting activities of dihydrolipoamide dehydrogenase:
            Biotechnological and biomedical applications
  JOURNAL   J Mol Recognit 34 (11), e2924 (2021)
   PUBMED   34164859
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Carothers,D.J., Pons,G. and Patel,M.S.
  TITLE     Dihydrolipoamide dehydrogenase: functional similarities and
            divergent evolution of the pyridine nucleotide-disulfide
            oxidoreductases
  JOURNAL   Arch Biochem Biophys 268 (2), 409-425 (1989)
   PUBMED   2643922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..492
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51020
     Region          14..492
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
ORIGIN      
        1 maateatkaa deaydvivlg agptgenlad rahaaglsav vveselvgge csywacmpsk
       61 allrpvtars esrrvpglkd avdvaldapa vlahrdafts ywkddgqvrw ldslgidlvr
      121 gqgrlagprr vvvdggrvlt arhavavctg sravlpgipg laearpwtsr datsaksvpg
      181 rlvvvgggvv gvematawra lgasvtllvr gdgllprmep faghlvaesl aeagvflrtg
      241 vevrevrrea pggpvtvlld sppgpggpgg tpsdeiiade lliatgrapr tedvgldtvg
      301 ltpgswldvd dscrvtgvtg gwlygvgdvn hrallthqgk yqariagaai aarargvpil
      361 esdrwgahaa tadtlavpqv vfsdpeaasv gltaaaaeka gyrtrvvdhd laavagasly
      421 adgyrgrarm vvdldrevll gatfvgfgvg ellhsatvav agevpierlw havpsyptis
      481 evwlrlleay rg
//
LOCUS       WP_457697909             454 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457697909
VERSION     WP_457697909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..454
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47196
     Region          1..454
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mdliarlrag lpgeailtdp dvtgsyandm asfceagtpa vvvlprtveq vqhimrtate
       61 lrvpvvpqga rtglsgaana sdgcivlslv kmdriieinp vdriavvepg vinavlsrav
      121 nehglyyppd pssweqcsig gnigtasggl ccvkygvtae yvlgldvvla dgrlltcgrr
      181 takgvagydl trlfvgsegs lgivvravla lkpeppqqla laaefpstaa acaavceims
      241 rghapallel mdrtsiravn amaqmglpds tealllaafd tpepaadlaa vgalctaaga
      301 tevvpaetaa esdlllqarr ltltaleqvk satmiddvcv prsrlaemld gtaaiaekyg
      361 ltigvcahag dgnthptvcf daadpdesrr aresfddima lglqlggtit gehgvgvlkk
      421 ewlarelgpv gvelqrgike vfdplgilnp gklf
//
LOCUS       WP_457697913             155 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457697913
VERSION     WP_457697913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..155
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16489
     Region          1..137
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msidhldgal lellaeepri gvleasrrlg vargtvqarl drlqsngvir gfgpdvdpaa
       61 lgypvtafat leikqgqgnd vrahlttvpe vlelhtttgh gdmlcrlvar snadlqrvid
      121 rvvgfdgivr astaivmenp vplriiplvk qasgd
//
LOCUS       WP_457697914             215 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697914
VERSION     WP_457697914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 215)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22427
     Region          2..214
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 msfweyvgtr haqlltdtyq hasavfqcmv latllgvfig vmtyrsewag nlattstati
       61 ltipslalig llipivglgv pptvialtly gllpvvrnai vglrgvdpdl vdaargigms
      121 rtsqlfrvel plawppiltg irvatqmlmg iaaiaafasg pglgneifrg iaslgsansl
      181 nqvlsgtlgi ailallfdaa yvligrltis rgira
//
LOCUS       WP_457697918             296 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697918
VERSION     WP_457697918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31087
     Region          93..292
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 msprggsgeg pprrqrhpsd healvfrdev emaqrelasg eaptpsapsg arriswqkwt
       61 fmpvflvaal latwlwfrga rldsiahqav ddgkvwlalr qhiqltaist ffvliiaipl
      121 gialtrsklr ratpvamafa nlgqaipalg llillviwlg igarsaivgm viyavlpvla
      181 ntiaglrgid ptlteaargi gmsptgvltk velplavpli lagvrtalvl nvgtatlatf
      241 ggggglgdli sagivtqrmp vlilgsvltv alallvewla slaelllrpr glevta
//
LOCUS       WP_457697924             598 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457697924
VERSION     WP_457697924.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 598)
  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 598)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..598
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66285
     Region          18..544
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mttttsatnn hhlspafpgr apwgtanklr awqqaamdry iqtqprdfla vatpgagktt
       61 faltlaswll hhhvvqqvtv vaptehlkkq waeaaarigi kldpeysagp lgreyhgvai
      121 tyagvgvrpm lhrnrieqrk tlvildeihh agdskswgea cleafepatr rlaltgtpfr
      181 sdtnpipfvt yeegndgirr ssadytygyg nalgdgvvrp viflsysgnm rwrtkagdei
      241 aarlgepmtk davsqawrta ldprgewmpn vlraadqrls evrksipdag alviasdqeq
      301 arayaklire itgegatlvl sddsgasqri ddfahsqdrw mvavrmvseg vdvprlavgv
      361 yattistplf faqavgrfvr srkrgetasv flptvpmllg fanemeverd hvldkpkkdg
      421 eedpyaesek emeeankeqd edtgeqeqfs fealeseavf drvlydgaef gmqahagsee
      481 eqdylgipgl lepdqvqmll qkrqarqiah skkrpdaead llelpaerrp vvthkellel
      541 rkqlntlvga yvhqsgkphg vihtelrrvc ggppsaeata gqlserikkv rewatrmr
//
LOCUS       WP_457697928             254 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457697928
VERSION     WP_457697928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27167
     Region          1..254
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mwvrstlayr tsfvmmavgs faangldfva imlmfsqida lggftlpeva flygtsgial
       61 gladlllgsi eglgrrirdg tldtlllrpv pvfaqiaadr falrrvgrit qallvlgwal
      121 prievdwtvg rvlmvplmav cgtaifaavf tagaafqfwa qdaaevqnsf tyggnallqy
      181 pptvfaqelv rgvtylvpla fvnwlpalrl lghpdplglp gwvdflgpvv aalmctgagl
      241 awrlglrgyr stgs
//
LOCUS       WP_457697948             386 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457697948
VERSION     WP_457697948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 386)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41314
     Region          2..360
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mkigivcpya wdvpggvqfh irdladhlir lghdvsvlap addetplppy vvsagravpv
       61 pyngsvarln fgflsaarvr rwlqhgafdv ihihepasps lgllacwaaq gpivatfhts
      121 nprsramiaa ypilqpalek isariavsey arrtlvehlg gdavvipngv dvdffasaep
      181 kaewqgrtig figrideprk glpvlmkalp ailaevpdar llvagrgdee eavaalpael
      241 rsrveflgmv sdedkarllr svdlyvapnt ggesfgiilv eamsagapvl asdldafaqv
      301 ldqgeagelf tnedadalaa aavrllgdpa rlaelrdrgt rhvrrfdwst vgadilavye
      361 tvttgatsva tdervgprnr lwpakd
//
LOCUS       WP_457697960             185 aa            linear   BCT 27-JAN-2026
DEFINITION  HIT family protein [Streptomyces nigrescens].
ACCESSION   WP_457697960
VERSION     WP_457697960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19903
     Region          48..174
                     /region_name="FHIT"
                     /note="FHIT (fragile histidine family): FHIT proteins,
                     related to the HIT family carry a motif HxHxH/Qxx (x, is a
                     hydrophobic amino acid), On the basis of sequence,
                     substrate specificity, structure, evolution and mechanism,
                     HIT proteins are classified into...; cd01275"
                     /db_xref="CDD:238606"
     Site            order(73,75..76,83,85,131,139,141,145,147)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(143,145,147..149)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            145
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mlarmtsepe qqigvgtqda fqrlwtphrm ayiqgenkpt gpgaddgcpf ctipeksded
       61 glviargehv yavlnlypyn gghlmivplr hvadyteldg petaelaeft kramtalrta
      121 sgahgfnigm nqgtvagagi aahlhqhvvp rwggdtnfmp vvghtkvlpq lladtramla
      181 hawpa
//
LOCUS       WP_457697962             215 aa            linear   BCT 27-JAN-2026
DEFINITION  potassium channel family protein [Streptomyces nigrescens].
ACCESSION   WP_457697962
VERSION     WP_457697962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13585897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..215
                     /product="potassium channel family protein"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24292
     Region          19..188
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          <152..>188
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mpvdrdvrlq ewerraqpyl fiasllflts ytirvlnpdl spawyalwet vtivswavfv
       61 aeylarlafs hdrwhfvrtr wldlivtvlp llrplrmidl hermqlrrav pglalearvm
      121 tysglaalll gfaaslavyh dersaphani htfgdavwwa cstltttgyg datpvtargr
      181 viavglmfvg valvgavvgs fssylmrrfr qeger
//
LOCUS       WP_457697972             188 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697972
VERSION     WP_457697972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20145
     Region          10..176
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 miithdtrca ldavvdllnt apegeapgap dsltdlaale efvqrndvsd vgalgagdla
       61 avrsvrarfa rvfaadddrt aaeqlnalva sagttpqltd hdgydwhvhy fapgasvahh
      121 laadggmala flvvagerer lrhceapdcr hafvdlsrnr srrycdsrtc gnrlhvaayr
      181 arrreaag
//
LOCUS       WP_457697976             175 aa            linear   BCT 27-JAN-2026
DEFINITION  DsbA family protein [Streptomyces nigrescens].
ACCESSION   WP_457697976
VERSION     WP_457697976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..175
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19007
     Region          14..167
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mndatsspar pvrpvldvwc elqcpdchta ledlralrer ygdrldirlr hfplpkhpqa
       61 yaaaqaaeea ieqgqgwpyi eavlarteel gkhgdkllle vagelgldae eldtalidgr
      121 hllivdadqa egkaigvtgt ptyviggerl dggksqeglr arieeiadrl laeqg
//
LOCUS       WP_457697978             276 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697978
VERSION     WP_457697978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29336
     Region          194..268
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtttlrpagp eerhddghra rpydvcvnsr rvggirlttd arfgpaagri aeltidepdr
       61 hrgratvaal aaeevlrgwg crqieltvpa daeaagrlaa algytersrm mskpltaapp
      121 lpegssdral seaeypawrd aalaehvrtq tgqgmtrara eetaaaghra llpegaetpd
      181 qalrvlahgg advgsvwval rmpdqpggyv vdvrvapghr ghghgrtlmr iaereslaag
      241 rttlglnvya gnapalglya slgyrptgyl lwkpil
//
LOCUS       WP_457697980             274 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class IV [Streptomyces nigrescens].
ACCESSION   WP_457697980
VERSION     WP_457697980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  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   2  (residues 1 to 274)
  AUTHORS   Denessiouk,K.A., Denesyuk,A.I., Lehtonen,J.V., Korpela,T. and
            Johnson,M.S.
  TITLE     Common structural elements in the architecture of the
            cofactor-binding domains in unrelated families of pyridoxal
            phosphate-dependent enzymes
  JOURNAL   Proteins 35 (2), 250-261 (1999)
   PUBMED   10223296
REFERENCE   3  (residues 1 to 274)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="aminotransferase class IV"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28984
     Region          1..270
                     /region_name="IlvE"
                     /note="Branched-chain amino acid
                     aminotransferase/4-amino-4-deoxychorismate lyase [Amino
                     acid transport and metabolism, Coenzyme transport and
                     metabolism]; COG0115"
                     /db_xref="CDD:439885"
ORIGIN      
        1 mkiwldgglq daesarvsvf dhgltvgdgv fetikaehgr afaltrhler lttsarglgl
       61 pdpdldevrr gceavmaanp malgrlrlty tggvsplgsd rgdagptlvi alsetrrrpd
      121 ttavvtvpwt rnergalsgl kttsygenvv alararerga sealfantvg alcegtgsnv
      181 fvvldgelht pplhsgclag itraltvawa gaketdlpld aleraeeifl tstlrdvqav
      241 nridgrqlad gpgpvtaeam rifdeqsagd fdpr
//
LOCUS       WP_457697984              92 aa            linear   BCT 27-JAN-2026
DEFINITION  TFIIB-type zinc ribbon-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457697984
VERSION     WP_457697984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Elsby,L.M. and Roberts,S.G.
  TITLE     Interaction of the TFIIB zinc ribbon with RNA polymerase II
  JOURNAL   Biochem Soc Trans 36 (Pt 4), 595-598 (2008)
   PUBMED   18631123
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Hahn,S. and Roberts,S.
  TITLE     The zinc ribbon domains of the general transcription factors TFIIB
            and Brf: conserved functional surfaces but different roles in
            transcription initiation
  JOURNAL   Genes Dev 14 (6), 719-730 (2000)
   PUBMED   10733531
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008034
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..92
                     /product="TFIIB-type zinc ribbon-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10026
     Region          1..>43
                     /region_name="COG3809"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-finger domain [General function prediction only]"
                     /db_xref="CDD:443022"
ORIGIN      
        1 mqcpkchapm htyhrngvqi eqcagcrgif ldygeleala rlesqwsqqa ppspapqayp
       61 aapawgaphq ghhghhghhg hhrsfghilf ss
//
LOCUS       WP_457697990             450 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457697990
VERSION     WP_457697990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..450
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=47067
     Region          17..258
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,43,45,77,93..96,100,102,139,141,
                     143..144,146,155..156,159,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,43,45,77,93..96,100,141,143..144,
                     146,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,100,102,139,141,143,159,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,69,74,79..82,94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(155..163,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mammrlrred prvvgtfrlh rrlgaggmgv vylgsdkrgq rvalkvirpd laedqefrsr
       61 farevsaarr irggctarlv aadldadrpw fatqyvpgps lhdkvneegp lspaqvasig
      121 aalsegllav hdagvvhrdl kpsnillspk gpriidfgia watgastlth vgtavgspgf
      181 lapeqvrgaa vtpatdifal gatlayacta dspfgqgsse vmlyrvvhee aqlagvpdal
      241 apllasclak dptdrpstls lslrlkeiaa reahglsggp lengsgagag werverrase
      301 rptgqraeey arqrterrta gtssprphps rppvprdaaa rpagpvsgag knprtggrng
      361 rhvpaarptg rngsrtpvrt tsggrrpgpd rrllrqrviv fvvvtllval giaaaqgcqg
      421 parglgaerp vpavpsagvg gpygvgeqnp
//
LOCUS       WP_457697992             271 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697992
VERSION     WP_457697992.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28941
     Region          7..253
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 maeiitvddp ddprladytg ltdvelrrrr epaeglfiae gekvirrarh agyvmrsmll
       61 sakwvdvmrd videvpapvy avspalaerv tgyhvhrgal asmqrkplpp atellagarr
      121 ivvmeavndh tnigaifrsa aalgmdavll spdcadplyr rsvkvsmgav fsvpyarles
      181 wprdlaavre agfkllaltp aekataidea aphtleraal mlgaegdgls tgalraadew
      241 vripmahgvd slnvgaaaav afyavatgrp a
//
LOCUS       WP_457697999             211 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457697999
VERSION     WP_457697999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23345
     Region          8..191
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mtstfpdisi stdrlvlrpf eeadvpslaa mmndelvaaw taipqpyted aariwttena
       61 haertaghgi dfavtefltq rlvgvvqlrn tdwrirssei syvvaswarg egyaseasla
      121 vahwlfqdqk ferielrtaa gntasqqvaq kigcisegvl rnafiarsrt edggwtdirt
      181 dlivwsllpe dlegvpgrla dangfsypew n
//
LOCUS       WP_457698001             293 aa            linear   BCT 27-JAN-2026
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Streptomyces nigrescens].
ACCESSION   WP_457698001
VERSION     WP_457698001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30974
     Region          32..288
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mnkkealfvr ntlkisvaia aasavalgas acsapsdtta ggdkgdknap lvvaasptph
       61 gtildfvkne laekeglklv vkpfndykip nkvtddgqvd anffqhkpfl dtfnkength
      121 ivpvqnvlie plgvyskkid klselkagst vsvpndpsne gralklladn gvitlkpgvg
      181 sdakltdvkd dkgikitele aaqtapridd vdaaiingnf aigahlkpsk dalalekakd
      241 npyanflavk kgnesdprik klakllnspe vkkfledkyk dgsvipafgp aks
//
LOCUS       WP_457698003             244 aa            linear   BCT 27-JAN-2026
DEFINITION  methionine ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698003
VERSION     WP_457698003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="methionine ABC transporter permease"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=25780
     Region          1..218
                     /region_name="MetP"
                     /note="ABC-type methionine transport system, permease
                     component [Amino acid transport and metabolism]; COG2011"
                     /db_xref="CDD:441614"
ORIGIN      
        1 mswsemqpll ydntldtlfm vwwstfyavl igipagvvlh ltdrgallqn vvvnkvlgai
       61 vnigrsfpfl ilivvlipft rlvvgvsigp tgavvplaia aipffarlve salrevdhgl
      121 veaaqamggg twtivfkvll pqalpalvaa vtttviqlig ysaiagavgg gglgnlayty
      181 gyqqyetslm ittvvelill vtlvqllgdl vvrrlagrgt rasslrvglr rarteepaav
      241 teaa
//
LOCUS       WP_457698005             364 aa            linear   BCT 27-JAN-2026
DEFINITION  methionine ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698005
VERSION     WP_457698005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 364)
  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 364)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38589
     Region          1..328
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mitttgltkv yrsgdrevta ldgvdlhvre gevygvigqs gagkstlirc lnllerptsg
       61 tvtvagqelt siagrgkras aqlraarshi gmvfqhfnll ssrtvqdnve lpleilkvdr
      121 rersrkalel ldlvgladka qaypaqlsgg qkqrvgiara lagdpkvlls deatsaldpe
      181 ttrsilqllr dlnrqlglti vlithemdvv kticdsaalm kngrvieqgt vaellatpgs
      241 elarelfpvg gepsaddrtv vditfhgsaa trpviselsr tynvdisilg aamdtvggkq
      301 igrmrielpg rfeenvvpig flreqglqvd vadvagadga aaaetapdpv ipapatplqk
      361 egak
//
LOCUS       WP_457698009             171 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457698009
VERSION     WP_457698009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..171
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18470
     Region          7..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mgtsvtisaa tdqdaeqilk lqylcyqqea alyddygiep ltqtlqalra elgegcvvva
       61 rlgeevvgsv rgtvdedgtg riaklivhpr mqrhglggrl ldavegrlaa ersatryrlf
      121 tghrsegnlr lyrshgyvpv gteqltprln vvtlekevpq pagtgelvaq a
//
LOCUS       WP_457698013             656 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            nigrescens].
ACCESSION   WP_457698013
VERSION     WP_457698013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 656)
  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 656)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..656
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69970
     Region          42..567
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mrdigrrsff taagalatas aigsnayatg hardaatade yvdvqllnit dlhgylqgap
       61 gahsiitgag gktytvggva ymaahlerlr ngrrnslffa pgdlfsgwef daaafadept
      121 iealnamgld fasagnhefd ksarfltshm edgvsfpvvg hddaftdstg rrfrgaefpy
      181 ysanmvwnan gkpvlppyni eyvdagggrr lpvgfihlta igsesfpgsy qpglrtldel
      241 etanrcaael ksrgvraivl smhdgavags dfssgsnpsg payelalrvs pdidaivtgh
      301 whcaftmmlp dpdgvprpfv eagcygqiin einlrldprt gavireltta tnhpntrevt
      361 pdpelksiag ywadygsrra rsrlgtqtas ftrrrnavge stmgnlvadw alwagsrplg
      421 pmddpaghpn tpadlaviav aprvgqavia gdlirneetd gtvtfaqawn svgygdpimt
      481 vtvtgrqihd aleeqwapta ggglgfspla vsanvrytfd aagpvgrrie paevfingta
      541 ldltrryrla alsytlinqd gfsaftgfta pvrhtrdfes fvsfirtkkq lkpaplnrva
      601 vknaevpgar tgtitqrqql lqpdgsvvpr peaalrtalt ggaegqrapg gfrvpc
//
LOCUS       WP_457698011             378 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces nigrescens].
ACCESSION   WP_457698011
VERSION     WP_457698011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Van Der Rest,B., Rolland,N., Boisson,A.M., Ferro,M., Bligny,R. and
            Douce,R.
  TITLE     Identification and characterization of plant glycerophosphodiester
            phosphodiesterase
  JOURNAL   Biochem J 379 (Pt 3), 601-607 (2004)
   PUBMED   14750903
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tommassen,J., Eiglmeier,K., Cole,S.T., Overduin,P., Larson,T.J. and
            Boos,W.
  TITLE     Characterization of two genes, glpQ and ugpQ, encoding
            glycerophosphoryl diester phosphodiesterases of Escherichia coli
  JOURNAL   Mol Gen Genet 226 (1-2), 321-327 (1991)
   PUBMED   1851953
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Larson,T.J., Ehrmann,M. and Boos,W.
  TITLE     Periplasmic glycerophosphodiester phosphodiesterase of Escherichia
            coli, a new enzyme of the glp regulon
  JOURNAL   J Biol Chem 258 (9), 5428-5432 (1983)
   PUBMED   6304089
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171238
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="glycerophosphodiester phosphodiesterase"
                     /EC_number="3.1.4.46"
                     /GO_function="GO:0008889 - glycerophosphodiester
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_process="GO:0006071 - glycerol metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41371
     Region          46..365
                     /region_name="GDPD_ScGlpQ1_like"
                     /note="Glycerophosphodiester phosphodiesterase domain of
                     Streptomycin coelicolor (GlpQ1) and similar proteins;
                     cd08602"
                     /db_xref="CDD:176544"
     Site            order(51,78,80,93,187,224,320)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176544"
     Site            order(51,93)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176544"
     Site            order(78,80,187)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:176544"
ORIGIN      
        1 mhkrqqpgrr tvlgaaalga gaavfggagq asaagragvp relpvplivg hrgasgyrpe
       61 htfgsyqlal dmgadvieqd lvptkdghlv crhenditat tdvsahpefa drkttksvdg
      121 vkltgwfted ftlaelktlr akeripgtrq hntvydgvwe vptfeevlqw aereglkrgr
      181 rvwlhietkh ptyfrklglg leervakalr ahgrhrrnsp nflqsfepss iqrlgklvdc
      241 pkvvllstld srpwdfveag dprkvadlvt peglkwlagf aqgigpdltv iiprdkdgkl
      301 geptsvvkda haaglvlhpy tvrnentflp adyrrgtdpd aygdalgvfk aylntgidgl
      361 fsdnpdtall aaaefrkr
//
LOCUS       WP_457698018             258 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698018
VERSION     WP_457698018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..258
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26446
     Region          72..244
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
     Site            order(77..80,130..135,168,170..171,194,200..201,224,226)
                     /site_type="other"
                     /note="NodB motif"
                     /db_xref="CDD:213022"
     Site            order(79..80,130,134,170..172,194,224,226)
                     /site_type="active"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mlraaasaaa agalvtgcdp hrdedpgaar saggpspsga ghappapvra arpptrvpgl
       61 pvqiehgprn gravaltfhg rgdpktatal lgeaeragak vtvlaigdwl deqpavarri
      121 ldgghelgnh tmhhrnical paaeayaeis gcadrlrklt gtigswfrps qtrratplvt
      181 elartagyph vlsydvdsld andpgaaavq rtvldsvgpg svvslhlgha gtvaalppil
      241 dglrrrglra vtttelvt
//
LOCUS       WP_457698022             222 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457698022
VERSION     WP_457698022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23834
     Region          2..217
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mrydlvifdn dgvlvdsepv snrilaeylt elghpttyed slrdymggam hrihervler
       61 sgqrlpagfd esfharvfee frrslepvag vgevleklaa dgvpycvgss gsherirval
      121 tktglwerfe gagggagari fssqdvgrgk papdlflyaa qemgvaperc avvedsplgv
      181 raavaagmdv ygftamtsae klteagatal fahmaelpal lq
//
LOCUS       WP_457698030             331 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698030
VERSION     WP_457698030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Valentine,W.J., Shimizu,T. and Shindou,H.
  TITLE     Lysophospholipid acyltransferases orchestrate the compositional
            diversity of phospholipids
  JOURNAL   Biochimie 215, 24-33 (2023)
   PUBMED   37611890
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10168420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=36209
     Region          98..321
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(124,128,131,148..151,196..198)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
ORIGIN      
        1 madakvipfg eeprarrkar ragragrgaa lapvpearte hppavpprpn pgrslderia
       61 gglaflrrri tgdyevddfg ydkeltdqvl msllrpfyek yfrvevkgie nipsdggali
      121 vanhsgtlpl dglmlqvgvh dnhpaqrhlr llaadlvfvl pvinelarka ghtlacaeda
      181 qrllergeiv gvmpegfkgi gkpfadrykl qrfgrggfvs talkagapiv pcsivgaeei
      241 ypmignaktl arvlglpyfp vtptfpwlgp lgavplptkw tiqfgepipt agyppeaadd
      301 pmlmfnltdq vretiqhtly kllvqrrsvf f
//
LOCUS       WP_457698056             397 aa            linear   BCT 27-JAN-2026
DEFINITION  RtcB family protein [Streptomyces nigrescens].
ACCESSION   WP_457698056
VERSION     WP_457698056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..397
                     /product="RtcB family protein"
                     /EC_number="6.5.1.8"
                     /GO_function="GO:0008452 - RNA ligase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=43388
     Region          4..397
                     /region_name="RtcB"
                     /note="RNA-splicing ligase RtcB, repairs tRNA damage
                     [Translation, ribosomal structure and biogenesis];
                     COG1690"
                     /db_xref="CDD:441296"
ORIGIN      
        1 msyvevpgaq vpirmwtdpa tvegvamqql rnvatlpwik glavmpdvhy gkgatvgsvi
       61 amrgavcpaa vgvdigcgms avrtsltand lpgdlsrlrs kieqaipvgr gmhddpvdpg
      121 rihgfptarw ddfwarfdgv adavkfrqer atkqmgslgs gnhfiefcld ddgavwlmlh
      181 sgsrnigkel aefhmtqaqk lphnqglvdr dlavfiadtp pmaayrndlf waqeyakhnr
      241 avmmglfqdv vrrefkkakv tfedvischh nyvaeerydg mdllvtrkga iragsgeygi
      301 ipgsmgtgsy ivkglgnaas fnsashgagr kmsrnaakkr fstrdleeqt rgvecrkdsg
      361 vvdeipgayk piervidqqr dlvevvaklk qvicvkg
//
LOCUS       WP_457698058             541 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457698058
VERSION     WP_457698058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..541
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57220
     Region          <196..>318
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          414..507
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mlisgplagr rrgaavitav vtcstvltgp glataggppp psasapqlaw rpcvqgsafd
       61 catakvpldy rhpggrtiel avvkrkatgp grrigtlffn pggpggpgtv qmpqnyaffp
      121 relrerfdiv swdprgvgss tavncfaspq earawltskp agfpvgaqqr aawiaaykdl
      181 srrcqqrdpe llrhvstadt ardldglrqa vgdpqlsylg isygtylgat yanlfpgkvr
      241 amaldstidp qawtnhashd dprlttfqrm gadrgaaail dqflarcgat ttarcafsag
      301 spkatrdkls rlmrrlrehp vgtwtygrtv gdlvnglyiv hgwtglagrl qtlwqgrapd
      361 pspvppgppv phpdpylgde qaaavfcgds pnprdpgvyh aleeasalra gdpgrfwtwa
      421 aepcatwpav aaqgyrgpwn rptahpvlvi gttydpatpy sgaqamakel aharllthhg
      481 yghtallnps scinayesry fidgtlppag aacrqdtppf satgprggva tgggamaglv
      541 p
//
LOCUS       WP_457698062             241 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457698062
VERSION     WP_457698062.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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   2  (residues 1 to 241)
  AUTHORS   Kedzierska,S.
  TITLE     [Structure, function and mechanisms of action of ATPases from the
            AAA superfamily of proteins]
  JOURNAL   Postepy Biochem 52 (3), 330-338 (2006)
   PUBMED   17201069
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26348
     Region          1..237
                     /region_name="COG3910"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443116"
ORIGIN      
        1 mlierayvdv pegagaaedg wpwtvpcvrq laeeglafra pvtflvgeng sgkstlaeal
       61 aegfgldpyg gkagykyvss rersllgglm rfdptqegrr mvrgprvrrk gfflraetam
      121 valngelsqs pddmshgegf lmafrerfsq rglyvmdepe aalsfsscle lvglmdelgs
      181 ggaqiicath splltalpga eivevgehgm rrvewaelgl vdhwrrylnd praylrhvle
      241 g
//
LOCUS       WP_457698070             169 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457698070
VERSION     WP_457698070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14398362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..169
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18300
     Region          10..160
                     /region_name="cupin_YML079wp"
                     /note="Saccharomyces cerevisiae YML079wp and related
                     proteins, cupin domain; cd06121"
                     /db_xref="CDD:380376"
     Site            order(16,32..33,44,49,68,72..74,100,108..109,132)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380376"
     Site            order(22,29,31,48,139)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:380376"
ORIGIN      
        1 mdehrtdrlp ealidfyglv plpreggryr rtwagperpd grpegtaivm lltaepgdfs
       61 alhrlpadei whfyrgdplt llllredggg gtartvvlgp dvlagqhvqf tvpagtwmaa
      121 evadggswtl fgctmapgft fedyehgdaa vlaarfpeea gritalsrp
//
LOCUS       WP_457698071             268 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457698071
VERSION     WP_457698071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27487
     Region          19..264
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtdtpsdatd rpgrpglpdl rgqvalvtga agvlgrgial rfaaagaavv ahyrtgadaa
       61 relvvqiead ggsalalrad laveeechrl vteaagwrgr ltalvnnagv qptqelaams
      121 ladwravadp nvhsvfactq aaasvmraag ggsvthiasi eadrpaprha hycaskaavv
      181 mharaaaley gpdgirvnsv spglidrpgl aedwpegvhr wqaavpagrl gtpqdvgdac
      241 vflaspmasw itghelvvdg gvsarptw
//
LOCUS       WP_457698076             226 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698076
VERSION     WP_457698076.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24635
     Region          9..192
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 msseditvvh lvrhgevhnp dgvlygrrpg yhlsdlgrkm adrvaehlae rdithvvasp
       61 leraqetaap vagalglela tderlieaan vfegktfgvg dgalkkpgnw kyltnpfrps
      121 wgepyieqvv rmmaalgaar daargheava vshqlpiwiv rsfaerrrlw hdprkrqctl
      181 asltsftfhg dkiisvgyse pardlvpshl lagakpvkgk akafga
//
LOCUS       WP_457698078             204 aa            linear   BCT 27-JAN-2026
DEFINITION  TlpA family protein disulfide reductase [Streptomyces nigrescens].
ACCESSION   WP_457698078
VERSION     WP_457698078.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Crow,A., Le Brun,N.E. and Oubrie,A.
  TITLE     The role of ResA in type II cytochrome c maturation
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 149-151 (2005)
   PUBMED   15667290
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Capitani,G., Rossmann,R., Sargent,D.F., Grutter,M.G., Richmond,T.J.
            and Hennecke,H.
  TITLE     Structure of the soluble domain of a membrane-anchored
            thioredoxin-like protein from Bradyrhizobium japonicum reveals
            unusual properties
  JOURNAL   J Mol Biol 311 (5), 1037-1048 (2001)
   PUBMED   11531338
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21560
     Region          58..203
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msacraprrl tgrrrvalla agaaaaaltl sacgdgasgg saqtrfvqgk ngvdtvkkge
       61 rqpapelsge tttgkkldva dykgkvviln vwgswcgpci aeapnfskva netkdkgvqf
      121 lgintrdsek sqatsfeeeh kvpypslfdp tgrlmlrfpk gslnpqsips tvaidrhgki
      181 aarsigplae ddlrkmvdpl iaek
//
LOCUS       WP_457698080             600 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome c biogenesis protein ResB [Streptomyces nigrescens].
ACCESSION   WP_457698080
VERSION     WP_457698080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Dreyfuss,B.W., Hamel,P.P., Nakamoto,S.S. and Merchant,S.
  TITLE     Functional analysis of a divergent system II protein, Ccs1,
            involved in c-type cytochrome biogenesis
  JOURNAL   J Biol Chem 278 (4), 2604-2613 (2003)
   PUBMED   12427747
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Le Brun,N.E., Bengtsson,J. and Hederstedt,L.
  TITLE     Genes required for cytochrome c synthesis in Bacillus subtilis
  JOURNAL   Mol Microbiol 36 (3), 638-650 (2000)
   PUBMED   10844653
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Inoue,K., Dreyfuss,B.W., Kindle,K.L., Stern,D.B., Merchant,S. and
            Sodeinde,O.A.
  TITLE     Ccs1, a nuclear gene required for the post-translational assembly
            of chloroplast c-type cytochromes
  JOURNAL   J Biol Chem 272 (50), 31747-31754 (1997)
   PUBMED   9395519
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..600
                     /gene="resB"
     Protein         1..600
                     /product="cytochrome c biogenesis protein ResB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=64118
     Region          39..531
                     /region_name="ResB"
                     /note="Cytochrome c biogenesis protein ResB [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG1333"
                     /db_xref="CDD:440944"
ORIGIN      
        1 mstktgtprd pgpaadpgsd lgaagsqlst aptedvtlps lgplgwarwf wrqltsmrva
       61 llllfllsvg aipgslipqt sidpvkvdrf kaehttladi ydklgmfhvy ssvwfsaiyl
      121 llfisligci vprswqfvgq lrgrppaapr rltrlpaytt wrtdaapeev lgaaqrllkk
      181 rrfrahqdgt avaaekgylr evgnlvfhla livmlvafav gslwkseggk litegdgfan
      241 sltqyddfts gaffdtdtle pfgftldkfe atyersgpek gtprvfrahi ryfsgadgke
      301 hktaievntp ldiagskvyl lnhgyapevt vkdgrdkvvy kgavpflpqd pknftstgvv
      361 kvpgaqtkdg krnqlgfqgf fvptfggkgs gsmfsqfpal dypvltltay hgdlgvgsgl
      421 pqnvyqldkk rlkqykakga pvakmmlpge tmklpngdgs iqftgikswa sfkishqpgn
      481 glaltgaaaa llglagslfi qrrrvwvrae adadghtvve vaglgrsesa rlpeelaela
      541 lalepdapla patdngrapd pkpgpaadtg pgpdsgpdse dpaeptdsdg padpsegara
//
LOCUS       WP_457698086             306 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase enzyme family protein [Streptomyces nigrescens].
ACCESSION   WP_457698086
VERSION     WP_457698086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..306
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34381
     Region          22..290
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mpsdaeritg egltstgapr vlaaacrrag ldddgarlir fgenalfrlt ahpvvvriar
       61 steyldsaqg evqvsrwlar egfpvtravd dleqplivdg hpvtfwhlie estrkptyge
      121 lgavlrdlhs lslpdtlslp pypvldrtdq ridaavgipe ddraflrkra helrdrvadl
      181 rfesekgpvh gdahvqnlmv grndqvilid lerfsfdfpe wdlmvtateh hslgwqtkee
      241 ygayvgaygr dlrtwpgfpt lravqefnmt twlmqnvsen aetaaeyarr iaslrnedap
      301 rdwnpg
//
LOCUS       WP_457698097             181 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleoside deaminase [Streptomyces nigrescens].
ACCESSION   WP_457698097
VERSION     WP_457698097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19670
     Region          35..170
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mdrtqdwgqd rdefrlhgsv dghsdptghp ghlqeqaram latavaeara glaeggipig
       61 aalygadgtl lgrghnrrvq dddptlhaet aafraagrqr syrgttmvtt lspcwycsgl
      121 vrqfgisrvv igeartfhgg hdwlarhgvr ivllddpeca smmrdfigar pelwredigg
      181 e
//
LOCUS       WP_457698109             242 aa            linear   BCT 27-JAN-2026
DEFINITION  UbiX family flavin prenyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457698109
VERSION     WP_457698109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /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=25479
     Region          16..227
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mepphndtsk qgpgrrrpwv vgisgasgtp yaasvlrgll aageavdliv srasrltlld
       61 etgiafrdah wradlrewla rgadgkpatf pvteadladv rywpagdlaa gpssgsypvk
      121 gmlivpasta cvagvalgls kdllqrvasv tlkerrrlvv avretplngp tlkhlvtlde
      181 agavvlpasp afyagathiq dlvdfvagra ldavevphgl yrrwegelrg gskdveeape
      241 ap
//
LOCUS       WP_457698107             197 aa            linear   BCT 27-JAN-2026
DEFINITION  rhomboid family intramembrane serine protease [Streptomyces
            nigrescens].
ACCESSION   WP_457698107
VERSION     WP_457698107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20442
     Region          16..181
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mtsrakpaif lmlgwvallw llegvdfatg galdtfgiap repaeladvv paaflhfgfg
       61 hlaantlpll llglvaalrs gvrrflaval liilasglgv wftaapdsnt agasgvvfgl
      121 fgyllvrgfi erklldigig lvvgvlygsi lwgalptdsg iswqghlfgl iggvlaafvf
      181 rvrapghlta advrpit
//
LOCUS       WP_457698123             242 aa            linear   BCT 27-JAN-2026
DEFINITION  type 1 glutamine amidotransferase [Streptomyces nigrescens].
ACCESSION   WP_457698123
VERSION     WP_457698123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Noldeke,E.R., Muckenfuss,L.M., Niemann,V., Muller,A., Stork,E.,
            Zocher,G., Schneider,T. and Stehle,T.
  TITLE     Structural basis of cell wall peptidoglycan amidation by the
            GatD/MurT complex of Staphylococcus aureus
  JOURNAL   Sci Rep 8 (1), 12953 (2018)
   PUBMED   30154570
  REMARK    Erratum:[Sci Rep. 2018 Dec 21;8(1):18073. doi:
            10.1038/s41598-018-37082-9. PMID: 30573753]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Morlot,C., Straume,D., Peters,K., Hegnar,O.A., Simon,N.,
            Villard,A.M., Contreras-Martel,C., Leisico,F., Breukink,E.,
            Gravier-Pelletier,C., Le Corre,L., Vollmer,W., Pietrancosta,N.,
            Havarstein,L.S. and Zapun,A.
  TITLE     Structure of the essential peptidoglycan amidotransferase MurT/GatD
            complex from Streptococcus pneumoniae
  JOURNAL   Nat Commun 9 (1), 3180 (2018)
   PUBMED   30093673
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="type 1 glutamine amidotransferase"
                     /GO_function="GO:0004359 - glutaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26234
     Region          6..236
                     /region_name="COG3442"
                     /note="Glutamine amidotransferase related to the GATase
                     domain of CobQ [General function prediction only]"
                     /db_xref="CDD:442666"
ORIGIN      
        1 msdnslrlvw iypdllstyg dqgnalvver rarqrgldvq rldvrsdqqi ptsgdiylig
       61 ggedrpqrla serlirdggl sravsngaiv fsvcagyqil ghefindlge rqqglglldv
      121 vsargeaerc vgdvladidp qlglppltgf enhqgvthlg ktarpfakvr fgkgngvgdg
      181 yegawndtvf gtymhgpvma rnphiadlli klaldvnalp pvddhwyeal rqeriaaatq
      241 pa
//
LOCUS       WP_457698129             409 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698129
VERSION     WP_457698129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..409
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44256
     Region          6..407
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 maeftmelnd eqkevrdwih gfavdvmrpa aaewdereet pwpviqeaak iglysldfya
       61 qqffdptglg ipmameelfw gdagiglsiv gtglaavgvl angteeqigt wvpqmygdvh
      121 dvkvaafcss epdagsdvaa mrtravydea kdewvlngtk twatnggian vhvvvavvdp
      181 dagskghasf ivppntpgls qgqkfkkhgi rashtaevvl envrvpghcl lggkeklder
      241 lararenakk dgvgrvknaa matfeasrpa vgamavgtar aayeealeya ktrsqfgrpi
      301 idnqgvafql admrtqidaa rllvwraswm avtgkpftsa egsmsklfas evakkvtaqa
      361 vqilggngft reypvermhr daaiytifeg tseiqrlvia rtlsgmpir
//
LOCUS       WP_457698142             174 aa            linear   BCT 27-JAN-2026
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457698142
VERSION     WP_457698142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..174
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17837
     Region          1..167
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtlyttldsp lgelllvgee satapgglal aslsvpgqkg gatvqdgwmy dpaafagiah
       61 qlrayfdgkl tcfgiayapa rgtdfqrrvw qaleaipygt tttygkiaad igaargavra
      121 igtaiganpl lvvrpchrvi aadgslsgya ggpvrkrqll giegalpdvl pdvl
//
LOCUS       WP_457698151             129 aa            linear   BCT 27-JAN-2026
DEFINITION  carboxymuconolactone decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698151
VERSION     WP_457698151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..129
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14151
     Region          <8..105
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 malrfqkhya rfaprvglta ahisslthgt sadacwtter drllldaada lhthhdiddt
       61 lwerlsaefs peqlldlltl cgwyhaisft aratrltpep dapkfhdfpp papgtpeapr
      121 skpgptads
//
LOCUS       WP_457698150             842 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698150
VERSION     WP_457698150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19095030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..842
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84540
     Region          41..483
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide)-like multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17504"
                     /db_xref="CDD:341047"
     Site            order(48..49,52..53,56,88,138..139,141..143,146,165,
                     168..169,172,296,299..300,303..305,308,342,346,396..397,
                     401,405,421,424..425,428..429,432)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341047"
     Region          <595..>829
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
ORIGIN      
        1 mnrtttdqlp gravgtpavp papdpavggr rrtsggivpv lafsgivvav mqtllvpvik
       61 dlpvllntap snatwvmtat llagavstpi mgrlgdlygk rrmllsslav mvvgslicgf
      121 tsdlvtmivg rslqgfamga iplgigimrd elprerlgsa mglmsssigv ggglalpvaa
      181 lvaqhadwht lffgaaglgv lsmlltllvv petavraqgr fdvagaigls aglvalllpl
      241 tkgsdwgwgs pttlilfgva alvlvlwgvm elrlsdplvd lrttarrevl ltnlasitvg
      301 vafyaislvl pqllqlptst gyglgqsmvv aglcmaplgl tmmfvaplya riaarrgpkv
      361 slllgmlvia igygagiglm daawqtviia vvvgagigla ysslpaliig avdasetgaa
      421 nglntlmrsi gtsvssavig mvlahmsksv gpvtvptmag frvsfliata avligvalas
      481 flpsqrkasr ptlvaqstdd eaadaadtdg aqgaegraak paapivatpp apadpaaaae
      541 ayepaesagq ltspmkpaps waqpaaerha alarpvlaat atgsdaagfr grvvdssgsp
      601 vpgasitlid rqgrqagvtt adadghyald apsagtyvlt gaapghtpha asatyhgkga
      661 strvdlilap tgrlagtllg gtegtplagg sivvtdaega vvarttsgae gswdvprlrp
      721 ghytlvlsaa ghqpqarama lsggaperqd arlqptatvr gtvrgpdgrp ladaavtlve
      781 dgtvaghtvt gpdgafafsd lsgphytlta agyppnaapi sltagagetl dldlaqrpta
      841 ag
//
LOCUS       WP_457698153             177 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457698153
VERSION     WP_457698153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19821
     Region          2..161
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mteirtprli lrrwtdddla pmadinadpl vmrwigdgst ldldrtaeei erweeewdde
       61 gfglfavell asgelagcag lsvpeflpea rhevaiswrl grqywgqgya seaaqavlef
      121 alqdrgldrv vainrlghes sqnvvrklgm afereathpe yghaltvhsi dlteyqg
//
LOCUS       WP_457698169             126 aa            linear   BCT 27-JAN-2026
DEFINITION  hydrogenase maturation nickel metallochaperone HypA/HybF
            [Streptomyces nigrescens].
ACCESSION   WP_457698169
VERSION     WP_457698169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Xia,W., Li,H., Sze,K.H. and Sun,H.
  TITLE     Structure of a nickel chaperone, HypA, from Helicobacter pylori
            reveals two distinct metal binding sites
  JOURNAL   J Am Chem Soc 131 (29), 10031-10040 (2009)
   PUBMED   19621959
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Hube,M., Blokesch,M. and Bock,A.
  TITLE     Network of hydrogenase maturation in Escherichia coli: role of
            accessory proteins HypA and HybF
  JOURNAL   J Bacteriol 184 (14), 3879-3885 (2002)
   PUBMED   12081959
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Olson,J.W., Mehta,N.S. and Maier,R.J.
  TITLE     Requirement of nickel metabolism proteins HypA and HypB for full
            activity of both hydrogenase and urease in Helicobacter pylori
  JOURNAL   Mol Microbiol 39 (1), 176-182 (2001)
   PUBMED   11123699
  REMARK    Erratum:[Mol Microbiol 2001 Apr;40(1):270]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001253
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="hydrogenase maturation nickel metallochaperone
                     HypA/HybF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /GO_process="GO:0051604 - protein maturation [Evidence
                     IEA]"
                     /calculated_mol_wt=12830
     Region          1..111
                     /region_name="HybF"
                     /note="Hydrogenase maturation factor HypA/HybF,
                     metallochaperone involved in Ni insertion
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0375"
                     /db_xref="CDD:440144"
ORIGIN      
        1 mhemsialav vdqvesaarp agattvnsvr lqvgelagvv pdalafsfal acagtvlega
       61 elvtepvvar arcgpcadtw pvgmppqlsc pgcggatael lsgrelqivs vcwndapvhv
      121 ptheer
//
LOCUS       WP_457698183             546 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457698183
VERSION     WP_457698183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..546
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57737
     Region          19..470
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 maerqvsgeg dgtdvpevqa qerrlrrdlg fwgltgigfs nivgsgwlfa amyaaqtagp
       61 aallswvgag llcglvalvm ielgasrpeg ggtvrwplfa sgrlvgtlig wstllsvggt
      121 aaeisaimqy aahylpgiyn ghtltlsgla laaglstvlt alnwfavrmf aqlnnlvsvf
      181 kivipvvtvi aliasgwhsg rltdhggfap ygyvacltal agggivysvn gfqapldfsg
      241 etrnprrtip aavltgigla vimylalqla flftvpehll gngwqgvsfe spfgqlalil
      301 nlhwlaslly adavlspggs ayvgvainar htyalakngt ipryfmkvne rfgiprrala
      361 inlvvimifl lpfggwqdiv svmgtmylli yaasavavav fraepggrta gwvpglrwia
      421 plsfvvasef vywsgwhdlr lalplvlggl liflamrrpg ardkaalesd gagpsrslga
      481 elrtgawlvv ylialtvlsw lgtfegsgrl papydsvtva alalavffwa vrsgvrhlev
      541 arpaaa
//
LOCUS       WP_457698185             277 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457698185
VERSION     WP_457698185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=28831
     Region          <2..270
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mlrrrpprsa saddllttlg rltaqarega ekqrarvela ealqremlpa vlpgipglra
       61 aatyaparhg ldiggdwydg fplpdgslaf cvgdvqghdv eaaafmgqir fglravagha
      121 adpgevlsra ndlllsvdcg lfatctfvrf dpvaweltga raghvpgiwa ttdgrsglad
      181 dpgglplgiv pgerypvtrr rfatagafvl ltdgvvegps fpieagltqv trlvsanadg
      241 dpatvadvam svaeftghtd dsavlvlrfd aapprag
//
LOCUS       WP_457698189             136 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457698189
VERSION     WP_457698189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Rosinski,J.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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15070
     Region          61..126
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdsrhvrrfd fsrllhpagp raalgravta lsaerrapga ellrdpvgvt larsrmpapt
       61 dprrvrlcrl iaresmttld laarlsmtap qvsrllralr dlglvrters grfvryrldl
      121 aaverlgqdv vtglqh
//
LOCUS       WP_457698194             408 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457698194
VERSION     WP_457698194.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=43634
     Region          9..407
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mstagidyaa vfqalpgavl lltpefviad aneallrrag rerhqligrf vfevfpdnpd
       61 dpdasgirnl raslervvas gapdtmalqr ydieapgrpg vfeerywspv napvldadgr
      121 vqlivhrvee vtetvragag grggdrerre aelytraqel qevnerlrqa ndwerevvla
      181 lqeamlpapq pvghhraavr yrpavgalnv cgdwydlael sgdrmavavg dvvgnglaaa
      241 cvmgqlrsal saaarvvsgp aralevlgiy arsvdgaest tavqavidwt thtiayssag
      301 hpppallhpd gtvelldrat dpplgarpeh varpearvsf addavlvlyt dglierrred
      361 idvglgrlad altrhrgada ealadallae llppggatdd aalviirl
//
LOCUS       WP_457698213             328 aa            linear   BCT 27-JAN-2026
DEFINITION  MASE1 domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457698213
VERSION     WP_457698213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Pfiffer,V., Sarenko,O., Possling,A. and Hengge,R.
  TITLE     Genetic dissection of Escherichia coli's master diguanylate cyclase
            DgcE: Role of the N-terminal MASE1 domain and direct signal input
            from a GTPase partner system
  JOURNAL   PLoS Genet 15 (4), e1008059 (2019)
   PUBMED   31022167
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Lacey,M., Agasing,A., Lowry,R. and Green,J.
  TITLE     Identification of the YfgF MASE1 domain as a modulator of bacterial
            responses to aspartate
  JOURNAL   Open Biol 3 (6), 130046 (2013)
   PUBMED   23740576
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Nikolskaya,A.N., Mulkidjanian,A.Y., Beech,I.B. and Galperin,M.Y.
  TITLE     MASE1 and MASE2: two novel integral membrane sensory domains
  JOURNAL   J Mol Microbiol Biotechnol 5 (1), 11-16 (2003)
   PUBMED   12673057
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="MASE1 domain-containing protein"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34655
     Region          1..>272
                     /region_name="MASE1"
                     /note="Integral membrane sensor domain MASE1 [Signal
                     transduction mechanisms]; COG3447"
                     /db_xref="CDD:442670"
ORIGIN      
        1 mvrteelrrl apaaltilvl agvyygtaqi glleqvviag arvtplwppt gislscllll
       61 glwtwpgial gtllvvasls pldvsvlgim agntlapvca flmlrrvgfh tgldrlrdgv
      121 alvalgafag mlisatlgsg tlllsgalpa ggfwrtwaaw wvgdamgilv vtplvlacrk
      181 vrwprgvpay rwaeaaalli asvvvslvav tselsllflv fplivwaalr fqlagaapcv
      241 llvsvlaima atrrtgpfeg qslleamvnl qalntsaalt alllsaivte qnsirrkieq
      301 acreladvvd rlapgesrrr wppegeds
//
LOCUS       WP_457698215             530 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457698215
VERSION     WP_457698215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 530)
  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 530)
  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 530)
  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 530)
  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 530)
  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..530
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..530
                     /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=57705
     Region          36..190
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mfltsaepsh esaagldpsr vaevivscgd eagrrgsgyl vamgrvlkaa hvvndarsiq
       61 vrfdadqpte qthlaevawa dtqvdiavls vlgeqrrvsw sdfgrvierd avlrcsamgf
      121 pvfkmrrdrd gtryrdacha vgtcavlsnr regtldlrva pphtdshsgh spwegmsgaa
      181 vfsgdsiigi varhhrsdgp dhlavlradr wheqlsaaea rrledgigtp lhparltdvw
      241 cqphavarqn agavlgqplh alphehalvl evhpaieadg egqalgtlpp ylhrpgvddq
      301 lhevvsvaqr hsrmvmlvgg sstgktraaw eairscfpdg wrlwhpltpd rpisalealr
      361 agrvgprtvi wlnesqlyls prshgeevav vlqelladhe vapvlilgsl wpsywrelta
      421 kpeaepdqpp pddphaaara llgqatvinl pdafaeedll thkrlldsdp rltlaagsag
      481 gritqflaga pelirryqqa ppparavawa amdarrlltf kawcrradvs
//
LOCUS       WP_457698217             319 aa            linear   BCT 27-JAN-2026
DEFINITION  pirin family protein [Streptomyces nigrescens].
ACCESSION   WP_457698217
VERSION     WP_457698217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..319
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34135
     Region          29..285
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msnlelrpap slcggtgrtg pvrdvqpgkq vplgestvvr rllpnlgrrm vggwcfvdhy
       61 gpddiadepg mqvpphphmg lqtvswlheg evlhrdslgs lqtvrprelg lmtsgraiah
      121 seesphghgp flhgaqlwva lpgehrdtap sfehhtelpv inggglsatv ilgelagats
      181 pgttysplvg adltltagtd trlpvdpdfe yaaltisges evdgvrlapg allylgcgrs
      241 elplradsds slmllggepf eeeivmwwnf vgrsqediae arsdwmdgsr fgevhgydgd
      301 rlpapelppv alkprgrvr
//
LOCUS       WP_457698220             129 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457698220
VERSION     WP_457698220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..129
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13285
     Region          8..>81
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mspqpltlti dptaaaapfe qvrtqiadqa rdgglpvgyk lptvrglaed lglaantvak
       61 ayraletdgv ietrgrngsf iaaageaadk eaaaaaesya rrarrlgldh haartavena
      121 lratygada
//
LOCUS       WP_457698225             838 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457698225
VERSION     WP_457698225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 838)
  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   3  (residues 1 to 838)
  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   4  (residues 1 to 838)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..838
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=89114
     Region          14..255
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          249..680
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          691..804
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mcasqssrls gdgvfdltrt avvmadragv aqgwtkgaer llgyavseav grplaelfag
       61 vapgasqdnr wesrlaaadg wsgleavrhk dghrldlefr vlpvldater sarlvlaaem
      121 trtpwsgasr sflegilgms pigvamvnad lefvwlndal ehmggtsreq rlgkrladiq
      181 pglavealea emrkvlstgt psvgyeylgr pqsdpereha ystsffrled eagqvlgvcy
      241 mvldvtesyr arqrmallnr agerigssld vwqtaqelad aavpdladfv tvdlldalls
      301 geepapgpvd aavlvtmrra gqqsvregcp eavvaigeaa ayppsapvvl sliegdstlf
      361 qtldlaagdw paddpvrvah lrelgfhslm vvplrargvf lgaatfarwq htgpfqpddv
      421 vlaeefvtra aisidnarry trehnaaltl qhsllphdlp eqcaveaayr ylpadslsgv
      481 ggdwfdvipl sgarvalvvg dvvghglhaa atmgrlraav qaladldlsp eevlahlddm
      541 lnrvahdtna ddgvigatcl yavydpvgcr ctlaraghpa pllvsptgng rllelptgpp
      601 lglggmpfes velplpegsl lalytnglll gkaldldggi trlrtaladp qapledlcdt
      661 vigglpggrp vddvalllar tralapaqla tweipadpsa vgqarrsaag rlaewgleel
      721 dfstelivse lvtnairhas gpiglrmira ralicevsds sstsphlrha rttdeggrgl
      781 fliaryaerw gtrytpqgki iwaeqplrsa agagpandls allddlddpa pftgaegr
//
LOCUS       WP_457698229             155 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698229
VERSION     WP_457698229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..155
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17394
     Region          1..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddidsaivr elqrdarqtn rdlarrlnia pstclervra lrargvitgy ratvdlraln
       61 rpvqalltvr irpmnrevie rfkafltslp evlsvyvvag gddflvhvav pdvdrlhall
      121 mdqvfkrrev vdcrssviyq hvandiieal ppnga
//
LOCUS       WP_457698231             427 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457698231
VERSION     WP_457698231.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..427
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41896
     Region          17..>330
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtvqqtslpa serpdvrrlg vgsgtalcag avlgpgvltl pslaadaagp asilawvvll
       61 alcvpvaasf aalgarfpdg ggvatyvhra igpraaavvg wwfygavpig vvsaawiggk
      121 yvadaaawgd tgaavvagav lavalvsnav glrmsgrvql llggllavvl lgtvlaaapq
      181 vsarhftpfl pggwssvgsa agvlffafag weaashlsge fadpgrdlpr vtrrtlavit
      241 vlylglavtt igalgpaaag tdtpltella rsvggaarpv aaaaalfltf gavnsylaga
      301 srlgaalard gaaprglakg gapgevprrs lavlggaavl vaaaagfgga dldllmrata
      361 tclaavtlag laaalvllpr rtplwcggca salltaavla fsgrlllipa glacaafgfl
      421 tlrrvtr
//
LOCUS       WP_457698234             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698234
VERSION     WP_457698234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20522
     Region          2..>112
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marpprfdta qlldaavrla aesgpsgvtm savaaavgap sgslyhrfag rsallaevwl
       61 rtvegfqagy fealessddp rtggraaarh vvawsrahpa eaalllygaq efgrddwsde
      121 yllraeegnm qvraalaala galglhgreg fdrvtlaavd lplslvrrhl rggtplppha
      181 edlaeqctda llavd
//
LOCUS       WP_457698236             299 aa            linear   BCT 27-JAN-2026
DEFINITION  esterase/lipase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698236
VERSION     WP_457698236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31278
     Region          61..175
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mklrwsrtlt llpalalalg vtttsaaaad spglrpggpp lshpsssavs sgwnnysckp
       61 saahprpvil vhgtlgnsid nwlglapylv argycvfsld ygqlpgvpff hglgavdasa
      121 rqlaayvdrv laatgtqkad lvghsqggmm srvylkfhgg agkvntlvgl apdnhgtdln
      181 gltrlldhfp gakryidklt pglsdqiags dlldrlnegg dtlpgvhytv iatkydevvt
      241 pyrsafldgp dvrnvvlqdl caidlsehva iglidrvafh etanaldpah atatnclsg
//
LOCUS       WP_457698240             365 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase Y family protein [Streptomyces nigrescens].
ACCESSION   WP_457698240
VERSION     WP_457698240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Yang,W.
  TITLE     Damage repair DNA polymerases Y
  JOURNAL   Curr Opin Struct Biol 13 (1), 23-30 (2003)
   PUBMED   12581656
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..365
                     /product="DNA polymerase Y family protein"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003684 - damaged DNA binding [Evidence
                     IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=38491
     Region          <38..300
                     /region_name="DinP"
                     /note="Nucleotidyltransferase/DNA polymerase DinP involved
                     in DNA repair [Replication, recombination and repair];
                     COG0389"
                     /db_xref="CDD:440158"
ORIGIN      
        1 mtpaprppaa ppdppgaprq pgmlhvrfrt adgtpvsaec feqllgllaq ftpviealpp
       61 daaladvrga lryfdrdaag iaelvrlral awhgvrctig iganpllarm aaqgaapgei
      121 rgvpddaetv aafldrrpas alhgvgpata ralcayglds vgriaaappa tlqrilgart
      181 grivyerarg idptpvtpna aarsmgaehr fahdeldpvr rrrallslad dlgarmrasg
      241 qvaraltltv ryadrstttr trrldgptah gpalteaaya lhtalglqra rvrsvalrae
      301 dlcraeraar qltfdpsddk ahrieaaldr ararfgtgsv rpaatlgrtp pppgtkplgp
      361 gtnrp
//
LOCUS       WP_457698242            1188 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA polymerase III subunit alpha [Streptomyces nigrescens].
ACCESSION   WP_457698242
VERSION     WP_457698242.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   Kelman,Z. and O'Donnell,M.
  TITLE     DNA polymerase III holoenzyme: structure and function of a
            chromosomal replicating machine
  JOURNAL   Annu Rev Biochem 64, 171-200 (1995)
   PUBMED   7574479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1188
                     /product="DNA polymerase III subunit alpha"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008408 - 3'-5' exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /GO_process="GO:0006261 - DNA-templated DNA replication
                     [Evidence IEA]"
                     /calculated_mol_wt=128212
     Region          2..1077
                     /region_name="DnaE"
                     /note="DNA polymerase III, alpha subunit [Replication,
                     recombination and repair]; COG0587"
                     /db_xref="CDD:440352"
ORIGIN      
        1 mpgfthlhta sgfslrygas hperlaeraa ergmdalalt drdglsgavr fakaaaeagv
       61 rplfgselav aeresaptpt arrrtpvrgg afldesaara vflardgaag waalcrlvsa
      121 ahagqgeqpv lpwsalesat dgltvllgpd sevgralaag rpdraaklia pwrerygeal
      181 rlevvdhgrp gsgpgsprla artlgfavdq glravltnav ryadpgqgpv advldsarrl
      241 vpvdrrrpea rgsgerwlkd gatmshtaer iaeaagfrrg lahrllamte etageclvdp
      301 qddiglgrih fpeprlvgag hrtaarvlrs rcaagmvlhg ydhdrerwar lhdelrtier
      361 lgypsyfltv arvvddirem girvaargsg agslvnhllg iahadpvehg llmerflser
      421 raalpdidid vesarrlevy raifdrfgae rvatvsmpet yrvrhavrdv gaalgmdpaq
      481 vdrlakafph irardaraal aelpelrgvr eaggeqlwpl vealdalprg iamhpcgvll
      541 sdatlldrtp vvptsgegfa msqfdkddve emgllkldvl gvrmqsamah avaeigratg
      601 rridlddpaq vppgdpatyd lirstetlgc fqiespgqrd lvgrlqpatf hdlvvdislf
      661 rpgpvaadmv rpfiearhgr kavryphpdl eeplretygv vvfheqiiel lrimtgcard
      721 eadekrrals hpelqgrvra wfaqcaerrg yapeviartw eiveafgsyg fckahavafa
      781 vptyqsawlk ahhpaafyag llthdpgmyp krllladarr rgvpvlpldv nrsavahrie
      841 lvsgdgsggp gdrsavwglr lalsdvhgms eaeaqrieag qpyhslqdlw qrarpgrpva
      901 erlarvgald afggnrrdll lhiaelhhrg rrapggqltl pgraldgaga epvdpvepag
      961 lpdlseverl saelgvlgmd asrhlmadhr eflaelgalp arllrsarhg etvlvagaka
     1021 atqtppirsg rrvifttldd stglvdcaff ddshaacaht ifhswlllvr gtvqrrgprs
     1081 lsvvgaaawn laelaelrre ggleavaarl aevpdtepae adtpaaepgq gtgeesgtdr
     1141 epapaatpgr tirlttgyel hpwadlqppg eraatgrklw hsspgsag
//
LOCUS       WP_457698248             256 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457698248
VERSION     WP_457698248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25940
     Region          1..256
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mkrfdgrrvl itgagsgigq atvhrilteg grvvaadida tglritadra aaegtdgrle
       61 tvvldvadea avragvaaav tglggldvlv naagilraah thetgldlfh qvisinltgt
      121 flmirealpa llegeapvvv nfsstsasfa hpymsayaas kggiqsmtha iaseyskqgl
      181 ravcvapgsi asgmtsgpvp glpedadmsl ftklfpaige gfagpetvag viamlasrdg
      241 afitgteiri dggthm
//
LOCUS       WP_457698249             246 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698249
VERSION     WP_457698249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25865
     Region          18..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptaprtttp pprpslterr kaetqleiar taaalfaerg aavtadeiar tsgvalrtfy
       61 ryfrtkedav vpllaggvrq widdlatppa spdalpvrev leraahralt padepaaeal
      121 rrtrgllram pgdpalravw hrvhhdseea lrpvlarltg adpsaarlaa aaantamrva
      181 veewaagdaa pdgpqgpael vvrtlralta glpeldrayg akerdggenp grrgggegaa
      241 aggrgr
//
LOCUS       WP_457698255             358 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457698255
VERSION     WP_457698255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36773
     Region          104..156
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          172..354
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(204,229,263,266..270,272,280..284,287,291..294,296,
                     304,309..314,329..331,336,340)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(204,292,294,296,309..314,329..331)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mkhrripnrr aviagagala laatatvtla nanasqapap eptlakltsv aatklasqlk
       61 tdtagafyda kakklvvnvv nkaaakavra kgaearlvqh tfaqldsarq tlkskatipg
      121 tswgidpqsn kvvvtadrtv kgtkldrltt vakalgdkve vrhskgefkp figggdaiwg
      181 sgarcslgfn vvkdgqphfl taghcgneik swsdqqggsa iattedskfp gddyslakyt
      241 gdtahpsevd lyngstqkit kaaeatvgek vqrsgsttqv hdgtvkalna svnyqegtve
      301 gliqtdvcae pgdsggalfd getalgltsg gsgdcsggge tffqpvteal qaygaeig
//
LOCUS       WP_457698253             277 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698253
VERSION     WP_457698253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..277
                     /product="metallophosphoesterase family protein"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28616
     Region          22..229
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mdtsdagtda gpnsvrphga gvavlsdiha vlpaleavla epdvraadri vltgdllagp
       61 lprqtlarlr algdravwis gnadremaav rqgttdapad amdawaagql gpddldflgs
      121 lpatvtleva glgpvlfcha tprndteial vdsrperwae vlegvpdavr tvvcghthmp
      181 fvrfthgrlv vnpgsigmpy grpgahwall gpgggavtlr htafdheaac ariaresdhp
      241 saaawadtyv rarhsaeeal aafgpgdgre tapgtgg
//
LOCUS       WP_457698257             307 aa            linear   BCT 27-JAN-2026
DEFINITION  slipin family protein [Streptomyces nigrescens].
ACCESSION   WP_457698257
VERSION     WP_457698257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Green,J.B. and Young,J.P.
  TITLE     Slipins: ancient origin, duplication and diversification of the
            stomatin protein family
  JOURNAL   BMC Evol Biol 8, 44 (2008)
   PUBMED   18267007
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="slipin family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33074
     Region          55..232
                     /region_name="SPFH_eoslipins_u1"
                     /note="Uncharacterized prokaryotic subgroup of the
                     stomatin-like proteins (slipins) family; belonging to the
                     SPFH (stomatin, prohibitin, flotillin, and HflK/C)
                     superfamily; cd08826"
                     /db_xref="CDD:259808"
     Site            order(55..62,65..66,76,84..86,99..100,102..104,133,
                     136..137,162,165..171,173,177,181)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:259808"
ORIGIN      
        1 mveelvtagv alactgtvyl maaarvvkqy ergvvlrlgr lasqvrepgf tmivpvidrm
       61 rkvnmqivtm pvpaqegitr dnvtvrvdav vyfkvvdaad avirvedyrf avsqmaqtsl
      121 rsiigkseld dllsnrekln qglelmmdsp aigwgvtvdr veikdvslpe tmkrsmarqa
      181 eatrdrrarv inadaelqas kklaeaaaam sdqpaalqlr llqtvvavaa eknstlvlpf
      241 pvellrfler sglqaqaeta aaeaerdgsr rpaapaapra pgtavehgae aglpseladl
      301 ppvedlp
//
LOCUS       WP_457698259             302 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457698259
VERSION     WP_457698259.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30607
     Region          52..102
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          118..298
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(150,176,206,209..213,215,223..227,230,234..237,239,
                     248,253..258,273..275,281,284)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(150,235,237,239,253..258,273..275)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mrnertiprs gvarrtrlia vasglvavga iaiptanaqn papaqtfsad rltaagnavr
       61 aadvpgtawr vdsatrtlvv tadrtvsrae iakieraags nadalrvdri agtfrkfisg
      121 gdaiyapswr cslgfnvrsg styylltagh ctdgnppwyt nssrttsigp tagssfpgnd
      181 ygivkytnss vahagtvgsq ditsagnpsv gqsvtrrgst tgthsgkvta lnatvnyggg
      241 divsgliqtt vcaepgdsgg plysgtkalg ltsggsgdct sggttffqpv tealsaygvs
      301 vy
//
LOCUS       WP_457698260             273 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698260
VERSION     WP_457698260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..273
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29645
     Region          7..272
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mstqgamvev rsvrksfgsl dvlkgvdldv rtgevtvvlg psgsgkstll rtinhlekvd
       61 sgsvsvdgal vgyrrddkaa arrasrkggg grragklyel rereilrqrt eigfvfqnfh
      121 lfphltvlen iteapvaalr rpkreaveaa rtllarvgla ekadaypkql sggqqqrvai
      181 aralalepkl llfdeptsal dpelvgevle vikdlahqgt tmivvtheig farevadsvv
      241 fmdggriveq gppgevldrp rhertksfls kvl
//
LOCUS       WP_457698264             289 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698264
VERSION     WP_457698264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="amino acid ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31221
     Region          59..284
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 mpsdtldart aspaappddg tphtvprivp rrrtgqwaaa aavlallala igsvlrndaf
       61 qwdvvadyfl ttavlrglgl tlwltvlvma lgfvlgtlla tmrlsgnpvl rsvswayvwl
      121 frsmpvlvql lfwfnigaly ptilgiktvd llgpvtiali gltlheaaya aevvrggils
      181 vdkgqweaaq slglgawrrl rrivlpqamr sivppagnml igtlkgtsiv sviavqdlly
      241 svqlvyhrty qviplllvat lwyivvtsal gvgqyylerh yargtagar
//
LOCUS       WP_457698268             149 aa            linear   BCT 27-JAN-2026
DEFINITION  cell division protein SepF [Streptomyces nigrescens].
ACCESSION   WP_457698268
VERSION     WP_457698268.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Duman,R., Ishikawa,S., Celik,I., Strahl,H., Ogasawara,N., Troc,P.,
            Lowe,J. and Hamoen,L.W.
  TITLE     Structural and genetic analyses reveal the protein SepF as a new
            membrane anchor for the Z ring
  JOURNAL   Proc Natl Acad Sci U S A 110 (48), E4601-E4610 (2013)
   PUBMED   24218584
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Cendrowicz,E., van Kessel,S.P., van Bezouwen,L.S., Kumar,N.,
            Boekema,E.J. and Scheffers,D.J.
  TITLE     Bacillus subtilis SepF binds to the C-terminus of FtsZ
  JOURNAL   PLoS One 7 (8), e43293 (2012)
   PUBMED   22912848
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Hamoen,L.W., Meile,J.C., de Jong,W., Noirot,P. and Errington,J.
  TITLE     SepF, a novel FtsZ-interacting protein required for a late step in
            cell division
  JOURNAL   Mol Microbiol 59 (3), 989-999 (2006)
   PUBMED   16420366
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004532
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..149
                     /product="cell division protein SepF"
                     /GO_process="GO:0000917 - division septum assembly
                     [Evidence IEA]"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0090529 - cell septum assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15975
     Region          1..148
                     /region_name="SepF"
                     /note="Cell division protein SepF/YlmF, interacts with
                     FtsZ [Cell cycle control, cell division, chromosome
                     partitioning]; COG1799"
                     /db_xref="CDD:441404"
ORIGIN      
        1 mgsvrkasaw lglvddsdde ryydddyaeg pdagdsgasp wvtdprvrva detaqdqgtr
       61 iatvspesfr dargigelfr dgvpvivnlt smesadakrv vdfaagltfg lrgsiervat
      121 rvflltpady kvvsgearah rnggffnqs
//
LOCUS       WP_457698275             346 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphatase PAP2 family protein [Streptomyces nigrescens].
ACCESSION   WP_457698275
VERSION     WP_457698275.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130261
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..346
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:1901137 - carbohydrate derivative
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=38007
     Region          44..223
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(126,133,154..156,195,201,205)
                     /site_type="active"
                     /db_xref="CDD:239486"
ORIGIN      
        1 mrtddkldqm edqrptdrvr pprmtrtrlw llwgtlavyl aivagvlats wlvtfdwqvm
       61 ffrpykqwpe ihafldyfvv lgqrgptava vaawlgwrcw rqrnlhpllv fgasllllni
      121 tvgaaklgmg rlgphyatvv gahemwlggd ifpsghtana vvtwgvlayl attslrrrtl
      181 sviaalgalg vgmttvylgt hwvsdvllgw aagllvllam pwlepgitwf edrlmgillr
      241 lwlrlrpdsl rgplpvgsla pgvsrqrias dgevlvreti sagtggrats ghtpdgwphh
      301 psrpysirse rapatpagsr rpphadrfpr ttpmsptsgr grngsg
//
LOCUS       WP_457698281             344 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698281
VERSION     WP_457698281.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /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=37334
     Region          16..308
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsarllr llsllqahre wsgaelagrl dvtprtvrrd idrlrelgyp vhsapgtagg
       61 yrlgagaelp pllldddeav avavglrtaa aggvdgieea svralakleq vlphrlrrrv
      121 galtaftvpi ldaggprvdp htltelahac rddqrfrfdy tthdgtvsrr ivephrlvca
      181 rrhwylvawd tdradwrtfr adritptpph gprftprtpp aedlaayvsq gisagayarq
      241 atvllhasle qaaerispaa gvleavdeqh cllrtgahsl elmvlhivlt gfdfevrepp
      301 elldqvrevr drlsralaps paaspppgga drtrgtrsgs sags
//
LOCUS       WP_457698285             419 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457698285
VERSION     WP_457698285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 419)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45033
     Region          3..373
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(15,209..211,271,293)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
ORIGIN      
        1 mhisflihna ygiggtirtt fnlartlaeq hdveivsvlr hrddpvfdlg pgvalrplvd
       61 lrenspghdg adpaharpak vfpaaegrfg qyseltdrri aqhlrrtead vvvgtrpgln
      121 vhiakqarrg pvrigqehlt ldthsrplkl alrgayprld avttvteada hayrrtlrlp
      181 gvrveavpns vpapalppad gsgkwvvaag rlarvkrydv lirafaqvaa erpdwrlriy
      241 gggaekatlr alidelglyn hvflmgpanp lepewakgsi aavssslesf gmtiveamrc
      301 glpvvatncp hgpgeiiddg vdgklvpvgn pealagsllt linddaarkr mgvaalassa
      361 rfdpatvagr ydalfgella rrrdsrwhss lhrargalls gayatkdaar aalrgvrtv
//
LOCUS       WP_457698296             218 aa            linear   BCT 27-JAN-2026
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698296
VERSION     WP_457698296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415180
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22954
     Region          14..217
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtdssrapsa agaavgrrig iglmyglwrp rvlgawrvps agpvilavnh shgidgpmlm
       61 gtaprpvhfl ikkeafvgpl dpflrgigql kvdrhtadrk aitdalgvla hggvlgifpe
      121 gtrgegdfas lraglayfav rsgapvvpva vlgskerhsr ltpavpplrs rvdvvfgdaf
      181 eagdssgrrt rkaldaatvr iqerltahla earrltgr
//
LOCUS       WP_457698304             231 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698304
VERSION     WP_457698304.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 231)
  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
REFERENCE   2  (residues 1 to 231)
  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 10007540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..231
                     /product="nucleotidyltransferase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25737
     Region          13..228
                     /region_name="YcgL"
                     /note="Predicted nucleotidyltransferase YcgL [General
                     function prediction only]; COG3541"
                     /db_xref="CDD:442762"
ORIGIN      
        1 mseaatghsl vtehtvyacv mgsrafglat etsdtdrrgv flaptplfwg fekppthvdg
       61 preeefswel erfcqlalra nptvleclhs plveridatg rellalreaf lsrqvhrtfa
      121 gyagsqlkql radvrqhgap rwkhamhllr llacsrdllr tgvltldvgr nredllavrr
      181 gevawntver rmarlseeae aavsgsplpa epdrarvadf lfrarrssal g
//
LOCUS       WP_457698307             125 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457698307
VERSION     WP_457698307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..125
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13701
     Region          8..123
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 miadlqcvvl dcpdpgqlae fyrsllggav nqqdrrwalg edwatlhsps glvlafqqva
       61 dyqppqwpda arpqqfhldf gvpdldrahe qilalgatvl dagsdgrgwr iyadlaghpf
      121 clvrh
//
LOCUS       WP_457698312             200 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698312
VERSION     WP_457698312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21373
     Region          19..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdavrpgra drvatlppre rildaaeelf hsegirgvgv qavaekagtt kaalyrhfgt
       61 kdalvaqwll ivaadyvsaf dkieerwpdd praqikglaa fiadslsais hrgcpfinsl
      121 aelpdrshpa rqvidahkaq qlrrlvamct aagltdpega aaeitfafeg aqvsaqngsv
      181 dhvgerliaf veavmawhga
//
LOCUS       WP_457698316             226 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457698316
VERSION     WP_457698316.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 226)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25863
     Region          60..205
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkidflllrd ntygeyclyc haeavkwivv dgrkrctcgs cgreaeravv idpriswwtd
       61 sdgeywhesa gvfvrdrrar flffqrtafp ysltvpaghv ergeepkcaa arelweevgi
      121 hdangglrlv adeylkgdvc rrgsdahrwh ayllevdehr eagahrevtv neegeapvwl
      181 tldqarsrqt tfaveriidq yserllravp rtpgerrqnp sdgsra
//
LOCUS       WP_457698318             474 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698318
VERSION     WP_457698318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..474
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47909
     Region          69..454
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mwrairscwp ssawttdpds rggrcsvinp patrppghpv vptldgrlrg ttrrplqgep
       61 vrdrkrgsqr rvstspwtya lvtwlagvla avglgavspa gsalrsslgl sggalawats
      121 sitavsavlg ipagwwvrrf gaqralswgl lvmslaaags atagswglll gsriaegvgy
      181 llvfvagpvv ltrltqgrir ssalalwgtc vptglaiaaa mggalaswwt whqwlaltal
      241 gplimagvlt avlppsprta vqrahreaga wngalrlgva ygslslvgva vvmvlppfli
      301 ehrqatpvva gtvvavvclg savgglaasw llrrgsalss lvplgalmpv aclpafsagl
      361 plavsggaat lvlvvdglli savfaavpas vsrpehvdva ngilnqlggv gilmgppvfg
      421 lviaaagwga vaaatlvfgg lgmvllltta rpsetgsaag vsqppdapeg mdvr
//
LOCUS       WP_457698320             177 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP cyclohydrolase I [Streptomyces nigrescens].
ACCESSION   WP_457698320
VERSION     WP_457698320.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Rebelo,J., Auerbach,G., Bader,G., Bracher,A., Nar,H., Hosl,C.,
            Schramek,N., Kaiser,J., Bacher,A., Huber,R. and Fischer,M.
  TITLE     Biosynthesis of pteridines. Reaction mechanism of GTP
            cyclohydrolase I
  JOURNAL   J Mol Biol 326 (2), 503-516 (2003)
   PUBMED   12559918
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Colloc'h,N., Poupon,A. and Mornon,J.P.
  TITLE     Sequence and structural features of the T-fold, an original
            tunnelling building unit
  JOURNAL   Proteins 39 (2), 142-154 (2000)
   PUBMED   10737935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     gene            1..177
                     /gene="folE"
     Protein         1..177
                     /product="GTP cyclohydrolase I"
                     /EC_number="3.5.4.16"
                     /GO_function="GO:0003934 - GTP cyclohydrolase I activity
                     [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0042559 - pteridine-containing compound
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19757
     Region          29..165
                     /region_name="FolE"
                     /note="GTP cyclohydrolase I [Coenzyme transport and
                     metabolism]; COG0302"
                     /db_xref="CDD:440071"
ORIGIN      
        1 mtieewlktn vttdtralgw ysgpecedri vrayrellsg yeidtskilk ttcvvdgeha
       61 gvvrvqennf fsicahhflp ffgkvnisyv pgerilglgk fprlvqafsr rfqiqeylvk
      121 diaeeimssg gakavrvtsr grhlcmcsrg psdqtvitdt syvagnqell akfgldd
//
LOCUS       WP_457698322             216 aa            linear   BCT 27-JAN-2026
DEFINITION  TMEM175 family protein [Streptomyces nigrescens].
ACCESSION   WP_457698322
VERSION     WP_457698322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Brunner,J.D., Jakob,R.P., Schulze,T., Neldner,Y., Moroni,A.,
            Thiel,G., Maier,T. and Schenck,S.
  TITLE     Structural basis for ion selectivity in TMEM175 K+ channels
  JOURNAL   Elife 9, 53683 (2020)
   PUBMED   32267231
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Cang,C., Aranda,K., Seo,Y.J., Gasnier,B. and Ren,D.
  TITLE     TMEM175 Is an Organelle K(+) Channel Regulating Lysosomal Function
  JOURNAL   Cell 162 (5), 1101-1112 (2015)
   PUBMED   26317472
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007546
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="TMEM175 family protein"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0022841 - potassium ion leak channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=23045
     Region          17..208
                     /region_name="COG3548"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442769"
ORIGIN      
        1 mvnggrrvrd degsavrlla lsdgvfaiam tllaldislp dgldsggfaq alsdvmpkvw
       61 ayalsllvia afwrghyqlf qyvrdvdgtv irlvllslgl valmpfpttl laeygdlpqs
      121 vaiysgavaa mgatqlaltl vlwkrpwlet aampdpivrn dvadlastvl vfaaavplaf
      181 vsptgaklww avlipirivt gkrgkrlraa aqrfsa
//
LOCUS       WP_457698325             364 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457698325
VERSION     WP_457698325.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=38667
     Region          13..345
                     /region_name="AAT_like"
                     /note="Aspartate aminotransferase family. This family
                     belongs to pyridoxal phosphate (PLP)-dependent aspartate
                     aminotransferase superfamily (fold I). Pyridoxal phosphate
                     combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine...; cd00609"
                     /db_xref="CDD:99734"
     Site            order(76..78,102,139,170,197,199..200,208)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(79,112,163,206..208,237,240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            200
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mierqaraaq hggqptwdls eallrglpts tgrvefsaea ypdpqgerel rrriaarena
       61 kyglslnedh ivvthgatea lfllahtfld pgdrvavqap sflfyreile nlgagvvpln
      121 aesdsarpar mrllhspsnp dglvlaegal slhaeaagad gallvldqvy delivggarp
      181 redqalldgg hvvkvnsvsk afgcpgvrvg wittapavae vltgvaerlr mgpslvaqqa
      241 aaglleqpvd rnlqllaerr aiavealstl dvfeaakppa gglflwlkla dpnagaqqfc
      301 dralaeagvr lmpglgfwqg tddrvrlsfg avpeylgaaf drlrrltvpp rrygagltta
      361 cgsa
//
LOCUS       WP_457698324             427 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698324
VERSION     WP_457698324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44416
     Region          20..404
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(30..31,34..35,38,71,126..127,129..131,134,154,
                     157..158,161,236,239..240,243..245,248,272,273,331..332,
                     336,340,356,359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mmpsatqapp qgglrrnrdf qifwigetis lfgaevslla lpitalvvlg adaadlgllr
       61 faeylpflvl alplgvlvdr rrrhpllvia naarallvga ipvlaalgwl tmswlvvlat
      121 gigtftvlfd lclmaylpkf vasedllsan grvsmsqaaa evagpglfgl lvhwlsaslc
      181 lalnagsylv svlslllikr pepeptrvag tpwqdlydgl rflvrsplmr avtiagslyn
      241 lawaifqtaf lvymnrilgf nvgvvlavga agglagaaca pwltrrlpvg vtylaaaaai
      301 avpalvipav sgqkaalalv vtallvlmng glaifsvlta tlrqsvtpdg lmgrvvagyr
      361 alvfggislg glvtawlgaf agprailwva glffvaavap illspvprlr gfgaggrlls
      421 gtesppe
//
LOCUS       WP_457698327             592 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698327
VERSION     WP_457698327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..592
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=66017
     Region          25..346
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtlfspehse tpddtpwydv vvcggglaga tfarqlrrth pdasvlvidg qtypvplaah
       61 kvgestvdia gfyfssvlgl geymadkhlp klglryffgr agepfahape iglsafsgrs
      121 tyqidrgvle ndlyemncea gveiatgstv revdlgpdra shlvhyvdgd gvprsarcrw
      181 vvdamgrary lqrklglqrp tegefnaawf rvagrldved fvsddnvdwh ervpgrrrrl
      241 stvhlmgpgy wvwliplgsg ntsvgivtsg elhdidgmst lpgavewleq nepavasalv
      301 hhevldflav rdysytssqv fsadrwgcvg eaaafadpfy spgsnmiafe nsalvglige
      361 daqddlrper veelsrfmls qndwlaynih ssysyfgepl imalsfiwdt llswttatpq
      421 iyngifldee kaaavraatp glygltvqvk rlfkqwerka grgrdfrfid yykipflhea
      481 yernlvegks vaelvddhrh smdvleevaq aifliavedt mperrahlde hpwlnawaig
      541 ldperwradg lfqpttpprs ldrtystlta lfdapspqpd ttpaalpiel rl
//
LOCUS       WP_457698340             422 aa            linear   BCT 27-JAN-2026
DEFINITION  3-isopropylmalate dehydratase large subunit [Streptomyces
            nigrescens].
ACCESSION   WP_457698340
VERSION     WP_457698340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10000557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="3-isopropylmalate dehydratase large subunit"
                     /EC_number="4.2.1.33"
                     /GO_function="GO:0003861 - 3-isopropylmalate dehydratase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44719
     Region          3..421
                     /region_name="LeuC"
                     /note="Homoaconitase/3-isopropylmalate dehydratase large
                     subunit [Amino acid transport and metabolism]; COG0065"
                     /db_xref="CDD:439835"
ORIGIN      
        1 mtpqtmtdki laraagrdhv vageivevgi dmafthdpvc eglrrefraa fgpdatvwdp
       61 erialfedhl vpakdaesrr laagmaqfaa eqgiahhypy genygichvm mceeglvqpg
      121 tvvlgtdshs vtygafnafg sgvgmidmvn afytgdlwfr vpesievrie gelapgvlak
      181 dviltligdl glggasgrsi eftgstidtm sveermtlcn mvveagavng imalspaaad
      241 ylaarprtva yepvtsdpga pyarrleyra eqlrpavayp hrpdnvhsid eamadrirvd
      301 qvyigsctga kfddievaaa elagkhvapg vrlmivpatm giyrrlalsg tmatllaaga
      361 vvespgckac ygahggvvgd gevclsttnr nfrgrmgnpk ssvylaspiv aarsalagri
      421 te
//
LOCUS       WP_457698342             362 aa            linear   BCT 27-JAN-2026
DEFINITION  isocitrate/isopropylmalate dehydrogenase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457698342
VERSION     WP_457698342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Howell,D.M., Graupner,M., Xu,H. and White,R.H.
  TITLE     Identification of enzymes homologous to isocitrate dehydrogenase
            that are involved in coenzyme B and leucine biosynthesis in
            methanoarchaea
  JOURNAL   J Bacteriol 182 (17), 5013-5016 (2000)
   PUBMED   10940051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="isocitrate/isopropylmalate dehydrogenase family
                     protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=39221
     Region          8..351
                     /region_name="LeuB"
                     /note="Isocitrate/isopropylmalate dehydrogenase [Energy
                     production and conversion, Amino acid transport and
                     metabolism]; COG0473"
                     /db_xref="CDD:440241"
ORIGIN      
        1 mmpatvptvl vlpgegigpe vvgaarhvle hvldraglda tirehavglp ayertgqwlp
       61 dpvrdeldqv aatprgavlf gatadepige lrsrydlfan lrparplral rdvsplrper
      121 ldgvdllivr elvsdvyygr rrtgvdagqr wagqemyyre deirrivrca lqhaegrrrr
      181 ltlvhkanai pdvfglwlev laeeapahpq vevrdmfadt mamqmvlrpa dfdvivtsnl
      241 lgdvlseitg avcgslgllp satlsptgfa lyepvggtap diagtgranp lgtigsvelm
      301 lrhtfdaprw adflagaver aveswrtpdi agprnapctt hemaaavcda ldavvaeeat
      361 qr
//
LOCUS       WP_457698352             427 aa            linear   BCT 27-JAN-2026
DEFINITION  cation:proton antiporter [Streptomyces nigrescens].
ACCESSION   WP_457698352
VERSION     WP_457698352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..427
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44344
     Region          20..371
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 msapdassll lavlvlvcqv maalarrlgq psvigeivgg vllgptlfgg rltdtlfpad
       61 vrpllgafan vgvalfmflv glefdrrvmr eqagtmgwlg agalvvpfgf galfalwlld
      121 ehpsrqpavf vvflgtamav tafpvlarii vdrgllssrv gglalalaav gdviawtvla
      181 vvvavvgteg hswrlllllp yaatmvfvvp rllrsravgr lpqqavmllv magvlasgaa
      241 tewmglhlif gafllglvvp rtglrggfre glgtsvepla sflmpiyfvv agfrvdlshl
      301 dadavgelll illvacggkl lgvyggaraa rldhrsaltl atlmnvrglt elvlltvgls
      361 lglldpdlys lmvvmavvtt vasgpmlrss tgspakgega gkgapgarip asspseddre
      421 hpptrqp
//
LOCUS       WP_457698355             278 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698355
VERSION     WP_457698355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=30635
     Region          1..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 mhyailgplh lvvngeprsi rsrnlsvila tllvkagsiv tvddligevw aqppqrarda
       61 iyvhisklrq qlgdesqgdv iwsqfpgylm rlqgeqldlq lfhrhridgh rnmvngdyks
      121 aardwksgls lcrgallgga yagpilgsfd swlqqsradc veltawsqls aglchevidf
      181 lslhltqypl neilyqqlml afflsrhraq slgvfhracq vlaeevginp ggdlrtiqdi
      241 iladdtgrak rviaaavasr vsslrpsgql qlhphsva
//
LOCUS       WP_457698359             279 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698359
VERSION     WP_457698359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28812
     Region          1..207
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mivvtgatgn vgrpltralt eageqvtavs rhaaavpdgv rhvaadlaep agltpaldga
       61 kalflllsgd lhapgarptd iiglaeasgv rrivllssqg vatrplgpsr vamraledal
      121 resgldwavl rpggfasnal awaesvrtqg avaapfgdvg vpvvdpadia evaaaclldd
      181 rhtggvyelt gpevitprqq aeaiaaalgs pvrfheltrd eakaamtqfv paeladdtld
      241 iiaapnpael risphmervl graprpfngw varniaafr
//
LOCUS       WP_457698361             123 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698361
VERSION     WP_457698361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..123
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14020
     Region          15..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mregaqltqv eavhryevfh tdcpardvvd hvtsrwgiwv lislrsndlr fyelrdsiqg
       61 isekmlaqtl ralvkdglvw revepttppq vtygltefgq eigetltdlf nritqrlppr
      121 spg
//
LOCUS       WP_457698381             339 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698381
VERSION     WP_457698381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  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   2  (residues 1 to 339)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..339
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34908
     Region          4..332
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 maevtlkdva lasgcsiatv srvlagtrpv gvetartvre aadrlgyrpn qvaralrsrs
       61 tgtvglvlpq itnpffpslv relehalhae gravlladcd ddpvteaari gallgrqvda
      121 lllipvderr sreavasaaa qvplvlldrg cgpgvadsva vdnaagmalv ldhlaatgrr
      181 rpcfvgavgt asaaverraa yeagaaaldp tapgrielgd fsvewgraav driwpsrpda
      241 licandliaa galqrlrqlg advpgeiavt gfddiplagl adpalttvrq pvgelaaeaa
      301 rllshrpsag apgprrtvrl apqlvvrass tpvgapsah
//
LOCUS       WP_457698383             172 aa            linear   BCT 27-JAN-2026
DEFINITION  lytic polysaccharide monooxygenase auxiliary activity family 9
            protein [Streptomyces nigrescens].
ACCESSION   WP_457698383
VERSION     WP_457698383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Morgenstern,I., Powlowski,J. and Tsang,A.
  TITLE     Fungal cellulose degradation by oxidative enzymes: from
            dysfunctional GH61 family to powerful lytic polysaccharide
            monooxygenase family
  JOURNAL   Brief Funct Genomics 13 (6), 471-481 (2014)
   PUBMED   25217478
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Lo Leggio,L., Welner,D. and De Maria,L.
  TITLE     A structural overview of GH61 proteins - fungal cellulose degrading
            polysaccharide monooxygenases
  JOURNAL   Comput Struct Biotechnol J 2, e201209019 (2012)
   PUBMED   24688660
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15340566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="lytic polysaccharide monooxygenase auxiliary
                     activity family 9 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17883
     Region          31..169
                     /region_name="LPMO_AA10"
                     /note="lytic polysaccharide monooxygenase (LPMO) auxiliary
                     activity family 10 (AA10); cd21177"
                     /db_xref="CDD:410624"
ORIGIN      
        1 mhrkrrlala igagiapllv vtlpvspasa hgyvssppsr qaqcaagtid cgpikwepqs
       61 vegpkgltsc sggnsqfael dddskgwkvt pvgssqtfnw kltarhstst wqyfvggkkv
      121 aefndggaqp patvshtvnf ggitgkqkil avwniadtan afyacidvti gg
//
LOCUS       WP_457698387             973 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698387
VERSION     WP_457698387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 973)
  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 973)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Rosinski,J.A. 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 973)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..973
                     /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_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=103827
     Region          <15..917
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          902..956
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mtfahsrdac gddwplvgrd relaamddva advlaggprv vqlegsagig ksallstwwa
       61 rheqfrvlra rchplerefa fgavrqlfkp llaavsdter arllegsaaa tlralddaav
      121 tepppeaanv taatlrelda lvsrlsrrqp lllavdalqw idqpslrwlv hfvgradslp
      181 vliavttrsa egrrldplfa elvrpancht lvvepldvdg vgqlvrtlwg aeepdeafca
      241 achaatgghp lfvrallhqa qrcgvkptte frdriptvtl stlggeishr lcqasdevva
      301 laralaflgd rkppellaay cgtgravvqs aaeelrslgl lradgnprft hpvvrdtvla
      361 tlspeelgfg haraarvscl sgrpdeevaa hllaagpvhg swvlpalrra atealrrgap
      421 etavtylrsa vhqpldeser arvllemgta ashydaalai scvtgalegl tdeaarsdal
      481 gvlaysllls rgsrtdlssv drkiaalser pttglgaadr elalrmralr swmeferpsv
      541 tgpapapaps pgadddladr tagerqllai rafhalraal papyvaalie rasvnlpafs
      601 hdlfplhyfv aqtllyldel dtadrlnrhl treisgrgme llvssltvyr avlalrrgni
      661 aealgaaqda adhaspagrl pyaltvdtir idallaqgrv eaaekvavth avagqtevaw
      721 erprflmsla alriaqgelr aglsllrecg hhcealgtvs pamspwrsra vavhlalgdt
      781 gaaralveqe ldlarrcrip ralgvalraa gtvteglrgl dmlaeavtvl rttparlela
      841 rachdfgaal lrrddkrgar galrdgldla vgcgatvlaa rleerlhlag grvarsgsqg
      901 irgltageer vctlaaqgys nkqiaellvv slrtvethlt gayrklgitg rphlaaamah
      961 adrcrggsep ads
//
LOCUS       WP_457698396             620 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698396
VERSION     WP_457698396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 620)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 620)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 620)
  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 620)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..620
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65494
     Region          17..598
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtttsggkpq sppgedrstr aavatvfrlt aghrasiava tvltvvgsav glaqplvakh
       61 ivdasghgrv fwplllllav lfvteaatga vgrfvlertg egvvrglrhg lvarllrlem
      121 reydrhrsgd lisrvtvdtt llrevvaqal sdlvsgvlvg agaivlmvwi dplllllial
      181 tiaaaaaiva sllngiraas ermqnavgai sadleralga lpmvrvhrae krearriger
      241 vesaysagvr taklasmmsp avelavqgsf llvlvigglr vnghanslgd lvafllyasy
      301 lvlplssafr avgliqrgmg ayqrieqvla lpaepaqrdt tavggpplrr akepetggap
      361 plalrdvhfg ygpdrpvlrg vsfvvphgrq valvgrsgag kstifalvar fyepdsgtll
      421 fdgrpaaeld rgecrariav vdqnthvvhg tlwdnityae peatedevrr vvelahleev
      481 verlpgglsg vlgergstls ggerqrvala rallarpsll lldeptahld alneaaltgv
      541 mkdvaqecal lviahrlstv qhadrivvve dgrtvasghh eelltsspiy rglaagqmlr
      601 paeappsagr aahagtrhtr
//
LOCUS       WP_457698398             185 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457698398
VERSION     WP_457698398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 185)
  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 185)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..185
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20911
     Region          1..88
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          92..179
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 maldhailvs llekpgsgye larrfersig yfwtathqqi yrvlkrmesd gwvdvrevpq
       61 qarpdkkeys vaalgraals awlhepieae svrhdlavki rgaafddpaa lireverhhq
      121 ihtdrlahyl agerrdftgp eapatpdagq elqhvvlrgg iayermtlaw lddvlatlhr
      181 lraeh
//
LOCUS       WP_457698399             573 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698399
VERSION     WP_457698399.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..573
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=63694
     Region          16..395
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 madpllfnpr tydpahfdpe trrllratvd wfeergkrkl ieayrsrawl sdflefstke
       61 glfatfltpa saaegnqdkr wdtariaaln eifgfygldy wyawqvtilg lgpvwqsdnd
      121 avrsraaell sqgevfafgl sekthgadiy stdmllepdg dggfrasgsk yyigngnaag
      181 lvsvfgrrtd iegpdgyvff aadsrhpayh lvknvvdssk yvsefrledy pvaaddilht
      241 graafdaaln tvnvgkfnlc tgaigiceha myeavthaqn rilygrpvta fphvrreltd
      301 ayvrlvgmkl fsdravdyfr sagpddrryl lfnpmtkmkv ttegekvidl mwdviaakgf
      361 ekdtyfaqaa teirglpkle gtvhvnlali lkfmgnhlln paeyapvptr ldaaddtflf
      421 hqgparglga vrfhdwrtay dafagvpnva rfreqadalc efvttaapde eqsrdldlll
      481 avgqlfalvv hgqlileqas ltgldedvld elfavlvrdf sahavelhgk dsataeqqsw
      541 algavrrpvv ddarstrvwq rvealsgaye map
//
LOCUS       WP_457698402             159 aa            linear   BCT 27-JAN-2026
DEFINITION  HIT family protein [Streptomyces nigrescens].
ACCESSION   WP_457698402
VERSION     WP_457698402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..159
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18116
     Region          12..128
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mtddwrmdri gaalrgenpt vlrrlesgfa vigdvqflpg ysvllvdepd vqrlsdlpkg
       61 krlsflsdmd qlgeaverac rrldpafrrv nleilgntdp flhahvwprf ewepaelvga
      121 pvwlyprdrw sgeqfrlgpq hdvlreaigs eldrlraka
//
LOCUS       WP_457698406             553 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698406
VERSION     WP_457698406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..553
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61149
     Region          47..530
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtspneqrsg asatlddsae alrhamsgls gpeatgwtga vrpagtpgeg akvlilgagv
       61 agltaayels mlgyrvtvle aqervggrnr tarkgdklye idehgavtpt htcafddgly
      121 lnlgpgripy hhrrvlkycr dfgvalepyi mettanrvrp phaevtwpnr rvandtrghl
      181 aaklaetlvs rdaftgelrd llrvfgalda ngkyrgstrs gyldrpeiee wpvsapplsf
      241 eelvnsgfwk arfyqpvdyl wqatmfqpvg gmdhivkala reakragakf vlgaevreie
      301 idprglgvtv myrkgddefh ddarycvsni papvlrkvkl srfsdpfeqa irlvefektc
      361 kvgwqanrrf wegdlggwdd tegiyggisw tghnitqmwy psndyfsdkg tltgaynfdg
      421 aadtlgkltp ekrlrlareg aiqlhpefkd rklvpdekgv siawhkvpyq lggwaawkpq
      481 veshkkaykq llqpegtdaf fvtgdqispl pgwqegamms ahyviqqilg implsapeev
      541 avpdsvaltq glf
//
LOCUS       WP_457698408             628 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha-keto acid decarboxylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698408
VERSION     WP_457698408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Pohl,M., Lingen,B. and Muller,M.
  TITLE     Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric
            C-C bond formation
  JOURNAL   Chemistry 8 (23), 5288-5295 (2002)
   PUBMED   12432496
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..628
                     /product="alpha-keto acid decarboxylase family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68313
     Region          3..609
                     /region_name="PDC1"
                     /note="TPP-dependent 2-oxoacid decarboxylase, includes
                     indolepyruvate decarboxylase [Carbohydrate transport and
                     metabolism, Coenzyme transport and metabolism, General
                     function prediction only]; COG3961"
                     /db_xref="CDD:443161"
ORIGIN      
        1 mttsqtctva eylarrleql githlfgvpg dhlgpflstl hekttvrwvg tpteggagqa
       61 adayarvtsa daeialgeqg igavavtysv gafnllnaig gafaeyvpli ainaapsyeq
      121 wlnqqaigll tshmsqrpes nlevyrqvtv daqaisnpgl aptqidsait aclshrrpvy
      181 levmddvwga qcpapqgrlt rrerpvtvkn ermldravta cvelvrhyrn pilwageeid
      241 rfrlsdefek lvretripfc ttigaksvvs eytpgfsgvy ngkasnpeva evfnnagcri
      301 glgswatskn lggarsigdd wavaaqdgvh vgasyfpdvq larflpalre rlvvefgdga
      361 faadyfarah edglevadst aaylasqtgg pypetvtyds ffrhinafle eqtseppgar
      421 snpftvvcda afaligsmnl rmaerasyva qnswlsigys vgaatgvalg rshagkrpmv
      481 fvgdgsfqet cqemsthvrh glrpvvfvld neafygieqm lvhpcyyqdg tprsdgadfy
      541 nelhpwryek ladvfgstkh pmhgfavrrh deltdllkri gepsdainqg pvvvrvqler
      601 hdypealkyk iaencppsgg apsegkav
//
LOCUS       WP_457698410             709 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin monoamine oxidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698410
VERSION     WP_457698410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..709
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78642
     Region          55..677
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mndsrhelrg ehagaerane ktyqqlarel llvgpepane dlklryldvl idkglerpaa
       61 pkrilivgag iaglvagdll traghdvtil eananrvggr iktfhakkge pppftdpaqy
      121 aeagamrlps fhpltlalid klglkrrlff nvdidpstgn qtapvppvvy ksfkdgkiwt
      181 ngdpspefre pdkrnhtwir tnraqvrrah yakdpsqine gfhltgcesr ltvsemvnqa
      241 lepvrdyysv lqsdgkrvnk pfkewldgwa gvvrdfdgfs mgrflreyag fsdeaieavg
      301 tienmtsrlh laffhsflgr sdidptatyw eieggsrklp ealakdlrdq ivmgqrmvrl
      361 eyydpgrdgh hgglagpsgp avaiqtvpeg dpygevetwt gdlaivtipf sslrftavtp
      421 pfsykkrrav iethydqatk vllefsrrww efteedwkre ldaiapglyd yyqqrgedea
      481 eaamavpqsl relptgllga hpsvdekris pqqveyyrns plsggvrpat haygggsttd
      541 npnrfmyyps hpvpgsqggv vlagyswsdd aarwdsfeda erysyallnl qsvhgrriev
      601 fytgagqtqs wlrdpyacge aavytphqmt sfhldvvrpe gpvhfagehv slkhawiega
      661 vetavraaia vneapaades afggraaapr errsatgsse qpregvlts
//
LOCUS       WP_457698412             492 aa            linear   BCT 27-JAN-2026
DEFINITION  Dyp-type peroxidase [Streptomyces nigrescens].
ACCESSION   WP_457698412
VERSION     WP_457698412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Sugano,Y. and Yoshida,T.
  TITLE     DyP-Type Peroxidases: Recent Advances and Perspectives
  JOURNAL   Int J Mol Sci 22 (11) (2021)
   PUBMED   34074047
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Colpa,D.I., Fraaije,M.W. and van Bloois,E.
  TITLE     DyP-type peroxidases: a promising and versatile class of enzymes
  JOURNAL   J Ind Microbiol Biotechnol 41 (1), 1-7 (2014)
   PUBMED   24212472
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Sugano,Y.
  TITLE     DyP-type peroxidases comprise a novel heme peroxidase family
  JOURNAL   Cell Mol Life Sci 66 (8), 1387-1403 (2009)
   PUBMED   19099183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..492
                     /product="Dyp-type peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=53360
     Region          28..481
                     /region_name="EfeB"
                     /note="Periplasmic deferrochelatase/peroxidase EfeB
                     [Inorganic ion transport and metabolism]; COG2837"
                     /db_xref="CDD:442085"
ORIGIN      
        1 mtttslrptg apeieqlpep plrrsleiqg nilsafnkdy mafryvrfad gaggrgwlsv
       61 mlntvsvtat vedfneefsl srraygqdps iaatwvgvsl tfqgllqvar epekvkqdlt
      121 pfasfvkgaa gqaadlgddg tsapehwhfg sdrtgtgvha vlivaadtea alneklknia
      181 aadsahevtl vhqddgrtlt gdlrghehfg ykdgisqpgv kdfhredren pgfrdnrpgs
      241 tlvepgefvf gyksesgapp eapqwldngs lqvvrrlrqd vpgwndavvr eaakfrpngi
      301 spdllgaclv grkkdgtpla qgenpvtgvg perndftyan dgqgkqtpca ahirrshprh
      361 feptqkhrvm rrgipygpay tgsngdtdrg lmfvcygtsl erqfeflqra wsnnpnflpg
      421 dsgapngidk mtgtirqggs gspdahivle dgqegtvsmn rfvqttgavy aftpsistlr
      481 rlaahqslhe kg
//
LOCUS       WP_457698417             192 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457698417
VERSION     WP_457698417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..192
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21827
     Region          15..180
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msdygdgqql rpdpmdglrv dftaffkevq hgyigyamql lrnrqdaedv vqiagmkiha
       61 kwdeflahsn yralglrilr daikdylrsr nrvtrreraa aaeagryqsc vdqilhlgtf
      121 daldramdel arrepvqadc vrlrvaqlsy eeiaetlgit pgtartyysr grklakelaa
      181 sylrneqege ps
//
LOCUS       WP_457698431             616 aa            linear   BCT 27-JAN-2026
DEFINITION  S9 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457698431
VERSION     WP_457698431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..616
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65038
     Region          36..>100
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          340..588
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msttaahpaa lppsgagfrv yhpalpevcp rdparmalaa dadgrceift wnaatgtarq
       61 vtdsphgtlh caldadarvw wfaedrsglg lwyfqdfegg arhpgltglp pglphglavs
      121 dagtvaiglg dgrgmtvhlg rpggparqvw tvdgqallag ispsggllal sgaagsdrav
      181 tlltcsgavl drlsghhgrl walgfapspa gtelllvqeh hdhyrlatwr pgsgllpqdw
      241 crfdteitar wyptgrrvli rqdrhgrstl aaadldrrtl tpvpsppgtl ldvaphrgde
      301 vhylwtdtat pprmrstagt rlpelatlpa pmpgrhrelw tpgpdgpvht llstpdpmtg
      361 rrpplvflvh ggpadhdrda ydpevhslva sgfavarvny rgstgygprw raaygagvgl
      421 tqvadlvavr adllrrglar adaiglwgts wggylallal gtrpdlwqag vavkpvadca
      481 aayrtgtpal ralderlfgg tpdavperya rssplhyaad vrapllvvaa tldakcppgq
      541 vrsylgalrq agaahesmwl etghdgytga hhvavlrral gfldqhlrra paahrtprpp
      601 vdgvsggtgp sgapgs
//
LOCUS       WP_457698425             216 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698425
VERSION     WP_457698425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23495
     Region          14..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maarmaraeq vsgtrerilt aaerlfaerg vyavsnrqvs eaakqgnnaa vgyhfgtkad
       61 lvraitrkht erieqarvrm laevgdssdi gdwvaclvrp ttehlasmgs ptwfarfcaq
      121 vmtdpalqdi vaeesltspa lrqtleglnr clpelpadvh iergamarrl ivhtcaerer
      181 alagntatpr aswhdaatgl idaivglwra pvtpcr
//
LOCUS       WP_457698438             352 aa            linear   BCT 27-JAN-2026
DEFINITION  RICIN domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457698438
VERSION     WP_457698438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..352
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37267
     Region          45..169
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(56..58,69,71,77..78)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(102..103,108,110,117..118)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(144..146,157,159,166..167)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mrpprrsglr rtfavlital avtlglsaqa gtahaddgsg lsgltftsvn sgrnldvqng
       61 ntgdgvfivt nsapghhqkw sanaqpdgsf tlvndatgkc ieaghplkqr scsgasglrw
      121 yfqpvngtnd tylirnagdn kcvdvvlgaq yddawtqsyg cngskaqqwk ipssatgavf
      181 kaavayaskr cqkdaatcsw tkgsqapaep lpkqcispvw yngtetpvpw tfslntssgw
      241 ssqlgvsfts tlgtgmaspv qtsvsltlsg qvtydlrtdl gnsltitvps rhyawvalse
      301 latkvtgewt fdangfpwka kdtvtvplrs ddqgrssiyl aqtspdfttc ns
//
LOCUS       WP_457698440             315 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457698440
VERSION     WP_457698440.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..315
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32183
     Region          7..266
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 msradgrala aasvtvvlwa ssfiairssa adfgpgalal grlavasvvl salllarrgg
       61 fppreawpgv iasgvlwfga ymvalnwger hvdagtaslv vnvgpilmal lggwllkegf
      121 ppklmagmav sfggavvvgl smsgggkasl lgvllclfaa layavgvvlq kptlkhatpm
      181 qvttfgalag tvaclpfagq lvsqvsrapv satlqmvylg vfptalaftt wayavsrttv
      241 gkmgattyav pvlvvfmswl flgevpgwlt llggllclsg vavsrirgka qaqvpedgrr
      301 sraaaqpdvs aesar
//
LOCUS       WP_457698444             123 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698444
VERSION     WP_457698444.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..123
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13902
     Region          3..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 merepeeeac revlqilgli gskwsilivg qlrdrtlrfg elhrtvngis qrmltltlrq
       61 lerdglltrt vhpsvpprvd yaltelgatl ldsvvalgew atahrheins nrrrydathp
      121 ars
//
LOCUS       WP_457698441             243 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457698441
VERSION     WP_457698441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24647
     Region          1..>180
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 maktlvvvga gpglgmgvar afglqgfqvg llartkgklh tmvgelaelg itaaafpadi
       61 rdrdaltaal aaagdtlgpi dvleyspspt gpithaaqtt vdsvtaqfel hvlgavtavg
      121 hvlpqmlarg dgtlllttgv sstipapfla nvgmamaglr nwahtlhtel tphgihvgtv
      181 tiasgitpgg geadpdaiga ryysmyqqrn rveevigdld afrslvaqtg ghgnsptptn
      241 tas
//
LOCUS       WP_457698448             409 aa            linear   BCT 27-JAN-2026
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein, partial
            [Streptomyces nigrescens].
ACCESSION   WP_457698448
VERSION     WP_457698448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..>409
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          48..307
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 maidarvsrk agavaliava gvsltsipaa aneatarqpa vagaevqapt apgsprlpsg
       61 lsalswmvad adtgsvlaak sphrrlapas tlktlfavtv lpkfsagtvr rvssadlagi
      121 gagssvvgvk qgrrytvgdl wrgvflrsgn davhvlaamn ggwrttaeem qenarklgar
      181 dttvkspdgy dapgqvssah dltvfaragl anedfaryca tpratfpaag gttqientnr
      241 llvgshgmsr ypgiigvkng yttkagntli aaarrngrtl lvtvlnpqsk eynavykeag
      301 alldwgfrta gttqpvgtlh avraaydggg ptrpvaadvt gaearggspr rttlaleagg
      361 agvaalggvs pisvglrrla phlaalshhp rtpspramlr lamhgtrrr
//
LOCUS       WP_457698450             407 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457698450
VERSION     WP_457698450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 407)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..407
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=43927
     Region          22..407
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(59,66,89..90,97,101,108,241..242,245,249..250,253,
                     286,291..292,295..296,298,321,348..350,353..354,356..358,
                     362)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(66,83,85,88,90..91,173..174,183,240..241,244..245,
                     249,292,295..297,397)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mqntaetgpd apidvtplld dpyaayaalr dagpvhritg adghpawlvt ryddvrrala
       61 dprlsldkkh aapggyrgfs lppaldanll nmdppdhtrv rrlvvkaftp grvealrapv
      121 rriadellda maergradli adyagplsia vicdllgiph rdrrdflaws dalitpdpgr
      181 pelmkeaiga mlefytglia akraepgddl lsdliavrdd aaagaggdrl tedeltslaf
      241 lmlfagyent ghlignavla lldhpdqlrq lqrnpadlpv aveeflrfdg pypvairrfp
      301 kedveiggvr ipagesvlls iasanrdpar fpapdaldcg rdpsghlamg hgihyclaap
      361 larleavtal dallgrfpgl rlgvprgelr hrralrargl islpvtw
//
LOCUS       WP_457698455             286 aa            linear   BCT 27-JAN-2026
DEFINITION  thioesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698455
VERSION     WP_457698455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 12150045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="thioesterase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31413
     Region          29..271
                     /region_name="4HBT_3"
                     /note="Thioesterase-like superfamily; pfam13622"
                     /db_xref="CDD:463937"
ORIGIN      
        1 mgtkdappai adafyerlde atytsswsta gpwgpkaqha gppsallamq lqnahprpgf
       61 hparmtfell gqipvadltv rtavehstnr tdllsgelly sgkvvalarm wrfraapdsl
      121 ermretrlqq glldfadsvp avtplvlayd dsvsppvple ltghtegyls avewrfeeer
      181 pfaafgpgra wvrpriplvl gepdtpfgrl mviadscwsv crridmtkhf ainteitvhc
      241 hrlpegdwlr ldgktvtspg gaavshatmg dhrdecayvl qsmfva
//
LOCUS       WP_457698465             436 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine desulfurase [Streptomyces nigrescens].
ACCESSION   WP_457698465
VERSION     WP_457698465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10797682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..436
                     /product="cysteine desulfurase"
                     /EC_number="2.8.1.7"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46244
     Region          10..420
                     /region_name="sufS"
                     /note="cysteine desulfurases, SufSfamily; TIGR01979"
                     /db_xref="CDD:131034"
     Site            order(96..97,100,135,212,214..215,235,237..238)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99746"
     Site            238
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99746"
ORIGIN      
        1 martldplqv radfpilhrt vgdgqrlvyl dsgatsqkpv qvldaertfa etsnaavhrg
       61 ahqlaeeate ayeqargqia dfigvhpgev vftknategi nlvayamsna atsgdaaarf
      121 rlgpgdeivv temehhanlv pwqelcrrtg atlrwlgvtd egrldlsrld evitrrtrlv
      181 afahqsnvlg tinpvrqiva raaevgaltl ldacqsvpha evdfhafgvd favfsghkml
      241 gpsgvgvlyg rrellevmpp fltggsmiev vtmaestfap ppqrfeagvp mvsqavglaa
      301 avrylttvgm esiaaherll teaalgtlsa idgvrvlgpt ttadrgsavs fvvdgvhphd
      361 vsqildahgv avrvghhcaw plhrrlgvpa svrasfylyn eladieplaa gileaqslfg
      421 arapgpelsg gtaaca
//
LOCUS       WP_457698469             199 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457698469
VERSION     WP_457698469.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..199
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22498
     Region          8..156
                     /region_name="YfbR"
                     /note="5'-deoxynucleotidase YfbR and related HD
                     superfamily hydrolases [Nucleotide transport and
                     metabolism, General function prediction only]; COG1896"
                     /db_xref="CDD:441500"
ORIGIN      
        1 mdgnlrevfd fisftarlre verhnnatps rkesvaehsw hlaliswilh referesgrs
       61 ldlekmlkmc lmhdlveiea gdpsawssrd addkarveee vaqrrfaplp dglgaeflsl
      121 wheyeeggtp earivrgvdr lnpalmrllt gqgwqdvgad aealdrlqlp rvqvsetlta
      181 lyqevrdaav trdlltpap
//
LOCUS       WP_457698471             489 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698471
VERSION     WP_457698471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50709
     Region          23..469
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,282,285..286,289..291,294,322,326,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 msaviqerpp vqagriptvv rllvlatfvv ilnetilina iprlmdslhi tqqsaqwvst
       61 afmltmaavi pvtgwflqrv ttrqayaiam gvflagtals avapsfevll lgrivqaagt
      121 avmmpllmtt lmivvpeqdr grvmgnvtla isvapalgpa vsglilqvgs wrmlfvvvlp
      181 iaalvtlfgl rkvdnisepq vssidwlsvs vaalgfgglv yglsllgetg grvglgigiv
      241 iagvaaiavf virqlklqrt gvplmdlrtl gnrtyglsla lisigflaml gsmillplyl
      301 qnmrglsple tgllvmpggl amgllgptvg kvfdrvgsrp lvlpgsigmv lalggftqvs
      361 mtmpfwqvlg lhallmvsla atftpvftlg mgalpphlys hgssmlgtlq qvaaafgtal
      421 vvtvmtarts hlvadgvaav paelsgmkla fgvaaaltlv tivvaaklpr riaaadaqdg
      481 stadqptgs
//
LOCUS       WP_457698473             214 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457698473
VERSION     WP_457698473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..214
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21994
     Region          3..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mvstesilaf aamsllvivi pgpsvlfvig ralahgrrta latvcgnlvg syalviavaw
       61 glgalvessa avfmgvktag aaylvylgvq afrhrkemrt admeapageq rgdlrtildg
      121 ifvgvtnpkg ivffaavlpq fvdhsaghvp lqmmvlglvp vaiglitdtl wglgasaars
      181 wfarsdrrls mvggaggfam iglgvtvaat grad
//
LOCUS       WP_457698481             302 aa            linear   BCT 27-JAN-2026
DEFINITION  transketolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698481
VERSION     WP_457698481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31609
     Region          1..298
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mdtmrerfas vtsqllaedp rlalvladig aagfaeaekq hpdrvvnvgi reqlligvgg
       61 glaltglrpi mhtfasflve rpfeqlkldl ghqgvggvlv sagasydwps ggfthmapgd
      121 ialldtldgw tvhvpghpde aedllrhaaa agddkvyvrl svqanaaprp vdgarfrtvr
      181 eggdgvviav gpmldpvlaa teglsvtvly attvrpfdaa tlrsaagaag tsdvvivepy
      241 lagtstrlaa ealedsphrl lglgvgrqel rrygqldehl aahgldprgl reriagfvta
      301 gs
//
LOCUS       WP_457698486             445 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698486
VERSION     WP_457698486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..445
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48294
     Region          1..380
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mhryftdqrh ealrhrvrdf aesevrpria emeasrsvch dlsrliarqg wigatvhray
       61 ggmgaghvak tliieelsrv saamgamvqa sqlgvakivh fgseeqkktw lpaiasgdcl
      121 ptiavtepqs gghvlgmsst avrdgddyvl ngrkiyvgns hvgdlhgvvv rtgegskgls
      181 aflvesdtpg frvgehqpam glhgfsfgel ffdncrvpaa nllgregdgl svaysssvly
      241 grpnltavsl gihqavldet trfcterqry gkpladlgni klklgriqsr lllarlsayh
      301 avhlldqglp cdaelmnakl vnvesalesa rdamdihaac glftdrpver flrdahhifa
      361 pagtsdiqll rlgelalgra qgewssrlad llrlepsewp eedevpdeap adppaptvra
      421 egttptvpgq rtgpahrhsw farpr
//
LOCUS       WP_457698488             201 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457698488
VERSION     WP_457698488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..201
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22261
     Region          <47..>200
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mnhpasrvpy isydptrhll ltpqddeapa rvarlralgi gdsplpafde farklarttr
       61 apysmvnfid errqyfagly tpsqdqavel gpapasaqpg rvmdrdhgyc phvivrrkal
      121 vledvcdypr fagnpvvdei girsylgapl idrtgtalgt vcvvdleprp wgregletik
      181 smaaelveqi hrmekqqtda p
//
LOCUS       WP_457698490             206 aa            linear   BCT 27-JAN-2026
DEFINITION  GTP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698490
VERSION     WP_457698490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Takai,Y., Sasaki,T. and Matozaki,T.
  TITLE     Small GTP-binding proteins
  JOURNAL   Physiol Rev 81 (1), 153-208 (2001)
   PUBMED   11152757
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006198
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="GTP-binding protein"
                     /EC_number="3.6.5.-"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=22156
     Region          21..204
                     /region_name="Srp102"
                     /note="Signal recognition particle receptor subunit beta,
                     a GTPase [Intracellular trafficking, secretion, and
                     vesicular transport]; COG2229"
                     /db_xref="CDD:441830"
ORIGIN      
        1 mdfandcdpr aqgdpatdlf ptalkilvag gfgvgkttfv gavseiepls teelltqisv
       61 gtddlagvee kntttvamdf gritlspahi lylfgtpgqq rfwfmwdels ngalgavila
      121 dtrrldqcfa avdfferrgi qfivavnefe gsyrydpdev rsamdvspdi pvvlcdarrg
      181 gsatqvlvsl vqhlltpala atpelp
//
LOCUS       WP_457698495             312 aa            linear   BCT 27-JAN-2026
DEFINITION  GlxA family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457698495
VERSION     WP_457698495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..312
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33550
     Region          2..312
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlald kvipfdlstp ievftrtrlp dgrpgyqvrv caerpevdag tftlrapwgl
       61 dgltdadtvi vpgtadpaap lppavhdaln aaaangtria sictgtfsla aaglldglra
      121 tthwiaagml aaahpdidvd pdvlyvdngq lltsagaaag ldlclhlirr dygsavaaha
      181 arlsvmpler eggqaqfivr pypstprgsa leplltwlqd nlardlmlad iaaradmstr
      241 tlirrfreqt gttplqwlhr arvrqaqhll ettthsveri gaqvgfgspt afrdrfkrtt
      301 gvspqtyrrt fr
//
LOCUS       WP_457698500             394 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698500
VERSION     WP_457698500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..394
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41802
     Region          4..378
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
ORIGIN      
        1 mpttpapqia vigagpgglt carvlqrhgi gvtvydrdas adarnqggtl dlhadsgqia
       61 lqeagllddf halarpegqa mrmltrhgev lvdyrptdee daapeidrgq lrtllanslt
      121 pgtvrwghtl tsatpgpagt hrltfdngvt rdvdlvigad gawsrvrplv saatpvhtgi
      181 tflearfekv dtehpavael vghgqvfatg dhkgligqrn snqhvrayia lrddaegrsa
      241 agidlddtea vraallrafa gwderllvli tdndgpyvnr plfvlpapht wphtpgvtll
      301 gdaahlmtpv ggnganfaml dgcelalala rhdsldeavt ayertmlsra aaagdgaaal
      361 erlfgpgdrs radvpdfakd keqyrqgaaa yrsr
//
LOCUS       WP_457698508             468 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698508
VERSION     WP_457698508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..468
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49481
     Region          16..357
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 maehsngght aiviggglag mlavtaligq vdtvtvierd rypaghafrk gvpqarhlhi
       61 llsggrrale ellpgtvaal geagarslyl srdlltrtpt gwqrrfderr hltlsvtrpv
      121 ldavvrervl raaagsatrv evleatevtg ltgdagrvtg vrvrsrdgap ggrserelpa
      181 alvvdasgrg srtpqwfael grsapqeetv daglayatrm yrpkdpatap dagvnvpgwp
      241 ecprgaayvp vedgkwlltl sgvrghhppt daaeftafsa tigdpyihel laqaeplspv
      301 hgfrdtcnrr rhferpgalp egflvlgdag ctfnpvygqg msvaalgala vrttladggg
      361 lrpgitaevq ravaravepa wlaavgadrp yaspddakag vgerlstwyi drlfaraaid
      421 pvvgaafrdv fcltapptrl vapqiflrtv flprrpglpg ppaaieav
//
LOCUS       WP_457698514             288 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698514
VERSION     WP_457698514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31976
     Region          18..74
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     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          103..274
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 madprsagap tvlrvvlgkr lqdlrekagl sfeqaaaald vthatirrme kaevglklpy
       61 vekllatygv tdedeiegfv slareankpg wwhrfrdvlp ewfsafvsle seanlirayq
      121 phyvpgllqt edyaaavlka gmphasakdi drivalrmer qslltrdnap mlwvvmdetv
      181 lrrpiggpkv mrdqvtrlme atglpnvrlq impfaagphp amygpfhifr fpipelpdia
      241 yaeslvgavy fdqrndvsqf lealdrmcaq aapahttgai lggfrkei
//
LOCUS       WP_457698510             336 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698510
VERSION     WP_457698510.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..336
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34892
     Region          14..302
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mtfqqvsety daydvlvvgg sgvdtlvsvg alpvpladsy pvpplhegag htgtgvalgc
       61 aalglatgfv dflgddhpgt lvrerlagtg vdfrplisph gtrravnlva pdgrrmsfyd
      121 ardpvdlrmp pehylpplrr arhvhlsimh farflyddie algipvstdl hdwdgltdhh
      181 refalrsdlv flstagager igavmreilh egraeaviat agaggaylls addrtprpvp
      241 aavppgpvvd sngagdafts gflygrlagr sleecarlga vagayactsr gthtalvgpe
      301 elhaalgata tvttapagag hrvpgppdaq vsrtga
//
LOCUS       WP_457698518             266 aa            linear   BCT 27-JAN-2026
DEFINITION  SGNH/GDSL hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698518
VERSION     WP_457698518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..266
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=28690
     Region          18..202
                     /region_name="SGNH_hydrolase_like_1"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01832"
                     /db_xref="CDD:238870"
     Site            order(25,184,187)
                     /site_type="active"
                     /db_xref="CDD:238870"
     Site            order(25,184,187)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238870"
     Site            order(25,68,97)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238870"
ORIGIN      
        1 maddskyfsn gapgaiesya avgdsftegv gdpgpdgayi gwadrlavll sdqqaegdfr
       61 yanlavrgrl ldqiveeqvp rakalapalv tfcaggndil rpgsdpdava eryeaavadl
      121 reavgavllc tgfdtrgvpv lkhlrgkiat ytahvraiad rhgcpvldlw slksvqdrra
      181 wsddrlhlsa dghtrvalra aqvlglgvpa dpdqpwppet ersaaearrd niqwarehlv
      241 pwigrrlrge ssgdhvepkr pdllpl
//
LOCUS       WP_457698520             269 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457698520
VERSION     WP_457698520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Alonso,A., Nunes-Xavier,C.E., Bayon,Y. and Pulido,R.
  TITLE     The Extended Family of Protein Tyrosine Phosphatases
  JOURNAL   Methods Mol Biol 1447, 1-23 (2016)
   PUBMED   27514797
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Tonks,N.K.
  TITLE     Protein tyrosine phosphatases: from genes, to function, to disease
  JOURNAL   Nat Rev Mol Cell Biol 7 (11), 833-846 (2006)
   PUBMED   17057753
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10595285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="tyrosine-protein phosphatase"
                     /EC_number="3.1.3.48"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=29366
     Region          13..268
                     /region_name="Y_phosphatase3"
                     /note="Tyrosine phosphatase family; pfam13350"
                     /db_xref="CDD:463853"
ORIGIN      
        1 mtqqtpqvpq aqpeltevrn frdvgglptv dgrrvregrl frsghlahat etdaaflagl
       61 glhtifdfrn asdiklegpd valpgvrnvn ipltdpadga efwtmvrdge leqlrsalgd
      121 gkaaarmaat yrhiittrte dhsrvlhala edsvpalmhc aagkdragls vavallavgv
      181 erdaieadyl ksndphrryk irrsdnsavg msqevmells plfgahtdyl taaydaiert
      241 wgstekyltd glgltpatre rlrdqlltd
//
LOCUS       WP_457698516             153 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698516
VERSION     WP_457698516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..153
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16253
     Region          25..144
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 massnnapsl grcggfvaqy pqdafhlpaq rtsvpearrr vsallcewga dqqvrddvel
       61 vvselftnav rhtdsekvgc elalfgahir ieitdqggpa dsaphiqpgs vdqecgrglf
      121 lvgalseswg srpadsgqgr vvwadlpyss lah
//
LOCUS       WP_457698529             198 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698529
VERSION     WP_457698529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21352
     Region          5..156
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgrrerkkaa trqaladaal qlflergydq vsikdiaeaa dvstttlfkh fpgkealvfd
       61 adsdheaalv aavrerpdgr slpaalrdhi lrshietlad pafarfreli tstpalrdyg
      121 hrmwmrheta laqaiaadvg apeddpacaa lahfaleapa largqddpra avdaafnlle
      181 hgwqpptrrp apgsaagh
//
LOCUS       WP_457698535             134 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698535
VERSION     WP_457698535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..134
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14559
     Region          25..132
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mtatlsddlk qlldtpvfvt vttvqpdgsp qaspvwvkrd gddllisttv grrkeknirr
       61 dprvsvvvqp sdapytyaev rgtaslsteg gqelidelsr kytgklyadf npagvtdder
      121 vvvritprkv vgsi
//
LOCUS       WP_457698541             242 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotidyltransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698541
VERSION     WP_457698541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /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=26320
     Region          11..237
                     /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 mtgaqhpspt qavvlaggqg srlrpytddr pkpmveipgt gtpiighqln wlaeegvtda
       61 viscghlagv lqdwldraql plrvttvvet eplgrggglk yaagslprpd epwyatngdi
      121 wtrfplrema afhheraaea tlalarprip wgavetdafg hvldfiespp spylinagvy
      181 vfsaaftell pdrgdhertt fprlarerrl agfplpqgsy wraidtakdl teaakelsaq
      241 gr
//
LOCUS       WP_457698545             378 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698545
VERSION     WP_457698545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40539
     Region          1..376
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtydqat riypgtdkpa vdkldiaied geflvlvgps gcgkstslrm lagledvdgg
       61 airigdrdvt hlppkdrdia mvfqnyalyp hmtvadnmgf alkiagvpka eirqkvedaa
      121 kildlteyla rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvqtrtqiag
      181 lqrrlgittv yvthdqveam tmgdrvavlk dgllqqidsp rnmydrpanl fvagfigspa
      241 mnlvevpitd ggvkfgnsvv pvnrealsta adkgdrtvtv gvrpehfdiv eqngaaaksl
      301 skesadapag lavtvnvvee lgadgyvygt aevggkvkdl vvrvngrqvp ekgsrlhvvp
      361 rpgethvfst ssgerltd
//
LOCUS       WP_457698548             238 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698548
VERSION     WP_457698548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26098
     Region          17..>58
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins.
                     Prokaryotic DNA binding proteins belonging to the
                     xenobiotic response element family of transcriptional
                     regulators; cd00093"
                     /db_xref="CDD:238045"
     Site            order(21,25,54)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,53)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,47,50,54..55)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 meqstewaer laatiageil ryrrnqkmsa qrlsdrcael gmevpratis nlengrrtsv
       61 svaellvlaa aldvppaalv fpvgyteete alpgaltspy eavrwfggee hsatpqaaaq
      121 dptsplrhls wrmegaagea ltgyrraeri aetglkhadr adhmradayd leektardal
      181 vqaarkqddk aqsehaslmq vldtlhdlga tvepttlhvs lfrqttrgnq prdnqkes
//
LOCUS       WP_457698550              92 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457698550
VERSION     WP_457698550.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 92)
  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 92)
  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 92)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..92
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=9910
     Region          12..>88
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 meygpddqve rdapqppfqq lagilrarvk rgdwkpnrai psenalaeqy glsrptvrra
       61 iaaladeglv yavsgrgtyv aeqttdepas ge
//
LOCUS       WP_457698565             279 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698565
VERSION     WP_457698565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31005
     Region          17..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..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvnrreldpe sspeaaygar lrrlredrgw gqedlagvme yssqhisave tarkpptlrf
       61 srsadrafgi aetadtferq yreikhgsll egfpqfvgqe graaeirlye vgvipgllqt
      121 peyatimads evqrgaitpe qahervtlva erqaalvrtp pplvivvlde scirrpigep
      181 avmdaqlarl aefaelpntm lqvapfdmga rrpfnlpitv ltmpdrslms yaesaqrghl
      241 erdnrfvlpm vtayhqlqaq apsqaqsvam iselrkgtl
//
LOCUS       WP_457698577             787 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein [Streptomyces nigrescens].
ACCESSION   WP_457698577
VERSION     WP_457698577.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Plisson,C., White,H.E., Auzat,I., Zafarani,A., Sao-Jose,C.,
            Lhuillier,S., Tavares,P. and Orlova,E.V.
  TITLE     Structure of bacteriophage SPP1 tail reveals trigger for DNA
            ejection
  JOURNAL   EMBO J 26 (15), 3720-3728 (2007)
   PUBMED   17611601
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..787
                     /product="phage tail protein"
                     /GO_component="GO:0044423 - virion component [Evidence
                     IEA]"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=78268
     Region          45..713
                     /region_name="COG5412"
                     /note="Phage-related protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444167"
ORIGIN      
        1 maltigelvg tidldasgar qgvaqadral qglqrsadgr lrdvrgrfvs asaalgaavg
       61 ngitagttqa aaaadnlgna vadgvaagad qarastsglg aqignairgg aerarsalsa
      121 lgpalsvlrt stvalsggal aaggalaaip alfagigika aassqqvkda fgglkdhvts
      181 qvqgmvgpir qqlvaiagda rstfdkiaps lksafaavap qirsvaqgvl glveklapal
      241 artasaatpv iqaisgglvk lgsglagffd glaagaqgaa qgfsglftgi gqllpvlgkl
      301 lgqlaqaggp llstvattvs qlasqllgvl gpalttlagp lrtlvqtvgv alrpvlaalg
      361 pvlkqaavav gelvraaapl lvtagklaas llpaltpvlr vvgsifrqla pvvrqlastl
      421 qaalapilaq lpglirpfat ilqslagtvl silgqqikal spaltslgks fgqilvaaqp
      481 llgalaslin sglralmpil tpliglagkl asilakvlat qitlvvipal kiltsllrgd
      541 fsgawrqtkt lvanvgaflr vlfiklgiwv aagiakavaw iktlpgrams algplagrlf
      601 taasnafqrm nlaiiakanq alawlrglpg rmvsalgdlg sllvsaggdv vrglwrgiqs
      661 mgawlrstlt swaknlipgp iakalgiasp srvmardvgr wipagvaagi tsgqgavega
      721 mrrlvpvpsi psmaapgtag apygraagss pygnrsgall hvenwhagsa tpdqtaaala
      781 wkmkarg
//
LOCUS       WP_457698583             145 aa            linear   BCT 27-JAN-2026
DEFINITION  minor capsid protein [Streptomyces nigrescens].
ACCESSION   WP_457698583
VERSION     WP_457698583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10577426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..145
                     /product="minor capsid protein"
                     /calculated_mol_wt=15747
     Region          16..137
                     /region_name="Minor_capsid_3"
                     /note="Bacteriophage minor capsid protein; pfam12691"
                     /db_xref="CDD:432722"
ORIGIN      
        1 madrepfdyl dafarylder rlltydptgi cgdtfietlp pspheavsls lygagatdar
       61 ngwdtrslqv rvrgtsdpri srrraealyg alhglarcel pggiwlvlaa avaapapvgt
      121 dangrhehvv nlrldieapt thrdn
//
LOCUS       WP_457698605             147 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease signature motif containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698605
VERSION     WP_457698605.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598305
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16603
     Region          44..88
                     /region_name="HNH_3"
                     /note="HNH endonuclease; pfam13392"
                     /db_xref="CDD:433169"
ORIGIN      
        1 mkregwldrf lskivetpag cwqwtgyllp ngyaqfwrgg qklyahrvay eavrgpipdg
       61 lvidhlcrnr gcanpdhlea vtsrintlrg igfcairarq thcihghafd aantyvapng
      121 trkcrtcrae ardrsrrrrr evtraaa
//
LOCUS       WP_457698609             172 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698609
VERSION     WP_457698609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  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 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   3  (residues 1 to 172)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10622089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /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=18659
     Site            order(3..5,36..37,39..41)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
     Region          3..40
                     /region_name="HTH_38"
                     /note="Helix-turn-helix domain; pfam13936"
                     /db_xref="CDD:433591"
ORIGIN      
        1 mqrrpvtdae rddvrrrhaa getrneiara lnrsastisr iasdeglrfe ggarvvpate
       61 arqldlaeqr rqlvgrlyar aaanldrvea pdgyvrvell pdgrtrritt ddppaqderh
      121 hsqaigsylt saarlaeida gnsagevrsm lsdlarglre afaddegdtg gg
//
LOCUS       WP_457698630             350 aa            linear   BCT 27-JAN-2026
DEFINITION  YqaJ viral recombinase family nuclease [Streptomyces nigrescens].
ACCESSION   WP_457698630
VERSION     WP_457698630.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Hao,Z., Lu,D., Li,X., Raheem,A., Zhao,G., Dawood,A.S., Chen,Y.,
            Chen,X., Hu,C., Chen,J., Zhang,L., Zhu,X. and Guo,A.
  TITLE     Novel Nuclease MbovP701 with a Yqaj Domain Is Interrelated with the
            Growth of Mycoplasma bovis
  JOURNAL   Microorganisms 12 (12) (2024)
   PUBMED   39770711
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Liu,Q., Li,R., Shi,H., Yang,R., Shen,Q., Cui,Q., Wang,X., Li,A.,
            Zhang,Y. and Fu,J.
  TITLE     A recombineering system for Bacillus subtilis based on the native
            phage recombinase pair YqaJ/YqaK
  JOURNAL   Eng Microbiol 3 (3), 100099 (2023)
   PUBMED   39628932
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="YqaJ viral recombinase family nuclease"
                     /GO_function="GO:0004527 - exonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38358
     Region          21..347
                     /region_name="COG5377"
                     /note="Phage-related protein, predicted endonuclease
                     [Mobilome: prophages, transposons]"
                     /db_xref="CDD:444142"
ORIGIN      
        1 mkayscraap tavvvapsgl ereqwlaarr qgiggsdiat vlgmsrytsp ielyldkvge
       61 lgdvprspel vetafwghqh eptiakvfae rtglgvaegp gmlthidrrw mlanvdryvi
      121 epgertpssl leiktrsafq ldewllgvpd gpalqthwyl avtgythahv aallggnrll
      181 ihrverdegl vehlveivgr fwqnvldrip ppadgseatr ellahlydva pgsvtvadpa
      241 tilplleqra aikareqqva delrlvdnql ktaageaeiv kaagetaftw kqngtfaakk
      301 fadahpdlaa qythqvdald tkrlaaehpg lfrkfrarrl vvpakketsc
//
LOCUS       WP_457698631             100 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698631
VERSION     WP_457698631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..100
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10548
     Region          18..74
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 magpipeprl rlvdadllrr lmartgtgcg isvrqlaaas gvshgtidnl lkgriktarh
       61 dvahqicrvi gvdllilwap tgravpvegh eapphlrlas
//
LOCUS       WP_457698637             144 aa            linear   BCT 27-JAN-2026
DEFINITION  phage tail protein [Streptomyces nigrescens].
ACCESSION   WP_457698637
VERSION     WP_457698637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Desfosses,A., Venugopal,H., Joshi,T., Felix,J., Jessop,M.,
            Jeong,H., Hyun,J., Heymann,J.B., Hurst,M.R.H., Gutsche,I. and
            Mitra,A.K.
  TITLE     Atomic structures of an entire contractile injection system in both
            the extended and contracted states
  JOURNAL   Nat Microbiol 4 (11), 1885-1894 (2019)
   PUBMED   31384001
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Jiang,F., Li,N., Wang,X., Cheng,J., Huang,Y., Yang,Y., Yang,J.,
            Cai,B., Wang,Y.P., Jin,Q. and Gao,N.
  TITLE     Cryo-EM Structure and Assembly of an Extracellular Contractile
            Injection System
  JOURNAL   Cell 177 (2), 370-383 (2019)
   PUBMED   30905475
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Fokine,A., Zhang,Z., Kanamaru,S., Bowman,V.D., Aksyuk,A.A.,
            Arisaka,F., Rao,V.B. and Rossmann,M.G.
  TITLE     The molecular architecture of the bacteriophage T4 neck
  JOURNAL   J Mol Biol 425 (10), 1731-1744 (2013)
   PUBMED   23434847
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Leiman,P.G., Kanamaru,S., Mesyanzhinov,V.V., Arisaka,F. and
            Rossmann,M.G.
  TITLE     Structure and morphogenesis of bacteriophage T4
  JOURNAL   Cell Mol Life Sci 60 (11), 2356-2370 (2003)
   PUBMED   14625682
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Ishimoto,L.K., Ishimoto,K.S., Cascino,A., Cipollaro,M. and
            Eiserling,F.A.
  TITLE     The structure of three bacteriophage T4 genes required for
            tail-tube assembly
  JOURNAL   Virology 164 (1), 81-90 (1988)
   PUBMED   3363870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..144
                     /product="phage tail protein"
                     /GO_component="GO:0098015 - virus tail [Evidence IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15616
     Region          7..141
                     /region_name="Phage_T4_gp19"
                     /note="T4-like virus tail tube protein gp19; pfam06841"
                     /db_xref="CDD:429149"
ORIGIN      
        1 mdhnllthkf aidlggiqve tlqsvsglty gqdvveikqv tadgellnrk qpgpaqtgqv
       61 titrgmdksr aftdwikttr enhdhgsarq nvtialldpg hnvvnrihlv nawasswtaa
      121 dldaessgaa ietvniefdd mvie
//
LOCUS       WP_457698641             209 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698641
VERSION     WP_457698641.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22401
     Region          13..208
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mgaltpargp kqpqqersra trlklleaav sclaergwsg stvavvaera gvsrgaaqhh
       61 frtredlfta avehvaekrq gavkavahnl ppagsvartw iiveelvgly tgplfraalh
      121 lwvaasdedq lrdrvtalea rvgreahrta valldadeav agvretvqgl ldmarglgla
      181 nlltddsarr ervveqwaki idailcpdg
//
LOCUS       WP_457698644             402 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698644
VERSION     WP_457698644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..402
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=45399
     Region          1..376
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlsgrryrle mtaeqaeqcq efgdicravw ntaleqrrey rrrgawmnyv pqcaelaeak
       61 rdhpwlktap aqllqqtlrd ldracrehsa fkvrwrskar wspsfrfpag ksivverqgr
      121 kwgrvkllkl gwvrfrwsrp lggeirsatv srrggqwfvs flvdeghetp qehampdsav
      181 gidrgvtvaa vtsdgtfhdr qfitvgetar crrlqkklar qkkgsanrrk tvavlrritr
      241 rvadrrtdfc aytanritar nalvvlenlr trnmtasasg tldrpgrnvr qkaglnraif
      301 dkgwhklela lrsaarhtgs eillvnpayt sqtcnqcghv dprsrksqaa fectacghrd
      361 hadvnaaknq rdaglafpac gdlgtsrsak qepvsratgr np
//
LOCUS       WP_457698646             387 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698646
VERSION     WP_457698646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41245
     Region          8..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtptiesee hralrkavaa lgnrygreyf trvvaegaht delwaeaael gylgvnlpee
       61 yggggggive lslvleelga agcpllmlvv spaicgtvla rfgteeqkrt wlpgladgsr
      121 kmafgitepd agsnshritt tarregedwv lngrkvfisg vdiadatliv grtedartgr
      181 lkpclfivpr dtpgfgcspi amelsapekq feltldevrl paealvgded agllqlfagl
      241 nperimtaaf algmgryalg ravdyartrq vwkepigahq slahplaqah ielelarlmm
      301 qkaahlydag ddmgageaan makyaaaeaa vhavdqavht lggngltqey glasmitaar
      361 variapvsre milnfvshqs lglpksy
//
LOCUS       WP_457698650             535 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces nigrescens].
ACCESSION   WP_457698650
VERSION     WP_457698650.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..535
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56632
     Region          21..533
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvlgtgldp sgaeyaerrt amlaklaeie tehakatagg gekyvarhrk rgkllareri
       61 ellvdpdtpf lelsplaawg saspeypvga slvtgigtva gvecvitand ptvrggasnp
      121 wtlkkalran eiafanrlpv islvesggad lpsqkeifip ggalfrdltr lsaagiptva
      181 vvfgnstagg ayvpgmsdhv imvkerakvf lggpplvkma tgeesddesl ggaemharts
      241 gladhfavde pdalrqarrv varlnrrkaq pdpgpaappk ydeeellgiv pgdlkapfdp
      301 reviarivdg sdfdefkply gpslttgwae lhgypvgila naqgvlfsae sqkaaqfiql
      361 anqrdipllf lhnttgymvg keyeqggiik hgamminavs nskvphlsvl mgasygaghy
      421 gmcgrafdpr flfawpsaks avmgpqqlag vlsivarasa aakgqpydde adaglramve
      481 qqieseslpm flsgrlyddg vidprdtrtv lglclsalhn apvegarggf gifrm
//
LOCUS       WP_457698653             289 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457698653
VERSION     WP_457698653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31117
     Region          3..284
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 msielrhfrc flaiadtlsi traaerlhlt qpavsrtlrq leqalgvrlv drsthhlalt
       61 pdglsfrdra avavaafdra lgyahhtawp lrlghawaga gtdttallrr whqehpatpl
      121 ellriddrta glargevdaa llrgevrvpg literlttep rvaglpaddp larrtalsla
      181 dladrtiavn tvsgitsldl wppsarpast itigntddwl aaitagravg vttsatadmh
      241 phpamayvpl tdappvpvvi awrdgpghpr ipdlirlahe vmgqhhgrp
//
LOCUS       WP_457698662             283 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698662
VERSION     WP_457698662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31670
     Region          7..>65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          106..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mstdfqqare algdrlrelr hscpegrltg aqlaerlnwp hskiskleng rqtataddlr
       61 awaeatsqpe aageltsrma alesqvrswr rqlasehrav qdthnaehvr tsvfhawqga
      121 mivgqlqtad yarhiftrya slhesprdte davrarlqrq eglykagkky riimweavlh
      181 alvcppsvla aqldrlagvi gldtvelgiv pfsaplkipp anafwvlder vaivedwhae
      241 lwlddaqsit tymkvwntlq ksavygskaq nvingarral nah
//
LOCUS       WP_457698670             294 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698670
VERSION     WP_457698670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32716
     Region          13..74
                     /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          100..279
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpaggkatvr srrlgtalkr hreaagldqa dgaeailksv skisrlesgq tsasalevrt
       61 lldrygveda eerarllewa rksnergwwi dyqemvrpgy adhitlenda tyirswsptr
      121 ipgllqtpdy teavitigpk fippdrvvel vklrqerqrr ieeggthfta iiwepavtal
      181 tcerhvrtgq lthllevsqr qnitlqllpa aesliagmsg afvafsfgme anveavtlen
      241 pantnvveap edldlyvnvf dqlrsaalsp dettdrirqm ldggpqcrer drea
//
LOCUS       WP_457698672             157 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698672
VERSION     WP_457698672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16512
     Region          24..142
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mstrarpaat rpaaapqpaa ayhlpgdrqs aaqarkalrq dlqiwgvege ladsaellls
       61 elvtnavqaq asaspeigvr fawsdgrlrl evrdasdepp vmndakedee cgrglvlvda
      121 lasgwgvdrd dtgktvwael avcdasapcr apalrsp
//
LOCUS       WP_457698677             494 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698677
VERSION     WP_457698677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..494
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50959
     Region          50..474
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 meindldlpp vlaldpaala allahvrgpv lapgddgyda ersgfqlarq hrpavivgar
       61 caedvvaavr fareqglpva vqatghglsa atgggllist rrmagvrvda aagtahveag
      121 vvwgqvieaa aphglaplng sspgvgvisy tlgggvgvla rtygfaadqv rsvglvtadg
      181 rlrhitadsd pelfrallgg ghglgvvtam efglvpvarl yggqlvfgge qidgalaayl
      241 rwtetvpdel tsslaliayp dlpqlpeslr grylaqiria ytgsaaeger lvaplravgp
      301 rvsdelremp yaeshtihrd psdphaydgd nallsgldaa alrrvaeltg paaprmtvvq
      361 lnhlggalsa gtgavghrda ryalrllspl rgaaagdgpg gdghdaelat vralhaeala
      421 avapwrlgrs vnflfgghgd rpdaaevars vhdadehrrl aelknrhdpe nvfrfhpaga
      481 atadrapaaa tcsg
//
LOCUS       WP_457698679             351 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698679
VERSION     WP_457698679.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (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   4  (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   5  (residues 1 to 351)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /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=37578
     Region          1..330
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mksarllsii lllqtrgrvp aaelaerlev strtvyrdie alsaagvpvy aergrhggia
       61 llpgfrtdvt gmttdearal filaaqgahs alglddalrs alrkvmaalp aphrpaaelt
      121 grrilvdpdk wttrpsstaa pgdgpsghga aarpavdldv lhtavftdlr lrihyrhsge
      181 trlrtytvdp yglvakagtw ylvadrrgrp qlfradrvas aaltdvpvrr ragvelaevw
      241 qqlrrqvedr padvrvtari rrerldlavr ilggaltgpp rtgdgheagd gepagagdgw
      301 atlelaypvl pavrqllqfg dslevlappe arrvmaeaaa avtavyagdt p
//
LOCUS       WP_457698687             256 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698687
VERSION     WP_457698687.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27253
     Region          51..>137
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          98..245
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mtttehsgsg dvsrslellw glgerpsrgp kpgltldriv aaavavadad glgalsmrrv
       61 atdlgvgtms lyryvpgkae lldlmldkvv efdadahpdp adgwrpamea largsrqqyq
      121 rhpwllqvdq arpllgpnal dsleysvlal agtgltdrek ihvlvsfggf ltgiarteln
      181 salaekrtgi snadfwqsqe pvlskvmltg rypalaalde dtfanddssv felglsalld
      241 giaaliatrt artdap
//
LOCUS       WP_457698683             290 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698683
VERSION     WP_457698683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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 290)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30647
     Region          86..287
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msagtvlhip rgdgpapwgp agaddgparr lywafadclt ivrrdlthlv rqpviiawql
       61 gfpivsvllf vyvfgsamnv gggvdyptfa mpgifamtis fgfmntavav vvdrdhgvtd
      121 rfrslpmaps avvsgrgvad vigasvdlvv lagiavvvgw rshgspaatl aafglllllr
      181 faltwigvyl gllapnqesa gglyavafpf gmissvftpp smmpdwlgtv amwnpvssta
      241 gairelfgnp attggswveq havlmavlwp vvltavflpl avrrfrrlsr
//
LOCUS       WP_457698700             489 aa            linear   BCT 27-JAN-2026
DEFINITION  NCS2 family permease [Streptomyces nigrescens].
ACCESSION   WP_457698700
VERSION     WP_457698700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..489
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50530
     Region          21..482
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mspsattpvd tlknpgpkpp kngfdrffki sergstvgre lrgglatffa mayiivlnpi
       61 ilgsgvdkfg hhldnaqlvt atalmaglst vlmglignvp iaiaaglgin avvslqlapk
      121 mswpdamgmv vlaglvlmil vasglrqrvm daipnglrrs iaigigmfis liglvdagfv
      181 trnpdaahtt vpmglgqggq lkgwpvlvfv iglalmfvli vrkvrgaili gmvsmavvai
      241 ginavvdipd aawglavpnv pekiidtpdf gligqislfg gfqevgvltg clfvftvlls
      301 gffdamgtii gvgeeagltd engnlpgmgr ilmvdgiava gggfgsasan tcfvestagv
      361 gegartglan lmtgglflla liftplatvv psqaatpalv vvgflimasn vqaidwgdft
      421 igipafltii smpftysitn gigigvlafi llraatgrfk eipwllnavg fcflvyfllh
      481 pieqalgvk
//
LOCUS       WP_457698698             496 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698698
VERSION     WP_457698698.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..496
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52671
     Region          56..435
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(66..67,70..71,74,106,161..162,164..166,169,189,
                     192..193,196,271,274..275,278..280,283,307,311,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mstgsgahsa papnshedtv sddatattpg tapgvaagpa atprkgtfss lrirnyrlfa
       61 tgqmvsntgt wmqriaqdwl vlsltgssta vgittalqfl pmllfglygg viadrfakrk
      121 lllftqsamg ltglalaalt lsgqvqvwhv ylvafvlglv tvldnpsrqa fvsemvgqde
      181 lrnavslnsa nfqsarligp avagvlitaf gsgwafllng lsfiapltgl lmmrtaelhk
      241 vdrvprskgq lreglryvsg rpdliwpivl vgfigtfgfn fpiwltafvh hvfhqgagty
      301 slfnalmaag sligallaar rassrlrllv gaamlfgvle iaaalapsfw vfaallvlig
      361 tvgltinvta nssvqmatdp lmrgrvmslf mmvfvggtpl gaplvgwitd sfgprigfma
      421 ggavslaaav viglilarvg glrlridlrr ghrhlafvpr rpaptpsaeq eqeqeqeqeq
      481 eqeqeqeqeq kltpaa
//
LOCUS       WP_457698711             294 aa            linear   BCT 27-JAN-2026
DEFINITION  EamA family transporter [Streptomyces nigrescens].
ACCESSION   WP_457698711
VERSION     WP_457698711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Vastermark,A., Almen,M.S., Simmen,M.W., Fredriksson,R. and
            Schioth,H.B.
  TITLE     Functional specialization in nucleotide sugar transporters occurred
            through differentiation of the gene cluster EamA (DUF6) before the
            radiation of Viridiplantae
  JOURNAL   BMC Evol Biol 11, 123 (2011)
   PUBMED   21569384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="EamA family transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29327
     Region          22..291
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mtaeaqagta gaagargrig svalviggiv slqfgasvav llfpragalg vvtlrlvvas
       61 lvllivcrpr lrghtrgdwa tvlafgvala gmnslfyeai driplgaavt leflgplils
      121 vvtsrrllsl vwaalalggv vllgqegfdg lnltgaafal aagglwaayi llsartgqrf
      181 pqadglalam tvgallslpl givsagsall npvtlglgaa valmssvlpy tlellalrkl
      241 paagfavmms lepaaaatag flvlhqalgw aevlaiglvv iasvgavrsa gahs
//
LOCUS       WP_457698708             390 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698708
VERSION     WP_457698708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42445
     Region          11..70
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msaeitapgp ganvkvlrle rgwlqdhlag rarmstsmlg kiergerplt qgmgavlana
       61 fgitldellg qvpvnagdqd rltelraamr rfdlpadepv redrlaydla elfrlrgdad
      121 lsavthqlpg llrrvqdrah atglpedwsk vaevysavyw laarhrwmtl aelavvrqrq
      181 aaeranaltl avaardeagt flnggdfagg lavvdralvq aesgmrgrtr hlalgllhlr
      241 gmtlagrlrd kktverhikg arksaavids dvnvhgmhfg pentlvhvla thvdlkknae
      301 alaegerylr dghtlpatri gplhmniara klalkdrdga vdslaeawdi apqmakvhpt
      361 slelsrvlvs lhkrsnpkvt alakragikl
//
LOCUS       WP_457698717             538 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD-binding oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698717
VERSION     WP_457698717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..538
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=55509
     Region          69..531
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mkrrtllqag gglaatsval atgcdnktgt agaassgaat eaaagagaar tnaaaaggga
       61 kgrasqsswt algksldgkl vrasdaayas arrlyntryd tlkpsaiayv khpadiaecl
      121 afarrydtpv airsgghsya gwssgngkli vdvsalskvg apsggvtrig agaklidvye
      181 glgahgvtip ggscptvgis gltlggghgv asraygltcd slvgatlvta dgktidcdkk
      241 qhadlfwalr gagngnfgvv telrfrthpa pravmayltw pwakaakvva swqkwgpvqa
      301 deiwsachld arpgntpsvs vaafslgsyr elqnaldkla dqpggpgpak svrltptgyl
      361 damesyagcs skstaqchmp gslpgqtgsg qlgretyaar shffdralst agirtlmdqi
      421 etggrkgvsg nvaltalgga inrvgrtdta fvhrgskfla qyltswpang spgtrtawln
      481 sfhdamrrhs sgaayqnytd pgltnwksay ygaaatrlae vkrtydpqrl fstfpqal
//
LOCUS       WP_457698735             477 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457698735
VERSION     WP_457698735.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..477
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=51143
     Region          102..477
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpvpvphqrt vvlphqagpa ddacadtarv adapgagdat aqgtsapapa vgqeparsap
       61 qgfpepgrpq saeqrlsadh gplhqgltll ligedpnshv pemwdwagrk vrlrtarnlt
      121 eaerlltddv hcilldlppa eptadrdsgd agapgdelgm lrdvlrmats havlvltyet
      181 daeraadavr vgaqdylfrd eldgavlsra vryaverkra dlaqrqltes rmlaqenarl
      241 ergllptpll dgsdlrfaac yrpgrsrall ggdfydtvrt pdgtvhamig dvcghgpdea
      301 algvelriaw raltfaglcg dellatlqkv leheraddei fatlctvdis adgrraglcl
      361 aghpapllar agehpqllpy efggpalgll pharwprrqv elggswslmm ytdgliegri
      421 gkgnqrlgqe gmtelvsrqm aaglsgeell dasvrevrdl nggeltddva vllldrr
//
LOCUS       WP_457698738             147 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698738
VERSION     WP_457698738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..147
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15796
     Region          8..>67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maslnvgnlg eflreqrrta qlslrqlada agvsnpylsq ierglrkpsa eilqqlakal
       61 risaetlyvq agilderrgl dgvevqtail tdpalnerqk qvllqiyesf rkenglgnsk
      121 daaasghedg rgtdsletea dggphat
//
LOCUS       WP_457698743             406 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698743
VERSION     WP_457698743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41294
     Region          13..381
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,63,114..115,117..119,122,142,
                     145..146,149,223,226..227,230..232,235,252,256,309..310,
                     314,318,333,336..337,340..341,344)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrsyrtlfrt peftpfllsf aafaaaqtig glalgtlvfr atgspllsav smfgpqlaql
       61 lgatfllsga drlppratls glavafaagt gvlalpglpv gavfavllaq gliaslgggv
      121 ragllndils kdgyvlgrsv fnmlwglmqv agfatggall allspracll laaalyvmsa
      181 lgtrlgltar pprssgrpsv satwrtnall wssrsrrlty lglwipnglv vgceslfvsy
      241 apgaagtlfa cgalgmfvgd vavgrlvppa lrprlavplr lllaapylff vlqpgvalsa
      301 vatavasvgf gaslvlqerl msrtpddlag qalglhfvgm stlqgvgaal agtlaqltsp
      361 atamtvlaag svtvtltlav ldrhgerqpa vpgtrpgvlp epadtp
//
LOCUS       WP_457698741             332 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457698741
VERSION     WP_457698741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 332)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..332
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35676
     Region          <259..307
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mglwqidtdt larsrfvlsp faetfaslkl lhagtgahpg eeawlrahlp gyrarlagdp
       61 vtallvraal spswiadffc ptscdgesfe esvarvraag agkaranlrv slrgplpaal
      121 erddlperat alltyvweet vrpywgrrrr vleadvvart arvsqggwaa vldslrpgtr
      181 wlgesrfqvn lnayppreia agaellfmpv tpktgwvswe greryavvyp clgvlaedhd
      241 rrpvpaglga ligtaragll vllgtplstt qlvavtgqal gsvgrhlrvl ldaglverrr
      301 agrsvlyvrt aagevlvkas gagtgdrepg vh
//
LOCUS       WP_457698750             108 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698750
VERSION     WP_457698750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..108
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11262
     Region          22..100
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 msgtrdgahp rheldeviha pvrfsivatl aaaekaefaf vrdtvevsds vlsrqvatle
       61 kagyvavtkg yvgkrprtwl altsggraaf aahcqalrai agdgadgd
//
LOCUS       WP_457698752             330 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457698752
VERSION     WP_457698752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  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 330)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 330)
  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 330)
  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 14442355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..330
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=35230
     Region          7..306
                     /region_name="AKR_AKR13A_13D"
                     /note="AKR13A and AKR13D families of aldo-keto reductase
                     (AKR); cd19076"
                     /db_xref="CDD:381302"
     Site            order(24,205..208,211,261,279..283,286,289..290)
                     /site_type="active"
                     /db_xref="CDD:381302"
     Site            order(54,59,84,126)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381302"
ORIGIN      
        1 mtttniptrh lgglavsaqg lgcmgmshgy gesddaqsaa tinraldlgv slldtadfyg
       61 vghneeligr aiagrrdeav latkfgfanr lgeptvirgd aayvreacda slrrlgvdhi
      121 dlyyqhrvdp evpieetvga maelvaagkv rhlglseasa atlrrahavh piaalqsews
      181 lwtrdledei apvcrelgig lvpfsplgrg fltgrytsvq glpetdvrrs qprfadgnle
      241 qnlaivekld elaaekgvsa gqlalawvqh rgtdvvpipg trrqkyleen lgalaielta
      301 eeltaidaaa pagriagtry devsmtfvdg
//
LOCUS       WP_457698756             276 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457698756
VERSION     WP_457698756.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29312
     Region          47..145
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 matvqeeflr tfhaahpavt vramahgqal dgrssyemlr dkvsecgrvl dlgcgdglll
       61 ellagraaga psvlagldls aeelalarrr pgveradlrv graqqlpfad grfdgcvshm
      121 almlmneaer vaaelarvle pggtlaavlg agaaggeace rflqlaaplf raapaaqrip
      181 plgdprlrth egfdavfrpa rfgpaewetv ridltgpper iwrtvgtyyd lglldaavta
      241 elrarfeaes aamalpdgri pcgmnvhiat avrrgs
//
LOCUS       WP_457698758             119 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698758
VERSION     WP_457698758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..119
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13185
     Region          8..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msarkgpyec gldaavdvig gkwkvlllwa laqhphrfge lrrelpkise kvltqqlrel
       61 eadgivhres fpqvppkvey sltgfgrsln ealaplgawg rahmthleat ypqrhpada
//
LOCUS       WP_457698762             194 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698762
VERSION     WP_457698762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21047
     Region          1..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mvrnperraa lvdaaievla rdgargltfr avdtaagvpn gtasnyfagr ddllaqvtaq
       61 ihqriapdpd evtavmaapp sralvvelmg winrrvtenr tgylamlelr leatrrpelr
      121 aeltrairat ldddirfhle sglpgdrtav vliylamtgl mleqltlpgv vpdeetegli
      181 salvdraigp edek
//
LOCUS       WP_457698764             188 aa            linear   BCT 27-JAN-2026
DEFINITION  NADPH-dependent FMN reductase [Streptomyces nigrescens].
ACCESSION   WP_457698764
VERSION     WP_457698764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH dehydrogenase (quinone)
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20935
     Region          7..153
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msehpyrlav iigstregrf apvianwftr hteshphidv dvidldavrp yelrygseey
       61 etfakrvdea dafvvitpey nhsfpaplkh aidllhpqwq akpvgfvsyg gisgglrave
      121 qlrlvfaelh attvretvsf pltgnlfdds ghlhdpapaa qaadtllhql twwavtlrea
      181 ratrpygg
//
LOCUS       WP_457698766             143 aa            linear   BCT 27-JAN-2026
DEFINITION  ankyrin repeat domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457698766
VERSION     WP_457698766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=14894
     Region          <30..>139
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(34..36,38..39,43,46,55,57,59,63..64,67..69,71..72,
                     76,79,88,90,92,96..97,100..102,104..105,109,112)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          57..88
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          90..119
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msdansepqg peaiehahdp evlqlaakvf dlarhgdtdt vaayvdagvp anltndkgds
       61 lvmlaayhgh patvevllqr gadadrpndr gqtplagavf kaedevvkvl mahgadptag
      121 tpsaidtarm fekaellklf gae
//
LOCUS       WP_457698776             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698776
VERSION     WP_457698776.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27652
     Region          2..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mridvtdlsv evagnrlvhd itlragsgrv vglvgpngsg kstllrcvyr alrpaagtvr
       61 lddadlhamd artgarllaa lpqeastefd ftvaevvamg rlphqrgsgr asaadrerct
      121 ralarvgadh lagrgflsls ggekqrvlia ralvqdprvl vldeptnhld iaqqlavlal
      181 vrdsgltvlt alhdlnlaal hcdelyvidr grivaagppy dvltpellae vfgvrahrvr
      241 hpesgavqll fdrltapads
//
LOCUS       WP_457698778             364 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698778
VERSION     WP_457698778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36383
     Region          42..357
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mattsahptt dgtgappaar rlpvppllaa ltavllgsll cgvglgaagl swaevlrylg
       61 agltggriss devaaytivw elrfpravla avvgaglaal gvavqalvrn aladpfvlgi
      121 ssgaavgana vllfgalgal gvwalsaaaf vsallamalv yaaartahgl tplrlvltgt
      181 amyygfsalt tlmvftadrg eaarsammwl lgslsgagwg svpiaaaava aalahlllsa
      241 grlnalamgd etatalgvqv hrlrrelflv aaagtgavva vsgaigfvgl mvphvarmlv
      301 gadhrrvlav apllgavllv wvdllsrvll apvelpvgvl tavigvpcfv vlmrrrgytf
      361 ggga
//
LOCUS       WP_457698781             281 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase [Streptomyces nigrescens].
ACCESSION   WP_457698781
VERSION     WP_457698781.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31344
     Region          13..276
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msrsdvlvda dwveahledp kvvlvevded tsaydknhik navridwkqd lqdpvrrdfv
       61 dqagfeklls akgianddtv vlyggnnnwf asyaywyfkl yghdsvklld ggrkkwelds
      121 rdlvdgsevp qrpatdykak aqntairafr ddviaaigdl nlvdvrspde fsgkllapah
      181 lpqeqsqrpg hvpsarnipw sknanddgtf ksddelkaly egesvdlakd tiaycriger
      241 saltwfvlhe llgqtnvkny dgswteygsl vgvpielgaa k
//
LOCUS       WP_457698783             233 aa            linear   BCT 27-JAN-2026
DEFINITION  LmeA family phospholipid-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698783
VERSION     WP_457698783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Rahlwes,K.C., Osman,S.H. and Morita,Y.S.
  TITLE     Role of LmeA, a Mycobacterial Periplasmic Protein, in Maintaining
            the Mannosyltransferase MptA and Its Product Lipomannan under
            Stress
  JOURNAL   mSphere 5 (6) (2020)
   PUBMED   33148829
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Rahlwes,K.C., Ha,S.A., Motooka,D., Mayfield,J.A., Baumoel,L.R.,
            Strickland,J.N., Torres-Ocampo,A.P., Nakamura,S. and Morita,Y.S.
  TITLE     The cell envelope-associated phospholipid-binding protein LmeA is
            required for mannan polymerization in mycobacteria
  JOURNAL   J Biol Chem 292 (42), 17407-17417 (2017)
   PUBMED   28855252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10567863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..233
                     /product="LmeA family phospholipid-binding protein"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24254
     Region          20..225
                     /region_name="LmeA"
                     /note="LmeA-like phospholipid-binding; pfam11209"
                     /db_xref="CDD:431728"
ORIGIN      
        1 mralrvllvl vvilgglfva adrvavglae dkaaekiras qgldktptva ikgfpfltqv
       61 agrslqevda dlggiearae gralridrls ahffdvglts dytsiesaat atgnaritya
      121 dltkaagggv kisyggekng rsqvkispnv plpvslnvtg sltivngttv rlradglpgm
      181 ckalpgceak vraqtdhdwk ldqlpgnlkl dkvvtmhegi sisasgkdvk lpg
//
LOCUS       WP_457698786             577 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698786
VERSION     WP_457698786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 577)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 577)
  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 577)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..577
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62961
     Region          2..574
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mlvrlarahl rphrrsisli vllqliqtla tlylptlnad iidngvvqgd tgyilrvggf
       61 mvavtllqiv caigavyfga rtamalgrdi raavfdrvqs fsarevgtfg apslitrttn
      121 dvqqvqmlvl mtftmmvsap imcvggvima lnqdvplsgl llvivpvlgm lvslivrrmr
      181 plfrgvqeri dtvnrvlreq itgirviraf vrdrhererf agantdlydv slragrlmsm
      241 mfplvmlivn lssvavvwfg glridsgamq igaltaflsy lmyilmsimm atfmvmmlpr
      301 aevcaeriqe vlatdssvtp pehpvtelrr hgelelrgve frfpgaeqpv lkdisltarp
      361 gettavigst gsgkstllgl vprlfdatgg tvlvdgedvr tldqetlaka iglvpqkpyl
      421 fsgtvatnlr ygnpdatdde lwhaletaqa rdfvermesg ldapiaqggg nisggqrqrl
      481 aiaralvrrp eiylfddsfs aldyatdaal raalaretdr atvvivaqrv stirgahriv
      541 vldegrvvgt gthaelmadn etyreivlsq lteqeaa
//
LOCUS       WP_457698788             672 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698788
VERSION     WP_457698788.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 672)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 672)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 672)
  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 672)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..672
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71967
     Region          48..666
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mttadkgaap eaeapaatde tpqpatrrgp apavgparmm ggqpteksmd fkgsgkrlla
       61 qmrpergims ialalgalsv altvvgpkvl ghatdlimsg iigrqlpdgl traqaagrlr
      121 ahgqdgladm igtmpvvpgh gidfgavgqv llwvtliyaa aslfgfiqar iatrvvqqav
      181 frmreqveek larlplsyfd kqqrgevlsr atndidniqq tlqqtlsqiv aslltivgvl
      241 ammfwispll alvalitvpv svvvatkvgk raqpqfvqqw kttgklnahi eemytghslv
      301 kvfgrqresa elfreqneal yaagfkaqfi sgiiqpammf ignlnyvlva vvgglrvasg
      361 alsigdvqaf iqysrqfsqp ltqvasmanl vqsgvasaer vfelldaaeq dpdpeqparp
      421 driegrvefe dvsfryapdk pliedlslav hpgqtvaivg ptgagkttlv nllmrfyevr
      481 ggritldgvd iaamsreelr ahigmvlqdt wlfggtiaen iaygapagtp mdkivaaara
      541 thvdrfvrtl pdgydtvldd eggnvsvgek qlitiarafl aepailvlde atssvdtrte
      601 vliqhamaql rtgrtsfvia hrlstirdad vilvmengai veqgphdall aangayarly
      661 aaqfaepvse tg
//
LOCUS       WP_457698790             193 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698790
VERSION     WP_457698790.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19954
     Region          2..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mivaaalplv aeygaavtts qiaraagige atifrafkdk devldacvae avgtdhvlre
       61 lasisldepl agrlaeaaea lrahmermgt vvgalhasgh rrgrgpgagt rdgedpppds
      121 rtqsvtalrn avieliepdr tafrlspekv aaaflgllft rlqtpapead apltpeelia
      181 vllhgtlnap gsa
//
LOCUS       WP_457698800             117 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457698800
VERSION     WP_457698800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..117
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12945
     Region          15..113
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mepdiagkpv agkaesqlrk gvleycvlai lrdgprygve lletlgavnv matsqgtiyp
       61 llsrlrrdgl vetrwqesps gpprryyelt ppghaalkef taiwphfrda vdhfitd
//
LOCUS       WP_457698802             172 aa            linear   BCT 27-JAN-2026
DEFINITION  SigE family RNA polymerase sigma factor [Streptomyces nigrescens].
ACCESSION   WP_457698802
VERSION     WP_457698802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Paget,M.S. and Helmann,J.D.
  TITLE     The sigma70 family of sigma factors
  JOURNAL   Genome Biol 4 (1), 203 (2003)
   PUBMED   12540296
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Lonetto,M., Gribskov,M. and Gross,C.A.
  TITLE     The sigma 70 family: sequence conservation and evolutionary
            relationships
  JOURNAL   J Bacteriol 174 (12), 3843-3849 (1992)
   PUBMED   1597408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11496258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="SigE family RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18832
     Region          1..155
                     /region_name="SigE-fam_strep"
                     /note="RNA polymerase sigma-70 factor, sigma-E family;
                     TIGR02983"
                     /db_xref="CDD:132028"
ORIGIN      
        1 mnerefdafy sgsvgrltgq lyamtgdlae sqdvvqeafa rawerrtgld aggapeawvr
       61 tvawrlavsr wrrvraalal vrrqgppadv pppdpnhvll vealraipea qrraivlhhl
      121 cdlpvhevaa etgrpvgtvk vhlrrgraal arlladseld prsgelsevn rg
//
LOCUS       WP_457698815             378 aa            linear   BCT 27-JAN-2026
DEFINITION  epoxide hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698815
VERSION     WP_457698815.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42510
     Region          7..112
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          87..>198
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mvdsdsvvpf vlavsdeele dvrdrlrrvr lpeaetvddw sqgiprsyvr elcrywleey
       61 dwrrleaeln drgqwrtvid glgihflhvr spradarpll mthgwpgsvv efldildelt
      121 dppagepafh vvapslpgfg fsdkpagtgw gieriadawa elmarlgyer flaqggdwga
      181 fvttaigvrh pdrvealhtt mppvqppsgf tedelsefer adlaaarevl aaergymvlq
      241 strpqtlgyg ladspagqla wivekfqgwt dcdghpenav srqrlldnaa iywfgacgas
      301 sarlyweslp prnwtpvtvp savsrfpkep fraprawvea rfenlrywns ldrgghfpsl
      361 evphlfvsel raafgres
//
LOCUS       WP_457698819             233 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698819
VERSION     WP_457698819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..233
                     /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=25408
     Region          <87..217
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mdpqeqqasw lpqdaamsdr eraifwrnrv lilfdhiplp safceadgti rvvnpalate
       61 wgtlpgrltg rnalklfrpr tstpfdaiae avrlrrrsri psevswtsgs gaerqgeliv
      121 dvvsdlpdap pnlllmlrvl dqptpppapd pherpqvsam earilaltag gsttaqiata
      181 lgltpdgvny hfrtlsqrwg ttnraalvar ayttgvltpr twpptadhrg aqs
//
LOCUS       WP_457698823             207 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698823
VERSION     WP_457698823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22002
     Region          2..199
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkrvdheer raqiaealiq vagrrglhav gmrdvaaeag vslrlvqyyf etkekllfyg
       61 lqhltdrfta rvgarlraag pnpgpratte alllaslptd egsrtfhlly ssysilsvtd
      121 dalaaqpfid npdaaenalt glleqaqasg lagpgidart eaisllamta tmgtsilvgq
      181 rspesaiavl rhhldrifat vetsaag
//
LOCUS       WP_457698840             305 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698840
VERSION     WP_457698840.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30834
     Region          1..300
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,121,125,147..152,171..172,174,187,
                     210..211,232..233)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mlaltfaeyg npsvlqvnev pephagpgqv riavraagvn pidwkirsgf mkdvmplrlp
       61 aiagldaagv vdevgegveg vsvgtgvfgs gngvsaqyav ldhftakpas mswsqaaalp
      121 apaetaqrtl gilgppvagq tllidgaagg vgsvaaqfai adgvavigta sesnhdylrs
      181 lgivpttygp glkervagla psgvdfaldt agkgsvpeli eivgepgkvv siadfsapqy
      241 garvtgagtd pqrfdalpka arfyeegkla iaidsefpla eaakahkrse gghlsgkivl
      301 tvpqp
//
LOCUS       WP_457698842             326 aa            linear   BCT 27-JAN-2026
DEFINITION  NmrA/HSCARG family protein [Streptomyces nigrescens].
ACCESSION   WP_457698842
VERSION     WP_457698842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Stammers,D.K., Ren,J., Leslie,K., Nichols,C.E., Lamb,H.K.,
            Cocklin,S., Dodds,A. and Hawkins,A.R.
  TITLE     The structure of the negative transcriptional regulator NmrA
            reveals a structural superfamily which includes the short-chain
            dehydrogenase/reductases
  JOURNAL   EMBO J 20 (23), 6619-6626 (2001)
   PUBMED   11726498
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142859
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..326
                     /product="NmrA/HSCARG family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35558
     Region          8..263
                     /region_name="NmrA_like_SDR_a"
                     /note="NmrA (a transcriptional regulator) and HSCARG (an
                     NADPH sensor) like proteins, atypical (a) SDRs; cd05251"
                     /db_xref="CDD:187561"
     Site            order(12,14..17,40,82..83,85,126,155,174..177,180)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187561"
     Site            order(151,155)
                     /site_type="active"
                     /db_xref="CDD:187561"
     Site            220
                     /site_type="other"
                     /note="regulatory binding site [polypeptide binding]"
                     /db_xref="CDD:187561"
ORIGIN      
        1 mtstkkiiav vgatgaqggg lvrailadpd gpfavraltr naesdkarel aaqgaevvsa
       61 dlddenslrr afdgaygayv vtnfwvqrsp eeemartrae melaqaaaaa raakdaglqh
      121 vvwstledtr phfdrlgidv ptvmgtykvp hfdakgeana fftelgvptt flqptfyfea
      181 fitggqgpyr nergelvltm pmadnklali aaedigktal gifrrgrefv gktvsiageh
      241 ltgeelaakf tsvlgekvvy rpvthdemra sgqpgvlefa nmyqfysdas eyftgvrdia
      301 lvrqlnpdlr sldswlkehk hdiprd
//
LOCUS       WP_457698857             165 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphoribosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457698857
VERSION     WP_457698857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Moynie,L., Giraud,M.F., Breton,A., Boissier,F., Daignan-Fornier,B.
            and Dautant,A.
  TITLE     Functional significance of four successive glycine residues in the
            pyrophosphate binding loop of fungal 6-oxopurine
            phosphoribosyltransferases
  JOURNAL   Protein Sci 21 (8), 1185-1196 (2012)
   PUBMED   22610485
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Sinha,S.C. and Smith,J.L.
  TITLE     The PRT protein family
  JOURNAL   Curr Opin Struct Biol 11 (6), 733-739 (2001)
   PUBMED   11751055
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Vos,S., Parry,R.J., Burns,M.R., de Jersey,J. and Martin,J.L.
  TITLE     Structures of free and complexed forms of Escherichia coli
            xanthine-guanine phosphoribosyltransferase
  JOURNAL   J Mol Biol 282 (4), 875-889 (1998)
   PUBMED   9743633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0106130 - purine
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18190
     Region          1..153
                     /region_name="Hpt1"
                     /note="Hypoxanthine phosphoribosyltransferase [Coenzyme
                     transport and metabolism]; COG2236"
                     /db_xref="CDD:441837"
ORIGIN      
        1 msdvrenlty erfggairel aqtiaddgye pdvvlsiarg gvfvagglay aldcknihlv
       61 nvefytgvgt tlempvmlap vpnvidfsek kvliaddvad tgktlklvhd fcqgtvaevr
      121 saviyekshs lvkceyvwkr tdewinfpws veppvvrreg qilda
//
LOCUS       WP_457698865             314 aa            linear   BCT 27-JAN-2026
DEFINITION  Yip1 family protein [Streptomyces nigrescens].
ACCESSION   WP_457698865
VERSION     WP_457698865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Shaik,S., Pandey,H., Thirumalasetti,S.K. and Nakamura,N.
  TITLE     Characteristics and Functions of the Yip1 Domain Family (YIPF),
            Multi-Span Transmembrane Proteins Mainly Localized to the Golgi
            Apparatus
  JOURNAL   Front Cell Dev Biol 7, 130 (2019)
   PUBMED   31417902
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10522553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="Yip1 family protein"
                     /GO_function="GO:0031267 - small GTPase binding [Evidence
                     IEA]"
                     /GO_process="GO:0016192 - vesicle-mediated transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33373
     Region          146..300
                     /region_name="Yip1"
                     /note="Yip1 domain; pfam04893"
                     /db_xref="CDD:461468"
ORIGIN      
        1 mgrgrdarpa qngqqgqqgq qapygqqgpy gqqppsppgq wqpapqqygg gpqgqpqphg
       61 qygepeyfgd ggyqpqqqsy apysndnnpg htqqfsvgda pdaygapagr ydggtdeyga
      121 ggtyragqtg appagprlhw kqllpgivlr pdatfwqmrd hqvwapaliv tfvygllavf
      181 gfdkaredvl natlsniipw vgitavmfii galilgavth tmarqlggdg awqptiglam
      241 limtisdapr llfamflggd stlvqvlgwl twlatgyllt tmvskshdlp wpkalgaaai
      301 qlvallalvk lgtl
//
LOCUS       WP_457698875             212 aa            linear   BCT 27-JAN-2026
DEFINITION  LutC/YkgG family protein [Streptomyces nigrescens].
ACCESSION   WP_457698875
VERSION     WP_457698875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..212
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22183
     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 mtataretvl rrvrdaltls dgpevtvpra yrtgrslpde erlalfvdrl vdyraqvrtc
       61 tagttaavla evlqahgaqr tgvpagldpa wlagydgetv tdsadvpvlr ldaldgvvta
      121 stvscaetgt ifldgaaadq grraltlvpd lhicvvdlss vragvpeava qltpehpitl
      181 isgpsatsdi elervegvhg prtlvvvirt da
//
LOCUS       WP_457698871             126 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457698871
VERSION     WP_457698871.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 126)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..126
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13395
     Region          27..99
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(28..29,31,34,37..38,41..42,45,75,94..95,97..99,
                     101..103)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(29..30,34..36,49..51,60..63,65..66,69..70,72..73,
                     79..81,86..88)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(49,52,94)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mghgmddrrt ttrerldavg aadvaatlqa lstpsrlhil arlqegpcav gdlaaavgme
       61 qsacshqlrl lrnlglvtge rngrsivyal ydhhvaelld qalfhvehlr lglrdapsga
      121 advmhg
//
LOCUS       WP_457698883             261 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698883
VERSION     WP_457698883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28133
     Region          6..236
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtaewrpvrq srthelvler ieervlagel kagdrlpper elapvlgvsr salrealrvl
       61 etigvlvaqa grgpdagari vrnpddalgr llrlhfalgs yrlhdvlear vvlerssfea
      121 aaehasaadl deaeallgrm repgvgaadf ndldtrfhva iarssgnqlt stltsavres
      181 vrplilqale aaedwpatae alnaehtell rlvragkgaq aadlaeahir gfhgrlvden
      241 apaeqeqeqv qgdegraatd g
//
LOCUS       WP_457698879             255 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698879
VERSION     WP_457698879.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..255
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27158
     Region          <2..241
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrialfatcl gdtlfpeavk stavllarlg hdvvfppqqt ccgqmhvntg yqrepvplvr
       61 nfaeqfgdps ieavvvpsgs cagsvrhqha svaerygdaa lcagvatvrt ktyelseflv
      121 dvldvsdvga yfphrvtyhp tchslrmlrv gekplrllra vegidlvelp eadvccgfgg
      181 tfavknaets tamlrdkmgh vtgtgaevct agdssclmhi agglsrirag trtlhlaqil
      241 astrttphvl teaar
//
LOCUS       WP_457698891             390 aa            linear   BCT 27-JAN-2026
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            nigrescens].
ACCESSION   WP_457698891
VERSION     WP_457698891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ferraro,D.J., Gakhar,L. and Ramaswamy,S.
  TITLE     Rieske business: structure-function of Rieske non-heme oxygenases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 175-190 (2005)
   PUBMED   16168954
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Boyd,D.R., Sharma,N.D. and Allen,C.C.
  TITLE     Aromatic dioxygenases: molecular biocatalysis and applications
  JOURNAL   Curr Opin Biotechnol 12 (6), 564-573 (2001)
   PUBMED   11849939
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Schmidt,C.L. and Shaw,L.
  TITLE     A comprehensive phylogenetic analysis of Rieske and Rieske-type
            iron-sulfur proteins
  JOURNAL   J Bioenerg Biomembr 33 (1), 9-26 (2001)
   PUBMED   11460929
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Nam,J.W., Nojiri,H., Yoshida,T., Habe,H., Yamane,H. and Omori,T.
  TITLE     New classification system for oxygenase components involved in
            ring-hydroxylating oxygenations
  JOURNAL   Biosci Biotechnol Biochem 65 (2), 254-263 (2001)
   PUBMED   11302156
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="aromatic ring-hydroxylating oxygenase subunit
                     alpha"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43514
     Region          27..381
                     /region_name="HcaE"
                     /note="Phenylpropionate dioxygenase or related
                     ring-hydroxylating dioxygenase, large terminal subunit
                     [Inorganic ion transport and metabolism, General function
                     prediction only]; COG4638"
                     /db_xref="CDD:443676"
ORIGIN      
        1 mtttptepsp tapttpatga spsliatlag hhytdpeifr qeqekiferl wfcavrgadl
       61 ekpgafrtvr igresvlitr nragelrafl nicrhrgaql cteesgevrr nlqcpyhawt
      121 ydldgrlvaa pnlqkmpdld rterglvtvp lrewlgyawv cladeppsfe dtvisaaier
      181 lgdaasldry rteglvlgkr ltydvranwk liienfmecy hcatihpelt dvlpefadgf
      241 aaqyyvghga afadeatgft vdgtegfgrl pgieetqdrr yyaitvrpqv fvnlvpdhvi
      301 vhrmfpmapd rtvvecdwly lpeivdsgad vsksvelfhr vnaqdfdace rtqpamssra
      361 yrdggvlvps ehhigafhqw vtdclegggg
//
LOCUS       WP_457698898             390 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698898
VERSION     WP_457698898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..390
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40795
     Region          1..385
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mksvavigas laglyaaral raqgfdgrlv ivgeehhrpy drpplskdfl tgatadqgql
       61 aladaeeiae ldaewllgtr atgldlhgrt vlldggrslt tdgvvlatga tprrlpgsap
      121 tgthtlrtle daqalraqlt rgavrvvvig ggfigaevas scarlghdvt vveaaplplv
      181 pqlgdtmagi csalhadhgv tlltgtgvar lhdggtgnrv tgveladgrl lpaevvvigi
      241 gvrpntawle gsglplddgv ccdaggvtpq hrivavgdva rvdgiraehw tsateqaava
      301 arnllagstv athqslpyfw sdqygvriqf agrrlptdtp rivegspddr sflacyerdg
      361 rttavlalnr prpfmrlrre laratqpvtt
//
LOCUS       WP_457698913             378 aa            linear   BCT 27-JAN-2026
DEFINITION  alkene reductase [Streptomyces nigrescens].
ACCESSION   WP_457698913
VERSION     WP_457698913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40645
     Region          12..341
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(32,34,66,108,235,305,325,327..329)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(32,34,66,108,110,117,185,188,235,242,305,325,
                     327..328)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(34,110,185,188,328)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msstlpttld qpllrradlg glplpnrvvm apltraraan aalvptelha ayygqratag
       61 liitegtwvs eraigfvhvp giyredqiag wrrvtdvvha lggrivlqlw htgaashpdh
      121 lggelpggps ainprtrsft aggfketvtp remttadiaa tvadfrtaae narragfdgv
      181 eigalgafli tqflnprlnh rtdayggdrt grrrllldiv davaepwhgr gvgvrlgpyw
      241 tegehfrade emladydalv telndrplay lhlrgrdrta adgapdlaal arfrqrfdgp
      301 lianngfgre sgnavidagl adavsfgthf ianpdlvsrf alrqepavgd pasyytggae
      361 gyvdypvsgm gvpllerr
//
LOCUS       WP_457698915             366 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698915
VERSION     WP_457698915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..366
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39785
     Region          5..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          180..310
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mhksvdltel dlsivhalql aprapwntlg evlgvdhttv arhwarleeq gsawlmayyp
       61 awhdglcrar vevdcaggav davaqalvhd phvvsvdlth nggdlqlmvs agnlgvlsry
      121 vtdrlhrlpg veriavhpvt reyadgrqwr ldalnaeqvr qltaispaph ggtvspgpee
      181 lrilsvlgpd grcswtqlae rtkvsaatvr rkvhrmmreg tlafrcevaa hsagwsvqvl
      241 ytaqcpanrl esaarelvvl pgvrsvaala gpanlavtaw lrsaadiqql evrmlrrvqe
      301 lvitrrsval ralkrmgrll gadgrrigyv pmdvwsdpvc ggsvkraltp sshrrssrgt
      361 pipltg
//
LOCUS       WP_457698917             545 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457698917
VERSION     WP_457698917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..545
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57675
     Region          8..545
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mhthpqtrtt dafttrifta drvhtlatgt alpafatvge wiaaagtvee lrarfpeapv
       61 hdfgdrtvvp gfndahqhpt smaeamlhvd lspervrthe qleaalrgra aelpsgawli
      121 garydhgktt ggtvikrqdl dricsdrpvm vthiashwav fnsaalsaag ldddseppag
      181 gdygrdaagr ldgilyeqam mhlrsspapg rdpvvpvspl adriealgry qrmmhsagit
      241 svgdaavage glellqaada tgaltlrvna lllytavpgm esiglrtglg strlriggvk
      301 alvdgavagg tclleepyeg tcehgiqams eaelhdvvrr vhgsggtvcv hangdrairl
      361 vldaveaaqa adprpgtrhr iehcslvddp ilrriavlgm vtvpfgsyva fhgdkltgwy
      421 gakrlermfa hrdlldagip tagssdypcg pyepllglqs cvtrqtadgt vlggnqrita
      481 aealalyttg aayaageeav kgrltpgmla dftvldedpl ttdpqrlaai gvsetwvgaq
      541 qvwqa
//
LOCUS       WP_457698921             472 aa            linear   BCT 27-JAN-2026
DEFINITION  sodium:solute symporter family protein [Streptomyces nigrescens].
ACCESSION   WP_457698921
VERSION     WP_457698921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 472)
  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) (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 472)
  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 472)
  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 472)
  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..472
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..472
                     /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=48704
     Region          1..468
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 maiavfcviv aaslviavaa rrgsgkgdvs hflvggrsfn glllfflsvg evysiatllg
       61 fpagiysqga gygvwfigyi llaypigyyv gplmwraakr ydamtvpdvm rarfgsrale
      121 itvalatvtf lltyaqfqfa glhaalaalg fhltpettvv itvaislvyv tltgikapam
      181 vsvlkdiali vavglvglfa vsglrgsaag pgalfdaare agspatltge plvhalttmv
      241 vqslgfylgt mglafvvagr sertvrrtiv vqplymlmyp llvfasyysl ahlkladpnh
      301 afpaaaqatg adwlvglsag aaaltglltv svlalgfggv lsrnllpaad parqrrwvsa
      361 stagylvvsa vlavtvqglm ldvlafayvi gsqvvpawlv tlfsrritap avltglvvgl
      421 gvgvalqasg hpvvhgvngg lialtvnlai tfgsglflar rtpapaaepa lt
//
LOCUS       WP_457698923             430 aa            linear   BCT 27-JAN-2026
DEFINITION  benzoate/H(+) symporter BenE family transporter [Streptomyces
            nigrescens].
ACCESSION   WP_457698923
VERSION     WP_457698923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..430
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43422
     Region          35..424
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mssktptphp daappgsapp epasaaegsp epgtrpglfr daslsavlag fvavvvsysg
       61 plvivlaaas aghlntaqts swvwaisigs gltcialslr tkmpvitaws tpgaallvts
      121 lgaysyaeai gafivtglvi tlvgltgvfg wlmrqvptav vsamlagilf sfgtgvftsl
      181 ktapviagsv lvayllakrw lpryavlval aagvaasavs srlhiqldri elakpvlttp
      241 efslasligi avpmilatla sqnapgmavl tasgyepkdr lligstglvs talapfgsha
      301 inlaaitaai ctgpeshrdp krryvagvsc gafylligaf gstlvvlfag lpkelvaava
      361 gvallgalag gltgavkeek dreaalitfl atasgvtlfg igsafwgllf gviahfvltr
      421 rrgtptasak
//
LOCUS       WP_457698925             400 aa            linear   BCT 27-JAN-2026
DEFINITION  trans-sulfuration enzyme family protein [Streptomyces nigrescens].
ACCESSION   WP_457698925
VERSION     WP_457698925.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Messerschmidt,A., Worbs,M., Steegborn,C., Wahl,M.C., Huber,R.,
            Laber,B. and Clausen,T.
  TITLE     Determinants of enzymatic specificity in the Cys-Met-metabolism
            PLP-dependent enzymes family: crystal structure of cystathionine
            gamma-lyase from yeast and intrafamiliar structure comparison
  JOURNAL   Biol Chem 384 (3), 373-386 (2003)
   PUBMED   12715888
REFERENCE   3  (residues 1 to 400)
  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   4  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="trans-sulfuration enzyme family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=42952
     Region          14..395
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mnnsetftpw tqeyrpetra aqgdgwrcpt tgavpppigl gatfardsey rapaglaylr
       61 dqgtpgyeqv ekvvaglegg sdalvfssgm aaatsvfqvl pagarvvvpq tmyfgltkwl
      121 lefgpqrgle vvqapmndld avaaavtaap talvwaespa nptwtvtdia acaeiahrag
      181 alfgvdntvp tpvhsrpfal gadlimhsgt kylnghtdvv agllvkapgs seardavwer
      241 lqlhrrltgp ilgpmetyll mrgirtlypr mrqisetama vaehfaehpr irrvaypgla
      301 tdpghdvaar qmtggfsgml slhvdgewqq slrtanhcel firatslggv esliehrytf
      361 egpgstspkd mlrlsigles padlvadleq alekavkedr
//
LOCUS       WP_457698927             616 aa            linear   BCT 27-JAN-2026
DEFINITION  FAD/NAD(P)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457698927
VERSION     WP_457698927.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468249
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..616
                     /product="FAD/NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66145
     Region          1..588
                     /region_name="YdhS"
                     /note="Uncharacterized NAD(P)/FAD-binding protein YdhS
                     [General function prediction only]; COG4529"
                     /db_xref="CDD:443597"
ORIGIN      
        1 mnhrpvsvai vgagsrglgv ferlvahcla qpapltvhli dpqpfgagfh lpaqpdhlll
       61 ntvcaqlsaf adphmvdgpv pisgpslhaw crrrdlrlad dgytvrpgag reiqpndflp
      121 rrllseyltw aageiadaap ehvtlvrhrt tavdihpgts etetvvladg tridadavfv
      181 tvghhslyrp appapdprlv trpyplpeal dsigpgerva ilgmgltamd viatltlgrg
      241 gahtttehgm sylpsgqepl ivltnrsgmp srsrprlhpg rmrfaplalt terldairar
      301 rtdrridfaa evlplveaem elayyrvllg remgdatdag lemarrcaqa gdetlldelr
      361 arfgttpvpg ilsaglsdrl wtgysayrdw ftaevaadla eareglgvsp lkealevlrd
      421 hrdvlravid ppgvddasla affgeftstv nrlvigpqld rsaellslid agivrlgpgp
      481 qpkivapagq gpwrlestcl aeplrmevdh vvqahvtepg adrapgtllg tlvaagrvrt
      541 lahrggtvhg ldvtrqgqgi drtgtpqprl fflgphtegs syynhyvpsp gapsralldg
      601 elalstalps litrkr
//
LOCUS       WP_457698937             334 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA family dioxygenase [Streptomyces nigrescens].
ACCESSION   WP_457698937
VERSION     WP_457698937.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Islam,M.S., Leissing,T.M., Chowdhury,R., Hopkinson,R.J. and
            Schofield,C.J.
  TITLE     2-Oxoglutarate-Dependent Oxygenases
  JOURNAL   Annu Rev Biochem 87, 585-620 (2018)
   PUBMED   29494239
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Schofield,C.J. and Zhang,Z.
  TITLE     Structural and mechanistic studies on 2-oxoglutarate-dependent
            oxygenases and related enzymes
  JOURNAL   Curr Opin Struct Biol 9 (6), 722-731 (1999)
   PUBMED   10607676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="TauD/TfdA family dioxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36491
     Region          33..309
                     /region_name="TauD"
                     /note="Taurine catabolism dioxygenase TauD, TfdA family;
                     pfam02668"
                     /db_xref="CDD:367137"
     Site            order(107,109,134,301)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(107,109,301)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
ORIGIN      
        1 mvsslpislp elerepgkpp llragatdsa ahwaaerrda lravvaehga vlvrglgmsd
       61 paevgavlqg lavaplcere afavrqtyse gvyssskwpp nqpmcmhhel sytlefpglm
      121 lfaclsapta ggttavadsa avldalppal terferegwl ltrsyhpeig atldqafgte
      181 drdaverycr ahaiectwqp dgglhtrqrr savvrhpvsg rrcwfnqiaf lnewtmapev
      241 rdylideygp dglpfnthyg ngdpltedvv hllnevyeah tarrpweagd lllvdnvgta
      301 hsrepfegpr dvvvaladpv rladcsptve vtlp
//
LOCUS       WP_457698941             276 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698941
VERSION     WP_457698941.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29294
     Region          78..275
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msattlaapl skpgadegri glranlrhig alvrrnalqi khdpesmfdv llmpvifill
       61 ftyvfggaia gkgnqqeyiq rlvpgmmamm gmniamavgm gvnedfrkgv mdrfrtmpia
      121 rssvliakiv veigrmliat aillgmgfll gleirgtipe flgaivlsta fgaalmwifi
      181 llglavstpq avqgmamvvl mplqfgssif apttsmpgwl egftqvnpvs nladaarali
      241 ngqgavahpa lvtlgwavai tavtmplavs rfrkkt
//
LOCUS       WP_457698943            1197 aa            linear   BCT 27-JAN-2026
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698943
VERSION     WP_457698943.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1197)
  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 1197)
  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   3  (residues 1 to 1197)
  AUTHORS   van der Biezen,E.A. and Jones,J.D.
  TITLE     The NB-ARC domain: a novel signalling motif shared by plant
            resistance gene products and regulators of cell death in animals
  JOURNAL   Curr Biol 8 (7), R226-R227 (1998)
   PUBMED   9545207
REFERENCE   4  (residues 1 to 1197)
  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 18717734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1197
                     /product="AfsR/SARP family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP 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=126788
     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"
     Region          189..1150
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhygilgttq agradgtpva lggarlrall aalalrpgra lspelligdi wgaeppadaa
       61 galqalvgrl rralghaaia svdggyrlcv epdavdlhrf erlaaeggra laaadparaa
      121 allddalalw rgpaladlpd agaeaaraer rrldaqctri aadlalgrat qalptllalc
      181 edhpldeplq alrlhalraa grtaealaay eeirtglaer lgadpgpelr tlhaellrpp
      241 ptpplpptpg dpapaptpng tgtsygtats ygtgtrpayg tgtsygtats ygtgtgpayg
      301 tgtphspgtp spgtphdtah tatpvpltvp rphpvphpra rpgnlrarlt sfvgrdsdla
      361 airadlsthr lvtllgpgga gktrlsqega etaaaavpda wphgvwlael apvddpqtvp
      421 eavltalgar etvvrgttae glraatdpta ldplarlaeh cagrrmllvl dncehvidaa
      481 aelaerllad cpgvtvlats replavpgev lrpveplpdp valrlladrg aaarpgfrve
      541 ddpaacteic rrldglplai elaaarlrll sprqladrld drfrlltsgs rtllprqqtl
      601 ravvdwswel tdeperavlr rlsvfaggcd laaaeevcag dgvdgrevag llgslidksl
      661 vvaapagqgg gagraagtgg qmryrlletv geyaaerlde agerggaerr hlvayrelar
      721 ttdpllrgpg qragmerlel ehdnlrtalr ralaahdehe alclvlslqw fwslrdhrsd
      781 arhwstaaaa lgpnpfaapv vpapdlherp idkpppmape qllearrear lvalasrdsd
      841 iaalrdpvvq eelagmltay rsgmpqtckv pgvmwyyavl itgrfdelae vvdgavracr
      901 dfgydwelay vlqlrskifn drpgglaqaa rdadealrlf rrlgdawgaa ealagrgenh
      961 ekrgaygaaa gdyraamvaa edlgahgqil llrcrlgavl iedgqaeage rmlrevlada
     1021 vkgnsgrdte pfarltlamw ltatgrlqea rvelqrvqel fisrapdlfa gmlqallisl
     1081 dvdegrregl lprfrqsmel mqdslaqtva pdlpvvqllt garvlmaerg ekagrdaarl
     1141 vgaydalrad gqvppqlvrr drarteaaar allgdtayar ahaeggglsl geatali
//
LOCUS       WP_457698944             268 aa            linear   BCT 27-JAN-2026
DEFINITION  site-2 protease family protein [Streptomyces nigrescens].
ACCESSION   WP_457698944
VERSION     WP_457698944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10150298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="site-2 protease family protein"
                     /EC_number="3.4.24.-"
                     /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=29169
     Region          44..221
                     /region_name="S2P-M50_like_1"
                     /note="Uncharacterized homologs of Site-2 protease (S2P),
                     zinc metalloproteases (MEROPS family M50) which cleave
                     transmembrane domains of substrate proteins, regulating
                     intramembrane proteolysis (RIP) of diverse signal
                     transduction mechanisms. Members of the...; cd06158"
                     /db_xref="CDD:100079"
     Site            order(58..59,62,178,186)
                     /site_type="active"
                     /db_xref="CDD:100079"
     Site            178..181
                     /site_type="other"
                     /note="putative substrate binding region [chemical
                     binding]"
                     /db_xref="CDD:100079"
ORIGIN      
        1 mttairradr rvspvflalv avmavsgwav wsgtlagstg vavfffvvsg wvvslclhey
       61 ahartalhsg disveakgyl tlnplkytha llsivlpvif vimggiglpg gavfiersri
      121 rgrwrhslis aagpltnilf aavctapfwl hglegvpatf ryalaflall qvtaailnfl
      181 pvpgldgygv iepwlsrklr rqvepfapfg llavfvflwv pevnrvffdl vdailrglgv
      241 sgletyigqe yfrfwqgepq lpqtgglf
//
LOCUS       WP_457698950             282 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698950
VERSION     WP_457698950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 282)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30820
     Region          1..281
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtrppvryri itaslltiaa lyflvpvywl ivsatknsad lfgtfgfwfs dhprplghlv
       61 dvltydhgiy arwfanslfy agigavcatl lsaaagyala kfpfrgreal fnvvlagvli
      121 pgtalalply flfsamglsn tywavlipst vspfgvylcr iyaaaavpds lleaaridga
      181 gearifgglg lrlmtpalvt vflfqfvhiw nnyflplvml sdsglypiql gltswtgyad
      241 rqpvlyqytv ggaflsvvpl mvlmtvlqry wrtgltegsv ka
//
LOCUS       WP_457698954             442 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698954
VERSION     WP_457698954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 442)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 442)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..442
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48085
     Region          27..342
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mtsnamhrrt vlggaaalaa gfalagcgdg ddgqapqerk egqkisltfw swvpgidkpv
       61 dlwnrkhpdv qvkvekvsav ngqqyakmha aikagnppdl gqiefpvvps flldnglldl
      121 aplgaarhkd kfsgwqwqqs vfgksvyaip qasgpmglfl rqdlfdkwdv ptprtwdeye
      181 taakavrkkg awietfaptn gnrfsglawq agakwygthg dtwivhldde ptrrvadywe
      241 slvrrklvkt ipdrqnawyk dlqtgaipaw vgaswgdall vgnapgtkgk wraaplpqwk
      301 ageqafanwg gsttavfaka ryprdaldfa vwlntdpesi allidggygf psakkgyttt
      361 dldvdkdffg gqayskvfad agahvdtswq wgpgvdtlyq rlgdaftdal adgssfrsvl
      421 tkvqgqtlad lkgkglkves gg
//
LOCUS       WP_457698952             328 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457698952
VERSION     WP_457698952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35279
     Region          42..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msrdtlsrpe pvparparrd trrprrrasr tearnaraaa afvlpffalf alcflapigy
       61 alhqslftte rtgplglggq erevfaglan yaqalsddrf ltgfgrvllf gavqiplmiv
      121 latalallle sasaravpff rsafflpygv pgviasilwg flyvpgispl vkiagsvgwd
      181 ldflsrgtvl wsianivtwq ftgynmlvli aqlkavpgel yeaaridgan awqvarhlki
      241 plirpalvlt gvfsiigtlq lfaepmvlrp lassidsgft pnlhayseaf vgnnqhaaaa
      301 eavllalvac aasfgflrlv ggrakerg
//
LOCUS       WP_457698956             363 aa            linear   BCT 27-JAN-2026
DEFINITION  sialidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457698956
VERSION     WP_457698956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468221
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..363
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38693
     Region          9..361
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
ORIGIN      
        1 mayessvpyr agtegytsfr ipamvrtrsg hllafaegrv ssaadsgtih lvlkrsadag
       61 rtwgplqvva hndtgtagnp apvvlaggrv lllqvhnaad atedrirrgq vlpadgrrvw
      121 lqhsdddgas wsppreitdq aklpqwrwya tgpghalqlr hgpyagrllv panhstpptd
      181 prdsgaepry ngghallsdd dgatwrigct dsdtdrsvap nettaaelpd gsvylnarne
      241 aaaawrrvda vstdggehlv rpfrpqagla gpavqgsalh lgdrgallfs gpahpsaral
      301 mtlrtsrdgg ltwrtahtvg glpaaysdlv rldrdsvgll yetgdfsays titfrripve
      361 ept
//
LOCUS       WP_457698960             322 aa            linear   BCT 27-JAN-2026
DEFINITION  dihydrodipicolinate synthase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698960
VERSION     WP_457698960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..322
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33284
     Region          6..316
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 malpaplhgv ippvctpldp rgeidtasla rlvnhlidgg vhglfalgst sevayltdaq
       61 rgtaleavik atdsrvpvla gvidtttprv ldhartaaal gadalvatap fytrthprei
      121 aahfrhlrta vdlplfaydi pvavhsklsp slvrelaedg tlaglkdssg degslrrllt
      181 alggrtarht gpapafsvlt gseltvdaal lagadgvvpg ignvdpaayv rlydaaragh
      241 weqaaaeqer lvalfslvdv gpetdmgrss salgafkaal hllgvidrga tafpqrplse
      301 eavaevrrrl vtagllpats gt
//
LOCUS       WP_457698958             228 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698958
VERSION     WP_457698958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..228
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25126
     Region          1..227
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 margtmsedv qaqikqlilq grltpgdplp teaelvglld vsrnsvreal kalqamrive
       61 irhgfgtyvg pltlepfveg vafraavrhh qgesslyelm evrealeagl igavardlpa
      121 edlavlkglv qrmaeeargg qvqsatdraf hlalyrslgn hllsevldaf waalrrvred
      181 laddrpdpiv thrqhqeivd aleagdgdra veaihrhfdg irrrlaeq
//
LOCUS       WP_457698967             223 aa            linear   BCT 27-JAN-2026
DEFINITION  biliverdin-producing heme oxygenase [Streptomyces nigrescens].
ACCESSION   WP_457698967
VERSION     WP_457698967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wilks,A.
  TITLE     Heme oxygenase: evolution, structure, and mechanism
  JOURNAL   Antioxid Redox Signal 4 (4), 603-614 (2002)
   PUBMED   12230872
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Ryter,S.W. and Tyrrell,R.M.
  TITLE     The heme synthesis and degradation pathways: role in oxidant
            sensitivity. Heme oxygenase has both pro- and antioxidant
            properties
  JOURNAL   Free Radic Biol Med 28 (2), 289-309 (2000)
   PUBMED   11281297
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Maines,M.D.
  TITLE     Heme oxygenase: function, multiplicity, regulatory mechanisms, and
            clinical applications
  JOURNAL   FASEB J 2 (10), 2557-2568 (1988)
   PUBMED   3290025
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..223
                     /product="biliverdin-producing heme oxygenase"
                     /EC_number="1.14.14.18"
                     /GO_function="GO:0004392 - heme oxygenase (decyclizing)
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006788 - heme oxidation [Evidence IEA]"
                     /calculated_mol_wt=24599
     Region          10..220
                     /region_name="COG5398"
                     /note="Heme oxygenase [Coenzyme transport and metabolism]"
                     /db_xref="CDD:444157"
ORIGIN      
        1 metssptppa pfstvirtas heqhteaens sfmsdllggr lgvrayrryt eqlwfvyral
       61 egasgplaed pvagpflrpe ltrtaalerd lahlggpswr dglaplpata ayadrvvaca
      121 rdwpagfvah hytrylgdls ggqiirgtae ktwgfarkgd gvrfyvfedi anpaafkrey
      181 ralldalpvd elekqrvvde ckrafrlnsa vfrelgeqfp lsa
//
LOCUS       WP_457698975             197 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698975
VERSION     WP_457698975.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21616
     Region          20..66
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          77..189
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mankaapdss rrsersrrai fdaaltlvge vgydkltieg iasragvgkq tiyrwwpska
       61 avlldafteg vdeyeglpdt gdlaadlkfv lratadefnd pafqapyral aaagandeel
      121 srtfvarlme pgtrvyvdrl raaqetgeva adidvriave mllspfsqrw lmrtgeltyd
      181 fvdtlvdqvl rgvrprg
//
LOCUS       WP_457698980             358 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457698980
VERSION     WP_457698980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37964
     Region          20..337
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 merlvrgvqa lpegrppwsp gvvvlagrgp vvaveaaagw alryraydpe rdrgldlprd
       61 lwepmrvgtv fdlaslsklf tavaavqqve rghlalddev rahlpafapg itvrqlltht
      121 sglapelpfy dhrdrtaqla llwqeaaaps ggrapvhrys dlnlialqli leqrtghrld
      181 alihdgitgp lgmsstsygp lapqgvaate dqrrpwakad rgmirgevhd enawalggva
      241 ghaglfstaq dlavlcrtll nggaygtari lgpdaiaall dppglgfgvd qpyfmgelag
      301 rgaaghtgft gtslvldrat dtflvllant vhprrrdsgs apraaaatrl aravsrat
//
LOCUS       WP_457698982             438 aa            linear   BCT 27-JAN-2026
DEFINITION  multidrug effflux MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457698982
VERSION     WP_457698982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="multidrug effflux MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45134
     Region          43..417
                     /region_name="MFS_MdfA_MDR_like"
                     /note="Multidrug transporter MdfA and similar multidrug
                     resistance (MDR) transporters of the Major Facilitator
                     Superfamily; cd17320"
                     /db_xref="CDD:340878"
     Site            order(45..46,49..50,74,77..78,135,166,169..170,253,256,
                     378)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340878"
ORIGIN      
        1 mtepgaaetq dlppiaerga aaapaasrrt sllvtlvlgg ltavpplsmd mylpalpqvt
       61 aalhspaatv qltlttclag malgqmivgp msdkwgrrrp llagmviyvl atalcavatn
      121 aelliafrll qglagaagiv iaravvrdly dgvamarffs tlmlisgvap vvapligsqi
      181 lrltdwrgvf vvltavgval tllvwrklhe tlpperrhsg glgqtlrtmr dlladrvfsg
      241 yvlvgafafa alfayisasp fvvqeiygas pqifsllfgi nsvglvavgq ingkllvgrv
      301 gldkvlgtgl vvialaatal llmsagvfgh vglvptaagl fvlmaamglv mpstntlall
      361 rtphaagsas allgtstfll gsvasplvgv agertavpma lvqlscavla lvsflgmcrp
      421 wqrrgesngs tagertrl
//
LOCUS       WP_457698983             543 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457698983
VERSION     WP_457698983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..543
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60010
     Region          57..541
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mthhapheqe iraaaahfgr rrfltatgaa aalafatnlp gtgaayaaea darkitenpf
       61 tlgvasgdpq pgsvvlwtrl aprpyepgng mpdarvtvrw evaydehfkr lagqgradah
      121 aefnhsvhie ptglapdrvy yyrfragswi spvgrtrtap tkgarisdlk laavscqayh
      181 dgyftahrhl aeedldvvfh lgdylyeypv saaggarnyt drtlpavfnr etvtledyrl
      241 ryalyksdpd lqaahaahpf ivtwddheve nnyasdised hlppaeflvr raaayraywe
      301 nqplrrpqrp qgadarlyrr lqygqlaqfd ildtrqyrsd qvygdgwhap gpeskdpart
      361 ltggaqerwl idgwressar wnvlpqqvtf serrnatgpg yqlsmdawdg yaasrdrvla
      421 gaesagvdnl vvltgdvhvh yafdikkdfk dpgsrtagve fvttsiasgk dgadkpanwd
      481 tylaanphlk fyngrrgylt vtldqdtara dfrtvsavtt pgapvrttas fvseagdpgl
      541 ksa
//
LOCUS       WP_457698986             311 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457698986
VERSION     WP_457698986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32042
     Region          58..304
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maentepara arttpmarag qvggtatapr ptlpaptsrg gqstqtapaa qetqqdgaap
       61 rqvavvtgag sgigravaha lsaagwtvvl agrraealae tsrlagpvdp dgpaimtvpt
      121 dvtrpeqvda lfaavherfg qldllfnnag tfgrpaplee lsyndwrtvv dvnltgsflc
      181 aqaaframka qepqggriin ngsvsahtpr phsvaytatk hamtgltksl sldgrpygia
      241 cgqidignaa temtgrmqtg ilqangrtav epvmdaadva rtvvhmaalp ltanvqfatv
      301 matnmpyigr g
//
LOCUS       WP_457698988             343 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457698988
VERSION     WP_457698988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..343
                     /product="trypsin-like serine 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=35419
     Region          134..342
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrrtvrgipa vhgipaphpg rrsraalgtl taagtllall lptgqagaap rpghhsataq
       61 ttlgafwtad rmraaapldl atptkrsapa avprsaplkv aptlpglpka gpllpgslpq
      121 aggpwtggga vvkttgrvff tyqgrnascs gdavtsgnks tvitaghcvk lqgawhtnwv
      181 fvpgyhdgqa pygkwpaakt latpqwtase einydvgaav vapldgkklt dvvggqglsf
      241 nsgynkamya fgfpaaapyd gskliycsgn tikdplfsnd hglscnmtgg ssggpwftsf
      301 dektgtglqt svnsfgyqfl pntmfgpyfg ddaknlydka qts
//
LOCUS       WP_457698998             264 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457698998
VERSION     WP_457698998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29018
     Region          75..220
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrsaawhlse aadvefllli ghhrrlaaai stlalspiry vearvaespr naarpgplpt
       61 grhhlsreqv vmsqrmrmlt ataeamkdkg yvgtsvaeii rragvsretf yqqfrskedc
      121 fiqaldaatk qlaglleaar qsaadppeat rpappeetfr rllhlylrtl teqsafarlf
      181 lvevyaagpe amairrewqr wfadaiaeif hvgdeggade rsfgcealva aaaqlvtahl
      241 vaddleglrg ledplvrlav rllg
//
LOCUS       WP_457699000             270 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699000
VERSION     WP_457699000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29254
     Region          1..89
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mrigelagli gvstravrhy hhlgllpepe rrangyrdyg lrdavalarv rrltelglgl
       61 devrdvladd agrelhevld eldadlarqe eelrvrrarl aavrrqaeeh gglpaegpvs
      121 delaalfaem artsaarpgp epamaskere vmvllesmgg eeankrvvel lrettaapga
      181 mertyevygl ldalveagtd dprveeaaqa ladcipdavi gevgreqwer aagpgaeadg
      241 gflaayyahf apaqaravrr aiqlvaerar
//
LOCUS       WP_457699010             219 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional 4-hydroxy-2-oxoglutarate
            aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Streptomyces
            nigrescens].
ACCESSION   WP_457699010
VERSION     WP_457699010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Walters,M.J., Srikannathasan,V., McEwan,A.R., Naismith,J.H.,
            Fierke,C.A. and Toone,E.J.
  TITLE     Characterization and crystal structure of Escherichia coli KDPGal
            aldolase
  JOURNAL   Bioorg Med Chem 16 (2), 710-720 (2008)
   PUBMED   17981470
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Fullerton,S.W., Griffiths,J.S., Merkel,A.B., Cheriyan,M.,
            Wymer,N.J., Hutchins,M.J., Fierke,C.A., Toone,E.J. and
            Naismith,J.H.
  TITLE     Mechanism of the Class I KDPG aldolase
  JOURNAL   Bioorg Med Chem 14 (9), 3002-3010 (2006)
   PUBMED   16403639
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Nishihara,H. and Dekker,E.E.
  TITLE     A stereospecific 2-keto-4-hydroxyglutarate aldolase from
            Escherichia coli
  JOURNAL   Biochim Biophys Acta 185 (1), 255-257 (1969)
   PUBMED   4894280
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="bifunctional 4-hydroxy-2-oxoglutarate
                     aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase"
                     /EC_number="4.1.2.14"
                     /EC_number="4.1.3.16"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016833 - oxo-acid-lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21830
     Region          17..217
                     /region_name="PRK05718"
                     /note="keto-hydroxyglutarate-aldolase/keto-deoxy-
                     phosphogluconate aldolase; Provisional"
                     /db_xref="CDD:235577"
     Site            order(27,52,56,80,140,142,168)
                     /site_type="active"
                     /db_xref="CDD:188632"
     Site            order(56,80,82,101..104,124..127,129,133,142..143,155,
                     159..160)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:188632"
     Site            140
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188632"
ORIGIN      
        1 mggvtsaass papsalsvlg iapvipvvvl hdaddavpla ralvagglpa ievtlrtpaa
       61 ldairavsee vpeavigagt lltpgqveaa lvagsrflvs pgwsprllga mkdsgvpflp
      121 gvstvsevvt lldegvtemk ffpaeaaggt pylhslaspl pqarfcptgg iglasapsyl
      181 alpnvgcvgg twmlpadala akdwdrirql aqeaaalta
//
LOCUS       WP_457699013             337 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA desaturase [Streptomyces nigrescens].
ACCESSION   WP_457699013
VERSION     WP_457699013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..337
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=37371
     Region          29..324
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtarpeaved ppipadsavg paagtpvpsa tlggeqrrsl eqitlllfit vpfvalvaav
       61 plawgwgvsw ldlglmvamy yigchgitig fhryfthgaf kakrplrial avmgslaveg
      121 plvrwvadhr khhkfsdaeg dphspwrfge tvpalmkglw wahigwmfde eqtpqqkyap
      181 dlikdsairt isrqfvlwtt vslmipplvg glvtwswqga lsaffwgslv rvallhhvtw
      241 sinsichavg krpfksrdrs gnvwwlavls cgeswhnlhh adptcarhgv mkgqldssar
      301 lirwfekagw aydvrwpdas rldarraeka aggasrr
//
LOCUS       WP_457699027             264 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457699027
VERSION     WP_457699027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..264
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27157
     Region          16..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msqqraphpa ngpygkrfeg rtvlvtgaaa gigaatadrl aaegagvlll diddargeht
       61 arriraaggr asyehcdvag eddwrravea arqrygpvdg lvsnafvpsv aaadrtplad
      121 wdrqlavnlt gsflgvraal adlrsrggav vltssvhalv glpgrpayaa akagltglgr
      181 qlaveygpev rvnsvlpgpv ltaawdgige eerqasaaet aarrlgrpee vaaaiaflls
      241 peasfvtgas lvvdggwsvy knss
//
LOCUS       WP_457699029             677 aa            linear   BCT 27-JAN-2026
DEFINITION  beta-galactosidase [Streptomyces nigrescens].
ACCESSION   WP_457699029
VERSION     WP_457699029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..677
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74147
     Region          1..622
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          614..676
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mgihfggdyn peqwpeevwa edlklmkaah vtmvtagifs wakveprpga wdfgwfdrvm
       61 dglagagiav clatmtaspp pwlsrahpei lpedadgrrr wpggrqhycp sspvyrahav
      121 rlveqlatry aghpalamwh igneygchtr hcycevsadd frrwlreryg svdalnaaws
      181 tafwsqaygd fdevlpprta ptfpnpaqql dylrfgdeal racylaekav lervtpgipa
      241 ttnlmpqhkp vdafawsshm damaldfyqd phvpddhvra gyvfdlmrsa rsgqpwmlle
      301 qapgavnwrp rngpkppgam rlwswqaiaq gadavlffqw rqslggaekf hsamlphggt
      361 dtrifrevsq lgrelaslpg iegtrsraea alladwhsww aleldskpst aldhsriald
      421 hyrplfeagv acdvvppqrd lsgyrlvvap nlyllttpda erlaayvrdg gqllvsffsg
      481 ivdahdrvhp ggcpaplral lglrvaefwp ldagrsvavd egttlrersr elggdctgra
      541 dlwseaidle gaevlahftd gelagrpavt rhsygrgtvw yvgtrlepal mrtlldvvra
      601 aagvepvlpg lpagvqatvr egaggrylfl lnhgtetvev glpaplrdal aargtagaga
      661 vdritlgarg vavltep
//
LOCUS       WP_457699038             241 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457699038
VERSION     WP_457699038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 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   Rosinski,J.A. 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 241)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13297907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..241
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24928
     Region          <79..204
                     /region_name="PRK10403"
                     /note="nitrate/nitrite response regulator protein NarP"
                     /db_xref="CDD:182431"
     Region          <145..217
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mgvrlmvvdd hrllaealas alklrghrvl aaaapsagaa elvvsrapev cllgtaapar
       61 pgafdpvvri kkerpqvavv vlgpvpsprg iaaafaagas gyvrnderie gverammkar
      121 agesavspql lqqafeellh paaqpddega rllelltpre vevlmrvadg edtrliaagm
      181 diapstarth vqrvlmklev gsrleaaala artglldrag grgvrgaaga gpdepaappl
      241 r
//
LOCUS       WP_457699046             599 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptomyces nigrescens].
ACCESSION   WP_457699046
VERSION     WP_457699046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..599
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66227
     Region          8..507
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          537..597
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mavnlvnlea vgkvygtral ldgvslgvne gdrigvvgrn gdgkttliri lakledtdtg
       61 rvthngglrl gvltqhdsld paatirhevi gdladhewag nakirdvltg lfgdlhmpgf
      121 thgldtvigp lsggerrria laklliaeqd livldeptnh ldvegiswla ghlrarrsal
      181 vvvthdrwfl dqvctrmwdv qrgdvheyeg gysdyvfara ereriaatee vkrqnlmrke
      241 lawlrrgapa rtskprfrie aaneliadvp pprdnaelmk fassrlgktv feledvsvqa
      301 gpkillkhlt wqlgpgdrig lvgvngagkt sllralaeat rtqgeaqpva gritvgktvk
      361 laylsqevge lpptlrvlea vqqvrervdl gkgremtagq lcekfgftke kqwtpvgdls
      421 ggerrrlqil rllmdepnvl fldeptndld ietltqledl ldgwpgsliv ishdryfier
      481 ttdrvhallg datlrmlprg ldeyldrrrq vieaatpapa pqtsapkkaa avnraaqkel
      541 qkierqldki gdkettlhaq iaenatdfek vagldaqlre lsaekdelem rwlelaeea
//
LOCUS       WP_457699050             250 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699050
VERSION     WP_457699050.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..250
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25557
     Region          25..219
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mapdmgttve terglvygps gkqldvyrpa gaprpaptvl lwhgigpder dvleplasta
       61 aahgllvlvp dwrsdaadgg rahlleslaf vrkeagglgg dgescvlagw sagagaalgi
      121 alrpeiaegw rpravvgvag rydlparttg tapladlaag repgvpvhlv hgsrdpvvea
      181 rysrdlaeal qaagrtvplq epdtdhagvi mtaydpatdr cvpttaehav ragrvvaevl
      241 teaavggcaa
//
LOCUS       WP_457699052             291 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699052
VERSION     WP_457699052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32586
     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 marrkdidgs agvptfygke lrwqreaagl tlqqltegsf yglshlseie hgrrrmpqdl
       61 aehvdrvlkt dgffarrcad arkakgkghs dyyaevvele graqdieewm pdlfpgplql
      121 epyiravvha ahpnepeegv sakvsarqer awlfedsksp etwvvlselv llrpildpgg
      181 maeqlahvve varhrrfipq ilpwnvaahp ftmgttrlla fadapplmyt egmysgqlie
      241 dpscirqyak aydrlraaal ppdvslkaie kaaedyrngk hprgleqgpl a
//
LOCUS       WP_457699065             579 aa            linear   BCT 27-JAN-2026
DEFINITION  dolichyl-phosphate-mannose--protein mannosyltransferase
            [Streptomyces nigrescens].
ACCESSION   WP_457699065
VERSION     WP_457699065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11449133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..579
                     /product="dolichyl-phosphate-mannose--protein
                     mannosyltransferase"
                     /EC_number="2.4.1.109"
                     /GO_function="GO:0004169 -
                     dolichyl-phosphate-mannose-protein mannosyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=64499
     Region          76..579
                     /region_name="PMT1"
                     /note="Dolichyl-phosphate-mannose--protein O-mannosyl
                     transferase [Posttranslational modification, protein
                     turnover, chaperones]; COG1928"
                     /db_xref="CDD:441531"
ORIGIN      
        1 mgrvtsdtta tdaaaqyape ppgappvwqr rlrrfglpvr pqtdvrarlv pafpepsgrl
       61 wavfgagpea aarltrwsgw agpllvalfa gvlrfwnlgg prkvifdety ypkdawsllq
      121 ygyegtwakn andalvghpp elllspehsy vvhppmgkwl ialgewafgm npfgwrfmva
      181 llgtlsvlli crigrrllrs talgclagal lavdglhfvm srtalldliv mfwvvaafgc
      241 llvdrdrtra rlaaalpvgp dqvthpdesv gdrlrlgwrp wriaaglclg laaatkwngl
      301 yylaafalma vlwdvaarrt agarrpfrsa lrrdvlpafg atvvvavaty laswsgwiat
      361 kggyyrdwat tpegrtgawv wvpdwlrslw hyqtevysfh tglttphayq snpwswlvlg
      421 rpvsyfyedp kagqdgctaa egcarevlal gtpllwwaac fallyvlyrw lfkrdwraga
      481 ivcavvagyl pwflyqerti flfyavvfvp flclalammi gaivgppgst errrtigavg
      541 agvlvlliaw nfiyfyplyt gmpipksawh hrmwfdtwv
//
LOCUS       WP_457699062             291 aa            linear   BCT 27-JAN-2026
DEFINITION  TatD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699062
VERSION     WP_457699062.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..291
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30598
     Region          22..290
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mapqdkntpp plpeplrvav adshthldmq dgtveealak aasvgvttvv qvgcdlagsq
       61 waaetaaahd svhatvalhp neaprivlgd pdgwsrqgar eaggnsalda alteidklag
      121 lpqvrgvget gldyfrtgpe gmaaqeasfr ahieiakrhg kalvihdrea hddvlrilre
      181 egapdrvvfh cysgdaemak icaaagyfms fagnvtfkna qplrdalaia ppelvlvetd
      241 apfltpapyr granapylip vtlramaevm altedalata iaantarafg y
//
LOCUS       WP_457699072             461 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699072
VERSION     WP_457699072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..461
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50805
     Region          91..>211
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          359..452
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mrtikwsacp kaeppfpaps krtrcgtlev pvdwakpdgp tmkiavarqk atdpkkrigv
       61 llsnpggpgt tglddayfad npvegydkni rsrfdiigfd prgigrsgql rcddklagki
      121 parpknaief egmrslnkql adscrkrsgp vvdhmdsvsv ardmdairaa lgekkisflg
      181 hsygtlmgrq yarlfpqklr alaldsamdp srpdaerfla egsaaaengv rqladwcakd
      241 sscalkgqdv qavvrglfar adagrlfepg rhgptrkkvt adqlsgflfd ylqkwnpqtt
      301 aeqlgalnsg kgkvswtdss palawrtvmc rdydfrlrdy ahyrelrqrt qsanphsryn
      361 sqaldmilgc qgwpaapepe parakgplpp vlvvnakhdl atplpgarrm aqefpkgkla
      421 ildamdhwly rkcqsplpar aidtylrtlk tpphgtvyph r
//
LOCUS       WP_457699079             319 aa            linear   BCT 27-JAN-2026
DEFINITION  cation diffusion facilitator family transporter [Streptomyces
            nigrescens].
ACCESSION   WP_457699079
VERSION     WP_457699079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..319
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33396
     Region          6..302
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msasggtkai vaalganlai aaakfvafaf sgsssmlaeg vhsiadsgnq gllllggkka
       61 kraataehpf gygreryiyg flvsivlfti ggvfalyegy ekihdphald nwywpvgvlv
      121 faiiaesfsf rtaikesnel rgkqtwaqfv rrakapelpv vlledlgalv glvlalggvc
      181 ltlatgdaiw dgigtmciga llvlialvla aetkslllge aagpeqiaki raavvdgrvv
      241 trvihmrtlh lgpeellvaa kiavrhdgta teiadainaa earireavpi arviylepdi
      301 yneataaadt dpsktpggn
//
LOCUS       WP_457699095             182 aa            linear   BCT 27-JAN-2026
DEFINITION  cysteine dioxygenase [Streptomyces nigrescens].
ACCESSION   WP_457699095
VERSION     WP_457699095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Chen,M., Zhu,J.Y., Mu,W.J. and Guo,L.
  TITLE     Cysteine dioxygenase type 1 (CDO1): Its functional role in
            physiological and pathophysiological processes
  JOURNAL   Genes Dis 10 (3), 877-890 (2022)
   PUBMED   37396540
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Joseph,C.A. and Maroney,M.J.
  TITLE     Cysteine dioxygenase: structure and mechanism
  JOURNAL   Chem Commun (Camb) (32), 3338-3349 (2007)
   PUBMED   18019494
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14410663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..182
                     /product="cysteine dioxygenase"
                     /EC_number="1.13.11.20"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0017172 - cysteine dioxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18910
     Region          79..157
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mnsdvqiagd plaiphllpp vpahpatvag faglarsiaa draawaplvr ydattrwyhr
       61 lrtvpqalda araggapmgy evwllswvpg qgsgrhdhga ssgvltvleg eltehtedgp
      121 raltagaqrv fapgyvhevv ndaltpavsl hvyfpgltnm pmhpsqatds gavttppgip
      181 ap
//
LOCUS       WP_457699107             368 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457699107
VERSION     WP_457699107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..368
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=39403
     Region          55..324
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 maavgitgav lagagtgwav yaklnsniht dsaterelrk weserppagp pnaenvllig
       61 sdsrnggngr yghsrgqrsd ttmllhlaan rksatavsip rdlmvevphc krpdgtetep
      121 rsaqfnaafa aggpactirt vekltgirig hyliidfvgf tkmvdavdgv evclpqpvhd
      181 peahltlpag rqtlhgeeal gyvrarkslg ngsdtqrmer qqrflgalvk kvqsngvlln
      241 ptrlypvlda atsslttdta laslrglyel vrsarriptd rvqfmtvprq eyrldpnrde
      301 lvqpdaarlf gqlhrdlpvt vtpphdagee pvrsgngssd grpgeppaps pssgptfpgt
      361 taehgice
//
LOCUS       WP_457699113             343 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457699113
VERSION     WP_457699113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 343)
  AUTHORS   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 10118577
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..343
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36564
     Region          9..254
                     /region_name="Succinoglycan_BP_ExoA"
                     /note="ExoA is involved in the biosynthesis of
                     succinoglycan; cd02525"
                     /db_xref="CDD:133016"
     Site            order(14,16,97)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133016"
ORIGIN      
        1 mpqqqppavs vimpvlneer hlrnsvrhil eqeyagemev vialgpstdr tdeiaaelva
       61 edarvhtvpn ptgrtpaaln aaikasrhpv vvrvdghgml sqnyiatavr lleetgaanv
      121 ggimhaegen aweeavaaam tskigvgnaa fhtggqagpa etvylgvfrr ealeqqggyn
      181 eefiraqdwe lnfrireagg qvwfspelkv qyrprpsika lakqykdygk wrhvvaryha
      241 gsinlrylap ptavcaiaag lvvgaavtpw glvvpagyla aitagsvpag kglslkaraq
      301 ipvalatmhm awgtgfltsp rslarkvias rrpavmapaa dae
//
LOCUS       WP_457699103             454 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidoglycan recognition protein family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699103
VERSION     WP_457699103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Dziarski,R. and Gupta,D.
  TITLE     The peptidoglycan recognition proteins (PGRPs)
  JOURNAL   Genome Biol 7 (8), 232 (2006)
   PUBMED   16930467
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Guan,R., Roychowdhury,A., Ember,B., Kumar,S., Boons,G.J. and
            Mariuzza,R.A.
  TITLE     Structural basis for peptidoglycan binding by peptidoglycan
            recognition proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17168-17173 (2004)
   PUBMED   15572450
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Steiner,H.
  TITLE     Peptidoglycan recognition proteins: on and off switches for innate
            immunity
  JOURNAL   Immunol Rev 198, 83-96 (2004)
   PUBMED   15199956
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Dziarski,R.
  TITLE     Peptidoglycan recognition proteins (PGRPs)
  JOURNAL   Mol Immunol 40 (12), 877-886 (2004)
   PUBMED   14698226
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11274790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..454
                     /product="peptidoglycan recognition protein family
                     protein"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0016019 - peptidoglycan immune receptor
                     activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045087 - innate immune response [Evidence
                     IEA]"
                     /calculated_mol_wt=47449
     Region          259..406
                     /region_name="PGRP"
                     /note="Animal peptidoglycan recognition proteins
                     homologous to Bacteriophage T3 lysozyme; smart00701"
                     /db_xref="CDD:128941"
     Site            order(290,325,424,430,432)
                     /site_type="active"
                     /note="amidase catalytic site [active]"
                     /db_xref="CDD:133475"
     Site            order(290,424,432)
                     /site_type="other"
                     /note="Zn binding residues [ion binding]"
                     /db_xref="CDD:133475"
     Site            order(291..292,321,325,339,350..351,356,424,428,430..432)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133475"
ORIGIN      
        1 msrilsmrpf laiclgavct aalalplapt agasaapaaa prpapagelp gstqslpvaa
       61 lgaaaphpda rdstsapvpq slglpartvr pfsllgvvwd daaaelrgrv qvrtratgrg
      121 dwsgwqdvqv hnddapdlgs aerrdsevrg staplwvgds davqlritpe srhraraalp
      181 gglrlelvdp grapravrga hadppapltp eateasaana elaplgatei paldqtssrt
      241 dlaavggspp ahnyagprpr ivtragwgad eklrekafty trtvraafvh hsgsgnnydc
      301 aeassliram yrfhvksnhw rdigynflid rcgtvyegra ggvakpvmga htlgfntdst
      361 giavlgtftd deppqpavda iarltawklg lysvdpratt rllsgggnrf pkgtkvplhv
      421 isghrdgftt dcpgvhlydk laatrlaaaa lqgr
//
LOCUS       WP_457699099             301 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA-3-methyladenine glycosylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699099
VERSION     WP_457699099.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Kanchan,S., Mehrotra,R. and Chowdhury,S.
  TITLE     In Silico Analysis of the Endonuclease III Protein Family
            Identifies Key Residues and Processes During Evolution
  JOURNAL   J Mol Evol 81 (1-2), 54-67 (2015)
   PUBMED   26149779
REFERENCE   2  (residues 1 to 301)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414762
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..301
                     /product="DNA-3-methyladenine glycosylase family protein"
                     /EC_number="3.2.2.-"
                     /EC_number="4.2.99.18"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0019104 - DNA N-glycosylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=33342
     Region          11..282
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mpartwdppg pfdlhrtlgv lqrgpgdpaf avrdgelwra crtpegpgtl riaarpaagr
       61 veaeawgpga dwllerlpel lgesddpaql tarhrivhea rrrhpgvrla rtglvlesli
      121 psileqkvts deayrawrll lqrhgepapg pwtrmrvmpe prgwalipsw ewhragvdak
      181 rssailravr aarrmeeaar mdladatrrl malpgigpwt aaetlqrtlg apdaitvgdl
      241 hlpkiigyal tgrrgttdee mlellapyeg qrhraarlil lsgrtpprra prfpvgdiar
      301 l
//
LOCUS       WP_457699121             184 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457699121
VERSION     WP_457699121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20013
     Region          17..157
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mtelvtdnpe gevvgkptsv sritlshimt agdtnllgtv hggvimklvd daagavagrh
       61 sggpavtasm demaflepvr igdlvhvraq vnwtgrssme vgvrvlaerw nesspaqqvg
      121 saylvfaavd eqgkprrvpp vlpeterdqr ryqeaqirrt hrlarrraim elrerraaeg
      181 ldda
//
LOCUS       WP_457699123             431 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457699123
VERSION     WP_457699123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..431
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=46316
     Region          159..427
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mnewpngwsg dqsgnryghg sgsaepegar amrqvrrdag pgyqrseppl ppsmsprgga
       61 tvppqqsqgy ddaydgyntg qvygggrggg ggyddgygdg rggrprprwg krikwtvitl
      121 vavlavtsva tyfwadgklr rkvdlskvid rpetgdgtny livgsdsreg mtaeqkrklh
      181 tgsaegkrtd smmilhdgss gptlislprd sdveiptfvg sdsgkkyqgt grhtklnaay
      241 aedgpellvr tveyntklhi dhyveigfag fanivdaigg vemdlpkaik drdsgadfpa
      301 gkqtlngqqa layvrtrhaf aqqdldrtkn qqkflatlas qtatpatvln pfklyptmsa
      361 gldtlivdkd mslwslgemf famkgvtgge gksmnmpvsg snggnlvwdk aklsqlvqql
      421 nndekvtvsg n
//
LOCUS       WP_457699125             446 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-glucose dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699125
VERSION     WP_457699125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Price,M.J., Nguyen,A.D., Byemerwa,J.K., Flowers,J., Baeta,C.D. and
            Goodwin,C.R.
  TITLE     UDP-glucose dehydrogenase (UGDH) in clinical oncology and cancer
            biology
  JOURNAL   Oncotarget 14, 843-857 (2023)
   PUBMED   37769033
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..446
                     /product="UDP-glucose dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=47834
     Region          4..444
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mplkitvigt gylgathaaa maelgfevlg ldvvpekiem lqrgevpmye pgleellrrh
       61 vagiegstgr lrfttsyeea gafgdvhfvc vntpqkhgey acdmsyvesa fdalaphltg
      121 ptlvvgkstv pvgsaarlar rlaaaapage aaelawnpef lregfavkdt lhpdrivagv
      181 agaraeellr evyatpiaeg spfivmdypt selvktsans flatkisfin amaevceaad
      241 gdvvklaeai ghddrigkkf lragigfggg clpkdlrafm aragelgadq altflreids
      301 inmrrrghmv eltrdavggg flgkrvavlg atfkpdsddv rdspalnvag qihlqggqvt
      361 vydpkgmena rrlfptlaya dtaleavrga dvvlhltewr efreldpaal gevvaerril
      421 dgrnaldpal wrkagwtyra lgrpqa
//
LOCUS       WP_457699129             122 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457699129
VERSION     WP_457699129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..122
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13558
     Region          9..120
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 msaikfgvia ldcpdprala nfyaevldwq vtggddewie vagptgrtla fqrvtdyrpp
       61 qwpgqdvpqq lhldfdvaha dideaerkiv algaklvqrd aeardwrvyl dpaghpfclc
      121 lk
//
LOCUS       WP_457699127             182 aa            linear   BCT 27-JAN-2026
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699127
VERSION     WP_457699127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..182
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18876
     Region          4..181
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 maartapdsl rlvqdlvntl dietgedalt aglgaflrdh gvpaghgeat algelqelre
       61 alrevclaht agtavpepat rtldrllaaa plvldvqpdg gaalrpaagl ggaayltalv
      121 aagiasavag gtwtrlkace ahdcrwvfyd kspagrsrwc tmavcgsrak mrtyrakrae
      181 se
//
LOCUS       WP_457699137             262 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699137
VERSION     WP_457699137.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  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 262)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27567
     Region          69..262
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mttaphtaga phtapapfsa srtlataarv lrqlrhdprt ialmlvvpcv miallryvfd
       61 drpatfdgig asllgifpmi tmflvtsiat lrertsgtle rllamplgka elisgyalaf
      121 gllaivqsal atglsvwllg ldvtgspwll llvavldall gtalglfvsa faasefqavq
      181 fmpavlmpql llcglftprd tmqpaleals aalpmsyavd gmnevlehpd itgdflrdav
      241 ivtgcallvl algaatlrrr ta
//
LOCUS       WP_457699138             269 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699138
VERSION     WP_457699138.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28738
     Region          10..245
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mmnygrdpav hargltavrg grtvldalaf dvprgrvtgl lgpsgcgkst lmraivgtqa
       61 kvtgtldvlg hpagdprlrp rigyvtqdps vyddltvrqn ldyfaavlhp grsargrrre
      121 svtraiedvd ltrhadalag nlsggqrsrv slavallgap ellvldeptv gldpvlrrdl
      181 whlfhtlaad rgatllvssh vmdeaerchr llllregrll aedapdalrd rtgsdtveaa
      241 flhlvdeaga aaarppepar pttaqesar
//
LOCUS       WP_457699142             522 aa            linear   BCT 27-JAN-2026
DEFINITION  SulP family inorganic anion transporter [Streptomyces nigrescens].
ACCESSION   WP_457699142
VERSION     WP_457699142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Alper,S.L. and Sharma,A.K.
  TITLE     The SLC26 gene family of anion transporters and channels
  JOURNAL   Mol Aspects Med 34 (2-3), 494-515 (2013)
   PUBMED   23506885
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Mount,D.B. and Romero,M.F.
  TITLE     The SLC26 gene family of multifunctional anion exchangers
  JOURNAL   Pflugers Arch 447 (5), 710-721 (2004)
   PUBMED   12759755
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429357
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..522
                     /product="SulP family inorganic anion transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53499
     Region          25..507
                     /region_name="SUL1"
                     /note="Sulfate permease or related transporter, MFS
                     superfamily [Inorganic ion transport and metabolism];
                     COG0659"
                     /db_xref="CDD:440424"
ORIGIN      
        1 mrrfriarqr psrpsipsrq alsvwradft aslvvflvav plcvgvavas gvpaelglvt
       61 givgglltgl lpgsslqvsg paagltvlvy eavqkfglgt lgalvliagv lqlvmgalrl
      121 grwfraisva vvqgmlagig lvliagqlya ladarppgng panlgglpdl aantagsgta
      181 laalavgagt iallvlwpkw qraarvlpap lvavalativ vfvldlpvar vevagllevi
      241 qppggadfar lteagavvga lgtvlafali asaeslfsaa avdrlhdgpk tdydkelmaq
      301 gvgntvcgll galpmtaviv rsaanvhaga rtkasrvlhg vwllvfaaaf paalgvvpla
      361 alagvlvhag vkllpvkqwr plwrehrgea vvlaatavai vatnmfegvl lgllmavaks
      421 awetshvhle ivgldepagh gepvvvgprr pirvralgna tflrlpklld qlealpkdre
      481 veldltglrh ldhacaaalg aweeqrrgpg ggarqeapsv ap
//
LOCUS       WP_457699144             475 aa            linear   BCT 27-JAN-2026
DEFINITION  M1 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457699144
VERSION     WP_457699144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Luan,Y. and Xu,W.
  TITLE     The structure and main functions of aminopeptidase N
  JOURNAL   Curr Med Chem 14 (6), 639-647 (2007)
   PUBMED   17346152
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Albiston,A.L., Ye,S. and Chai,S.Y.
  TITLE     Membrane bound members of the M1 family: more than aminopeptidases
  JOURNAL   Protein Pept Lett 11 (5), 491-500 (2004)
   PUBMED   15544570
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..475
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52425
     Region          59..466
                     /region_name="M1_APN_like"
                     /note="Peptidase M1 family similar to aminopeptidase N
                     catalytic domain; cd09603"
                     /db_xref="CDD:341066"
     Site            order(169,171..172,305..309,324,327..328,331,346,350,405)
                     /site_type="active"
                     /db_xref="CDD:341066"
ORIGIN      
        1 msadpgsavn rrplrscgat aalsvallls sctssgvrga agsggvgdpl fpslgnggyq
       61 vrhygldldy dvkkrqldat aeitaeatad lrsfqldlqg lrvtdvqvdg edaefsrkgh
      121 kvivrpdeal rkgaefrtrv dyegtpqelk dpdqstegwv ktrdgafvsg qpagamtwfp
      181 gnnhprdkaa ydftitvpkg ytavangelk sertakgrtt frwhngrpma sylatatigr
      241 fevhtsrtpe glplyvavdp aeakaskgal eklpeivkwq sklfgpypfs sagaivddtp
      301 kriewiales qtkpvyagap dtatvvhema hqwfgdsvtp ktwadtwlne sfatyaewlw
      361 eereggktpq eqfdalyddt tdparwafpp gkpgqaknvt gtpvyergam llqelrnavg
      421 dkafftilre wpteyrygna daqdfidfcq eytdedlepl fkkwlyekgk pered
//
LOCUS       WP_457699146             381 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457699146
VERSION     WP_457699146.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - obsolete NADH oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=39879
     Region          23..364
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mksvakrggs rgrktrgrta rgrvvvlggg yagtmaalrl apyaqvtlvd psdrftervr
       61 lhelaagrpe vshsrarmlh gtgiehlaar atsldpdara vhtdsgrtll ydrlvyalgs
      121 htdprglgek aftaesaaal hkrlldgpga ltvvgggltg iemateiaes hpawrvrllt
      181 ggeiggglsv rgrahvrtvl drlgvrveeg hrvadadgvd adavlwagvl ratgglahda
      241 glvtdpvtgr lrvdamlrsv shpdiyaagd aaaartprag alrmacatal ptgshvagai
      301 aaelrgaapr plsygffvqc vslgrhdali qsvraddrpr ervltgrpaa rvkeqvvrna
      361 vrvlhlaarr pgviplipgi g
//
LOCUS       WP_457699150             279 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699150
VERSION     WP_457699150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29550
     Region          52..182
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mphrseqeql ppapqplqpp tpphhatlar afdavaaqya aarpgyppal fdaieelagq
       61 plagarvldv gagtgiatkl laergaqvta vepgaamaae lhtahpaipl vralgdalpf
      121 rddaafdlvg yaqawhwtdp arsvpealrv lrpggalalw wnipdpdvdw aaeqeariar
      181 rlpdyhshsv apetadlirg lglglhpvsr vlhwtrrvpl dthlamlgsr syfsaigpaa
      241 aapvlaaera alrdvfpdgi veeayaldlt vtlrpsaps
//
LOCUS       WP_457699157             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699157
VERSION     WP_457699157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31362
     Region          21..72
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Region          93..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpprravtgr sqeprqryve elrllraqkg dslrhlgdvl gwdwslfgkm ekgetiggpe
       61 vaqaldqhyg tpgllltlwe laladpsqfr eqyrrymvle seavslwhya vgvlpgllqt
      121 egyayevlaa ggikgseltr qvearmgrrk lltgddpppf rtilsetvlr tpmrdaqawr
      181 dqlqhlteva erpnmtlqvl phgpclhala ntdvmflrll dghtvaytes alhgelvees
      241 gsverlqray davrdlalsp desrksigrm leevpcepst
//
LOCUS       WP_457699161             298 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699161
VERSION     WP_457699161.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32046
     Region          3..295
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mklnlhrlwv feqvvacggf saaarklyms qpsvsqhvhk levslrttli drsgprlrlt
       61 aqgevllqya qqisslaqev aaaidqvsga psgrlmvgst styssylllp vfgrfaelfp
      121 gverqlrtgn tteilrqlad gevrlavlpg yqggasphhr mepileeqll lvappghpla
      181 gravtpadla qqrflfreeg satrraqgda lalwglppsr cpgvtgnetl kqaviadlgi
      241 avmprrcvaq elrdghlall spdpalpact ivlatsreta lspaeqefar llrtanda
//
LOCUS       WP_457699163             376 aa            linear   BCT 27-JAN-2026
DEFINITION  RICIN domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457699163
VERSION     WP_457699163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..376
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40970
     Region          40..140
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(44..46,61,63,70..71)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mafvaatisp lgagqaqaad gdcaqelecl vvasemedgs rvleiarswh gdgeaakgsa
       61 yifpnknsen qrwqfrntgd gsfqmivrds kkclssgmgw sleqdctntd eqkyylqpsp
      121 sggfmirsvk ddmclnglgg hsgqnfvyks nhagpygcas gdegsvfniy diagpdapsg
      181 ntqammnlaa eyamtkcdkd esyckwetiq kgeptygppv crgdsqyndt gsdapftftk
      241 teksinsstv ggyiqhsnea gvtlqlgnkd igsltiaqkf tetwqknyar tvgeeevyeq
      301 kanftipdgh ygwleeqpqi rkltgkfvfd snnwaqweyg adannpmvad vvlggdgkqn
      361 nslwtmrtsp nrptsc
//
LOCUS       WP_457699167             216 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699167
VERSION     WP_457699167.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841242
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22854
     Region          40..86
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          107..213
                     /region_name="TetR_C_16"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17920"
                     /db_xref="CDD:465568"
ORIGIN      
        1 msggrddass gpgtppapar rrgrparaaa eagpgardri laaartefae rgydktsvrg
       61 iakaagvdaa lvhhyfgtke qvfaaaielt fapaltmpda lagggadvge rmarfmfgvw
      121 enpvsrqpll aimrsaltnd taaavlrgli errmlqrvag eldvpdpefr vqlaaghlig
      181 iamlryvikm dpvasadpee iivmvaptlq ryltqp
//
LOCUS       WP_457699200             164 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699200
VERSION     WP_457699200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..164
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17706
     Region          29..161
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 msaghraaar teqggaateg prrsaalhra ealrllgtvs lgrivftrha lpaihpvphl
       61 vddgdivlrt hegaalttrd rragaggvvv ayeadaidpv thlgwsvvvt gychlvtdpa
      121 alaryrrllh pgwsrpdehp rrerphehvl rirpdlvtgi rlta
//
LOCUS       WP_457699202             387 aa            linear   BCT 27-JAN-2026
DEFINITION  pseudouridine synthase [Streptomyces nigrescens].
ACCESSION   WP_457699202
VERSION     WP_457699202.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=41770
     Region          149..368
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrssgrnnds grgnyrgagg gasqpkaggk rdekqqragr prpeerrydv ggtggpggkd
       61 erggaksggg pksgapksgg srgaaargga kggprtgaks gpgakggpqr grgqaparpr
      121 eydaqveern rarhnkpqik tpktfgdqeg erlqkvlara gmgsrracee lidqarvevn
      181 gqivmeqgvr vdpekdeikv dgltvatqsy lffalnkpag vvstmedpdg rqclgdyvtn
      241 retrlfhvgr ldtetegiil ltnhgelahr lthprygvkk tylaaiqgpl prdlgkqlkd
      301 giqledgyar adhfrvvent gknylvevtl hegrkhivrr mlseagfpvd klvrtsfgpi
      361 algdqksgwl rrmtntevgm lmrevel
//
LOCUS       WP_457699218             347 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 16 protein [Streptomyces nigrescens].
ACCESSION   WP_457699218
VERSION     WP_457699218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Henrissat,B. and Bairoch,A.
  TITLE     Updating the sequence-based classification of glycosyl hydrolases
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 695-696 (1996)
   PUBMED   8687420
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Henrissat,B.
  TITLE     A classification of glycosyl hydrolases based on amino acid
            sequence similarities
  JOURNAL   Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
   PUBMED   1747104
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10115061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="glycoside hydrolase family 16 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36665
     Region          53..321
                     /region_name="GH16_Strep_laminarinase_like"
                     /note="Streptomyces laminarinase-like, member of glycosyl
                     hydrolase family 16; cd02182"
                     /db_xref="CDD:185691"
     Site            order(124,127,129,163,165,167,185,187,190,201,203,283,285,
                     287)
                     /site_type="active"
                     /db_xref="CDD:185691"
     Site            order(185,187,190)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185691"
ORIGIN      
        1 msmrfrpgnr vrhrarapll algavlvttc altlptasaq qaapvakaap aafqevwrtd
       61 fdgaagsrpa addwiidtgt gypsgppnwg tgerqtytdr penlqldgag hlritarkdg
      121 atwtsgries rrsdfaapsg gtlrieasir mpefsgdaal gywpafwtlg adyrgtywnw
      181 pgigefdime nvngvnkvwg vlhcgvnpgg pcnesqgrgs srecpgsacq agfhtyalel
      241 drtnsaaesl nwyvdgqkfh tvsaaamdad twarathhgh fllinlamgg afpdgaagfa
      301 tptdatrpgg sllvdhvavs vrqpagartg raatptdrhp apqgaps
//
LOCUS       WP_457699220             350 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699220
VERSION     WP_457699220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 350)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37469
     Region          9..349
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mvsepngprp tleavaalag vsratvsrvv nggagvraav qervrqavte lgyvpnsaar
       61 slvtrrtgav avviaepetr vfsdpffgrq lrgisrelaa adtqlllmfv ehradydrig
      121 rylsaghvdg almfslhrdd plpamadrag lptvyggrpg wagadrvprp lyvdtdnrgg
      181 arqavrhllg rgrrriavit gpldqtsavd rldgyreals taepdprlia dggftahgge
      241 ramaelldaa pdldavfvcs dlmasgalrt lrahgrrvpe evavvgyddl epaawadppl
      301 ttvrqdveem grlmarlllr lldprktega davelapvit earlvvresg
//
LOCUS       WP_457699222             543 aa            linear   BCT 27-JAN-2026
DEFINITION  PucR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699222
VERSION     WP_457699222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..543
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=57952
     Region          16..136
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          247..538
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgqeakieae itvrralelp alrrglpevl aggdrldrav rwvhagevph iasllkggel
       61 llttglglga rpseqrafir kladreiaal vvelgsrfas lptalvdaar dcglpliqlh
      121 revpyvtvte aihteiinsh yallrradei lrrctdvllr gggvpevlrl lavftgnplc
      181 leapdgsply aagpegdddg padadpllaw eglrdtglrv dvpggghgpd avrarlvllp
      241 vnaplapvhr iaaeraadll avvmlqsrqe evlaargrgd fladlaegqi saaeapvqar
      301 llgfrpgaep vfpvvmrlpa glpspgswal laqalreela apgvpvllgv rpvegrvpml
      361 valragqdrd alagriaeal ragivragld rpathrpvvv vgtpgdwaaa gpglqhaaea
      421 aaaaqglpeq pwydarrldi elllwrmreh geqgvltdfv eraigpllah draarqpllp
      481 tleaylasag rkaetardln vnrqtlydrl ariaqllgtd lddpqtvlgl rlalrarrht
      541 dkp
//
LOCUS       WP_457699224             237 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457699224
VERSION     WP_457699224.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23887
     Region          1..234
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtaavagfal fallvtmapg pdtllvlrnc vrggrrtgaa tavgaavgsl awavaaavgl
       61 aaalqrwdaa ftvvrlagaa ylavlggqal wahrrsaavt tpaaapgpdp fdapdlfdap
      121 epdgapipdg sataslaplr afrqgllscl lnpkvgiffv avvpqflpeg hsvlgttlll
      181 gavdaviaag wlllvvvcag rllrrlrrpr vhrtlerttg gvlialgigt aaetvag
//
LOCUS       WP_457699228             399 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457699228
VERSION     WP_457699228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..399
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=42401
     Region          32..361
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mvrpppiqep dhvistptsa hglsplrtvq vlgrgsagsa ahvrslaegl vargvrvtvc
       61 atpeteeayd ftgagarfvq vpprmdpasv avlrsacwda dlvhahglra glrasmalrg
      121 lrgprggrrv plvitwhtka hiegaragvv hlmerrvara aavvlgacsd lvdrarerga
      181 rdarlapvai prprsggtpn aledhdrrrh keraelgavd rplllavgrl dpnqghdlll
      241 daahawcald prplvaiage geqrtalqrr idseqlpvql lgrrddvpel laaadlvvlp
      301 srwearslia qealragvpl vatdtggtre lvgraaelvr ygdaaalart vlalladpar
      361 rdalaaagra qaagwpsend tvtqvlsvyd eltqpiqpv
//
LOCUS       WP_457699235             293 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699235
VERSION     WP_457699235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31106
     Region          3..256
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msrltaenvt laydqrviae nlsvaipdhs ftvivgpnac gkstllrals rmlkpakgsv
       61 lldgaaissl pakkvartlg llpqssiapd gitvsdlvar gryphqgllr qwspederiv
      121 eesmaatgvg eladryvdel sggqrqrvwi amalaqqtpl flldepttyl diqhqievld
      181 lcaelheeqg rtlvavlhdl nhaaryathl iamkdgavia egapadivta elveqvfglg
      241 cqiiedpetg tplvvpaark prnggsragr pttekapaga ekepagagqa rgr
//
LOCUS       WP_457699237             377 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699237
VERSION     WP_457699237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="FecCD family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38643
     Region          32..351
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msatvksgeg tgpeaenvpa avrrvravrt kgglslrldm raavvallll avalaagial
       61 igsgdypmtp aevlatltgd gdpgqqyivh elrlprvlvg llvgaafgis gavfqtvsrn
      121 plgspdvlgf aqgssvgalv aivyfqagaf gvaagavvgg vstgiaifll awkrgihgyr
      181 fvlvgigasa mlyamvlflm tkaniveatr attwmtgsln grdwdqvqpl aavcavlvpl
      241 llfhgrplrm lemgddaaya lgvrvdrvri tvllaavvlv aaataaagpi sfvaltapqv
      301 arrltlprwl kggggapmpg pnlvlsalmg avllvaadwt sqrlfgadql pvgvltgvlg
      361 ggyllwllat erkagrv
//
LOCUS       WP_457699239             349 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699239
VERSION     WP_457699239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..349
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35707
     Region          43..345
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlvdsppeaa tapdpvtprr rpllrsaglv vsvavlaviv vlgiavgakq ipldqvwhgv
       61 fhysgsdtdv virdvrfprt llglivgaal glagtvmqal trnpladpgv lginagasaa
      121 vvsaisffgi tsltgyvwfa fagaavvnva vyvlggtrga tpvrlalaga altavligyi
      181 navnlmdtaa ldkmrfwtvg slasatlptv tgiapflavg gvlalliarp lnaialgddq
      241 aralgarltr trvlamlavt llcggataac gpivyvglmv phavravtgp dmrwilpysa
      301 vlspvlllga dvlgrvvarp gelqvgivta vlggpvfiyl vrrrrmaql
//
LOCUS       WP_457699241             342 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699241
VERSION     WP_457699241.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..342
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36112
     Region          66..339
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mstsrnvtps rrgilaagga vgigallaac gggkdsggan gdaktgpwsf tddrkqkvsl
       61 knspqrivaf tgtaaalhdf giddqivgvf gptklkngkp dpqagdldvd kvtiignayn
      121 qfnvekyasl rpdllvtnmy epgalwfvpd dskdkitpla ksvaitsarv pllkiierya
      181 dlakslgadl gakkvtdaka rfekasaalr kaakshpvkv lacsgspdlf yasnpginad
      241 lmyykslgvd livpdhldkg gyfeslswen adkykadvll ldnrtatlqp kdlaakpswa
      301 klpavkagqi tpwsseprfs yagaaplies lakaiegakk vk
//
LOCUS       WP_457699243             296 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457699243
VERSION     WP_457699243.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..296
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32580
     Region          12..280
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtttaapata pfrffdvhvv rarrvspsvv ritfggdrld elasggrdqr fklflpqphq
       61 drpvfhdtgd swyttwraqd paeravmrsy tireqrhdpr efdvdfalhg agpgadplag
      121 gpasrwaaha rpgdrltvla pavednggvd frppsgtdwi litgdetalp aiagilswls
      181 pgtrakvwie iaheddrqql psfadaditw lvrdeataar repvldalra aelpegtpya
      241 wvageagtvk avrrhlvrer gidrravkft gywrrgasee dllaeltagp akpeed
//
LOCUS       WP_457699247             534 aa            linear   BCT 27-JAN-2026
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457699247
VERSION     WP_457699247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
REFERENCE   2  (residues 1 to 534)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..534
                     /product="pyridoxal phosphate-dependent decarboxylase
                     family protein"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0016830 - carbon-carbon lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019752 - carboxylic acid metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=58108
     Region          27..519
                     /region_name="GadA"
                     /note="Glutamate or tyrosine decarboxylase or a related
                     PLP-dependent protein [Amino acid transport and
                     metabolism]; COG0076"
                     /db_xref="CDD:439846"
ORIGIN      
        1 msllahsaed padgraylln ngtarryhsa vtesvtrisa kiagtarpft gitvdgltpt
       61 vsgvdldtpl hdaaaaldel eevylrdavy fhhprylahl ncpvvipalv geavlsavns
      121 sldtwdqsag gtlierrlid wtadriglge aadgiftsgg sqsnlqamll ardeacrrel
      181 tregatspkf stppplstsf ergdpheqgg ppsrltdvlp rlriltsecs hfsirksatl
      241 lgmgaeavia vpsdgdkrmr tdelaaelar crrdglipma vvatagttdf gsidplpeia
      301 glcaaygawm hvdaaygcgl lvsrrralls gieransvtv dyhksffqpv sssailvrdr
      361 atlrhvtyha dylnprrmve qripnqvdks iqttrrfdal klwltlrimg aqavgelfde
      421 vidrsadawk llhddprfev vveprlstlv fryvpttdqd pelsdrvnlh arealfasge
      481 aivastvvdg rhylkftlln pettlediat vldliaehag sflaeqsrpa lsar
//
LOCUS       WP_457699249             439 aa            linear   BCT 27-JAN-2026
DEFINITION  lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457699249
VERSION     WP_457699249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Visca,P., Ciervo,A. and Orsi,N.
  TITLE     Cloning and nucleotide sequence of the pvdA gene encoding the
            pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in
            Pseudomonas aeruginosa
  JOURNAL   J Bacteriol 176 (4), 1128-1140 (1994)
   PUBMED   8106324
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790239
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..439
                     /product="lysine N(6)-hydroxylase/L-ornithine
                     N(5)-oxygenase family protein"
                     /EC_number="1.14.13.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49067
     Region          4..430
                     /region_name="IucD"
                     /note="Lysine/ornithine N-monooxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3486"
                     /db_xref="CDD:442709"
ORIGIN      
        1 msapydfiai glgpfnlgla cltepidgld glfldnkasf dwhpgmmlds shlqvpflad
       61 lvtladptsp fsflnylkes grlysfyire nfyplraefn dycrwaagkl asvrfahqvt
      121 tveydereel yvvhaeqlpt gerhtfrarr lvlgtgtpph ipeacqdlgg dllhnagyld
      181 akaalqakds itligsgqsa aeiyfdllqd idshgyhltw atrsprffpl eytkltlemt
      241 speyvdyfha lppatrdhln atqkhlykgi dsalindifd llyqknlagp vptrlltnta
      301 lcqagydeas gtytlglrqe eqgtdfaldt qglilatgyr yrvpdflsav rdrivwddag
      361 rydvarnysi dttgrgifvq naelhthgfv tpdlgmaayr naciirellg reyypvekai
      421 afqefaapag shhpmelpv
//
LOCUS       WP_457699251             189 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699251
VERSION     WP_457699251.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20838
     Region          22..166
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mstplftrtd atlgefslrp vdpygdaell hrwvthpkaa fwlmqdcdla avekefaris
       61 adpfhdaflg lhngtpaflm erydpahrel vgihaaepgd vgmhflsapt dtpvhgftla
      121 vittvmemlf adpatrrvvv epdarntavh alnkavgfei lrtvslpskd aylsictrdq
      181 flatrgdhr
//
LOCUS       WP_457699253             605 aa            linear   BCT 27-JAN-2026
DEFINITION  IucA/IucC family protein [Streptomyces nigrescens].
ACCESSION   WP_457699253
VERSION     WP_457699253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   de Lorenzo,V. and Neilands,J.B.
  TITLE     Characterization of iucA and iucC genes of the aerobactin system of
            plasmid ColV-K30 in Escherichia coli
  JOURNAL   J Bacteriol 167 (1), 350-355 (1986)
   PUBMED   3087960
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468178
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..605
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67166
     Region          20..600
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtapsdgtpt lsardavahl tpdlwaranr llirkglaef aherlltpkr lpqdghyair
       61 sddgtteyrf aarrraldhw qidadsitrh rddselplda laffielrds lglgeailpv
      121 yleeisstls gtayklaagr tgaaelakap fqaietgmte ghpcfvanng rlgfgiheyh
      181 ayapetaapl rliwlaarrd hatftagagl dydalirdel pegtrtrfaa tlttlgldpa
      241 dyyffpthpw qwwnklsvtf aaevaqqrlv clgpgdddyl aqqsirtffn ttdpakhyvk
      301 talsvlnmgf mrglsasyme atpaindwla rliaaddtfr aarfsiirer aaigyhhrqy
      361 eaatakgspy rkmlaalwre spvptlepgq rlatmasllh vdhdggslaa alieesglep
      421 avwlrrylda yltpvlhafy aydlvfmphg enailviedg avarvifkdi aeeiavldpd
      481 avlpptveri radvpedkkl lsvftdvfdc ffrflsgtld dhgildedtf wrtvaacvtd
      541 yqaatphlad kfdrynlftd efalsclnrl qlrnnqemvd lqdpagalql igtlrnplap
      601 yapas
//
LOCUS       WP_457699265             224 aa            linear   BCT 27-JAN-2026
DEFINITION  urease accessory protein UreF [Streptomyces nigrescens].
ACCESSION   WP_457699265
VERSION     WP_457699265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22548
     Region          2..224
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 msraallvla dgrfpaggha hsggaepava agrikdaatl eafcrgrlht aglvaaglaa
       61 aaaaghdpll lddaadartp vpalrqvarr lgrqmmraar atwpsaalda lavarprgah
      121 qpvvlglaar saglppvdaa yavayenisg pataavrlls ldpfdatavl arltadldrv
      181 aeqgaeaarr vaaegvdalp aasaplldit aqqhagwpvr lfas
//
LOCUS       WP_457699269             314 aa            linear   BCT 27-JAN-2026
DEFINITION  M28 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457699269
VERSION     WP_457699269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 314)
  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 314)
  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 10133821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..314
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32924
     Region          42..314
                     /region_name="M28_SGAP_like"
                     /note="M28 Zn-peptidase Streptomyces griseus
                     aminopeptidase and similar proteins; cd03876"
                     /db_xref="CDD:349873"
     Site            order(123,135..136,169..170,197..198,236,239..240,256,
                     283..284)
                     /site_type="active"
                     /db_xref="CDD:349873"
ORIGIN      
        1 mtrstrirra alatgavtav aatlftaaga yagdapaaap didvkavqgd lgqlqsiada
       61 nggnrahgqp gykasvdfik gkldkagftt kveefdgggt kgynlvadwp ggdesktvma
      121 gahldsvpdg pgindngsgs agilevalav akaelkptkh lrfawfgdee dgmvgsqayv
      181 dklgadkski daylnfdmig spnpgyfvyd ddtrlekvfk dffakknlat eketegdgrs
      241 dhapfkeagv pvgglfsgad ykkteeqakn wggeagkafd acyhqscdds knidekaldn
      301 ntdaiahalw elss
//
LOCUS       WP_457699271             104 aa            linear   BCT 27-JAN-2026
DEFINITION  type II toxin-antitoxin system Phd/YefM family antitoxin
            [Streptomyces nigrescens].
ACCESSION   WP_457699271
VERSION     WP_457699271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Alonso,J.C.
  TITLE     Toxin-Antitoxin Systems in Pathogenic Bacteria
  JOURNAL   Toxins (Basel) 13 (2) (2021)
   PUBMED   33498357
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Fraikin,N., Goormaghtigh,F. and Van Melderen,L.
  TITLE     Type II Toxin-Antitoxin Systems: Evolution and Revolutions
  JOURNAL   J Bacteriol 202 (7) (2020)
   PUBMED   31932311
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10019301
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..104
                     /product="type II toxin-antitoxin system Phd/YefM family
                     antitoxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /calculated_mol_wt=11253
     Region          4..54
                     /region_name="phd_fam"
                     /note="prevent-host-death family protein; TIGR01552"
                     /db_xref="CDD:273688"
ORIGIN      
        1 mayeipvtqa raeladlinr vvyggervvv trhgkplval vsaadlqlld elgrreqgae
       61 eeqvistvst vrqlpsapge rrrfgiaaeh rdpaagdrrp gres
//
LOCUS       WP_457699277             157 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457699277
VERSION     WP_457699277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=16696
     Region          <7..156
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mtvrmhtpnl laragtvtal tlvtlsgttv apgaagnaea asvsgyalri aaskrgapyq
       61 ygaqgphafd csgltlysfk ragralprta aaqygrtrhi pttlrrrgdl vffhsgrgiy
      121 hvgiyagrgr mwhapkagsv vrleriwsrt vtygrvg
//
LOCUS       WP_457699281             305 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699281
VERSION     WP_457699281.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31674
     Region          17..300
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mydptrlaal vavaeagsit raaarlgyta palsqqlakl ereagtpllv rhhrgarlta
       61 agellvvrar rvldeldqar helsrltgls ggrlrvgtfm tagthllppa lsafrrahpd
      121 velsiteyvp pqaaaavalg evdlalthey vpgeampppe gvrlepllte elvlvtapgh
      181 alsagagrlp laelagqplv smapanpnrr aveavlaaag asvavrcesp syavvcalvs
      241 aglgmavvpe mmaegsvtpl girrldppel hrrisvvyrp gggspaadtl rallrgafsr
      301 hspap
//
LOCUS       WP_457699279             219 aa            linear   BCT 27-JAN-2026
DEFINITION  LysE family translocator [Streptomyces nigrescens].
ACCESSION   WP_457699279
VERSION     WP_457699279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21906
     Region          4..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdgqliaftg iaagmvtmpg adfavvvrna ldsrragvat avgvaggllv htalavagla
       61 avlvavpalf gavqllggvy llylgagali aavrrtgara dsvtgpaaap adgppallgt
      121 arslrqgflt nalnpkapvl flsllpqfvp agepalprtl llatmvvama lvwfpaiall
      181 vdrlgswlrr pqvtraleat tgalltalgg illvelvla
//
LOCUS       WP_457699283             142 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699283
VERSION     WP_457699283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..142
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15209
     Region          8..137
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 madhhesslt lpsapasvlt arrhalavla ewglpaesal adslrlivse latnavvhts
       61 gqspdftvel rldrdeqlri gitdshprrp rrlpaavqqd ngrglviiry laaeaggrls
      121 vvptesggkt vwitvpwqta vr
//
LOCUS       WP_457699284             408 aa            linear   BCT 27-JAN-2026
DEFINITION  8-amino-7-oxononanoate synthase [Streptomyces nigrescens].
ACCESSION   WP_457699284
VERSION     WP_457699284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="8-amino-7-oxononanoate synthase"
                     /EC_number="2.3.1.47"
                     /GO_function="GO:0008710 - 8-amino-7-oxononanoate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41305
     Region          32..405
                     /region_name="PRK05958"
                     /note="8-amino-7-oxononanoate synthase; Reviewed"
                     /db_xref="CDD:235655"
     Site            order(129..130,133,195,224,227,256,259)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99742"
     Site            259
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99742"
ORIGIN      
        1 mpqdtapsll hdttpatpde paaapsrpvy gaafdwidea raarhraglv rtlrprpads
       61 rlldlasndy lglarhpevt rgaaaaahrw gagatgsrlv tgstelharl eaelaafcgf
      121 eaalvlssgy aanlaavtal tapgtlvvsd agnhaslidg crlsrartev aphadpeavr
      181 ealtahdgra lavtdavfsv dgdaaplpal aevcraagaa llvddahglg vlgeggrgal
      241 waaglagdgd vvttvtlsks lgsqggavlg parviehlvn tarsfifdtg lapaaaggal
      301 talrllrrep qraaragqva relhdrltaa glsavrpdaa vvsvrapspe aavrwaadcr
      361 aaglavgcfr ppsvpdgisr lrltaradlt daqldtavgt ivatapav
//
LOCUS       WP_457699292             223 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699292
VERSION     WP_457699292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..223
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23822
     Region          38..159
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mwqrrrvphg tvhhpvfarf yasccgpaad aragvaalrk elltgatgrv ievgagtgln
       61 fahypgtvse vvaiepeptl revarsaaar aevpvdlvpg vaealpvkse afdtavaslv
      121 lcsvyevqra lmelrrvlrp ggelrffehg raagrglaav qwsldrtvwp llmggchtgr
      181 dplgeirtag fevlrvrrlk vpergptlpt spavlgtarr pad
//
LOCUS       WP_457699296             493 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457699296
VERSION     WP_457699296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..493
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51091
     Region          1..458
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtdrhgaaqp davahhtvde vperarhgct relftlgfgt hiaplalvtg amavqvfhqp
       61 lwsgvlavlv gqllggvfma phrapgpqlg lpqmirsrar sgslgalpgv vvaaalyvtf
      121 faahlvlagr slhvlapglp vgagillgaa gsavlcligh rllhalnkva avvlglgiva
      181 gfalaairgl pstdfftrgg ftfagwlaiv slsalwqpal apyaaapsra lpgtvrttat
      241 fwatygsscl gsllpflaga avapvcpgpd taagigaaag sfgpvllvlf lfsvlhhtal
      301 nlyramqatl tigqtfrarw qprprvrgav salvlacgpa lalglagdfv trfadlvlvl
      361 laalvpwaai nlvdisllrh gsqdpdelca pdgapcrrfd qvalgsyavg iavqipflat
      421 glytgppaah fsgadlswlv gpavtaplyf lwarsrrrce ggtvlgmreq aarildplrp
      481 lypedvrgfa dtr
//
LOCUS       WP_457699298             493 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457699298
VERSION     WP_457699298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..493
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52006
     Region          8..433
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msvpapvphl rrslrrfdim amgvaavisf dvigqiaagg gqavtwiavi avvfllpyal
       61 vfaetgaafp qeggpyvwve vafgrpaavl tttfywvtnp vwlggslvfv aagawdgfvr
      121 plgsgtvady vfklvfiwaa iltavvslrr gkwittagag akvlalafft gtavaygvqh
      181 gfrglqgsgf sptgvgflal vpvllfafvg feapnaagde mldpqrdvpv aigvsgaiat
      241 ccyllpvlai lsaappgrvt gvggfmdaar lvfgiygdwr gplltfvavl fvvalltqgs
      301 awmivadrmq amaaadggff srglgafhpr lgtpvrmnll sgvtatvfma aamnlakgda
      361 savfgvvltv aittlllsyl avvpallalr lrhrevprpy rvpfgtlgft vatllvyawi
      421 vlgswvalfp gtleqlfgip ydfravwgvs rltfeaftlg tvvlllvvaa agyltqrmht
      481 qsqdderqar par
//
LOCUS       WP_457699309             438 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457699309
VERSION     WP_457699309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44366
     Region          35..398
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(45..46,49..50,53,86,139..140,142..144,147,167,
                     170..171,174,252,255..256,259..261,264,292,296,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 myladgrpap stsvspggrr agrsrrvraa vpstvlvlga vslitdisse mvtavlplyl
       61 vaelglsplg fgvldgvyng vsalvrlvgg rlsdrgggrg hkavaavgyg lsalckplll
      121 mvhslpliga vlavdrtgkg lrtaprdami slaaepaarg rafgvhramd tagalcgplv
      181 afvllraaae gydavftvsf cvavlgvvvl llfvpgralp atedtagarp agprtpvral
      241 lalpqvrrlt gcavllgltt vsdsflylal qrrldlpagw fpllplgtaa aflslavpmg
      301 aiadrigrrr lfvaghlvll gayglllapf gdgaalvcav lvlhgafyaa tdgvlaaata
      361 davpedargs glavvqtgqt aarfvcslaf gaawtawgdr tavlasavgl alaaalsarl
      421 lrpvspapap nspsehtp
//
LOCUS       WP_457699315             412 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457699315
VERSION     WP_457699315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..412
                     /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=43675
     Region          197..410
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpsslpavlr pfsravtytr wlhlliasva gmltgflyne pffaggwltw lwmavlplpl
       61 lvlaalipvv rrveglqaql lltpgphgle araasgiatt psgswsdrgr tavwlllrle
      121 vgvalsaltv qlpmlagvfm maaagrrthl kglpaieaph wwygllaplp lvllaavavg
      181 agsltaaaar lllgpsaaer laelearter mlghnrlaqe lhdaighalt vtvvqagaar
      241 aagspdfter alaaiedtgr qaladleral rllredaprp adrptltdae rllesaraag
      301 sdlraelsgp leslpgpvsr egyrmvqeal tnvlrhagpv pvavrmaada dalelevrnp
      361 lpvispnpgs ggrgrglrgi reraallgge aetgpdggew rvrarlplrq lr
//
LOCUS       WP_457699319             390 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699319
VERSION     WP_457699319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=40684
     Region          20..66
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          82..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 lhalraadsp tltdlvqvtg lsrptvegvv eglietglvv
       61 evpaeegetr rqgrparrfr frteaghllg ieigphrvaa llsdlggrvl dtaqrpvdet
      121 apaderlerv ravvadllrr tgvprsslra vgaagpgive adgtvrlsta lpgwtglplg
      181 erlrrsfrcp vlvendanaa avaehwlgaa tgsddivfvl aglspgagsl iggrlhrgfg
      241 gaageigalh llgreatpek llsttgeplh pldeaqvaav faaardgetq areavdrfir
      301 rlvhdvaalv laldpelvvi ggwaaglagv leplrgelar yclrppqvvl sqlgeaavat
      361 galrlaldhv egelfavegt vtarrgtaar
//
LOCUS       WP_457699321             248 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699321
VERSION     WP_457699321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26303
     Region          10..237
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mgttqletvp epkywhlktv lsealdsefa vgeilpnerd laarfgvara tlrqaleqle
       61 legrlqrrrg vgttvapprv gvavaparht wpgaagddwq pvdsvqsdtv paavahllet
      121 aagdrvhivr rsrvtqgrpl aaellyvpaa avpgcqeida lsgparahav lqelqslele
      181 gqdrtvelgs araedakqld rlpgapvlvv ttryvsggrt tavavstyra dtcrltfges
      241 davallag
//
LOCUS       WP_457699327             134 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457699327
VERSION     WP_457699327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..134
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14827
     Region          18..127
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mpangsahlr iarpsrglaa aerfwkqglg lselyrhhse agehallmlg wpdahwhlel
       61 tldpsgalep sptaddllvv ylgeevpadl varlercggk rvaahnpywd ewgvtledpd
      121 gyrlvlsrre wsns
//
LOCUS       WP_457699329             524 aa            linear   BCT 27-JAN-2026
DEFINITION  alkaline phosphatase D family protein [Streptomyces nigrescens].
ACCESSION   WP_457699329
VERSION     WP_457699329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Zambonelli,C. and Roberts,M.F.
  TITLE     An iron-dependent bacterial phospholipase D reminiscent of purple
            acid phosphatases
  JOURNAL   J Biol Chem 278 (16), 13706-13711 (2003)
   PUBMED   12519726
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Yang,H. and Roberts,M.F.
  TITLE     Cloning, overexpression, and characterization of a bacterial
            Ca2+-dependent phospholipase D
  JOURNAL   Protein Sci 11 (12), 2958-2968 (2002)
   PUBMED   12441393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..524
                     /product="alkaline phosphatase D family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57870
     Region          9..510
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 maqgsgsgfg rrsllqgaaa gsvalalptl scaapaqars grpsadwgvq vgdvttssgl
       61 vwvrsdrpar mvvqtaates frrarswpgp vigpdtdftg vtslhglpsg eqihyrvlla
      121 dpddprrtge pvsgtfrtap agrradlrfh wsgdlagqgw ginpdrggyr iyedmrrrnp
      181 dfflcsgdni yadnpiperv tlpdgriwrn vtteekskva etlaefrgaf rynllddnlr
      241 rfnaqvptit qwddhevhnn wypgqllddd rytekdtdvl sarslrafge yfpirtlrad
      301 rggrvyrvvh hgplldvfvl dmrryrnans pgrqtddpqg ilgaeqlrwl krelsrsqav
      361 wkviasdmpl glvvpdgktn feavaqgdpg aplgrelqla ellrhikhdr itgtvwlttd
      421 vhytsaqhya peraafkdfe pfwefvsgpl naggfqalkl dgtfgpaqpf ikapdrants
      481 paespqyfge vdidggsgel tvrlrqeggq vlfskvlqpg rvgq
//
LOCUS       WP_457699331             465 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699331
VERSION     WP_457699331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Chipman,D.M. and Shaanan,B.
  TITLE     The ACT domain family
  JOURNAL   Curr Opin Struct Biol 11 (6), 694-700 (2001)
   PUBMED   11751050
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18937972
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..465
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49911
     Region          106..159
                     /region_name="ACT"
                     /note="ACT domains are commonly involved in specifically
                     binding an amino acid or other small ligand leading to
                     regulation of the enzyme; cd02116"
                     /db_xref="CDD:153139"
     Region          296..424
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mteassanss rrphwrrdiv elaalftava vadavantva hgprgpvllc aaavallata
       61 gfhiwwsrrh enappptdtd atapssagra pgadgqetal wrmrttvrde pgslaalcta
      121 lgerrvdils lqthplsngt vdefllrapg altpaeltrt vagaggshsw leradahdlv
      181 daptrmlgla trtaldsael plalrqllgr ctihsvpkhs lrgqplaeqv ptegvleehl
      241 mkfrdpsggs ltierpqlpf tptefarvra lvdldarlgq rvpprrdvlt lpegneitvr
      301 radtsdlaaa remhdrcssk tlglryhgpv gdadrylghl lsprfgrtla vetasgrlva
      361 lghllwdgde tevallveda wqqrgigael lrrlvamaae agcesvyavt qasntgmvaa
      421 mrglrlpldy qieegtlvit arpagmpaar epresirihd gsgrr
//
LOCUS       WP_457699337             338 aa            linear   BCT 27-JAN-2026
DEFINITION  TolB family protein [Streptomyces nigrescens].
ACCESSION   WP_457699337
VERSION     WP_457699337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Bonsor,D.A., Hecht,O., Vankemmelbeke,M., Sharma,A., Krachler,A.M.,
            Housden,N.G., Lilly,K.J., James,R., Moore,G.R. and Kleanthous,C.
  TITLE     Allosteric beta-propeller signalling in TolB and its manipulation
            by translocating colicins
  JOURNAL   EMBO J 28 (18), 2846-2857 (2009)
   PUBMED   19696740
  REMARK    Erratum:[EMBO J. 2009 Sep 16;28(18):2858]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Abergel,C., Rigal,A., Chenivesse,S., Lazdunski,C., Claverie,J.M.,
            Bouveret,E. and Benedetti,H.
  TITLE     Crystallization and preliminary crystallographic study of a
            component of the Escherichia coli tol system: TolB
  JOURNAL   Acta Crystallogr D Biol Crystallogr 54 (Pt 1), 102-104 (1998)
   PUBMED   9761825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36597
     Region          215..>337
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
ORIGIN      
        1 mnrtarllil latvlvlggv avgatlhaag radrkdrtqs ggpevaagpv rlddprhglf
       61 rnmawgphrd eitavpegrl tgprtasgvr clrfhaasgt giclqavhge lrdtyravvl
      121 dnrlrelrhy dlagtptrar vspsgrtvaw tvfvsgdsya gtafstrtsv vdtrgrhlda
      181 nletyaltvd ghrvhavdin vwgvtfaddt hfyataatag ktylvrgnrs trtlralhpn
      241 vecpslspdg triaykkria gadpdapwrl yvldlrtlre tatgehrnid dqavwrdgrt
      301 lvyslpgdyg sdlwtvpang tgtphrllsa alapafsr
//
LOCUS       WP_457699349             361 aa            linear   BCT 27-JAN-2026
DEFINITION  mechanosensitive ion channel family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699349
VERSION     WP_457699349.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..361
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=38490
     Region          82..346
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mnravtlhdl ivagaalaag ivagvllrva lrwlgkhalk trwsgddilv dalravvpwa
       61 aitgglaaaa aalpltetag htvnrtlmvl lilvvtltaa rvitgvvral aqsrsgvags
      121 atifanitri ivlamgflvv lqtlgisiap lltalgvggl avalalqdtl anlfagvhil
      181 asktvqpgdy irlssgeegy vvdvnwrntv vrqlsnnlvi ipntqlagtn mtnftrpeqk
      241 ltilvqvgvg ydsdlghver vtmeviesvm kdvdggdpdh epavrfhtfg dsrisftvil
      301 gvgefsdqyr ikhefikrlh qryraegiri pspartvalq kpeeiviphq rdvadivppv
      361 p
//
LOCUS       WP_457699361             362 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699361
VERSION     WP_457699361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..362
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38017
     Region          160..>285
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 matsagvtpg aspdqdrvqe flervitdag aavaglctsl gdrlglytam agagpltsaq
       61 laartglaer yvrewlaaqv ageyvsyapd tdtyllpaeh aavladpelp tyaagfftam
      121 qalyatedtl ieafrtgegv gweehgpalf agtakffrpg yaaalvpewl taldgvvekl
      181 ergarvadvg cgygysttlm arafprshfh gfdfhrpsie aargiadeag lgdrvsfdva
      241 taqdfpgedf dlitffdclh dtgdpggalh haeevladgg tcmvvepnas ehaqentnpi
      301 graltaasva vclpsalaqh gpqalgnhag eeamreiadd aglhhwrlaa espvnrvyav
      361 gr
//
LOCUS       WP_457699364             181 aa            linear   BCT 27-JAN-2026
DEFINITION  PadR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699364
VERSION     WP_457699364.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..181
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20443
     Region          8..89
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          96..167
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 maefsparyv vlgliarhgp mtpyelkarv eddiqpfwpi lhaqlyripa elaqagllre
       61 eaetegrrrr ifhltdtgra alerwladpd taeaetrdpa qlklffadlg dpadivalaa
      121 qqaerhrkwl ahyeslrsal appadsrqrs rarllrlgvl herahaefwe svaadperld
      181 g
//
LOCUS       WP_457699366             351 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699366
VERSION     WP_457699366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36398
     Region          115..321
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpgnggcgvd agdlrnasda ggprggagaa teprarpyvh pelaavlasl parpenpyad
       61 vaavragfra lmapqmpahd prvtvrhtsv pgpdgnaiev qvlrpagaeg vlpgvlyvhg
      121 ggfvygeldg pgpmardaca aagavvvnvh yrlapehpyp agaedcyavl ewmaaaagel
      181 gldagriavt gasaggclsa alclmardrq gpriafqcll vpclddrggt asarraedrr
      241 iangpgirht wdtylgpgrr sdvpayaapa ratdlsglpp aylltcgldp lrdegldyar
      301 rlmeadvpve vkdvpgawhf feayapesrp arrttahwlg alrsaltedd a
//
LOCUS       WP_457699373             189 aa            linear   BCT 27-JAN-2026
DEFINITION  histidine phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699373
VERSION     WP_457699373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20503
     Region          23..186
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 msvrlkllaa arnsslletr fdddrpldaa gwheaeraap vlcrlaaael rycspsarcr
       61 qtgealglrp laqpalrdcd mgrwrgrtlg evtaaeprav eawladprsa phggesllef
      121 itrigswldt rpaedaagll avaepavvra alvyvfqapp haywridvqp lsvttltgrs
      181 gkwdlllea
//
LOCUS       WP_457699375             150 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699375
VERSION     WP_457699375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16182
     Region          <60..129
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mndhaldgye istdparlda dlvhywlatd aywavdrpre lhdravagsl nfglyasgsg
       61 rqagyarvvt dhatfawlcd vyicrddrgk glgtalveav adhltpsgls rltlatkdah
      121 gvyekigfra lvapeqwmtl glidpgpvgi
//
LOCUS       WP_457699377             499 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase-like domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699377
VERSION     WP_457699377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Freda,I., Exertier,C., Barile,A., Chaves-Sanjuan,A., Vega,M.V.,
            Isupov,M.N., Harmer,N.J., Gugole,E., Swuec,P., Bolognesi,M.,
            Scipioni,A., Savino,C., Di Salvo,M.L., Contestabile,R., Vallone,B.,
            Tramonti,A. and Montemiglio,L.C.
  TITLE     Structural insights into the DNA recognition mechanism by the
            bacterial transcription factor PdxR
  JOURNAL   Nucleic Acids Res 51 (15), 8237-8254 (2023)
   PUBMED   37378428
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..499
                     /product="aminotransferase-like domain-containing protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51744
     Region          20..494
                     /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 mqerssgael atilraelnr yspgeklpss ralverhrvs pvtvsralae laaeglvttr
       61 pgagafraep rseaprpvdt swqeialsae pggdqvprsv dasgvvatlg vpgpgvieln
      121 ggylhsdlqp eralaaalar agrrpgawgr ppvegvpelr awfareiaga ggplaasdvl
      181 vtaggqsalt aalralaapg apvlvespty pgmlavaras glrpvpvpld adgvrtdlla
      241 dafrasgarl fvcqplfqnp tgavlaaerr revlrvaraa gafvieddfa rllvhgdapt
      301 ppptliaddr dgtvvhvrsl tkatsanlrv galaargpvl drlraiqvvd sffvprplqe
      361 aalelvgspa wprhlrliag eltarrnalt talhqqlpal agpghgtayg ndhafgglyv
      421 ppggyhlwlr lpdgtdegal tgaalragva vaagrpyfpa eppaahlrls fasasgtgei
      481 tegvrrlrta ceelgvpvs
//
LOCUS       WP_457699378             320 aa            linear   BCT 27-JAN-2026
DEFINITION  DMT family transporter [Streptomyces nigrescens].
ACCESSION   WP_457699378
VERSION     WP_457699378.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Jack,D.L., Yang,N.M. and Saier,M.H. Jr.
  TITLE     The drug/metabolite transporter superfamily
  JOURNAL   Eur J Biochem 268 (13), 3620-3639 (2001)
   PUBMED   11432728
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="DMT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32141
     Region          51..296
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrdndsatat vaiavnapaa agqaiptaaa pargtlasrg allaalgvaa fsltfpataw
       61 alegmgpwtv vmlrsvlaav laggalavfr vrlperrhwa giavvaggvv lgfpllttla
      121 lqtsttshaa vvvgllpltt aaysavrtga rpsrtfwvas magaavvigf avqqsggapg
      181 rgdlllfaal lvcaagyaeg grlarhlpgw qvigwalvla lpvtvagaav alsteplrlt
      241 ahaiggvlwl atgstflgmv awyrgmaaig ihkasqlqla qplltlvwsv lllgerlppa
      301 apaaalavla ciavtqrsrg
//
LOCUS       WP_457699387             404 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457699387
VERSION     WP_457699387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Yang,X., Kang,C.M., Brody,M.S. and Price,C.W.
  TITLE     Opposing pairs of serine protein kinases and phosphatases transmit
            signals of environmental stress to activate a bacterial
            transcription factor
  JOURNAL   Genes Dev 10 (18), 2265-2275 (1996)
   PUBMED   8824586
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Barak,I., Behari,J., Olmedo,G., Guzman,P., Brown,D.P., Castro,E.,
            Walker,D., Westpheling,J. and Youngman,P.
  TITLE     Structure and function of the Bacillus SpoIIE protein and its
            localization to sites of sporulation septum assembly
  JOURNAL   Mol Microbiol 19 (5), 1047-1060 (1996)
   PUBMED   8830262
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537757
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..404
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /calculated_mol_wt=42105
     Region          173..382
                     /region_name="SpoIIE"
                     /note="Stage II sporulation protein E (SpoIIE); pfam07228"
                     /db_xref="CDD:462119"
ORIGIN      
        1 mirnrargga ragaasarha fvfvlpglwv lgvvawelsh ptsgqllqll aaapaiacag
       61 tgrrqcvllg glcallalvp fgevepgtgl gtrlmtcgav lavigasylt agrrlrlvre
      121 lecsrevaaa aqrvllrplp rridgvllaa dhlsasegav vggdlyevvg trhgvravig
      181 dvrghgldam gtvaamlgsf revvhdepel gdvlrrlers hqrhlrerar tegpaadgep
      241 gsplaeefvt llllevardg svtalncghp wpyriacrav apvapadpmp plglfplpke
      301 lsavrcgrlr pgeglflhtd gaadardaag effplaqelr ssveaaaapc gpspagvvgs
      361 vrkallrhag grltddvall mlsndrvrvp vqaagtappt vrlp
//
LOCUS       WP_457699395             284 aa            linear   BCT 27-JAN-2026
DEFINITION  TrmH family RNA methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699395
VERSION     WP_457699395.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Krishnamohan,A. and Jackman,J.E.
  TITLE     A Family Divided: Distinct Structural and Mechanistic Features of
            the SpoU-TrmD (SPOUT) Methyltransferase Superfamily
  JOURNAL   Biochemistry 58 (5), 336-345 (2019)
   PUBMED   30457841
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Tkaczuk,K.L., Dunin-Horkawicz,S., Purta,E. and Bujnicki,J.M.
  TITLE     Structural and evolutionary bioinformatics of the SPOUT superfamily
            of methyltransferases
  JOURNAL   BMC Bioinformatics 8, 73 (2007)
   PUBMED   17338813
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Toyooka,T. and Hori,H.
  TITLE     Differences in substrate selectivities of the SPOUT superfamily of
            methyltransferases
  JOURNAL   Nucleic Acids Symp Ser (Oxf) (51), 445-446 (2007)
   PUBMED   18029778
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Anantharaman,V., Koonin,E.V. and Aravind,L.
  TITLE     SPOUT: a class of methyltransferases that includes spoU and trmD
            RNA methylase superfamilies, and novel superfamilies of predicted
            prokaryotic RNA methylases
  JOURNAL   J Mol Microbiol Biotechnol 4 (1), 71-75 (2002)
   PUBMED   11763972
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Koonin,E.V. and Rudd,K.E.
  TITLE     SpoU protein of Escherichia coli belongs to a new family of
            putative rRNA methylases
  JOURNAL   Nucleic Acids Res 21 (23), 5519 (1993)
   PUBMED   8265370
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="TrmH family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29389
     Region          8..274
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mgtpelispr sprvtaarrl arrafrgker rfiaegpqav reaiahrtgg aptlielfat
       61 veaaerhtei veaaraagvr vhyaddrtva disqtvtpqg llgvcgflds pfeeilaarp
      121 qliavlanvr dpgnagtvlr cadaagadav vltdasvdly npksvrasvg slfhlpvavg
      181 vpvervvsgl qaagvrilaa dgagdrdlda eldtgsmggp tawvfgneaw glpeetrala
      241 davvrvpihg kaeslnlata aavclyasar aqrspggcra vspa
//
LOCUS       WP_457699410             279 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457699410
VERSION     WP_457699410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  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 279)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..279
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29928
     Region          26..205
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 msslllltna lqpstevlpa lglllhsvrv apaegpalid tpgadvilid grrdlphvrs
       61 lcqllrstgp gcplvlvvte gglaavtadw giddvlldta gpaevearlr lamgrqqitt
      121 ddspmeirng dlsvdeatys aklkgrvldl tfkefellky laqhpgrvft raqllqevwg
      181 ydyfggtrtv dvhvrrlrak lgpeheslig tvrnvgyrfv tpekveraae akakeeaaka
      241 aksarsaepa egrahedgdg sgkavttgad srdarparr
//
LOCUS       WP_457699412             353 aa            linear   BCT 27-JAN-2026
DEFINITION  S1C family serine protease [Streptomyces nigrescens].
ACCESSION   WP_457699412
VERSION     WP_457699412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34936
     Region          145..>343
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtqsyrrsgd empqdrpyay gddhgqgygh eayggtpgag fseqavpplp pyapeprrra
       61 rrpvaliaav alasgliggg saaliagatq ssaqnssstp lvnagktsgg gvsgvakavs
      121 paiveikart agggstgsgv vvtsdgeivt nnhvlkgadt vtvtfndgsr ktaevvgtdp
      181 dkdlalvkvr gaknltaasl gdsdkitvgd qvvaigspeg ltgsvtsgiv saldrdvtvp
      241 keedqgqqgg pgdgggwpfe fggnqyngdt gssktsykai qtdaslnpgn sggalinmqg
      301 qiiginsamy spssessgss agsvglgfai pintvkddld alrgggnsgn sgv
//
LOCUS       WP_457699413             245 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457699413
VERSION     WP_457699413.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  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 245)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26989
     Region          10..221
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mspaehgdhp arilivddep avrealqrsl vfegyvteqa vdgldavekv avydpelivl
       61 dvlmprmdgl taarrlrasg vtvpilmlta rdtvgdrvtg ldagaddylv kpfeldella
      121 rirallrrss yaaaagappe egevlsfadl rmdlatrevt rgsrqveltr teftllemfl
      181 ahprqvltre qilkavwgfd feptsnsldv yvmylrrkte aggeprlvht vrgvgyvlrt
      241 dggae
//
LOCUS       WP_457699416             464 aa            linear   BCT 27-JAN-2026
DEFINITION  LmeA family phospholipid-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699416
VERSION     WP_457699416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Rahlwes,K.C., Osman,S.H. and Morita,Y.S.
  TITLE     Role of LmeA, a Mycobacterial Periplasmic Protein, in Maintaining
            the Mannosyltransferase MptA and Its Product Lipomannan under
            Stress
  JOURNAL   mSphere 5 (6) (2020)
   PUBMED   33148829
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Rahlwes,K.C., Ha,S.A., Motooka,D., Mayfield,J.A., Baumoel,L.R.,
            Strickland,J.N., Torres-Ocampo,A.P., Nakamura,S. and Morita,Y.S.
  TITLE     The cell envelope-associated phospholipid-binding protein LmeA is
            required for mannan polymerization in mycobacteria
  JOURNAL   J Biol Chem 292 (42), 17407-17417 (2017)
   PUBMED   28855252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10567863
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..464
                     /product="LmeA family phospholipid-binding protein"
                     /GO_function="GO:0005543 - phospholipid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50410
     Region          144..>293
                     /region_name="LmeA"
                     /note="LmeA-like phospholipid-binding; pfam11209"
                     /db_xref="CDD:431728"
ORIGIN      
        1 mrtptrissp sptpaaqrph slapgaqddp tgdtrkldtv npyadlaala dpepepepgp
       61 efgsfdadgt prrrtylner ddsddplglg lrsddeaaea wkppnhrrkn rrkkrglsrf
      121 aamsitvkll vavlvgtsfl tlfdrfavly aqnaaakkvk dalhlnatpe vdikgfpflt
      181 qvmdkrvdqv kvtipdlaad rvslakfeat gndvridgdl ptsikgatig tmngsvllaf
      241 ddmnrelgas qvkfsergpn avravgqlpi aghelrvrae ariqragdrg istdisqmrl
      301 digdiavyrp gtgkeeglrl trktaaelsr qaakvksmlg ipaiadrigi prpyiqealr
      361 neeklheltg sprfvqklmk vnlvdvvadh pwllqkvgid pkilgaltgl tkpqladqls
      421 lsfqlpktpg nirlrnisve edgiraditg selpiggakk epkk
//
LOCUS       WP_457699421             308 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699421
VERSION     WP_457699421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=33927
     Region          39..262
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mlprvdtdde wdaivpdeav mrpgvaalct rlgiradplt rypagsqpvy avgkryvlkl
       61 fpaaaaddgv tearvlahlq gqlplptpyv hdageyengw ryilmsrlrg tdlavtwpri
      121 pradqdriat eagetlaalh aldpsplagv lgpgdwgafl drqrttavgr qrdhglpepw
      181 leqisaflas tppsapgpgv llhtefmrqh ltvdehddwr ltglldfepa migqraydfv
      241 avglfvsrad prllsrifra ygktftptel lahtllhvys nlprylrelp tppeptldsv
      301 aetwfgtg
//
LOCUS       WP_457699429             272 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699429
VERSION     WP_457699429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29117
     Region          36..167
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtdpsaehda avtdrailtg sayktgrdls arqsiyqwqt prydlpgivv eqlrgtrgtv
       61 vdvgcgngkf ierlrrdrpe mrllgldvsl gilagvprpv avadaaqlpl astsvdgvla
      121 lhmlyhvedi paaikelarv vkpggvvlas tnsardkael dhlweraagd vlgvdkgpar
      181 islsarfsle qasgllgaaf dkvetielpg tiavrspepv vahmksyraw adqhavpfae
      241 tverareivs ehiertgafe igclggmlic tr
//
LOCUS       WP_457699431             602 aa            linear   BCT 27-JAN-2026
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            nigrescens].
ACCESSION   WP_457699431
VERSION     WP_457699431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 602)
  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 602)
  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 11432654
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..602
                     /product="bifunctional metallophosphatase/5'-nucleotidase"
                     /EC_number="3.1.-.-"
                     /EC_number="3.1.3.5"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0008253 - 5'-nucleotidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009166 - nucleotide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62990
     Region          46..582
                     /region_name="UshA"
                     /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or
                     3'-nucleotidase, 5'-nucleotidase family [Nucleotide
                     transport and metabolism, Defense mechanisms]; COG0737"
                     /db_xref="CDD:440500"
ORIGIN      
        1 mpatpqrrrt vrrltigaav laaagmaaga lpagadtgha artdrtvdvq llsfndfhgn
       61 leppqgssgt veeiqadgsk ksvpaggaey laqslrtark ghpysvtaaa gdlvgaspll
      121 sglfhdeptv eamnkldldv tsvgnhefde grkeltrlqk ggchpkdgcy edgkkfrgag
      181 fpyltanvtd dktgkpllkp ytvwkhkgvk igfigvtleg tpdivnaegi kglkfhdevk
      241 tinkyakvln rqgvksvval ihegglpast synyncdspg pgdgisgpit diakhvtprv
      301 dalvtghthq ayactipdps gkprtvtsaa sygklytdtt ltydrrthdi vrtavkapga
      361 anhvvdrtqp kaadmtslia rwnklaapva grpvghisad iagrganape splgdvisda
      421 qleatkadgk ggaqlalmnp ggvrsdlafk asgqegdgvv tygeaftvqp ftnmmnvldl
      481 tgaqlltglq qqvsgpnaas pkilqvskgl tytldmtksg adrvvkdsvk lngaaldpak
      541 tyrvamnefl agggdgfpaf kegknkyvgp sdldaftayl tahssadkpl tppkadritv
      601 vk
//
LOCUS       WP_457699433             207 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699433
VERSION     WP_457699433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23495
     Region          19..193
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 matssapatp plpytpdypi rterldlrpv thddfeaiht yqrrpevcry lywgpldeag
       61 srasvatktt rttlrgsgdv lqlavvvres gvligdvtfv wnsrehrqgg igyvfhpdha
      121 ghgyateasr allklgfeel klhriqaeld grntasarll erlgmrregh lrenefldge
      181 wsdeviyaml arewraqqee rqeqrqg
//
LOCUS       WP_457699436             842 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces sp. 900105755].
ACCESSION   WP_457699436
VERSION     WP_457699436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 900105755
  ORGANISM  Streptomyces sp. 900105755
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 842)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11905783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Streptomyces sp. 900105755"
                     /db_xref="taxon:3154389"
     Protein         1..842
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=87387
     Region          157..837
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
     Region          606..837
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mmlryalktv rarkagflga flallcaaal isacgtlldt glrgtirter yaatpvvvsa
       61 dqyvhrttvk hkhgktkvkh kakpiaeraw lpagletrla rtpgvarvvp eltflaqplt
      121 pagtggrsay ghawesaalt pyrlvsgtap kaasdlvvdr dlaarahlrt gdaltvqstq
      181 aprayritgi aapasdvrhq talffsaaea rrlaahpgqv tafgvlpahg tdprrlkdav
      241 trtlrgttaq vstgdargta efldaaaarv rlvsmgaamg gtsllvavlv vvgtfaltvq
      301 qrhrelallr aiaatpgqir rvlgrealii gvvagslgal lglplgawlh arfvalgavp
      361 ttlqhttgvv pplaalaatl agawtaaria srritrirpt ealaesrvep arpawgriaa
      421 gllllaggav lvvlltslrt epastpvtfl avvvlatsva llgpllvraa alllagplrl
      481 tghggrlata nlrgnaarma svvtpltlli gmtctvlfvq atlddaaraq aragvtadwv
      541 vaargpgvpa aaarqlraph dtvtevvrtt vrigldkypa qgvtpeglar twnpevtags
      601 lgrltdrtva vselaadqhr lrpgstlklt lgdgtpatlt vaavyarglg fgdltfahdl
      661 vshhvddpla ssvlvrtart haqlattlre fpgldilspa aadslqahrr qdnaevnlla
      721 mglvlaftai avvntiamsi adrvrefall rlagatrrqv lrmlrtevls vltlatalgs
      781 gialavltaf svgmtgraap tvtpllyvtv vatagllalm atalpgrval rvpavtaata
      841 kd
//
LOCUS       WP_457699442             139 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699442
VERSION     WP_457699442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 139)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..139
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15221
     Region          8..130
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
ORIGIN      
        1 mtspqnpvra agcvlwrrat tedgleialv hrpkyddwsh pkgklkrged alagavreva
       61 eetgmacrpg aplptsyyha ngrpktvryw aaealagaft pntevdrlew lspaearlrl
      121 tqerdrplvd allaalhla
//
LOCUS       WP_457699455             278 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699455
VERSION     WP_457699455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  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 278)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..278
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30130
     Region          52..159
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 marrpsvsaa apatapsrpv gnatrgttnp nrlrrmdrwi aaehgaalrr aadpvavdlg
       61 ygaapwtave llgrlrtvrp darvvgieid parvtaaray eqpgldfvhg gfevplpgqr
      121 trapvliraa nvlrqydede vaavwrrlca rlapggllve gtcdeigrrh vwvalgpegp
      181 rtvtfatrls alqtpsdlae rlpkalihrn vpgepvhafl rdfdrawata aplgalgarq
      241 rwraavaala tdwpltgdpr rrrqgevtvr wealaprs
//
LOCUS       WP_457699461             471 aa            linear   BCT 27-JAN-2026
DEFINITION  MDR family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457699461
VERSION     WP_457699461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..471
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48210
     Region          30..400
                     /region_name="MFS_MdtH_MDR_like"
                     /note="Multidrug resistance protein MdtH and similar
                     multidrug resistance (MDR) transporters of the Major
                     Facilitator Superfamily; cd17329"
                     /db_xref="CDD:340887"
     Site            order(39..40,43..44,46,79,129..130,132..134,137,157,
                     160..161,164,244,247..248,251..253,256,283,287,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 msastsgstr raglrravve svsglprqfw wlwtstlinr lgafvatfla lyltvergys
       61 asyaglvaal yglggvissv gagvmadrlg rrptmliaql staasvallg fmtdpvaiaa
      121 vaglvglatn asrpavqamm adivapqdrv rafslnywai nlgfaissta agliaehgyl
      181 tlflgeatlv lacalvifwk lpesrptagt pggpddaagg papapvsmlt vlrdgrfmtv
      241 vglnlllall fqqayvsmpv smgqdgfsst dfgmvvavng vlvvllqipv trfiehrspa
      301 mllvgsalla gygfgltala gsvamyavav ivwtlgeivn sptqmglvvr lsplhgrgry
      361 qgmyalswsv atltapllgg lvidhygada lwagcaavgt laalgyglll rglpeqtgae
      421 tvasgqpvta tataaqesse pvessepvas parrgreaga aagaatgepv a
//
LOCUS       WP_457699453             287 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699453
VERSION     WP_457699453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..287
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31453
     Region          <41..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          110..277
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mlyaeieiss flkarraald padlglpggv nrrrvrglrr eevaqlagis vdyytrieqg
       61 rapaisdsvl daiaralrls ggevtylrni avprrpaadc cavpargqtv rpeirqvlda
      121 maatvpalvi grgldilawn tlggriafdl ealapdrrnt allvfldpaa ralhpdweak
      181 avevvgnlra dsgrhpddlr icevvnella hspdfrriwe tqsvheclrg tkrilhphvg
      241 eldvtfesfr lstdpdqalv tytaprgset errirelgal tdpvlta
//
LOCUS       WP_457699473            1135 aa            linear   BCT 27-JAN-2026
DEFINITION  GH92 family glycosyl hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699473
VERSION     WP_457699473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1135
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=122292
     Region          244..1015
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mrlrhrhspl rgiarpaala aaalliitvp gpaqaappqp sqgatefrss fesgepqpdw
       61 tdtvdtgpdg kprtsgvtpe tapaapgmtt gtdtgprdsp takahagftg ghalryagth
      121 tahgrgysyn kifdvnapvt aatslsykif pemaksdpey pathaaidla ftdgtylsel
      181 savdqhgapl tprgqaaskt lyvnqwnnre arigavaagk tvdrilvgyd apeaprtapa
      241 frgwvddltl apkppdkpla hlsdyavttr gtlssgsfsr gntfpatavp ngfnfwtpvt
      301 nagsadwlye yarknnadnl ptlqafsash epspwmgdrq tfqvmpsvaa gtpdasrtgr
      361 alpfhhanet akphyygvtf dnglkteitp tdhaalmrft fpgdrgslif dnvnnkggls
      421 ldtergtvtg fsdvrsglsv gatrlfvygv fdapvtgggr leggggkdvt gylrfrpgad
      481 rtvtmriats lvsvdqakan ltreipdgst fagikdraqs qwdgllgrie vqgasrdqlt
      541 tlysnlyrly lypnsgfeqv gsrsryaspf spqvgrdtpt htgskivdge vyvnngfwdt
      601 yrttwpaysl ltpkragkmv dgfvqqykdg gwisrwsspg yadlmtgtss dvafadayak
      661 gvefdaeaay aaavknatva ppqpgvgrkg matapflgyt statregmsw alegylndfg
      721 iarmgkalye ktkkprykee sayflsraqn yvklfdrkvg ffqgkdargn wrlppgtfdp
      781 rvwghdytet nawsfaftap qdtrglanly ggraalakkl dayfstpeaa skefagsygd
      841 vihemteard trmgmyghsn qpshhiayvy daagrpwkaq ekvreamsrl ylgseigqgy
      901 pgdedngems awyvfsslgf yplvmgqgey avgsplftka tvhlengrdl tvnaprnnar
      961 nvyvqglrvn gkpwnstalp hrllarggtl dftmgdrpsa wgtgahaapt sitqddkvpt
     1021 ppadvtdpat gplfdntset agsfttaava pagparvssy tltsadrata pagwtlegsp
     1081 dgkrwtrldh rdgesftwdh qtrvfgisdp gsyrhyrlvp dgtgtlaeie llgap
//
LOCUS       WP_457699476             307 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699476
VERSION     WP_457699476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34029
     Region          2..304
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mkhgkyrfia gflalplaiy aifvispfvq aiyysftdwt glspdmkmvg fdnyarlfqd
       61 dvfwsavgns vtlllllpvv tlslglffaf mlnvggrrrr kaviggvrgs gtykilyffp
      121 qvlsvpival lfqfaynpes galnaffdai gldnvqpdwl gdpqialwcv maamvwanvg
      181 fyvvlfsagm ssipkdfyea alldganrfn tffritlpll wdtvqtgwiy mgilaldvsa
      241 fafvqimsvg pggpdystev lplyvyqktf rdgqagyata igvsllivtl ifsavvmrlg
      301 rrerlef
//
LOCUS       WP_457699477             321 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699477
VERSION     WP_457699477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 321)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..321
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34267
     Region          49..321
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 msaqtdpadl pgvtkehppp pgasrlpgpr ggqgrkggag sgggssegkv lnvfshgvlv
       61 iwgllvtmpl lwavvssfkd dteifgspwg lpsvlhfdnw srawdkahmg qyflnslivv
      121 ggsligtmll gamaayvlar fdfpgnrfly flfvggmgfp cilalvplff vmknmalldt
      181 yhglilvyia yslpftvffl sgffktlpts vaeaalidga shtrtffqvm lpmakpglis
      241 vgifnflgqw nqyllptvln vgdpdqkmlt qglvalavsq gykgdwsglf agltiamlpv
      301 laayiifqrq vvagltagal k
//
LOCUS       WP_457699479             399 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699479
VERSION     WP_457699479.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=40244
     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 avrmagsltq aeiarstgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vvgvdfghsh lrvavgnlah qvlaeeaepi dvdasaaegf
      121 draeqlvnrl iaatgidagk vvgvglgvpg pidvesgtlg stailpgwtg tnpgqelsgr
      181 lgvpvhvdnd anlgalgelv wgggrgasdl ayikvasgvg aglvisgqiy rgpggtagei
      241 ghitldeagp vcrcgnrgcl etftaaryvl pllqpshgpd ltmsrvvqla regdpgcrrv
      301 iadvgrhigs gvanlcnlln psrvvlggdl aeagelvlap iresvsryai psaarqlgiv
      361 pgtlggraev lgalalvlse mgdstlldgv qspdapala
//
LOCUS       WP_457699481             364 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699481
VERSION     WP_457699481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  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 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   3  (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   4  (residues 1 to 364)
  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 364)
  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   6  (residues 1 to 364)
  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 364)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (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   9  (residues 1 to 364)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The 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 11467991
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..364
                     /product="sugar ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38699
     Region          37..349
                     /region_name="XylF"
                     /note="ABC-type xylose transport system, periplasmic
                     component [Carbohydrate transport and metabolism];
                     COG4213"
                     /db_xref="CDD:443359"
ORIGIN      
        1 mnvwtrrvvi gtaavsmals vaacgkagdg aksgggdnkt iglllpenkt tryetfdrpl
       61 meakikalcs dckvkynnaa qetetqkkqf dalitqgvkv iildavdyka tkswvnqaak
      121 kgvkvvaydr laegnisayv sydnekigrl qgealvkalg dkakdsnvvm ingsptdpnm
      181 pffkkgahsv ldkqvkkiay eqdipdwspd eankkmsaal dslgkdgfqg vysgndgmag
      241 giitalkqkg vevpvggqda elaglqrvlk gdqaftiykq ikpqadstae iavkllkgek
      301 lgsltdskvd slsgevkdip aklydaqivt kdniastilk dkvykasqic agdakkacea
      361 agik
//
LOCUS       WP_457699483             435 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699483
VERSION     WP_457699483.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..435
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44795
     Region          50..430
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtdltkqppa gedeattaap aadiaqpaav dprllvreqg fagylndfkr rvrggelgsl
       61 pviiglfvia vvfqlknssf lsadslanig vytsglgima vgivfvlllg eidlsvgsva
      121 gvgaavwavl svtngvndwl avliaiatgv vigalhgfff akigvpafvv tlagflgwsg
      181 lqiwmmgkeg sintpsgsvv enltgyyfen kaaayglalv avlayagsll ldskrrkaae
      241 lpsrplsevl lrtgvvaala fvvayvlnep agarglplal vlflavlvia dfvvrrttyg
      301 rqifavggna eaarraginv nkirisvfav sgmlaafggl fiaslsggat knlgsgntlm
      361 nviaaavigg tslfggrgki wsallgmlvi qsiqqglnll gmaseiqymi tgavllaavv
      421 idsvsrrtqk tagrt
//
LOCUS       WP_457699492             406 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699492
VERSION     WP_457699492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 406)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..406
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=43126
     Region          6..399
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mprtardvvf vdgvrtpfgk agpkgiyhet raddlvvkai rellrrnpal dpakidevai
       61 aattqigdqg ltigrtagil aglpqsvpgy sidrmcagal tavtatagsi afgaydavia
      121 ggvehmgrhp mgegvdpnpr fvseklvdqs alfmgmtaen lhdrypqitk qradeyavrs
      181 qekaakayan gkiqqdlvpi svrntnaevg etgwglvtad epmrpgttle nlaglktpfr
      241 thgrvtagna aglndgatas iiasedfare hdlpvkmrlv syafvgvepe vmgygpipat
      301 ekalakaglg iedidlfein eafavqvlaf ldhygiaddd arvnqyggai afghplassg
      361 vrlmtqlarq feeqpqvryg lttmcvgfgm gatviwenpn fdggsk
//
LOCUS       WP_457699503             398 aa            linear   BCT 27-JAN-2026
DEFINITION  thiolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699503
VERSION     WP_457699503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 398)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..398
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41438
     Region          7..398
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mtdprvrdvy ivdavrtpvg kyggalagvr pddlaahvvk alvdrtpdld pariddvcfg
       61 dangagednr nvarmavlla glpvtvpgvt vnrlcgsgle aviqaaraia hgdahiavag
      121 gvesmsrapy vlrkperafp aghqemfsst lgwrmvnprm qpewtvalge gaeqiadqhg
      181 itreqqdvfa lashqkavra wregaydaev vplpdvdllr detireassl eslsklkpvf
      241 rtaggtvtag nssplndgaa alllvdeegl ratgreplar irasavtgve pqlfglgpve
      301 avrralersg rgfddvatfe lneafaaqal gcigqwpeld pavinprgga iaighplgas
      361 garlagsvah qlaalgsgtg laalcigvgq glalvler
//
LOCUS       WP_457699508             562 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699508
VERSION     WP_457699508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..562
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60965
     Region          94..>274
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          456..534
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mralalygti gslmvtalat apaggatgaa aappapvahr iefgrcaave hlpssvecgr
       61 ltvpldyarp dgkkihltvs riratarger qgslvfnpgg pgassmefpl ygalpkwskv
      121 araydfvgya prgvgrsapl scqdpkefak tptdsrmhpd aafkrqkrae akeyargcvr
      181 ragadlpyyn sinnardldm lraalgekkl tfmgasygty fgavyatlfp ghvrrmifds
      241 vvnpsprkiw yqnnldqdva ferrwgdwls wvarhdkhyh lgttkkavqq sydkaahklr
      301 rkplngkiga gqlqsaflkt gyndafwpmr aealsgylhg dpkpliaqal prvagaaade
      361 nsnavytave cndapwprdw qtwdrdntev ariapfetwd nawmnlpcay wpgrsasata
      421 eldaavrrad hpaagqdlvd vaghaartqv ddalhgrrgp ldvhtepgal ppvlllaaer
      481 daatpyrgal elqrrlpgss lvtengagth gvafndnacv nkyaeayllh gkipghkvyc
      541 apraqpvpgq qatraqhalp gk
//
LOCUS       WP_457699514             249 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoacyl-tRNA hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699514
VERSION     WP_457699514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Das,G. and Varshney,U.
  TITLE     Peptidyl-tRNA hydrolase and its critical role in protein
            biosynthesis
  JOURNAL   Microbiology (Reading) 152 (Pt 8), 2191-2195 (2006)
   PUBMED   16849786
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..249
                     /product="aminoacyl-tRNA hydrolase"
                     /EC_number="3.1.1.29"
                     /GO_function="GO:0004045 - peptidyl-tRNA hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006412 - translation [Evidence IEA]"
                     /calculated_mol_wt=26708
     Region          160..236
                     /region_name="PTH2"
                     /note="Peptidyl-tRNA hydrolase PTH2; pfam01981"
                     /db_xref="CDD:460403"
ORIGIN      
        1 mtstetagep gnsatspfeh aetdrdaapq fvlplvvrie reappartda letaaravlv
       61 llsdersagd gewaaavrdw qdarirkvvr rarraewrra galpgitvtg heaevrvfpp
      121 vpldgwpkdl arlqvsgtel ddpqppgapa agpvlwfnpe lemsagkema qaghgaqlaw
      181 welseeeraa wraagfplsv rsagraewda ltrsglpvvr dagfteiapg sctvvadhpa
      241 lrralprtg
//
LOCUS       WP_457699525             106 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699525
VERSION     WP_457699525.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..106
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11620
     Region          28..75
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mpteeeliar aaellargpl lpppterkrl reaagltqqd vatalqtkre tvngwetgrt
       61 tprpprlaay qhllngwaer ypatddadvr rpkgddapda saprde
//
LOCUS       WP_457699537             155 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699537
VERSION     WP_457699537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..155
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16629
     Region          16..148
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 maefaiprda eltsvsltlp avlpsarqar aftakslrrw geneevieaa vlivcelttn
       61 airhgarlaa ecgrerglds viilklalep evlhievhdg stilpvqrta ghdedcgrgm
      121 liinalaesw tcgqdpeggk wvratlsrtp dalqg
//
LOCUS       WP_457699539             290 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699539
VERSION     WP_457699539.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 290)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30990
     Region          27..290
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 mtrmpraahr lpaparrrrr ksaylgllaw lcgllfflpv awmvltslhs etdaatnpps
       61 lgvsltlhgy reffgegsgi spwpplinsl tasvvstllv lalafpaaya lsikpvrkwr
      121 dvlffflstk mlplvagllp vylvaqhthl ldsiwllvll ytsmnlpiav wmmrsflaev
      181 pveileaasi dgaglaatlt riiapiampg iaatalisfi fswnellfar vltgvvagta
      241 pvfltgfvts qglflakvca aatvislpvi aagfaaqdkl vqglslgavk
//
LOCUS       WP_457699540             316 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar-binding transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699540
VERSION     WP_457699540.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..316
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33787
     Region          18..316
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mrahhtgpey lvqtaamarr fylegkskte iaeefgisrf kvartlesal hdgliqleir
       61 lpaeldagls dalrtryglr haividsqqe vpddtvqatr rlgavtadll aeivtendvl
      121 glvwgpevea vglalttlar ctvvqlcgat plrpvdatav eavrraatis rgvvypiyap
      181 lllpdataar mlreqpgivd avsrfsqvtk aivtvggwgp glstvfdals gseredyrhr
      241 gvcaevaghl ldaegciivp elterviais fdelrevpev ilmadgtera taasaalktg
      301 lfngvvtdar vaesll
//
LOCUS       WP_457699544             190 aa            linear   BCT 27-JAN-2026
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces nigrescens].
ACCESSION   WP_457699544
VERSION     WP_457699544.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Wood,C.S., Schmitz,K.R., Bessman,N.J., Setty,T.G., Ferguson,K.M.
            and Burd,C.G.
  TITLE     PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase
            signaling to retrograde Golgi trafficking
  JOURNAL   J Cell Biol 187 (7), 967-975 (2009)
   PUBMED   20026658
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="GOLPH3/VPS74 family protein"
                     /GO_component="GO:0005802 - trans-Golgi network [Evidence
                     IEA]"
                     /GO_function="GO:0070273 -
                     phosphatidylinositol-4-phosphate binding [Evidence IEA]"
                     /GO_process="GO:0034067 - protein localization to Golgi
                     apparatus [Evidence IEA]"
                     /calculated_mol_wt=20257
     Region          5..190
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 maitlaeeim llslddesgs akqrsaagwa vsggillelv larrvsvagk hlaltdttpt
       61 gdqlldsrta lietwlrgrk kgrvtewltk dqaksvgaal eslcqrgvvv eekrkalgvf
      121 pirlypeadg aveaelrerl ravvlggaep dtrtaglial ihsaklqrla fpdsprkeva
      181 armaqvaagq
//
LOCUS       WP_457699547             453 aa            linear   BCT 27-JAN-2026
DEFINITION  erythromycin esterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699547
VERSION     WP_457699547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Bazan,J.F., Macdonald,B.T. and He,X.
  TITLE     The TIKI/TraB/PrgY family: a common protease fold for cell
            signaling from bacteria to metazoa?
  JOURNAL   Dev Cell 25 (3), 225-227 (2013)
   PUBMED   23673329
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Morar,M., Pengelly,K., Koteva,K. and Wright,G.D.
  TITLE     Mechanism and diversity of the erythromycin esterase family of
            enzymes
  JOURNAL   Biochemistry 51 (8), 1740-1751 (2012)
   PUBMED   22303981
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Biskri,L. and Mazel,D.
  TITLE     Erythromycin esterase gene ere(A) is located in a functional gene
            cassette in an unusual class 2 integron
  JOURNAL   Antimicrob Agents Chemother 47 (10), 3326-3331 (2003)
   PUBMED   14506050
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Arthur,M., Brisson-Noel,A. and Courvalin,P.
  TITLE     Origin and evolution of genes specifying resistance to macrolide,
            lincosamide and streptogramin antibiotics: data and hypotheses
  JOURNAL   J Antimicrob Chemother 20 (6), 783-802 (1987)
   PUBMED   3326871
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Arthur,M., Autissier,D. and Courvalin,P.
  TITLE     Analysis of the nucleotide sequence of the ereB gene encoding the
            erythromycin esterase type II
  JOURNAL   Nucleic Acids Res 14 (12), 4987-4999 (1986)
   PUBMED   3523438
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12999453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..453
                     /product="erythromycin esterase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=50497
     Region          77..444
                     /region_name="Ere-like"
                     /note="Erythromycin esterase and succinoglycan
                     biosynthesis related proteins; cd14728"
                     /db_xref="CDD:350610"
     Site            order(90,118,293..294,320)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:350610"
ORIGIN      
        1 marhrkrisr rgllvtamva mgavlvpvav qattagtadr aggkqnpvra leqaahplrs
       61 tepgrntadl ralgsvigda kvvglgeath gshefftmke rvfrylveek gfttfalels
      121 wsaelqiddy lqtgkgdark iaeetltntp wdreefvsli ewmrdynrrh pgrtvhfmgd
      181 digapavsde ffgrvtgyvq qnhpealprl nelytglrpi ddafahmrkp laerqqlatk
      241 aqqalelvss qkgsggaafe waeqnarsia qtarfltmnp ndsdslpsfq rfrdevmaqn
      301 vtwwqqrtgq killsahndh vayaasnpev ypktqgsflr dtmgknalpi gvtfnqgsfl
      361 skdaalggdw kkftvdaaep grnehtldqv ryrdfyldvr ntpaparawl ntarptlnvg
      421 tqfpvkprdv tfakgfdvli hlhevreadk rmp
//
LOCUS       WP_457699548             261 aa            linear   BCT 27-JAN-2026
DEFINITION  polysaccharide deacetylase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699548
VERSION     WP_457699548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27551
     Region          65..>116
                     /region_name="CE4_NodB_like_6s_7s"
                     /note="Catalytic NodB homology domain of rhizobial
                     NodB-like proteins; cd10917"
                     /db_xref="CDD:213022"
ORIGIN      
        1 mivgrkkiwl gaaaslaaaa slaagilrpd rispgearsr ashtearpaa gttayggavd
       61 cgelrcialt fdagpgkdtp elldllkkeq vpatffllge nhvlkhpktv rrmatearan
      121 rrgrqrpsat rsrspaptsp naaalavpgr rhrgaivqwr gplqtwptpr gpcprrrerg
      181 gratveaara kqaddllasv vsevprpafg ggpvdaparp gvfrrtahat ggrpprrsgr
      241 veplvpghgr hgirlsasrt s
//
LOCUS       WP_457699549             415 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457699549
VERSION     WP_457699549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /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=44199
     Region          168..415
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrhvlrlspa ldpgspprpg pggrfpfatr avdalavlva afttgiagdg iallpqfdfw
       61 plnavfvslg ltwvsphewt gavilcgvlw wrrrwptava vglllaglly plllpsliav
      121 ftvavhrptr ttawvaglal vpfplhyayf vsmwfsypaf taekmlpgvl gvalvaaavg
      181 wglfvralhe rvdraetqaa rrteeaqraa reeiaremhd vlghrlslls lhagalefsp
      241 gapeaeiaht aaviresahq alqelrtvig vlraptveet ggtrpqaglg dlerlfaesr
      301 eagtdirarl evtaseqvaa ltgrtvhriv qegltnarkh apgaevrvev tggpsegvsv
      361 elsnpvpsda srtavpgggl gliglserae laggrltygr geggyhlraw lpwaa
//
LOCUS       WP_457699568             221 aa            linear   BCT 27-JAN-2026
DEFINITION  nitroreductase [Streptomyces nigrescens].
ACCESSION   WP_457699568
VERSION     WP_457699568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   de Oliveira,I.M., Henriques,J.A. and Bonatto,D.
  TITLE     In silico identification of a new group of specific bacterial and
            fungal nitroreductases-like proteins
  JOURNAL   Biochem Biophys Res Commun 355 (4), 919-925 (2007)
   PUBMED   17331467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10114820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="nitroreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24217
     Region          6..216
                     /region_name="PnbA_NfnB-like"
                     /note="nitroreductase similar to Mycobacterium smegmatis
                     NfnB; cd02136"
                     /db_xref="CDD:380313"
     Site            order(6..8,10,27,30..32,34..37,39..43,45..51,135..136,
                     138..144,147..148,151..152,154..155,159..160,168,171,173,
                     190,207..210,212,215..216)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380313"
     Site            order(10..12,14,37..41,124,145,148,165..169,191,207,209)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380313"
ORIGIN      
        1 mdvyeavdsr ravrafsdep vpkevlgrvl taatrapssg nlqpwhvyvv tgeplaelkr
       61 rataralagd pgderefpmy pdeltspyld rfsaaaaqry ealgierddp drpqkiatln
      121 seafgapvvl fcyldrtmgp gqwgdagmyl qtvmlllrae alhscpqvmw tmyrktvsrt
      181 vgaddglvlf cgisvgfeke gvprlrtgra gmtetvnfig v
//
LOCUS       WP_457699570             298 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457699570
VERSION     WP_457699570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32720
     Region          13..270
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mdrakararr apllptlvfl iivtqlpfvt tvvisflrwn alapenrgpa sfdnyravft
       61 dpalrssvwt tilltvtvvl vslllglgia llldrsfrgr gtvrtllitp flivpvaaal
      121 lwkhalfnts ygflngaltw lwslfgsdsp pqpdwmtstp laavevaliw qwtpfmmlil
      181 laglqsrpad vveaalvdga ssfdifrylt lshlrrylel aallgtifvv qnfdavftlt
      241 sgglgtanlp ytiyqtfyqa hdygrasaqg vvvllcslvv atfalrtvss llreesvr
//
LOCUS       WP_457699572             440 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699572
VERSION     WP_457699572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47797
     Region          26..423
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(139,141,267,269,302..304,345)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 malavilaaa gcyrgagdvg ntgkntinvv mvnnpqmvdl qrltaehftk etgikvnftv
       61 lpeddlrdkm sqdfssqagq ydvaslsnye tpiyarngwl telgtraakd rafdqgdilt
      121 pvrksltaad gkvyaepfyg essflmyrkd llkaagltmp arptwhqvaa maakldgirk
      181 gmkgiclrgq pgwgqliapl ttvvntfggt wftkdwqakv dspeftratr fyvdlvrkhg
      241 epgapqagyt eclndmqqar vamwydatag agslesgdsk vagkvgytla pvertavsgw
      301 lytwawglqk asthqdaawk firwassksy erlvgrelgw skvpggkras lyrdpeytks
      361 arafagpter aissarpdnp gvqprpvpgi qfvdipefad lgtktsqeis saiagkqsva
      421 aalrhsqrla aevarayagh
//
LOCUS       WP_457699582             280 aa            linear   BCT 27-JAN-2026
DEFINITION  patatin-like phospholipase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699582
VERSION     WP_457699582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28562
     Region          18..>206
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 magtalvlgg ggltgigwei gmlaglaeag idltdadvvi gtsagsivga hltsrhvple
       61 emyarqlavp earsaarmgp aalarfaaia lrsrdtvsfg vrmgklalaa rtvleaeqrt
      121 vmartlgltd wparrlvita vdaatgerta fddtsgvgll davgascavp giyppvtidg
      181 trwidggvhs tanadlasgy grvvvvapma asggpiagpr aqgerlvrgg arvcvitpdr
      241 aarsafgrdv ldpakradaa ragrrqaavh aaeirrvwsd
//
LOCUS       WP_457699584             284 aa            linear   BCT 27-JAN-2026
DEFINITION  spermidine synthase [Streptomyces nigrescens].
ACCESSION   WP_457699584
VERSION     WP_457699584.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  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 284)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..284
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29768
     Region          31..226
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mdqapepipv trtvdcgtak llpdvdrpra wlltvdgapq syvdldapth lefeyvrrla
       61 hvldeaadpg rpldalhlgg galtlpryla atrphsrqdv veadrgllal vteqlplpgn
      121 cgitvhaeda rtaleaaped sadvivadvf ggsrvpaqlt sveyaraaar vlrpdgcyaa
      181 nladsapfgf lrgqlanfat vfehlaliae psvlrgrrfg navllasrap lpvaalarrt
      241 agdafparve hgtalrrlia davpvgdaea vaspvppdga fsvg
//
LOCUS       WP_457699586             455 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457699586
VERSION     WP_457699586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45769
     Region          40..418
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(50..51,54..55,58,90,145..146,148..150,153,173,
                     176..177,180,255,258..259,262..264,267,291,295,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpgtpraptg rpapeavrhg tlpagvvvvr alppwagrny llltgatvia slgssgalia
       61 tafavlaagg satdvglvaa artiplvffl liggavadrl prhrvmvaan alscvsqglf
      121 allvlagepq lwqmallaal ggtgqaffap asegmvlasv sgdqagrafa vyrmgmngan
      181 iggaalggal vaavgpgwvl avdsaafala aalrafldvs gvperapggg mlhdlrdgwr
      241 evasrpwlwa vvvqfslvna vvsaaeavyg plvaeqhlgg pgpwglalaa fgvgtvggal
      301 lmarvrprrm lltgalcvfp lalpsaalav plpvagltai mfgtgiaiev favtwmtalh
      361 qeipeekfsr vssydwlgsl amaplatala gpvqdligrt aalwgcsavi vlltaavlcv
      421 pdvrrltrrt rtgpaagapa praagaaepd tagae
//
LOCUS       WP_457699589             216 aa            linear   BCT 27-JAN-2026
DEFINITION  DedA family protein [Streptomyces nigrescens].
ACCESSION   WP_457699589
VERSION     WP_457699589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23044
     Region          2..187
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mhiqewlesv pavsvyllvg vvigleslgi plpgeivlvs aailaatqdh inpyvlgaca
       61 tggaiigdsi gymigrkggq pllqwagrkf pkhfgpdhva maeakfdkwg mwavffgrfv
      121 allrifagpl agvlkmpywk flianvlggi vwaggttali ysvgivaesw lkrfswlglv
      181 aallfgigsf flmkhrakka aaareveesp vavtvd
//
LOCUS       WP_457699593             684 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699593
VERSION     WP_457699593.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     STAND, a class of P-loop NTPases including animal and plant
            regulators of programmed cell death: multiple, complex domain
            architectures, unusual phyletic patterns, and evolution by
            horizontal gene transfer
  JOURNAL   J Mol Biol 343 (1), 1-28 (2004)
   PUBMED   15381417
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008120
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..684
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72379
     Region          2..683
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtaraerrpl pgvvgraveh elvsglldsa plvtltggag vgksllarav leehsarhdg
       61 tilrvgcwdg ltegglleal frearaadga hrdtatalvr rtapscvgep vggragrtda
      121 ptgrapaddt aiaalaahcr rsratvlldd cdplrdecaq lvrqllradp tlrivatarg
      181 alglpeeriv eiaplpvtlg egiagpavel laartgaaap ellvavcqal egsplaiala
      241 aqqldrmslp qlaaqvgsdg plfysgpaat vrhtslyaaq aagyalcspt drrvwarlsv
      301 lpgdfdpwla gcvctscdvp aaavegaler llnasvierv reaggaqedt gaalppryrl
      361 praardfgrt qlreageesa alrrfrqaca alaaeaqiaw qgpnqqvavr lvedeqanld
      421 aaltrppqda edalgaleia vslwfhwaac gfrregrahl drllllsrdd talraralwl
      481 agylaaqehs lgaaetlldq awaaavmhad sdglariaha hgvlalyrgn taaavaclde
      541 aarhrsrdpw fgpgpahswa llavalssld aeraraaarr awetrhsdgd fwlystvlya
      601 caaiervhge psaalracrk alaakkligd plfiagarnl laglrrelrg geplpdrdee
      661 dpwwrpggpg vppqpffsrl ragp
//
LOCUS       WP_457699595             331 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699595
VERSION     WP_457699595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..331
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35898
     Region          4..323
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mkclrvraav svvalgllag cgdgrdlvda ssvprlpaha adalngqprv vpprgprssf
       61 tafrptgadg trvvttkwhg rksgytgdiw awvppqyhqa ryaksgfpvl ialpgaygyp
      121 fnywagegfa leeriaewsr qgktlpfivv mpvlnpgrty ydgsdipgqp kmgtwltedv
      181 pdfaranfrt ydsrdgwafm gsssggfaal kavlkepqkf kaavvngpdt apdsplwqgh
      241 paemrandpr hlarqlaarn glpvylafel gskeaavpdv krfirdhtgg pvhstlfeip
      301 dgvhsghtyi qrmadslhwi saqmqgpvps v
//
LOCUS       WP_457699606             253 aa            linear   BCT 27-JAN-2026
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699606
VERSION     WP_457699606.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26523
     Region          8..246
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mmhdfksllv tqegpvltvq lncpetgnai sggmldella vlgaldddsg irvlvfsgag
       61 edfclggdra efpallaedp sgvelralgn karrvcdala stdavtiarl hggvvgagvg
      121 lavfcdlrvg adtcrfrlpe lglgvppawg gimprllhev gaakirelil tadsfdaata
      181 qelsilhkav peeqldsavt qwikplvrrs psalrtaklm lnayanvnrl adatlfdael
      241 lssaltvaas trr
//
LOCUS       WP_457699602             456 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 [Streptomyces nigrescens].
ACCESSION   WP_457699602
VERSION     WP_457699602.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Manikandan,P. and Nagini,S.
  TITLE     Cytochrome P450 Structure, Function and Clinical Significance: A
            Review
  JOURNAL   Curr Drug Targets 19 (1), 38-54 (2018)
   PUBMED   28124606
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Guengerich,F.P., Waterman,M.R. and Egli,M.
  TITLE     Recent Structural Insights into Cytochrome P450 Function
  JOURNAL   Trends Pharmacol Sci 37 (8), 625-640 (2016)
   PUBMED   27267697
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Pochapsky,T.C., Kazanis,S. and Dang,M.
  TITLE     Conformational plasticity and structure/function relationships in
            cytochromes P450
  JOURNAL   Antioxid Redox Signal 13 (8), 1273-1296 (2010)
   PUBMED   20446763
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   5  (residues 1 to 456)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Degtyarenko,K.N. and Archakov,A.I.
  TITLE     Molecular evolution of P450 superfamily and P450-containing
            monooxygenase systems
  JOURNAL   FEBS Lett 332 (1-2), 1-8 (1993)
   PUBMED   8405421
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Nelson,D.R., Kamataki,T., Waxman,D.J., Guengerich,F.P.,
            Estabrook,R.W., Feyereisen,R., Gonzalez,F.J., Coon,M.J.,
            Gunsalus,I.C., Gotoh,O. et al.
  TITLE     The P450 superfamily: update on new sequences, gene mapping,
            accession numbers, early trivial names of enzymes, and nomenclature
  JOURNAL   DNA Cell Biol 12 (1), 1-51 (1993)
   PUBMED   7678494
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15334917
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..456
                     /product="cytochrome P450"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=49477
     Region          45..409
                     /region_name="CYP_unk"
                     /note="unknown subfamily of actinobacterial cytochrome
                     P450s; cd20623"
                     /db_xref="CDD:410716"
     Site            order(116,120,127,171,246..247,250..251,254..255,258,292,
                     302,304,327,350..352,356..360,363..364)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410716"
     Site            order(192..193,246,249..250,254,300..303)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410716"
ORIGIN      
        1 mqshsefqsp ppgcpahagg eraplhgpef aaapdafydm lrqygpsapv elapgveael
       61 vteyatalhv lqnpdtfard srrwralneg rvpldspvlp mmmyrpncmf sdgaehlrlr
      121 qavtdsfgrl dmhrvsrhvd rvaayltdqf smrgkadlis dyaqllpllv fndlfgcpae
      181 igdrlisais nlfdgvdaer anevmagalf elvtlkrgtp geditswlmq hpsrlsdeem
      241 vhqlalliga gtepvqnlia nalrlllsde qfaggpqggg dllvedaine vlwnsppian
      301 yathypvqdv elsgnklaag tpllvsfaaa ntdpslsasr qtfskrahla wgagphacpa
      361 kdpallisir aiekllntlp dielgvpadt ltwrpgpfhr alnvlparft pvrserrgpq
      421 saaaggpggg dtrgreqqsk pqkgswwsgf lswwrv
//
LOCUS       WP_457699608             179 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma carbonic anhydrase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699608
VERSION     WP_457699608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..179
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18335
     Region          7..173
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 maepalispv ggkepkvdqk aftaptsvvl gevtmgpgas vwyqavlrad cgpivlgads
       61 niqdnctvhv dpgfpvtvge rvsvghnavl hgctveddvl igmgatvlng ahigagslva
      121 aqalvpqgmq vppgslvagv pakvkreltd eeretiklna vmylelvaqh reavtaaee
//
LOCUS       WP_457699610             248 aa            linear   BCT 27-JAN-2026
DEFINITION  acyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699610
VERSION     WP_457699610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..248
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=26429
     Region          62..207
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mfssvaawrr ravsrvvhrg arwvreaaav taerpgpyrf rrigtgtrla fpqgtvfgdp
       61 wielgdhcii aqdvtmtagm mpdldlgaep iltlgngvvl grgshviadv rltigddcff
      121 gpgvyvtttn hsyddpevpv gkqwprsdpv aigpgswigt gavilpgarl grnvvvaaga
      181 vvrgevpdha vvagapariv rrwdprqgwq pplrtpapvp ipegvtpeql valeawqaee
      241 ageayets
//
LOCUS       WP_457699614             190 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699614
VERSION     WP_457699614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rosinski,J.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 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20379
     Region          5..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          80..180
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mtdldqltqs larnlkhwra ergftldala aragvsrgmi iqieqartnp svgttvkiad
       61 algvsittll dyeqgpqvri vapeeavrlw stdagsfttl lvgaeapgpy elwdwrlmpg
      121 dnsssdphpp gtvellhvra gtltlvvdge ehevpagssa tfeakvahgy rndgtepvem
      181 tmsviippvr
//
LOCUS       WP_457699631             150 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457699631
VERSION     WP_457699631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 150)
  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 150)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /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=15621
     Region          <21..141
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlksasdggg pslgpqptlv dldrlldqsr aagvsveryd egtpqrlptl lehaayrvvq
       61 ealtnvhkha gtahadvvvr ylasdlevvv sntapsapae slpgsgtglv glrervelld
      121 gvfeaqprhg ggftvsarlp lslpaleera
//
LOCUS       WP_457699628             503 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457699628
VERSION     WP_457699628.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..503
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54415
     Region          6..455
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpelldermg fvrriglfqa tainmsqmcg igpfvtiplm vaafggpqav tgflagavla
       61 ladgliwael gaslpgaggs yvylrqafqy rtgklmpflf vwtamlfipl gmstgvigfv
      121 qylgylwpdm tpgqgdfvgi avtvgivvll wrrveniakl tvvlwtvmit svllvivaaf
      181 thfsperaft ypahafelta shfwtgfaag ltigiydylg yntiaymgae irepgrtipr
      241 aiitailgim tiylllqigt lgivnwqdml dphstasssv asavlekawg kgaadtvtvl
      301 ilitavasvf tgllggsrvp ydaarervff rpygtlhprh rfpvlglltm gavmaggfli
      361 grhtdlatii qllttvmviv qalaqvaavt vlrrrqpglh rpyrmwlypl psivaligwl
      421 viygyadrna pgrhpiewsl awvgagvvaf lawaryerew pfgpkritee ylhssdpadk
      481 graggegrek gpggtvvgat dpg
//
LOCUS       WP_457699635             388 aa            linear   BCT 27-JAN-2026
DEFINITION  exonuclease SbcCD subunit D [Streptomyces nigrescens].
ACCESSION   WP_457699635
VERSION     WP_457699635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=41989
     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 lgrsfhrvnl lsaqrafldh lvetvrarei davlvagdvy dravpplaav
       61 elfddalhrl aglgvptvmi sgnhdsarrl gvgsglmera gihlrtdpad cgtpvllada
      121 hgpvalyglp ylepamvrdt lgarradhae vlgaamgrvr adlagrpagt rsvvlahafv
      181 tggavsdser ditvggvasv pvavfdgvdy aalghlhgcq tltervrysg splaysfsea
      241 dhrksswiid ldadgavhae rvdcpvprpl arirgrlvql ledpeaarhe dswveatltd
      301 tarphepmar lvkrfphlvs lvfdpddgpt rslasyaqrl rgrsdqeiae dfvehvrsgr
      361 gaddqerael rsaidevrvd dmaaevar
//
LOCUS       WP_457699639             148 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699639
VERSION     WP_457699639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..148
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16017
     Region          7..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtgyspdatd wrildvlqhn gragyaelar avnmsasavt ervrrleeag visgyaavid
       61 periglpvla fvrlqyphgn dkpfhdllet tpeileahhv tgddcfvikv aarsmkhlee
      121 vsgrigalga vttsvvyssp larrpvsr
//
LOCUS       WP_457699640             272 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699640
VERSION     WP_457699640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Keller,L.M. and Weber-Ban,E.
  TITLE     An emerging class of nucleic acid-sensing regulators in bacteria:
            WYL domain-containing proteins
  JOURNAL   Curr Opin Microbiol 74, 102296 (2023)
   PUBMED   37027901
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Makarova,K.S., Anantharaman,V., Grishin,N.V., Koonin,E.V. and
            Aravind,L.
  TITLE     CARF and WYL domains: ligand-binding regulators of prokaryotic
            defense systems
  JOURNAL   Front Genet 5, 102 (2014)
   PUBMED   24817877
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /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=29855
     Region          17..>239
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mdldptirtl tlltllqsgg ewtaadlaer lgtsvrtvrr daqrlrrlgy tvearpgpgs
       61 ayrlrpgvkv ppllftadei talvaglhli rawlpedava ssallkldqv lprplrrraa
      121 atdlatevlq qpgavvaaat vgviadavae dgrlrfrytd qhgrpstrlv epyrhflrag
      181 hwylvafdvd rddwrtfrld ritdispvag tyrphefpdv sierwlttdf gratarsprs
      241 aaaepdigge gepggevrgg tgpsredhrh pp
//
LOCUS       WP_457699647              65 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699647
VERSION     WP_457699647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..65
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7536
     Region          3..54
                     /region_name="HTH_33"
                     /note="Winged helix-turn helix; pfam13592"
                     /db_xref="CDD:433335"
ORIGIN      
        1 mdlervgavv ervtgvslsr asvwrlltgr lgwslqrper raverdesei arwithewpr
       61 ikrgr
//
LOCUS       WP_457699653             377 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457699653
VERSION     WP_457699653.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..377
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39850
     Region          <14..365
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mrvlpvwsrv rrwvpalvia laalvdlltp tsvssaplla vapvtavslf gpvgivgvgl
       61 tamvvqagla fvagsydwqg daavqitlas vtalavglnr slrmqhasas raryaaevaq
      121 ravlpsppsr lgdlriaary vpaedmalig gdlyvmqetp fgvramvgdv rgkglsavta
      181 vsvdigvfry aadhepdlpa lvgcmeeall resqrregld ategfttali vqfaddlsqv
      241 hivnrghpap vllhadgrar vlepeeaapp lgitglgawp spvetypfpp gamllcftdg
      301 vteardpagv fydpadrvph mvqsylrqts hfpdpstvld llardvsrhs ggapqddqal
      361 lalhrplpqq dllartg
//
LOCUS       WP_457699655             224 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699655
VERSION     WP_457699655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..224
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23749
     Region          7..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mavhshaelt avavgladqg glsavsmrqv akglgtgqas lyryvsgrdd lldlmtdavt
       61 geidldiplh gdpvedlval aarakavhlr hpwlpdvppe plrlgprsmd fleyalrama
      121 pvrlpgrtkm eivalmsalv aqfaraeiqg grattdrqaa qaaylsktas qgdhpyveaa
      181 madhtgsgad pvadpqllfe rtmhrvltgl vlvditaade etet
//
LOCUS       WP_457699660             184 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699660
VERSION     WP_457699660.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20162
     Region          7..176
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 meqpaeilrs dqvelrrwrg qdievldrli tesrdhllpw mpfaashdrk qgeaflsrce
       61 eewaseeayh yaittggvav gscslmrrig pggldigywl hqtwvgkgla tmasaalvea
      121 grrmpgidri eihhdeanpa sgavarrlgf tevgrvqvpd gpaapgetgv dviwrlqtrp
      181 spsa
//
LOCUS       WP_457699659             198 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699659
VERSION     WP_457699659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21262
     Region          17..165
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mttddtgavp rsaeasirqe hsddhpavra lhlaafegde hvpaladalr raeapltpms
       61 fvatvegqvv ghvllsagrl daprrivdvl vlsplgvlpe fqnqgigtrl iehalaaada
      121 hhtplvfleg spryyakrgf eradtmgfrs pslripppaf qvarlaahep wmtgtlvysd
      181 tfwaldcvgl rdteastg
//
LOCUS       WP_457699672             424 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457699672
VERSION     WP_457699672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41887
     Region          9..416
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 magsvgsvgp gelqrrlgvt davviglgsm igagvfaala paaaaagsgl lvglalaavv
       61 afcnatssar laarypasgg tyvygrerlg dfwgylagwg fivgktasca amaltvgsyv
      121 wpgqahavav aavvaltavn yagvqksawl traivavvla vlaavvcaal tsgqadavrl
      181 digddasltg vlqaagllff afagyariat lgeevrdpgr tipravplal gitlvvyaav
      241 avaalvvlgp rqlaeatapl sdavraagad glvpvvraga avaalgslla lilgvsrttl
      301 amardrhlph alaavhpkfk vphraelvvg avvavlaata dvrgaigfss fgvlayyaia
      361 naaawtlapt eggppriipv aglagclvla falpltsvis gaavlvggav aygvrrtlsa
      421 rrap
//
LOCUS       WP_457699693             165 aa            linear   BCT 27-JAN-2026
DEFINITION  peptidylprolyl isomerase [Streptomyces nigrescens].
ACCESSION   WP_457699693
VERSION     WP_457699693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Ke,H. and Huai,Q.
  TITLE     Crystal structures of cyclophilin and its partners
  JOURNAL   Front Biosci 9, 2285-2296 (2004)
   PUBMED   15353287
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..165
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=17573
     Region          5..161
                     /region_name="cyclophilin_ABH_like"
                     /note="Cyclophilin A, B and H-like cyclophilin-type
                     peptidylprolyl cis- trans isomerase (PPIase) domain. This
                     family represents the archetypal cystolic cyclophilin
                     similar to human cyclophilins A, B and H. PPIase is an
                     enzyme which accelerates protein folding...; cd01926"
                     /db_xref="CDD:238907"
     Site            order(53..54,59,110,112,120)
                     /site_type="active"
                     /db_xref="CDD:238907"
ORIGIN      
        1 msndvyfdit ingdpagriv ftlfddvvpk taqnfrelat grhgfgyegs gfhrvipdfm
       61 lqggdftagn gtggksiyge kfadenfkik htkpgqlsma nagpntngsq ffittivtdw
      121 ldnkhvvfge vvegmelvrk ieslgshgga tkadiviaks gviga
//
LOCUS       WP_457699697             274 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457699697
VERSION     WP_457699697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30108
     Region          17..251
                     /region_name="F420_Rv2161c"
                     /note="probable F420-dependent oxidoreductase, Rv2161c
                     family; TIGR03619"
                     /db_xref="CDD:274680"
ORIGIN      
        1 mkfgvstfit dqgiapaalg raveerglds lliaehthip vdrrspypgg gelpeiyyrt
       61 ldpfvalsaa aavterillg tgialvaqrd pvitakevas ldlvsggrav fgigvgwnre
      121 emanhgtdpr trgrlvderl ramrelwtre kaefhgefvd fdpvyswpkp vqrphppiyv
      181 gggeaafdrv aalgdawlan slppqelgpk idrlrsiagr svpvtvyava depeiieqyt
      241 qldverllfy lptlpepetl syldrlsdva arfr
//
LOCUS       WP_457699699             293 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699699
VERSION     WP_457699699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..293
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32577
     Region          92..203
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mgasrselks lrstkytssa rteggverlr algyrsglra ldladrvlgr drkmvpprry
       61 rrfigngdfa kvgasithym reelgllpsh dvldagcgvg riavpltsyl tegsylgfdi
      121 vphaidwchs aitsrhpnfr fshvdikqei ynpegtltsa dfrfpadgqa fdmvalvgli
      181 shllpeevdn yvaesarvlr pggkcfatay lvddmvaerv regrtaftft hsrgthfihs
      241 eqeptyaiay rldhiqevaa rhglrlerep qlgtwsssta rpasmdllvl ert
//
LOCUS       WP_457699702             328 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457699702
VERSION     WP_457699702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34627
     Region          6..320
                     /region_name="oxido_grp_1"
                     /note="luciferase family oxidoreductase, group 1;
                     TIGR03558"
                     /db_xref="CDD:274646"
ORIGIN      
        1 mldiplsale vamvqtgara vdtlrdtaaf aqglellgyh riwyaehhhs paigafppvv
       61 ltthaaasts airlgsggvl apnhapitla eqfgtlaalh pdridlgigr gpgtfdeaia
      121 ralrrgaapa tdaeyerdva ailaflvdev algplpepwl lasstagaal aaglglpiav
      181 ahhirpdntq avleryraaf tpsrwceqpr vlvcvetvca eseeeaarrv gpmdvvkagl
      241 lkglseipfp tpadaaahhf taeerkalag fraqqavgtp etvvhrltql ageagadelm
      301 lttpvydlgd rirsyelikk yseattal
//
LOCUS       WP_457699709             167 aa            linear   BCT 27-JAN-2026
DEFINITION  MogA/MoaB family molybdenum cofactor biosynthesis protein
            [Streptomyces nigrescens].
ACCESSION   WP_457699709
VERSION     WP_457699709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Kanaujia,S.P., Jeyakanthan,J., Shinkai,A., Kuramitsu,S.,
            Yokoyama,S. and Sekar,K.
  TITLE     Crystal structures, dynamics and functional implications of
            molybdenum-cofactor biosynthesis protein MogA from two thermophilic
            organisms
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 1), 2-16
            (2011)
   PUBMED   21206014
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Bevers,L.E., Hagedoorn,P.L., Santamaria-Araujo,J.A., Magalon,A.,
            Hagen,W.R. and Schwarz,G.
  TITLE     Function of MoaB proteins in the biosynthesis of the molybdenum and
            tungsten cofactors
  JOURNAL   Biochemistry 47 (3), 949-956 (2008)
   PUBMED   18154309
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Schwarz,G.
  TITLE     Molybdenum cofactor biosynthesis and deficiency
  JOURNAL   Cell Mol Life Sci 62 (23), 2792-2810 (2005)
   PUBMED   16261263
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="MogA/MoaB family molybdenum cofactor
                     biosynthesis protein"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16495
     Region          1..161
                     /region_name="MoaB"
                     /note="Molybdopterin biosynthesis enzyme MoaB/MogA
                     [Coenzyme transport and metabolism]; COG0521"
                     /db_xref="CDD:440287"
ORIGIN      
        1 mtparalvvt ashraaagvy adkggpllae glaamgfevd gpqvvpdgep veaalrgavs
       61 aaryaviltt ggtglsptdr tpeatrrvld yevpgipeai raagrakvpt aalsrglagv
      121 agttlivnlp gssggvrdgl avladllpha vdqirggdhp rpagsps
//
LOCUS       WP_457699711             204 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699711
VERSION     WP_457699711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..204
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23236
     Region          1..182
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mvltdgevtl rpirvrdqra wrevnrrnrd wlrpweatip ppppglapph rptyrqmvrh
       61 lraeahagrm lpfvveyrgr lvgqltvagi twgsmcsghv gywvdqevag rgviptaval
      121 avdhcfrsvg lhrieicirp entpsrrvve klgfreegir prylhidgaw rdhavyalta
      181 eevpegllnr wrrgkprtpg aphk
//
LOCUS       WP_457699715             195 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699715
VERSION     WP_457699715.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20429
     Region          5..47
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          61..>142
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mdhkilqttr elidevgypa ltvdqvatra gvgkaaiyrr yaskaemafv atvheqqlpp
       61 pagtgslhgd llalvrtfhv rmaapaarql apaliselag npeldtrfqd tflateqaaf
      121 aeiieqavar gelagpvdpa mahllllgsl asalyilnlp vddamvtdla aattagital
      181 anrhhstpdg aaeph
//
LOCUS       WP_457699718             206 aa            linear   BCT 27-JAN-2026
DEFINITION  M23 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457699718
VERSION     WP_457699718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..206
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22744
     Region          <29..170
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mttfrkstpl rrmlllaiap talgcvltla asqvavaapa gnwshptkar hrisspygvr
       61 gtwqaghhtg idlavragtk vrsvgsgtvv lakrsgaygk avtirmndgr ytlfghlsri
      121 tvrpgqkvra rtrlgysgat gratgphlhf evrtsrrygt dinpltylak hgirltphts
      181 aaprhrhrhh hkhphrhhrh hhrhhh
//
LOCUS       WP_457699720             425 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699720
VERSION     WP_457699720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  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 425)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..425
                     /product="glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=44439
     Region          3..397
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(13..14,16,166,169..170,174,205,262,327,329,331..332,
                     335)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(13,262,327,329,331..332)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            14
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
ORIGIN      
        1 mtnilitaag sygdiapytg vgarlraagh evtlathdsy aplvraagle frrlpadprt
       61 rrtdtadaae qarptapggk rdlmrqataf ikelgggiad aaredtglll lsattaplgh
      121 hlaeargips ldlplvpgap tgdfapvvsg grslgrwgnr aagrlslrii nrlyadasre
      181 mrarlglppa tprtvrrrae aagrpvlygf sevlvprptd wrtgldvvgn wwpwyapddr
      241 lppvvedfla agpppvyigf gsmaggeger lstlaaaalr rakvrgilqs gwaglttrht
      301 sadadlltig evphallfpr msavvhhcga gtaaagvrag vptipvpvta dqpfwaarla
      361 slgvatapip fkdlstdhav drlahaltqa taaparrdha taaahrlaae dgagevlkav
      421 erlva
//
LOCUS       WP_457699722             262 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699722
VERSION     WP_457699722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29314
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          132..251
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 msysvgqvsg fagitvrtlh hydqtgllsp sdrspagyrl ysdadlarlq qilfyrelgf
       61 pldeiatile dpqanaldql rarhrllndq isklqrlvev aehamevqqt gveltpeerf
      121 evfgevafdl tyatqahlkw qhheghqrsm araaahsked wakimaetad wrlrllaafd
      181 agepadgtpa mdlaeehrqh iarwftpcpt dmhgriaddf atdprafalv vppteqrpgl
      241 apylrtavha navrqsppph eg
//
LOCUS       WP_457699727             309 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699727
VERSION     WP_457699727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..309
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33490
     Region          9..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdpspwaie aeglgkryrr gwalrdcsfr lpaghicalv gpngagkstf lgtatrlvqp
       61 ttgtlklfgv pvsdpavlar vsflaqdkpl yprftvaetl rlgrelnprw dqelaerivr
      121 sgkvplsari gtlsggqrtr vafalafgkr pelllldepm sdldplarhe msgllmaeaa
      181 ehgttvlmss hmlsemevmc dyllvlaegr lrmagqtedl ipahllvtgv aegddgvpee
      241 lrrqhtvves rvtgrqfsam irtggplsds wevlspsmee vllaylrspd aptliadesr
      301 vdgpreaaa
//
LOCUS       WP_457699729             160 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699729
VERSION     WP_457699729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17715
     Region          1..144
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 meirpvrydh pdavaldelv qqeyarrygd gdmtpldpem ftpphgayli aydgarplat
       61 ggwrrqedaa egytvgdaei krmfvvpear grglarrila aletdartag rsrmvletgi
      121 kqpealelya scgyvlvekf glyrtyddsr cmakplaaeg
//
LOCUS       WP_457699743             268 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457699743
VERSION     WP_457699743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 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   4  (residues 1 to 268)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29809
     Region          22..248
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(24..26,40,56..58)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(70,73,77..78,87,108,112,118,122,125..126)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 maanentqde qtdpadhrra refrmadlar eagitvrtlr fyrerklipp prregriawy
       61 nehhlarlrt igallerght lggiaellsa fdtgrdvgel lglenalvpp wseetpvrlt
      121 peeladhfse ditaenlsts ldigylavdg defvhisrrl ldastelvnq giplaavlea
      181 grqvrahada ladvfttlir thllsdvlar lsacedvgph evdhitetie klrplskgvv
      241 eaelsmamdr rvraevakwl peegregk
//
LOCUS       WP_457699744             509 aa            linear   BCT 27-JAN-2026
DEFINITION  flavin-containing monooxygenase [Streptomyces nigrescens].
ACCESSION   WP_457699744
VERSION     WP_457699744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Paul,C.E., Eggerichs,D., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.H.
  TITLE     Flavoprotein monooxygenases: Versatile biocatalysts
  JOURNAL   Biotechnol Adv 51, 107712 (2021)
   PUBMED   33588053
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Torres Pazmino,D.E., Dudek,H.M. and Fraaije,M.W.
  TITLE     Baeyer-Villiger monooxygenases: recent advances and future
            challenges
  JOURNAL   Curr Opin Chem Biol 14 (2), 138-144 (2010)
   PUBMED   20015679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..509
                     /product="flavin-containing monooxygenase"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016709 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen, NAD(P)H as one donor, and incorporation
                     of one atom of oxygen [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55655
     Region          7..446
                     /region_name="CzcO"
                     /note="Predicted flavoprotein CzcO associated with the
                     cation diffusion facilitator CzcD [Inorganic ion transport
                     and metabolism]; COG2072"
                     /db_xref="CDD:441675"
ORIGIN      
        1 maererrhvr vavigsgfgg lgaavrlrrq gitdfvvleq adavggtwrd nsypgcacdv
       61 pshlysfsfa pnpewprsfs gqphirayle rvtdtfglrp hlrfnsevrs lrwngealhw
      121 evetasgplt advvvsatgp lsdpkvpgip gldtfpgkvs hsarwdhdyd lrgkrvamig
      181 tgasaiqivp aiqpdverlt lfqrtppwvl pradrkisaa ekwlhsklpa traarrgllw
      241 giremqvsaf tkrpnelgli eflarnhmkr aikdpglraa ltpdyrigck rillsntyyp
      301 alaqpnvdlv aggltevrgs tlvgsdgsev eadaivfgtg fhvtdmpiah rvtgahgttl
      361 aeewkdgmea lrgasaagfp nfltligpnt glgnssmilm ieaqlnylad fmrqldvlgg
      421 kialaarpsa vqdwnrriqq rmtrtvwnng gcdswyldan grnttvwpgt taefkkvtrq
      481 vdlaeyevlr ppgtepagrs tgeraevaa
//
LOCUS       WP_457699755             378 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter permease [Streptomyces
            nigrescens].
ACCESSION   WP_457699755
VERSION     WP_457699755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Rempel,S., Stanek,W.K. and Slotboom,D.J.
  TITLE     ECF-Type ATP-Binding Cassette Transporters
  JOURNAL   Annu Rev Biochem 88, 551-576 (2019)
   PUBMED   30485755
REFERENCE   2  (residues 1 to 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   3  (residues 1 to 378)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18403195
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="energy-coupling factor ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37430
     Region          1..215
                     /region_name="CbiM"
                     /note="ABC-type Co2+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG0310"
                     /db_xref="CDD:440079"
     Region          267..350
                     /region_name="PDGLE"
                     /note="PDGLE domain; pfam13190"
                     /db_xref="CDD:463803"
ORIGIN      
        1 mhvpdgfina pvsaatgvva avavavslrg arrelagaag qagaaaaert aplaglvaaf
       61 ifavqmlnfp vaagtsghll ggalaailvg pytgvlcvsv vllmqgvlfa dggltalgvn
      121 itdmaivttv vayalfrglv kvlprrrssi tvasfvaall svpaaavaft alyalggtad
      181 vpidkvftam vgvhlligig eaaitaltvg aviavrpdlv ygargltkpl elrtsplaap
      241 adepapeaap apvpaaaapa parrsvrrvw laglaaalvc aggisyyasa spdglekvaq
      301 dhgidakaed haakdsplad ysvkditdpr lsgglagvig vgatlavgtg vfvvvrrrrs
      361 aataerpdag agrpsesv
//
LOCUS       WP_457699759             257 aa            linear   BCT 27-JAN-2026
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Streptomyces nigrescens].
ACCESSION   WP_457699759
VERSION     WP_457699759.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27421
     Region          13..238
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mdplstatpa pslavsrlay aypdghqalf gvdltvgrge rvallgpnga gkttlvlhln
       61 gileagagtv avaglpvare nlaeirrrvg ivfqdpddql fmptvredva fgpasaglrg
      121 aaldervtea ltrvgmaefa drpphhlsfg qrrrvavatv lamrpeilvl depssnldpa
      181 srreladilr sldvtvlmvt hdlpyalelc prsvvlsggv lvadgttqel lcdeelmrth
      241 rlelpfgfdp rsvdvpl
//
LOCUS       WP_457699760             408 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699760
VERSION     WP_457699760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42614
     Region          39..403
                     /region_name="Beta-lactamase"
                     /note="pfam00144"
                     /db_xref="CDD:395092"
ORIGIN      
        1 mdgsrqrrmn gkresvvdvq gtvedgfepv rdafmanfar rgergaavav yrhgrkvvdl
       61 wggtkdgdad gdaaapweag taqvirsatk giaalvplll hqrgqldlda pvgtywpefk
      121 aagkervlvr hllshraglp aldtpltpdl aidgvsgpaa laaqapawep gtdhgyhaqt
      181 yswllgelvl rvtgrtigsw iadeiagplg ldlwiglpee aqsrvgrlaa vetpappaas
      241 glrvrpkqsv adaytdpgsl tsrafaaisp apdenapeyr aaelpasagv atarslarcy
      301 aaligpvddh srlfapatlt larteesagl drtllvhtrf glgfmlhgpa spllapgafg
      361 hpgrggalac adpesglafg yvtngmqrnv tadaraqall ravshvag
//
LOCUS       WP_457699762            1112 aa            linear   BCT 27-JAN-2026
DEFINITION  S41 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457699762
VERSION     WP_457699762.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   4  (residues 1 to 1112)
  AUTHORS   Brandstetter,H., Kim,J.S., Groll,M. and Huber,R.
  TITLE     Crystal structure of the tricorn protease reveals a protein
            disassembly line
  JOURNAL   Nature 414 (6862), 466-470 (2001)
   PUBMED   11719810
REFERENCE   5  (residues 1 to 1112)
  AUTHORS   Pallen,M.J., Lam,A.C. and Loman,N.
  TITLE     Tricorn-like proteases in bacteria
  JOURNAL   Trends Microbiol 9 (11), 518-521 (2001)
   PUBMED   11825690
REFERENCE   6  (residues 1 to 1112)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   7  (residues 1 to 1112)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18792775
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1112
                     /product="S41 family peptidase"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=120267
     Region          12..1086
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mparpdppgg sylrfphlhg dllcfaaedd lwiapiapdg eepgrawrlt vdrtrvghpr
       61 fspdgqqiaf ttwrsldpev hlapveggpa rrltywgstd arvcgwtppd heghshilav
      121 sshgqpfsyy swayslptdg spggqlpwgp vsdiavadia gehrtlllsg kpphepaswk
      181 ryrggamgrm wlhgtrllpd lrghldsvmf vdgrvaflsd hegianvysc lpdstdlrrh
      241 sdhgdfyarh astdgerivy qcagdlwlid dlapdavprk lavrlggpra grrsyqvpaa
      301 shvtalavdt tgrasavgvr gslywlthrd gpartihdvp gvrvrlpeml gasgriayvt
      361 daegadaiei tnlprasapg eprrlaagel grvhemtaap dgerlavaan dgrlllvdva
      421 rpeegaseee tasggvteli rstngpvrdl afspdsrwlt wshpgigrsl rqikmarlad
      481 rhivdvtngr fedeqpvftr dgrylaflsw rgfdpvydvh tgdlsfplgc rpylvplssa
      541 tpspfalspe grpaaggldp devpppageg pllvevegle nrvtpfpvaa skysslepvs
      601 ggglvwlrwp isgalgetfa npaetsgrpt lehfdltkar rteltssldg falsgdgsrl
      661 vvndegelra vpateqpdsd stvfldlrri lhdvdpvaew hqafeeagri trayfwepqm
      721 cgidwdavla qyrplldrva spdefadllr evmgelgtsh ayvtgarrne gpphyqramg
      781 llganlvcrd ghwvvtrilp gessdskars plagtgireg aalthvdgrp vdpvtgpypl
      841 laaaggttve ltfsppedeg parrvavvpl iderplryqd wvakrravvr elssgrcgyl
      901 hipdmggsgw aqfnrdlrme vsrpalivdv rgnaggnise lviekltrti mgwdltrdae
      961 pvsytsnapr gpvvavadem tssdgdmita afklqglgpv vgmrtwggvv gmtgrhrlad
     1021 gtaitvpmna awfrlygwgv enhgvevdie alrsplhwae grhpqlgvai rtalellerh
     1081 paatppdlsd vpdlrrpplp prsggaaaaa ga
//
LOCUS       WP_457699764             539 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457699764
VERSION     WP_457699764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..539
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56287
     Region          31..516
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,82,132..133,135..137,140,160,
                     163..164,167,292,295..296,299..301,304,332,336,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 matsptapgt pparqipdri hrrrwailst lmlsllivvl dnsilnvamk tiatpapvgl
       61 gatqselewa insytlvfag llftagllgd rvgrkkvllf glavfgagsv lagvsgspte
      121 lvvfravmgl ggafvmpatl ailmnvferd eqpraigiwa ggvgiaiavg piaggllldh
      181 fwwgsvfmin apivlfslva mvvlvpdskd phpgrmdpfg vllsvvglvl lvygiikggq
      241 ladftdpqvv gtvvgglvvl tvfvlhqkrs dhpsidisyf rtpafsaaia aialvffalm
      301 gvsffavfyi qsvrgysplq agllflplaa aqmlfaprar lavdrygsra vctfsmfvva
      361 dtmlgllllt edtpiwilea llflqgagma himppatvav mqslprekag sgsalnnvfr
      421 qvggtlgvav lgsllstsyr dgiqdhldav pglpaatrha agesieatlg ladrmgpagr
      481 plaaaaddaf ihamhitalg saavallgal vsvlflpgkm gpvpqaaepq eerkagvqr
//
LOCUS       WP_457699766             219 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699766
VERSION     WP_457699766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23264
     Region          37..84
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          94..207
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 msraaedpeg aaaegrpgpa apagrgrprs aaadsaiiea vlrliedgvs igelsmeria
       61 reagvgkatv yrrwsgksal mldvmrsldv pspppaglsv rddlvsllef lrrrglakrs
      121 sallrtvvsh vqaqpelwae yhdtvvrarr eallavlrrg vasgeirgdr dletladlfv
      181 gpmlarallh ewkelpegls adivdtvleg vrpaagtag
//
LOCUS       WP_457699778             415 aa            linear   BCT 27-JAN-2026
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces nigrescens].
ACCESSION   WP_457699778
VERSION     WP_457699778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46453
     Region          82..407
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maghiqdrwy ktetdpngkt trvktsrhgi gmryraryig pdgteksksf pdgkkrlaek
       61 wltkieadmd sgryvdprag qttfrqyaek wlqsqttdpt trepvavqir rhaipylgsr
      121 plgsfkpehi rewlselera lpassyrrvi fasvsavfta avddeylhrn pcqassvrap
      181 apnsarvvpw trqrtfavrt alpqeyramv dlgagcglrq geifglstda igfdtgwlhv
      241 alqvkvsngk lvfarpkrdk erdvplsdrv ahtlkhhmea hppvsvtlpw lrpdgplltk
      301 rllftrtngd gavrrtdfnt rvwkpalvka gvlpepepgk rhssaredgm halrhfyasv
      361 lldagenika lstylghtdp gftlrvythl lpssdgrtrn avdslypavk hgsgr
//
LOCUS       WP_457699780              82 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699780
VERSION     WP_457699780.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..82
                     /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=9138
     Region          20..74
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msrtsfaqsd pratlrdglp dryltpedlv tlfglesvet vytwrkkrtg ptgfrvgkhi
       61 rydpadvraw viqqtaaeae aa
//
LOCUS       WP_457699802             221 aa            linear   BCT 27-JAN-2026
DEFINITION  GGDEF domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457699802
VERSION     WP_457699802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=23717
     Region          33..185
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(65,109)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(70,73..74,78,82,105,107..110)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(101,129)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 msqtlvalaa alpvaagwsl hslmlrrrie tarrdplsgl wtrepfeera rktlglrpga
       61 vmvldldgfk qindtyghav gdaviavtgr rlarwstfyg gvagrlggde faasiccysp
      121 qglrqamddl aeqlrapvef eghvlwvgfs agvvraqrgc cpaelprlmr cadevmygak
      181 qtgggwmlga dnaapayrtv ngrrdgrrgt sadhsleggs l
//
LOCUS       WP_457699806             256 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699806
VERSION     WP_457699806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   McLaughlin,M., Fiebig,A. and Crosson,S.
  TITLE     XRE transcription factors conserved in Caulobacter and phiCbK
            modulate adhesin development and phage production
  JOURNAL   PLoS Genet 19 (11), e1011048 (2023)
   PUBMED   37972151
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..256
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28537
     Region          4..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 manerlrgai vesgltleqv aarlgvspkt verwiaepnr kpyrrfqyav asmlrrevsy
       61 lwpdertsde vtassdsevl klyphrsvvp qdawaklyad atmhfdvlvy sgfwltedpr
      121 fhrlvreksa agvpvrfmmg dpnspvvavr gddegigsam aakirnalln yaplfrlsgv
      181 efrlhattly nsiyradnel langhvygvg aymapvlhlq rvpggelfdt yaesvervwe
      241 sarpissptd yeggat
//
LOCUS       WP_457699810             189 aa            linear   BCT 27-JAN-2026
DEFINITION  HD domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457699810
VERSION     WP_457699810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..189
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20773
     Region          22..>93
                     /region_name="HD"
                     /note="HD domain; pfam01966"
                     /db_xref="CDD:460398"
ORIGIN      
        1 mdlteraysl aesllseplp rrwshslgva erartlrpil dddatlmeaa avlhdigysp
       61 riastgfhpl dgarflrdqe gmddrvvrlv ahhscallea eerglreele tefelerpal
      121 vdalvfcdmt ttpdggctss rdrvaeivgr ygpdtivgrf iqraapeiha avqrvegrlr
      181 eagavgqpm
//
LOCUS       WP_457699808             157 aa            linear   BCT 27-JAN-2026
DEFINITION  NUDIX hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699808
VERSION     WP_457699808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17236
     Region          20..144
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 msridyfrdp napkansvvp svtavvrdar gdillihktd ndlwalpggg hdvgesvaqt
       61 vireveeetg iavnvedivg lytdpqhvma yddgevrqqf sicfharptg gtlrtssesk
      121 evrwvsptdl ddleihpsmr lridhgldds rtapyig
//
LOCUS       WP_457699820             334 aa            linear   BCT 27-JAN-2026
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457699820
VERSION     WP_457699820.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..334
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35376
     Region          60..334
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mtepgqghtp gqagsraerl rnwwrpegtw rrglvlvvla vllgllmilh akvpntpgnw
       61 gslletflpw vglgipllli aavlrrsasa lvalllptiv wvnffgnqvt dkageggnlt
      121 vlthnvnaan pdpagtakdl vasgadvval eelsgdaltt yrqglakayp yhtiegtvgl
      181 wskrpltdtr pvdtkmgwnr alratvtaad gqqfavyvah lpsvrvnaak gftanrrdas
      241 vealgeaiaa dpvkkvmllg dlngtmndrs lapvtsqmrs aqgaagdgfg fswpaafpma
      301 ridqimmkgm dpvkawvlps tgsdhlpvaa svki
//
LOCUS       WP_457699821             354 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD(+)/NADH kinase [Streptomyces nigrescens].
ACCESSION   WP_457699821
VERSION     WP_457699821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10000530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="NAD(+)/NADH kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006741 - NADP+ biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0019674 - NAD+ metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=37457
     Region          4..315
                     /region_name="NadK"
                     /note="NAD kinase [Coenzyme transport and metabolism];
                     COG0061"
                     /db_xref="CDD:439831"
ORIGIN      
        1 msvqrvgivv hggrpgavat advvrrwcer qdvgcvaidv wsqdelrrda reevgaagsp
       61 dlivtlggdg tflrgarlaa qndalvlgvd lgtlgfltev paddvecald tihrgqvnve
      121 trlmltmras cplqlpegme allrygrgpa lppppvrpdc avardwgval nvtalndivl
      181 eklardrqvs lgvylagrll asysadavlv atptgstays faaggpvvsp radaivftpv
      241 aphmafnrsv vaapdeaval rvlghsgraa vsidgqlrgv ldpgdwigvy aapqrlrvar
      301 lgptdfygrl rermrltdap atadaditpm wphtspppdd lahlrlpplp ahvd
//
LOCUS       WP_457699829             320 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699829
VERSION     WP_457699829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10015415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..320
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=34664
     Region          19..279
                     /region_name="mthyl_TIGR00027"
                     /note="methyltransferase, TIGR00027 family"
                     /db_xref="CDD:272862"
ORIGIN      
        1 mvgtvhrktg vedveggvgl talmvaaara iethrhdsla rdvyaehfvl aapasagwpv
       61 rmqqvpdgda nplwgrfary fglrtrvldd fllrsmhaga rqvvllgagl dsrafrldwp
      121 pgcvifeidr egvlafkhkv lsglsatpka arvpipidlr adwvgaltda gfdttapsvw
      181 laegllfylp naaetylidt vdrlstagsa lafevklekd lleyrdsply tatkhqigid
      241 llhlfdgepr pdsagglagk gwstsvhtpf dftrrhgrgp lpeqndalag nrwvfahkpw
      301 aggtrlpgkg rpslsppsrp
//
LOCUS       WP_457699846             289 aa            linear   BCT 27-JAN-2026
DEFINITION  sulfurtransferase [Streptomyces nigrescens].
ACCESSION   WP_457699846
VERSION     WP_457699846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29947
     Region          19..279
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mnepvpgalp gplvgtdwva prlgtpglvv ldasigghrd ageripgarp fdidgalsdh
       61 sgplphtmpg adhftrelra lgvddgdtvv vydgaglyss arawwmlram gldrvavldg
      121 glpawraagl pletgtpapa prpgdftarp rpglivgsde vaaaltdpas avfdartrdr
      181 fagavaeprp glrpghmpga lnlpfgelqr dgrmrpasql rdafaplage rrrlffscgs
      241 gvtacilalg aelagyddla vydgswsewg lphadrpvvt gpqsggppa
//
LOCUS       WP_457699844             403 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-grasp domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457699844
VERSION     WP_457699844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     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=43494
     Region          58..306
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mphvlvfakt pyaktpydrw lagsgvvpvi ltttefaagy ghlphvhafd dydtnqlvek
       61 talrlareha vtavfaraea dvvraaqlrd lldlpgqrta salafrdkvv mkdhlvggpv
      121 eipayrplds aytalefvae hgypvvikpl sesgslgaai irdeaelday larpwrgase
      181 ievfvpgqmy hvdglvvdge vvfahpfryl ndclsfrand wvanlpltpq dpvhdrllka
      241 aravlaelpt pphtafhael witpddrtvf ceiasrtggg missmvrhaf gidldkewly
      301 aecglpstlg spayrptgal cippsdgvlt hlpsgdepac vkevaltgrv gqefhggvks
      361 glflagyvvg gdteedvaan lenvaawfad raewspaptg gtr
//
LOCUS       WP_457699859             167 aa            linear   BCT 27-JAN-2026
DEFINITION  lamin tail domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457699859
VERSION     WP_457699859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Eldirany,S.A., Lomakin,I.B., Ho,M. and Bunick,C.G.
  TITLE     Recent insight into intermediate filament structure
  JOURNAL   Curr Opin Cell Biol 68, 132-143 (2021)
   PUBMED   33190098
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Dittmer,T.A. and Misteli,T.
  TITLE     The lamin protein family
  JOURNAL   Genome Biol 12 (5), 222 (2011)
   PUBMED   21639948
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Dhe-Paganon,S., Werner,E.D., Chi,Y.I. and Shoelson,S.E.
  TITLE     Structure of the globular tail of nuclear lamin
  JOURNAL   J Biol Chem 277 (20), 17381-17384 (2002)
   PUBMED   11901143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="lamin tail domain-containing protein"
                     /GO_component="GO:0005882 - intermediate filament
                     [Evidence IEA]"
                     /calculated_mol_wt=18495
     Region          51..150
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
ORIGIN      
        1 msrnasriaa avvgsaalaa tavlpaaaag hdhhapaphh hyrsavslga iqydspgrdd
       61 rsnrslnaey vtvkntghra vnlrgwtlsd rsgqtyrfgd vrlrghsqvr vhtgigrdnr
      121 wnlyqdrrty vwdnndtatl rndhrrivdv eswgrhgghh ghwghsh
//
LOCUS       WP_457699865             501 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699865
VERSION     WP_457699865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..501
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53686
     Region          92..>337
                     /region_name="Abhydrolase"
                     /note="alpha/beta hydrolases; cl21494"
                     /db_xref="CDD:473884"
     Region          396..492
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 mkrqrsigls salavvlgls gslvaavava dgprapqvrw gtcpkdvvae atptelqcat
       61 vpvpvdytdp egaridlmis rlastnpekr rgtlmlnpgg pggsglaqpa llvarglpad
      121 vldsydligm dtrgighsap vkcgftldgp ytanippyaa ddaavtkqak vaeqvakqca
      181 rhdrdgllrh lttantardm driraalgee ktsylgysyg talgaayasm fpersdrivl
      241 dsnigdthld rdgmrryalg meqafpafak waaarhdsyg lgrtpaqvrr tyftlaerld
      301 kapvagfdgn llrqftfgnl fkkmqypkla qqwqtlagsd daaarllsqn atagkasssi
      361 dnplavfaav tcndikwpks vdtyrhgvak dreryplfga aaanitpcaf wphapaeppv
      421 avnddgprnv llvqnlrdpa tphhggkmlr qkftdrsrll svddsghgay vlgdnpcaln
      481 tttrylvegk mpgkdmlcra g
//
LOCUS       WP_457699867             143 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699867
VERSION     WP_457699867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15954
     Region          62..141
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mitrredgye vatdpdrldi dlvhhwlstd afwalgrsre tveqsirgsl nfglyddsga
       61 qvayarvvtd latfawlcdv yvapthrgkg lgtwlaaavr dhlapyklkr tllstldahe
      121 vyakvgfvpf pdpqhlmimk paq
//
LOCUS       WP_457699874             226 aa            linear   BCT 27-JAN-2026
DEFINITION  rhomboid family intramembrane serine protease [Streptomyces
            nigrescens].
ACCESSION   WP_457699874
VERSION     WP_457699874.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24478
     Region          1..203
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mtnvliglcc avfvlgpasg lnriygtgda llkaqtayfe rwgvipldlw ggsvralitp
       61 ltalfvhgsw lhllgnmlfl yvfgamaear mgrlpftafy liigylallg yaaahadsgq
      121 tlvgasgsis gvlgaflylf ptarvtslfp flfflplrfp awivllfwfa lqwqaaqddp
      181 rgpgvaylah vlgfalgfly awarygrdsv gatrandrat eeesqp
//
LOCUS       WP_457699886             598 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457699886
VERSION     WP_457699886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..598
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64480
     Region          1..598
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefslpaly evpadgnltd lirrnaaqhp dvavmgrkvn gvwqdvtaat flaevraaak
       61 gliasgvrpg drvglmsrtr yewtlldfai wsagaitvpv yetssaeqiq wilgdsgava
      121 clvespthea tvesvrdrlp elaniwqier dalarlqaag dgipddevea rsaladadsp
      181 ativytsgtt grpkgcvlsh rsffaecgni verlrplfrt gessvllflp iahvfgrlvq
      241 vaavmapikl ghapdiknlt ddlasfrpkl vlgvprvfek vynsarakaq adgrgkifdk
      301 aadvaiaysr aldtpegpsl glklkykvfd rlvygrlrav lggrathais ggaplgerlg
      361 hfyrgigftv legygltesc aatafnpwdr qkigsvgqpl pgsvvriadd gevllhgehl
      421 fteywnnpsa tkealsdgwf htgdlgtlde dgylaitgrk keilvtaggk nvapaviedr
      481 irahaliaec mvvgdgrpfi galvtldeef lprwaeehgr pagvtpaqla edpqllaavq
      541 ravddgnaav skaesvrkfr ilptqftees ghvtpslklk rnvvakdfae diealyra
//
LOCUS       WP_457699888             258 aa            linear   BCT 27-JAN-2026
DEFINITION  metallophosphoesterase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699888
VERSION     WP_457699888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=28225
     Region          79..257
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mrvhvvsdvh gnsrdlaaag agadalvclg dlvlfldyad hsrgifpdlf gvanadalve
       61 lrtarrfeea ralgrrlwgd ldrtgvsres viegavrrqy aelfaafptp tyatygnvdi
      121 prlwpeyagp gttvldgqrv eiggrvfgfv ggglttpmrt pyeisdeeya akieavgevd
      181 vlcthippdv pelcydtvar rfergsaall hairttrpry slfghvhqpl arriridgte
      241 cvnvghfnat gtpyvlew
//
LOCUS       WP_457699892             400 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457699892
VERSION     WP_457699892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Castillo,R. and Saier,M.H.
  TITLE     Functional Promiscuity of Homologues of the Bacterial ArsA ATPases
  JOURNAL   Int J Microbiol 2010, 187373 (2010)
   PUBMED   20981284
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Erzberger,J.P. and Berger,J.M.
  TITLE     Evolutionary relationships and structural mechanisms of AAA+
            proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 35, 93-114 (2006)
   PUBMED   16689629
REFERENCE   3  (residues 1 to 400)
  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 400)
  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 400)
  AUTHORS   Zhou,T., Radaev,S., Rosen,B.P. and Gatti,D.L.
  TITLE     Structure of the ArsA ATPase: the catalytic subunit of a heavy
            metal resistance pump
  JOURNAL   EMBO J 19 (17), 4838-4845 (2000)
   PUBMED   10970874
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Rosen,B.P., Bhattacharjee,H. and Shi,W.
  TITLE     Mechanisms of metalloregulation of an anion-translocating ATPase
  JOURNAL   J Bioenerg Biomembr 27 (1), 85-91 (1995)
   PUBMED   7629056
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Rosen,B.P.
  TITLE     The plasmid-encoded arsenical resistance pump: an
            anion-translocating ATPase
  JOURNAL   Res Microbiol 141 (3), 336-341 (1990)
   PUBMED   1704144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14288110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..400
                     /product="ArsA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42491
     Region          29..296
                     /region_name="ArsA"
                     /note="Anion-transporting ATPase, ArsA/GET3 family
                     [Inorganic ion transport and metabolism]; COG0003"
                     /db_xref="CDD:439774"
     Region          327..389
                     /region_name="ArsA_HSP20"
                     /note="HSP20-like domain found in ArsA; pfam17886"
                     /db_xref="CDD:436117"
ORIGIN      
        1 mrivlvtgsg gagrttlaaa talagarrge ralllttgcs apetvlgtpl gagaptpiap
       61 glharridpg drfrqeflaf qeragaaldl lgaapldede ltelpgsedf allhalraeh
      121 tsddwdlvvv dmpsaaetir llalpaqvrr ylrrllpper qaaralrpvl aqlagvpmpa
      181 qklydaaerw etelaavqrt iddpgtsvrl vteagpvaaa tlrtiragla lhgrrtdgvv
      241 vnrllptgsa dpflaalsgs qqttlkalre efpdvpvhev phlgrdpqgv deldeliggp
      301 ageigaaapa dgprpdpwtv edrlatdgil vwrvplpgae rrglglvrrg deivvtvgrf
      361 rrirtlpsal rrctvsgagl rdgsleirft pdpdlwpksd
//
LOCUS       WP_457699906             338 aa            linear   BCT 27-JAN-2026
DEFINITION  2-hydroxyacid dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457699906
VERSION     WP_457699906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10187446
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="2-hydroxyacid dehydrogenase"
                     /EC_number="1.1.1.28"
                     /GO_function="GO:0008720 - D-lactate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0070404 - NADH binding [Evidence IEA]"
                     /calculated_mol_wt=36486
     Region          1..327
                     /region_name="LDH_like_2"
                     /note="D-Lactate and related Dehydrogenases, NAD-binding
                     and catalytic domains; cd12183"
                     /db_xref="CDD:240659"
     Site            order(75..77,99,233,294,297)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:240659"
     Site            order(99,104,150,152..155,172..174,203..206,210,213,
                     231..233,257..258,294,296..297)
                     /site_type="other"
                     /note="putative NAD binding site [chemical binding]"
                     /db_xref="CDD:240659"
ORIGIN      
        1 meivafgvqt derpflekaf agrhqvrsld vflnrdtapi argyeivsss vnadlgadvl
       61 qtlaaggtkm iaqrstgfnn idleaaadlg msvgrvahys psavaefawa lalavnrriv
      121 ratnrtrnfd frldglmgrd lrgrtagvlg tgkigeaftr iahgfgmnll gwdlaenprc
      181 valgmeyvar erlfaeadll tlhlplvest rhlidaaala amkddailin ssrgglvdta
      241 alvetlkagr ltgvgldvye eeaaffffdk sldiigddtl arlmtfgnvl itshqayftq
      301 eavgqiieat vanvedylah rtnenmlvtr gqlpaaar
//
LOCUS       WP_457699900             265 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699900
VERSION     WP_457699900.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28555
     Region          5..248
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mpllpgaepf rrdggevgvl vchgftgspq svrpwaeyla drgltvalpl lpghgtrwqd
       61 lqittwqdwy aevdrelral terctkvfvc glsmggalal rlaakhgdai sgvavvnpan
      121 kvhdaaapll pvlrylvrtt kgvvsdiakp gaeevgyerm plhaahslrr ffqqvdselp
      181 gvtqpllvmt spqdhvvpaa dserilaris stdvrqtlle rsyhvatldh daeqifrdtf
      241 afisrlapqa radaaqegaa asgga
//
LOCUS       WP_457699915             299 aa            linear   BCT 27-JAN-2026
DEFINITION  deoxyribonuclease IV [Streptomyces nigrescens].
ACCESSION   WP_457699915
VERSION     WP_457699915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Asano,R., Ishikawa,H., Nakane,S., Nakagawa,N., Kuramitsu,S. and
            Masui,R.
  TITLE     An additional C-terminal loop in endonuclease IV, an
            apurinic/apyrimidinic endonuclease, controls binding affinity to
            DNA
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 3), 149-155 (2011)
   PUBMED   21358045
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Garcin,E.D., Hosfield,D.J., Desai,S.A., Haas,B.J., Bjoras,M.,
            Cunningham,R.P. and Tainer,J.A.
  TITLE     DNA apurinic-apyrimidinic site binding and excision by endonuclease
            IV
  JOURNAL   Nat Struct Mol Biol 15 (5), 515-522 (2008)
   PUBMED   18408731
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Ivanov,I., Tainer,J.A. and McCammon,J.A.
  TITLE     Unraveling the three-metal-ion catalytic mechanism of the DNA
            repair enzyme endonuclease IV
  JOURNAL   Proc Natl Acad Sci U S A 104 (5), 1465-1470 (2007)
   PUBMED   17242363
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Mol,C.D., Hosfield,D.J. and Tainer,J.A.
  TITLE     Abasic site recognition by two apurinic/apyrimidinic endonuclease
            families in DNA base excision repair: the 3' ends justify the means
  JOURNAL   Mutat Res 460 (3-4), 211-229 (2000)
   PUBMED   10946230
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Hosfield,D.J., Guan,Y., Haas,B.J., Cunningham,R.P. and Tainer,J.A.
  TITLE     Structure of the DNA repair enzyme endonuclease IV and its DNA
            complex: double-nucleotide flipping at abasic sites and
            three-metal-ion catalysis
  JOURNAL   Cell 98 (3), 397-408 (1999)
   PUBMED   10458614
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Barzilay,G. and Hickson,I.D.
  TITLE     Structure and function of apurinic/apyrimidinic endonucleases
  JOURNAL   Bioessays 17 (8), 713-719 (1995)
   PUBMED   7661852
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..299
                     /product="deoxyribonuclease IV"
                     /EC_number="3.1.21.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003906 - DNA-(apurinic or apyrimidinic
                     site) endonuclease activity [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=31285
     Region          20..298
                     /region_name="Nfo"
                     /note="Endonuclease IV [Replication, recombination and
                     repair]; COG0648"
                     /db_xref="CDD:440413"
ORIGIN      
        1 mstssspkga eqrararnpv gghvpvaggl akagipyare mgdeavqvfv anprgwattp
       61 gnpeqdeafr aacalqgipa yvhapylinf gshteatvdk svaslrhslr rgreigalgv
      121 vvhtgsatgg rpraaamaqv rermrpllee lthpddpwll leptagqgas lcaraedlgp
      181 yfdaldrhpk lgicldtcha faaghdmaap ggmkalldel vevtgegrlk lihandskdv
      241 vgahkdrhen igaghigaep fgelfvhpat agvplvvetp ggkeghaadv arlkelrap
//
LOCUS       WP_457699918             380 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 4 protein [Streptomyces nigrescens].
ACCESSION   WP_457699918
VERSION     WP_457699918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..380
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009101 - glycoprotein biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40440
     Region          3..380
                     /region_name="GT4_PimA-like"
                     /note="phosphatidyl-myo-inositol mannosyltransferase;
                     cd03801"
                     /db_xref="CDD:340831"
ORIGIN      
        1 mhktlivtnd fpprpggiqa flhsmalrld ptqvvvyast wkrsaegraa taafdaeqpf
       61 pvirdrttml lptprvtrra tgllrehgcs svwfgaaapl glmapalrsa garrivatth
      121 gheagwaqlp aarqllrrig tgtdtltylg eytrsriaga ltpeaaarmv qlppgvdekt
      181 fhpgsggdav rdrlglagrp vvvcvsrlvp rkgqdtliea mpailsavpd avllivgggp
      241 yeqdlhalar ekgvadavhf tgavpweelp ahygagdvfa mpcrtrrggl dveglgivyl
      301 easatglpvv agdsggapda vlegetgwvv pggspaptad riitllrdpa lrrsmgergr
      361 awveekwrwd llaerlkell
//
LOCUS       WP_457699926             353 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457699926
VERSION     WP_457699926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..353
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37518
     Region          38..353
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrmppralrh siltaaaaav tlvtackapq pdavgsvqvs aqtgtkqaaq ltydfgdtay
       61 appglegkrt elkaavtypr glgngkhpll mmlhgwadtc sagdkpvrpq vwpcgkgarp
      121 vdnylgysyl aralaekgyi vvsvsangiq aqeqgqghia rralldkhle mwqqlaagkg
      181 plralkpftd hvdlnrvgtl ghsrggggvi aqvldshkrp pgvnirgala lapamngida
      241 gkeritrvpi avvagtcdam wddskiplam aaknpharhy svtganhnff ntvwtpgsgp
      301 sfasddvaie nrnlpggrck stngtgnprq lkpaeqrqaa iryvttffdk yvr
//
LOCUS       WP_457699936             450 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457699936
VERSION     WP_457699936.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46192
     Region          42..402
                     /region_name="MFS_NepI_like"
                     /note="Purine ribonucleoside efflux pump NepI and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17324"
                     /db_xref="CDD:340882"
     Site            order(43..44,47,79,128..129,131..133,136,156,159..160,163,
                     238,241..242,245..247,250,278,282,332..333,337,341,356,
                     359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340882"
ORIGIN      
        1 mpgngeavtr rtqarseegs afvlsrgvvt lfavaggaav anvyfsqpll vtmghdlams
       61 palvgsvvtl thvgyglglf flvplgdmad rrrlivaqll llvmalavva aahtaallla
      121 gmaatgllav vtqtlvafaa slappegrgr vvglvtsgvv tgillartas gfmadlagwr
      181 svylasaslt allalvlyrv lprhsdappt tvrygqllrs tialfarerl lrlralfgll
      241 ifaafstlws svalplseap yflphsaiga lgligvagal aataagrlnd rglarrttgi
      301 alallaaswl plaftrsslw alvvgvlfld lavqavhvtn qtliyalhpd agsrliggym
      361 vfysigsatg aiaatslytv agwgavcalg atfsclglal waftrhgtpd vtvgpicsad
      421 rhasvlgehp ppgadrpdga qaadlgtgcr
//
LOCUS       WP_457699938             150 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699938
VERSION     WP_457699938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..150
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16580
     Region          3..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtrtrfdds ecpvarsvda igdwwslliv rdafdgsrrf gefqrslgva kniltarlrt
       61 liaggvlesv pasdgsayre yvltpkgkal fpvivalrqw geqnffapge phsqlvdrrq
      121 gqrlravevl sadgrrlnpd dttvhnistq
//
LOCUS       WP_457699954             290 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457699954
VERSION     WP_457699954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32911
     Region          6..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          107..273
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdrntalgef lrsrraritp rqaglsddgg trrvpglrre eiaqlagvsv dyyvrlergr
       61 rlnvsetvld aisralrldp verthlfqla kpaagrprrt atrpqpvrpg lrdllrileh
      121 tpalvlgrrl dvlasnqmar alltdfdalp hrernlvrfm fcdetarsly thwdthaqdi
      181 vaslrldagr hphdpllael vgelsitded frrwwayqnv yrhthgskhf hhpivgpltl
      241 nyesltlpad pdqrlsvyta eagssseeal rllaawirqp etshgqhadh
//
LOCUS       WP_457699958             187 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699958
VERSION     WP_457699958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20943
     Region          5..183
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 metyleterl alrrftadda dllieldsdp avmryltggn ptapelvrer ylprilagye
       61 kwggdlglfa aqekdggafi gwfilrpepe gpldevelgy rlrqaawgkg yategsrall
      121 gkaftelgvr mvwaetmsvn hssrnimekl emaladtipt psdmemiegs ehggvryeit
      181 keqweqq
//
LOCUS       WP_457699970             243 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457699970
VERSION     WP_457699970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..243
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24858
     Region          3..239
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mllenktaiv yggagaigsa varvfagega tvhlvgrtha pleelagtia esggrvevat
       61 ldatdraave qhadavarhs vgidiafnat snddlqgtpl vdmadedvlr pvtkavtthl
      121 tlatavarhm iprhtgvila mgggreaipg lggshiawsa lsglcrqlas elgphgiraa
      181 wllspgspdp sippeddpea tttllhrrpr ledvayaaaf lasdraptmt atevnvtgga
      241 vvd
//
LOCUS       WP_457699974             271 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457699974
VERSION     WP_457699974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27762
     Region          22..244
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mseqrvvlvt gggtgigaat arllrtaghq vvisgrrpep lrrvaeetga lahpsdaadp
       61 eavrelvett vtaygrldgv vlnagigrgg avgdtevedw eellrtnltg pflllraalp
      121 hllaargavv avasvaalrn svgnaayats kagllhlcrs lavdygpqgl ranavcpgwv
      181 rtemadqrma rfaaeaglag gaeaayeean rltpagrpgd peevagaidw llspaasyvn
      241 gavltvdggv ttvgvggaaf dyrieartpr l
//
LOCUS       WP_457699910              84 aa            linear   BCT 27-JAN-2026
DEFINITION  (2Fe-2S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457699910
VERSION     WP_457699910.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Wijerathne,H., Yao,H., Wang,Y., Lovell,S., Battaile,K.P. and
            Rivera,M.
  TITLE     Bfd, a New Class of [2Fe-2S] Protein That Functions in Bacterial
            Iron Homeostasis, Requires a Structural Anion Binding Site
  JOURNAL   Biochemistry 57 (38), 5533-5543 (2018)
   PUBMED   30183257
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Rivera,M.
  TITLE     Bacterioferritin: Structure, Dynamics, and Protein-Protein
            Interactions at Play in Iron Storage and Mobilization
  JOURNAL   Acc Chem Res 50 (2), 331-340 (2017)
   PUBMED   28177216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..84
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=8463
     Region          1..49
                     /region_name="Bfd"
                     /note="Bacterioferritin-associated ferredoxin [Inorganic
                     ion transport and metabolism]; COG2906"
                     /db_xref="CDD:442150"
ORIGIN      
        1 myvcscfgit ekqvrehadt gactprqias ackagtdcgg cvrriqsllg rgdcprreli
       61 dsgapeplga eagaaapaal seva
//
LOCUS       WP_457699978             385 aa            linear   BCT 27-JAN-2026
DEFINITION  Dyp-type peroxidase [Streptomyces nigrescens].
ACCESSION   WP_457699978
VERSION     WP_457699978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Sugano,Y. and Yoshida,T.
  TITLE     DyP-Type Peroxidases: Recent Advances and Perspectives
  JOURNAL   Int J Mol Sci 22 (11) (2021)
   PUBMED   34074047
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Colpa,D.I., Fraaije,M.W. and van Bloois,E.
  TITLE     DyP-type peroxidases: a promising and versatile class of enzymes
  JOURNAL   J Ind Microbiol Biotechnol 41 (1), 1-7 (2014)
   PUBMED   24212472
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Sugano,Y.
  TITLE     DyP-type peroxidases comprise a novel heme peroxidase family
  JOURNAL   Cell Mol Life Sci 66 (8), 1387-1403 (2009)
   PUBMED   19099183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..385
                     /product="Dyp-type peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=40029
     Region          51..357
                     /region_name="EfeB"
                     /note="Periplasmic deferrochelatase/peroxidase EfeB
                     [Inorganic ion transport and metabolism]; COG2837"
                     /db_xref="CDD:442085"
ORIGIN      
        1 mrradhhpsr rtfldvtgam maagltagct sdsaqrgrha ptsgatpmpv patgrhqagi
       61 tlpqpaqpnl lavvadlgat vapgpllael gqairtltag tdtrllglps gdltvtvgvg
      121 prlvrtagas lpgaadlprf sreriapqar ggdlliqica sdalllpvvv aalldgagdr
      181 irerwrqsar rganvsvgng ltaprnplgf idgivgphtt aeqqrdlwlt gpptvaggtl
      241 avlrrmeldl prfaalsvae qeavfgrrra sgvplsggpv asgpelgakt pdgrylvpad
      301 ahvrrahatv vgvglmlrrs ystdepapgl lfisfqndlr tfsatlthmd tsdallqftt
      361 ttasatflil pgfdrqhplg sqlfg
//
LOCUS       WP_457699986             269 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457699986
VERSION     WP_457699986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..269
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28076
     Region          86..262
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mfkreprral amtavlflal tsvtacagrd aetapqgsam aenrrsteeg tiavrefsat
       61 pdrlpscfhg vrgatayrpp gssgdgrlvt lgtgprgvvf apiswgdace waaeakrlaa
      121 dgyhvvtfdw ggdrrrtvse atrllrsrga tnvawvggcm ggtlmlgmlt drtdrpagva
      181 gisplaslgg ysagngtayd gellllgtad dplsdegrlr evahsfpkae vtvlpgtlha
      241 aeifagphga karrsldgfl drtfapads
//
LOCUS       WP_457699988             169 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457699988
VERSION     WP_457699988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..169
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17817
     Region          24..160
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mepdhvdeii sawghelpei aglplelakr tallvsafdi aagaeleklg ltqaeygvla
       61 tlrrigapyr lkptdlthal llssggtsnv ikrlvaagyv traaaeddar sswvqltpsg
      121 vataeaavra ttavharlvd ripeptakal seqlrialaa ieegvlirr
//
LOCUS       WP_457699994             225 aa            linear   BCT 27-JAN-2026
DEFINITION  O-methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457699994
VERSION     WP_457699994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..225
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23916
     Region          64..221
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttattaldd ervgavldei artaehndpd vmkrayataa dwpqpptaqe aaelcaqaal
       61 pvhpqvgtfl yqlirslrpa lvvefgtsfg astiyaaaal rdngggriig selhagkadr
      121 arshleragl agyaeirtgd areqlatlpg pvdlllldgw kelylpvlkl lepalrtggl
      181 vvsdnlpmlp peftdhvraa gsgylsqqlp lgdgiefsvr lqeea
//
LOCUS       WP_457699995             313 aa            linear   BCT 27-JAN-2026
DEFINITION  TauD/TfdA family dioxygenase [Streptomyces nigrescens].
ACCESSION   WP_457699995
VERSION     WP_457699995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Islam,M.S., Leissing,T.M., Chowdhury,R., Hopkinson,R.J. and
            Schofield,C.J.
  TITLE     2-Oxoglutarate-Dependent Oxygenases
  JOURNAL   Annu Rev Biochem 87, 585-620 (2018)
   PUBMED   29494239
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schofield,C.J. and Zhang,Z.
  TITLE     Structural and mechanistic studies on 2-oxoglutarate-dependent
            oxygenases and related enzymes
  JOURNAL   Curr Opin Struct Biol 9 (6), 722-731 (1999)
   PUBMED   10607676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..313
                     /product="TauD/TfdA family dioxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34284
     Region          6..289
                     /region_name="TauD"
                     /note="Taurine catabolism dioxygenase TauD, TfdA family;
                     pfam02668"
                     /db_xref="CDD:367137"
     Site            order(94,96,121,279)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(94,96,279)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
ORIGIN      
        1 mttiadvrpy gaatgrlvlp aedrslgald pawvtgllad agfllfrgfr tdleeftsfv
       61 kahssritld parsfhggev aqkvdagtva vglhlengns pfgpdltwfl cekaaasgsq
      121 ttvcdgyrvw daasdtarav fgvkdimysr rveepkwkaf vchqtegrkk ldditfadmk
      181 dlvggsvstt lqlnddgsih yayrvgavhp tlfgsrlswa nsvfgpsyny eapritfadg
      241 teipeellae frrlteelte eldwqdgdva lidntrvmhg rreildtdrt iynaqsyldp
      301 alpaavrdgr aqg
//
LOCUS       WP_457700009             143 aa            linear   BCT 27-JAN-2026
DEFINITION  HIT family protein [Streptomyces nigrescens].
ACCESSION   WP_457700009
VERSION     WP_457700009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..143
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15130
     Region          28..140
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mvsygefrev agdtpdarpq rprtarrpgc pfclivcgra patvlrewpe tiairprhgg
       61 vtaghvlvip rvhvadvaed pvvsaatmlr aaelaaeagd cnvitsrgps atqtvrhlhl
      121 hlvpraegdg lllpwtavrp agt
//
LOCUS       WP_457700022             203 aa            linear   BCT 27-JAN-2026
DEFINITION  toll/interleukin-1 receptor domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700022
VERSION     WP_457700022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..203
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=22139
     Region          4..>107
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 magvfinyrt gdgavaavll deelkdvfgp envfrdrrtt ppgahfppel wrhlescgvl
       61 lvligpnwls lcdtdgrrri dvpgdyvhde ihralmwrkt vipvlidsae lpskdqlpad
      121 iaelterqfm qlrvpyahld lpvitdalrs hvpvrrtepq pappaggapq pgshstyndc
      181 avsngsgnat vnqgrdaqsg grq
//
LOCUS       WP_457700033             148 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700033
VERSION     WP_457700033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..148
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15328
     Region          9..131
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mvtaspvlel qldcysevvg parhlaatfl erlepsldkd ardavilvvs elvtnavrha
       61 ggklctlrlt sdpqsvvvav gdsspvlprp rtpdvtgggg gfgwsmvcrl aasvevrrnp
      121 agktvtavis rqgashsges drdarata
//
LOCUS       WP_457700037             188 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700037
VERSION     WP_457700037.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20272
     Region          10..143
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtfpeadtpp alrtqvselr deawppdsas apgtfahdpa lrpvsmllvd gatvlaaldi
       61 ltkelvhagq ryraaglstv vtrgtvrgkg hgrrlvtaar eamaamdldi glftcdrplq
      121 pfyesagwqh lpgavliggt pqapfpsdrp gfdkvtladf fssrgrshrs sfphsriely
      181 pgeidklw
//
LOCUS       WP_457700041             295 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700041
VERSION     WP_457700041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..295
                     /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]"
                     /calculated_mol_wt=31859
     Region          27..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myhtwmryft pspvhhrlgl vclgvglqhg tlptvgprtl dhhvalvisa grgwftasdg
       61 rrrpvtapal lwlvpgvphh ygadpetgwd esfvdftgpa aatytelgyi epdrplvpla
      121 dtgpartaig riaraarrgn pllevetsaa vhellvalrr aradtdadgd pvlqalarda
      181 flplsvaeha arhgmtpael rtavrrgagc spkdyllair lgrakellvg telpvaavar
      241 rvgyddpayf srlftrrvgt apvrfrdrqv hnvpggwstq ipdpddppvv sgwsg
//
LOCUS       WP_457700047             349 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457700047
VERSION     WP_457700047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..349
                     /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=35649
     Region          125..345
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mahqparpht imaatavavc lcavpadrip ltaraaaaaa isltgsavll agphpsqvwg
       61 lgeglallll laavvrrapg rtaavlgpll glacvltplr dlrpgiftvv qavlavvvaa
      121 ysltlrrqda qrlrdlaavr aaerlelare lhdlvahhvt givvqaraar ftalegppag
      181 atferietag sealgamrrl vrvlredgar ahplaglaev ramtdafsrt gppvvlaldt
      241 gaanalpaev aaavhrivre altnvrkhaa datavriglr svprgvelrv andggaparl
      301 seqargggfg laglteraea mggrliagpa aeggweltav lpldggata
//
LOCUS       WP_457700051             265 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457700051
VERSION     WP_457700051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  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 265)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475742
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..265
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27139
     Region          8..264
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrsyrkhlkr atavgavala afslqpgsas aapapepstk vvggtkadqg efpfmvrlsm
       61 gcggalyakd ivltaahcvd gsgdntsita tagvvdleda gavkvnstkv lqapgydgkg
      121 kdwaliklak pidqptlkia eddklnngdf tiagwgadke ggeqqryllk atvpfvddaa
      181 cqkaygdqlt pgdelcagkl dtggtdtcqg dsggpmfrkd dagqwlqvgi vswgegcarp
      241 gkpgvysevs afaanikkaa gelgg
//
LOCUS       WP_457700056             348 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700056
VERSION     WP_457700056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  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   2  (residues 1 to 348)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..348
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36235
     Region          11..347
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtdrpgprat ptpptsaava rragvsratv syvlngraag rvgertqarv raaaeelgyv
       61 phaaarslra grgsivllaa padaaevfgp lftrflagfq talhrlgytg vlhgaparsp
      121 maaarawael rpaavlnlhg ppldapavel lhragttavl vlgrsappga htllldqrea
      181 glragehlla hgrrrigvvr paepgpadca elrlagvraa aathpgaevr pldlartees
      241 aaglaavwpe ldldavfgyn deyamllmra lqdaghtvga dgpdrlavvg addlllarll
      301 rprltsvrae itpperiagl vadllldpaa ppethrlgtf hvmaresg
//
LOCUS       WP_457700058             244 aa            linear   BCT 27-JAN-2026
DEFINITION  MBL fold metallo-hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457700058
VERSION     WP_457700058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25210
     Region          11..223
                     /region_name="yflN-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis yflN; MBL-fold metallo hydrolase domain; cd07721"
                     /db_xref="CDD:293807"
     Site            order(66,68,70..71,160..161,179,222)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293807"
ORIGIN      
        1 mealteitpt vwqlafpvgh vylvalpddg faavdtgvpg sapavlgala rlggrpdqlr
       61 qivlthshmd hmgsaadlva atgarvlaga ldapyirgta pepaavlspa eqslhegima
      121 dfaaaglppl rhtevdvalh dgdtldgwpe pvrvlhvpgh tpggialhlp asrllfpgdi
      181 igttpdgtra vlgpfnvare eaiasfrrla aldevdtvcv phgaplrtga rdvlaaatpe
      241 kdwq
//
LOCUS       WP_457700062             158 aa            linear   BCT 27-JAN-2026
DEFINITION  PPOX class F420-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457700062
VERSION     WP_457700062.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Canaan,S., Sulzenbacher,G., Roig-Zamboni,V., Scappuccini-Calvo,L.,
            Frassinetti,F., Maurin,D., Cambillau,C. and Bourne,Y.
  TITLE     Crystal structure of the conserved hypothetical protein Rv1155 from
            Mycobacterium tuberculosis
  JOURNAL   FEBS Lett 579 (1), 215-221 (2005)
   PUBMED   15620716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11497257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="PPOX class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17410
     Region          16..142
                     /region_name="Rv1155_F420"
                     /note="PPOX class probable F420-dependent enzyme;
                     TIGR03618"
                     /db_xref="CDD:274679"
ORIGIN      
        1 mspstatntr vdlpellefv rprhraillt rrsdgtpqgs pltcgvddsg rlvmatyper
       61 akvrnarrvs svsvivlsde wngpwvqidg eaevidapds ieplveyyrn iagehpdwde
      121 yreamrkqgk slirvtplrw gpvatggfpa rlteggda
//
LOCUS       WP_457700065             193 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457700065
VERSION     WP_457700065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..193
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20935
     Region          48..176
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 marefeakdg dghpgaeasp ypveeiaaaw ererpgtpvs sigivtpiwq lakllgddrr
       61 rvlaragmdp atldllsvlr rsgepytltt relgrrsmvt agavsqrvar aereglvtrr
      121 pgegrprtvl veltpaghel ieatvdqvlh reaelidglt pgqqeqlagl lrillqdtqr
      181 klgddrigqv gea
//
LOCUS       WP_457700064             240 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457700064
VERSION     WP_457700064.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..240
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24752
     Region          3..235
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msrtilvtgg gtgigravah hfadrgddvi vtgrrlaple etaagrrtvr plvcdhtepg
       61 sltellarlp eridvlvnna ggntdfdtde atdlasyard franldanlv saalttrald
      121 grlaaggavv hlgsiaadqg agaygaakag laswnvelar tlgprditan vvapgyvagt
      181 effrdrltde rrdhlvaaaa vgrpgspedi agtvaflasp aarhltgqvl nvnggtrttr
//
LOCUS       WP_457700067             253 aa            linear   BCT 27-JAN-2026
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457700067
VERSION     WP_457700067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Roy,R., Samanta,S., Patra,S., Mahato,N.K. and Saha,R.P.
  TITLE     In silico identification and characterization of sensory motifs in
            the transcriptional regulators of the ArsR-SmtB family
  JOURNAL   Metallomics 10 (10), 1476-1500 (2018)
   PUBMED   30191942
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Saha,R.P., Samanta,S., Patra,S., Sarkar,D., Saha,A. and Singh,M.K.
  TITLE     Metal homeostasis in bacteria: the role of ArsR-SmtB family of
            transcriptional repressors in combating varying metal
            concentrations in the environment
  JOURNAL   Biometals 30 (4), 459-503 (2017)
   PUBMED   28512703
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Ren,S., Li,Q., Xie,L. and Xie,J.
  TITLE     Molecular Mechanisms Underlying the Function Diversity of ArsR
            Family Metalloregulator
  JOURNAL   Crit Rev Eukaryot Gene Expr 27 (1), 19-35 (2017)
   PUBMED   28436329
REFERENCE   4  (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   5  (residues 1 to 253)
  AUTHORS   Busenlehner,L.S., Pennella,M.A. and Giedroc,D.P.
  TITLE     The SmtB/ArsR family of metalloregulatory transcriptional
            repressors: Structural insights into prokaryotic metal resistance
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 131-143 (2003)
   PUBMED   12829264
REFERENCE   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..253
                     /product="ArsR/SmtB family transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26993
     Region          26..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkrwdadqes vaetpdlaal aalladrtra aicmalldgg twtagelaey aavapsttte
       61 hlnllvsggl laeerqgrrr yvrlagpeta etlenlagla pyrqvpirsl aeanhrramh
      121 hartcydhia galgvaiaea mtergllard yglvltvaga dwlaalgipd aappaahrah
      181 vrtcldwtvr rqhlsgavga alyryalerd wvvkavatri ltltaagraa fraqlglpde
      241 alfpslalps prt
//
LOCUS       WP_457700077             423 aa            linear   BCT 27-JAN-2026
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700077
VERSION     WP_457700077.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Heider,J.
  TITLE     A new family of CoA-transferases
  JOURNAL   FEBS Lett 509 (3), 345-349 (2001)
   PUBMED   11749953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..423
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44465
     Region          30..423
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
ORIGIN      
        1 mtdpslsgap rpaagehtvp dspapespvp gplaglrvld latlfagpla atllgdfgae
       61 vikvehprrp dpsrghgpak dgiglwwkll grnkrtmtld lshpggrdvl lrlaagtdvi
      121 venfrpgtle rwglgwdels avnprlvlar vtgfgqfgpy arrpgfgtla eamsgfaait
      181 gepdgpptlp pfgladaiaa lttsyavlaa lrgrettgrg qvidlaliep iltalgpqpl
      241 wydqlghvqp rtgnrspnva prntyrtadg swvavstste svaervmrlv grpevidepw
      301 fatgagragh adeldaavgg wiarhdraev vaafekaeaa vapvydirev madpqyaalg
      361 sitevpddel gtvrmqnvlf rlsetpgaih wagrphgadt davlaglglt daeidglrta
      421 gal
//
LOCUS       WP_457700079             338 aa            linear   BCT 27-JAN-2026
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700079
VERSION     WP_457700079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..338
                     /product="HpcH/HpaI aldolase/citrate lyase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34480
     Region          18..336
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msraphpprq apgptpltwl yvpgdrpevv akalgcgadv vvvdledava pdrkdhalra
       61 taellsdpvp vpvhvrvnal dgplaeneir tltalpglag lrlpkvqgpa dvhraagwat
      121 taaepvpehl pyaaegpvrp agrasaghaa pvrtppgtta tltpaappva salpatpaly
      181 allesalgie hafaiatahp alrgialgea dlcgelgvrd dtglawprsr tvvaaraagl
      241 apppqsvhpd ihdldglars cargralgfl graaihprql pvieaaylps aeeiaaaqei
      301 vraataegga lalpdgrfvd aavvagarrv ldlagrrp
//
LOCUS       WP_457700084             152 aa            linear   BCT 27-JAN-2026
DEFINITION  Crp/Fnr family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700084
VERSION     WP_457700084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..152
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=17166
     Region          8..>142
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mttikdmfde lppdrrrrlt diavevslpr atrlfeegrr adrfwiirsg qvaldqhvpg
       61 rraaivetlg rdellgwswl fppylwhlga etvgpveave fdaravrdlc esdpvlgrav
      121 yryvaktvad rlhgtrtrll dlygpqgsgl dp
//
LOCUS       WP_457700093             452 aa            linear   BCT 27-JAN-2026
DEFINITION  chloride channel protein [Streptomyces nigrescens].
ACCESSION   WP_457700093
VERSION     WP_457700093.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Miller,C.
  TITLE     ClC chloride channels viewed through a transporter lens
  JOURNAL   Nature 440 (7083), 484-489 (2006)
   PUBMED   16554809
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Suzuki,M., Morita,T. and Iwamoto,T.
  TITLE     Diversity of Cl(-) channels
  JOURNAL   Cell Mol Life Sci 63 (1), 12-24 (2006)
   PUBMED   16314923
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Jentsch,T.J., Stein,V., Weinreich,F. and Zdebik,A.A.
  TITLE     Molecular structure and physiological function of chloride channels
  JOURNAL   Physiol Rev 82 (2), 503-568 (2002)
   PUBMED   11917096
  REMARK    Erratum:[Physiol Rev. 2003 Apr;83(2):following table of contents]
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Mindell,J.A. and Maduke,M.
  TITLE     ClC chloride channels
  JOURNAL   Genome Biol 2 (2), REVIEWS3003 (2001)
   PUBMED   11182894
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Schmidt-Rose,T. and Jentsch,T.J.
  TITLE     Transmembrane topology of a CLC chloride channel
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7633-7638 (1997)
   PUBMED   9207144
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Jentsch,T.J. and Gunther,W.
  TITLE     Chloride channels: an emerging molecular picture
  JOURNAL   Bioessays 19 (2), 117-126 (1997)
   PUBMED   9046241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..452
                     /product="chloride channel protein"
                     /GO_function="GO:0005247 - voltage-gated chloride channel
                     activity [Evidence IEA]"
                     /GO_process="GO:0006821 - chloride transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44808
     Region          45..418
                     /region_name="Voltage_gated_ClC"
                     /note="CLC voltage-gated chloride channel. The ClC
                     chloride channels catalyse the selective flow of Cl- ions
                     across cell membranes, thereby regulating electrical
                     excitation in skeletal muscle and the flow of salt and
                     water across epithelial barriers. This...; cd00400"
                     /db_xref="CDD:238233"
     Site            order(107..111,138..142,357..361)
                     /site_type="active"
                     /note="Cl- selectivity filter [active]"
                     /db_xref="CDD:238233"
     Site            order(108,110,140..141,357..359)
                     /site_type="other"
                     /note="Cl- binding residues [ion binding]"
                     /db_xref="CDD:238233"
     Site            140
                     /site_type="active"
                     /note="pore gating glutamate residue [active]"
                     /db_xref="CDD:238233"
     Site            order(187,196,213,220,398,401,409,417)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238233"
ORIGIN      
        1 maigpagpvg gapttvpqdp yalvrtrgyl klllvaaaig fpvcavafgf lalvhelepl
       61 iyqdlpralg fagtpiwwpv pmlvvagllv gltvrylpgg gghepadgla lsgapppsal
      121 pgvflaalas lsfgvvlgpe aplialgggl aagavrlmgr gmpaqavatv gaagsfaais
      181 allgspllga fllmevsglg gpmlgivlvp gllasglgal iftglgdwtg lgtyslalhd
      241 ipkaaeptlp efgwalvigl aagfaatgvr rfarflkghv vrhrvpatvl mglvvgalav
      301 afaaatgkpa semlysgqsa lgslfrdsag ytvgalllli lckglaycas lsafrggpif
      361 palflgaagg vvlshlpgls ltaafamgvg amcvamlrlp mtsvllatll lgksgltvmp
      421 lvivavvvay vvalrltpat apdapaaaph aa
//
LOCUS       WP_457700095             302 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700095
VERSION     WP_457700095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   3  (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   4  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31512
     Region          5..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..294
                     /region_name="PBP2_LTTR_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08423"
                     /db_xref="CDD:176115"
     Site            order(108..109,111..112,115,119,121..127,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176115"
ORIGIN      
        1 miearrlhil ravadhrtvt aaaaalyltp savsqqlaal eqetghrlve rsargvrlta
       61 agdillthan avleqlerae selaaygsge agtvtvaafa tgiglvvapa ltalartapg
      121 irvhvqdaeg dasllmvldr qvdvavavey rgapgaddpr ltrvplyaep fdavlppghr
      181 laeaaqvava dlaadpwigp ypgnpchdvv vlaceyagfq prlehssddf ravvalasaa
      241 agvalvprsa lrdmdltgvv vrpvddvapt rrvfaavrrg aeehplfrpv laalreaaas
      301 qg
//
LOCUS       WP_457700100             510 aa            linear   BCT 27-JAN-2026
DEFINITION  S1 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457700100
VERSION     WP_457700100.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Sauter,N.K., Mau,T., Rader,S.D. and Agard,D.A.
  TITLE     Structure of alpha-lytic protease complexed with its pro region
  JOURNAL   Nat Struct Biol 5 (11), 945-950 (1998)
   PUBMED   9808037
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Silen,J.L., McGrath,C.N., Smith,K.R. and Agard,D.A.
  TITLE     Molecular analysis of the gene encoding alpha-lytic protease:
            evidence for a preproenzyme
  JOURNAL   Gene 69 (2), 237-244 (1988)
   PUBMED   3234766
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Henderson,G., Krygsman,P., Liu,C.J., Davey,C.C. and Malek,L.T.
  TITLE     Characterization and structure of genes for proteases A and B from
            Streptomyces griseus
  JOURNAL   J Bacteriol 169 (8), 3778-3784 (1987)
   PUBMED   3112129
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15890625
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..510
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47185
     Region          <112..>139
                     /region_name="Pro_Al_protease"
                     /note="Alpha-lytic protease prodomain; pfam02983"
                     /db_xref="CDD:460772"
     Region          238..422
                     /region_name="alphaLP-like"
                     /note="alpha-lytic protease (alpha-LP), a bacterial serine
                     protease of the chymotrypsin family, and similar proteins;
                     cd21112"
                     /db_xref="CDD:411050"
     Site            order(269,295,330,333..337,339,347..351,354,358..361,363,
                     372,377..382,397..399,405,408)
                     /site_type="other"
                     /note="pro domain interface [polypeptide binding]"
                     /db_xref="CDD:411050"
     Site            order(269,359,361,363,377..382,397..399)
                     /site_type="other"
                     /note="peptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411050"
ORIGIN      
        1 mnkrtgaivg aaavaiagaa illpnanast dqpaalktls ahsatqlats lkadlgdqsa
       61 gwyldssngh lvmnvlsedd aasvtakgav akvvqnsmta lksgaqtlrd nasvpgtaws
      121 idpktnkivv vadrtvtgak matltkttkg mgegmvtvkr sqgefkrydg gdagsaagga
      181 agsaaggagd aaggagdaag gagdaaggag daaggagdaa ggagdggagg geqaagpigg
      241 saifggnarc slgfnvtvkg apafltaghc gndsktwtad qggsqplgtv sdsqfpktdf
      301 alvtyddana qpqsavdlqn gstqeitkaa eaavgmkvqr sgsttglsdg tvtgldatvn
      361 ygngdivngl iqtdvcaepg dsggamfsdd savgltsggs gdctaggetf fqpvtdalea
      421 tgaeigaggg gaggagggdd gaaggngagg gdagagnaga gnagagnaga gnagagagdp
      481 gagaqdpgtg aedpgagaqd pgaaggdaln
//
LOCUS       WP_457700106             803 aa            linear   BCT 27-JAN-2026
DEFINITION  SpoIIE family protein phosphatase [Streptomyces nigrescens].
ACCESSION   WP_457700106
VERSION     WP_457700106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Hefti,M.H., Francoijs,K.J., de Vries,S.C., Dixon,R. and Vervoort,J.
  TITLE     The PAS fold. A redefinition of the PAS domain based upon
            structural prediction
  JOURNAL   Eur J Biochem 271 (6), 1198-1208 (2004)
   PUBMED   15009198
REFERENCE   2  (residues 1 to 803)
  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   3  (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   4  (residues 1 to 803)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   5  (residues 1 to 803)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Ponting,C.P. and Aravind,L.
  TITLE     PAS: a multifunctional domain family comes to light
  JOURNAL   Curr Biol 7 (11), R674-R677 (1997)
   PUBMED   9382818
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   9  (residues 1 to 803)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18588748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..803
                     /product="SpoIIE family protein phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=86266
     Region          6..260
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          253..664
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
     Region          676..786
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mnawnaaesa dfrgpldvtr aatavldaqd liigwspaaq rllgylpeei vgqpletlvp
       61 pavkgsgqap eealsgdrel tvrhrngrlv rmaamicpla kvsegsgsqp arvlvaaele
      121 ahrmwesrqa mlhglatqsp vglgiydtdl rltwannayi revglplref lgaradelyp
      181 dgefmtegyp rtldavmhhv idtgepfldl hfvgqqpsdp gpdhvwscsy yrlqdtrgqv
      241 lgvcedafdi tgryqaqqrl nllveagari gttldmtvta reitevavpg fattvtvdlm
      301 qsvlngdepe paggalptlv rvatrsaqag pdgpphsphr veyppgslqy rsmssggmvr
      361 dentivvplr aggtplglvt frrgapmtaf drgeielade lvtrtavcld narrfareht
      421 aaltlqrnll pqhlaspsav dlayrylpsd dragvggdwf dviglsgtrv glvvgdvvgh
      481 glqaaatmgr lrttvralar ldlapdellg rlddlveqta eeqaatvgtd igtddvatgv
      541 tclyavydpv srrctmarag hlppavvdpe ggvsfpdlpa gpplglgglp fesleielpv
      601 gslvalftng lvearnhdvd egldtlgrvl gehrrpldel cdhalaellp dgpatddsal
      661 llvrtrelda gqvaawelpa epaavgkare latgqlrawg ltelsyatel vvselvtnav
      721 rhasgplhlr llrdrtllte vsdtghtsph lrhsasddeg grglfivaql vqrwgtrytp
      781 ygktiwteqa fpprysgvpr par
//
LOCUS       WP_457700109             294 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700109
VERSION     WP_457700109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16006267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..294
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31205
     Region          53..130
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
     Region          167..287
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mpsfgnapdp qpvtgelsvs taslddwhqv aqwaadeewn pgrgdtacfh ptdpagffig
       61 rragqtvsav svvnysdaya flgyylvhpd hrrqglglat wraafphaga rtvgldavpa
      121 qqatyrragf apahetvrya grptgpgtpa pgvvpvtrah ldaladydrr cfpadrrafv
      181 trwltapght alaylrdgai agygvlrpar tghrigplfa dttaaaealf dalaasagpa
      241 deifldvpgp rhaahtlvts rgltpqshtv rmytgpvppa ehertfgvts lelg
//
LOCUS       WP_457700113             177 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700113
VERSION     WP_457700113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 177)
  AUTHORS   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 177)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 177)
  AUTHORS   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..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /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=19345
     Region          87..172
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(106,125..126,143,146,154..155,165,170)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mlmnssttpl alrpdadfgr pptagpgegp plavdrlpdg twqltlhale pisvhrlpsd
       61 evhiilappr eaaageppag rsrpepirid taartvfirg rqldlprlef dllahlvlhp
      121 rraftreqlm aavwpscqss nrtvdvhiar lrrrlgpglr dsistvfgig ykyqpaa
//
LOCUS       WP_457700137             172 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700137
VERSION     WP_457700137.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18933
     Region          11..152
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mksvhtplpa velrvpteed alhwhrafhh pdvmefhgga paelseydel tarqrrhhae
       61 lgfclytlvd padgavigft gaqpwphdwg pageieigwr lgraywgkgy attaaqaale
      121 svrsagvrhv vamvaaaner slavtqrlgm rraetvitpk gqrkaychrl dl
//
LOCUS       WP_457700149             644 aa            linear   BCT 27-JAN-2026
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces nigrescens].
ACCESSION   WP_457700149
VERSION     WP_457700149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..644
                     /product="AMP-dependent synthetase/ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015645 - fatty acid ligase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69087
     Region          44..642
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mshqesaptg sltaptptpa ptltepqktl vdgtvrevyv pplappvrsg slgdlpflna
       61 heapadvvla rkqpsgiwrd itaaefaaev ravakgliah glrpgdrlai marttyewtl
      121 vdfaawaagl vtvplyptss ahqaqwilhd sgaracvveg vdetrlisgl rtelpaldhl
      181 wqfntgavsq lvsagrdvpd eavdqrraat gpyalatliy tsgttgrpkg calthanffa
      241 eadnavellh pvfksvseep aatllflpls hvfgrmvavg clrarvrlgh apsirtddll
      301 adlagfrptf llaipyvlek vfntgratae kmgraasfdr avriarsyge aveakehgtg
      361 pgpgvalkga rklydplvyr riraalggkv ryvlcggspl grrlaafytg agieifegyg
      421 ltettaattv tpplrprigt vgwplpgtav riaddgeili hgdhvfsgyw dadlgaarpv
      481 tdrgwfatgd lgaldpdgyl sitgrkkeii vttggknvap apledrlrsh plvgqcmvig
      541 dnrpyitali tlepdglahw rqmnkkqdlp seqlvrdehl ladlqravdd anelvsraes
      601 irrfavlpvd fteetghltp slklrraava rdfaediagl yesg
//
LOCUS       WP_457700153             268 aa            linear   BCT 27-JAN-2026
DEFINITION  C40 family peptidase [Streptomyces nigrescens].
ACCESSION   WP_457700153
VERSION     WP_457700153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..268
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27568
     Region          61..267
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mspnalipsh rkprrpsass ralragvtgg fltlavtgat vpanaaekpv setqemptit
       61 talatsaars adtaeqvafn yerqalqdsa fsqaakaaek hkseavkkak aaakkkaeea
      121 rkaeeaaqar asrsserstl sapssstatg tgstatlvsf lkaqlgkayv lgstgpssyd
      181 csgltqaafs qigidlprvs qdqstqgtqv gldnlqvgdi lywgsagsay hvgvyvgdgn
      241 figaqnsstg iverpldydm ptgavrvl
//
LOCUS       WP_457700155             448 aa            linear   BCT 27-JAN-2026
DEFINITION  geranylgeranyl reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700155
VERSION     WP_457700155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Isobe,K., Ogawa,T., Hirose,K., Yokoi,T., Yoshimura,T. and Hemmi,H.
  TITLE     Geranylgeranyl reductase and ferredoxin from Methanosarcina
            acetivorans are required for the synthesis of fully reduced
            archaeal membrane lipid in Escherichia coli cells
  JOURNAL   J Bacteriol 196 (2), 417-423 (2014)
   PUBMED   24214941
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Murakami,M., Shibuya,K., Nakayama,T., Nishino,T., Yoshimura,T. and
            Hemmi,H.
  TITLE     Geranylgeranyl reductase involved in the biosynthesis of archaeal
            membrane lipids in the hyperthermophilic archaeon Archaeoglobus
            fulgidus
  JOURNAL   FEBS J 274 (3), 805-814 (2007)
   PUBMED   17288560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..448
                     /product="geranylgeranyl reductase family protein"
                     /EC_number="1.3.1.83"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=48535
     Region          32..354
                     /region_name="GG-red-SF"
                     /note="geranylgeranyl reductase family; TIGR02032"
                     /db_xref="CDD:273936"
ORIGIN      
        1 msryrlpgds avtesasvtd svtparsehs advivvgagp agsatayhla ksgldvllle
       61 ktafprekvc gdgltpratk qlvamgidis eeagwlrnkg lriigggsrl qldwpelasy
      121 pdyglvrkrd dfdeqlarqa qkagarlher cnvgapivne ltghitgvha klgeektpvt
      181 fhaplvvaad gnstrlslam glhrredrpm gvavrtyfts prhdddyles wlelwdrrga
      241 qdrllpgygw ifgmgdgtsn vglgilnsss afreldwrei lkawcasmpa dwgytpenmt
      301 gpirgaalpm afnrqphytk glllvgdagg lvnpfngegi ayamesgaia aevivqahar
      361 atyaqrelal qrypkilkdt yggyyslgra fvklignpkv mkiatqrglt hpllmrftlk
      421 mlanltdptg gdamdriing lskvapka
//
LOCUS       WP_457700156             235 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein, partial [Streptomyces
            nigrescens].
ACCESSION   WP_457700156
VERSION     WP_457700156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         <1..235
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          16..234
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 rvygtgagkg sataalnriv rrkpssgvre vhavkgvsft ayrgesigli gsngsgkstl
       61 lkavagllpa ergkvythgq psllgvnaal mndltgeknv ilgglamgmt reqvreryeg
      121 ivdfsginek gdfislpmrt yssgmgsrlr fsiaaakdhd vlmidealat gdrsfqkrsq
      181 arirelrkea gtvflvshnn ksirdtcdrv lwlergellm dgptdevika yeahr
//
LOCUS       WP_457700158            1653 aa            linear   BCT 27-JAN-2026
DEFINITION  NAD-glutamate dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457700158
VERSION     WP_457700158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1653)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1653
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..1653
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=183412
     Region          1..1649
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mqtkldeakt ellaraarvv esspaggkhp vrgldpdtls gylqryylht apedladrdp
       61 vdvvgaalsh yrlaemrpqg tanvrvhtpt veengwtcsh svvevvtddm pflvdsvtne
      121 lsrqgrgihv vihpqvivrr dvtgklievf dsncdahgkt gkgkgtklph davteswihv
      181 emdretdred lqqitadlrr vlsdvreave dwekmraaag riadelpcep vaedlgaqei
      241 eeaqellrwl sadhftflgy reyelttapg eggvdedvlt avpgtglgil radpthreta
      301 dghpvspsfn rlpadaraka rehklliltk ansratvhrp syldyvgvkk fdaegnvvge
      361 rrflglfssa aytesvrrvp virrkvaevl egagfspdsh dgrdllqile typrdelfqt
      421 pvdelrsiat svlylqerrr lrlylrqdey gryysalvyl prdryttgvr lrlidilkee
      481 lggtsvdfta wntesilsrl hfvirvepga slpeltdadv drlesrlvea arswadgfae
      541 alnaevgeer aaellrrygh afpegykadn sprsavadvq hlekltgepg hdfsvslyep
      601 vdagpgerrf kiyrrgepvs lsrvlpglnr lgvevvderp helrcadstv awvydfglrm
      661 pehikgddar erfqdaftav wtgaaesdgf ntlvlragln wrqamvlray akylrqagst
      721 fsqtymedtl snnvhttrll vslfearmsp drqragtelt dglleeldga ldqvaslded
      781 rilrsfltvi katlrtnhyq kdsqgrahsy lsmkldpqai pdlpaprpay eiwvyspkve
      841 gvhlrfgkva rgglrwsdrr edfrteilgl vkaqmvkntv ivpvgakggf vgkqlpdpsq
      901 drdawlaegi acyktfisgl lditdnlvgg evehpkdvvr hdeddtylvv aadkgtatfs
      961 dianevaesy gfwlgdafas ggsagydhkg mgitargawe svkrhfrelg vdtqsedftv
     1021 vgvgdmsgdv fgngmllseh irlvaafdhr hifidpnpda atsyaerrrl felprsswad
     1081 yntellsqgg gihprsaksi qinaqvraal gieagvkkmt padlmqailk apvdllwngg
     1141 igtyvkssae snadvgdksn dtirvngedl rvkavgeggn lgltqlgrie famaggkinn
     1201 daidnsagvd tsdhevniki llnavvadgd mtvkqrnkll aemtdevgal vlrnnyaqnt
     1261 alalalaqss smlnaqqrfm rrlvrdgdld raleflptdr qirerlnagr gltqpetavl
     1321 laytkitvad aliqtglpdd pylqrllhay fpsalhdrfp eqvdghalrr eivttvlvnd
     1381 tvntggtsfl hrmreetgas leevvrahta araifrlgqv wddvealdnv vaadvqtrir
     1441 lhsrrlverg trwllnnrpq plelsetigf fadrvsqvws elpkllqggd lewfqailee
     1501 ltdagvpeql avqvsgfssv fpaldivava drldkepldv aevyydlgdr lrinqlldri
     1561 lelprndrwq smarasired lfaahaalta dvlsvgngss tpeqrfkawe qanaailsra
     1621 ratleeihgs egfdlanlsv amrtmrtllr trn
//
LOCUS       WP_457700162             207 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700162
VERSION     WP_457700162.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..207
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22629
     Region          4..181
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
ORIGIN      
        1 mkpvtltter lvlrpfepsd aptvhaacqe pdiprwtsvp spygvadaeq fvgtavpagw
       61 rddtayhfav vtradgtlag amglvrldrl rtperqaelg ywaakeqrgr gytveaarav
      121 lrwafrdlgv ermewraeag nepsravark lgfrmegtlr aklvhegtrr dvwigsllps
      181 dlaeepgpyg sggpaspdst pylpyps
//
LOCUS       WP_457700164             408 aa            linear   BCT 27-JAN-2026
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700164
VERSION     WP_457700164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44837
     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 mtavtqpaal pptvtglsrd darrialraq gllgapdrra gvrgvlrhlg avqldtisvl
       61 arshelvpya rlgavgrpav eaaywataps daptarphsf eywshaacil pieewphfaf
      121 rrrarrakgh rwhvmedser scaavldrlt adgplttsdl gggrnggeww dwsetkiave
      181 wlldtgqvvc tqrrawkrvy dlaeravpda llhddlddae clrrlvaqag tamgvatrad
      241 ladyhrlkae qvdavvadsg lvpvevegwg kpawadpaal aapprgrhrt tllspfdsli
      301 wdrprterif gfthrleayv prpkrihgyf ampllaggrl vgrvdpareg ttliarqvsm
      361 qgpkavtpma qalreaatwv gcdsvrvdrc ddrkladalr selthmsd
//
LOCUS       WP_457700168             242 aa            linear   BCT 27-JAN-2026
DEFINITION  ComF family protein [Streptomyces nigrescens].
ACCESSION   WP_457700168
VERSION     WP_457700168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=24695
     Region          1..201
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mqgvwrelag lvlpvdcagc grprtelcae crrvlarngr garrvrpwpe pvglprvwag
       61 apyadevrav llahkergal rlagplgavl agavrglrag ggplllvpvp sarrsvagrg
      121 hdpvrriala aagelrragp garvlavlrq rravadqagl sarqrlanvt galevragag
      181 rlltgraavl vddlvttgat laeaaravta aggrvagaav vaapsgafei dgarievlpr
      241 gq
//
LOCUS       WP_457700182             220 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457700182
VERSION     WP_457700182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Koonin,E.V. and Tatusov,R.L.
  TITLE     Computer analysis of bacterial haloacid dehalogenases defines a
            large superfamily of hydrolases with diverse specificity.
            Application of an iterative approach to database search
  JOURNAL   J Mol Biol 244 (1), 125-132 (1994)
   PUBMED   7966317
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..220
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23833
     Region          6..213
                     /region_name="Gph"
                     /note="Phosphoglycolate phosphatase, HAD superfamily
                     [Energy production and conversion]; COG0546"
                     /db_xref="CDD:440312"
ORIGIN      
        1 mgkhathivw dwngtlfhdi davigatnsa faeiglepit letyrelycv pvprfyerlm
       61 grlpteaewl vmdeafhrhy sthrlgcela egvhallegw qsagrsqsil smyghdelip
      121 ivrdfgiesr fvrvdgrtgp sggtksahmv rhlaamesvd partivigda vddavaaqda
      181 gayavlytgg shsrgsleta gvpvvdtlae avemageivf
//
LOCUS       WP_457700190             260 aa            linear   BCT 27-JAN-2026
DEFINITION  sporulation protein [Streptomyces nigrescens].
ACCESSION   WP_457700190
VERSION     WP_457700190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Sonoda,Y., Mizutani,K. and Mikami,B.
  TITLE     Structure of Spo0M, a sporulation-control protein from Bacillus
            subtilis
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 12), 1488-1497 (2015)
   PUBMED   26625291
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Han,W.D., Kawamoto,S., Hosoya,Y., Fujita,M., Sadaie,Y., Suzuki,K.,
            Ohashi,Y., Kawamura,F. and Ochi,K.
  TITLE     A novel sporulation-control gene (spo0M) of Bacillus subtilis with
            a sigmaH-regulated promoter
  JOURNAL   Gene 217 (1-2), 31-40 (1998)
   PUBMED   9795118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="sporulation protein"
                     /GO_process="GO:0030435 - sporulation resulting in
                     formation of a cellular spore [Evidence IEA]"
                     /calculated_mol_wt=28334
     Region          1..255
                     /region_name="Spo0M"
                     /note="Stage 0 sporulation-control protein Spo0M [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG4326"
                     /db_xref="CDD:443467"
ORIGIN      
        1 mgfkkllasl gaggasvetv lfeenvvpgg vvqgevriqg gsvaqeiqgl svglqarvev
       61 esgdeeykrn veftkvqlgg eftvqpgaah tvpfgleipw etpittflgt hlhgmsvgvt
      121 telaiaravd sgdldpvnvh plpaqqaild afgrlgfrfk aadleqgrir gtrqklpfyq
      181 eieffapqqy rglnqvelsf vaderemdvv lemdkkpglf segsdtyrsf tvglndyegt
      241 dwagylnqwl aevggkrnwl
//
LOCUS       WP_457700193             167 aa            linear   BCT 27-JAN-2026
DEFINITION  HNH endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457700193
VERSION     WP_457700193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..167
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18533
     Region          66..122
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mretlvlnas feplstvslr ravvlvmqdk avvehahpgl riraasvdlp vpqvirlsry
       61 vrvpfrrrap wsrrgvlvrd qhrcaycgrr attvdhvvpr shgggdtwln tvascaednh
      121 rkadrtpeqa gmqllrrpfe ptpadallst lgvsvrdglp ewlpvpa
//
LOCUS       WP_457700195             270 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700195
VERSION     WP_457700195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29352
     Region          8..258
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 mgdnalmsdv lelvdvsvvr egralvdqvs wsvkegerwv ilgpngagkt tllnlassyl
       61 fpssgsasil geqlgkvdvf dlrprigiag ialadklprs qtvlqtvlta aygmtaswqe
      121 nydeideqra rafldrlgmt ayldrkfgtl segerkrtli arammtdpel llldepaagl
      181 dlggredlvr rlgrlardpy apsmvmvthh veeiapgfth vlmirqgkvl aagpldlelt
      241 ssnlshcfgl plvverngnd rwtaqglplt
//
LOCUS       WP_457700199              81 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457700199
VERSION     WP_457700199.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..81
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=7597
     Region          30..80
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mntakkaalv lavtglalga aagsafatpg aqadgkatns pgigsgnlaq vpvhvpvnat
       61 gntanvigvl nptfdntssn n
//
LOCUS       WP_457700200              80 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457700200
VERSION     WP_457700200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..80
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=7594
     Region          25..79
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mknikramav tvaasglala gagvasahtp qaqgatvhsp givsgnnvqa pvhvpvnacg
       61 itatvigaln ptfgspclnp
//
LOCUS       WP_457700202             381 aa            linear   BCT 27-JAN-2026
DEFINITION  GAF domain-containing sensor histidine kinase [Streptomyces
            nigrescens].
ACCESSION   WP_457700202
VERSION     WP_457700202.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   4  (residues 1 to 381)
  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   5  (residues 1 to 381)
  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 381)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12128685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..381
                     /product="GAF domain-containing 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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40174
     Region          22..166
                     /region_name="GAF_2"
                     /note="GAF domain; pfam13185"
                     /db_xref="CDD:433019"
     Region          154..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtngpgagip avstailams rhlevrdvlk tivasarell daeyaalgvp ddhggfaqfv
       61 vdgvsaeqwk aigplprqhg ilaamlhnat perladvred prfggwpaah pdmsdflglp
      121 vadgdeilga lflankrcpk paggcgftee derllgilaq haaialtnar lyersrelti
      181 agerarlahe lhdavaqklf slrltaqaat alvdrdpara kdelhqvaal aaeaadelra
      241 avielrpaal dedglvatlr sqaqvldrah sarvtfaahs vralpasqee avlrvaqeal
      301 hnalrhsgae tvevtltrng qgallriadd gcgfdprtvr ragrhlglvs mhdraggvgg
      361 kltvesepgk gtavemevpg g
//
LOCUS       WP_457700204             292 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457700204
VERSION     WP_457700204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=29547
     Region          1..269
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mpvaiitgas kglgralaaa lagrgwdlvv darsagplee aarelraagr gagarvvalp
       61 gdvadaghra alvaaagelg gldllvnnas algaeplvrl adhpldglrt alevnvvapl
      121 gliqqalpll rvssylasye eftpqaeraf rgggdengea ydshpytrna rnaglsdspp
      181 yigtggaila issdaaveay ptwggygaak aaldqqsavl aveepglrvw wvdpgdmrtd
      241 lyaaavpded algrplpgtv vpallrlldg aapsgrytaa svaaapgevn ar
//
LOCUS       WP_457700213             172 aa            linear   BCT 27-JAN-2026
DEFINITION  SixA phosphatase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700213
VERSION     WP_457700213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..172
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18754
     Region          9..170
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 msadtprriv llrhakaews dssdherpla drgrkdapva grwlagagit pdltlcstsv
       61 rtretwklav helpqrpktv yeeriyeasl geliallnet sdevkdlmlv ghnpgvhala
      121 dalsgeadgd llprmnrsgf ptasvavlaf ngswksvehg vgrlvaywtp he
//
LOCUS       WP_457700217             440 aa            linear   BCT 27-JAN-2026
DEFINITION  CynX/NimT family MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457700217
VERSION     WP_457700217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Law,C.J., Maloney,P.C. and Wang,D.N.
  TITLE     Ins and outs of major facilitator superfamily antiporters
  JOURNAL   Annu Rev Microbiol 62, 289-305 (2008)
   PUBMED   18537473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..440
                     /product="CynX/NimT family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44355
     Region          53..432
                     /region_name="MFS_NIMT_CynX_like"
                     /note="2-nitroimidazole and cyanate transporters and
                     similar proteins of the Major Facilitator Superfamily of
                     transporters; cd17339"
                     /db_xref="CDD:340897"
     Site            order(63..64,67..68,71,103,153..154,156..158,161,180,
                     183..184,187,264,267..268,271..273,276,303,307,356,360,
                     364,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 madddlatlg paagarttst drpadgpehp qpgpgqaapa agptgrrlpr lviaglvlaa
       61 lnlrpaitsl galleevrtg lgmsgtvagl ltsvpalcfa afgiaaprla rrwgpgaivc
      121 agmaaitvgv vvrpyaggtg gflaasalal agiavsnvlm pvvikswfpg rvgsmtglys
      181 malalgtsla aaltvpmtea lggswrtgls vwaalaavav lawvvvvrqr raiagpatsa
      241 aarppeapvr itssptawal avffglqata ayitmgwmpq ifrdagvsag tagvllavtm
      301 amgvplsfvl prlaarmrhq gplvvllglc glagytglwl apaagawvwa llmgisncaf
      361 plaltmigmr stssagvvkl safaqsvgyl isipgpllvg tlyqhsggwg lpialmaglm
      421 vpqivvgvla grdrriedea
//
LOCUS       WP_457700219             226 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700219
VERSION     WP_457700219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..226
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24211
     Region          7..215
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mpltsprrsa ladqviaqlr aqitsgewpv gsriptepal veqlgvarnt vreavralah
       61 nglldirqgs gtyvvatsel agvmnrrfaa aeprhvaelr saleasaarl aaerrtpqdl
      121 rqidallerr erawesgaae afveadatlh maivsashne vlaeiyadlg gvlrdflrad
      181 vgeelrpeah mdharlveai ragdgdraaa easahpfgcr ltvpgp
//
LOCUS       WP_457700222             517 aa            linear   BCT 27-JAN-2026
DEFINITION  TldD/PmbA family protein [Streptomyces nigrescens].
ACCESSION   WP_457700222
VERSION     WP_457700222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..517
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54942
     Region          33..508
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mpaphavdet flalplrala daalararal gadhadfrle rirsaswrlr dartsgtsdt
       61 tdlgyavrvv hggawgfasg vdltmdaaar vaaqavamak lsakviraag sagsapsgsw
      121 grvelaaepa hpdrtwvssy einpfdvpda dktgllaews trllaaegva hadaalltvq
      181 enkfyadtag tsttqqrvrl hpqltavavd pasgdfdsmr tlappvgrgw eylagghydw
      241 dgelaripeh laekmraptv eagtydlvvd psnlwltihe sighateldr algyeaayag
      301 tsfatfdqlg klaygsgimh vtgdrtaehg latigyddeg vaaqswdlik dgtlvgyqld
      361 rriaqltgft rsngcayads pghvpvqrma nvslqpaadg psteelisgv ergiyvvgdr
      421 swsidmqryn fqftqqraha irngrlcgqv rdvayqattt dfwgsmtavg gpetyvlgga
      481 fncgkaqpgq vaavshgcps alfqgvniln ttqeagr
//
LOCUS       WP_457700228             137 aa            linear   BCT 27-JAN-2026
DEFINITION  NfeD family protein [Streptomyces nigrescens].
ACCESSION   WP_457700228
VERSION     WP_457700228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..137
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13697
     Region          1..136
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mwwliaavgl giplvvtamp efgmlavgav agavtagigg gtvlqfivfa avsvaliavv
       61 rpianrhrgq spqlasgvda lkgrsatvle rvdgggggri klagevwsar aldgsqvyep
      121 gqqvdvveie gatavvi
//
LOCUS       WP_457700234             411 aa            linear   BCT 27-JAN-2026
DEFINITION  acetate kinase [Streptomyces nigrescens].
ACCESSION   WP_457700234
VERSION     WP_457700234.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011301
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..411
                     /product="acetate kinase"
                     /EC_number="2.7.2.1"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008776 - acetate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006085 - acetyl-CoA biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43287
     Region          8..411
                     /region_name="PRK00180"
                     /note="acetate kinase A/propionate kinase 2; Reviewed"
                     /db_xref="CDD:234680"
ORIGIN      
        1 mtatatrvlv lnsgsssvky qlldmnpesv sgsaagtrla vglverigee tsrlahtpla
       61 tggdkreteg piadheaalk avaaelsadg lgldspqlaa ighrvvhggl kftaptvidd
      121 avlkeierlv pvaplhnpan itgirtaqal rpdlpqvavf dtafhttmpe yaaryaidve
      181 tadahrirry gfhgtshayv srktaellgk dpsevnvivl hlgngasasa vaggrcvdts
      241 mgltpleglv mgtrsgdidp avtfhlkrva gmseddvdvl lnkksglvgl cgdndmreir
      301 rridegdera rlafdiyihr lkkyigayta vlgrvdavaf tagvgenaap vraaaiagle
      361 emglavdadl navrsgeprl ispeyarvav avvptdeele iaqqtyalvn a
//
LOCUS       WP_457700243             218 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700243
VERSION     WP_457700243.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23458
     Region          28..71
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          84..202
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mvarmhhsas prkgrtgrpr saetdqailc atraalvdlg wgrltmsdva aragvakttl
       61 yrrwanknel vvdavavlfd elelpdrgsl rsdiegvvlq fgallarpet ktalmavvae
      121 sttdealrer irsaivdrqk rlvllgrsra qargelppdt pgeegeraaa rnmdlifdvi
      181 agaivhrtlv sgepvdaawg rdftalflsg lgglgehd
//
LOCUS       WP_457700248             240 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457700248
VERSION     WP_457700248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  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 240)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..240
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25890
     Region          13..217
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 msmpptpgnt papkilvvdd epevraaved glavegytvr gaadglaals evaawqpdal
       61 vldvlmpvld glavcrrlra lddrtpilvl taldsvserv dgldagaddy lvkpfaldel
      121 varvrallrr asttavedtq lsfgdlvvdp vtrtghragr plefsrtewa llellllhpg
      181 qvlprevile rvwgrdfgpd snslavyigy lrrkleagge prlvhtvhgv gyrldhaegv
//
LOCUS       WP_457700247             386 aa            linear   BCT 27-JAN-2026
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Streptomyces nigrescens].
ACCESSION   WP_457700247
VERSION     WP_457700247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 386)
  AUTHORS   Davies,G.J., Gloster,T.M. and Henrissat,B.
  TITLE     Recent structural insights into the expanding world of
            carbohydrate-active enzymes
  JOURNAL   Curr Opin Struct Biol 15 (6), 637-645 (2005)
   PUBMED   16263268
REFERENCE   3  (residues 1 to 386)
  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 386)
  AUTHORS   van Heijenoort,J.
  TITLE     Recent advances in the formation of the bacterial peptidoglycan
            monomer unit
  JOURNAL   Nat Prod Rep 18 (5), 503-519 (2001)
   PUBMED   11699883
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Ha,S., Gross,B. and Walker,S.
  TITLE     E. Coli MurG: a paradigm for a superfamily of glycosyltransferases
  JOURNAL   Curr Drug Targets Infect Disord 1 (2), 201-213 (2001)
   PUBMED   12455415
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="UDP-N-acetylglucosamine--N-acetylmuramyl-
                     (pentapeptide) pyrophosphoryl-undecaprenol
                     N-acetylglucosamine transferase"
                     /EC_number="2.4.1.227"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0050511 -
                     undecaprenyldiphospho-muramoylpentapeptide
                     beta-N-acetylglucosaminyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051991 -
                     UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-
                     glutamyl-meso-2,
                     6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol
                     4-beta-N-acetylglucosaminlytransferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0030259 - obsolete lipid glycosylation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=40017
     Region          4..352
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 mrtplsvvig aggtgghiyp glaladalrr avpeavisfv gtergletrl ipqagyrlht
       61 vdmipfdpal garryllpaa llrsggqcra ilkeqnaqva vgmggypsap vivgarmagl
      121 pslihesnav pgrankfaar ltphlalafd rsrehlagge raetvgmplv gplaeldrgk
      181 lrptarrefg vpdgarlllf nggslgaarl teaavglagr yrtrtdlrll iktgpaalee
      241 trarlaangg davaeavpyl drmdlaysaa dlvvcragsa tvaelatigm pavlvpypha
      301 pgdhqthnar vlsdagaall lpdpetsder ldalvtplld dpgrlaamga aadpgthara
      361 adllaakala laghplahhl rmketa
//
LOCUS       WP_457700250             465 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457700250
VERSION     WP_457700250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..465
                     /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=49604
     Region          104..464
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtgtrglgar wrrrrplrar lalaassava lvavgvcaaa ffvidhqmtr qlelnltqta
       61 tqairerqnw gptpsdtlcq ypaspctqiv psdpakdpre ryvlpvsdat rqvadgrraa
      121 fyseltvagq pvrmlttrlg vkdeavqvaq rsatvdrgve qaawalsgvg gagvllaaal
      181 gywvsrtgla pvarltaiae riaatrdarh rielpagpta redeitrlat sfntmlgele
      241 qsvtaqrrlv adashelrtp ltalrtnael laradrltga qrdrasaalg rqlrevttlv
      301 ndlielarde epqplveqvr paallehavg aarehwpelt fttaidpaaa gtvipgvppr
      361 larllsnlld naakfsppgg pvetelacva galeltvrdh gpgieagdlp hvfdrfyrak
      421 aaralpgsgl glamarqiar ahdadltaeq apgggalfrl riplp
//
LOCUS       WP_457700252             566 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA mutase large subunit family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700252
VERSION     WP_457700252.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Banerjee,R. and Vlasie,M.
  TITLE     Controlling the reactivity of radical intermediates by coenzyme
            B(12)-dependent methylmalonyl-CoA mutase
  JOURNAL   Biochem Soc Trans 30 (4), 621-624 (2002)
   PUBMED   12196149
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Marsh,E.N.
  TITLE     Coenzyme B12 (cobalamin)-dependent enzymes
  JOURNAL   Essays Biochem 34, 139-154 (1999)
   PUBMED   10730193
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Ludwig,M.L. and Matthews,R.G.
  TITLE     Structure-based perspectives on B12-dependent enzymes
  JOURNAL   Annu Rev Biochem 66, 269-313 (1997)
   PUBMED   9242908
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..566
                     /product="acyl-CoA mutase large subunit family protein"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0016866 - intramolecular transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_process="GO:0006637 - acyl-CoA metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61984
     Region          18..564
                     /region_name="Sbm"
                     /note="Methylmalonyl-CoA mutase, N-terminal domain/subunit
                     [Lipid transport and metabolism]; COG1884"
                     /db_xref="CDD:441488"
ORIGIN      
        1 mdadaidegr rrwqarydsa rkrdadfttl sgdpvepayg prpgdsvegf erigwpgefp
       61 ftrglyptgy rgrtwtirqf agfgnaeqtn erykmilkag ggglsvafdm ptlmgrdsdd
      121 prslgevghc gvaidsaadm evlfrdiplg dvttsmtisg pavpvfcmyl vaaerqgidp
      181 gvlngtlqtd ifkeyiaqke wlfqpephlr ligdlmehca rgipaykpls vsgyhireag
      241 ataaqelayt ladgfgyvel glsrgldvnt fapglsfffd ahldffeeia kfraarriwa
      301 rwmrdvygat sekaqwlrfh tqtagvslta qqpynnvvrt avealaavlg gtnslhtnal
      361 detlalpseq aaeialrtqq vlmeetgvan vadplggswf iesltdriea daekifdqik
      421 ergrravpng ehpigpitsg ilrgiedgwf tgeiaesafr yqqalekgdk kvvgvnchhg
      481 svtgdleilr vshevereqv ralgtrkaar ddarvqaalk tmleaarggs nmiepmleav
      541 raeatlgeic galrdewgiy tepagf
//
LOCUS       WP_457700255             456 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457700255
VERSION     WP_457700255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..456
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45926
     Region          45..424
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(55..56,59..60,63,95,146..147,149..151,154,175,
                     178..179,182,261,264..265,268..270,273,296,300,353..354,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpspsgpaps grlpacpatd aadagshggp arpdgyravf avpefrfvfa ahllsslgvv
       61 vceialsvlv frltasplls altfalgllp yvvggtllsa vadrcparrv lvgcdvlcal
      121 aaagmvvpgt pvavllvlrc vlaaiapvfa gtraatlgei lgagelfvlg rsvirivnqs
      181 aqlagfaagg lllavvspea vlaltagtfl gsalllrlgt larpardgvr gaergallaa
      241 slggirrlla drrvrallll twlppafvvi peallipyag llgigpagmg lllcampvga
      301 vvaeslvgtf lgprararlt fpmgvfavlp slgfaaqpsl gwavlllvlt gtgisynfgv
      361 drwfvaavpd ellgqamtvm qagrmtvmgl amgvagvaae yaplrvvmpa agvlgavsvl
      421 avifevrrta rgpagadrac agavrgpdgp vpetgk
//
LOCUS       WP_457700269             238 aa            linear   BCT 27-JAN-2026
DEFINITION  response regulator transcription factor [Streptomyces nigrescens].
ACCESSION   WP_457700269
VERSION     WP_457700269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  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 238)
  AUTHORS   Itou,H. and Tanaka,I.
  TITLE     The OmpR-family of proteins: insight into the tertiary structure
            and functions of two-component regulator proteins
  JOURNAL   J Biochem 129 (3), 343-350 (2001)
   PUBMED   11226872
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..238
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25712
     Region          18..226
                     /region_name="OmpR"
                     /note="DNA-binding response regulator, OmpR family,
                     contains REC and winged-helix (wHTH) domain [Signal
                     transduction mechanisms, Transcription]; COG0745"
                     /db_xref="CDD:440508"
ORIGIN      
        1 mhphvtqhrp pgstahrpyr llivedekrl alslakglta egyavdvvhd glaglhqase
       61 esydlvvldi mlpgmngyrv cgalraaghe vpilmltakd geydeaegld tgaddyltkp
      121 fsyvvlvarv kallrrrgrs appvlqvgsl aidqgarrve rdgvevtltt kefavleqla
      181 vragevvska eilehvwdfa yegdvniiev yvsalrrklg aghivtvrga gyrlvagg
//
LOCUS       WP_457700272             760 aa            linear   BCT 27-JAN-2026
DEFINITION  (Fe-S)-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700272
VERSION     WP_457700272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..760
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=83229
     Region          233..739
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mqlaaiivsl vliavavalf grallqiyrq mrlgqpvpag trtdapaqrt vtvakeflgh
       61 trmnrwgvvg vahwfvavgf ftllltivna igqlfqadwl ipviggwlpw emfveamgtm
      121 ttvgilaliv irqlnrpgga grksrfagsn tgqayfvetv ilivgicivt lhalegaqhg
      181 vdhyepaffv syplvaffkg mslgtlqnlt yffaalkiat sfiwmitvsl ktdmgvawhr
      241 flafpniwfk readgdvalg alqpmtsagk pidfedpged dqfgvsqveh fswkglldfs
      301 tctecgrcqs qcpawntgkp lspkllimal rdhahakapy llagggkdme gneqataeql
      361 advpaaalae aerpligtle engvidpdvl wscttcgacv eqcpvdiehi dhivdmrryq
      421 vmiessfpse agtmlknlek kgnpwglakk qrlawtkevd fevpvvgqdv edlteveyly
      481 wvgcagaled rakkttkafa ellhiagvkf aimggdekct gdsprrlgne flfqqlgaen
      541 vatlnaafge slnedggvde stkkpksskk ivatcphcfn tianeypqlg geyevihhtq
      601 llqhlvdegk ltpvtpvegl ityhdpcylg rhnkvytppr eiiakvpglr neemhrhker
      661 gfccgaggar mwmeerigkr innervdeal slnpdivsta cpfclvmltd svngkkndgk
      721 akesiqvvdv aqllldsvkt pvdpagdeep edapepepvk
//
LOCUS       WP_457700283             198 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457700283
VERSION     WP_457700283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..198
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=20372
     Region          23..101
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 msielpgevv wimdlmglew pdidedelra waghvrefgq nlaeghsgld stlngladay
       61 egasydalls rwnqvsgehh taltnccevl atalevaatg vvvakgvvia qlvitavema
      121 aaaaaavatl giaaaaeaaa ieigrriire viqeiedvli aelvsmaiep fqaeiekavs
      181 glvfkgvdaa lgaaggaa
//
LOCUS       WP_457700303             511 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457700303
VERSION     WP_457700303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..511
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52482
     Region          25..463
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,282,285..286,289..291,294,322,326,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msepsapgav rlasaqgrwv lltavlgsgm alldgtvvnv alprigedlh adlavlqwtv
       61 taylltlssl illggalgdr fgrrrmfvig vvwfavasll cglaphagvl iaaralqgvg
      121 gallmpgsla liqavlhpdd rargvgawsg lggvaaavgp figgwlvdga gwrwvfflnv
      181 plaavcvpva lrhvpetrer garahrgfdv rgavlgalal agvtyaliaa pdggtgpgvl
      241 fpavagvllg vlfvqverrr adpmlppaif rirqfsaina vtvcvyaafs gffflsvlql
      301 qvvvgysalq agtallpttv lmlllsarsg elgqrigpri pltvgpllca aglllmmrvg
      361 vgasyfadvl palvvlgagm vtlvapltat vlasvdvdra glasginnaa araaglmava
      421 alpllagfgp eayrsadafg aaflramplc agvlvagali awltvrtdal rpepgaeepc
      481 rakttfhcgv nappldpget reddeqrepe r
//
LOCUS       WP_457700309             251 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700309
VERSION     WP_457700309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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 251)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26826
     Region          55..251
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mstllsdtal ifgryarqtl rsklqmlfgv lvpllyllff gplltdlpls ssgsswqvlv
       61 pglllqlalf gasfcgfgii iekqygvver mrvtpvsrla lllgrvlrda llfvfqavll
      121 vlaalamglr aplpgiligf afvavltval aslsyalaln vstpqefgpv inavtmpsml
      181 lsglmlpmal gpkwldvlsh fmpfrylvda vraafvgsya ssamlygalv avafaalsvt
      241 yctrafrrsa a
//
LOCUS       WP_457700305             190 aa            linear   BCT 27-JAN-2026
DEFINITION  Uma2 family endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457700305
VERSION     WP_457700305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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 190)
  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 10529412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..190
                     /product="Uma2 family endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20491
     Region          15..180
                     /region_name="Uma2"
                     /note="Putative restriction endonuclease; pfam05685"
                     /db_xref="CDD:428585"
     Site            order(29,45,88,116..117,129)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411709"
ORIGIN      
        1 mahepmptqd dtllegflal etptgfrael iegeiavtpp pdgdhedyls tvfeqvmrms
       61 atamqfsghk glvlshaagq padhvipdat iapralrlfr gappwmpsgg vamvvevtss
      121 kpqkdrvakr hgyaragipl yllvdrdksa vtlfsepege dyltthtapf gkplplpapf
      181 sfdletadfl
//
LOCUS       WP_457700313             213 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700313
VERSION     WP_457700313.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23625
     Region          7..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maeglrerkk rqtrqyisdv atglflargf davtiaeiae aaevsvntvy nyfpakedlf
       61 fdrskgvvgr lsrfvrgraa gesaaaavlr elreeveavs prvglmegyd qfmrvvhgap
      121 tlkarlwymq qevhtnleet lreetgaaag dplpglmagq igwvhqslmg withemldgr
      181 kpdeasreal vlldemeell gekvlnyavr tad
//
LOCUS       WP_457700311             260 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700311
VERSION     WP_457700311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27075
     Region          4..250
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mpvlsasgla rtftskrgav eavrgidlta ergeilgflg pngagktttl rmlttllapt
       61 ggaatvagcd lvrdpagvrr asgyvaqsgg vdphvsvree lvtqarlyrl gkaeaharte
      121 elaaglgldg lldrrtatls ggqrrrldia mglthrpqvl fldepttgld pgsradlwel
      181 vrrvrdghgt tvfltthyld eadaladrlv ivdkgvvvae gtpealkrah agspdaslqd
      241 tflaitgrga tphgpapvav
//
LOCUS       WP_457700315             282 aa            linear   BCT 27-JAN-2026
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700315
VERSION     WP_457700315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..282
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - (3S)-3-hydroxyacyl-CoA
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=29835
     Region          3..281
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 makklaviga glmgsgiaqv saqagwdvvl rdvtdealar gkggieasye kfvakgklaa
       61 sdaeqalari ttttdleava dadivveavf erieikreif qaldklvkde avlasntsai
      121 pitkiaaats rpervvgahf fspvpmmqlc elvrgyktsd etlatarqfa esvgktcvvv
      181 nrdvagfvtt rlisalvvea aklyesgvas aedidtackl gfghamgpla tadltgvdil
      241 lhatdniyte sqdekfappe imrrmvdagd igrksgqgfy eh
//
LOCUS       WP_457700323             347 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457700323
VERSION     WP_457700323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085931
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..347
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36438
     Region          1..>42
                     /region_name="Flavin_utilizing_monoxygenases"
                     /note="Flavin-utilizing monoxygenases; cd00347"
                     /db_xref="CDD:238209"
     Region          31..347
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mrvgafilaa qfpgqgqgea lhravrsaev aeqaglddvw laehhfvpyg vcpnavtlaa
       61 lllgrtrrig vgtavsvlpt qhpvalgeqa allhltsdgr ftlgvgrggp wvdlevfgsg
      121 laaydhgfpe sldllmrwlr eprvgaqger yafrevavvp rpaealtdpd esgppgppvv
      181 vactspssvr taaerglpml lgmhcgdeek aemvalwrsa aleagrdgde vaaaghvsag
      241 vvqiadarea aaetlikamp gwlqqglgah vtvdgryram rdplaytell cglhpvgppq
      301 lcadrlaats ertgisrfal lvegsgdlaa teenvrrlgt evlpqlg
//
LOCUS       WP_457700327             419 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700327
VERSION     WP_457700327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43614
     Region          2..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mieavgltkr ygaktavynl sfqvrpgtvt gflgpngsgk sttmrmilgl daptsgrati
       61 agrpfrslpn aprqvgalld akavhggrsa rqhllslaqv sgiparrvde vlgvvglqev
      121 agrrskgfsl gmgqrlgiaa allgdpqvll fdepvngldp egilwvrnlm kqlasegrtv
      181 fvsshlmsem altaehlivi grgqlladms vkdfisansa dfarvrtpdt epeqreklta
      241 avgeaggqtt pepdgalrvt glplprisel ahqadvrlwe lsphqaslee aymqmtqgav
      301 dyrstadara glqeapagya pqgyaggpgy ppgqpgvpgq apagvagqgq pnpyaqqdpy
      361 aqqapgaapg pgypppaqgh pyggpepyga phpygqqpaa pmppaapadl ptphhedar
//
LOCUS       WP_457700331             341 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700331
VERSION     WP_457700331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..341
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36652
     Region          2..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mielegltkh ygdkvavdhl tftvrpgivt gflgpngagk sttmrmmldl dnptsgtvri
       61 dgrhyrqlrd pltyigalle aksvhggrsa anhllclaqs ngiprrrvae vldtvglstv
      121 akkrskgfsl gmsqrlgiaa allgdpqvll fdepvngldp egihwirnlm knlagqgrtv
      181 fvsshlmsem altaehlivi gqgrlmadts mkdfihqnsr syvrmrspqq eklldllhde
      241 gidavavgng sleidgvpad rlgelaarhq lvlhelspqq asledafmql taesveyhah
      301 dgdpvpaqsg arpagepqpa gaqpgkpqpt gwgadwqkkg s
//
LOCUS       WP_457700339             211 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700339
VERSION     WP_457700339.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23376
     Region          17..178
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matsssqttr sgarrqrlde nqrraqimta aveeladcgy dglsltrvae ragvskgliw
       61 hyfadkddlm estakaamtt irdriansld laepvpdiir aalrrvaalt vthrgeltal
      121 nrivhnlrhp dgtprltped yeetyqaqes lfrrgqsegt lrdfdtrvma ityqgaidmm
      181 lgylgtsqph inpddyadkl adillagiqr s
//
LOCUS       WP_457700343             246 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            nigrescens].
ACCESSION   WP_457700343
VERSION     WP_457700343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 246)
  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   3  (residues 1 to 246)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..246
                     /product="class I SAM-dependent DNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26978
     Region          10..>141
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtsselwtra iadrydaeet etssaavlgp tlaflaelag dgralefaig tgrvgvplre
       61 cgvpvvgiel sehmaamlrr kidegtlpva igdmattvvp geftlvylvy ntitnlltqd
      121 eqvecfrnaa rhlapggrfv ielgvpplrf lppgqvavpf dvseqhlgfd tfdlveqilv
      181 shhltrdgdd gryrrgnsrh ryawpaeldl mariaglele qrvadwdgap ftqdsakhis
      241 vwrkpt
//
LOCUS       WP_457700365             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700365
VERSION     WP_457700365.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Aravind,L. and Koonin,E.V.
  TITLE     DNA-binding proteins and evolution of transcription regulation in
            the archaea
  JOURNAL   Nucleic Acids Res 27 (23), 4658-4670 (1999)
   PUBMED   10556324
REFERENCE   3  (residues 1 to 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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31474
     Region          7..>52
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          98..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mstdfqtarv llgarlrelr teaglngkdm agrlgwqrsk vsrlehgkqt pshqdlnawa
       61 aaagqddaaa elqgrlqgle tqyrtwrrql anghrprqel avaetartkt irgvevarip
      121 glfqtadyar hlftanaefr rtprdtdaav rariqrqeal yeagrsfrfl lweaalyaqv
      181 cpkevmtaql drlcgligld tvelgiipfs aalqrtpahg fwiyddrlvt vetinaelwl
      241 ddsdsidlya rawtwlhesa vyghsahrli traraqlglt
//
LOCUS       WP_457700393             563 aa            linear   BCT 27-JAN-2026
DEFINITION  purine-cytosine permease family protein [Streptomyces nigrescens].
ACCESSION   WP_457700393
VERSION     WP_457700393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..563
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60257
     Region          27..501
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msaeprviap dsnrrsphae apaeapseav adravnetle dytlrfaprs yrrwtpmvva
       61 ttalggiayl adfsigagig lthgtgnala ailvaavvif vtgfplayyg arynidldli
      121 trgsgfgyyg svltsvifas ftfiffaleg simaqglklg fglplwlgyv istfmviplv
      181 iygmkalskl qvwttpiwll lmvgplvhlv atdpgtvhaf lsytgahggg gvnaasvllg
      241 agvclsliaq igeqvdylrf mppkteqnkr awwtavvmag pgwvvlgalk qaigvflavy
      301 ilaevgpaaa tepiqqftga ftammpswlv iplavvlvvi sqikinvtna ysgslawtns
      361 ftrvtkrypg rmvfvlanla falilmeadm fsflnnilgf ysncaiawiv tvatdiivnk
      421 yllklsphap efrrgmlyav npvgvvafia asglsialyf halgdtlqpy spvaaaviaf
      481 vvtplmavlt kgrfylrrts dgidaplldp dgnpssatfp chvcrqdfer pdltachshg
      541 amvcslclst drtgvhllpa ers
//
LOCUS       WP_457700394              79 aa            linear   BCT 27-JAN-2026
DEFINITION  chaplin [Streptomyces nigrescens].
ACCESSION   WP_457700394
VERSION     WP_457700394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Talbot,N.J.
  TITLE     Aerial morphogenesis: enter the chaplins
  JOURNAL   Curr Biol 13 (18), R696-R698 (2003)
   PUBMED   13678605
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Elliot,M.A., Karoonuthaisiri,N., Huang,J., Bibb,M.J., Cohen,S.N.,
            Kao,C.M. and Buttner,M.J.
  TITLE     The chaplins: a family of hydrophobic cell-surface proteins
            involved in aerial mycelium formation in Streptomyces coelicolor
  JOURNAL   Genes Dev 17 (14), 1727-1740 (2003)
   PUBMED   12832397
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10510227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..79
                     /product="chaplin"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=7444
     Region          <37..76
                     /region_name="ChpA-C"
                     /note="pfam03777"
                     /db_xref="CDD:397719"
ORIGIN      
        1 mahriksalv tagacalvlg gagiagaesg aggaaldspg vvsgnniqip iqipvhlcgn
       61 tvnviglfnp avgdpcltd
//
LOCUS       WP_457700398             242 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700398
VERSION     WP_457700398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18795604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..242
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26609
     Region          20..217
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
     Region          60..155
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mfapqgptfr elavqalssv ergydllapk fdhtpfrtpd rvltpvsral hrlgpfdsgl
       61 dlccgtgagm dvlrqvcrer vtgvdisagm lsvgrtrerv saaaprfewv radaralpfg
      121 pvfdlavsfg afghflprer pglfaqvhsv lrpggrfvfp igaparpgsa gywtllafda
      181 vmrvrnavwr pdfvmyyrtf rlaevraeli qagfevqlqa lpelgrrpdg sprcrlvvat
      241 ra
//
LOCUS       WP_457700406             196 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700406
VERSION     WP_457700406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..196
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21007
     Region          20..66
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          77..188
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mseerqgtri sggprkaqei fdatlellae kgyegltieg vaqrsgvnkt tiyrwwpskg
       61 allgaaliga rqldftppdt gsltgdleal lhtvvtlltt rpasditvsv lgaatqspel
      121 avhirdffad rialeqpvfd ralargelta dtdtmllvdl lagaawvrvv lrrlplekdf
      181 vsravgtvln galtrt
//
LOCUS       WP_457700422             305 aa            linear   BCT 27-JAN-2026
DEFINITION  NADP-dependent oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457700422
VERSION     WP_457700422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10143069
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..305
                     /product="NADP-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30880
     Region          1..303
                     /region_name="MDR_like_2"
                     /note="alcohol dehydrogenase and quinone reductase-like
                     medium chain degydrogenases/reductases; cd05289"
                     /db_xref="CDD:176191"
     Site            order(40..42,45,123,127,148..153,172..173,175,188,
                     211..212,234..235,251..253)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176191"
ORIGIN      
        1 mraiiydtfg gaevlrlgdt gkpvpgpgdv rvkvvtvgvn pldykrrygw veqfypttfp
       61 avpglefagv vdalgdgagd efavgdevfg ttrtgayaey alagdiarkp aalsfeaaaa
      121 lpvagetaqr vldllglttg etlllhgaag avgqvavqla vargatvvgt aspanhdflr
      181 algavsvayg agladrvrav apqgvdavfd aaghdalpvs ialrggttdr ivtiadmnaa
      241 ehgvpfsagg tpseqiragl aaharlaveg rlalpvvetf pladaakaqe lseaghvrgk
      301 lvitv
//
LOCUS       WP_457700451             252 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700451
VERSION     WP_457700451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..252
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27469
     Region          2..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mradarhnrv rillaarqlf vhegpdvple eiasragvgi atlyrrfpsr aaliravavd
       61 vmealyeaat daaqresdpf ealrrfmhta ldskagavmp slfgrveivr lldeerdavg
      121 plgrliarar eagllrddvv tgdivfmilr ltrpmpgggf sqdealahrq ldiyldglrp
      181 paaglrrggl pepaisagwv rhirawmatg rpaatspplp eswrgrsatr arprplsshr
      241 stghrpnngg pq
//
LOCUS       WP_457700464             251 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457700464
VERSION     WP_457700464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25936
     Region          1..245
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnrftnktvl vtggssgmgf aaarrlldeg ayvvitgrdq grldsavarl naaeralavr
       61 advssladld hlmrrvetwr ggldavfana gvgifkpaae iteadfvhtv dvnfkgvfft
      121 vhkalpllrd ggavvinasw tlhrglsvas vysaskaavh nlartlgadl aprgirvnsv
      181 spgyidtamy rganpepgae ardaaqvplg slghpddiaa avaflasdda syitgqdliv
      241 dgglagcvpa a
//
LOCUS       WP_457700466             285 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700466
VERSION     WP_457700466.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30819
     Region          <50..96
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(50,61,64,68..69)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          114..277
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mgisglsvda rrrrsaelre flrsrrarlt pgdvgmpggg grrtpglrre evavlagvgv
       61 swytwleqgr einvsadvld avarvlrldg aerehlylla glnppqsppa areispqllr
      121 vidgwlprpa yvidrhwhla avnraarvvf gygeddhncl vsfftnarfr seichwedaa
      181 raivgqfrad aarypddpef grmaadmcaa spafaevwae hpvgtategt kalahpagge
      241 lvfeytalpl adlpghrlll ytpaagtgte arlaallgvr esgaa
//
LOCUS       WP_457700477             518 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457700477
VERSION     WP_457700477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..518
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54804
     Region          29..484
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mseqslrqae rqqqqgapqd aaqrqpgghv dagdagyqks lksrhinmia iggaigtglf
       61 lgaggrlada gpslavayal cglfaflvvr algelvlhrp ssgafvsyar eflgekgafv
      121 agwmyflnwa ttgiaditav atythywgmf sevpqwvial ialavvlavn lisvkifgel
      181 efwfaivkvg alvvfmligi fllvtqhpva ghspgpslma dhgglfptgt lamllviqgv
      241 vfayasvelv gvtagetaep ekimpkains imwrvavfyv gsvvllamll pwsaysakes
      301 pfvtvlsnvg vpaaggvmnl vvltaamssl nsglystgri lrsmamsgsa prftgvmsrs
      361 qvpyggillt sgicvlgvgl nyvvpseafe ivlnfaaigi lstwamimlc hllfwrkart
      421 geltrpsyrl pgspwtqivt laflafvlvl mwadggagrt tvlslpviva alvggwflvr
      481 grvgtlrdaa arasgehpdt alptqrtent hstesten
//
LOCUS       WP_457700479             245 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700479
VERSION     WP_457700479.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27129
     Region          14..234
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mnlsdsqtag dvprrisame avlnhlrgai ergeyavgdk lpseaelcrr levsrpvlre
       61 alralqtmgl tvsrtgkgtf visdgavadp tfgdyvasdl levrrhveip vagyaavrrt
      121 aedldqlthl lermeqetdt tawvamdslf hlaiaqaarn pvfrrvieei rdalarqsaf
      181 lnelggrreq snrehraive alvdrsehda veamahhlar vettlttivr pqhrtapste
      241 dedha
//
LOCUS       WP_457700487             271 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700487
VERSION     WP_457700487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29548
     Region          3..260
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msshtspaie lrgtskafrt psgalhtavr dldlvverge fvavvgptgc gksttltlvs
       61 gleeptegev lvagepvrgi gdkigfvfqq davfpwrtvl snvmagprfr gvpkaearrr
      121 ardwlarvgl aafedryphq lsggqrkrva laatfvnepe lllmdepfsa ldvqtralms
      181 dellelwsgt gasvvfvthd leesialadk vvvmtagpat vkevfeidlp rprkvesvrl
      241 eprfleiyre iwsslgeevr itrergaadv a
//
LOCUS       WP_457700489             290 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700489
VERSION     WP_457700489.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dean,M., Moitra,K. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Hum Mutat 43 (9), 1162-1182 (2022)
   PUBMED   35642569
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31253
     Region          50..282
                     /region_name="TauC"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, permease component [Inorganic ion transport and
                     metabolism]; COG0600"
                     /db_xref="CDD:440365"
ORIGIN      
        1 mspetvalak spagtgrtdr srararaarn htflvhgtrv lllvgllglw ewlartavid
       61 pfnfsmpski wdqmsqwalh gtpqgslweq iwytlyeall gwvigviggv vlgialgrir
      121 fladvlgpyi kvlnalpriv lapifliwfg lgpaskvasa vvlvffpvff nafqgarevd
      181 rnlvansril gasnrqvtlq vvipsatswi ftslhvsfgf aligaivgey igatkglgll
      241 vsasqgtfna agvyaamvil avvallaegl laflerrlfr wkpadsagdr
//
LOCUS       WP_457700485             586 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457700485
VERSION     WP_457700485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Adam,K. and Hunter,T.
  TITLE     Histidine kinases and the missing phosphoproteome from prokaryotes
            to eukaryotes
  JOURNAL   Lab Invest 98 (2), 233-247 (2018)
   PUBMED   29058706
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Upadhyay,A.A., Fleetwood,A.D., Adebali,O., Finn,R.D. and
            Zhulin,I.B.
  TITLE     Cache Domains That are Homologous to, but Different from PAS
            Domains Comprise the Largest Superfamily of Extracellular Sensors
            in Prokaryotes
  JOURNAL   PLoS Comput Biol 12 (4), e1004862 (2016)
   PUBMED   27049771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Ortet,P., Whitworth,D.E., Santaella,C., Achouak,W. and Barakat,M.
  TITLE     P2CS: updates of the prokaryotic two-component systems database
  JOURNAL   Nucleic Acids Res 43 (Database issue), D536-D541 (2015)
   PUBMED   25324303
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Attwood,P.V.
  TITLE     Histidine kinases from bacteria to humans
  JOURNAL   Biochem Soc Trans 41 (4), 1023-1028 (2013)
   PUBMED   23863173
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Zhang,Z. and Hendrickson,W.A.
  TITLE     Structural characterization of the predominant family of histidine
            kinase sensor domains
  JOURNAL   J Mol Biol 400 (3), 335-353 (2010)
   PUBMED   20435045
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Cache - a signaling domain common to animal Ca(2+)-channel subunits
            and a class of prokaryotic chemotaxis receptors
  JOURNAL   Trends Biochem Sci 25 (11), 535-537 (2000)
   PUBMED   11084361
REFERENCE   7  (residues 1 to 586)
  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   8  (residues 1 to 586)
  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   9  (residues 1 to 586)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20761992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..586
                     /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=62321
     Region          36..174
                     /region_name="sCache_3_2"
                     /note="Single cache domain 3; pfam17203"
                     /db_xref="CDD:435783"
     Region          197..537
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mrirwprrvf aqvltaqval ttgvmvlats lflaplsael ddqamrrals iaqttaadpd
       61 larklvatep dahgpvqaga erirtatgal yivvmdtrgv rwshthpaei grhvstdpsr
      121 tlagrqvrqi dtgtlgrsar akvplrddrg rivgavsvgi aydsvrsrll gtipgllrya
      181 gaalavgvla aivlsrrlrr rthgvafadi salldeream lhgiregvva fdrrgrirlv
      241 ndeagrllgl daqaagrald evlppgrttd vlagrvagtd llavsggrvl vanrmptqdg
      301 gavvtlrdrt elellgreld stqglldalr aqdhehanql htlrgllelg ryekavefvt
      361 evasaqrasa eeiaervpdp llsallvgka aiaaergvsl rvspatqlpd avvdprdlvt
      421 vlgnlldnal daaterrcae pfvevelrae hstavlrvsd tgpgvppelr drifaegwst
      481 kaarplpgeg sptgpvafhr grgiglalvr rlaeryggma rvtaraggga vftvvlpeal
      541 apedgspgrr rtaaagaavr gaprhperpe rtesrkrrpm gsgash
//
LOCUS       WP_457700491             345 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700491
VERSION     WP_457700491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 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   3  (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 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..345
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36480
     Region          28..321
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mrtalkfsaa laaatlaltt ltacggksga tamedkdgki kimvggldkv iylparltqq
       61 lgyfedegvh vtlltepagv qattslvsgd vegvvgfydh tldlqvkgkq vesvvqlaha
      121 pgevevvsnk aageltsptd fkgkklgvtg lgsstdfltk ylavkngvqt neftpvavga
      181 gqtfisalqq gsieggmttd ptvaqivdkn lgkvlidmrt pegsqkalgg pypssslymn
      241 tdwvnshket vrklanafvk tlkwmsthtp eqiaakmpsd yaqggkelya raikdtlpmf
      301 tedgvmpadg patvervlka fnpnlknatv dlkktyttef vkksg
//
LOCUS       WP_457700493             354 aa            linear   BCT 27-JAN-2026
DEFINITION  trypsin-like serine peptidase [Streptomyces nigrescens].
ACCESSION   WP_457700493
VERSION     WP_457700493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Families and clans of serine peptidases
  JOURNAL   Arch Biochem Biophys 318 (2), 247-250 (1995)
   PUBMED   7733651
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007588
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..354
                     /product="trypsin-like serine 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=37900
     Region          133..350
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mhsrrrspva agpeqvfsdl revaarvkdg lsweipesle elsaeelpag qiaqfaqqer
       61 trvlsagvsg leklaegrad eidddesfgm eaivllegrp ailvqnhdfa pqqgdwavld
      121 ghraairasl srvgrvelsg hlsldwlgta flvgpdvvmt nrhvaaefar gdgtgwtfqq
      181 gigarldmge eyggdmgggg paydvvevlg ihedvdlall rvappaggga lpaplavaad
      241 apadlpgrpv ycvgypaydg rrnepesmrr ifmdiynvkr lqpgtatelv pdrnvikhdc
      301 stlggnsgsp vidltdhrvl glhfggrygf gnfavplwql vddpllgrae infv
//
LOCUS       WP_457700502             298 aa            linear   BCT 27-JAN-2026
DEFINITION  DNA/RNA non-specific endonuclease [Streptomyces nigrescens].
ACCESSION   WP_457700502
VERSION     WP_457700502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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 11448985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..298
                     /product="DNA/RNA non-specific endonuclease"
                     /EC_number="3.1.30.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32625
     Region          24..270
                     /region_name="NUC1"
                     /note="DNA/RNA endonuclease G, NUC1 [Nucleotide transport
                     and metabolism]; COG1864"
                     /db_xref="CDD:441469"
ORIGIN      
        1 mipsdspraa gatagttsrp plvdragyde hflgvpvplp mpsrpevetv vlpythftvv
       61 lrpdrrmaaa tavcidgrrl qedvaressw tfdprldrah qtgndvyrdn sldkghlvrr
      121 ldpvwgtaae anranedtfh ytnaapqadv fnqgkklwqg lenylldhaa dfdrklcvlt
      181 gpvlhdsdpp yrgvqvplrf wkvaaflqdg alaatayvld qspdltrdad ralagaqaga
      241 ppplgafrtf qvpvkdvael tsldlgplpa vdlmpvvlap aerwkrlash ddimlqrs
//
LOCUS       WP_457700508             437 aa            linear   BCT 27-JAN-2026
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700508
VERSION     WP_457700508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Karvelis,T., Druteika,G., Bigelyte,G., Budre,K., Zedaveinyte,R.,
            Silanskas,A., Kazlauskas,D., Venclovas,C. and Siksnys,V.
  TITLE     Transposon-associated TnpB is a programmable RNA-guided DNA
            endonuclease
  JOURNAL   Nature 599 (7886), 692-696 (2021)
   PUBMED   34619744
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Siguier,P., Gourbeyre,E. and Chandler,M.
  TITLE     Bacterial insertion sequences: their genomic impact and diversity
  JOURNAL   FEMS Microbiol Rev 38 (5), 865-891 (2014)
   PUBMED   24499397
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Rice,P.A. and Baker,T.A.
  TITLE     Comparative architecture of transposase and integrase complexes
  JOURNAL   Nat Struct Biol 8 (4), 302-307 (2001)
   PUBMED   11276247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..437
                     /product="RNA-guided endonuclease InsQ/TnpB family
                     protein"
                     /EC_number="3.1.21.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=48417
     Region          16..422
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtaeaktsge sgharftyrl rvsstaraal eaewdrcrwv wnecvakskq vgawnktrpe
       61 gaekqtcgpv qlaamltear artewlrega cvpqqqlird fgksrakalk dikarlpvrq
      121 ragmpkykkk rdafptleyt rrgfrlkdgr lhlaggivat vvwsrelpkl pssvrvcrds
      181 ighwyasfvv ptvtqvlpet gavigidwgv ketatttsda hdlphpqhgk kaaqrlahyq
      241 rmmarrkpkr gqpgskgyqa akhqaaklhk kvsrqrqdta rmgspllers srawgrakrv
      301 vrdhdalave dfrpkflaks tmarkaadaa vgatkaalve mgrkhgravh lvhpahttmd
      361 caqcgartkh alplsertyt ctvcgvvslr dknsarvmlv raglnpagad rvrpadppgr
      421 rrrelgipll qlgedsm
//
LOCUS       WP_457700513             237 aa            linear   BCT 27-JAN-2026
DEFINITION  HAD family hydrolase [Streptomyces nigrescens].
ACCESSION   WP_457700513
VERSION     WP_457700513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..237
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24903
     Region          17..220
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtssipavgt rtaeaatlqa vfldldgtlv dtegfwweae aevfaelghi lddthrevvv
       61 ggpmtrsagy liqatgvdis ltelsmllna aflarirrgv plmpgarrll aelaahgvpt
      121 alvsashrai vdqmlhslgp enfrltlagd dlertkphpd pyltaaarlg adpvccavie
      181 dtltgvtage aagcpvvavp svtpippalg rtvvrsleev dlsflrtlit esrgtvh
//
LOCUS       WP_457700517             254 aa            linear   BCT 27-JAN-2026
DEFINITION  IclR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700517
VERSION     WP_457700517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..254
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27289
     Region          2..253
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 martiqsler aaamlrllag gerrlglsdi ssslglakgt ahgilrtlqq egfveqdaas
       61 gryqlgaell rlgnsyldvh elraralvwt ddlarssges vylgvlhqqg vlivhhvfrp
      121 ddsrqvlevg amqplhstal gkvlsaydpv ahseiveadr qaftprtvtg lgdfeglldl
      181 trargwaadv eetwegvasl aapihdrrrm pvgavgvtga vervcqdgel rpeiiaavrd
      241 caravsrdlg agrf
//
LOCUS       WP_457700519             262 aa            linear   BCT 27-JAN-2026
DEFINITION  MIP/aquaporin family protein [Streptomyces nigrescens].
ACCESSION   WP_457700519
VERSION     WP_457700519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26581
     Region          6..262
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 msssdifise tigtavllll gggvcaavtf krskafnagw vaiafgwgfa vltgayiaak
       61 sgahlnpavt igiaiqggie wsqvpvylag emlgamigav lvwvtymgqf qahlsdpevl
      121 adhtseeglv dqsaapkagp vlgifstgpe irnvaqnllt eiiatvvlvl siltlglsdn
      181 gkgvgvigtl lvalvvtgig lslggptgya inpvrdlgpr ivhallplrn kggsdwgyaw
      241 ipvvgpligg aiaggiyqva fa
//
LOCUS       WP_457700527             223 aa            linear   BCT 27-JAN-2026
DEFINITION  FadR/GntR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700527
VERSION     WP_457700527.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..223
                     /product="FadR/GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23926
     Region          3..223
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mavtdeaiek ikgmivsgal rpgdrlpkes elaselglsr nslreavral slirildvrq
       61 gdgtyvtsld pqllleamsf vvdfhrddtv leflavrril epaatamaag rigleeldal
      121 eaqlnalgps psvealvacd lefhrgivaa sgnsvlcsll dglsgpttra rvwrgltqkd
      181 avartltehr ailgalrdrd aeaarawatv hiasveqwlr asl
//
LOCUS       WP_457700529             261 aa            linear   BCT 27-JAN-2026
DEFINITION  3-oxoacyl-ACP reductase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700529
VERSION     WP_457700529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481062
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..261
                     /product="3-oxoacyl-ACP reductase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26053
     Region          19..261
                     /region_name="fabG"
                     /note="3-ketoacyl-(acyl-carrier-protein) reductase;
                     Validated; PRK05557"
                     /db_xref="CDD:235500"
ORIGIN      
        1 mtatvltatt tagngtrplt gkaalvtggs rgigraialr laadgaaval tyrngpdqae
       61 qvvkeierag gqawavrads gdaeavwasv agtvdrfgrl dilvnnagig vlgpfegisl
      121 ddvdrvlwtn vrapflaaqa aaahlteggr iisigscmae rvafpggtly atskaaltgl
      181 tktlarelgp rgitanlvhp gpidtdmnpa dgesaamqag ftalgaygra sdvaatvahl
      241 agdggryitg asiavdggfa a
//
LOCUS       WP_457700531             285 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700531
VERSION     WP_457700531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 10007618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="amidohydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30268
     Region          2..273
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mridahhhlw dlsrreqpwm dgpwaapirr syalsdltph ltghgvdgtv lvqssssyee
       61 taelltlaag egpvtgvvgw adlrdpalad alaalpaglv girhqvqdep dpdwltrpdv
      121 lrglgvlada glvydllvtp relpaahiav ralpqlsfvl dhaakppvvt gewqpwadav
      181 talaahpnls cklsglvtea dwdawrpqqi lpyarhvlda fgpgrvmfgs dwpvctlaag
      241 yedvvalaea atgqlapaer sdvfggtagr vygvgvpsaq eppgr
//
LOCUS       WP_457700532             333 aa            linear   BCT 27-JAN-2026
DEFINITION  aldo/keto reductase [Streptomyces nigrescens].
ACCESSION   WP_457700532
VERSION     WP_457700532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  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 333)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..333
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35412
     Region          19..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(24..26,56,61,87,145..146,177..178,199,227..233,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(56,61,87,145)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mryppygpre lgrtgvtvpp lglgcaplgn lyravpeaqa revvrtalat gagyfdtaph
       61 ygvglseerl gralhghdra aytlstkvgr rlrplapger aagegfvdtp ararvrdlsr
      121 dgiratldas larlgvnavd ivylhdvedq lrevyetgfp alaelraqgv vraigfgmnh
      181 saplarlvad ldadvvlcag rwtllertav ddllpvcarr gtsvvvggiy nsglladpsp
      241 gapynyapap vplldrarql gavcaefdvp lkaaalrfpf ghravaaavv gaatpeemae
      301 narlltrhip delwhtlvar glldpdlplp lnd
//
LOCUS       WP_457700534             344 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700534
VERSION     WP_457700534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35858
     Region          29..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtetasppat dpvdrppprr rprieparwr dfslvpvifv lgvigfivsp afltrdnlig
       61 viqqstelgl lvlgealili sgrmdlsles tiglapvlal wlvmpadgar faglelfpaw
      121 taiplcvavg aavgaangfl iltlrvngfi atlgmltmlr glqvgisegr signvpesfa
      181 ylgkadwlgv paavwiclal falggaalgy lrhgralyai ggnpeaaraa girvdrltwi
      241 vlalggvlaa fagilytghy gavsasqgng wifqvfaaav iggiglkggr gtlfgaltgv
      301 ltlqlvinvm tlggvpplwt qflngmiiiv alvisrftsg ekqd
//
LOCUS       WP_457700536             528 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700536
VERSION     WP_457700536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..528
                     /product="sugar ABC transporter ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /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=55468
     Region          7..499
                     /region_name="MglA"
                     /note="ABC-type sugar transport system, ATPase component
                     [Carbohydrate transport and metabolism]; COG1129"
                     /db_xref="CDD:440745"
ORIGIN      
        1 metddraaav haegivkryg ptvaldgarl tvrpgeahal vgrngagkst lvsvltgmer
       61 pdagrvtfgg epapgwgdta awqrrvacvy qksmtvpelt vaenlylnrf qgartirwra
      121 lhtrarella eygvevdpaa rirdlgveqr qfveiarals fgarliilde ptarldaggi
      181 drlfaklrgl raqgvaflfi shhlqevhel cdtvtvfrda rqvltapvpg laedalvaam
      241 tgeetaavrq prpgvrrage pvlrtealav dghfapldlt vragevvgla gataggstai
      301 gealvglrtp dagriavrgr pvrtgsvpha ldagigyvpe drhreglipd rsvaenatlt
      361 vtgrlgpmgt vlpsrtrefa rrmiasldir ttgpgqpvsg lsggnqqkvv iaralarepa
      421 vlvairptng vdvkskdall gvvrevadgg sgavivsdel ddlrvcdrvl avfhgrvtae
      481 fpagwrdhel vaamegmaag grgqgvppgt gggrdaapdt egtegtap
//
LOCUS       WP_457700538             343 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700538
VERSION     WP_457700538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 343)
  AUTHORS   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   6  (residues 1 to 343)
  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 343)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling 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   9  (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 11449010
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..343
                     /product="sugar ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36716
     Region          26..329
                     /region_name="RbsB"
                     /note="ABC-type sugar transport system, periplasmic
                     component, contains N-terminal xre family HTH domain
                     [Carbohydrate transport and metabolism]; COG1879"
                     /db_xref="CDD:441483"
ORIGIN      
        1 mrlrttgaaa caavlaiaal agcnrgsdta ggrigidmpr tdtdfwnsyq qylekdldhg
       61 gpaalplsns qndiakvvsn vqaltdqgar aivmapqdtg aisaelqrla ekkipvvsvd
      121 trpdegevym vvradnrayg eksceylgkq lggkgrvael qgdlssingr drseafascm
      181 qrkypkitvh elatdwkgev asgklqslla qhpdlngiym qaggaflqpt lalleqkkll
      241 rpagsdghit iisndgipde ldairagkid atlsqpadly akyalyyaka gldgktfkpg
      301 ptehgstivk ikngledqlp aplvtkdtvd dkklwanqle kkk
//
LOCUS       WP_457700558             110 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457700558
VERSION     WP_457700558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..110
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=11829
     Region          7..97
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 mvagkafdvd pdvlhtqgna fvhigsdfsk askklqddle glgsswencd fgdifemiyt
       61 pirdgmfqsm dslgerlegi gdklqnmags ytesdeqgih tisavgrpai
//
LOCUS       WP_457700568             247 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457700568
VERSION     WP_457700568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Huppert,L.A., Ramsdell,T.L., Chase,M.R., Sarracino,D.A.,
            Fortune,S.M. and Burton,B.M.
  TITLE     The ESX system in Bacillus subtilis mediates protein secretion
  JOURNAL   PLoS One 9 (5), e96267 (2014)
   PUBMED   24798022
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..247
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=24685
     Region          6..>64
                     /region_name="EsxA"
                     /note="Secreted virulence factor YukE/EsxA, WXG100 family
                     [Defense mechanisms]; COG4842"
                     /db_xref="CDD:443870"
ORIGIN      
        1 mserrnpeal heaaagwrem gkhldglvrd ldrhvgtaaa anwhgpagea fagewhrlkr
       61 svddslpafe laaadlenaa aappedkgge ehheappvkn sagsqsssgt evaygfmalg
      121 qlanglggaf gkrgggggqs rgpvvrhtwe tstaaqgpdp fgpakdgeat trggagiakg
      181 vrtqpavaep apgeerapka eqekkgtaak paaaaaggda pakgtpasgg eapgrpgpdv
      241 tqhgafg
//
LOCUS       WP_457700570             419 aa            linear   BCT 27-JAN-2026
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700570
VERSION     WP_457700570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18605663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43989
     Region          <86..>167
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
     Region          337..410
                     /region_name="Thump_like"
                     /note="THUMP domain-like; pfam18096"
                     /db_xref="CDD:465646"
ORIGIN      
        1 mnthdtfsal ltpegqalla elrdhdpade laaatrlrre hpaelvsaal gqarlrqraa
       61 akfgadawrm yftpngveqs tratvathra trlaalgvrt ladlccgigg dalalaragi
      121 rvlavdrdpl acaaaranae alglaeliev rcadvtevdt agydavfvdp arrtkarggr
      181 vfdpeayapp lswaveaark apvaalkiap gvphealped aetewisdgg dvkeavvwfg
      241 tgeggaprpv pggrratllp agdsllgtgl pdpsaapaed asphppvgpv gdwlyepdga
      301 virahlvadv arqvggrlid ptiayitadr ltatpyatay aitdvlpfhv krlkallrer
      361 evgiavikkr gsavepeelr kklklgggrk sctifltrvd gapsmllghp atdpvtpgr
//
LOCUS       WP_457700588             272 aa            linear   BCT 27-JAN-2026
DEFINITION  L,D-transpeptidase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700588
VERSION     WP_457700588.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..272
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..272
                     /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=29668
     Region          73..131
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          159..265
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(223..224,227,239..242,244)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkrtlsallv casllvvagp pavavapspa vavtppsaay rlpdlvpgvp ragrqttgsr
       61 hieyvprsea ahagtralrc sastgpyqrq aerylgrqvd grqstgdcra irrfqrahri
      121 apatgfagpv tgatvrlmra kkdpnragrc pdlpqrtacv dlnrqlmwvq qsgrvllepv
      181 airsgaptme trtgsyriyl rhrrhisnly gtrmpyaqff drgealhgvy edifsgpgsh
      241 gcvnltmtda rrawevlrkg dtvhvwgrkp gv
//
LOCUS       WP_457700599             378 aa            linear   BCT 27-JAN-2026
DEFINITION  WXG100 family type VII secretion target [Streptomyces nigrescens].
ACCESSION   WP_457700599
VERSION     WP_457700599.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Poulsen,C., Panjikar,S., Holton,S.J., Wilmanns,M. and Song,Y.H.
  TITLE     WXG100 protein superfamily consists of three subfamilies and
            exhibits an alpha-helical C-terminal conserved residue pattern
  JOURNAL   PLoS One 9 (2), e89313 (2014)
   PUBMED   24586681
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Garufi,G., Butler,E. and Missiakas,D.
  TITLE     ESAT-6-like protein secretion in Bacillus anthracis
  JOURNAL   J Bacteriol 190 (21), 7004-7011 (2008)
   PUBMED   18723613
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Pallen,M.J.
  TITLE     The ESAT-6/WXG100 superfamily -- and a new Gram-positive secretion
            system?
  JOURNAL   Trends Microbiol 10 (5), 209-212 (2002)
   PUBMED   11973144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..378
                     /product="WXG100 family type VII secretion target"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=37913
     Region          24..107
                     /region_name="WXG100_ESAT6"
                     /note="WXG100 family type VII secretion target; TIGR03930"
                     /db_xref="CDD:274862"
ORIGIN      
        1 msnegvgeei veaglelinp ggrpdvlraa atswrnmgse lesafdaldk kvqatlgehw
       61 kgdsadafeh hwnalkqgiq kteptftkag kglddaadsi eevneeihai yveigvsigv
      121 gvalsfvtlg fggaaaaana trlaaqatrv sarlasmltr iassfrhitq lakankfltn
      181 vainwagnta gsvagkawsg ggvsgadlwe atwqggvgaa agtapglrma kyvggkfgdd
      241 asvllreaas gaaggatgnv vggwttegak aaigeefnle daawgtaana vggaaggagv
      301 agvgrlnqpt egfqapegyt pppprdgpsm sidgpmggis aglagagqel aqgddeggdk
      361 kpeaksapqs rsvkdtfg
//
LOCUS       WP_457700608             290 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700608
VERSION     WP_457700608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32512
     Region          11..70
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(17,21,46)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(20,45)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(27..28,39,42,46..47)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mefghpprsr rlggalrryr eaakldqqha adhivgskak isriesgqvt arpgdvrlll
       61 elygvedpev yrqleqlard snkrgwwvny pwalepkyad yvtlesdaty irtwqplymp
      121 gllqtdgyiq alleagvtap tteaverata grrerrksie eggaryaavv wepvltapmp
      181 svdvhrdqlh hlltvaqrrn vtlqvlplse wqaahrashf vmfsfgaepa peavafdstt
      241 stvfvedled makhaeifee lrsaaltptq tlsflrehid slpdsegeva
//
LOCUS       WP_457700614             271 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease, partial [Streptomyces
            nigrescens].
ACCESSION   WP_457700614
VERSION     WP_457700614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   2  (residues 1 to 271)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..>271
                     /product="carbohydrate ABC transporter permease"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          21..271
                     /region_name="UgpE"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     permease component [Carbohydrate transport and
                     metabolism]; COG0395"
                     /db_xref="CDD:440164"
ORIGIN      
        1 masttarapr ttaraprtag rrrsptappr afrwlrrifl taltgfvllp vyvmlssslk
       61 pledvsgafr wlpseltirp yldiwdtvpl aryflnsliv agsatvcsvv vavfaayavs
      121 rytfrgkrif tvtvlstqmf pgilfllplf liyvnigntt gvalygsrgg lvltyltfsl
      181 pfsiwmlagy fasvprelde aayvdgcgpl galfrvvvpa alpgiiavav yafmtawgev
      241 lfasvmtndt trtlsvglqg yatqndvywn p
//
LOCUS       WP_457700612              74 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700612
VERSION     WP_457700612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 74)
  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 74)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13014796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..74
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=8184
     Region          <24..66
                     /region_name="HATPase_RsbW-like"
                     /note="Histidine kinase-like ATPase domain of RsbW, an
                     anti sigma-B factor and serine-protein kinase involved in
                     regulating sigma-B during stress in Bacilli, and related
                     domains; cd16936"
                     /db_xref="CDD:340413"
     Site            order(31,41)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340413"
ORIGIN      
        1 mllvelrrla ipperpteap tawrmpelqk papddvsgrg lflvdalsen wgvrprdpgk
       61 tvwahlalhr tgqp
//
LOCUS       WP_457700616             307 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700616
VERSION     WP_457700616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..307
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33968
     Region          31..280
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrgftrlrrv glpyllllpa lllellvhlv pmvigivmsf keltqlqiah wdaapwkalg
       61 nyrvivdfda pvgatllhsf vvtcafsvlt vglcwllgta aaiflqenfr grgllravfl
      121 tpyalpvyaa vitwaflfqr dnglvnhvlh dqlqltgdrp fwllgdnsfl allvvsvwkt
      181 wpfaflvvma alqsipkdly eaaaldgagi vrqirritlp slrpinqvll lvlflwsfnd
      241 fntpyvlfgk aapeaadlls ihiyqssfvt wnfgtgsams vllllfllvv tagyllatsr
      301 grktadg
//
LOCUS       WP_457700618             438 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700618
VERSION     WP_457700618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..438
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46433
     Region          40..436
                     /region_name="PBP2_TMBP_like"
                     /note="The periplasmic-binding component of ABC transport
                     systems specific for trehalose/maltose and similar
                     oligosaccharides; possess type 2 periplasmic binding fold;
                     cd13585"
                     /db_xref="CDD:270303"
     Site            order(155,157,281,283,320..322,363)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrrlraatvt atvtalaava agcgggtsfd ggssddsprt ltywasnqgp nveadkkilg
       61 pelrkfeqqt gikvklevip wpellnrila attsgqgpdv lnigntwsas lqatgallpw
      121 drknldtigg rgrflapale atgapgkdpa avplyslaya lyynkrmfqe agiskppatw
      181 delvaagkri srdgtwglga eggqltnnih qafalgkqhg adffdssgkp tftsdgavaa
      241 vkqyidfmak dkiiapgnae ygqnqslrdf atgrtamvlw qaaattfaad gmkpadwgva
      301 pvpvpsgtpg tgrrinsmla giniavfknt rnlqgarkfv kfmtsdteqr llnktygsip
      361 pvkaaqqdpa fnrqdtrvlr etlirsaapl pqiaeesqfe tsvgtaikdl fadaaaghpv
      421 ttasvkarla kaqqqmaq
//
LOCUS       WP_457700621             565 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457700621
VERSION     WP_457700621.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..565
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60374
     Region          19..563
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mdlsttpdar tpgsaeggpa dlvflagpvh tvdsartras avavrgdril tvgheeevra
       61 lvgpatevvd lhgkllipgf qdahvhpvgg grelalcdls aavtaeayre lisayaaahp
      121 rtpwitgggw smeafpggmp trefldalvp drpvflvnrd hhggwantca leragltdrt
      181 pdpsdgrier dadgrptgml qegamqlvag lipeptvaeq tegllraqrl lhgygvtawq
      241 damlgyapgm pdvtpayvaa rrdgkltarv tgalwwdrar gaeqipelia rraeltegrl
      301 qatsvkimqd giaenhtaam lspyltacgc asdnsgisfi dpealrsyvt rldaegfqvh
      361 fhalgdravr ealdaveaar rtnglrdtrp hlahlqvvhp ediprfrrlg ataniqalwa
      421 ahepqmdelt ipflgprrag wqypfgdllr sgatlaagsd wpvsspdpia alhvavnrra
      481 pedppsapvf lpeqridlga alaaytagsa yanhldetgt iqpgkladlv vldrdpfdgp
      541 deeiaatrvl qtfvggqrvy aadda
//
LOCUS       WP_457700620             442 aa            linear   BCT 27-JAN-2026
DEFINITION  ROK family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700620
VERSION     WP_457700620.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=45617
     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..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 maertqrtvr dlrrtnrtav lqrlysdgpl srqelgpatg lssgsvsnva aeliedglle
       61 eagvvgsdgg rprtllrvaa gsgcligvdv getrvrvelf dlamgelars elplkhhgyd
      121 vdlivrhiad giatvlrese aspdrllgvg vgvpgildrs rpggavvhgq tigwdavple
      181 ellqhtvalp pgvgfflsng akalgqaemw fgggrgarna aivlfgsgvg aclvtdgvid
      241 ggardsagew ghltvsvggr rcrcgargcl eaytgseall qrwqeaggrp padadeetal
      301 aalvaaahpp dggpaadpva rsvldetaey lgagisdlin lfspervlig gwaglqlgph
      361 llpavrahat ayslahpagr vtidlgrlgp davtvgaatl pladffangg rrraapapea
      421 gervtapgwr taleerarag rd
//
LOCUS       WP_457700623             508 aa            linear   BCT 27-JAN-2026
DEFINITION  APC family permease [Streptomyces nigrescens].
ACCESSION   WP_457700623
VERSION     WP_457700623.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..508
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53351
     Region          39..434
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpsavqqdpg parmrrslgv kdgvaiaass taattsigig mgtlaayagr qtpallllaf
       61 vpilgialsy arlnrsepnc gsgytwvgrs igpwpgfltg wvvlvgnvif maytgavtgs
      121 vvlqflnklg lysvwglrld pastgistav glvalvvvtv taitgvraat rlqmgllife
      181 yavllvfcgy alvigdqpfs lswlnpleig slqavaqgmv lavffywgwd aafsvneetr
      241 sstdaarggl ialvvmmglf lvgalafqrv mstgelmhng pqaltflgaq lapepwaslp
      301 laalmcsafa slqssvipta rgalamardr tlgpvwqrvh prygspavgt llimalaall
      361 avlavgipkl ndmiltavns igltvalyyg ltalacavrf rsslragvvr alrdvlvpaa
      421 salalfglgs ylvwdyatms dhfevnpdng wfmlllpalf ilaglataaw akwvrrapyf
      481 rtgrgtdada itlpmdgdgr plpspveg
//
LOCUS       WP_457700627             405 aa            linear   BCT 27-JAN-2026
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            nigrescens].
ACCESSION   WP_457700627
VERSION     WP_457700627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Jia,Z.
  TITLE     Protein phosphatases: structures and implications
  JOURNAL   Biochem Cell Biol 75 (1), 17-26 (1997)
   PUBMED   9192069
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Mumby,M.C. and Walter,G.
  TITLE     Protein serine/threonine phosphatases: structure, regulation, and
            functions in cell growth
  JOURNAL   Physiol Rev 73 (4), 673-699 (1993)
   PUBMED   8415923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..405
                     /product="PP2C family protein-serine/threonine
                     phosphatase"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=41819
     Region          <1..391
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mlipigiiva vctidvlapp hihlgpllva apaitaafag prltaaigvl avaaqvfigi
       61 arhvlftenl eaqiaalvvv salvvlftvv rdrnerrlrq srsvaavaqq vllrplpvrs
      121 gsleiaslyl aaeeeaemgg dlfaaartts strliigdvr gkglpaysha alilgafraa
      181 ahreatlprl avhldgavrw dssqwgnapg aeagadataa pasdvgsdpt pasdvgsapa
      241 paapvpgpdp vidtdtdetf atvilldlpd rqpvvhtitc ghppplllrd grvrtlsaew
      301 palpiglggl pgapgyeveg fpfepgdlll lytdgvsear ddkgtfypla eragawsdcs
      361 prqvlrqlrt dllahtngrl gddaaavalr rlpgrpsggg gpgap
//
LOCUS       WP_457700651             251 aa            linear   BCT 27-JAN-2026
DEFINITION  polyprenol monophosphomannose synthase [Streptomyces nigrescens].
ACCESSION   WP_457700651
VERSION     WP_457700651.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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 251)
  AUTHORS   Colussi,P.A., Taron,C.H., Mack,J.C. and Orlean,P.
  TITLE     Human and Saccharomyces cerevisiae dolichol phosphate mannose
            synthases represent two classes of the enzyme, but both function in
            Schizosaccharomyces pombe
  JOURNAL   Proc Natl Acad Sci U S A 94 (15), 7873-7878 (1997)
   PUBMED   9223280
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10157756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..251
                     /product="polyprenol monophosphomannose synthase"
                     /EC_number="2.4.1.-"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27313
     Region          16..239
                     /region_name="DPM1_like"
                     /note="DPM1_like represents putative enzymes similar to
                     eukaryotic DPM1; cd06442"
                     /db_xref="CDD:133062"
     Site            order(19,21,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133062"
     Site            order(48,103..104)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133062"
     Site            102..104
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133062"
ORIGIN      
        1 mtdgqrqygp lgttlviipt yneaenikpv vsrvrsavpe ahvlvaddns pdgtgklade
       61 laaddeqvhv lhrkgkeglg aaylagfrwg idngygvlve mdadgshqpe elprlltalk
      121 gadlvlgsrw vpggrtvnwp kyrqlisrgg stysrlaldl plrditggyr afraealtgl
      181 glddvasqgy cfqvdlarra vqagyhvvev pitfvereyg dskmsrdivv ealwrvtawg
      241 vgsrvdkirg r
//
LOCUS       WP_457700652             562 aa            linear   BCT 27-JAN-2026
DEFINITION  amidohydrolase [Streptomyces nigrescens].
ACCESSION   WP_457700652
VERSION     WP_457700652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..562
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57829
     Region          14..557
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 msertpdpvr qhpsgparpr tvllrggevh spadpfatam vvegdriawv geegaadsfa
       61 egvdeivpld galvtpaftd ahvhttatgl altgldlsga atlsdalari rgyaaaread
      121 rillghgwda sawpegrpps raeldtatgg rplyltrvdv hsavvttall dlvpgvrela
      181 gfradapltg dahhavrqaa yatvtpaqra eaqaaalara aalgigsvhe cagpdisged
      241 dftallalar egngprvvgy waelvasakd aerirelgai gaagdlfvdg slgshtahlh
      301 apyadspssd ggtpshtgaa hldaeavaah vaacteaglq agfhaigdaa ltgvvdgvra
      361 aaerlglari raarhrveha emltdhtiag fadlaltasv qpafdaawgg aegmyaarlg
      421 vdrartlnpy aallkagvpl algsdspvtp ldpwgtvraa vfhrtrahgi saraaftaht
      481 rggwraigrd dagvlvpgap adyavwrtge llvqapderv erwstdprsg tpglpdltpg
      541 ndlpvclrtv vggrtvfgpp ne
//
LOCUS       WP_457700657             387 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphotransferase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700657
VERSION     WP_457700657.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42584
     Region          55..327
                     /region_name="ACAD10_11_N-like"
                     /note="N-terminal domain of Acyl-CoA dehydrogenase (ACAD)
                     10 and 11, and similar proteins; cd05154"
                     /db_xref="CDD:270703"
     Site            order(57..59,62,89,91,126,145..148,257,259,261..262,264,
                     274..275,278,293..294,297)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:270703"
     Site            order(57..59,257,259,262,275,278,293..294,297)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:270703"
     Site            order(58,62,89,91,126,145..148,257,261..262,264,274..275)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270703"
ORIGIN      
        1 mtqhpspaep pggvpaglrp rtttrdpeal trrltawlgt rlpgaravaa tvpdsngmss
       61 etllfdidhp gppspelsap legvplscal rlaadpaayt vfprydmarq yrtmrlvaah
      121 tdlpvprtlw leedpahlga pffvmaradg rvppdvmpyt yggnwlhdat daqrdhlaaa
      181 svsvlarlhd qvppaaadfl atpgtgsalh rhveaqrayy swvidgrprs pliergfarl
      241 adrwpsdpge tvltwgdari gnivydgfep aavldwemaa lgpreldlgw mvslhrffqd
      301 lteaggkrgl pdflsrdrve sryaaltghp prdmdfhtly aalrhaivml rvayrqvhfg
      361 eipvpadada lilhrdmlea miegryw
//
LOCUS       WP_457700654             146 aa            linear   BCT 27-JAN-2026
DEFINITION  Lrp/AsnC family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700654
VERSION     WP_457700654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..146
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15913
     Region          1..135
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meeldrqivd llvkdgrmsy tdlgkatgls tsavhqrvrr leqrgvirgy aaivdpeavg
       61 lpltafisvk pfdpsapddi adrlgevpel eachsvagde nyilkvrvat plelehlltr
      121 irtlagvstr ttvvlstpye arppri
//
LOCUS       WP_457700665             422 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 18 protein [Streptomyces nigrescens].
ACCESSION   WP_457700665
VERSION     WP_457700665.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Fukamizo,T.
  TITLE     Chitinolytic enzymes: catalysis, substrate binding, and their
            application
  JOURNAL   Curr Protein Pept Sci 1 (1), 105-124 (2000)
   PUBMED   12369923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="glycoside hydrolase family 18 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008061 - chitin binding [Evidence IEA]"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44394
     Region          56..421
                     /region_name="ChiA"
                     /note="Chitinase, GH18 family [Carbohydrate transport and
                     metabolism]; COG3325"
                     /db_xref="CDD:442554"
ORIGIN      
        1 mlrphrmrsp rrvlaaatal ctaalagtll agpasaspan aptapraaap aaaaaggkvv
       61 gyftnwgvyd rnyhvkniet sgsaaklthi nyafgnvqgg kcaigdsyad ydkaytadqs
      121 vdgtadtwdn galrgnfnql rklkklhpnl kviwsfggwt wsggfgeaak npaafaqscy
      181 dlvedkrwad vfdgididwe ypnacgltcd tsgrdaftnv mkalrskfgq snlvtaaita
      241 dasaggkida adyagaaqyv dwynpmtydy fgawdakgpt aphspltsys gipkagfnst
      301 dtisklkglg vpaskmllgl gfygrgwsgv tqdapggtat gaapgkyeag iddykvlksr
      361 cpatgkvggt ayakcgdqww sydtpetigt kmafkdaqgl ggtffwelsg dttngelika
      421 ik
//
LOCUS       WP_457700678             225 aa            linear   BCT 27-JAN-2026
DEFINITION  GntR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700678
VERSION     WP_457700678.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..225
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24755
     Region          6..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maaggdssvi rrstlrqqia dalrdevlag rlpsghpftv keiaeqygvs atpvrealld
       61 lcaqglldve qhrgfkvhaf taadframve artliiegif rsgadqalra tsagvlisir
      121 rradeaeraa ragdldvlig ydlrfwrels sivnnayisd fldrirvqtw mfavpllrre
      181 pdlrgllwqg hsaladaliq hdlataqrli aeynehslal vgtrg
//
LOCUS       WP_457700684             187 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457700684
VERSION     WP_457700684.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19352
     Region          30..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msasradgpr spehpapegp papellsrsa lavfrlngqf lsvadglahp agltaawwqv
       61 lgavlpeplp vagiaramgi trqsvqriad llvarglaey rpnpahrrak llapteegra
      121 avaritpgha efaarlreql ggpdgfqrvt taleelsaal delpgppktp paaeaqglsd
      181 gsgsdrp
//
LOCUS       WP_457700686             582 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457700686
VERSION     WP_457700686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..582
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=59288
     Region          36..290
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(42..43,45..48,50,62,64,96,112..115,119,121,159,161,
                     163..164,166,175..176,179,199..202)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(42..43,45..48,50,62,64,96,112..115,119,161,163..164,
                     166,175..176)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(46,119,121,159,161,163,179,199..202)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(58..59,88,93,98..101,113)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(175..183,195..202)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 meqpiragqq grpgraerag wlrpldaqdp arigdyrllg rlgqggmgrv flarsdrgrt
       61 vavklvhsel ageeefrarf rrevraaqqv ggewtapvld adteaetpwv atgyiagpsl
      121 qrvvggsgtp lpersvrila aglaralgai haagiihrdl kpsnvlltid gprvidfgia
      181 raleavtgng etrtgasvgs pgfmspeqvr gepltpacdv fclgavlaya atgrqpfgta
      241 dsiahavmyr iaqeepdlsa lpdglrelvs gclakdpeqr ptpaelvaqa ergtgdgpga
      301 ddepwlpaal iarlgrhave lleaedpqdg edgedaqggd ragapsaaps pasqgpgvha
      361 lptavshtpa pgrtpatppp rpvapgpash ppyaarghhg aaapapapaa aprrrrrgag
      421 aalftavalv lggagaatay avlsdgggvr aedggtgkdg qaaqsaangg iptdylgtwe
      481 ttldgsdlna rrltliqget gdtvltmtat gasyrcafaa tltsagppvr lgpstvvsgp
      541 sdscrpgess tlemvggtlr rvsddgkals yrktgaaaak pg
//
LOCUS       WP_457700688             603 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457700688
VERSION     WP_457700688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..603
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=62652
     Region          18..277
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,103,146,148,
                     150..151,153,162..163,166,186..189)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,148,150..151,
                     153,162..163)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(28,101,103,146,148,150,166,186..189)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(162..170,182..189)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mdglrgltad dpqwigdyrl lsrlgsggmg rvylarsegg rtvavklvka elaaeeefrd
       61 rfraevaaar rvggrwtapv ldadteaavp wvatgyiagp tlsevvgsys rsgsygplpe
      121 hslrrlaygl scalrdihgv glvhrdlkps nvlltidgpr vidfgiaral davgeqtqtr
      181 agtvlgspsf mspeqvtgqr vapasdvfcv gsvlayaatg rqpfgnpasg vhavmfkiaq
      241 ekpdvaavpd girglildcl akdpaarptp eelaerlgpv pggpsappwl paeliarlgr
      301 havllldtdt ppggqpptvl ttrplpsqap ppaptaaerr rrrrrlplva tavvaaataa
      361 aavpllsgga daddsasdip aryvgtwsgp vlrdgtptgq qrrfvithgt vgevvansts
      421 lgatyecrsd grlvsvtrqd ghpalrldtk vvrsvpagrc aalgehtlee ggagtltwaa
      481 agrtatlhrv apadgtvpag flgtwrrpnd dgfgsqqltv kqapagstal stvvmgragr
      541 ctahadlyaa eggkltvgpt vvdraapgct psstsvlsla gdgtlhrefl gddkqprgys
      601 rvk
//
LOCUS       WP_457700692             211 aa            linear   BCT 27-JAN-2026
DEFINITION  GbsR/MarR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700692
VERSION     WP_457700692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8) (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..211
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23341
     Region          24..171
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mseqpqqsad rtddtrqdsg dikrddeavs qfverfasql veagmqrmsa rvfacllasd
       61 sgvltsaelg erlqvspaav sgairylsqv dmvsrerepg srrdryrvhs dqwyeamtrr
      121 dnmltrwest lregvaglge ttpagrrlge tlaffefmqk elggmlerwr nhrdelrtdh
      181 esqtgtpgap ltrsaaaaaa rppaapstyg s
//
LOCUS       WP_457700697             453 aa            linear   BCT 27-JAN-2026
DEFINITION  sensor histidine kinase [Streptomyces nigrescens].
ACCESSION   WP_457700697
VERSION     WP_457700697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  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 453)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..453
                     /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=48462
     Region          190..442
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnettqtqds lhseariahg vlhrlrqdlf vdafafrplp pledakisrw vpwlperlrr
       61 warwlphvtv gffsafvllv dlassgpgpl hgmvaagfsl llaaplmltl frpvgaywls
      121 laafavgafa eaaspfanlf sngafathvm vmvlvvlrtr prlamemwlv tfavaavltv
      181 ltgtdpgdpa pvavfcgvvl isaaavrawr eerrqvvrtq tateeertrr tlleeralia
      241 relhdvvahh msviaiqaea apyrvkdtpp elatsfatir enavaalael rrilgvvrsa
      301 dpdafaesdp eapqptlghl dslldsvrga gltveavvtg sprplpqgve lsayrivqeg
      361 lsnalrhspg adarveisyv lgglgvrivn gapsrlakps pgaghgvlgm rervqmlgge
      421 mtadhtedgg fevaafipva katgetkagg ara
//
LOCUS       WP_457700699             262 aa            linear   BCT 27-JAN-2026
DEFINITION  alpha/beta hydrolase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700699
VERSION     WP_457700699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26353
     Region          50..238
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msvadeesal lglapvapdr tmaygphpdq lvdvyaprag dggraevrgp lvvllhggfw
       61 raaydrrhls plaaelagqg mpvalaeyrr vgagggapqt fedvaaaiga ahaalaktaa
      121 dpavvlvghs agghlallaa arpgtpvtrv lavspvadla rahelglsdg avaellgagp
      181 glpgrlaaad parhppagvp vtilhgtddp dvpvdlsrry aarspgttdl celpgvghya
      241 pvtpgspsch tlfrclsrpc st
//
LOCUS       WP_457700708             938 aa            linear   BCT 27-JAN-2026
DEFINITION  DEAD/DEAH box helicase [Streptomyces nigrescens].
ACCESSION   WP_457700708
VERSION     WP_457700708.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 938)
  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 938)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..938
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=104092
     Region          12..935
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtedmspaer yaaaklraae qatalapfre mydfgldpfq veacraleag kgvlvaaptg
       61 sgktivgefa vhlaleqgrk cfyttpikal snqkyqdlvk rygaekvgll tgdnsvnsea
      121 pvvvmttevl rnmlyagsqs lvglgyvvmd evhylsdrfr gavweeviih lpesvtlvsl
      181 satvsnaeef gdwldtvrgd tavivsehrp vplwqhvlag rriydlfeer dgqsggrrev
      241 npdlerlarm ensrptfgrd krrgrnmrea drererrqra riwtpsrpev idrldnegll
      301 paitfifsra gceaavqqcl vsglrlndqe greqvrrive artagilddd lhvlgyfewl
      361 eglergiaah hagmlptfke vveelfvkgl vkavfatetl alginmpars vvleklvkwn
      421 geqhaditpg eytqltgrag rrgidiegha vvlwqrgmnp galaglagtr typlrssfkp
      481 synmavnlvs qfgrhrsrel lemsfaqfqa dksvvgisrq vqkneegleg yrgsmtchlg
      541 dfeeysrlrr elkdretela kqgaaqrrva aaaaleklkp gdvihvptgk yaglalvldp
      601 gmpsgrtngh rgfdaqdgpr plvltaerqv krlasidfpv pvkaldrmri pksfnarspq
      661 srrdlasalr tkaghvvpsr hrkprseaad dreiarlrte irahpchgca eredharwae
      721 ryhrllrdtr qlerriegrt ntiartfdri callteldyl egdtvtdegr rlarlygeld
      781 llaseclrdg vweglgpael aacasalvye arqaddavap klpagkarda lgemvriwgr
      841 ldaleedhki nqaegvgqre pdlgfawaay rwasgfglde vlreaempag dfvrwckqli
      901 dilgqiaaaa ppggtvarta rkamdgvlrg vvayssvg
//
LOCUS       WP_457700710             372 aa            linear   BCT 27-JAN-2026
DEFINITION  LLM class flavin-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457700710
VERSION     WP_457700710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099592
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..372
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40419
     Region          4..246
                     /region_name="Alkanesulfonate_monoxygenase"
                     /note="Alkanesulfonate monoxygenase is the monoxygenase of
                     a two-component system that catalyzes the conversion of
                     alkanesulfonates to the corresponding aldehyde and
                     sulfite. Alkanesulfonate monoxygenase (SsuD) has an
                     absolute requirement for reduced flavin...; cd01094"
                     /db_xref="CDD:238527"
     Site            order(8,12,53,106,126,179..180,194,228,230)
                     /site_type="active"
                     /db_xref="CDD:238527"
     Site            order(50..55,58,61..62,65,82,84..85,88..89,92,95,112,
                     115..116,155,157..160,162..163)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238527"
     Site            75..76
                     /site_type="active"
                     /note="non-prolyl cis peptide bond [active]"
                     /db_xref="CDD:238527"
     Site            order(108..116,123..125,155..168,231..234,241..246)
                     /site_type="other"
                     /note="insertion regions"
                     /db_xref="CDD:238527"
ORIGIN      
        1 mpveflgiaa tndgsevtpr sgasfdkdyt lklarahqey gwdrvlfayg sgspdpspaa
       61 ayvaartetl qilvahrpnv syptfaaktf atldrisdgr lavhfitggn dheqgregdt
      121 ltkderydrt reyirlvkki wtthepfdhe gthyrfhdfv sdtfplqqph pqvsfggssa
      181 aayaaggaea diyclwgepl aqtaeqiaav kaaaqaagrs evpriqvafr piiapteela
      241 wekahrtler ikarkaggal srrhpltnpq nagsqrllav aaegerhdra lwtptaaetg
      301 gagnstalvg tpetvaqall dyydlgveil sargydlldd aidfgryvip ivreevakrd
      361 aeraaadgrh as
//
LOCUS       WP_457700720             285 aa            linear   BCT 27-JAN-2026
DEFINITION  siderophore-interacting protein [Streptomyces nigrescens].
ACCESSION   WP_457700720
VERSION     WP_457700720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..285
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31030
     Region          5..260
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 maaerpsrkk paahrarvqr teqltphmvr vvlggeglae ftageysdhy vklvfpqpgv
       61 qypepfdiaq iraefprdqw pstrtytvrt wdaatreltv dfvvhgdegl agpwaaaaqp
      121 geeifllgpg gayvpeatad whllagdesa lpaiaaslar mpagvpvhaf ievagpeerq
      181 eldapagaei swlyrggapv grelvaavra lefpsgrvqa fvhgeagfvk elrrllrver
      241 eiprealsis gywraghded gwqaskrdwn qqveaeqeaa taaas
//
LOCUS       WP_457700721             413 aa            linear   BCT 27-JAN-2026
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700721
VERSION     WP_457700721.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 413)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 413)
  AUTHORS   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 413)
  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 413)
  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..413
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..413
                     /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=43713
     Region          1..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 msrlqaehly kvfgrrpeda vrkleagagr eelraegtta avidasievd egqifvvmgl
       61 sgsgkstllr tlngllepta gtvrfdgqdl tslsdkelrk vrsekismvf qhfalfphrs
      121 vlenaaygle vqgvpraern rratealelt glkgwekswp delsggmqqr vglaralatn
      181 adlllmdesf saldplirrd mqdqllelqk tlkktivfit hdlneamrlg driavmrdgr
      241 ivqigsaedi lvtpandyva sftqdvdrtr vltagaimae vgtvlgattp egkklttaae
      301 fraaapatvg vdtplvelft pcsastvpva vtdehgdlvg avaaerllav lgeparqaaa
      361 ggvpaqapaa dgtavalgkt pavdapddep aavkhsvatp gdnepedkvi aga
//
LOCUS       WP_457700718             216 aa            linear   BCT 27-JAN-2026
DEFINITION  MerR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700718
VERSION     WP_457700718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..216
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22993
     Region          1..87
                     /region_name="HTH_MerR-like_sg5"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04780"
                     /db_xref="CDD:133407"
     Site            order(2..4,18,35..37)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133407"
ORIGIN      
        1 mrigelsret gvaiptikyy vregllpagr ltspnqasyd dghvrrlrli rglidvgels
       61 vstvrevlaa vdspeesvhe vlgaaqhait prpavtpegv erarqavael irrrgwrvgl
      121 dhpafektav alatfrgigh gefeevlddy aeacervaaa dlawagrnae vdglvesvvv
      181 gtvlgdavlt amrrlahvea sarsfedaaa egaggr
//
LOCUS       WP_457700723             866 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter permease/substrate binding protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700723
VERSION     WP_457700723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 866)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 866)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..866
                     /product="ABC transporter permease/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=94372
     Region          1..270
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          334..589
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(342,344,389,417,448,452..453,501)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
     Region          609..864
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(615,617,662,690,721,725..726,773)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mpriqigswa egavnwlrdn ldwlftlitk vlnglydaih tvlagpepll lagilavlaw
       61 wlrglpaavl tflgfalids veqwgpties lslvlvacli tvvvavplgi waarsrvvgg
      121 vlrpvldlmq tmpamvylip gilffglgvv pgivativfs mppavrmtel girqvdgelv
      181 eaaeafgthp rrtlfrvqlp lalptimagi nqvimlalsm vviagmvggg glgssvynai
      241 ssvdvalgae sgiavvilam yldrmtgaln qrvsplgrra lakaqaslgg mkflqwrpat
      301 svavvgivvl allaggmgmm gksdgqaggg ngrpislgyv nwdegkatty lwkeileqrg
      361 ykpkvqalea gplfagqarg didvqtnawl ptthdsywkk yqdkledlgs wydktsleia
      421 vpsymkgvkt lddlkgkgge lggkitgiep gagemkilkd kvlkdyglgg eykvqessta
      481 smlaeldrsl rakkpiavtl wsphwaydky kltklkdpkg sfgsgdslhl lgrkgfaede
      541 pevakwmkkf hmdeeqltsl endiksageg heqdgvrtwl kkhpglvdkv apsadatyak
      601 gkdagkapni gypawdegia ttylwknile krgyqpnirn ldvgpmwtgl stgqidvetd
      661 awlpvaqkqy wdkykkdlvd vgpwydktsl eiavpsyvkg vktmddlreh kdefkgkiig
      721 iepgtgemkr lkdtvapayg lqdfevtsag tsamlteldr ayrkkepvav vlwsphways
      781 kykltkladp qgtwgannqi ktlghksfpk kfpefhgwlk nwkmnaeelg slenaiqdag
      841 kgnenkgvek wigdhpgivd kmapvk
//
LOCUS       WP_457700727             310 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700727
VERSION     WP_457700727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32309
     Region          19..77
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          108..305
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(123..124,126..127,130,134,136..142,236..240,
                     246..247,249..250)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mgaedetvav slshrvpdlg alelllavar lgslgraara rgitqpaass rirsmerqlg
       61 valversprg srltdagalv tdwarrvvea aeafdagaqa lrgrrdsrlr vaasmtiaey
      121 llpgwlialr aqrpdtavsl lagnssavae rllggaadlg fveglevpag ldgtvigqdr
      181 livvaapshp warrraelta aelaatplil rergsgtrqv ldaalarhgg laepllelas
      241 ttavkaavvs eaapsvlsel avgeeltarr lveipvrglr lgrelravwp tgqrpagpar
      301 ellgltrgap
//
LOCUS       WP_457700729             232 aa            linear   BCT 27-JAN-2026
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Streptomyces nigrescens].
ACCESSION   WP_457700729
VERSION     WP_457700729.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..232
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=23673
     Region          8..222
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msqpligist yqeearwgvw tlpaalvpag ypqqvqrsgg laallppgdp ataaaavarl
       61 dglviaggad vqparygaep hprtgppald rdawelalie aalaggvpll gicrglqlln
      121 valggtliqh ldghagapgv feqheikpvp gtllgrtlpe pvavptyhhq avdrigrgll
      181 asaysedgti ealelpgayg falavqwhpe agddtrvmda lvaaargssa ga
//
LOCUS       WP_457700732             304 aa            linear   BCT 27-JAN-2026
DEFINITION  5'-3' exonuclease [Streptomyces nigrescens].
ACCESSION   WP_457700732
VERSION     WP_457700732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     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=32330
     Region          1..298
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpesv kapdgtpvna vrglldfiar lvqdhhpddl vacmdfdwrp
       61 qwrvdlipsy kahrvaeeap agspepdeee ipdtlspqvp viedvldalg iarigaagye
      121 addvigtlta qaegpvdivt gdrdlfqlvd drrgirilyp lkgvgtlqit deallrekyg
      181 vdgpgyadla llrgdpsdgl pgvpgigekt aakllatygd lagimaaadd paskvtpaqr
      241 krllearpyl avapkvvkva advpvpavgh alpaepadpe rlealaaqwg lggalhrllv
      301 tlrr
//
LOCUS       WP_457700734             419 aa            linear   BCT 27-JAN-2026
DEFINITION  MFS transporter [Streptomyces nigrescens].
ACCESSION   WP_457700734
VERSION     WP_457700734.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43448
     Region          11..386
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(21..22,25..26,29,62,117..118,120..122,125,145,
                     148..149,152,229,232..233,236..238,241,265,269,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mgvrrslgrq fgwlwtaygv stfgtrlafd afpliavlvl htgptevsll aaagtavgaa
       61 vavplgpwme frrkrpvmia mdlarcaall tipaafavgl lsfaqllvvs vivaaadltf
      121 qaaggaflka lvpptdllva narfestnwt atvlgpplgg aaiglfgpvl tvvadavsyl
      181 lsavglraig gkeprpvrtg aprlragevl egwryilthp alrplffntv lvnglimats
      241 pllavlmlgr lgfapwqygl afavpcvggl igsrlarrlv arfgqhkvlf tagalracwl
      301 pglafigpgt aglvlvmave lglitcmgvf npvfatsrld haepgrvart lsawavtgka
      361 tiaaltglwg llagiagprt aialagllsl ttplllprha htprhepgaa pdtplmaad
//
LOCUS       WP_457700736             310 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700736
VERSION     WP_457700736.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the 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   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33618
     Region          1..291
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdltavrtvv avadagqfqe aaatlsitqq avskriaale kdlgvrlftr targarltid
       61 gqaflphare llrveerava svrpksralr vdvigrrlap avllrdfhra hpgtaldvvt
      121 tlfdadaala avrsgtidas fravtlparq lpdgvevarv fdepiqlltg paheyaaara
      181 vtlarlaghr iwmpgivagt ewaayydela aefgltieat gpdfgtepll dtiadsaslv
      241 tfvgaqtrlv wpadqdlrrv pvhdptpvyp hsliwrsdnp hpalttlrty lgstrpthrd
      301 dgtwtpkwar
//
LOCUS       WP_457700739             262 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700739
VERSION     WP_457700739.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28010
     Region          3..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mnveieelhv gyagrnvvag vqlmaaegei aglvgpngsg kstvlrtvyr hlrptagrvl
       61 lagtdirtls pgrtaqqvaa lpqergsdfe ltvrevvtmg rtpykrafag edrtdretva
      121 ralaavgmag qgarrfstls ggerqralla rafaqdpevl vldeptnhld vrhqvellal
      181 lrdrrrttli slhdlnaaas lcdrlhvlha grvvasgtpr avltpqllae vfgvraavte
      241 hpltgdplia fdhreplpad gg
//
LOCUS       WP_457700740             422 aa            linear   BCT 27-JAN-2026
DEFINITION  cytochrome P450 family protein [Streptomyces nigrescens].
ACCESSION   WP_457700740
VERSION     WP_457700740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Munro,A.W., Girvan,H.M. and McLean,K.J.
  TITLE     Cytochrome P450--redox partner fusion enzymes
  JOURNAL   Biochim Biophys Acta 1770 (3), 345-359 (2007)
   PUBMED   17023115
REFERENCE   2  (residues 1 to 422)
  AUTHORS   McLean,K.J., Sabri,M., Marshall,K.R., Lawson,R.J., Lewis,D.G.,
            Clift,D., Balding,P.R., Dunford,A.J., Warman,A.J., McVey,J.P.,
            Quinn,A.M., Sutcliffe,M.J., Scrutton,N.S. and Munro,A.W.
  TITLE     Biodiversity of cytochrome P450 redox systems
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 796-801 (2005)
   PUBMED   16042601
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Degtyarenko,K.N.
  TITLE     Structural domains of P450-containing monooxygenase systems
  JOURNAL   Protein Eng 8 (8), 737-747 (1995)
   PUBMED   8637843
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15296244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..422
                     /product="cytochrome P450 family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=46519
     Region          19..405
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,91..92,99,103,110,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,85,87,90,92..93,175..176,189,238..239,242..243,
                     247,290,293..295,395)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mspssepvel ygpeykrnpy plyaelrerg pvhrvrfpsg vcawlvtgyd aahqaltdpr
       61 lgkhhsrgna awrarasimp epqhsqlqvh llhqdpprht alrrlitdaf apqrvealrp
      121 rfqamadall dglpdsggtd lvelfaarfp fqvlaevigl paqfadrfdr dwgkvvqpvg
      181 pedpgrpaye arlrglqqyi adlvrhkrte rgedllsrlv aardadrlgq eeldsmvfql
      241 lvagqepvtn qittalvtll rhpghlaela arpellprav eellrhdsaf elttwrffae
      301 dtelhgtrip agdsvivsls aanrdsrqfp dadalhfdrt pnphlafghg ihfcpgatla
      361 rielqialga vlrrlpglrl avpedelewt pavlargvgr lpvtygscpy agsgangpda
      421 ac
//
LOCUS       WP_457700744             800 aa            linear   BCT 27-JAN-2026
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces nigrescens].
ACCESSION   WP_457700744
VERSION     WP_457700744.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..800
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82045
     Region          20..778
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtpeprpgtp tpdlapapar sttltiggmt caacvgrvek klgrldgvaa tvnlatgrak
       61 vshpatvsvt dlittveaag ftaqlpepap epdpedrlsp tdrpdapdap dtqgsqdtqg
      121 sqddgaraer hrllvtalls lpvlvlsmvp gwqfrdwqwl cfvlaapvav wgaapfhara
      181 lrglrhgaat mdtlvslgva asflwsayal ffggagapgm tmpfsllpta gdgaahlyle
      241 aavgvplfvl agrrmearar rgtgaalral aelaakdvav rtpegerrip vgrlrvgdhf
      301 lvrpgervat dgtvvegssa ldlslisges rpvevgpgaa avggavnsgg llevradavg
      361 adtqlaritr lvedaqtgkt kvqrladava avfvpavltv svsvlgfwlg agaepqaait
      421 aavavlvvac pcalglatpt allaatgrga qlgilvrgpe alerlrridt vvldktgtlt
      481 tgrmsvtalt prtggldaaa alrlaatveq gsehplarav tayaeerqpg qplppvadfs
      541 atpgygvrgt adgrrvevtr pgdltglpap lpdavhtaee aghtavlvtv dgtpeavlai
      601 gdalrpdsyr avdrlrrlgl rpvlatgdra ataravaghl aiteihaear pedkaalvtt
      661 lkeqggrvav vgdgvndaaa laladlgiam gsgtdaaiga advtlvredl qaiadavhla
      721 rrtlgtirgn lvwafgynlv tvplaavgll spmlaaaams assllvvgns lrlrawrpgg
      781 agtsarrphs praqarwetr
//
LOCUS       WP_457700746             157 aa            linear   BCT 27-JAN-2026
DEFINITION  copper chaperone PCu(A)C [Streptomyces nigrescens].
ACCESSION   WP_457700746
VERSION     WP_457700746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Fisher,O.S., Sendzik,M.R., Ross,M.O., Lawton,T.J., Hoffman,B.M. and
            Rosenzweig,A.C.
  TITLE     PCuAC domains from methane-oxidizing bacteria use a histidine brace
            to bind copper
  JOURNAL   J Biol Chem 294 (44), 16351-16363 (2019)
   PUBMED   31527086
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Abriata,L.A., Banci,L., Bertini,I., Ciofi-Baffoni,S., Gkazonis,P.,
            Spyroulias,G.A., Vila,A.J. and Wang,S.
  TITLE     Mechanism of Cu(A) assembly
  JOURNAL   Nat Chem Biol 4 (10), 599-601 (2008)
   PUBMED   18758441
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10515835
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="copper chaperone PCu(A)C"
                     /GO_function="GO:0016531 - copper chaperone activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16024
     Region          48..147
                     /region_name="PCuAC"
                     /note="Copper chaperone PCu(A)C; pfam04314"
                     /db_xref="CDD:461259"
ORIGIN      
        1 mkrlplpava vplltclvtl nilalwtatg nagtpaalsv pegrvliagg seataaffti
       61 rntggaddvl tgvtgpaghr amlsrtvdig nnarsmamvr tvtvpagaal tmtptgldvm
      121 vsppprlapg drltftlhfr hsppqtvrar airpgdg
//
LOCUS       WP_457700755              71 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457700755
VERSION     WP_457700755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..71
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7473
     Region          5..62
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mtweveidpq qciasgscaa iapdlfvvdg aharplkdri eederaldaa dvcpamaitl
       61 rdgtkvvgpr p
//
LOCUS       WP_457700758             208 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700758
VERSION     WP_457700758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21756
     Region          14..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvktpqqgta nasrrdaqgt rlrlldaase lfaergyera tvreiasrag anqallfryf
       61 gskkalfgev marggheqlr ttpaerlfev alrgmlagga egadrslevc lrsiggsdei
      121 aealrglgee yaevlatlse sdtgslradl alswllgigl mrvvvakepl asadpdtica
      181 lvadalgnll eslpkdgptg gesggipe
//
LOCUS       WP_457700764             274 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family oxidoreductase [Streptomyces nigrescens].
ACCESSION   WP_457700764
VERSION     WP_457700764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..274
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28862
     Region          2..272
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mkvliiggsg flgtelvrqa taagwetsat yhsrpgsipg aawypldvra pgridevlat
       61 vapravinat sgqsdwavta dgsvrvamaa trhgcrlvhv ssdavfsgsr irydesclpd
      121 pvtpygaaka aaetavrlla paaavartsl iignggsahe rmvhtlaanp hdgvlftddi
      181 rcpvhvedla salrelalsd rpgichlaga dalsrhelgv liarrdglda trlpagrrad
      241 tripgaldir ldssatqrhl rtrlrgaref lqvr
//
LOCUS       WP_457700766             358 aa            linear   BCT 27-JAN-2026
DEFINITION  FecCD family ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700766
VERSION     WP_457700766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..358
                     /product="FecCD family ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36493
     Region          40..353
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvaephgcee raegagrrtp ragllavglg valvvaltaa vslgatdiap ghvwsvvfrr
       61 lggapprpgt ddlivwqlrv prallaalvg aglglvgtat qalvrnplad pyllgisnga
      121 slgavtaivl gataggglgl glsgaafaga lgsfalvwwm arrgggfspl rlvlagvgvg
      181 qflsgftsyl vlqagdeqqt rsvlfwlmgs lsgatwqvlw lpalavavgl palqararam
      241 nalimgdeta agvgvdvtrl rrelfvvagl ltgvlvavsg aigfvglmvp hlcrlliggd
      301 hrrllplsal tgslllvvvd lvcrtamdtq elpigvvtam igapallfil drrleadr
//
LOCUS       WP_457700770             173 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700770
VERSION     WP_457700770.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..173
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19193
     Region          14..164
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mneitfrlag gggdlaalvt lydgaarwmq esgidqwkpg ekdeehfrrr qkdgevwlae
       61 aagrmvgafe lwwrdepawg pqppeagyvh rlmvdrrhap agtgrallaq aerriaeagr
      121 twcrldcvss nprlrtyyeg agytvvgeqp fkegtggsry avtllekrlg das
//
LOCUS       WP_457700774             136 aa            linear   BCT 27-JAN-2026
DEFINITION  cupin domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457700774
VERSION     WP_457700774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..136
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13692
     Region          1..111
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 msvvnlfraa valpdawssr plgevgtacv kvlrmdelpv eeeshgtaev llvldgrlql
       61 svedtevtvg qgemylvkag arhavrpgsr gtlvivevpe gsggggplaa dglqgagpsa
      121 pspadqalrg gigrsa
//
LOCUS       WP_457700776             127 aa            linear   BCT 27-JAN-2026
DEFINITION  VOC family protein [Streptomyces nigrescens].
ACCESSION   WP_457700776
VERSION     WP_457700776.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..127
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13855
     Region          8..116
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mvsvvqnvai dcadayelar fwsevlgcpl hpedkpgaae tevmlpegpv lhfnrvpepk
       61 tvknrihlcl rpktsreeev erllglgatl vtdrresdga gwavladpeg nefcvlrses
      121 draamss
//
LOCUS       WP_457700778             157 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700778
VERSION     WP_457700778.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..157
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16735
     Region          22..154
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 msaqaasraa qgpvtvrtft qrfsatrrga rlarylavqq ldvwgfpygg evsdavaliv
       61 gelaanaath grvpgrdfel rltklpgsar pgtlrievad trtekhpprp gtlappppds
      121 etgrglllva alatcwtvld rprvgkvvra elhlqel
//
LOCUS       WP_457700780             280 aa            linear   BCT 27-JAN-2026
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700780
VERSION     WP_457700780.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31871
     Region          <31..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"
     Region          97..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtacnddqhg tsepepsgsl ktfgavyqcf renagftqes lspavryssh yigsveqgrr
       61 lpskkfidrs eevldargvl rkaaknlsrq rglaswfrqw aaleeeaitl ytyesrlipg
      121 llqtepyart lfseqlppld ddqietqwta radrqrllre rpntaysfil eeqlflrrtg
      181 gvevtrdlie hvletaesrn ieiqvmplvq ethaglagpm qlletpenqw faynecqrgg
      241 lfisdpkevs vlqmryarmr sqaltpedsv sllkrmrgal
//
LOCUS       WP_457700787             552 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces nigrescens].
ACCESSION   WP_457700787
VERSION     WP_457700787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 552)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..552
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=60879
     Region          27..487
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(83,86,123,126,171,189,193,225,293,354..355)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(225,293,355)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          469..550
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 mtsphhatpd dvtpgdatpd naapatdwwr daviyqvypr sfadangdgm gdlagvrsrl
       61 pylrdlgvda vwlspfyasp qadagydvad yraidpmfgt lpdaeavire ahrldlriiv
      121 dlvpnhcsdq hewfrralae gpgsttrerf hfrkgrgeng eeppndwesl fggpawtrvp
      181 dgewylhlfa peqpdfnwdh pavqdefrsi lrfwldlgvd gfrvdvahgl vkapglpdmg
      241 rgeqlkllgn qvlpffdqdg vheiyrswrt vldeyspslr pgvppgsria vaeawtpsad
      301 rtalylrpde lhqafnfhyl dtgwdaaalr eaidssldam rpvaapttwv lsnhdvvrhr
      361 trlgggpdra raatllmlal pgsaylyqge elglpevtdl pdevrqdpsf frdagqeglr
      421 dgcrvplpws gdappygfgd ggswlpqpdd wagltveaqt gdpastlely rtaltlrrth
      481 pglgagesve wldapdgvla frrpgglict vntteapacl ptpgrmllas rqlsapqgdf
      541 elpadttvww ee
//
LOCUS       WP_457700793             543 aa            linear   BCT 27-JAN-2026
DEFINITION  glycoside hydrolase family 13 protein [Streptomyces nigrescens].
ACCESSION   WP_457700793
VERSION     WP_457700793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 543)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10183204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..543
                     /product="glycoside hydrolase family 13 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004574 - oligo-1,6-glucosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0009311 - oligosaccharide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=58641
     Region          23..481
                     /region_name="AmyAc_OligoGlu_TS"
                     /note="Alpha amylase catalytic domain found in
                     oligo-1,6-glucosidase (also called isomaltase;
                     sucrase-isomaltase; alpha-limit dextrinase), trehalose
                     synthase (also called maltose
                     alpha-D-glucosyltransferase), and related proteins;
                     cd11332"
                     /db_xref="CDD:200471"
     Site            order(78,81,118,121,160,178,182,214,277,338..339)
                     /site_type="active"
                     /db_xref="CDD:200471"
     Site            order(214,277,339)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200471"
     Region          462..541
                     /region_name="DUF3459"
                     /note="Domain of unknown function (DUF3459); pfam11941"
                     /db_xref="CDD:432205"
ORIGIN      
        1 mtqeltspsp apqapgtgrg pgwwrdaviy qvyvrsfads dgdgigdlrg ararlpylkd
       61 lgvdavwltp fyaspqadgg ydvadyravd plfgslqdad dlirtahdlg lrvivdivpn
      121 htsdrhpwfq dpelarqryl frpgkgegge lppndwesvf ggpawtrtar gdwylhlfap
      181 eqpdlnwdnp evhaefeail rfwldlgvdg frvdvahgmi kapglpdigh gqqaklignq
      241 vlpffdqdgv htihrawrrl ldgygeahsk qvvgvaeawa ptaerlalyv rpdelhqafn
      301 fqflnapwaa dalrsvidas laattsvgap ttwvlsnhdv vrhstrlggg ldraraatll
      361 mlalpgsayl yqgeelglpe vtdlpdevrq dpaffrggrt agaaatsgqd gfrdgcrvpl
      421 pwsgelppyg fgdggswlpq pddwaaltve aqtgdpastl elyrtalalr rrlpglgdge
      481 mswapapdgv laftragvlc avntlgheve lpppgallla sapvtgngaa avlpgdsctw
      541 wai
//
LOCUS       WP_457700795             350 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700795
VERSION     WP_457700795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 350)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..350
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36992
     Region          3..337
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtarlsdiaa qagvseatvs rvlngkpgvs attrqsvlaa ldvlgyerpv rlrqrsaglv
       61 glitpelenp ifpafaqvig qaltrqgytp vlatqtpggs tedeltemlv drgvagiifv
      121 sglhadtsad mqryeqlrgq gvpfvlingf sdkvqapfvs pddraavdla vthlsalghr
      181 riglalgpkr fvpvqrkieg fvrsmqerlq tgpaeaepfi qhslytlegg qaaasalier
      241 gataivcasd mmalgairaa rqrgldvpre isvvgfddsp liaftdpplt tirqpvtamg
      301 qaavrallee iggtpaphse fvfhpelvvr gstasapktt aripkplrat
//
LOCUS       WP_457700789             286 aa            linear   BCT 27-JAN-2026
DEFINITION  sugar ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700789
VERSION     WP_457700789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..286
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30922
     Region          11..286
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 mtrthttrpa rkrnersrpa siglhaglav aavlavfppl wllvtsfkpk ndafstglvt
       61 hftfanythv ladtefltwf knsviivglt tvlgvfiaat tgyavsrfrf pgmrplmwll
      121 lvtqmfpvav livplynlla slgllnqpag lvityltiav pfcawmmkgf fdtipveide
      181 agrvdglnpf gtfwrlvlpl arpglavtgf ytfvtawaev ayasafmtge enltlagglq
      241 tfvnqytndw gsmtaaavii avpaalvfaf aqrhlvaglt agttkg
//
LOCUS       WP_457700799             292 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate ABC transporter permease [Streptomyces nigrescens].
ACCESSION   WP_457700799
VERSION     WP_457700799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Ford,R.C. and Beis,K.
  TITLE     Learning the ABCs one at a time: structure and mechanism of ABC
            transporters
  JOURNAL   Biochem Soc Trans 47 (1), 23-36 (2019)
   PUBMED   30626703
REFERENCE   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..292
                     /product="carbohydrate ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32095
     Region          1..265
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvapvvlvig viigyplvrg vflsltdane anvernigvn hlpatykftg ldnyqavlsd
       61 gvfwdrlgwt vlwtvgcvsl tfltglalan mlnrtlrgrt vyrlalilpw aipafisvft
      121 wrmlynekng ilnkllaggg idavpwlndp twaklsviav nvwlgvpfml vallgglqsi
      181 pgelyeaaem dgasawqrfr hitvpglrav sstvillsti wtfnmfpvif lltrggpgda
      241 teilvtyayr lsfidsprnf sesaawgvli lvllsvvavv yrralrkqge vw
//
LOCUS       WP_457700803             308 aa            linear   BCT 27-JAN-2026
DEFINITION  cyclase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700803
VERSION     WP_457700803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 10004822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="cyclase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32972
     Region          86..308
                     /region_name="COG1878"
                     /note="Kynurenine formamidase [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:441482"
ORIGIN      
        1 mplpqefhdi akrvnnwgrw gtddeigtln litgqvvrea atgirsgrri plalplrhdg
       61 vqtglipgrv nplhtmtain qeifgpgtva tsddavtmgl qaathwdgla hvshsgrlyn
      121 nrpadsvtah dgatrlgmek atpivsrgvl ldvarvhgtd vlpgghavtp edldaaeela
      181 gttvragdiv lvrtgqlrhy lagdrqayaf pspglslrtp ewfhardvaa vandtltfei
      241 fppeienlwm pvhaldlvem gmlqgqnwnl eelstacaee grfafflsam aepfvgasga
      301 pvapvail
//
LOCUS       WP_457700805             161 aa            linear   BCT 27-JAN-2026
DEFINITION  ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700805
VERSION     WP_457700805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..161
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17149
     Region          7..132
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mqvlqvqldv rpdpaevgra rrwarsrlvg sgigadepla etlillisel vtnavvhtga
       61 aaelrmcfsg sgavvgtvrv evvdvsarpp rqrhadgddt ngrglelvdg ladrwgwqqe
      121 gagkriwcev drgrpllraa gsdlgayeph cavsravthq a
//
LOCUS       WP_457700807             344 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700807
VERSION     WP_457700807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..344
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=36423
     Region          1..321
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqltdeqr alkggtrell agrfgrdrlr aavedpgpdr alwrelgaag ffalrlperd
       61 ggvglglpea vlvleeagra llpgplvacq vlagvvdgva tgekivglce garepvlweh
      121 pagcdelilm edgdgprdgp ydgphdgprd graggevega rgraggvyrs apdrvscapf
      181 asvdpltpla rvldlprtep valdvprlrr eaalltaaqq lgsavrtvem aagharereq
      241 fgapigsfqa vkqlcaqmlv raeiarsavy aasitesvld itvakllade aavrnardcl
      301 qvhggmgftw eadvhlhlkr awlhaerwtt aaeaeellaa glia
//
LOCUS       WP_457700817             158 aa            linear   BCT 27-JAN-2026
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces nigrescens].
ACCESSION   WP_457700817
VERSION     WP_457700817.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Alekshun,M.N. and Levy,S.B.
  TITLE     The mar regulon: multiple resistance to antibiotics and other toxic
            chemicals
  JOURNAL   Trends Microbiol 7 (10), 410-413 (1999)
   PUBMED   10498949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..158
                     /product="MarR family winged helix-turn-helix
                     transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16962
     Region          11..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 meeavsggvg arrerlaeel rnygasftel grrfaarigv hstdafalle iasaaergap
       61 lspaslgrri plssgamtal lnrleeagyv trtrghadrr ivtlhssprv reladeffgp
      121 vnarqdavls rypaelleqf etllselgaa medgpdsp
//
LOCUS       WP_457700821             568 aa            linear   BCT 27-JAN-2026
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Streptomyces
            nigrescens].
ACCESSION   WP_457700821
VERSION     WP_457700821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..568
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=61941
     Region          39..543
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mrtailgpaq raealarmae reldilvvga gvvgagtald aatrglstgl veardwasgt
       61 ssrssklihg glrylemldf alvrealker glllerlaph lvkpvpflyp lqhkgwerwy
      121 agsgvalyda msvssghgrg lpvhrhlshk ralqvapclk kdalvgalqy ydaqmddary
      181 vatmvrtaaa ygaqvanrar vvgflreger vvgvrvedve gggdyeiraq qivnatgvwt
      241 ddtqaliger gqfhvraskg ihlvvpkdri hstsglilrt eksvlfvipw grhwivgttd
      301 tdwdldkahp aassadidyl lehvndvlat pltrddvegv yaglrpllag esdatsklsr
      361 ehtvahpvpg lvvvaggkyt tyrvmakdav deavhaldqr vadcvtedvp lvgaegyral
      421 wnarariaar tglhvarieh llnrygslte ellelvvadp slgeplahad dylraeavya
      481 cthegarhld dvltrrtris ietfdrgtrs arevaeliap algwdsdqve keiahyqkrv
      541 eaeresqrqp ddltadaarl gapdivpl
//
LOCUS       WP_457700823             415 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleotide sugar dehydrogenase [Streptomyces nigrescens].
ACCESSION   WP_457700823
VERSION     WP_457700823.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..415
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=44204
     Region          4..408
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mpadlavigl ghlglplaqa ataagigtig ydpdphtagl sgtdgplsat elrrllsagf
       61 rtttdpttlg rvrtavlcap tplgedrald ltaladaart laaqlrphtt vilestaypg
      121 tteeflrpll eegsgltagr dfhlacspgr hdpgnrthry antpkviggl tpacteaaaa
      181 fygrltdkvv rargpreaet aklletnyrh inialmnema vfchdigvdl wdvircaetk
      241 pfgfqafrpg pgvgghaapi dpnylsykgr slghplrmve laqevngrmp ryviqrcatl
      301 lnehgksarg arilllgvty kpdigdqags pareiasrlm elgahltyhd pyvpqwnvlg
      361 rpvpradsly eaaaaadltv llqahrtydl qglavkaqll ldtrgatptg aahrl
//
LOCUS       WP_457700825             696 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457700825
VERSION     WP_457700825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..696
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72766
     Region          12..266
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(12,36..37,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mngkegrlla gryrladvlg rggmgtvwra rdevlgrtva vkelrfpggv eedekrrlit
       61 rtlreakaia rirnngavtv ydvvdeddrp wivmelvegr slaevvrddg pltprraaev
      121 glavldvlra ahtegilhrd vkpsnvlmsd dgrvvltdfg iaqvegdpsv tstgmlvgap
      181 syisperarg qkpgppadmw slggllyacv egvppydkgs aiatltavmt epveppksag
      241 aleevifgll vkdpagrldd agarallldv vhapeaqkpe ppldetramv lptvpkerat
      301 akpesppkpk papksrvprk pkpkpaaapv agpaagsgpa sdgtkagksk agaakaaaar
      361 aaatstpert erpqqaatpa akeatgadra gsgasrptlt rpgfdtdaak erlraalqtv
      421 raaaaaarar aesrpgdgnr pstrasvtdv vprrtliiva livalavlgt vlavalsggd
      481 ttknsgkpag kqdkassaak akpstesadt gedakdrpgs papqppggvs paedkgdtgk
      541 dgkavpdgfa qvsngrfhfg mampkgfkqt atagqgsgvi ysgsggfprv qvdynakpgt
      601 daaaswrsle pavrgssedy hlisiksvkw rgyptvadws ftrrqsgqqv rvldrgfkad
      661 dqhgyaimit ceadawsdke cknvvetafk tfaikd
//
LOCUS       WP_457700828              95 aa            linear   BCT 27-JAN-2026
DEFINITION  YlxR family protein [Streptomyces nigrescens].
ACCESSION   WP_457700828
VERSION     WP_457700828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Osipiuk,J., Gornicki,P., Maj,L., Dementieva,I., Laskowski,R. and
            Joachimiak,A.
  TITLE     Streptococcus pneumonia YlxR at 1.35 A shows a putative new fold
  JOURNAL   Acta Crystallogr D Biol Crystallogr 57 (Pt 11), 1747-1751 (2001)
   PUBMED   11679764
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..95
                     /product="YlxR family protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=10480
     Region          11..93
                     /region_name="YlxR"
                     /note="Nucleoid-associated protein YlxR, Predicted
                     RNA-binding, DUF448 family [General function prediction
                     only]; COG2740"
                     /db_xref="CDD:442042"
     Site            order(13,29,51)
                     /site_type="other"
                     /note="putative RNA binding cleft [nucleotide binding]"
                     /db_xref="CDD:238173"
ORIGIN      
        1 msgrthacac pertclgcre raakgdllri veiegecvpd prgtlpgrga yvhptlvcld
       61 lavrrrafnr ayrargpfdt talrqyvera eqplq
//
LOCUS       WP_457700836             303 aa            linear   BCT 27-JAN-2026
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700836
VERSION     WP_457700836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  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
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Davies,J. and Wright,G.D.
  TITLE     Bacterial resistance to aminoglycoside antibiotics
  JOURNAL   Trends Microbiol 5 (6), 234-240 (1997)
   PUBMED   9211644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="aminoglycoside phosphotransferase family
                     protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32479
     Region          5..303
                     /region_name="StrB"
                     /note="Streptomycin 6-kinase [Defense mechanisms];
                     COG3570"
                     /db_xref="CDD:442791"
ORIGIN      
        1 matapieppq rlvsslsgdp espvrqwlta lptlvqqrle aweltlervh apggrsslla
       61 lvrqqdgtpa alkfpvpgrv sahegaalev wdgwgavrll rsddqsgall lerlqggvsl
      121 rslpeakall eaagtvrrlw vqpgpghpfe tlaarteeaa eglrtagalt raagplveqa
      181 lelrrglpdg sdeqfllhga frqgkvlaga rapwlavgpa pvvgeraydl aalvldrfed
      241 llagsgaaaa arrrvaklad slevdrdrlr dwtlyravdt gvrevavger qrgeqllefa
      301 awl
//
LOCUS       WP_457700839             177 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700839
VERSION     WP_457700839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..177
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19402
     Region          13..156
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          91..163
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mddvavgpld laarvddala vqalafglsd eeiavrrhiv lrhlgcpgar algattpdgr
       61 ltgfvygmpn drthwwstvv epylrnegld hwlddsftit elhvhpayqh rgigralitr
      121 itdeateprs ilsaidtesp arrlyrslgy rdlarrvlfp saptpyavmg aplplkg
//
LOCUS       WP_457700841             281 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700841
VERSION     WP_457700841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20674832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..281
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30328
     Region          48..153
                     /region_name="DUF4081"
                     /note="Domain of unknown function (DUF4081); pfam13312"
                     /db_xref="CDD:433108"
     Region          199..281
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mlttttikvl epgelddala vldrdpvana fvaarvqiag ldpwrlggem wgwyvdghle
       61 slcyaganlv pvcatseair gfaerarrqg rrcssivgpa eataelwsll epywgparei
      121 rahqplmvtt apsaeiapdp yvrrirknem dlimpacvam fteevgispm agdggllyqa
      181 rvaelvgagr sfartengkv ifkaeigaat qracqiqgvw vdpayrgkgl setgmaavlr
      241 yalsdvapvv slyvndfnta arasyrrvgf eevgafmsvl f
//
LOCUS       WP_457700845             639 aa            linear   BCT 27-JAN-2026
DEFINITION  acyl-CoA dehydrogenase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700845
VERSION     WP_457700845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..639
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=69880
     Region          60..440
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtapsirnvs erearqvaea areqdwrkps fakelflgrf rldlihphpt pavddvrrge
       61 kflatlrefc etevdgarie regqipdetv dglkalgafg mkidpkyggl gltqvyynra
      121 lslvgtaspa igallsahqs igvpqplklf gtkeqketfl prcartdisa flltepdvgs
      181 dparlatmav pdgtdyvldg vklwttngvv adllvvmarv paseghkggi tafvveadsp
      241 gitvenrnaf mglrglengv trfhrvrvpa anrigpegag lkialttlnt grlslpamcv
      301 gsgkwclkia rewsgareqw grpvakheav gakisfiaat tfaleavvdl ssqmadenrn
      361 dirieaalak lygsemgwlm adelvqirgg rgfetadsla argeravpae qmlrdmrinr
      421 ifegsteimh lliareavda hlsvagdlid pdktladkgr aaaraggfya rwlpklvagp
      481 gqlpstyqef grlsghlryv ertsrklars tfyamsrwqg rmetkqgflg rivdigaelf
      541 amsaacvrae ylretddhgr eaqqladvfc rqarirveel fgrlwtntde ldrkvvsgvl
      601 dgsyawleeg iidpsgdgpw iadatpgpsm tdnvrrpir
//
LOCUS       WP_457700847             318 aa            linear   BCT 27-JAN-2026
DEFINITION  RecB family exonuclease [Streptomyces nigrescens].
ACCESSION   WP_457700847
VERSION     WP_457700847.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Steczkiewicz,K., Muszewska,A., Knizewski,L., Rychlewski,L. and
            Ginalski,K.
  TITLE     Sequence, structure and functional diversity of PD-(D/E)XK
            phosphodiesterase superfamily
  JOURNAL   Nucleic Acids Res 40 (15), 7016-7045 (2012)
   PUBMED   22638584
REFERENCE   2  (residues 1 to 318)
  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   3  (residues 1 to 318)
  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   4  (residues 1 to 318)
  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 10006768
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..318
                     /product="RecB family exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_component="GO:0009338 - exodeoxyribonuclease V complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008854 - exodeoxyribonuclease V activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34705
     Region          40..291
                     /region_name="Slr0479"
                     /note="RecB family exonuclease [Replication, recombination
                     and repair]; COG2887"
                     /db_xref="CDD:442133"
ORIGIN      
        1 mgwsteqaea gtqsgqsgge pgaetagaga rsgeqprppv alspsrasdf mqcpllyrfr
       61 vidrlpekps aaatrgtvvh avlerlfdap aaertaagar amvpgewekl lakrpelael
      121 faedpegerl agwlaeaeal verwfsledp trlepadrel yvetvldsgl qlrgfidrvd
      181 iaptgevriv dyktgkaprp qfaegalfqm kfyalvvwrl rgvvprrlql vylgsgdvvt
      241 ydpveadlrg verkllalwe aiqlatatgd wrprptklcg wcdhqahcpe fggtppvypl
      301 qvrpaeggvp pqgrmgei
//
LOCUS       WP_457700851             308 aa            linear   BCT 27-JAN-2026
DEFINITION  tRNA (adenine-N1)-methyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700851
VERSION     WP_457700851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  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 308)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..308
                     /product="tRNA (adenine-N1)-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016426 - tRNA (adenine)
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0030488 - tRNA methylation [Evidence IEA]"
                     /calculated_mol_wt=33057
     Region          17..267
                     /region_name="Gcd14"
                     /note="tRNA A58 N-methylase Trm61 [Translation, ribosomal
                     structure and biogenesis]; COG2519"
                     /db_xref="CDD:442009"
ORIGIN      
        1 mseptgaarr rgpfkvgdqv qltdpkgrhy tftleegksf hthkgafphd eligapegsv
       61 vrttgnvayl alrpllpdyv lsmprgaavv ypkdagqila madifpgarv veagvgsgsl
      121 ssfllraigd dgmlhsyerr adfaeiatqn veryfggphp awtltvgdlq dnlsdadvdr
      181 vildmlapwe cleavskalv pggilcayva tttqmartve airehgtfne psawetmvrt
      241 whveglavrp dhrmightgf lltarrladg vepplrrrrp akgaygedyt gpgkdpaaas
      301 gggsadrg
//
LOCUS       WP_457700835             171 aa            linear   BCT 27-JAN-2026
DEFINITION  ferritin-like domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457700835
VERSION     WP_457700835.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 171)
  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 171)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..171
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17441
     Region          23..153
                     /region_name="DUF4439"
                     /note="Domain of unknown function (DUF4439); pfam14530"
                     /db_xref="CDD:434020"
ORIGIN      
        1 mtagtargsr rdnddsgree ltavqaalaa ehaavygygv vggriagdrr keaqaaydgh
       61 rarrdalrrv vrdlggtpqa aaaayklpfp vpdaaaaarl aaeledrlaa vyadlvragg
      121 svrrreaaaa lreaavrsvr wrgsgvafpg lveraadaap sgaasapaga l
//
LOCUS       WP_457700842             433 aa            linear   BCT 27-JAN-2026
DEFINITION  M50 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457700842
VERSION     WP_457700842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Verhelst,S.H.L.
  TITLE     Intramembrane proteases as drug targets
  JOURNAL   FEBS J 284 (10), 1489-1502 (2017)
   PUBMED   27889944
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Kroos,L. and Akiyama,Y.
  TITLE     Biochemical and structural insights into intramembrane
            metalloprotease mechanisms
  JOURNAL   Biochim Biophys Acta 1828 (12), 2873-2885 (2013)
   PUBMED   24099006
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Makinoshima,H. and Glickman,M.S.
  TITLE     Site-2 proteases in prokaryotes: regulated intramembrane
            proteolysis expands to microbial pathogenesis
  JOURNAL   Microbes Infect 8 (7), 1882-1888 (2006)
   PUBMED   16731018
REFERENCE   4  (residues 1 to 433)
  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 11433527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..433
                     /product="M50 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46484
     Region          5..428
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
ORIGIN      
        1 mttwmtilgi vvfvvgllfs iawhelghls taklfgirvp qymvgfgptl fsrkkgdtey
       61 gikavplggy irmigmfppg ddgklqarst spfrgmieda rsaafeelqp gdekrlfytr
      121 kpwkriivmf agpfmnlila vvifmsvlmg fgintqttqv gsvsecvisa aaktdkcpag
      181 akdspakaag lragdkivsf nghsvpdwga lqqqirdttg patlvverhg arttlradli
      241 enkvaktdgh ggyvpgefvt agflgftpas gvvqqsfgqs vdrmgnmveq gvsslinvpa
      301 kvpdlwdaaf nggerkqdsp mgvvgaarvg gevfsldipp eqrvatmlfl vagfnlslfl
      361 fnmlpllpld gghiagamwe svrrafakiv rrpdpgpfdv aklmpvayvv agificftll
      421 vfvadvvnpv klt
//
LOCUS       WP_457700853              97 aa            linear   BCT 27-JAN-2026
DEFINITION  ferredoxin [Streptomyces nigrescens].
ACCESSION   WP_457700853
VERSION     WP_457700853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Kim,J.D., Rodriguez-Granillo,A., Case,D.A., Nanda,V. and
            Falkowski,P.G.
  TITLE     Energetic selection of topology in ferredoxins
  JOURNAL   PLoS Comput Biol 8 (4), e1002463 (2012)
   PUBMED   22496635
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Ikeda,T., Yamamoto,M., Arai,H., Ohmori,D., Ishii,M. and Igarashi,Y.
  TITLE     Two tandemly arranged ferredoxin genes in the Hydrogenobacter
            thermophilus genome: comparative characterization of the
            recombinant [4Fe-4S] ferredoxins
  JOURNAL   Biosci Biotechnol Biochem 69 (6), 1172-1177 (2005)
   PUBMED   15973049
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Fukuyama,K., Matsubara,H., Tsukihara,T. and Katsube,Y.
  TITLE     Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus
            refined at 2.3 A resolution. Structural comparisons of bacterial
            ferredoxins
  JOURNAL   J Mol Biol 210 (2), 383-398 (1989)
   PUBMED   2600971
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10603167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..97
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=10536
     Region          12..82
                     /region_name="Fer4_15"
                     /note="4Fe-4S single cluster domain; pfam13459"
                     /db_xref="CDD:404359"
ORIGIN      
        1 mtaqdeapel evwidqdlct gdgicaqyap evfeldidgl ayvkstddel lqdkgattpv
       61 plkllndvrd sakecpgdci hvrrvndlve vygpdae
//
LOCUS       WP_457700862             386 aa            linear   BCT 27-JAN-2026
DEFINITION  LacI family DNA-binding transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700862
VERSION     WP_457700862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 386)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..386
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39440
     Region          43..373
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mtsneatppp gestvpqalg sarageapit gaagaahpgr paaarvtsrd varaagvsqa
       61 avslvlgdkw rgrvspgkad avraaarelg yrpnlaarsl rmgrtrtvll vvpaltteff
      121 arvytgaarv aaehgfgvvl ypspegigpa rnpfdsaaat ldgviassma aealtalrea
      181 dlplvmldsd paddradatv nldiadgvrq ltghlsalgh rrithlaadv rswtfelrar
      241 avadslhslp gallrrqpaa lgvdaglhaa haaltgpgpr ptallcdddi iaagackavr
      301 rlglrvpedv svtgfddlal avavepeltt vrlpaeefge agmralmtvl dgrpanaptl
      361 pvelvtrgst appvdapgna arpggq
//
LOCUS       WP_457700869             460 aa            linear   BCT 27-JAN-2026
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Streptomyces
            nigrescens].
ACCESSION   WP_457700869
VERSION     WP_457700869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 460)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..460
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=48572
     Region          38..439
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 msvsavaadr slcaplpvlg rdvlvplvtg gevdyaaldy aasapalqrv wddvaayapy
       61 ygsvhrgagy lsqlstdlfe nsretiaefl gcraedqvvf trsttdslnl laavlpqgtr
      121 vfvfetehha sllpweqrpd vavtylnapr tpqqavdtle kalatrepyg palvcvtgas
      181 nvtgelwpvq elaaaahahg arivldaaql vphhpvdlge ldvdwvafsg hklyapfgag
      241 vlagradwlr daepylaggg asrkvsrrtd ggvdvewhtt aarheagspn vigvyaiasa
      301 cqalteagfd glvareqeli arlragladv pevtvlslfg edaarvgvls fvvegwnssh
      361 faaalsaeyg igvrdglfca hplvrtllgs epqdpgecga pdaapgeksl nairvslgvg
      421 tpdehvdrfv ravtelvtng arwnyrtegg rcvpaarsav
//
LOCUS       WP_457700865             328 aa            linear   BCT 27-JAN-2026
DEFINITION  FKBP-type peptidyl-prolyl cis-trans isomerase [Streptomyces
            nigrescens].
ACCESSION   WP_457700865
VERSION     WP_457700865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            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 11425492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..328
                     /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]"
                     /calculated_mol_wt=33829
     Region          225..326
                     /region_name="FkpA"
                     /note="FKBP-type peptidyl-prolyl cis-trans isomerase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0545"
                     /db_xref="CDD:440311"
ORIGIN      
        1 mnltkntrra aaaltvpill ftaacgsddg kgasggavvk vegkagekpk itvpkgakps
       61 dkavtktlie gkgatvkkgd lvrldfeaks mkgqnlggsw tpqpgskpgg prtqvvsevt
      121 dqmtqqmlpp kvlsavagqk vgsrfevegt akaligagln pqagikpgdg lvwvvdvvga
      181 kkvdkkakae geqaepedgl pevtapdgka akievpkgek apkdlkeqvl iegkgpevka
      241 gdgliaqytg vkwedgkkfd sswdhggata fqigtgqvvq gwdkalvgkh vgdrveivip
      301 pklgygaspq helakntlvf svdivgtv
//
LOCUS       WP_457700882             324 aa            linear   BCT 27-JAN-2026
DEFINITION  carbohydrate kinase family protein [Streptomyces nigrescens].
ACCESSION   WP_457700882
VERSION     WP_457700882.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..324
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35134
     Region          2..294
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,254,257)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(195,223,252,255..256,259,281,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 mriavtgsia tdhlmtfpgr fadqlvadql htvslsflvd qldvrrggva anicfgmgql
       61 gtepilvgaa gndfeeyraw ldrhgvdtrs vrisevlhta rfvcttdadh nqigsfytga
      121 msearlielq hvaervggld lvligaddpe amirhteecr srgipfaadf sqqiarmdgd
      181 airtlledaa ylfsneyekg liesktgwtd eeilakvgtr vttlgsngvr iervgepaie
      241 vgvpeenaka dptgvgdafr agflsglawg vgleraaqig cmlatlviet vgtqeyelhr
      301 shfmdrftka ygheaaaevq qhla
//
LOCUS       WP_457700894             244 aa            linear   BCT 27-JAN-2026
DEFINITION  ABC transporter ATP-binding protein [Streptomyces nigrescens].
ACCESSION   WP_457700894
VERSION     WP_457700894.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..244
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25174
     Region          15..236
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mrsgvvvagp paagpmvvve dlhrsygtaa gavhalrgvs csvprgelva lrgrsgsgkt
       61 tllnliggld tpdsgritvd gtpladlges gllemrrdri gfvfqsfgli pilsaaenvg
      121 vplrlrkvpp reredrvall lslvglsdha eqrpgelsgg qqqrvaiara lanrpallia
      181 deptgqldae tgmevmdllr avvrsegvta lvathdpnll gladrvlels dgviteagtg
      241 pgvg
//
LOCUS       WP_457700897             197 aa            linear   BCT 27-JAN-2026
DEFINITION  PaaI family thioesterase [Streptomyces nigrescens].
ACCESSION   WP_457700897
VERSION     WP_457700897.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..197
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20580
     Region          50..161
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msgtdeprar ltpptdavap vrhaeapapg ellgahydrc fgcgtgqphg lhlearagdg
       61 vsvsaeftvk eahqgapgla hggvlatald etlgslnwll rviavtgrle tdfvrpvplg
      121 tvlhldarvt avhgrkiysa avgriggpdg pvavraeavf ievkvdhfid ngrteeiqaa
      181 madpdqvkra rafevnp
//
LOCUS       WP_457700892             187 aa            linear   BCT 27-JAN-2026
DEFINITION  GNAT family N-acetyltransferase [Streptomyces nigrescens].
ACCESSION   WP_457700892
VERSION     WP_457700892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7) (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..187
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20394
     Region          27..149
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mteahlttpr mtdmhiahta dlgaatlkaa rtllydvfdd mtaedwehsl gglhalihed
       61 gelighasvv qrrllhdgra lrcgyvegvg vradrrgrgh gaalmdaler vvrsgydlga
      121 lgaadeaatf yaargwqrwr grswaltpdg iqrtadedgc iyvlpaaatq ldldtdltcd
      181 wrdgdvw
//
LOCUS       WP_457700909             459 aa            linear   BCT 27-JAN-2026
DEFINITION  M16 family metallopeptidase [Streptomyces nigrescens].
ACCESSION   WP_457700909
VERSION     WP_457700909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Becker,A.B. and Roth,R.A.
  TITLE     An unusual active site identified in a family of zinc
            metalloendopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3835-3839 (1992)
   PUBMED   1570301
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..459
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49715
     Region          29..448
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtsrthttta rtstegrava rtqtllkgta gagtvrrttl pgglrivtet lptvrsvtfg
       61 iwanvgsrde tpslngathy lehllfkgte rrsaldisaa vdavggemna ftakeytcyy
      121 arvldtdlpl aidvvcdmlt gslveaedvd aergvileei amteddpgdc vhdlfahtml
      181 gdtplgrpvl gtvdtvnalt perirrfykk hydpthlvvt aagnidhakv vrlvrrafeq
      241 agaldrtdat pmaprsgara irtagrvell nrkteqahvi lgmpgmartd drrwamgvln
      301 talgggmssr lfqevrekrg laysvysyts gfadcglfgv yagcrpsqvh dvlkicrdel
      361 dqvashgltd deirraigql rgstvlgled tgalmhrigk selcwgeqms vdemlariaa
      421 vtpdevreva rdvlgtrpsl svigplkdrq aarlddvva
//
LOCUS       WP_457700951             513 aa            linear   BCT 27-JAN-2026
DEFINITION  nucleobase:cation symporter-2 family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700951
VERSION     WP_457700951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..513
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53896
     Region          33..446
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 marvsrhdpe qfsrqrahpv devlpvgklt lygfqhvlaf yagavivpiv lgnalglsre
       61 elvylinadl ltcgvasiiq algvwkigar lplvqgvtft avspmiaigl gagggtagll
      121 vvygavitag iatflfapff sklvkyfppi vigtiltvig ltlipqglkd aaggaqligh
      181 pgygdpknla yalgtllfil lvvrlgkpyl sslavllglv agtgvawllg dvdfggvkna
      241 dwfgvsspfh ygmpkfelfp iiamvvvmli tmvettgdvy aigeitrkkv dnttvanalr
      301 adgvatvlgg ifnsfpyvaf aeniglvrms kvmsrfvvva aggfmivmgl lpkagsvvaa
      361 iphpvlggaa iamfgmvaav giqilgkvdl reernalila vslaaallpn avepffermp
      421 edvravlnsg itlgsltavl lnfffnvftr rktmeidwde ieggdepaet hepfgahgpa
      481 dpyapqphhr pgppnppgpq hpqggpdwgi pgh
//
LOCUS       WP_457700920             561 aa            linear   BCT 27-JAN-2026
DEFINITION  ribonuclease J [Streptomyces nigrescens].
ACCESSION   WP_457700920
VERSION     WP_457700920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..561
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60979
     Region          14..561
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mshphpelga ppklpkgglr vtplgglgei grnmtvfeyd grllivdcgv lfpeeeqpgi
       61 dlilpdftsi rdrlddidgi vlthghedhi ggvpyllrek pdipligskl tlalieaklq
      121 ehrirpytle vkeghterig sfdcefvavn hsipdalava irtpagmvvh tgdfkmdqlp
      181 ldrrltdlpa farlgeegid lllsdstnae vpgfvpperd isnvlrtvfa naqkriivas
      241 fashvhriqq ildaaheygr rvafvgrsmv rnmgiarelg ylkvpaglvv dvkalddlpd
      301 devvlvctgs qgepmaalsr manrdhqiri vqgdtvilas slipgnenav yrvingltrw
      361 gadvvhkgna kvhvsghasa gellyfynic kpknlmpvhg ewrhlranae lgaltgvrkd
      421 riviaedgvv vdlvdgvaki vgkvkagyvy vdglsvgdvt eahlkdrril gdegiisvyv
      481 vvdsttgkiv ggpdihargs giddsafsgv mpkidealak saqdgiteph qlqqlvrrtv
      541 gkwvsdnyrr rpmilpvvve v
//
LOCUS       WP_457700926             387 aa            linear   BCT 27-JAN-2026
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700926
VERSION     WP_457700926.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..387
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40771
     Region          6..368
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msqhggadeg fgavadafar nftedrelga avavfvdghk vvdlwggtad drtgrpwded
       61 tvlpvmslak glvsvcahll aqqgkldlda pvaeywpefa qrgkegittr mvlahtagip
      121 laekqltfee ltrwtpvira leeqqvlyep gtayeyhaha ygfivgelir rltgrtpggy
      181 freaigdalg lrtwigmpqe evprlarlae aegrsplpss dllpmraltm ngvlpfpgld
      241 dphgynspal ltaefpgaga vstarglaal yaavatgvdg aprllgadtv tdavrqlsgg
      301 aswsgfpdlg arwgsgfltd spfrrllgtr sfgnsgaggq fafgddefgv gfaytanrmg
      361 aggdprvdrl igalrtcvga pepatgg
//
LOCUS       WP_457700946             345 aa            linear   BCT 27-JAN-2026
DEFINITION  serine/threonine-protein kinase [Streptomyces nigrescens].
ACCESSION   WP_457700946
VERSION     WP_457700946.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..345
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=37181
     Region          28..293
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,55,57,89,105..108,112,114,151,153,
                     155..156,158,174..175,178,196..199)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,55,57,89,105..108,112,153,155..156,
                     158,174..175)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(38,112,114,151,153,155,178,196..199)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(51..52,81,86,91..94,106)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(174..181,183,192..199)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mnggpgrsqe rstapdssgl rgrqiaeyll qdeigrggma vvyraedlrl grtvalklla
       61 pelarndtfr qrfahesrva aaidhphivp vfeagetegv lyiamryvqg rdlralldrd
      121 gplplettcr ialqvasald aahahdlvhr dvkpgnilia egtdsdrpeh ayltdfgltk
      181 kslsltgfts vgqfvgtldy vapeqisgrp vdgrcdvysl acvlfemltg sppfrrdddm
      241 allwahqydp ppamtelrpd lpeavdavfa qslakapenr yetcrgfvaa lraagratvp
      301 pvaagtpqah pmtqvdaqad pggrhsaapp ppprwatpmf pgrag
//
LOCUS       WP_457700935             351 aa            linear   BCT 27-JAN-2026
DEFINITION  AAA family ATPase [Streptomyces nigrescens].
ACCESSION   WP_457700935
VERSION     WP_457700935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  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 351)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..351
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38438
     Region          67..>321
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msdwliyrga gaphdgieql pppppwrdfd ggplvappaa ldpsserrlg vqhreashhr
       61 pgeterelvn aalylrrpll vtgapgsgks tlahsvayel glgrvlgwpv vsrstlrdgl
      121 ydydaigrlq dlqiaraapa aaesgaapdp dptdepgggi gryirlgplg tallpaarpr
      181 vllvdeldks didlpndlln vleegefrip elerlagsap evevlsddga rvtvrdgrvr
      241 ckafpfivlt sngerdfpap llrrcihlhi papdkerlaa mvrahfgega aeryeavidr
      301 fldrepgdvr avdqlfnaih ltqragwtde deeetrrrlt aelmrpldrt r
//
LOCUS       WP_457700955             469 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457700955
VERSION     WP_457700955.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..469
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49242
     Region          15..456
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mhdattqage palgagtger eplsaglkqr hltmlglggv igaglfvgsg agiavagpgi
       61 vlsyliagal amlvmrmlge msaampasga fsvhaeralg rwagfsvgwl ywfllvvvla
      121 veatgaaqia ngwvpavpqw gwvlifmivf tvanlaavkn fgefefwfaa lkvtaivlfl
      181 alsllavfgv lpdtepvgla nltghggflp hgwggvisgv lavvfafggl evvtiaaaes
      241 ddparavgra vrsavwrilf fyvgsmlviv tllpwssmqp gkspyvavld sigvpgagqi
      301 mnivvfvall salnanlygs srmvfslaer geaprallkv sggvprravl asvafgfisv
      361 llnlkwpdsv flymlnavga vllfvwglia vsqlrlrpri ereapgkltl rmwafpyltw
      421 aalvamggvl vlmltddtar pqllwsagat gavllvagvr elrgrrarr
//
LOCUS       WP_457700957             480 aa            linear   BCT 27-JAN-2026
DEFINITION  amino acid permease [Streptomyces nigrescens].
ACCESSION   WP_457700957
VERSION     WP_457700957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..480
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50297
     Region          19..469
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mnrtpssaap areqtdavqg agpdsgstls nglkqrhlsm ialggvigag lfvgsregia
       61 aagpsivlay avsgalvmli mrmlgemaaa npasgsfsvh aersigswag ftvgwmftal
      121 lcvavaaeam gaadimvqwf pgsepwmwvl lfmviftgtn laavsnfgef efwfaalkva
      181 aiaiflvlgl laifgllpgt sapgtthltg dggflpkgvd glmigllasv fayggletvt
      241 iaaaeskdpv rgvaravrta mwrialfyvg smaiivtvip wsapsiaksg pyvavldyle
      301 ipaagqvmnv vilvallsav nanlygasrm ayslisrgqg paflgkvsgg vprravllca
      361 afgffavvls flwpdtlfqw llnmvgaavl vvwgfiavaq lrmrrtlere apeklvvkmw
      421 afpvltwval agiavvlllm lrdenqriql lftggfgval tvigllrqra lgrgaslske
//
LOCUS       WP_457700968             200 aa            linear   BCT 27-JAN-2026
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            nigrescens].
ACCESSION   WP_457700968
VERSION     WP_457700968.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21187
     Region          2..196
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpktvnreeq rrqigaavlr laaeqgldev svrtvaaaad rspgavqkyf rtkdemlafa
       61 aelagerfee rmaavdrglp phealralvl atlpvdaerr aeaaaqlafa traahhpglg
      121 airrqvdqdv realggwlas aghgrgpdpa adclaladav ialsdglalr llyapddrea
      181 llraldrala alipppvphp
//
LOCUS       WP_457700975             221 aa            linear   BCT 27-JAN-2026
DEFINITION  MOSC domain-containing protein [Streptomyces nigrescens].
ACCESSION   WP_457700975
VERSION     WP_457700975.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..221
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23711
     Region          1..180
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mkllsvnvgr papsrhtdae ggtgidkrpv dgpvavaapg pkgvggsglt gdavvdlrhh
       61 ggddqavyay aredlddwqr elgrelanga fgenlttsgv evtgahiger wrvgprllle
      121 vsspripcrt fhgwigergw irrftqagvp gaylrviepg eiragdavev vhrpdhevti
      181 glmfralttr rellprllea gaalpeearr kalkyaeraa g
//
LOCUS       WP_457700974             257 aa            linear   BCT 27-JAN-2026
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            nigrescens].
ACCESSION   WP_457700974
VERSION     WP_457700974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..257
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27386
     Region          1..240
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mttalitgat agigaafarr lasdghsvvl vardekrlhe qatelhdrhg ieaevlsadl
       61 ateegiaave arlsdtrhpv dmlvnnagfg nkgeylevpm adeltmlkvh ceavlrltta
      121 gvrgmrdrrr gavvnvasva afvprgtyga skawvvqftq gaardlagsg vrlmalcpgf
      181 vrtefhqrag mgtdnipgwm wldadklvda amkdltrgks lsipdpryka lmgavklapr
      241 gvlggltsrt grkygpr
//
LOCUS       WP_457700977             303 aa            linear   BCT 27-JAN-2026
DEFINITION  LysR family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700977
VERSION     WP_457700977.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein 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 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   3  (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   4  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31804
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..297
                     /region_name="PBP2_LTTR_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08423"
                     /db_xref="CDD:176115"
     Site            order(108..109,111..112,115,119,121..127,228..233,
                     239..240,242..243)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176115"
ORIGIN      
        1 miearhlrvl ravsrtgsfs aaarelgctq pavsqqmkal eqsagtpllv ragremrltq
       61 agealvrhav gilagltaae eeiaaiaglr agrvrlvsfp sgsstlvpta latmraahpg
      121 trvslveaep prsiemlrng dceialafry pevrgadpaa gaewddlvvr piladrlval
      181 vpdghrlaka gaarfaelad eawiagcprc rrhlvevces agftpridfa tddypavigl
      241 vgaglgvaal peltlasvrp kgatavrlep avhreivalt lpdlaqvpav eatlnqlvda
      301 arr
//
LOCUS       WP_457700979             110 aa            linear   BCT 27-JAN-2026
DEFINITION  WhiB family transcriptional regulator [Streptomyces nigrescens].
ACCESSION   WP_457700979
VERSION     WP_457700979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Zheng,F., Long,Q. and Xie,J.
  TITLE     The function and regulatory network of WhiB and WhiB-like protein
            from comparative genomics and systems biology perspectives
  JOURNAL   Cell Biochem Biophys 63 (2), 103-108 (2012)
   PUBMED   22388511
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..110
                     /product="WhiB family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11891
     Region          17..86
                     /region_name="Whib"
                     /note="Transcription factor WhiB; pfam02467"
                     /db_xref="CDD:426788"
ORIGIN      
        1 madfsrlpgp nadlwdwqll aacrgvdssl ffhpegerga arsaretsak evcmrcpvra
       61 ecaahalavr epygvwgglt edereelmgr arhrlvpass mtghagisra
//
LOCUS       WP_457700981             450 aa            linear   BCT 27-JAN-2026
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Streptomyces
            nigrescens].
ACCESSION   WP_457700981
VERSION     WP_457700981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..450
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47977
     Region          64..448
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mtfaalaqap drrktearll alvvliavfg yaytglsmsg rlpgglavft vtmllmallp
       61 hlvlrrfapr adplilpvat lltgiglvll hrldityaqt prlktvaaan gqlvwtaigv
      121 avciaillil rdhrilqryi yltmvialvl lmapaffgad mygakrwill gplslqpgef
      181 vkimisvffa gyltvnrdal alagrralgi qlppgrqlap iftiwavsll vliferdlgt
      241 sliffgvfvi mlymatdrts wvvcgllmat vgaavvgsle phvhgrvtaw ldpmraftke
      301 graehmsdql gqallsfgsg gisgsglgqg hpeligfagn sdfilttvge elglagvmav
      361 imlyvllaqr glrvglsard pfgkllavgl sgalllqvfv vsggvtglip ltgkalpfla
      421 kggsslvanw vsvalllris dhaqrrrepv
//
LOCUS       WP_457700988             335 aa            linear   BCT 27-JAN-2026
DEFINITION  SMI1/KNR4 family protein [Streptomyces nigrescens].
ACCESSION   WP_457700988
VERSION     WP_457700988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Hong,Z., Mann,P., Brown,N.H., Tran,L.E., Shaw,K.J., Hare,R.S. and
            DiDomenico,B.
  TITLE     Cloning and characterization of KNR4, a yeast gene involved in
            (1,3)-beta-glucan synthesis
  JOURNAL   Mol Cell Biol 14 (2), 1017-1025 (1994)
   PUBMED   8289782
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10627618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..335
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=35924
     Region          106..145
                     /region_name="WHH"
                     /note="A nuclease of the HNH/ENDO VII superfamily with
                     conserved WHH; pfam14414"
                     /db_xref="CDD:433943"
     Region          173..307
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mttgrqglga lpgpraagha appnsayagq vvhfpdpvra arypagvrmd ergfpefspy
       61 araaaeiaep pegfgvdelr ltdyvsanaa lhaqghelwi dvpavatphg wtwhhvagtr
      121 rmelvpvevk allrhhggla taavahdkrg trplqetrpa hfglphrdls vgeeqlaqae
      181 ealgyrlpga yrsflkaagg capvgaalda elgllvdqpf ftvrddaavn dllyvnkclr
      241 dhftkdylgv afvqggvvav kvrgealgsv wfcpyddard qdgwtvqerv erlllpcged
      301 fddflqrlag nppeletvad lmvdggfaya vavgg
//
LOCUS       WP_457700994             311 aa            linear   BCT 27-JAN-2026
DEFINITION  LCP family protein [Streptomyces nigrescens].
ACCESSION   WP_457700994
VERSION     WP_457700994.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Kawai,Y., Marles-Wright,J., Cleverley,R.M., Emmins,R., Ishikawa,S.,
            Kuwano,M., Heinz,N., Bui,N.K., Hoyland,C.N., Ogasawara,N.,
            Lewis,R.J., Vollmer,W., Daniel,R.A. and Errington,J.
  TITLE     A widespread family of bacterial cell wall assembly proteins
  JOURNAL   EMBO J 30 (24), 4931-4941 (2011)
   PUBMED   21964069
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..311
                     /product="LCP family protein"
                     /GO_process="GO:0070726 - cell wall assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=33006
     Region          45..310
                     /region_name="Cps2a"
                     /note="Anionic cell wall polymer biosynthesis enzyme
                     TagV/TagU, LytR-Cps2A-Psr (LCP) family (peptidoglycan
                     teichoic acid transferase) [Cell wall/membrane/envelope
                     biogenesis]; COG1316"
                     /db_xref="CDD:440927"
ORIGIN      
        1 mtllvlvalv caggawlyvs agrqlqhvda lgeyagrpaa gkgtnwllvg tdsrtaltpq
       61 qreklhvgnn evqntdtimv lhsgehgptl vslprdsyvp ipghgsrkin eayadggpkl
      121 ltrtveqatg lridryaevn flgfvqvvda ldgvrlclda plkdeksgad fpagcqqmng
      181 aealafvrar yadpegdlgr vkrqrqliga vanemaapsv lldpdrltrv rdaslaallv
      241 ddgadvarll dmgwsmkqia ggggtattvp vnrpgvmvsg vgsvlpwden garelfealr
      301 hddriptsgt k
//
LOCUS       WP_457700998             290 aa            linear   BCT 27-JAN-2026
DEFINITION  glycosyltransferase family 2 protein [Streptomyces nigrescens].
ACCESSION   WP_457700998
VERSION     WP_457700998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 11440371
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..290
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32001
     Region          1..246
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mrlgavvltm gnrpeelral ldsvakqtgd pieivvvgng splpelpdgv rtvelpenvg
       61 ipagrnvgie afgpggsdvd gllfldddgl laredtaelc reafaadpel giisfriadp
      121 dtgetqrrhv prlrasdpmr ssrvttflgg anavrthvfe evgglpddff yaheetdlaw
      181 raldagwqid yrsdmvlfhp ttaparhavy hrmvarnrvw larrnlptll vpvylgvwll
      241 ltlarrpsrp alrawlggfk egwvtpcgpr rpmkwatvwr ltrlgrppvi
//
LOCUS       WP_457701002             245 aa            linear   BCT 27-JAN-2026
DEFINITION  phosphocholine cytidylyltransferase family protein [Streptomyces
            nigrescens].
ACCESSION   WP_457701002
VERSION     WP_457701002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces nigrescens
  ORGANISM  Streptomyces nigrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Jackowski,S. and Fagone,P.
  TITLE     CTP: Phosphocholine cytidylyltransferase: paving the way from gene
            to membrane
  JOURNAL   J Biol Chem 280 (2), 853-856 (2005)
   PUBMED   15536089
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kwak,B.Y., Zhang,Y.M., Yun,M., Heath,R.J., Rock,C.O., Jackowski,S.
            and Park,H.W.
  TITLE     Structure and mechanism of CTP:phosphocholine cytidylyltransferase
            (LicC) from Streptococcus pneumoniae
  JOURNAL   J Biol Chem 277 (6), 4343-4350 (2002)
   PUBMED   11706035
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Kent,C.
  TITLE     CTP:phosphocholine cytidylyltransferase
  JOURNAL   Biochim Biophys Acta 1348 (1-2), 79-90 (1997)
   PUBMED   9370319
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces nigrescens"
                     /db_xref="taxon:1920"
     Protein         1..245
                     /product="phosphocholine cytidylyltransferase family
                     protein"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26830
     Region          3..243
                     /region_name="COG1213"
                     /note="Choline kinase [Lipid transport and metabolism]"
                     /db_xref="CDD:440826"
ORIGIN      
        1 miglvlaaga grrlrpytdt lpkalvpvdg dttildltlg nfaeigltev aiivgyrkea
       61 vyerkealeq kyglkltlid ndkaeewnna yslwcgrdai khdvilangd tvhpvsvekt
      121 llaargngqk iilaldtvkq ladeemkviv dpakgvqkit klmdpaeatg